data_9F9C
# 
_entry.id   9F9C 
# 
_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   9F9C         pdb_00009f9c 10.2210/pdb9f9c/pdb 
WWPDB D_1292138398 ?            ?                   
# 
_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                        9F9C 
_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   13 ? ? ? ? 
3 non-polymer syn '(2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate'                                         356.540   4  ? ? ? ? 
4 non-polymer man RETINAL                                                                                  284.436   1  ? ? ? ? 
5 water       nat water                                                                                    18.015    35 ? ? ? ? 
# 
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  301 303 LI1 LI1 A . 
C 2 LI1 1  302 305 LI1 LI1 A . 
D 2 LI1 1  303 306 LI1 LI1 A . 
E 2 LI1 1  304 307 LI1 LI1 A . 
F 2 LI1 1  305 308 LI1 LI1 A . 
G 3 OLC 1  306 309 OLC OLC A . 
H 3 OLC 1  307 310 OLC OLC A . 
I 3 OLC 1  308 311 OLC OLC A . 
J 3 OLC 1  309 312 OLC OLC A . 
K 2 LI1 1  310 313 LI1 LI1 A . 
L 2 LI1 1  311 314 LI1 LI1 A . 
M 2 LI1 1  312 315 LI1 LI1 A . 
N 2 LI1 1  313 316 LI1 LI1 A . 
O 2 LI1 1  314 317 LI1 LI1 A . 
P 2 LI1 1  315 318 LI1 LI1 A . 
Q 2 LI1 1  316 319 LI1 LI1 A . 
R 2 LI1 1  317 320 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  402 441 HOH HOH A . 
T 5 HOH 3  403 404 HOH HOH A . 
T 5 HOH 4  404 475 HOH HOH A . 
T 5 HOH 5  405 407 HOH HOH A . 
T 5 HOH 6  406 434 HOH HOH A . 
T 5 HOH 7  407 402 HOH HOH A . 
T 5 HOH 8  408 400 HOH HOH A . 
T 5 HOH 9  409 480 HOH HOH A . 
T 5 HOH 10 410 476 HOH HOH A . 
T 5 HOH 11 411 403 HOH HOH A . 
T 5 HOH 12 412 417 HOH HOH A . 
T 5 HOH 13 413 488 HOH HOH A . 
T 5 HOH 14 414 401 HOH HOH A . 
T 5 HOH 15 415 411 HOH HOH A . 
T 5 HOH 16 416 456 HOH HOH A . 
T 5 HOH 17 417 416 HOH HOH A . 
T 5 HOH 18 418 418 HOH HOH A . 
T 5 HOH 19 419 415 HOH HOH A . 
T 5 HOH 20 420 478 HOH HOH A . 
T 5 HOH 21 421 422 HOH HOH A . 
T 5 HOH 22 422 494 HOH HOH A . 
T 5 HOH 23 423 486 HOH HOH A . 
T 5 HOH 24 424 495 HOH HOH A . 
T 5 HOH 25 425 487 HOH HOH A . 
T 5 HOH 26 426 491 HOH HOH A . 
T 5 HOH 27 427 492 HOH HOH A . 
T 5 HOH 28 428 414 HOH HOH A . 
T 5 HOH 29 429 493 HOH HOH A . 
T 5 HOH 30 430 419 HOH HOH A . 
T 5 HOH 31 431 482 HOH HOH A . 
T 5 HOH 32 432 489 HOH HOH A . 
T 5 HOH 33 433 490 HOH HOH A . 
T 5 HOH 34 434 496 HOH HOH A . 
T 5 HOH 35 435 477 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 N 1 A LI1 301 ? C1  ? B LI1 1   C1  
7   1 N 1 A LI1 301 ? C2  ? B LI1 1   C2  
8   1 N 1 A LI1 301 ? C3  ? B LI1 1   C3  
9   1 N 1 A LI1 301 ? O1  ? B LI1 1   O1  
10  1 N 1 A LI1 301 ? O2  ? B LI1 1   O2  
11  1 N 1 A LI1 301 ? O3  ? B LI1 1   O3  
12  1 N 1 A LI1 301 ? C41 ? B LI1 1   C41 
13  1 N 1 A LI1 301 ? C42 ? B LI1 1   C42 
14  1 N 1 A LI1 301 ? C43 ? B LI1 1   C43 
15  1 N 1 A LI1 301 ? C44 ? B LI1 1   C44 
16  1 N 1 A LI1 301 ? C45 ? B LI1 1   C45 
17  1 N 1 A LI1 301 ? C11 ? B LI1 1   C11 
18  1 N 1 A LI1 301 ? C12 ? B LI1 1   C12 
19  1 N 1 A LI1 301 ? C13 ? B LI1 1   C13 
20  1 N 1 A LI1 301 ? C14 ? B LI1 1   C14 
21  1 N 1 A LI1 301 ? C15 ? B LI1 1   C15 
22  1 N 1 A LI1 301 ? C16 ? B LI1 1   C16 
23  1 N 1 A LI1 301 ? C17 ? B LI1 1   C17 
24  1 N 1 A LI1 301 ? C18 ? B LI1 1   C18 
25  1 N 1 A LI1 301 ? C19 ? B LI1 1   C19 
26  1 N 1 A LI1 301 ? C20 ? B LI1 1   C20 
27  1 N 1 A LI1 301 ? C21 ? B LI1 1   C21 
28  1 N 1 A LI1 301 ? C22 ? B LI1 1   C22 
29  1 N 1 A LI1 301 ? C23 ? B LI1 1   C23 
30  1 N 1 A LI1 301 ? C24 ? B LI1 1   C24 
31  1 N 1 A LI1 301 ? C25 ? B LI1 1   C25 
32  1 N 1 A LI1 301 ? C26 ? B LI1 1   C26 
33  1 N 1 A LI1 301 ? C27 ? B LI1 1   C27 
34  1 N 1 A LI1 301 ? C28 ? B LI1 1   C28 
35  1 N 1 A LI1 301 ? C29 ? B LI1 1   C29 
36  1 N 1 A LI1 301 ? C30 ? B LI1 1   C30 
37  1 N 1 A LI1 302 ? C1  ? C LI1 1   C1  
38  1 N 1 A LI1 302 ? C2  ? C LI1 1   C2  
39  1 N 1 A LI1 302 ? C3  ? C LI1 1   C3  
40  1 N 1 A LI1 302 ? O1  ? C LI1 1   O1  
41  1 N 1 A LI1 302 ? O2  ? C LI1 1   O2  
42  1 N 1 A LI1 302 ? O3  ? C LI1 1   O3  
43  1 N 1 A LI1 302 ? C41 ? C LI1 1   C41 
44  1 N 1 A LI1 302 ? C42 ? C LI1 1   C42 
45  1 N 1 A LI1 302 ? C43 ? C LI1 1   C43 
46  1 N 1 A LI1 302 ? C44 ? C LI1 1   C44 
47  1 N 1 A LI1 302 ? C45 ? C LI1 1   C45 
48  1 N 1 A LI1 302 ? C46 ? C LI1 1   C46 
49  1 N 1 A LI1 302 ? C47 ? C LI1 1   C47 
50  1 N 1 A LI1 302 ? C48 ? C LI1 1   C48 
51  1 N 1 A LI1 302 ? C49 ? C LI1 1   C49 
52  1 N 1 A LI1 302 ? C59 ? C LI1 1   C59 
53  1 N 1 A LI1 302 ? C60 ? C LI1 1   C60 
54  1 N 1 A LI1 302 ? C11 ? C LI1 1   C11 
55  1 N 1 A LI1 302 ? C12 ? C LI1 1   C12 
56  1 N 1 A LI1 302 ? C13 ? C LI1 1   C13 
57  1 N 1 A LI1 302 ? C14 ? C LI1 1   C14 
58  1 N 1 A LI1 302 ? C15 ? C LI1 1   C15 
59  1 N 1 A LI1 302 ? C16 ? C LI1 1   C16 
60  1 N 1 A LI1 302 ? C17 ? C LI1 1   C17 
61  1 N 1 A LI1 302 ? C18 ? C LI1 1   C18 
62  1 N 1 A LI1 302 ? C19 ? C LI1 1   C19 
63  1 N 1 A LI1 302 ? C20 ? C LI1 1   C20 
64  1 N 1 A LI1 302 ? C21 ? C LI1 1   C21 
65  1 N 1 A LI1 302 ? C22 ? C LI1 1   C22 
66  1 N 1 A LI1 302 ? C23 ? C LI1 1   C23 
67  1 N 1 A LI1 302 ? C24 ? C LI1 1   C24 
68  1 N 1 A LI1 302 ? C25 ? C LI1 1   C25 
69  1 N 1 A LI1 302 ? C26 ? C LI1 1   C26 
70  1 N 1 A LI1 302 ? C27 ? C LI1 1   C27 
71  1 N 1 A LI1 302 ? C28 ? C LI1 1   C28 
72  1 N 1 A LI1 302 ? C29 ? C LI1 1   C29 
73  1 N 1 A LI1 302 ? C30 ? C LI1 1   C30 
74  1 N 1 A LI1 303 ? C1  ? D LI1 1   C1  
75  1 N 1 A LI1 303 ? C2  ? D LI1 1   C2  
76  1 N 1 A LI1 303 ? C3  ? D LI1 1   C3  
77  1 N 1 A LI1 303 ? O1  ? D LI1 1   O1  
78  1 N 1 A LI1 303 ? O2  ? D LI1 1   O2  
79  1 N 1 A LI1 303 ? O3  ? D LI1 1   O3  
80  1 N 1 A LI1 303 ? C41 ? D LI1 1   C41 
81  1 N 1 A LI1 303 ? C42 ? D LI1 1   C42 
82  1 N 1 A LI1 303 ? C43 ? D LI1 1   C43 
83  1 N 1 A LI1 303 ? C44 ? D LI1 1   C44 
84  1 N 1 A LI1 303 ? C49 ? D LI1 1   C49 
85  1 N 1 A LI1 303 ? C59 ? D LI1 1   C59 
86  1 N 1 A LI1 303 ? C60 ? D LI1 1   C60 
87  1 N 1 A LI1 303 ? C11 ? D LI1 1   C11 
88  1 N 1 A LI1 303 ? C12 ? D LI1 1   C12 
89  1 N 1 A LI1 303 ? C13 ? D LI1 1   C13 
90  1 N 1 A LI1 303 ? C14 ? D LI1 1   C14 
91  1 N 1 A LI1 303 ? C15 ? D LI1 1   C15 
92  1 N 1 A LI1 303 ? C16 ? D LI1 1   C16 
93  1 N 1 A LI1 303 ? C17 ? D LI1 1   C17 
94  1 N 1 A LI1 303 ? C18 ? D LI1 1   C18 
95  1 N 1 A LI1 303 ? C19 ? D LI1 1   C19 
96  1 N 1 A LI1 303 ? C20 ? D LI1 1   C20 
97  1 N 1 A LI1 303 ? C21 ? D LI1 1   C21 
98  1 N 1 A LI1 303 ? C22 ? D LI1 1   C22 
99  1 N 1 A LI1 303 ? C23 ? D LI1 1   C23 
100 1 N 1 A LI1 303 ? C24 ? D LI1 1   C24 
101 1 N 1 A LI1 303 ? C25 ? D LI1 1   C25 
102 1 N 1 A LI1 303 ? C26 ? D LI1 1   C26 
103 1 N 1 A LI1 303 ? C27 ? D LI1 1   C27 
104 1 N 1 A LI1 303 ? C28 ? D LI1 1   C28 
105 1 N 1 A LI1 303 ? C29 ? D LI1 1   C29 
106 1 N 1 A LI1 303 ? C30 ? D LI1 1   C30 
107 1 N 1 A LI1 304 ? C1  ? E LI1 1   C1  
108 1 N 1 A LI1 304 ? C2  ? E LI1 1   C2  
109 1 N 1 A LI1 304 ? C3  ? E LI1 1   C3  
110 1 N 1 A LI1 304 ? O1  ? E LI1 1   O1  
111 1 N 1 A LI1 304 ? O2  ? E LI1 1   O2  
112 1 N 1 A LI1 304 ? O3  ? E LI1 1   O3  
113 1 N 1 A LI1 304 ? C41 ? E LI1 1   C41 
114 1 N 1 A LI1 304 ? C42 ? E LI1 1   C42 
115 1 N 1 A LI1 304 ? C43 ? E LI1 1   C43 
116 1 N 1 A LI1 304 ? C44 ? E LI1 1   C44 
117 1 N 1 A LI1 304 ? C49 ? E LI1 1   C49 
118 1 N 1 A LI1 304 ? C60 ? E LI1 1   C60 
119 1 N 1 A LI1 304 ? C11 ? E LI1 1   C11 
120 1 N 1 A LI1 304 ? C12 ? E LI1 1   C12 
121 1 N 1 A LI1 304 ? C13 ? E LI1 1   C13 
122 1 N 1 A LI1 304 ? C14 ? E LI1 1   C14 
123 1 N 1 A LI1 304 ? C15 ? E LI1 1   C15 
124 1 N 1 A LI1 304 ? C16 ? E LI1 1   C16 
125 1 N 1 A LI1 304 ? C17 ? E LI1 1   C17 
126 1 N 1 A LI1 304 ? C18 ? E LI1 1   C18 
127 1 N 1 A LI1 304 ? C19 ? E LI1 1   C19 
128 1 N 1 A LI1 304 ? C20 ? E LI1 1   C20 
129 1 N 1 A LI1 304 ? C21 ? E LI1 1   C21 
130 1 N 1 A LI1 304 ? C22 ? E LI1 1   C22 
131 1 N 1 A LI1 304 ? C23 ? E LI1 1   C23 
132 1 N 1 A LI1 304 ? C24 ? E LI1 1   C24 
133 1 N 1 A LI1 304 ? C25 ? E LI1 1   C25 
134 1 N 1 A LI1 304 ? C26 ? E LI1 1   C26 
135 1 N 1 A LI1 304 ? C27 ? E LI1 1   C27 
136 1 N 1 A LI1 304 ? C28 ? E LI1 1   C28 
137 1 N 1 A LI1 304 ? C29 ? E LI1 1   C29 
138 1 N 1 A LI1 304 ? C30 ? E LI1 1   C30 
139 1 N 1 A LI1 305 ? C1  ? F LI1 1   C1  
140 1 N 1 A LI1 305 ? C2  ? F LI1 1   C2  
141 1 N 1 A LI1 305 ? C3  ? F LI1 1   C3  
142 1 N 1 A LI1 305 ? O1  ? F LI1 1   O1  
143 1 N 1 A LI1 305 ? O2  ? F LI1 1   O2  
144 1 N 1 A LI1 305 ? O3  ? F LI1 1   O3  
145 1 N 1 A LI1 305 ? C41 ? F LI1 1   C41 
146 1 N 1 A LI1 305 ? C42 ? F LI1 1   C42 
147 1 N 1 A LI1 305 ? C43 ? F LI1 1   C43 
148 1 N 1 A LI1 305 ? C44 ? F LI1 1   C44 
149 1 N 1 A LI1 305 ? C45 ? F LI1 1   C45 
150 1 N 1 A LI1 305 ? C49 ? F LI1 1   C49 
151 1 N 1 A LI1 305 ? C11 ? F LI1 1   C11 
152 1 N 1 A LI1 305 ? C12 ? F LI1 1   C12 
153 1 N 1 A LI1 305 ? C13 ? F LI1 1   C13 
154 1 N 1 A LI1 305 ? C14 ? F LI1 1   C14 
155 1 N 1 A LI1 305 ? C15 ? F LI1 1   C15 
156 1 N 1 A LI1 305 ? C16 ? F LI1 1   C16 
157 1 N 1 A LI1 305 ? C17 ? F LI1 1   C17 
158 1 N 1 A LI1 305 ? C18 ? F LI1 1   C18 
159 1 N 1 A LI1 305 ? C19 ? F LI1 1   C19 
160 1 N 1 A LI1 305 ? C20 ? F LI1 1   C20 
161 1 N 1 A LI1 305 ? C21 ? F LI1 1   C21 
162 1 N 1 A LI1 305 ? C22 ? F LI1 1   C22 
163 1 N 1 A LI1 305 ? C23 ? F LI1 1   C23 
164 1 N 1 A LI1 305 ? C24 ? F LI1 1   C24 
165 1 N 1 A LI1 305 ? C25 ? F LI1 1   C25 
166 1 N 1 A LI1 305 ? C26 ? F LI1 1   C26 
167 1 N 1 A LI1 305 ? C27 ? F LI1 1   C27 
168 1 N 1 A LI1 305 ? C28 ? F LI1 1   C28 
169 1 N 1 A LI1 305 ? C29 ? F LI1 1   C29 
170 1 N 1 A LI1 305 ? C30 ? F LI1 1   C30 
171 1 N 1 A LI1 310 ? C1  ? K LI1 1   C1  
172 1 N 1 A LI1 310 ? C2  ? K LI1 1   C2  
173 1 N 1 A LI1 310 ? C3  ? K LI1 1   C3  
174 1 N 1 A LI1 310 ? O1  ? K LI1 1   O1  
175 1 N 1 A LI1 310 ? O2  ? K LI1 1   O2  
176 1 N 1 A LI1 310 ? O3  ? K LI1 1   O3  
177 1 N 1 A LI1 310 ? C41 ? K LI1 1   C41 
178 1 N 1 A LI1 310 ? C42 ? K LI1 1   C42 
179 1 N 1 A LI1 310 ? C43 ? K LI1 1   C43 
180 1 N 1 A LI1 310 ? C44 ? K LI1 1   C44 
181 1 N 1 A LI1 310 ? C45 ? K LI1 1   C45 
182 1 N 1 A LI1 310 ? C11 ? K LI1 1   C11 
183 1 N 1 A LI1 310 ? C12 ? K LI1 1   C12 
184 1 N 1 A LI1 310 ? C13 ? K LI1 1   C13 
185 1 N 1 A LI1 310 ? C14 ? K LI1 1   C14 
186 1 N 1 A LI1 310 ? C15 ? K LI1 1   C15 
187 1 N 1 A LI1 310 ? C16 ? K LI1 1   C16 
188 1 N 1 A LI1 310 ? C17 ? K LI1 1   C17 
189 1 N 1 A LI1 310 ? C18 ? K LI1 1   C18 
190 1 N 1 A LI1 310 ? C19 ? K LI1 1   C19 
191 1 N 1 A LI1 310 ? C20 ? K LI1 1   C20 
192 1 N 1 A LI1 310 ? C21 ? K LI1 1   C21 
193 1 N 1 A LI1 310 ? C22 ? K LI1 1   C22 
194 1 N 1 A LI1 310 ? C23 ? K LI1 1   C23 
195 1 N 1 A LI1 310 ? C24 ? K LI1 1   C24 
196 1 N 1 A LI1 310 ? C25 ? K LI1 1   C25 
197 1 N 1 A LI1 310 ? C26 ? K LI1 1   C26 
198 1 N 1 A LI1 310 ? C27 ? K LI1 1   C27 
199 1 N 1 A LI1 310 ? C28 ? K LI1 1   C28 
200 1 N 1 A LI1 310 ? C29 ? K LI1 1   C29 
201 1 N 1 A LI1 310 ? C30 ? K LI1 1   C30 
202 1 N 1 A LI1 311 ? C1  ? L LI1 1   C1  
203 1 N 1 A LI1 311 ? C2  ? L LI1 1   C2  
204 1 N 1 A LI1 311 ? C3  ? L LI1 1   C3  
205 1 N 1 A LI1 311 ? O1  ? L LI1 1   O1  
206 1 N 1 A LI1 311 ? O2  ? L LI1 1   O2  
207 1 N 1 A LI1 311 ? O3  ? L LI1 1   O3  
208 1 N 1 A LI1 311 ? C41 ? L LI1 1   C41 
209 1 N 1 A LI1 311 ? C42 ? L LI1 1   C42 
210 1 N 1 A LI1 311 ? C43 ? L LI1 1   C43 
211 1 N 1 A LI1 311 ? C44 ? L LI1 1   C44 
212 1 N 1 A LI1 311 ? C45 ? L LI1 1   C45 
213 1 N 1 A LI1 311 ? C46 ? L LI1 1   C46 
214 1 N 1 A LI1 311 ? C47 ? L LI1 1   C47 
215 1 N 1 A LI1 311 ? C48 ? L LI1 1   C48 
216 1 N 1 A LI1 311 ? C49 ? L LI1 1   C49 
217 1 N 1 A LI1 311 ? C59 ? L LI1 1   C59 
218 1 N 1 A LI1 311 ? C60 ? L LI1 1   C60 
219 1 N 1 A LI1 311 ? C11 ? L LI1 1   C11 
220 1 N 1 A LI1 311 ? C12 ? L LI1 1   C12 
221 1 N 1 A LI1 311 ? C13 ? L LI1 1   C13 
222 1 N 1 A LI1 311 ? C14 ? L LI1 1   C14 
223 1 N 1 A LI1 311 ? C15 ? L LI1 1   C15 
224 1 N 1 A LI1 311 ? C16 ? L LI1 1   C16 
225 1 N 1 A LI1 311 ? C17 ? L LI1 1   C17 
226 1 N 1 A LI1 311 ? C18 ? L LI1 1   C18 
227 1 N 1 A LI1 311 ? C19 ? L LI1 1   C19 
228 1 N 1 A LI1 311 ? C20 ? L LI1 1   C20 
229 1 N 1 A LI1 311 ? C21 ? L LI1 1   C21 
230 1 N 1 A LI1 311 ? C22 ? L LI1 1   C22 
231 1 N 1 A LI1 311 ? C23 ? L LI1 1   C23 
232 1 N 1 A LI1 311 ? C24 ? L LI1 1   C24 
233 1 N 1 A LI1 311 ? C25 ? L LI1 1   C25 
234 1 N 1 A LI1 311 ? C26 ? L LI1 1   C26 
235 1 N 1 A LI1 311 ? C27 ? L LI1 1   C27 
236 1 N 1 A LI1 311 ? C28 ? L LI1 1   C28 
237 1 N 1 A LI1 311 ? C29 ? L LI1 1   C29 
238 1 N 1 A LI1 311 ? C30 ? L LI1 1   C30 
239 1 N 1 A LI1 312 ? C1  ? M LI1 1   C1  
240 1 N 1 A LI1 312 ? C2  ? M LI1 1   C2  
241 1 N 1 A LI1 312 ? C3  ? M LI1 1   C3  
242 1 N 1 A LI1 312 ? O1  ? M LI1 1   O1  
243 1 N 1 A LI1 312 ? O2  ? M LI1 1   O2  
244 1 N 1 A LI1 312 ? O3  ? M LI1 1   O3  
245 1 N 1 A LI1 312 ? C41 ? M LI1 1   C41 
246 1 N 1 A LI1 312 ? C42 ? M LI1 1   C42 
247 1 N 1 A LI1 312 ? C43 ? M LI1 1   C43 
248 1 N 1 A LI1 312 ? C44 ? M LI1 1   C44 
249 1 N 1 A LI1 312 ? C49 ? M LI1 1   C49 
250 1 N 1 A LI1 312 ? C57 ? M LI1 1   C57 
251 1 N 1 A LI1 312 ? C58 ? M LI1 1   C58 
252 1 N 1 A LI1 312 ? C59 ? M LI1 1   C59 
253 1 N 1 A LI1 312 ? C60 ? M LI1 1   C60 
254 1 N 1 A LI1 312 ? C11 ? M LI1 1   C11 
255 1 N 1 A LI1 312 ? C12 ? M LI1 1   C12 
256 1 N 1 A LI1 312 ? C13 ? M LI1 1   C13 
257 1 N 1 A LI1 312 ? C14 ? M LI1 1   C14 
258 1 N 1 A LI1 312 ? C15 ? M LI1 1   C15 
259 1 N 1 A LI1 312 ? C16 ? M LI1 1   C16 
260 1 N 1 A LI1 312 ? C17 ? M LI1 1   C17 
261 1 N 1 A LI1 312 ? C18 ? M LI1 1   C18 
262 1 N 1 A LI1 312 ? C19 ? M LI1 1   C19 
263 1 N 1 A LI1 312 ? C20 ? M LI1 1   C20 
264 1 N 1 A LI1 312 ? C21 ? M LI1 1   C21 
265 1 N 1 A LI1 312 ? C22 ? M LI1 1   C22 
266 1 N 1 A LI1 312 ? C23 ? M LI1 1   C23 
267 1 N 1 A LI1 312 ? C24 ? M LI1 1   C24 
268 1 N 1 A LI1 312 ? C25 ? M LI1 1   C25 
269 1 N 1 A LI1 312 ? C26 ? M LI1 1   C26 
270 1 N 1 A LI1 312 ? C27 ? M LI1 1   C27 
271 1 N 1 A LI1 312 ? C28 ? M LI1 1   C28 
272 1 N 1 A LI1 312 ? C29 ? M LI1 1   C29 
273 1 N 1 A LI1 312 ? C30 ? M LI1 1   C30 
274 1 N 1 A LI1 313 ? C1  ? N LI1 1   C1  
275 1 N 1 A LI1 313 ? C2  ? N LI1 1   C2  
276 1 N 1 A LI1 313 ? C3  ? N LI1 1   C3  
277 1 N 1 A LI1 313 ? O1  ? N LI1 1   O1  
278 1 N 1 A LI1 313 ? O2  ? N LI1 1   O2  
279 1 N 1 A LI1 313 ? O3  ? N LI1 1   O3  
280 1 N 1 A LI1 313 ? C41 ? N LI1 1   C41 
281 1 N 1 A LI1 313 ? C42 ? N LI1 1   C42 
282 1 N 1 A LI1 313 ? C43 ? N LI1 1   C43 
283 1 N 1 A LI1 313 ? C44 ? N LI1 1   C44 
284 1 N 1 A LI1 313 ? C49 ? N LI1 1   C49 
285 1 N 1 A LI1 313 ? C60 ? N LI1 1   C60 
286 1 N 1 A LI1 313 ? C11 ? N LI1 1   C11 
287 1 N 1 A LI1 313 ? C12 ? N LI1 1   C12 
288 1 N 1 A LI1 313 ? C13 ? N LI1 1   C13 
289 1 N 1 A LI1 313 ? C14 ? N LI1 1   C14 
290 1 N 1 A LI1 313 ? C15 ? N LI1 1   C15 
291 1 N 1 A LI1 313 ? C16 ? N LI1 1   C16 
292 1 N 1 A LI1 313 ? C17 ? N LI1 1   C17 
293 1 N 1 A LI1 313 ? C18 ? N LI1 1   C18 
294 1 N 1 A LI1 313 ? C19 ? N LI1 1   C19 
295 1 N 1 A LI1 313 ? C20 ? N LI1 1   C20 
296 1 N 1 A LI1 313 ? C21 ? N LI1 1   C21 
297 1 N 1 A LI1 313 ? C22 ? N LI1 1   C22 
298 1 N 1 A LI1 313 ? C23 ? N LI1 1   C23 
299 1 N 1 A LI1 313 ? C24 ? N LI1 1   C24 
300 1 N 1 A LI1 313 ? C25 ? N LI1 1   C25 
301 1 N 1 A LI1 313 ? C26 ? N LI1 1   C26 
302 1 N 1 A LI1 313 ? C27 ? N LI1 1   C27 
303 1 N 1 A LI1 313 ? C28 ? N LI1 1   C28 
304 1 N 1 A LI1 313 ? C29 ? N LI1 1   C29 
305 1 N 1 A LI1 313 ? C30 ? N LI1 1   C30 
306 1 N 1 A LI1 314 ? C1  ? O LI1 1   C1  
307 1 N 1 A LI1 314 ? C2  ? O LI1 1   C2  
308 1 N 1 A LI1 314 ? C3  ? O LI1 1   C3  
309 1 N 1 A LI1 314 ? O1  ? O LI1 1   O1  
310 1 N 1 A LI1 314 ? O2  ? O LI1 1   O2  
311 1 N 1 A LI1 314 ? O3  ? O LI1 1   O3  
312 1 N 1 A LI1 314 ? C41 ? O LI1 1   C41 
313 1 N 1 A LI1 314 ? C42 ? O LI1 1   C42 
314 1 N 1 A LI1 314 ? C43 ? O LI1 1   C43 
315 1 N 1 A LI1 314 ? C44 ? O LI1 1   C44 
316 1 N 1 A LI1 314 ? C45 ? O LI1 1   C45 
317 1 N 1 A LI1 314 ? C46 ? O LI1 1   C46 
318 1 N 1 A LI1 314 ? C47 ? O LI1 1   C47 
319 1 N 1 A LI1 314 ? C48 ? O LI1 1   C48 
320 1 N 1 A LI1 314 ? C49 ? O LI1 1   C49 
321 1 N 1 A LI1 314 ? C59 ? O LI1 1   C59 
322 1 N 1 A LI1 314 ? C60 ? O LI1 1   C60 
323 1 N 1 A LI1 314 ? C11 ? O LI1 1   C11 
324 1 N 1 A LI1 314 ? C12 ? O LI1 1   C12 
325 1 N 1 A LI1 314 ? C13 ? O LI1 1   C13 
326 1 N 1 A LI1 314 ? C14 ? O LI1 1   C14 
327 1 N 1 A LI1 314 ? C15 ? O LI1 1   C15 
328 1 N 1 A LI1 314 ? C16 ? O LI1 1   C16 
329 1 N 1 A LI1 314 ? C17 ? O LI1 1   C17 
330 1 N 1 A LI1 314 ? C18 ? O LI1 1   C18 
331 1 N 1 A LI1 314 ? C19 ? O LI1 1   C19 
332 1 N 1 A LI1 314 ? C20 ? O LI1 1   C20 
333 1 N 1 A LI1 314 ? C21 ? O LI1 1   C21 
334 1 N 1 A LI1 314 ? C22 ? O LI1 1   C22 
335 1 N 1 A LI1 314 ? C23 ? O LI1 1   C23 
336 1 N 1 A LI1 314 ? C24 ? O LI1 1   C24 
337 1 N 1 A LI1 314 ? C25 ? O LI1 1   C25 
338 1 N 1 A LI1 314 ? C26 ? O LI1 1   C26 
339 1 N 1 A LI1 314 ? C27 ? O LI1 1   C27 
340 1 N 1 A LI1 314 ? C28 ? O LI1 1   C28 
341 1 N 1 A LI1 314 ? C29 ? O LI1 1   C29 
342 1 N 1 A LI1 314 ? C30 ? O LI1 1   C30 
343 1 N 1 A LI1 315 ? C1  ? P LI1 1   C1  
344 1 N 1 A LI1 315 ? C2  ? P LI1 1   C2  
345 1 N 1 A LI1 315 ? C3  ? P LI1 1   C3  
346 1 N 1 A LI1 315 ? O1  ? P LI1 1   O1  
347 1 N 1 A LI1 315 ? O2  ? P LI1 1   O2  
348 1 N 1 A LI1 315 ? O3  ? P LI1 1   O3  
349 1 N 1 A LI1 315 ? C41 ? P LI1 1   C41 
350 1 N 1 A LI1 315 ? C42 ? P LI1 1   C42 
351 1 N 1 A LI1 315 ? C43 ? P LI1 1   C43 
352 1 N 1 A LI1 315 ? C44 ? P LI1 1   C44 
353 1 N 1 A LI1 315 ? C49 ? P LI1 1   C49 
354 1 N 1 A LI1 315 ? C60 ? P LI1 1   C60 
355 1 N 1 A LI1 315 ? C11 ? P LI1 1   C11 
356 1 N 1 A LI1 315 ? C12 ? P LI1 1   C12 
357 1 N 1 A LI1 315 ? C13 ? P LI1 1   C13 
358 1 N 1 A LI1 315 ? C14 ? P LI1 1   C14 
359 1 N 1 A LI1 315 ? C15 ? P LI1 1   C15 
360 1 N 1 A LI1 315 ? C16 ? P LI1 1   C16 
361 1 N 1 A LI1 315 ? C17 ? P LI1 1   C17 
362 1 N 1 A LI1 315 ? C18 ? P LI1 1   C18 
363 1 N 1 A LI1 315 ? C19 ? P LI1 1   C19 
364 1 N 1 A LI1 315 ? C20 ? P LI1 1   C20 
365 1 N 1 A LI1 315 ? C21 ? P LI1 1   C21 
366 1 N 1 A LI1 315 ? C22 ? P LI1 1   C22 
367 1 N 1 A LI1 315 ? C23 ? P LI1 1   C23 
368 1 N 1 A LI1 315 ? C24 ? P LI1 1   C24 
369 1 N 1 A LI1 315 ? C25 ? P LI1 1   C25 
370 1 N 1 A LI1 315 ? C26 ? P LI1 1   C26 
371 1 N 1 A LI1 315 ? C27 ? P LI1 1   C27 
372 1 N 1 A LI1 315 ? C28 ? P LI1 1   C28 
373 1 N 1 A LI1 315 ? C29 ? P LI1 1   C29 
374 1 N 1 A LI1 315 ? C30 ? P LI1 1   C30 
375 1 N 1 A LI1 316 ? C1  ? Q LI1 1   C1  
376 1 N 1 A LI1 316 ? C2  ? Q LI1 1   C2  
377 1 N 1 A LI1 316 ? C3  ? Q LI1 1   C3  
378 1 N 1 A LI1 316 ? O1  ? Q LI1 1   O1  
379 1 N 1 A LI1 316 ? O2  ? Q LI1 1   O2  
380 1 N 1 A LI1 316 ? O3  ? Q LI1 1   O3  
381 1 N 1 A LI1 316 ? C41 ? Q LI1 1   C41 
382 1 N 1 A LI1 316 ? C42 ? Q LI1 1   C42 
383 1 N 1 A LI1 316 ? C43 ? Q LI1 1   C43 
384 1 N 1 A LI1 316 ? C44 ? Q LI1 1   C44 
385 1 N 1 A LI1 316 ? C45 ? Q LI1 1   C45 
386 1 N 1 A LI1 316 ? C49 ? Q LI1 1   C49 
387 1 N 1 A LI1 316 ? C11 ? Q LI1 1   C11 
388 1 N 1 A LI1 316 ? C12 ? Q LI1 1   C12 
389 1 N 1 A LI1 316 ? C13 ? Q LI1 1   C13 
390 1 N 1 A LI1 316 ? C14 ? Q LI1 1   C14 
391 1 N 1 A LI1 316 ? C15 ? Q LI1 1   C15 
392 1 N 1 A LI1 316 ? C16 ? Q LI1 1   C16 
393 1 N 1 A LI1 316 ? C17 ? Q LI1 1   C17 
394 1 N 1 A LI1 316 ? C18 ? Q LI1 1   C18 
395 1 N 1 A LI1 316 ? C19 ? Q LI1 1   C19 
396 1 N 1 A LI1 316 ? C20 ? Q LI1 1   C20 
397 1 N 1 A LI1 316 ? C21 ? Q LI1 1   C21 
398 1 N 1 A LI1 316 ? C22 ? Q LI1 1   C22 
399 1 N 1 A LI1 316 ? C23 ? Q LI1 1   C23 
400 1 N 1 A LI1 316 ? C24 ? Q LI1 1   C24 
401 1 N 1 A LI1 316 ? C25 ? Q LI1 1   C25 
402 1 N 1 A LI1 316 ? C26 ? Q LI1 1   C26 
403 1 N 1 A LI1 316 ? C27 ? Q LI1 1   C27 
404 1 N 1 A LI1 316 ? C28 ? Q LI1 1   C28 
405 1 N 1 A LI1 316 ? C29 ? Q LI1 1   C29 
406 1 N 1 A LI1 316 ? C30 ? Q LI1 1   C30 
407 1 N 1 A LI1 317 ? C1  ? R LI1 1   C1  
408 1 N 1 A LI1 317 ? C2  ? R LI1 1   C2  
409 1 N 1 A LI1 317 ? C3  ? R LI1 1   C3  
410 1 N 1 A LI1 317 ? O1  ? R LI1 1   O1  
411 1 N 1 A LI1 317 ? O2  ? R LI1 1   O2  
412 1 N 1 A LI1 317 ? O3  ? R LI1 1   O3  
413 1 N 1 A LI1 317 ? C41 ? R LI1 1   C41 
414 1 N 1 A LI1 317 ? C42 ? R LI1 1   C42 
415 1 N 1 A LI1 317 ? C43 ? R LI1 1   C43 
416 1 N 1 A LI1 317 ? C44 ? R LI1 1   C44 
417 1 N 1 A LI1 317 ? C45 ? R LI1 1   C45 
418 1 N 1 A LI1 317 ? C46 ? R LI1 1   C46 
419 1 N 1 A LI1 317 ? C47 ? R LI1 1   C47 
420 1 N 1 A LI1 317 ? C48 ? R LI1 1   C48 
421 1 N 1 A LI1 317 ? C49 ? R LI1 1   C49 
422 1 N 1 A LI1 317 ? C50 ? R LI1 1   C50 
423 1 N 1 A LI1 317 ? C51 ? R LI1 1   C51 
424 1 N 1 A LI1 317 ? C59 ? R LI1 1   C59 
425 1 N 1 A LI1 317 ? C60 ? R LI1 1   C60 
426 1 N 1 A LI1 317 ? C11 ? R LI1 1   C11 
427 1 N 1 A LI1 317 ? C12 ? R LI1 1   C12 
428 1 N 1 A LI1 317 ? C13 ? R LI1 1   C13 
429 1 N 1 A LI1 317 ? C14 ? R LI1 1   C14 
430 1 N 1 A LI1 317 ? C15 ? R LI1 1   C15 
431 1 N 1 A LI1 317 ? C16 ? R LI1 1   C16 
432 1 N 1 A LI1 317 ? C17 ? R LI1 1   C17 
433 1 N 1 A LI1 317 ? C18 ? R LI1 1   C18 
434 1 N 1 A LI1 317 ? C19 ? R LI1 1   C19 
435 1 N 1 A LI1 317 ? C20 ? R LI1 1   C20 
436 1 N 1 A LI1 317 ? C21 ? R LI1 1   C21 
437 1 N 1 A LI1 317 ? C22 ? R LI1 1   C22 
438 1 N 1 A LI1 317 ? C23 ? R LI1 1   C23 
439 1 N 1 A LI1 317 ? C24 ? R LI1 1   C24 
440 1 N 1 A LI1 317 ? C25 ? R LI1 1   C25 
441 1 N 1 A LI1 317 ? C26 ? R LI1 1   C26 
442 1 N 1 A LI1 317 ? C27 ? R LI1 1   C27 
443 1 N 1 A LI1 317 ? C28 ? R LI1 1   C28 
444 1 N 1 A LI1 317 ? C29 ? R LI1 1   C29 
445 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                     9F9C 
_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                         9F9C 
_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                   9F9C 
_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    '0.1M Na/K phosphate pH5.4, 30% PEG 2000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     293 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     CCD 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         MPCCD 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2016-02-04 
_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   1.63 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      'FREE ELECTRON LASER' 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SACLA BEAMLINE BL3' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.63 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL3 
_diffrn_source.pdbx_synchrotron_site       SACLA 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9F9C 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.95 
_reflns.d_resolution_low                               38.92 
_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                                     18140 
_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                                369 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          12.5 
_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                                   0.0632 
_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                                    1.95 
_reflns_shell.d_res_low                                     2.00 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.111 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1820 
_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                               64 
_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                                  0.825 
_reflns_shell.pdbx_R_split                                  0.7803 
_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                                 9F9C 
_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                            2.00 
_refine.ls_d_res_low                             15.74 
_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                     16509 
_refine.ls_number_reflns_R_free                  1653 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    97.50 
_refine.ls_percent_reflns_R_free                 10.01 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2167 
_refine.ls_R_factor_R_free                       0.2591 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2120 
_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                          0.00 
_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                 32.49 
_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                            0.40 
_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        1799 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         245 
_refine_hist.number_atoms_solvent             35 
_refine_hist.number_atoms_total               2079 
_refine_hist.d_res_high                       2.00 
_refine_hist.d_res_low                        15.74 
# 
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' ? 0.002  ? 2122 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.792  ? 2821 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 15.023 ? 813  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.035  ? 309  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.011  ? 331  ? 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' 2.00 2.06  . . 125 1143 90.00  . . . . 0.5700 . . . . . . . . . . . 0.6615 
'X-RAY DIFFRACTION' 2.06 2.12  . . 132 1189 96.00  . . . . 0.4621 . . . . . . . . . . . 0.4750 
'X-RAY DIFFRACTION' 2.13 2.20  . . 142 1237 97.00  . . . . 0.3254 . . . . . . . . . . . 0.3500 
'X-RAY DIFFRACTION' 2.20 2.29  . . 136 1242 98.00  . . . . 0.2725 . . . . . . . . . . . 0.3180 
'X-RAY DIFFRACTION' 2.29 2.39  . . 137 1242 98.00  . . . . 0.2160 . . . . . . . . . . . 0.2826 
'X-RAY DIFFRACTION' 2.39 2.52  . . 141 1259 98.00  . . . . 0.1997 . . . . . . . . . . . 0.2059 
'X-RAY DIFFRACTION' 2.52 2.68  . . 131 1236 98.00  . . . . 0.1785 . . . . . . . . . . . 0.2656 
'X-RAY DIFFRACTION' 2.68 2.88  . . 140 1243 98.00  . . . . 0.1703 . . . . . . . . . . . 0.2332 
'X-RAY DIFFRACTION' 2.88 3.17  . . 140 1255 99.00  . . . . 0.1658 . . . . . . . . . . . 0.2134 
'X-RAY DIFFRACTION' 3.17 3.62  . . 143 1250 99.00  . . . . 0.1667 . . . . . . . . . . . 0.2120 
'X-RAY DIFFRACTION' 3.62 4.54  . . 144 1281 100.00 . . . . 0.1543 . . . . . . . . . . . 0.2070 
'X-RAY DIFFRACTION' 4.55 15.74 . . 142 1279 99.00  . . . . 0.1836 . . . . . . . . . . . 0.2151 
# 
_struct.entry_id                     9F9C 
_struct.title                        
'Laser excitation effects on BR: Reprocessed Extrapolated 16 ns Light dataset recorded at 0.04 GW/cm2 from Nango et al.' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        9F9C 
_struct_keywords.text            
'Bacteriorhodospin, Proton transport, Membrane, RETINAL, TIME-RESOLVED CRYSTALLOGRAPHY, SERIAL CRYSTALLOGRAPHY, Laser excitation' 
_struct_keywords.pdbx_keywords   'PROTON TRANSPORT' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 2 ? 
D N N 2 ? 
E N N 2 ? 
F N N 2 ? 
G N N 3 ? 
H N N 3 ? 
I N N 3 ? 
J N N 3 ? 
K N N 2 ? 
L N N 2 ? 
M N N 2 ? 
N N N 2 ? 
O N N 2 ? 
P N N 2 ? 
Q N N 2 ? 
R N N 2 ? 
S N N 4 ? 
T N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    BACR_HALSA 
_struct_ref.pdbx_db_accession          P02945 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;TGRPEWIWLALGTALMGLGTLYFLVKGMGVSDPDAKKFYAITTLVPAIAFTMYLSMLLGYGLTMVPFGGEQNPIYWARYA
DWLFTTPLLLLDLALLVDADQGTILALVGADGIMIGTGLVGALTKVYSYRFVWWAISTAAMLYILYVLFFGFTSKAESMR
PEVASTFKVLRNVTVVLWSAYPVVWLIGSEGAGIVPLNIETLLFMVLDVSAKVGFGLILLRSRAIFGEAE
;
_struct_ref.pdbx_align_begin           18 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9F9C 
_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             9F9C 
_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)' 3950  ? 
1 MORE         -58   ? 
1 'SSA (A^2)'  12510 ? 
# 
_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 ? PHE A 151 ? VAL A 130 PHE A 154 1 ? 25 
HELX_P HELX_P6 AA6 PHE A 153 ? GLU A 158 ? PHE A 156 GLU A 161 1 ? 6  
HELX_P HELX_P7 AA7 ARG A 161 ? GLY A 189 ? ARG A 164 GLY A 192 1 ? 29 
HELX_P HELX_P8 AA8 PRO A 197 ? ARG A 222 ? PRO A 200 ARG A 225 1 ? 26 
HELX_P HELX_P9 AA9 SER A 223 ? PHE A 227 ? SER A 226 PHE A 230 5 ? 5  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_conn.id                            covale1 
_struct_conn.conn_type_id                  covale 
_struct_conn.pdbx_leaving_atom_flag        one 
_struct_conn.pdbx_PDB_id                   ? 
_struct_conn.ptnr1_label_asym_id           A 
_struct_conn.ptnr1_label_comp_id           LYS 
_struct_conn.ptnr1_label_seq_id            213 
_struct_conn.ptnr1_label_atom_id           NZ 
_struct_conn.pdbx_ptnr1_label_alt_id       ? 
_struct_conn.pdbx_ptnr1_PDB_ins_code       ? 
_struct_conn.pdbx_ptnr1_standard_comp_id   ? 
_struct_conn.ptnr1_symmetry                1_555 
_struct_conn.ptnr2_label_asym_id           S 
_struct_conn.ptnr2_label_comp_id           RET 
_struct_conn.ptnr2_label_seq_id            . 
_struct_conn.ptnr2_label_atom_id           C15 
_struct_conn.pdbx_ptnr2_label_alt_id       ? 
_struct_conn.pdbx_ptnr2_PDB_ins_code       ? 
_struct_conn.ptnr1_auth_asym_id            A 
_struct_conn.ptnr1_auth_comp_id            LYS 
_struct_conn.ptnr1_auth_seq_id             216 
_struct_conn.ptnr2_auth_asym_id            A 
_struct_conn.ptnr2_auth_comp_id            RET 
_struct_conn.ptnr2_auth_seq_id             318 
_struct_conn.ptnr2_symmetry                1_555 
_struct_conn.pdbx_ptnr3_label_atom_id      ? 
_struct_conn.pdbx_ptnr3_label_seq_id       ? 
_struct_conn.pdbx_ptnr3_label_comp_id      ? 
_struct_conn.pdbx_ptnr3_label_asym_id      ? 
_struct_conn.pdbx_ptnr3_label_alt_id       ? 
_struct_conn.pdbx_ptnr3_PDB_ins_code       ? 
_struct_conn.details                       ? 
_struct_conn.pdbx_dist_value               1.336 
_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 LEU A 63 ? PHE A 68 ? LEU A 66 PHE A 71 
AA1 2 GLU A 71 ? TYR A 76 ? GLU A 74 TYR A 79 
# 
_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                   9F9C 
_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 
# 
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 22.4601 26.5137 33.6758 0.1289 ? 0.0311  ? -0.0192 ? 0.1049 ? 0.0090  ? 0.2554 ? 3.4813 ? 0.5020  
? -1.9650 ? 3.4646 ? -2.0886 ? 6.5917 ? -0.0095 ? -0.0704 ? -0.2586 ? 0.0984  ? -0.1376 ? -0.3250 ? 0.4313  ? 0.5556  ? 0.0602  ? 
2 'X-RAY DIFFRACTION' ? refined 11.9840 37.9840 34.7086 0.1149 ? -0.0184 ? -0.0211 ? 0.1327 ? 0.0209  ? 0.1859 ? 1.3374 ? -0.3262 
? -0.2248 ? 1.8478 ? 0.5662  ? 0.5411 ? -0.0241 ? -0.0756 ? -0.0203 ? -0.0464 ? 0.0263  ? 0.0191  ? 0.0307  ? 0.0067  ? -0.0060 ? 
3 'X-RAY DIFFRACTION' ? refined 12.5447 53.2431 31.2373 0.1360 ? -0.0291 ? -0.0007 ? 0.0611 ? 0.0146  ? 0.1791 ? 4.0753 ? -0.2359 
? 1.4171  ? 2.5578 ? -0.9844 ? 6.3917 ? 0.0509  ? -0.0724 ? 0.2000  ? 0.1455  ? -0.0553 ? -0.2694 ? -0.2623 ? 0.0656  ? 0.0662  ? 
4 'X-RAY DIFFRACTION' ? refined 17.7228 46.9513 57.9320 0.5708 ? -0.0290 ? 0.0834  ? 0.7785 ? -0.0805 ? 0.4973 ? 8.2842 ? -7.3971 
? 6.6046  ? 6.8585 ? -5.4754 ? 5.9985 ? -0.8012 ? -1.0838 ? 0.1876  ? 1.2016  ? 0.8197  ? 0.5851  ? -1.1589 ? -0.4108 ? -0.0765 ? 
5 'X-RAY DIFFRACTION' ? refined 23.0207 42.3652 35.1730 0.1166 ? -0.0360 ? -0.0530 ? 0.1707 ? 0.0126  ? 0.2037 ? 1.0107 ? -0.0201 
? 0.1082  ? 1.1883 ? -0.4422 ? 2.2596 ? 0.0385  ? -0.0200 ? 0.0824  ? 0.0810  ? -0.0385 ? -0.2410 ? -0.1323 ? 0.3141  ? -0.0191 ? 
6 'X-RAY DIFFRACTION' ? refined 21.5746 30.9517 59.8706 0.5553 ? 0.0503  ? -0.0940 ? 0.4995 ? 0.1025  ? 0.2706 ? 2.9793 ? 0.9972  
? 0.3358  ? 3.3388 ? -2.7350 ? 2.7358 ? -0.2818 ? -0.6207 ? -0.3902 ? 0.4261  ? -0.2926 ? -0.4745 ? 1.3293  ? 1.3294  ? 0.6786  ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 4 through 36 )
;
2 'X-RAY DIFFRACTION' 2 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 37 through 127 )
;
3 'X-RAY DIFFRACTION' 3 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 128 through 154 )
;
4 'X-RAY DIFFRACTION' 4 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 155 through 164 )
;
5 'X-RAY DIFFRACTION' 5 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 165 through 224 )
;
6 'X-RAY DIFFRACTION' 6 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 225 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                    9F9C 
_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   ? 20.124 25.189 13.964 1.00 115.63 ? 4   ALA A N    1 
ATOM   2    C CA   . ALA A 1 1   ? 20.082 26.376 14.810 1.00 90.86  ? 4   ALA A CA   1 
ATOM   3    C C    . ALA A 1 1   ? 21.460 27.020 14.916 1.00 96.04  ? 4   ALA A C    1 
ATOM   4    O O    . ALA A 1 1   ? 21.612 28.089 15.507 1.00 85.13  ? 4   ALA A O    1 
ATOM   5    C CB   . ALA A 1 1   ? 19.552 26.023 16.192 1.00 87.52  ? 4   ALA A CB   1 
ATOM   6    N N    . THR A 1 2   ? 22.463 26.362 14.337 1.00 98.42  ? 5   THR A N    1 
ATOM   7    C CA   . THR A 1 2   ? 23.836 26.845 14.399 1.00 78.43  ? 5   THR A CA   1 
ATOM   8    C C    . THR A 1 2   ? 24.145 27.902 13.346 1.00 75.71  ? 5   THR A C    1 
ATOM   9    O O    . THR A 1 2   ? 25.278 28.394 13.304 1.00 72.22  ? 5   THR A O    1 
ATOM   10   C CB   . THR A 1 2   ? 24.811 25.674 14.246 1.00 90.14  ? 5   THR A CB   1 
ATOM   11   O OG1  . THR A 1 2   ? 24.590 25.023 12.989 1.00 110.39 ? 5   THR A OG1  1 
ATOM   12   C CG2  . THR A 1 2   ? 24.619 24.672 15.376 1.00 72.41  ? 5   THR A CG2  1 
ATOM   13   H HA   . THR A 1 2   ? 23.981 27.245 15.271 0.00 94.13  ? 5   THR A HA   1 
ATOM   14   H HB   . THR A 1 2   ? 25.722 26.004 14.280 0.00 108.18 ? 5   THR A HB   1 
ATOM   15   H HG1  . THR A 1 2   ? 23.798 24.745 12.944 0.00 132.48 ? 5   THR A HG1  1 
ATOM   16   H HG21 . THR A 1 2   ? 24.492 25.140 16.216 0.00 86.90  ? 5   THR A HG21 1 
ATOM   17   H HG22 . THR A 1 2   ? 23.840 24.121 15.202 0.00 86.90  ? 5   THR A HG22 1 
ATOM   18   H HG23 . THR A 1 2   ? 25.399 24.100 15.448 0.00 86.90  ? 5   THR A HG23 1 
ATOM   19   N N    . GLY A 1 3   ? 23.179 28.261 12.498 1.00 68.21  ? 6   GLY A N    1 
ATOM   20   C CA   . GLY A 1 3   ? 23.402 29.324 11.536 1.00 58.00  ? 6   GLY A CA   1 
ATOM   21   C C    . GLY A 1 3   ? 23.557 30.692 12.164 1.00 76.35  ? 6   GLY A C    1 
ATOM   22   O O    . GLY A 1 3   ? 24.129 31.590 11.537 1.00 88.81  ? 6   GLY A O    1 
ATOM   23   H H    . GLY A 1 3   ? 22.397 27.905 12.465 0.00 81.86  ? 6   GLY A H    1 
ATOM   24   H HA2  . GLY A 1 3   ? 24.210 29.131 11.034 0.00 69.62  ? 6   GLY A HA2  1 
ATOM   25   H HA3  . GLY A 1 3   ? 22.651 29.358 10.923 0.00 69.62  ? 6   GLY A HA3  1 
ATOM   26   N N    . ARG A 1 4   ? 23.063 30.871 13.388 1.00 54.45  ? 7   ARG A N    1 
ATOM   27   C CA   . ARG A 1 4   ? 23.171 32.147 14.081 1.00 49.95  ? 7   ARG A CA   1 
ATOM   28   C C    . ARG A 1 4   ? 24.486 32.196 14.850 1.00 34.66  ? 7   ARG A C    1 
ATOM   29   O O    . ARG A 1 4   ? 24.725 31.322 15.694 1.00 34.76  ? 7   ARG A O    1 
ATOM   30   C CB   . ARG A 1 4   ? 22.005 32.338 15.036 1.00 42.60  ? 7   ARG A CB   1 
ATOM   31   C CG   . ARG A 1 4   ? 20.635 32.198 14.388 1.00 44.90  ? 7   ARG A CG   1 
ATOM   32   C CD   . ARG A 1 4   ? 19.539 32.099 15.436 1.00 52.03  ? 7   ARG A CD   1 
ATOM   33   N NE   . ARG A 1 4   ? 19.223 30.713 15.762 1.00 65.21  ? 7   ARG A NE   1 
ATOM   34   C CZ   . ARG A 1 4   ? 18.840 30.283 16.958 1.00 52.23  ? 7   ARG A CZ   1 
ATOM   35   N NH1  . ARG A 1 4   ? 18.706 31.109 17.983 1.00 31.99  ? 7   ARG A NH1  1 
ATOM   36   N NH2  . ARG A 1 4   ? 18.584 28.989 17.129 1.00 54.23  ? 7   ARG A NH2  1 
ATOM   37   H H    . ARG A 1 4   ? 22.657 30.262 13.840 0.00 65.36  ? 7   ARG A H    1 
ATOM   38   H HA   . ARG A 1 4   ? 23.162 32.872 13.437 0.00 59.95  ? 7   ARG A HA   1 
ATOM   39   H HB2  . ARG A 1 4   ? 22.067 31.672 15.738 0.00 51.14  ? 7   ARG A HB2  1 
ATOM   40   H HB3  . ARG A 1 4   ? 22.060 33.228 15.417 0.00 51.14  ? 7   ARG A HB3  1 
ATOM   41   H HG2  . ARG A 1 4   ? 20.460 32.975 13.834 0.00 53.89  ? 7   ARG A HG2  1 
ATOM   42   H HG3  . ARG A 1 4   ? 20.615 31.393 13.847 0.00 53.89  ? 7   ARG A HG3  1 
ATOM   43   H HD2  . ARG A 1 4   ? 19.832 32.543 16.248 0.00 62.45  ? 7   ARG A HD2  1 
ATOM   44   H HD3  . ARG A 1 4   ? 18.734 32.523 15.099 0.00 62.45  ? 7   ARG A HD3  1 
ATOM   45   H HE   . ARG A 1 4   ? 19.289 30.131 15.132 0.00 78.27  ? 7   ARG A HE   1 
ATOM   46   H HH11 . ARG A 1 4   ? 18.868 31.947 17.884 0.00 38.41  ? 7   ARG A HH11 1 
ATOM   47   H HH12 . ARG A 1 4   ? 18.457 30.807 18.749 0.00 38.41  ? 7   ARG A HH12 1 
ATOM   48   H HH21 . ARG A 1 4   ? 18.667 28.443 16.470 0.00 65.09  ? 7   ARG A HH21 1 
ATOM   49   H HH22 . ARG A 1 4   ? 18.336 28.698 17.899 0.00 65.09  ? 7   ARG A HH22 1 
ATOM   50   N N    . PRO A 1 5   ? 25.357 33.180 14.604 1.00 35.82  ? 8   PRO A N    1 
ATOM   51   C CA   . PRO A 1 5   ? 26.654 33.194 15.302 1.00 39.63  ? 8   PRO A CA   1 
ATOM   52   C C    . PRO A 1 5   ? 26.542 33.310 16.813 1.00 32.20  ? 8   PRO A C    1 
ATOM   53   O O    . PRO A 1 5   ? 27.479 32.912 17.516 1.00 35.19  ? 8   PRO A O    1 
ATOM   54   C CB   . PRO A 1 5   ? 27.371 34.413 14.702 1.00 32.72  ? 8   PRO A CB   1 
ATOM   55   C CG   . PRO A 1 5   ? 26.303 35.237 14.075 1.00 46.55  ? 8   PRO A CG   1 
ATOM   56   C CD   . PRO A 1 5   ? 25.233 34.291 13.645 1.00 36.92  ? 8   PRO A CD   1 
ATOM   57   H HA   . PRO A 1 5   ? 27.150 32.389 15.082 0.00 47.57  ? 8   PRO A HA   1 
ATOM   58   H HB2  . PRO A 1 5   ? 27.821 34.907 15.404 0.00 39.28  ? 8   PRO A HB2  1 
ATOM   59   H HB3  . PRO A 1 5   ? 28.015 34.120 14.038 0.00 39.28  ? 8   PRO A HB3  1 
ATOM   60   H HG2  . PRO A 1 5   ? 25.959 35.870 14.724 0.00 55.87  ? 8   PRO A HG2  1 
ATOM   61   H HG3  . PRO A 1 5   ? 26.666 35.711 13.310 0.00 55.87  ? 8   PRO A HG3  1 
ATOM   62   H HD2  . PRO A 1 5   ? 24.359 34.707 13.710 0.00 44.32  ? 8   PRO A HD2  1 
ATOM   63   H HD3  . PRO A 1 5   ? 25.388 33.983 12.739 0.00 44.32  ? 8   PRO A HD3  1 
ATOM   64   N N    . GLU A 1 6   ? 25.438 33.841 17.337 1.00 27.90  ? 9   GLU A N    1 
ATOM   65   C CA   . GLU A 1 6   ? 25.276 33.996 18.778 1.00 22.10  ? 9   GLU A CA   1 
ATOM   66   C C    . GLU A 1 6   ? 24.891 32.698 19.477 1.00 26.97  ? 9   GLU A C    1 
ATOM   67   O O    . GLU A 1 6   ? 24.730 32.700 20.703 1.00 20.24  ? 9   GLU A O    1 
ATOM   68   C CB   . GLU A 1 6   ? 24.225 35.074 19.075 1.00 32.02  ? 9   GLU A CB   1 
ATOM   69   C CG   . GLU A 1 6   ? 22.788 34.698 18.719 1.00 23.17  ? 9   GLU A CG   1 
ATOM   70   C CD   . GLU A 1 6   ? 22.430 35.035 17.285 1.00 33.68  ? 9   GLU A CD   1 
ATOM   71   O OE1  . GLU A 1 6   ? 23.350 35.142 16.448 1.00 33.14  ? 9   GLU A OE1  1 
ATOM   72   O OE2  . GLU A 1 6   ? 21.225 35.184 16.993 1.00 29.10  ? 9   GLU A OE2  1 
ATOM   73   H H    . GLU A 1 6   ? 24.768 34.120 16.876 0.00 33.49  ? 9   GLU A H    1 
ATOM   74   H HA   . GLU A 1 6   ? 26.120 34.292 19.153 0.00 26.54  ? 9   GLU A HA   1 
ATOM   75   H HB2  . GLU A 1 6   ? 24.247 35.270 20.025 0.00 38.44  ? 9   GLU A HB2  1 
ATOM   76   H HB3  . GLU A 1 6   ? 24.451 35.869 18.567 0.00 38.44  ? 9   GLU A HB3  1 
ATOM   77   H HG2  . GLU A 1 6   ? 22.672 33.743 18.840 0.00 27.82  ? 9   GLU A HG2  1 
ATOM   78   H HG3  . GLU A 1 6   ? 22.181 35.182 19.301 0.00 27.82  ? 9   GLU A HG3  1 
ATOM   79   N N    . TRP A 1 7   ? 24.745 31.595 18.737 1.00 20.81  ? 10  TRP A N    1 
ATOM   80   C CA   . TRP A 1 7   ? 24.286 30.352 19.347 1.00 19.87  ? 10  TRP A CA   1 
ATOM   81   C C    . TRP A 1 7   ? 25.235 29.871 20.437 1.00 19.51  ? 10  TRP A C    1 
ATOM   82   O O    . TRP A 1 7   ? 24.791 29.269 21.421 1.00 19.84  ? 10  TRP A O    1 
ATOM   83   C CB   . TRP A 1 7   ? 24.119 29.274 18.274 1.00 21.86  ? 10  TRP A CB   1 
ATOM   84   C CG   . TRP A 1 7   ? 25.393 28.571 17.918 1.00 39.02  ? 10  TRP A CG   1 
ATOM   85   C CD1  . TRP A 1 7   ? 26.255 28.894 16.911 1.00 44.61  ? 10  TRP A CD1  1 
ATOM   86   C CD2  . TRP A 1 7   ? 25.950 27.422 18.569 1.00 36.54  ? 10  TRP A CD2  1 
ATOM   87   N NE1  . TRP A 1 7   ? 27.314 28.019 16.894 1.00 43.04  ? 10  TRP A NE1  1 
ATOM   88   C CE2  . TRP A 1 7   ? 27.151 27.106 17.902 1.00 48.09  ? 10  TRP A CE2  1 
ATOM   89   C CE3  . TRP A 1 7   ? 25.551 26.631 19.651 1.00 47.46  ? 10  TRP A CE3  1 
ATOM   90   C CZ2  . TRP A 1 7   ? 27.955 26.032 18.281 1.00 53.73  ? 10  TRP A CZ2  1 
ATOM   91   C CZ3  . TRP A 1 7   ? 26.352 25.565 20.026 1.00 37.59  ? 10  TRP A CZ3  1 
ATOM   92   C CH2  . TRP A 1 7   ? 27.539 25.276 19.343 1.00 52.55  ? 10  TRP A CH2  1 
ATOM   93   H H    . TRP A 1 7   ? 24.903 31.544 17.893 0.00 24.99  ? 10  TRP A H    1 
ATOM   94   H HA   . TRP A 1 7   ? 23.420 30.509 19.756 0.00 23.76  ? 10  TRP A HA   1 
ATOM   95   H HB2  . TRP A 1 7   ? 23.493 28.607 18.597 0.00 26.16  ? 10  TRP A HB2  1 
ATOM   96   H HB3  . TRP A 1 7   ? 23.775 29.688 17.467 0.00 26.16  ? 10  TRP A HB3  1 
ATOM   97   H HD1  . TRP A 1 7   ? 26.141 29.604 16.321 0.00 53.55  ? 10  TRP A HD1  1 
ATOM   98   H HE1  . TRP A 1 7   ? 27.972 28.041 16.341 0.00 51.66  ? 10  TRP A HE1  1 
ATOM   99   H HE3  . TRP A 1 7   ? 24.764 26.817 20.110 0.00 56.97  ? 10  TRP A HE3  1 
ATOM   100  H HZ2  . TRP A 1 7   ? 28.745 25.838 17.830 0.00 64.49  ? 10  TRP A HZ2  1 
ATOM   101  H HZ3  . TRP A 1 7   ? 26.096 25.032 20.744 0.00 45.13  ? 10  TRP A HZ3  1 
ATOM   102  H HH2  . TRP A 1 7   ? 28.057 24.554 19.617 0.00 63.08  ? 10  TRP A HH2  1 
ATOM   103  N N    . ILE A 1 8   ? 26.538 30.121 20.285 1.00 24.88  ? 11  ILE A N    1 
ATOM   104  C CA   . ILE A 1 8   ? 27.500 29.626 21.266 1.00 24.83  ? 11  ILE A CA   1 
ATOM   105  C C    . ILE A 1 8   ? 27.205 30.208 22.643 1.00 22.12  ? 11  ILE A C    1 
ATOM   106  O O    . ILE A 1 8   ? 27.307 29.514 23.662 1.00 25.06  ? 11  ILE A O    1 
ATOM   107  C CB   . ILE A 1 8   ? 28.942 29.939 20.816 1.00 26.75  ? 11  ILE A CB   1 
ATOM   108  C CG1  . ILE A 1 8   ? 29.956 29.436 21.850 1.00 36.69  ? 11  ILE A CG1  1 
ATOM   109  C CG2  . ILE A 1 8   ? 29.134 31.436 20.600 1.00 30.57  ? 11  ILE A CG2  1 
ATOM   110  C CD1  . ILE A 1 8   ? 29.772 27.985 22.257 1.00 37.82  ? 11  ILE A CD1  1 
ATOM   111  H H    . ILE A 1 8   ? 26.882 30.566 19.635 0.00 29.87  ? 11  ILE A H    1 
ATOM   112  H HA   . ILE A 1 8   ? 27.410 28.662 21.323 0.00 29.81  ? 11  ILE A HA   1 
ATOM   113  H HB   . ILE A 1 8   ? 29.089 29.478 19.975 0.00 32.11  ? 11  ILE A HB   1 
ATOM   114  H HG12 . ILE A 1 8   ? 30.847 29.526 21.478 0.00 44.05  ? 11  ILE A HG12 1 
ATOM   115  H HG13 . ILE A 1 8   ? 29.874 29.977 22.651 0.00 44.05  ? 11  ILE A HG13 1 
ATOM   116  H HG21 . ILE A 1 8   ? 30.031 31.595 20.266 0.00 36.70  ? 11  ILE A HG21 1 
ATOM   117  H HG22 . ILE A 1 8   ? 28.481 31.749 19.955 0.00 36.70  ? 11  ILE A HG22 1 
ATOM   118  H HG23 . ILE A 1 8   ? 29.010 31.896 21.446 0.00 36.70  ? 11  ILE A HG23 1 
ATOM   119  H HD11 . ILE A 1 8   ? 30.552 27.696 22.756 0.00 45.40  ? 11  ILE A HD11 1 
ATOM   120  H HD12 . ILE A 1 8   ? 28.979 27.909 22.810 0.00 45.40  ? 11  ILE A HD12 1 
ATOM   121  H HD13 . ILE A 1 8   ? 29.672 27.443 21.459 0.00 45.40  ? 11  ILE A HD13 1 
ATOM   122  N N    . TRP A 1 9   ? 26.830 31.488 22.698 1.00 21.81  ? 12  TRP A N    1 
ATOM   123  C CA   . TRP A 1 9   ? 26.555 32.113 23.987 1.00 20.03  ? 12  TRP A CA   1 
ATOM   124  C C    . TRP A 1 9   ? 25.219 31.656 24.555 1.00 26.57  ? 12  TRP A C    1 
ATOM   125  O O    . TRP A 1 9   ? 25.069 31.557 25.779 1.00 19.51  ? 12  TRP A O    1 
ATOM   126  C CB   . TRP A 1 9   ? 26.593 33.634 23.844 1.00 17.17  ? 12  TRP A CB   1 
ATOM   127  C CG   . TRP A 1 9   ? 27.819 34.117 23.128 1.00 23.92  ? 12  TRP A CG   1 
ATOM   128  C CD1  . TRP A 1 9   ? 27.863 34.920 22.025 1.00 24.76  ? 12  TRP A CD1  1 
ATOM   129  C CD2  . TRP A 1 9   ? 29.180 33.816 23.459 1.00 23.21  ? 12  TRP A CD2  1 
ATOM   130  N NE1  . TRP A 1 9   ? 29.168 35.140 21.651 1.00 26.43  ? 12  TRP A NE1  1 
ATOM   131  C CE2  . TRP A 1 9   ? 29.996 34.472 22.515 1.00 23.81  ? 12  TRP A CE2  1 
ATOM   132  C CE3  . TRP A 1 9   ? 29.789 33.055 24.463 1.00 24.88  ? 12  TRP A CE3  1 
ATOM   133  C CZ2  . TRP A 1 9   ? 31.387 34.393 22.547 1.00 40.82  ? 12  TRP A CZ2  1 
ATOM   134  C CZ3  . TRP A 1 9   ? 31.170 32.977 24.492 1.00 30.17  ? 12  TRP A CZ3  1 
ATOM   135  C CH2  . TRP A 1 9   ? 31.954 33.642 23.541 1.00 30.48  ? 12  TRP A CH2  1 
ATOM   136  H H    . TRP A 1 9   ? 26.731 32.004 22.017 0.00 26.18  ? 12  TRP A H    1 
ATOM   137  H HA   . TRP A 1 9   ? 27.246 31.858 24.618 0.00 24.05  ? 12  TRP A HA   1 
ATOM   138  H HB2  . TRP A 1 9   ? 25.817 33.924 23.341 0.00 20.53  ? 12  TRP A HB2  1 
ATOM   139  H HB3  . TRP A 1 9   ? 26.584 34.035 24.728 0.00 20.53  ? 12  TRP A HB3  1 
ATOM   140  H HD1  . TRP A 1 9   ? 27.118 35.267 21.589 0.00 29.72  ? 12  TRP A HD1  1 
ATOM   141  H HE1  . TRP A 1 9   ? 29.423 35.619 20.984 0.00 31.73  ? 12  TRP A HE1  1 
ATOM   142  H HE3  . TRP A 1 9   ? 29.275 32.611 25.098 0.00 29.87  ? 12  TRP A HE3  1 
ATOM   143  H HZ2  . TRP A 1 9   ? 31.911 34.833 21.916 0.00 49.00  ? 12  TRP A HZ2  1 
ATOM   144  H HZ3  . TRP A 1 9   ? 31.585 32.474 25.155 0.00 36.22  ? 12  TRP A HZ3  1 
ATOM   145  H HH2  . TRP A 1 9   ? 32.880 33.572 23.586 0.00 36.60  ? 12  TRP A HH2  1 
ATOM   146  N N    . LEU A 1 10  ? 24.244 31.364 23.692 1.00 18.17  ? 13  LEU A N    1 
ATOM   147  C CA   . LEU A 1 10  ? 22.969 30.837 24.170 1.00 22.70  ? 13  LEU A CA   1 
ATOM   148  C C    . LEU A 1 10  ? 23.129 29.425 24.719 1.00 14.40  ? 13  LEU A C    1 
ATOM   149  O O    . LEU A 1 10  ? 22.484 29.061 25.710 1.00 14.56  ? 13  LEU A O    1 
ATOM   150  C CB   . LEU A 1 10  ? 21.937 30.858 23.043 1.00 17.60  ? 13  LEU A CB   1 
ATOM   151  C CG   . LEU A 1 10  ? 21.593 32.234 22.467 1.00 22.17  ? 13  LEU A CG   1 
ATOM   152  C CD1  . LEU A 1 10  ? 20.637 32.090 21.292 1.00 19.02  ? 13  LEU A CD1  1 
ATOM   153  C CD2  . LEU A 1 10  ? 20.998 33.140 23.537 1.00 16.87  ? 13  LEU A CD2  1 
ATOM   154  H H    . LEU A 1 10  ? 24.295 31.460 22.839 0.00 21.82  ? 13  LEU A H    1 
ATOM   155  H HA   . LEU A 1 10  ? 22.646 31.406 24.887 0.00 27.25  ? 13  LEU A HA   1 
ATOM   156  H HB2  . LEU A 1 10  ? 22.277 30.319 22.312 0.00 21.13  ? 13  LEU A HB2  1 
ATOM   157  H HB3  . LEU A 1 10  ? 21.113 30.475 23.382 0.00 21.13  ? 13  LEU A HB3  1 
ATOM   158  H HG   . LEU A 1 10  ? 22.407 32.653 22.147 0.00 26.62  ? 13  LEU A HG   1 
ATOM   159  H HD11 . LEU A 1 10  ? 20.412 32.972 20.958 0.00 22.83  ? 13  LEU A HD11 1 
ATOM   160  H HD12 . LEU A 1 10  ? 21.070 31.573 20.594 0.00 22.83  ? 13  LEU A HD12 1 
ATOM   161  H HD13 . LEU A 1 10  ? 19.835 31.634 21.591 0.00 22.83  ? 13  LEU A HD13 1 
ATOM   162  H HD21 . LEU A 1 10  ? 20.669 33.950 23.118 0.00 20.26  ? 13  LEU A HD21 1 
ATOM   163  H HD22 . LEU A 1 10  ? 20.269 32.674 23.975 0.00 20.26  ? 13  LEU A HD22 1 
ATOM   164  H HD23 . LEU A 1 10  ? 21.687 33.358 24.184 0.00 20.26  ? 13  LEU A HD23 1 
ATOM   165  N N    . ALA A 1 11  ? 23.979 28.612 24.085 1.00 18.11  ? 14  ALA A N    1 
ATOM   166  C CA   . ALA A 1 11  ? 24.209 27.255 24.571 1.00 23.73  ? 14  ALA A CA   1 
ATOM   167  C C    . ALA A 1 11  ? 24.960 27.266 25.896 1.00 24.89  ? 14  ALA A C    1 
ATOM   168  O O    . ALA A 1 11  ? 24.673 26.458 26.788 1.00 16.20  ? 14  ALA A O    1 
ATOM   169  C CB   . ALA A 1 11  ? 24.979 26.448 23.526 1.00 18.85  ? 14  ALA A CB   1 
ATOM   170  H H    . ALA A 1 11  ? 24.428 28.821 23.381 0.00 21.74  ? 14  ALA A H    1 
ATOM   171  H HA   . ALA A 1 11  ? 23.351 26.824 24.712 0.00 28.49  ? 14  ALA A HA   1 
ATOM   172  H HB1  . ALA A 1 11  ? 25.130 25.553 23.867 0.00 22.54  ? 14  ALA A HB1  1 
ATOM   173  H HB2  . ALA A 1 11  ? 24.457 26.407 22.710 0.00 22.54  ? 14  ALA A HB2  1 
ATOM   174  H HB3  . ALA A 1 11  ? 25.829 26.884 23.354 0.00 22.54  ? 14  ALA A HB3  1 
ATOM   175  N N    . LEU A 1 12  ? 25.927 28.172 26.042 1.00 25.26  ? 15  LEU A N    1 
ATOM   176  C CA   . LEU A 1 12  ? 26.678 28.256 27.289 1.00 25.83  ? 15  LEU A CA   1 
ATOM   177  C C    . LEU A 1 12  ? 25.803 28.791 28.417 1.00 26.36  ? 15  LEU A C    1 
ATOM   178  O O    . LEU A 1 12  ? 25.844 28.276 29.541 1.00 18.59  ? 15  LEU A O    1 
ATOM   179  C CB   . LEU A 1 12  ? 27.917 29.129 27.082 1.00 29.18  ? 15  LEU A CB   1 
ATOM   180  C CG   . LEU A 1 12  ? 28.975 29.176 28.186 1.00 43.36  ? 15  LEU A CG   1 
ATOM   181  C CD1  . LEU A 1 12  ? 29.410 27.778 28.599 1.00 54.88  ? 15  LEU A CD1  1 
ATOM   182  C CD2  . LEU A 1 12  ? 30.176 29.990 27.723 1.00 40.11  ? 15  LEU A CD2  1 
ATOM   183  H H    . LEU A 1 12  ? 26.163 28.741 25.442 1.00 30.32  ? 15  LEU A H    1 
ATOM   184  H HA   . LEU A 1 12  ? 26.979 27.371 27.549 1.00 31.01  ? 15  LEU A HA   1 
ATOM   185  H HB2  . LEU A 1 12  ? 28.366 28.813 26.282 1.00 35.04  ? 15  LEU A HB2  1 
ATOM   186  H HB3  . LEU A 1 12  ? 27.612 30.041 26.952 1.00 35.04  ? 15  LEU A HB3  1 
ATOM   187  H HG   . LEU A 1 12  ? 28.590 29.602 28.968 1.00 52.05  ? 15  LEU A HG   1 
ATOM   188  H HD11 . LEU A 1 12  ? 30.171 27.847 29.196 1.00 65.87  ? 15  LEU A HD11 1 
ATOM   189  H HD12 . LEU A 1 12  ? 28.673 27.339 29.052 1.00 65.87  ? 15  LEU A HD12 1 
ATOM   190  H HD13 . LEU A 1 12  ? 29.657 27.277 27.806 1.00 65.87  ? 15  LEU A HD13 1 
ATOM   191  H HD21 . LEU A 1 12  ? 30.667 30.299 28.500 1.00 48.15  ? 15  LEU A HD21 1 
ATOM   192  H HD22 . LEU A 1 12  ? 30.745 29.428 27.174 1.00 48.15  ? 15  LEU A HD22 1 
ATOM   193  H HD23 . LEU A 1 12  ? 29.862 30.749 27.206 1.00 48.15  ? 15  LEU A HD23 1 
ATOM   194  N N    . GLY A 1 13  ? 24.993 29.814 28.133 1.00 16.52  ? 16  GLY A N    1 
ATOM   195  C CA   . GLY A 1 13  ? 24.048 30.292 29.129 1.00 14.46  ? 16  GLY A CA   1 
ATOM   196  C C    . GLY A 1 13  ? 23.043 29.228 29.529 1.00 18.62  ? 16  GLY A C    1 
ATOM   197  O O    . GLY A 1 13  ? 22.713 29.085 30.709 1.00 23.98  ? 16  GLY A O    1 
ATOM   198  H H    . GLY A 1 13  ? 24.975 30.237 27.384 0.00 19.84  ? 16  GLY A H    1 
ATOM   199  H HA2  . GLY A 1 13  ? 24.531 30.570 29.922 0.00 17.37  ? 16  GLY A HA2  1 
ATOM   200  H HA3  . GLY A 1 13  ? 23.562 31.052 28.772 0.00 17.37  ? 16  GLY A HA3  1 
ATOM   201  N N    . THR A 1 14  ? 22.543 28.466 28.553 1.00 16.44  ? 17  THR A N    1 
ATOM   202  C CA   . THR A 1 14  ? 21.651 27.353 28.864 1.00 13.58  ? 17  THR A CA   1 
ATOM   203  C C    . THR A 1 14  ? 22.320 26.373 29.820 1.00 23.98  ? 17  THR A C    1 
ATOM   204  O O    . THR A 1 14  ? 21.728 25.964 30.826 1.00 13.58  ? 17  THR A O    1 
ATOM   205  C CB   . THR A 1 14  ? 21.233 26.637 27.578 1.00 22.27  ? 17  THR A CB   1 
ATOM   206  O OG1  . THR A 1 14  ? 20.499 27.536 26.737 1.00 19.56  ? 17  THR A OG1  1 
ATOM   207  C CG2  . THR A 1 14  ? 20.370 25.423 27.896 1.00 22.21  ? 17  THR A CG2  1 
ATOM   208  H H    . THR A 1 14  ? 22.704 28.573 27.715 0.00 19.75  ? 17  THR A H    1 
ATOM   209  H HA   . THR A 1 14  ? 20.853 27.703 29.289 0.00 16.31  ? 17  THR A HA   1 
ATOM   210  H HB   . THR A 1 14  ? 22.026 26.334 27.108 0.00 26.74  ? 17  THR A HB   1 
ATOM   211  H HG1  . THR A 1 14  ? 20.977 28.195 26.534 0.00 23.49  ? 17  THR A HG1  1 
ATOM   212  H HG21 . THR A 1 14  ? 19.917 25.118 27.095 0.00 26.67  ? 17  THR A HG21 1 
ATOM   213  H HG22 . THR A 1 14  ? 20.924 24.703 28.238 0.00 26.67  ? 17  THR A HG22 1 
ATOM   214  H HG23 . THR A 1 14  ? 19.706 25.653 28.565 0.00 26.67  ? 17  THR A HG23 1 
ATOM   215  N N    . ALA A 1 15  ? 23.562 25.985 29.518 1.00 20.20  ? 18  ALA A N    1 
ATOM   216  C CA   . ALA A 1 15  ? 24.261 25.020 30.360 1.00 35.95  ? 18  ALA A CA   1 
ATOM   217  C C    . ALA A 1 15  ? 24.512 25.579 31.755 1.00 26.68  ? 18  ALA A C    1 
ATOM   218  O O    . ALA A 1 15  ? 24.315 24.882 32.756 1.00 22.19  ? 18  ALA A O    1 
ATOM   219  C CB   . ALA A 1 15  ? 25.580 24.611 29.704 1.00 24.58  ? 18  ALA A CB   1 
ATOM   220  H H    . ALA A 1 15  ? 24.013 26.262 28.841 0.00 24.25  ? 18  ALA A H    1 
ATOM   221  H HA   . ALA A 1 15  ? 23.708 24.227 30.450 0.00 43.15  ? 18  ALA A HA   1 
ATOM   222  H HB1  . ALA A 1 15  ? 26.032 23.972 30.276 0.00 29.51  ? 18  ALA A HB1  1 
ATOM   223  H HB2  . ALA A 1 15  ? 25.392 24.209 28.842 0.00 29.51  ? 18  ALA A HB2  1 
ATOM   224  H HB3  . ALA A 1 15  ? 26.132 25.400 29.588 0.00 29.51  ? 18  ALA A HB3  1 
ATOM   225  N N    . LEU A 1 16  ? 24.946 26.839 31.842 1.00 22.71  ? 19  LEU A N    1 
ATOM   226  C CA   . LEU A 1 16  ? 25.265 27.417 33.144 1.00 20.71  ? 19  LEU A CA   1 
ATOM   227  C C    . LEU A 1 16  ? 24.021 27.549 34.014 1.00 20.96  ? 19  LEU A C    1 
ATOM   228  O O    . LEU A 1 16  ? 24.075 27.292 35.222 1.00 16.36  ? 19  LEU A O    1 
ATOM   229  C CB   . LEU A 1 16  ? 25.941 28.777 32.963 1.00 30.31  ? 19  LEU A CB   1 
ATOM   230  C CG   . LEU A 1 16  ? 27.387 28.732 32.461 1.00 30.23  ? 19  LEU A CG   1 
ATOM   231  C CD1  . LEU A 1 16  ? 27.875 30.126 32.094 1.00 20.76  ? 19  LEU A CD1  1 
ATOM   232  C CD2  . LEU A 1 16  ? 28.304 28.100 33.500 1.00 28.91  ? 19  LEU A CD2  1 
ATOM   233  H H    . LEU A 1 16  ? 25.062 27.368 31.175 0.00 27.26  ? 19  LEU A H    1 
ATOM   234  H HA   . LEU A 1 16  ? 25.888 26.829 33.600 0.00 24.86  ? 19  LEU A HA   1 
ATOM   235  H HB2  . LEU A 1 16  ? 25.427 29.289 32.320 0.00 36.39  ? 19  LEU A HB2  1 
ATOM   236  H HB3  . LEU A 1 16  ? 25.947 29.231 33.820 0.00 36.39  ? 19  LEU A HB3  1 
ATOM   237  H HG   . LEU A 1 16  ? 27.420 28.183 31.662 0.00 36.29  ? 19  LEU A HG   1 
ATOM   238  H HD11 . LEU A 1 16  ? 28.774 30.062 31.735 0.00 24.93  ? 19  LEU A HD11 1 
ATOM   239  H HD12 . LEU A 1 16  ? 27.279 30.503 31.428 0.00 24.93  ? 19  LEU A HD12 1 
ATOM   240  H HD13 . LEU A 1 16  ? 27.875 30.680 32.890 0.00 24.93  ? 19  LEU A HD13 1 
ATOM   241  H HD21 . LEU A 1 16  ? 29.225 28.199 33.210 0.00 34.71  ? 19  LEU A HD21 1 
ATOM   242  H HD22 . LEU A 1 16  ? 28.175 28.550 34.350 0.00 34.71  ? 19  LEU A HD22 1 
ATOM   243  H HD23 . LEU A 1 16  ? 28.083 27.160 33.586 0.00 34.71  ? 19  LEU A HD23 1 
ATOM   244  N N    . MET A 1 17  ? 22.892 27.950 33.426 1.00 16.19  ? 20  MET A N    1 
ATOM   245  C CA   . MET A 1 17  ? 21.662 28.043 34.206 1.00 18.51  ? 20  MET A CA   1 
ATOM   246  C C    . MET A 1 17  ? 21.185 26.663 34.642 1.00 14.03  ? 20  MET A C    1 
ATOM   247  O O    . MET A 1 17  ? 20.649 26.504 35.745 1.00 19.51  ? 20  MET A O    1 
ATOM   248  C CB   . MET A 1 17  ? 20.573 28.752 33.401 1.00 16.70  ? 20  MET A CB   1 
ATOM   249  C CG   . MET A 1 17  ? 20.932 30.171 32.995 1.00 17.06  ? 20  MET A CG   1 
ATOM   250  S SD   . MET A 1 17  ? 20.804 31.334 34.367 1.00 15.35  ? 20  MET A SD   1 
ATOM   251  C CE   . MET A 1 17  ? 21.334 32.842 33.560 1.00 14.77  ? 20  MET A CE   1 
ATOM   252  H H    . MET A 1 17  ? 22.815 28.169 32.598 0.00 19.44  ? 20  MET A H    1 
ATOM   253  H HA   . MET A 1 17  ? 21.840 28.579 34.995 0.00 22.23  ? 20  MET A HA   1 
ATOM   254  H HB2  . MET A 1 17  ? 20.406 28.246 32.590 0.00 20.06  ? 20  MET A HB2  1 
ATOM   255  H HB3  . MET A 1 17  ? 19.766 28.795 33.938 0.00 20.06  ? 20  MET A HB3  1 
ATOM   256  H HG2  . MET A 1 17  ? 21.847 30.186 32.671 0.00 20.48  ? 20  MET A HG2  1 
ATOM   257  H HG3  . MET A 1 17  ? 20.328 30.463 32.295 0.00 20.48  ? 20  MET A HG3  1 
ATOM   258  H HE1  . MET A 1 17  ? 21.275 33.576 34.192 0.00 17.74  ? 20  MET A HE1  1 
ATOM   259  H HE2  . MET A 1 17  ? 22.251 32.736 33.263 0.00 17.74  ? 20  MET A HE2  1 
ATOM   260  H HE3  . MET A 1 17  ? 20.757 33.013 32.800 0.00 17.74  ? 20  MET A HE3  1 
ATOM   261  N N    . GLY A 1 18  ? 21.372 25.653 33.791 1.00 13.88  ? 21  GLY A N    1 
ATOM   262  C CA   . GLY A 1 18  ? 20.990 24.305 34.174 1.00 19.49  ? 21  GLY A CA   1 
ATOM   263  C C    . GLY A 1 18  ? 21.823 23.771 35.323 1.00 31.85  ? 21  GLY A C    1 
ATOM   264  O O    . GLY A 1 18  ? 21.293 23.162 36.256 1.00 26.40  ? 21  GLY A O    1 
ATOM   265  H H    . GLY A 1 18  ? 21.710 25.724 33.004 0.00 16.67  ? 21  GLY A H    1 
ATOM   266  H HA2  . GLY A 1 18  ? 20.058 24.300 34.444 0.00 23.40  ? 21  GLY A HA2  1 
ATOM   267  H HA3  . GLY A 1 18  ? 21.101 23.712 33.414 0.00 23.40  ? 21  GLY A HA3  1 
ATOM   268  N N    . LEU A 1 19  ? 23.139 23.997 35.276 1.00 27.30  ? 22  LEU A N    1 
ATOM   269  C CA   . LEU A 1 19  ? 24.005 23.529 36.352 1.00 22.78  ? 22  LEU A CA   1 
ATOM   270  C C    . LEU A 1 19  ? 23.740 24.290 37.645 1.00 23.44  ? 22  LEU A C    1 
ATOM   271  O O    . LEU A 1 19  ? 23.815 23.714 38.736 1.00 21.33  ? 22  LEU A O    1 
ATOM   272  C CB   . LEU A 1 19  ? 25.471 23.665 35.939 1.00 34.49  ? 22  LEU A CB   1 
ATOM   273  C CG   . LEU A 1 19  ? 25.926 22.860 34.716 1.00 54.94  ? 22  LEU A CG   1 
ATOM   274  C CD1  . LEU A 1 19  ? 27.442 22.868 34.620 1.00 59.95  ? 22  LEU A CD1  1 
ATOM   275  C CD2  . LEU A 1 19  ? 25.402 21.426 34.738 1.00 53.62  ? 22  LEU A CD2  1 
ATOM   276  H H    . LEU A 1 19  ? 23.545 24.413 34.643 1.00 32.78  ? 22  LEU A H    1 
ATOM   277  H HA   . LEU A 1 19  ? 23.825 22.590 36.514 1.00 27.35  ? 22  LEU A HA   1 
ATOM   278  H HB2  . LEU A 1 19  ? 25.640 24.599 35.742 1.00 41.40  ? 22  LEU A HB2  1 
ATOM   279  H HB3  . LEU A 1 19  ? 26.020 23.379 36.686 1.00 41.40  ? 22  LEU A HB3  1 
ATOM   280  H HG   . LEU A 1 19  ? 25.555 23.281 33.924 1.00 65.94  ? 22  LEU A HG   1 
ATOM   281  H HD11 . LEU A 1 19  ? 27.712 22.355 33.842 1.00 71.96  ? 22  LEU A HD11 1 
ATOM   282  H HD12 . LEU A 1 19  ? 27.748 23.784 34.535 1.00 71.96  ? 22  LEU A HD12 1 
ATOM   283  H HD13 . LEU A 1 19  ? 27.811 22.469 35.423 1.00 71.96  ? 22  LEU A HD13 1 
ATOM   284  H HD21 . LEU A 1 19  ? 25.729 20.958 33.954 1.00 64.35  ? 22  LEU A HD21 1 
ATOM   285  H HD22 . LEU A 1 19  ? 25.719 20.987 35.542 1.00 64.35  ? 22  LEU A HD22 1 
ATOM   286  H HD23 . LEU A 1 19  ? 24.432 21.444 34.732 1.00 64.35  ? 22  LEU A HD23 1 
ATOM   287  N N    . GLY A 1 20  ? 23.435 25.585 37.546 1.00 21.34  ? 23  GLY A N    1 
ATOM   288  C CA   . GLY A 1 20  ? 23.073 26.337 38.736 1.00 19.90  ? 23  GLY A CA   1 
ATOM   289  C C    . GLY A 1 20  ? 21.801 25.819 39.378 1.00 16.95  ? 23  GLY A C    1 
ATOM   290  O O    . GLY A 1 20  ? 21.724 25.673 40.600 1.00 23.35  ? 23  GLY A O    1 
ATOM   291  H H    . GLY A 1 20  ? 23.431 26.039 36.815 0.00 25.62  ? 23  GLY A H    1 
ATOM   292  H HA2  . GLY A 1 20  ? 23.791 26.275 39.386 0.00 23.89  ? 23  GLY A HA2  1 
ATOM   293  H HA3  . GLY A 1 20  ? 22.940 27.268 38.500 0.00 23.89  ? 23  GLY A HA3  1 
ATOM   294  N N    . THR A 1 21  ? 20.786 25.530 38.560 1.00 21.07  ? 24  THR A N    1 
ATOM   295  C CA   . THR A 1 21  ? 19.544 24.964 39.077 1.00 18.40  ? 24  THR A CA   1 
ATOM   296  C C    . THR A 1 21  ? 19.807 23.670 39.835 1.00 23.62  ? 24  THR A C    1 
ATOM   297  O O    . THR A 1 21  ? 19.306 23.473 40.949 1.00 22.66  ? 24  THR A O    1 
ATOM   298  C CB   . THR A 1 21  ? 18.564 24.712 37.928 1.00 18.85  ? 24  THR A CB   1 
ATOM   299  O OG1  . THR A 1 21  ? 18.340 25.929 37.205 1.00 16.51  ? 24  THR A OG1  1 
ATOM   300  C CG2  . THR A 1 21  ? 17.237 24.182 38.460 1.00 15.96  ? 24  THR A CG2  1 
ATOM   301  H H    . THR A 1 21  ? 20.793 25.651 37.708 0.00 25.29  ? 24  THR A H    1 
ATOM   302  H HA   . THR A 1 21  ? 19.143 25.602 39.688 0.00 22.10  ? 24  THR A HA   1 
ATOM   303  H HB   . THR A 1 21  ? 18.938 24.048 37.328 0.00 22.63  ? 24  THR A HB   1 
ATOM   304  H HG1  . THR A 1 21  ? 19.061 26.200 36.868 0.00 19.82  ? 24  THR A HG1  1 
ATOM   305  H HG21 . THR A 1 21  ? 16.569 24.193 37.756 0.00 19.17  ? 24  THR A HG21 1 
ATOM   306  H HG22 . THR A 1 21  ? 17.345 23.272 38.776 0.00 19.17  ? 24  THR A HG22 1 
ATOM   307  H HG23 . THR A 1 21  ? 16.929 24.736 39.195 0.00 19.17  ? 24  THR A HG23 1 
ATOM   308  N N    . LEU A 1 22  ? 20.590 22.769 39.241 1.00 19.70  ? 25  LEU A N    1 
ATOM   309  C CA   . LEU A 1 22  ? 20.853 21.487 39.883 1.00 34.96  ? 25  LEU A CA   1 
ATOM   310  C C    . LEU A 1 22  ? 21.636 21.668 41.177 1.00 20.08  ? 25  LEU A C    1 
ATOM   311  O O    . LEU A 1 22  ? 21.369 20.982 42.171 1.00 35.73  ? 25  LEU A O    1 
ATOM   312  C CB   . LEU A 1 22  ? 21.606 20.568 38.922 1.00 29.06  ? 25  LEU A CB   1 
ATOM   313  C CG   . LEU A 1 22  ? 20.822 20.055 37.709 1.00 40.59  ? 25  LEU A CG   1 
ATOM   314  C CD1  . LEU A 1 22  ? 21.698 19.127 36.880 1.00 38.89  ? 25  LEU A CD1  1 
ATOM   315  C CD2  . LEU A 1 22  ? 19.537 19.344 38.121 1.00 46.36  ? 25  LEU A CD2  1 
ATOM   316  H H    . LEU A 1 22  ? 20.974 22.875 38.478 0.00 23.65  ? 25  LEU A H    1 
ATOM   317  H HA   . LEU A 1 22  ? 20.007 21.066 40.102 0.00 41.96  ? 25  LEU A HA   1 
ATOM   318  H HB2  . LEU A 1 22  ? 22.373 21.054 38.581 0.00 34.88  ? 25  LEU A HB2  1 
ATOM   319  H HB3  . LEU A 1 22  ? 21.901 19.789 39.420 0.00 34.88  ? 25  LEU A HB3  1 
ATOM   320  H HG   . LEU A 1 22  ? 20.565 20.817 37.166 0.00 48.72  ? 25  LEU A HG   1 
ATOM   321  H HD11 . LEU A 1 22  ? 21.188 18.808 36.119 0.00 46.69  ? 25  LEU A HD11 1 
ATOM   322  H HD12 . LEU A 1 22  ? 22.476 19.618 36.574 0.00 46.69  ? 25  LEU A HD12 1 
ATOM   323  H HD13 . LEU A 1 22  ? 21.974 18.379 37.431 0.00 46.69  ? 25  LEU A HD13 1 
ATOM   324  H HD21 . LEU A 1 22  ? 19.098 19.000 37.327 0.00 55.65  ? 25  LEU A HD21 1 
ATOM   325  H HD22 . LEU A 1 22  ? 19.758 18.613 38.719 0.00 55.65  ? 25  LEU A HD22 1 
ATOM   326  H HD23 . LEU A 1 22  ? 18.957 19.977 38.572 0.00 55.65  ? 25  LEU A HD23 1 
ATOM   327  N N    . TYR A 1 23  ? 22.605 22.585 41.188 1.00 20.09  ? 26  TYR A N    1 
ATOM   328  C CA   . TYR A 1 23  ? 23.383 22.811 42.402 1.00 27.94  ? 26  TYR A CA   1 
ATOM   329  C C    . TYR A 1 23  ? 22.487 23.272 43.545 1.00 21.69  ? 26  TYR A C    1 
ATOM   330  O O    . TYR A 1 23  ? 22.481 22.671 44.625 1.00 23.49  ? 26  TYR A O    1 
ATOM   331  C CB   . TYR A 1 23  ? 24.489 23.832 42.138 1.00 22.25  ? 26  TYR A CB   1 
ATOM   332  C CG   . TYR A 1 23  ? 25.338 24.110 43.356 1.00 24.73  ? 26  TYR A CG   1 
ATOM   333  C CD1  . TYR A 1 23  ? 26.284 23.191 43.792 1.00 53.28  ? 26  TYR A CD1  1 
ATOM   334  C CD2  . TYR A 1 23  ? 25.185 25.286 44.078 1.00 41.23  ? 26  TYR A CD2  1 
ATOM   335  C CE1  . TYR A 1 23  ? 27.059 23.438 44.909 1.00 36.75  ? 26  TYR A CE1  1 
ATOM   336  C CE2  . TYR A 1 23  ? 25.955 25.542 45.197 1.00 37.68  ? 26  TYR A CE2  1 
ATOM   337  C CZ   . TYR A 1 23  ? 26.890 24.614 45.608 1.00 33.32  ? 26  TYR A CZ   1 
ATOM   338  O OH   . TYR A 1 23  ? 27.656 24.868 46.722 1.00 49.20  ? 26  TYR A OH   1 
ATOM   339  H H    . TYR A 1 23  ? 22.825 23.080 40.520 0.00 24.03  ? 26  TYR A H    1 
ATOM   340  H HA   . TYR A 1 23  ? 23.804 21.976 42.662 0.00 33.55  ? 26  TYR A HA   1 
ATOM   341  H HB2  . TYR A 1 23  ? 25.071 23.493 41.440 0.00 26.63  ? 26  TYR A HB2  1 
ATOM   342  H HB3  . TYR A 1 23  ? 24.086 24.668 41.857 0.00 26.63  ? 26  TYR A HB3  1 
ATOM   343  H HD1  . TYR A 1 23  ? 26.398 22.396 43.323 0.00 63.95  ? 26  TYR A HD1  1 
ATOM   344  H HD2  . TYR A 1 23  ? 24.554 25.912 43.805 0.00 49.49  ? 26  TYR A HD2  1 
ATOM   345  H HE1  . TYR A 1 23  ? 27.691 22.814 45.188 0.00 44.12  ? 26  TYR A HE1  1 
ATOM   346  H HE2  . TYR A 1 23  ? 25.844 26.334 45.671 0.00 45.23  ? 26  TYR A HE2  1 
ATOM   347  H HH   . TYR A 1 23  ? 27.389 25.568 47.101 0.00 59.06  ? 26  TYR A HH   1 
ATOM   348  N N    . PHE A 1 24  ? 21.714 24.339 43.320 1.00 19.81  ? 27  PHE A N    1 
ATOM   349  C CA   . PHE A 1 24  ? 20.809 24.826 44.357 1.00 26.45  ? 27  PHE A CA   1 
ATOM   350  C C    . PHE A 1 24  ? 19.826 23.743 44.782 1.00 25.14  ? 27  PHE A C    1 
ATOM   351  O O    . PHE A 1 24  ? 19.478 23.639 45.965 1.00 28.54  ? 27  PHE A O    1 
ATOM   352  C CB   . PHE A 1 24  ? 20.052 26.061 43.859 1.00 24.59  ? 27  PHE A CB   1 
ATOM   353  C CG   . PHE A 1 24  ? 20.935 27.240 43.536 1.00 22.71  ? 27  PHE A CG   1 
ATOM   354  C CD1  . PHE A 1 24  ? 22.172 27.397 44.144 1.00 21.48  ? 27  PHE A CD1  1 
ATOM   355  C CD2  . PHE A 1 24  ? 20.520 28.197 42.623 1.00 19.26  ? 27  PHE A CD2  1 
ATOM   356  C CE1  . PHE A 1 24  ? 22.976 28.484 43.844 1.00 25.43  ? 27  PHE A CE1  1 
ATOM   357  C CE2  . PHE A 1 24  ? 21.321 29.284 42.319 1.00 20.50  ? 27  PHE A CE2  1 
ATOM   358  C CZ   . PHE A 1 24  ? 22.548 29.428 42.930 1.00 19.51  ? 27  PHE A CZ   1 
ATOM   359  H H    . PHE A 1 24  ? 21.697 24.790 42.588 0.00 23.70  ? 27  PHE A H    1 
ATOM   360  H HA   . PHE A 1 24  ? 21.334 25.085 45.130 0.00 31.76  ? 27  PHE A HA   1 
ATOM   361  H HB2  . PHE A 1 24  ? 19.570 25.824 43.051 0.00 29.53  ? 27  PHE A HB2  1 
ATOM   362  H HB3  . PHE A 1 24  ? 19.428 26.340 44.548 0.00 29.53  ? 27  PHE A HB3  1 
ATOM   363  H HD1  . PHE A 1 24  ? 22.465 26.765 44.760 0.00 25.79  ? 27  PHE A HD1  1 
ATOM   364  H HD2  . PHE A 1 24  ? 19.692 28.107 42.209 0.00 23.13  ? 27  PHE A HD2  1 
ATOM   365  H HE1  . PHE A 1 24  ? 23.804 28.578 44.257 0.00 30.53  ? 27  PHE A HE1  1 
ATOM   366  H HE2  . PHE A 1 24  ? 21.031 29.918 41.703 0.00 24.61  ? 27  PHE A HE2  1 
ATOM   367  H HZ   . PHE A 1 24  ? 23.087 30.159 42.728 0.00 23.43  ? 27  PHE A HZ   1 
ATOM   368  N N    . LEU A 1 25  ? 19.367 22.924 43.833 1.00 24.77  ? 28  LEU A N    1 
ATOM   369  C CA   . LEU A 1 25  ? 18.404 21.876 44.158 1.00 36.03  ? 28  LEU A CA   1 
ATOM   370  C C    . LEU A 1 25  ? 19.001 20.871 45.135 1.00 34.36  ? 28  LEU A C    1 
ATOM   371  O O    . LEU A 1 25  ? 18.427 20.601 46.197 1.00 35.51  ? 28  LEU A O    1 
ATOM   372  C CB   . LEU A 1 25  ? 17.942 21.172 42.881 1.00 33.16  ? 28  LEU A CB   1 
ATOM   373  C CG   . LEU A 1 25  ? 16.482 21.372 42.461 1.00 43.43  ? 28  LEU A CG   1 
ATOM   374  C CD1  . LEU A 1 25  ? 16.207 20.614 41.172 1.00 57.58  ? 28  LEU A CD1  1 
ATOM   375  C CD2  . LEU A 1 25  ? 15.511 20.931 43.552 1.00 38.43  ? 28  LEU A CD2  1 
ATOM   376  H H    . LEU A 1 25  ? 19.595 22.956 43.004 0.00 29.74  ? 28  LEU A H    1 
ATOM   377  H HA   . LEU A 1 25  ? 17.629 22.284 44.576 0.00 43.25  ? 28  LEU A HA   1 
ATOM   378  H HB2  . LEU A 1 25  ? 18.492 21.491 42.149 0.00 39.81  ? 28  LEU A HB2  1 
ATOM   379  H HB3  . LEU A 1 25  ? 18.072 20.219 43.003 0.00 39.81  ? 28  LEU A HB3  1 
ATOM   380  H HG   . LEU A 1 25  ? 16.333 22.319 42.312 0.00 52.13  ? 28  LEU A HG   1 
ATOM   381  H HD11 . LEU A 1 25  ? 15.280 20.748 40.919 0.00 69.11  ? 28  LEU A HD11 1 
ATOM   382  H HD12 . LEU A 1 25  ? 16.792 20.950 40.476 0.00 69.11  ? 28  LEU A HD12 1 
ATOM   383  H HD13 . LEU A 1 25  ? 16.375 19.670 41.319 0.00 69.11  ? 28  LEU A HD13 1 
ATOM   384  H HD21 . LEU A 1 25  ? 14.603 21.052 43.234 0.00 46.13  ? 28  LEU A HD21 1 
ATOM   385  H HD22 . LEU A 1 25  ? 15.668 19.995 43.755 0.00 46.13  ? 28  LEU A HD22 1 
ATOM   386  H HD23 . LEU A 1 25  ? 15.659 21.470 44.344 0.00 46.13  ? 28  LEU A HD23 1 
ATOM   387  N N    . VAL A 1 26  ? 20.158 20.303 44.791 1.00 26.68  ? 29  VAL A N    1 
ATOM   388  C CA   . VAL A 1 26  ? 20.813 19.354 45.687 1.00 33.80  ? 29  VAL A CA   1 
ATOM   389  C C    . VAL A 1 26  ? 21.153 20.030 47.009 1.00 35.07  ? 29  VAL A C    1 
ATOM   390  O O    . VAL A 1 26  ? 20.927 19.473 48.090 1.00 29.91  ? 29  VAL A O    1 
ATOM   391  C CB   . VAL A 1 26  ? 22.068 18.765 45.018 1.00 38.84  ? 29  VAL A CB   1 
ATOM   392  C CG1  . VAL A 1 26  ? 22.842 17.902 46.005 1.00 42.38  ? 29  VAL A CG1  1 
ATOM   393  C CG2  . VAL A 1 26  ? 21.688 17.965 43.781 1.00 37.04  ? 29  VAL A CG2  1 
ATOM   394  H H    . VAL A 1 26  ? 20.577 20.448 44.054 0.00 32.03  ? 29  VAL A H    1 
ATOM   395  H HA   . VAL A 1 26  ? 20.199 18.625 45.867 0.00 40.57  ? 29  VAL A HA   1 
ATOM   396  H HB   . VAL A 1 26  ? 22.646 19.492 44.739 0.00 46.62  ? 29  VAL A HB   1 
ATOM   397  H HG11 . VAL A 1 26  ? 23.486 17.364 45.517 0.00 50.87  ? 29  VAL A HG11 1 
ATOM   398  H HG12 . VAL A 1 26  ? 23.302 18.477 46.636 0.00 50.87  ? 29  VAL A HG12 1 
ATOM   399  H HG13 . VAL A 1 26  ? 22.220 17.325 46.476 0.00 50.87  ? 29  VAL A HG13 1 
ATOM   400  H HG21 . VAL A 1 26  ? 22.493 17.602 43.381 0.00 44.47  ? 29  VAL A HG21 1 
ATOM   401  H HG22 . VAL A 1 26  ? 21.093 17.245 44.042 0.00 44.47  ? 29  VAL A HG22 1 
ATOM   402  H HG23 . VAL A 1 26  ? 21.240 18.552 43.151 0.00 44.47  ? 29  VAL A HG23 1 
ATOM   403  N N    . LYS A 1 27  ? 21.712 21.237 46.946 1.00 33.35  ? 30  LYS A N    1 
ATOM   404  C CA   . LYS A 1 27  ? 22.130 21.977 48.164 1.00 31.73  ? 30  LYS A CA   1 
ATOM   405  C C    . LYS A 1 27  ? 20.918 22.183 49.083 1.00 41.24  ? 30  LYS A C    1 
ATOM   406  O O    . LYS A 1 27  ? 21.103 22.129 50.306 1.00 39.46  ? 30  LYS A O    1 
ATOM   407  C CB   . LYS A 1 27  ? 22.806 23.292 47.781 1.00 37.60  ? 30  LYS A CB   1 
ATOM   408  C CG   . LYS A 1 27  ? 23.479 24.054 48.911 1.00 39.74  ? 30  LYS A CG   1 
ATOM   409  C CD   . LYS A 1 27  ? 24.366 25.164 48.399 1.00 63.72  ? 30  LYS A CD   1 
ATOM   410  C CE   . LYS A 1 27  ? 25.068 25.930 49.499 1.00 63.69  ? 30  LYS A CE   1 
ATOM   411  N NZ   . LYS A 1 27  ? 24.105 26.699 50.319 1.00 70.34  ? 30  LYS A NZ   1 
ATOM   412  H H    . LYS A 1 27  ? 21.864 21.680 46.164 0.00 40.04  ? 30  LYS A H    1 
ATOM   413  H HA   . LYS A 1 27  ? 22.786 21.422 48.642 0.00 38.09  ? 30  LYS A HA   1 
ATOM   414  H HB2  . LYS A 1 27  ? 23.479 23.102 47.096 0.00 45.14  ? 30  LYS A HB2  1 
ATOM   415  H HB3  . LYS A 1 27  ? 22.130 23.875 47.377 0.00 45.14  ? 30  LYS A HB3  1 
ATOM   416  H HG2  . LYS A 1 27  ? 22.789 24.435 49.494 0.00 47.71  ? 30  LYS A HG2  1 
ATOM   417  H HG3  . LYS A 1 27  ? 24.017 23.430 49.443 0.00 47.71  ? 30  LYS A HG3  1 
ATOM   418  H HD2  . LYS A 1 27  ? 25.041 24.782 47.800 0.00 76.48  ? 30  LYS A HD2  1 
ATOM   419  H HD3  . LYS A 1 27  ? 23.821 25.790 47.878 0.00 76.48  ? 30  LYS A HD3  1 
ATOM   420  H HE2  . LYS A 1 27  ? 25.550 25.307 50.075 0.00 76.44  ? 30  LYS A HE2  1 
ATOM   421  H HE3  . LYS A 1 27  ? 25.716 26.546 49.107 0.00 76.44  ? 30  LYS A HE3  1 
ATOM   422  H HZ1  . LYS A 1 27  ? 24.551 27.202 50.927 0.00 84.43  ? 30  LYS A HZ1  1 
ATOM   423  H HZ2  . LYS A 1 27  ? 23.615 27.243 49.785 0.00 84.43  ? 30  LYS A HZ2  1 
ATOM   424  H HZ3  . LYS A 1 27  ? 23.546 26.130 50.751 0.00 84.43  ? 30  LYS A HZ3  1 
ATOM   425  N N    . GLY A 1 28  ? 19.720 22.385 48.531 1.00 39.82  ? 31  GLY A N    1 
ATOM   426  C CA   . GLY A 1 28  ? 18.539 22.605 49.344 1.00 29.24  ? 31  GLY A CA   1 
ATOM   427  C C    . GLY A 1 28  ? 17.950 21.362 49.972 1.00 42.50  ? 31  GLY A C    1 
ATOM   428  O O    . GLY A 1 28  ? 17.000 21.473 50.752 1.00 38.84  ? 31  GLY A O    1 
ATOM   429  H H    . GLY A 1 28  ? 19.574 22.407 47.684 0.00 47.80  ? 31  GLY A H    1 
ATOM   430  H HA2  . GLY A 1 28  ? 18.767 23.218 50.061 0.00 35.11  ? 31  GLY A HA2  1 
ATOM   431  H HA3  . GLY A 1 28  ? 17.853 23.008 48.790 0.00 35.11  ? 31  GLY A HA3  1 
ATOM   432  N N    . MET A 1 29  ? 18.475 20.186 49.644 1.00 43.72  ? 32  MET A N    1 
ATOM   433  C CA   . MET A 1 29  ? 17.974 18.896 50.189 1.00 53.93  ? 32  MET A CA   1 
ATOM   434  C C    . MET A 1 29  ? 18.306 18.812 51.681 1.00 62.41  ? 32  MET A C    1 
ATOM   435  O O    . MET A 1 29  ? 19.452 19.096 52.032 1.00 59.58  ? 32  MET A O    1 
ATOM   436  C CB   . MET A 1 29  ? 18.608 17.700 49.472 1.00 56.00  ? 32  MET A CB   1 
ATOM   437  C CG   . MET A 1 29  ? 18.220 17.559 48.020 1.00 56.30  ? 32  MET A CG   1 
ATOM   438  S SD   . MET A 1 29  ? 18.746 15.977 47.292 1.00 76.62  ? 32  MET A SD   1 
ATOM   439  C CE   . MET A 1 29  ? 19.798 15.308 48.580 1.00 41.90  ? 32  MET A CE   1 
ATOM   440  H H    . MET A 1 29  ? 19.183 20.098 49.076 0.00 52.47  ? 32  MET A H    1 
ATOM   441  H HA   . MET A 1 29  ? 16.997 18.868 50.079 0.00 64.73  ? 32  MET A HA   1 
ATOM   442  H HB2  . MET A 1 29  ? 19.580 17.784 49.532 0.00 67.22  ? 32  MET A HB2  1 
ATOM   443  H HB3  . MET A 1 29  ? 18.351 16.888 49.948 0.00 67.22  ? 32  MET A HB3  1 
ATOM   444  H HG2  . MET A 1 29  ? 17.245 17.636 47.940 0.00 67.58  ? 32  MET A HG2  1 
ATOM   445  H HG3  . MET A 1 29  ? 18.623 18.292 47.508 0.00 67.58  ? 32  MET A HG3  1 
ATOM   446  H HE1  . MET A 1 29  ? 20.203 14.489 48.269 0.00 50.29  ? 32  MET A HE1  1 
ATOM   447  H HE2  . MET A 1 29  ? 20.489 15.947 48.794 0.00 50.29  ? 32  MET A HE2  1 
ATOM   448  H HE3  . MET A 1 29  ? 19.270 15.128 49.366 0.00 50.29  ? 32  MET A HE3  1 
ATOM   449  N N    . GLY A 1 30  ? 17.344 18.468 52.527 1.00 61.71  ? 33  GLY A N    1 
ATOM   450  C CA   . GLY A 1 30  ? 17.526 18.312 53.951 1.00 85.48  ? 33  GLY A CA   1 
ATOM   451  C C    . GLY A 1 30  ? 17.302 19.568 54.766 1.00 87.37  ? 33  GLY A C    1 
ATOM   452  O O    . GLY A 1 30  ? 17.051 19.469 55.972 1.00 112.42 ? 33  GLY A O    1 
ATOM   453  H H    . GLY A 1 30  ? 16.555 18.259 52.255 0.00 74.07  ? 33  GLY A H    1 
ATOM   454  H HA2  . GLY A 1 30  ? 16.905 17.638 54.271 0.00 102.59 ? 33  GLY A HA2  1 
ATOM   455  H HA3  . GLY A 1 30  ? 18.432 18.010 54.116 0.00 102.59 ? 33  GLY A HA3  1 
ATOM   456  N N    . VAL A 1 31  ? 17.388 20.747 54.148 1.00 62.49  ? 34  VAL A N    1 
ATOM   457  C CA   . VAL A 1 31  ? 17.156 21.987 54.878 1.00 59.53  ? 34  VAL A CA   1 
ATOM   458  C C    . VAL A 1 31  ? 15.743 21.966 55.442 1.00 62.55  ? 34  VAL A C    1 
ATOM   459  O O    . VAL A 1 31  ? 14.760 21.896 54.693 1.00 70.60  ? 34  VAL A O    1 
ATOM   460  C CB   . VAL A 1 31  ? 17.385 23.200 53.970 1.00 58.11  ? 34  VAL A CB   1 
ATOM   461  C CG1  . VAL A 1 31  ? 16.940 24.480 54.666 1.00 47.63  ? 34  VAL A CG1  1 
ATOM   462  C CG2  . VAL A 1 31  ? 18.848 23.289 53.566 1.00 55.08  ? 34  VAL A CG2  1 
ATOM   463  H H    . VAL A 1 31  ? 17.578 20.852 53.316 0.00 75.00  ? 34  VAL A H    1 
ATOM   464  H HA   . VAL A 1 31  ? 17.780 22.043 55.618 0.00 71.45  ? 34  VAL A HA   1 
ATOM   465  H HB   . VAL A 1 31  ? 16.853 23.095 53.166 0.00 69.74  ? 34  VAL A HB   1 
ATOM   466  H HG11 . VAL A 1 31  ? 17.309 25.241 54.191 0.00 57.17  ? 34  VAL A HG11 1 
ATOM   467  H HG12 . VAL A 1 31  ? 15.971 24.523 54.658 0.00 57.17  ? 34  VAL A HG12 1 
ATOM   468  H HG13 . VAL A 1 31  ? 17.264 24.471 55.580 0.00 57.17  ? 34  VAL A HG13 1 
ATOM   469  H HG21 . VAL A 1 31  ? 18.977 24.079 53.018 0.00 66.11  ? 34  VAL A HG21 1 
ATOM   470  H HG22 . VAL A 1 31  ? 19.394 23.350 54.366 0.00 66.11  ? 34  VAL A HG22 1 
ATOM   471  H HG23 . VAL A 1 31  ? 19.086 22.495 53.063 0.00 66.11  ? 34  VAL A HG23 1 
ATOM   472  N N    . SER A 1 32  ? 15.635 22.023 56.771 1.00 51.58  ? 35  SER A N    1 
ATOM   473  C CA   . SER A 1 32  ? 14.348 21.980 57.449 1.00 51.96  ? 35  SER A CA   1 
ATOM   474  C C    . SER A 1 32  ? 13.904 23.325 58.004 1.00 61.19  ? 35  SER A C    1 
ATOM   475  O O    . SER A 1 32  ? 12.713 23.492 58.285 1.00 72.03  ? 35  SER A O    1 
ATOM   476  C CB   . SER A 1 32  ? 14.387 20.963 58.599 1.00 73.63  ? 35  SER A CB   1 
ATOM   477  O OG   . SER A 1 32  ? 15.612 21.044 59.306 1.00 75.01  ? 35  SER A OG   1 
ATOM   478  H H    . SER A 1 32  ? 16.305 22.087 57.307 0.00 61.91  ? 35  SER A H    1 
ATOM   479  H HA   . SER A 1 32  ? 13.674 21.688 56.815 0.00 62.36  ? 35  SER A HA   1 
ATOM   480  H HB2  . SER A 1 32  ? 13.657 21.150 59.210 0.00 88.37  ? 35  SER A HB2  1 
ATOM   481  H HB3  . SER A 1 32  ? 14.293 20.070 58.233 0.00 88.37  ? 35  SER A HB3  1 
ATOM   482  H HG   . SER A 1 32  ? 15.694 21.805 59.652 0.00 90.03  ? 35  SER A HG   1 
ATOM   483  N N    . ASP A 1 33  ? 14.819 24.273 58.173 1.00 62.17  ? 36  ASP A N    1 
ATOM   484  C CA   . ASP A 1 33  ? 14.446 25.593 58.659 1.00 54.21  ? 36  ASP A CA   1 
ATOM   485  C C    . ASP A 1 33  ? 13.379 26.196 57.747 1.00 41.22  ? 36  ASP A C    1 
ATOM   486  O O    . ASP A 1 33  ? 13.592 26.281 56.529 1.00 38.99  ? 36  ASP A O    1 
ATOM   487  C CB   . ASP A 1 33  ? 15.674 26.502 58.712 1.00 53.50  ? 36  ASP A CB   1 
ATOM   488  C CG   . ASP A 1 33  ? 15.435 27.769 59.514 1.00 63.92  ? 36  ASP A CG   1 
ATOM   489  O OD1  . ASP A 1 33  ? 14.277 28.233 59.574 1.00 82.29  ? 36  ASP A OD1  1 
ATOM   490  O OD2  . ASP A 1 33  ? 16.410 28.308 60.078 1.00 64.78  ? 36  ASP A OD2  1 
ATOM   491  H H    . ASP A 1 33  ? 15.659 24.177 58.014 0.00 74.62  ? 36  ASP A H    1 
ATOM   492  H HA   . ASP A 1 33  ? 14.080 25.522 59.555 0.00 65.07  ? 36  ASP A HA   1 
ATOM   493  H HB2  . ASP A 1 33  ? 16.407 26.019 59.126 0.00 64.22  ? 36  ASP A HB2  1 
ATOM   494  H HB3  . ASP A 1 33  ? 15.915 26.760 57.809 0.00 64.22  ? 36  ASP A HB3  1 
ATOM   495  N N    . PRO A 1 34  ? 12.226 26.616 58.281 1.00 52.57  ? 37  PRO A N    1 
ATOM   496  C CA   . PRO A 1 34  ? 11.208 27.212 57.398 1.00 54.85  ? 37  PRO A CA   1 
ATOM   497  C C    . PRO A 1 34  ? 11.678 28.485 56.719 1.00 39.83  ? 37  PRO A C    1 
ATOM   498  O O    . PRO A 1 34  ? 11.343 28.721 55.551 1.00 50.87  ? 37  PRO A O    1 
ATOM   499  C CB   . PRO A 1 34  ? 10.026 27.470 58.346 1.00 48.11  ? 37  PRO A CB   1 
ATOM   500  C CG   . PRO A 1 34  ? 10.617 27.498 59.711 1.00 58.45  ? 37  PRO A CG   1 
ATOM   501  C CD   . PRO A 1 34  ? 11.770 26.548 59.680 1.00 54.50  ? 37  PRO A CD   1 
ATOM   502  H HA   . PRO A 1 34  ? 10.940 26.568 56.724 0.00 65.84  ? 37  PRO A HA   1 
ATOM   503  H HB2  . PRO A 1 34  ? 9.611  28.320 58.131 0.00 57.75  ? 37  PRO A HB2  1 
ATOM   504  H HB3  . PRO A 1 34  ? 9.377  26.754 58.265 0.00 57.75  ? 37  PRO A HB3  1 
ATOM   505  H HG2  . PRO A 1 34  ? 10.919 28.396 59.918 0.00 70.15  ? 37  PRO A HG2  1 
ATOM   506  H HG3  . PRO A 1 34  ? 9.955  27.213 60.360 0.00 70.15  ? 37  PRO A HG3  1 
ATOM   507  H HD2  . PRO A 1 34  ? 12.470 26.835 60.286 0.00 65.42  ? 37  PRO A HD2  1 
ATOM   508  H HD3  . PRO A 1 34  ? 11.482 25.649 59.907 0.00 65.42  ? 37  PRO A HD3  1 
ATOM   509  N N    . ASP A 1 35  ? 12.451 29.318 57.419 1.00 47.23  ? 38  ASP A N    1 
ATOM   510  C CA   . ASP A 1 35  ? 12.948 30.549 56.813 1.00 45.24  ? 38  ASP A CA   1 
ATOM   511  C C    . ASP A 1 35  ? 13.929 30.247 55.688 1.00 33.20  ? 38  ASP A C    1 
ATOM   512  O O    . ASP A 1 35  ? 13.841 30.828 54.599 1.00 32.36  ? 38  ASP A O    1 
ATOM   513  C CB   . ASP A 1 35  ? 13.603 31.428 57.879 1.00 61.70  ? 38  ASP A CB   1 
ATOM   514  C CG   . ASP A 1 35  ? 12.595 32.036 58.832 1.00 71.13  ? 38  ASP A CG   1 
ATOM   515  O OD1  . ASP A 1 35  ? 11.449 32.289 58.405 1.00 62.41  ? 38  ASP A OD1  1 
ATOM   516  O OD2  . ASP A 1 35  ? 12.948 32.260 60.009 1.00 102.03 ? 38  ASP A OD2  1 
ATOM   517  H H    . ASP A 1 35  ? 12.698 29.194 58.233 0.00 56.69  ? 38  ASP A H    1 
ATOM   518  H HA   . ASP A 1 35  ? 12.200 31.039 56.438 0.00 54.30  ? 38  ASP A HA   1 
ATOM   519  H HB2  . ASP A 1 35  ? 14.221 30.889 58.397 0.00 74.05  ? 38  ASP A HB2  1 
ATOM   520  H HB3  . ASP A 1 35  ? 14.080 32.152 57.443 0.00 74.05  ? 38  ASP A HB3  1 
ATOM   521  N N    . ALA A 1 36  ? 14.878 29.339 55.933 1.00 26.90  ? 39  ALA A N    1 
ATOM   522  C CA   . ALA A 1 36  ? 15.823 28.966 54.887 1.00 44.21  ? 39  ALA A CA   1 
ATOM   523  C C    . ALA A 1 36  ? 15.120 28.297 53.714 1.00 31.04  ? 39  ALA A C    1 
ATOM   524  O O    . ALA A 1 36  ? 15.557 28.440 52.566 1.00 34.77  ? 39  ALA A O    1 
ATOM   525  C CB   . ALA A 1 36  ? 16.900 28.042 55.458 1.00 27.31  ? 39  ALA A CB   1 
ATOM   526  H H    . ALA A 1 36  ? 14.991 28.933 56.683 0.00 32.20  ? 39  ALA A H    1 
ATOM   527  H HA   . ALA A 1 36  ? 16.261 29.767 54.560 0.00 53.07  ? 39  ALA A HA   1 
ATOM   528  H HB1  . ALA A 1 36  ? 17.562 27.866 54.771 0.00 32.69  ? 39  ALA A HB1  1 
ATOM   529  H HB2  . ALA A 1 36  ? 17.319 28.476 56.217 0.00 32.69  ? 39  ALA A HB2  1 
ATOM   530  H HB3  . ALA A 1 36  ? 16.487 27.211 55.739 0.00 32.69  ? 39  ALA A HB3  1 
ATOM   531  N N    . LYS A 1 37  ? 14.033 27.567 53.977 1.00 34.16  ? 40  LYS A N    1 
ATOM   532  C CA   . LYS A 1 37  ? 13.300 26.918 52.895 1.00 40.95  ? 40  LYS A CA   1 
ATOM   533  C C    . LYS A 1 37  ? 12.703 27.946 51.944 1.00 25.03  ? 40  LYS A C    1 
ATOM   534  O O    . LYS A 1 37  ? 12.703 27.748 50.723 1.00 35.93  ? 40  LYS A O    1 
ATOM   535  C CB   . LYS A 1 37  ? 12.204 26.018 53.467 1.00 33.86  ? 40  LYS A CB   1 
ATOM   536  C CG   . LYS A 1 37  ? 12.713 24.679 53.981 1.00 36.15  ? 40  LYS A CG   1 
ATOM   537  C CD   . LYS A 1 37  ? 11.743 24.048 54.974 1.00 55.54  ? 40  LYS A CD   1 
ATOM   538  C CE   . LYS A 1 37  ? 10.633 23.275 54.278 1.00 57.28  ? 40  LYS A CE   1 
ATOM   539  N NZ   . LYS A 1 37  ? 11.151 22.170 53.425 1.00 65.87  ? 40  LYS A NZ   1 
ATOM   540  H H    . LYS A 1 37  ? 13.705 27.435 54.762 0.00 41.01  ? 40  LYS A H    1 
ATOM   541  H HA   . LYS A 1 37  ? 13.913 26.360 52.391 0.00 49.15  ? 40  LYS A HA   1 
ATOM   542  H HB2  . LYS A 1 37  ? 11.780 26.477 54.209 0.00 40.65  ? 40  LYS A HB2  1 
ATOM   543  H HB3  . LYS A 1 37  ? 11.552 25.839 52.771 0.00 40.65  ? 40  LYS A HB3  1 
ATOM   544  H HG2  . LYS A 1 37  ? 12.821 24.070 53.234 0.00 43.40  ? 40  LYS A HG2  1 
ATOM   545  H HG3  . LYS A 1 37  ? 13.563 24.811 54.428 0.00 43.40  ? 40  LYS A HG3  1 
ATOM   546  H HD2  . LYS A 1 37  ? 12.227 23.432 55.546 0.00 66.66  ? 40  LYS A HD2  1 
ATOM   547  H HD3  . LYS A 1 37  ? 11.335 24.746 55.510 0.00 66.66  ? 40  LYS A HD3  1 
ATOM   548  H HE2  . LYS A 1 37  ? 10.048 22.888 54.947 0.00 68.75  ? 40  LYS A HE2  1 
ATOM   549  H HE3  . LYS A 1 37  ? 10.132 23.882 53.710 0.00 68.75  ? 40  LYS A HE3  1 
ATOM   550  H HZ1  . LYS A 1 37  ? 10.477 21.666 53.135 0.00 79.05  ? 40  LYS A HZ1  1 
ATOM   551  H HZ2  . LYS A 1 37  ? 11.584 22.504 52.723 0.00 79.05  ? 40  LYS A HZ2  1 
ATOM   552  H HZ3  . LYS A 1 37  ? 11.711 21.660 53.893 0.00 79.05  ? 40  LYS A HZ3  1 
ATOM   553  N N    . LYS A 1 38  ? 12.186 29.051 52.486 1.00 23.02  ? 41  LYS A N    1 
ATOM   554  C CA   . LYS A 1 38  ? 11.661 30.117 51.637 1.00 30.38  ? 41  LYS A CA   1 
ATOM   555  C C    . LYS A 1 38  ? 12.726 30.615 50.669 1.00 29.51  ? 41  LYS A C    1 
ATOM   556  O O    . LYS A 1 38  ? 12.482 30.733 49.462 1.00 24.46  ? 41  LYS A O    1 
ATOM   557  C CB   . LYS A 1 38  ? 11.150 31.270 52.502 1.00 28.73  ? 41  LYS A CB   1 
ATOM   558  C CG   . LYS A 1 38  ? 9.879  30.961 53.275 1.00 54.05  ? 41  LYS A CG   1 
ATOM   559  C CD   . LYS A 1 38  ? 9.291  32.220 53.897 1.00 58.67  ? 41  LYS A CD   1 
ATOM   560  C CE   . LYS A 1 38  ? 10.141 32.720 55.055 1.00 63.77  ? 41  LYS A CE   1 
ATOM   561  N NZ   . LYS A 1 38  ? 9.555  33.927 55.702 1.00 73.16  ? 41  LYS A NZ   1 
ATOM   562  H H    . LYS A 1 38  ? 12.129 29.205 53.330 0.00 27.55  ? 41  LYS A H    1 
ATOM   563  H HA   . LYS A 1 38  ? 10.916 29.768 51.123 0.00 36.47  ? 41  LYS A HA   1 
ATOM   564  H HB2  . LYS A 1 38  ? 11.837 31.502 53.146 0.00 34.49  ? 41  LYS A HB2  1 
ATOM   565  H HB3  . LYS A 1 38  ? 10.966 32.030 51.926 0.00 34.49  ? 41  LYS A HB3  1 
ATOM   566  H HG2  . LYS A 1 38  ? 9.221  30.581 52.673 0.00 64.87  ? 41  LYS A HG2  1 
ATOM   567  H HG3  . LYS A 1 38  ? 10.080 30.334 53.987 0.00 64.87  ? 41  LYS A HG3  1 
ATOM   568  H HD2  . LYS A 1 38  ? 9.247  32.919 53.226 0.00 70.41  ? 41  LYS A HD2  1 
ATOM   569  H HD3  . LYS A 1 38  ? 8.402  32.026 54.232 0.00 70.41  ? 41  LYS A HD3  1 
ATOM   570  H HE2  . LYS A 1 38  ? 10.210 32.022 55.724 0.00 76.54  ? 41  LYS A HE2  1 
ATOM   571  H HE3  . LYS A 1 38  ? 11.023 32.953 54.725 0.00 76.54  ? 41  LYS A HE3  1 
ATOM   572  H HZ1  . LYS A 1 38  ? 10.066 34.185 56.383 0.00 87.81  ? 41  LYS A HZ1  1 
ATOM   573  H HZ2  . LYS A 1 38  ? 9.500  34.592 55.114 0.00 87.81  ? 41  LYS A HZ2  1 
ATOM   574  H HZ3  . LYS A 1 38  ? 8.739  33.743 56.008 0.00 87.81  ? 41  LYS A HZ3  1 
ATOM   575  N N    . PHE A 1 39  ? 13.920 30.912 51.185 1.00 21.02  ? 42  PHE A N    1 
ATOM   576  C CA   . PHE A 1 39  ? 14.973 31.466 50.341 1.00 28.25  ? 42  PHE A CA   1 
ATOM   577  C C    . PHE A 1 39  ? 15.441 30.453 49.303 1.00 23.81  ? 42  PHE A C    1 
ATOM   578  O O    . PHE A 1 39  ? 15.713 30.816 48.153 1.00 18.63  ? 42  PHE A O    1 
ATOM   579  C CB   . PHE A 1 39  ? 16.141 31.932 51.209 1.00 31.28  ? 42  PHE A CB   1 
ATOM   580  C CG   . PHE A 1 39  ? 15.847 33.179 51.995 1.00 24.05  ? 42  PHE A CG   1 
ATOM   581  C CD1  . PHE A 1 39  ? 15.840 34.419 51.376 1.00 31.44  ? 42  PHE A CD1  1 
ATOM   582  C CD2  . PHE A 1 39  ? 15.568 33.111 53.349 1.00 23.87  ? 42  PHE A CD2  1 
ATOM   583  C CE1  . PHE A 1 39  ? 15.565 35.568 52.094 1.00 39.78  ? 42  PHE A CE1  1 
ATOM   584  C CE2  . PHE A 1 39  ? 15.292 34.257 54.073 1.00 36.04  ? 42  PHE A CE2  1 
ATOM   585  C CZ   . PHE A 1 39  ? 15.291 35.487 53.445 1.00 31.27  ? 42  PHE A CZ   1 
ATOM   586  H H    . PHE A 1 39  ? 14.142 30.804 52.009 0.00 25.15  ? 42  PHE A H    1 
ATOM   587  H HA   . PHE A 1 39  ? 14.625 32.237 49.866 0.00 33.92  ? 42  PHE A HA   1 
ATOM   588  H HB2  . PHE A 1 39  ? 16.362 31.229 51.840 0.00 37.55  ? 42  PHE A HB2  1 
ATOM   589  H HB3  . PHE A 1 39  ? 16.903 32.116 50.637 0.00 37.55  ? 42  PHE A HB3  1 
ATOM   590  H HD1  . PHE A 1 39  ? 16.022 34.478 50.466 0.00 37.75  ? 42  PHE A HD1  1 
ATOM   591  H HD2  . PHE A 1 39  ? 15.566 32.286 53.777 0.00 28.66  ? 42  PHE A HD2  1 
ATOM   592  H HE1  . PHE A 1 39  ? 15.565 36.395 51.668 0.00 47.76  ? 42  PHE A HE1  1 
ATOM   593  H HE2  . PHE A 1 39  ? 15.107 34.199 54.983 0.00 43.27  ? 42  PHE A HE2  1 
ATOM   594  H HZ   . PHE A 1 39  ? 15.105 36.258 53.930 0.00 37.54  ? 42  PHE A HZ   1 
ATOM   595  N N    . TYR A 1 40  ? 15.542 29.179 49.687 1.00 20.55  ? 43  TYR A N    1 
ATOM   596  C CA   . TYR A 1 40  ? 15.943 28.157 48.727 1.00 22.29  ? 43  TYR A CA   1 
ATOM   597  C C    . TYR A 1 40  ? 14.905 28.005 47.622 1.00 19.26  ? 43  TYR A C    1 
ATOM   598  O O    . TYR A 1 40  ? 15.257 27.852 46.446 1.00 18.70  ? 43  TYR A O    1 
ATOM   599  C CB   . TYR A 1 40  ? 16.164 26.824 49.440 1.00 21.66  ? 43  TYR A CB   1 
ATOM   600  C CG   . TYR A 1 40  ? 17.592 26.607 49.878 1.00 23.89  ? 43  TYR A CG   1 
ATOM   601  C CD1  . TYR A 1 40  ? 18.542 26.112 48.995 1.00 22.19  ? 43  TYR A CD1  1 
ATOM   602  C CD2  . TYR A 1 40  ? 17.992 26.903 51.174 1.00 27.96  ? 43  TYR A CD2  1 
ATOM   603  C CE1  . TYR A 1 40  ? 19.851 25.915 49.391 1.00 32.76  ? 43  TYR A CE1  1 
ATOM   604  C CE2  . TYR A 1 40  ? 19.296 26.709 51.580 1.00 27.83  ? 43  TYR A CE2  1 
ATOM   605  C CZ   . TYR A 1 40  ? 20.221 26.216 50.685 1.00 35.85  ? 43  TYR A CZ   1 
ATOM   606  O OH   . TYR A 1 40  ? 21.520 26.022 51.087 1.00 35.64  ? 43  TYR A OH   1 
ATOM   607  H H    . TYR A 1 40  ? 15.386 28.888 50.481 0.00 24.58  ? 43  TYR A H    1 
ATOM   608  H HA   . TYR A 1 40  ? 16.782 28.422 48.320 0.00 26.76  ? 43  TYR A HA   1 
ATOM   609  H HB2  . TYR A 1 40  ? 15.602 26.794 50.231 0.00 26.01  ? 43  TYR A HB2  1 
ATOM   610  H HB3  . TYR A 1 40  ? 15.925 26.102 48.837 0.00 26.01  ? 43  TYR A HB3  1 
ATOM   611  H HD1  . TYR A 1 40  ? 18.294 25.909 48.122 0.00 26.64  ? 43  TYR A HD1  1 
ATOM   612  H HD2  . TYR A 1 40  ? 17.370 27.239 51.779 0.00 33.57  ? 43  TYR A HD2  1 
ATOM   613  H HE1  . TYR A 1 40  ? 20.477 25.582 48.790 0.00 39.33  ? 43  TYR A HE1  1 
ATOM   614  H HE2  . TYR A 1 40  ? 19.550 26.909 52.452 0.00 33.41  ? 43  TYR A HE2  1 
ATOM   615  H HH   . TYR A 1 40  ? 21.607 26.241 51.894 0.00 42.78  ? 43  TYR A HH   1 
ATOM   616  N N    . ALA A 1 41  ? 13.620 28.046 47.978 1.00 19.44  ? 44  ALA A N    1 
ATOM   617  C CA   . ALA A 1 41  ? 12.571 27.921 46.972 1.00 18.69  ? 44  ALA A CA   1 
ATOM   618  C C    . ALA A 1 41  ? 12.618 29.084 45.990 1.00 24.04  ? 44  ALA A C    1 
ATOM   619  O O    . ALA A 1 41  ? 12.612 28.883 44.770 1.00 20.88  ? 44  ALA A O    1 
ATOM   620  C CB   . ALA A 1 41  ? 11.203 27.839 47.649 1.00 19.28  ? 44  ALA A CB   1 
ATOM   621  H H    . ALA A 1 41  ? 13.335 28.144 48.784 0.00 23.25  ? 44  ALA A H    1 
ATOM   622  H HA   . ALA A 1 41  ? 12.709 27.099 46.475 0.00 22.35  ? 44  ALA A HA   1 
ATOM   623  H HB1  . ALA A 1 41  ? 10.518 27.752 46.968 0.00 23.06  ? 44  ALA A HB1  1 
ATOM   624  H HB2  . ALA A 1 41  ? 11.186 27.067 48.236 0.00 23.06  ? 44  ALA A HB2  1 
ATOM   625  H HB3  . ALA A 1 41  ? 11.056 28.648 48.164 0.00 23.06  ? 44  ALA A HB3  1 
ATOM   626  N N    . ILE A 1 42  ? 12.667 30.314 46.506 1.00 17.35  ? 45  ILE A N    1 
ATOM   627  C CA   . ILE A 1 42  ? 12.717 31.486 45.635 1.00 16.34  ? 45  ILE A CA   1 
ATOM   628  C C    . ILE A 1 42  ? 13.956 31.434 44.753 1.00 20.83  ? 45  ILE A C    1 
ATOM   629  O O    . ILE A 1 42  ? 13.882 31.618 43.532 1.00 17.06  ? 45  ILE A O    1 
ATOM   630  C CB   . ILE A 1 42  ? 12.684 32.781 46.469 1.00 19.88  ? 45  ILE A CB   1 
ATOM   631  C CG1  . ILE A 1 42  ? 11.351 32.927 47.203 1.00 19.46  ? 45  ILE A CG1  1 
ATOM   632  C CG2  . ILE A 1 42  ? 12.921 33.992 45.575 1.00 15.56  ? 45  ILE A CG2  1 
ATOM   633  C CD1  . ILE A 1 42  ? 11.393 33.917 48.351 1.00 30.39  ? 45  ILE A CD1  1 
ATOM   634  H H    . ILE A 1 42  ? 12.673 30.494 47.347 0.00 20.74  ? 45  ILE A H    1 
ATOM   635  H HA   . ILE A 1 42  ? 11.933 31.475 45.063 0.00 19.54  ? 45  ILE A HA   1 
ATOM   636  H HB   . ILE A 1 42  ? 13.393 32.728 47.129 0.00 23.87  ? 45  ILE A HB   1 
ATOM   637  H HG12 . ILE A 1 42  ? 10.679 33.232 46.573 0.00 23.37  ? 45  ILE A HG12 1 
ATOM   638  H HG13 . ILE A 1 42  ? 11.098 32.063 47.565 0.00 23.37  ? 45  ILE A HG13 1 
ATOM   639  H HG21 . ILE A 1 42  ? 12.642 34.793 46.047 0.00 18.60  ? 45  ILE A HG21 1 
ATOM   640  H HG22 . ILE A 1 42  ? 13.866 34.047 45.362 0.00 18.60  ? 45  ILE A HG22 1 
ATOM   641  H HG23 . ILE A 1 42  ? 12.404 33.890 44.761 0.00 18.60  ? 45  ILE A HG23 1 
ATOM   642  H HD11 . ILE A 1 42  ? 10.548 33.887 48.826 0.00 36.48  ? 45  ILE A HD11 1 
ATOM   643  H HD12 . ILE A 1 42  ? 12.118 33.676 48.949 0.00 36.48  ? 45  ILE A HD12 1 
ATOM   644  H HD13 . ILE A 1 42  ? 11.540 34.808 47.995 0.00 36.48  ? 45  ILE A HD13 1 
ATOM   645  N N    . THR A 1 43  ? 15.117 31.174 45.360 1.00 16.43  ? 46  THR A N    1 
ATOM   646  C CA   . THR A 1 43  ? 16.376 31.312 44.636 1.00 22.54  ? 46  THR A CA   1 
ATOM   647  C C    . THR A 1 43  ? 16.590 30.182 43.636 1.00 15.91  ? 46  THR A C    1 
ATOM   648  O O    . THR A 1 43  ? 17.216 30.395 42.593 1.00 24.12  ? 46  THR A O    1 
ATOM   649  C CB   . THR A 1 43  ? 17.540 31.377 45.624 1.00 18.79  ? 46  THR A CB   1 
ATOM   650  O OG1  . THR A 1 43  ? 17.264 32.369 46.622 1.00 17.24  ? 46  THR A OG1  1 
ATOM   651  C CG2  . THR A 1 43  ? 18.835 31.729 44.905 1.00 21.91  ? 46  THR A CG2  1 
ATOM   652  H H    . THR A 1 43  ? 15.199 30.920 46.177 0.00 19.64  ? 46  THR A H    1 
ATOM   653  H HA   . THR A 1 43  ? 16.355 32.144 44.136 0.00 27.07  ? 46  THR A HA   1 
ATOM   654  H HB   . THR A 1 43  ? 17.653 30.511 46.048 0.00 22.56  ? 46  THR A HB   1 
ATOM   655  H HG1  . THR A 1 43  ? 16.580 32.154 47.059 0.00 20.62  ? 46  THR A HG1  1 
ATOM   656  H HG21 . THR A 1 43  ? 19.533 31.916 45.552 0.00 26.31  ? 46  THR A HG21 1 
ATOM   657  H HG22 . THR A 1 43  ? 19.116 30.989 44.345 0.00 26.31  ? 46  THR A HG22 1 
ATOM   658  H HG23 . THR A 1 43  ? 18.703 32.513 44.349 0.00 26.31  ? 46  THR A HG23 1 
ATOM   659  N N    . THR A 1 44  ? 16.090 28.979 43.930 1.00 16.44  ? 47  THR A N    1 
ATOM   660  C CA   . THR A 1 44  ? 16.231 27.885 42.975 1.00 16.34  ? 47  THR A CA   1 
ATOM   661  C C    . THR A 1 44  ? 15.321 28.081 41.769 1.00 20.29  ? 47  THR A C    1 
ATOM   662  O O    . THR A 1 44  ? 15.654 27.637 40.664 1.00 17.62  ? 47  THR A O    1 
ATOM   663  C CB   . THR A 1 44  ? 15.933 26.546 43.656 1.00 22.63  ? 47  THR A CB   1 
ATOM   664  O OG1  . THR A 1 44  ? 16.807 26.375 44.779 1.00 23.68  ? 47  THR A OG1  1 
ATOM   665  C CG2  . THR A 1 44  ? 16.139 25.383 42.683 1.00 17.27  ? 47  THR A CG2  1 
ATOM   666  H H    . THR A 1 44  ? 15.677 28.778 44.656 0.00 19.66  ? 47  THR A H    1 
ATOM   667  H HA   . THR A 1 44  ? 17.148 27.859 42.662 0.00 19.54  ? 47  THR A HA   1 
ATOM   668  H HB   . THR A 1 44  ? 15.010 26.537 43.952 0.00 27.17  ? 47  THR A HB   1 
ATOM   669  H HG1  . THR A 1 44  ? 16.698 27.004 45.326 0.00 28.44  ? 47  THR A HG1  1 
ATOM   670  H HG21 . THR A 1 44  ? 15.982 24.540 43.136 0.00 20.65  ? 47  THR A HG21 1 
ATOM   671  H HG22 . THR A 1 44  ? 15.522 25.461 41.939 0.00 20.65  ? 47  THR A HG22 1 
ATOM   672  H HG23 . THR A 1 44  ? 17.047 25.393 42.342 0.00 20.65  ? 47  THR A HG23 1 
ATOM   673  N N    . LEU A 1 45  ? 14.182 28.754 41.954 1.00 15.89  ? 48  LEU A N    1 
ATOM   674  C CA   . LEU A 1 45  ? 13.254 28.959 40.847 1.00 14.79  ? 48  LEU A CA   1 
ATOM   675  C C    . LEU A 1 45  ? 13.824 29.900 39.794 1.00 19.84  ? 48  LEU A C    1 
ATOM   676  O O    . LEU A 1 45  ? 13.464 29.797 38.615 1.00 17.11  ? 48  LEU A O    1 
ATOM   677  C CB   . LEU A 1 45  ? 11.928 29.514 41.369 1.00 14.71  ? 48  LEU A CB   1 
ATOM   678  C CG   . LEU A 1 45  ? 10.853 28.491 41.739 1.00 27.23  ? 48  LEU A CG   1 
ATOM   679  C CD1  . LEU A 1 45  ? 9.706  29.176 42.467 1.00 39.12  ? 48  LEU A CD1  1 
ATOM   680  C CD2  . LEU A 1 45  ? 10.343 27.756 40.506 1.00 33.65  ? 48  LEU A CD2  1 
ATOM   681  H H    . LEU A 1 45  ? 13.928 29.095 42.702 0.00 19.08  ? 48  LEU A H    1 
ATOM   682  H HA   . LEU A 1 45  ? 13.086 28.101 40.428 0.00 17.76  ? 48  LEU A HA   1 
ATOM   683  H HB2  . LEU A 1 45  ? 12.113 30.032 42.168 0.00 17.58  ? 48  LEU A HB2  1 
ATOM   684  H HB3  . LEU A 1 45  ? 11.551 30.086 40.682 0.00 17.58  ? 48  LEU A HB3  1 
ATOM   685  H HG   . LEU A 1 45  ? 11.242 27.828 42.331 0.00 32.69  ? 48  LEU A HG   1 
ATOM   686  H HD11 . LEU A 1 45  ? 9.044  28.511 42.712 0.00 46.96  ? 48  LEU A HD11 1 
ATOM   687  H HD12 . LEU A 1 45  ? 10.051 29.608 43.264 0.00 46.96  ? 48  LEU A HD12 1 
ATOM   688  H HD13 . LEU A 1 45  ? 9.308  29.837 41.879 0.00 46.96  ? 48  LEU A HD13 1 
ATOM   689  H HD21 . LEU A 1 45  ? 9.655  27.128 40.775 0.00 40.39  ? 48  LEU A HD21 1 
ATOM   690  H HD22 . LEU A 1 45  ? 9.976  28.403 39.883 0.00 40.39  ? 48  LEU A HD22 1 
ATOM   691  H HD23 . LEU A 1 45  ? 11.082 27.282 40.094 0.00 40.39  ? 48  LEU A HD23 1 
ATOM   692  N N    . VAL A 1 46  ? 14.702 30.815 40.191 1.00 18.06  ? 49  VAL A N    1 
ATOM   693  C CA   . VAL A 1 46  ? 15.193 31.861 39.296 1.00 13.29  ? 49  VAL A CA   1 
ATOM   694  C C    . VAL A 1 46  ? 15.986 31.237 38.151 1.00 13.67  ? 49  VAL A C    1 
ATOM   695  O O    . VAL A 1 46  ? 15.637 31.452 36.980 1.00 17.76  ? 49  VAL A O    1 
ATOM   696  C CB   . VAL A 1 46  ? 16.028 32.896 40.069 1.00 13.40  ? 49  VAL A CB   1 
ATOM   697  C CG1  . VAL A 1 46  ? 16.854 33.750 39.112 1.00 13.03  ? 49  VAL A CG1  1 
ATOM   698  C CG2  . VAL A 1 46  ? 15.115 33.773 40.918 1.00 17.16  ? 49  VAL A CG2  1 
ATOM   699  H H    . VAL A 1 46  ? 15.034 30.852 40.983 0.00 21.69  ? 49  VAL A H    1 
ATOM   700  H HA   . VAL A 1 46  ? 14.432 32.314 38.901 0.00 15.87  ? 49  VAL A HA   1 
ATOM   701  H HB   . VAL A 1 46  ? 16.644 32.430 40.655 0.00 16.01  ? 49  VAL A HB   1 
ATOM   702  H HG11 . VAL A 1 46  ? 17.156 34.545 39.579 0.00 15.56  ? 49  VAL A HG11 1 
ATOM   703  H HG12 . VAL A 1 46  ? 17.617 33.235 38.807 0.00 15.56  ? 49  VAL A HG12 1 
ATOM   704  H HG13 . VAL A 1 46  ? 16.301 34.002 38.356 0.00 15.56  ? 49  VAL A HG13 1 
ATOM   705  H HG21 . VAL A 1 46  ? 15.658 34.401 41.420 0.00 20.60  ? 49  VAL A HG21 1 
ATOM   706  H HG22 . VAL A 1 46  ? 14.506 34.253 40.336 0.00 20.60  ? 49  VAL A HG22 1 
ATOM   707  H HG23 . VAL A 1 46  ? 14.614 33.209 41.528 0.00 20.60  ? 49  VAL A HG23 1 
ATOM   708  N N    . PRO A 1 47  ? 17.050 30.472 38.415 1.00 15.17  ? 50  PRO A N    1 
ATOM   709  C CA   . PRO A 1 47  ? 17.778 29.855 37.295 1.00 13.60  ? 50  PRO A CA   1 
ATOM   710  C C    . PRO A 1 47  ? 16.971 28.790 36.573 1.00 15.44  ? 50  PRO A C    1 
ATOM   711  O O    . PRO A 1 47  ? 17.198 28.565 35.378 1.00 14.39  ? 50  PRO A O    1 
ATOM   712  C CB   . PRO A 1 47  ? 19.030 29.269 37.962 1.00 17.91  ? 50  PRO A CB   1 
ATOM   713  C CG   . PRO A 1 47  ? 18.646 29.067 39.383 1.00 22.43  ? 50  PRO A CG   1 
ATOM   714  C CD   . PRO A 1 47  ? 17.665 30.152 39.715 1.00 14.25  ? 50  PRO A CD   1 
ATOM   715  H HA   . PRO A 1 47  ? 18.050 30.536 36.659 0.00 16.25  ? 50  PRO A HA   1 
ATOM   716  H HB2  . PRO A 1 47  ? 19.264 28.426 37.543 0.00 21.50  ? 50  PRO A HB2  1 
ATOM   717  H HB3  . PRO A 1 47  ? 19.768 29.893 37.887 0.00 21.50  ? 50  PRO A HB3  1 
ATOM   718  H HG2  . PRO A 1 47  ? 18.238 28.194 39.489 0.00 26.93  ? 50  PRO A HG2  1 
ATOM   719  H HG3  . PRO A 1 47  ? 19.434 29.136 39.945 0.00 26.93  ? 50  PRO A HG3  1 
ATOM   720  H HD2  . PRO A 1 47  ? 16.998 29.833 40.343 0.00 17.03  ? 50  PRO A HD2  1 
ATOM   721  H HD3  . PRO A 1 47  ? 18.120 30.927 40.081 0.00 17.03  ? 50  PRO A HD3  1 
ATOM   722  N N    . ALA A 1 48  ? 16.031 28.131 37.254 1.00 13.89  ? 51  ALA A N    1 
ATOM   723  C CA   . ALA A 1 48  ? 15.195 27.144 36.579 1.00 20.96  ? 51  ALA A CA   1 
ATOM   724  C C    . ALA A 1 48  ? 14.374 27.797 35.475 1.00 13.79  ? 51  ALA A C    1 
ATOM   725  O O    . ALA A 1 48  ? 14.289 27.279 34.355 1.00 17.04  ? 51  ALA A O    1 
ATOM   726  C CB   . ALA A 1 48  ? 14.286 26.444 37.590 1.00 16.05  ? 51  ALA A CB   1 
ATOM   727  H H    . ALA A 1 48  ? 15.862 28.235 38.091 0.00 16.59  ? 51  ALA A H    1 
ATOM   728  H HA   . ALA A 1 48  ? 15.765 26.470 36.176 0.00 25.16  ? 51  ALA A HA   1 
ATOM   729  H HB1  . ALA A 1 48  ? 13.741 25.791 37.125 0.00 19.28  ? 51  ALA A HB1  1 
ATOM   730  H HB2  . ALA A 1 48  ? 14.836 26.003 38.256 0.00 19.28  ? 51  ALA A HB2  1 
ATOM   731  H HB3  . ALA A 1 48  ? 13.719 27.106 38.015 0.00 19.28  ? 51  ALA A HB3  1 
ATOM   732  N N    . ILE A 1 49  ? 13.768 28.949 35.771 1.00 14.60  ? 52  ILE A N    1 
ATOM   733  C CA   . ILE A 1 49  ? 12.997 29.668 34.759 1.00 14.86  ? 52  ILE A CA   1 
ATOM   734  C C    . ILE A 1 49  ? 13.913 30.143 33.637 1.00 13.38  ? 52  ILE A C    1 
ATOM   735  O O    . ILE A 1 49  ? 13.616 29.967 32.449 1.00 14.32  ? 52  ILE A O    1 
ATOM   736  C CB   . ILE A 1 49  ? 12.236 30.841 35.403 1.00 14.18  ? 52  ILE A CB   1 
ATOM   737  C CG1  . ILE A 1 49  ? 11.102 30.313 36.287 1.00 16.80  ? 52  ILE A CG1  1 
ATOM   738  C CG2  . ILE A 1 49  ? 11.693 31.780 34.332 1.00 14.05  ? 52  ILE A CG2  1 
ATOM   739  C CD1  . ILE A 1 49  ? 10.616 31.312 37.318 1.00 17.42  ? 52  ILE A CD1  1 
ATOM   740  H H    . ILE A 1 49  ? 13.789 29.331 36.541 0.00 17.53  ? 52  ILE A H    1 
ATOM   741  H HA   . ILE A 1 49  ? 12.346 29.061 34.375 0.00 17.84  ? 52  ILE A HA   1 
ATOM   742  H HB   . ILE A 1 49  ? 12.854 31.340 35.959 0.00 17.04  ? 52  ILE A HB   1 
ATOM   743  H HG12 . ILE A 1 49  ? 10.349 30.080 35.721 0.00 20.17  ? 52  ILE A HG12 1 
ATOM   744  H HG13 . ILE A 1 49  ? 11.416 29.527 36.761 0.00 20.17  ? 52  ILE A HG13 1 
ATOM   745  H HG21 . ILE A 1 49  ? 11.001 32.337 34.722 0.00 16.87  ? 52  ILE A HG21 1 
ATOM   746  H HG22 . ILE A 1 49  ? 12.417 32.333 34.001 0.00 16.87  ? 52  ILE A HG22 1 
ATOM   747  H HG23 . ILE A 1 49  ? 11.322 31.251 33.608 0.00 16.87  ? 52  ILE A HG23 1 
ATOM   748  H HD11 . ILE A 1 49  ? 9.946  30.888 37.876 0.00 20.92  ? 52  ILE A HD11 1 
ATOM   749  H HD12 . ILE A 1 49  ? 11.368 31.596 37.861 0.00 20.92  ? 52  ILE A HD12 1 
ATOM   750  H HD13 . ILE A 1 49  ? 10.231 32.075 36.860 0.00 20.92  ? 52  ILE A HD13 1 
ATOM   751  N N    . ALA A 1 50  ? 15.043 30.756 33.997 1.00 13.46  ? 53  ALA A N    1 
ATOM   752  C CA   . ALA A 1 50  ? 15.970 31.239 32.979 1.00 17.50  ? 53  ALA A CA   1 
ATOM   753  C C    . ALA A 1 50  ? 16.490 30.098 32.114 1.00 16.11  ? 53  ALA A C    1 
ATOM   754  O O    . ALA A 1 50  ? 16.739 30.289 30.919 1.00 12.78  ? 53  ALA A O    1 
ATOM   755  C CB   . ALA A 1 50  ? 17.134 31.981 33.638 1.00 14.95  ? 53  ALA A CB   1 
ATOM   756  H H    . ALA A 1 50  ? 15.290 30.902 34.808 0.00 16.17  ? 53  ALA A H    1 
ATOM   757  H HA   . ALA A 1 50  ? 15.505 31.865 32.403 0.00 21.01  ? 53  ALA A HA   1 
ATOM   758  H HB1  . ALA A 1 50  ? 17.740 32.295 32.947 0.00 17.95  ? 53  ALA A HB1  1 
ATOM   759  H HB2  . ALA A 1 50  ? 16.785 32.734 34.139 0.00 17.95  ? 53  ALA A HB2  1 
ATOM   760  H HB3  . ALA A 1 50  ? 17.599 31.373 34.234 0.00 17.95  ? 53  ALA A HB3  1 
ATOM   761  N N    . PHE A 1 51  ? 16.658 28.907 32.695 1.00 13.11  ? 54  PHE A N    1 
ATOM   762  C CA   . PHE A 1 51  ? 17.103 27.762 31.908 1.00 13.45  ? 54  PHE A CA   1 
ATOM   763  C C    . PHE A 1 51  ? 16.133 27.474 30.768 1.00 16.89  ? 54  PHE A C    1 
ATOM   764  O O    . PHE A 1 51  ? 16.547 27.280 29.619 1.00 13.67  ? 54  PHE A O    1 
ATOM   765  C CB   . PHE A 1 51  ? 17.255 26.531 32.803 1.00 16.48  ? 54  PHE A CB   1 
ATOM   766  C CG   . PHE A 1 51  ? 17.304 25.236 32.039 1.00 19.41  ? 54  PHE A CG   1 
ATOM   767  C CD1  . PHE A 1 51  ? 18.475 24.820 31.429 1.00 15.32  ? 54  PHE A CD1  1 
ATOM   768  C CD2  . PHE A 1 51  ? 16.174 24.443 31.919 1.00 16.26  ? 54  PHE A CD2  1 
ATOM   769  C CE1  . PHE A 1 51  ? 18.521 23.631 30.720 1.00 21.13  ? 54  PHE A CE1  1 
ATOM   770  C CE2  . PHE A 1 51  ? 16.213 23.255 31.210 1.00 32.69  ? 54  PHE A CE2  1 
ATOM   771  C CZ   . PHE A 1 51  ? 17.387 22.850 30.610 1.00 17.07  ? 54  PHE A CZ   1 
ATOM   772  H H    . PHE A 1 51  ? 16.522 28.741 33.528 0.00 15.75  ? 54  PHE A H    1 
ATOM   773  H HA   . PHE A 1 51  ? 17.972 27.967 31.528 0.00 16.06  ? 54  PHE A HA   1 
ATOM   774  H HB2  . PHE A 1 51  ? 18.080 26.610 33.306 0.00 19.79  ? 54  PHE A HB2  1 
ATOM   775  H HB3  . PHE A 1 51  ? 16.499 26.490 33.409 0.00 19.79  ? 54  PHE A HB3  1 
ATOM   776  H HD1  . PHE A 1 51  ? 19.240 25.344 31.497 0.00 18.40  ? 54  PHE A HD1  1 
ATOM   777  H HD2  . PHE A 1 51  ? 15.379 24.713 32.319 0.00 19.52  ? 54  PHE A HD2  1 
ATOM   778  H HE1  . PHE A 1 51  ? 19.314 23.360 30.317 0.00 25.37  ? 54  PHE A HE1  1 
ATOM   779  H HE2  . PHE A 1 51  ? 15.449 22.731 31.139 0.00 39.25  ? 54  PHE A HE2  1 
ATOM   780  H HZ   . PHE A 1 51  ? 17.415 22.052 30.132 0.00 20.50  ? 54  PHE A HZ   1 
ATOM   781  N N    . THR A 1 52  ? 14.831 27.439 31.068 1.00 13.40  ? 55  THR A N    1 
ATOM   782  C CA   . THR A 1 52  ? 13.852 27.125 30.031 1.00 15.96  ? 55  THR A CA   1 
ATOM   783  C C    . THR A 1 52  ? 13.825 28.194 28.947 1.00 13.40  ? 55  THR A C    1 
ATOM   784  O O    . THR A 1 52  ? 13.600 27.880 27.773 1.00 13.73  ? 55  THR A O    1 
ATOM   785  C CB   . THR A 1 52  ? 12.456 26.965 30.639 1.00 14.67  ? 55  THR A CB   1 
ATOM   786  O OG1  . THR A 1 52  ? 11.975 28.240 31.085 1.00 24.39  ? 55  THR A OG1  1 
ATOM   787  C CG2  . THR A 1 52  ? 12.482 25.990 31.811 1.00 19.87  ? 55  THR A CG2  1 
ATOM   788  H H    . THR A 1 52  ? 14.498 27.590 31.846 0.00 16.00  ? 55  THR A H    1 
ATOM   789  H HA   . THR A 1 52  ? 14.100 26.280 29.624 0.00 19.17  ? 55  THR A HA   1 
ATOM   790  H HB   . THR A 1 52  ? 11.853 26.611 29.967 0.00 17.62  ? 55  THR A HB   1 
ATOM   791  H HG1  . THR A 1 52  ? 11.215 28.154 31.434 0.00 29.29  ? 55  THR A HG1  1 
ATOM   792  H HG21 . THR A 1 52  ? 11.576 25.774 32.083 0.00 23.86  ? 55  THR A HG21 1 
ATOM   793  H HG22 . THR A 1 52  ? 12.936 25.173 31.553 0.00 23.86  ? 55  THR A HG22 1 
ATOM   794  H HG23 . THR A 1 52  ? 12.950 26.386 32.562 0.00 23.86  ? 55  THR A HG23 1 
ATOM   795  N N    . MET A 1 53  ? 14.052 29.448 29.316 1.00 13.01  ? 56  MET A N    1 
ATOM   796  C CA   . MET A 1 53  ? 13.990 30.571 28.349 1.00 14.89  ? 56  MET A CA   1 
ATOM   797  C C    . MET A 1 53  ? 15.289 30.608 27.533 1.00 17.70  ? 56  MET A C    1 
ATOM   798  O O    . MET A 1 53  ? 15.206 30.883 26.351 1.00 15.04  ? 56  MET A O    1 
ATOM   799  C CB   . MET A 1 53  ? 13.737 31.897 29.065 1.00 14.57  ? 56  MET A CB   1 
ATOM   800  C CG   . MET A 1 53  ? 12.327 32.019 29.631 1.00 14.80  ? 56  MET A CG   1 
ATOM   801  S SD   . MET A 1 53  ? 11.007 31.859 28.389 1.00 27.15  ? 56  MET A SD   1 
ATOM   802  C CE   . MET A 1 53  ? 10.625 30.115 28.537 1.00 29.39  ? 56  MET A CE   1 
ATOM   803  H H    . MET A 1 53  ? 14.293 29.688 30.162 0.00 15.54  ? 56  MET A H    1 
ATOM   804  H HA   . MET A 1 53  ? 13.247 30.395 27.729 0.00 17.88  ? 56  MET A HA   1 
ATOM   805  H HB2  . MET A 1 53  ? 14.382 31.988 29.795 0.00 17.50  ? 56  MET A HB2  1 
ATOM   806  H HB3  . MET A 1 53  ? 13.893 32.629 28.436 0.00 17.50  ? 56  MET A HB3  1 
ATOM   807  H HG2  . MET A 1 53  ? 12.199 31.325 30.312 0.00 17.78  ? 56  MET A HG2  1 
ATOM   808  H HG3  . MET A 1 53  ? 12.235 32.890 30.072 0.00 17.78  ? 56  MET A HG3  1 
ATOM   809  H HE1  . MET A 1 53  ? 9.942  29.881 27.897 0.00 35.28  ? 56  MET A HE1  1 
ATOM   810  H HE2  . MET A 1 53  ? 11.420 29.596 28.365 0.00 35.28  ? 56  MET A HE2  1 
ATOM   811  H HE3  . MET A 1 53  ? 10.307 29.931 29.430 0.00 35.28  ? 56  MET A HE3  1 
ATOM   812  N N    . TYR A 1 54  ? 16.444 30.296 28.124 1.00 13.18  ? 57  TYR A N    1 
ATOM   813  C CA   . TYR A 1 54  ? 17.662 30.211 27.327 1.00 16.62  ? 57  TYR A CA   1 
ATOM   814  C C    . TYR A 1 54  ? 17.582 29.044 26.352 1.00 14.02  ? 57  TYR A C    1 
ATOM   815  O O    . TYR A 1 54  ? 18.044 29.148 25.210 1.00 14.43  ? 57  TYR A O    1 
ATOM   816  C CB   . TYR A 1 54  ? 18.884 30.085 28.237 1.00 13.54  ? 57  TYR A CB   1 
ATOM   817  C CG   . TYR A 1 54  ? 19.602 31.401 28.434 1.00 13.42  ? 57  TYR A CG   1 
ATOM   818  C CD1  . TYR A 1 54  ? 20.603 31.801 27.563 1.00 13.81  ? 57  TYR A CD1  1 
ATOM   819  C CD2  . TYR A 1 54  ? 19.265 32.252 29.481 1.00 14.90  ? 57  TYR A CD2  1 
ATOM   820  C CE1  . TYR A 1 54  ? 21.257 33.004 27.729 1.00 13.82  ? 57  TYR A CE1  1 
ATOM   821  C CE2  . TYR A 1 54  ? 19.915 33.460 29.657 1.00 15.13  ? 57  TYR A CE2  1 
ATOM   822  C CZ   . TYR A 1 54  ? 20.911 33.830 28.776 1.00 15.19  ? 57  TYR A CZ   1 
ATOM   823  O OH   . TYR A 1 54  ? 21.563 35.031 28.937 1.00 20.37  ? 57  TYR A OH   1 
ATOM   824  H H    . TYR A 1 54  ? 16.540 30.122 28.961 0.00 15.74  ? 57  TYR A H    1 
ATOM   825  H HA   . TYR A 1 54  ? 17.767 31.027 26.814 0.00 19.96  ? 57  TYR A HA   1 
ATOM   826  H HB2  . TYR A 1 54  ? 18.599 29.765 29.107 0.00 16.17  ? 57  TYR A HB2  1 
ATOM   827  H HB3  . TYR A 1 54  ? 19.510 29.458 27.842 0.00 16.17  ? 57  TYR A HB3  1 
ATOM   828  H HD1  . TYR A 1 54  ? 20.838 31.248 26.853 0.00 16.50  ? 57  TYR A HD1  1 
ATOM   829  H HD2  . TYR A 1 54  ? 18.590 32.005 30.072 0.00 17.89  ? 57  TYR A HD2  1 
ATOM   830  H HE1  . TYR A 1 54  ? 21.928 33.257 27.137 0.00 16.51  ? 57  TYR A HE1  1 
ATOM   831  H HE2  . TYR A 1 54  ? 19.684 34.018 30.364 0.00 18.17  ? 57  TYR A HE2  1 
ATOM   832  H HH   . TYR A 1 54  ? 21.250 35.441 29.600 0.00 24.46  ? 57  TYR A HH   1 
ATOM   833  N N    . LEU A 1 55  ? 16.976 27.932 26.776 1.00 14.09  ? 58  LEU A N    1 
ATOM   834  C CA   . LEU A 1 55  ? 16.806 26.801 25.873 1.00 19.34  ? 58  LEU A CA   1 
ATOM   835  C C    . LEU A 1 55  ? 15.897 27.167 24.708 1.00 14.87  ? 58  LEU A C    1 
ATOM   836  O O    . LEU A 1 55  ? 16.158 26.783 23.563 1.00 17.04  ? 58  LEU A O    1 
ATOM   837  C CB   . LEU A 1 55  ? 16.244 25.597 26.632 1.00 14.74  ? 58  LEU A CB   1 
ATOM   838  C CG   . LEU A 1 55  ? 15.982 24.335 25.801 1.00 15.39  ? 58  LEU A CG   1 
ATOM   839  C CD1  . LEU A 1 55  ? 17.259 23.839 25.131 1.00 15.84  ? 58  LEU A CD1  1 
ATOM   840  C CD2  . LEU A 1 55  ? 15.371 23.240 26.667 1.00 15.56  ? 58  LEU A CD2  1 
ATOM   841  H H    . LEU A 1 55  ? 16.661 27.813 27.568 0.00 16.83  ? 58  LEU A H    1 
ATOM   842  H HA   . LEU A 1 55  ? 17.673 26.551 25.517 0.00 23.22  ? 58  LEU A HA   1 
ATOM   843  H HB2  . LEU A 1 55  ? 16.876 25.357 27.327 0.00 17.61  ? 58  LEU A HB2  1 
ATOM   844  H HB3  . LEU A 1 55  ? 15.398 25.859 27.029 0.00 17.61  ? 58  LEU A HB3  1 
ATOM   845  H HG   . LEU A 1 55  ? 15.351 24.554 25.098 0.00 18.39  ? 58  LEU A HG   1 
ATOM   846  H HD11 . LEU A 1 55  ? 17.075 22.999 24.683 0.00 18.94  ? 58  LEU A HD11 1 
ATOM   847  H HD12 . LEU A 1 55  ? 17.554 24.500 24.485 0.00 18.94  ? 58  LEU A HD12 1 
ATOM   848  H HD13 . LEU A 1 55  ? 17.942 23.710 25.808 0.00 18.94  ? 58  LEU A HD13 1 
ATOM   849  H HD21 . LEU A 1 55  ? 15.242 22.445 26.127 0.00 18.59  ? 58  LEU A HD21 1 
ATOM   850  H HD22 . LEU A 1 55  ? 15.972 23.047 27.403 0.00 18.59  ? 58  LEU A HD22 1 
ATOM   851  H HD23 . LEU A 1 55  ? 14.517 23.549 27.010 0.00 18.59  ? 58  LEU A HD23 1 
ATOM   852  N N    . SER A 1 56  ? 14.821 27.910 24.980 1.00 14.55  ? 59  SER A N    1 
ATOM   853  C CA   . SER A 1 56  ? 13.901 28.284 23.910 1.00 17.98  ? 59  SER A CA   1 
ATOM   854  C C    . SER A 1 56  ? 14.576 29.195 22.891 1.00 15.16  ? 59  SER A C    1 
ATOM   855  O O    . SER A 1 56  ? 14.291 29.109 21.691 1.00 19.47  ? 59  SER A O    1 
ATOM   856  C CB   . SER A 1 56  ? 12.660 28.958 24.496 1.00 16.41  ? 59  SER A CB   1 
ATOM   857  O OG   . SER A 1 56  ? 12.861 30.349 24.655 1.00 17.73  ? 59  SER A OG   1 
ATOM   858  H H    . SER A 1 56  ? 14.607 28.204 25.759 0.00 17.39  ? 59  SER A H    1 
ATOM   859  H HA   . SER A 1 56  ? 13.616 27.479 23.449 0.00 21.59  ? 59  SER A HA   1 
ATOM   860  H HB2  . SER A 1 56  ? 11.912 28.815 23.895 0.00 19.71  ? 59  SER A HB2  1 
ATOM   861  H HB3  . SER A 1 56  ? 12.470 28.566 25.362 0.00 19.71  ? 59  SER A HB3  1 
ATOM   862  H HG   . SER A 1 56  ? 13.488 30.489 25.197 0.00 21.29  ? 59  SER A HG   1 
ATOM   863  N N    . MET A 1 57  ? 15.471 30.075 23.345 1.00 15.24  ? 60  MET A N    1 
ATOM   864  C CA   . MET A 1 57  ? 16.212 30.916 22.411 1.00 19.70  ? 60  MET A CA   1 
ATOM   865  C C    . MET A 1 57  ? 17.207 30.089 21.607 1.00 15.81  ? 60  MET A C    1 
ATOM   866  O O    . MET A 1 57  ? 17.354 30.288 20.395 1.00 23.08  ? 60  MET A O    1 
ATOM   867  C CB   . MET A 1 57  ? 16.929 32.034 23.172 1.00 14.74  ? 60  MET A CB   1 
ATOM   868  C CG   . MET A 1 57  ? 15.984 33.044 23.815 1.00 20.03  ? 60  MET A CG   1 
ATOM   869  S SD   . MET A 1 57  ? 16.800 34.571 24.325 1.00 23.17  ? 60  MET A SD   1 
ATOM   870  C CE   . MET A 1 57  ? 17.587 34.055 25.848 1.00 22.87  ? 60  MET A CE   1 
ATOM   871  H H    . MET A 1 57  ? 15.663 30.200 24.174 0.00 18.30  ? 60  MET A H    1 
ATOM   872  H HA   . MET A 1 57  ? 15.586 31.333 21.799 0.00 23.66  ? 60  MET A HA   1 
ATOM   873  H HB2  . MET A 1 57  ? 17.464 31.638 23.877 0.00 17.61  ? 60  MET A HB2  1 
ATOM   874  H HB3  . MET A 1 57  ? 17.500 32.515 22.553 0.00 17.61  ? 60  MET A HB3  1 
ATOM   875  H HG2  . MET A 1 57  ? 15.292 33.277 23.176 0.00 24.05  ? 60  MET A HG2  1 
ATOM   876  H HG3  . MET A 1 57  ? 15.586 32.642 24.603 0.00 24.05  ? 60  MET A HG3  1 
ATOM   877  H HE1  . MET A 1 57  ? 18.069 34.808 26.224 0.00 27.46  ? 60  MET A HE1  1 
ATOM   878  H HE2  . MET A 1 57  ? 16.905 33.755 26.469 0.00 27.46  ? 60  MET A HE2  1 
ATOM   879  H HE3  . MET A 1 57  ? 18.202 33.330 25.656 0.00 27.46  ? 60  MET A HE3  1 
ATOM   880  N N    . LEU A 1 58  ? 17.888 29.146 22.263 1.00 21.39  ? 61  LEU A N    1 
ATOM   881  C CA   . LEU A 1 58  ? 18.831 28.280 21.562 1.00 17.25  ? 61  LEU A CA   1 
ATOM   882  C C    . LEU A 1 58  ? 18.138 27.507 20.446 1.00 21.53  ? 61  LEU A C    1 
ATOM   883  O O    . LEU A 1 58  ? 18.635 27.445 19.316 1.00 19.97  ? 61  LEU A O    1 
ATOM   884  C CB   . LEU A 1 58  ? 19.489 27.320 22.556 1.00 24.44  ? 61  LEU A CB   1 
ATOM   885  C CG   . LEU A 1 58  ? 20.549 26.371 21.992 1.00 21.85  ? 61  LEU A CG   1 
ATOM   886  C CD1  . LEU A 1 58  ? 21.765 27.147 21.503 1.00 17.19  ? 61  LEU A CD1  1 
ATOM   887  C CD2  . LEU A 1 58  ? 20.949 25.345 23.042 1.00 32.95  ? 61  LEU A CD2  1 
ATOM   888  H H    . LEU A 1 58  ? 17.821 28.991 23.106 0.00 25.68  ? 61  LEU A H    1 
ATOM   889  H HA   . LEU A 1 58  ? 19.525 28.827 21.162 0.00 20.71  ? 61  LEU A HA   1 
ATOM   890  H HB2  . LEU A 1 58  ? 19.919 27.850 23.245 0.00 29.34  ? 61  LEU A HB2  1 
ATOM   891  H HB3  . LEU A 1 58  ? 18.793 26.769 22.946 0.00 29.34  ? 61  LEU A HB3  1 
ATOM   892  H HG   . LEU A 1 58  ? 20.179 25.898 21.230 0.00 26.23  ? 61  LEU A HG   1 
ATOM   893  H HD11 . LEU A 1 58  ? 22.444 26.519 21.212 0.00 20.55  ? 61  LEU A HD11 1 
ATOM   894  H HD12 . LEU A 1 58  ? 21.500 27.715 20.762 0.00 20.55  ? 61  LEU A HD12 1 
ATOM   895  H HD13 . LEU A 1 58  ? 22.106 27.690 22.231 0.00 20.55  ? 61  LEU A HD13 1 
ATOM   896  H HD21 . LEU A 1 58  ? 21.568 24.711 22.646 0.00 39.55  ? 61  LEU A HD21 1 
ATOM   897  H HD22 . LEU A 1 58  ? 21.374 25.802 23.785 0.00 39.55  ? 61  LEU A HD22 1 
ATOM   898  H HD23 . LEU A 1 58  ? 20.154 24.882 23.350 0.00 39.55  ? 61  LEU A HD23 1 
ATOM   899  N N    . LEU A 1 59  ? 16.984 26.909 20.745 1.00 16.86  ? 62  LEU A N    1 
ATOM   900  C CA   . LEU A 1 59  ? 16.252 26.132 19.753 1.00 17.59  ? 62  LEU A CA   1 
ATOM   901  C C    . LEU A 1 59  ? 15.511 27.003 18.746 1.00 25.74  ? 62  LEU A C    1 
ATOM   902  O O    . LEU A 1 59  ? 14.977 26.469 17.767 1.00 22.09  ? 62  LEU A O    1 
ATOM   903  C CB   . LEU A 1 59  ? 15.262 25.193 20.453 1.00 18.26  ? 62  LEU A CB   1 
ATOM   904  C CG   . LEU A 1 59  ? 15.879 24.211 21.454 1.00 25.36  ? 62  LEU A CG   1 
ATOM   905  C CD1  . LEU A 1 59  ? 14.804 23.359 22.114 1.00 19.61  ? 62  LEU A CD1  1 
ATOM   906  C CD2  . LEU A 1 59  ? 16.923 23.328 20.782 1.00 26.92  ? 62  LEU A CD2  1 
ATOM   907  H H    . LEU A 1 59  ? 16.606 26.941 21.517 0.00 20.15  ? 62  LEU A H    1 
ATOM   908  H HA   . LEU A 1 59  ? 16.882 25.585 19.260 0.00 21.03  ? 62  LEU A HA   1 
ATOM   909  H HB2  . LEU A 1 59  ? 14.619 25.735 20.937 0.00 21.93  ? 62  LEU A HB2  1 
ATOM   910  H HB3  . LEU A 1 59  ? 14.809 24.669 19.774 0.00 21.93  ? 62  LEU A HB3  1 
ATOM   911  H HG   . LEU A 1 59  ? 16.324 24.722 22.148 0.00 30.45  ? 62  LEU A HG   1 
ATOM   912  H HD11 . LEU A 1 59  ? 15.226 22.736 22.726 0.00 23.55  ? 62  LEU A HD11 1 
ATOM   913  H HD12 . LEU A 1 59  ? 14.195 23.938 22.597 0.00 23.55  ? 62  LEU A HD12 1 
ATOM   914  H HD13 . LEU A 1 59  ? 14.322 22.871 21.427 0.00 23.55  ? 62  LEU A HD13 1 
ATOM   915  H HD21 . LEU A 1 59  ? 17.202 22.639 21.406 0.00 32.32  ? 62  LEU A HD21 1 
ATOM   916  H HD22 . LEU A 1 59  ? 16.532 22.921 19.993 0.00 32.32  ? 62  LEU A HD22 1 
ATOM   917  H HD23 . LEU A 1 59  ? 17.684 23.874 20.530 0.00 32.32  ? 62  LEU A HD23 1 
ATOM   918  N N    . GLY A 1 60  ? 15.466 28.317 18.955 1.00 17.62  ? 63  GLY A N    1 
ATOM   919  C CA   . GLY A 1 60  ? 14.872 29.226 17.998 1.00 24.55  ? 63  GLY A CA   1 
ATOM   920  C C    . GLY A 1 60  ? 13.425 29.584 18.251 1.00 27.42  ? 63  GLY A C    1 
ATOM   921  O O    . GLY A 1 60  ? 12.854 30.363 17.477 1.00 24.21  ? 63  GLY A O    1 
ATOM   922  H H    . GLY A 1 60  ? 15.778 28.706 19.656 0.00 21.07  ? 63  GLY A H    1 
ATOM   923  H HA2  . GLY A 1 60  ? 15.383 30.050 17.998 0.00 29.47  ? 63  GLY A HA2  1 
ATOM   924  H HA3  . GLY A 1 60  ? 14.925 28.823 17.117 0.00 29.47  ? 63  GLY A HA3  1 
ATOM   925  N N    . TYR A 1 61  ? 12.810 29.051 19.309 1.00 24.16  ? 64  TYR A N    1 
ATOM   926  C CA   . TYR A 1 61  ? 11.401 29.338 19.556 1.00 26.77  ? 64  TYR A CA   1 
ATOM   927  C C    . TYR A 1 61  ? 11.205 30.760 20.070 1.00 18.48  ? 64  TYR A C    1 
ATOM   928  O O    . TYR A 1 61  ? 10.238 31.433 19.696 1.00 24.35  ? 64  TYR A O    1 
ATOM   929  C CB   . TYR A 1 61  ? 10.827 28.327 20.548 1.00 17.60  ? 64  TYR A CB   1 
ATOM   930  C CG   . TYR A 1 61  ? 9.346  28.501 20.798 1.00 25.59  ? 64  TYR A CG   1 
ATOM   931  C CD1  . TYR A 1 61  ? 8.408  27.877 19.986 1.00 22.50  ? 64  TYR A CD1  1 
ATOM   932  C CD2  . TYR A 1 61  ? 8.887  29.297 21.841 1.00 23.74  ? 64  TYR A CD2  1 
ATOM   933  C CE1  . TYR A 1 61  ? 7.052  28.037 20.209 1.00 35.01  ? 64  TYR A CE1  1 
ATOM   934  C CE2  . TYR A 1 61  ? 7.535  29.463 22.071 1.00 24.98  ? 64  TYR A CE2  1 
ATOM   935  C CZ   . TYR A 1 61  ? 6.621  28.831 21.252 1.00 29.71  ? 64  TYR A CZ   1 
ATOM   936  O OH   . TYR A 1 61  ? 5.275  28.993 21.479 1.00 50.06  ? 64  TYR A OH   1 
ATOM   937  H H    . TYR A 1 61  ? 13.179 28.531 19.885 0.00 29.01  ? 64  TYR A H    1 
ATOM   938  H HA   . TYR A 1 61  ? 10.915 29.252 18.720 0.00 32.14  ? 64  TYR A HA   1 
ATOM   939  H HB2  . TYR A 1 61  ? 10.966 27.433 20.199 0.00 21.14  ? 64  TYR A HB2  1 
ATOM   940  H HB3  . TYR A 1 61  ? 11.285 28.427 21.397 0.00 21.14  ? 64  TYR A HB3  1 
ATOM   941  H HD1  . TYR A 1 61  ? 8.695  27.343 19.282 0.00 27.01  ? 64  TYR A HD1  1 
ATOM   942  H HD2  . TYR A 1 61  ? 9.500  29.726 22.393 0.00 28.50  ? 64  TYR A HD2  1 
ATOM   943  H HE1  . TYR A 1 61  ? 6.434  27.613 19.658 0.00 42.03  ? 64  TYR A HE1  1 
ATOM   944  H HE2  . TYR A 1 61  ? 7.242  29.997 22.774 0.00 30.00  ? 64  TYR A HE2  1 
ATOM   945  H HH   . TYR A 1 61  ? 5.153  29.468 22.161 0.00 60.09  ? 64  TYR A HH   1 
ATOM   946  N N    . GLY A 1 62  ? 12.112 31.236 20.919 1.00 16.04  ? 65  GLY A N    1 
ATOM   947  C CA   . GLY A 1 62  ? 11.943 32.530 21.552 1.00 22.04  ? 65  GLY A CA   1 
ATOM   948  C C    . GLY A 1 62  ? 12.491 33.686 20.742 1.00 24.99  ? 65  GLY A C    1 
ATOM   949  O O    . GLY A 1 62  ? 12.979 34.668 21.308 1.00 16.65  ? 65  GLY A O    1 
ATOM   950  H H    . GLY A 1 62  ? 12.833 30.825 21.142 0.00 19.17  ? 65  GLY A H    1 
ATOM   951  H HA2  . GLY A 1 62  ? 10.997 32.688 21.697 0.00 26.46  ? 65  GLY A HA2  1 
ATOM   952  H HA3  . GLY A 1 62  ? 12.398 32.522 22.409 0.00 26.46  ? 65  GLY A HA3  1 
ATOM   953  N N    . LEU A 1 63  ? 12.409 33.587 19.417 1.00 28.10  ? 66  LEU A N    1 
ATOM   954  C CA   . LEU A 1 63  ? 12.942 34.599 18.517 1.00 21.07  ? 66  LEU A CA   1 
ATOM   955  C C    . LEU A 1 63  ? 11.873 34.992 17.509 1.00 22.38  ? 66  LEU A C    1 
ATOM   956  O O    . LEU A 1 63  ? 11.130 34.138 17.017 1.00 24.57  ? 66  LEU A O    1 
ATOM   957  C CB   . LEU A 1 63  ? 14.196 34.083 17.790 1.00 25.15  ? 66  LEU A CB   1 
ATOM   958  C CG   . LEU A 1 63  ? 14.792 34.962 16.686 1.00 36.61  ? 66  LEU A CG   1 
ATOM   959  C CD1  . LEU A 1 63  ? 15.651 36.062 17.287 1.00 27.90  ? 66  LEU A CD1  1 
ATOM   960  C CD2  . LEU A 1 63  ? 15.603 34.116 15.712 1.00 23.13  ? 66  LEU A CD2  1 
ATOM   961  H H    . LEU A 1 63  ? 12.040 32.927 19.008 0.00 33.74  ? 66  LEU A H    1 
ATOM   962  H HA   . LEU A 1 63  ? 13.188 35.393 19.017 0.00 25.30  ? 66  LEU A HA   1 
ATOM   963  H HB2  . LEU A 1 63  ? 14.892 33.957 18.454 0.00 30.20  ? 66  LEU A HB2  1 
ATOM   964  H HB3  . LEU A 1 63  ? 13.970 33.233 17.379 0.00 30.20  ? 66  LEU A HB3  1 
ATOM   965  H HG   . LEU A 1 63  ? 14.072 35.382 16.191 0.00 43.95  ? 66  LEU A HG   1 
ATOM   966  H HD11 . LEU A 1 63  ? 16.044 36.583 16.570 0.00 33.50  ? 66  LEU A HD11 1 
ATOM   967  H HD12 . LEU A 1 63  ? 15.093 36.631 17.841 0.00 33.50  ? 66  LEU A HD12 1 
ATOM   968  H HD13 . LEU A 1 63  ? 16.350 35.659 17.825 0.00 33.50  ? 66  LEU A HD13 1 
ATOM   969  H HD21 . LEU A 1 63  ? 16.013 34.698 15.053 0.00 27.77  ? 66  LEU A HD21 1 
ATOM   970  H HD22 . LEU A 1 63  ? 16.289 33.638 16.204 0.00 27.77  ? 66  LEU A HD22 1 
ATOM   971  H HD23 . LEU A 1 63  ? 15.011 33.485 15.273 0.00 27.77  ? 66  LEU A HD23 1 
ATOM   972  N N    . THR A 1 64  ? 11.800 36.287 17.206 1.00 19.53  ? 67  THR A N    1 
ATOM   973  C CA   . THR A 1 64  ? 10.870 36.802 16.212 1.00 23.50  ? 67  THR A CA   1 
ATOM   974  C C    . THR A 1 64  ? 11.545 37.916 15.423 1.00 26.15  ? 67  THR A C    1 
ATOM   975  O O    . THR A 1 64  ? 12.587 38.447 15.817 1.00 26.56  ? 67  THR A O    1 
ATOM   976  C CB   . THR A 1 64  ? 9.574  37.312 16.859 1.00 26.44  ? 67  THR A CB   1 
ATOM   977  O OG1  . THR A 1 64  ? 8.576  37.503 15.849 1.00 26.49  ? 67  THR A OG1  1 
ATOM   978  C CG2  . THR A 1 64  ? 9.812  38.629 17.590 1.00 29.54  ? 67  THR A CG2  1 
ATOM   979  H H    . THR A 1 64  ? 12.288 36.894 17.571 0.00 23.45  ? 67  THR A H    1 
ATOM   980  H HA   . THR A 1 64  ? 10.642 36.088 15.595 0.00 28.21  ? 67  THR A HA   1 
ATOM   981  H HB   . THR A 1 64  ? 9.262  36.661 17.506 0.00 31.75  ? 67  THR A HB   1 
ATOM   982  H HG1  . THR A 1 64  ? 7.866  37.788 16.197 0.00 31.80  ? 67  THR A HG1  1 
ATOM   983  H HG21 . THR A 1 64  ? 9.086  38.801 18.209 0.00 35.46  ? 67  THR A HG21 1 
ATOM   984  H HG22 . THR A 1 64  ? 10.645 38.587 18.086 0.00 35.46  ? 67  THR A HG22 1 
ATOM   985  H HG23 . THR A 1 64  ? 9.862  39.358 16.953 0.00 35.46  ? 67  THR A HG23 1 
ATOM   986  N N    . MET A 1 65  ? 10.938 38.265 14.292 1.00 24.71  ? 68  MET A N    1 
ATOM   987  C CA   . MET A 1 65  ? 11.414 39.341 13.434 1.00 24.39  ? 68  MET A CA   1 
ATOM   988  C C    . MET A 1 65  ? 10.494 40.543 13.589 1.00 38.63  ? 68  MET A C    1 
ATOM   989  O O    . MET A 1 65  ? 9.270  40.409 13.489 1.00 46.89  ? 68  MET A O    1 
ATOM   990  C CB   . MET A 1 65  ? 11.460 38.896 11.970 1.00 32.09  ? 68  MET A CB   1 
ATOM   991  C CG   . MET A 1 65  ? 12.180 37.572 11.739 1.00 43.67  ? 68  MET A CG   1 
ATOM   992  S SD   . MET A 1 65  ? 13.855 37.520 12.413 1.00 59.43  ? 68  MET A SD   1 
ATOM   993  C CE   . MET A 1 65  ? 14.529 39.069 11.818 1.00 40.07  ? 68  MET A CE   1 
ATOM   994  H H    . MET A 1 65  ? 10.229 37.881 13.995 0.00 29.67  ? 68  MET A H    1 
ATOM   995  H HA   . MET A 1 65  ? 12.314 39.589 13.698 0.00 29.28  ? 68  MET A HA   1 
ATOM   996  H HB2  . MET A 1 65  ? 10.550 38.796 11.648 0.00 38.53  ? 68  MET A HB2  1 
ATOM   997  H HB3  . MET A 1 65  ? 11.921 39.576 11.454 0.00 38.53  ? 68  MET A HB3  1 
ATOM   998  H HG2  . MET A 1 65  ? 11.670 36.863 12.161 0.00 52.42  ? 68  MET A HG2  1 
ATOM   999  H HG3  . MET A 1 65  ? 12.241 37.414 10.784 0.00 52.42  ? 68  MET A HG3  1 
ATOM   1000 H HE1  . MET A 1 65  ? 15.454 39.139 12.100 0.00 48.10  ? 68  MET A HE1  1 
ATOM   1001 H HE2  . MET A 1 65  ? 14.476 39.086 10.850 0.00 48.10  ? 68  MET A HE2  1 
ATOM   1002 H HE3  . MET A 1 65  ? 14.013 39.801 12.191 0.00 48.10  ? 68  MET A HE3  1 
ATOM   1003 N N    . VAL A 1 66  ? 11.081 41.709 13.833 1.00 36.08  ? 69  VAL A N    1 
ATOM   1004 C CA   . VAL A 1 66  ? 10.342 42.953 14.002 1.00 40.16  ? 69  VAL A CA   1 
ATOM   1005 C C    . VAL A 1 66  ? 10.810 43.925 12.924 1.00 50.80  ? 69  VAL A C    1 
ATOM   1006 O O    . VAL A 1 66  ? 12.009 44.201 12.824 1.00 31.55  ? 69  VAL A O    1 
ATOM   1007 C CB   . VAL A 1 66  ? 10.539 43.561 15.400 1.00 32.56  ? 69  VAL A CB   1 
ATOM   1008 C CG1  . VAL A 1 66  ? 9.788  44.882 15.515 1.00 31.97  ? 69  VAL A CG1  1 
ATOM   1009 C CG2  . VAL A 1 66  ? 10.080 42.586 16.475 1.00 29.47  ? 69  VAL A CG2  1 
ATOM   1010 H H    . VAL A 1 66  ? 11.932 41.807 13.908 0.00 43.31  ? 69  VAL A H    1 
ATOM   1011 H HA   . VAL A 1 66  ? 9.395  42.782 13.874 0.00 48.21  ? 69  VAL A HA   1 
ATOM   1012 H HB   . VAL A 1 66  ? 11.483 43.737 15.538 0.00 39.08  ? 69  VAL A HB   1 
ATOM   1013 H HG11 . VAL A 1 66  ? 9.788  45.166 16.443 0.00 38.38  ? 69  VAL A HG11 1 
ATOM   1014 H HG12 . VAL A 1 66  ? 10.232 45.547 14.966 0.00 38.38  ? 69  VAL A HG12 1 
ATOM   1015 H HG13 . VAL A 1 66  ? 8.876  44.755 15.208 0.00 38.38  ? 69  VAL A HG13 1 
ATOM   1016 H HG21 . VAL A 1 66  ? 10.183 43.002 17.345 0.00 35.38  ? 69  VAL A HG21 1 
ATOM   1017 H HG22 . VAL A 1 66  ? 9.148  42.363 16.323 0.00 35.38  ? 69  VAL A HG22 1 
ATOM   1018 H HG23 . VAL A 1 66  ? 10.624 41.784 16.426 0.00 35.38  ? 69  VAL A HG23 1 
ATOM   1019 N N    . PRO A 1 67  ? 9.916  44.469 12.094 1.00 46.04  ? 70  PRO A N    1 
ATOM   1020 C CA   . PRO A 1 67  ? 10.347 45.430 11.069 1.00 40.84  ? 70  PRO A CA   1 
ATOM   1021 C C    . PRO A 1 67  ? 10.435 46.839 11.638 1.00 48.84  ? 70  PRO A C    1 
ATOM   1022 O O    . PRO A 1 67  ? 9.444  47.391 12.119 1.00 49.25  ? 70  PRO A O    1 
ATOM   1023 C CB   . PRO A 1 67  ? 9.251  45.321 10.004 1.00 46.12  ? 70  PRO A CB   1 
ATOM   1024 C CG   . PRO A 1 67  ? 8.033  44.962 10.777 1.00 33.85  ? 70  PRO A CG   1 
ATOM   1025 C CD   . PRO A 1 67  ? 8.488  44.127 11.952 1.00 45.59  ? 70  PRO A CD   1 
ATOM   1026 H HA   . PRO A 1 67  ? 11.206 45.175 10.698 0.00 49.02  ? 70  PRO A HA   1 
ATOM   1027 H HB2  . PRO A 1 67  ? 9.141  46.171 9.549  0.00 55.36  ? 70  PRO A HB2  1 
ATOM   1028 H HB3  . PRO A 1 67  ? 9.476  44.629 9.362  0.00 55.36  ? 70  PRO A HB3  1 
ATOM   1029 H HG2  . PRO A 1 67  ? 7.596  45.772 11.085 0.00 40.64  ? 70  PRO A HG2  1 
ATOM   1030 H HG3  . PRO A 1 67  ? 7.430  44.454 10.212 0.00 40.64  ? 70  PRO A HG3  1 
ATOM   1031 H HD2  . PRO A 1 67  ? 7.997  44.365 12.754 0.00 54.72  ? 70  PRO A HD2  1 
ATOM   1032 H HD3  . PRO A 1 67  ? 8.379  43.182 11.765 0.00 54.72  ? 70  PRO A HD3  1 
ATOM   1033 N N    . PHE A 1 68  ? 11.634 47.415 11.592 1.00 39.66  ? 71  PHE A N    1 
ATOM   1034 C CA   . PHE A 1 68  ? 11.825 48.825 11.897 1.00 52.61  ? 71  PHE A CA   1 
ATOM   1035 C C    . PHE A 1 68  ? 13.136 49.272 11.268 1.00 60.55  ? 71  PHE A C    1 
ATOM   1036 O O    . PHE A 1 68  ? 14.040 48.462 11.046 1.00 54.59  ? 71  PHE A O    1 
ATOM   1037 C CB   . PHE A 1 68  ? 11.817 49.099 13.410 1.00 55.12  ? 71  PHE A CB   1 
ATOM   1038 C CG   . PHE A 1 68  ? 12.918 48.410 14.173 1.00 42.13  ? 71  PHE A CG   1 
ATOM   1039 C CD1  . PHE A 1 68  ? 14.206 48.922 14.183 1.00 49.38  ? 71  PHE A CD1  1 
ATOM   1040 C CD2  . PHE A 1 68  ? 12.656 47.262 14.902 1.00 39.58  ? 71  PHE A CD2  1 
ATOM   1041 C CE1  . PHE A 1 68  ? 15.214 48.294 14.892 1.00 41.89  ? 71  PHE A CE1  1 
ATOM   1042 C CE2  . PHE A 1 68  ? 13.660 46.629 15.614 1.00 40.12  ? 71  PHE A CE2  1 
ATOM   1043 C CZ   . PHE A 1 68  ? 14.940 47.147 15.609 1.00 41.83  ? 71  PHE A CZ   1 
ATOM   1044 H H    . PHE A 1 68  ? 12.360 47.003 11.383 0.00 47.60  ? 71  PHE A H    1 
ATOM   1045 H HA   . PHE A 1 68  ? 11.103 49.344 11.510 0.00 63.15  ? 71  PHE A HA   1 
ATOM   1046 H HB2  . PHE A 1 68  ? 11.915 50.054 13.551 0.00 66.15  ? 71  PHE A HB2  1 
ATOM   1047 H HB3  . PHE A 1 68  ? 10.972 48.795 13.775 0.00 66.15  ? 71  PHE A HB3  1 
ATOM   1048 H HD1  . PHE A 1 68  ? 14.395 49.699 13.707 0.00 59.27  ? 71  PHE A HD1  1 
ATOM   1049 H HD2  . PHE A 1 68  ? 11.795 46.912 14.914 0.00 47.51  ? 71  PHE A HD2  1 
ATOM   1050 H HE1  . PHE A 1 68  ? 16.075 48.644 14.885 0.00 50.29  ? 71  PHE A HE1  1 
ATOM   1051 H HE2  . PHE A 1 68  ? 13.473 45.856 16.095 0.00 48.15  ? 71  PHE A HE2  1 
ATOM   1052 H HZ   . PHE A 1 68  ? 15.615 46.724 16.088 0.00 50.22  ? 71  PHE A HZ   1 
ATOM   1053 N N    . GLY A 1 69  ? 13.224 50.567 10.978 1.00 72.14  ? 72  GLY A N    1 
ATOM   1054 C CA   . GLY A 1 69  ? 14.387 51.082 10.283 1.00 64.90  ? 72  GLY A CA   1 
ATOM   1055 C C    . GLY A 1 69  ? 14.580 50.503 8.901  1.00 74.03  ? 72  GLY A C    1 
ATOM   1056 O O    . GLY A 1 69  ? 15.703 50.497 8.391  1.00 71.37  ? 72  GLY A O    1 
ATOM   1057 H H    . GLY A 1 69  ? 12.630 51.157 11.172 0.00 86.58  ? 72  GLY A H    1 
ATOM   1058 H HA2  . GLY A 1 69  ? 14.301 52.044 10.195 0.00 77.90  ? 72  GLY A HA2  1 
ATOM   1059 H HA3  . GLY A 1 69  ? 15.180 50.882 10.805 0.00 77.90  ? 72  GLY A HA3  1 
ATOM   1060 N N    . GLY A 1 70  ? 13.511 50.010 8.279  1.00 69.39  ? 73  GLY A N    1 
ATOM   1061 C CA   . GLY A 1 70  ? 13.617 49.444 6.950  1.00 57.37  ? 73  GLY A CA   1 
ATOM   1062 C C    . GLY A 1 70  ? 14.280 48.089 6.889  1.00 68.21  ? 73  GLY A C    1 
ATOM   1063 O O    . GLY A 1 70  ? 14.819 47.723 5.842  1.00 65.80  ? 73  GLY A O    1 
ATOM   1064 H H    . GLY A 1 70  ? 12.717 49.994 8.608  0.00 83.28  ? 73  GLY A H    1 
ATOM   1065 H HA2  . GLY A 1 70  ? 12.725 49.354 6.579  0.00 68.86  ? 73  GLY A HA2  1 
ATOM   1066 H HA3  . GLY A 1 70  ? 14.131 50.050 6.393  0.00 68.86  ? 73  GLY A HA3  1 
ATOM   1067 N N    . GLU A 1 71  ? 14.257 47.328 7.981  1.00 69.92  ? 74  GLU A N    1 
ATOM   1068 C CA   . GLU A 1 71  ? 14.899 46.023 8.010  1.00 58.57  ? 74  GLU A CA   1 
ATOM   1069 C C    . GLU A 1 71  ? 14.137 45.108 8.956  1.00 52.48  ? 74  GLU A C    1 
ATOM   1070 O O    . GLU A 1 71  ? 13.451 45.562 9.875  1.00 45.88  ? 74  GLU A O    1 
ATOM   1071 C CB   . GLU A 1 71  ? 16.367 46.131 8.440  1.00 57.13  ? 74  GLU A CB   1 
ATOM   1072 H H    . GLU A 1 71  ? 13.874 47.549 8.719  0.00 83.92  ? 74  GLU A H    1 
ATOM   1073 H HA   . GLU A 1 71  ? 14.866 45.633 7.122  0.00 70.30  ? 74  GLU A HA   1 
ATOM   1074 N N    . GLN A 1 72  ? 14.263 43.806 8.711  1.00 48.77  ? 75  GLN A N    1 
ATOM   1075 C CA   . GLN A 1 72  ? 13.681 42.785 9.576  1.00 46.42  ? 75  GLN A CA   1 
ATOM   1076 C C    . GLN A 1 72  ? 14.704 42.440 10.652 1.00 39.21  ? 75  GLN A C    1 
ATOM   1077 O O    . GLN A 1 72  ? 15.692 41.749 10.382 1.00 62.20  ? 75  GLN A O    1 
ATOM   1078 C CB   . GLN A 1 72  ? 13.286 41.552 8.769  1.00 61.30  ? 75  GLN A CB   1 
ATOM   1079 C CG   . GLN A 1 72  ? 12.102 41.776 7.842  1.00 75.91  ? 75  GLN A CG   1 
ATOM   1080 C CD   . GLN A 1 72  ? 10.985 40.778 8.071  1.00 93.18  ? 75  GLN A CD   1 
ATOM   1081 O OE1  . GLN A 1 72  ? 10.085 41.010 8.879  1.00 84.09  ? 75  GLN A OE1  1 
ATOM   1082 N NE2  . GLN A 1 72  ? 11.036 39.658 7.359  1.00 94.46  ? 75  GLN A NE2  1 
ATOM   1083 H H    . GLN A 1 72  ? 14.689 43.483 8.038  0.00 58.53  ? 75  GLN A H    1 
ATOM   1084 H HA   . GLN A 1 72  ? 12.881 43.131 10.002 0.00 55.72  ? 75  GLN A HA   1 
ATOM   1085 H HB2  . GLN A 1 72  ? 14.041 41.282 8.223  0.00 73.57  ? 75  GLN A HB2  1 
ATOM   1086 H HB3  . GLN A 1 72  ? 13.049 40.840 9.384  0.00 73.57  ? 75  GLN A HB3  1 
ATOM   1087 H HG2  . GLN A 1 72  ? 11.746 42.665 7.992  0.00 91.11  ? 75  GLN A HG2  1 
ATOM   1088 H HG3  . GLN A 1 72  ? 12.399 41.688 6.922  0.00 91.11  ? 75  GLN A HG3  1 
ATOM   1089 H HE21 . GLN A 1 72  ? 11.680 39.530 6.803  0.00 113.37 ? 75  GLN A HE21 1 
ATOM   1090 H HE22 . GLN A 1 72  ? 10.425 39.060 7.453  0.00 113.37 ? 75  GLN A HE22 1 
ATOM   1091 N N    . ASN A 1 73  ? 14.469 42.922 11.867 1.00 45.24  ? 76  ASN A N    1 
ATOM   1092 C CA   . ASN A 1 73  ? 15.446 42.794 12.939 1.00 31.66  ? 76  ASN A CA   1 
ATOM   1093 C C    . ASN A 1 73  ? 15.110 41.600 13.820 1.00 38.74  ? 76  ASN A C    1 
ATOM   1094 O O    . ASN A 1 73  ? 13.960 41.477 14.267 1.00 36.91  ? 76  ASN A O    1 
ATOM   1095 C CB   . ASN A 1 73  ? 15.474 44.067 13.779 1.00 30.54  ? 76  ASN A CB   1 
ATOM   1096 C CG   . ASN A 1 73  ? 15.694 45.312 12.939 1.00 45.78  ? 76  ASN A CG   1 
ATOM   1097 O OD1  . ASN A 1 73  ? 16.831 45.702 12.674 1.00 44.30  ? 76  ASN A OD1  1 
ATOM   1098 N ND2  . ASN A 1 73  ? 14.603 45.936 12.506 1.00 31.71  ? 76  ASN A ND2  1 
ATOM   1099 H H    . ASN A 1 73  ? 13.747 43.329 12.097 0.00 54.30  ? 76  ASN A H    1 
ATOM   1100 H HA   . ASN A 1 73  ? 16.328 42.652 12.561 0.00 38.01  ? 76  ASN A HA   1 
ATOM   1101 H HB2  . ASN A 1 73  ? 14.625 44.162 14.240 0.00 36.66  ? 76  ASN A HB2  1 
ATOM   1102 H HB3  . ASN A 1 73  ? 16.196 44.007 14.423 0.00 36.66  ? 76  ASN A HB3  1 
ATOM   1103 H HD21 . ASN A 1 73  ? 14.676 46.646 12.026 0.00 38.07  ? 76  ASN A HD21 1 
ATOM   1104 H HD22 . ASN A 1 73  ? 13.825 45.629 12.705 0.00 38.07  ? 76  ASN A HD22 1 
ATOM   1105 N N    . PRO A 1 74  ? 16.059 40.701 14.093 1.00 36.99  ? 77  PRO A N    1 
ATOM   1106 C CA   . PRO A 1 74  ? 15.766 39.557 14.971 1.00 33.70  ? 77  PRO A CA   1 
ATOM   1107 C C    . PRO A 1 74  ? 15.686 39.999 16.425 1.00 28.88  ? 77  PRO A C    1 
ATOM   1108 O O    . PRO A 1 74  ? 16.636 40.565 16.969 1.00 35.09  ? 77  PRO A O    1 
ATOM   1109 C CB   . PRO A 1 74  ? 16.946 38.610 14.727 1.00 40.90  ? 77  PRO A CB   1 
ATOM   1110 C CG   . PRO A 1 74  ? 18.060 39.493 14.298 1.00 52.50  ? 77  PRO A CG   1 
ATOM   1111 C CD   . PRO A 1 74  ? 17.452 40.686 13.611 1.00 48.77  ? 77  PRO A CD   1 
ATOM   1112 H HA   . PRO A 1 74  ? 14.937 39.125 14.713 0.00 40.45  ? 77  PRO A HA   1 
ATOM   1113 H HB2  . PRO A 1 74  ? 17.169 38.142 15.547 0.00 49.09  ? 77  PRO A HB2  1 
ATOM   1114 H HB3  . PRO A 1 74  ? 16.720 37.972 14.032 0.00 49.09  ? 77  PRO A HB3  1 
ATOM   1115 H HG2  . PRO A 1 74  ? 18.566 39.774 15.077 0.00 63.01  ? 77  PRO A HG2  1 
ATOM   1116 H HG3  . PRO A 1 74  ? 18.636 39.009 13.686 0.00 63.01  ? 77  PRO A HG3  1 
ATOM   1117 H HD2  . PRO A 1 74  ? 17.913 41.501 13.867 0.00 58.54  ? 77  PRO A HD2  1 
ATOM   1118 H HD3  . PRO A 1 74  ? 17.480 40.578 12.647 0.00 58.54  ? 77  PRO A HD3  1 
ATOM   1119 N N    . ILE A 1 75  ? 14.545 39.732 17.055 1.00 23.48  ? 78  ILE A N    1 
ATOM   1120 C CA   . ILE A 1 75  ? 14.278 40.152 18.426 1.00 22.20  ? 78  ILE A CA   1 
ATOM   1121 C C    . ILE A 1 75  ? 14.008 38.906 19.256 1.00 20.17  ? 78  ILE A C    1 
ATOM   1122 O O    . ILE A 1 75  ? 13.035 38.184 19.005 1.00 20.68  ? 78  ILE A O    1 
ATOM   1123 C CB   . ILE A 1 75  ? 13.094 41.130 18.500 1.00 30.90  ? 78  ILE A CB   1 
ATOM   1124 C CG1  . ILE A 1 75  ? 13.439 42.444 17.787 1.00 19.01  ? 78  ILE A CG1  1 
ATOM   1125 C CG2  . ILE A 1 75  ? 12.701 41.387 19.949 1.00 30.15  ? 78  ILE A CG2  1 
ATOM   1126 C CD1  . ILE A 1 75  ? 14.498 43.281 18.489 1.00 24.97  ? 78  ILE A CD1  1 
ATOM   1127 H H    . ILE A 1 75  ? 13.894 39.298 16.698 0.00 28.19  ? 78  ILE A H    1 
ATOM   1128 H HA   . ILE A 1 75  ? 15.063 40.592 18.786 0.00 26.65  ? 78  ILE A HA   1 
ATOM   1129 H HB   . ILE A 1 75  ? 12.337 40.727 18.047 0.00 37.10  ? 78  ILE A HB   1 
ATOM   1130 H HG12 . ILE A 1 75  ? 13.770 42.237 16.899 0.00 22.74  ? 78  ILE A HG12 1 
ATOM   1131 H HG13 . ILE A 1 75  ? 12.634 42.982 17.724 0.00 22.74  ? 78  ILE A HG13 1 
ATOM   1132 H HG21 . ILE A 1 75  ? 12.156 42.189 19.991 0.00 36.19  ? 78  ILE A HG21 1 
ATOM   1133 H HG22 . ILE A 1 75  ? 12.196 40.627 20.279 0.00 36.19  ? 78  ILE A HG22 1 
ATOM   1134 H HG23 . ILE A 1 75  ? 13.505 41.505 20.478 0.00 36.19  ? 78  ILE A HG23 1 
ATOM   1135 H HD11 . ILE A 1 75  ? 14.681 44.071 17.957 0.00 29.98  ? 78  ILE A HD11 1 
ATOM   1136 H HD12 . ILE A 1 75  ? 14.167 43.541 19.363 0.00 29.98  ? 78  ILE A HD12 1 
ATOM   1137 H HD13 . ILE A 1 75  ? 15.306 42.753 18.585 0.00 29.98  ? 78  ILE A HD13 1 
ATOM   1138 N N    . TYR A 1 76  ? 14.870 38.653 20.239 1.00 16.42  ? 79  TYR A N    1 
ATOM   1139 C CA   . TYR A 1 76  ? 14.678 37.547 21.175 1.00 20.75  ? 79  TYR A CA   1 
ATOM   1140 C C    . TYR A 1 76  ? 13.678 37.993 22.234 1.00 28.31  ? 79  TYR A C    1 
ATOM   1141 O O    . TYR A 1 76  ? 14.041 38.652 23.211 1.00 14.50  ? 79  TYR A O    1 
ATOM   1142 C CB   . TYR A 1 76  ? 16.005 37.133 21.800 1.00 15.33  ? 79  TYR A CB   1 
ATOM   1143 C CG   . TYR A 1 76  ? 16.865 36.270 20.902 1.00 17.99  ? 79  TYR A CG   1 
ATOM   1144 C CD1  . TYR A 1 76  ? 16.629 34.906 20.786 1.00 22.80  ? 79  TYR A CD1  1 
ATOM   1145 C CD2  . TYR A 1 76  ? 17.916 36.816 20.176 1.00 17.85  ? 79  TYR A CD2  1 
ATOM   1146 C CE1  . TYR A 1 76  ? 17.411 34.110 19.971 1.00 16.55  ? 79  TYR A CE1  1 
ATOM   1147 C CE2  . TYR A 1 76  ? 18.707 36.026 19.357 1.00 25.94  ? 79  TYR A CE2  1 
ATOM   1148 C CZ   . TYR A 1 76  ? 18.448 34.673 19.261 1.00 24.86  ? 79  TYR A CZ   1 
ATOM   1149 O OH   . TYR A 1 76  ? 19.223 33.879 18.449 1.00 20.35  ? 79  TYR A OH   1 
ATOM   1150 H H    . TYR A 1 76  ? 15.582 39.112 20.386 0.00 19.63  ? 79  TYR A H    1 
ATOM   1151 H HA   . TYR A 1 76  ? 14.314 36.781 20.705 0.00 24.91  ? 79  TYR A HA   1 
ATOM   1152 H HB2  . TYR A 1 76  ? 16.511 37.933 22.013 0.00 18.32  ? 79  TYR A HB2  1 
ATOM   1153 H HB3  . TYR A 1 76  ? 15.825 36.630 22.609 0.00 18.32  ? 79  TYR A HB3  1 
ATOM   1154 H HD1  . TYR A 1 76  ? 15.931 34.522 21.266 0.00 27.37  ? 79  TYR A HD1  1 
ATOM   1155 H HD2  . TYR A 1 76  ? 18.092 37.727 20.241 0.00 21.44  ? 79  TYR A HD2  1 
ATOM   1156 H HE1  . TYR A 1 76  ? 17.238 33.198 19.903 0.00 19.79  ? 79  TYR A HE1  1 
ATOM   1157 H HE2  . TYR A 1 76  ? 19.407 36.405 18.875 0.00 31.14  ? 79  TYR A HE2  1 
ATOM   1158 H HH   . TYR A 1 76  ? 19.796 34.347 18.052 0.00 24.43  ? 79  TYR A HH   1 
ATOM   1159 N N    . TRP A 1 77  ? 12.406 37.638 22.041 1.00 15.12  ? 80  TRP A N    1 
ATOM   1160 C CA   . TRP A 1 77  ? 11.361 38.057 22.967 1.00 15.57  ? 80  TRP A CA   1 
ATOM   1161 C C    . TRP A 1 77  ? 11.347 37.237 24.250 1.00 13.94  ? 80  TRP A C    1 
ATOM   1162 O O    . TRP A 1 77  ? 10.780 37.690 25.251 1.00 16.79  ? 80  TRP A O    1 
ATOM   1163 C CB   . TRP A 1 77  ? 9.988  37.973 22.290 1.00 15.20  ? 80  TRP A CB   1 
ATOM   1164 C CG   . TRP A 1 77  ? 9.608  36.589 21.851 1.00 15.48  ? 80  TRP A CG   1 
ATOM   1165 C CD1  . TRP A 1 77  ? 9.722  36.068 20.595 1.00 23.11  ? 80  TRP A CD1  1 
ATOM   1166 C CD2  . TRP A 1 77  ? 9.049  35.548 22.667 1.00 18.50  ? 80  TRP A CD2  1 
ATOM   1167 N NE1  . TRP A 1 77  ? 9.272  34.769 20.577 1.00 22.16  ? 80  TRP A NE1  1 
ATOM   1168 C CE2  . TRP A 1 77  ? 8.854  34.426 21.836 1.00 27.94  ? 80  TRP A CE2  1 
ATOM   1169 C CE3  . TRP A 1 77  ? 8.697  35.456 24.018 1.00 19.72  ? 80  TRP A CE3  1 
ATOM   1170 C CZ2  . TRP A 1 77  ? 8.323  33.228 22.311 1.00 30.40  ? 80  TRP A CZ2  1 
ATOM   1171 C CZ3  . TRP A 1 77  ? 8.170  34.264 24.488 1.00 14.38  ? 80  TRP A CZ3  1 
ATOM   1172 C CH2  . TRP A 1 77  ? 7.989  33.167 23.637 1.00 18.64  ? 80  TRP A CH2  1 
ATOM   1173 H H    . TRP A 1 77  ? 12.127 37.157 21.385 0.00 18.07  ? 80  TRP A H    1 
ATOM   1174 H HA   . TRP A 1 77  ? 11.519 38.984 23.209 0.00 18.69  ? 80  TRP A HA   1 
ATOM   1175 H HB2  . TRP A 1 77  ? 9.313  38.279 22.916 0.00 18.17  ? 80  TRP A HB2  1 
ATOM   1176 H HB3  . TRP A 1 77  ? 9.993  38.541 21.504 0.00 18.17  ? 80  TRP A HB3  1 
ATOM   1177 H HD1  . TRP A 1 77  ? 10.056 36.526 19.858 0.00 27.75  ? 80  TRP A HD1  1 
ATOM   1178 H HE1  . TRP A 1 77  ? 9.256  34.256 19.887 0.00 26.61  ? 80  TRP A HE1  1 
ATOM   1179 H HE3  . TRP A 1 77  ? 8.815  36.181 24.589 0.00 23.68  ? 80  TRP A HE3  1 
ATOM   1180 H HZ2  . TRP A 1 77  ? 8.200  32.498 21.749 0.00 36.49  ? 80  TRP A HZ2  1 
ATOM   1181 H HZ3  . TRP A 1 77  ? 7.932  34.191 25.384 0.00 17.18  ? 80  TRP A HZ3  1 
ATOM   1182 H HH2  . TRP A 1 77  ? 7.634  32.379 23.980 0.00 22.38  ? 80  TRP A HH2  1 
ATOM   1183 N N    . ALA A 1 78  ? 11.958 36.049 24.248 1.00 13.89  ? 81  ALA A N    1 
ATOM   1184 C CA   . ALA A 1 78  ? 11.918 35.188 25.425 1.00 17.19  ? 81  ALA A CA   1 
ATOM   1185 C C    . ALA A 1 78  ? 12.636 35.799 26.621 1.00 17.37  ? 81  ALA A C    1 
ATOM   1186 O O    . ALA A 1 78  ? 12.358 35.404 27.759 1.00 12.57  ? 81  ALA A O    1 
ATOM   1187 C CB   . ALA A 1 78  ? 12.528 33.824 25.100 1.00 24.27  ? 81  ALA A CB   1 
ATOM   1188 H H    . ALA A 1 78  ? 12.397 35.724 23.583 0.00 16.64  ? 81  ALA A H    1 
ATOM   1189 H HA   . ALA A 1 78  ? 10.990 35.055 25.673 0.00 20.65  ? 81  ALA A HA   1 
ATOM   1190 H HB1  . ALA A 1 78  ? 12.529 33.279 25.902 0.00 29.14  ? 81  ALA A HB1  1 
ATOM   1191 H HB2  . ALA A 1 78  ? 11.997 33.396 24.410 0.00 29.14  ? 81  ALA A HB2  1 
ATOM   1192 H HB3  . ALA A 1 78  ? 13.437 33.951 24.785 0.00 29.14  ? 81  ALA A HB3  1 
ATOM   1193 N N    . ARG A 1 79  ? 13.556 36.743 26.396 1.00 12.91  ? 82  ARG A N    1 
ATOM   1194 C CA   . ARG A 1 79  ? 14.236 37.394 27.513 1.00 13.13  ? 82  ARG A CA   1 
ATOM   1195 C C    . ARG A 1 79  ? 13.238 38.053 28.456 1.00 13.86  ? 82  ARG A C    1 
ATOM   1196 O O    . ARG A 1 79  ? 13.402 38.008 29.680 1.00 16.03  ? 82  ARG A O    1 
ATOM   1197 C CB   . ARG A 1 79  ? 15.226 38.440 26.999 1.00 20.15  ? 82  ARG A CB   1 
ATOM   1198 C CG   . ARG A 1 79  ? 16.380 37.894 26.181 1.00 19.20  ? 82  ARG A CG   1 
ATOM   1199 C CD   . ARG A 1 79  ? 17.443 38.970 25.988 1.00 15.79  ? 82  ARG A CD   1 
ATOM   1200 N NE   . ARG A 1 79  ? 18.464 38.579 25.024 1.00 20.71  ? 82  ARG A NE   1 
ATOM   1201 C CZ   . ARG A 1 79  ? 19.441 37.718 25.276 1.00 19.47  ? 82  ARG A CZ   1 
ATOM   1202 N NH1  . ARG A 1 79  ? 19.557 37.129 26.455 1.00 24.65  ? 82  ARG A NH1  1 
ATOM   1203 N NH2  . ARG A 1 79  ? 20.325 37.444 24.322 1.00 26.90  ? 82  ARG A NH2  1 
ATOM   1204 H H    . ARG A 1 79  ? 13.799 37.019 25.618 0.00 15.42  ? 82  ARG A H    1 
ATOM   1205 H HA   . ARG A 1 79  ? 14.730 36.718 28.004 0.00 15.77  ? 82  ARG A HA   1 
ATOM   1206 H HB2  . ARG A 1 79  ? 14.744 39.067 26.437 0.00 24.19  ? 82  ARG A HB2  1 
ATOM   1207 H HB3  . ARG A 1 79  ? 15.606 38.902 27.763 0.00 24.19  ? 82  ARG A HB3  1 
ATOM   1208 H HG2  . ARG A 1 79  ? 16.781 37.141 26.644 0.00 23.06  ? 82  ARG A HG2  1 
ATOM   1209 H HG3  . ARG A 1 79  ? 16.059 37.614 25.310 0.00 23.06  ? 82  ARG A HG3  1 
ATOM   1210 H HD2  . ARG A 1 79  ? 17.019 39.780 25.664 0.00 18.96  ? 82  ARG A HD2  1 
ATOM   1211 H HD3  . ARG A 1 79  ? 17.881 39.140 26.836 0.00 18.96  ? 82  ARG A HD3  1 
ATOM   1212 H HE   . ARG A 1 79  ? 18.430 38.929 24.239 0.00 24.86  ? 82  ARG A HE   1 
ATOM   1213 H HH11 . ARG A 1 79  ? 18.991 37.300 27.079 0.00 29.59  ? 82  ARG A HH11 1 
ATOM   1214 H HH12 . ARG A 1 79  ? 20.198 36.574 26.597 0.00 29.59  ? 82  ARG A HH12 1 
ATOM   1215 H HH21 . ARG A 1 79  ? 20.259 37.823 23.553 0.00 32.29  ? 82  ARG A HH21 1 
ATOM   1216 H HH22 . ARG A 1 79  ? 20.963 36.887 24.474 0.00 32.29  ? 82  ARG A HH22 1 
ATOM   1217 N N    . TYR A 1 80  ? 12.199 38.678 27.900 1.00 12.46  ? 83  TYR A N    1 
ATOM   1218 C CA   . TYR A 1 80  ? 11.250 39.416 28.725 1.00 12.32  ? 83  TYR A CA   1 
ATOM   1219 C C    . TYR A 1 80  ? 10.334 38.478 29.499 1.00 16.49  ? 83  TYR A C    1 
ATOM   1220 O O    . TYR A 1 80  ? 9.942  38.792 30.629 1.00 12.60  ? 83  TYR A O    1 
ATOM   1221 C CB   . TYR A 1 80  ? 10.447 40.372 27.842 1.00 15.10  ? 83  TYR A CB   1 
ATOM   1222 C CG   . TYR A 1 80  ? 11.345 41.280 27.033 1.00 15.44  ? 83  TYR A CG   1 
ATOM   1223 C CD1  . TYR A 1 80  ? 11.798 42.484 27.556 1.00 19.19  ? 83  TYR A CD1  1 
ATOM   1224 C CD2  . TYR A 1 80  ? 11.767 40.919 25.759 1.00 13.45  ? 83  TYR A CD2  1 
ATOM   1225 C CE1  . TYR A 1 80  ? 12.633 43.311 26.829 1.00 22.16  ? 83  TYR A CE1  1 
ATOM   1226 C CE2  . TYR A 1 80  ? 12.603 41.741 25.023 1.00 13.90  ? 83  TYR A CE2  1 
ATOM   1227 C CZ   . TYR A 1 80  ? 13.034 42.935 25.565 1.00 18.16  ? 83  TYR A CZ   1 
ATOM   1228 O OH   . TYR A 1 80  ? 13.865 43.759 24.842 1.00 23.62  ? 83  TYR A OH   1 
ATOM   1229 H H    . TYR A 1 80  ? 12.025 38.689 27.058 0.00 14.97  ? 83  TYR A H    1 
ATOM   1230 H HA   . TYR A 1 80  ? 11.731 39.948 29.377 0.00 14.80  ? 83  TYR A HA   1 
ATOM   1231 H HB2  . TYR A 1 80  ? 9.902  39.857 27.227 0.00 18.13  ? 83  TYR A HB2  1 
ATOM   1232 H HB3  . TYR A 1 80  ? 9.882  40.926 28.403 0.00 18.13  ? 83  TYR A HB3  1 
ATOM   1233 H HD1  . TYR A 1 80  ? 11.535 42.738 28.411 0.00 23.04  ? 83  TYR A HD1  1 
ATOM   1234 H HD2  . TYR A 1 80  ? 11.484 40.112 25.396 0.00 16.07  ? 83  TYR A HD2  1 
ATOM   1235 H HE1  . TYR A 1 80  ? 12.924 44.116 27.191 0.00 26.60  ? 83  TYR A HE1  1 
ATOM   1236 H HE2  . TYR A 1 80  ? 12.873 41.490 24.169 0.00 16.61  ? 83  TYR A HE2  1 
ATOM   1237 H HH   . TYR A 1 80  ? 14.064 43.396 24.111 0.00 28.36  ? 83  TYR A HH   1 
ATOM   1238 N N    . ALA A 1 81  ? 9.987  37.328 28.915 1.00 12.32  ? 84  ALA A N    1 
ATOM   1239 C CA   . ALA A 1 81  ? 9.238  36.323 29.661 1.00 14.17  ? 84  ALA A CA   1 
ATOM   1240 C C    . ALA A 1 81  ? 10.066 35.788 30.821 1.00 14.39  ? 84  ALA A C    1 
ATOM   1241 O O    . ALA A 1 81  ? 9.532  35.509 31.901 1.00 21.64  ? 84  ALA A O    1 
ATOM   1242 C CB   . ALA A 1 81  ? 8.813  35.188 28.730 1.00 18.04  ? 84  ALA A CB   1 
ATOM   1243 H H    . ALA A 1 81  ? 10.170 37.112 28.103 0.00 14.80  ? 84  ALA A H    1 
ATOM   1244 H HA   . ALA A 1 81  ? 8.433  36.727 30.022 0.00 17.01  ? 84  ALA A HA   1 
ATOM   1245 H HB1  . ALA A 1 81  ? 8.311  34.533 29.239 0.00 21.66  ? 84  ALA A HB1  1 
ATOM   1246 H HB2  . ALA A 1 81  ? 8.259  35.551 28.021 0.00 21.66  ? 84  ALA A HB2  1 
ATOM   1247 H HB3  . ALA A 1 81  ? 9.606  34.776 28.352 0.00 21.66  ? 84  ALA A HB3  1 
ATOM   1248 N N    . ASP A 1 82  ? 11.374 35.631 30.609 1.00 18.66  ? 85  ASP A N    1 
ATOM   1249 C CA   . ASP A 1 82  ? 12.284 35.298 31.701 1.00 12.35  ? 85  ASP A CA   1 
ATOM   1250 C C    . ASP A 1 82  ? 12.264 36.390 32.765 1.00 14.32  ? 85  ASP A C    1 
ATOM   1251 O O    . ASP A 1 82  ? 11.923 36.144 33.928 1.00 12.12  ? 85  ASP A O    1 
ATOM   1252 C CB   . ASP A 1 82  ? 13.697 35.099 31.133 1.00 18.68  ? 85  ASP A CB   1 
ATOM   1253 C CG   . ASP A 1 82  ? 14.759 34.872 32.206 1.00 18.54  ? 85  ASP A CG   1 
ATOM   1254 O OD1  . ASP A 1 82  ? 14.532 35.186 33.393 1.00 11.76  ? 85  ASP A OD1  1 
ATOM   1255 O OD2  . ASP A 1 82  ? 15.849 34.376 31.845 1.00 17.17  ? 85  ASP A OD2  1 
ATOM   1256 H H    . ASP A 1 82  ? 11.758 35.712 29.844 0.00 22.41  ? 85  ASP A H    1 
ATOM   1257 H HA   . ASP A 1 82  ? 12.007 34.469 32.121 0.00 14.83  ? 85  ASP A HA   1 
ATOM   1258 H HB2  . ASP A 1 82  ? 13.694 34.323 30.551 0.00 22.43  ? 85  ASP A HB2  1 
ATOM   1259 H HB3  . ASP A 1 82  ? 13.947 35.890 30.631 0.00 22.43  ? 85  ASP A HB3  1 
ATOM   1260 N N    . TRP A 1 83  ? 12.616 37.616 32.372 1.00 11.49  ? 86  TRP A N    1 
ATOM   1261 C CA   . TRP A 1 83  ? 12.762 38.697 33.340 1.00 11.41  ? 86  TRP A CA   1 
ATOM   1262 C C    . TRP A 1 83  ? 11.446 39.019 34.034 1.00 17.11  ? 86  TRP A C    1 
ATOM   1263 O O    . TRP A 1 83  ? 11.448 39.468 35.186 1.00 11.53  ? 86  TRP A O    1 
ATOM   1264 C CB   . TRP A 1 83  ? 13.316 39.940 32.642 1.00 11.49  ? 86  TRP A CB   1 
ATOM   1265 C CG   . TRP A 1 83  ? 14.675 39.723 32.037 1.00 11.63  ? 86  TRP A CG   1 
ATOM   1266 C CD1  . TRP A 1 83  ? 15.586 38.767 32.390 1.00 11.67  ? 86  TRP A CD1  1 
ATOM   1267 C CD2  . TRP A 1 83  ? 15.273 40.473 30.973 1.00 11.90  ? 86  TRP A CD2  1 
ATOM   1268 N NE1  . TRP A 1 83  ? 16.714 38.878 31.613 1.00 15.05  ? 86  TRP A NE1  1 
ATOM   1269 C CE2  . TRP A 1 83  ? 16.547 39.918 30.736 1.00 14.86  ? 86  TRP A CE2  1 
ATOM   1270 C CE3  . TRP A 1 83  ? 14.855 41.560 30.199 1.00 13.71  ? 86  TRP A CE3  1 
ATOM   1271 C CZ2  . TRP A 1 83  ? 17.407 40.413 29.757 1.00 14.84  ? 86  TRP A CZ2  1 
ATOM   1272 C CZ3  . TRP A 1 83  ? 15.712 42.051 29.228 1.00 14.29  ? 86  TRP A CZ3  1 
ATOM   1273 C CH2  . TRP A 1 83  ? 16.971 41.477 29.015 1.00 16.61  ? 86  TRP A CH2  1 
ATOM   1274 H H    . TRP A 1 83  ? 12.775 37.844 31.558 0.00 13.72  ? 86  TRP A H    1 
ATOM   1275 H HA   . TRP A 1 83  ? 13.394 38.424 34.023 0.00 13.61  ? 86  TRP A HA   1 
ATOM   1276 H HB2  . TRP A 1 83  ? 12.710 40.197 31.930 0.00 13.71  ? 86  TRP A HB2  1 
ATOM   1277 H HB3  . TRP A 1 83  ? 13.390 40.658 33.290 0.00 13.71  ? 86  TRP A HB3  1 
ATOM   1278 H HD1  . TRP A 1 83  ? 15.461 38.133 33.059 0.00 13.92  ? 86  TRP A HD1  1 
ATOM   1279 H HE1  . TRP A 1 83  ? 17.410 38.377 31.668 0.00 18.08  ? 86  TRP A HE1  1 
ATOM   1280 H HE3  . TRP A 1 83  ? 14.019 41.945 30.333 0.00 16.47  ? 86  TRP A HE3  1 
ATOM   1281 H HZ2  . TRP A 1 83  ? 18.244 40.034 29.613 0.00 17.82  ? 86  TRP A HZ2  1 
ATOM   1282 H HZ3  . TRP A 1 83  ? 15.446 42.775 28.708 0.00 17.17  ? 86  TRP A HZ3  1 
ATOM   1283 H HH2  . TRP A 1 83  ? 17.525 41.827 28.355 0.00 19.95  ? 86  TRP A HH2  1 
ATOM   1284 N N    . LEU A 1 84  ? 10.316 38.799 33.356 1.00 13.37  ? 87  LEU A N    1 
ATOM   1285 C CA   . LEU A 1 84  ? 9.021  39.080 33.968 1.00 11.57  ? 87  LEU A CA   1 
ATOM   1286 C C    . LEU A 1 84  ? 8.835  38.310 35.268 1.00 24.61  ? 87  LEU A C    1 
ATOM   1287 O O    . LEU A 1 84  ? 8.194  38.811 36.200 1.00 20.21  ? 87  LEU A O    1 
ATOM   1288 C CB   . LEU A 1 84  ? 7.896  38.739 32.987 1.00 17.13  ? 87  LEU A CB   1 
ATOM   1289 C CG   . LEU A 1 84  ? 6.462  38.898 33.502 1.00 23.95  ? 87  LEU A CG   1 
ATOM   1290 C CD1  . LEU A 1 84  ? 6.131  40.365 33.737 1.00 21.91  ? 87  LEU A CD1  1 
ATOM   1291 C CD2  . LEU A 1 84  ? 5.473  38.272 32.529 1.00 25.82  ? 87  LEU A CD2  1 
ATOM   1292 H H    . LEU A 1 84  ? 10.274 38.493 32.554 0.00 16.05  ? 87  LEU A H    1 
ATOM   1293 H HA   . LEU A 1 84  ? 8.970  40.027 34.171 0.00 13.81  ? 87  LEU A HA   1 
ATOM   1294 H HB2  . LEU A 1 84  ? 7.987  39.319 32.215 0.00 20.57  ? 87  LEU A HB2  1 
ATOM   1295 H HB3  . LEU A 1 84  ? 8.002  37.812 32.721 0.00 20.57  ? 87  LEU A HB3  1 
ATOM   1296 H HG   . LEU A 1 84  ? 6.381  38.437 34.351 0.00 28.75  ? 87  LEU A HG   1 
ATOM   1297 H HD11 . LEU A 1 84  ? 5.208  40.438 34.027 0.00 26.31  ? 87  LEU A HD11 1 
ATOM   1298 H HD12 . LEU A 1 84  ? 6.722  40.717 34.421 0.00 26.31  ? 87  LEU A HD12 1 
ATOM   1299 H HD13 . LEU A 1 84  ? 6.256  40.854 32.908 0.00 26.31  ? 87  LEU A HD13 1 
ATOM   1300 H HD21 . LEU A 1 84  ? 4.575  38.376 32.881 0.00 31.00  ? 87  LEU A HD21 1 
ATOM   1301 H HD22 . LEU A 1 84  ? 5.547  38.720 31.672 0.00 31.00  ? 87  LEU A HD22 1 
ATOM   1302 H HD23 . LEU A 1 84  ? 5.682  37.330 32.429 0.00 31.00  ? 87  LEU A HD23 1 
ATOM   1303 N N    . PHE A 1 85  ? 9.382  37.098 35.354 1.00 13.04  ? 88  PHE A N    1 
ATOM   1304 C CA   . PHE A 1 85  ? 9.209  36.259 36.533 1.00 22.04  ? 88  PHE A CA   1 
ATOM   1305 C C    . PHE A 1 85  ? 10.438 36.209 37.430 1.00 13.46  ? 88  PHE A C    1 
ATOM   1306 O O    . PHE A 1 85  ? 10.291 36.036 38.645 1.00 25.64  ? 88  PHE A O    1 
ATOM   1307 C CB   . PHE A 1 85  ? 8.834  34.833 36.110 1.00 19.92  ? 88  PHE A CB   1 
ATOM   1308 C CG   . PHE A 1 85  ? 7.486  34.735 35.447 1.00 21.32  ? 88  PHE A CG   1 
ATOM   1309 C CD1  . PHE A 1 85  ? 6.323  34.801 36.197 1.00 25.08  ? 88  PHE A CD1  1 
ATOM   1310 C CD2  . PHE A 1 85  ? 7.384  34.584 34.073 1.00 26.67  ? 88  PHE A CD2  1 
ATOM   1311 C CE1  . PHE A 1 85  ? 5.080  34.714 35.590 1.00 37.68  ? 88  PHE A CE1  1 
ATOM   1312 C CE2  . PHE A 1 85  ? 6.144  34.497 33.459 1.00 29.67  ? 88  PHE A CE2  1 
ATOM   1313 C CZ   . PHE A 1 85  ? 4.991  34.562 34.219 1.00 21.46  ? 88  PHE A CZ   1 
ATOM   1314 H H    . PHE A 1 85  ? 9.862  36.739 34.737 0.00 15.67  ? 88  PHE A H    1 
ATOM   1315 H HA   . PHE A 1 85  ? 8.480  36.616 37.064 0.00 26.46  ? 88  PHE A HA   1 
ATOM   1316 H HB2  . PHE A 1 85  ? 9.498  34.509 35.482 0.00 23.92  ? 88  PHE A HB2  1 
ATOM   1317 H HB3  . PHE A 1 85  ? 8.819  34.268 36.898 0.00 23.92  ? 88  PHE A HB3  1 
ATOM   1318 H HD1  . PHE A 1 85  ? 6.377  34.905 37.120 0.00 30.11  ? 88  PHE A HD1  1 
ATOM   1319 H HD2  . PHE A 1 85  ? 8.156  34.540 33.556 0.00 32.02  ? 88  PHE A HD2  1 
ATOM   1320 H HE1  . PHE A 1 85  ? 4.307  34.758 36.104 0.00 45.23  ? 88  PHE A HE1  1 
ATOM   1321 H HE2  . PHE A 1 85  ? 6.088  34.395 32.536 0.00 35.62  ? 88  PHE A HE2  1 
ATOM   1322 H HZ   . PHE A 1 85  ? 4.158  34.503 33.809 0.00 25.76  ? 88  PHE A HZ   1 
ATOM   1323 N N    . THR A 1 86  ? 11.644 36.379 36.882 1.00 12.98  ? 89  THR A N    1 
ATOM   1324 C CA   . THR A 1 86  ? 12.838 36.248 37.712 1.00 14.93  ? 89  THR A CA   1 
ATOM   1325 C C    . THR A 1 86  ? 13.183 37.542 38.442 1.00 14.80  ? 89  THR A C    1 
ATOM   1326 O O    . THR A 1 86  ? 13.708 37.486 39.560 1.00 16.23  ? 89  THR A O    1 
ATOM   1327 C CB   . THR A 1 86  ? 14.034 35.787 36.873 1.00 11.86  ? 89  THR A CB   1 
ATOM   1328 O OG1  . THR A 1 86  ? 14.199 36.645 35.737 1.00 11.79  ? 89  THR A OG1  1 
ATOM   1329 C CG2  . THR A 1 86  ? 13.840 34.353 36.409 1.00 11.97  ? 89  THR A CG2  1 
ATOM   1330 H H    . THR A 1 86  ? 11.792 36.565 36.055 0.00 15.59  ? 89  THR A H    1 
ATOM   1331 H HA   . THR A 1 86  ? 12.664 35.565 38.378 0.00 17.93  ? 89  THR A HA   1 
ATOM   1332 H HB   . THR A 1 86  ? 14.838 35.826 37.415 0.00 14.15  ? 89  THR A HB   1 
ATOM   1333 H HG1  . THR A 1 86  ? 14.804 36.346 35.236 0.00 14.17  ? 89  THR A HG1  1 
ATOM   1334 H HG21 . THR A 1 86  ? 14.622 34.053 35.919 0.00 14.29  ? 89  THR A HG21 1 
ATOM   1335 H HG22 . THR A 1 86  ? 13.706 33.772 37.174 0.00 14.29  ? 89  THR A HG22 1 
ATOM   1336 H HG23 . THR A 1 86  ? 13.064 34.294 35.829 0.00 14.29  ? 89  THR A HG23 1 
ATOM   1337 N N    . THR A 1 87  ? 12.897 38.708 37.853 1.00 14.71  ? 90  THR A N    1 
ATOM   1338 C CA   . THR A 1 87  ? 13.271 39.946 38.531 1.00 17.53  ? 90  THR A CA   1 
ATOM   1339 C C    . THR A 1 87  ? 12.407 40.157 39.774 1.00 16.19  ? 90  THR A C    1 
ATOM   1340 O O    . THR A 1 87  ? 12.931 40.590 40.808 1.00 17.90  ? 90  THR A O    1 
ATOM   1341 C CB   . THR A 1 87  ? 13.192 41.162 37.592 1.00 14.52  ? 90  THR A CB   1 
ATOM   1342 O OG1  . THR A 1 87  ? 11.986 41.140 36.823 1.00 11.52  ? 90  THR A OG1  1 
ATOM   1343 C CG2  . THR A 1 87  ? 14.387 41.182 36.643 1.00 13.38  ? 90  THR A CG2  1 
ATOM   1344 H H    . THR A 1 87  ? 12.504 38.800 37.094 0.00 17.67  ? 90  THR A H    1 
ATOM   1345 H HA   . THR A 1 87  ? 14.195 39.868 38.817 0.00 21.05  ? 90  THR A HA   1 
ATOM   1346 H HB   . THR A 1 87  ? 13.201 41.968 38.132 0.00 17.44  ? 90  THR A HB   1 
ATOM   1347 H HG1  . THR A 1 87  ? 11.424 41.670 37.154 0.00 13.75  ? 90  THR A HG1  1 
ATOM   1348 H HG21 . THR A 1 87  ? 14.359 41.979 36.091 0.00 16.07  ? 90  THR A HG21 1 
ATOM   1349 H HG22 . THR A 1 87  ? 15.213 41.179 37.151 0.00 16.07  ? 90  THR A HG22 1 
ATOM   1350 H HG23 . THR A 1 87  ? 14.367 40.400 36.069 0.00 16.07  ? 90  THR A HG23 1 
ATOM   1351 N N    . PRO A 1 88  ? 11.101 39.859 39.741 1.00 22.64  ? 91  PRO A N    1 
ATOM   1352 C CA   . PRO A 1 88  ? 10.328 39.935 40.996 1.00 21.30  ? 91  PRO A CA   1 
ATOM   1353 C C    . PRO A 1 88  ? 10.847 38.998 42.071 1.00 26.55  ? 91  PRO A C    1 
ATOM   1354 O O    . PRO A 1 88  ? 10.897 39.377 43.249 1.00 16.27  ? 91  PRO A O    1 
ATOM   1355 C CB   . PRO A 1 88  ? 8.902  39.557 40.563 1.00 17.95  ? 91  PRO A CB   1 
ATOM   1356 C CG   . PRO A 1 88  ? 8.867  39.727 39.098 1.00 28.01  ? 91  PRO A CG   1 
ATOM   1357 C CD   . PRO A 1 88  ? 10.249 39.473 38.603 1.00 17.23  ? 91  PRO A CD   1 
ATOM   1358 H HA   . PRO A 1 88  ? 10.333 40.847 41.324 0.00 25.57  ? 91  PRO A HA   1 
ATOM   1359 H HB2  . PRO A 1 88  ? 8.720  38.636 40.808 0.00 21.56  ? 91  PRO A HB2  1 
ATOM   1360 H HB3  . PRO A 1 88  ? 8.263  40.147 40.993 0.00 21.56  ? 91  PRO A HB3  1 
ATOM   1361 H HG2  . PRO A 1 88  ? 8.245  39.089 38.714 0.00 33.63  ? 91  PRO A HG2  1 
ATOM   1362 H HG3  . PRO A 1 88  ? 8.589  40.631 38.884 0.00 33.63  ? 91  PRO A HG3  1 
ATOM   1363 H HD2  . PRO A 1 88  ? 10.370 38.536 38.385 0.00 20.69  ? 91  PRO A HD2  1 
ATOM   1364 H HD3  . PRO A 1 88  ? 10.442 40.022 37.827 0.00 20.69  ? 91  PRO A HD3  1 
ATOM   1365 N N    . LEU A 1 89  ? 11.222 37.771 41.698 1.00 17.26  ? 92  LEU A N    1 
ATOM   1366 C CA   . LEU A 1 89  ? 11.708 36.812 42.685 1.00 19.31  ? 92  LEU A CA   1 
ATOM   1367 C C    . LEU A 1 89  ? 12.999 37.297 43.332 1.00 17.35  ? 92  LEU A C    1 
ATOM   1368 O O    . LEU A 1 89  ? 13.207 37.113 44.537 1.00 23.47  ? 92  LEU A O    1 
ATOM   1369 C CB   . LEU A 1 89  ? 11.916 35.447 42.027 1.00 13.36  ? 92  LEU A CB   1 
ATOM   1370 C CG   . LEU A 1 89  ? 10.642 34.736 41.563 1.00 24.36  ? 92  LEU A CG   1 
ATOM   1371 C CD1  . LEU A 1 89  ? 10.977 33.528 40.694 1.00 16.65  ? 92  LEU A CD1  1 
ATOM   1372 C CD2  . LEU A 1 89  ? 9.792  34.323 42.755 1.00 22.62  ? 92  LEU A CD2  1 
ATOM   1373 H H    . LEU A 1 89  ? 11.205 37.476 40.891 0.00 20.73  ? 92  LEU A H    1 
ATOM   1374 H HA   . LEU A 1 89  ? 11.041 36.712 43.382 0.00 23.19  ? 92  LEU A HA   1 
ATOM   1375 H HB2  . LEU A 1 89  ? 12.480 35.568 41.247 0.00 15.95  ? 92  LEU A HB2  1 
ATOM   1376 H HB3  . LEU A 1 89  ? 12.355 34.865 42.667 0.00 15.95  ? 92  LEU A HB3  1 
ATOM   1377 H HG   . LEU A 1 89  ? 10.122 35.352 41.023 0.00 29.25  ? 92  LEU A HG   1 
ATOM   1378 H HD11 . LEU A 1 89  ? 10.153 33.080 40.444 0.00 20.00  ? 92  LEU A HD11 1 
ATOM   1379 H HD12 . LEU A 1 89  ? 11.443 33.831 39.899 0.00 20.00  ? 92  LEU A HD12 1 
ATOM   1380 H HD13 . LEU A 1 89  ? 11.542 32.923 41.199 0.00 20.00  ? 92  LEU A HD13 1 
ATOM   1381 H HD21 . LEU A 1 89  ? 9.081  33.738 42.449 0.00 27.16  ? 92  LEU A HD21 1 
ATOM   1382 H HD22 . LEU A 1 89  ? 10.352 33.856 43.395 0.00 27.16  ? 92  LEU A HD22 1 
ATOM   1383 H HD23 . LEU A 1 89  ? 9.414  35.117 43.164 0.00 27.16  ? 92  LEU A HD23 1 
ATOM   1384 N N    . LEU A 1 90  ? 13.882 37.917 42.547 1.00 16.43  ? 93  LEU A N    1 
ATOM   1385 C CA   . LEU A 1 90  ? 15.116 38.451 43.111 1.00 13.95  ? 93  LEU A CA   1 
ATOM   1386 C C    . LEU A 1 90  ? 14.829 39.592 44.078 1.00 13.97  ? 93  LEU A C    1 
ATOM   1387 O O    . LEU A 1 90  ? 15.461 39.690 45.136 1.00 18.47  ? 93  LEU A O    1 
ATOM   1388 C CB   . LEU A 1 90  ? 16.046 38.914 41.990 1.00 19.54  ? 93  LEU A CB   1 
ATOM   1389 C CG   . LEU A 1 90  ? 16.680 37.793 41.161 1.00 30.82  ? 93  LEU A CG   1 
ATOM   1390 C CD1  . LEU A 1 90  ? 17.239 38.338 39.855 1.00 21.19  ? 93  LEU A CD1  1 
ATOM   1391 C CD2  . LEU A 1 90  ? 17.766 37.084 41.958 1.00 13.76  ? 93  LEU A CD2  1 
ATOM   1392 H H    . LEU A 1 90  ? 13.790 38.039 41.700 0.00 19.73  ? 93  LEU A H    1 
ATOM   1393 H HA   . LEU A 1 90  ? 15.568 37.747 43.602 0.00 16.75  ? 93  LEU A HA   1 
ATOM   1394 H HB2  . LEU A 1 90  ? 15.536 39.471 41.382 0.00 23.47  ? 93  LEU A HB2  1 
ATOM   1395 H HB3  . LEU A 1 90  ? 16.768 39.427 42.385 0.00 23.47  ? 93  LEU A HB3  1 
ATOM   1396 H HG   . LEU A 1 90  ? 15.996 37.141 40.942 0.00 37.00  ? 93  LEU A HG   1 
ATOM   1397 H HD11 . LEU A 1 90  ? 17.614 37.605 39.341 0.00 25.45  ? 93  LEU A HD11 1 
ATOM   1398 H HD12 . LEU A 1 90  ? 16.522 38.758 39.355 0.00 25.45  ? 93  LEU A HD12 1 
ATOM   1399 H HD13 . LEU A 1 90  ? 17.930 38.989 40.054 0.00 25.45  ? 93  LEU A HD13 1 
ATOM   1400 H HD21 . LEU A 1 90  ? 18.202 36.432 41.388 0.00 16.43  ? 93  LEU A HD21 1 
ATOM   1401 H HD22 . LEU A 1 90  ? 18.411 37.740 42.265 0.00 16.43  ? 93  LEU A HD22 1 
ATOM   1402 H HD23 . LEU A 1 90  ? 17.360 36.640 42.719 0.00 16.43  ? 93  LEU A HD23 1 
ATOM   1403 N N    . LEU A 1 91  ? 13.882 40.468 43.734 1.00 16.58  ? 94  LEU A N    1 
ATOM   1404 C CA   . LEU A 1 91  ? 13.487 41.522 44.662 1.00 21.82  ? 94  LEU A CA   1 
ATOM   1405 C C    . LEU A 1 91  ? 12.885 40.931 45.929 1.00 17.04  ? 94  LEU A C    1 
ATOM   1406 O O    . LEU A 1 91  ? 13.123 41.435 47.034 1.00 15.38  ? 94  LEU A O    1 
ATOM   1407 C CB   . LEU A 1 91  ? 12.492 42.469 43.990 1.00 21.38  ? 94  LEU A CB   1 
ATOM   1408 C CG   . LEU A 1 91  ? 13.030 43.320 42.839 1.00 25.94  ? 94  LEU A CG   1 
ATOM   1409 C CD1  . LEU A 1 91  ? 11.912 44.154 42.233 1.00 21.08  ? 94  LEU A CD1  1 
ATOM   1410 C CD2  . LEU A 1 91  ? 14.174 44.211 43.308 1.00 20.86  ? 94  LEU A CD2  1 
ATOM   1411 H H    . LEU A 1 91  ? 13.462 40.472 42.983 0.00 19.91  ? 94  LEU A H    1 
ATOM   1412 H HA   . LEU A 1 91  ? 14.272 42.036 44.906 0.00 26.20  ? 94  LEU A HA   1 
ATOM   1413 H HB2  . LEU A 1 91  ? 11.763 41.936 43.634 0.00 25.67  ? 94  LEU A HB2  1 
ATOM   1414 H HB3  . LEU A 1 91  ? 12.157 43.080 44.665 0.00 25.67  ? 94  LEU A HB3  1 
ATOM   1415 H HG   . LEU A 1 91  ? 13.380 42.734 42.151 0.00 31.14  ? 94  LEU A HG   1 
ATOM   1416 H HD11 . LEU A 1 91  ? 12.270 44.677 41.499 0.00 25.31  ? 94  LEU A HD11 1 
ATOM   1417 H HD12 . LEU A 1 91  ? 11.217 43.560 41.907 0.00 25.31  ? 94  LEU A HD12 1 
ATOM   1418 H HD13 . LEU A 1 91  ? 11.552 44.743 42.914 0.00 25.31  ? 94  LEU A HD13 1 
ATOM   1419 H HD21 . LEU A 1 91  ? 14.396 44.838 42.602 0.00 25.05  ? 94  LEU A HD21 1 
ATOM   1420 H HD22 . LEU A 1 91  ? 13.894 44.693 44.102 0.00 25.05  ? 94  LEU A HD22 1 
ATOM   1421 H HD23 . LEU A 1 91  ? 14.943 43.656 43.512 0.00 25.05  ? 94  LEU A HD23 1 
ATOM   1422 N N    . LEU A 1 92  ? 12.105 39.856 45.790 1.00 16.05  ? 95  LEU A N    1 
ATOM   1423 C CA   . LEU A 1 92  ? 11.500 39.228 46.960 1.00 16.58  ? 95  LEU A CA   1 
ATOM   1424 C C    . LEU A 1 92  ? 12.565 38.662 47.891 1.00 23.24  ? 95  LEU A C    1 
ATOM   1425 O O    . LEU A 1 92  ? 12.428 38.736 49.118 1.00 25.17  ? 95  LEU A O    1 
ATOM   1426 C CB   . LEU A 1 92  ? 10.528 38.132 46.521 1.00 22.56  ? 95  LEU A CB   1 
ATOM   1427 C CG   . LEU A 1 92  ? 9.614  37.525 47.593 1.00 51.81  ? 95  LEU A CG   1 
ATOM   1428 C CD1  . LEU A 1 92  ? 8.943  38.592 48.456 1.00 43.94  ? 95  LEU A CD1  1 
ATOM   1429 C CD2  . LEU A 1 92  ? 8.568  36.634 46.943 1.00 51.06  ? 95  LEU A CD2  1 
ATOM   1430 H H    . LEU A 1 92  ? 11.915 39.478 45.042 1.00 19.28  ? 95  LEU A H    1 
ATOM   1431 H HA   . LEU A 1 92  ? 10.997 39.896 47.451 1.00 19.92  ? 95  LEU A HA   1 
ATOM   1432 H HB2  . LEU A 1 92  ? 9.949  38.505 45.838 1.00 27.09  ? 95  LEU A HB2  1 
ATOM   1433 H HB3  . LEU A 1 92  ? 11.050 37.403 46.151 1.00 27.09  ? 95  LEU A HB3  1 
ATOM   1434 H HG   . LEU A 1 92  ? 10.164 36.991 48.187 1.00 62.18  ? 95  LEU A HG   1 
ATOM   1435 H HD11 . LEU A 1 92  ? 8.366  38.157 49.103 1.00 52.74  ? 95  LEU A HD11 1 
ATOM   1436 H HD12 . LEU A 1 92  ? 9.628  39.104 48.914 1.00 52.74  ? 95  LEU A HD12 1 
ATOM   1437 H HD13 . LEU A 1 92  ? 8.420  39.176 47.885 1.00 52.74  ? 95  LEU A HD13 1 
ATOM   1438 H HD21 . LEU A 1 92  ? 7.999  36.260 47.633 1.00 61.29  ? 95  LEU A HD21 1 
ATOM   1439 H HD22 . LEU A 1 92  ? 8.037  37.166 46.329 1.00 61.29  ? 95  LEU A HD22 1 
ATOM   1440 H HD23 . LEU A 1 92  ? 9.015  35.921 46.461 1.00 61.29  ? 95  LEU A HD23 1 
ATOM   1441 N N    . ASP A 1 93  ? 13.635 38.093 47.328 1.00 24.58  ? 96  ASP A N    1 
ATOM   1442 C CA   . ASP A 1 93  ? 14.742 37.624 48.155 1.00 21.97  ? 96  ASP A CA   1 
ATOM   1443 C C    . ASP A 1 93  ? 15.282 38.750 49.028 1.00 30.36  ? 96  ASP A C    1 
ATOM   1444 O O    . ASP A 1 93  ? 15.543 38.553 50.221 1.00 24.01  ? 96  ASP A O    1 
ATOM   1445 C CB   . ASP A 1 93  ? 15.859 37.058 47.273 1.00 29.63  ? 96  ASP A CB   1 
ATOM   1446 C CG   . ASP A 1 93  ? 15.828 35.539 47.174 1.00 20.80  ? 96  ASP A CG   1 
ATOM   1447 O OD1  . ASP A 1 93  ? 15.186 34.882 48.020 1.00 20.50  ? 96  ASP A OD1  1 
ATOM   1448 O OD2  . ASP A 1 93  ? 16.455 34.999 46.238 1.00 21.40  ? 96  ASP A OD2  1 
ATOM   1449 H H    . ASP A 1 93  ? 13.740 37.969 46.483 0.00 29.51  ? 96  ASP A H    1 
ATOM   1450 H HA   . ASP A 1 93  ? 14.423 36.912 48.732 0.00 26.38  ? 96  ASP A HA   1 
ATOM   1451 H HB2  . ASP A 1 93  ? 15.764 37.417 46.377 0.00 35.58  ? 96  ASP A HB2  1 
ATOM   1452 H HB3  . ASP A 1 93  ? 16.716 37.315 47.645 0.00 35.58  ? 96  ASP A HB3  1 
ATOM   1453 N N    . LEU A 1 94  ? 15.456 39.940 48.449 1.00 18.82  ? 97  LEU A N    1 
ATOM   1454 C CA   . LEU A 1 94  ? 15.956 41.071 49.223 1.00 26.35  ? 97  LEU A CA   1 
ATOM   1455 C C    . LEU A 1 94  ? 14.923 41.548 50.237 1.00 22.75  ? 97  LEU A C    1 
ATOM   1456 O O    . LEU A 1 94  ? 15.260 41.808 51.398 1.00 27.34  ? 97  LEU A O    1 
ATOM   1457 C CB   . LEU A 1 94  ? 16.344 42.213 48.286 1.00 24.97  ? 97  LEU A CB   1 
ATOM   1458 C CG   . LEU A 1 94  ? 17.494 41.926 47.319 1.00 23.42  ? 97  LEU A CG   1 
ATOM   1459 C CD1  . LEU A 1 94  ? 17.569 43.005 46.248 1.00 22.62  ? 97  LEU A CD1  1 
ATOM   1460 C CD2  . LEU A 1 94  ? 18.813 41.818 48.069 1.00 23.96  ? 97  LEU A CD2  1 
ATOM   1461 H H    . LEU A 1 94  ? 15.294 40.114 47.623 0.00 22.60  ? 97  LEU A H    1 
ATOM   1462 H HA   . LEU A 1 94  ? 16.748 40.790 49.707 0.00 31.64  ? 97  LEU A HA   1 
ATOM   1463 H HB2  . LEU A 1 94  ? 15.569 42.442 47.751 0.00 29.98  ? 97  LEU A HB2  1 
ATOM   1464 H HB3  . LEU A 1 94  ? 16.608 42.973 48.829 0.00 29.98  ? 97  LEU A HB3  1 
ATOM   1465 H HG   . LEU A 1 94  ? 17.332 41.077 46.879 0.00 28.12  ? 97  LEU A HG   1 
ATOM   1466 H HD11 . LEU A 1 94  ? 18.280 42.783 45.626 0.00 27.16  ? 97  LEU A HD11 1 
ATOM   1467 H HD12 . LEU A 1 94  ? 16.721 43.044 45.779 0.00 27.16  ? 97  LEU A HD12 1 
ATOM   1468 H HD13 . LEU A 1 94  ? 17.753 43.858 46.671 0.00 27.16  ? 97  LEU A HD13 1 
ATOM   1469 H HD21 . LEU A 1 94  ? 19.536 41.736 47.427 0.00 28.77  ? 97  LEU A HD21 1 
ATOM   1470 H HD22 . LEU A 1 94  ? 18.937 42.615 48.607 0.00 28.77  ? 97  LEU A HD22 1 
ATOM   1471 H HD23 . LEU A 1 94  ? 18.788 41.034 48.640 0.00 28.77  ? 97  LEU A HD23 1 
ATOM   1472 N N    . ALA A 1 95  ? 13.661 41.666 49.817 1.00 17.63  ? 98  ALA A N    1 
ATOM   1473 C CA   . ALA A 1 95  ? 12.632 42.204 50.702 1.00 21.25  ? 98  ALA A CA   1 
ATOM   1474 C C    . ALA A 1 95  ? 12.397 41.295 51.903 1.00 25.50  ? 98  ALA A C    1 
ATOM   1475 O O    . ALA A 1 95  ? 12.226 41.779 53.028 1.00 32.20  ? 98  ALA A O    1 
ATOM   1476 C CB   . ALA A 1 95  ? 11.333 42.414 49.924 1.00 17.17  ? 98  ALA A CB   1 
ATOM   1477 H H    . ALA A 1 95  ? 13.380 41.445 49.035 0.00 21.17  ? 98  ALA A H    1 
ATOM   1478 H HA   . ALA A 1 95  ? 12.928 43.065 51.036 0.00 25.52  ? 98  ALA A HA   1 
ATOM   1479 H HB1  . ALA A 1 95  ? 10.661 42.776 50.523 0.00 20.53  ? 98  ALA A HB1  1 
ATOM   1480 H HB2  . ALA A 1 95  ? 11.497 43.034 49.197 0.00 20.53  ? 98  ALA A HB2  1 
ATOM   1481 H HB3  . ALA A 1 95  ? 11.035 41.561 49.570 0.00 20.53  ? 98  ALA A HB3  1 
ATOM   1482 N N    . LEU A 1 96  ? 12.372 39.977 51.688 1.00 29.15  ? 99  LEU A N    1 
ATOM   1483 C CA   . LEU A 1 96  ? 12.210 39.055 52.808 1.00 23.74  ? 99  LEU A CA   1 
ATOM   1484 C C    . LEU A 1 96  ? 13.421 39.084 53.730 1.00 33.41  ? 99  LEU A C    1 
ATOM   1485 O O    . LEU A 1 96  ? 13.284 38.875 54.941 1.00 27.46  ? 99  LEU A O    1 
ATOM   1486 C CB   . LEU A 1 96  ? 11.978 37.634 52.294 1.00 30.72  ? 99  LEU A CB   1 
ATOM   1487 C CG   . LEU A 1 96  ? 10.716 37.393 51.459 1.00 38.80  ? 99  LEU A CG   1 
ATOM   1488 C CD1  . LEU A 1 96  ? 10.572 35.911 51.151 1.00 31.06  ? 99  LEU A CD1  1 
ATOM   1489 C CD2  . LEU A 1 96  ? 9.471  37.919 52.160 1.00 45.89  ? 99  LEU A CD2  1 
ATOM   1490 H H    . LEU A 1 96  ? 12.445 39.600 50.918 0.00 34.99  ? 99  LEU A H    1 
ATOM   1491 H HA   . LEU A 1 96  ? 11.430 39.321 53.319 0.00 28.50  ? 99  LEU A HA   1 
ATOM   1492 H HB2  . LEU A 1 96  ? 12.735 37.390 51.738 0.00 36.88  ? 99  LEU A HB2  1 
ATOM   1493 H HB3  . LEU A 1 96  ? 11.926 37.044 53.062 0.00 36.88  ? 99  LEU A HB3  1 
ATOM   1494 H HG   . LEU A 1 96  ? 10.800 37.878 50.624 0.00 46.58  ? 99  LEU A HG   1 
ATOM   1495 H HD11 . LEU A 1 96  ? 9.764  35.773 50.633 0.00 37.29  ? 99  LEU A HD11 1 
ATOM   1496 H HD12 . LEU A 1 96  ? 11.344 35.617 50.644 0.00 37.29  ? 99  LEU A HD12 1 
ATOM   1497 H HD13 . LEU A 1 96  ? 10.518 35.419 51.986 0.00 37.29  ? 99  LEU A HD13 1 
ATOM   1498 H HD21 . LEU A 1 96  ? 8.686  37.620 51.676 0.00 55.08  ? 99  LEU A HD21 1 
ATOM   1499 H HD22 . LEU A 1 96  ? 9.451  37.577 53.068 0.00 55.08  ? 99  LEU A HD22 1 
ATOM   1500 H HD23 . LEU A 1 96  ? 9.502  38.889 52.173 0.00 55.08  ? 99  LEU A HD23 1 
ATOM   1501 N N    . LEU A 1 97  ? 14.608 39.345 53.180 1.00 20.65  ? 100 LEU A N    1 
ATOM   1502 C CA   . LEU A 1 97  ? 15.811 39.411 54.002 1.00 27.85  ? 100 LEU A CA   1 
ATOM   1503 C C    . LEU A 1 97  ? 15.692 40.486 55.075 1.00 34.06  ? 100 LEU A C    1 
ATOM   1504 O O    . LEU A 1 97  ? 16.037 40.255 56.239 1.00 40.80  ? 100 LEU A O    1 
ATOM   1505 C CB   . LEU A 1 97  ? 17.023 39.685 53.112 1.00 28.52  ? 100 LEU A CB   1 
ATOM   1506 C CG   . LEU A 1 97  ? 18.412 39.279 53.607 1.00 32.74  ? 100 LEU A CG   1 
ATOM   1507 C CD1  . LEU A 1 97  ? 18.462 37.835 54.080 1.00 37.27  ? 100 LEU A CD1  1 
ATOM   1508 C CD2  . LEU A 1 97  ? 19.422 39.512 52.494 1.00 46.83  ? 100 LEU A CD2  1 
ATOM   1509 H H    . LEU A 1 97  ? 14.740 39.487 52.342 0.00 24.70  ? 100 LEU A H    1 
ATOM   1510 H HA   . LEU A 1 97  ? 15.934 38.557 54.445 0.00 33.44  ? 100 LEU A HA   1 
ATOM   1511 H HB2  . LEU A 1 97  ? 16.882 39.214 52.276 0.00 34.24  ? 100 LEU A HB2  1 
ATOM   1512 H HB3  . LEU A 1 97  ? 17.057 40.641 52.953 0.00 34.24  ? 100 LEU A HB3  1 
ATOM   1513 H HG   . LEU A 1 97  ? 18.639 39.824 54.377 0.00 39.30  ? 100 LEU A HG   1 
ATOM   1514 H HD11 . LEU A 1 97  ? 19.379 37.604 54.296 0.00 44.74  ? 100 LEU A HD11 1 
ATOM   1515 H HD12 . LEU A 1 97  ? 17.904 37.741 54.868 0.00 44.74  ? 100 LEU A HD12 1 
ATOM   1516 H HD13 . LEU A 1 97  ? 18.134 37.259 53.372 0.00 44.74  ? 100 LEU A HD13 1 
ATOM   1517 H HD21 . LEU A 1 97  ? 19.414 40.451 52.251 0.00 56.21  ? 100 LEU A HD21 1 
ATOM   1518 H HD22 . LEU A 1 97  ? 20.304 39.259 52.809 0.00 56.21  ? 100 LEU A HD22 1 
ATOM   1519 H HD23 . LEU A 1 97  ? 19.177 38.971 51.727 0.00 56.21  ? 100 LEU A HD23 1 
ATOM   1520 N N    . VAL A 1 98  ? 15.221 41.674 54.698 1.00 29.73  ? 101 VAL A N    1 
ATOM   1521 C CA   . VAL A 1 98  ? 15.108 42.796 55.622 1.00 34.44  ? 101 VAL A CA   1 
ATOM   1522 C C    . VAL A 1 98  ? 13.717 42.885 56.247 1.00 35.69  ? 101 VAL A C    1 
ATOM   1523 O O    . VAL A 1 98  ? 13.434 43.835 56.978 1.00 39.35  ? 101 VAL A O    1 
ATOM   1524 C CB   . VAL A 1 98  ? 15.480 44.119 54.930 1.00 36.84  ? 101 VAL A CB   1 
ATOM   1525 C CG1  . VAL A 1 98  ? 16.933 44.080 54.477 1.00 42.94  ? 101 VAL A CG1  1 
ATOM   1526 C CG2  . VAL A 1 98  ? 14.551 44.402 53.759 1.00 26.88  ? 101 VAL A CG2  1 
ATOM   1527 H H    . VAL A 1 98  ? 14.956 41.857 53.900 0.00 35.69  ? 101 VAL A H    1 
ATOM   1528 H HA   . VAL A 1 98  ? 15.741 42.661 56.345 0.00 41.35  ? 101 VAL A HA   1 
ATOM   1529 H HB   . VAL A 1 98  ? 15.377 44.846 55.563 0.00 44.22  ? 101 VAL A HB   1 
ATOM   1530 H HG11 . VAL A 1 98  ? 17.151 44.919 54.041 0.00 51.54  ? 101 VAL A HG11 1 
ATOM   1531 H HG12 . VAL A 1 98  ? 17.502 43.953 55.252 0.00 51.54  ? 101 VAL A HG12 1 
ATOM   1532 H HG13 . VAL A 1 98  ? 17.051 43.345 53.856 0.00 51.54  ? 101 VAL A HG13 1 
ATOM   1533 H HG21 . VAL A 1 98  ? 14.803 45.246 53.353 0.00 32.27  ? 101 VAL A HG21 1 
ATOM   1534 H HG22 . VAL A 1 98  ? 14.632 43.686 53.111 0.00 32.27  ? 101 VAL A HG22 1 
ATOM   1535 H HG23 . VAL A 1 98  ? 13.639 44.452 54.085 0.00 32.27  ? 101 VAL A HG23 1 
ATOM   1536 N N    . ASP A 1 99  ? 12.842 41.918 55.975 1.00 28.38  ? 102 ASP A N    1 
ATOM   1537 C CA   . ASP A 1 99  ? 11.488 41.903 56.531 1.00 30.19  ? 102 ASP A CA   1 
ATOM   1538 C C    . ASP A 1 99  ? 10.735 43.186 56.178 1.00 34.23  ? 102 ASP A C    1 
ATOM   1539 O O    . ASP A 1 99  ? 10.179 43.870 57.040 1.00 34.23  ? 102 ASP A O    1 
ATOM   1540 C CB   . ASP A 1 99  ? 11.526 41.688 58.045 1.00 39.64  ? 102 ASP A CB   1 
ATOM   1541 C CG   . ASP A 1 99  ? 10.173 41.303 58.613 1.00 49.66  ? 102 ASP A CG   1 
ATOM   1542 O OD1  . ASP A 1 99  ? 9.171  41.387 57.872 1.00 76.55  ? 102 ASP A OD1  1 
ATOM   1543 O OD2  . ASP A 1 99  ? 10.112 40.914 59.796 1.00 79.64  ? 102 ASP A OD2  1 
ATOM   1544 H H    . ASP A 1 99  ? 13.011 41.249 55.462 0.00 34.07  ? 102 ASP A H    1 
ATOM   1545 H HA   . ASP A 1 99  ? 11.001 41.163 56.135 0.00 36.25  ? 102 ASP A HA   1 
ATOM   1546 H HB2  . ASP A 1 99  ? 12.151 40.975 58.248 0.00 47.58  ? 102 ASP A HB2  1 
ATOM   1547 H HB3  . ASP A 1 99  ? 11.809 42.510 58.475 0.00 47.58  ? 102 ASP A HB3  1 
ATOM   1548 N N    . ALA A 1 100 ? 10.716 43.506 54.888 1.00 28.74  ? 103 ALA A N    1 
ATOM   1549 C CA   . ALA A 1 100 ? 10.028 44.702 54.426 1.00 34.31  ? 103 ALA A CA   1 
ATOM   1550 C C    . ALA A 1 100 ? 8.523  44.566 54.632 1.00 39.60  ? 103 ALA A C    1 
ATOM   1551 O O    . ALA A 1 100 ? 7.974  43.462 54.677 1.00 26.23  ? 103 ALA A O    1 
ATOM   1552 C CB   . ALA A 1 100 ? 10.332 44.960 52.951 1.00 30.44  ? 103 ALA A CB   1 
ATOM   1553 H H    . ALA A 1 100 ? 11.092 43.049 54.264 0.00 34.50  ? 103 ALA A H    1 
ATOM   1554 H HA   . ALA A 1 100 ? 10.338 45.468 54.934 0.00 41.19  ? 103 ALA A HA   1 
ATOM   1555 H HB1  . ALA A 1 100 ? 9.862  45.759 52.667 0.00 36.55  ? 103 ALA A HB1  1 
ATOM   1556 H HB2  . ALA A 1 100 ? 11.288 45.082 52.842 0.00 36.55  ? 103 ALA A HB2  1 
ATOM   1557 H HB3  . ALA A 1 100 ? 10.034 44.198 52.429 0.00 36.55  ? 103 ALA A HB3  1 
ATOM   1558 N N    . ASP A 1 101 ? 7.856  45.709 54.765 1.00 31.60  ? 104 ASP A N    1 
ATOM   1559 C CA   . ASP A 1 101 ? 6.413  45.711 54.936 1.00 41.74  ? 104 ASP A CA   1 
ATOM   1560 C C    . ASP A 1 101 ? 5.723  45.331 53.628 1.00 33.39  ? 104 ASP A C    1 
ATOM   1561 O O    . ASP A 1 101 ? 6.295  45.423 52.538 1.00 33.05  ? 104 ASP A O    1 
ATOM   1562 C CB   . ASP A 1 101 ? 5.930  47.079 55.417 1.00 37.33  ? 104 ASP A CB   1 
ATOM   1563 C CG   . ASP A 1 101 ? 6.242  48.186 54.434 1.00 31.08  ? 104 ASP A CG   1 
ATOM   1564 O OD1  . ASP A 1 101 ? 5.500  48.324 53.439 1.00 48.49  ? 104 ASP A OD1  1 
ATOM   1565 O OD2  . ASP A 1 101 ? 7.227  48.919 54.657 1.00 42.28  ? 104 ASP A OD2  1 
ATOM   1566 H H    . ASP A 1 101 ? 8.216  46.490 54.759 0.00 37.93  ? 104 ASP A H    1 
ATOM   1567 H HA   . ASP A 1 101 ? 6.164  45.058 55.609 0.00 50.10  ? 104 ASP A HA   1 
ATOM   1568 H HB2  . ASP A 1 101 ? 4.969  47.050 55.541 1.00 44.81  ? 104 ASP A HB2  1 
ATOM   1569 H HB3  . ASP A 1 101 ? 6.367  47.292 56.257 1.00 44.81  ? 104 ASP A HB3  1 
ATOM   1570 N N    A GLN A 1 102 ? 4.466  44.899 53.753 0.48 36.06  ? 105 GLN A N    1 
ATOM   1571 N N    B GLN A 1 102 ? 4.466  44.898 53.750 0.52 36.05  ? 105 GLN A N    1 
ATOM   1572 C CA   A GLN A 1 102 ? 3.733  44.409 52.590 0.48 36.04  ? 105 GLN A CA   1 
ATOM   1573 C CA   B GLN A 1 102 ? 3.741  44.406 52.583 0.52 36.02  ? 105 GLN A CA   1 
ATOM   1574 C C    A GLN A 1 102 ? 3.527  45.511 51.558 0.48 39.28  ? 105 GLN A C    1 
ATOM   1575 C C    B GLN A 1 102 ? 3.523  45.511 51.555 0.52 39.31  ? 105 GLN A C    1 
ATOM   1576 O O    A GLN A 1 102 ? 3.596  45.261 50.349 0.48 30.21  ? 105 GLN A O    1 
ATOM   1577 O O    B GLN A 1 102 ? 3.581  45.263 50.345 0.52 30.19  ? 105 GLN A O    1 
ATOM   1578 C CB   A GLN A 1 102 ? 2.390  43.826 53.028 0.48 48.67  ? 105 GLN A CB   1 
ATOM   1579 C CB   B GLN A 1 102 ? 2.405  43.803 53.016 0.52 48.69  ? 105 GLN A CB   1 
ATOM   1580 C CG   A GLN A 1 102 ? 2.507  42.579 53.894 0.48 56.80  ? 105 GLN A CG   1 
ATOM   1581 C CG   B GLN A 1 102 ? 2.549  42.534 53.840 0.52 56.81  ? 105 GLN A CG   1 
ATOM   1582 C CD   A GLN A 1 102 ? 2.704  42.899 55.365 0.48 61.32  ? 105 GLN A CD   1 
ATOM   1583 C CD   B GLN A 1 102 ? 1.216  41.994 54.318 0.52 58.23  ? 105 GLN A CD   1 
ATOM   1584 O OE1  A GLN A 1 102 ? 2.759  44.064 55.759 0.48 58.68  ? 105 GLN A OE1  1 
ATOM   1585 O OE1  B GLN A 1 102 ? 0.241  42.734 54.442 0.52 57.23  ? 105 GLN A OE1  1 
ATOM   1586 N NE2  A GLN A 1 102 ? 2.812  41.861 56.186 0.48 61.35  ? 105 GLN A NE2  1 
ATOM   1587 N NE2  B GLN A 1 102 ? 1.169  40.695 54.590 0.52 68.91  ? 105 GLN A NE2  1 
ATOM   1588 H H    A GLN A 1 102 ? 4.023  44.880 54.489 0.48 43.29  ? 105 GLN A H    1 
ATOM   1589 H H    B GLN A 1 102 ? 4.020  44.880 54.484 0.52 43.27  ? 105 GLN A H    1 
ATOM   1590 H HA   A GLN A 1 102 ? 4.249  43.701 52.171 0.48 43.27  ? 105 GLN A HA   1 
ATOM   1591 H HA   B GLN A 1 102 ? 4.266  43.708 52.160 0.52 43.24  ? 105 GLN A HA   1 
ATOM   1592 H HB2  A GLN A 1 102 ? 1.913  44.498 53.541 0.48 58.42  ? 105 GLN A HB2  1 
ATOM   1593 H HB2  B GLN A 1 102 ? 1.928  44.454 53.553 0.52 58.44  ? 105 GLN A HB2  1 
ATOM   1594 H HB3  A GLN A 1 102 ? 1.881  43.590 52.237 0.48 58.42  ? 105 GLN A HB3  1 
ATOM   1595 H HB3  B GLN A 1 102 ? 1.890  43.584 52.223 0.52 58.44  ? 105 GLN A HB3  1 
ATOM   1596 H HG2  A GLN A 1 102 ? 1.694  42.057 53.807 0.48 68.17  ? 105 GLN A HG2  1 
ATOM   1597 H HG2  B GLN A 1 102 ? 2.973  41.851 53.299 0.52 68.18  ? 105 GLN A HG2  1 
ATOM   1598 H HG3  A GLN A 1 102 ? 3.269  42.058 53.596 0.48 68.17  ? 105 GLN A HG3  1 
ATOM   1599 H HG3  B GLN A 1 102 ? 3.093  42.725 54.621 0.52 68.18  ? 105 GLN A HG3  1 
ATOM   1600 H HE21 A GLN A 1 102 ? 2.769  41.060 55.875 0.48 73.64  ? 105 GLN A HE21 1 
ATOM   1601 H HE21 B GLN A 1 102 ? 1.872  40.209 54.492 0.52 82.71  ? 105 GLN A HE21 1 
ATOM   1602 H HE22 A GLN A 1 102 ? 2.925  41.989 57.029 0.48 73.64  ? 105 GLN A HE22 1 
ATOM   1603 H HE22 B GLN A 1 102 ? 0.435  40.340 54.865 0.52 82.71  ? 105 GLN A HE22 1 
ATOM   1604 N N    . GLY A 1 103 ? 3.267  46.737 52.015 1.00 36.13  ? 106 GLY A N    1 
ATOM   1605 C CA   . GLY A 1 103 ? 3.067  47.833 51.080 1.00 34.33  ? 106 GLY A CA   1 
ATOM   1606 C C    . GLY A 1 103 ? 4.294  48.103 50.230 1.00 33.85  ? 106 GLY A C    1 
ATOM   1607 O O    . GLY A 1 103 ? 4.187  48.331 49.022 1.00 20.40  ? 106 GLY A O    1 
ATOM   1608 H H    . GLY A 1 103 ? 3.207  46.949 52.846 0.00 43.37  ? 106 GLY A H    1 
ATOM   1609 H HA2  . GLY A 1 103 ? 2.328  47.620 50.490 0.00 41.21  ? 106 GLY A HA2  1 
ATOM   1610 H HA3  . GLY A 1 103 ? 2.855  48.640 51.574 0.00 41.21  ? 106 GLY A HA3  1 
ATOM   1611 N N    . THR A 1 104 ? 5.477  48.075 50.848 1.00 22.06  ? 107 THR A N    1 
ATOM   1612 C CA   . THR A 1 104 ? 6.707  48.322 50.103 1.00 24.58  ? 107 THR A CA   1 
ATOM   1613 C C    . THR A 1 104 ? 6.952  47.234 49.064 1.00 19.58  ? 107 THR A C    1 
ATOM   1614 O O    . THR A 1 104 ? 7.424  47.517 47.957 1.00 26.10  ? 107 THR A O    1 
ATOM   1615 C CB   . THR A 1 104 ? 7.891  48.414 51.067 1.00 26.98  ? 107 THR A CB   1 
ATOM   1616 O OG1  . THR A 1 104 ? 7.685  49.495 51.983 1.00 37.91  ? 107 THR A OG1  1 
ATOM   1617 C CG2  . THR A 1 104 ? 9.185  48.644 50.303 1.00 24.62  ? 107 THR A CG2  1 
ATOM   1618 H H    . THR A 1 104 ? 5.591  47.918 51.685 0.00 26.49  ? 107 THR A H    1 
ATOM   1619 H HA   . THR A 1 104 ? 6.626  49.170 49.639 0.00 29.51  ? 107 THR A HA   1 
ATOM   1620 H HB   . THR A 1 104 ? 7.970  47.582 51.560 0.00 32.39  ? 107 THR A HB   1 
ATOM   1621 H HG1  . THR A 1 104 ? 8.323  49.536 52.528 0.00 45.51  ? 107 THR A HG1  1 
ATOM   1622 H HG21 . THR A 1 104 ? 9.874  48.962 50.907 0.00 29.56  ? 107 THR A HG21 1 
ATOM   1623 H HG22 . THR A 1 104 ? 9.481  47.815 49.896 0.00 29.56  ? 107 THR A HG22 1 
ATOM   1624 H HG23 . THR A 1 104 ? 9.047  49.305 49.607 0.00 29.56  ? 107 THR A HG23 1 
ATOM   1625 N N    . ILE A 1 105 ? 6.638  45.982 49.402 1.00 23.63  ? 108 ILE A N    1 
ATOM   1626 C CA   . ILE A 1 105 ? 6.851  44.884 48.462 1.00 19.09  ? 108 ILE A CA   1 
ATOM   1627 C C    . ILE A 1 105 ? 5.965  45.060 47.235 1.00 19.75  ? 108 ILE A C    1 
ATOM   1628 O O    . ILE A 1 105 ? 6.413  44.900 46.093 1.00 23.81  ? 108 ILE A O    1 
ATOM   1629 C CB   . ILE A 1 105 ? 6.597  43.531 49.152 1.00 29.39  ? 108 ILE A CB   1 
ATOM   1630 C CG1  . ILE A 1 105 ? 7.714  43.229 50.153 1.00 21.49  ? 108 ILE A CG1  1 
ATOM   1631 C CG2  . ILE A 1 105 ? 6.493  42.416 48.120 1.00 22.52  ? 108 ILE A CG2  1 
ATOM   1632 C CD1  . ILE A 1 105 ? 7.348  42.176 51.181 1.00 35.96  ? 108 ILE A CD1  1 
ATOM   1633 H H    . ILE A 1 105 ? 6.306  45.745 50.159 0.00 28.37  ? 108 ILE A H    1 
ATOM   1634 H HA   . ILE A 1 105 ? 7.776  44.902 48.168 0.00 22.92  ? 108 ILE A HA   1 
ATOM   1635 H HB   . ILE A 1 105 ? 5.756  43.586 49.632 0.00 35.28  ? 108 ILE A HB   1 
ATOM   1636 H HG12 . ILE A 1 105 ? 8.491  42.910 49.667 0.00 25.80  ? 108 ILE A HG12 1 
ATOM   1637 H HG13 . ILE A 1 105 ? 7.934  44.044 50.631 0.00 25.80  ? 108 ILE A HG13 1 
ATOM   1638 H HG21 . ILE A 1 105 ? 6.614  41.562 48.564 0.00 27.04  ? 108 ILE A HG21 1 
ATOM   1639 H HG22 . ILE A 1 105 ? 5.617  42.451 47.705 0.00 27.04  ? 108 ILE A HG22 1 
ATOM   1640 H HG23 . ILE A 1 105 ? 7.182  42.541 47.449 0.00 27.04  ? 108 ILE A HG23 1 
ATOM   1641 H HD11 . ILE A 1 105 ? 8.061  42.112 51.836 0.00 43.16  ? 108 ILE A HD11 1 
ATOM   1642 H HD12 . ILE A 1 105 ? 6.521  42.434 51.617 0.00 43.16  ? 108 ILE A HD12 1 
ATOM   1643 H HD13 . ILE A 1 105 ? 7.233  41.323 50.733 0.00 43.16  ? 108 ILE A HD13 1 
ATOM   1644 N N    . LEU A 1 106 ? 4.690  45.392 47.453 1.00 21.52  ? 109 LEU A N    1 
ATOM   1645 C CA   A LEU A 1 106 ? 3.780  45.570 46.327 0.57 25.94  ? 109 LEU A CA   1 
ATOM   1646 C CA   B LEU A 1 106 ? 3.771  45.580 46.333 0.43 25.92  ? 109 LEU A CA   1 
ATOM   1647 C C    . LEU A 1 106 ? 4.263  46.676 45.397 1.00 19.38  ? 109 LEU A C    1 
ATOM   1648 O O    . LEU A 1 106 ? 4.131  46.566 44.173 1.00 25.87  ? 109 LEU A O    1 
ATOM   1649 C CB   A LEU A 1 106 ? 2.372  45.875 46.836 0.57 27.21  ? 109 LEU A CB   1 
ATOM   1650 C CB   B LEU A 1 106 ? 2.374  45.916 46.854 0.43 27.19  ? 109 LEU A CB   1 
ATOM   1651 C CG   A LEU A 1 106 ? 1.304  46.052 45.755 0.57 23.52  ? 109 LEU A CG   1 
ATOM   1652 C CG   B LEU A 1 106 ? 1.611  44.785 47.548 0.43 28.03  ? 109 LEU A CG   1 
ATOM   1653 C CD1  A LEU A 1 106 ? 1.173  44.798 44.902 0.57 26.74  ? 109 LEU A CD1  1 
ATOM   1654 C CD1  B LEU A 1 106 ? 0.701  45.339 48.633 0.43 23.68  ? 109 LEU A CD1  1 
ATOM   1655 C CD2  A LEU A 1 106 ? -0.022 46.406 46.388 0.57 25.83  ? 109 LEU A CD2  1 
ATOM   1656 C CD2  B LEU A 1 106 ? 0.811  43.979 46.538 0.43 30.05  ? 109 LEU A CD2  1 
ATOM   1657 H H    A LEU A 1 106 ? 4.337  45.517 48.227 0.57 25.84  ? 109 LEU A H    1 
ATOM   1658 H H    B LEU A 1 106 ? 4.338  45.513 48.228 0.43 25.84  ? 109 LEU A H    1 
ATOM   1659 H HA   A LEU A 1 106 ? 3.743  44.745 45.820 0.57 31.14  ? 109 LEU A HA   1 
ATOM   1660 H HA   B LEU A 1 106 ? 3.717  44.752 45.831 0.43 31.12  ? 109 LEU A HA   1 
ATOM   1661 H HB2  A LEU A 1 106 ? 2.089  45.142 47.405 0.57 32.67  ? 109 LEU A HB2  1 
ATOM   1662 H HB2  B LEU A 1 106 ? 2.458  46.638 47.497 0.43 32.65  ? 109 LEU A HB2  1 
ATOM   1663 H HB3  A LEU A 1 106 ? 2.404  46.698 47.348 0.57 32.67  ? 109 LEU A HB3  1 
ATOM   1664 H HB3  B LEU A 1 106 ? 1.834  46.204 46.102 0.43 32.65  ? 109 LEU A HB3  1 
ATOM   1665 H HG   A LEU A 1 106 ? 1.570  46.777 45.167 0.57 28.24  ? 109 LEU A HG   1 
ATOM   1666 H HG   B LEU A 1 106 ? 2.250  44.187 47.968 0.43 33.65  ? 109 LEU A HG   1 
ATOM   1667 H HD11 A LEU A 1 106 ? 0.407  44.894 44.315 0.57 32.11  ? 109 LEU A HD11 1 
ATOM   1668 H HD11 B LEU A 1 106 ? 0.224  44.605 49.050 0.43 28.43  ? 109 LEU A HD11 1 
ATOM   1669 H HD12 A LEU A 1 106 ? 1.981  44.689 44.375 0.57 32.11  ? 109 LEU A HD12 1 
ATOM   1670 H HD12 B LEU A 1 106 ? 1.242  45.801 49.293 0.43 28.43  ? 109 LEU A HD12 1 
ATOM   1671 H HD13 A LEU A 1 106 ? 1.051  44.032 45.483 0.57 32.11  ? 109 LEU A HD13 1 
ATOM   1672 H HD13 B LEU A 1 106 ? 0.071  45.957 48.231 0.43 28.43  ? 109 LEU A HD13 1 
ATOM   1673 H HD21 A LEU A 1 106 ? -0.675 46.562 45.688 0.57 31.01  ? 109 LEU A HD21 1 
ATOM   1674 H HD21 B LEU A 1 106 ? 0.315  43.290 47.006 0.43 36.08  ? 109 LEU A HD21 1 
ATOM   1675 H HD22 A LEU A 1 106 ? -0.310 45.671 46.951 0.57 31.01  ? 109 LEU A HD22 1 
ATOM   1676 H HD22 B LEU A 1 106 ? 0.198  44.572 46.075 0.43 36.08  ? 109 LEU A HD22 1 
ATOM   1677 H HD23 A LEU A 1 106 ? 0.087  47.208 46.923 0.57 31.01  ? 109 LEU A HD23 1 
ATOM   1678 H HD23 B LEU A 1 106 ? 1.422  43.573 45.903 0.43 36.08  ? 109 LEU A HD23 1 
ATOM   1679 N N    . ALA A 1 107 ? 4.829  47.747 45.959 1.00 24.31  ? 110 ALA A N    1 
ATOM   1680 C CA   . ALA A 1 107 ? 5.342  48.836 45.134 1.00 19.43  ? 110 ALA A CA   1 
ATOM   1681 C C    . ALA A 1 107 ? 6.517  48.378 44.280 1.00 22.03  ? 110 ALA A C    1 
ATOM   1682 O O    . ALA A 1 107 ? 6.628  48.763 43.110 1.00 23.24  ? 110 ALA A O    1 
ATOM   1683 C CB   . ALA A 1 107 ? 5.755  50.010 46.021 1.00 23.67  ? 110 ALA A CB   1 
ATOM   1684 H H    . ALA A 1 107 ? 4.927  47.864 46.805 0.00 29.18  ? 110 ALA A H    1 
ATOM   1685 H HA   . ALA A 1 107 ? 4.636  49.136 44.540 0.00 23.33  ? 110 ALA A HA   1 
ATOM   1686 H HB1  . ALA A 1 107 ? 6.190  50.681 45.473 0.00 28.42  ? 110 ALA A HB1  1 
ATOM   1687 H HB2  . ALA A 1 107 ? 4.963  50.385 46.437 0.00 28.42  ? 110 ALA A HB2  1 
ATOM   1688 H HB3  . ALA A 1 107 ? 6.368  49.690 46.702 0.00 28.42  ? 110 ALA A HB3  1 
ATOM   1689 N N    . LEU A 1 108 ? 7.409  47.564 44.849 1.00 23.02  ? 111 LEU A N    1 
ATOM   1690 C CA   . LEU A 1 108 ? 8.567  47.091 44.099 1.00 17.54  ? 111 LEU A CA   1 
ATOM   1691 C C    . LEU A 1 108 ? 8.145  46.161 42.969 1.00 19.08  ? 111 LEU A C    1 
ATOM   1692 O O    . LEU A 1 108 ? 8.596  46.309 41.827 1.00 18.05  ? 111 LEU A O    1 
ATOM   1693 C CB   . LEU A 1 108 ? 9.544  46.380 45.036 1.00 23.10  ? 111 LEU A CB   1 
ATOM   1694 C CG   . LEU A 1 108 ? 10.443 47.265 45.902 1.00 35.30  ? 111 LEU A CG   1 
ATOM   1695 C CD1  . LEU A 1 108 ? 11.186 46.421 46.926 1.00 26.06  ? 111 LEU A CD1  1 
ATOM   1696 C CD2  . LEU A 1 108 ? 11.423 48.048 45.045 1.00 32.03  ? 111 LEU A CD2  1 
ATOM   1697 H H    . LEU A 1 108 ? 7.365  47.276 45.658 0.00 27.64  ? 111 LEU A H    1 
ATOM   1698 H HA   . LEU A 1 108 ? 9.020  47.856 43.711 0.00 21.06  ? 111 LEU A HA   1 
ATOM   1699 H HB2  . LEU A 1 108 ? 9.028  45.824 45.640 0.00 27.74  ? 111 LEU A HB2  1 
ATOM   1700 H HB3  . LEU A 1 108 ? 10.129 45.827 44.494 0.00 27.74  ? 111 LEU A HB3  1 
ATOM   1701 H HG   . LEU A 1 108 ? 9.889  47.905 46.375 0.00 42.38  ? 111 LEU A HG   1 
ATOM   1702 H HD11 . LEU A 1 108 ? 11.809 46.986 47.409 0.00 31.28  ? 111 LEU A HD11 1 
ATOM   1703 H HD12 . LEU A 1 108 ? 10.544 46.033 47.541 0.00 31.28  ? 111 LEU A HD12 1 
ATOM   1704 H HD13 . LEU A 1 108 ? 11.668 45.717 46.464 0.00 31.28  ? 111 LEU A HD13 1 
ATOM   1705 H HD21 . LEU A 1 108 ? 12.061 48.495 45.624 0.00 38.45  ? 111 LEU A HD21 1 
ATOM   1706 H HD22 . LEU A 1 108 ? 11.887 47.435 44.454 0.00 38.45  ? 111 LEU A HD22 1 
ATOM   1707 H HD23 . LEU A 1 108 ? 10.934 48.704 44.524 0.00 38.45  ? 111 LEU A HD23 1 
ATOM   1708 N N    . VAL A 1 109 ? 7.279  45.192 43.272 1.00 13.55  ? 112 VAL A N    1 
ATOM   1709 C CA   . VAL A 1 109 ? 6.861  44.227 42.260 1.00 20.76  ? 112 VAL A CA   1 
ATOM   1710 C C    . VAL A 1 109 ? 6.034  44.909 41.178 1.00 16.03  ? 112 VAL A C    1 
ATOM   1711 O O    . VAL A 1 109 ? 6.169  44.599 39.987 1.00 17.78  ? 112 VAL A O    1 
ATOM   1712 C CB   . VAL A 1 109 ? 6.089  43.072 42.921 1.00 19.79  ? 112 VAL A CB   1 
ATOM   1713 C CG1  . VAL A 1 109 ? 5.483  42.160 41.863 1.00 33.17  ? 112 VAL A CG1  1 
ATOM   1714 C CG2  . VAL A 1 109 ? 7.004  42.289 43.849 1.00 24.37  ? 112 VAL A CG2  1 
ATOM   1715 H H    . VAL A 1 109 ? 6.924  45.074 44.046 0.00 16.19  ? 112 VAL A H    1 
ATOM   1716 H HA   . VAL A 1 109 ? 7.654  43.859 41.839 0.00 24.92  ? 112 VAL A HA   1 
ATOM   1717 H HB   . VAL A 1 109 ? 5.363  43.438 43.450 0.00 23.76  ? 112 VAL A HB   1 
ATOM   1718 H HG11 . VAL A 1 109 ? 5.224  41.323 42.278 0.00 39.81  ? 112 VAL A HG11 1 
ATOM   1719 H HG12 . VAL A 1 109 ? 4.705  42.594 41.480 0.00 39.81  ? 112 VAL A HG12 1 
ATOM   1720 H HG13 . VAL A 1 109 ? 6.144  41.996 41.172 0.00 39.81  ? 112 VAL A HG13 1 
ATOM   1721 H HG21 . VAL A 1 109 ? 6.495  41.580 44.271 0.00 29.26  ? 112 VAL A HG21 1 
ATOM   1722 H HG22 . VAL A 1 109 ? 7.731  41.911 43.330 0.00 29.26  ? 112 VAL A HG22 1 
ATOM   1723 H HG23 . VAL A 1 109 ? 7.357  42.890 44.524 0.00 29.26  ? 112 VAL A HG23 1 
ATOM   1724 N N    . GLY A 1 110 ? 5.163  45.841 41.568 1.00 19.30  ? 113 GLY A N    1 
ATOM   1725 C CA   . GLY A 1 110 ? 4.376  46.558 40.578 1.00 17.09  ? 113 GLY A CA   1 
ATOM   1726 C C    . GLY A 1 110 ? 5.243  47.375 39.640 1.00 13.89  ? 113 GLY A C    1 
ATOM   1727 O O    . GLY A 1 110 ? 5.059  47.350 38.421 1.00 17.96  ? 113 GLY A O    1 
ATOM   1728 H H    . GLY A 1 110 ? 5.014  46.069 42.384 0.00 23.17  ? 113 GLY A H    1 
ATOM   1729 H HA2  . GLY A 1 110 ? 3.867  45.923 40.050 0.00 20.53  ? 113 GLY A HA2  1 
ATOM   1730 H HA3  . GLY A 1 110 ? 3.762  47.159 41.029 0.00 20.53  ? 113 GLY A HA3  1 
ATOM   1731 N N    . ALA A 1 111 ? 6.208  48.110 40.199 1.00 13.18  ? 114 ALA A N    1 
ATOM   1732 C CA   . ALA A 1 111 ? 7.127  48.878 39.366 1.00 13.05  ? 114 ALA A CA   1 
ATOM   1733 C C    . ALA A 1 111 ? 7.982  47.959 38.505 1.00 22.28  ? 114 ALA A C    1 
ATOM   1734 O O    . ALA A 1 111 ? 8.294  48.285 37.353 1.00 12.60  ? 114 ALA A O    1 
ATOM   1735 C CB   . ALA A 1 111 ? 8.010  49.765 40.244 1.00 23.56  ? 114 ALA A CB   1 
ATOM   1736 H H    . ALA A 1 111 ? 6.348  48.178 41.044 0.00 15.74  ? 114 ALA A H    1 
ATOM   1737 H HA   . ALA A 1 111 ? 6.613  49.453 38.778 0.00 15.59  ? 114 ALA A HA   1 
ATOM   1738 H HB1  . ALA A 1 111 ? 8.612  50.271 39.677 0.00 28.28  ? 114 ALA A HB1  1 
ATOM   1739 H HB2  . ALA A 1 111 ? 7.445  50.370 40.750 0.00 28.28  ? 114 ALA A HB2  1 
ATOM   1740 H HB3  . ALA A 1 111 ? 8.519  49.203 40.849 0.00 28.28  ? 114 ALA A HB3  1 
ATOM   1741 N N    . ASP A 1 112 ? 8.377  46.806 39.049 1.00 19.31  ? 115 ASP A N    1 
ATOM   1742 C CA   . ASP A 1 112 ? 9.155  45.850 38.268 1.00 12.17  ? 115 ASP A CA   1 
ATOM   1743 C C    . ASP A 1 112 ? 8.352  45.335 37.080 1.00 15.54  ? 115 ASP A C    1 
ATOM   1744 O O    . ASP A 1 112 ? 8.875  45.236 35.963 1.00 16.54  ? 115 ASP A O    1 
ATOM   1745 C CB   . ASP A 1 112 ? 9.601  44.692 39.159 1.00 12.14  ? 115 ASP A CB   1 
ATOM   1746 C CG   . ASP A 1 112 ? 10.650 43.820 38.500 1.00 15.27  ? 115 ASP A CG   1 
ATOM   1747 O OD1  . ASP A 1 112 ? 10.273 42.937 37.703 1.00 17.78  ? 115 ASP A OD1  1 
ATOM   1748 O OD2  . ASP A 1 112 ? 11.851 44.015 38.781 1.00 26.59  ? 115 ASP A OD2  1 
ATOM   1749 H H    . ASP A 1 112 ? 8.208  46.558 39.855 0.00 23.18  ? 115 ASP A H    1 
ATOM   1750 H HA   . ASP A 1 112 ? 9.949  46.291 37.927 0.00 14.53  ? 115 ASP A HA   1 
ATOM   1751 H HB2  . ASP A 1 112 ? 9.979  45.049 39.978 0.00 14.49  ? 115 ASP A HB2  1 
ATOM   1752 H HB3  . ASP A 1 112 ? 8.833  44.136 39.363 0.00 14.49  ? 115 ASP A HB3  1 
ATOM   1753 N N    . GLY A 1 113 ? 7.078  45.004 37.302 1.00 17.39  ? 116 GLY A N    1 
ATOM   1754 C CA   . GLY A 1 113 ? 6.243  44.546 36.204 1.00 12.23  ? 116 GLY A CA   1 
ATOM   1755 C C    . GLY A 1 113 ? 6.077  45.598 35.125 1.00 14.01  ? 116 GLY A C    1 
ATOM   1756 O O    . GLY A 1 113 ? 6.056  45.283 33.932 1.00 16.40  ? 116 GLY A O    1 
ATOM   1757 H H    . GLY A 1 113 ? 6.685  45.036 38.066 0.00 20.88  ? 116 GLY A H    1 
ATOM   1758 H HA2  . GLY A 1 113 ? 6.643  43.759 35.803 0.00 14.60  ? 116 GLY A HA2  1 
ATOM   1759 H HA3  . GLY A 1 113 ? 5.364  44.316 36.544 0.00 14.60  ? 116 GLY A HA3  1 
ATOM   1760 N N    . ILE A 1 114 ? 5.957  46.864 35.526 1.00 12.62  ? 117 ILE A N    1 
ATOM   1761 C CA   . ILE A 1 114 ? 5.887  47.940 34.544 1.00 18.80  ? 117 ILE A CA   1 
ATOM   1762 C C    . ILE A 1 114 ? 7.209  48.060 33.796 1.00 20.16  ? 117 ILE A C    1 
ATOM   1763 O O    . ILE A 1 114 ? 7.232  48.260 32.576 1.00 14.11  ? 117 ILE A O    1 
ATOM   1764 C CB   . ILE A 1 114 ? 5.501  49.264 35.229 1.00 21.34  ? 117 ILE A CB   1 
ATOM   1765 C CG1  . ILE A 1 114 ? 4.047  49.206 35.708 1.00 13.53  ? 117 ILE A CG1  1 
ATOM   1766 C CG2  . ILE A 1 114 ? 5.711  50.434 34.274 1.00 13.63  ? 117 ILE A CG2  1 
ATOM   1767 C CD1  . ILE A 1 114 ? 3.664  50.324 36.660 1.00 19.52  ? 117 ILE A CD1  1 
ATOM   1768 H H    . ILE A 1 114 ? 5.915  47.121 36.346 0.00 15.07  ? 117 ILE A H    1 
ATOM   1769 H HA   . ILE A 1 114 ? 5.196  47.725 33.899 0.00 22.57  ? 117 ILE A HA   1 
ATOM   1770 H HB   . ILE A 1 114 ? 6.072  49.393 36.002 0.00 25.62  ? 117 ILE A HB   1 
ATOM   1771 H HG12 . ILE A 1 114 ? 3.463  49.264 34.935 0.00 16.17  ? 117 ILE A HG12 1 
ATOM   1772 H HG13 . ILE A 1 114 ? 3.905  48.364 36.169 0.00 16.17  ? 117 ILE A HG13 1 
ATOM   1773 H HG21 . ILE A 1 114 ? 5.232  51.207 34.612 0.00 16.28  ? 117 ILE A HG21 1 
ATOM   1774 H HG22 . ILE A 1 114 ? 6.659  50.630 34.219 0.00 16.28  ? 117 ILE A HG22 1 
ATOM   1775 H HG23 . ILE A 1 114 ? 5.372  50.192 33.398 0.00 16.28  ? 117 ILE A HG23 1 
ATOM   1776 H HD11 . ILE A 1 114 ? 2.764  50.168 36.986 0.00 23.44  ? 117 ILE A HD11 1 
ATOM   1777 H HD12 . ILE A 1 114 ? 4.287  50.334 37.403 0.00 23.44  ? 117 ILE A HD12 1 
ATOM   1778 H HD13 . ILE A 1 114 ? 3.701  51.170 36.186 0.00 23.44  ? 117 ILE A HD13 1 
ATOM   1779 N N    . MET A 1 115 ? 8.330  47.930 34.511 1.00 12.56  ? 118 MET A N    1 
ATOM   1780 C CA   . MET A 1 115 ? 9.637  48.053 33.872 1.00 16.19  ? 118 MET A CA   1 
ATOM   1781 C C    . MET A 1 115 ? 9.810  47.012 32.770 1.00 12.44  ? 118 MET A C    1 
ATOM   1782 O O    . MET A 1 115 ? 10.214 47.339 31.647 1.00 12.72  ? 118 MET A O    1 
ATOM   1783 C CB   . MET A 1 115 ? 10.741 47.920 34.924 1.00 12.40  ? 118 MET A CB   1 
ATOM   1784 C CG   . MET A 1 115 ? 12.154 47.797 34.357 1.00 13.99  ? 118 MET A CG   1 
ATOM   1785 S SD   . MET A 1 115 ? 13.388 47.549 35.650 1.00 17.35  ? 118 MET A SD   1 
ATOM   1786 C CE   . MET A 1 115 ? 13.397 45.757 35.752 1.00 16.78  ? 118 MET A CE   1 
ATOM   1787 H H    . MET A 1 115 ? 8.359  47.774 35.356 0.00 14.99  ? 118 MET A H    1 
ATOM   1788 H HA   . MET A 1 115 ? 9.709  48.935 33.475 0.00 19.45  ? 118 MET A HA   1 
ATOM   1789 H HB2  . MET A 1 115 ? 10.721 48.706 35.492 0.00 14.80  ? 118 MET A HB2  1 
ATOM   1790 H HB3  . MET A 1 115 ? 10.568 47.124 35.452 0.00 14.80  ? 118 MET A HB3  1 
ATOM   1791 H HG2  . MET A 1 115 ? 12.191 47.038 33.754 0.00 16.81  ? 118 MET A HG2  1 
ATOM   1792 H HG3  . MET A 1 115 ? 12.377 48.611 33.879 0.00 16.81  ? 118 MET A HG3  1 
ATOM   1793 H HE1  . MET A 1 115 ? 14.036 45.483 36.428 0.00 20.15  ? 118 MET A HE1  1 
ATOM   1794 H HE2  . MET A 1 115 ? 12.509 45.450 35.992 0.00 20.15  ? 118 MET A HE2  1 
ATOM   1795 H HE3  . MET A 1 115 ? 13.652 45.394 34.889 0.00 20.15  ? 118 MET A HE3  1 
ATOM   1796 N N    . ILE A 1 116 ? 9.507  45.749 33.072 1.00 12.15  ? 119 ILE A N    1 
ATOM   1797 C CA   . ILE A 1 116 ? 9.664  44.694 32.075 1.00 12.11  ? 119 ILE A CA   1 
ATOM   1798 C C    . ILE A 1 116 ? 8.592  44.812 30.999 1.00 14.20  ? 119 ILE A C    1 
ATOM   1799 O O    . ILE A 1 116 ? 8.863  44.614 29.808 1.00 12.71  ? 119 ILE A O    1 
ATOM   1800 C CB   . ILE A 1 116 ? 9.630  43.311 32.752 1.00 14.79  ? 119 ILE A CB   1 
ATOM   1801 C CG1  . ILE A 1 116 ? 10.709 43.211 33.834 1.00 13.44  ? 119 ILE A CG1  1 
ATOM   1802 C CG2  . ILE A 1 116 ? 9.808  42.210 31.715 1.00 19.21  ? 119 ILE A CG2  1 
ATOM   1803 C CD1  . ILE A 1 116 ? 12.114 43.504 33.337 1.00 17.27  ? 119 ILE A CD1  1 
ATOM   1804 H H    . ILE A 1 116 ? 9.213  45.481 33.835 0.00 14.51  ? 119 ILE A H    1 
ATOM   1805 H HA   . ILE A 1 116 ? 10.529 44.801 31.650 0.00 14.46  ? 119 ILE A HA   1 
ATOM   1806 H HB   . ILE A 1 116 ? 8.764  43.202 33.175 0.00 17.76  ? 119 ILE A HB   1 
ATOM   1807 H HG12 . ILE A 1 116 ? 10.505 43.850 34.535 0.00 16.14  ? 119 ILE A HG12 1 
ATOM   1808 H HG13 . ILE A 1 116 ? 10.705 42.311 34.194 0.00 16.14  ? 119 ILE A HG13 1 
ATOM   1809 H HG21 . ILE A 1 116 ? 9.997  41.375 32.171 0.00 23.06  ? 119 ILE A HG21 1 
ATOM   1810 H HG22 . ILE A 1 116 ? 8.992  42.128 31.198 0.00 23.06  ? 119 ILE A HG22 1 
ATOM   1811 H HG23 . ILE A 1 116 ? 10.547 42.443 31.131 0.00 23.06  ? 119 ILE A HG23 1 
ATOM   1812 H HD11 . ILE A 1 116 ? 12.750 43.261 34.028 0.00 20.73  ? 119 ILE A HD11 1 
ATOM   1813 H HD12 . ILE A 1 116 ? 12.281 42.983 32.536 0.00 20.73  ? 119 ILE A HD12 1 
ATOM   1814 H HD13 . ILE A 1 116 ? 12.188 44.450 33.138 0.00 20.73  ? 119 ILE A HD13 1 
ATOM   1815 N N    . GLY A 1 117 ? 7.361  45.136 31.400 1.00 14.04  ? 120 GLY A N    1 
ATOM   1816 C CA   . GLY A 1 117 ? 6.277  45.226 30.434 1.00 18.10  ? 120 GLY A CA   1 
ATOM   1817 C C    . GLY A 1 117 ? 6.520  46.289 29.379 1.00 23.60  ? 120 GLY A C    1 
ATOM   1818 O O    . GLY A 1 117 ? 6.377  46.036 28.180 1.00 21.81  ? 120 GLY A O    1 
ATOM   1819 H H    . GLY A 1 117 ? 7.134  45.306 32.212 0.00 16.86  ? 120 GLY A H    1 
ATOM   1820 H HA2  . GLY A 1 117 ? 6.175  44.372 29.987 0.00 21.74  ? 120 GLY A HA2  1 
ATOM   1821 H HA3  . GLY A 1 117 ? 5.453  45.441 30.897 0.00 21.74  ? 120 GLY A HA3  1 
ATOM   1822 N N    . THR A 1 118 ? 6.885  47.499 29.810 1.00 18.45  ? 121 THR A N    1 
ATOM   1823 C CA   . THR A 1 118 ? 7.176  48.556 28.846 1.00 14.40  ? 121 THR A CA   1 
ATOM   1824 C C    . THR A 1 118 ? 8.430  48.244 28.041 1.00 14.27  ? 121 THR A C    1 
ATOM   1825 O O    . THR A 1 118 ? 8.525  48.630 26.871 1.00 14.91  ? 121 THR A O    1 
ATOM   1826 C CB   . THR A 1 118 ? 7.322  49.904 29.557 1.00 14.35  ? 121 THR A CB   1 
ATOM   1827 O OG1  . THR A 1 118 ? 8.314  49.805 30.584 1.00 13.85  ? 121 THR A OG1  1 
ATOM   1828 C CG2  . THR A 1 118 ? 5.997  50.330 30.172 1.00 15.63  ? 121 THR A CG2  1 
ATOM   1829 H H    . THR A 1 118 ? 6.970  47.726 30.635 0.00 22.16  ? 121 THR A H    1 
ATOM   1830 H HA   . THR A 1 118 ? 6.429  48.627 28.231 0.00 17.30  ? 121 THR A HA   1 
ATOM   1831 H HB   . THR A 1 118 ? 7.592  50.578 28.914 0.00 17.15  ? 121 THR A HB   1 
ATOM   1832 H HG1  . THR A 1 118 ? 8.069  49.254 31.168 0.00 16.55  ? 121 THR A HG1  1 
ATOM   1833 H HG21 . THR A 1 118 ? 6.094  51.194 30.602 0.00 18.77  ? 121 THR A HG21 1 
ATOM   1834 H HG22 . THR A 1 118 ? 5.317  50.395 29.484 0.00 18.77  ? 121 THR A HG22 1 
ATOM   1835 H HG23 . THR A 1 118 ? 5.714  49.680 30.834 0.00 18.77  ? 121 THR A HG23 1 
ATOM   1836 N N    . GLY A 1 119 ? 9.399  47.552 28.643 1.00 16.20  ? 122 GLY A N    1 
ATOM   1837 C CA   . GLY A 1 119 ? 10.551 47.103 27.878 1.00 13.83  ? 122 GLY A CA   1 
ATOM   1838 C C    . GLY A 1 119 ? 10.162 46.162 26.755 1.00 15.35  ? 122 GLY A C    1 
ATOM   1839 O O    . GLY A 1 119 ? 10.732 46.212 25.662 1.00 19.97  ? 122 GLY A O    1 
ATOM   1840 H H    . GLY A 1 119 ? 9.410  47.335 29.475 0.00 19.46  ? 122 GLY A H    1 
ATOM   1841 H HA2  . GLY A 1 119 ? 11.000 47.872 27.492 0.00 16.52  ? 122 GLY A HA2  1 
ATOM   1842 H HA3  . GLY A 1 119 ? 11.168 46.640 28.467 0.00 16.52  ? 122 GLY A HA3  1 
ATOM   1843 N N    . LEU A 1 120 ? 9.181  45.293 27.006 1.00 14.48  ? 123 LEU A N    1 
ATOM   1844 C CA   . LEU A 1 120 ? 8.708  44.384 25.966 1.00 16.94  ? 123 LEU A CA   1 
ATOM   1845 C C    . LEU A 1 120 ? 8.010  45.145 24.845 1.00 15.05  ? 123 LEU A C    1 
ATOM   1846 O O    . LEU A 1 120 ? 8.224  44.853 23.662 1.00 18.16  ? 123 LEU A O    1 
ATOM   1847 C CB   . LEU A 1 120 ? 7.768  43.342 26.576 1.00 13.85  ? 123 LEU A CB   1 
ATOM   1848 C CG   . LEU A 1 120 ? 7.030  42.411 25.610 1.00 19.20  ? 123 LEU A CG   1 
ATOM   1849 C CD1  . LEU A 1 120 ? 8.008  41.545 24.834 1.00 19.88  ? 123 LEU A CD1  1 
ATOM   1850 C CD2  . LEU A 1 120 ? 6.037  41.547 26.369 1.00 25.62  ? 123 LEU A CD2  1 
ATOM   1851 H H    . LEU A 1 120 ? 8.778  45.211 27.762 0.00 17.40  ? 123 LEU A H    1 
ATOM   1852 H HA   . LEU A 1 120 ? 9.468  43.919 25.583 0.00 20.34  ? 123 LEU A HA   1 
ATOM   1853 H HB2  . LEU A 1 120 ? 8.293  42.778 27.165 0.00 16.55  ? 123 LEU A HB2  1 
ATOM   1854 H HB3  . LEU A 1 120 ? 7.091  43.815 27.085 0.00 16.55  ? 123 LEU A HB3  1 
ATOM   1855 H HG   . LEU A 1 120 ? 6.540  42.948 24.968 0.00 23.05  ? 123 LEU A HG   1 
ATOM   1856 H HD11 . LEU A 1 120 ? 7.510  40.940 24.263 0.00 23.87  ? 123 LEU A HD11 1 
ATOM   1857 H HD12 . LEU A 1 120 ? 8.576  42.117 24.295 0.00 23.87  ? 123 LEU A HD12 1 
ATOM   1858 H HD13 . LEU A 1 120 ? 8.548  41.039 25.461 0.00 23.87  ? 123 LEU A HD13 1 
ATOM   1859 H HD21 . LEU A 1 120 ? 5.573  40.973 25.740 0.00 30.76  ? 123 LEU A HD21 1 
ATOM   1860 H HD22 . LEU A 1 120 ? 6.518  41.008 27.016 0.00 30.76  ? 123 LEU A HD22 1 
ATOM   1861 H HD23 . LEU A 1 120 ? 5.402  42.122 26.824 0.00 30.76  ? 123 LEU A HD23 1 
ATOM   1862 N N    . VAL A 1 121 ? 7.171  46.124 25.195 1.00 17.49  ? 124 VAL A N    1 
ATOM   1863 C CA   . VAL A 1 121 ? 6.471  46.897 24.173 1.00 16.19  ? 124 VAL A CA   1 
ATOM   1864 C C    . VAL A 1 121 ? 7.468  47.654 23.306 1.00 16.78  ? 124 VAL A C    1 
ATOM   1865 O O    . VAL A 1 121 ? 7.327  47.715 22.079 1.00 17.67  ? 124 VAL A O    1 
ATOM   1866 C CB   . VAL A 1 121 ? 5.451  47.847 24.827 1.00 18.35  ? 124 VAL A CB   1 
ATOM   1867 C CG1  . VAL A 1 121 ? 4.895  48.827 23.800 1.00 17.41  ? 124 VAL A CG1  1 
ATOM   1868 C CG2  . VAL A 1 121 ? 4.327  47.053 25.479 1.00 16.01  ? 124 VAL A CG2  1 
ATOM   1869 H H    . VAL A 1 121 ? 6.995  46.355 26.004 0.00 21.00  ? 124 VAL A H    1 
ATOM   1870 H HA   . VAL A 1 121 ? 5.983  46.283 23.601 0.00 19.35  ? 124 VAL A HA   1 
ATOM   1871 H HB   . VAL A 1 121 ? 5.898  48.361 25.518 0.00 22.03  ? 124 VAL A HB   1 
ATOM   1872 H HG11 . VAL A 1 121 ? 4.088  49.232 24.155 0.00 20.82  ? 124 VAL A HG11 1 
ATOM   1873 H HG12 . VAL A 1 121 ? 5.559  49.512 23.625 0.00 20.82  ? 124 VAL A HG12 1 
ATOM   1874 H HG13 . VAL A 1 121 ? 4.692  48.346 22.983 0.00 20.82  ? 124 VAL A HG13 1 
ATOM   1875 H HG21 . VAL A 1 121 ? 3.712  47.670 25.907 0.00 19.14  ? 124 VAL A HG21 1 
ATOM   1876 H HG22 . VAL A 1 121 ? 3.863  46.544 24.796 0.00 19.14  ? 124 VAL A HG22 1 
ATOM   1877 H HG23 . VAL A 1 121 ? 4.707  46.453 26.140 0.00 19.14  ? 124 VAL A HG23 1 
ATOM   1878 N N    . GLY A 1 122 ? 8.491  48.245 23.928 1.00 16.42  ? 125 GLY A N    1 
ATOM   1879 C CA   . GLY A 1 122 ? 9.509  48.933 23.156 1.00 18.75  ? 125 GLY A CA   1 
ATOM   1880 C C    . GLY A 1 122 ? 10.303 47.996 22.270 1.00 17.26  ? 125 GLY A C    1 
ATOM   1881 O O    . GLY A 1 122 ? 10.801 48.403 21.217 1.00 18.94  ? 125 GLY A O    1 
ATOM   1882 H H    . GLY A 1 122 ? 8.611  48.259 24.780 0.00 19.63  ? 125 GLY A H    1 
ATOM   1883 H HA2  . GLY A 1 122 ? 9.086  49.600 22.592 0.00 22.52  ? 125 GLY A HA2  1 
ATOM   1884 H HA3  . GLY A 1 122 ? 10.125 49.376 23.761 0.00 22.52  ? 125 GLY A HA3  1 
ATOM   1885 N N    . ALA A 1 123 ? 10.430 46.731 22.676 1.00 16.54  ? 126 ALA A N    1 
ATOM   1886 C CA   . ALA A 1 123 ? 11.170 45.769 21.868 1.00 24.23  ? 126 ALA A CA   1 
ATOM   1887 C C    . ALA A 1 123 ? 10.403 45.380 20.611 1.00 22.80  ? 126 ALA A C    1 
ATOM   1888 O O    . ALA A 1 123 ? 11.019 45.047 19.592 1.00 18.39  ? 126 ALA A O    1 
ATOM   1889 C CB   . ALA A 1 123 ? 11.490 44.525 22.697 1.00 20.45  ? 126 ALA A CB   1 
ATOM   1890 H H    . ALA A 1 123 ? 10.101 46.411 23.404 0.00 19.78  ? 126 ALA A H    1 
ATOM   1891 H HA   . ALA A 1 123 ? 12.008 46.174 21.595 0.00 29.09  ? 126 ALA A HA   1 
ATOM   1892 H HB1  . ALA A 1 123 ? 11.983 43.897 22.146 0.00 24.56  ? 126 ALA A HB1  1 
ATOM   1893 H HB2  . ALA A 1 123 ? 12.027 44.785 23.462 0.00 24.56  ? 126 ALA A HB2  1 
ATOM   1894 H HB3  . ALA A 1 123 ? 10.660 44.122 22.996 0.00 24.56  ? 126 ALA A HB3  1 
ATOM   1895 N N    . LEU A 1 124 ? 9.071  45.417 20.658 1.00 17.74  ? 127 LEU A N    1 
ATOM   1896 C CA   . LEU A 1 124 ? 8.233  45.021 19.533 1.00 20.40  ? 127 LEU A CA   1 
ATOM   1897 C C    . LEU A 1 124 ? 7.646  46.204 18.773 1.00 20.28  ? 127 LEU A C    1 
ATOM   1898 O O    . LEU A 1 124 ? 6.907  45.993 17.806 1.00 24.25  ? 127 LEU A O    1 
ATOM   1899 C CB   . LEU A 1 124 ? 7.093  44.118 20.020 1.00 18.24  ? 127 LEU A CB   1 
ATOM   1900 C CG   . LEU A 1 124 ? 7.505  42.834 20.740 1.00 23.18  ? 127 LEU A CG   1 
ATOM   1901 C CD1  . LEU A 1 124 ? 6.283  42.126 21.306 1.00 28.20  ? 127 LEU A CD1  1 
ATOM   1902 C CD2  . LEU A 1 124 ? 8.275  41.916 19.805 1.00 17.69  ? 127 LEU A CD2  1 
ATOM   1903 H H    . LEU A 1 124 ? 8.623  45.675 21.345 0.00 21.21  ? 127 LEU A H    1 
ATOM   1904 H HA   . LEU A 1 124 ? 8.780  44.513 18.913 0.00 24.49  ? 127 LEU A HA   1 
ATOM   1905 H HB2  . LEU A 1 124 ? 6.547  44.629 20.637 0.00 21.81  ? 127 LEU A HB2  1 
ATOM   1906 H HB3  . LEU A 1 124 ? 6.566  43.856 19.249 0.00 21.81  ? 127 LEU A HB3  1 
ATOM   1907 H HG   . LEU A 1 124 ? 8.090  43.061 21.480 0.00 27.83  ? 127 LEU A HG   1 
ATOM   1908 H HD11 . LEU A 1 124 ? 6.570  41.330 21.781 0.00 33.85  ? 127 LEU A HD11 1 
ATOM   1909 H HD12 . LEU A 1 124 ? 5.823  42.726 21.914 0.00 33.85  ? 127 LEU A HD12 1 
ATOM   1910 H HD13 . LEU A 1 124 ? 5.694  41.880 20.576 0.00 33.85  ? 127 LEU A HD13 1 
ATOM   1911 H HD21 . LEU A 1 124 ? 8.447  41.076 20.259 0.00 21.16  ? 127 LEU A HD21 1 
ATOM   1912 H HD22 . LEU A 1 124 ? 7.743  41.759 19.009 0.00 21.16  ? 127 LEU A HD22 1 
ATOM   1913 H HD23 . LEU A 1 124 ? 9.113  42.340 19.565 0.00 21.16  ? 127 LEU A HD23 1 
ATOM   1914 N N    . THR A 1 125 ? 7.952  47.434 19.177 1.00 15.63  ? 128 THR A N    1 
ATOM   1915 C CA   . THR A 1 125 ? 7.400  48.603 18.504 1.00 15.72  ? 128 THR A CA   1 
ATOM   1916 C C    . THR A 1 125 ? 8.046  48.770 17.132 1.00 26.37  ? 128 THR A C    1 
ATOM   1917 O O    . THR A 1 125 ? 9.268  48.662 16.994 1.00 26.19  ? 128 THR A O    1 
ATOM   1918 C CB   . THR A 1 125 ? 7.617  49.856 19.353 1.00 16.84  ? 128 THR A CB   1 
ATOM   1919 O OG1  . THR A 1 125 ? 6.820  49.777 20.542 1.00 18.30  ? 128 THR A OG1  1 
ATOM   1920 C CG2  . THR A 1 125 ? 7.236  51.108 18.573 1.00 15.62  ? 128 THR A CG2  1 
ATOM   1921 H H    . THR A 1 125 ? 8.474  47.617 19.835 0.00 18.69  ? 128 THR A H    1 
ATOM   1922 H HA   . THR A 1 125 ? 6.445  48.485 18.380 0.00 18.88  ? 128 THR A HA   1 
ATOM   1923 H HB   . THR A 1 125 ? 8.554  49.921 19.594 0.00 20.23  ? 128 THR A HB   1 
ATOM   1924 H HG1  . THR A 1 125 ? 6.911  50.478 20.996 0.00 21.97  ? 128 THR A HG1  1 
ATOM   1925 H HG21 . THR A 1 125 ? 7.085  51.846 19.184 0.00 18.76  ? 128 THR A HG21 1 
ATOM   1926 H HG22 . THR A 1 125 ? 7.949  51.347 17.961 0.00 18.76  ? 128 THR A HG22 1 
ATOM   1927 H HG23 . THR A 1 125 ? 6.425  50.949 18.066 0.00 18.76  ? 128 THR A HG23 1 
ATOM   1928 N N    . LYS A 1 126 ? 7.221  49.037 16.117 1.00 22.46  ? 129 LYS A N    1 
ATOM   1929 C CA   . LYS A 1 126 ? 7.687  49.135 14.739 1.00 31.57  ? 129 LYS A CA   1 
ATOM   1930 C C    . LYS A 1 126 ? 8.081  50.550 14.333 1.00 25.75  ? 129 LYS A C    1 
ATOM   1931 O O    . LYS A 1 126 ? 8.824  50.713 13.358 1.00 32.13  ? 129 LYS A O    1 
ATOM   1932 C CB   . LYS A 1 126 ? 6.607  48.622 13.779 1.00 31.29  ? 129 LYS A CB   1 
ATOM   1933 C CG   . LYS A 1 126 ? 5.903  47.354 14.246 1.00 42.48  ? 129 LYS A CG   1 
ATOM   1934 C CD   . LYS A 1 126 ? 4.732  47.004 13.343 1.00 52.88  ? 129 LYS A CD   1 
ATOM   1935 C CE   . LYS A 1 126 ? 4.885  45.618 12.742 1.00 63.18  ? 129 LYS A CE   1 
ATOM   1936 N NZ   . LYS A 1 126 ? 3.680  45.206 11.970 1.00 90.04  ? 129 LYS A NZ   1 
ATOM   1937 H H    . LYS A 1 126 ? 6.375  49.167 16.205 0.00 26.97  ? 129 LYS A H    1 
ATOM   1938 H HA   . LYS A 1 126 ? 8.471  48.571 14.641 0.00 37.90  ? 129 LYS A HA   1 
ATOM   1939 H HB2  . LYS A 1 126 ? 5.932  49.311 13.675 0.00 37.56  ? 129 LYS A HB2  1 
ATOM   1940 H HB3  . LYS A 1 126 ? 7.019  48.430 12.922 0.00 37.56  ? 129 LYS A HB3  1 
ATOM   1941 H HG2  . LYS A 1 126 ? 6.530  46.614 14.233 0.00 51.00  ? 129 LYS A HG2  1 
ATOM   1942 H HG3  . LYS A 1 126 ? 5.565  47.486 15.146 0.00 51.00  ? 129 LYS A HG3  1 
ATOM   1943 H HD2  . LYS A 1 126 ? 3.911  47.023 13.859 0.00 63.48  ? 129 LYS A HD2  1 
ATOM   1944 H HD3  . LYS A 1 126 ? 4.683  47.647 12.618 0.00 63.48  ? 129 LYS A HD3  1 
ATOM   1945 H HE2  . LYS A 1 126 ? 5.646  45.613 12.141 0.00 75.84  ? 129 LYS A HE2  1 
ATOM   1946 H HE3  . LYS A 1 126 ? 5.022  44.975 13.455 0.00 75.84  ? 129 LYS A HE3  1 
ATOM   1947 H HZ1  . LYS A 1 126 ? 3.793  44.386 11.644 0.00 108.06 ? 129 LYS A HZ1  1 
ATOM   1948 H HZ2  . LYS A 1 126 ? 2.964  45.211 12.498 0.00 108.06 ? 129 LYS A HZ2  1 
ATOM   1949 H HZ3  . LYS A 1 126 ? 3.545  45.769 11.294 0.00 108.06 ? 129 LYS A HZ3  1 
ATOM   1950 N N    . VAL A 1 127 ? 7.599  51.568 15.040 1.00 24.54  ? 130 VAL A N    1 
ATOM   1951 C CA   . VAL A 1 127 ? 8.031  52.941 14.798 1.00 24.11  ? 130 VAL A CA   1 
ATOM   1952 C C    . VAL A 1 127 ? 9.319  53.176 15.579 1.00 23.39  ? 130 VAL A C    1 
ATOM   1953 O O    . VAL A 1 127 ? 9.325  53.135 16.814 1.00 23.16  ? 130 VAL A O    1 
ATOM   1954 C CB   . VAL A 1 127 ? 6.944  53.947 15.200 1.00 33.95  ? 130 VAL A CB   1 
ATOM   1955 C CG1  . VAL A 1 127 ? 7.447  55.376 15.016 1.00 24.61  ? 130 VAL A CG1  1 
ATOM   1956 C CG2  . VAL A 1 127 ? 5.676  53.714 14.387 1.00 30.99  ? 130 VAL A CG2  1 
ATOM   1957 H H    . VAL A 1 127 ? 7.017  51.489 15.668 0.00 29.46  ? 130 VAL A H    1 
ATOM   1958 H HA   . VAL A 1 127 ? 8.214  53.061 13.853 0.00 28.95  ? 130 VAL A HA   1 
ATOM   1959 H HB   . VAL A 1 127 ? 6.729  53.822 16.137 0.00 40.75  ? 130 VAL A HB   1 
ATOM   1960 H HG11 . VAL A 1 127 ? 6.694  55.985 15.071 0.00 29.55  ? 130 VAL A HG11 1 
ATOM   1961 H HG12 . VAL A 1 127 ? 8.088  55.578 15.715 0.00 29.55  ? 130 VAL A HG12 1 
ATOM   1962 H HG13 . VAL A 1 127 ? 7.871  55.452 14.146 0.00 29.55  ? 130 VAL A HG13 1 
ATOM   1963 H HG21 . VAL A 1 127 ? 5.018  54.384 14.629 0.00 37.21  ? 130 VAL A HG21 1 
ATOM   1964 H HG22 . VAL A 1 127 ? 5.888  53.784 13.443 0.00 37.21  ? 130 VAL A HG22 1 
ATOM   1965 H HG23 . VAL A 1 127 ? 5.334  52.828 14.584 0.00 37.21  ? 130 VAL A HG23 1 
ATOM   1966 N N    . TYR A 1 128 ? 10.409 53.435 14.855 1.00 31.01  ? 131 TYR A N    1 
ATOM   1967 C CA   . TYR A 1 128 ? 11.735 53.442 15.467 1.00 21.50  ? 131 TYR A CA   1 
ATOM   1968 C C    . TYR A 1 128 ? 11.814 54.432 16.625 1.00 24.13  ? 131 TYR A C    1 
ATOM   1969 O O    . TYR A 1 128 ? 12.276 54.089 17.719 1.00 19.75  ? 131 TYR A O    1 
ATOM   1970 C CB   . TYR A 1 128 ? 12.788 53.768 14.407 1.00 25.82  ? 131 TYR A CB   1 
ATOM   1971 C CG   . TYR A 1 128 ? 14.212 53.684 14.908 1.00 44.05  ? 131 TYR A CG   1 
ATOM   1972 C CD1  . TYR A 1 128 ? 14.785 52.460 15.228 1.00 39.35  ? 131 TYR A CD1  1 
ATOM   1973 C CD2  . TYR A 1 128 ? 14.985 54.828 15.059 1.00 42.07  ? 131 TYR A CD2  1 
ATOM   1974 C CE1  . TYR A 1 128 ? 16.088 52.378 15.687 1.00 35.72  ? 131 TYR A CE1  1 
ATOM   1975 C CE2  . TYR A 1 128 ? 16.287 54.756 15.516 1.00 45.51  ? 131 TYR A CE2  1 
ATOM   1976 C CZ   . TYR A 1 128 ? 16.833 53.530 15.829 1.00 43.12  ? 131 TYR A CZ   1 
ATOM   1977 O OH   . TYR A 1 128 ? 18.129 53.456 16.284 1.00 47.35  ? 131 TYR A OH   1 
ATOM   1978 H H    . TYR A 1 128 ? 10.408 53.608 14.013 0.00 37.23  ? 131 TYR A H    1 
ATOM   1979 H HA   . TYR A 1 128 ? 11.918 52.559 15.824 0.00 25.82  ? 131 TYR A HA   1 
ATOM   1980 H HB2  . TYR A 1 128 ? 12.696 53.140 13.674 0.00 30.99  ? 131 TYR A HB2  1 
ATOM   1981 H HB3  . TYR A 1 128 ? 12.640 54.673 14.089 0.00 30.99  ? 131 TYR A HB3  1 
ATOM   1982 H HD1  . TYR A 1 128 ? 14.285 51.682 15.132 0.00 47.24  ? 131 TYR A HD1  1 
ATOM   1983 H HD2  . TYR A 1 128 ? 14.619 55.657 14.848 0.00 50.50  ? 131 TYR A HD2  1 
ATOM   1984 H HE1  . TYR A 1 128 ? 16.458 51.552 15.898 0.00 42.88  ? 131 TYR A HE1  1 
ATOM   1985 H HE2  . TYR A 1 128 ? 16.793 55.531 15.612 0.00 54.62  ? 131 TYR A HE2  1 
ATOM   1986 H HH   . TYR A 1 128 ? 18.450 54.228 16.365 0.00 56.84  ? 131 TYR A HH   1 
ATOM   1987 N N    A SER A 1 129 ? 11.363 55.669 16.400 0.54 18.92  ? 132 SER A N    1 
ATOM   1988 N N    B SER A 1 129 ? 11.361 55.668 16.402 0.46 18.92  ? 132 SER A N    1 
ATOM   1989 C CA   A SER A 1 129 ? 11.488 56.697 17.429 0.54 23.36  ? 132 SER A CA   1 
ATOM   1990 C CA   B SER A 1 129 ? 11.491 56.695 17.432 0.46 23.36  ? 132 SER A CA   1 
ATOM   1991 C C    A SER A 1 129 ? 10.686 56.350 18.677 0.54 20.71  ? 132 SER A C    1 
ATOM   1992 C C    B SER A 1 129 ? 10.682 56.355 18.677 0.46 20.74  ? 132 SER A C    1 
ATOM   1993 O O    A SER A 1 129 ? 11.101 56.685 19.792 0.54 26.07  ? 132 SER A O    1 
ATOM   1994 O O    B SER A 1 129 ? 11.090 56.701 19.792 0.46 26.03  ? 132 SER A O    1 
ATOM   1995 C CB   A SER A 1 129 ? 11.040 58.050 16.875 0.54 25.17  ? 132 SER A CB   1 
ATOM   1996 C CB   B SER A 1 129 ? 11.059 58.051 16.875 0.46 25.17  ? 132 SER A CB   1 
ATOM   1997 O OG   A SER A 1 129 ? 9.627  58.153 16.865 0.54 23.74  ? 132 SER A OG   1 
ATOM   1998 O OG   B SER A 1 129 ? 11.929 58.472 15.839 0.46 25.74  ? 132 SER A OG   1 
ATOM   1999 H H    A SER A 1 129 ? 10.989 55.933 15.673 0.54 22.64  ? 132 SER A H    1 
ATOM   2000 H H    B SER A 1 129 ? 10.982 55.932 15.677 0.46 22.63  ? 132 SER A H    1 
ATOM   2001 H HA   A SER A 1 129 ? 12.421 56.767 17.684 0.54 28.04  ? 132 SER A HA   1 
ATOM   2002 H HA   B SER A 1 129 ? 12.423 56.756 17.691 0.46 28.05  ? 132 SER A HA   1 
ATOM   2003 H HB2  A SER A 1 129 ? 11.404 58.755 17.433 0.54 30.22  ? 132 SER A HB2  1 
ATOM   2004 H HB2  B SER A 1 129 ? 10.160 57.975 16.520 0.46 30.22  ? 132 SER A HB2  1 
ATOM   2005 H HB3  A SER A 1 129 ? 11.369 58.143 15.967 0.54 30.22  ? 132 SER A HB3  1 
ATOM   2006 H HB3  B SER A 1 129 ? 11.079 58.707 17.589 0.46 30.22  ? 132 SER A HB3  1 
ATOM   2007 H HG   A SER A 1 129 ? 9.396  58.901 16.562 0.54 28.51  ? 132 SER A HG   1 
ATOM   2008 H HG   B SER A 1 129 ? 11.699 59.230 15.560 0.46 30.91  ? 132 SER A HG   1 
ATOM   2009 N N    . TYR A 1 130 ? 9.539  55.683 18.516 1.00 19.79  ? 133 TYR A N    1 
ATOM   2010 C CA   . TYR A 1 130 ? 8.727  55.314 19.672 1.00 14.40  ? 133 TYR A CA   1 
ATOM   2011 C C    . TYR A 1 130 ? 9.408  54.273 20.551 1.00 15.43  ? 133 TYR A C    1 
ATOM   2012 O O    . TYR A 1 130 ? 9.062  54.158 21.732 1.00 18.80  ? 133 TYR A O    1 
ATOM   2013 C CB   . TYR A 1 130 ? 7.364  54.777 19.226 1.00 14.61  ? 133 TYR A CB   1 
ATOM   2014 C CG   . TYR A 1 130 ? 6.470  55.787 18.535 1.00 25.62  ? 133 TYR A CG   1 
ATOM   2015 C CD1  . TYR A 1 130 ? 6.763  57.146 18.554 1.00 31.66  ? 133 TYR A CD1  1 
ATOM   2016 C CD2  . TYR A 1 130 ? 5.325  55.376 17.864 1.00 29.07  ? 133 TYR A CD2  1 
ATOM   2017 C CE1  . TYR A 1 130 ? 5.944  58.062 17.921 1.00 41.60  ? 133 TYR A CE1  1 
ATOM   2018 C CE2  . TYR A 1 130 ? 4.502  56.283 17.229 1.00 35.33  ? 133 TYR A CE2  1 
ATOM   2019 C CZ   . TYR A 1 130 ? 4.814  57.625 17.260 1.00 48.10  ? 133 TYR A CZ   1 
ATOM   2020 O OH   . TYR A 1 130 ? 3.992  58.529 16.628 1.00 49.93  ? 133 TYR A OH   1 
ATOM   2021 H H    . TYR A 1 130 ? 9.217  55.438 17.757 0.00 23.76  ? 133 TYR A H    1 
ATOM   2022 H HA   . TYR A 1 130 ? 8.579  56.114 20.201 0.00 17.20  ? 133 TYR A HA   1 
ATOM   2023 H HB2  . TYR A 1 130 ? 7.511  54.047 18.604 0.00 17.46  ? 133 TYR A HB2  1 
ATOM   2024 H HB3  . TYR A 1 130 ? 6.890  54.456 20.008 0.00 17.46  ? 133 TYR A HB3  1 
ATOM   2025 H HD1  . TYR A 1 130 ? 7.523  57.444 19.001 0.00 38.00  ? 133 TYR A HD1  1 
ATOM   2026 H HD2  . TYR A 1 130 ? 5.109  54.472 17.843 0.00 34.90  ? 133 TYR A HD2  1 
ATOM   2027 H HE1  . TYR A 1 130 ? 6.153  58.968 17.940 0.00 49.93  ? 133 TYR A HE1  1 
ATOM   2028 H HE2  . TYR A 1 130 ? 3.741  55.991 16.782 0.00 42.41  ? 133 TYR A HE2  1 
ATOM   2029 H HH   . TYR A 1 130 ? 4.283  59.309 16.740 0.00 59.94  ? 133 TYR A HH   1 
ATOM   2030 N N    . ARG A 1 131 ? 10.356 53.506 20.004 1.00 15.95  ? 134 ARG A N    1 
ATOM   2031 C CA   . ARG A 1 131 ? 11.045 52.500 20.806 1.00 16.99  ? 134 ARG A CA   1 
ATOM   2032 C C    . ARG A 1 131 ? 11.767 53.129 21.990 1.00 17.35  ? 134 ARG A C    1 
ATOM   2033 O O    . ARG A 1 131 ? 11.859 52.514 23.060 1.00 22.62  ? 134 ARG A O    1 
ATOM   2034 C CB   . ARG A 1 131 ? 12.039 51.724 19.939 1.00 16.60  ? 134 ARG A CB   1 
ATOM   2035 C CG   . ARG A 1 131 ? 11.390 50.854 18.874 1.00 19.30  ? 134 ARG A CG   1 
ATOM   2036 C CD   . ARG A 1 131 ? 12.428 50.242 17.940 1.00 25.81  ? 134 ARG A CD   1 
ATOM   2037 N NE   . ARG A 1 131 ? 13.163 49.152 18.571 1.00 23.69  ? 134 ARG A NE   1 
ATOM   2038 C CZ   . ARG A 1 131 ? 12.704 47.915 18.713 1.00 32.17  ? 134 ARG A CZ   1 
ATOM   2039 N NH1  . ARG A 1 131 ? 11.506 47.566 18.271 1.00 28.75  ? 134 ARG A NH1  1 
ATOM   2040 N NH2  . ARG A 1 131 ? 13.465 47.005 19.315 1.00 23.75  ? 134 ARG A NH2  1 
ATOM   2041 H H    . ARG A 1 131 ? 10.614 53.550 19.184 0.00 19.16  ? 134 ARG A H    1 
ATOM   2042 H HA   . ARG A 1 131 ? 10.389 51.874 21.148 0.00 20.40  ? 134 ARG A HA   1 
ATOM   2043 H HB2  . ARG A 1 131 ? 12.618 52.358 19.488 0.00 19.94  ? 134 ARG A HB2  1 
ATOM   2044 H HB3  . ARG A 1 131 ? 12.565 51.145 20.512 0.00 19.94  ? 134 ARG A HB3  1 
ATOM   2045 H HG2  . ARG A 1 131 ? 10.904 50.132 19.302 0.00 23.18  ? 134 ARG A HG2  1 
ATOM   2046 H HG3  . ARG A 1 131 ? 10.784 51.394 18.344 0.00 23.18  ? 134 ARG A HG3  1 
ATOM   2047 H HD2  . ARG A 1 131 ? 11.981 49.890 17.154 0.00 30.99  ? 134 ARG A HD2  1 
ATOM   2048 H HD3  . ARG A 1 131 ? 13.065 50.926 17.681 0.00 30.99  ? 134 ARG A HD3  1 
ATOM   2049 H HE   . ARG A 1 131 ? 13.951 49.322 18.872 0.00 28.44  ? 134 ARG A HE   1 
ATOM   2050 H HH11 . ARG A 1 131 ? 11.005 48.146 17.881 0.00 34.51  ? 134 ARG A HH11 1 
ATOM   2051 H HH12 . ARG A 1 131 ? 11.228 46.758 18.374 0.00 34.51  ? 134 ARG A HH12 1 
ATOM   2052 H HH21 . ARG A 1 131 ? 14.244 47.222 19.607 0.00 28.52  ? 134 ARG A HH21 1 
ATOM   2053 H HH22 . ARG A 1 131 ? 13.177 46.201 19.413 0.00 28.52  ? 134 ARG A HH22 1 
ATOM   2054 N N    . PHE A 1 132 ? 12.282 54.348 21.822 1.00 13.01  ? 135 PHE A N    1 
ATOM   2055 C CA   . PHE A 1 132 ? 13.032 55.009 22.881 1.00 12.98  ? 135 PHE A CA   1 
ATOM   2056 C C    . PHE A 1 132 ? 12.130 55.703 23.892 1.00 22.42  ? 135 PHE A C    1 
ATOM   2057 O O    . PHE A 1 132 ? 12.579 55.992 25.006 1.00 18.49  ? 135 PHE A O    1 
ATOM   2058 C CB   . PHE A 1 132 ? 14.012 56.007 22.264 1.00 18.54  ? 135 PHE A CB   1 
ATOM   2059 C CG   . PHE A 1 132 ? 14.973 55.377 21.297 1.00 21.27  ? 135 PHE A CG   1 
ATOM   2060 C CD1  . PHE A 1 132 ? 16.055 54.643 21.756 1.00 21.77  ? 135 PHE A CD1  1 
ATOM   2061 C CD2  . PHE A 1 132 ? 14.783 55.495 19.931 1.00 20.23  ? 135 PHE A CD2  1 
ATOM   2062 C CE1  . PHE A 1 132 ? 16.938 54.051 20.872 1.00 30.23  ? 135 PHE A CE1  1 
ATOM   2063 C CE2  . PHE A 1 132 ? 15.661 54.907 19.040 1.00 28.64  ? 135 PHE A CE2  1 
ATOM   2064 C CZ   . PHE A 1 132 ? 16.740 54.183 19.512 1.00 35.25  ? 135 PHE A CZ   1 
ATOM   2065 H H    . PHE A 1 132 ? 12.208 54.812 21.102 0.00 15.53  ? 135 PHE A H    1 
ATOM   2066 H HA   . PHE A 1 132 ? 13.550 54.349 23.368 0.00 15.51  ? 135 PHE A HA   1 
ATOM   2067 H HB2  . PHE A 1 132 ? 13.509 56.685 21.785 0.00 22.26  ? 135 PHE A HB2  1 
ATOM   2068 H HB3  . PHE A 1 132 ? 14.530 56.418 22.973 0.00 22.26  ? 135 PHE A HB3  1 
ATOM   2069 H HD1  . PHE A 1 132 ? 16.190 54.547 22.672 0.00 26.14  ? 135 PHE A HD1  1 
ATOM   2070 H HD2  . PHE A 1 132 ? 14.055 55.977 19.609 0.00 24.29  ? 135 PHE A HD2  1 
ATOM   2071 H HE1  . PHE A 1 132 ? 17.663 53.565 21.192 0.00 36.29  ? 135 PHE A HE1  1 
ATOM   2072 H HE2  . PHE A 1 132 ? 15.526 54.998 18.125 0.00 34.38  ? 135 PHE A HE2  1 
ATOM   2073 H HZ   . PHE A 1 132 ? 17.332 53.786 18.914 0.00 42.31  ? 135 PHE A HZ   1 
ATOM   2074 N N    . VAL A 1 133 ? 10.873 55.973 23.534 1.00 16.50  ? 136 VAL A N    1 
ATOM   2075 C CA   . VAL A 1 133 ? 9.908  56.449 24.521 1.00 20.32  ? 136 VAL A CA   1 
ATOM   2076 C C    . VAL A 1 133 ? 9.655  55.367 25.563 1.00 13.72  ? 136 VAL A C    1 
ATOM   2077 O O    . VAL A 1 133 ? 9.685  55.621 26.774 1.00 24.91  ? 136 VAL A O    1 
ATOM   2078 C CB   . VAL A 1 133 ? 8.602  56.880 23.827 1.00 22.55  ? 136 VAL A CB   1 
ATOM   2079 C CG1  . VAL A 1 133 ? 7.502  57.121 24.852 1.00 15.35  ? 136 VAL A CG1  1 
ATOM   2080 C CG2  . VAL A 1 133 ? 8.836  58.125 22.982 1.00 26.76  ? 136 VAL A CG2  1 
ATOM   2081 H H    . VAL A 1 133 ? 10.560 55.890 22.737 0.00 19.81  ? 136 VAL A H    1 
ATOM   2082 H HA   . VAL A 1 133 ? 10.277 57.224 24.972 0.00 24.40  ? 136 VAL A HA   1 
ATOM   2083 H HB   . VAL A 1 133 ? 8.310  56.166 23.239 0.00 27.08  ? 136 VAL A HB   1 
ATOM   2084 H HG11 . VAL A 1 133 ? 6.784  57.622 24.433 0.00 18.43  ? 136 VAL A HG11 1 
ATOM   2085 H HG12 . VAL A 1 133 ? 7.169  56.266 25.166 0.00 18.43  ? 136 VAL A HG12 1 
ATOM   2086 H HG13 . VAL A 1 133 ? 7.867  57.627 25.595 0.00 18.43  ? 136 VAL A HG13 1 
ATOM   2087 H HG21 . VAL A 1 133 ? 8.000  58.383 22.562 0.00 32.12  ? 136 VAL A HG21 1 
ATOM   2088 H HG22 . VAL A 1 133 ? 9.152  58.841 23.556 0.00 32.12  ? 136 VAL A HG22 1 
ATOM   2089 H HG23 . VAL A 1 133 ? 9.500  57.927 22.304 0.00 32.12  ? 136 VAL A HG23 1 
ATOM   2090 N N    . TRP A 1 134 ? 9.411  54.137 25.105 1.00 12.22  ? 137 TRP A N    1 
ATOM   2091 C CA   . TRP A 1 134 ? 9.175  53.033 26.029 1.00 12.98  ? 137 TRP A CA   1 
ATOM   2092 C C    . TRP A 1 134 ? 10.423 52.724 26.845 1.00 14.50  ? 137 TRP A C    1 
ATOM   2093 O O    . TRP A 1 134 ? 10.329 52.394 28.034 1.00 14.72  ? 137 TRP A O    1 
ATOM   2094 C CB   . TRP A 1 134 ? 8.715  51.799 25.253 1.00 11.49  ? 137 TRP A CB   1 
ATOM   2095 C CG   . TRP A 1 134 ? 7.387  52.000 24.602 1.00 20.33  ? 137 TRP A CG   1 
ATOM   2096 C CD1  . TRP A 1 134 ? 7.138  52.128 23.268 1.00 11.89  ? 137 TRP A CD1  1 
ATOM   2097 C CD2  . TRP A 1 134 ? 6.121  52.111 25.261 1.00 13.95  ? 137 TRP A CD2  1 
ATOM   2098 N NE1  . TRP A 1 134 ? 5.791  52.308 23.054 1.00 18.03  ? 137 TRP A NE1  1 
ATOM   2099 C CE2  . TRP A 1 134 ? 5.145  52.301 24.262 1.00 15.98  ? 137 TRP A CE2  1 
ATOM   2100 C CE3  . TRP A 1 134 ? 5.717  52.067 26.599 1.00 14.07  ? 137 TRP A CE3  1 
ATOM   2101 C CZ2  . TRP A 1 134 ? 3.791  52.446 24.559 1.00 12.24  ? 137 TRP A CZ2  1 
ATOM   2102 C CZ3  . TRP A 1 134 ? 4.372  52.209 26.892 1.00 17.03  ? 137 TRP A CZ3  1 
ATOM   2103 C CH2  . TRP A 1 134 ? 3.425  52.398 25.876 1.00 15.55  ? 137 TRP A CH2  1 
ATOM   2104 H H    . TRP A 1 134 ? 9.376  53.920 24.274 0.00 14.68  ? 137 TRP A H    1 
ATOM   2105 H HA   . TRP A 1 134 ? 8.469  53.280 26.648 0.00 15.59  ? 137 TRP A HA   1 
ATOM   2106 H HB2  . TRP A 1 134 ? 9.364  51.601 24.560 0.00 13.80  ? 137 TRP A HB2  1 
ATOM   2107 H HB3  . TRP A 1 134 ? 8.642  51.049 25.864 0.00 13.80  ? 137 TRP A HB3  1 
ATOM   2108 H HD1  . TRP A 1 134 ? 7.784  52.098 22.600 0.00 14.29  ? 137 TRP A HD1  1 
ATOM   2109 H HE1  . TRP A 1 134 ? 5.416  52.409 22.287 0.00 21.65  ? 137 TRP A HE1  1 
ATOM   2110 H HE3  . TRP A 1 134 ? 6.340  51.946 27.279 0.00 16.90  ? 137 TRP A HE3  1 
ATOM   2111 H HZ2  . TRP A 1 134 ? 3.160  52.571 23.887 0.00 14.61  ? 137 TRP A HZ2  1 
ATOM   2112 H HZ3  . TRP A 1 134 ? 4.091  52.178 27.779 0.00 20.45  ? 137 TRP A HZ3  1 
ATOM   2113 H HH2  . TRP A 1 134 ? 2.528  52.493 26.103 0.00 18.68  ? 137 TRP A HH2  1 
ATOM   2114 N N    . TRP A 1 135 ? 11.599 52.821 26.222 1.00 14.07  ? 138 TRP A N    1 
ATOM   2115 C CA   . TRP A 1 135 ? 12.843 52.640 26.963 1.00 16.91  ? 138 TRP A CA   1 
ATOM   2116 C C    . TRP A 1 135 ? 12.945 53.636 28.111 1.00 19.22  ? 138 TRP A C    1 
ATOM   2117 O O    . TRP A 1 135 ? 13.348 53.275 29.224 1.00 18.27  ? 138 TRP A O    1 
ATOM   2118 C CB   . TRP A 1 135 ? 14.036 52.784 26.018 1.00 15.48  ? 138 TRP A CB   1 
ATOM   2119 C CG   . TRP A 1 135 ? 15.354 52.704 26.713 1.00 15.86  ? 138 TRP A CG   1 
ATOM   2120 C CD1  . TRP A 1 135 ? 16.101 51.583 26.925 1.00 16.72  ? 138 TRP A CD1  1 
ATOM   2121 C CD2  . TRP A 1 135 ? 16.084 53.789 27.295 1.00 15.39  ? 138 TRP A CD2  1 
ATOM   2122 N NE1  . TRP A 1 135 ? 17.252 51.903 27.601 1.00 17.25  ? 138 TRP A NE1  1 
ATOM   2123 C CE2  . TRP A 1 135 ? 17.265 53.252 27.842 1.00 20.85  ? 138 TRP A CE2  1 
ATOM   2124 C CE3  . TRP A 1 135 ? 15.853 55.164 27.407 1.00 37.10  ? 138 TRP A CE3  1 
ATOM   2125 C CZ2  . TRP A 1 135 ? 18.213 54.039 28.490 1.00 20.54  ? 138 TRP A CZ2  1 
ATOM   2126 C CZ3  . TRP A 1 135 ? 16.795 55.944 28.051 1.00 35.72  ? 138 TRP A CZ3  1 
ATOM   2127 C CH2  . TRP A 1 135 ? 17.960 55.380 28.584 1.00 32.43  ? 138 TRP A CH2  1 
ATOM   2128 H H    . TRP A 1 135 ? 11.701 52.989 25.385 0.00 16.90  ? 138 TRP A H    1 
ATOM   2129 H HA   . TRP A 1 135 ? 12.861 51.745 27.337 0.00 20.31  ? 138 TRP A HA   1 
ATOM   2130 H HB2  . TRP A 1 135 ? 14.003 52.073 25.359 0.00 18.59  ? 138 TRP A HB2  1 
ATOM   2131 H HB3  . TRP A 1 135 ? 13.984 53.647 25.577 0.00 18.59  ? 138 TRP A HB3  1 
ATOM   2132 H HD1  . TRP A 1 135 ? 15.865 50.726 26.651 0.00 20.08  ? 138 TRP A HD1  1 
ATOM   2133 H HE1  . TRP A 1 135 ? 17.866 51.347 27.835 0.00 20.72  ? 138 TRP A HE1  1 
ATOM   2134 H HE3  . TRP A 1 135 ? 15.081 55.545 27.056 0.00 44.54  ? 138 TRP A HE3  1 
ATOM   2135 H HZ2  . TRP A 1 135 ? 18.988 53.668 28.845 0.00 24.66  ? 138 TRP A HZ2  1 
ATOM   2136 H HZ3  . TRP A 1 135 ? 16.652 56.859 28.132 0.00 42.88  ? 138 TRP A HZ3  1 
ATOM   2137 H HH2  . TRP A 1 135 ? 18.577 55.930 29.012 0.00 38.93  ? 138 TRP A HH2  1 
ATOM   2138 N N    . ALA A 1 136 ? 12.572 54.893 27.864 1.00 13.72  ? 139 ALA A N    1 
ATOM   2139 C CA   . ALA A 1 136 ? 12.669 55.913 28.904 1.00 17.61  ? 139 ALA A CA   1 
ATOM   2140 C C    . ALA A 1 136 ? 11.714 55.624 30.057 1.00 22.83  ? 139 ALA A C    1 
ATOM   2141 O O    . ALA A 1 136 ? 12.085 55.771 31.228 1.00 18.65  ? 139 ALA A O    1 
ATOM   2142 C CB   . ALA A 1 136 ? 12.390 57.293 28.309 1.00 16.27  ? 139 ALA A CB   1 
ATOM   2143 H H    . ALA A 1 136 ? 12.264 55.177 27.113 0.00 16.48  ? 139 ALA A H    1 
ATOM   2144 H HA   . ALA A 1 136 ? 13.572 55.913 29.257 0.00 21.15  ? 139 ALA A HA   1 
ATOM   2145 H HB1  . ALA A 1 136 ? 12.453 57.959 29.012 0.00 19.53  ? 139 ALA A HB1  1 
ATOM   2146 H HB2  . ALA A 1 136 ? 13.045 57.478 27.618 0.00 19.53  ? 139 ALA A HB2  1 
ATOM   2147 H HB3  . ALA A 1 136 ? 11.497 57.298 27.929 0.00 19.53  ? 139 ALA A HB3  1 
ATOM   2148 N N    . ILE A 1 137 ? 10.481 55.218 29.748 1.00 11.14  ? 140 ILE A N    1 
ATOM   2149 C CA   . ILE A 1 137 ? 9.522  54.906 30.803 1.00 14.52  ? 140 ILE A CA   1 
ATOM   2150 C C    . ILE A 1 137 ? 9.990  53.699 31.604 1.00 14.14  ? 140 ILE A C    1 
ATOM   2151 O O    . ILE A 1 137 ? 9.877  53.672 32.836 1.00 17.54  ? 140 ILE A O    1 
ATOM   2152 C CB   . ILE A 1 137 ? 8.122  54.677 30.205 1.00 18.78  ? 140 ILE A CB   1 
ATOM   2153 C CG1  . ILE A 1 137 ? 7.566  55.982 29.631 1.00 20.90  ? 140 ILE A CG1  1 
ATOM   2154 C CG2  . ILE A 1 137 ? 7.176  54.127 31.264 1.00 10.75  ? 140 ILE A CG2  1 
ATOM   2155 C CD1  . ILE A 1 137 ? 6.493  55.775 28.588 1.00 27.03  ? 140 ILE A CD1  1 
ATOM   2156 H H    . ILE A 1 137 ? 10.181 55.118 28.948 0.00 13.38  ? 140 ILE A H    1 
ATOM   2157 H HA   . ILE A 1 137 ? 9.470  55.666 31.404 0.00 17.44  ? 140 ILE A HA   1 
ATOM   2158 H HB   . ILE A 1 137 ? 8.201  54.029 29.488 0.00 22.55  ? 140 ILE A HB   1 
ATOM   2159 H HG12 . ILE A 1 137 ? 7.181  56.502 30.353 0.00 25.10  ? 140 ILE A HG12 1 
ATOM   2160 H HG13 . ILE A 1 137 ? 8.291  56.475 29.216 0.00 25.10  ? 140 ILE A HG13 1 
ATOM   2161 H HG21 . ILE A 1 137 ? 6.261  54.249 30.964 0.00 12.82  ? 140 ILE A HG21 1 
ATOM   2162 H HG22 . ILE A 1 137 ? 7.359  53.183 31.392 0.00 12.82  ? 140 ILE A HG22 1 
ATOM   2163 H HG23 . ILE A 1 137 ? 7.318  54.607 32.095 0.00 12.82  ? 140 ILE A HG23 1 
ATOM   2164 H HD11 . ILE A 1 137 ? 6.202  56.639 28.258 0.00 32.45  ? 140 ILE A HD11 1 
ATOM   2165 H HD12 . ILE A 1 137 ? 6.858  55.248 27.859 0.00 32.45  ? 140 ILE A HD12 1 
ATOM   2166 H HD13 . ILE A 1 137 ? 5.746  55.306 28.992 0.00 32.45  ? 140 ILE A HD13 1 
ATOM   2167 N N    . SER A 1 138 ? 10.517 52.680 30.921 1.00 15.70  ? 141 SER A N    1 
ATOM   2168 C CA   . SER A 1 138 ? 11.032 51.509 31.623 1.00 17.75  ? 141 SER A CA   1 
ATOM   2169 C C    . SER A 1 138 ? 12.193 51.885 32.535 1.00 12.28  ? 141 SER A C    1 
ATOM   2170 O O    . SER A 1 138 ? 12.276 51.413 33.676 1.00 14.95  ? 141 SER A O    1 
ATOM   2171 C CB   . SER A 1 138 ? 11.466 50.444 30.614 1.00 18.32  ? 141 SER A CB   1 
ATOM   2172 O OG   . SER A 1 138 ? 11.946 49.279 31.266 1.00 17.43  ? 141 SER A OG   1 
ATOM   2173 H H    . SER A 1 138 ? 10.587 52.645 30.064 0.00 18.85  ? 141 SER A H    1 
ATOM   2174 H HA   . SER A 1 138 ? 10.326 51.134 32.171 0.00 21.31  ? 141 SER A HA   1 
ATOM   2175 H HB2  . SER A 1 138 ? 10.704 50.204 30.064 0.00 22.00  ? 141 SER A HB2  1 
ATOM   2176 H HB3  . SER A 1 138 ? 12.174 50.807 30.059 0.00 22.00  ? 141 SER A HB3  1 
ATOM   2177 H HG   . SER A 1 138 ? 11.346 48.958 31.758 0.00 20.93  ? 141 SER A HG   1 
ATOM   2178 N N    . THR A 1 139 ? 13.095 52.743 32.052 1.00 13.14  ? 142 THR A N    1 
ATOM   2179 C CA   . THR A 1 139 ? 14.250 53.132 32.854 1.00 13.38  ? 142 THR A CA   1 
ATOM   2180 C C    . THR A 1 139 ? 13.826 53.940 34.075 1.00 15.72  ? 142 THR A C    1 
ATOM   2181 O O    . THR A 1 139 ? 14.417 53.804 35.152 1.00 21.95  ? 142 THR A O    1 
ATOM   2182 C CB   . THR A 1 139 ? 15.237 53.927 31.996 1.00 23.00  ? 142 THR A CB   1 
ATOM   2183 O OG1  . THR A 1 139 ? 15.801 53.067 30.998 1.00 20.53  ? 142 THR A OG1  1 
ATOM   2184 C CG2  . THR A 1 139 ? 16.356 54.508 32.851 1.00 29.17  ? 142 THR A CG2  1 
ATOM   2185 H H    . THR A 1 139 ? 13.062 53.106 31.273 0.00 15.79  ? 142 THR A H    1 
ATOM   2186 H HA   . THR A 1 139 ? 14.701 52.333 33.167 0.00 16.07  ? 142 THR A HA   1 
ATOM   2187 H HB   . THR A 1 139 ? 14.770 54.662 31.569 0.00 27.62  ? 142 THR A HB   1 
ATOM   2188 H HG1  . THR A 1 139 ? 15.194 52.768 30.500 0.00 24.65  ? 142 THR A HG1  1 
ATOM   2189 H HG21 . THR A 1 139 ? 17.087 54.802 32.285 0.00 35.01  ? 142 THR A HG21 1 
ATOM   2190 H HG22 . THR A 1 139 ? 16.027 55.267 33.358 0.00 35.01  ? 142 THR A HG22 1 
ATOM   2191 H HG23 . THR A 1 139 ? 16.686 53.836 33.468 0.00 35.01  ? 142 THR A HG23 1 
ATOM   2192 N N    . ALA A 1 140 ? 12.804 54.786 33.928 1.00 13.06  ? 143 ALA A N    1 
ATOM   2193 C CA   . ALA A 1 140 ? 12.308 55.543 35.073 1.00 17.81  ? 143 ALA A CA   1 
ATOM   2194 C C    . ALA A 1 140 ? 11.747 54.613 36.141 1.00 15.44  ? 143 ALA A C    1 
ATOM   2195 O O    . ALA A 1 140 ? 11.871 54.885 37.341 1.00 19.92  ? 143 ALA A O    1 
ATOM   2196 C CB   . ALA A 1 140 ? 11.244 56.543 34.622 1.00 23.48  ? 143 ALA A CB   1 
ATOM   2197 H H    . ALA A 1 140 ? 12.389 54.937 33.190 0.00 15.69  ? 143 ALA A H    1 
ATOM   2198 H HA   . ALA A 1 140 ? 13.043 56.042 35.462 0.00 21.39  ? 143 ALA A HA   1 
ATOM   2199 H HB1  . ALA A 1 140 ? 10.930 57.040 35.393 0.00 28.19  ? 143 ALA A HB1  1 
ATOM   2200 H HB2  . ALA A 1 140 ? 11.636 57.150 33.975 0.00 28.19  ? 143 ALA A HB2  1 
ATOM   2201 H HB3  . ALA A 1 140 ? 10.508 56.059 34.217 0.00 28.19  ? 143 ALA A HB3  1 
ATOM   2202 N N    . ALA A 1 141 ? 11.121 53.508 35.723 1.00 12.80  ? 144 ALA A N    1 
ATOM   2203 C CA   . ALA A 1 141 ? 10.612 52.540 36.690 1.00 12.17  ? 144 ALA A CA   1 
ATOM   2204 C C    . ALA A 1 141 ? 11.754 51.826 37.403 1.00 15.26  ? 144 ALA A C    1 
ATOM   2205 O O    . ALA A 1 141 ? 11.649 51.513 38.595 1.00 16.59  ? 144 ALA A O    1 
ATOM   2206 C CB   . ALA A 1 141 ? 9.701  51.531 35.993 1.00 11.48  ? 144 ALA A CB   1 
ATOM   2207 H H    . ALA A 1 141 ? 10.982 53.302 34.900 0.00 15.37  ? 144 ALA A H    1 
ATOM   2208 H HA   . ALA A 1 141 ? 10.086 53.010 37.355 0.00 14.53  ? 144 ALA A HA   1 
ATOM   2209 H HB1  . ALA A 1 141 ? 9.377  50.893 36.648 0.00 13.78  ? 144 ALA A HB1  1 
ATOM   2210 H HB2  . ALA A 1 141 ? 8.953  52.003 35.594 0.00 13.78  ? 144 ALA A HB2  1 
ATOM   2211 H HB3  . ALA A 1 141 ? 10.207 51.071 35.305 0.00 13.78  ? 144 ALA A HB3  1 
ATOM   2212 N N    . MET A 1 142 ? 12.848 51.550 36.690 1.00 18.74  ? 145 MET A N    1 
ATOM   2213 C CA   . MET A 1 142 ? 14.012 50.948 37.333 1.00 17.97  ? 145 MET A CA   1 
ATOM   2214 C C    . MET A 1 142 ? 14.629 51.902 38.346 1.00 15.82  ? 145 MET A C    1 
ATOM   2215 O O    . MET A 1 142 ? 15.024 51.485 39.441 1.00 19.16  ? 145 MET A O    1 
ATOM   2216 C CB   . MET A 1 142 ? 15.047 50.551 36.281 1.00 27.37  ? 145 MET A CB   1 
ATOM   2217 C CG   . MET A 1 142 ? 16.222 49.751 36.839 1.00 25.06  ? 145 MET A CG   1 
ATOM   2218 S SD   . MET A 1 142 ? 17.651 49.714 35.736 1.00 28.75  ? 145 MET A SD   1 
ATOM   2219 C CE   . MET A 1 142 ? 18.149 51.436 35.745 1.00 22.05  ? 145 MET A CE   1 
ATOM   2220 H H    . MET A 1 142 ? 12.940 51.700 35.848 0.00 22.50  ? 145 MET A H    1 
ATOM   2221 H HA   . MET A 1 142 ? 13.727 50.141 37.790 0.00 21.58  ? 145 MET A HA   1 
ATOM   2222 H HB2  . MET A 1 142 ? 14.612 50.007 35.607 0.00 32.85  ? 145 MET A HB2  1 
ATOM   2223 H HB3  . MET A 1 142 ? 15.404 51.357 35.877 0.00 32.85  ? 145 MET A HB3  1 
ATOM   2224 H HG2  . MET A 1 142 ? 16.504 50.150 37.677 0.00 30.09  ? 145 MET A HG2  1 
ATOM   2225 H HG3  . MET A 1 142 ? 15.937 48.836 36.986 0.00 30.09  ? 145 MET A HG3  1 
ATOM   2226 H HE1  . MET A 1 142 ? 18.932 51.541 35.182 0.00 26.47  ? 145 MET A HE1  1 
ATOM   2227 H HE2  . MET A 1 142 ? 17.421 51.978 35.403 0.00 26.47  ? 145 MET A HE2  1 
ATOM   2228 H HE3  . MET A 1 142 ? 18.358 51.700 36.654 0.00 26.47  ? 145 MET A HE3  1 
ATOM   2229 N N    . LEU A 1 143 ? 14.726 53.188 37.998 1.00 16.95  ? 146 LEU A N    1 
ATOM   2230 C CA   . LEU A 1 143 ? 15.286 54.159 38.932 1.00 18.65  ? 146 LEU A CA   1 
ATOM   2231 C C    . LEU A 1 143 ? 14.456 54.244 40.204 1.00 19.65  ? 146 LEU A C    1 
ATOM   2232 O O    . LEU A 1 143 ? 15.005 54.467 41.290 1.00 23.11  ? 146 LEU A O    1 
ATOM   2233 C CB   . LEU A 1 143 ? 15.386 55.528 38.264 1.00 16.62  ? 146 LEU A CB   1 
ATOM   2234 C CG   . LEU A 1 143 ? 16.463 55.637 37.182 1.00 34.92  ? 146 LEU A CG   1 
ATOM   2235 C CD1  . LEU A 1 143 ? 16.311 56.932 36.404 1.00 23.62  ? 146 LEU A CD1  1 
ATOM   2236 C CD2  . LEU A 1 143 ? 17.855 55.536 37.792 1.00 34.52  ? 146 LEU A CD2  1 
ATOM   2237 H H    . LEU A 1 143 ? 14.480 53.515 37.242 0.00 20.36  ? 146 LEU A H    1 
ATOM   2238 H HA   . LEU A 1 143 ? 16.182 53.882 39.176 0.00 22.40  ? 146 LEU A HA   1 
ATOM   2239 H HB2  . LEU A 1 143 ? 14.533 55.730 37.848 0.00 19.87  ? 146 LEU A HB2  1 
ATOM   2240 H HB3  . LEU A 1 143 ? 15.588 56.188 38.945 0.00 19.87  ? 146 LEU A HB3  1 
ATOM   2241 H HG   . LEU A 1 143 ? 16.357 54.899 36.562 0.00 41.92  ? 146 LEU A HG   1 
ATOM   2242 H HD11 . LEU A 1 143 ? 16.991 56.968 35.713 0.00 28.36  ? 146 LEU A HD11 1 
ATOM   2243 H HD12 . LEU A 1 143 ? 15.429 56.957 36.000 0.00 28.36  ? 146 LEU A HD12 1 
ATOM   2244 H HD13 . LEU A 1 143 ? 16.417 57.681 37.012 0.00 28.36  ? 146 LEU A HD13 1 
ATOM   2245 H HD21 . LEU A 1 143 ? 18.512 55.787 37.123 0.00 41.44  ? 146 LEU A HD21 1 
ATOM   2246 H HD22 . LEU A 1 143 ? 17.911 56.136 38.552 0.00 41.44  ? 146 LEU A HD22 1 
ATOM   2247 H HD23 . LEU A 1 143 ? 18.008 54.622 38.079 0.00 41.44  ? 146 LEU A HD23 1 
ATOM   2248 N N    . TYR A 1 144 ? 13.137 54.068 40.097 1.00 20.51  ? 147 TYR A N    1 
ATOM   2249 C CA   . TYR A 1 144 ? 12.310 54.006 41.296 1.00 20.02  ? 147 TYR A CA   1 
ATOM   2250 C C    . TYR A 1 144 ? 12.669 52.789 42.139 1.00 18.16  ? 147 TYR A C    1 
ATOM   2251 O O    . TYR A 1 144 ? 12.782 52.886 43.366 1.00 20.42  ? 147 TYR A O    1 
ATOM   2252 C CB   . TYR A 1 144 ? 10.830 53.974 40.917 1.00 30.34  ? 147 TYR A CB   1 
ATOM   2253 C CG   . TYR A 1 144 ? 9.917  53.822 42.112 1.00 24.59  ? 147 TYR A CG   1 
ATOM   2254 C CD1  . TYR A 1 144 ? 9.509  54.931 42.842 1.00 33.63  ? 147 TYR A CD1  1 
ATOM   2255 C CD2  . TYR A 1 144 ? 9.478  52.569 42.522 1.00 28.20  ? 147 TYR A CD2  1 
ATOM   2256 C CE1  . TYR A 1 144 ? 8.681  54.798 43.939 1.00 29.69  ? 147 TYR A CE1  1 
ATOM   2257 C CE2  . TYR A 1 144 ? 8.650  52.426 43.618 1.00 35.77  ? 147 TYR A CE2  1 
ATOM   2258 C CZ   . TYR A 1 144 ? 8.255  53.544 44.324 1.00 45.45  ? 147 TYR A CZ   1 
ATOM   2259 O OH   . TYR A 1 144 ? 7.431  53.408 45.416 1.00 38.58  ? 147 TYR A OH   1 
ATOM   2260 H H    . TYR A 1 144 ? 12.708 53.983 39.356 0.00 24.63  ? 147 TYR A H    1 
ATOM   2261 H HA   . TYR A 1 144 ? 12.466 54.804 41.825 0.00 24.04  ? 147 TYR A HA   1 
ATOM   2262 H HB2  . TYR A 1 144 ? 10.601 54.803 40.470 0.00 36.42  ? 147 TYR A HB2  1 
ATOM   2263 H HB3  . TYR A 1 144 ? 10.673 53.223 40.324 0.00 36.42  ? 147 TYR A HB3  1 
ATOM   2264 H HD1  . TYR A 1 144 ? 9.798  55.777 42.587 0.00 40.37  ? 147 TYR A HD1  1 
ATOM   2265 H HD2  . TYR A 1 144 ? 9.745  51.814 42.049 0.00 33.85  ? 147 TYR A HD2  1 
ATOM   2266 H HE1  . TYR A 1 144 ? 8.413  55.550 44.416 0.00 35.64  ? 147 TYR A HE1  1 
ATOM   2267 H HE2  . TYR A 1 144 ? 8.360  51.582 43.879 0.00 42.94  ? 147 TYR A HE2  1 
ATOM   2268 H HH   . TYR A 1 144 ? 7.261  52.597 45.549 0.00 46.31  ? 147 TYR A HH   1 
ATOM   2269 N N    . ILE A 1 145 ? 12.851 51.634 41.495 1.00 22.71  ? 148 ILE A N    1 
ATOM   2270 C CA   . ILE A 1 145 ? 13.235 50.426 42.223 1.00 17.98  ? 148 ILE A CA   1 
ATOM   2271 C C    . ILE A 1 145 ? 14.559 50.645 42.945 1.00 21.53  ? 148 ILE A C    1 
ATOM   2272 O O    . ILE A 1 145 ? 14.707 50.312 44.127 1.00 20.54  ? 148 ILE A O    1 
ATOM   2273 C CB   . ILE A 1 145 ? 13.309 49.224 41.264 1.00 22.12  ? 148 ILE A CB   1 
ATOM   2274 C CG1  . ILE A 1 145 ? 11.901 48.794 40.842 1.00 21.08  ? 148 ILE A CG1  1 
ATOM   2275 C CG2  . ILE A 1 145 ? 14.053 48.061 41.917 1.00 18.94  ? 148 ILE A CG2  1 
ATOM   2276 C CD1  . ILE A 1 145 ? 11.875 47.912 39.606 1.00 18.32  ? 148 ILE A CD1  1 
ATOM   2277 H H    . ILE A 1 145 ? 12.760 51.524 40.647 0.00 27.27  ? 148 ILE A H    1 
ATOM   2278 H HA   . ILE A 1 145 ? 12.557 50.238 42.891 0.00 21.59  ? 148 ILE A HA   1 
ATOM   2279 H HB   . ILE A 1 145 ? 13.799 49.495 40.472 0.00 26.56  ? 148 ILE A HB   1 
ATOM   2280 H HG12 . ILE A 1 145 ? 11.496 48.297 41.569 0.00 25.31  ? 148 ILE A HG12 1 
ATOM   2281 H HG13 . ILE A 1 145 ? 11.377 49.587 40.650 0.00 25.31  ? 148 ILE A HG13 1 
ATOM   2282 H HG21 . ILE A 1 145 ? 13.850 47.245 41.433 0.00 22.75  ? 148 ILE A HG21 1 
ATOM   2283 H HG22 . ILE A 1 145 ? 15.006 48.237 41.883 0.00 22.75  ? 148 ILE A HG22 1 
ATOM   2284 H HG23 . ILE A 1 145 ? 13.764 47.979 42.839 0.00 22.75  ? 148 ILE A HG23 1 
ATOM   2285 H HD11 . ILE A 1 145 ? 10.954 47.784 39.330 0.00 22.00  ? 148 ILE A HD11 1 
ATOM   2286 H HD12 . ILE A 1 145 ? 12.376 48.345 38.898 0.00 22.00  ? 148 ILE A HD12 1 
ATOM   2287 H HD13 . ILE A 1 145 ? 12.277 47.056 39.821 0.00 22.00  ? 148 ILE A HD13 1 
ATOM   2288 N N    . LEU A 1 146 ? 15.544 51.211 42.242 1.00 21.51  ? 149 LEU A N    1 
ATOM   2289 C CA   . LEU A 1 146 ? 16.850 51.440 42.854 1.00 32.38  ? 149 LEU A CA   1 
ATOM   2290 C C    . LEU A 1 146 ? 16.745 52.400 44.033 1.00 34.44  ? 149 LEU A C    1 
ATOM   2291 O O    . LEU A 1 146 ? 17.404 52.206 45.061 1.00 29.11  ? 149 LEU A O    1 
ATOM   2292 C CB   . LEU A 1 146 ? 17.829 51.981 41.809 1.00 31.67  ? 149 LEU A CB   1 
ATOM   2293 C CG   . LEU A 1 146 ? 18.157 51.070 40.621 1.00 26.67  ? 149 LEU A CG   1 
ATOM   2294 C CD1  . LEU A 1 146 ? 19.348 51.615 39.849 1.00 32.83  ? 149 LEU A CD1  1 
ATOM   2295 C CD2  . LEU A 1 146 ? 18.421 49.640 41.068 1.00 24.94  ? 149 LEU A CD2  1 
ATOM   2296 H H    . LEU A 1 146 ? 15.482 51.467 41.424 0.00 25.83  ? 149 LEU A H    1 
ATOM   2297 H HA   . LEU A 1 146 ? 17.194 50.595 43.182 0.00 38.87  ? 149 LEU A HA   1 
ATOM   2298 H HB2  . LEU A 1 146 ? 17.455 52.798 41.444 0.00 38.02  ? 149 LEU A HB2  1 
ATOM   2299 H HB3  . LEU A 1 146 ? 18.668 52.172 42.258 0.00 38.02  ? 149 LEU A HB3  1 
ATOM   2300 H HG   . LEU A 1 146 ? 17.388 51.050 40.029 0.00 32.02  ? 149 LEU A HG   1 
ATOM   2301 H HD11 . LEU A 1 146 ? 19.523 51.038 39.090 0.00 39.41  ? 149 LEU A HD11 1 
ATOM   2302 H HD12 . LEU A 1 146 ? 19.142 52.512 39.543 0.00 39.41  ? 149 LEU A HD12 1 
ATOM   2303 H HD13 . LEU A 1 146 ? 20.121 51.635 40.435 0.00 39.41  ? 149 LEU A HD13 1 
ATOM   2304 H HD21 . LEU A 1 146 ? 18.794 49.140 40.326 0.00 29.94  ? 149 LEU A HD21 1 
ATOM   2305 H HD22 . LEU A 1 146 ? 19.048 49.651 41.808 0.00 29.94  ? 149 LEU A HD22 1 
ATOM   2306 H HD23 . LEU A 1 146 ? 17.584 49.238 41.350 0.00 29.94  ? 149 LEU A HD23 1 
ATOM   2307 N N    . TYR A 1 147 ? 15.922 53.443 43.902 1.00 28.36  ? 150 TYR A N    1 
ATOM   2308 C CA   . TYR A 1 147 ? 15.758 54.395 44.996 1.00 30.38  ? 150 TYR A CA   1 
ATOM   2309 C C    . TYR A 1 147 ? 15.224 53.710 46.249 1.00 33.61  ? 150 TYR A C    1 
ATOM   2310 O O    . TYR A 1 147 ? 15.704 53.968 47.359 1.00 33.53  ? 150 TYR A O    1 
ATOM   2311 C CB   . TYR A 1 147 ? 14.824 55.526 44.568 1.00 27.51  ? 150 TYR A CB   1 
ATOM   2312 C CG   . TYR A 1 147 ? 14.339 56.379 45.718 1.00 46.39  ? 150 TYR A CG   1 
ATOM   2313 C CD1  . TYR A 1 147 ? 15.183 57.294 46.333 1.00 48.90  ? 150 TYR A CD1  1 
ATOM   2314 C CD2  . TYR A 1 147 ? 13.037 56.272 46.186 1.00 46.66  ? 150 TYR A CD2  1 
ATOM   2315 C CE1  . TYR A 1 147 ? 14.745 58.076 47.385 1.00 58.61  ? 150 TYR A CE1  1 
ATOM   2316 C CE2  . TYR A 1 147 ? 12.589 57.049 47.237 1.00 52.90  ? 150 TYR A CE2  1 
ATOM   2317 C CZ   . TYR A 1 147 ? 13.447 57.950 47.833 1.00 68.14  ? 150 TYR A CZ   1 
ATOM   2318 O OH   . TYR A 1 147 ? 13.005 58.727 48.880 1.00 86.20  ? 150 TYR A OH   1 
ATOM   2319 H H    . TYR A 1 147 ? 15.455 53.618 43.201 0.00 34.04  ? 150 TYR A H    1 
ATOM   2320 H HA   . TYR A 1 147 ? 16.623 54.779 45.208 0.00 36.47  ? 150 TYR A HA   1 
ATOM   2321 H HB2  . TYR A 1 147 ? 15.296 56.103 43.948 0.00 33.02  ? 150 TYR A HB2  1 
ATOM   2322 H HB3  . TYR A 1 147 ? 14.045 55.141 44.135 0.00 33.02  ? 150 TYR A HB3  1 
ATOM   2323 H HD1  . TYR A 1 147 ? 16.058 57.382 46.032 0.00 58.69  ? 150 TYR A HD1  1 
ATOM   2324 H HD2  . TYR A 1 147 ? 12.455 55.667 45.786 0.00 56.01  ? 150 TYR A HD2  1 
ATOM   2325 H HE1  . TYR A 1 147 ? 15.322 58.683 47.788 0.00 70.35  ? 150 TYR A HE1  1 
ATOM   2326 H HE2  . TYR A 1 147 ? 11.714 56.965 47.542 0.00 63.50  ? 150 TYR A HE2  1 
ATOM   2327 H HH   . TYR A 1 147 ? 13.624 59.228 49.147 0.00 103.46 ? 150 TYR A HH   1 
ATOM   2328 N N    . VAL A 1 148 ? 14.231 52.833 46.090 1.00 28.33  ? 151 VAL A N    1 
ATOM   2329 C CA   . VAL A 1 148 ? 13.644 52.157 47.245 1.00 26.12  ? 151 VAL A CA   1 
ATOM   2330 C C    . VAL A 1 148 ? 14.680 51.278 47.933 1.00 33.94  ? 151 VAL A C    1 
ATOM   2331 O O    . VAL A 1 148 ? 14.764 51.241 49.167 1.00 35.53  ? 151 VAL A O    1 
ATOM   2332 C CB   . VAL A 1 148 ? 12.409 51.345 46.811 1.00 32.88  ? 151 VAL A CB   1 
ATOM   2333 C CG1  . VAL A 1 148 ? 11.969 50.400 47.920 1.00 28.49  ? 151 VAL A CG1  1 
ATOM   2334 C CG2  . VAL A 1 148 ? 11.275 52.279 46.413 1.00 24.79  ? 151 VAL A CG2  1 
ATOM   2335 H H    . VAL A 1 148 ? 13.884 52.615 45.334 0.00 34.01  ? 151 VAL A H    1 
ATOM   2336 H HA   . VAL A 1 148 ? 13.355 52.829 47.882 0.00 31.27  ? 151 VAL A HA   1 
ATOM   2337 H HB   . VAL A 1 148 ? 12.642 50.806 46.038 0.00 39.47  ? 151 VAL A HB   1 
ATOM   2338 H HG11 . VAL A 1 148 ? 11.060 50.111 47.747 0.00 34.20  ? 151 VAL A HG11 1 
ATOM   2339 H HG12 . VAL A 1 148 ? 12.563 49.633 47.935 0.00 34.20  ? 151 VAL A HG12 1 
ATOM   2340 H HG13 . VAL A 1 148 ? 12.012 50.868 48.769 0.00 34.20  ? 151 VAL A HG13 1 
ATOM   2341 H HG21 . VAL A 1 148 ? 10.509 51.749 46.145 0.00 29.68  ? 151 VAL A HG21 1 
ATOM   2342 H HG22 . VAL A 1 148 ? 11.043 52.835 47.174 0.00 29.68  ? 151 VAL A HG22 1 
ATOM   2343 H HG23 . VAL A 1 148 ? 11.568 52.835 45.674 0.00 29.68  ? 151 VAL A HG23 1 
ATOM   2344 N N    . LEU A 1 149 ? 15.487 50.559 47.150 1.00 25.78  ? 152 LEU A N    1 
ATOM   2345 C CA   . LEU A 1 149 ? 16.484 49.669 47.733 1.00 32.33  ? 152 LEU A CA   1 
ATOM   2346 C C    . LEU A 1 149 ? 17.527 50.420 48.550 1.00 37.49  ? 152 LEU A C    1 
ATOM   2347 O O    . LEU A 1 149 ? 18.155 49.822 49.430 1.00 42.69  ? 152 LEU A O    1 
ATOM   2348 C CB   . LEU A 1 149 ? 17.180 48.863 46.631 1.00 30.48  ? 152 LEU A CB   1 
ATOM   2349 C CG   . LEU A 1 149 ? 16.341 47.825 45.879 1.00 37.96  ? 152 LEU A CG   1 
ATOM   2350 C CD1  . LEU A 1 149 ? 17.214 47.057 44.898 1.00 36.66  ? 152 LEU A CD1  1 
ATOM   2351 C CD2  . LEU A 1 149 ? 15.647 46.865 46.834 1.00 35.69  ? 152 LEU A CD2  1 
ATOM   2352 H H    . LEU A 1 149 ? 15.476 50.570 46.290 0.00 30.86  ? 152 LEU A H    1 
ATOM   2353 H HA   . LEU A 1 149 ? 16.031 49.047 48.323 0.00 38.81  ? 152 LEU A HA   1 
ATOM   2354 H HB2  . LEU A 1 149 ? 17.511 49.490 45.969 0.00 36.59  ? 152 LEU A HB2  1 
ATOM   2355 H HB3  . LEU A 1 149 ? 17.921 48.386 47.036 0.00 36.59  ? 152 LEU A HB3  1 
ATOM   2356 H HG   . LEU A 1 149 ? 15.648 48.290 45.385 0.00 45.57  ? 152 LEU A HG   1 
ATOM   2357 H HD11 . LEU A 1 149 ? 16.659 46.440 44.398 0.00 44.00  ? 152 LEU A HD11 1 
ATOM   2358 H HD12 . LEU A 1 149 ? 17.638 47.686 44.293 0.00 44.00  ? 152 LEU A HD12 1 
ATOM   2359 H HD13 . LEU A 1 149 ? 17.890 46.568 45.393 0.00 44.00  ? 152 LEU A HD13 1 
ATOM   2360 H HD21 . LEU A 1 149 ? 15.258 46.137 46.324 0.00 42.84  ? 152 LEU A HD21 1 
ATOM   2361 H HD22 . LEU A 1 149 ? 16.299 46.517 47.462 0.00 42.84  ? 152 LEU A HD22 1 
ATOM   2362 H HD23 . LEU A 1 149 ? 14.951 47.343 47.312 0.00 42.84  ? 152 LEU A HD23 1 
ATOM   2363 N N    . PHE A 1 150 ? 17.728 51.711 48.283 1.00 46.76  ? 153 PHE A N    1 
ATOM   2364 C CA   . PHE A 1 150 ? 18.729 52.511 48.982 1.00 39.85  ? 153 PHE A CA   1 
ATOM   2365 C C    . PHE A 1 150 ? 18.136 53.331 50.121 1.00 38.02  ? 153 PHE A C    1 
ATOM   2366 O O    . PHE A 1 150 ? 18.668 53.320 51.235 1.00 58.66  ? 153 PHE A O    1 
ATOM   2367 C CB   . PHE A 1 150 ? 19.435 53.448 47.995 1.00 50.27  ? 153 PHE A CB   1 
ATOM   2368 C CG   . PHE A 1 150 ? 20.619 52.829 47.313 1.00 48.82  ? 153 PHE A CG   1 
ATOM   2369 C CD1  . PHE A 1 150 ? 21.778 52.553 48.020 1.00 64.06  ? 153 PHE A CD1  1 
ATOM   2370 C CD2  . PHE A 1 150 ? 20.575 52.529 45.964 1.00 47.20  ? 153 PHE A CD2  1 
ATOM   2371 C CE1  . PHE A 1 150 ? 22.869 51.983 47.393 1.00 50.14  ? 153 PHE A CE1  1 
ATOM   2372 C CE2  . PHE A 1 150 ? 21.663 51.962 45.333 1.00 69.71  ? 153 PHE A CE2  1 
ATOM   2373 C CZ   . PHE A 1 150 ? 22.811 51.687 46.049 1.00 53.85  ? 153 PHE A CZ   1 
ATOM   2374 H H    . PHE A 1 150 ? 17.288 52.152 47.690 0.00 56.12  ? 153 PHE A H    1 
ATOM   2375 H HA   . PHE A 1 150 ? 19.390 51.910 49.359 0.00 47.84  ? 153 PHE A HA   1 
ATOM   2376 H HB2  . PHE A 1 150 ? 18.803 53.712 47.309 0.00 60.34  ? 153 PHE A HB2  1 
ATOM   2377 H HB3  . PHE A 1 150 ? 19.747 54.230 48.477 0.00 60.34  ? 153 PHE A HB3  1 
ATOM   2378 H HD1  . PHE A 1 150 ? 21.822 52.754 48.927 0.00 76.89  ? 153 PHE A HD1  1 
ATOM   2379 H HD2  . PHE A 1 150 ? 19.804 52.711 45.477 0.00 56.66  ? 153 PHE A HD2  1 
ATOM   2380 H HE1  . PHE A 1 150 ? 23.641 51.800 47.878 0.00 60.19  ? 153 PHE A HE1  1 
ATOM   2381 H HE2  . PHE A 1 150 ? 21.622 51.765 44.425 0.00 83.66  ? 153 PHE A HE2  1 
ATOM   2382 H HZ   . PHE A 1 150 ? 23.544 51.304 45.624 0.00 64.64  ? 153 PHE A HZ   1 
ATOM   2383 N N    . PHE A 1 151 ? 17.047 54.048 49.863 1.00 49.79  ? 154 PHE A N    1 
ATOM   2384 C CA   . PHE A 1 151 ? 16.439 54.951 50.833 1.00 53.87  ? 154 PHE A CA   1 
ATOM   2385 C C    . PHE A 1 151 ? 15.152 54.364 51.402 1.00 63.21  ? 154 PHE A C    1 
ATOM   2386 O O    . PHE A 1 151 ? 14.186 55.080 51.673 1.00 87.03  ? 154 PHE A O    1 
ATOM   2387 C CB   . PHE A 1 151 ? 16.177 56.315 50.199 1.00 68.22  ? 154 PHE A CB   1 
ATOM   2388 C CG   . PHE A 1 151 ? 17.383 56.909 49.525 1.00 72.88  ? 154 PHE A CG   1 
ATOM   2389 C CD1  . PHE A 1 151 ? 17.750 56.509 48.250 1.00 51.96  ? 154 PHE A CD1  1 
ATOM   2390 C CD2  . PHE A 1 151 ? 18.153 57.864 50.168 1.00 83.34  ? 154 PHE A CD2  1 
ATOM   2391 C CE1  . PHE A 1 151 ? 18.859 57.051 47.629 1.00 57.07  ? 154 PHE A CE1  1 
ATOM   2392 C CE2  . PHE A 1 151 ? 19.263 58.410 49.550 1.00 87.55  ? 154 PHE A CE2  1 
ATOM   2393 C CZ   . PHE A 1 151 ? 19.616 58.002 48.279 1.00 79.07  ? 154 PHE A CZ   1 
ATOM   2394 H H    . PHE A 1 151 ? 16.631 54.027 49.111 0.00 59.77  ? 154 PHE A H    1 
ATOM   2395 H HA   . PHE A 1 151 ? 17.055 55.079 51.571 0.00 64.66  ? 154 PHE A HA   1 
ATOM   2396 H HB2  . PHE A 1 151 ? 15.481 56.220 49.531 0.00 81.88  ? 154 PHE A HB2  1 
ATOM   2397 H HB3  . PHE A 1 151 ? 15.891 56.931 50.892 0.00 81.88  ? 154 PHE A HB3  1 
ATOM   2398 H HD1  . PHE A 1 151 ? 17.243 55.867 47.807 0.00 62.36  ? 154 PHE A HD1  1 
ATOM   2399 H HD2  . PHE A 1 151 ? 17.921 58.141 51.024 0.00 100.02 ? 154 PHE A HD2  1 
ATOM   2400 H HE1  . PHE A 1 151 ? 19.094 56.774 46.772 0.00 68.50  ? 154 PHE A HE1  1 
ATOM   2401 H HE2  . PHE A 1 151 ? 19.772 59.051 49.991 0.00 105.08 ? 154 PHE A HE2  1 
ATOM   2402 H HZ   . PHE A 1 151 ? 20.362 58.368 47.863 0.00 94.90  ? 154 PHE A HZ   1 
ATOM   2403 N N    . GLY A 1 152 ? 15.130 53.047 51.589 1.00 53.48  ? 155 GLY A N    1 
ATOM   2404 C CA   . GLY A 1 152 ? 13.982 52.374 52.162 1.00 73.11  ? 155 GLY A CA   1 
ATOM   2405 C C    . GLY A 1 152 ? 14.369 51.102 52.886 1.00 70.71  ? 155 GLY A C    1 
ATOM   2406 O O    . GLY A 1 152 ? 13.981 50.889 54.038 1.00 76.61  ? 155 GLY A O    1 
ATOM   2407 H H    . GLY A 1 152 ? 15.779 52.518 51.388 0.00 64.20  ? 155 GLY A H    1 
ATOM   2408 H HA2  . GLY A 1 152 ? 13.544 52.966 52.794 0.00 87.74  ? 155 GLY A HA2  1 
ATOM   2409 H HA3  . GLY A 1 152 ? 13.356 52.148 51.456 0.00 87.74  ? 155 GLY A HA3  1 
ATOM   2410 N N    . PHE A 1 153 ? 15.143 50.246 52.215 1.00 79.62  ? 156 PHE A N    1 
ATOM   2411 C CA   . PHE A 1 153 ? 15.594 49.004 52.831 1.00 81.16  ? 156 PHE A CA   1 
ATOM   2412 C C    . PHE A 1 153 ? 16.834 49.231 53.688 1.00 86.48  ? 156 PHE A C    1 
ATOM   2413 O O    . PHE A 1 153 ? 16.896 48.779 54.837 1.00 92.00  ? 156 PHE A O    1 
ATOM   2414 C CB   . PHE A 1 153 ? 15.890 47.957 51.755 1.00 65.75  ? 156 PHE A CB   1 
ATOM   2415 C CG   . PHE A 1 153 ? 14.666 47.319 51.156 1.00 51.95  ? 156 PHE A CG   1 
ATOM   2416 C CD1  . PHE A 1 153 ? 13.408 47.871 51.331 1.00 43.11  ? 156 PHE A CD1  1 
ATOM   2417 C CD2  . PHE A 1 153 ? 14.783 46.158 50.410 1.00 49.07  ? 156 PHE A CD2  1 
ATOM   2418 C CE1  . PHE A 1 153 ? 12.294 47.274 50.776 1.00 65.17  ? 156 PHE A CE1  1 
ATOM   2419 C CE2  . PHE A 1 153 ? 13.672 45.558 49.853 1.00 51.23  ? 156 PHE A CE2  1 
ATOM   2420 C CZ   . PHE A 1 153 ? 12.426 46.117 50.037 1.00 62.68  ? 156 PHE A CZ   1 
ATOM   2421 H H    . PHE A 1 153 ? 15.417 50.362 51.408 0.00 95.56  ? 156 PHE A H    1 
ATOM   2422 H HA   . PHE A 1 153 ? 14.884 48.665 53.399 0.00 97.41  ? 156 PHE A HA   1 
ATOM   2423 H HB2  . PHE A 1 153 ? 16.381 48.384 51.035 0.00 78.92  ? 156 PHE A HB2  1 
ATOM   2424 H HB3  . PHE A 1 153 ? 16.427 47.251 52.149 0.00 78.92  ? 156 PHE A HB3  1 
ATOM   2425 H HD1  . PHE A 1 153 ? 13.313 48.652 51.828 0.00 51.66  ? 156 PHE A HD1  1 
ATOM   2426 H HD2  . PHE A 1 153 ? 15.622 45.777 50.283 0.00 58.90  ? 156 PHE A HD2  1 
ATOM   2427 H HE1  . PHE A 1 153 ? 11.454 47.653 50.901 0.00 78.21  ? 156 PHE A HE1  1 
ATOM   2428 H HE2  . PHE A 1 153 ? 13.765 44.779 49.355 0.00 61.49  ? 156 PHE A HE2  1 
ATOM   2429 H HZ   . PHE A 1 153 ? 11.676 45.715 49.662 0.00 75.23  ? 156 PHE A HZ   1 
ATOM   2430 N N    . THR A 1 154 ? 17.835 49.927 53.139 1.00 80.21  ? 157 THR A N    1 
ATOM   2431 C CA   . THR A 1 154 ? 19.087 50.134 53.860 1.00 97.83  ? 157 THR A CA   1 
ATOM   2432 C C    . THR A 1 154 ? 18.853 50.744 55.235 1.00 97.41  ? 157 THR A C    1 
ATOM   2433 O O    . THR A 1 154 ? 19.576 50.427 56.187 1.00 96.70  ? 157 THR A O    1 
ATOM   2434 C CB   . THR A 1 154 ? 20.021 51.030 53.041 1.00 90.88  ? 157 THR A CB   1 
ATOM   2435 O OG1  . THR A 1 154 ? 20.364 50.377 51.810 1.00 46.17  ? 157 THR A OG1  1 
ATOM   2436 C CG2  . THR A 1 154 ? 21.294 51.340 53.820 1.00 102.76 ? 157 THR A CG2  1 
ATOM   2437 H H    . THR A 1 154 ? 17.812 50.284 52.357 0.00 96.26  ? 157 THR A H    1 
ATOM   2438 H HA   . THR A 1 154 ? 19.520 49.275 53.982 0.00 117.42 ? 157 THR A HA   1 
ATOM   2439 H HB   . THR A 1 154 ? 19.572 51.867 52.847 0.00 109.07 ? 157 THR A HB   1 
ATOM   2440 H HG1  . THR A 1 154 ? 19.668 50.205 51.373 0.00 55.42  ? 157 THR A HG1  1 
ATOM   2441 H HG21 . THR A 1 154 ? 21.976 51.679 53.220 0.00 123.32 ? 157 THR A HG21 1 
ATOM   2442 H HG22 . THR A 1 154 ? 21.112 52.008 54.499 0.00 123.32 ? 157 THR A HG22 1 
ATOM   2443 H HG23 . THR A 1 154 ? 21.624 50.535 54.250 0.00 123.32 ? 157 THR A HG23 1 
ATOM   2444 N N    . SER A 1 155 ? 17.852 51.618 55.362 1.00 93.93  ? 158 SER A N    1 
ATOM   2445 C CA   . SER A 1 155 ? 17.561 52.231 56.652 1.00 100.47 ? 158 SER A CA   1 
ATOM   2446 C C    . SER A 1 155 ? 16.973 51.237 57.645 1.00 109.26 ? 158 SER A C    1 
ATOM   2447 O O    . SER A 1 155 ? 17.071 51.459 58.856 1.00 110.18 ? 158 SER A O    1 
ATOM   2448 C CB   . SER A 1 155 ? 16.600 53.407 56.468 1.00 112.43 ? 158 SER A CB   1 
ATOM   2449 H H    . SER A 1 155 ? 17.334 51.868 54.723 0.00 112.73 ? 158 SER A H    1 
ATOM   2450 H HA   . SER A 1 155 ? 18.387 52.573 57.027 0.00 120.58 ? 158 SER A HA   1 
ATOM   2451 N N    . LYS A 1 156 ? 16.368 50.152 57.162 1.00 114.36 ? 159 LYS A N    1 
ATOM   2452 C CA   . LYS A 1 156 ? 15.776 49.140 58.029 1.00 118.61 ? 159 LYS A CA   1 
ATOM   2453 C C    . LYS A 1 156 ? 16.680 47.934 58.236 1.00 116.84 ? 159 LYS A C    1 
ATOM   2454 O O    . LYS A 1 156 ? 16.573 47.266 59.269 1.00 116.06 ? 159 LYS A O    1 
ATOM   2455 C CB   . LYS A 1 156 ? 14.430 48.681 57.451 1.00 112.12 ? 159 LYS A CB   1 
ATOM   2456 C CG   . LYS A 1 156 ? 14.015 47.259 57.816 1.00 100.90 ? 159 LYS A CG   1 
ATOM   2457 C CD   . LYS A 1 156 ? 12.600 46.953 57.340 1.00 87.95  ? 159 LYS A CD   1 
ATOM   2458 C CE   . LYS A 1 156 ? 11.552 47.715 58.139 1.00 121.13 ? 159 LYS A CE   1 
ATOM   2459 N NZ   . LYS A 1 156 ? 10.171 47.251 57.830 1.00 99.32  ? 159 LYS A NZ   1 
ATOM   2460 H H    . LYS A 1 156 ? 16.287 49.979 56.324 0.00 137.24 ? 159 LYS A H    1 
ATOM   2461 H HA   . LYS A 1 156 ? 15.604 49.527 58.901 0.00 142.34 ? 159 LYS A HA   1 
ATOM   2462 H HB2  . LYS A 1 156 ? 13.738 49.277 57.778 0.00 134.56 ? 159 LYS A HB2  1 
ATOM   2463 H HB3  . LYS A 1 156 ? 14.480 48.730 56.484 0.00 134.56 ? 159 LYS A HB3  1 
ATOM   2464 H HG2  . LYS A 1 156 ? 14.621 46.629 57.394 0.00 121.10 ? 159 LYS A HG2  1 
ATOM   2465 H HG3  . LYS A 1 156 ? 14.043 47.152 58.779 0.00 121.10 ? 159 LYS A HG3  1 
ATOM   2466 H HD2  . LYS A 1 156 ? 12.514 47.209 56.408 0.00 105.56 ? 159 LYS A HD2  1 
ATOM   2467 H HD3  . LYS A 1 156 ? 12.427 46.004 57.441 0.00 105.56 ? 159 LYS A HD3  1 
ATOM   2468 H HE2  . LYS A 1 156 ? 11.712 47.580 59.086 0.00 145.37 ? 159 LYS A HE2  1 
ATOM   2469 H HE3  . LYS A 1 156 ? 11.610 48.659 57.924 0.00 145.37 ? 159 LYS A HE3  1 
ATOM   2470 H HZ1  . LYS A 1 156 ? 9.581  47.707 58.315 0.00 119.20 ? 159 LYS A HZ1  1 
ATOM   2471 H HZ2  . LYS A 1 156 ? 9.994  47.377 56.967 0.00 119.20 ? 159 LYS A HZ2  1 
ATOM   2472 H HZ3  . LYS A 1 156 ? 10.092 46.385 58.018 0.00 119.20 ? 159 LYS A HZ3  1 
ATOM   2473 N N    . ALA A 1 157 ? 17.570 47.642 57.284 1.00 96.23  ? 160 ALA A N    1 
ATOM   2474 C CA   . ALA A 1 157 ? 18.494 46.527 57.456 1.00 84.84  ? 160 ALA A CA   1 
ATOM   2475 C C    . ALA A 1 157 ? 19.491 46.804 58.574 1.00 86.92  ? 160 ALA A C    1 
ATOM   2476 O O    . ALA A 1 157 ? 19.888 45.887 59.302 1.00 75.98  ? 160 ALA A O    1 
ATOM   2477 C CB   . ALA A 1 157 ? 19.229 46.250 56.145 1.00 64.08  ? 160 ALA A CB   1 
ATOM   2478 H H    . ALA A 1 157 ? 17.655 48.069 56.542 0.00 115.49 ? 160 ALA A H    1 
ATOM   2479 H HA   . ALA A 1 157 ? 17.987 45.735 57.692 0.00 101.82 ? 160 ALA A HA   1 
ATOM   2480 H HB1  . ALA A 1 157 ? 19.835 45.504 56.274 0.00 76.92  ? 160 ALA A HB1  1 
ATOM   2481 H HB2  . ALA A 1 157 ? 18.579 46.033 55.458 0.00 76.92  ? 160 ALA A HB2  1 
ATOM   2482 H HB3  . ALA A 1 157 ? 19.729 47.041 55.889 0.00 76.92  ? 160 ALA A HB3  1 
ATOM   2483 N N    . GLU A 1 158 ? 19.905 48.064 58.727 1.00 90.94  ? 161 GLU A N    1 
ATOM   2484 C CA   . GLU A 1 158 ? 20.897 48.410 59.737 1.00 88.41  ? 161 GLU A CA   1 
ATOM   2485 C C    . GLU A 1 158 ? 20.387 48.191 61.155 1.00 92.60  ? 161 GLU A C    1 
ATOM   2486 O O    . GLU A 1 158 ? 21.196 48.123 62.086 1.00 115.67 ? 161 GLU A O    1 
ATOM   2487 C CB   . GLU A 1 158 ? 21.333 49.865 59.559 1.00 91.90  ? 161 GLU A CB   1 
ATOM   2488 C CG   . GLU A 1 158 ? 22.179 50.102 58.318 1.00 97.39  ? 161 GLU A CG   1 
ATOM   2489 C CD   . GLU A 1 158 ? 22.320 51.572 57.977 1.00 115.14 ? 161 GLU A CD   1 
ATOM   2490 O OE1  . GLU A 1 158 ? 21.897 52.417 58.793 1.00 124.96 ? 161 GLU A OE1  1 
ATOM   2491 O OE2  . GLU A 1 158 ? 22.855 51.882 56.891 1.00 102.31 ? 161 GLU A OE2  1 
ATOM   2492 H H    . GLU A 1 158 ? 19.626 48.731 58.261 0.00 109.14 ? 161 GLU A H    1 
ATOM   2493 H HA   . GLU A 1 158 ? 21.675 47.844 59.615 0.00 106.10 ? 161 GLU A HA   1 
ATOM   2494 H HB2  . GLU A 1 158 ? 20.541 50.421 59.489 0.00 110.30 ? 161 GLU A HB2  1 
ATOM   2495 H HB3  . GLU A 1 158 ? 21.857 50.130 60.331 0.00 110.30 ? 161 GLU A HB3  1 
ATOM   2496 H HG2  . GLU A 1 158 ? 23.068 49.742 58.468 0.00 116.88 ? 161 GLU A HG2  1 
ATOM   2497 H HG3  . GLU A 1 158 ? 21.764 49.657 57.563 0.00 116.88 ? 161 GLU A HG3  1 
ATOM   2498 N N    . SER A 1 159 ? 19.071 48.078 61.342 1.00 101.14 ? 162 SER A N    1 
ATOM   2499 C CA   . SER A 1 159 ? 18.479 47.840 62.651 1.00 103.30 ? 162 SER A CA   1 
ATOM   2500 C C    . SER A 1 159 ? 18.151 46.369 62.877 1.00 106.59 ? 162 SER A C    1 
ATOM   2501 O O    . SER A 1 159 ? 17.337 46.049 63.751 1.00 102.64 ? 162 SER A O    1 
ATOM   2502 C CB   . SER A 1 159 ? 17.220 48.692 62.820 1.00 87.96  ? 162 SER A CB   1 
ATOM   2503 O OG   . SER A 1 159 ? 16.247 48.360 61.845 1.00 106.37 ? 162 SER A OG   1 
ATOM   2504 H H    . SER A 1 159 ? 18.492 48.138 60.710 0.00 121.39 ? 162 SER A H    1 
ATOM   2505 H HA   . SER A 1 159 ? 19.118 48.109 63.330 0.00 123.98 ? 162 SER A HA   1 
ATOM   2506 H HB2  . SER A 1 159 ? 16.849 48.533 63.702 0.00 105.57 ? 162 SER A HB2  1 
ATOM   2507 H HB3  . SER A 1 159 ? 17.458 49.627 62.723 0.00 105.57 ? 162 SER A HB3  1 
ATOM   2508 H HG   . SER A 1 159 ? 16.555 48.491 61.075 0.00 127.66 ? 162 SER A HG   1 
ATOM   2509 N N    . MET A 1 160 ? 18.768 45.473 62.115 1.00 103.25 ? 163 MET A N    1 
ATOM   2510 C CA   . MET A 1 160 ? 18.496 44.044 62.181 1.00 94.87  ? 163 MET A CA   1 
ATOM   2511 C C    . MET A 1 160 ? 19.749 43.298 62.638 1.00 75.61  ? 163 MET A C    1 
ATOM   2512 O O    . MET A 1 160 ? 20.753 43.900 63.031 1.00 71.18  ? 163 MET A O    1 
ATOM   2513 C CB   . MET A 1 160 ? 18.005 43.529 60.825 1.00 86.91  ? 163 MET A CB   1 
ATOM   2514 C CG   . MET A 1 160 ? 16.853 44.338 60.218 1.00 102.45 ? 163 MET A CG   1 
ATOM   2515 S SD   . MET A 1 160 ? 15.171 43.747 60.562 1.00 121.22 ? 163 MET A SD   1 
ATOM   2516 C CE   . MET A 1 160 ? 15.314 41.959 60.494 1.00 65.81  ? 163 MET A CE   1 
ATOM   2517 H H    . MET A 1 160 ? 19.367 45.677 61.533 0.00 123.91 ? 163 MET A H    1 
ATOM   2518 H HA   . MET A 1 160 ? 17.792 43.905 62.834 0.00 113.86 ? 163 MET A HA   1 
ATOM   2519 H HB2  . MET A 1 160 ? 18.745 43.556 60.198 0.00 104.31 ? 163 MET A HB2  1 
ATOM   2520 H HB3  . MET A 1 160 ? 17.696 42.616 60.935 0.00 104.31 ? 163 MET A HB3  1 
ATOM   2521 H HG2  . MET A 1 160 ? 16.910 45.244 60.559 0.00 122.95 ? 163 MET A HG2  1 
ATOM   2522 H HG3  . MET A 1 160 ? 16.961 44.338 59.254 0.00 122.95 ? 163 MET A HG3  1 
ATOM   2523 H HE1  . MET A 1 160 ? 14.435 41.567 60.616 0.00 78.98  ? 163 MET A HE1  1 
ATOM   2524 H HE2  . MET A 1 160 ? 15.673 41.703 59.630 0.00 78.98  ? 163 MET A HE2  1 
ATOM   2525 H HE3  . MET A 1 160 ? 15.909 41.663 61.201 0.00 78.98  ? 163 MET A HE3  1 
ATOM   2526 N N    . ARG A 1 161 ? 19.677 41.972 62.585 1.00 71.35  ? 164 ARG A N    1 
ATOM   2527 C CA   . ARG A 1 161 ? 20.821 41.153 62.958 1.00 60.05  ? 164 ARG A CA   1 
ATOM   2528 C C    . ARG A 1 161 ? 22.030 41.564 62.120 1.00 47.51  ? 164 ARG A C    1 
ATOM   2529 O O    . ARG A 1 161 ? 21.882 41.880 60.934 1.00 53.43  ? 164 ARG A O    1 
ATOM   2530 C CB   . ARG A 1 161 ? 20.533 39.660 62.755 1.00 58.57  ? 164 ARG A CB   1 
ATOM   2531 C CG   . ARG A 1 161 ? 19.056 39.272 62.687 1.00 70.29  ? 164 ARG A CG   1 
ATOM   2532 C CD   . ARG A 1 161 ? 18.834 37.796 62.992 1.00 63.17  ? 164 ARG A CD   1 
ATOM   2533 N NE   . ARG A 1 161 ? 19.673 36.928 62.173 1.00 56.38  ? 164 ARG A NE   1 
ATOM   2534 C CZ   . ARG A 1 161 ? 19.339 35.705 61.780 1.00 51.22  ? 164 ARG A CZ   1 
ATOM   2535 N NH1  . ARG A 1 161 ? 18.170 35.169 62.094 1.00 61.06  ? 164 ARG A NH1  1 
ATOM   2536 N NH2  . ARG A 1 161 ? 20.200 35.000 61.052 1.00 49.36  ? 164 ARG A NH2  1 
ATOM   2537 H H    . ARG A 1 161 ? 18.984 41.527 62.338 0.00 85.63  ? 164 ARG A H    1 
ATOM   2538 H HA   . ARG A 1 161 ? 21.017 41.289 63.898 0.00 72.07  ? 164 ARG A HA   1 
ATOM   2539 H HB2  . ARG A 1 161 ? 20.942 39.382 61.921 0.00 70.30  ? 164 ARG A HB2  1 
ATOM   2540 H HB3  . ARG A 1 161 ? 20.925 39.171 63.496 0.00 70.30  ? 164 ARG A HB3  1 
ATOM   2541 H HG2  . ARG A 1 161 ? 18.560 39.793 63.338 0.00 84.36  ? 164 ARG A HG2  1 
ATOM   2542 H HG3  . ARG A 1 161 ? 18.721 39.450 61.794 0.00 84.36  ? 164 ARG A HG3  1 
ATOM   2543 H HD2  . ARG A 1 161 ? 19.047 37.629 63.924 0.00 75.82  ? 164 ARG A HD2  1 
ATOM   2544 H HD3  . ARG A 1 161 ? 17.907 37.572 62.818 0.00 75.82  ? 164 ARG A HD3  1 
ATOM   2545 H HE   . ARG A 1 161 ? 20.440 37.230 61.927 0.00 67.67  ? 164 ARG A HE   1 
ATOM   2546 H HH11 . ARG A 1 161 ? 17.605 35.615 62.565 0.00 73.29  ? 164 ARG A HH11 1 
ATOM   2547 H HH12 . ARG A 1 161 ? 17.975 34.375 61.828 0.00 73.29  ? 164 ARG A HH12 1 
ATOM   2548 H HH21 . ARG A 1 161 ? 20.962 35.337 60.841 0.00 59.25  ? 164 ARG A HH21 1 
ATOM   2549 H HH22 . ARG A 1 161 ? 19.994 34.206 60.791 0.00 59.25  ? 164 ARG A HH22 1 
ATOM   2550 N N    . PRO A 1 162 ? 23.236 41.582 62.696 1.00 39.20  ? 165 PRO A N    1 
ATOM   2551 C CA   . PRO A 1 162 ? 24.402 41.996 61.896 1.00 43.08  ? 165 PRO A CA   1 
ATOM   2552 C C    . PRO A 1 162 ? 24.606 41.153 60.649 1.00 47.92  ? 165 PRO A C    1 
ATOM   2553 O O    . PRO A 1 162 ? 24.908 41.700 59.581 1.00 44.15  ? 165 PRO A O    1 
ATOM   2554 C CB   . PRO A 1 162 ? 25.571 41.856 62.880 1.00 37.07  ? 165 PRO A CB   1 
ATOM   2555 C CG   . PRO A 1 162 ? 24.954 41.925 64.230 1.00 47.19  ? 165 PRO A CG   1 
ATOM   2556 C CD   . PRO A 1 162 ? 23.597 41.309 64.099 1.00 40.78  ? 165 PRO A CD   1 
ATOM   2557 H HA   . PRO A 1 162 ? 24.308 42.927 61.640 0.00 51.72  ? 165 PRO A HA   1 
ATOM   2558 H HB2  . PRO A 1 162 ? 26.016 41.005 62.745 0.00 44.50  ? 165 PRO A HB2  1 
ATOM   2559 H HB3  . PRO A 1 162 ? 26.200 42.583 62.749 0.00 44.50  ? 165 PRO A HB3  1 
ATOM   2560 H HG2  . PRO A 1 162 ? 25.496 41.427 64.862 0.00 56.64  ? 165 PRO A HG2  1 
ATOM   2561 H HG3  . PRO A 1 162 ? 24.884 42.851 64.510 0.00 56.64  ? 165 PRO A HG3  1 
ATOM   2562 H HD2  . PRO A 1 162 ? 23.634 40.354 64.266 0.00 48.95  ? 165 PRO A HD2  1 
ATOM   2563 H HD3  . PRO A 1 162 ? 22.967 41.728 64.705 0.00 48.95  ? 165 PRO A HD3  1 
ATOM   2564 N N    . GLU A 1 163 ? 24.453 39.830 60.752 1.00 33.95  ? 166 GLU A N    1 
ATOM   2565 C CA   . GLU A 1 163 ? 24.635 38.981 59.579 1.00 41.60  ? 166 GLU A CA   1 
ATOM   2566 C C    . GLU A 1 163 ? 23.621 39.309 58.492 1.00 34.33  ? 166 GLU A C    1 
ATOM   2567 O O    . GLU A 1 163 ? 23.921 39.170 57.301 1.00 36.63  ? 166 GLU A O    1 
ATOM   2568 C CB   . GLU A 1 163 ? 24.538 37.506 59.975 1.00 41.73  ? 166 GLU A CB   1 
ATOM   2569 C CG   . GLU A 1 163 ? 23.202 37.091 60.579 1.00 50.84  ? 166 GLU A CG   1 
ATOM   2570 C CD   . GLU A 1 163 ? 23.227 37.070 62.093 1.00 48.13  ? 166 GLU A CD   1 
ATOM   2571 O OE1  . GLU A 1 163 ? 23.919 37.922 62.689 1.00 59.51  ? 166 GLU A OE1  1 
ATOM   2572 O OE2  . GLU A 1 163 ? 22.554 36.201 62.687 1.00 72.97  ? 166 GLU A OE2  1 
ATOM   2573 H H    . GLU A 1 163 ? 24.249 39.410 61.474 0.00 40.76  ? 166 GLU A H    1 
ATOM   2574 H HA   . GLU A 1 163 ? 25.522 39.133 59.218 0.00 49.94  ? 166 GLU A HA   1 
ATOM   2575 H HB2  . GLU A 1 163 ? 24.680 36.965 59.182 0.00 50.09  ? 166 GLU A HB2  1 
ATOM   2576 H HB3  . GLU A 1 163 ? 25.226 37.318 60.633 0.00 50.09  ? 166 GLU A HB3  1 
ATOM   2577 H HG2  . GLU A 1 163 ? 22.518 37.720 60.299 0.00 61.02  ? 166 GLU A HG2  1 
ATOM   2578 H HG3  . GLU A 1 163 ? 22.978 36.199 60.271 0.00 61.02  ? 166 GLU A HG3  1 
ATOM   2579 N N    . VAL A 1 164 ? 22.421 39.746 58.878 1.00 33.63  ? 167 VAL A N    1 
ATOM   2580 C CA   . VAL A 1 164 ? 21.409 40.109 57.891 1.00 35.81  ? 167 VAL A CA   1 
ATOM   2581 C C    . VAL A 1 164 ? 21.791 41.412 57.200 1.00 36.46  ? 167 VAL A C    1 
ATOM   2582 O O    . VAL A 1 164 ? 21.713 41.530 55.972 1.00 33.33  ? 167 VAL A O    1 
ATOM   2583 C CB   . VAL A 1 164 ? 20.025 40.211 58.558 1.00 44.11  ? 167 VAL A CB   1 
ATOM   2584 C CG1  . VAL A 1 164 ? 19.074 41.046 57.706 1.00 46.64  ? 167 VAL A CG1  1 
ATOM   2585 C CG2  . VAL A 1 164 ? 19.450 38.824 58.805 1.00 42.02  ? 167 VAL A CG2  1 
ATOM   2586 H H    . VAL A 1 164 ? 22.172 39.840 59.696 0.00 40.37  ? 167 VAL A H    1 
ATOM   2587 H HA   . VAL A 1 164 ? 21.368 39.413 57.217 0.00 42.98  ? 167 VAL A HA   1 
ATOM   2588 H HB   . VAL A 1 164 ? 20.124 40.654 59.415 0.00 52.95  ? 167 VAL A HB   1 
ATOM   2589 H HG11 . VAL A 1 164 ? 18.165 40.902 58.014 0.00 55.98  ? 167 VAL A HG11 1 
ATOM   2590 H HG12 . VAL A 1 164 ? 19.309 41.982 57.796 0.00 55.98  ? 167 VAL A HG12 1 
ATOM   2591 H HG13 . VAL A 1 164 ? 19.156 40.771 56.779 0.00 55.98  ? 167 VAL A HG13 1 
ATOM   2592 H HG21 . VAL A 1 164 ? 18.600 38.912 59.265 0.00 50.44  ? 167 VAL A HG21 1 
ATOM   2593 H HG22 . VAL A 1 164 ? 19.320 38.380 57.952 0.00 50.44  ? 167 VAL A HG22 1 
ATOM   2594 H HG23 . VAL A 1 164 ? 20.071 38.317 59.351 0.00 50.44  ? 167 VAL A HG23 1 
ATOM   2595 N N    . ALA A 1 165 ? 22.211 42.410 57.981 1.00 26.26  ? 168 ALA A N    1 
ATOM   2596 C CA   . ALA A 1 165 ? 22.556 43.705 57.407 1.00 38.55  ? 168 ALA A CA   1 
ATOM   2597 C C    . ALA A 1 165 ? 23.752 43.593 56.471 1.00 31.35  ? 168 ALA A C    1 
ATOM   2598 O O    . ALA A 1 165 ? 23.795 44.249 55.424 1.00 36.27  ? 168 ALA A O    1 
ATOM   2599 C CB   . ALA A 1 165 ? 22.843 44.711 58.522 1.00 42.43  ? 168 ALA A CB   1 
ATOM   2600 H H    . ALA A 1 165 ? 22.303 42.361 58.835 0.00 31.53  ? 168 ALA A H    1 
ATOM   2601 H HA   . ALA A 1 165 ? 21.801 44.030 56.892 0.00 46.27  ? 168 ALA A HA   1 
ATOM   2602 H HB1  . ALA A 1 165 ? 23.043 45.573 58.126 0.00 50.93  ? 168 ALA A HB1  1 
ATOM   2603 H HB2  . ALA A 1 165 ? 22.061 44.781 59.092 0.00 50.93  ? 168 ALA A HB2  1 
ATOM   2604 H HB3  . ALA A 1 165 ? 23.602 44.400 59.039 0.00 50.93  ? 168 ALA A HB3  1 
ATOM   2605 N N    . SER A 1 166 ? 24.736 42.768 56.831 1.00 31.71  ? 169 SER A N    1 
ATOM   2606 C CA   . SER A 1 166 ? 25.933 42.651 56.004 1.00 33.43  ? 169 SER A CA   1 
ATOM   2607 C C    . SER A 1 166 ? 25.629 41.938 54.692 1.00 34.68  ? 169 SER A C    1 
ATOM   2608 O O    . SER A 1 166 ? 26.131 42.336 53.634 1.00 34.91  ? 169 SER A O    1 
ATOM   2609 C CB   . SER A 1 166 ? 27.030 41.916 56.773 1.00 40.08  ? 169 SER A CB   1 
ATOM   2610 O OG   . SER A 1 166 ? 28.299 42.137 56.184 1.00 67.60  ? 169 SER A OG   1 
ATOM   2611 H H    . SER A 1 166 ? 24.735 42.275 57.535 0.00 38.06  ? 169 SER A H    1 
ATOM   2612 H HA   . SER A 1 166 ? 26.257 43.540 55.794 0.00 40.14  ? 169 SER A HA   1 
ATOM   2613 H HB2  . SER A 1 166 ? 27.046 42.242 57.687 0.00 48.11  ? 169 SER A HB2  1 
ATOM   2614 H HB3  . SER A 1 166 ? 26.839 40.965 56.763 0.00 48.11  ? 169 SER A HB3  1 
ATOM   2615 H HG   . SER A 1 166 ? 28.894 41.743 56.627 0.00 81.13  ? 169 SER A HG   1 
ATOM   2616 N N    . THR A 1 167 ? 24.812 40.884 54.738 1.00 35.60  ? 170 THR A N    1 
ATOM   2617 C CA   . THR A 1 167 ? 24.470 40.167 53.513 1.00 31.52  ? 170 THR A CA   1 
ATOM   2618 C C    . THR A 1 167 ? 23.612 41.027 52.595 1.00 30.20  ? 170 THR A C    1 
ATOM   2619 O O    . THR A 1 167 ? 23.812 41.034 51.374 1.00 32.94  ? 170 THR A O    1 
ATOM   2620 C CB   . THR A 1 167 ? 23.748 38.863 53.849 1.00 35.60  ? 170 THR A CB   1 
ATOM   2621 O OG1  . THR A 1 167 ? 24.595 38.042 54.661 1.00 36.74  ? 170 THR A OG1  1 
ATOM   2622 C CG2  . THR A 1 167 ? 23.384 38.108 52.578 1.00 34.64  ? 170 THR A CG2  1 
ATOM   2623 H H    . THR A 1 167 ? 24.450 40.570 55.452 0.00 42.74  ? 170 THR A H    1 
ATOM   2624 H HA   . THR A 1 167 ? 25.290 39.945 53.044 0.00 37.83  ? 170 THR A HA   1 
ATOM   2625 H HB   . THR A 1 167 ? 22.930 39.062 54.330 0.00 42.74  ? 170 THR A HB   1 
ATOM   2626 H HG1  . THR A 1 167 ? 24.140 37.444 55.038 0.00 44.11  ? 170 THR A HG1  1 
ATOM   2627 H HG21 . THR A 1 167 ? 23.107 37.204 52.796 0.00 41.58  ? 170 THR A HG21 1 
ATOM   2628 H HG22 . THR A 1 167 ? 22.656 38.559 52.121 0.00 41.58  ? 170 THR A HG22 1 
ATOM   2629 H HG23 . THR A 1 167 ? 24.150 38.068 51.985 0.00 41.58  ? 170 THR A HG23 1 
ATOM   2630 N N    . PHE A 1 168 ? 22.652 41.760 53.161 1.00 29.24  ? 171 PHE A N    1 
ATOM   2631 C CA   . PHE A 1 168 ? 21.806 42.620 52.341 1.00 39.32  ? 171 PHE A CA   1 
ATOM   2632 C C    . PHE A 1 168 ? 22.633 43.684 51.631 1.00 30.28  ? 171 PHE A C    1 
ATOM   2633 O O    . PHE A 1 168 ? 22.489 43.896 50.422 1.00 34.29  ? 171 PHE A O    1 
ATOM   2634 C CB   . PHE A 1 168 ? 20.726 43.275 53.200 1.00 25.33  ? 171 PHE A CB   1 
ATOM   2635 C CG   . PHE A 1 168 ? 20.017 44.399 52.507 1.00 38.47  ? 171 PHE A CG   1 
ATOM   2636 C CD1  . PHE A 1 168 ? 19.052 44.138 51.549 1.00 28.49  ? 171 PHE A CD1  1 
ATOM   2637 C CD2  . PHE A 1 168 ? 20.332 45.717 52.793 1.00 36.84  ? 171 PHE A CD2  1 
ATOM   2638 C CE1  . PHE A 1 168 ? 18.404 45.170 50.901 1.00 43.27  ? 171 PHE A CE1  1 
ATOM   2639 C CE2  . PHE A 1 168 ? 19.687 46.753 52.148 1.00 38.98  ? 171 PHE A CE2  1 
ATOM   2640 C CZ   . PHE A 1 168 ? 18.725 46.478 51.199 1.00 36.68  ? 171 PHE A CZ   1 
ATOM   2641 H H    . PHE A 1 168 ? 22.475 41.776 54.002 0.00 35.11  ? 171 PHE A H    1 
ATOM   2642 H HA   . PHE A 1 168 ? 21.369 42.072 51.671 0.00 47.19  ? 171 PHE A HA   1 
ATOM   2643 H HB2  . PHE A 1 168 ? 20.065 42.606 53.437 0.00 30.41  ? 171 PHE A HB2  1 
ATOM   2644 H HB3  . PHE A 1 168 ? 21.138 43.633 54.002 0.00 30.41  ? 171 PHE A HB3  1 
ATOM   2645 H HD1  . PHE A 1 168 ? 18.839 43.257 51.339 0.00 34.21  ? 171 PHE A HD1  1 
ATOM   2646 H HD2  . PHE A 1 168 ? 20.984 45.906 53.428 0.00 44.22  ? 171 PHE A HD2  1 
ATOM   2647 H HE1  . PHE A 1 168 ? 17.752 44.984 50.265 0.00 51.93  ? 171 PHE A HE1  1 
ATOM   2648 H HE2  . PHE A 1 168 ? 19.901 47.634 52.352 0.00 46.79  ? 171 PHE A HE2  1 
ATOM   2649 H HZ   . PHE A 1 168 ? 18.293 47.175 50.760 0.00 44.03  ? 171 PHE A HZ   1 
ATOM   2650 N N    . LYS A 1 169 ? 23.506 44.371 52.372 1.00 28.13  ? 172 LYS A N    1 
ATOM   2651 C CA   . LYS A 1 169 ? 24.300 45.439 51.773 1.00 37.40  ? 172 LYS A CA   1 
ATOM   2652 C C    . LYS A 1 169 ? 25.140 44.918 50.613 1.00 38.57  ? 172 LYS A C    1 
ATOM   2653 O O    . LYS A 1 169 ? 25.341 45.622 49.617 1.00 41.56  ? 172 LYS A O    1 
ATOM   2654 C CB   . LYS A 1 169 ? 25.190 46.083 52.836 1.00 40.32  ? 172 LYS A CB   1 
ATOM   2655 C CG   . LYS A 1 169 ? 24.505 47.189 53.626 1.00 54.16  ? 172 LYS A CG   1 
ATOM   2656 C CD   . LYS A 1 169 ? 25.516 48.081 54.327 1.00 71.36  ? 172 LYS A CD   1 
ATOM   2657 C CE   . LYS A 1 169 ? 24.826 49.168 55.137 1.00 90.65  ? 172 LYS A CE   1 
ATOM   2658 N NZ   . LYS A 1 169 ? 25.155 50.533 54.638 1.00 86.53  ? 172 LYS A NZ   1 
ATOM   2659 H H    . LYS A 1 169 ? 23.653 44.240 53.209 0.00 33.78  ? 172 LYS A H    1 
ATOM   2660 H HA   . LYS A 1 169 ? 23.702 46.120 51.427 0.00 44.90  ? 172 LYS A HA   1 
ATOM   2661 N N    . VAL A 1 170 ? 25.636 43.685 50.722 1.00 34.64  ? 173 VAL A N    1 
ATOM   2662 C CA   . VAL A 1 170 ? 26.421 43.102 49.638 1.00 37.65  ? 173 VAL A CA   1 
ATOM   2663 C C    . VAL A 1 170 ? 25.527 42.796 48.442 1.00 32.28  ? 173 VAL A C    1 
ATOM   2664 O O    . VAL A 1 170 ? 25.862 43.120 47.297 1.00 28.65  ? 173 VAL A O    1 
ATOM   2665 C CB   . VAL A 1 170 ? 27.157 41.843 50.133 1.00 39.88  ? 173 VAL A CB   1 
ATOM   2666 C CG1  . VAL A 1 170 ? 27.666 41.013 48.958 1.00 33.78  ? 173 VAL A CG1  1 
ATOM   2667 C CG2  . VAL A 1 170 ? 28.304 42.230 51.054 1.00 43.26  ? 173 VAL A CG2  1 
ATOM   2668 H H    . VAL A 1 170 ? 25.533 43.172 51.404 0.00 41.58  ? 173 VAL A H    1 
ATOM   2669 H HA   . VAL A 1 170 ? 27.088 43.747 49.355 0.00 45.19  ? 173 VAL A HA   1 
ATOM   2670 H HB   . VAL A 1 170 ? 26.534 41.294 50.634 0.00 47.87  ? 173 VAL A HB   1 
ATOM   2671 H HG11 . VAL A 1 170 ? 28.245 40.311 49.294 0.00 40.55  ? 173 VAL A HG11 1 
ATOM   2672 H HG12 . VAL A 1 170 ? 26.909 40.624 48.494 0.00 40.55  ? 173 VAL A HG12 1 
ATOM   2673 H HG13 . VAL A 1 170 ? 28.162 41.590 48.355 0.00 40.55  ? 173 VAL A HG13 1 
ATOM   2674 H HG21 . VAL A 1 170 ? 28.753 41.424 51.355 0.00 51.93  ? 173 VAL A HG21 1 
ATOM   2675 H HG22 . VAL A 1 170 ? 28.926 42.792 50.565 0.00 51.93  ? 173 VAL A HG22 1 
ATOM   2676 H HG23 . VAL A 1 170 ? 27.948 42.714 51.815 0.00 51.93  ? 173 VAL A HG23 1 
ATOM   2677 N N    . LEU A 1 171 ? 24.376 42.165 48.691 1.00 26.82  ? 174 LEU A N    1 
ATOM   2678 C CA   . LEU A 1 171 ? 23.465 41.831 47.600 1.00 25.83  ? 174 LEU A CA   1 
ATOM   2679 C C    . LEU A 1 171 ? 22.836 43.078 46.993 1.00 27.55  ? 174 LEU A C    1 
ATOM   2680 O O    . LEU A 1 171 ? 22.532 43.097 45.794 1.00 22.89  ? 174 LEU A O    1 
ATOM   2681 C CB   . LEU A 1 171 ? 22.377 40.879 48.097 1.00 22.98  ? 174 LEU A CB   1 
ATOM   2682 C CG   . LEU A 1 171 ? 22.843 39.489 48.538 1.00 20.95  ? 174 LEU A CG   1 
ATOM   2683 C CD1  . LEU A 1 171 ? 21.672 38.684 49.082 1.00 35.24  ? 174 LEU A CD1  1 
ATOM   2684 C CD2  . LEU A 1 171 ? 23.517 38.746 47.394 1.00 28.92  ? 174 LEU A CD2  1 
ATOM   2685 H H    . LEU A 1 171 ? 24.104 41.924 49.470 0.00 32.20  ? 174 LEU A H    1 
ATOM   2686 H HA   . LEU A 1 171 ? 23.967 41.378 46.904 0.00 31.01  ? 174 LEU A HA   1 
ATOM   2687 H HB2  . LEU A 1 171 ? 21.942 41.290 48.860 0.00 27.59  ? 174 LEU A HB2  1 
ATOM   2688 H HB3  . LEU A 1 171 ? 21.737 40.752 47.379 0.00 27.59  ? 174 LEU A HB3  1 
ATOM   2689 H HG   . LEU A 1 171 ? 23.498 39.592 49.246 0.00 25.16  ? 174 LEU A HG   1 
ATOM   2690 H HD11 . LEU A 1 171 ? 21.987 37.802 49.336 0.00 42.30  ? 174 LEU A HD11 1 
ATOM   2691 H HD12 . LEU A 1 171 ? 21.307 39.141 49.855 0.00 42.30  ? 174 LEU A HD12 1 
ATOM   2692 H HD13 . LEU A 1 171 ? 20.994 38.607 48.392 0.00 42.30  ? 174 LEU A HD13 1 
ATOM   2693 H HD21 . LEU A 1 171 ? 23.671 37.827 47.662 0.00 34.72  ? 174 LEU A HD21 1 
ATOM   2694 H HD22 . LEU A 1 171 ? 22.939 38.772 46.616 0.00 34.72  ? 174 LEU A HD22 1 
ATOM   2695 H HD23 . LEU A 1 171 ? 24.362 39.178 47.192 0.00 34.72  ? 174 LEU A HD23 1 
ATOM   2696 N N    . ARG A 1 172 ? 22.624 44.119 47.800 1.00 22.29  ? 175 ARG A N    1 
ATOM   2697 C CA   . ARG A 1 172 ? 22.095 45.371 47.268 1.00 29.91  ? 175 ARG A CA   1 
ATOM   2698 C C    . ARG A 1 172 ? 23.105 46.038 46.343 1.00 26.11  ? 175 ARG A C    1 
ATOM   2699 O O    . ARG A 1 172 ? 22.733 46.586 45.299 1.00 31.55  ? 175 ARG A O    1 
ATOM   2700 C CB   . ARG A 1 172 ? 21.710 46.301 48.422 1.00 30.22  ? 175 ARG A CB   1 
ATOM   2701 C CG   . ARG A 1 172 ? 21.247 47.699 48.009 1.00 40.04  ? 175 ARG A CG   1 
ATOM   2702 C CD   . ARG A 1 172 ? 21.571 48.725 49.087 1.00 41.77  ? 175 ARG A CD   1 
ATOM   2703 N NE   . ARG A 1 172 ? 23.008 48.880 49.280 1.00 51.27  ? 175 ARG A NE   1 
ATOM   2704 C CZ   . ARG A 1 172 ? 23.565 49.541 50.286 1.00 52.47  ? 175 ARG A CZ   1 
ATOM   2705 N NH1  . ARG A 1 172 ? 22.832 50.133 51.215 1.00 49.74  ? 175 ARG A NH1  1 
ATOM   2706 N NH2  . ARG A 1 172 ? 24.891 49.609 50.362 1.00 52.06  ? 175 ARG A NH2  1 
ATOM   2707 H H    . ARG A 1 172 ? 22.776 44.126 48.647 1.00 26.76  ? 175 ARG A H    1 
ATOM   2708 H HA   . ARG A 1 172 ? 21.294 45.189 46.752 1.00 35.91  ? 175 ARG A HA   1 
ATOM   2709 H HB2  . ARG A 1 172 ? 20.984 45.890 48.916 1.00 36.28  ? 175 ARG A HB2  1 
ATOM   2710 H HB3  . ARG A 1 172 ? 22.483 46.410 48.997 1.00 36.28  ? 175 ARG A HB3  1 
ATOM   2711 H HG2  . ARG A 1 172 ? 21.698 47.960 47.191 1.00 48.06  ? 175 ARG A HG2  1 
ATOM   2712 H HG3  . ARG A 1 172 ? 20.286 47.693 47.871 1.00 48.06  ? 175 ARG A HG3  1 
ATOM   2713 H HD2  . ARG A 1 172 ? 21.206 49.586 48.828 1.00 50.13  ? 175 ARG A HD2  1 
ATOM   2714 H HD3  . ARG A 1 172 ? 21.182 48.439 49.928 1.00 50.13  ? 175 ARG A HD3  1 
ATOM   2715 H HE   . ARG A 1 172 ? 23.531 48.517 48.702 1.00 61.54  ? 175 ARG A HE   1 
ATOM   2716 H HH11 . ARG A 1 172 ? 21.974 50.095 51.175 1.00 59.71  ? 175 ARG A HH11 1 
ATOM   2717 H HH12 . ARG A 1 172 ? 23.214 50.557 51.858 1.00 59.71  ? 175 ARG A HH12 1 
ATOM   2718 H HH21 . ARG A 1 172 ? 25.376 49.228 49.764 1.00 62.49  ? 175 ARG A HH21 1 
ATOM   2719 H HH22 . ARG A 1 172 ? 25.263 50.035 51.010 1.00 62.49  ? 175 ARG A HH22 1 
ATOM   2720 N N    . ASN A 1 173 ? 24.388 46.006 46.711 1.00 29.55  ? 176 ASN A N    1 
ATOM   2721 C CA   . ASN A 1 173 ? 25.418 46.585 45.855 1.00 27.02  ? 176 ASN A CA   1 
ATOM   2722 C C    . ASN A 1 173 ? 25.535 45.809 44.549 1.00 19.49  ? 176 ASN A C    1 
ATOM   2723 O O    . ASN A 1 173 ? 25.604 46.401 43.466 1.00 25.07  ? 176 ASN A O    1 
ATOM   2724 C CB   . ASN A 1 173 ? 26.758 46.606 46.592 1.00 31.54  ? 176 ASN A CB   1 
ATOM   2725 C CG   . ASN A 1 173 ? 26.763 47.562 47.771 1.00 46.37  ? 176 ASN A CG   1 
ATOM   2726 O OD1  . ASN A 1 173 ? 25.828 48.341 47.960 1.00 30.64  ? 176 ASN A OD1  1 
ATOM   2727 N ND2  . ASN A 1 173 ? 27.818 47.503 48.575 1.00 39.87  ? 176 ASN A ND2  1 
ATOM   2728 H H    . ASN A 1 173 ? 24.682 45.658 47.440 0.00 35.48  ? 176 ASN A H    1 
ATOM   2729 H HA   . ASN A 1 173 ? 25.176 47.500 45.644 0.00 32.44  ? 176 ASN A HA   1 
ATOM   2730 H HB2  . ASN A 1 173 ? 26.949 45.716 46.926 0.00 37.87  ? 176 ASN A HB2  1 
ATOM   2731 H HB3  . ASN A 1 173 ? 27.453 46.885 45.975 0.00 37.87  ? 176 ASN A HB3  1 
ATOM   2732 H HD21 . ASN A 1 173 ? 27.869 48.024 49.257 0.00 47.85  ? 176 ASN A HD21 1 
ATOM   2733 H HD22 . ASN A 1 173 ? 28.451 46.943 48.413 0.00 47.85  ? 176 ASN A HD22 1 
ATOM   2734 N N    . VAL A 1 174 ? 25.562 44.477 44.636 1.00 20.12  ? 177 VAL A N    1 
ATOM   2735 C CA   . VAL A 1 174 ? 25.609 43.647 43.436 1.00 21.29  ? 177 VAL A CA   1 
ATOM   2736 C C    . VAL A 1 174 ? 24.416 43.952 42.539 1.00 21.95  ? 177 VAL A C    1 
ATOM   2737 O O    . VAL A 1 174 ? 24.553 44.109 41.320 1.00 23.04  ? 177 VAL A O    1 
ATOM   2738 C CB   . VAL A 1 174 ? 25.654 42.157 43.822 1.00 23.56  ? 177 VAL A CB   1 
ATOM   2739 C CG1  . VAL A 1 174 ? 25.267 41.280 42.638 1.00 28.63  ? 177 VAL A CG1  1 
ATOM   2740 C CG2  . VAL A 1 174 ? 27.033 41.783 44.344 1.00 35.10  ? 177 VAL A CG2  1 
ATOM   2741 H H    . VAL A 1 174 ? 25.555 44.035 45.374 0.00 24.15  ? 177 VAL A H    1 
ATOM   2742 H HA   . VAL A 1 174 ? 26.417 43.857 42.943 0.00 25.57  ? 177 VAL A HA   1 
ATOM   2743 H HB   . VAL A 1 174 ? 25.011 41.999 44.531 0.00 28.29  ? 177 VAL A HB   1 
ATOM   2744 H HG11 . VAL A 1 174 ? 25.555 40.370 42.811 0.00 34.37  ? 177 VAL A HG11 1 
ATOM   2745 H HG12 . VAL A 1 174 ? 24.303 41.306 42.527 0.00 34.37  ? 177 VAL A HG12 1 
ATOM   2746 H HG13 . VAL A 1 174 ? 25.701 41.618 41.839 0.00 34.37  ? 177 VAL A HG13 1 
ATOM   2747 H HG21 . VAL A 1 174 ? 27.035 40.844 44.589 0.00 42.13  ? 177 VAL A HG21 1 
ATOM   2748 H HG22 . VAL A 1 174 ? 27.689 41.945 43.648 0.00 42.13  ? 177 VAL A HG22 1 
ATOM   2749 H HG23 . VAL A 1 174 ? 27.235 42.327 45.122 0.00 42.13  ? 177 VAL A HG23 1 
ATOM   2750 N N    . THR A 1 175 ? 23.226 44.042 43.135 1.00 26.54  ? 178 THR A N    1 
ATOM   2751 C CA   . THR A 1 175 ? 22.014 44.271 42.354 1.00 20.25  ? 178 THR A CA   1 
ATOM   2752 C C    . THR A 1 175 ? 22.083 45.597 41.605 1.00 14.87  ? 178 THR A C    1 
ATOM   2753 O O    . THR A 1 175 ? 21.767 45.669 40.412 1.00 22.98  ? 178 THR A O    1 
ATOM   2754 C CB   . THR A 1 175 ? 20.794 44.237 43.279 1.00 32.46  ? 178 THR A CB   1 
ATOM   2755 O OG1  . THR A 1 175 ? 20.620 42.912 43.799 1.00 19.06  ? 178 THR A OG1  1 
ATOM   2756 C CG2  . THR A 1 175 ? 19.533 44.661 42.538 1.00 24.31  ? 178 THR A CG2  1 
ATOM   2757 H H    . THR A 1 175 ? 23.095 43.974 43.982 0.00 31.86  ? 178 THR A H    1 
ATOM   2758 H HA   . THR A 1 175 ? 21.921 43.563 41.698 0.00 24.31  ? 178 THR A HA   1 
ATOM   2759 H HB   . THR A 1 175 ? 20.932 44.858 44.012 0.00 38.97  ? 178 THR A HB   1 
ATOM   2760 H HG1  . THR A 1 175 ? 21.312 42.673 44.212 0.00 22.88  ? 178 THR A HG1  1 
ATOM   2761 H HG21 . THR A 1 175 ? 18.749 44.439 43.064 0.00 29.18  ? 178 THR A HG21 1 
ATOM   2762 H HG22 . THR A 1 175 ? 19.546 45.619 42.382 0.00 29.18  ? 178 THR A HG22 1 
ATOM   2763 H HG23 . THR A 1 175 ? 19.480 44.204 41.684 0.00 29.18  ? 178 THR A HG23 1 
ATOM   2764 N N    . VAL A 1 176 ? 22.500 46.661 42.292 1.00 16.73  ? 179 VAL A N    1 
ATOM   2765 C CA   . VAL A 1 176 ? 22.487 47.990 41.688 1.00 16.91  ? 179 VAL A CA   1 
ATOM   2766 C C    . VAL A 1 176 ? 23.421 48.041 40.486 1.00 26.98  ? 179 VAL A C    1 
ATOM   2767 O O    . VAL A 1 176 ? 23.079 48.604 39.438 1.00 21.06  ? 179 VAL A O    1 
ATOM   2768 C CB   . VAL A 1 176 ? 22.857 49.050 42.740 1.00 33.58  ? 179 VAL A CB   1 
ATOM   2769 C CG1  . VAL A 1 176 ? 23.088 50.400 42.079 1.00 48.20  ? 179 VAL A CG1  1 
ATOM   2770 C CG2  . VAL A 1 176 ? 21.769 49.142 43.795 1.00 30.17  ? 179 VAL A CG2  1 
ATOM   2771 H H    . VAL A 1 176 ? 22.792 46.640 43.101 0.00 20.09  ? 179 VAL A H    1 
ATOM   2772 H HA   . VAL A 1 176 ? 21.589 48.177 41.370 0.00 20.31  ? 179 VAL A HA   1 
ATOM   2773 H HB   . VAL A 1 176 ? 23.682 48.789 43.178 0.00 40.31  ? 179 VAL A HB   1 
ATOM   2774 H HG11 . VAL A 1 176 ? 23.055 51.093 42.757 0.00 57.86  ? 179 VAL A HG11 1 
ATOM   2775 H HG12 . VAL A 1 176 ? 23.959 50.397 41.651 0.00 57.86  ? 179 VAL A HG12 1 
ATOM   2776 H HG13 . VAL A 1 176 ? 22.395 50.550 41.418 0.00 57.86  ? 179 VAL A HG13 1 
ATOM   2777 H HG21 . VAL A 1 176 ? 22.174 49.362 44.649 0.00 36.22  ? 179 VAL A HG21 1 
ATOM   2778 H HG22 . VAL A 1 176 ? 21.139 49.833 43.540 0.00 36.22  ? 179 VAL A HG22 1 
ATOM   2779 H HG23 . VAL A 1 176 ? 21.315 48.286 43.856 0.00 36.22  ? 179 VAL A HG23 1 
ATOM   2780 N N    . VAL A 1 177 ? 24.612 47.457 40.614 1.00 25.01  ? 180 VAL A N    1 
ATOM   2781 C CA   . VAL A 1 177 ? 25.578 47.491 39.520 1.00 16.99  ? 180 VAL A CA   1 
ATOM   2782 C C    . VAL A 1 177 ? 25.067 46.682 38.334 1.00 21.07  ? 180 VAL A C    1 
ATOM   2783 O O    . VAL A 1 177 ? 25.051 47.163 37.195 1.00 31.56  ? 180 VAL A O    1 
ATOM   2784 C CB   . VAL A 1 177 ? 26.947 46.981 40.005 1.00 23.64  ? 180 VAL A CB   1 
ATOM   2785 C CG1  . VAL A 1 177 ? 27.901 46.805 38.829 1.00 22.40  ? 180 VAL A CG1  1 
ATOM   2786 C CG2  . VAL A 1 177 ? 27.533 47.938 41.035 1.00 22.88  ? 180 VAL A CG2  1 
ATOM   2787 H H    . VAL A 1 177 ? 24.882 47.040 41.316 0.00 30.02  ? 180 VAL A H    1 
ATOM   2788 H HA   . VAL A 1 177 ? 25.683 48.410 39.229 0.00 20.31  ? 180 VAL A HA   1 
ATOM   2789 H HB   . VAL A 1 177 ? 26.829 46.115 40.426 0.00 28.38  ? 180 VAL A HB   1 
ATOM   2790 H HG11 . VAL A 1 177 ? 28.808 46.737 39.166 0.00 26.89  ? 180 VAL A HG11 1 
ATOM   2791 H HG12 . VAL A 1 177 ? 27.664 45.996 38.349 0.00 26.89  ? 180 VAL A HG12 1 
ATOM   2792 H HG13 . VAL A 1 177 ? 27.823 47.573 38.242 0.00 26.89  ? 180 VAL A HG13 1 
ATOM   2793 H HG21 . VAL A 1 177 ? 28.401 47.607 41.315 0.00 27.47  ? 180 VAL A HG21 1 
ATOM   2794 H HG22 . VAL A 1 177 ? 27.628 48.815 40.633 0.00 27.47  ? 180 VAL A HG22 1 
ATOM   2795 H HG23 . VAL A 1 177 ? 26.935 47.986 41.797 0.00 27.47  ? 180 VAL A HG23 1 
ATOM   2796 N N    . LEU A 1 178 ? 24.633 45.445 38.583 1.00 16.37  ? 181 LEU A N    1 
ATOM   2797 C CA   . LEU A 1 178 ? 24.276 44.555 37.482 1.00 15.79  ? 181 LEU A CA   1 
ATOM   2798 C C    . LEU A 1 178 ? 23.003 45.012 36.777 1.00 19.40  ? 181 LEU A C    1 
ATOM   2799 O O    . LEU A 1 178 ? 22.933 44.993 35.542 1.00 14.61  ? 181 LEU A O    1 
ATOM   2800 C CB   . LEU A 1 178 ? 24.118 43.124 38.000 1.00 14.10  ? 181 LEU A CB   1 
ATOM   2801 C CG   . LEU A 1 178 ? 25.405 42.427 38.453 1.00 34.53  ? 181 LEU A CG   1 
ATOM   2802 C CD1  . LEU A 1 178 ? 25.120 40.982 38.831 1.00 20.82  ? 181 LEU A CD1  1 
ATOM   2803 C CD2  . LEU A 1 178 ? 26.484 42.497 37.379 1.00 24.73  ? 181 LEU A CD2  1 
ATOM   2804 H H    . LEU A 1 178 ? 24.539 45.103 39.366 0.00 19.65  ? 181 LEU A H    1 
ATOM   2805 H HA   . LEU A 1 178 ? 24.994 44.566 36.830 0.00 18.96  ? 181 LEU A HA   1 
ATOM   2806 H HB2  . LEU A 1 178 ? 23.519 43.144 38.762 0.00 16.84  ? 181 LEU A HB2  1 
ATOM   2807 H HB3  . LEU A 1 178 ? 23.735 42.586 37.290 0.00 16.84  ? 181 LEU A HB3  1 
ATOM   2808 H HG   . LEU A 1 178 ? 25.744 42.888 39.236 0.00 41.45  ? 181 LEU A HG   1 
ATOM   2809 H HD11 . LEU A 1 178 ? 25.946 40.562 39.118 0.00 25.00  ? 181 LEU A HD11 1 
ATOM   2810 H HD12 . LEU A 1 178 ? 24.473 40.966 39.552 0.00 25.00  ? 181 LEU A HD12 1 
ATOM   2811 H HD13 . LEU A 1 178 ? 24.765 40.517 38.057 0.00 25.00  ? 181 LEU A HD13 1 
ATOM   2812 H HD21 . LEU A 1 178 ? 27.187 41.865 37.596 0.00 29.70  ? 181 LEU A HD21 1 
ATOM   2813 H HD22 . LEU A 1 178 ? 26.091 42.272 36.521 0.00 29.70  ? 181 LEU A HD22 1 
ATOM   2814 H HD23 . LEU A 1 178 ? 26.845 43.397 37.352 0.00 29.70  ? 181 LEU A HD23 1 
ATOM   2815 N N    . TRP A 1 179 ? 21.983 45.421 37.536 1.00 15.57  ? 182 TRP A N    1 
ATOM   2816 C CA   . TRP A 1 179 ? 20.722 45.820 36.914 1.00 23.04  ? 182 TRP A CA   1 
ATOM   2817 C C    . TRP A 1 179 ? 20.892 47.069 36.056 1.00 19.64  ? 182 TRP A C    1 
ATOM   2818 O O    . TRP A 1 179 ? 20.251 47.198 35.007 1.00 21.44  ? 182 TRP A O    1 
ATOM   2819 C CB   . TRP A 1 179 ? 19.654 46.062 37.981 1.00 16.45  ? 182 TRP A CB   1 
ATOM   2820 C CG   . TRP A 1 179 ? 19.150 44.819 38.646 1.00 21.46  ? 182 TRP A CG   1 
ATOM   2821 C CD1  . TRP A 1 179 ? 19.888 43.744 39.047 1.00 26.78  ? 182 TRP A CD1  1 
ATOM   2822 C CD2  . TRP A 1 179 ? 17.791 44.525 38.993 1.00 19.68  ? 182 TRP A CD2  1 
ATOM   2823 N NE1  . TRP A 1 179 ? 19.074 42.799 39.623 1.00 32.75  ? 182 TRP A NE1  1 
ATOM   2824 C CE2  . TRP A 1 179 ? 17.781 43.254 39.603 1.00 21.35  ? 182 TRP A CE2  1 
ATOM   2825 C CE3  . TRP A 1 179 ? 16.582 45.213 38.848 1.00 21.90  ? 182 TRP A CE3  1 
ATOM   2826 C CZ2  . TRP A 1 179 ? 16.609 42.656 40.064 1.00 21.82  ? 182 TRP A CZ2  1 
ATOM   2827 C CZ3  . TRP A 1 179 ? 15.419 44.618 39.308 1.00 23.56  ? 182 TRP A CZ3  1 
ATOM   2828 C CH2  . TRP A 1 179 ? 15.442 43.352 39.908 1.00 16.54  ? 182 TRP A CH2  1 
ATOM   2829 H H    . TRP A 1 179 ? 21.995 45.475 38.394 0.00 18.70  ? 182 TRP A H    1 
ATOM   2830 H HA   . TRP A 1 179 ? 20.424 45.094 36.343 0.00 27.67  ? 182 TRP A HA   1 
ATOM   2831 H HB2  . TRP A 1 179 ? 20.030 46.632 38.671 0.00 19.75  ? 182 TRP A HB2  1 
ATOM   2832 H HB3  . TRP A 1 179 ? 18.895 46.501 37.565 0.00 19.75  ? 182 TRP A HB3  1 
ATOM   2833 H HD1  . TRP A 1 179 ? 20.809 43.663 38.945 0.00 32.15  ? 182 TRP A HD1  1 
ATOM   2834 H HE1  . TRP A 1 179 ? 19.333 42.044 39.944 0.00 39.32  ? 182 TRP A HE1  1 
ATOM   2835 H HE3  . TRP A 1 179 ? 16.559 46.054 38.451 0.00 26.29  ? 182 TRP A HE3  1 
ATOM   2836 H HZ2  . TRP A 1 179 ? 16.620 41.815 40.462 0.00 26.20  ? 182 TRP A HZ2  1 
ATOM   2837 H HZ3  . TRP A 1 179 ? 14.610 45.066 39.217 0.00 28.28  ? 182 TRP A HZ3  1 
ATOM   2838 H HH2  . TRP A 1 179 ? 14.645 42.977 40.207 0.00 19.87  ? 182 TRP A HH2  1 
ATOM   2839 N N    A SER A 1 180 ? 21.746 48.001 36.486 0.56 20.08  ? 183 SER A N    1 
ATOM   2840 N N    B SER A 1 180 ? 21.748 48.000 36.487 0.44 20.08  ? 183 SER A N    1 
ATOM   2841 C CA   A SER A 1 180 ? 21.920 49.249 35.750 0.56 17.72  ? 183 SER A CA   1 
ATOM   2842 C CA   B SER A 1 180 ? 21.930 49.249 35.756 0.44 17.26  ? 183 SER A CA   1 
ATOM   2843 C C    A SER A 1 180 ? 22.557 49.036 34.383 0.56 23.04  ? 183 SER A C    1 
ATOM   2844 C C    B SER A 1 180 ? 22.556 49.035 34.384 0.44 22.97  ? 183 SER A C    1 
ATOM   2845 O O    A SER A 1 180 ? 22.439 49.911 33.518 0.56 20.26  ? 183 SER A O    1 
ATOM   2846 O O    B SER A 1 180 ? 22.427 49.906 33.517 0.44 20.25  ? 183 SER A O    1 
ATOM   2847 C CB   A SER A 1 180 ? 22.769 50.227 36.564 0.56 22.59  ? 183 SER A CB   1 
ATOM   2848 C CB   B SER A 1 180 ? 22.795 50.213 36.569 0.44 22.63  ? 183 SER A CB   1 
ATOM   2849 O OG   A SER A 1 180 ? 22.109 50.600 37.761 0.56 26.44  ? 183 SER A OG   1 
ATOM   2850 O OG   B SER A 1 180 ? 24.103 49.699 36.754 0.44 30.69  ? 183 SER A OG   1 
ATOM   2851 H H    A SER A 1 180 ? 22.231 47.934 37.193 0.56 24.11  ? 183 SER A H    1 
ATOM   2852 H H    B SER A 1 180 ? 22.230 47.931 37.196 0.44 24.11  ? 183 SER A H    1 
ATOM   2853 H HA   A SER A 1 180 ? 21.046 49.647 35.614 0.56 21.28  ? 183 SER A HA   1 
ATOM   2854 H HA   B SER A 1 180 ? 21.060 49.658 35.627 0.44 20.73  ? 183 SER A HA   1 
ATOM   2855 H HB2  A SER A 1 180 ? 23.611 49.801 36.789 0.56 27.12  ? 183 SER A HB2  1 
ATOM   2856 H HB2  B SER A 1 180 ? 22.854 51.058 36.096 0.44 27.17  ? 183 SER A HB2  1 
ATOM   2857 H HB3  A SER A 1 180 ? 22.930 51.022 36.032 0.56 27.12  ? 183 SER A HB3  1 
ATOM   2858 H HB3  B SER A 1 180 ? 22.385 50.347 37.438 0.44 27.17  ? 183 SER A HB3  1 
ATOM   2859 H HG   A SER A 1 180 ? 21.963 49.921 38.233 0.56 31.75  ? 183 SER A HG   1 
ATOM   2860 H HG   B SER A 1 180 ? 24.492 49.629 36.012 0.44 36.85  ? 183 SER A HG   1 
ATOM   2861 N N    . ALA A 1 181 ? 23.231 47.905 34.167 1.00 14.82  ? 184 ALA A N    1 
ATOM   2862 C CA   . ALA A 1 181 ? 23.845 47.635 32.873 1.00 21.94  ? 184 ALA A CA   1 
ATOM   2863 C C    . ALA A 1 181 ? 22.834 47.206 31.815 1.00 14.36  ? 184 ALA A C    1 
ATOM   2864 O O    . ALA A 1 181 ? 23.092 47.391 30.621 1.00 20.08  ? 184 ALA A O    1 
ATOM   2865 C CB   . ALA A 1 181 ? 24.919 46.555 33.018 1.00 18.82  ? 184 ALA A CB   1 
ATOM   2866 H H    . ALA A 1 181 ? 23.344 47.285 34.752 0.00 17.71  ? 184 ALA A H    1 
ATOM   2867 H HA   . ALA A 1 181 ? 24.273 48.447 32.561 0.00 26.34  ? 184 ALA A HA   1 
ATOM   2868 H HB1  . ALA A 1 181 ? 25.318 46.388 32.149 0.00 22.60  ? 184 ALA A HB1  1 
ATOM   2869 H HB2  . ALA A 1 181 ? 25.597 46.866 33.638 0.00 22.60  ? 184 ALA A HB2  1 
ATOM   2870 H HB3  . ALA A 1 181 ? 24.508 45.744 33.355 0.00 22.60  ? 184 ALA A HB3  1 
ATOM   2871 N N    . TYR A 1 182 ? 21.694 46.644 32.219 1.00 13.40  ? 185 TYR A N    1 
ATOM   2872 C CA   . TYR A 1 182 ? 20.724 46.146 31.244 1.00 15.69  ? 185 TYR A CA   1 
ATOM   2873 C C    . TYR A 1 182 ? 20.190 47.242 30.333 1.00 18.20  ? 185 TYR A C    1 
ATOM   2874 O O    . TYR A 1 182 ? 20.235 47.068 29.102 1.00 15.22  ? 185 TYR A O    1 
ATOM   2875 C CB   . TYR A 1 182 ? 19.582 45.440 31.979 1.00 16.68  ? 185 TYR A CB   1 
ATOM   2876 C CG   . TYR A 1 182 ? 19.913 44.024 32.396 1.00 13.67  ? 185 TYR A CG   1 
ATOM   2877 C CD1  . TYR A 1 182 ? 20.688 43.775 33.520 1.00 16.55  ? 185 TYR A CD1  1 
ATOM   2878 C CD2  . TYR A 1 182 ? 19.449 42.937 31.666 1.00 13.10  ? 185 TYR A CD2  1 
ATOM   2879 C CE1  . TYR A 1 182 ? 20.995 42.482 33.906 1.00 23.63  ? 185 TYR A CE1  1 
ATOM   2880 C CE2  . TYR A 1 182 ? 19.748 41.639 32.045 1.00 11.47  ? 185 TYR A CE2  1 
ATOM   2881 C CZ   . TYR A 1 182 ? 20.522 41.418 33.166 1.00 23.32  ? 185 TYR A CZ   1 
ATOM   2882 O OH   . TYR A 1 182 ? 20.824 40.131 33.550 1.00 23.02  ? 185 TYR A OH   1 
ATOM   2883 H H    . TYR A 1 182 ? 21.461 46.540 33.040 0.00 16.01  ? 185 TYR A H    1 
ATOM   2884 H HA   . TYR A 1 182 ? 21.180 45.498 30.684 0.00 18.85  ? 185 TYR A HA   1 
ATOM   2885 H HB2  . TYR A 1 182 ? 19.369 45.942 32.781 0.00 20.03  ? 185 TYR A HB2  1 
ATOM   2886 H HB3  . TYR A 1 182 ? 18.809 45.403 31.394 0.00 20.03  ? 185 TYR A HB3  1 
ATOM   2887 H HD1  . TYR A 1 182 ? 21.008 44.490 34.023 0.00 19.87  ? 185 TYR A HD1  1 
ATOM   2888 H HD2  . TYR A 1 182 ? 18.929 43.084 30.909 0.00 15.73  ? 185 TYR A HD2  1 
ATOM   2889 H HE1  . TYR A 1 182 ? 21.517 42.331 34.661 0.00 28.38  ? 185 TYR A HE1  1 
ATOM   2890 H HE2  . TYR A 1 182 ? 19.429 40.921 31.547 0.00 13.78  ? 185 TYR A HE2  1 
ATOM   2891 H HH   . TYR A 1 182 ? 20.471 39.583 33.019 0.00 27.64  ? 185 TYR A HH   1 
ATOM   2892 N N    . PRO A 1 183 ? 19.665 48.362 30.837 1.00 13.81  ? 186 PRO A N    1 
ATOM   2893 C CA   . PRO A 1 183 ? 19.171 49.401 29.918 1.00 13.75  ? 186 PRO A CA   1 
ATOM   2894 C C    . PRO A 1 183 ? 20.244 49.939 28.991 1.00 15.97  ? 186 PRO A C    1 
ATOM   2895 O O    . PRO A 1 183 ? 19.924 50.390 27.884 1.00 20.06  ? 186 PRO A O    1 
ATOM   2896 C CB   . PRO A 1 183 ? 18.636 50.492 30.861 1.00 18.66  ? 186 PRO A CB   1 
ATOM   2897 C CG   . PRO A 1 183 ? 19.155 50.153 32.224 1.00 18.81  ? 186 PRO A CG   1 
ATOM   2898 C CD   . PRO A 1 183 ? 19.364 48.676 32.244 1.00 15.89  ? 186 PRO A CD   1 
ATOM   2899 H HA   . PRO A 1 183 ? 18.436 49.050 29.391 0.00 16.43  ? 186 PRO A HA   1 
ATOM   2900 H HB2  . PRO A 1 183 ? 18.964 51.359 30.575 0.00 22.41  ? 186 PRO A HB2  1 
ATOM   2901 H HB3  . PRO A 1 183 ? 17.666 50.483 30.851 0.00 22.41  ? 186 PRO A HB3  1 
ATOM   2902 H HG2  . PRO A 1 183 ? 19.992 50.618 32.378 0.00 22.59  ? 186 PRO A HG2  1 
ATOM   2903 H HG3  . PRO A 1 183 ? 18.503 50.414 32.894 0.00 22.59  ? 186 PRO A HG3  1 
ATOM   2904 H HD2  . PRO A 1 183 ? 20.110 48.440 32.818 0.00 19.09  ? 186 PRO A HD2  1 
ATOM   2905 H HD3  . PRO A 1 183 ? 18.562 48.217 32.537 0.00 19.09  ? 186 PRO A HD3  1 
ATOM   2906 N N    . VAL A 1 184 ? 21.511 49.907 29.407 1.00 17.93  ? 187 VAL A N    1 
ATOM   2907 C CA   . VAL A 1 184 ? 22.583 50.400 28.548 1.00 17.49  ? 187 VAL A CA   1 
ATOM   2908 C C    . VAL A 1 184 ? 22.842 49.426 27.405 1.00 15.49  ? 187 VAL A C    1 
ATOM   2909 O O    . VAL A 1 184 ? 23.024 49.836 26.253 1.00 25.44  ? 187 VAL A O    1 
ATOM   2910 C CB   . VAL A 1 184 ? 23.855 50.653 29.377 1.00 18.10  ? 187 VAL A CB   1 
ATOM   2911 C CG1  . VAL A 1 184 ? 25.006 51.068 28.472 1.00 21.87  ? 187 VAL A CG1  1 
ATOM   2912 C CG2  . VAL A 1 184 ? 23.594 51.713 30.436 1.00 24.00  ? 187 VAL A CG2  1 
ATOM   2913 H H    . VAL A 1 184 ? 21.772 49.608 30.170 0.00 21.54  ? 187 VAL A H    1 
ATOM   2914 H HA   . VAL A 1 184 ? 22.303 51.244 28.161 0.00 21.00  ? 187 VAL A HA   1 
ATOM   2915 H HB   . VAL A 1 184 ? 24.107 49.832 29.827 0.00 21.74  ? 187 VAL A HB   1 
ATOM   2916 H HG11 . VAL A 1 184 ? 25.717 51.441 29.016 0.00 26.25  ? 187 VAL A HG11 1 
ATOM   2917 H HG12 . VAL A 1 184 ? 25.330 50.287 27.995 0.00 26.25  ? 187 VAL A HG12 1 
ATOM   2918 H HG13 . VAL A 1 184 ? 24.689 51.732 27.841 0.00 26.25  ? 187 VAL A HG13 1 
ATOM   2919 H HG21 . VAL A 1 184 ? 24.406 51.856 30.947 0.00 28.82  ? 187 VAL A HG21 1 
ATOM   2920 H HG22 . VAL A 1 184 ? 23.329 52.538 29.999 0.00 28.82  ? 187 VAL A HG22 1 
ATOM   2921 H HG23 . VAL A 1 184 ? 22.884 51.407 31.021 0.00 28.82  ? 187 VAL A HG23 1 
ATOM   2922 N N    . VAL A 1 185 ? 22.868 48.123 27.701 1.00 16.15  ? 188 VAL A N    1 
ATOM   2923 C CA   . VAL A 1 185 ? 23.062 47.126 26.650 1.00 22.86  ? 188 VAL A CA   1 
ATOM   2924 C C    . VAL A 1 185 ? 21.919 47.190 25.645 1.00 18.59  ? 188 VAL A C    1 
ATOM   2925 O O    . VAL A 1 185 ? 22.137 47.154 24.427 1.00 15.39  ? 188 VAL A O    1 
ATOM   2926 C CB   . VAL A 1 185 ? 23.194 45.720 27.267 1.00 24.14  ? 188 VAL A CB   1 
ATOM   2927 C CG1  . VAL A 1 185 ? 23.226 44.658 26.178 1.00 17.12  ? 188 VAL A CG1  1 
ATOM   2928 C CG2  . VAL A 1 185 ? 24.440 45.631 28.136 1.00 23.51  ? 188 VAL A CG2  1 
ATOM   2929 H H    . VAL A 1 185 ? 22.776 47.797 28.492 0.00 19.39  ? 188 VAL A H    1 
ATOM   2930 H HA   . VAL A 1 185 ? 23.887 47.326 26.182 0.00 27.45  ? 188 VAL A HA   1 
ATOM   2931 H HB   . VAL A 1 185 ? 22.421 45.553 27.829 0.00 28.98  ? 188 VAL A HB   1 
ATOM   2932 H HG11 . VAL A 1 185 ? 23.552 43.826 26.557 0.00 20.56  ? 188 VAL A HG11 1 
ATOM   2933 H HG12 . VAL A 1 185 ? 22.329 44.533 25.832 0.00 20.56  ? 188 VAL A HG12 1 
ATOM   2934 H HG13 . VAL A 1 185 ? 23.817 44.952 25.468 0.00 20.56  ? 188 VAL A HG13 1 
ATOM   2935 H HG21 . VAL A 1 185 ? 24.493 44.743 28.523 0.00 28.23  ? 188 VAL A HG21 1 
ATOM   2936 H HG22 . VAL A 1 185 ? 25.222 45.799 27.586 0.00 28.23  ? 188 VAL A HG22 1 
ATOM   2937 H HG23 . VAL A 1 185 ? 24.382 46.296 28.840 0.00 28.23  ? 188 VAL A HG23 1 
ATOM   2938 N N    . TRP A 1 186 ? 20.685 47.282 26.143 1.00 13.73  ? 189 TRP A N    1 
ATOM   2939 C CA   . TRP A 1 186 ? 19.522 47.418 25.271 1.00 17.99  ? 189 TRP A CA   1 
ATOM   2940 C C    . TRP A 1 186 ? 19.667 48.621 24.345 1.00 15.61  ? 189 TRP A C    1 
ATOM   2941 O O    . TRP A 1 186 ? 19.432 48.524 23.135 1.00 20.02  ? 189 TRP A O    1 
ATOM   2942 C CB   . TRP A 1 186 ? 18.265 47.550 26.133 1.00 23.13  ? 189 TRP A CB   1 
ATOM   2943 C CG   . TRP A 1 186 ? 16.965 47.284 25.436 1.00 22.04  ? 189 TRP A CG   1 
ATOM   2944 C CD1  . TRP A 1 186 ? 16.267 46.112 25.427 1.00 19.90  ? 189 TRP A CD1  1 
ATOM   2945 C CD2  . TRP A 1 186 ? 16.188 48.218 24.674 1.00 16.34  ? 189 TRP A CD2  1 
ATOM   2946 N NE1  . TRP A 1 186 ? 15.111 46.254 24.701 1.00 20.77  ? 189 TRP A NE1  1 
ATOM   2947 C CE2  . TRP A 1 186 ? 15.037 47.538 24.228 1.00 24.25  ? 189 TRP A CE2  1 
ATOM   2948 C CE3  . TRP A 1 186 ? 16.355 49.562 24.323 1.00 16.28  ? 189 TRP A CE3  1 
ATOM   2949 C CZ2  . TRP A 1 186 ? 14.059 48.154 23.447 1.00 24.07  ? 189 TRP A CZ2  1 
ATOM   2950 C CZ3  . TRP A 1 186 ? 15.383 50.173 23.545 1.00 16.63  ? 189 TRP A CZ3  1 
ATOM   2951 C CH2  . TRP A 1 186 ? 14.250 49.468 23.117 1.00 21.26  ? 189 TRP A CH2  1 
ATOM   2952 H H    . TRP A 1 186 ? 20.495 47.269 26.981 0.00 16.41  ? 189 TRP A H    1 
ATOM   2953 H HA   . TRP A 1 186 ? 19.441 46.626 24.716 0.00 21.60  ? 189 TRP A HA   1 
ATOM   2954 H HB2  . TRP A 1 186 ? 18.332 46.919 26.867 0.00 27.77  ? 189 TRP A HB2  1 
ATOM   2955 H HB3  . TRP A 1 186 ? 18.226 48.456 26.477 0.00 27.77  ? 189 TRP A HB3  1 
ATOM   2956 H HD1  . TRP A 1 186 ? 16.536 45.330 25.852 0.00 23.89  ? 189 TRP A HD1  1 
ATOM   2957 H HE1  . TRP A 1 186 ? 14.527 45.637 24.566 0.00 24.94  ? 189 TRP A HE1  1 
ATOM   2958 H HE3  . TRP A 1 186 ? 17.104 50.036 24.605 0.00 19.55  ? 189 TRP A HE3  1 
ATOM   2959 H HZ2  . TRP A 1 186 ? 13.306 47.689 23.161 0.00 28.89  ? 189 TRP A HZ2  1 
ATOM   2960 H HZ3  . TRP A 1 186 ? 15.484 51.065 23.304 0.00 19.97  ? 189 TRP A HZ3  1 
ATOM   2961 H HH2  . TRP A 1 186 ? 13.614 49.903 22.597 0.00 25.52  ? 189 TRP A HH2  1 
ATOM   2962 N N    . LEU A 1 187 ? 20.066 49.766 24.903 1.00 16.95  ? 190 LEU A N    1 
ATOM   2963 C CA   . LEU A 1 187 ? 20.062 51.012 24.142 1.00 15.93  ? 190 LEU A CA   1 
ATOM   2964 C C    . LEU A 1 187 ? 21.048 50.962 22.980 1.00 22.22  ? 190 LEU A C    1 
ATOM   2965 O O    . LEU A 1 187 ? 20.726 51.387 21.864 1.00 26.60  ? 190 LEU A O    1 
ATOM   2966 C CB   . LEU A 1 187 ? 20.384 52.182 25.074 1.00 16.34  ? 190 LEU A CB   1 
ATOM   2967 C CG   . LEU A 1 187 ? 20.287 53.588 24.481 1.00 23.46  ? 190 LEU A CG   1 
ATOM   2968 C CD1  . LEU A 1 187 ? 18.852 53.917 24.104 1.00 26.34  ? 190 LEU A CD1  1 
ATOM   2969 C CD2  . LEU A 1 187 ? 20.831 54.611 25.466 1.00 22.44  ? 190 LEU A CD2  1 
ATOM   2970 H H    . LEU A 1 187 ? 20.341 49.847 25.714 0.00 20.36  ? 190 LEU A H    1 
ATOM   2971 H HA   . LEU A 1 187 ? 19.177 51.151 23.769 0.00 19.13  ? 190 LEU A HA   1 
ATOM   2972 H HB2  . LEU A 1 187 ? 19.767 52.146 25.821 0.00 19.53  ? 190 LEU A HB2  1 
ATOM   2973 H HB3  . LEU A 1 187 ? 21.295 52.070 25.389 0.00 19.53  ? 190 LEU A HB3  1 
ATOM   2974 H HG   . LEU A 1 187 ? 20.821 53.629 23.673 0.00 28.17  ? 190 LEU A HG   1 
ATOM   2975 H HD11 . LEU A 1 187 ? 18.811 54.833 23.787 0.00 31.62  ? 190 LEU A HD11 1 
ATOM   2976 H HD12 . LEU A 1 187 ? 18.563 53.311 23.404 0.00 31.62  ? 190 LEU A HD12 1 
ATOM   2977 H HD13 . LEU A 1 187 ? 18.288 53.813 24.886 0.00 31.62  ? 190 LEU A HD13 1 
ATOM   2978 H HD21 . LEU A 1 187 ? 20.800 55.491 25.058 0.00 26.94  ? 190 LEU A HD21 1 
ATOM   2979 H HD22 . LEU A 1 187 ? 20.285 54.599 26.268 0.00 26.94  ? 190 LEU A HD22 1 
ATOM   2980 H HD23 . LEU A 1 187 ? 21.748 54.381 25.687 0.00 26.94  ? 190 LEU A HD23 1 
ATOM   2981 N N    . ILE A 1 188 ? 22.258 50.450 23.223 1.00 16.57  ? 191 ILE A N    1 
ATOM   2982 C CA   . ILE A 1 188 ? 23.280 50.395 22.180 1.00 24.01  ? 191 ILE A CA   1 
ATOM   2983 C C    . ILE A 1 188 ? 23.226 49.109 21.367 1.00 22.55  ? 191 ILE A C    1 
ATOM   2984 O O    . ILE A 1 188 ? 23.973 48.978 20.385 1.00 22.42  ? 191 ILE A O    1 
ATOM   2985 C CB   . ILE A 1 188 ? 24.688 50.555 22.789 1.00 22.57  ? 191 ILE A CB   1 
ATOM   2986 C CG1  . ILE A 1 188 ? 25.051 49.333 23.638 1.00 24.20  ? 191 ILE A CG1  1 
ATOM   2987 C CG2  . ILE A 1 188 ? 24.756 51.822 23.629 1.00 35.00  ? 191 ILE A CG2  1 
ATOM   2988 C CD1  . ILE A 1 188 ? 26.300 49.517 24.470 1.00 30.74  ? 191 ILE A CD1  1 
ATOM   2989 H H    . ILE A 1 188 ? 22.509 50.129 23.980 0.00 19.81  ? 191 ILE A H    1 
ATOM   2990 H HA   . ILE A 1 188 ? 23.122 51.132 21.569 0.00 28.83  ? 191 ILE A HA   1 
ATOM   2991 H HB   . ILE A 1 188 ? 25.328 50.624 22.063 0.00 27.10  ? 191 ILE A HB   1 
ATOM   2992 H HG12 . ILE A 1 188 ? 24.317 49.146 24.244 0.00 29.05  ? 191 ILE A HG12 1 
ATOM   2993 H HG13 . ILE A 1 188 ? 25.196 48.576 23.050 0.00 29.05  ? 191 ILE A HG13 1 
ATOM   2994 H HG21 . ILE A 1 188 ? 25.687 52.058 23.768 0.00 42.01  ? 191 ILE A HG21 1 
ATOM   2995 H HG22 . ILE A 1 188 ? 24.300 52.537 23.159 0.00 42.01  ? 191 ILE A HG22 1 
ATOM   2996 H HG23 . ILE A 1 188 ? 24.325 51.658 24.482 0.00 42.01  ? 191 ILE A HG23 1 
ATOM   2997 H HD11 . ILE A 1 188 ? 26.621 48.646 24.755 0.00 36.91  ? 191 ILE A HD11 1 
ATOM   2998 H HD12 . ILE A 1 188 ? 26.976 49.958 23.932 0.00 36.91  ? 191 ILE A HD12 1 
ATOM   2999 H HD13 . ILE A 1 188 ? 26.087 50.060 25.245 0.00 36.91  ? 191 ILE A HD13 1 
ATOM   3000 N N    . GLY A 1 189 ? 22.368 48.163 21.735 1.00 25.94  ? 192 GLY A N    1 
ATOM   3001 C CA   . GLY A 1 189 ? 22.290 46.880 21.071 1.00 22.72  ? 192 GLY A CA   1 
ATOM   3002 C C    . GLY A 1 189 ? 21.333 46.879 19.897 1.00 22.55  ? 192 GLY A C    1 
ATOM   3003 O O    . GLY A 1 189 ? 20.931 47.925 19.380 1.00 26.03  ? 192 GLY A O    1 
ATOM   3004 H H    . GLY A 1 189 ? 21.810 48.249 22.384 0.00 31.14  ? 192 GLY A H    1 
ATOM   3005 H HA2  . GLY A 1 189 ? 23.170 46.635 20.746 0.00 27.28  ? 192 GLY A HA2  1 
ATOM   3006 H HA3  . GLY A 1 189 ? 21.991 46.210 21.706 0.00 27.28  ? 192 GLY A HA3  1 
ATOM   3007 N N    A SER A 1 190 ? 20.961 45.667 19.477 0.50 20.07  ? 193 SER A N    1 
ATOM   3008 N N    B SER A 1 190 ? 20.957 45.669 19.475 0.50 20.07  ? 193 SER A N    1 
ATOM   3009 C CA   A SER A 1 190 ? 20.112 45.513 18.300 0.50 25.97  ? 193 SER A CA   1 
ATOM   3010 C CA   B SER A 1 190 ? 20.117 45.529 18.290 0.50 25.98  ? 193 SER A CA   1 
ATOM   3011 C C    A SER A 1 190 ? 18.730 46.113 18.515 0.50 22.73  ? 193 SER A C    1 
ATOM   3012 C C    B SER A 1 190 ? 18.721 46.100 18.510 0.50 22.73  ? 193 SER A C    1 
ATOM   3013 O O    A SER A 1 190 ? 18.106 46.588 17.559 0.50 27.83  ? 193 SER A O    1 
ATOM   3014 O O    B SER A 1 190 ? 18.079 46.540 17.550 0.50 27.81  ? 193 SER A O    1 
ATOM   3015 C CB   A SER A 1 190 ? 19.992 44.032 17.936 0.50 26.51  ? 193 SER A CB   1 
ATOM   3016 C CB   B SER A 1 190 ? 20.026 44.059 17.882 0.50 26.49  ? 193 SER A CB   1 
ATOM   3017 O OG   A SER A 1 190 ? 19.318 43.312 18.954 0.50 29.39  ? 193 SER A OG   1 
ATOM   3018 O OG   B SER A 1 190 ? 21.225 43.627 17.262 0.50 32.31  ? 193 SER A OG   1 
ATOM   3019 H H    A SER A 1 190 ? 21.185 44.926 19.853 0.50 24.10  ? 193 SER A H    1 
ATOM   3020 H H    B SER A 1 190 ? 21.172 44.927 19.852 0.50 24.10  ? 193 SER A H    1 
ATOM   3021 H HA   A SER A 1 190 ? 20.527 45.978 17.557 0.50 31.18  ? 193 SER A HA   1 
ATOM   3022 H HA   B SER A 1 190 ? 20.528 46.022 17.563 0.50 31.19  ? 193 SER A HA   1 
ATOM   3023 H HB2  A SER A 1 190 ? 19.492 43.951 17.109 0.50 31.83  ? 193 SER A HB2  1 
ATOM   3024 H HB2  B SER A 1 190 ? 19.870 43.522 18.675 0.50 31.80  ? 193 SER A HB2  1 
ATOM   3025 H HB3  A SER A 1 190 ? 20.881 43.662 17.824 0.50 31.83  ? 193 SER A HB3  1 
ATOM   3026 H HB3  B SER A 1 190 ? 19.292 43.950 17.258 0.50 31.80  ? 193 SER A HB3  1 
ATOM   3027 H HG   A SER A 1 190 ? 19.734 43.382 19.680 0.50 35.28  ? 193 SER A HG   1 
ATOM   3028 H HG   B SER A 1 190 ? 21.401 44.118 16.604 0.50 38.78  ? 193 SER A HG   1 
ATOM   3029 N N    . GLU A 1 191 ? 18.231 46.099 19.752 1.00 20.26  ? 194 GLU A N    1 
ATOM   3030 C CA   . GLU A 1 191 ? 16.902 46.636 20.021 1.00 25.48  ? 194 GLU A CA   1 
ATOM   3031 C C    . GLU A 1 191 ? 16.861 48.154 19.933 1.00 28.15  ? 194 GLU A C    1 
ATOM   3032 O O    . GLU A 1 191 ? 15.789 48.717 19.687 1.00 21.79  ? 194 GLU A O    1 
ATOM   3033 C CB   . GLU A 1 191 ? 16.419 46.203 21.406 1.00 15.11  ? 194 GLU A CB   1 
ATOM   3034 C CG   . GLU A 1 191 ? 16.101 44.721 21.525 1.00 28.68  ? 194 GLU A CG   1 
ATOM   3035 C CD   . GLU A 1 191 ? 17.291 43.907 21.984 1.00 36.08  ? 194 GLU A CD   1 
ATOM   3036 O OE1  . GLU A 1 191 ? 18.355 44.506 22.245 1.00 38.49  ? 194 GLU A OE1  1 
ATOM   3037 O OE2  . GLU A 1 191 ? 17.162 42.670 22.088 1.00 30.07  ? 194 GLU A OE2  1 
ATOM   3038 H H    . GLU A 1 191 ? 18.646 45.798 20.443 0.00 24.33  ? 194 GLU A H    1 
ATOM   3039 H HA   . GLU A 1 191 ? 16.293 46.272 19.360 0.00 30.59  ? 194 GLU A HA   1 
ATOM   3040 H HB2  . GLU A 1 191 ? 17.112 46.407 22.053 0.00 18.15  ? 194 GLU A HB2  1 
ATOM   3041 H HB3  . GLU A 1 191 ? 15.610 46.695 21.619 0.00 18.15  ? 194 GLU A HB3  1 
ATOM   3042 H HG2  . GLU A 1 191 ? 15.387 44.601 22.172 0.00 34.43  ? 194 GLU A HG2  1 
ATOM   3043 H HG3  . GLU A 1 191 ? 15.823 44.386 20.659 0.00 34.43  ? 194 GLU A HG3  1 
ATOM   3044 N N    . GLY A 1 192 ? 17.993 48.824 20.135 1.00 25.21  ? 195 GLY A N    1 
ATOM   3045 C CA   . GLY A 1 192 ? 18.024 50.273 20.145 1.00 16.74  ? 195 GLY A CA   1 
ATOM   3046 C C    . GLY A 1 192 ? 18.781 50.864 18.975 1.00 17.79  ? 195 GLY A C    1 
ATOM   3047 O O    . GLY A 1 192 ? 18.333 50.779 17.827 1.00 24.29  ? 195 GLY A O    1 
ATOM   3048 H H    . GLY A 1 192 ? 18.758 48.456 20.269 0.00 30.27  ? 195 GLY A H    1 
ATOM   3049 H HA2  . GLY A 1 192 ? 17.115 50.610 20.117 0.00 20.10  ? 195 GLY A HA2  1 
ATOM   3050 H HA3  . GLY A 1 192 ? 18.449 50.576 20.963 0.00 20.10  ? 195 GLY A HA3  1 
ATOM   3051 N N    . ALA A 1 193 ? 19.939 51.462 19.256 1.00 20.24  ? 196 ALA A N    1 
ATOM   3052 C CA   . ALA A 1 193 ? 20.691 52.174 18.231 1.00 30.38  ? 196 ALA A CA   1 
ATOM   3053 C C    . ALA A 1 193 ? 21.461 51.244 17.304 1.00 24.60  ? 196 ALA A C    1 
ATOM   3054 O O    . ALA A 1 193 ? 21.904 51.686 16.238 1.00 25.64  ? 196 ALA A O    1 
ATOM   3055 C CB   . ALA A 1 193 ? 21.660 53.161 18.887 1.00 22.64  ? 196 ALA A CB   1 
ATOM   3056 H H    . ALA A 1 193 ? 20.309 51.468 20.033 0.00 24.31  ? 196 ALA A H    1 
ATOM   3057 H HA   . ALA A 1 193 ? 20.067 52.679 17.687 0.00 36.47  ? 196 ALA A HA   1 
ATOM   3058 H HB1  . ALA A 1 193 ? 22.153 53.627 18.193 0.00 27.18  ? 196 ALA A HB1  1 
ATOM   3059 H HB2  . ALA A 1 193 ? 21.153 53.796 19.416 0.00 27.18  ? 196 ALA A HB2  1 
ATOM   3060 H HB3  . ALA A 1 193 ? 22.273 52.670 19.456 0.00 27.18  ? 196 ALA A HB3  1 
ATOM   3061 N N    . GLY A 1 194 ? 21.636 49.980 17.678 1.00 22.42  ? 197 GLY A N    1 
ATOM   3062 C CA   . GLY A 1 194 ? 22.324 49.039 16.812 1.00 32.45  ? 197 GLY A CA   1 
ATOM   3063 C C    . GLY A 1 194 ? 23.800 49.314 16.630 1.00 27.30  ? 197 GLY A C    1 
ATOM   3064 O O    . GLY A 1 194 ? 24.338 49.066 15.548 1.00 38.74  ? 197 GLY A O    1 
ATOM   3065 H H    . GLY A 1 194 ? 21.367 49.647 18.424 0.00 26.92  ? 197 GLY A H    1 
ATOM   3066 H HA2  . GLY A 1 194 ? 22.232 48.148 17.185 0.00 38.96  ? 197 GLY A HA2  1 
ATOM   3067 H HA3  . GLY A 1 194 ? 21.908 49.060 15.936 0.00 38.96  ? 197 GLY A HA3  1 
ATOM   3068 N N    . ILE A 1 195 ? 24.474 49.822 17.663 1.00 31.99  ? 198 ILE A N    1 
ATOM   3069 C CA   . ILE A 1 195 ? 25.906 50.082 17.560 1.00 33.49  ? 198 ILE A CA   1 
ATOM   3070 C C    . ILE A 1 195 ? 26.703 48.806 17.798 1.00 32.70  ? 198 ILE A C    1 
ATOM   3071 O O    . ILE A 1 195 ? 27.750 48.590 17.179 1.00 32.29  ? 198 ILE A O    1 
ATOM   3072 C CB   . ILE A 1 195 ? 26.309 51.198 18.541 1.00 32.17  ? 198 ILE A CB   1 
ATOM   3073 C CG1  . ILE A 1 195 ? 25.943 52.566 17.964 1.00 28.39  ? 198 ILE A CG1  1 
ATOM   3074 C CG2  . ILE A 1 195 ? 27.801 51.141 18.844 1.00 42.93  ? 198 ILE A CG2  1 
ATOM   3075 C CD1  . ILE A 1 195 ? 25.395 53.530 18.994 1.00 40.88  ? 198 ILE A CD1  1 
ATOM   3076 H H    . ILE A 1 195 ? 24.129 50.021 18.425 0.00 38.41  ? 198 ILE A H    1 
ATOM   3077 H HA   . ILE A 1 195 ? 26.103 50.389 16.661 0.00 40.20  ? 198 ILE A HA   1 
ATOM   3078 H HB   . ILE A 1 195 ? 25.821 51.061 19.368 0.00 38.62  ? 198 ILE A HB   1 
ATOM   3079 H HG12 . ILE A 1 195 ? 26.738 52.966 17.578 0.00 34.08  ? 198 ILE A HG12 1 
ATOM   3080 H HG13 . ILE A 1 195 ? 25.266 52.446 17.280 0.00 34.08  ? 198 ILE A HG13 1 
ATOM   3081 H HG21 . ILE A 1 195 ? 28.073 51.980 19.247 0.00 51.53  ? 198 ILE A HG21 1 
ATOM   3082 H HG22 . ILE A 1 195 ? 27.971 50.409 19.456 0.00 51.53  ? 198 ILE A HG22 1 
ATOM   3083 H HG23 . ILE A 1 195 ? 28.286 51.000 18.015 0.00 51.53  ? 198 ILE A HG23 1 
ATOM   3084 H HD11 . ILE A 1 195 ? 25.207 54.379 18.563 0.00 49.08  ? 198 ILE A HD11 1 
ATOM   3085 H HD12 . ILE A 1 195 ? 24.579 53.162 19.368 0.00 49.08  ? 198 ILE A HD12 1 
ATOM   3086 H HD13 . ILE A 1 195 ? 26.055 53.653 19.694 0.00 49.08  ? 198 ILE A HD13 1 
ATOM   3087 N N    . VAL A 1 196 ? 26.225 47.947 18.693 1.00 23.65  ? 199 VAL A N    1 
ATOM   3088 C CA   . VAL A 1 196 ? 26.874 46.673 18.992 1.00 25.46  ? 199 VAL A CA   1 
ATOM   3089 C C    . VAL A 1 196 ? 26.140 45.573 18.231 1.00 30.52  ? 199 VAL A C    1 
ATOM   3090 O O    . VAL A 1 196 ? 24.901 45.559 18.226 1.00 28.20  ? 199 VAL A O    1 
ATOM   3091 C CB   . VAL A 1 196 ? 26.881 46.388 20.503 1.00 37.47  ? 199 VAL A CB   1 
ATOM   3092 C CG1  . VAL A 1 196 ? 27.978 45.398 20.849 1.00 51.89  ? 199 VAL A CG1  1 
ATOM   3093 C CG2  . VAL A 1 196 ? 27.058 47.678 21.297 1.00 53.69  ? 199 VAL A CG2  1 
ATOM   3094 H H    . VAL A 1 196 ? 25.510 48.081 19.152 0.00 28.39  ? 199 VAL A H    1 
ATOM   3095 H HA   . VAL A 1 196 ? 27.795 46.703 18.688 0.00 30.57  ? 199 VAL A HA   1 
ATOM   3096 H HB   . VAL A 1 196 ? 26.027 46.000 20.749 0.00 44.98  ? 199 VAL A HB   1 
ATOM   3097 H HG11 . VAL A 1 196 ? 27.964 45.234 21.805 0.00 62.28  ? 199 VAL A HG11 1 
ATOM   3098 H HG12 . VAL A 1 196 ? 27.819 44.570 20.369 0.00 62.28  ? 199 VAL A HG12 1 
ATOM   3099 H HG13 . VAL A 1 196 ? 28.834 45.772 20.590 0.00 62.28  ? 199 VAL A HG13 1 
ATOM   3100 H HG21 . VAL A 1 196 ? 27.078 47.466 22.243 0.00 64.45  ? 199 VAL A HG21 1 
ATOM   3101 H HG22 . VAL A 1 196 ? 27.892 48.098 21.035 0.00 64.45  ? 199 VAL A HG22 1 
ATOM   3102 H HG23 . VAL A 1 196 ? 26.315 48.271 21.107 0.00 64.45  ? 199 VAL A HG23 1 
ATOM   3103 N N    . PRO A 1 197 ? 26.837 44.643 17.581 1.00 35.47  ? 200 PRO A N    1 
ATOM   3104 C CA   . PRO A 1 197 ? 26.136 43.577 16.857 1.00 36.29  ? 200 PRO A CA   1 
ATOM   3105 C C    . PRO A 1 197 ? 25.514 42.564 17.808 1.00 23.52  ? 200 PRO A C    1 
ATOM   3106 O O    . PRO A 1 197 ? 25.872 42.462 18.983 1.00 26.87  ? 200 PRO A O    1 
ATOM   3107 C CB   . PRO A 1 197 ? 27.231 42.940 15.996 1.00 36.27  ? 200 PRO A CB   1 
ATOM   3108 C CG   . PRO A 1 197 ? 28.503 43.265 16.678 1.00 31.63  ? 200 PRO A CG   1 
ATOM   3109 C CD   . PRO A 1 197 ? 28.299 44.552 17.426 1.00 33.32  ? 200 PRO A CD   1 
ATOM   3110 H HA   . PRO A 1 197 ? 25.448 43.948 16.283 0.00 43.56  ? 200 PRO A HA   1 
ATOM   3111 H HB2  . PRO A 1 197 ? 27.098 41.980 15.952 0.00 43.53  ? 200 PRO A HB2  1 
ATOM   3112 H HB3  . PRO A 1 197 ? 27.210 43.319 15.103 0.00 43.53  ? 200 PRO A HB3  1 
ATOM   3113 H HG2  . PRO A 1 197 ? 28.729 42.550 17.293 0.00 37.97  ? 200 PRO A HG2  1 
ATOM   3114 H HG3  . PRO A 1 197 ? 29.205 43.368 16.016 0.00 37.97  ? 200 PRO A HG3  1 
ATOM   3115 H HD2  . PRO A 1 197 ? 28.735 44.517 18.292 0.00 40.00  ? 200 PRO A HD2  1 
ATOM   3116 H HD3  . PRO A 1 197 ? 28.638 45.303 16.914 0.00 40.00  ? 200 PRO A HD3  1 
ATOM   3117 N N    . LEU A 1 198 ? 24.567 41.797 17.262 1.00 24.15  ? 201 LEU A N    1 
ATOM   3118 C CA   . LEU A 1 198 ? 23.748 40.919 18.092 1.00 23.37  ? 201 LEU A CA   1 
ATOM   3119 C C    . LEU A 1 198 ? 24.593 39.874 18.812 1.00 30.82  ? 201 LEU A C    1 
ATOM   3120 O O    . LEU A 1 198 ? 24.327 39.546 19.975 1.00 23.91  ? 201 LEU A O    1 
ATOM   3121 C CB   . LEU A 1 198 ? 22.677 40.246 17.230 1.00 23.72  ? 201 LEU A CB   1 
ATOM   3122 C CG   . LEU A 1 198 ? 21.834 39.151 17.892 1.00 42.59  ? 201 LEU A CG   1 
ATOM   3123 C CD1  . LEU A 1 198 ? 21.069 39.696 19.093 1.00 25.78  ? 201 LEU A CD1  1 
ATOM   3124 C CD2  . LEU A 1 198 ? 20.878 38.539 16.880 1.00 23.87  ? 201 LEU A CD2  1 
ATOM   3125 H H    . LEU A 1 198 ? 24.381 41.768 16.423 0.00 29.00  ? 201 LEU A H    1 
ATOM   3126 H HA   . LEU A 1 198 ? 23.305 41.453 18.769 0.00 28.06  ? 201 LEU A HA   1 
ATOM   3127 H HB2  . LEU A 1 198 ? 22.061 40.933 16.930 0.00 28.48  ? 201 LEU A HB2  1 
ATOM   3128 H HB3  . LEU A 1 198 ? 23.119 39.841 16.468 0.00 28.48  ? 201 LEU A HB3  1 
ATOM   3129 H HG   . LEU A 1 198 ? 22.426 38.454 18.215 0.00 51.12  ? 201 LEU A HG   1 
ATOM   3130 H HD11 . LEU A 1 198 ? 20.547 38.979 19.486 0.00 30.95  ? 201 LEU A HD11 1 
ATOM   3131 H HD12 . LEU A 1 198 ? 21.703 40.038 19.743 0.00 30.95  ? 201 LEU A HD12 1 
ATOM   3132 H HD13 . LEU A 1 198 ? 20.482 40.408 18.797 0.00 30.95  ? 201 LEU A HD13 1 
ATOM   3133 H HD21 . LEU A 1 198 ? 20.355 37.849 17.316 0.00 28.66  ? 201 LEU A HD21 1 
ATOM   3134 H HD22 . LEU A 1 198 ? 20.291 39.233 16.540 0.00 28.66  ? 201 LEU A HD22 1 
ATOM   3135 H HD23 . LEU A 1 198 ? 21.391 38.155 16.152 0.00 28.66  ? 201 LEU A HD23 1 
ATOM   3136 N N    A ASN A 1 199 ? 25.622 39.343 18.148 0.61 22.93  ? 202 ASN A N    1 
ATOM   3137 N N    B ASN A 1 199 ? 25.610 39.334 18.134 0.39 23.05  ? 202 ASN A N    1 
ATOM   3138 C CA   A ASN A 1 199 ? 26.421 38.290 18.771 0.61 25.43  ? 202 ASN A CA   1 
ATOM   3139 C CA   B ASN A 1 199 ? 26.445 38.304 18.743 0.39 25.48  ? 202 ASN A CA   1 
ATOM   3140 C C    A ASN A 1 199 ? 27.148 38.805 20.009 0.61 27.74  ? 202 ASN A C    1 
ATOM   3141 C C    B ASN A 1 199 ? 27.119 38.818 20.008 0.39 27.66  ? 202 ASN A C    1 
ATOM   3142 O O    A ASN A 1 199 ? 27.276 38.083 21.005 0.61 22.74  ? 202 ASN A O    1 
ATOM   3143 O O    B ASN A 1 199 ? 27.179 38.111 21.021 0.39 22.85  ? 202 ASN A O    1 
ATOM   3144 C CB   A ASN A 1 199 ? 27.412 37.703 17.764 0.61 29.79  ? 202 ASN A CB   1 
ATOM   3145 C CB   B ASN A 1 199 ? 27.493 37.820 17.739 0.39 29.82  ? 202 ASN A CB   1 
ATOM   3146 C CG   A ASN A 1 199 ? 28.193 38.765 17.019 0.61 29.83  ? 202 ASN A CG   1 
ATOM   3147 C CG   B ASN A 1 199 ? 28.207 36.564 18.200 0.39 34.07  ? 202 ASN A CG   1 
ATOM   3148 O OD1  A ASN A 1 199 ? 29.063 39.424 17.584 0.61 44.29  ? 202 ASN A OD1  1 
ATOM   3149 O OD1  B ASN A 1 199 ? 27.904 36.017 19.259 0.39 38.59  ? 202 ASN A OD1  1 
ATOM   3150 N ND2  A ASN A 1 199 ? 27.888 38.933 15.737 0.61 44.26  ? 202 ASN A ND2  1 
ATOM   3151 N ND2  B ASN A 1 199 ? 29.164 36.103 17.404 0.39 41.71  ? 202 ASN A ND2  1 
ATOM   3152 H H    A ASN A 1 199 ? 25.872 39.569 17.357 0.61 27.53  ? 202 ASN A H    1 
ATOM   3153 H H    B ASN A 1 199 ? 25.832 39.545 17.330 0.39 27.68  ? 202 ASN A H    1 
ATOM   3154 H HA   A ASN A 1 199 ? 25.826 37.576 19.049 0.61 30.53  ? 202 ASN A HA   1 
ATOM   3155 H HA   B ASN A 1 199 ? 25.886 37.549 18.985 0.39 30.59  ? 202 ASN A HA   1 
ATOM   3156 H HB2  A ASN A 1 199 ? 28.046 37.141 18.236 0.61 35.76  ? 202 ASN A HB2  1 
ATOM   3157 H HB2  B ASN A 1 199 ? 27.056 37.625 16.896 0.39 35.80  ? 202 ASN A HB2  1 
ATOM   3158 H HB3  A ASN A 1 199 ? 26.924 37.177 17.111 0.61 35.76  ? 202 ASN A HB3  1 
ATOM   3159 H HB3  B ASN A 1 199 ? 28.158 38.516 17.616 0.39 35.80  ? 202 ASN A HB3  1 
ATOM   3160 H HD21 A ASN A 1 199 ? 27.275 38.451 15.374 0.61 53.13  ? 202 ASN A HD21 1 
ATOM   3161 H HD21 B ASN A 1 199 ? 29.349 36.513 16.671 0.39 50.06  ? 202 ASN A HD21 1 
ATOM   3162 H HD22 A ASN A 1 199 ? 28.303 39.524 15.270 0.61 53.13  ? 202 ASN A HD22 1 
ATOM   3163 H HD22 B ASN A 1 199 ? 29.599 35.393 17.621 0.39 50.06  ? 202 ASN A HD22 1 
ATOM   3164 N N    . ILE A 1 200 ? 27.631 40.048 19.970 1.00 24.52  ? 203 ILE A N    1 
ATOM   3165 C CA   . ILE A 1 200 ? 28.271 40.618 21.151 1.00 18.57  ? 203 ILE A CA   1 
ATOM   3166 C C    . ILE A 1 200 ? 27.227 40.941 22.213 1.00 22.25  ? 203 ILE A C    1 
ATOM   3167 O O    . ILE A 1 200 ? 27.447 40.713 23.409 1.00 17.93  ? 203 ILE A O    1 
ATOM   3168 C CB   . ILE A 1 200 ? 29.092 41.864 20.772 1.00 47.97  ? 203 ILE A CB   1 
ATOM   3169 C CG1  . ILE A 1 200 ? 30.187 41.511 19.760 1.00 37.01  ? 203 ILE A CG1  1 
ATOM   3170 C CG2  . ILE A 1 200 ? 29.696 42.500 22.019 1.00 24.53  ? 203 ILE A CG2  1 
ATOM   3171 C CD1  . ILE A 1 200 ? 31.147 40.433 20.225 1.00 31.83  ? 203 ILE A CD1  1 
ATOM   3172 H H    . ILE A 1 200 ? 27.600 40.568 19.285 0.00 29.43  ? 203 ILE A H    1 
ATOM   3173 H HA   . ILE A 1 200 ? 28.881 39.958 21.516 0.00 22.20  ? 203 ILE A HA   1 
ATOM   3174 H HB   . ILE A 1 200 ? 28.494 42.503 20.355 0.00 57.57  ? 203 ILE A HB   1 
ATOM   3175 H HG12 . ILE A 1 200 ? 29.766 41.197 18.945 0.00 44.42  ? 203 ILE A HG12 1 
ATOM   3176 H HG13 . ILE A 1 200 ? 30.708 42.309 19.578 0.00 44.42  ? 203 ILE A HG13 1 
ATOM   3177 H HG21 . ILE A 1 200 ? 30.386 43.127 21.751 0.00 29.45  ? 203 ILE A HG21 1 
ATOM   3178 H HG22 . ILE A 1 200 ? 28.997 42.966 22.505 0.00 29.45  ? 203 ILE A HG22 1 
ATOM   3179 H HG23 . ILE A 1 200 ? 30.078 41.804 22.575 0.00 29.45  ? 203 ILE A HG23 1 
ATOM   3180 H HD11 . ILE A 1 200 ? 31.889 40.380 19.602 0.00 38.21  ? 203 ILE A HD11 1 
ATOM   3181 H HD12 . ILE A 1 200 ? 31.475 40.662 21.109 0.00 38.21  ? 203 ILE A HD12 1 
ATOM   3182 H HD13 . ILE A 1 200 ? 30.679 39.584 20.255 0.00 38.21  ? 203 ILE A HD13 1 
ATOM   3183 N N    . GLU A 1 201 ? 26.078 41.477 21.799 1.00 24.58  ? 204 GLU A N    1 
ATOM   3184 C CA   . GLU A 1 201 ? 25.018 41.764 22.760 1.00 20.50  ? 204 GLU A CA   1 
ATOM   3185 C C    . GLU A 1 201 ? 24.618 40.504 23.517 1.00 21.07  ? 204 GLU A C    1 
ATOM   3186 O O    . GLU A 1 201 ? 24.471 40.522 24.744 1.00 20.70  ? 204 GLU A O    1 
ATOM   3187 C CB   . GLU A 1 201 ? 23.807 42.363 22.046 1.00 19.91  ? 204 GLU A CB   1 
ATOM   3188 C CG   . GLU A 1 201 ? 22.628 42.619 22.974 1.00 28.06  ? 204 GLU A CG   1 
ATOM   3189 C CD   . GLU A 1 201 ? 21.402 43.114 22.246 1.00 25.93  ? 204 GLU A CD   1 
ATOM   3190 O OE1  . GLU A 1 201 ? 21.484 43.353 21.022 1.00 25.10  ? 204 GLU A OE1  1 
ATOM   3191 O OE2  . GLU A 1 201 ? 20.352 43.259 22.903 1.00 35.82  ? 204 GLU A OE2  1 
ATOM   3192 H H    . GLU A 1 201 ? 25.892 41.680 20.985 0.00 29.51  ? 204 GLU A H    1 
ATOM   3193 H HA   . GLU A 1 201 ? 25.344 42.417 23.398 0.00 24.61  ? 204 GLU A HA   1 
ATOM   3194 H HB2  . GLU A 1 201 ? 24.064 43.209 21.649 0.00 23.91  ? 204 GLU A HB2  1 
ATOM   3195 H HB3  . GLU A 1 201 ? 23.514 41.748 21.355 0.00 23.91  ? 204 GLU A HB3  1 
ATOM   3196 H HG2  . GLU A 1 201 ? 22.395 41.792 23.425 0.00 33.68  ? 204 GLU A HG2  1 
ATOM   3197 H HG3  . GLU A 1 201 ? 22.880 43.292 23.626 0.00 33.68  ? 204 GLU A HG3  1 
ATOM   3198 N N    . THR A 1 202 ? 24.427 39.398 22.794 1.00 17.77  ? 205 THR A N    1 
ATOM   3199 C CA   . THR A 1 202 ? 24.070 38.140 23.442 1.00 19.49  ? 205 THR A CA   1 
ATOM   3200 C C    . THR A 1 202 ? 25.124 37.734 24.463 1.00 19.59  ? 205 THR A C    1 
ATOM   3201 O O    . THR A 1 202 ? 24.792 37.265 25.558 1.00 15.98  ? 205 THR A O    1 
ATOM   3202 C CB   . THR A 1 202 ? 23.891 37.045 22.390 1.00 20.89  ? 205 THR A CB   1 
ATOM   3203 O OG1  . THR A 1 202 ? 22.942 37.478 21.406 1.00 17.99  ? 205 THR A OG1  1 
ATOM   3204 C CG2  . THR A 1 202 ? 23.403 35.750 23.029 1.00 16.31  ? 205 THR A CG2  1 
ATOM   3205 H H    . THR A 1 202 ? 24.498 39.351 21.938 0.00 21.33  ? 205 THR A H    1 
ATOM   3206 H HA   . THR A 1 202 ? 23.226 38.252 23.907 0.00 23.40  ? 205 THR A HA   1 
ATOM   3207 H HB   . THR A 1 202 ? 24.744 36.866 21.963 0.00 25.08  ? 205 THR A HB   1 
ATOM   3208 H HG1  . THR A 1 202 ? 23.231 38.159 21.008 0.00 21.60  ? 205 THR A HG1  1 
ATOM   3209 H HG21 . THR A 1 202 ? 23.206 35.094 22.342 0.00 19.58  ? 205 THR A HG21 1 
ATOM   3210 H HG22 . THR A 1 202 ? 24.087 35.393 23.618 0.00 19.58  ? 205 THR A HG22 1 
ATOM   3211 H HG23 . THR A 1 202 ? 22.599 35.917 23.545 0.00 19.58  ? 205 THR A HG23 1 
ATOM   3212 N N    . LEU A 1 203 ? 26.402 37.909 24.121 1.00 16.74  ? 206 LEU A N    1 
ATOM   3213 C CA   . LEU A 1 203 ? 27.468 37.625 25.074 1.00 19.39  ? 206 LEU A CA   1 
ATOM   3214 C C    . LEU A 1 203 ? 27.320 38.473 26.331 1.00 16.12  ? 206 LEU A C    1 
ATOM   3215 O O    . LEU A 1 203 ? 27.480 37.971 27.450 1.00 22.53  ? 206 LEU A O    1 
ATOM   3216 C CB   . LEU A 1 203 ? 28.827 37.870 24.417 1.00 17.95  ? 206 LEU A CB   1 
ATOM   3217 C CG   . LEU A 1 203 ? 30.050 37.855 25.337 1.00 33.82  ? 206 LEU A CG   1 
ATOM   3218 C CD1  . LEU A 1 203 ? 30.159 36.525 26.066 1.00 24.32  ? 206 LEU A CD1  1 
ATOM   3219 C CD2  . LEU A 1 203 ? 31.316 38.140 24.542 1.00 41.16  ? 206 LEU A CD2  1 
ATOM   3220 H H    . LEU A 1 203 ? 26.672 38.188 23.353 0.00 20.11  ? 206 LEU A H    1 
ATOM   3221 H HA   . LEU A 1 203 ? 27.421 36.692 25.334 0.00 23.28  ? 206 LEU A HA   1 
ATOM   3222 H HB2  . LEU A 1 203 ? 28.966 37.180 23.749 0.00 21.46  ? 206 LEU A HB2  1 
ATOM   3223 H HB3  . LEU A 1 203 ? 28.802 38.742 23.992 0.00 21.46  ? 206 LEU A HB3  1 
ATOM   3224 H HG   . LEU A 1 203 ? 29.950 38.551 26.006 0.00 40.60  ? 206 LEU A HG   1 
ATOM   3225 H HD11 . LEU A 1 203 ? 30.971 36.521 26.597 0.00 29.20  ? 206 LEU A HD11 1 
ATOM   3226 H HD12 . LEU A 1 203 ? 29.386 36.416 26.643 0.00 29.20  ? 206 LEU A HD12 1 
ATOM   3227 H HD13 . LEU A 1 203 ? 30.187 35.808 25.413 0.00 29.20  ? 206 LEU A HD13 1 
ATOM   3228 H HD21 . LEU A 1 203 ? 32.072 38.162 25.149 0.00 49.40  ? 206 LEU A HD21 1 
ATOM   3229 H HD22 . LEU A 1 203 ? 31.440 37.439 23.883 0.00 49.40  ? 206 LEU A HD22 1 
ATOM   3230 H HD23 . LEU A 1 203 ? 31.223 38.998 24.098 0.00 49.40  ? 206 LEU A HD23 1 
ATOM   3231 N N    . LEU A 1 204 ? 27.008 39.761 26.167 1.00 15.88  ? 207 LEU A N    1 
ATOM   3232 C CA   . LEU A 1 204 ? 26.898 40.653 27.318 1.00 16.38  ? 207 LEU A CA   1 
ATOM   3233 C C    . LEU A 1 204 ? 25.749 40.238 28.231 1.00 21.43  ? 207 LEU A C    1 
ATOM   3234 O O    . LEU A 1 204 ? 25.913 40.148 29.453 1.00 17.88  ? 207 LEU A O    1 
ATOM   3235 C CB   . LEU A 1 204 ? 26.713 42.094 26.843 1.00 21.43  ? 207 LEU A CB   1 
ATOM   3236 C CG   . LEU A 1 204 ? 27.924 42.729 26.153 1.00 20.69  ? 207 LEU A CG   1 
ATOM   3237 C CD1  . LEU A 1 204 ? 27.538 44.048 25.503 1.00 29.96  ? 207 LEU A CD1  1 
ATOM   3238 C CD2  . LEU A 1 204 ? 29.066 42.930 27.138 1.00 27.69  ? 207 LEU A CD2  1 
ATOM   3239 H H    . LEU A 1 204 ? 26.858 40.137 25.409 0.00 18.98  ? 207 LEU A H    1 
ATOM   3240 H HA   . LEU A 1 204 ? 27.720 40.604 27.830 0.00 19.67  ? 207 LEU A HA   1 
ATOM   3241 H HB2  . LEU A 1 204 ? 25.978 42.113 26.209 0.00 25.73  ? 207 LEU A HB2  1 
ATOM   3242 H HB3  . LEU A 1 204 ? 26.500 42.643 27.614 0.00 25.73  ? 207 LEU A HB3  1 
ATOM   3243 H HG   . LEU A 1 204 ? 28.236 42.129 25.457 0.00 24.84  ? 207 LEU A HG   1 
ATOM   3244 H HD11 . LEU A 1 204 ? 28.316 44.422 25.061 0.00 35.97  ? 207 LEU A HD11 1 
ATOM   3245 H HD12 . LEU A 1 204 ? 26.835 43.887 24.854 0.00 35.97  ? 207 LEU A HD12 1 
ATOM   3246 H HD13 . LEU A 1 204 ? 27.222 44.658 26.188 0.00 35.97  ? 207 LEU A HD13 1 
ATOM   3247 H HD21 . LEU A 1 204 ? 29.771 43.436 26.704 0.00 33.24  ? 207 LEU A HD21 1 
ATOM   3248 H HD22 . LEU A 1 204 ? 28.736 43.417 27.909 0.00 33.24  ? 207 LEU A HD22 1 
ATOM   3249 H HD23 . LEU A 1 204 ? 29.402 42.063 27.413 0.00 33.24  ? 207 LEU A HD23 1 
ATOM   3250 N N    . PHE A 1 205 ? 24.569 39.989 27.654 1.00 18.82  ? 208 PHE A N    1 
ATOM   3251 C CA   . PHE A 1 205 ? 23.427 39.581 28.469 1.00 16.59  ? 208 PHE A CA   1 
ATOM   3252 C C    . PHE A 1 205 ? 23.707 38.270 29.190 1.00 15.89  ? 208 PHE A C    1 
ATOM   3253 O O    . PHE A 1 205 ? 23.283 38.078 30.335 1.00 18.36  ? 208 PHE A O    1 
ATOM   3254 C CB   . PHE A 1 205 ? 22.176 39.443 27.598 1.00 15.85  ? 208 PHE A CB   1 
ATOM   3255 C CG   . PHE A 1 205 ? 21.446 40.739 27.353 1.00 14.63  ? 208 PHE A CG   1 
ATOM   3256 C CD1  . PHE A 1 205 ? 21.216 41.637 28.382 1.00 24.81  ? 208 PHE A CD1  1 
ATOM   3257 C CD2  . PHE A 1 205 ? 20.976 41.048 26.086 1.00 27.44  ? 208 PHE A CD2  1 
ATOM   3258 C CE1  . PHE A 1 205 ? 20.542 42.822 28.150 1.00 12.23  ? 208 PHE A CE1  1 
ATOM   3259 C CE2  . PHE A 1 205 ? 20.301 42.231 25.850 1.00 14.01  ? 208 PHE A CE2  1 
ATOM   3260 C CZ   . PHE A 1 205 ? 20.084 43.118 26.884 1.00 19.68  ? 208 PHE A CZ   1 
ATOM   3261 H H    . PHE A 1 205 ? 24.409 40.048 26.812 0.00 22.59  ? 208 PHE A H    1 
ATOM   3262 H HA   . PHE A 1 205 ? 23.261 40.269 29.132 0.00 19.93  ? 208 PHE A HA   1 
ATOM   3263 H HB2  . PHE A 1 205 ? 22.437 39.085 26.735 0.00 19.04  ? 208 PHE A HB2  1 
ATOM   3264 H HB3  . PHE A 1 205 ? 21.559 38.836 28.036 0.00 19.04  ? 208 PHE A HB3  1 
ATOM   3265 H HD1  . PHE A 1 205 ? 21.518 41.440 29.239 0.00 29.79  ? 208 PHE A HD1  1 
ATOM   3266 H HD2  . PHE A 1 205 ? 21.117 40.452 25.386 0.00 32.94  ? 208 PHE A HD2  1 
ATOM   3267 H HE1  . PHE A 1 205 ? 20.399 43.420 28.848 0.00 14.69  ? 208 PHE A HE1  1 
ATOM   3268 H HE2  . PHE A 1 205 ? 19.993 42.429 24.995 0.00 16.82  ? 208 PHE A HE2  1 
ATOM   3269 H HZ   . PHE A 1 205 ? 19.629 43.914 26.727 0.00 23.63  ? 208 PHE A HZ   1 
ATOM   3270 N N    . MET A 1 206 ? 24.417 37.351 28.534 1.00 13.92  ? 209 MET A N    1 
ATOM   3271 C CA   . MET A 1 206 ? 24.693 36.059 29.152 1.00 19.92  ? 209 MET A CA   1 
ATOM   3272 C C    . MET A 1 206 ? 25.541 36.226 30.408 1.00 20.03  ? 209 MET A C    1 
ATOM   3273 O O    . MET A 1 206 ? 25.254 35.627 31.451 1.00 15.99  ? 209 MET A O    1 
ATOM   3274 C CB   . MET A 1 206 ? 25.384 35.142 28.145 1.00 20.22  ? 209 MET A CB   1 
ATOM   3275 C CG   . MET A 1 206 ? 25.470 33.695 28.584 1.00 19.24  ? 209 MET A CG   1 
ATOM   3276 S SD   . MET A 1 206 ? 27.081 33.318 29.290 1.00 41.62  ? 209 MET A SD   1 
ATOM   3277 C CE   . MET A 1 206 ? 27.927 32.756 27.823 1.00 20.70  ? 209 MET A CE   1 
ATOM   3278 H H    . MET A 1 206 ? 24.744 37.450 27.745 0.00 16.72  ? 209 MET A H    1 
ATOM   3279 H HA   . MET A 1 206 ? 23.852 35.645 29.401 0.00 23.92  ? 209 MET A HA   1 
ATOM   3280 H HB2  . MET A 1 206 ? 24.889 35.167 27.311 0.00 24.28  ? 209 MET A HB2  1 
ATOM   3281 H HB3  . MET A 1 206 ? 26.288 35.461 28.004 0.00 24.28  ? 209 MET A HB3  1 
ATOM   3282 H HG2  . MET A 1 206 ? 24.794 33.522 29.258 0.00 23.10  ? 209 MET A HG2  1 
ATOM   3283 H HG3  . MET A 1 206 ? 25.330 33.117 27.818 0.00 23.10  ? 209 MET A HG3  1 
ATOM   3284 H HE1  . MET A 1 206 ? 28.821 32.467 28.065 0.00 24.86  ? 209 MET A HE1  1 
ATOM   3285 H HE2  . MET A 1 206 ? 27.433 32.015 27.437 0.00 24.86  ? 209 MET A HE2  1 
ATOM   3286 H HE3  . MET A 1 206 ? 27.977 33.487 27.187 0.00 24.86  ? 209 MET A HE3  1 
ATOM   3287 N N    . VAL A 1 207 ? 26.593 37.045 30.328 1.00 17.72  ? 210 VAL A N    1 
ATOM   3288 C CA   . VAL A 1 207 ? 27.426 37.289 31.502 1.00 23.89  ? 210 VAL A CA   1 
ATOM   3289 C C    . VAL A 1 207 ? 26.609 37.953 32.602 1.00 15.51  ? 210 VAL A C    1 
ATOM   3290 O O    . VAL A 1 207 ? 26.747 37.622 33.787 1.00 17.22  ? 210 VAL A O    1 
ATOM   3291 C CB   . VAL A 1 207 ? 28.654 38.138 31.119 1.00 22.29  ? 210 VAL A CB   1 
ATOM   3292 C CG1  . VAL A 1 207 ? 29.358 38.650 32.368 1.00 20.28  ? 210 VAL A CG1  1 
ATOM   3293 C CG2  . VAL A 1 207 ? 29.609 37.331 30.255 1.00 17.35  ? 210 VAL A CG2  1 
ATOM   3294 H H    . VAL A 1 207 ? 26.839 37.463 29.618 0.00 21.28  ? 210 VAL A H    1 
ATOM   3295 H HA   . VAL A 1 207 ? 27.745 36.436 31.837 0.00 28.68  ? 210 VAL A HA   1 
ATOM   3296 H HB   . VAL A 1 207 ? 28.357 38.905 30.604 0.00 26.76  ? 210 VAL A HB   1 
ATOM   3297 H HG11 . VAL A 1 207 ? 30.255 38.934 32.131 0.00 24.35  ? 210 VAL A HG11 1 
ATOM   3298 H HG12 . VAL A 1 207 ? 28.858 39.400 32.728 0.00 24.35  ? 210 VAL A HG12 1 
ATOM   3299 H HG13 . VAL A 1 207 ? 29.399 37.936 33.023 0.00 24.35  ? 210 VAL A HG13 1 
ATOM   3300 H HG21 . VAL A 1 207 ? 30.372 37.885 30.026 0.00 20.74  ? 210 VAL A HG21 1 
ATOM   3301 H HG22 . VAL A 1 207 ? 29.903 36.552 30.752 0.00 20.74  ? 210 VAL A HG22 1 
ATOM   3302 H HG23 . VAL A 1 207 ? 29.148 37.054 29.448 0.00 20.74  ? 210 VAL A HG23 1 
ATOM   3303 N N    . LEU A 1 208 ? 25.745 38.899 32.231 1.00 14.11  ? 211 LEU A N    1 
ATOM   3304 C CA   . LEU A 1 208 ? 24.925 39.582 33.226 1.00 18.94  ? 211 LEU A CA   1 
ATOM   3305 C C    . LEU A 1 208 ? 23.906 38.631 33.845 1.00 16.09  ? 211 LEU A C    1 
ATOM   3306 O O    . LEU A 1 208 ? 23.757 38.580 35.072 1.00 20.67  ? 211 LEU A O    1 
ATOM   3307 C CB   . LEU A 1 208 ? 24.224 40.783 32.588 1.00 17.65  ? 211 LEU A CB   1 
ATOM   3308 C CG   . LEU A 1 208 ? 25.129 41.922 32.109 1.00 20.82  ? 211 LEU A CG   1 
ATOM   3309 C CD1  . LEU A 1 208 ? 24.314 42.970 31.364 1.00 27.76  ? 211 LEU A CD1  1 
ATOM   3310 C CD2  . LEU A 1 208 ? 25.880 42.556 33.274 1.00 21.14  ? 211 LEU A CD2  1 
ATOM   3311 H H    . LEU A 1 208 ? 25.618 39.160 31.421 0.00 16.86  ? 211 LEU A H    1 
ATOM   3312 H HA   . LEU A 1 208 ? 25.501 39.909 33.935 0.00 22.74  ? 211 LEU A HA   1 
ATOM   3313 H HB2  . LEU A 1 208 ? 23.728 40.468 31.816 0.00 21.20  ? 211 LEU A HB2  1 
ATOM   3314 H HB3  . LEU A 1 208 ? 23.614 41.159 33.243 0.00 21.20  ? 211 LEU A HB3  1 
ATOM   3315 H HG   . LEU A 1 208 ? 25.789 41.557 31.500 0.00 25.00  ? 211 LEU A HG   1 
ATOM   3316 H HD11 . LEU A 1 208 ? 24.900 43.698 31.103 0.00 33.33  ? 211 LEU A HD11 1 
ATOM   3317 H HD12 . LEU A 1 208 ? 23.921 42.562 30.576 0.00 33.33  ? 211 LEU A HD12 1 
ATOM   3318 H HD13 . LEU A 1 208 ? 23.615 43.301 31.949 0.00 33.33  ? 211 LEU A HD13 1 
ATOM   3319 H HD21 . LEU A 1 208 ? 26.376 43.324 32.949 0.00 25.38  ? 211 LEU A HD21 1 
ATOM   3320 H HD22 . LEU A 1 208 ? 25.241 42.836 33.948 0.00 25.38  ? 211 LEU A HD22 1 
ATOM   3321 H HD23 . LEU A 1 208 ? 26.491 41.903 33.650 0.00 25.38  ? 211 LEU A HD23 1 
ATOM   3322 N N    . ASP A 1 209 ? 23.195 37.869 33.009 1.00 16.57  ? 212 ASP A N    1 
ATOM   3323 C CA   . ASP A 1 209 ? 22.152 36.975 33.509 1.00 12.31  ? 212 ASP A CA   1 
ATOM   3324 C C    . ASP A 1 209 ? 22.719 35.967 34.502 1.00 12.56  ? 212 ASP A C    1 
ATOM   3325 O O    . ASP A 1 209 ? 22.163 35.766 35.588 1.00 22.28  ? 212 ASP A O    1 
ATOM   3326 C CB   . ASP A 1 209 ? 21.478 36.247 32.341 1.00 14.64  ? 212 ASP A CB   1 
ATOM   3327 C CG   . ASP A 1 209 ? 20.524 37.137 31.558 1.00 16.39  ? 212 ASP A CG   1 
ATOM   3328 O OD1  . ASP A 1 209 ? 20.036 38.143 32.114 1.00 13.54  ? 212 ASP A OD1  1 
ATOM   3329 O OD2  . ASP A 1 209 ? 20.256 36.822 30.378 1.00 13.53  ? 212 ASP A OD2  1 
ATOM   3330 H H    . ASP A 1 209 ? 23.297 37.851 32.155 0.00 19.90  ? 212 ASP A H    1 
ATOM   3331 H HA   . ASP A 1 209 ? 21.482 37.509 33.965 0.00 14.79  ? 212 ASP A HA   1 
ATOM   3332 H HB2  . ASP A 1 209 ? 22.161 35.930 31.731 0.00 17.59  ? 212 ASP A HB2  1 
ATOM   3333 H HB3  . ASP A 1 209 ? 20.970 35.497 32.689 0.00 17.59  ? 212 ASP A HB3  1 
ATOM   3334 N N    . VAL A 1 210 ? 23.825 35.314 34.142 1.00 13.24  ? 213 VAL A N    1 
ATOM   3335 C CA   . VAL A 1 210 ? 24.406 34.302 35.020 1.00 17.12  ? 213 VAL A CA   1 
ATOM   3336 C C    . VAL A 1 210 ? 24.845 34.929 36.339 1.00 20.01  ? 213 VAL A C    1 
ATOM   3337 O O    . VAL A 1 210 ? 24.626 34.360 37.416 1.00 15.01  ? 213 VAL A O    1 
ATOM   3338 C CB   . VAL A 1 210 ? 25.575 33.591 34.312 1.00 24.93  ? 213 VAL A CB   1 
ATOM   3339 C CG1  . VAL A 1 210 ? 26.284 32.639 35.266 1.00 30.50  ? 213 VAL A CG1  1 
ATOM   3340 C CG2  . VAL A 1 210 ? 25.076 32.842 33.084 1.00 29.87  ? 213 VAL A CG2  1 
ATOM   3341 H H    . VAL A 1 210 ? 24.252 35.438 33.405 0.00 15.81  ? 213 VAL A H    1 
ATOM   3342 H HA   . VAL A 1 210 ? 23.727 33.639 35.219 0.00 20.56  ? 213 VAL A HA   1 
ATOM   3343 H HB   . VAL A 1 210 ? 26.217 34.259 34.022 0.00 29.93  ? 213 VAL A HB   1 
ATOM   3344 H HG11 . VAL A 1 210 ? 26.866 32.055 34.756 0.00 36.62  ? 213 VAL A HG11 1 
ATOM   3345 H HG12 . VAL A 1 210 ? 26.807 33.157 35.898 0.00 36.62  ? 213 VAL A HG12 1 
ATOM   3346 H HG13 . VAL A 1 210 ? 25.620 32.114 35.739 0.00 36.62  ? 213 VAL A HG13 1 
ATOM   3347 H HG21 . VAL A 1 210 ? 25.834 32.446 32.626 0.00 35.86  ? 213 VAL A HG21 1 
ATOM   3348 H HG22 . VAL A 1 210 ? 24.460 32.148 33.366 0.00 35.86  ? 213 VAL A HG22 1 
ATOM   3349 H HG23 . VAL A 1 210 ? 24.623 33.467 32.496 0.00 35.86  ? 213 VAL A HG23 1 
ATOM   3350 N N    . SER A 1 211 ? 25.467 36.110 36.277 1.00 14.20  ? 214 SER A N    1 
ATOM   3351 C CA   . SER A 1 211 ? 25.912 36.775 37.500 1.00 20.92  ? 214 SER A CA   1 
ATOM   3352 C C    . SER A 1 211 ? 24.730 37.150 38.384 1.00 20.53  ? 214 SER A C    1 
ATOM   3353 O O    . SER A 1 211 ? 24.786 36.992 39.610 1.00 16.71  ? 214 SER A O    1 
ATOM   3354 C CB   . SER A 1 211 ? 26.726 38.024 37.156 1.00 24.32  ? 214 SER A CB   1 
ATOM   3355 O OG   . SER A 1 211 ? 27.914 37.697 36.457 1.00 24.66  ? 214 SER A OG   1 
ATOM   3356 H H    . SER A 1 211 ? 25.641 36.539 35.552 0.00 16.96  ? 214 SER A H    1 
ATOM   3357 H HA   . SER A 1 211 ? 26.482 36.164 37.992 0.00 25.11  ? 214 SER A HA   1 
ATOM   3358 H HB2  . SER A 1 211 ? 26.186 38.606 36.599 0.00 29.20  ? 214 SER A HB2  1 
ATOM   3359 H HB3  . SER A 1 211 ? 26.963 38.479 37.980 0.00 29.20  ? 214 SER A HB3  1 
ATOM   3360 H HG   . SER A 1 211 ? 27.725 37.331 35.725 0.00 29.61  ? 214 SER A HG   1 
ATOM   3361 N N    . ALA A 1 212 ? 23.654 37.647 37.782 1.00 19.47  ? 215 ALA A N    1 
ATOM   3362 C CA   . ALA A 1 212 ? 22.530 38.192 38.536 1.00 25.84  ? 215 ALA A CA   1 
ATOM   3363 C C    . ALA A 1 212 ? 21.622 37.102 39.097 1.00 30.09  ? 215 ALA A C    1 
ATOM   3364 O O    . ALA A 1 212 ? 20.834 37.355 40.009 1.00 28.92  ? 215 ALA A O    1 
ATOM   3365 C CB   . ALA A 1 212 ? 21.726 39.139 37.655 1.00 16.39  ? 215 ALA A CB   1 
ATOM   3366 H H    . ALA A 1 212 ? 23.550 37.681 36.929 0.00 23.38  ? 215 ALA A H    1 
ATOM   3367 H HA   . ALA A 1 212 ? 22.885 38.685 39.292 0.00 31.02  ? 215 ALA A HA   1 
ATOM   3368 H HB1  . ALA A 1 212 ? 20.972 39.478 38.162 0.00 19.68  ? 215 ALA A HB1  1 
ATOM   3369 H HB2  . ALA A 1 212 ? 22.296 39.874 37.379 0.00 19.68  ? 215 ALA A HB2  1 
ATOM   3370 H HB3  . ALA A 1 212 ? 21.411 38.654 36.876 0.00 19.68  ? 215 ALA A HB3  1 
ATOM   3371 N N    . LYS A 1 213 ? 21.717 35.901 38.540 1.00 21.82  ? 216 LYS A N    1 
ATOM   3372 C CA   . LYS A 1 213 ? 20.815 34.793 38.940 1.00 18.47  ? 216 LYS A CA   1 
ATOM   3373 C C    . LYS A 1 213 ? 21.602 33.712 39.696 1.00 27.03  ? 216 LYS A C    1 
ATOM   3374 O O    . LYS A 1 213 ? 21.386 33.646 40.932 1.00 35.73  ? 216 LYS A O    1 
ATOM   3375 C CB   . LYS A 1 213 ? 20.098 34.258 37.706 1.00 19.94  ? 216 LYS A CB   1 
ATOM   3376 C CG   . LYS A 1 213 ? 19.146 35.251 37.071 1.00 23.47  ? 216 LYS A CG   1 
ATOM   3377 C CD   . LYS A 1 213 ? 18.459 34.738 35.818 1.00 24.20  ? 216 LYS A CD   1 
ATOM   3378 C CE   . LYS A 1 213 ? 17.601 35.809 35.177 1.00 24.98  ? 216 LYS A CE   1 
ATOM   3379 N NZ   . LYS A 1 213 ? 18.320 37.076 35.130 1.00 33.85  ? 216 LYS A NZ   1 
ATOM   3380 H HA   . LYS A 1 213 ? 20.163 35.178 39.559 1.00 22.17  ? 216 LYS A HA   1 
ATOM   3381 H HB2  . LYS A 1 213 ? 20.767 33.994 37.042 1.00 23.94  ? 216 LYS A HB2  1 
ATOM   3382 H HB3  . LYS A 1 213 ? 19.623 33.437 37.944 1.00 23.94  ? 216 LYS A HB3  1 
ATOM   3383 H HG2  . LYS A 1 213 ? 18.467 35.561 37.704 1.00 28.18  ? 216 LYS A HG2  1 
ATOM   3384 H HG3  . LYS A 1 213 ? 19.671 36.041 36.831 1.00 28.18  ? 216 LYS A HG3  1 
ATOM   3385 H HD2  . LYS A 1 213 ? 19.126 34.408 35.181 1.00 29.06  ? 216 LYS A HD2  1 
ATOM   3386 H HD3  . LYS A 1 213 ? 17.905 33.970 36.067 1.00 29.06  ? 216 LYS A HD3  1 
ATOM   3387 H HE2  . LYS A 1 213 ? 17.352 35.568 34.262 1.00 29.99  ? 216 LYS A HE2  1 
ATOM   3388 H HE3  . LYS A 1 213 ? 16.808 35.980 35.723 1.00 29.99  ? 216 LYS A HE3  1 
ATOM   3389 H HZ2  . LYS A 1 213 ? 19.181 37.038 34.937 1.00 40.63  ? 216 LYS A HZ2  1 
ATOM   3390 N N    . VAL A 1 214 ? 22.678 33.185 39.102 1.00 23.86  ? 217 VAL A N    1 
ATOM   3391 C CA   . VAL A 1 214 ? 23.485 32.163 39.756 1.00 17.08  ? 217 VAL A CA   1 
ATOM   3392 C C    . VAL A 1 214 ? 24.433 32.813 40.758 1.00 16.82  ? 217 VAL A C    1 
ATOM   3393 O O    . VAL A 1 214 ? 24.455 32.439 41.931 1.00 18.49  ? 217 VAL A O    1 
ATOM   3394 C CB   . VAL A 1 214 ? 24.262 31.324 38.729 1.00 22.49  ? 217 VAL A CB   1 
ATOM   3395 C CG1  . VAL A 1 214 ? 25.049 30.222 39.429 1.00 24.43  ? 217 VAL A CG1  1 
ATOM   3396 C CG2  . VAL A 1 214 ? 23.308 30.735 37.703 1.00 21.03  ? 217 VAL A CG2  1 
ATOM   3397 H H    . VAL A 1 214 ? 22.952 33.408 38.318 0.00 28.65  ? 217 VAL A H    1 
ATOM   3398 H HA   . VAL A 1 214 ? 22.898 31.560 40.239 0.00 20.51  ? 217 VAL A HA   1 
ATOM   3399 H HB   . VAL A 1 214 ? 24.894 31.895 38.265 0.00 27.00  ? 217 VAL A HB   1 
ATOM   3400 H HG11 . VAL A 1 214 ? 25.420 29.625 38.760 0.00 29.33  ? 217 VAL A HG11 1 
ATOM   3401 H HG12 . VAL A 1 214 ? 25.764 30.624 39.947 0.00 29.33  ? 217 VAL A HG12 1 
ATOM   3402 H HG13 . VAL A 1 214 ? 24.452 29.731 40.015 0.00 29.33  ? 217 VAL A HG13 1 
ATOM   3403 H HG21 . VAL A 1 214 ? 23.782 30.073 37.175 0.00 25.25  ? 217 VAL A HG21 1 
ATOM   3404 H HG22 . VAL A 1 214 ? 22.564 30.318 38.165 0.00 25.25  ? 217 VAL A HG22 1 
ATOM   3405 H HG23 . VAL A 1 214 ? 22.984 31.445 37.128 0.00 25.25  ? 217 VAL A HG23 1 
ATOM   3406 N N    . GLY A 1 215 ? 25.217 33.789 40.290 1.00 20.13  ? 218 GLY A N    1 
ATOM   3407 C CA   . GLY A 1 215 ? 26.132 34.479 41.186 1.00 25.56  ? 218 GLY A CA   1 
ATOM   3408 C C    . GLY A 1 215 ? 25.423 35.078 42.385 1.00 27.07  ? 218 GLY A C    1 
ATOM   3409 O O    . GLY A 1 215 ? 25.872 34.937 43.525 1.00 24.84  ? 218 GLY A O    1 
ATOM   3410 H H    . GLY A 1 215 ? 25.235 34.061 39.474 0.00 24.17  ? 218 GLY A H    1 
ATOM   3411 H HA2  . GLY A 1 215 ? 26.801 33.854 41.506 0.00 30.69  ? 218 GLY A HA2  1 
ATOM   3412 H HA3  . GLY A 1 215 ? 26.575 35.195 40.703 0.00 30.69  ? 218 GLY A HA3  1 
ATOM   3413 N N    . PHE A 1 216 ? 24.303 35.760 42.138 1.00 20.01  ? 219 PHE A N    1 
ATOM   3414 C CA   . PHE A 1 216 ? 23.492 36.284 43.232 1.00 26.88  ? 219 PHE A CA   1 
ATOM   3415 C C    . PHE A 1 216 ? 23.071 35.168 44.181 1.00 24.27  ? 219 PHE A C    1 
ATOM   3416 O O    . PHE A 1 216 ? 23.122 35.331 45.405 1.00 20.96  ? 219 PHE A O    1 
ATOM   3417 C CB   . PHE A 1 216 ? 22.269 37.006 42.657 1.00 23.87  ? 219 PHE A CB   1 
ATOM   3418 C CG   . PHE A 1 216 ? 21.349 37.591 43.694 1.00 21.90  ? 219 PHE A CG   1 
ATOM   3419 C CD1  . PHE A 1 216 ? 20.393 36.804 44.318 1.00 30.69  ? 219 PHE A CD1  1 
ATOM   3420 C CD2  . PHE A 1 216 ? 21.423 38.935 44.027 1.00 20.81  ? 219 PHE A CD2  1 
ATOM   3421 C CE1  . PHE A 1 216 ? 19.540 37.341 45.267 1.00 25.67  ? 219 PHE A CE1  1 
ATOM   3422 C CE2  . PHE A 1 216 ? 20.572 39.479 44.974 1.00 21.14  ? 219 PHE A CE2  1 
ATOM   3423 C CZ   . PHE A 1 216 ? 19.628 38.679 45.594 1.00 18.16  ? 219 PHE A CZ   1 
ATOM   3424 H H    . PHE A 1 216 ? 23.995 35.931 41.354 0.00 24.03  ? 219 PHE A H    1 
ATOM   3425 H HA   . PHE A 1 216 ? 24.009 36.926 43.743 0.00 32.27  ? 219 PHE A HA   1 
ATOM   3426 H HB2  . PHE A 1 216 ? 22.577 37.734 42.094 0.00 28.66  ? 219 PHE A HB2  1 
ATOM   3427 H HB3  . PHE A 1 216 ? 21.755 36.374 42.131 0.00 28.66  ? 219 PHE A HB3  1 
ATOM   3428 H HD1  . PHE A 1 216 ? 20.324 35.904 44.096 0.00 36.84  ? 219 PHE A HD1  1 
ATOM   3429 H HD2  . PHE A 1 216 ? 22.053 39.478 43.609 0.00 24.98  ? 219 PHE A HD2  1 
ATOM   3430 H HE1  . PHE A 1 216 ? 18.908 36.801 45.684 0.00 30.82  ? 219 PHE A HE1  1 
ATOM   3431 H HE2  . PHE A 1 216 ? 20.634 40.380 45.193 0.00 25.38  ? 219 PHE A HE2  1 
ATOM   3432 H HZ   . PHE A 1 216 ? 19.054 39.043 46.230 0.00 21.81  ? 219 PHE A HZ   1 
ATOM   3433 N N    . GLY A 1 217 ? 22.665 34.020 43.633 1.00 22.46  ? 220 GLY A N    1 
ATOM   3434 C CA   . GLY A 1 217 ? 22.220 32.923 44.473 1.00 14.79  ? 220 GLY A CA   1 
ATOM   3435 C C    . GLY A 1 217 ? 23.330 32.311 45.305 1.00 23.59  ? 220 GLY A C    1 
ATOM   3436 O O    . GLY A 1 217 ? 23.091 31.873 46.434 1.00 22.19  ? 220 GLY A O    1 
ATOM   3437 H H    . GLY A 1 217 ? 22.640 33.859 42.789 0.00 26.97  ? 220 GLY A H    1 
ATOM   3438 H HA2  . GLY A 1 217 ? 21.533 33.245 45.077 0.00 17.67  ? 220 GLY A HA2  1 
ATOM   3439 H HA3  . GLY A 1 217 ? 21.846 32.226 43.912 0.00 17.67  ? 220 GLY A HA3  1 
ATOM   3440 N N    . LEU A 1 218 ? 24.551 32.265 44.766 1.00 23.34  ? 221 LEU A N    1 
ATOM   3441 C CA   . LEU A 1 218 ? 25.663 31.686 45.515 1.00 18.38  ? 221 LEU A CA   1 
ATOM   3442 C C    . LEU A 1 218 ? 25.981 32.509 46.757 1.00 31.22  ? 221 LEU A C    1 
ATOM   3443 O O    . LEU A 1 218 ? 26.297 31.952 47.814 1.00 27.28  ? 221 LEU A O    1 
ATOM   3444 C CB   . LEU A 1 218 ? 26.897 31.574 44.620 1.00 26.43  ? 221 LEU A CB   1 
ATOM   3445 C CG   . LEU A 1 218 ? 26.856 30.467 43.566 1.00 31.40  ? 221 LEU A CG   1 
ATOM   3446 C CD1  . LEU A 1 218 ? 27.965 30.664 42.543 1.00 35.65  ? 221 LEU A CD1  1 
ATOM   3447 C CD2  . LEU A 1 218 ? 26.962 29.093 44.219 1.00 26.23  ? 221 LEU A CD2  1 
ATOM   3448 H H    . LEU A 1 218 ? 24.757 32.556 43.984 0.00 28.02  ? 221 LEU A H    1 
ATOM   3449 H HA   . LEU A 1 218 ? 25.414 30.793 45.800 0.00 22.07  ? 221 LEU A HA   1 
ATOM   3450 H HB2  . LEU A 1 218 ? 27.007 32.416 44.150 0.00 31.73  ? 221 LEU A HB2  1 
ATOM   3451 H HB3  . LEU A 1 218 ? 27.667 31.406 45.185 0.00 31.73  ? 221 LEU A HB3  1 
ATOM   3452 H HG   . LEU A 1 218 ? 26.007 30.508 43.100 0.00 37.69  ? 221 LEU A HG   1 
ATOM   3453 H HD11 . LEU A 1 218 ? 27.905 29.964 41.874 0.00 42.80  ? 221 LEU A HD11 1 
ATOM   3454 H HD12 . LEU A 1 218 ? 27.858 31.532 42.125 0.00 42.80  ? 221 LEU A HD12 1 
ATOM   3455 H HD13 . LEU A 1 218 ? 28.822 30.617 42.994 0.00 42.80  ? 221 LEU A HD13 1 
ATOM   3456 H HD21 . LEU A 1 218 ? 27.055 28.420 43.526 0.00 31.49  ? 221 LEU A HD21 1 
ATOM   3457 H HD22 . LEU A 1 218 ? 27.738 29.079 44.800 0.00 31.49  ? 221 LEU A HD22 1 
ATOM   3458 H HD23 . LEU A 1 218 ? 26.158 28.927 44.736 0.00 31.49  ? 221 LEU A HD23 1 
ATOM   3459 N N    . ILE A 1 219 ? 25.904 33.836 46.651 1.00 27.42  ? 222 ILE A N    1 
ATOM   3460 C CA   . ILE A 1 219 ? 26.200 34.688 47.798 1.00 27.25  ? 222 ILE A CA   1 
ATOM   3461 C C    . ILE A 1 219 ? 25.134 34.523 48.875 1.00 26.68  ? 222 ILE A C    1 
ATOM   3462 O O    . ILE A 1 219 ? 25.445 34.445 50.069 1.00 24.92  ? 222 ILE A O    1 
ATOM   3463 C CB   . ILE A 1 219 ? 26.325 36.155 47.349 1.00 29.03  ? 222 ILE A CB   1 
ATOM   3464 C CG1  . ILE A 1 219 ? 27.538 36.332 46.434 1.00 31.57  ? 222 ILE A CG1  1 
ATOM   3465 C CG2  . ILE A 1 219 ? 26.432 37.074 48.559 1.00 35.37  ? 222 ILE A CG2  1 
ATOM   3466 C CD1  . ILE A 1 219 ? 27.468 37.569 45.564 1.00 34.97  ? 222 ILE A CD1  1 
ATOM   3467 H H    . ILE A 1 219 ? 25.685 34.261 45.936 0.00 32.91  ? 222 ILE A H    1 
ATOM   3468 H HA   . ILE A 1 219 ? 27.050 34.413 48.175 0.00 32.72  ? 222 ILE A HA   1 
ATOM   3469 H HB   . ILE A 1 219 ? 25.526 36.391 46.851 0.00 34.86  ? 222 ILE A HB   1 
ATOM   3470 H HG12 . ILE A 1 219 ? 28.335 36.401 46.982 0.00 37.90  ? 222 ILE A HG12 1 
ATOM   3471 H HG13 . ILE A 1 219 ? 27.603 35.561 45.849 0.00 37.90  ? 222 ILE A HG13 1 
ATOM   3472 H HG21 . ILE A 1 219 ? 26.790 37.930 48.275 0.00 42.45  ? 222 ILE A HG21 1 
ATOM   3473 H HG22 . ILE A 1 219 ? 25.549 37.196 48.942 0.00 42.45  ? 222 ILE A HG22 1 
ATOM   3474 H HG23 . ILE A 1 219 ? 27.023 36.668 49.212 0.00 42.45  ? 222 ILE A HG23 1 
ATOM   3475 H HD11 . ILE A 1 219 ? 28.238 37.585 44.975 0.00 41.98  ? 222 ILE A HD11 1 
ATOM   3476 H HD12 . ILE A 1 219 ? 26.652 37.540 45.040 0.00 41.98  ? 222 ILE A HD12 1 
ATOM   3477 H HD13 . ILE A 1 219 ? 27.469 38.355 46.131 0.00 41.98  ? 222 ILE A HD13 1 
ATOM   3478 N N    . LEU A 1 220 ? 23.864 34.459 48.473 1.00 25.61  ? 223 LEU A N    1 
ATOM   3479 C CA   . LEU A 1 220 ? 22.778 34.422 49.447 1.00 24.94  ? 223 LEU A CA   1 
ATOM   3480 C C    . LEU A 1 220 ? 22.724 33.079 50.168 1.00 22.09  ? 223 LEU A C    1 
ATOM   3481 O O    . LEU A 1 220 ? 22.708 33.027 51.403 1.00 26.38  ? 223 LEU A O    1 
ATOM   3482 C CB   . LEU A 1 220 ? 21.448 34.711 48.748 1.00 29.23  ? 223 LEU A CB   1 
ATOM   3483 C CG   . LEU A 1 220 ? 20.175 34.585 49.591 1.00 17.23  ? 223 LEU A CG   1 
ATOM   3484 C CD1  . LEU A 1 220 ? 20.103 35.696 50.624 1.00 27.36  ? 223 LEU A CD1  1 
ATOM   3485 C CD2  . LEU A 1 220 ? 18.943 34.601 48.697 1.00 26.07  ? 223 LEU A CD2  1 
ATOM   3486 H H    . LEU A 1 220 ? 23.609 34.436 47.652 0.00 30.74  ? 223 LEU A H    1 
ATOM   3487 H HA   . LEU A 1 220 ? 22.931 35.111 50.112 0.00 29.94  ? 223 LEU A HA   1 
ATOM   3488 H HB2  . LEU A 1 220 ? 21.477 35.621 48.415 0.00 35.09  ? 223 LEU A HB2  1 
ATOM   3489 H HB3  . LEU A 1 220 ? 21.359 34.090 48.008 0.00 35.09  ? 223 LEU A HB3  1 
ATOM   3490 H HG   . LEU A 1 220 ? 20.193 33.739 50.066 0.00 20.70  ? 223 LEU A HG   1 
ATOM   3491 H HD11 . LEU A 1 220 ? 19.287 35.596 51.140 0.00 32.85  ? 223 LEU A HD11 1 
ATOM   3492 H HD12 . LEU A 1 220 ? 20.874 35.634 51.209 0.00 32.85  ? 223 LEU A HD12 1 
ATOM   3493 H HD13 . LEU A 1 220 ? 20.102 36.552 50.168 0.00 32.85  ? 223 LEU A HD13 1 
ATOM   3494 H HD21 . LEU A 1 220 ? 18.152 34.505 49.249 0.00 31.30  ? 223 LEU A HD21 1 
ATOM   3495 H HD22 . LEU A 1 220 ? 18.912 35.443 48.217 0.00 31.30  ? 223 LEU A HD22 1 
ATOM   3496 H HD23 . LEU A 1 220 ? 18.999 33.863 48.069 0.00 31.30  ? 223 LEU A HD23 1 
ATOM   3497 N N    . LEU A 1 221 ? 22.693 31.980 49.413 1.00 28.48  ? 224 LEU A N    1 
ATOM   3498 C CA   . LEU A 1 221 ? 22.468 30.670 50.012 1.00 27.92  ? 224 LEU A CA   1 
ATOM   3499 C C    . LEU A 1 221 ? 23.652 30.176 50.832 1.00 34.33  ? 224 LEU A C    1 
ATOM   3500 O O    . LEU A 1 221 ? 23.521 29.152 51.511 1.00 37.40  ? 224 LEU A O    1 
ATOM   3501 C CB   . LEU A 1 221 ? 22.130 29.652 48.921 1.00 29.67  ? 224 LEU A CB   1 
ATOM   3502 C CG   . LEU A 1 221 ? 20.832 29.931 48.156 1.00 25.20  ? 224 LEU A CG   1 
ATOM   3503 C CD1  . LEU A 1 221 ? 20.618 28.903 47.055 1.00 16.47  ? 224 LEU A CD1  1 
ATOM   3504 C CD2  . LEU A 1 221 ? 19.639 29.959 49.103 1.00 25.53  ? 224 LEU A CD2  1 
ATOM   3505 H H    . LEU A 1 221 ? 22.798 31.969 48.559 0.00 34.19  ? 224 LEU A H    1 
ATOM   3506 H HA   . LEU A 1 221 ? 21.708 30.733 50.612 0.00 33.52  ? 224 LEU A HA   1 
ATOM   3507 H HB2  . LEU A 1 221 ? 22.853 29.643 48.275 0.00 35.62  ? 224 LEU A HB2  1 
ATOM   3508 H HB3  . LEU A 1 221 ? 22.042 28.778 49.334 0.00 35.62  ? 224 LEU A HB3  1 
ATOM   3509 H HG   . LEU A 1 221 ? 20.903 30.804 47.738 0.00 30.26  ? 224 LEU A HG   1 
ATOM   3510 H HD11 . LEU A 1 221 ? 19.794 29.108 46.587 0.00 19.69  ? 224 LEU A HD11 1 
ATOM   3511 H HD12 . LEU A 1 221 ? 21.366 28.940 46.439 0.00 19.69  ? 224 LEU A HD12 1 
ATOM   3512 H HD13 . LEU A 1 221 ? 20.561 28.021 47.454 0.00 19.69  ? 224 LEU A HD13 1 
ATOM   3513 H HD21 . LEU A 1 221 ? 18.822 29.934 48.582 0.00 30.65  ? 224 LEU A HD21 1 
ATOM   3514 H HD22 . LEU A 1 221 ? 19.683 29.186 49.688 0.00 30.65  ? 224 LEU A HD22 1 
ATOM   3515 H HD23 . LEU A 1 221 ? 19.672 30.774 49.628 0.00 30.65  ? 224 LEU A HD23 1 
ATOM   3516 N N    . ARG A 1 222 ? 24.792 30.863 50.793 1.00 36.50  ? 225 ARG A N    1 
ATOM   3517 C CA   . ARG A 1 222 ? 25.932 30.530 51.637 1.00 39.59  ? 225 ARG A CA   1 
ATOM   3518 C C    . ARG A 1 222 ? 25.991 31.372 52.903 1.00 48.45  ? 225 ARG A C    1 
ATOM   3519 O O    . ARG A 1 222 ? 26.863 31.140 53.746 1.00 44.43  ? 225 ARG A O    1 
ATOM   3520 C CB   . ARG A 1 222 ? 27.239 30.691 50.855 1.00 42.09  ? 225 ARG A CB   1 
ATOM   3521 C CG   . ARG A 1 222 ? 27.383 29.733 49.686 1.00 71.23  ? 225 ARG A CG   1 
ATOM   3522 C CD   . ARG A 1 222 ? 28.803 29.730 49.142 1.00 86.54  ? 225 ARG A CD   1 
ATOM   3523 N NE   . ARG A 1 222 ? 29.618 28.685 49.751 1.00 108.83 ? 225 ARG A NE   1 
ATOM   3524 C CZ   . ARG A 1 222 ? 29.588 27.408 49.395 1.00 103.92 ? 225 ARG A CZ   1 
ATOM   3525 N NH1  . ARG A 1 222 ? 28.793 26.978 48.428 1.00 95.47  ? 225 ARG A NH1  1 
ATOM   3526 N NH2  . ARG A 1 222 ? 30.373 26.539 50.026 1.00 111.67 ? 225 ARG A NH2  1 
ATOM   3527 H H    . ARG A 1 222 ? 24.930 31.537 50.276 1.00 43.72  ? 225 ARG A H    1 
ATOM   3528 H HA   . ARG A 1 222 ? 25.858 29.598 51.898 1.00 47.44  ? 225 ARG A HA   1 
ATOM   3529 H HB2  . ARG A 1 222 ? 27.281 31.594 50.503 1.00 50.44  ? 225 ARG A HB2  1 
ATOM   3530 H HB3  . ARG A 1 222 ? 27.983 30.535 51.458 1.00 50.44  ? 225 ARG A HB3  1 
ATOM   3531 H HG2  . ARG A 1 222 ? 27.166 28.834 49.979 1.00 85.49  ? 225 ARG A HG2  1 
ATOM   3532 H HG3  . ARG A 1 222 ? 26.783 30.003 48.973 1.00 85.49  ? 225 ARG A HG3  1 
ATOM   3533 H HD2  . ARG A 1 222 ? 28.778 29.575 48.184 1.00 103.87 ? 225 ARG A HD2  1 
ATOM   3534 H HD3  . ARG A 1 222 ? 29.219 30.586 49.329 1.00 103.87 ? 225 ARG A HD3  1 
ATOM   3535 H HE   . ARG A 1 222 ? 30.154 28.912 50.384 1.00 130.61 ? 225 ARG A HE   1 
ATOM   3536 H HH11 . ARG A 1 222 ? 28.281 27.531 48.015 1.00 114.58 ? 225 ARG A HH11 1 
ATOM   3537 H HH12 . ARG A 1 222 ? 28.789 26.145 48.213 1.00 114.58 ? 225 ARG A HH12 1 
ATOM   3538 H HH21 . ARG A 1 222 ? 30.892 26.808 50.656 1.00 134.02 ? 225 ARG A HH21 1 
ATOM   3539 H HH22 . ARG A 1 222 ? 30.361 25.709 49.803 1.00 134.02 ? 225 ARG A HH22 1 
ATOM   3540 N N    . SER A 1 223 ? 25.089 32.335 53.057 1.00 34.96  ? 226 SER A N    1 
ATOM   3541 C CA   . SER A 1 223 ? 25.058 33.182 54.237 1.00 33.64  ? 226 SER A CA   1 
ATOM   3542 C C    . SER A 1 223 ? 24.228 32.536 55.339 1.00 52.97  ? 226 SER A C    1 
ATOM   3543 O O    . SER A 1 223 ? 23.322 31.740 55.079 1.00 43.22  ? 226 SER A O    1 
ATOM   3544 C CB   . SER A 1 223 ? 24.481 34.556 53.895 1.00 41.29  ? 226 SER A CB   1 
ATOM   3545 O OG   . SER A 1 223 ? 23.776 35.096 54.999 1.00 51.81  ? 226 SER A OG   1 
ATOM   3546 H H    . SER A 1 223 ? 24.476 32.518 52.483 0.00 41.97  ? 226 SER A H    1 
ATOM   3547 H HA   . SER A 1 223 ? 25.962 33.303 54.569 0.00 40.39  ? 226 SER A HA   1 
ATOM   3548 H HB2  . SER A 1 223 ? 25.208 35.154 53.662 0.00 49.56  ? 226 SER A HB2  1 
ATOM   3549 H HB3  . SER A 1 223 ? 23.872 34.465 53.146 0.00 49.56  ? 226 SER A HB3  1 
ATOM   3550 H HG   . SER A 1 223 ? 23.343 35.775 54.759 0.00 62.19  ? 226 SER A HG   1 
ATOM   3551 N N    . ARG A 1 224 ? 24.550 32.889 56.582 1.00 38.33  ? 227 ARG A N    1 
ATOM   3552 C CA   . ARG A 1 224 ? 23.762 32.455 57.727 1.00 51.35  ? 227 ARG A CA   1 
ATOM   3553 C C    . ARG A 1 224 ? 22.556 33.350 57.978 1.00 45.21  ? 227 ARG A C    1 
ATOM   3554 O O    . ARG A 1 224 ? 21.795 33.089 58.916 1.00 32.14  ? 227 ARG A O    1 
ATOM   3555 C CB   . ARG A 1 224 ? 24.639 32.409 58.982 1.00 45.88  ? 227 ARG A CB   1 
ATOM   3556 C CG   . ARG A 1 224 ? 25.149 31.016 59.330 1.00 68.92  ? 227 ARG A CG   1 
ATOM   3557 C CD   . ARG A 1 224 ? 24.284 30.334 60.386 1.00 57.91  ? 227 ARG A CD   1 
ATOM   3558 N NE   . ARG A 1 224 ? 24.990 29.227 61.024 1.00 106.83 ? 227 ARG A NE   1 
ATOM   3559 C CZ   . ARG A 1 224 ? 24.792 27.942 60.753 1.00 114.31 ? 227 ARG A CZ   1 
ATOM   3560 N NH1  . ARG A 1 224 ? 23.873 27.546 59.886 1.00 74.60  ? 227 ARG A NH1  1 
ATOM   3561 N NH2  . ARG A 1 224 ? 25.539 27.029 61.368 1.00 98.52  ? 227 ARG A NH2  1 
ATOM   3562 H H    . ARG A 1 224 ? 25.225 33.382 56.787 0.00 46.02  ? 227 ARG A H    1 
ATOM   3563 H HA   . ARG A 1 224 ? 23.438 31.556 57.561 0.00 61.63  ? 227 ARG A HA   1 
ATOM   3564 H HB2  . ARG A 1 224 ? 25.411 32.979 58.843 0.00 55.07  ? 227 ARG A HB2  1 
ATOM   3565 H HB3  . ARG A 1 224 ? 24.121 32.730 59.736 0.00 55.07  ? 227 ARG A HB3  1 
ATOM   3566 H HG2  . ARG A 1 224 ? 25.140 30.465 58.532 0.00 82.72  ? 227 ARG A HG2  1 
ATOM   3567 H HG3  . ARG A 1 224 ? 26.052 31.084 59.677 0.00 82.72  ? 227 ARG A HG3  1 
ATOM   3568 H HD2  . ARG A 1 224 ? 24.047 30.979 61.071 0.00 69.50  ? 227 ARG A HD2  1 
ATOM   3569 H HD3  . ARG A 1 224 ? 23.482 29.985 59.968 0.00 69.50  ? 227 ARG A HD3  1 
ATOM   3570 H HE   . ARG A 1 224 ? 25.578 29.421 61.620 0.00 128.21 ? 227 ARG A HE   1 
ATOM   3571 H HH11 . ARG A 1 224 ? 23.384 28.127 59.482 0.00 89.53  ? 227 ARG A HH11 1 
ATOM   3572 H HH12 . ARG A 1 224 ? 23.764 26.708 59.728 0.00 89.53  ? 227 ARG A HH12 1 
ATOM   3573 H HH21 . ARG A 1 224 ? 26.139 27.274 61.933 0.00 118.24 ? 227 ARG A HH21 1 
ATOM   3574 H HH22 . ARG A 1 224 ? 25.421 26.194 61.201 0.00 118.24 ? 227 ARG A HH22 1 
ATOM   3575 N N    . ALA A 1 225 ? 22.361 34.390 57.162 1.00 44.16  ? 228 ALA A N    1 
ATOM   3576 C CA   . ALA A 1 225 ? 21.225 35.285 57.339 1.00 43.97  ? 228 ALA A CA   1 
ATOM   3577 C C    . ALA A 1 225 ? 19.904 34.630 56.959 1.00 30.70  ? 228 ALA A C    1 
ATOM   3578 O O    . ALA A 1 225 ? 18.849 35.095 57.403 1.00 42.80  ? 228 ALA A O    1 
ATOM   3579 C CB   . ALA A 1 225 ? 21.426 36.554 56.510 1.00 33.79  ? 228 ALA A CB   1 
ATOM   3580 H H    . ALA A 1 225 ? 22.873 34.595 56.501 0.00 53.00  ? 228 ALA A H    1 
ATOM   3581 H HA   . ALA A 1 225 ? 21.175 35.537 58.274 0.00 52.78  ? 228 ALA A HA   1 
ATOM   3582 H HB1  . ALA A 1 225 ? 20.671 37.146 56.651 0.00 40.56  ? 228 ALA A HB1  1 
ATOM   3583 H HB2  . ALA A 1 225 ? 22.245 36.989 56.792 0.00 40.56  ? 228 ALA A HB2  1 
ATOM   3584 H HB3  . ALA A 1 225 ? 21.486 36.312 55.572 0.00 40.56  ? 228 ALA A HB3  1 
ATOM   3585 N N    . ILE A 1 226 ? 19.935 33.566 56.154 1.00 29.93  ? 229 ILE A N    1 
ATOM   3586 C CA   . ILE A 1 226 ? 18.696 32.929 55.720 1.00 39.70  ? 229 ILE A CA   1 
ATOM   3587 C C    . ILE A 1 226 ? 18.106 32.019 56.791 1.00 36.36  ? 229 ILE A C    1 
ATOM   3588 O O    . ILE A 1 226 ? 16.932 31.640 56.689 1.00 33.97  ? 229 ILE A O    1 
ATOM   3589 C CB   . ILE A 1 226 ? 18.922 32.131 54.423 1.00 43.05  ? 229 ILE A CB   1 
ATOM   3590 C CG1  . ILE A 1 226 ? 19.880 30.959 54.666 1.00 36.09  ? 229 ILE A CG1  1 
ATOM   3591 C CG2  . ILE A 1 226 ? 19.460 33.046 53.331 1.00 28.52  ? 229 ILE A CG2  1 
ATOM   3592 C CD1  . ILE A 1 226 ? 20.125 30.103 53.441 1.00 40.57  ? 229 ILE A CD1  1 
ATOM   3593 H H    . ILE A 1 226 ? 20.651 33.200 55.850 0.00 35.93  ? 229 ILE A H    1 
ATOM   3594 H HA   . ILE A 1 226 ? 18.049 33.629 55.540 0.00 47.65  ? 229 ILE A HA   1 
ATOM   3595 H HB   . ILE A 1 226 ? 18.069 31.769 54.135 0.00 51.68  ? 229 ILE A HB   1 
ATOM   3596 H HG12 . ILE A 1 226 ? 20.736 31.311 54.956 0.00 43.32  ? 229 ILE A HG12 1 
ATOM   3597 H HG13 . ILE A 1 226 ? 19.505 30.388 55.355 0.00 43.32  ? 229 ILE A HG13 1 
ATOM   3598 H HG21 . ILE A 1 226 ? 19.447 32.571 52.485 0.00 34.23  ? 229 ILE A HG21 1 
ATOM   3599 H HG22 . ILE A 1 226 ? 18.899 33.836 53.275 0.00 34.23  ? 229 ILE A HG22 1 
ATOM   3600 H HG23 . ILE A 1 226 ? 20.369 33.301 53.552 0.00 34.23  ? 229 ILE A HG23 1 
ATOM   3601 H HD11 . ILE A 1 226 ? 20.612 29.307 53.704 0.00 48.70  ? 229 ILE A HD11 1 
ATOM   3602 H HD12 . ILE A 1 226 ? 19.271 29.855 53.053 0.00 48.70  ? 229 ILE A HD12 1 
ATOM   3603 H HD13 . ILE A 1 226 ? 20.645 30.612 52.799 0.00 48.70  ? 229 ILE A HD13 1 
ATOM   3604 N N    . PHE A 1 227 ? 18.881 31.654 57.807 1.00 34.62  ? 230 PHE A N    1 
ATOM   3605 C CA   . PHE A 1 227 ? 18.407 30.803 58.888 1.00 31.96  ? 230 PHE A CA   1 
ATOM   3606 C C    . PHE A 1 227 ? 17.951 31.652 60.068 1.00 34.41  ? 230 PHE A C    1 
ATOM   3607 O O    . PHE A 1 227 ? 18.479 32.738 60.319 1.00 32.50  ? 230 PHE A O    1 
ATOM   3608 C CB   . PHE A 1 227 ? 19.502 29.836 59.344 1.00 35.65  ? 230 PHE A CB   1 
ATOM   3609 C CG   . PHE A 1 227 ? 19.903 28.837 58.298 1.00 34.83  ? 230 PHE A CG   1 
ATOM   3610 C CD1  . PHE A 1 227 ? 20.919 29.124 57.402 1.00 45.73  ? 230 PHE A CD1  1 
ATOM   3611 C CD2  . PHE A 1 227 ? 19.266 27.610 58.211 1.00 44.01  ? 230 PHE A CD2  1 
ATOM   3612 C CE1  . PHE A 1 227 ? 21.290 28.207 56.436 1.00 42.43  ? 230 PHE A CE1  1 
ATOM   3613 C CE2  . PHE A 1 227 ? 19.635 26.688 57.249 1.00 43.13  ? 230 PHE A CE2  1 
ATOM   3614 C CZ   . PHE A 1 227 ? 20.648 26.988 56.360 1.00 42.53  ? 230 PHE A CZ   1 
ATOM   3615 H H    . PHE A 1 227 ? 19.702 31.893 57.893 0.00 41.56  ? 230 PHE A H    1 
ATOM   3616 H HA   . PHE A 1 227 ? 17.652 30.281 58.575 0.00 38.37  ? 230 PHE A HA   1 
ATOM   3617 H HB2  . PHE A 1 227 ? 20.291 30.348 59.582 0.00 42.79  ? 230 PHE A HB2  1 
ATOM   3618 H HB3  . PHE A 1 227 ? 19.181 29.343 60.116 0.00 42.79  ? 230 PHE A HB3  1 
ATOM   3619 H HD1  . PHE A 1 227 ? 21.356 29.943 57.450 0.00 54.89  ? 230 PHE A HD1  1 
ATOM   3620 H HD2  . PHE A 1 227 ? 18.582 27.404 58.807 0.00 52.83  ? 230 PHE A HD2  1 
ATOM   3621 H HE1  . PHE A 1 227 ? 21.972 28.412 55.838 0.00 50.93  ? 230 PHE A HE1  1 
ATOM   3622 H HE2  . PHE A 1 227 ? 19.201 25.867 57.200 0.00 51.78  ? 230 PHE A HE2  1 
ATOM   3623 H HZ   . PHE A 1 227 ? 20.897 26.370 55.711 0.00 51.05  ? 230 PHE A HZ   1 
ATOM   3624 N N    . GLY A 1 228 ? 16.959 31.142 60.794 1.00 46.89  ? 231 GLY A N    1 
ATOM   3625 C CA   . GLY A 1 228 ? 16.498 31.827 61.984 1.00 42.35  ? 231 GLY A CA   1 
ATOM   3626 C C    . GLY A 1 228 ? 17.489 31.701 63.126 1.00 52.72  ? 231 GLY A C    1 
ATOM   3627 O O    . GLY A 1 228 ? 18.249 30.737 63.222 1.00 50.79  ? 231 GLY A O    1 
ATOM   3628 H H    . GLY A 1 228 ? 16.545 30.409 60.618 0.00 56.29  ? 231 GLY A H    1 
ATOM   3629 H HA2  . GLY A 1 228 ? 16.374 32.769 61.787 0.00 50.83  ? 231 GLY A HA2  1 
ATOM   3630 H HA3  . GLY A 1 228 ? 15.651 31.449 62.267 0.00 50.83  ? 231 GLY A HA3  1 
ATOM   3631 N N    . GLU A 1 229 ? 17.479 32.700 64.002 1.00 46.11  ? 232 GLU A N    1 
ATOM   3632 C CA   . GLU A 1 229 ? 18.359 32.711 65.170 1.00 58.53  ? 232 GLU A CA   1 
ATOM   3633 C C    . GLU A 1 229 ? 17.870 31.659 66.155 1.00 64.46  ? 232 GLU A C    1 
ATOM   3634 O O    . GLU A 1 229 ? 16.914 31.882 66.902 1.00 77.07  ? 232 GLU A O    1 
ATOM   3635 C CB   . GLU A 1 229 ? 18.384 34.097 65.804 1.00 65.11  ? 232 GLU A CB   1 
ATOM   3636 C CG   . GLU A 1 229 ? 19.775 34.580 66.180 1.00 61.99  ? 232 GLU A CG   1 
ATOM   3637 C CD   . GLU A 1 229 ? 19.745 35.785 67.099 1.00 57.83  ? 232 GLU A CD   1 
ATOM   3638 O OE1  . GLU A 1 229 ? 18.739 36.525 67.080 1.00 59.51  ? 232 GLU A OE1  1 
ATOM   3639 O OE2  . GLU A 1 229 ? 20.727 35.990 67.844 1.00 48.53  ? 232 GLU A OE2  1 
ATOM   3640 H H    . GLU A 1 229 ? 16.969 33.390 63.944 0.00 55.34  ? 232 GLU A H    1 
ATOM   3641 H HA   . GLU A 1 229 ? 19.263 32.488 64.898 0.00 70.25  ? 232 GLU A HA   1 
ATOM   3642 H HB2  . GLU A 1 229 ? 18.010 34.734 65.175 0.00 78.15  ? 232 GLU A HB2  1 
ATOM   3643 H HB3  . GLU A 1 229 ? 17.850 34.078 66.614 0.00 78.15  ? 232 GLU A HB3  1 
ATOM   3644 H HG2  . GLU A 1 229 ? 20.246 33.865 66.636 0.00 74.40  ? 232 GLU A HG2  1 
ATOM   3645 H HG3  . GLU A 1 229 ? 20.252 34.829 65.373 0.00 74.40  ? 232 GLU A HG3  1 
ATOM   3646 N N    . ALA A 1 230 ? 18.525 30.500 66.160 1.00 40.89  ? 233 ALA A N    1 
ATOM   3647 C CA   . ALA A 1 230 ? 18.128 29.380 66.999 1.00 66.88  ? 233 ALA A CA   1 
ATOM   3648 C C    . ALA A 1 230 ? 19.333 28.863 67.772 1.00 69.65  ? 233 ALA A C    1 
ATOM   3649 O O    . ALA A 1 230 ? 20.486 29.101 67.404 1.00 64.49  ? 233 ALA A O    1 
ATOM   3650 C CB   . ALA A 1 230 ? 17.513 28.245 66.168 1.00 84.49  ? 233 ALA A CB   1 
ATOM   3651 H H    . ALA A 1 230 ? 19.215 30.338 65.674 0.00 49.08  ? 233 ALA A H    1 
ATOM   3652 H HA   . ALA A 1 230 ? 17.467 29.682 67.641 0.00 80.28  ? 233 ALA A HA   1 
ATOM   3653 H HB1  . ALA A 1 230 ? 17.264 27.519 66.761 0.00 101.40 ? 233 ALA A HB1  1 
ATOM   3654 H HB2  . ALA A 1 230 ? 16.728 28.580 65.707 0.00 101.40 ? 233 ALA A HB2  1 
ATOM   3655 H HB3  . ALA A 1 230 ? 18.168 27.935 65.523 0.00 101.40 ? 233 ALA A HB3  1 
ATOM   3656 N N    . GLU A 1 231 ? 19.045 28.145 68.853 1.00 70.18  ? 234 GLU A N    1 
ATOM   3657 C CA   . GLU A 1 231 ? 20.083 27.582 69.707 1.00 84.53  ? 234 GLU A CA   1 
ATOM   3658 C C    . GLU A 1 231 ? 20.558 26.236 69.169 1.00 95.10  ? 234 GLU A C    1 
ATOM   3659 O O    . GLU A 1 231 ? 20.395 25.203 69.818 1.00 100.48 ? 234 GLU A O    1 
ATOM   3660 C CB   . GLU A 1 231 ? 19.564 27.426 71.140 1.00 58.14  ? 234 GLU A CB   1 
ATOM   3661 C CG   . GLU A 1 231 ? 20.653 27.262 72.189 1.00 66.20  ? 234 GLU A CG   1 
ATOM   3662 C CD   . GLU A 1 231 ? 21.571 28.466 72.274 1.00 66.04  ? 234 GLU A CD   1 
ATOM   3663 O OE1  . GLU A 1 231 ? 21.086 29.602 72.088 1.00 55.94  ? 234 GLU A OE1  1 
ATOM   3664 O OE2  . GLU A 1 231 ? 22.778 28.276 72.534 1.00 62.94  ? 234 GLU A OE2  1 
ATOM   3665 H H    . GLU A 1 231 ? 18.245 27.968 69.116 0.00 84.24  ? 234 GLU A H    1 
ATOM   3666 H HA   . GLU A 1 231 ? 20.844 28.183 69.727 0.00 101.45 ? 234 GLU A HA   1 
ATOM   3667 H HB2  . GLU A 1 231 ? 19.051 28.216 71.371 0.00 69.78  ? 234 GLU A HB2  1 
ATOM   3668 H HB3  . GLU A 1 231 ? 18.998 26.639 71.180 0.00 69.78  ? 234 GLU A HB3  1 
ATOM   3669 H HG2  . GLU A 1 231 ? 20.239 27.139 73.057 0.00 79.45  ? 234 GLU A HG2  1 
ATOM   3670 H HG3  . GLU A 1 231 ? 21.193 26.488 71.965 0.00 79.45  ? 234 GLU A HG3  1 
HETATM 3671 C C46  . LI1 B 2 .   ? 5.008  61.501 19.949 1.00 58.48  ? 301 LI1 A C46  1 
HETATM 3672 C C47  . LI1 B 2 .   ? 4.109  61.563 21.225 1.00 61.28  ? 301 LI1 A C47  1 
HETATM 3673 C C48  . LI1 B 2 .   ? 4.961  61.247 22.474 1.00 55.83  ? 301 LI1 A C48  1 
HETATM 3674 C C49  . LI1 B 2 .   ? 5.424  59.798 22.417 1.00 54.85  ? 301 LI1 A C49  1 
HETATM 3675 C C50  . LI1 B 2 .   ? 4.125  61.467 23.742 1.00 53.75  ? 301 LI1 A C50  1 
HETATM 3676 C C51  . LI1 B 2 .   ? 4.927  60.977 24.983 1.00 53.31  ? 301 LI1 A C51  1 
HETATM 3677 C C52  . LI1 B 2 .   ? 4.053  61.118 26.259 1.00 59.58  ? 301 LI1 A C52  1 
HETATM 3678 C C53  . LI1 B 2 .   ? 4.951  61.533 27.455 1.00 74.44  ? 301 LI1 A C53  1 
HETATM 3679 C C55  . LI1 B 2 .   ? 6.087  60.495 27.635 1.00 63.05  ? 301 LI1 A C55  1 
HETATM 3680 C C56  . LI1 B 2 .   ? 6.864  60.798 28.941 1.00 91.60  ? 301 LI1 A C56  1 
HETATM 3681 C C57  . LI1 B 2 .   ? 8.175  59.976 28.970 1.00 70.76  ? 301 LI1 A C57  1 
HETATM 3682 C C58  . LI1 B 2 .   ? 9.024  60.383 30.205 1.00 72.65  ? 301 LI1 A C58  1 
HETATM 3683 C C59  . LI1 B 2 .   ? 8.305  61.514 30.982 1.00 87.39  ? 301 LI1 A C59  1 
HETATM 3684 C C60  . LI1 B 2 .   ? 9.220  59.163 31.132 1.00 53.46  ? 301 LI1 A C60  1 
HETATM 3685 H H461 . LI1 B 2 .   ? 5.954  62.005 20.146 1.00 70.19  ? 301 LI1 A H461 1 
HETATM 3686 H H462 . LI1 B 2 .   ? 5.198  60.460 19.686 1.00 70.19  ? 301 LI1 A H462 1 
HETATM 3687 H H471 . LI1 B 2 .   ? 3.683  62.560 21.320 1.00 73.55  ? 301 LI1 A H471 1 
HETATM 3688 H H472 . LI1 B 2 .   ? 3.307  60.833 21.139 1.00 73.55  ? 301 LI1 A H472 1 
HETATM 3689 H H48  . LI1 B 2 .   ? 5.827  61.908 22.496 1.00 67.01  ? 301 LI1 A H48  1 
HETATM 3690 C C50  . LI1 C 2 .   ? 23.794 22.746 24.235 1.00 37.48  ? 302 LI1 A C50  1 
HETATM 3691 C C51  . LI1 C 2 .   ? 22.768 22.466 25.372 1.00 50.28  ? 302 LI1 A C51  1 
HETATM 3692 C C52  . LI1 C 2 .   ? 23.456 22.664 26.750 1.00 60.24  ? 302 LI1 A C52  1 
HETATM 3693 C C53  . LI1 C 2 .   ? 23.343 21.359 27.582 1.00 72.43  ? 302 LI1 A C53  1 
HETATM 3694 C C55  . LI1 C 2 .   ? 22.098 21.427 28.502 1.00 55.28  ? 302 LI1 A C55  1 
HETATM 3695 C C56  . LI1 C 2 .   ? 22.397 20.669 29.820 1.00 70.55  ? 302 LI1 A C56  1 
HETATM 3696 C C57  . LI1 C 2 .   ? 23.587 21.346 30.542 1.00 62.04  ? 302 LI1 A C57  1 
HETATM 3697 C C58  . LI1 C 2 .   ? 24.094 20.431 31.688 1.00 74.88  ? 302 LI1 A C58  1 
HETATM 3698 C C45  . LI1 D 2 .   ? -1.893 30.922 18.777 1.00 46.52  ? 303 LI1 A C45  1 
HETATM 3699 C C46  . LI1 D 2 .   ? -1.054 31.087 20.090 1.00 66.15  ? 303 LI1 A C46  1 
HETATM 3700 C C47  . LI1 D 2 .   ? -2.015 31.375 21.286 1.00 50.74  ? 303 LI1 A C47  1 
HETATM 3701 C C48  . LI1 D 2 .   ? -1.313 31.031 22.617 1.00 32.88  ? 303 LI1 A C48  1 
HETATM 3702 C C50  . LI1 D 2 .   ? -1.726 32.054 23.683 1.00 62.34  ? 303 LI1 A C50  1 
HETATM 3703 C C51  . LI1 D 2 .   ? -1.152 31.633 25.067 1.00 50.49  ? 303 LI1 A C51  1 
HETATM 3704 C C52  . LI1 D 2 .   ? -2.071 30.554 25.700 1.00 42.56  ? 303 LI1 A C52  1 
HETATM 3705 C C53  . LI1 D 2 .   ? -2.051 30.696 27.245 1.00 44.81  ? 303 LI1 A C53  1 
HETATM 3706 C C55  . LI1 D 2 .   ? -2.645 32.069 27.649 1.00 41.59  ? 303 LI1 A C55  1 
HETATM 3707 C C56  . LI1 D 2 .   ? -2.293 32.372 29.128 1.00 40.75  ? 303 LI1 A C56  1 
HETATM 3708 C C57  . LI1 D 2 .   ? -3.202 33.514 29.644 1.00 66.77  ? 303 LI1 A C57  1 
HETATM 3709 C C58  . LI1 D 2 .   ? -2.597 34.123 30.937 1.00 47.14  ? 303 LI1 A C58  1 
HETATM 3710 H H451 . LI1 D 2 .   ? -1.253 31.099 17.914 1.00 55.83  ? 303 LI1 A H451 1 
HETATM 3711 H H452 . LI1 D 2 .   ? -2.710 31.642 18.775 1.00 55.83  ? 303 LI1 A H452 1 
HETATM 3712 H H461 . LI1 D 2 .   ? -0.357 31.917 19.975 1.00 79.39  ? 303 LI1 A H461 1 
HETATM 3713 H H462 . LI1 D 2 .   ? -0.497 30.170 20.284 1.00 79.39  ? 303 LI1 A H462 1 
HETATM 3714 C C45  . LI1 E 2 .   ? 26.639 59.852 53.312 1.00 95.48  ? 304 LI1 A C45  1 
HETATM 3715 C C46  . LI1 E 2 .   ? 25.607 60.385 52.259 1.00 89.54  ? 304 LI1 A C46  1 
HETATM 3716 C C47  . LI1 E 2 .   ? 24.613 59.244 51.877 1.00 84.63  ? 304 LI1 A C47  1 
HETATM 3717 C C48  . LI1 E 2 .   ? 23.610 59.764 50.824 1.00 73.94  ? 304 LI1 A C48  1 
HETATM 3718 C C50  . LI1 E 2 .   ? 24.297 59.819 49.453 1.00 73.88  ? 304 LI1 A C50  1 
HETATM 3719 C C51  . LI1 E 2 .   ? 23.259 60.211 48.362 1.00 59.60  ? 304 LI1 A C51  1 
HETATM 3720 C C52  . LI1 E 2 .   ? 23.109 59.042 47.350 1.00 82.52  ? 304 LI1 A C52  1 
HETATM 3721 C C53  . LI1 E 2 .   ? 22.728 59.599 45.953 1.00 82.75  ? 304 LI1 A C53  1 
HETATM 3722 C C55  . LI1 E 2 .   ? 23.943 60.336 45.335 1.00 52.87  ? 304 LI1 A C55  1 
HETATM 3723 C C56  . LI1 E 2 .   ? 23.580 60.820 43.908 1.00 61.78  ? 304 LI1 A C56  1 
HETATM 3724 C C57  . LI1 E 2 .   ? 23.030 59.632 43.083 1.00 82.88  ? 304 LI1 A C57  1 
HETATM 3725 C C58  . LI1 E 2 .   ? 22.763 60.089 41.624 1.00 86.82  ? 304 LI1 A C58  1 
HETATM 3726 C C59  . LI1 E 2 .   ? 23.325 59.035 40.637 1.00 75.00  ? 304 LI1 A C59  1 
HETATM 3727 H H451 . LI1 E 2 .   ? 26.110 59.345 54.116 1.00 114.59 ? 304 LI1 A H451 1 
HETATM 3728 H H452 . LI1 E 2 .   ? 27.321 59.154 52.829 1.00 114.59 ? 304 LI1 A H452 1 
HETATM 3729 H H461 . LI1 E 2 .   ? 25.054 61.222 52.685 1.00 107.46 ? 304 LI1 A H461 1 
HETATM 3730 H H462 . LI1 E 2 .   ? 26.138 60.718 51.367 1.00 107.46 ? 304 LI1 A H462 1 
HETATM 3731 H H471 . LI1 E 2 .   ? 24.072 58.923 52.765 1.00 101.57 ? 304 LI1 A H471 1 
HETATM 3732 H H472 . LI1 E 2 .   ? 25.167 58.403 51.466 1.00 101.57 ? 304 LI1 A H472 1 
HETATM 3733 C C46  . LI1 F 2 .   ? 26.243 52.386 44.774 1.00 81.10  ? 305 LI1 A C46  1 
HETATM 3734 C C47  . LI1 F 2 .   ? 25.302 53.198 43.827 1.00 92.07  ? 305 LI1 A C47  1 
HETATM 3735 C C48  . LI1 F 2 .   ? 25.394 52.636 42.392 1.00 88.38  ? 305 LI1 A C48  1 
HETATM 3736 C C50  . LI1 F 2 .   ? 26.864 52.532 41.967 1.00 84.93  ? 305 LI1 A C50  1 
HETATM 3737 C C51  . LI1 F 2 .   ? 26.936 52.109 40.472 1.00 62.28  ? 305 LI1 A C51  1 
HETATM 3738 C C52  . LI1 F 2 .   ? 28.414 52.134 39.996 1.00 78.29  ? 305 LI1 A C52  1 
HETATM 3739 C C53  . LI1 F 2 .   ? 28.480 52.758 38.578 1.00 74.48  ? 305 LI1 A C53  1 
HETATM 3740 C C55  . LI1 F 2 .   ? 27.456 52.046 37.659 1.00 63.92  ? 305 LI1 A C55  1 
HETATM 3741 C C56  . LI1 F 2 .   ? 27.994 52.028 36.207 1.00 81.65  ? 305 LI1 A C56  1 
HETATM 3742 C C57  . LI1 F 2 .   ? 27.059 51.169 35.323 1.00 78.66  ? 305 LI1 A C57  1 
HETATM 3743 C C58  . LI1 F 2 .   ? 27.808 50.760 34.027 1.00 90.10  ? 305 LI1 A C58  1 
HETATM 3744 C C59  . LI1 F 2 .   ? 26.780 50.473 32.904 1.00 50.99  ? 305 LI1 A C59  1 
HETATM 3745 C C60  . LI1 F 2 .   ? 28.654 49.494 34.293 1.00 75.38  ? 305 LI1 A C60  1 
HETATM 3746 H H461 . LI1 F 2 .   ? 26.229 51.334 44.487 1.00 97.34  ? 305 LI1 A H461 1 
HETATM 3747 H H462 . LI1 F 2 .   ? 27.260 52.772 44.696 1.00 97.34  ? 305 LI1 A H462 1 
HETATM 3748 H H471 . LI1 F 2 .   ? 25.605 54.243 43.826 1.00 110.50 ? 305 LI1 A H471 1 
HETATM 3749 H H472 . LI1 F 2 .   ? 24.277 53.118 44.181 1.00 110.50 ? 305 LI1 A H472 1 
HETATM 3750 C C18  . OLC G 3 .   ? 20.211 19.246 32.831 1.00 92.74  ? 306 OLC A C18  1 
HETATM 3751 C C10  . OLC G 3 .   ? 12.890 20.981 35.883 1.00 61.30  ? 306 OLC A C10  1 
HETATM 3752 C C9   . OLC G 3 .   ? 12.265 21.023 37.073 1.00 65.01  ? 306 OLC A C9   1 
HETATM 3753 C C17  . OLC G 3 .   ? 19.371 19.928 33.934 1.00 81.34  ? 306 OLC A C17  1 
HETATM 3754 C C11  . OLC G 3 .   ? 13.326 22.180 34.999 1.00 63.70  ? 306 OLC A C11  1 
HETATM 3755 C C8   . OLC G 3 .   ? 11.578 21.748 38.269 1.00 51.07  ? 306 OLC A C8   1 
HETATM 3756 C C24  . OLC G 3 .   ? 11.332 22.765 49.274 1.00 82.44  ? 306 OLC A C24  1 
HETATM 3757 C C16  . OLC G 3 .   ? 18.583 21.110 33.317 1.00 64.50  ? 306 OLC A C16  1 
HETATM 3758 C C12  . OLC G 3 .   ? 14.791 22.551 35.362 1.00 57.99  ? 306 OLC A C12  1 
HETATM 3759 C C7   . OLC G 3 .   ? 12.120 21.135 39.588 1.00 51.85  ? 306 OLC A C7   1 
HETATM 3760 C C15  . OLC G 3 .   ? 18.223 22.150 34.411 1.00 61.56  ? 306 OLC A C15  1 
HETATM 3761 C C13  . OLC G 3 .   ? 15.768 21.551 34.681 1.00 48.78  ? 306 OLC A C13  1 
HETATM 3762 C C6   . OLC G 3 .   ? 11.752 21.963 40.859 1.00 63.66  ? 306 OLC A C6   1 
HETATM 3763 C C14  . OLC G 3 .   ? 17.152 21.597 35.390 1.00 44.19  ? 306 OLC A C14  1 
HETATM 3764 C C5   . OLC G 3 .   ? 12.065 23.487 40.760 1.00 31.63  ? 306 OLC A C5   1 
HETATM 3765 C C4   . OLC G 3 .   ? 11.578 24.143 42.085 1.00 47.77  ? 306 OLC A C4   1 
HETATM 3766 C C3   . OLC G 3 .   ? 12.778 24.315 43.058 1.00 45.98  ? 306 OLC A C3   1 
HETATM 3767 C C2   . OLC G 3 .   ? 12.235 24.722 44.455 1.00 40.05  ? 306 OLC A C2   1 
HETATM 3768 C C21  . OLC G 3 .   ? 13.267 23.549 47.908 1.00 54.31  ? 306 OLC A C21  1 
HETATM 3769 C C1   . OLC G 3 .   ? 13.006 24.008 45.592 1.00 34.34  ? 306 OLC A C1   1 
HETATM 3770 C C22  . OLC G 3 .   ? 12.456 23.805 49.185 1.00 70.57  ? 306 OLC A C22  1 
HETATM 3771 O O19  . OLC G 3 .   ? 13.660 23.041 45.366 1.00 58.93  ? 306 OLC A O19  1 
HETATM 3772 O O25  . OLC G 3 .   ? 10.436 23.115 50.305 1.00 73.21  ? 306 OLC A O25  1 
HETATM 3773 O O23  . OLC G 3 .   ? 13.287 23.688 50.300 1.00 88.46  ? 306 OLC A O23  1 
HETATM 3774 O O20  . OLC G 3 .   ? 12.912 24.496 46.917 1.00 51.10  ? 306 OLC A O20  1 
HETATM 3775 H H18  . OLC G 3 .   ? 20.875 19.978 32.377 0.00 111.31 ? 306 OLC A H18  1 
HETATM 3776 H H18A . OLC G 3 .   ? 20.800 18.443 33.269 0.00 111.31 ? 306 OLC A H18A 1 
HETATM 3777 H H18B . OLC G 3 .   ? 19.548 18.837 32.072 0.00 111.31 ? 306 OLC A H18B 1 
HETATM 3778 H H10  . OLC G 3 .   ? 13.951 20.797 36.035 0.00 73.58  ? 306 OLC A H10  1 
HETATM 3779 H H9   . OLC G 3 .   ? 12.543 22.073 37.116 0.00 78.03  ? 306 OLC A H9   1 
HETATM 3780 H H17  . OLC G 3 .   ? 20.031 20.300 34.717 0.00 97.62  ? 306 OLC A H17  1 
HETATM 3781 H H17A . OLC G 3 .   ? 18.673 19.208 34.359 0.00 97.62  ? 306 OLC A H17A 1 
HETATM 3782 H H11  . OLC G 3 .   ? 13.267 21.901 33.946 0.00 76.45  ? 306 OLC A H11  1 
HETATM 3783 H H11A . OLC G 3 .   ? 12.672 23.033 35.187 0.00 76.45  ? 306 OLC A H11A 1 
HETATM 3784 H H8   . OLC G 3 .   ? 10.499 21.607 38.214 0.00 61.30  ? 306 OLC A H8   1 
HETATM 3785 H H8A  . OLC G 3 .   ? 11.808 22.813 38.236 0.00 61.30  ? 306 OLC A H8A  1 
HETATM 3786 H H24  . OLC G 3 .   ? 11.760 21.787 49.485 0.00 98.94  ? 306 OLC A H24  1 
HETATM 3787 H H24A . OLC G 3 .   ? 10.796 22.730 48.327 0.00 98.94  ? 306 OLC A H24A 1 
HETATM 3788 H H16  . OLC G 3 .   ? 19.195 21.589 32.553 0.00 77.41  ? 306 OLC A H16  1 
HETATM 3789 H H16A . OLC G 3 .   ? 17.666 20.732 32.864 0.00 77.41  ? 306 OLC A H16A 1 
HETATM 3790 H H12  . OLC G 3 .   ? 15.006 23.561 35.014 0.00 69.60  ? 306 OLC A H12  1 
HETATM 3791 H H12A . OLC G 3 .   ? 14.920 22.505 36.442 0.00 69.60  ? 306 OLC A H12A 1 
HETATM 3792 H H7   . OLC G 3 .   ? 11.707 20.132 39.698 0.00 62.24  ? 306 OLC A H7   1 
HETATM 3793 H H7A  . OLC G 3 .   ? 13.206 21.074 39.519 0.00 62.24  ? 306 OLC A H7A  1 
HETATM 3794 H H15  . OLC G 3 .   ? 17.834 23.047 33.932 0.00 73.89  ? 306 OLC A H15  1 
HETATM 3795 H H15A . OLC G 3 .   ? 19.122 22.398 34.973 0.00 73.89  ? 306 OLC A H15A 1 
HETATM 3796 H H13  . OLC G 3 .   ? 15.890 21.821 33.634 0.00 58.55  ? 306 OLC A H13  1 
HETATM 3797 H H13A . OLC G 3 .   ? 15.360 20.544 34.751 0.00 58.55  ? 306 OLC A H13A 1 
HETATM 3798 H H6   . OLC G 3 .   ? 10.683 21.848 41.041 0.00 76.41  ? 306 OLC A H6   1 
HETATM 3799 H H6A  . OLC G 3 .   ? 12.309 21.556 41.703 0.00 76.41  ? 306 OLC A H6A  1 
HETATM 3800 H H14  . OLC G 3 .   ? 17.091 22.246 36.264 0.00 53.04  ? 306 OLC A H14  1 
HETATM 3801 H H14A . OLC G 3 .   ? 17.433 20.591 35.703 0.00 53.04  ? 306 OLC A H14A 1 
HETATM 3802 H H5   . OLC G 3 .   ? 11.538 23.923 39.912 0.00 37.97  ? 306 OLC A H5   1 
HETATM 3803 H H5A  . OLC G 3 .   ? 13.137 23.641 40.640 0.00 37.97  ? 306 OLC A H5A  1 
HETATM 3804 H H4   . OLC G 3 .   ? 11.145 25.119 41.867 0.00 57.33  ? 306 OLC A H4   1 
HETATM 3805 H H4A  . OLC G 3 .   ? 10.824 23.506 42.548 0.00 57.33  ? 306 OLC A H4A  1 
HETATM 3806 H H3   . OLC G 3 .   ? 13.324 23.375 43.136 0.00 55.19  ? 306 OLC A H3   1 
HETATM 3807 H H3A  . OLC G 3 .   ? 13.444 25.092 42.683 0.00 55.19  ? 306 OLC A H3A  1 
HETATM 3808 H H2   . OLC G 3 .   ? 12.342 25.799 44.577 0.00 48.07  ? 306 OLC A H2   1 
HETATM 3809 H H2A  . OLC G 3 .   ? 11.181 24.453 44.518 0.00 48.07  ? 306 OLC A H2A  1 
HETATM 3810 H H21  . OLC G 3 .   ? 14.330 23.640 48.131 0.00 65.19  ? 306 OLC A H21  1 
HETATM 3811 H H21A . OLC G 3 .   ? 13.057 22.544 47.541 0.00 65.19  ? 306 OLC A H21A 1 
HETATM 3812 H H22  . OLC G 3 .   ? 12.033 24.809 49.158 0.00 84.70  ? 306 OLC A H22  1 
HETATM 3813 H HO25 . OLC G 3 .   ? 9.995  22.338 50.617 0.00 87.86  ? 306 OLC A HO25 1 
HETATM 3814 H HO23 . OLC G 3 .   ? 12.838 24.024 51.066 0.00 106.17 ? 306 OLC A HO23 1 
HETATM 3815 C C18  . OLC H 3 .   ? 6.153  32.310 41.768 1.00 52.57  ? 307 OLC A C18  1 
HETATM 3816 C C10  . OLC H 3 .   ? 7.918  29.359 32.518 1.00 52.31  ? 307 OLC A C10  1 
HETATM 3817 C C9   . OLC H 3 .   ? 7.957  29.155 31.189 1.00 54.27  ? 307 OLC A C9   1 
HETATM 3818 C C17  . OLC H 3 .   ? 5.635  32.442 40.319 1.00 55.45  ? 307 OLC A C17  1 
HETATM 3819 C C11  . OLC H 3 .   ? 6.660  29.599 33.392 1.00 41.86  ? 307 OLC A C11  1 
HETATM 3820 C C8   . OLC H 3 .   ? 7.307  28.994 29.783 1.00 67.73  ? 307 OLC A C8   1 
HETATM 3821 C C24  . OLC H 3 .   ? 4.556  32.570 19.098 1.00 79.18  ? 307 OLC A C24  1 
HETATM 3822 C C16  . OLC H 3 .   ? 6.153  31.252 39.474 1.00 49.97  ? 307 OLC A C16  1 
HETATM 3823 C C12  . OLC H 3 .   ? 7.105  29.947 34.842 1.00 39.06  ? 307 OLC A C12  1 
HETATM 3824 C C7   . OLC H 3 .   ? 7.091  30.383 29.125 1.00 56.79  ? 307 OLC A C7   1 
HETATM 3825 C C15  . OLC H 3 .   ? 5.874  31.517 37.973 1.00 49.49  ? 307 OLC A C15  1 
HETATM 3826 C C13  . OLC H 3 .   ? 5.901  30.522 35.640 1.00 29.67  ? 307 OLC A C13  1 
HETATM 3827 C C6   . OLC H 3 .   ? 6.138  30.207 27.907 1.00 74.45  ? 307 OLC A C6   1 
HETATM 3828 C C14  . OLC H 3 .   ? 6.078  30.213 37.156 1.00 48.28  ? 307 OLC A C14  1 
HETATM 3829 C C5   . OLC H 3 .   ? 5.484  31.565 27.527 1.00 57.68  ? 307 OLC A C5   1 
HETATM 3830 C C4   . OLC H 3 .   ? 4.323  31.296 26.525 1.00 50.47  ? 307 OLC A C4   1 
HETATM 3831 C C3   . OLC H 3 .   ? 4.521  32.101 25.212 1.00 59.10  ? 307 OLC A C3   1 
HETATM 3832 C C2   . OLC H 3 .   ? 3.656  31.442 24.105 1.00 54.82  ? 307 OLC A C2   1 
HETATM 3833 C C21  . OLC H 3 .   ? 2.845  33.183 20.840 1.00 55.00  ? 307 OLC A C21  1 
HETATM 3834 C C1   . OLC H 3 .   ? 3.183  32.513 23.097 1.00 69.33  ? 307 OLC A C1   1 
HETATM 3835 C C22  . OLC H 3 .   ? 3.059  32.621 19.428 1.00 82.10  ? 307 OLC A C22  1 
HETATM 3836 O O19  . OLC H 3 .   ? 2.436  33.371 23.444 1.00 84.77  ? 307 OLC A O19  1 
HETATM 3837 O O25  . OLC H 3 .   ? 5.061  33.883 18.993 1.00 84.99  ? 307 OLC A O25  1 
HETATM 3838 O O23  . OLC H 3 .   ? 2.529  31.330 19.367 1.00 87.35  ? 307 OLC A O23  1 
HETATM 3839 O O20  . OLC H 3 .   ? 3.639  32.458 21.759 1.00 62.92  ? 307 OLC A O20  1 
HETATM 3840 H H18  . OLC H 3 .   ? 5.797  33.152 42.358 0.00 63.10  ? 307 OLC A H18  1 
HETATM 3841 H H18A . OLC H 3 .   ? 5.785  31.382 42.201 0.00 63.10  ? 307 OLC A H18A 1 
HETATM 3842 H H18B . OLC H 3 .   ? 7.241  32.303 41.765 0.00 63.10  ? 307 OLC A H18B 1 
HETATM 3843 H H10  . OLC H 3 .   ? 8.015  28.408 33.036 0.00 62.79  ? 307 OLC A H10  1 
HETATM 3844 H H9   . OLC H 3 .   ? 6.955  29.577 31.160 0.00 65.13  ? 307 OLC A H9   1 
HETATM 3845 H H17  . OLC H 3 .   ? 4.546  32.439 40.321 0.00 66.56  ? 307 OLC A H17  1 
HETATM 3846 H H17A . OLC H 3 .   ? 5.995  33.376 39.889 0.00 66.56  ? 307 OLC A H17A 1 
HETATM 3847 H H11  . OLC H 3 .   ? 6.081  30.426 32.980 0.00 50.25  ? 307 OLC A H11  1 
HETATM 3848 H H11A . OLC H 3 .   ? 6.047  28.697 33.405 0.00 50.25  ? 307 OLC A H11A 1 
HETATM 3849 H H8   . OLC H 3 .   ? 6.345  28.492 29.887 0.00 81.29  ? 307 OLC A H8   1 
HETATM 3850 H H8A  . OLC H 3 .   ? 7.962  28.395 29.150 0.00 81.29  ? 307 OLC A H8A  1 
HETATM 3851 H H24  . OLC H 3 .   ? 4.702  32.049 18.154 0.00 95.03  ? 307 OLC A H24  1 
HETATM 3852 H H24A . OLC H 3 .   ? 5.084  32.041 19.890 0.00 95.03  ? 307 OLC A H24A 1 
HETATM 3853 H H16  . OLC H 3 .   ? 7.226  31.137 39.629 0.00 59.98  ? 307 OLC A H16  1 
HETATM 3854 H H16A . OLC H 3 .   ? 5.641  30.340 39.782 0.00 59.98  ? 307 OLC A H16A 1 
HETATM 3855 H H12  . OLC H 3 .   ? 7.468  29.046 35.334 0.00 46.89  ? 307 OLC A H12  1 
HETATM 3856 H H12A . OLC H 3 .   ? 7.903  30.687 34.807 0.00 46.89  ? 307 OLC A H12A 1 
HETATM 3857 H H7   . OLC H 3 .   ? 6.643  31.066 29.847 0.00 68.16  ? 307 OLC A H7   1 
HETATM 3858 H H7A  . OLC H 3 .   ? 8.047  30.784 28.790 0.00 68.16  ? 307 OLC A H7A  1 
HETATM 3859 H H15  . OLC H 3 .   ? 6.560  32.282 37.608 0.00 59.40  ? 307 OLC A H15  1 
HETATM 3860 H H15A . OLC H 3 .   ? 4.849  31.862 37.851 0.00 59.40  ? 307 OLC A H15A 1 
HETATM 3861 H H13  . OLC H 3 .   ? 4.979  30.065 35.284 0.00 35.62  ? 307 OLC A H13  1 
HETATM 3862 H H13A . OLC H 3 .   ? 5.852  31.600 35.494 0.00 35.62  ? 307 OLC A H13A 1 
HETATM 3863 H H6   . OLC H 3 .   ? 6.709  29.833 27.057 0.00 89.35  ? 307 OLC A H6   1 
HETATM 3864 H H6A  . OLC H 3 .   ? 5.357  29.491 28.163 0.00 89.35  ? 307 OLC A H6A  1 
HETATM 3865 H H14  . OLC H 3 .   ? 5.342  29.471 37.465 0.00 57.95  ? 307 OLC A H14  1 
HETATM 3866 H H14A . OLC H 3 .   ? 7.081  29.825 37.333 0.00 57.95  ? 307 OLC A H14A 1 
HETATM 3867 H H5   . OLC H 3 .   ? 5.092  32.047 28.422 0.00 69.23  ? 307 OLC A H5   1 
HETATM 3868 H H5A  . OLC H 3 .   ? 6.227  32.213 27.061 0.00 69.23  ? 307 OLC A H5A  1 
HETATM 3869 H H4   . OLC H 3 .   ? 4.295  30.232 26.290 0.00 60.58  ? 307 OLC A H4   1 
HETATM 3870 H H4A  . OLC H 3 .   ? 3.380  31.592 26.985 0.00 60.58  ? 307 OLC A H4A  1 
HETATM 3871 H H3   . OLC H 3 .   ? 4.207  33.134 25.360 0.00 70.93  ? 307 OLC A H3   1 
HETATM 3872 H H3A  . OLC H 3 .   ? 5.572  32.079 24.921 0.00 70.93  ? 307 OLC A H3A  1 
HETATM 3873 H H2   . OLC H 3 .   ? 4.248  30.692 23.583 0.00 65.80  ? 307 OLC A H2   1 
HETATM 3874 H H2A  . OLC H 3 .   ? 2.788  30.967 24.560 0.00 65.80  ? 307 OLC A H2A  1 
HETATM 3875 H H21  . OLC H 3 .   ? 3.133  34.234 20.860 0.00 66.02  ? 307 OLC A H21  1 
HETATM 3876 H H21A . OLC H 3 .   ? 1.794  33.090 21.113 0.00 66.02  ? 307 OLC A H21A 1 
HETATM 3877 H H22  . OLC H 3 .   ? 2.559  33.266 18.706 0.00 98.53  ? 307 OLC A H22  1 
HETATM 3878 H HO25 . OLC H 3 .   ? 5.659  33.932 18.262 0.00 102.00 ? 307 OLC A HO25 1 
HETATM 3879 H HO23 . OLC H 3 .   ? 2.100  31.126 20.188 0.00 104.84 ? 307 OLC A HO23 1 
HETATM 3880 C C18  . OLC I 3 .   ? 18.208 57.698 41.508 1.00 38.42  ? 308 OLC A C18  1 
HETATM 3881 C C10  . OLC I 3 .   ? 22.711 54.210 37.500 1.00 65.86  ? 308 OLC A C10  1 
HETATM 3882 C C9   . OLC I 3 .   ? 21.984 54.201 36.365 1.00 74.75  ? 308 OLC A C9   1 
HETATM 3883 C C17  . OLC I 3 .   ? 18.344 57.103 42.929 1.00 74.32  ? 308 OLC A C17  1 
HETATM 3884 C C11  . OLC I 3 .   ? 22.460 55.022 38.801 1.00 88.45  ? 308 OLC A C11  1 
HETATM 3885 C C8   . OLC I 3 .   ? 20.772 54.626 35.488 1.00 74.75  ? 308 OLC A C8   1 
HETATM 3886 C C24  . OLC I 3 .   ? 26.052 56.454 24.464 1.00 133.64 ? 308 OLC A C24  1 
HETATM 3887 C C16  . OLC I 3 .   ? 19.043 55.722 42.862 1.00 55.90  ? 308 OLC A C16  1 
HETATM 3888 C C12  . OLC I 3 .   ? 22.697 54.103 40.034 1.00 70.58  ? 308 OLC A C12  1 
HETATM 3889 C C7   . OLC I 3 .   ? 20.909 54.057 34.051 1.00 53.65  ? 308 OLC A C7   1 
HETATM 3890 C C15  . OLC I 3 .   ? 20.566 55.904 42.633 1.00 66.48  ? 308 OLC A C15  1 
HETATM 3891 C C13  . OLC I 3 .   ? 22.522 54.948 41.327 1.00 88.24  ? 308 OLC A C13  1 
HETATM 3892 C C6   . OLC I 3 .   ? 21.545 55.134 33.125 1.00 89.38  ? 308 OLC A C6   1 
HETATM 3893 C C14  . OLC I 3 .   ? 21.183 54.603 42.046 1.00 81.12  ? 308 OLC A C14  1 
HETATM 3894 C C5   . OLC I 3 .   ? 21.486 54.653 31.646 1.00 77.44  ? 308 OLC A C5   1 
HETATM 3895 C C4   . OLC I 3 .   ? 21.505 55.888 30.696 1.00 81.49  ? 308 OLC A C4   1 
HETATM 3896 C C3   . OLC I 3 .   ? 22.638 55.747 29.640 1.00 88.35  ? 308 OLC A C3   1 
HETATM 3897 C C2   . OLC I 3 .   ? 22.301 56.649 28.423 1.00 97.96  ? 308 OLC A C2   1 
HETATM 3898 C C21  . OLC I 3 .   ? 24.876 58.027 26.030 1.00 132.45 ? 308 OLC A C21  1 
HETATM 3899 C C1   . OLC I 3 .   ? 23.585 57.326 27.891 1.00 110.98 ? 308 OLC A C1   1 
HETATM 3900 C C22  . OLC I 3 .   ? 25.166 57.703 24.557 1.00 113.53 ? 308 OLC A C22  1 
HETATM 3901 O O19  . OLC I 3 .   ? 24.166 58.113 28.567 1.00 105.69 ? 308 OLC A O19  1 
HETATM 3902 O O25  . OLC I 3 .   ? 27.391 56.840 24.250 1.00 127.66 ? 308 OLC A O25  1 
HETATM 3903 O O23  . OLC I 3 .   ? 23.964 57.472 23.886 1.00 105.07 ? 308 OLC A O23  1 
HETATM 3904 O O20  . OLC I 3 .   ? 24.063 57.015 26.596 1.00 125.02 ? 308 OLC A O20  1 
HETATM 3905 H H18  . OLC I 3 .   ? 17.587 58.592 41.547 0.00 46.11  ? 308 OLC A H18  1 
HETATM 3906 H H18A . OLC I 3 .   ? 19.193 57.958 41.127 0.00 46.11  ? 308 OLC A H18A 1 
HETATM 3907 H H18B . OLC I 3 .   ? 17.746 56.965 40.850 0.00 46.11  ? 308 OLC A H18B 1 
HETATM 3908 H H10  . OLC I 3 .   ? 23.585 54.841 37.364 0.00 79.05  ? 308 OLC A H10  1 
HETATM 3909 H H9   . OLC I 3 .   ? 21.515 55.107 36.740 0.00 89.72  ? 308 OLC A H9   1 
HETATM 3910 H H17  . OLC I 3 .   ? 17.354 56.985 43.367 0.00 89.20  ? 308 OLC A H17  1 
HETATM 3911 H H17A . OLC I 3 .   ? 18.936 57.777 43.546 0.00 89.20  ? 308 OLC A H17A 1 
HETATM 3912 H H11  . OLC I 3 .   ? 21.432 55.387 38.811 0.00 106.16 ? 308 OLC A H11  1 
HETATM 3913 H H11A . OLC I 3 .   ? 23.147 55.869 38.841 0.00 106.16 ? 308 OLC A H11A 1 
HETATM 3914 H H8   . OLC I 3 .   ? 20.729 55.714 35.440 0.00 89.71  ? 308 OLC A H8   1 
HETATM 3915 H H8A  . OLC I 3 .   ? 19.854 54.246 35.937 0.00 89.71  ? 308 OLC A H8A  1 
HETATM 3916 H H24  . OLC I 3 .   ? 25.717 55.834 23.634 0.00 160.38 ? 308 OLC A H24  1 
HETATM 3917 H H24A . OLC I 3 .   ? 25.981 55.889 25.392 0.00 160.38 ? 308 OLC A H24A 1 
HETATM 3918 H H16  . OLC I 3 .   ? 18.621 55.144 42.039 0.00 67.09  ? 308 OLC A H16  1 
HETATM 3919 H H16A . OLC I 3 .   ? 18.881 55.190 43.800 0.00 67.09  ? 308 OLC A H16A 1 
HETATM 3920 H H12  . OLC I 3 .   ? 21.974 53.288 40.027 0.00 84.71  ? 308 OLC A H12  1 
HETATM 3921 H H12A . OLC I 3 .   ? 23.705 53.694 39.997 0.00 84.71  ? 308 OLC A H12A 1 
HETATM 3922 H H7   . OLC I 3 .   ? 21.545 53.173 34.070 0.00 64.39  ? 308 OLC A H7   1 
HETATM 3923 H H7A  . OLC I 3 .   ? 19.923 53.788 33.671 0.00 64.39  ? 308 OLC A H7A  1 
HETATM 3924 H H15  . OLC I 3 .   ? 21.047 56.134 43.582 0.00 79.79  ? 308 OLC A H15  1 
HETATM 3925 H H15A . OLC I 3 .   ? 20.729 56.725 41.936 0.00 79.79  ? 308 OLC A H15A 1 
HETATM 3926 H H13  . OLC I 3 .   ? 22.522 56.005 41.065 0.00 105.90 ? 308 OLC A H13  1 
HETATM 3927 H H13A . OLC I 3 .   ? 23.351 54.741 42.002 0.00 105.90 ? 308 OLC A H13A 1 
HETATM 3928 H H6   . OLC I 3 .   ? 20.993 56.069 33.224 0.00 107.28 ? 308 OLC A H6   1 
HETATM 3929 H H6A  . OLC I 3 .   ? 22.584 55.293 33.413 0.00 107.28 ? 308 OLC A H6A  1 
HETATM 3930 H H14  . OLC I 3 .   ? 20.489 54.161 41.331 0.00 97.35  ? 308 OLC A H14  1 
HETATM 3931 H H14A . OLC I 3 .   ? 21.374 53.895 42.852 0.00 97.35  ? 308 OLC A H14A 1 
HETATM 3932 H H5   . OLC I 3 .   ? 20.571 54.085 31.485 0.00 92.95  ? 308 OLC A H5   1 
HETATM 3933 H H5A  . OLC I 3 .   ? 22.349 54.020 31.436 0.00 92.95  ? 308 OLC A H5A  1 
HETATM 3934 H H4   . OLC I 3 .   ? 20.545 55.961 30.184 0.00 97.81  ? 308 OLC A H4   1 
HETATM 3935 H H4A  . OLC I 3 .   ? 21.672 56.790 31.283 0.00 97.81  ? 308 OLC A H4A  1 
HETATM 3936 H H3   . OLC I 3 .   ? 23.587 56.059 30.077 0.00 106.04 ? 308 OLC A H3   1 
HETATM 3937 H H3A  . OLC I 3 .   ? 22.711 54.708 29.318 0.00 106.04 ? 308 OLC A H3A  1 
HETATM 3938 H H2   . OLC I 3 .   ? 21.861 56.041 27.634 0.00 117.57 ? 308 OLC A H2   1 
HETATM 3939 H H2A  . OLC I 3 .   ? 21.590 57.416 28.728 0.00 117.57 ? 308 OLC A H2A  1 
HETATM 3940 H H21  . OLC I 3 .   ? 25.816 58.084 26.579 0.00 158.96 ? 308 OLC A H21  1 
HETATM 3941 H H21A . OLC I 3 .   ? 24.359 58.984 26.094 0.00 158.96 ? 308 OLC A H21A 1 
HETATM 3942 H H22  . OLC I 3 .   ? 25.685 58.546 24.100 0.00 136.25 ? 308 OLC A H22  1 
HETATM 3943 H HO25 . OLC I 3 .   ? 27.551 57.672 24.672 0.00 153.20 ? 308 OLC A HO25 1 
HETATM 3944 H HO23 . OLC I 3 .   ? 23.378 56.981 24.448 0.00 126.10 ? 308 OLC A HO23 1 
HETATM 3945 C C18  . OLC J 3 .   ? 35.447 35.675 35.472 1.00 81.03  ? 309 OLC A C18  1 
HETATM 3946 C C10  . OLC J 3 .   ? 33.826 40.533 28.176 1.00 83.37  ? 309 OLC A C10  1 
HETATM 3947 C C9   . OLC J 3 .   ? 33.239 41.061 27.094 1.00 57.46  ? 309 OLC A C9   1 
HETATM 3948 C C17  . OLC J 3 .   ? 36.010 34.848 34.297 1.00 77.18  ? 309 OLC A C17  1 
HETATM 3949 C C11  . OLC J 3 .   ? 33.225 39.474 29.133 1.00 70.55  ? 309 OLC A C11  1 
HETATM 3950 C C8   . OLC J 3 .   ? 33.204 42.002 25.856 1.00 75.58  ? 309 OLC A C8   1 
HETATM 3951 C C24  . OLC J 3 .   ? 31.317 46.257 15.740 1.00 90.17  ? 309 OLC A C24  1 
HETATM 3952 C C16  . OLC J 3 .   ? 35.294 35.257 32.988 1.00 71.06  ? 309 OLC A C16  1 
HETATM 3953 C C12  . OLC J 3 .   ? 34.300 38.378 29.386 1.00 72.26  ? 309 OLC A C12  1 
HETATM 3954 C C7   . OLC J 3 .   ? 33.666 41.220 24.597 1.00 76.75  ? 309 OLC A C7   1 
HETATM 3955 C C15  . OLC J 3 .   ? 35.847 36.609 32.470 1.00 59.71  ? 309 OLC A C15  1 
HETATM 3956 C C13  . OLC J 3 .   ? 34.422 38.033 30.894 1.00 79.40  ? 309 OLC A C13  1 
HETATM 3957 C C6   . OLC J 3 .   ? 34.236 42.237 23.568 1.00 73.27  ? 309 OLC A C6   1 
HETATM 3958 C C14  . OLC J 3 .   ? 35.374 36.809 31.007 1.00 74.19  ? 309 OLC A C14  1 
HETATM 3959 C C5   . OLC J 3 .   ? 34.628 41.532 22.237 1.00 56.30  ? 309 OLC A C5   1 
HETATM 3960 C C4   . OLC J 3 .   ? 34.729 42.627 21.135 1.00 68.48  ? 309 OLC A C4   1 
HETATM 3961 C C3   . OLC J 3 .   ? 34.663 42.018 19.707 1.00 63.41  ? 309 OLC A C3   1 
HETATM 3962 C C2   . OLC J 3 .   ? 33.981 43.078 18.802 1.00 92.05  ? 309 OLC A C2   1 
HETATM 3963 C C21  . OLC J 3 .   ? 32.714 44.391 16.606 1.00 107.47 ? 309 OLC A C21  1 
HETATM 3964 C C1   . OLC J 3 .   ? 34.472 43.002 17.336 1.00 105.41 ? 309 OLC A C1   1 
HETATM 3965 C C22  . OLC J 3 .   ? 32.075 44.985 15.345 1.00 93.06  ? 309 OLC A C22  1 
HETATM 3966 O O19  . OLC J 3 .   ? 35.599 42.709 17.091 1.00 76.93  ? 309 OLC A O19  1 
HETATM 3967 O O25  . OLC J 3 .   ? 32.236 47.259 16.112 1.00 102.98 ? 309 OLC A O25  1 
HETATM 3968 O O23  . OLC J 3 .   ? 33.066 45.299 14.415 1.00 109.64 ? 309 OLC A O23  1 
HETATM 3969 O O20  . OLC J 3 .   ? 33.572 43.309 16.286 1.00 124.86 ? 309 OLC A O20  1 
HETATM 3970 H H18  . OLC J 3 .   ? 35.838 35.285 36.409 0.00 97.25  ? 309 OLC A H18  1 
HETATM 3971 H H18A . OLC J 3 .   ? 35.745 36.715 35.359 0.00 97.25  ? 309 OLC A H18A 1 
HETATM 3972 H H18B . OLC J 3 .   ? 34.361 35.607 35.475 0.00 97.25  ? 309 OLC A H18B 1 
HETATM 3973 H H10  . OLC J 3 .   ? 34.533 39.765 27.872 0.00 100.06 ? 309 OLC A H10  1 
HETATM 3974 H H9   . OLC J 3 .   ? 34.238 41.364 26.790 0.00 68.96  ? 309 OLC A H9   1 
HETATM 3975 H H17  . OLC J 3 .   ? 37.078 35.036 34.200 0.00 92.63  ? 309 OLC A H17  1 
HETATM 3976 H H17A . OLC J 3 .   ? 35.843 33.788 34.486 0.00 92.63  ? 309 OLC A H17A 1 
HETATM 3977 H H11  . OLC J 3 .   ? 32.949 39.945 30.078 0.00 84.68  ? 309 OLC A H11  1 
HETATM 3978 H H11A . OLC J 3 .   ? 32.341 39.026 28.678 0.00 84.68  ? 309 OLC A H11A 1 
HETATM 3979 H H8   . OLC J 3 .   ? 33.872 42.847 26.023 0.00 90.72  ? 309 OLC A H8   1 
HETATM 3980 H H8A  . OLC J 3 .   ? 32.188 42.366 25.705 0.00 90.72  ? 309 OLC A H8A  1 
HETATM 3981 H H24  . OLC J 3 .   ? 30.657 46.041 16.579 0.00 108.22 ? 309 OLC A H24  1 
HETATM 3982 H H24A . OLC J 3 .   ? 30.726 46.604 14.893 0.00 108.22 ? 309 OLC A H24A 1 
HETATM 3983 H H16  . OLC J 3 .   ? 35.458 34.488 32.233 0.00 85.28  ? 309 OLC A H16  1 
HETATM 3984 H H16A . OLC J 3 .   ? 34.225 35.355 33.179 0.00 85.28  ? 309 OLC A H16A 1 
HETATM 3985 H H12  . OLC J 3 .   ? 34.023 37.479 28.839 0.00 86.72  ? 309 OLC A H12  1 
HETATM 3986 H H12A . OLC J 3 .   ? 35.263 38.739 29.027 0.00 86.72  ? 309 OLC A H12A 1 
HETATM 3987 H H7   . OLC J 3 .   ? 34.439 40.503 24.872 0.00 92.11  ? 309 OLC A H7   1 
HETATM 3988 H H7A  . OLC J 3 .   ? 32.818 40.692 24.161 0.00 92.11  ? 309 OLC A H7A  1 
HETATM 3989 H H15  . OLC J 3 .   ? 36.936 36.598 32.506 0.00 71.67  ? 309 OLC A H15  1 
HETATM 3990 H H15A . OLC J 3 .   ? 35.472 37.421 33.092 0.00 71.67  ? 309 OLC A H15A 1 
HETATM 3991 H H13  . OLC J 3 .   ? 33.443 37.784 31.301 0.00 95.30  ? 309 OLC A H13  1 
HETATM 3992 H H13A . OLC J 3 .   ? 34.835 38.880 31.439 0.00 95.30  ? 309 OLC A H13A 1 
HETATM 3993 H H6   . OLC J 3 .   ? 33.479 42.994 23.360 0.00 87.94  ? 309 OLC A H6   1 
HETATM 3994 H H6A  . OLC J 3 .   ? 35.119 42.714 23.992 0.00 87.94  ? 309 OLC A H6A  1 
HETATM 3995 H H14  . OLC J 3 .   ? 34.846 35.915 30.676 0.00 89.05  ? 309 OLC A H14  1 
HETATM 3996 H H14A . OLC J 3 .   ? 36.243 36.974 30.370 0.00 89.05  ? 309 OLC A H14A 1 
HETATM 3997 H H5   . OLC J 3 .   ? 33.867 40.801 21.966 0.00 67.58  ? 309 OLC A H5   1 
HETATM 3998 H H5A  . OLC J 3 .   ? 35.589 41.031 22.352 0.00 67.58  ? 309 OLC A H5A  1 
HETATM 3999 H H4   . OLC J 3 .   ? 33.903 43.328 21.258 0.00 82.19  ? 309 OLC A H4   1 
HETATM 4000 H H4A  . OLC J 3 .   ? 35.675 43.156 21.250 0.00 82.19  ? 309 OLC A H4A  1 
HETATM 4001 H H3   . OLC J 3 .   ? 35.668 41.803 19.343 0.00 76.11  ? 309 OLC A H3   1 
HETATM 4002 H H3A  . OLC J 3 .   ? 34.076 41.099 19.717 0.00 76.11  ? 309 OLC A H3A  1 
HETATM 4003 H H2   . OLC J 3 .   ? 32.905 42.914 18.820 0.00 110.48 ? 309 OLC A H2   1 
HETATM 4004 H H2A  . OLC J 3 .   ? 34.204 44.069 19.195 0.00 110.48 ? 309 OLC A H2A  1 
HETATM 4005 H H21  . OLC J 3 .   ? 33.291 45.166 17.111 0.00 128.98 ? 309 OLC A H21  1 
HETATM 4006 H H21A . OLC J 3 .   ? 31.926 44.035 17.270 0.00 128.98 ? 309 OLC A H21A 1 
HETATM 4007 H H22  . OLC J 3 .   ? 31.392 44.262 14.899 0.00 111.68 ? 309 OLC A H22  1 
HETATM 4008 H HO25 . OLC J 3 .   ? 32.846 47.408 15.404 0.00 123.60 ? 309 OLC A HO25 1 
HETATM 4009 H HO23 . OLC J 3 .   ? 33.650 44.558 14.312 0.00 131.58 ? 309 OLC A HO23 1 
HETATM 4010 C C46  . LI1 K 2 .   ? 15.399 58.546 16.146 1.00 51.25  ? 310 LI1 A C46  1 
HETATM 4011 C C47  . LI1 K 2 .   ? 15.666 58.743 17.672 1.00 65.97  ? 310 LI1 A C47  1 
HETATM 4012 C C48  . LI1 K 2 .   ? 15.258 60.173 18.088 1.00 78.23  ? 310 LI1 A C48  1 
HETATM 4013 C C49  . LI1 K 2 .   ? 16.459 60.891 18.688 1.00 75.75  ? 310 LI1 A C49  1 
HETATM 4014 C C50  . LI1 K 2 .   ? 14.134 60.098 19.129 1.00 50.68  ? 310 LI1 A C50  1 
HETATM 4015 C C51  . LI1 K 2 .   ? 14.748 60.173 20.556 1.00 56.42  ? 310 LI1 A C51  1 
HETATM 4016 C C52  . LI1 K 2 .   ? 13.796 59.473 21.564 1.00 58.11  ? 310 LI1 A C52  1 
HETATM 4017 C C53  . LI1 K 2 .   ? 13.910 60.156 22.952 1.00 36.39  ? 310 LI1 A C53  1 
HETATM 4018 C C55  . LI1 K 2 .   ? 13.677 59.097 24.059 1.00 58.67  ? 310 LI1 A C55  1 
HETATM 4019 C C56  . LI1 K 2 .   ? 12.695 59.654 25.119 1.00 53.75  ? 310 LI1 A C56  1 
HETATM 4020 C C57  . LI1 K 2 .   ? 13.047 61.128 25.426 1.00 67.00  ? 310 LI1 A C57  1 
HETATM 4021 C C58  . LI1 K 2 .   ? 12.831 61.403 26.938 1.00 66.19  ? 310 LI1 A C58  1 
HETATM 4022 C C59  . LI1 K 2 .   ? 11.397 61.942 27.166 1.00 54.55  ? 310 LI1 A C59  1 
HETATM 4023 C C60  . LI1 K 2 .   ? 13.853 62.459 27.414 1.00 76.42  ? 310 LI1 A C60  1 
HETATM 4024 H H461 . LI1 K 2 .   ? 14.402 58.910 15.900 1.00 61.52  ? 310 LI1 A H461 1 
HETATM 4025 H H462 . LI1 K 2 .   ? 15.470 57.486 15.899 1.00 61.52  ? 310 LI1 A H462 1 
HETATM 4026 H H471 . LI1 K 2 .   ? 16.724 58.594 17.876 1.00 79.17  ? 310 LI1 A H471 1 
HETATM 4027 H H472 . LI1 K 2 .   ? 15.082 58.020 18.238 1.00 79.17  ? 310 LI1 A H472 1 
HETATM 4028 H H48  . LI1 K 2 .   ? 14.909 60.721 17.213 1.00 93.90  ? 310 LI1 A H48  1 
HETATM 4029 C C50  . LI1 L 2 .   ? 9.679  59.277 46.403 1.00 59.77  ? 311 LI1 A C50  1 
HETATM 4030 C C51  . LI1 L 2 .   ? 10.911 59.691 45.526 1.00 76.40  ? 311 LI1 A C51  1 
HETATM 4031 C C52  . LI1 L 2 .   ? 10.885 58.897 44.181 1.00 58.27  ? 311 LI1 A C52  1 
HETATM 4032 C C53  . LI1 L 2 .   ? 12.053 59.363 43.284 1.00 50.67  ? 311 LI1 A C53  1 
HETATM 4033 C C55  . LI1 L 2 .   ? 11.895 58.758 41.883 1.00 66.69  ? 311 LI1 A C55  1 
HETATM 4034 C C56  . LI1 L 2 .   ? 13.273 58.743 41.162 1.00 62.38  ? 311 LI1 A C56  1 
HETATM 4035 C C57  . LI1 L 2 .   ? 13.062 58.522 39.639 1.00 58.91  ? 311 LI1 A C57  1 
HETATM 4036 C C58  . LI1 L 2 .   ? 11.668 57.889 39.389 1.00 53.11  ? 311 LI1 A C58  1 
HETATM 4037 H H501 . LI1 L 2 .   ? 10.025 58.727 47.276 1.00 71.73  ? 311 LI1 A H501 1 
HETATM 4038 H H502 . LI1 L 2 .   ? 9.013  58.645 45.818 1.00 71.73  ? 311 LI1 A H502 1 
HETATM 4039 H H511 . LI1 L 2 .   ? 11.831 59.464 46.063 1.00 91.69  ? 311 LI1 A H511 1 
HETATM 4040 H H512 . LI1 L 2 .   ? 10.865 60.760 45.317 1.00 91.69  ? 311 LI1 A H512 1 
HETATM 4041 H H521 . LI1 L 2 .   ? 9.941  59.079 43.671 1.00 69.94  ? 311 LI1 A H521 1 
HETATM 4042 H H522 . LI1 L 2 .   ? 10.987 57.834 44.386 1.00 69.94  ? 311 LI1 A H522 1 
HETATM 4043 C C45  . LI1 M 2 .   ? 30.798 33.763 46.791 1.00 62.16  ? 312 LI1 A C45  1 
HETATM 4044 C C46  . LI1 M 2 .   ? 30.233 33.364 45.384 1.00 76.98  ? 312 LI1 A C46  1 
HETATM 4045 C C47  . LI1 M 2 .   ? 31.387 33.373 44.333 1.00 87.50  ? 312 LI1 A C47  1 
HETATM 4046 C C48  . LI1 M 2 .   ? 31.430 34.743 43.622 1.00 89.60  ? 312 LI1 A C48  1 
HETATM 4047 C C50  . LI1 M 2 .   ? 30.682 34.658 42.284 1.00 76.89  ? 312 LI1 A C50  1 
HETATM 4048 C C51  . LI1 M 2 .   ? 29.437 35.591 42.327 1.00 73.04  ? 312 LI1 A C51  1 
HETATM 4049 C C52  . LI1 M 2 .   ? 29.893 37.054 42.584 1.00 81.18  ? 312 LI1 A C52  1 
HETATM 4050 C C53  . LI1 M 2 .   ? 29.255 37.998 41.530 1.00 66.30  ? 312 LI1 A C53  1 
HETATM 4051 C C55  . LI1 M 2 .   ? 29.664 37.544 40.107 1.00 69.90  ? 312 LI1 A C55  1 
HETATM 4052 C C56  . LI1 M 2 .   ? 29.896 38.790 39.216 1.00 69.85  ? 312 LI1 A C56  1 
HETATM 4053 H H451 . LI1 M 2 .   ? 29.973 34.011 47.455 1.00 74.61  ? 312 LI1 A H451 1 
HETATM 4054 H H452 . LI1 M 2 .   ? 31.453 34.627 46.688 1.00 74.61  ? 312 LI1 A H452 1 
HETATM 4055 H H461 . LI1 M 2 .   ? 29.799 32.366 45.437 1.00 92.39  ? 312 LI1 A H461 1 
HETATM 4056 H H462 . LI1 M 2 .   ? 29.466 34.079 45.086 1.00 92.39  ? 312 LI1 A H462 1 
HETATM 4057 H H471 . LI1 M 2 .   ? 31.214 32.589 43.598 1.00 105.02 ? 312 LI1 A H471 1 
HETATM 4058 H H472 . LI1 M 2 .   ? 32.336 33.196 44.835 1.00 105.02 ? 312 LI1 A H472 1 
HETATM 4059 C C45  . LI1 N 2 .   ? 29.965 27.021 45.539 1.00 79.66  ? 313 LI1 A C45  1 
HETATM 4060 C C46  . LI1 N 2 .   ? 30.201 27.241 44.007 1.00 68.25  ? 313 LI1 A C46  1 
HETATM 4061 C C47  . LI1 N 2 .   ? 28.946 26.743 43.228 1.00 74.59  ? 313 LI1 A C47  1 
HETATM 4062 C C48  . LI1 N 2 .   ? 29.244 25.437 42.468 1.00 61.36  ? 313 LI1 A C48  1 
HETATM 4063 C C50  . LI1 N 2 .   ? 29.075 25.740 40.975 1.00 70.01  ? 313 LI1 A C50  1 
HETATM 4064 C C51  . LI1 N 2 .   ? 27.644 25.359 40.497 1.00 65.33  ? 313 LI1 A C51  1 
HETATM 4065 C C52  . LI1 N 2 .   ? 27.369 26.024 39.120 1.00 39.38  ? 313 LI1 A C52  1 
HETATM 4066 C C53  . LI1 N 2 .   ? 28.011 27.436 39.132 1.00 75.00  ? 313 LI1 A C53  1 
HETATM 4067 C C55  . LI1 N 2 .   ? 27.884 28.105 37.741 1.00 48.43  ? 313 LI1 A C55  1 
HETATM 4068 C C56  . LI1 N 2 .   ? 28.804 29.349 37.694 1.00 61.77  ? 313 LI1 A C56  1 
HETATM 4069 C C57  . LI1 N 2 .   ? 28.597 30.198 38.971 1.00 50.45  ? 313 LI1 A C57  1 
HETATM 4070 C C58  . LI1 N 2 .   ? 28.944 31.680 38.666 1.00 53.23  ? 313 LI1 A C58  1 
HETATM 4071 C C59  . LI1 N 2 .   ? 29.911 32.231 39.740 1.00 54.60  ? 313 LI1 A C59  1 
HETATM 4072 H H451 . LI1 N 2 .   ? 29.645 25.996 45.707 1.00 95.61  ? 313 LI1 A H451 1 
HETATM 4073 H H452 . LI1 N 2 .   ? 29.186 27.700 45.881 1.00 95.61  ? 313 LI1 A H452 1 
HETATM 4074 H H461 . LI1 N 2 .   ? 31.077 26.679 43.686 1.00 81.92  ? 313 LI1 A H461 1 
HETATM 4075 H H462 . LI1 N 2 .   ? 30.350 28.304 43.811 1.00 81.92  ? 313 LI1 A H462 1 
HETATM 4076 H H471 . LI1 N 2 .   ? 28.647 27.506 42.512 1.00 89.52  ? 313 LI1 A H471 1 
HETATM 4077 H H472 . LI1 N 2 .   ? 28.135 26.570 43.935 1.00 89.52  ? 313 LI1 A H472 1 
HETATM 4078 C C50  . LI1 O 2 .   ? 28.879 25.488 24.276 1.00 46.76  ? 314 LI1 A C50  1 
HETATM 4079 C C51  . LI1 O 2 .   ? 28.690 23.959 24.496 1.00 53.91  ? 314 LI1 A C51  1 
HETATM 4080 C C52  . LI1 O 2 .   ? 28.031 23.717 25.881 1.00 46.77  ? 314 LI1 A C52  1 
HETATM 4081 C C53  . LI1 O 2 .   ? 28.862 22.672 26.670 1.00 72.05  ? 314 LI1 A C53  1 
HETATM 4082 C C55  . LI1 O 2 .   ? 28.661 22.893 28.190 1.00 69.55  ? 314 LI1 A C55  1 
HETATM 4083 C C56  . LI1 O 2 .   ? 30.008 23.317 28.828 1.00 91.47  ? 314 LI1 A C56  1 
HETATM 4084 C C57  . LI1 O 2 .   ? 29.866 23.356 30.368 1.00 75.49  ? 314 LI1 A C57  1 
HETATM 4085 C C58  . LI1 O 2 .   ? 30.865 24.389 30.954 1.00 60.65  ? 314 LI1 A C58  1 
HETATM 4086 C C45  . LI1 P 2 .   ? 2.766  40.120 46.776 1.00 43.66  ? 315 LI1 A C45  1 
HETATM 4087 C C46  . LI1 P 2 .   ? 4.123  39.336 46.765 1.00 44.31  ? 315 LI1 A C46  1 
HETATM 4088 C C47  . LI1 P 2 .   ? 4.237  38.517 45.441 1.00 63.69  ? 315 LI1 A C47  1 
HETATM 4089 C C48  . LI1 P 2 .   ? 5.687  38.579 44.913 1.00 59.41  ? 315 LI1 A C48  1 
HETATM 4090 C C50  . LI1 P 2 .   ? 5.664  38.843 43.403 1.00 49.14  ? 315 LI1 A C50  1 
HETATM 4091 C C51  . LI1 P 2 .   ? 5.209  37.557 42.655 1.00 46.14  ? 315 LI1 A C51  1 
HETATM 4092 C C52  . LI1 P 2 .   ? 6.456  36.735 42.231 1.00 45.97  ? 315 LI1 A C52  1 
HETATM 4093 C C53  . LI1 P 2 .   ? 6.260  36.225 40.780 1.00 60.70  ? 315 LI1 A C53  1 
HETATM 4094 C C55  . LI1 P 2 .   ? 5.909  37.420 39.859 1.00 53.63  ? 315 LI1 A C55  1 
HETATM 4095 C C56  . LI1 P 2 .   ? 4.873  36.965 38.801 1.00 70.14  ? 315 LI1 A C56  1 
HETATM 4096 C C57  . LI1 P 2 .   ? 4.823  37.992 37.645 1.00 58.10  ? 315 LI1 A C57  1 
HETATM 4097 C C58  . LI1 P 2 .   ? 4.657  39.422 38.225 1.00 52.65  ? 315 LI1 A C58  1 
HETATM 4098 C C59  . LI1 P 2 .   ? 3.415  40.093 37.586 1.00 62.38  ? 315 LI1 A C59  1 
HETATM 4099 C C46  . LI1 Q 2 .   ? 30.876 32.848 34.010 1.00 91.79  ? 316 LI1 A C46  1 
HETATM 4100 C C47  . LI1 Q 2 .   ? 30.526 33.596 32.685 1.00 56.48  ? 316 LI1 A C47  1 
HETATM 4101 C C48  . LI1 Q 2 .   ? 31.460 33.113 31.553 1.00 90.95  ? 316 LI1 A C48  1 
HETATM 4102 C C50  . LI1 Q 2 .   ? 31.426 31.580 31.480 1.00 108.98 ? 316 LI1 A C50  1 
HETATM 4103 C C51  . LI1 Q 2 .   ? 32.649 31.068 30.667 1.00 94.49  ? 316 LI1 A C51  1 
HETATM 4104 C C52  . LI1 Q 2 .   ? 32.637 29.515 30.640 1.00 96.85  ? 316 LI1 A C52  1 
HETATM 4105 C C53  . LI1 Q 2 .   ? 34.092 28.983 30.724 1.00 89.19  ? 316 LI1 A C53  1 
HETATM 4106 C C55  . LI1 Q 2 .   ? 34.086 27.443 30.557 1.00 94.64  ? 316 LI1 A C55  1 
HETATM 4107 C C56  . LI1 Q 2 .   ? 34.113 27.090 29.049 1.00 84.44  ? 316 LI1 A C56  1 
HETATM 4108 C C57  . LI1 Q 2 .   ? 33.623 25.635 28.852 1.00 85.34  ? 316 LI1 A C57  1 
HETATM 4109 C C58  . LI1 Q 2 .   ? 33.824 25.219 27.371 1.00 96.32  ? 316 LI1 A C58  1 
HETATM 4110 C C59  . LI1 Q 2 .   ? 34.373 26.424 26.566 1.00 75.77  ? 316 LI1 A C59  1 
HETATM 4111 C C60  . LI1 Q 2 .   ? 32.469 24.777 26.774 1.00 84.32  ? 316 LI1 A C60  1 
HETATM 4112 C C52  . LI1 R 2 .   ? 30.036 20.403 45.223 1.00 90.09  ? 317 LI1 A C52  1 
HETATM 4113 C C53  . LI1 R 2 .   ? 29.791 19.622 46.560 1.00 66.55  ? 317 LI1 A C53  1 
HETATM 4114 C C55  . LI1 R 2 .   ? 28.292 19.196 46.653 1.00 77.10  ? 317 LI1 A C55  1 
HETATM 4115 C C56  . LI1 R 2 .   ? 27.811 18.680 45.280 1.00 77.02  ? 317 LI1 A C56  1 
HETATM 4116 C C57  . LI1 R 2 .   ? 26.915 19.734 44.617 1.00 54.57  ? 317 LI1 A C57  1 
HETATM 4117 C C58  . LI1 R 2 .   ? 26.442 19.212 43.229 1.00 61.41  ? 317 LI1 A C58  1 
HETATM 4118 C C1   . RET S 4 .   ? 14.957 46.384 29.637 1.00 22.18  ? 318 RET A C1   1 
HETATM 4119 C C2   . RET S 4 .   ? 14.494 47.282 28.481 1.00 22.01  ? 318 RET A C2   1 
HETATM 4120 C C3   . RET S 4 .   ? 15.296 48.571 28.384 1.00 21.48  ? 318 RET A C3   1 
HETATM 4121 C C4   . RET S 4 .   ? 15.124 49.401 29.641 1.00 18.19  ? 318 RET A C4   1 
HETATM 4122 C C5   . RET S 4 .   ? 15.102 48.568 30.893 1.00 23.40  ? 318 RET A C5   1 
HETATM 4123 C C6   . RET S 4 .   ? 15.297 47.240 30.862 1.00 15.95  ? 318 RET A C6   1 
HETATM 4124 C C7   . RET S 4 .   ? 15.768 46.537 32.071 1.00 16.80  ? 318 RET A C7   1 
HETATM 4125 C C8   . RET S 4 .   ? 15.940 45.248 32.353 1.00 17.34  ? 318 RET A C8   1 
HETATM 4126 C C9   . RET S 4 .   ? 16.417 44.699 33.612 1.00 15.56  ? 318 RET A C9   1 
HETATM 4127 C C10  . RET S 4 .   ? 16.609 43.364 33.728 1.00 13.83  ? 318 RET A C10  1 
HETATM 4128 C C11  . RET S 4 .   ? 17.205 42.674 34.820 1.00 18.06  ? 318 RET A C11  1 
HETATM 4129 C C12  . RET S 4 .   ? 17.435 41.360 34.897 1.00 17.76  ? 318 RET A C12  1 
HETATM 4130 C C13  . RET S 4 .   ? 18.302 40.704 35.860 1.00 30.16  ? 318 RET A C13  1 
HETATM 4131 C C14  . RET S 4 .   ? 18.588 39.394 35.691 1.00 39.11  ? 318 RET A C14  1 
HETATM 4132 C C15  . RET S 4 .   ? 17.766 38.280 35.299 1.00 28.27  ? 318 RET A C15  1 
HETATM 4133 C C16  . RET S 4 .   ? 16.187 45.614 29.143 1.00 20.80  ? 318 RET A C16  1 
HETATM 4134 C C17  . RET S 4 .   ? 13.820 45.402 29.944 1.00 15.62  ? 318 RET A C17  1 
HETATM 4135 C C18  . RET S 4 .   ? 14.905 49.372 32.148 1.00 20.47  ? 318 RET A C18  1 
HETATM 4136 C C19  . RET S 4 .   ? 16.816 45.668 34.690 1.00 15.65  ? 318 RET A C19  1 
HETATM 4137 C C20  . RET S 4 .   ? 19.161 41.586 36.722 1.00 37.98  ? 318 RET A C20  1 
HETATM 4138 H H21  . RET S 4 .   ? 14.582 46.803 27.632 1.00 26.42  ? 318 RET A H21  1 
HETATM 4139 H H22  . RET S 4 .   ? 13.544 47.496 28.577 1.00 26.42  ? 318 RET A H22  1 
HETATM 4140 H H31  . RET S 4 .   ? 14.996 49.086 27.609 1.00 25.80  ? 318 RET A H31  1 
HETATM 4141 H H32  . RET S 4 .   ? 16.244 48.374 28.237 1.00 25.80  ? 318 RET A H32  1 
HETATM 4142 H H41  . RET S 4 .   ? 14.286 49.905 29.589 1.00 21.84  ? 318 RET A H41  1 
HETATM 4143 H H42  . RET S 4 .   ? 15.852 50.054 29.685 1.00 21.84  ? 318 RET A H42  1 
HETATM 4144 H H7   . RET S 4 .   ? 16.058 47.168 32.760 1.00 20.17  ? 318 RET A H7   1 
HETATM 4145 H H8   . RET S 4 .   ? 15.806 44.596 31.638 1.00 20.82  ? 318 RET A H8   1 
HETATM 4146 H H10  . RET S 4 .   ? 16.333 42.800 32.977 1.00 16.61  ? 318 RET A H10  1 
HETATM 4147 H H11  . RET S 4 .   ? 17.365 43.192 35.633 1.00 21.69  ? 318 RET A H11  1 
HETATM 4148 H H12  . RET S 4 .   ? 17.001 40.785 34.234 1.00 21.32  ? 318 RET A H12  1 
HETATM 4149 H H14  . RET S 4 .   ? 19.515 39.113 35.832 1.00 46.95  ? 318 RET A H14  1 
HETATM 4150 H H15  . RET S 4 .   ? 16.816 38.431 35.115 1.00 33.94  ? 318 RET A H15  1 
HETATM 4151 H H161 . RET S 4 .   ? 15.986 45.095 28.338 1.00 24.97  ? 318 RET A H161 1 
HETATM 4152 H H162 . RET S 4 .   ? 16.909 46.232 28.909 1.00 24.97  ? 318 RET A H162 1 
HETATM 4153 H H163 . RET S 4 .   ? 16.542 44.994 29.810 1.00 24.97  ? 318 RET A H163 1 
HETATM 4154 H H171 . RET S 4 .   ? 13.033 45.880 30.276 1.00 18.76  ? 318 RET A H171 1 
HETATM 4155 H H172 . RET S 4 .   ? 14.058 44.734 30.618 1.00 18.76  ? 318 RET A H172 1 
HETATM 4156 H H173 . RET S 4 .   ? 13.552 44.926 29.133 1.00 18.76  ? 318 RET A H173 1 
HETATM 4157 H H181 . RET S 4 .   ? 14.306 50.139 32.035 1.00 24.58  ? 318 RET A H181 1 
HETATM 4158 H H182 . RET S 4 .   ? 15.766 49.712 32.467 1.00 24.58  ? 318 RET A H182 1 
HETATM 4159 H H183 . RET S 4 .   ? 14.518 48.808 32.849 1.00 24.58  ? 318 RET A H183 1 
HETATM 4160 H H191 . RET S 4 .   ? 17.602 46.178 34.404 1.00 18.79  ? 318 RET A H191 1 
HETATM 4161 H H192 . RET S 4 .   ? 16.127 46.338 34.882 1.00 18.79  ? 318 RET A H192 1 
HETATM 4162 H H193 . RET S 4 .   ? 17.011 45.224 35.540 1.00 18.79  ? 318 RET A H193 1 
HETATM 4163 H H201 . RET S 4 .   ? 18.703 42.413 36.972 1.00 45.60  ? 318 RET A H201 1 
HETATM 4164 H H202 . RET S 4 .   ? 19.431 41.123 37.542 1.00 45.60  ? 318 RET A H202 1 
HETATM 4165 H H203 . RET S 4 .   ? 19.995 41.828 36.270 1.00 45.60  ? 318 RET A H203 1 
HETATM 4166 O O    . HOH T 5 .   ? 21.832 19.500 51.720 1.00 46.11  ? 401 HOH A O    1 
HETATM 4167 O O    . HOH T 5 .   ? 22.903 35.093 67.160 1.00 48.90  ? 402 HOH A O    1 
HETATM 4168 O O    . HOH T 5 .   ? 15.494 41.326 23.457 1.00 31.16  ? 403 HOH A O    1 
HETATM 4169 O O    . HOH T 5 .   ? 25.687 40.084 14.825 1.00 50.61  ? 404 HOH A O    1 
HETATM 4170 O O    . HOH T 5 .   ? 16.915 23.701 46.622 1.00 32.96  ? 405 HOH A O    1 
HETATM 4171 O O    . HOH T 5 .   ? 22.892 45.640 16.491 1.00 38.92  ? 406 HOH A O    1 
HETATM 4172 O O    . HOH T 5 .   ? 18.347 35.255 32.104 1.00 26.05  ? 407 HOH A O    1 
HETATM 4173 O O    . HOH T 5 .   ? 18.145 36.892 28.718 1.00 23.93  ? 408 HOH A O    1 
HETATM 4174 O O    . HOH T 5 .   ? 20.628 25.009 11.324 1.00 73.08  ? 409 HOH A O    1 
HETATM 4175 O O    . HOH T 5 .   ? 10.641 31.677 15.990 1.00 50.30  ? 410 HOH A O    1 
HETATM 4176 O O    . HOH T 5 .   ? 19.319 29.595 74.152 1.00 38.92  ? 411 HOH A O    1 
HETATM 4177 O O    . HOH T 5 .   ? 23.859 42.312 14.663 1.00 42.73  ? 412 HOH A O    1 
HETATM 4178 O O    . HOH T 5 .   ? 18.823 26.547 11.935 1.00 63.06  ? 413 HOH A O    1 
HETATM 4179 O O    . HOH T 5 .   ? 16.617 34.588 29.188 1.00 21.11  ? 414 HOH A O    1 
HETATM 4180 O O    . HOH T 5 .   ? 19.240 37.575 69.649 1.00 32.37  ? 415 HOH A O    1 
HETATM 4181 O O    . HOH T 5 .   ? 8.711  28.422 54.562 1.00 29.79  ? 416 HOH A O    1 
HETATM 4182 O O    . HOH T 5 .   ? 4.586  51.750 20.555 1.00 17.01  ? 417 HOH A O    1 
HETATM 4183 O O    . HOH T 5 .   ? 8.349  49.496 10.540 1.00 43.39  ? 418 HOH A O    1 
HETATM 4184 O O    . HOH T 5 .   ? 22.316 35.995 26.211 1.00 22.34  ? 419 HOH A O    1 
HETATM 4185 O O    . HOH T 5 .   ? 20.318 35.669 14.322 1.00 51.29  ? 420 HOH A O    1 
HETATM 4186 O O    . HOH T 5 .   ? 17.153 40.496 20.140 1.00 28.37  ? 421 HOH A O    1 
HETATM 4187 O O    . HOH T 5 .   ? 19.147 46.374 14.829 1.00 55.65  ? 422 HOH A O    1 
HETATM 4188 O O    . HOH T 5 .   ? 21.426 31.429 65.857 1.00 54.57  ? 423 HOH A O    1 
HETATM 4189 O O    . HOH T 5 .   ? 28.058 29.374 14.370 1.00 56.88  ? 424 HOH A O    1 
HETATM 4190 O O    . HOH T 5 .   ? 20.450 24.016 67.100 1.00 56.13  ? 425 HOH A O    1 
HETATM 4191 O O    . HOH T 5 .   ? 8.457  33.236 17.945 1.00 49.57  ? 426 HOH A O    1 
HETATM 4192 O O    . HOH T 5 .   ? 18.945 40.052 22.488 1.00 43.36  ? 427 HOH A O    1 
HETATM 4193 O O    . HOH T 5 .   ? 19.055 48.691 15.562 1.00 52.49  ? 428 HOH A O    1 
HETATM 4194 O O    . HOH T 5 .   ? 7.405  31.247 18.556 1.00 51.33  ? 429 HOH A O    1 
HETATM 4195 O O    . HOH T 5 .   ? 20.555 40.492 40.992 1.00 29.42  ? 430 HOH A O    1 
HETATM 4196 O O    . HOH T 5 .   ? 10.367 50.031 8.428  1.00 60.12  ? 431 HOH A O    1 
HETATM 4197 O O    . HOH T 5 .   ? 11.092 32.842 14.127 1.00 48.71  ? 432 HOH A O    1 
HETATM 4198 O O    . HOH T 5 .   ? 8.848  61.347 16.615 1.00 53.75  ? 433 HOH A O    1 
HETATM 4199 O O    . HOH T 5 .   ? 22.697 28.840 64.649 1.00 68.11  ? 434 HOH A O    1 
HETATM 4200 O O    . HOH T 5 .   ? 18.083 34.868 12.474 1.00 43.19  ? 435 HOH A O    1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . ALA A 1   ? 1.5708 1.5321 1.2904 -0.0401 0.0547  -0.1090 4   ALA A N   
2    C CA  . ALA A 1   ? 1.2173 1.2271 1.0077 -0.0284 0.0452  -0.0803 4   ALA A CA  
3    C C   . ALA A 1   ? 1.2681 1.2885 1.0924 0.0016  0.0668  -0.0674 4   ALA A C   
4    O O   . ALA A 1   ? 1.1016 1.1557 0.9772 0.0097  0.0627  -0.0452 4   ALA A O   
5    C CB  . ALA A 1   ? 1.1676 1.1649 0.9929 -0.0340 0.0332  -0.0805 4   ALA A CB  
6    N N   . THR A 2   ? 1.3184 1.3092 1.1120 0.0170  0.0915  -0.0812 5   THR A N   
7    C CA  . THR A 2   ? 1.0479 1.0563 0.8759 0.0444  0.1137  -0.0679 5   THR A CA  
8    C C   . THR A 2   ? 1.0014 1.0497 0.8254 0.0466  0.1210  -0.0510 5   THR A C   
9    O O   . THR A 2   ? 0.9400 1.0099 0.7940 0.0650  0.1399  -0.0375 5   THR A O   
10   C CB  . THR A 2   ? 1.2198 1.1839 1.0212 0.0660  0.1417  -0.0855 5   THR A CB  
11   O OG1 . THR A 2   ? 1.5130 1.4429 1.2385 0.0584  0.1532  -0.1066 5   THR A OG1 
12   C CG2 . THR A 2   ? 1.0065 0.9287 0.8159 0.0679  0.1374  -0.0970 5   THR A CG2 
19   N N   . GLY A 3   ? 0.9132 0.9762 0.7021 0.0277  0.1064  -0.0486 6   GLY A N   
20   C CA  . GLY A 3   ? 0.7728 0.8736 0.5575 0.0307  0.1127  -0.0279 6   GLY A CA  
21   C C   . GLY A 3   ? 0.9722 1.1093 0.8195 0.0358  0.1082  0.0020  6   GLY A C   
22   O O   . GLY A 3   ? 1.1197 1.2812 0.9734 0.0428  0.1215  0.0214  6   GLY A O   
26   N N   . ARG A 4   ? 0.6814 0.8171 0.5704 0.0313  0.0921  0.0056  7   ARG A N   
27   C CA  . ARG A 4   ? 0.6002 0.7570 0.5405 0.0339  0.0896  0.0300  7   ARG A CA  
28   C C   . ARG A 4   ? 0.3938 0.5487 0.3745 0.0444  0.1045  0.0305  7   ARG A C   
29   O O   . ARG A 4   ? 0.3973 0.5340 0.3892 0.0481  0.1025  0.0154  7   ARG A O   
30   C CB  . ARG A 4   ? 0.5008 0.6563 0.4616 0.0247  0.0679  0.0336  7   ARG A CB  
31   C CG  . ARG A 4   ? 0.5354 0.7058 0.4647 0.0126  0.0499  0.0359  7   ARG A CG  
32   C CD  . ARG A 4   ? 0.6178 0.7886 0.5704 0.0048  0.0313  0.0367  7   ARG A CD  
33   N NE  . ARG A 4   ? 0.7997 0.9461 0.7319 -0.0075 0.0230  0.0104  7   ARG A NE  
34   C CZ  . ARG A 4   ? 0.6328 0.7635 0.5882 -0.0114 0.0153  0.0035  7   ARG A CZ  
35   N NH1 . ARG A 4   ? 0.3603 0.4975 0.3578 -0.0039 0.0142  0.0187  7   ARG A NH1 
36   N NH2 . ARG A 4   ? 0.6758 0.7783 0.6063 -0.0239 0.0104  -0.0194 7   ARG A NH2 
50   N N   . PRO A 5   ? 0.3936 0.5699 0.3974 0.0478  0.1190  0.0493  8   PRO A N   
51   C CA  . PRO A 5   ? 0.4244 0.6117 0.4695 0.0536  0.1310  0.0515  8   PRO A CA  
52   C C   . PRO A 5   ? 0.3204 0.5000 0.4032 0.0469  0.1160  0.0499  8   PRO A C   
53   O O   . PRO A 5   ? 0.3453 0.5350 0.4568 0.0521  0.1203  0.0472  8   PRO A O   
54   C CB  . PRO A 5   ? 0.3234 0.5362 0.3836 0.0500  0.1465  0.0749  8   PRO A CB  
55   C CG  . PRO A 5   ? 0.5087 0.7159 0.5440 0.0435  0.1391  0.0881  8   PRO A CG  
56   C CD  . PRO A 5   ? 0.4053 0.5995 0.3979 0.0453  0.1257  0.0715  8   PRO A CD  
64   N N   . GLU A 6   ? 0.2705 0.4360 0.3535 0.0370  0.0997  0.0532  9   GLU A N   
65   C CA  . GLU A 6   ? 0.1915 0.3456 0.3027 0.0303  0.0874  0.0508  9   GLU A CA  
66   C C   . GLU A 6   ? 0.2612 0.3978 0.3657 0.0347  0.0766  0.0320  9   GLU A C   
67   O O   . GLU A 6   ? 0.1729 0.2999 0.2964 0.0301  0.0664  0.0296  9   GLU A O   
68   C CB  . GLU A 6   ? 0.3212 0.4629 0.4327 0.0224  0.0796  0.0629  9   GLU A CB  
69   C CG  . GLU A 6   ? 0.2190 0.3559 0.3054 0.0245  0.0676  0.0606  9   GLU A CG  
70   C CD  . GLU A 6   ? 0.3556 0.5092 0.4149 0.0277  0.0723  0.0728  9   GLU A CD  
71   O OE1 . GLU A 6   ? 0.3477 0.5121 0.3994 0.0306  0.0866  0.0763  9   GLU A OE1 
72   O OE2 . GLU A 6   ? 0.2995 0.4607 0.3456 0.0275  0.0618  0.0809  9   GLU A OE2 
79   N N   . TRP A 7   ? 0.1970 0.3239 0.2699 0.0422  0.0802  0.0184  10  TRP A N   
80   C CA  . TRP A 7   ? 0.1982 0.2982 0.2585 0.0438  0.0720  0.0010  10  TRP A CA  
81   C C   . TRP A 7   ? 0.1839 0.2835 0.2738 0.0536  0.0748  -0.0002 10  TRP A C   
82   O O   . TRP A 7   ? 0.1938 0.2737 0.2865 0.0519  0.0643  -0.0070 10  TRP A O   
83   C CB  . TRP A 7   ? 0.2460 0.3257 0.2589 0.0475  0.0799  -0.0155 10  TRP A CB  
84   C CG  . TRP A 7   ? 0.4662 0.5414 0.4749 0.0672  0.1021  -0.0209 10  TRP A CG  
85   C CD1 . TRP A 7   ? 0.5323 0.6277 0.5350 0.0774  0.1216  -0.0144 10  TRP A CD1 
86   C CD2 . TRP A 7   ? 0.4423 0.4927 0.4535 0.0829  0.1101  -0.0306 10  TRP A CD2 
87   N NE1 . TRP A 7   ? 0.5145 0.6025 0.5182 0.0998  0.1424  -0.0195 10  TRP A NE1 
88   C CE2 . TRP A 7   ? 0.5864 0.6458 0.5952 0.1050  0.1357  -0.0287 10  TRP A CE2 
89   C CE3 . TRP A 7   ? 0.5889 0.6107 0.6038 0.0824  0.1000  -0.0381 10  TRP A CE3 
90   C CZ2 . TRP A 7   ? 0.6629 0.7039 0.6746 0.1301  0.1523  -0.0326 10  TRP A CZ2 
91   C CZ3 . TRP A 7   ? 0.4711 0.4711 0.4861 0.1051  0.1151  -0.0421 10  TRP A CZ3 
92   C CH2 . TRP A 7   ? 0.6575 0.6674 0.6717 0.1303  0.1412  -0.0387 10  TRP A CH2 
103  N N   . ILE A 8   ? 0.2350 0.3618 0.3485 0.0635  0.0886  0.0091  11  ILE A N   
104  C CA  . ILE A 8   ? 0.2198 0.3591 0.3643 0.0745  0.0900  0.0124  11  ILE A CA  
105  C C   . ILE A 8   ? 0.1764 0.3184 0.3458 0.0596  0.0712  0.0173  11  ILE A C   
106  O O   . ILE A 8   ? 0.2132 0.3478 0.3913 0.0653  0.0639  0.0149  11  ILE A O   
107  C CB  . ILE A 8   ? 0.2228 0.4022 0.3914 0.0826  0.1045  0.0249  11  ILE A CB  
108  C CG1 . ILE A 8   ? 0.3350 0.5299 0.5292 0.0887  0.0971  0.0296  11  ILE A CG1 
109  C CG2 . ILE A 8   ? 0.2578 0.4611 0.4425 0.0618  0.1015  0.0379  11  ILE A CG2 
110  C CD1 . ILE A 8   ? 0.3653 0.5284 0.5431 0.1088  0.0992  0.0200  11  ILE A CD1 
122  N N   . TRP A 9   ? 0.1683 0.3160 0.3444 0.0415  0.0653  0.0248  12  TRP A N   
123  C CA  . TRP A 9   ? 0.1427 0.2846 0.3337 0.0267  0.0512  0.0272  12  TRP A CA  
124  C C   . TRP A 9   ? 0.2437 0.3517 0.4143 0.0253  0.0400  0.0175  12  TRP A C   
125  O O   . TRP A 9   ? 0.1548 0.2540 0.3324 0.0205  0.0299  0.0157  12  TRP A O   
126  C CB  . TRP A 9   ? 0.1027 0.2490 0.3008 0.0091  0.0539  0.0377  12  TRP A CB  
127  C CG  . TRP A 9   ? 0.1723 0.3508 0.3857 0.0063  0.0656  0.0479  12  TRP A CG  
128  C CD1 . TRP A 9   ? 0.1846 0.3663 0.3899 0.0029  0.0779  0.0570  12  TRP A CD1 
129  C CD2 . TRP A 9   ? 0.1471 0.3561 0.3787 0.0066  0.0643  0.0500  12  TRP A CD2 
130  N NE1 . TRP A 9   ? 0.1921 0.4020 0.4101 -0.0006 0.0847  0.0629  12  TRP A NE1 
131  C CE2 . TRP A 9   ? 0.1462 0.3759 0.3825 0.0017  0.0764  0.0589  12  TRP A CE2 
132  C CE3 . TRP A 9   ? 0.1590 0.3824 0.4039 0.0116  0.0543  0.0474  12  TRP A CE3 
133  C CZ2 . TRP A 9   ? 0.3424 0.6088 0.5999 0.0006  0.0789  0.0645  12  TRP A CZ2 
134  C CZ3 . TRP A 9   ? 0.2066 0.4680 0.4717 0.0122  0.0562  0.0546  12  TRP A CZ3 
135  C CH2 . TRP A 9   ? 0.2006 0.4841 0.4736 0.0063  0.0684  0.0627  12  TRP A CH2 
146  N N   . LEU A 10  ? 0.1506 0.2440 0.2958 0.0276  0.0411  0.0123  13  LEU A N   
147  C CA  . LEU A 10  ? 0.2208 0.2910 0.3506 0.0238  0.0307  0.0050  13  LEU A CA  
148  C C   . LEU A 10  ? 0.1242 0.1761 0.2470 0.0312  0.0287  -0.0058 13  LEU A C   
149  O O   . LEU A 10  ? 0.1319 0.1674 0.2541 0.0269  0.0200  -0.0085 13  LEU A O   
150  C CB  . LEU A 10  ? 0.1642 0.2345 0.2700 0.0202  0.0300  0.0045  13  LEU A CB  
151  C CG  . LEU A 10  ? 0.2156 0.3015 0.3255 0.0172  0.0330  0.0200  13  LEU A CG  
152  C CD1 . LEU A 10  ? 0.1803 0.2769 0.2654 0.0150  0.0297  0.0221  13  LEU A CD1 
153  C CD2 . LEU A 10  ? 0.1461 0.2233 0.2714 0.0131  0.0293  0.0285  13  LEU A CD2 
165  N N   . ALA A 11  ? 0.1740 0.2248 0.2891 0.0445  0.0398  -0.0106 14  ALA A N   
166  C CA  . ALA A 11  ? 0.2571 0.2820 0.3626 0.0564  0.0427  -0.0184 14  ALA A CA  
167  C C   . ALA A 11  ? 0.2571 0.2964 0.3922 0.0629  0.0374  -0.0085 14  ALA A C   
168  O O   . ALA A 11  ? 0.1567 0.1728 0.2862 0.0662  0.0325  -0.0106 14  ALA A O   
169  C CB  . ALA A 11  ? 0.2046 0.2202 0.2913 0.0739  0.0614  -0.0247 14  ALA A CB  
175  N N   . LEU A 12  ? 0.2386 0.3176 0.4035 0.0622  0.0376  0.0033  15  LEU A N   
176  C CA  . LEU A 12  ? 0.2293 0.3313 0.4208 0.0631  0.0289  0.0136  15  LEU A CA  
177  C C   . LEU A 12  ? 0.2428 0.3293 0.4296 0.0448  0.0137  0.0117  15  LEU A C   
178  O O   . LEU A 12  ? 0.1455 0.2270 0.3337 0.0475  0.0054  0.0143  15  LEU A O   
179  C CB  . LEU A 12  ? 0.2475 0.3967 0.4647 0.0581  0.0310  0.0251  15  LEU A CB  
180  C CG  . LEU A 12  ? 0.4098 0.5920 0.6459 0.0548  0.0201  0.0352  15  LEU A CG  
181  C CD1 . LEU A 12  ? 0.5586 0.7355 0.7911 0.0792  0.0221  0.0383  15  LEU A CD1 
182  C CD2 . LEU A 12  ? 0.3480 0.5725 0.6036 0.0456  0.0236  0.0435  15  LEU A CD2 
194  N N   . GLY A 13  ? 0.1237 0.2015 0.3026 0.0290  0.0121  0.0089  16  GLY A N   
195  C CA  . GLY A 13  ? 0.1071 0.1650 0.2774 0.0163  0.0033  0.0069  16  GLY A CA  
196  C C   . GLY A 13  ? 0.1750 0.2046 0.3278 0.0210  0.0002  0.0007  16  GLY A C   
197  O O   . GLY A 13  ? 0.2480 0.2662 0.3971 0.0171  -0.0066 0.0013  16  GLY A O   
201  N N   . THR A 14  ? 0.1567 0.1733 0.2948 0.0262  0.0055  -0.0056 17  THR A N   
202  C CA  . THR A 14  ? 0.1362 0.1236 0.2560 0.0254  0.0033  -0.0121 17  THR A CA  
203  C C   . THR A 14  ? 0.2718 0.2467 0.3927 0.0371  0.0028  -0.0094 17  THR A C   
204  O O   . THR A 14  ? 0.1481 0.1054 0.2623 0.0330  -0.0023 -0.0081 17  THR A O   
205  C CB  . THR A 14  ? 0.2585 0.2316 0.3561 0.0247  0.0093  -0.0218 17  THR A CB  
206  O OG1 . THR A 14  ? 0.2186 0.2099 0.3147 0.0142  0.0072  -0.0201 17  THR A OG1 
207  C CG2 . THR A 14  ? 0.2769 0.2146 0.3525 0.0178  0.0077  -0.0295 17  THR A CG2 
215  N N   . ALA A 15  ? 0.2167 0.2038 0.3469 0.0540  0.0097  -0.0055 18  ALA A N   
216  C CA  . ALA A 15  ? 0.4173 0.3976 0.5508 0.0712  0.0107  0.0023  18  ALA A CA  
217  C C   . ALA A 15  ? 0.2873 0.2906 0.4360 0.0647  -0.0031 0.0130  18  ALA A C   
218  O O   . ALA A 15  ? 0.2390 0.2249 0.3791 0.0691  -0.0071 0.0182  18  ALA A O   
219  C CB  . ALA A 15  ? 0.2630 0.2626 0.4082 0.0943  0.0231  0.0086  18  ALA A CB  
225  N N   . LEU A 16  ? 0.2193 0.2577 0.3857 0.0519  -0.0097 0.0161  19  LEU A N   
226  C CA  . LEU A 16  ? 0.1856 0.2430 0.3582 0.0408  -0.0231 0.0232  19  LEU A CA  
227  C C   . LEU A 16  ? 0.2074 0.2318 0.3572 0.0283  -0.0275 0.0173  19  LEU A C   
228  O O   . LEU A 16  ? 0.1523 0.1753 0.2942 0.0271  -0.0357 0.0231  19  LEU A O   
229  C CB  . LEU A 16  ? 0.2904 0.3818 0.4795 0.0236  -0.0269 0.0246  19  LEU A CB  
230  C CG  . LEU A 16  ? 0.2627 0.4039 0.4821 0.0327  -0.0249 0.0361  19  LEU A CG  
231  C CD1 . LEU A 16  ? 0.1300 0.2966 0.3623 0.0096  -0.0258 0.0360  19  LEU A CD1 
232  C CD2 . LEU A 16  ? 0.2315 0.4051 0.4619 0.0418  -0.0354 0.0506  19  LEU A CD2 
244  N N   . MET A 17  ? 0.1577 0.1604 0.2970 0.0201  -0.0215 0.0084  20  MET A N   
245  C CA  . MET A 17  ? 0.2010 0.1790 0.3233 0.0113  -0.0222 0.0058  20  MET A CA  
246  C C   . MET A 17  ? 0.1562 0.1103 0.2664 0.0189  -0.0214 0.0077  20  MET A C   
247  O O   . MET A 17  ? 0.2343 0.1751 0.3320 0.0147  -0.0238 0.0109  20  MET A O   
248  C CB  . MET A 17  ? 0.1808 0.1526 0.3013 0.0044  -0.0154 0.0012  20  MET A CB  
249  C CG  . MET A 17  ? 0.1787 0.1630 0.3064 -0.0023 -0.0126 0.0015  20  MET A CG  
250  S SD  . MET A 17  ? 0.1671 0.1361 0.2801 -0.0149 -0.0127 0.0008  20  MET A SD  
251  C CE  . MET A 17  ? 0.1566 0.1293 0.2753 -0.0238 -0.0056 0.0010  20  MET A CE  
261  N N   . GLY A 18  ? 0.1586 0.1012 0.2675 0.0293  -0.0156 0.0055  21  GLY A N   
262  C CA  . GLY A 18  ? 0.2464 0.1551 0.3389 0.0350  -0.0120 0.0072  21  GLY A CA  
263  C C   . GLY A 18  ? 0.4021 0.3130 0.4948 0.0487  -0.0161 0.0205  21  GLY A C   
264  O O   . GLY A 18  ? 0.3457 0.2337 0.4235 0.0473  -0.0166 0.0262  21  GLY A O   
268  N N   . LEU A 19  ? 0.3274 0.2717 0.4383 0.0618  -0.0194 0.0285  22  LEU A N   
269  C CA  . LEU A 19  ? 0.2634 0.2238 0.3783 0.0761  -0.0262 0.0458  22  LEU A CA  
270  C C   . LEU A 19  ? 0.2700 0.2442 0.3765 0.0588  -0.0397 0.0489  22  LEU A C   
271  O O   . LEU A 19  ? 0.2489 0.2184 0.3432 0.0650  -0.0448 0.0615  22  LEU A O   
272  C CB  . LEU A 19  ? 0.3866 0.3942 0.5296 0.0923  -0.0273 0.0565  22  LEU A CB  
273  C CG  . LEU A 19  ? 0.6524 0.6455 0.7895 0.1101  -0.0103 0.0506  22  LEU A CG  
274  C CD1 . LEU A 19  ? 0.6912 0.7349 0.8519 0.1249  -0.0110 0.0631  22  LEU A CD1 
275  C CD2 . LEU A 19  ? 0.6652 0.6011 0.7709 0.1198  0.0002  0.0470  22  LEU A CD2 
287  N N   . GLY A 20  ? 0.2389 0.2253 0.3467 0.0381  -0.0437 0.0380  23  GLY A N   
288  C CA  . GLY A 20  ? 0.2268 0.2127 0.3163 0.0210  -0.0518 0.0368  23  GLY A CA  
289  C C   . GLY A 20  ? 0.2101 0.1578 0.2759 0.0190  -0.0451 0.0360  23  GLY A C   
290  O O   . GLY A 20  ? 0.2993 0.2427 0.3451 0.0164  -0.0504 0.0430  23  GLY A O   
294  N N   . THR A 21  ? 0.2697 0.1937 0.3370 0.0183  -0.0339 0.0286  24  THR A N   
295  C CA  . THR A 21  ? 0.2512 0.1462 0.3018 0.0136  -0.0267 0.0300  24  THR A CA  
296  C C   . THR A 21  ? 0.3277 0.2042 0.3655 0.0249  -0.0272 0.0432  24  THR A C   
297  O O   . THR A 21  ? 0.3261 0.1904 0.3446 0.0211  -0.0264 0.0504  24  THR A O   
298  C CB  . THR A 21  ? 0.2583 0.1413 0.3165 0.0080  -0.0179 0.0221  24  THR A CB  
299  O OG1 . THR A 21  ? 0.2181 0.1206 0.2885 0.0017  -0.0168 0.0145  24  THR A OG1 
300  C CG2 . THR A 21  ? 0.2322 0.0973 0.2771 -0.0016 -0.0104 0.0251  24  THR A CG2 
308  N N   . LEU A 22  ? 0.2773 0.1482 0.3229 0.0412  -0.0256 0.0480  25  LEU A N   
309  C CA  . LEU A 22  ? 0.4836 0.3290 0.5155 0.0568  -0.0221 0.0636  25  LEU A CA  
310  C C   . LEU A 22  ? 0.2879 0.1610 0.3142 0.0642  -0.0346 0.0804  25  LEU A C   
311  O O   . LEU A 22  ? 0.4996 0.3528 0.5052 0.0684  -0.0333 0.0943  25  LEU A O   
312  C CB  . LEU A 22  ? 0.4122 0.2470 0.4449 0.0747  -0.0144 0.0613  25  LEU A CB  
313  C CG  . LEU A 22  ? 0.5724 0.3764 0.5934 0.0628  -0.0050 0.0428  25  LEU A CG  
314  C CD1 . LEU A 22  ? 0.5537 0.3469 0.5771 0.0801  0.0019  0.0411  25  LEU A CD1 
315  C CD2 . LEU A 22  ? 0.6620 0.4340 0.6655 0.0442  -0.0027 0.0408  25  LEU A CD2 
327  N N   . TYR A 23  ? 0.2669 0.1873 0.3091 0.0630  -0.0474 0.0803  26  TYR A N   
328  C CA  . TYR A 23  ? 0.3575 0.3124 0.3918 0.0639  -0.0632 0.0956  26  TYR A CA  
329  C C   . TYR A 23  ? 0.2948 0.2333 0.2961 0.0450  -0.0652 0.0917  26  TYR A C   
330  O O   . TYR A 23  ? 0.3270 0.2596 0.3060 0.0510  -0.0686 0.1080  26  TYR A O   
331  C CB  . TYR A 23  ? 0.2595 0.2698 0.3162 0.0561  -0.0772 0.0931  26  TYR A CB  
332  C CG  . TYR A 23  ? 0.2793 0.3338 0.3267 0.0502  -0.0976 0.1083  26  TYR A CG  
333  C CD1 . TYR A 23  ? 0.6262 0.7132 0.6849 0.0749  -0.1053 0.1362  26  TYR A CD1 
334  C CD2 . TYR A 23  ? 0.4934 0.5561 0.5171 0.0201  -0.1083 0.0956  26  TYR A CD2 
335  C CE1 . TYR A 23  ? 0.4033 0.5402 0.4529 0.0672  -0.1270 0.1519  26  TYR A CE1 
336  C CE2 . TYR A 23  ? 0.4400 0.5436 0.4479 0.0087  -0.1294 0.1074  26  TYR A CE2 
337  C CZ  . TYR A 23  ? 0.3655 0.5121 0.3882 0.0313  -0.1410 0.1368  26  TYR A CZ  
338  O OH  . TYR A 23  ? 0.5569 0.7494 0.5632 0.0180  -0.1620 0.1474  26  TYR A OH  
348  N N   . PHE A 24  ? 0.2758 0.2052 0.2717 0.0247  -0.0605 0.0720  27  PHE A N   
349  C CA  . PHE A 24  ? 0.3774 0.2876 0.3401 0.0102  -0.0565 0.0676  27  PHE A CA  
350  C C   . PHE A 24  ? 0.3770 0.2526 0.3255 0.0169  -0.0440 0.0777  27  PHE A C   
351  O O   . PHE A 24  ? 0.4337 0.2996 0.3512 0.0132  -0.0431 0.0856  27  PHE A O   
352  C CB  . PHE A 24  ? 0.3567 0.2575 0.3202 -0.0050 -0.0470 0.0477  27  PHE A CB  
353  C CG  . PHE A 24  ? 0.3227 0.2473 0.2929 -0.0168 -0.0565 0.0373  27  PHE A CG  
354  C CD1 . PHE A 24  ? 0.2981 0.2553 0.2627 -0.0229 -0.0752 0.0437  27  PHE A CD1 
355  C CD2 . PHE A 24  ? 0.2774 0.1946 0.2599 -0.0234 -0.0468 0.0234  27  PHE A CD2 
356  C CE1 . PHE A 24  ? 0.3385 0.3182 0.3094 -0.0400 -0.0839 0.0342  27  PHE A CE1 
357  C CE2 . PHE A 24  ? 0.2867 0.2192 0.2730 -0.0368 -0.0532 0.0148  27  PHE A CE2 
358  C CZ  . PHE A 24  ? 0.2661 0.2286 0.2465 -0.0474 -0.0716 0.0190  27  PHE A CZ  
368  N N   . LEU A 25  ? 0.3732 0.2278 0.3401 0.0237  -0.0334 0.0772  28  LEU A N   
369  C CA  . LEU A 25  ? 0.5323 0.3508 0.4859 0.0237  -0.0206 0.0861  28  LEU A CA  
370  C C   . LEU A 25  ? 0.5211 0.3293 0.4551 0.0389  -0.0242 0.1089  28  LEU A C   
371  O O   . LEU A 25  ? 0.5494 0.3428 0.4569 0.0347  -0.0194 0.1196  28  LEU A O   
372  C CB  . LEU A 25  ? 0.4975 0.2933 0.4691 0.0228  -0.0109 0.0790  28  LEU A CB  
373  C CG  . LEU A 25  ? 0.6284 0.4164 0.6053 0.0033  0.0000  0.0694  28  LEU A CG  
374  C CD1 . LEU A 25  ? 0.8076 0.5876 0.7926 -0.0029 0.0007  0.0573  28  LEU A CD1 
375  C CD2 . LEU A 25  ? 0.5746 0.3513 0.5344 -0.0056 0.0086  0.0800  28  LEU A CD2 
387  N N   . VAL A 26  ? 0.4163 0.2343 0.3632 0.0592  -0.0309 0.1195  29  VAL A N   
388  C CA  . VAL A 26  ? 0.5126 0.3272 0.4443 0.0787  -0.0343 0.1454  29  VAL A CA  
389  C C   . VAL A 26  ? 0.5250 0.3740 0.4335 0.0730  -0.0499 0.1557  29  VAL A C   
390  O O   . VAL A 26  ? 0.4741 0.3091 0.3533 0.0770  -0.0485 0.1744  29  VAL A O   
391  C CB  . VAL A 26  ? 0.5623 0.3955 0.5178 0.1001  -0.0384 0.1486  29  VAL A CB  
392  C CG1 . VAL A 26  ? 0.6072 0.4508 0.5522 0.1180  -0.0439 0.1718  29  VAL A CG1 
393  C CG2 . VAL A 26  ? 0.5481 0.3444 0.5150 0.0990  -0.0229 0.1317  29  VAL A CG2 
403  N N   . LYS A 27  ? 0.4860 0.3784 0.4029 0.0604  -0.0648 0.1424  30  LYS A N   
404  C CA  . LYS A 27  ? 0.4643 0.3892 0.3521 0.0475  -0.0820 0.1465  30  LYS A CA  
405  C C   . LYS A 27  ? 0.6098 0.5004 0.4568 0.0324  -0.0702 0.1408  30  LYS A C   
406  O O   . LYS A 27  ? 0.5965 0.4961 0.4068 0.0300  -0.0788 0.1542  30  LYS A O   
407  C CB  . LYS A 27  ? 0.5211 0.4855 0.4221 0.0294  -0.0961 0.1280  30  LYS A CB  
408  C CG  . LYS A 27  ? 0.5464 0.5476 0.4161 0.0107  -0.1175 0.1301  30  LYS A CG  
409  C CD  . LYS A 27  ? 0.8301 0.8719 0.7189 -0.0083 -0.1322 0.1158  30  LYS A CD  
410  C CE  . LYS A 27  ? 0.8297 0.9074 0.6827 -0.0349 -0.1556 0.1154  30  LYS A CE  
411  N NZ  . LYS A 27  ? 0.9491 0.9790 0.7446 -0.0577 -0.1455 0.0945  30  LYS A NZ  
425  N N   . GLY A 28  ? 0.6010 0.4583 0.4539 0.0235  -0.0509 0.1243  31  GLY A N   
426  C CA  . GLY A 28  ? 0.4863 0.3179 0.3068 0.0119  -0.0358 0.1212  31  GLY A CA  
427  C C   . GLY A 28  ? 0.6694 0.4721 0.4734 0.0205  -0.0239 0.1433  31  GLY A C   
428  O O   . GLY A 28  ? 0.6379 0.4236 0.4141 0.0117  -0.0099 0.1447  31  GLY A O   
432  N N   . MET A 29  ? 0.6831 0.4760 0.5019 0.0381  -0.0260 0.1615  32  MET A N   
433  C CA  . MET A 29  ? 0.8258 0.5888 0.6345 0.0440  -0.0133 0.1814  32  MET A CA  
434  C C   . MET A 29  ? 0.9424 0.7182 0.7107 0.0475  -0.0213 0.2016  32  MET A C   
435  O O   . MET A 29  ? 0.8986 0.7077 0.6574 0.0571  -0.0422 0.2112  32  MET A O   
436  C CB  . MET A 29  ? 0.8451 0.5991 0.6838 0.0587  -0.0147 0.1866  32  MET A CB  
437  C CG  . MET A 29  ? 0.8429 0.5820 0.7144 0.0523  -0.0062 0.1657  32  MET A CG  
438  S SD  . MET A 29  ? 1.1047 0.8153 0.9913 0.0669  -0.0008 0.1682  32  MET A SD  
439  C CE  . MET A 29  ? 0.6687 0.3884 0.5348 0.0908  -0.0093 0.1984  32  MET A CE  
449  N N   . GLY A 30  ? 0.9466 0.7046 0.6935 0.0382  -0.0068 0.2076  33  GLY A N   
450  C CA  . GLY A 30  ? 1.2577 1.0258 0.9642 0.0395  -0.0119 0.2263  33  GLY A CA  
451  C C   . GLY A 30  ? 1.2933 1.0734 0.9531 0.0268  -0.0130 0.2156  33  GLY A C   
452  O O   . GLY A 30  ? 1.6219 1.4049 1.2447 0.0231  -0.0095 0.2264  33  GLY A O   
456  N N   . VAL A 31  ? 0.9774 0.7610 0.6358 0.0170  -0.0180 0.1915  34  VAL A N   
457  C CA  . VAL A 31  ? 0.9519 0.7412 0.5687 -0.0003 -0.0170 0.1720  34  VAL A CA  
458  C C   . VAL A 31  ? 1.0082 0.7670 0.6016 -0.0055 0.0134  0.1723  34  VAL A C   
459  O O   . VAL A 31  ? 1.1031 0.8481 0.7313 -0.0069 0.0335  0.1658  34  VAL A O   
460  C CB  . VAL A 31  ? 0.9214 0.7232 0.5632 -0.0113 -0.0222 0.1413  34  VAL A CB  
461  C CG1 . VAL A 31  ? 0.8092 0.5976 0.4028 -0.0283 -0.0121 0.1190  34  VAL A CG1 
462  C CG2 . VAL A 31  ? 0.8633 0.7041 0.5254 -0.0090 -0.0521 0.1432  34  VAL A CG2 
472  N N   . SER A 32  ? 0.8832 0.6461 0.4305 -0.0088 0.0164  0.1784  35  SER A N   
473  C CA  . SER A 32  ? 0.8973 0.6453 0.4316 -0.0120 0.0453  0.1789  35  SER A CA  
474  C C   . SER A 32  ? 1.0327 0.7697 0.5227 -0.0221 0.0594  0.1544  35  SER A C   
475  O O   . SER A 32  ? 1.1730 0.8996 0.6641 -0.0215 0.0878  0.1514  35  SER A O   
476  C CB  . SER A 32  ? 1.1758 0.9316 0.6902 -0.0068 0.0442  0.2055  35  SER A CB  
477  O OG  . SER A 32  ? 1.1967 0.9769 0.6765 -0.0049 0.0179  0.2135  35  SER A OG  
483  N N   . ASP A 33  ? 1.0558 0.7964 0.5101 -0.0320 0.0407  0.1364  36  ASP A N   
484  C CA  . ASP A 33  ? 0.9762 0.6963 0.3873 -0.0427 0.0561  0.1085  36  ASP A CA  
485  C C   . ASP A 33  ? 0.8075 0.5073 0.2513 -0.0373 0.0854  0.0951  36  ASP A C   
486  O O   . ASP A 33  ? 0.7650 0.4677 0.2488 -0.0363 0.0789  0.0918  36  ASP A O   
487  C CB  . ASP A 33  ? 0.9744 0.7025 0.3559 -0.0601 0.0284  0.0881  36  ASP A CB  
488  C CG  . ASP A 33  ? 1.1336 0.8340 0.4609 -0.0736 0.0426  0.0593  36  ASP A CG  
489  O OD1 . ASP A 33  ? 1.3779 1.0475 0.7014 -0.0652 0.0775  0.0501  36  ASP A OD1 
490  O OD2 . ASP A 33  ? 1.1523 0.8636 0.4453 -0.0920 0.0194  0.0467  36  ASP A OD2 
495  N N   . PRO A 34  ? 0.7868 0.6934 0.5173 0.0788  0.0231  0.1529  37  PRO A N   
496  C CA  . PRO A 34  ? 0.8023 0.7192 0.5627 0.0659  0.0336  0.1441  37  PRO A CA  
497  C C   . PRO A 34  ? 0.5981 0.5361 0.3792 0.0627  0.0209  0.1270  37  PRO A C   
498  O O   . PRO A 34  ? 0.7246 0.6710 0.5375 0.0538  0.0225  0.1203  37  PRO A O   
499  C CB  . PRO A 34  ? 0.7261 0.6363 0.4657 0.0637  0.0511  0.1479  37  PRO A CB  
500  C CG  . PRO A 34  ? 0.8738 0.7763 0.5706 0.0759  0.0455  0.1531  37  PRO A CG  
501  C CD  . PRO A 34  ? 0.8282 0.7228 0.5199 0.0844  0.0320  0.1608  37  PRO A CD  
509  N N   . ASP A 35  ? 0.6948 0.6411 0.4585 0.0701  0.0082  0.1195  38  ASP A N   
510  C CA  . ASP A 35  ? 0.6564 0.6219 0.4406 0.0671  -0.0032 0.1032  38  ASP A CA  
511  C C   . ASP A 35  ? 0.4932 0.4644 0.3040 0.0664  -0.0149 0.1000  38  ASP A C   
512  O O   . ASP A 35  ? 0.4694 0.4512 0.3087 0.0586  -0.0156 0.0911  38  ASP A O   
513  C CB  . ASP A 35  ? 0.8705 0.8429 0.6308 0.0756  -0.0144 0.0953  38  ASP A CB  
514  C CG  . ASP A 35  ? 0.9979 0.9684 0.7364 0.0746  -0.0025 0.0941  38  ASP A CG  
515  O OD1 . ASP A 35  ? 0.8820 0.8536 0.6357 0.0652  0.0119  0.0930  38  ASP A OD1 
516  O OD2 . ASP A 35  ? 1.4007 1.3689 1.1070 0.0837  -0.0077 0.0937  38  ASP A OD2 
521  N N   . ALA A 36  ? 0.4190 0.3827 0.2203 0.0749  -0.0239 0.1073  39  ALA A N   
522  C CA  . ALA A 36  ? 0.6281 0.5966 0.4552 0.0745  -0.0337 0.1043  39  ALA A CA  
523  C C   . ALA A 36  ? 0.4547 0.4184 0.3063 0.0649  -0.0226 0.1083  39  ALA A C   
524  O O   . ALA A 36  ? 0.4904 0.4622 0.3686 0.0603  -0.0272 0.1012  39  ALA A O   
525  C CB  . ALA A 36  ? 0.4218 0.3819 0.2338 0.0862  -0.0449 0.1120  39  ALA A CB  
531  N N   . LYS A 37  ? 0.5014 0.4518 0.3447 0.0618  -0.0075 0.1190  40  LYS A N   
532  C CA  . LYS A 37  ? 0.5806 0.5268 0.4484 0.0528  0.0027  0.1216  40  LYS A CA  
533  C C   . LYS A 37  ? 0.3667 0.3266 0.2579 0.0430  0.0050  0.1095  40  LYS A C   
534  O O   . LYS A 37  ? 0.4953 0.4584 0.4114 0.0372  0.0045  0.1057  40  LYS A O   
535  C CB  . LYS A 37  ? 0.5004 0.4301 0.3561 0.0511  0.0193  0.1344  40  LYS A CB  
536  C CG  . LYS A 37  ? 0.5402 0.4526 0.3809 0.0590  0.0190  0.1485  40  LYS A CG  
537  C CD  . LYS A 37  ? 0.7989 0.6941 0.6171 0.0597  0.0355  0.1618  40  LYS A CD  
538  C CE  . LYS A 37  ? 0.8161 0.7033 0.6570 0.0498  0.0517  0.1661  40  LYS A CE  
539  N NZ  . LYS A 37  ? 0.9205 0.8010 0.7810 0.0497  0.0481  0.1699  40  LYS A NZ  
553  N N   . LYS A 38  ? 0.3415 0.3089 0.2243 0.0416  0.0073  0.1033  41  LYS A N   
554  C CA  . LYS A 38  ? 0.4235 0.4034 0.3276 0.0335  0.0083  0.0920  41  LYS A CA  
555  C C   . LYS A 38  ? 0.4028 0.3934 0.3249 0.0332  -0.0045 0.0829  41  LYS A C   
556  O O   . LYS A 38  ? 0.3301 0.3247 0.2748 0.0265  -0.0035 0.0785  41  LYS A O   
557  C CB  . LYS A 38  ? 0.4048 0.3911 0.2957 0.0338  0.0110  0.0861  41  LYS A CB  
558  C CG  . LYS A 38  ? 0.7326 0.7101 0.6109 0.0316  0.0270  0.0930  41  LYS A CG  
559  C CD  . LYS A 38  ? 0.7905 0.7764 0.6621 0.0304  0.0304  0.0845  41  LYS A CD  
560  C CE  . LYS A 38  ? 0.8638 0.8517 0.7076 0.0395  0.0216  0.0820  41  LYS A CE  
561  N NZ  . LYS A 38  ? 0.9824 0.9780 0.8193 0.0385  0.0255  0.0729  41  LYS A NZ  
575  N N   . PHE A 39  ? 0.2971 0.2922 0.2094 0.0407  -0.0166 0.0797  42  PHE A N   
576  C CA  . PHE A 39  ? 0.3790 0.3848 0.3097 0.0403  -0.0276 0.0702  42  PHE A CA  
577  C C   . PHE A 39  ? 0.3188 0.3200 0.2659 0.0389  -0.0286 0.0737  42  PHE A C   
578  O O   . PHE A 39  ? 0.2443 0.2518 0.2119 0.0339  -0.0306 0.0669  42  PHE A O   
579  C CB  . PHE A 39  ? 0.4193 0.4313 0.3380 0.0489  -0.0404 0.0652  42  PHE A CB  
580  C CG  . PHE A 39  ? 0.3287 0.3485 0.2368 0.0494  -0.0413 0.0573  42  PHE A CG  
581  C CD1 . PHE A 39  ? 0.4125 0.4438 0.3384 0.0438  -0.0428 0.0457  42  PHE A CD1 
582  C CD2 . PHE A 39  ? 0.3376 0.3523 0.2172 0.0556  -0.0400 0.0615  42  PHE A CD2 
583  C CE1 . PHE A 39  ? 0.5184 0.5567 0.4366 0.0442  -0.0434 0.0377  42  PHE A CE1 
584  C CE2 . PHE A 39  ? 0.4925 0.5146 0.3624 0.0561  -0.0406 0.0530  42  PHE A CE2 
585  C CZ  . PHE A 39  ? 0.4212 0.4553 0.3117 0.0503  -0.0424 0.0407  42  PHE A CZ  
595  N N   . TYR A 40  ? 0.2846 0.2738 0.2222 0.0434  -0.0268 0.0844  43  TYR A N   
596  C CA  . TYR A 40  ? 0.3030 0.2870 0.2568 0.0422  -0.0271 0.0874  43  TYR A CA  
597  C C   . TYR A 40  ? 0.2594 0.2420 0.2306 0.0324  -0.0172 0.0864  43  TYR A C   
598  O O   . TYR A 40  ? 0.2451 0.2304 0.2350 0.0288  -0.0191 0.0818  43  TYR A O   
599  C CB  . TYR A 40  ? 0.3045 0.2743 0.2444 0.0492  -0.0264 0.0998  43  TYR A CB  
600  C CG  . TYR A 40  ? 0.3337 0.3054 0.2687 0.0592  -0.0400 0.0992  43  TYR A CG  
601  C CD1 . TYR A 40  ? 0.3047 0.2786 0.2597 0.0600  -0.0461 0.0960  43  TYR A CD1 
602  C CD2 . TYR A 40  ? 0.3933 0.3649 0.3043 0.0681  -0.0471 0.1011  43  TYR A CD2 
603  C CE1 . TYR A 40  ? 0.4380 0.4146 0.3920 0.0693  -0.0590 0.0946  43  TYR A CE1 
604  C CE2 . TYR A 40  ? 0.3917 0.3658 0.2997 0.0779  -0.0613 0.0997  43  TYR A CE2 
605  C CZ  . TYR A 40  ? 0.4847 0.4617 0.4158 0.0784  -0.0672 0.0964  43  TYR A CZ  
606  O OH  . TYR A 40  ? 0.4807 0.4611 0.4122 0.0883  -0.0816 0.0941  43  TYR A OH  
616  N N   . ALA A 41  ? 0.2649 0.2432 0.2304 0.0283  -0.0067 0.0901  44  ALA A N   
617  C CA  . ALA A 41  ? 0.2497 0.2275 0.2329 0.0195  0.0015  0.0881  44  ALA A CA  
618  C C   . ALA A 41  ? 0.3087 0.2986 0.3063 0.0146  -0.0030 0.0768  44  ALA A C   
619  O O   . ALA A 41  ? 0.2627 0.2537 0.2769 0.0102  -0.0035 0.0731  44  ALA A O   
620  C CB  . ALA A 41  ? 0.2613 0.2336 0.2375 0.0163  0.0136  0.0931  44  ALA A CB  
626  N N   . ILE A 42  ? 0.2233 0.2219 0.2141 0.0155  -0.0061 0.0712  45  ILE A N   
627  C CA  . ILE A 42  ? 0.2028 0.2115 0.2066 0.0113  -0.0097 0.0613  45  ILE A CA  
628  C C   . ILE A 42  ? 0.2552 0.2671 0.2693 0.0123  -0.0175 0.0571  45  ILE A C   
629  O O   . ILE A 42  ? 0.2022 0.2159 0.2302 0.0076  -0.0173 0.0529  45  ILE A O   
630  C CB  . ILE A 42  ? 0.2480 0.2645 0.2428 0.0129  -0.0119 0.0558  45  ILE A CB  
631  C CG1 . ILE A 42  ? 0.2461 0.2602 0.2333 0.0108  -0.0024 0.0585  45  ILE A CG1 
632  C CG2 . ILE A 42  ? 0.1856 0.2112 0.1943 0.0092  -0.0161 0.0463  45  ILE A CG2 
633  C CD1 . ILE A 42  ? 0.3874 0.4069 0.3602 0.0143  -0.0038 0.0545  45  ILE A CD1 
645  N N   . THR A 43  ? 0.2015 0.2139 0.2088 0.0190  -0.0245 0.0581  46  THR A N   
646  C CA  . THR A 43  ? 0.2733 0.2908 0.2925 0.0202  -0.0316 0.0523  46  THR A CA  
647  C C   . THR A 43  ? 0.1877 0.1989 0.2179 0.0186  -0.0296 0.0551  46  THR A C   
648  O O   . THR A 43  ? 0.2861 0.3009 0.3295 0.0162  -0.0315 0.0493  46  THR A O   
649  C CB  . THR A 43  ? 0.2271 0.2484 0.2384 0.0283  -0.0407 0.0512  46  THR A CB  
650  O OG1 . THR A 43  ? 0.2098 0.2364 0.2090 0.0300  -0.0424 0.0481  46  THR A OG1 
651  C CG2 . THR A 43  ? 0.2587 0.2875 0.2862 0.0288  -0.0474 0.0432  46  THR A CG2 
659  N N   . THR A 44  ? 0.1995 0.2006 0.2247 0.0197  -0.0251 0.0636  47  THR A N   
660  C CA  . THR A 44  ? 0.1964 0.1911 0.2334 0.0180  -0.0229 0.0653  47  THR A CA  
661  C C   . THR A 44  ? 0.2426 0.2377 0.2905 0.0100  -0.0175 0.0612  47  THR A C   
662  O O   . THR A 44  ? 0.2055 0.1992 0.2647 0.0078  -0.0176 0.0580  47  THR A O   
663  C CB  . THR A 44  ? 0.2824 0.2650 0.3123 0.0214  -0.0191 0.0757  47  THR A CB  
664  O OG1 . THR A 44  ? 0.3004 0.2819 0.3175 0.0301  -0.0255 0.0800  47  THR A OG1 
665  C CG2 . THR A 44  ? 0.2121 0.1880 0.2561 0.0199  -0.0171 0.0765  47  THR A CG2 
673  N N   . LEU A 45  ? 0.1873 0.1843 0.2320 0.0061  -0.0133 0.0607  48  LEU A N   
674  C CA  . LEU A 45  ? 0.1699 0.1674 0.2247 -0.0005 -0.0098 0.0566  48  LEU A CA  
675  C C   . LEU A 45  ? 0.2296 0.2337 0.2907 -0.0025 -0.0141 0.0487  48  LEU A C   
676  O O   . LEU A 45  ? 0.1928 0.1955 0.2616 -0.0065 -0.0130 0.0452  48  LEU A O   
677  C CB  . LEU A 45  ? 0.1695 0.1683 0.2213 -0.0034 -0.0048 0.0574  48  LEU A CB  
678  C CG  . LEU A 45  ? 0.3301 0.3209 0.3836 -0.0054 0.0031  0.0635  48  LEU A CG  
679  C CD1 . LEU A 45  ? 0.4809 0.4744 0.5310 -0.0074 0.0085  0.0637  48  LEU A CD1 
680  C CD2 . LEU A 45  ? 0.4075 0.3948 0.4761 -0.0100 0.0047  0.0607  48  LEU A CD2 
692  N N   . VAL A 46  ? 0.2060 0.2166 0.2637 0.0002  -0.0186 0.0455  49  VAL A N   
693  C CA  . VAL A 46  ? 0.1418 0.1578 0.2053 -0.0021 -0.0209 0.0385  49  VAL A CA  
694  C C   . VAL A 46  ? 0.1448 0.1582 0.2163 -0.0028 -0.0211 0.0362  49  VAL A C   
695  O O   . VAL A 46  ? 0.1960 0.2077 0.2710 -0.0068 -0.0192 0.0330  49  VAL A O   
696  C CB  . VAL A 46  ? 0.1415 0.1652 0.2025 0.0009  -0.0253 0.0350  49  VAL A CB  
697  C CG1 . VAL A 46  ? 0.1326 0.1602 0.2022 -0.0011 -0.0266 0.0284  49  VAL A CG1 
698  C CG2 . VAL A 46  ? 0.1904 0.2172 0.2443 0.0004  -0.0242 0.0350  49  VAL A CG2 
708  N N   . PRO A 47  ? 0.1633 0.1758 0.2374 0.0013  -0.0234 0.0372  50  PRO A N   
709  C CA  . PRO A 47  ? 0.1413 0.1512 0.2242 0.0004  -0.0224 0.0341  50  PRO A CA  
710  C C   . PRO A 47  ? 0.1665 0.1686 0.2514 -0.0023 -0.0185 0.0361  50  PRO A C   
711  O O   . PRO A 47  ? 0.1524 0.1522 0.2422 -0.0047 -0.0168 0.0318  50  PRO A O   
712  C CB  . PRO A 47  ? 0.1941 0.2054 0.2809 0.0063  -0.0264 0.0349  50  PRO A CB  
713  C CG  . PRO A 47  ? 0.2550 0.2654 0.3317 0.0105  -0.0289 0.0412  50  PRO A CG  
714  C CD  . PRO A 47  ? 0.1529 0.1667 0.2220 0.0074  -0.0274 0.0408  50  PRO A CD  
722  N N   . ALA A 48  ? 0.1497 0.1471 0.2310 -0.0021 -0.0167 0.0418  51  ALA A N   
723  C CA  . ALA A 48  ? 0.2398 0.2303 0.3262 -0.0052 -0.0130 0.0425  51  ALA A CA  
724  C C   . ALA A 48  ? 0.1482 0.1402 0.2356 -0.0103 -0.0123 0.0371  51  ALA A C   
725  O O   . ALA A 48  ? 0.1890 0.1775 0.2811 -0.0125 -0.0116 0.0330  51  ALA A O   
726  C CB  . ALA A 48  ? 0.1803 0.1656 0.2641 -0.0046 -0.0097 0.0497  51  ALA A CB  
732  N N   . ILE A 49  ? 0.1584 0.1553 0.2410 -0.0117 -0.0131 0.0365  52  ILE A N   
733  C CA  . ILE A 49  ? 0.1612 0.1592 0.2441 -0.0154 -0.0138 0.0319  52  ILE A CA  
734  C C   . ILE A 49  ? 0.1429 0.1411 0.2243 -0.0157 -0.0149 0.0270  52  ILE A C   
735  O O   . ILE A 49  ? 0.1561 0.1508 0.2373 -0.0178 -0.0150 0.0232  52  ILE A O   
736  C CB  . ILE A 49  ? 0.1522 0.1552 0.2316 -0.0161 -0.0143 0.0325  52  ILE A CB  
737  C CG1 . ILE A 49  ? 0.1849 0.1866 0.2667 -0.0168 -0.0111 0.0365  52  ILE A CG1 
738  C CG2 . ILE A 49  ? 0.1504 0.1543 0.2292 -0.0186 -0.0164 0.0280  52  ILE A CG2 
739  C CD1 . ILE A 49  ? 0.1925 0.1993 0.2700 -0.0163 -0.0104 0.0378  52  ILE A CD1 
751  N N   . ALA A 50  ? 0.1431 0.1451 0.2233 -0.0136 -0.0156 0.0266  53  ALA A N   
752  C CA  . ALA A 50  ? 0.1943 0.1962 0.2743 -0.0142 -0.0146 0.0222  53  ALA A CA  
753  C C   . ALA A 50  ? 0.1772 0.1741 0.2609 -0.0142 -0.0126 0.0198  53  ALA A C   
754  O O   . ALA A 50  ? 0.1371 0.1309 0.2178 -0.0159 -0.0106 0.0158  53  ALA A O   
755  C CB  . ALA A 50  ? 0.1592 0.1669 0.2419 -0.0120 -0.0154 0.0213  53  ALA A CB  
761  N N   . PHE A 51  ? 0.1380 0.1330 0.2272 -0.0121 -0.0127 0.0224  54  PHE A N   
762  C CA  . PHE A 51  ? 0.1422 0.1321 0.2366 -0.0119 -0.0106 0.0196  54  PHE A CA  
763  C C   . PHE A 51  ? 0.1884 0.1734 0.2798 -0.0153 -0.0099 0.0160  54  PHE A C   
764  O O   . PHE A 51  ? 0.1493 0.1311 0.2391 -0.0163 -0.0079 0.0108  54  PHE A O   
765  C CB  . PHE A 51  ? 0.1793 0.1665 0.2805 -0.0088 -0.0110 0.0241  54  PHE A CB  
766  C CG  . PHE A 51  ? 0.2163 0.1969 0.3244 -0.0093 -0.0087 0.0214  54  PHE A CG  
767  C CD1 . PHE A 51  ? 0.1627 0.1426 0.2768 -0.0077 -0.0071 0.0169  54  PHE A CD1 
768  C CD2 . PHE A 51  ? 0.1773 0.1526 0.2878 -0.0115 -0.0078 0.0223  54  PHE A CD2 
769  C CE1 . PHE A 51  ? 0.2360 0.2098 0.3571 -0.0081 -0.0047 0.0134  54  PHE A CE1 
770  C CE2 . PHE A 51  ? 0.3849 0.3540 0.5033 -0.0121 -0.0059 0.0186  54  PHE A CE2 
771  C CZ  . PHE A 51  ? 0.1858 0.1540 0.3088 -0.0102 -0.0044 0.0142  54  PHE A CZ  
781  N N   . THR A 52  ? 0.1447 0.1291 0.2354 -0.0170 -0.0115 0.0181  55  THR A N   
782  C CA  . THR A 52  ? 0.1786 0.1593 0.2686 -0.0197 -0.0125 0.0136  55  THR A CA  
783  C C   . THR A 52  ? 0.1498 0.1306 0.2290 -0.0207 -0.0139 0.0095  55  THR A C   
784  O O   . THR A 52  ? 0.1567 0.1333 0.2318 -0.0217 -0.0147 0.0042  55  THR A O   
785  C CB  . THR A 52  ? 0.1604 0.1418 0.2552 -0.0213 -0.0138 0.0160  55  THR A CB  
786  O OG1 . THR A 52  ? 0.2837 0.2701 0.3731 -0.0216 -0.0156 0.0180  55  THR A OG1 
787  C CG2 . THR A 52  ? 0.2243 0.2038 0.3270 -0.0201 -0.0109 0.0218  55  THR A CG2 
795  N N   . MET A 53  ? 0.1453 0.1300 0.2191 -0.0203 -0.0143 0.0120  56  MET A N   
796  C CA  . MET A 53  ? 0.1733 0.1563 0.2361 -0.0210 -0.0150 0.0098  56  MET A CA  
797  C C   . MET A 53  ? 0.2114 0.1914 0.2697 -0.0206 -0.0104 0.0070  56  MET A C   
798  O O   . MET A 53  ? 0.1831 0.1577 0.2305 -0.0212 -0.0098 0.0039  56  MET A O   
799  C CB  . MET A 53  ? 0.1684 0.1560 0.2294 -0.0208 -0.0164 0.0132  56  MET A CB  
800  C CG  . MET A 53  ? 0.1692 0.1594 0.2338 -0.0214 -0.0201 0.0147  56  MET A CG  
801  S SD  . MET A 53  ? 0.3282 0.3142 0.3891 -0.0224 -0.0253 0.0102  56  MET A SD  
802  C CE  . MET A 53  ? 0.3531 0.3379 0.4256 -0.0235 -0.0247 0.0081  56  MET A CE  
812  N N   . TYR A 54  ? 0.1505 0.1333 0.2168 -0.0195 -0.0071 0.0076  57  TYR A N   
813  C CA  . TYR A 54  ? 0.1952 0.1755 0.2607 -0.0194 -0.0015 0.0039  57  TYR A CA  
814  C C   . TYR A 54  ? 0.1647 0.1392 0.2287 -0.0197 -0.0002 -0.0009 57  TYR A C   
815  O O   . TYR A 54  ? 0.1745 0.1440 0.2300 -0.0203 0.0042  -0.0050 57  TYR A O   
816  C CB  . TYR A 54  ? 0.1501 0.1360 0.2283 -0.0175 0.0003  0.0047  57  TYR A CB  
817  C CG  . TYR A 54  ? 0.1472 0.1370 0.2258 -0.0179 0.0026  0.0049  57  TYR A CG  
818  C CD1 . TYR A 54  ? 0.1529 0.1405 0.2313 -0.0191 0.0096  0.0011  57  TYR A CD1 
819  C CD2 . TYR A 54  ? 0.1635 0.1588 0.2436 -0.0174 -0.0012 0.0082  57  TYR A CD2 
820  C CE1 . TYR A 54  ? 0.1511 0.1416 0.2326 -0.0201 0.0127  0.0009  57  TYR A CE1 
821  C CE2 . TYR A 54  ? 0.1645 0.1632 0.2472 -0.0181 0.0009  0.0074  57  TYR A CE2 
822  C CZ  . TYR A 54  ? 0.1656 0.1618 0.2498 -0.0195 0.0079  0.0038  57  TYR A CZ  
823  O OH  . TYR A 54  ? 0.2285 0.2276 0.3179 -0.0207 0.0110  0.0026  57  TYR A OH  
833  N N   . LEU A 55  ? 0.1631 0.1373 0.2349 -0.0193 -0.0032 -0.0006 58  LEU A N   
834  C CA  . LEU A 55  ? 0.2313 0.1999 0.3035 -0.0197 -0.0024 -0.0063 58  LEU A CA  
835  C C   . LEU A 55  ? 0.1810 0.1451 0.2388 -0.0211 -0.0051 -0.0103 58  LEU A C   
836  O O   . LEU A 55  ? 0.2128 0.1717 0.2630 -0.0212 -0.0028 -0.0164 58  LEU A O   
837  C CB  . LEU A 55  ? 0.1688 0.1372 0.2541 -0.0194 -0.0048 -0.0046 58  LEU A CB  
838  C CG  . LEU A 55  ? 0.1774 0.1402 0.2670 -0.0201 -0.0043 -0.0113 58  LEU A CG  
839  C CD1 . LEU A 55  ? 0.1835 0.1437 0.2747 -0.0189 0.0012  -0.0164 58  LEU A CD1 
840  C CD2 . LEU A 55  ? 0.1751 0.1368 0.2792 -0.0201 -0.0056 -0.0084 58  LEU A CD2 
852  N N   . SER A 56  ? 0.1777 0.1438 0.2313 -0.0216 -0.0104 -0.0073 59  SER A N   
853  C CA  . SER A 56  ? 0.2269 0.1890 0.2672 -0.0218 -0.0149 -0.0111 59  SER A CA  
854  C C   . SER A 56  ? 0.1990 0.1559 0.2211 -0.0211 -0.0113 -0.0119 59  SER A C   
855  O O   . SER A 56  ? 0.2605 0.2112 0.2682 -0.0204 -0.0129 -0.0168 59  SER A O   
856  C CB  . SER A 56  ? 0.2050 0.1710 0.2476 -0.0221 -0.0212 -0.0077 59  SER A CB  
857  O OG  . SER A 56  ? 0.2241 0.1912 0.2583 -0.0215 -0.0206 -0.0031 59  SER A OG  
863  N N   . MET A 57  ? 0.1993 0.1582 0.2215 -0.0212 -0.0061 -0.0074 60  MET A N   
864  C CA  . MET A 57  ? 0.2630 0.2159 0.2698 -0.0211 -0.0001 -0.0076 60  MET A CA  
865  C C   . MET A 57  ? 0.2158 0.1644 0.2206 -0.0212 0.0072  -0.0132 60  MET A C   
866  O O   . MET A 57  ? 0.3167 0.2571 0.3032 -0.0208 0.0107  -0.0161 60  MET A O   
867  C CB  . MET A 57  ? 0.1971 0.1539 0.2092 -0.0217 0.0040  -0.0024 60  MET A CB  
868  C CG  . MET A 57  ? 0.2632 0.2230 0.2748 -0.0214 -0.0021 0.0025  60  MET A CG  
869  S SD  . MET A 57  ? 0.3016 0.2632 0.3155 -0.0222 0.0033  0.0069  60  MET A SD  
870  C CE  . MET A 57  ? 0.2867 0.2595 0.3230 -0.0222 0.0038  0.0069  60  MET A CE  
880  N N   . LEU A 58  ? 0.2789 0.2323 0.3015 -0.0213 0.0097  -0.0148 61  LEU A N   
881  C CA  . LEU A 58  ? 0.2270 0.1770 0.2513 -0.0213 0.0168  -0.0210 61  LEU A CA  
882  C C   . LEU A 58  ? 0.2875 0.2308 0.2996 -0.0209 0.0141  -0.0277 61  LEU A C   
883  O O   . LEU A 58  ? 0.2747 0.2113 0.2730 -0.0208 0.0202  -0.0328 61  LEU A O   
884  C CB  . LEU A 58  ? 0.3083 0.2645 0.3557 -0.0205 0.0175  -0.0211 61  LEU A CB  
885  C CG  . LEU A 58  ? 0.2739 0.2278 0.3285 -0.0201 0.0248  -0.0278 61  LEU A CG  
886  C CD1 . LEU A 58  ? 0.2161 0.1693 0.2677 -0.0208 0.0348  -0.0291 61  LEU A CD1 
887  C CD2 . LEU A 58  ? 0.4052 0.3642 0.4825 -0.0183 0.0227  -0.0269 61  LEU A CD2 
899  N N   . LEU A 59  ? 0.2260 0.1710 0.2434 -0.0208 0.0053  -0.0286 62  LEU A N   
900  C CA  . LEU A 59  ? 0.2398 0.1796 0.2489 -0.0205 0.0011  -0.0365 62  LEU A CA  
901  C C   . LEU A 59  ? 0.3531 0.2873 0.3375 -0.0193 -0.0035 -0.0374 62  LEU A C   
902  O O   . LEU A 59  ? 0.3122 0.2416 0.2857 -0.0182 -0.0076 -0.0451 62  LEU A O   
903  C CB  . LEU A 59  ? 0.2410 0.1849 0.2680 -0.0211 -0.0061 -0.0376 62  LEU A CB  
904  C CG  . LEU A 59  ? 0.3221 0.2694 0.3720 -0.0215 -0.0024 -0.0358 62  LEU A CG  
905  C CD1 . LEU A 59  ? 0.2434 0.1926 0.3092 -0.0224 -0.0082 -0.0358 62  LEU A CD1 
906  C CD2 . LEU A 59  ? 0.3423 0.2857 0.3948 -0.0209 0.0045  -0.0428 62  LEU A CD2 
918  N N   . GLY A 60  ? 0.2534 0.1875 0.2286 -0.0189 -0.0035 -0.0301 63  GLY A N   
919  C CA  . GLY A 60  ? 0.3517 0.2789 0.3021 -0.0169 -0.0074 -0.0295 63  GLY A CA  
920  C C   . GLY A 60  ? 0.3867 0.3168 0.3382 -0.0158 -0.0198 -0.0281 63  GLY A C   
921  O O   . GLY A 60  ? 0.3549 0.2790 0.2860 -0.0132 -0.0250 -0.0273 63  GLY A O   
925  N N   . TYR A 61  ? 0.3350 0.2736 0.3095 -0.0173 -0.0244 -0.0276 64  TYR A N   
926  C CA  . TYR A 61  ? 0.3653 0.3076 0.3442 -0.0165 -0.0353 -0.0275 64  TYR A CA  
927  C C   . TYR A 61  ? 0.2611 0.2048 0.2362 -0.0157 -0.0362 -0.0191 64  TYR A C   
928  O O   . TYR A 61  ? 0.3386 0.2809 0.3055 -0.0135 -0.0446 -0.0189 64  TYR A O   
929  C CB  . TYR A 61  ? 0.2379 0.1878 0.2431 -0.0188 -0.0375 -0.0292 64  TYR A CB  
930  C CG  . TYR A 61  ? 0.3346 0.2892 0.3487 -0.0185 -0.0475 -0.0305 64  TYR A CG  
931  C CD1 . TYR A 61  ? 0.2957 0.2492 0.3100 -0.0176 -0.0562 -0.0398 64  TYR A CD1 
932  C CD2 . TYR A 61  ? 0.3061 0.2664 0.3295 -0.0191 -0.0483 -0.0237 64  TYR A CD2 
933  C CE1 . TYR A 61  ? 0.4485 0.4073 0.4746 -0.0174 -0.0655 -0.0421 64  TYR A CE1 
934  C CE2 . TYR A 61  ? 0.3168 0.2819 0.3507 -0.0189 -0.0565 -0.0256 64  TYR A CE2 
935  C CZ  . TYR A 61  ? 0.3760 0.3406 0.4123 -0.0181 -0.0651 -0.0348 64  TYR A CZ  
936  O OH  . TYR A 61  ? 0.6272 0.5975 0.6774 -0.0179 -0.0733 -0.0378 64  TYR A OH  
946  N N   . GLY A 62  ? 0.2269 0.1736 0.2090 -0.0173 -0.0283 -0.0129 65  GLY A N   
947  C CA  . GLY A 62  ? 0.3021 0.2510 0.2844 -0.0170 -0.0288 -0.0059 65  GLY A CA  
948  C C   . GLY A 62  ? 0.3493 0.2895 0.3108 -0.0155 -0.0248 -0.0023 65  GLY A C   
949  O O   . GLY A 62  ? 0.2424 0.1837 0.2066 -0.0162 -0.0202 0.0033  65  GLY A O   
953  N N   . LEU A 63  ? 0.3989 0.3297 0.3392 -0.0133 -0.0262 -0.0056 66  LEU A N   
954  C CA  . LEU A 63  ? 0.3213 0.2410 0.2382 -0.0116 -0.0209 -0.0016 66  LEU A CA  
955  C C   . LEU A 63  ? 0.3477 0.2595 0.2433 -0.0071 -0.0313 -0.0024 66  LEU A C   
956  O O   . LEU A 63  ? 0.3758 0.2885 0.2692 -0.0054 -0.0399 -0.0095 66  LEU A O   
957  C CB  . LEU A 63  ? 0.3784 0.2919 0.2854 -0.0127 -0.0094 -0.0045 66  LEU A CB  
958  C CG  . LEU A 63  ? 0.5372 0.4368 0.4169 -0.0112 -0.0014 -0.0009 66  LEU A CG  
959  C CD1 . LEU A 63  ? 0.4244 0.3240 0.3118 -0.0135 0.0085  0.0063  66  LEU A CD1 
960  C CD2 . LEU A 63  ? 0.3729 0.2660 0.2397 -0.0114 0.0070  -0.0070 66  LEU A CD2 
972  N N   . THR A 64  ? 0.3191 0.2231 0.1999 -0.0048 -0.0309 0.0045  67  THR A N   
973  C CA  . THR A 64  ? 0.3802 0.2748 0.2378 0.0007  -0.0411 0.0052  67  THR A CA  
974  C C   . THR A 64  ? 0.4278 0.3070 0.2590 0.0027  -0.0327 0.0129  67  THR A C   
975  O O   . THR A 64  ? 0.4315 0.3094 0.2681 -0.0007 -0.0197 0.0179  67  THR A O   
976  C CB  . THR A 64  ? 0.4103 0.3122 0.2822 0.0027  -0.0538 0.0063  67  THR A CB  
977  O OG1 . THR A 64  ? 0.4198 0.3145 0.2722 0.0088  -0.0667 0.0043  67  THR A OG1 
978  C CG2 . THR A 64  ? 0.4474 0.3489 0.3260 0.0018  -0.0488 0.0151  67  THR A CG2 
986  N N   . MET A 65  ? 0.4230 0.2902 0.2257 0.0086  -0.0403 0.0138  68  MET A N   
987  C CA  . MET A 65  ? 0.4347 0.2842 0.2078 0.0116  -0.0331 0.0224  68  MET A CA  
988  C C   . MET A 65  ? 0.6169 0.4627 0.3880 0.0160  -0.0428 0.0295  68  MET A C   
989  O O   . MET A 65  ? 0.7198 0.5695 0.4921 0.0205  -0.0593 0.0259  68  MET A O   
990  C CB  . MET A 65  ? 0.5489 0.3847 0.2858 0.0162  -0.0341 0.0191  68  MET A CB  
991  C CG  . MET A 65  ? 0.6932 0.5333 0.4330 0.0126  -0.0268 0.0097  68  MET A CG  
992  S SD  . MET A 65  ? 0.8850 0.7289 0.6440 0.0047  -0.0045 0.0120  68  MET A SD  
993  C CE  . MET A 65  ? 0.6547 0.4796 0.3883 0.0060  0.0088  0.0246  68  MET A CE  
1003 N N   . VAL A 66  ? 0.5874 0.4259 0.3575 0.0148  -0.0327 0.0389  69  VAL A N   
1004 C CA  . VAL A 66  ? 0.6411 0.4745 0.4104 0.0188  -0.0398 0.0464  69  VAL A CA  
1005 C C   . VAL A 66  ? 0.7950 0.6055 0.5297 0.0227  -0.0319 0.0563  69  VAL A C   
1006 O O   . VAL A 66  ? 0.5549 0.3583 0.2855 0.0184  -0.0142 0.0604  69  VAL A O   
1007 C CB  . VAL A 66  ? 0.5297 0.3748 0.3325 0.0138  -0.0351 0.0487  69  VAL A CB  
1008 C CG1 . VAL A 66  ? 0.5246 0.3633 0.3267 0.0182  -0.0418 0.0560  69  VAL A CG1 
1009 C CG2 . VAL A 66  ? 0.4734 0.3392 0.3071 0.0102  -0.0417 0.0400  69  VAL A CG2 
1019 N N   . PRO A 67  ? 0.7472 0.5452 0.4568 0.0310  -0.0439 0.0606  70  PRO A N   
1020 C CA  . PRO A 67  ? 0.7014 0.4751 0.3752 0.0353  -0.0357 0.0717  70  PRO A CA  
1021 C C   . PRO A 67  ? 0.8009 0.5687 0.4863 0.0348  -0.0302 0.0820  70  PRO A C   
1022 O O   . PRO A 67  ? 0.7998 0.5725 0.4991 0.0384  -0.0435 0.0831  70  PRO A O   
1023 C CB  . PRO A 67  ? 0.7819 0.5459 0.4245 0.0456  -0.0541 0.0710  70  PRO A CB  
1024 C CG  . PRO A 67  ? 0.6102 0.3934 0.2827 0.0468  -0.0729 0.0630  70  PRO A CG  
1025 C CD  . PRO A 67  ? 0.7390 0.5435 0.4497 0.0373  -0.0658 0.0548  70  PRO A CD  
1033 N N   . PHE A 68  ? 0.6890 0.4466 0.3712 0.0300  -0.0100 0.0886  71  PHE A N   
1034 C CA  . PHE A 68  ? 0.8547 0.6018 0.5427 0.0297  -0.0026 0.0990  71  PHE A CA  
1035 C C   . PHE A 68  ? 0.9671 0.6962 0.6371 0.0262  0.0202  0.1064  71  PHE A C   
1036 O O   . PHE A 68  ? 0.8915 0.6236 0.5591 0.0213  0.0320  0.1013  71  PHE A O   
1037 C CB  . PHE A 68  ? 0.8647 0.6316 0.5979 0.0237  -0.0029 0.0949  71  PHE A CB  
1038 C CG  . PHE A 68  ? 0.6868 0.4687 0.4452 0.0145  0.0101  0.0877  71  PHE A CG  
1039 C CD1 . PHE A 68  ? 0.7798 0.5543 0.5420 0.0088  0.0301  0.0915  71  PHE A CD1 
1040 C CD2 . PHE A 68  ? 0.6403 0.4435 0.4202 0.0117  0.0021  0.0769  71  PHE A CD2 
1041 C CE1 . PHE A 68  ? 0.6718 0.4609 0.4590 0.0012  0.0404  0.0841  71  PHE A CE1 
1042 C CE2 . PHE A 68  ? 0.6352 0.4514 0.4376 0.0043  0.0127  0.0708  71  PHE A CE2 
1043 C CZ  . PHE A 68  ? 0.6578 0.4675 0.4641 -0.0006 0.0311  0.0741  71  PHE A CZ  
1053 N N   . GLY A 69  ? 1.1241 0.8341 0.7827 0.0287  0.0270  0.1185  72  GLY A N   
1054 C CA  . GLY A 69  ? 1.0397 0.7377 0.6886 0.0251  0.0485  0.1236  72  GLY A CA  
1055 C C   . GLY A 69  ? 1.1711 0.8587 0.7832 0.0289  0.0514  0.1230  72  GLY A C   
1056 O O   . GLY A 69  ? 1.1415 0.8226 0.7475 0.0244  0.0707  0.1237  72  GLY A O   
1060 N N   . GLY A 70  ? 1.1201 0.8070 0.7094 0.0371  0.0325  0.1206  73  GLY A N   
1061 C CA  . GLY A 70  ? 0.9828 0.6603 0.5366 0.0414  0.0337  0.1189  73  GLY A CA  
1062 C C   . GLY A 70  ? 1.1194 0.8031 0.6692 0.0368  0.0406  0.1092  73  GLY A C   
1063 O O   . GLY A 70  ? 1.1004 0.7750 0.6248 0.0377  0.0499  0.1080  73  GLY A O   
1067 N N   . GLU A 71  ? 1.1281 0.8265 0.7020 0.0320  0.0366  0.1022  74  GLU A N   
1068 C CA  . GLU A 71  ? 0.9794 0.6880 0.5579 0.0270  0.0429  0.0914  74  GLU A CA  
1069 C C   . GLU A 71  ? 0.8825 0.6171 0.4943 0.0256  0.0250  0.0797  74  GLU A C   
1070 O O   . GLU A 71  ? 0.7867 0.5322 0.4245 0.0257  0.0140  0.0805  74  GLU A O   
1071 C CB  . GLU A 71  ? 0.9532 0.6642 0.5534 0.0174  0.0674  0.0915  74  GLU A CB  
1074 N N   . GLN A 72  ? 0.8329 0.5766 0.4434 0.0244  0.0229  0.0686  75  GLN A N   
1075 C CA  . GLN A 72  ? 0.7847 0.5520 0.4272 0.0222  0.0091  0.0571  75  GLN A CA  
1076 C C   . GLN A 72  ? 0.6755 0.4582 0.3559 0.0129  0.0224  0.0532  75  GLN A C   
1077 O O   . GLN A 72  ? 0.9669 0.7499 0.6466 0.0090  0.0357  0.0484  75  GLN A O   
1078 C CB  . GLN A 72  ? 0.9790 0.7474 0.6026 0.0257  -0.0001 0.0468  75  GLN A CB  
1079 C CG  . GLN A 72  ? 1.1787 0.9360 0.7696 0.0357  -0.0184 0.0481  75  GLN A CG  
1080 C CD  . GLN A 72  ? 1.3868 1.1604 0.9931 0.0380  -0.0393 0.0359  75  GLN A CD  
1081 O OE1 . GLN A 72  ? 1.2591 1.0447 0.8912 0.0386  -0.0526 0.0354  75  GLN A OE1 
1082 N NE2 . GLN A 72  ? 1.4077 1.1818 0.9997 0.0390  -0.0417 0.0255  75  GLN A NE2 
1091 N N   . ASN A 73  ? 0.7366 0.5322 0.4500 0.0100  0.0184  0.0547  76  ASN A N   
1092 C CA  . ASN A 73  ? 0.5487 0.3577 0.2966 0.0023  0.0299  0.0520  76  ASN A CA  
1093 C C   . ASN A 73  ? 0.6221 0.4522 0.3977 -0.0001 0.0202  0.0419  76  ASN A C   
1094 O O   . ASN A 73  ? 0.5932 0.4316 0.3777 0.0026  0.0043  0.0400  76  ASN A O   
1095 C CB  . ASN A 73  ? 0.5280 0.3379 0.2945 0.0005  0.0324  0.0592  76  ASN A CB  
1096 C CG  . ASN A 73  ? 0.7373 0.5247 0.4776 0.0032  0.0416  0.0704  76  ASN A CG  
1097 O OD1 . ASN A 73  ? 0.7222 0.5008 0.4602 -0.0008 0.0601  0.0737  76  ASN A OD1 
1098 N ND2 . ASN A 73  ? 0.5687 0.3463 0.2898 0.0102  0.0288  0.0763  76  ASN A ND2 
1105 N N   . PRO A 74  ? 0.5921 0.4305 0.3827 -0.0049 0.0296  0.0355  77  PRO A N   
1106 C CA  . PRO A 74  ? 0.5356 0.3923 0.3525 -0.0069 0.0211  0.0271  77  PRO A CA  
1107 C C   . PRO A 74  ? 0.4593 0.3299 0.3082 -0.0099 0.0184  0.0287  77  PRO A C   
1108 O O   . PRO A 74  ? 0.5324 0.4050 0.3958 -0.0136 0.0293  0.0311  77  PRO A O   
1109 C CB  . PRO A 74  ? 0.6248 0.4833 0.4458 -0.0105 0.0337  0.0210  77  PRO A CB  
1110 C CG  . PRO A 74  ? 0.7783 0.6256 0.5908 -0.0127 0.0511  0.0265  77  PRO A CG  
1111 C CD  . PRO A 74  ? 0.7455 0.5767 0.5310 -0.0085 0.0490  0.0356  77  PRO A CD  
1119 N N   . ILE A 75  ? 0.3837 0.2641 0.2443 -0.0082 0.0040  0.0266  78  ILE A N   
1120 C CA  . ILE A 75  ? 0.3543 0.2472 0.2419 -0.0102 0.0003  0.0279  78  ILE A CA  
1121 C C   . ILE A 75  ? 0.3168 0.2244 0.2253 -0.0120 -0.0055 0.0212  78  ILE A C   
1122 O O   . ILE A 75  ? 0.3234 0.2333 0.2291 -0.0098 -0.0159 0.0172  78  ILE A O   
1123 C CB  . ILE A 75  ? 0.4669 0.3569 0.3503 -0.0065 -0.0103 0.0325  78  ILE A CB  
1124 C CG1 . ILE A 75  ? 0.3280 0.2020 0.1923 -0.0047 -0.0034 0.0406  78  ILE A CG1 
1125 C CG2 . ILE A 75  ? 0.4433 0.3475 0.3547 -0.0085 -0.0145 0.0320  78  ILE A CG2 
1126 C CD1 . ILE A 75  ? 0.3977 0.2730 0.2779 -0.0091 0.0093  0.0439  78  ILE A CD1 
1138 N N   . TYR A 76  ? 0.2589 0.1761 0.1887 -0.0157 0.0010  0.0199  79  TYR A N   
1139 C CA  . TYR A 76  ? 0.3028 0.2328 0.2527 -0.0171 -0.0035 0.0153  79  TYR A CA  
1140 C C   . TYR A 76  ? 0.3912 0.3296 0.3548 -0.0166 -0.0119 0.0172  79  TYR A C   
1141 O O   . TYR A 76  ? 0.2100 0.1542 0.1869 -0.0181 -0.0091 0.0195  79  TYR A O   
1142 C CB  . TYR A 76  ? 0.2269 0.1630 0.1925 -0.0201 0.0058  0.0135  79  TYR A CB  
1143 C CG  . TYR A 76  ? 0.2648 0.1958 0.2229 -0.0206 0.0133  0.0093  79  TYR A CG  
1144 C CD1 . TYR A 76  ? 0.3236 0.2576 0.2850 -0.0203 0.0096  0.0039  79  TYR A CD1 
1145 C CD2 . TYR A 76  ? 0.2689 0.1917 0.2177 -0.0218 0.0251  0.0103  79  TYR A CD2 
1146 C CE1 . TYR A 76  ? 0.2480 0.1775 0.2035 -0.0206 0.0166  -0.0009 79  TYR A CE1 
1147 C CE2 . TYR A 76  ? 0.3750 0.2933 0.3174 -0.0223 0.0331  0.0058  79  TYR A CE2 
1148 C CZ  . TYR A 76  ? 0.3590 0.2809 0.3047 -0.0216 0.0285  -0.0001 79  TYR A CZ  
1149 O OH  . TYR A 76  ? 0.3052 0.2227 0.2454 -0.0220 0.0366  -0.0056 79  TYR A OH  
1159 N N   . TRP A 77  ? 0.2246 0.1640 0.1860 -0.0145 -0.0222 0.0153  80  TRP A N   
1160 C CA  . TRP A 77  ? 0.2232 0.1703 0.1979 -0.0140 -0.0295 0.0165  80  TRP A CA  
1161 C C   . TRP A 77  ? 0.1916 0.1505 0.1874 -0.0164 -0.0292 0.0145  80  TRP A C   
1162 O O   . TRP A 77  ? 0.2214 0.1871 0.2293 -0.0167 -0.0317 0.0160  80  TRP A O   
1163 C CB  . TRP A 77  ? 0.2218 0.1663 0.1895 -0.0108 -0.0408 0.0143  80  TRP A CB  
1164 C CG  . TRP A 77  ? 0.2244 0.1707 0.1931 -0.0109 -0.0450 0.0078  80  TRP A CG  
1165 C CD1 . TRP A 77  ? 0.3298 0.2678 0.2805 -0.0091 -0.0465 0.0041  80  TRP A CD1 
1166 C CD2 . TRP A 77  ? 0.2527 0.2088 0.2415 -0.0129 -0.0477 0.0038  80  TRP A CD2 
1167 N NE1 . TRP A 77  ? 0.3129 0.2558 0.2733 -0.0100 -0.0506 -0.0027 80  TRP A NE1 
1168 C CE2 . TRP A 77  ? 0.3746 0.3281 0.3588 -0.0125 -0.0510 -0.0026 80  TRP A CE2 
1169 C CE3 . TRP A 77  ? 0.2581 0.2239 0.2673 -0.0151 -0.0469 0.0051  80  TRP A CE3 
1170 C CZ2 . TRP A 77  ? 0.3976 0.3578 0.3996 -0.0145 -0.0532 -0.0075 80  TRP A CZ2 
1171 C CZ3 . TRP A 77  ? 0.1834 0.1551 0.2077 -0.0168 -0.0485 0.0012  80  TRP A CZ3 
1172 C CH2 . TRP A 77  ? 0.2392 0.2079 0.2610 -0.0167 -0.0514 -0.0049 80  TRP A CH2 
1183 N N   . ALA A 78  ? 0.1892 0.1497 0.1888 -0.0178 -0.0257 0.0114  81  ALA A N   
1184 C CA  . ALA A 78  ? 0.2221 0.1917 0.2395 -0.0194 -0.0255 0.0106  81  ALA A CA  
1185 C C   . ALA A 78  ? 0.2191 0.1948 0.2462 -0.0203 -0.0211 0.0139  81  ALA A C   
1186 O O   . ALA A 78  ? 0.1519 0.1347 0.1909 -0.0207 -0.0221 0.0146  81  ALA A O   
1187 C CB  . ALA A 78  ? 0.3115 0.2799 0.3308 -0.0202 -0.0225 0.0070  81  ALA A CB  
1193 N N   . ARG A 79  ? 0.1653 0.1379 0.1874 -0.0205 -0.0160 0.0156  82  ARG A N   
1194 C CA  . ARG A 79  ? 0.1624 0.1414 0.1950 -0.0212 -0.0129 0.0171  82  ARG A CA  
1195 C C   . ARG A 79  ? 0.1677 0.1522 0.2065 -0.0207 -0.0177 0.0186  82  ARG A C   
1196 O O   . ARG A 79  ? 0.1894 0.1815 0.2382 -0.0208 -0.0176 0.0187  82  ARG A O   
1197 C CB  . ARG A 79  ? 0.2544 0.2285 0.2825 -0.0219 -0.0065 0.0179  82  ARG A CB  
1198 C CG  . ARG A 79  ? 0.2453 0.2147 0.2696 -0.0227 0.0007  0.0159  82  ARG A CG  
1199 C CD  . ARG A 79  ? 0.2025 0.1689 0.2284 -0.0242 0.0087  0.0165  82  ARG A CD  
1200 N NE  . ARG A 79  ? 0.2685 0.2289 0.2894 -0.0252 0.0173  0.0145  82  ARG A NE  
1201 C CZ  . ARG A 79  ? 0.2473 0.2129 0.2796 -0.0258 0.0209  0.0107  82  ARG A CZ  
1202 N NH1 . ARG A 79  ? 0.3043 0.2804 0.3518 -0.0249 0.0161  0.0092  82  ARG A NH1 
1203 N NH2 . ARG A 79  ? 0.3448 0.3045 0.3728 -0.0269 0.0299  0.0084  82  ARG A NH2 
1217 N N   . TYR A 80  ? 0.1535 0.1340 0.1860 -0.0197 -0.0221 0.0195  83  TYR A N   
1218 C CA  . TYR A 80  ? 0.1477 0.1332 0.1874 -0.0191 -0.0258 0.0202  83  TYR A CA  
1219 C C   . TYR A 80  ? 0.1951 0.1873 0.2441 -0.0194 -0.0290 0.0190  83  TYR A C   
1220 O O   . TYR A 80  ? 0.1407 0.1395 0.1984 -0.0196 -0.0290 0.0193  83  TYR A O   
1221 C CB  . TYR A 80  ? 0.1878 0.1665 0.2193 -0.0173 -0.0300 0.0215  83  TYR A CB  
1222 C CG  . TYR A 80  ? 0.1988 0.1684 0.2195 -0.0171 -0.0252 0.0240  83  TYR A CG  
1223 C CD1 . TYR A 80  ? 0.2444 0.2143 0.2704 -0.0177 -0.0216 0.0255  83  TYR A CD1 
1224 C CD2 . TYR A 80  ? 0.1818 0.1419 0.1874 -0.0165 -0.0233 0.0245  83  TYR A CD2 
1225 C CE1 . TYR A 80  ? 0.2877 0.2484 0.3058 -0.0180 -0.0156 0.0280  83  TYR A CE1 
1226 C CE2 . TYR A 80  ? 0.1943 0.1448 0.1892 -0.0166 -0.0169 0.0274  83  TYR A CE2 
1227 C CZ  . TYR A 80  ? 0.2457 0.1963 0.2479 -0.0176 -0.0127 0.0294  83  TYR A CZ  
1228 O OH  . TYR A 80  ? 0.3212 0.2614 0.3148 -0.0182 -0.0047 0.0325  83  TYR A OH  
1238 N N   . ALA A 81  ? 0.1435 0.1337 0.1912 -0.0196 -0.0310 0.0172  84  ALA A N   
1239 C CA  . ALA A 81  ? 0.1615 0.1569 0.2199 -0.0205 -0.0320 0.0162  84  ALA A CA  
1240 C C   . ALA A 81  ? 0.1610 0.1609 0.2247 -0.0211 -0.0271 0.0182  84  ALA A C   
1241 O O   . ALA A 81  ? 0.2488 0.2535 0.3200 -0.0214 -0.0261 0.0194  84  ALA A O   
1242 C CB  . ALA A 81  ? 0.2121 0.2039 0.2695 -0.0208 -0.0348 0.0130  84  ALA A CB  
1248 N N   . ASP A 82  ? 0.2172 0.2150 0.2768 -0.0208 -0.0238 0.0185  85  ASP A N   
1249 C CA  . ASP A 82  ? 0.1342 0.1365 0.1985 -0.0202 -0.0207 0.0200  85  ASP A CA  
1250 C C   . ASP A 82  ? 0.1566 0.1645 0.2232 -0.0196 -0.0208 0.0209  85  ASP A C   
1251 O O   . ASP A 82  ? 0.1260 0.1383 0.1961 -0.0189 -0.0206 0.0224  85  ASP A O   
1252 C CB  . ASP A 82  ? 0.2160 0.2157 0.2780 -0.0200 -0.0176 0.0188  85  ASP A CB  
1253 C CG  . ASP A 82  ? 0.2105 0.2153 0.2785 -0.0184 -0.0161 0.0195  85  ASP A CG  
1254 O OD1 . ASP A 82  ? 0.1221 0.1322 0.1926 -0.0173 -0.0175 0.0210  85  ASP A OD1 
1255 O OD2 . ASP A 82  ? 0.1929 0.1966 0.2630 -0.0179 -0.0138 0.0179  85  ASP A OD2 
1260 N N   . TRP A 83  ? 0.1219 0.1288 0.1860 -0.0198 -0.0205 0.0199  86  TRP A N   
1261 C CA  . TRP A 83  ? 0.1178 0.1300 0.1855 -0.0193 -0.0203 0.0194  86  TRP A CA  
1262 C C   . TRP A 83  ? 0.1881 0.2036 0.2585 -0.0191 -0.0223 0.0198  86  TRP A C   
1263 O O   . TRP A 83  ? 0.1146 0.1357 0.1879 -0.0184 -0.0218 0.0191  86  TRP A O   
1264 C CB  . TRP A 83  ? 0.1206 0.1292 0.1867 -0.0199 -0.0187 0.0183  86  TRP A CB  
1265 C CG  . TRP A 83  ? 0.1235 0.1294 0.1891 -0.0205 -0.0149 0.0173  86  TRP A CG  
1266 C CD1 . TRP A 83  ? 0.1216 0.1306 0.1910 -0.0198 -0.0138 0.0163  86  TRP A CD1 
1267 C CD2 . TRP A 83  ? 0.1304 0.1294 0.1922 -0.0216 -0.0109 0.0172  86  TRP A CD2 
1268 N NE1 . TRP A 83  ? 0.1652 0.1710 0.2356 -0.0208 -0.0093 0.0147  86  TRP A NE1 
1269 C CE2 . TRP A 83  ? 0.1668 0.1661 0.2319 -0.0222 -0.0067 0.0154  86  TRP A CE2 
1270 C CE3 . TRP A 83  ? 0.1578 0.1496 0.2136 -0.0220 -0.0101 0.0188  86  TRP A CE3 
1271 C CZ2 . TRP A 83  ? 0.1694 0.1622 0.2323 -0.0237 -0.0002 0.0148  86  TRP A CZ2 
1272 C CZ3 . TRP A 83  ? 0.1692 0.1533 0.2205 -0.0232 -0.0039 0.0194  86  TRP A CZ3 
1273 C CH2 . TRP A 83  ? 0.1972 0.1819 0.2522 -0.0243 0.0016  0.0172  86  TRP A CH2 
1284 N N   . LEU A 84  ? 0.1417 0.1542 0.2119 -0.0197 -0.0245 0.0200  87  LEU A N   
1285 C CA  . LEU A 84  ? 0.1157 0.1320 0.1919 -0.0197 -0.0257 0.0195  87  LEU A CA  
1286 C C   . LEU A 84  ? 0.2781 0.2993 0.3575 -0.0197 -0.0227 0.0207  87  LEU A C   
1287 O O   . LEU A 84  ? 0.2197 0.2454 0.3027 -0.0195 -0.0214 0.0200  87  LEU A O   
1288 C CB  . LEU A 84  ? 0.1866 0.1996 0.2646 -0.0201 -0.0296 0.0185  87  LEU A CB  
1289 C CG  . LEU A 84  ? 0.2681 0.2856 0.3563 -0.0203 -0.0307 0.0169  87  LEU A CG  
1290 C CD1 . LEU A 84  ? 0.2408 0.2602 0.3316 -0.0191 -0.0320 0.0157  87  LEU A CD1 
1291 C CD2 . LEU A 84  ? 0.2911 0.3064 0.3836 -0.0206 -0.0354 0.0146  87  LEU A CD2 
1303 N N   . PHE A 85  ? 0.1329 0.1524 0.2104 -0.0197 -0.0212 0.0226  88  PHE A N   
1304 C CA  . PHE A 85  ? 0.2459 0.2674 0.3241 -0.0192 -0.0178 0.0253  88  PHE A CA  
1305 C C   . PHE A 85  ? 0.1384 0.1620 0.2110 -0.0167 -0.0172 0.0267  88  PHE A C   
1306 O O   . PHE A 85  ? 0.2928 0.3188 0.3624 -0.0152 -0.0150 0.0287  88  PHE A O   
1307 C CB  . PHE A 85  ? 0.2194 0.2366 0.3009 -0.0204 -0.0166 0.0269  88  PHE A CB  
1308 C CG  . PHE A 85  ? 0.2346 0.2512 0.3243 -0.0225 -0.0179 0.0245  88  PHE A CG  
1309 C CD1 . PHE A 85  ? 0.2786 0.2984 0.3758 -0.0236 -0.0149 0.0244  88  PHE A CD1 
1310 C CD2 . PHE A 85  ? 0.3034 0.3164 0.3935 -0.0232 -0.0221 0.0215  88  PHE A CD2 
1311 C CE1 . PHE A 85  ? 0.4342 0.4548 0.5425 -0.0254 -0.0168 0.0209  88  PHE A CE1 
1312 C CE2 . PHE A 85  ? 0.3385 0.3518 0.4369 -0.0244 -0.0251 0.0182  88  PHE A CE2 
1313 C CZ  . PHE A 85  ? 0.2295 0.2470 0.3387 -0.0256 -0.0227 0.0176  88  PHE A CZ  
1323 N N   . THR A 86  ? 0.1331 0.1559 0.2042 -0.0160 -0.0190 0.0254  89  THR A N   
1324 C CA  . THR A 86  ? 0.1576 0.1833 0.2262 -0.0131 -0.0197 0.0256  89  THR A CA  
1325 C C   . THR A 86  ? 0.1541 0.1857 0.2225 -0.0121 -0.0211 0.0222  89  THR A C   
1326 O O   . THR A 86  ? 0.1721 0.2075 0.2370 -0.0091 -0.0224 0.0221  89  THR A O   
1327 C CB  . THR A 86  ? 0.1188 0.1421 0.1895 -0.0128 -0.0203 0.0246  89  THR A CB  
1328 O OG1 . THR A 86  ? 0.1181 0.1396 0.1904 -0.0151 -0.0199 0.0216  89  THR A OG1 
1329 C CG2 . THR A 86  ? 0.1220 0.1398 0.1932 -0.0131 -0.0190 0.0274  89  THR A CG2 
1337 N N   . THR A 87  ? 0.1518 0.1837 0.2235 -0.0140 -0.0212 0.0192  90  THR A N   
1338 C CA  . THR A 87  ? 0.1851 0.2221 0.2588 -0.0132 -0.0223 0.0150  90  THR A CA  
1339 C C   . THR A 87  ? 0.1679 0.2090 0.2383 -0.0119 -0.0217 0.0148  90  THR A C   
1340 O O   . THR A 87  ? 0.1885 0.2347 0.2568 -0.0096 -0.0232 0.0117  90  THR A O   
1341 C CB  . THR A 87  ? 0.1462 0.1809 0.2247 -0.0154 -0.0218 0.0125  90  THR A CB  
1342 O OG1 . THR A 87  ? 0.1100 0.1401 0.1877 -0.0169 -0.0215 0.0147  90  THR A OG1 
1343 C CG2 . THR A 87  ? 0.1320 0.1634 0.2129 -0.0163 -0.0209 0.0116  90  THR A CG2 
1351 N N   . PRO A 88  ? 0.2502 0.2895 0.3205 -0.0133 -0.0193 0.0172  91  PRO A N   
1352 C CA  . PRO A 88  ? 0.2332 0.2760 0.3000 -0.0121 -0.0167 0.0171  91  PRO A CA  
1353 C C   . PRO A 88  ? 0.3030 0.3460 0.3598 -0.0090 -0.0161 0.0203  91  PRO A C   
1354 O O   . PRO A 88  ? 0.1738 0.2205 0.2237 -0.0065 -0.0157 0.0186  91  PRO A O   
1355 C CB  . PRO A 88  ? 0.1900 0.2302 0.2619 -0.0146 -0.0136 0.0191  91  PRO A CB  
1356 C CG  . PRO A 88  ? 0.3167 0.3532 0.3945 -0.0165 -0.0166 0.0186  91  PRO A CG  
1357 C CD  . PRO A 88  ? 0.1820 0.2164 0.2561 -0.0157 -0.0188 0.0191  91  PRO A CD  
1365 N N   . LEU A 89  ? 0.1875 0.2259 0.2426 -0.0086 -0.0161 0.0250  92  LEU A N   
1366 C CA  . LEU A 89  ? 0.2173 0.2541 0.2624 -0.0049 -0.0159 0.0294  92  LEU A CA  
1367 C C   . LEU A 89  ? 0.1923 0.2340 0.2330 -0.0008 -0.0215 0.0257  92  LEU A C   
1368 O O   . LEU A 89  ? 0.2732 0.3160 0.3025 0.0034  -0.0225 0.0270  92  LEU A O   
1369 C CB  . LEU A 89  ? 0.1434 0.1737 0.1904 -0.0052 -0.0151 0.0344  92  LEU A CB  
1370 C CG  . LEU A 89  ? 0.2827 0.3082 0.3348 -0.0088 -0.0098 0.0376  92  LEU A CG  
1371 C CD1 . LEU A 89  ? 0.1855 0.2050 0.2421 -0.0095 -0.0100 0.0403  92  LEU A CD1 
1372 C CD2 . LEU A 89  ? 0.2636 0.2871 0.3087 -0.0080 -0.0036 0.0420  92  LEU A CD2 
1384 N N   . LEU A 90  ? 0.1767 0.2211 0.2263 -0.0017 -0.0252 0.0209  93  LEU A N   
1385 C CA  . LEU A 90  ? 0.1431 0.1935 0.1933 0.0017  -0.0308 0.0157  93  LEU A CA  
1386 C C   . LEU A 90  ? 0.1427 0.1988 0.1894 0.0027  -0.0318 0.0101  93  LEU A C   
1387 O O   . LEU A 90  ? 0.2005 0.2610 0.2403 0.0073  -0.0364 0.0072  93  LEU A O   
1388 C CB  . LEU A 90  ? 0.2093 0.2608 0.2724 -0.0006 -0.0323 0.0114  93  LEU A CB  
1389 C CG  . LEU A 90  ? 0.3525 0.3995 0.4191 -0.0006 -0.0321 0.0148  93  LEU A CG  
1390 C CD1 . LEU A 90  ? 0.2272 0.2733 0.3048 -0.0042 -0.0303 0.0113  93  LEU A CD1 
1391 C CD2 . LEU A 90  ? 0.1361 0.1858 0.2008 0.0049  -0.0374 0.0148  93  LEU A CD2 
1403 N N   . LEU A 91  ? 0.1740 0.2303 0.2256 -0.0010 -0.0281 0.0081  94  LEU A N   
1404 C CA  . LEU A 91  ? 0.2395 0.3009 0.2886 -0.0001 -0.0280 0.0024  94  LEU A CA  
1405 C C   . LEU A 91  ? 0.1844 0.2453 0.2177 0.0032  -0.0256 0.0057  94  LEU A C   
1406 O O   . LEU A 91  ? 0.1647 0.2301 0.1896 0.0066  -0.0280 0.0009  94  LEU A O   
1407 C CB  . LEU A 91  ? 0.2310 0.2916 0.2896 -0.0043 -0.0243 0.0004  94  LEU A CB  
1408 C CG  . LEU A 91  ? 0.2847 0.3444 0.3565 -0.0072 -0.0257 -0.0029 94  LEU A CG  
1409 C CD1 . LEU A 91  ? 0.2216 0.2789 0.3004 -0.0101 -0.0227 -0.0034 94  LEU A CD1 
1410 C CD2 . LEU A 91  ? 0.2166 0.2821 0.2940 -0.0057 -0.0297 -0.0108 94  LEU A CD2 
1422 N N   . LEU A 92  ? 0.1756 0.2302 0.2040 0.0022  -0.0205 0.0137  95  LEU A N   
1423 C CA  . LEU A 92  ? 0.1884 0.2405 0.2012 0.0049  -0.0160 0.0182  95  LEU A CA  
1424 C C   . LEU A 92  ? 0.2777 0.3296 0.2756 0.0113  -0.0215 0.0199  95  LEU A C   
1425 O O   . LEU A 92  ? 0.3076 0.3599 0.2890 0.0154  -0.0208 0.0196  95  LEU A O   
1426 C CB  . LEU A 92  ? 0.2661 0.3108 0.2804 0.0020  -0.0089 0.0262  95  LEU A CB  
1427 C CG  . LEU A 92  ? 0.6423 0.6827 0.6435 0.0032  -0.0005 0.0316  95  LEU A CG  
1428 C CD1 . LEU A 92  ? 0.5424 0.5878 0.5393 0.0033  0.0032  0.0257  95  LEU A CD1 
1429 C CD2 . LEU A 92  ? 0.6317 0.6662 0.6422 -0.0013 0.0069  0.0372  95  LEU A CD2 
1441 N N   . ASP A 93  ? 0.2934 0.3444 0.2961 0.0129  -0.0274 0.0213  96  ASP A N   
1442 C CA  . ASP A 93  ? 0.2639 0.3157 0.2553 0.0198  -0.0348 0.0218  96  ASP A CA  
1443 C C   . ASP A 93  ? 0.3686 0.4290 0.3560 0.0232  -0.0411 0.0121  96  ASP A C   
1444 O O   . ASP A 93  ? 0.2942 0.3546 0.2633 0.0296  -0.0448 0.0124  96  ASP A O   
1445 C CB  . ASP A 93  ? 0.3569 0.4086 0.3604 0.0203  -0.0402 0.0222  96  ASP A CB  
1446 C CG  . ASP A 93  ? 0.2500 0.2925 0.2476 0.0223  -0.0380 0.0323  96  ASP A CG  
1447 O OD1 . ASP A 93  ? 0.2538 0.2898 0.2352 0.0248  -0.0338 0.0396  96  ASP A OD1 
1448 O OD2 . ASP A 93  ? 0.2541 0.2952 0.2638 0.0212  -0.0397 0.0330  96  ASP A OD2 
1453 N N   . LEU A 94  ? 0.2148 0.2818 0.2185 0.0194  -0.0425 0.0032  97  LEU A N   
1454 C CA  . LEU A 94  ? 0.3075 0.3829 0.3109 0.0219  -0.0483 -0.0076 97  LEU A CA  
1455 C C   . LEU A 94  ? 0.2667 0.3422 0.2555 0.0227  -0.0434 -0.0091 97  LEU A C   
1456 O O   . LEU A 94  ? 0.3283 0.4076 0.3028 0.0283  -0.0482 -0.0140 97  LEU A O   
1457 C CB  . LEU A 94  ? 0.2806 0.3612 0.3069 0.0169  -0.0492 -0.0159 97  LEU A CB  
1458 C CG  . LEU A 94  ? 0.2555 0.3369 0.2975 0.0160  -0.0531 -0.0165 97  LEU A CG  
1459 C CD1 . LEU A 94  ? 0.2383 0.3210 0.3003 0.0099  -0.0501 -0.0218 97  LEU A CD1 
1460 C CD2 . LEU A 94  ? 0.2602 0.3483 0.3019 0.0222  -0.0634 -0.0226 97  LEU A CD2 
1472 N N   . ALA A 95  ? 0.2018 0.2737 0.1943 0.0176  -0.0338 -0.0056 98  ALA A N   
1473 C CA  . ALA A 95  ? 0.2508 0.3234 0.2332 0.0177  -0.0276 -0.0081 98  ALA A CA  
1474 C C   . ALA A 95  ? 0.3152 0.3827 0.2712 0.0230  -0.0249 -0.0016 98  ALA A C   
1475 O O   . ALA A 95  ? 0.4043 0.4742 0.3449 0.0266  -0.0244 -0.0066 98  ALA A O   
1476 C CB  . ALA A 95  ? 0.1958 0.2657 0.1908 0.0113  -0.0185 -0.0056 98  ALA A CB  
1482 N N   . LEU A 96  ? 0.3662 0.4256 0.3157 0.0239  -0.0225 0.0095  99  LEU A N   
1483 C CA  . LEU A 96  ? 0.3088 0.3610 0.2320 0.0294  -0.0193 0.0174  99  LEU A CA  
1484 C C   . LEU A 96  ? 0.4360 0.4911 0.3425 0.0380  -0.0311 0.0137  99  LEU A C   
1485 O O   . LEU A 96  ? 0.3705 0.4220 0.2509 0.0438  -0.0299 0.0159  99  LEU A O   
1486 C CB  . LEU A 96  ? 0.4007 0.4427 0.3238 0.0282  -0.0144 0.0301  99  LEU A CB  
1487 C CG  . LEU A 96  ? 0.4991 0.5376 0.4377 0.0205  -0.0032 0.0340  99  LEU A CG  
1488 C CD1 . LEU A 96  ? 0.4052 0.4331 0.3418 0.0203  0.0013  0.0458  99  LEU A CD1 
1489 C CD2 . LEU A 96  ? 0.5908 0.6295 0.5234 0.0184  0.0076  0.0321  99  LEU A CD2 
1501 N N   . LEU A 97  ? 0.2672 0.3288 0.1885 0.0391  -0.0423 0.0078  100 LEU A N   
1502 C CA  . LEU A 97  ? 0.3607 0.4269 0.2707 0.0474  -0.0553 0.0025  100 LEU A CA  
1503 C C   . LEU A 97  ? 0.4413 0.5140 0.3389 0.0504  -0.0577 -0.0083 100 LEU A C   
1504 O O   . LEU A 97  ? 0.5356 0.6070 0.4078 0.0587  -0.0635 -0.0086 100 LEU A O   
1505 C CB  . LEU A 97  ? 0.3584 0.4321 0.2933 0.0464  -0.0651 -0.0043 100 LEU A CB  
1506 C CG  . LEU A 97  ? 0.4120 0.4892 0.3425 0.0549  -0.0793 -0.0071 100 LEU A CG  
1507 C CD1 . LEU A 97  ? 0.4802 0.5466 0.3894 0.0614  -0.0798 0.0062  100 LEU A CD1 
1508 C CD2 . LEU A 97  ? 0.5782 0.6622 0.5389 0.0516  -0.0847 -0.0131 100 LEU A CD2 
1520 N N   . VAL A 98  ? 0.3786 0.4578 0.2932 0.0443  -0.0539 -0.0176 101 VAL A N   
1521 C CA  . VAL A 98  ? 0.4385 0.5246 0.3456 0.0465  -0.0560 -0.0298 101 VAL A CA  
1522 C C   . VAL A 98  ? 0.4614 0.5424 0.3523 0.0448  -0.0427 -0.0266 101 VAL A C   
1523 O O   . VAL A 98  ? 0.5079 0.5941 0.3931 0.0458  -0.0420 -0.0369 101 VAL A O   
1524 C CB  . VAL A 98  ? 0.4557 0.5517 0.3922 0.0413  -0.0596 -0.0429 101 VAL A CB  
1525 C CG1 . VAL A 98  ? 0.5258 0.6276 0.4781 0.0434  -0.0721 -0.0477 101 VAL A CG1 
1526 C CG2 . VAL A 98  ? 0.3236 0.4167 0.2809 0.0324  -0.0491 -0.0391 101 VAL A CG2 
1536 N N   . ASP A 99  ? 0.3739 0.4452 0.2593 0.0421  -0.0317 -0.0135 102 ASP A N   
1537 C CA  . ASP A 99  ? 0.4026 0.4689 0.2756 0.0400  -0.0173 -0.0100 102 ASP A CA  
1538 C C   . ASP A 99  ? 0.4445 0.5180 0.3382 0.0338  -0.0121 -0.0204 102 ASP A C   
1539 O O   . ASP A 99  ? 0.4471 0.5230 0.3304 0.0349  -0.0071 -0.0275 102 ASP A O   
1540 C CB  . ASP A 99  ? 0.5356 0.5981 0.3724 0.0481  -0.0170 -0.0096 102 ASP A CB  
1541 C CG  . ASP A 99  ? 0.6706 0.7246 0.4918 0.0461  0.0004  -0.0023 102 ASP A CG  
1542 O OD1 . ASP A 99  ? 1.0042 1.0578 0.8463 0.0383  0.0111  -0.0004 102 ASP A OD1 
1543 O OD2 . ASP A 99  ? 1.0635 1.1110 0.8515 0.0526  0.0035  0.0013  102 ASP A OD2 
1548 N N   . ALA A 100 ? 0.3644 0.4405 0.2870 0.0276  -0.0132 -0.0213 103 ALA A N   
1549 C CA  . ALA A 100 ? 0.4260 0.5076 0.3700 0.0222  -0.0092 -0.0299 103 ALA A CA  
1550 C C   . ALA A 100 ? 0.4948 0.5726 0.4373 0.0188  0.0051  -0.0261 103 ALA A C   
1551 O O   . ALA A 100 ? 0.3310 0.4012 0.2643 0.0183  0.0128  -0.0152 103 ALA A O   
1552 C CB  . ALA A 100 ? 0.3673 0.4503 0.3391 0.0170  -0.0133 -0.0296 103 ALA A CB  
1558 N N   . ASP A 101 ? 0.3880 0.4710 0.3417 0.0165  0.0092  -0.0358 104 ASP A N   
1559 C CA  . ASP A 101 ? 0.5158 0.5968 0.4731 0.0131  0.0228  -0.0343 104 ASP A CA  
1560 C C   . ASP A 101 ? 0.4031 0.4814 0.3840 0.0072  0.0260  -0.0275 104 ASP A C   
1561 O O   . ASP A 101 ? 0.3935 0.4725 0.3899 0.0054  0.0179  -0.0264 104 ASP A O   
1562 C CB  . ASP A 101 ? 0.4551 0.5429 0.4203 0.0127  0.0255  -0.0476 104 ASP A CB  
1563 C CG  . ASP A 101 ? 0.3650 0.4580 0.3580 0.0097  0.0178  -0.0551 104 ASP A CG  
1564 O OD1 . ASP A 101 ? 0.5785 0.6705 0.5935 0.0051  0.0209  -0.0524 104 ASP A OD1 
1565 O OD2 . ASP A 101 ? 0.5052 0.6029 0.4983 0.0121  0.0086  -0.0639 104 ASP A OD2 
1570 N N   A GLN A 102 ? 0.4371 0.5124 0.4208 0.0044  0.0384  -0.0234 105 GLN A N   
1571 N N   B GLN A 102 ? 0.4369 0.5122 0.4206 0.0044  0.0384  -0.0234 105 GLN A N   
1572 C CA  A GLN A 102 ? 0.4304 0.5034 0.4357 -0.0006 0.0411  -0.0174 105 GLN A CA  
1573 C CA  B GLN A 102 ? 0.4301 0.5031 0.4354 -0.0006 0.0410  -0.0174 105 GLN A CA  
1574 C C   A GLN A 102 ? 0.4608 0.5390 0.4928 -0.0035 0.0354  -0.0244 105 GLN A C   
1575 C C   B GLN A 102 ? 0.4611 0.5393 0.4931 -0.0036 0.0354  -0.0243 105 GLN A C   
1576 O O   A GLN A 102 ? 0.3417 0.4180 0.3881 -0.0060 0.0302  -0.0203 105 GLN A O   
1577 O O   B GLN A 102 ? 0.3414 0.4177 0.3880 -0.0061 0.0303  -0.0203 105 GLN A O   
1578 C CB  A GLN A 102 ? 0.5911 0.6610 0.5972 -0.0032 0.0560  -0.0137 105 GLN A CB  
1579 C CB  B GLN A 102 ? 0.5914 0.6612 0.5974 -0.0032 0.0559  -0.0135 105 GLN A CB  
1580 C CG  A GLN A 102 ? 0.7053 0.7671 0.6856 -0.0008 0.0634  -0.0040 105 GLN A CG  
1581 C CG  B GLN A 102 ? 0.7055 0.7670 0.6860 -0.0008 0.0629  -0.0036 105 GLN A CG  
1582 C CD  A GLN A 102 ? 0.7720 0.8334 0.7245 0.0041  0.0681  -0.0077 105 GLN A CD  
1583 C CD  B GLN A 102 ? 0.7239 0.7818 0.7066 -0.0039 0.0799  -0.0002 105 GLN A CD  
1584 O OE1 A GLN A 102 ? 0.7358 0.8041 0.6897 0.0055  0.0656  -0.0188 105 GLN A OE1 
1585 O OE1 B GLN A 102 ? 0.7045 0.7677 0.7022 -0.0064 0.0873  -0.0077 105 GLN A OE1 
1586 N NE2 A GLN A 102 ? 0.7841 0.8367 0.7104 0.0071  0.0747  0.0015  105 GLN A NE2 
1587 N NE2 B GLN A 102 ? 0.8668 0.9154 0.8361 -0.0037 0.0869  0.0110  105 GLN A NE2 
1604 N N   . GLY A 103 ? 0.4170 0.5007 0.4549 -0.0029 0.0363  -0.0348 106 GLY A N   
1605 C CA  . GLY A 103 ? 0.3849 0.4719 0.4475 -0.0050 0.0311  -0.0408 106 GLY A CA  
1606 C C   . GLY A 103 ? 0.3779 0.4641 0.4441 -0.0046 0.0192  -0.0401 106 GLY A C   
1607 O O   . GLY A 103 ? 0.2026 0.2869 0.2857 -0.0069 0.0150  -0.0380 106 GLY A O   
1611 N N   . THR A 104 ? 0.2336 0.3209 0.2837 -0.0014 0.0138  -0.0422 107 THR A N   
1612 C CA  . THR A 104 ? 0.2638 0.3509 0.3192 -0.0013 0.0037  -0.0425 107 THR A CA  
1613 C C   . THR A 104 ? 0.2020 0.2836 0.2585 -0.0030 0.0014  -0.0318 107 THR A C   
1614 O O   . THR A 104 ? 0.2810 0.3608 0.3498 -0.0048 -0.0038 -0.0308 107 THR A O   
1615 C CB  . THR A 104 ? 0.2983 0.3889 0.3379 0.0030  -0.0020 -0.0479 107 THR A CB  
1616 O OG1 . THR A 104 ? 0.4351 0.5310 0.4744 0.0045  -0.0006 -0.0595 107 THR A OG1 
1617 C CG2 . THR A 104 ? 0.2653 0.3564 0.3138 0.0027  -0.0115 -0.0490 107 THR A CG2 
1625 N N   . ILE A 105 ? 0.2588 0.3368 0.3021 -0.0024 0.0060  -0.0239 108 ILE A N   
1626 C CA  . ILE A 105 ? 0.2026 0.2753 0.2474 -0.0039 0.0042  -0.0146 108 ILE A CA  
1627 C C   . ILE A 105 ? 0.2052 0.2760 0.2693 -0.0079 0.0053  -0.0130 108 ILE A C   
1628 O O   . ILE A 105 ? 0.2552 0.3231 0.3265 -0.0093 0.0001  -0.0099 108 ILE A O   
1629 C CB  . ILE A 105 ? 0.3401 0.4083 0.3682 -0.0025 0.0101  -0.0065 108 ILE A CB  
1630 C CG1 . ILE A 105 ? 0.2470 0.3155 0.2539 0.0028  0.0057  -0.0065 108 ILE A CG1 
1631 C CG2 . ILE A 105 ? 0.2530 0.3155 0.2871 -0.0049 0.0100  0.0021  108 ILE A CG2 
1632 C CD1 . ILE A 105 ? 0.4391 0.5022 0.4249 0.0054  0.0131  0.0006  108 ILE A CD1 
1644 N N   . LEU A 106 ? 0.2241 0.2966 0.2969 -0.0094 0.0119  -0.0155 109 LEU A N   
1645 C CA  A LEU A 106 ? 0.2741 0.3455 0.3660 -0.0123 0.0114  -0.0147 109 LEU A CA  
1646 C CA  B LEU A 106 ? 0.2738 0.3452 0.3658 -0.0123 0.0114  -0.0148 109 LEU A CA  
1647 C C   . LEU A 106 ? 0.1875 0.2586 0.2903 -0.0123 0.0038  -0.0183 109 LEU A C   
1648 O O   . LEU A 106 ? 0.2680 0.3354 0.3795 -0.0137 -0.0003 -0.0149 109 LEU A O   
1649 C CB  A LEU A 106 ? 0.2857 0.3604 0.3878 -0.0133 0.0195  -0.0186 109 LEU A CB  
1650 C CB  B LEU A 106 ? 0.2854 0.3603 0.3876 -0.0133 0.0195  -0.0189 109 LEU A CB  
1651 C CG  A LEU A 106 ? 0.2318 0.3064 0.3556 -0.0155 0.0181  -0.0189 109 LEU A CG  
1652 C CG  B LEU A 106 ? 0.2983 0.3720 0.3946 -0.0144 0.0295  -0.0144 109 LEU A CG  
1653 C CD1 A LEU A 106 ? 0.2736 0.3438 0.3986 -0.0173 0.0166  -0.0116 109 LEU A CD1 
1654 C CD1 B LEU A 106 ? 0.2412 0.3192 0.3394 -0.0142 0.0393  -0.0207 109 LEU A CD1 
1655 C CD2 A LEU A 106 ? 0.2553 0.3346 0.3916 -0.0162 0.0265  -0.0242 109 LEU A CD2 
1656 C CD2 B LEU A 106 ? 0.3198 0.3910 0.4310 -0.0174 0.0298  -0.0100 109 LEU A CD2 
1679 N N   . ALA A 107 ? 0.2490 0.3234 0.3512 -0.0108 0.0021  -0.0252 110 ALA A N   
1680 C CA  . ALA A 107 ? 0.1841 0.2568 0.2972 -0.0111 -0.0037 -0.0283 110 ALA A CA  
1681 C C   . ALA A 107 ? 0.2201 0.2885 0.3285 -0.0115 -0.0091 -0.0233 110 ALA A C   
1682 O O   . ALA A 107 ? 0.2344 0.2979 0.3508 -0.0126 -0.0124 -0.0211 110 ALA A O   
1683 C CB  . ALA A 107 ? 0.2358 0.3131 0.3505 -0.0096 -0.0038 -0.0379 110 ALA A CB  
1689 N N   . LEU A 108 ? 0.2367 0.3064 0.3316 -0.0103 -0.0098 -0.0215 111 LEU A N   
1690 C CA  . LEU A 108 ? 0.1693 0.2357 0.2614 -0.0105 -0.0143 -0.0176 111 LEU A CA  
1691 C C   . LEU A 108 ? 0.1905 0.2510 0.2835 -0.0123 -0.0142 -0.0098 111 LEU A C   
1692 O O   . LEU A 108 ? 0.1775 0.2334 0.2748 -0.0135 -0.0170 -0.0077 111 LEU A O   
1693 C CB  . LEU A 108 ? 0.2433 0.3127 0.3219 -0.0079 -0.0159 -0.0178 111 LEU A CB  
1694 C CG  . LEU A 108 ? 0.3960 0.4712 0.4742 -0.0057 -0.0193 -0.0267 111 LEU A CG  
1695 C CD1 . LEU A 108 ? 0.2833 0.3613 0.3455 -0.0019 -0.0219 -0.0262 111 LEU A CD1 
1696 C CD2 . LEU A 108 ? 0.3506 0.4248 0.4417 -0.0074 -0.0230 -0.0299 111 LEU A CD2 
1708 N N   . VAL A 109 ? 0.1219 0.1822 0.2108 -0.0125 -0.0105 -0.0059 112 VAL A N   
1709 C CA  . VAL A 109 ? 0.2141 0.2695 0.3050 -0.0142 -0.0108 0.0002  112 VAL A CA  
1710 C C   . VAL A 109 ? 0.1509 0.2039 0.2541 -0.0155 -0.0129 -0.0007 112 VAL A C   
1711 O O   . VAL A 109 ? 0.1745 0.2223 0.2786 -0.0162 -0.0163 0.0025  112 VAL A O   
1712 C CB  . VAL A 109 ? 0.2033 0.2589 0.2897 -0.0145 -0.0053 0.0039  112 VAL A CB  
1713 C CG1 . VAL A 109 ? 0.3721 0.4234 0.4647 -0.0166 -0.0058 0.0082  112 VAL A CG1 
1714 C CG2 . VAL A 109 ? 0.2664 0.3219 0.3378 -0.0122 -0.0044 0.0066  112 VAL A CG2 
1724 N N   . GLY A 110 ? 0.1884 0.2445 0.3005 -0.0152 -0.0113 -0.0053 113 GLY A N   
1725 C CA  . GLY A 110 ? 0.1573 0.2108 0.2814 -0.0153 -0.0146 -0.0061 113 GLY A CA  
1726 C C   . GLY A 110 ? 0.1188 0.1666 0.2423 -0.0148 -0.0192 -0.0055 113 GLY A C   
1727 O O   . GLY A 110 ? 0.1721 0.2138 0.2967 -0.0147 -0.0231 -0.0022 113 GLY A O   
1731 N N   . ALA A 111 ? 0.1099 0.1593 0.2315 -0.0145 -0.0185 -0.0089 114 ALA A N   
1732 C CA  . ALA A 111 ? 0.1100 0.1535 0.2325 -0.0147 -0.0209 -0.0083 114 ALA A CA  
1733 C C   . ALA A 111 ? 0.2314 0.2701 0.3450 -0.0156 -0.0221 -0.0029 114 ALA A C   
1734 O O   . ALA A 111 ? 0.1116 0.1426 0.2244 -0.0158 -0.0236 0.0002  114 ALA A O   
1735 C CB  . ALA A 111 ? 0.2407 0.2882 0.3661 -0.0145 -0.0196 -0.0146 114 ALA A CB  
1741 N N   . ASP A 112 ? 0.1950 0.2374 0.3011 -0.0157 -0.0210 -0.0015 115 ASP A N   
1742 C CA  . ASP A 112 ? 0.1084 0.1465 0.2075 -0.0164 -0.0219 0.0029  115 ASP A CA  
1743 C C   . ASP A 112 ? 0.1534 0.1855 0.2514 -0.0168 -0.0238 0.0071  115 ASP A C   
1744 O O   . ASP A 112 ? 0.1698 0.1953 0.2635 -0.0172 -0.0249 0.0098  115 ASP A O   
1745 C CB  . ASP A 112 ? 0.1088 0.1514 0.2011 -0.0158 -0.0207 0.0038  115 ASP A CB  
1746 C CG  . ASP A 112 ? 0.1512 0.1905 0.2386 -0.0161 -0.0214 0.0069  115 ASP A CG  
1747 O OD1 . ASP A 112 ? 0.1853 0.2202 0.2700 -0.0169 -0.0217 0.0108  115 ASP A OD1 
1748 O OD2 . ASP A 112 ? 0.2937 0.3351 0.3814 -0.0156 -0.0219 0.0045  115 ASP A OD2 
1753 N N   . GLY A 113 ? 0.1747 0.2092 0.2768 -0.0167 -0.0240 0.0070  116 GLY A N   
1754 C CA  . GLY A 113 ? 0.1104 0.1405 0.2137 -0.0166 -0.0274 0.0094  116 GLY A CA  
1755 C C   . GLY A 113 ? 0.1350 0.1583 0.2391 -0.0153 -0.0313 0.0099  116 GLY A C   
1756 O O   . GLY A 113 ? 0.1695 0.1860 0.2676 -0.0147 -0.0347 0.0127  116 GLY A O   
1760 N N   . ILE A 114 ? 0.1150 0.1390 0.2256 -0.0144 -0.0308 0.0074  117 ILE A N   
1761 C CA  . ILE A 114 ? 0.1960 0.2116 0.3067 -0.0127 -0.0339 0.0090  117 ILE A CA  
1762 C C   . ILE A 114 ? 0.2192 0.2271 0.3198 -0.0135 -0.0319 0.0123  117 ILE A C   
1763 O O   . ILE A 114 ? 0.1484 0.1464 0.2413 -0.0123 -0.0342 0.0163  117 ILE A O   
1764 C CB  . ILE A 114 ? 0.2236 0.2416 0.3457 -0.0116 -0.0330 0.0051  117 ILE A CB  
1765 C CG1 . ILE A 114 ? 0.1187 0.1432 0.2523 -0.0104 -0.0348 0.0018  117 ILE A CG1 
1766 C CG2 . ILE A 114 ? 0.1298 0.1370 0.2510 -0.0099 -0.0349 0.0079  117 ILE A CG2 
1767 C CD1 . ILE A 114 ? 0.1889 0.2180 0.3347 -0.0097 -0.0324 -0.0037 117 ILE A CD1 
1779 N N   . MET A 115 ? 0.1216 0.1336 0.2219 -0.0154 -0.0276 0.0104  118 MET A N   
1780 C CA  . MET A 115 ? 0.1716 0.1775 0.2661 -0.0167 -0.0245 0.0124  118 MET A CA  
1781 C C   . MET A 115 ? 0.1300 0.1300 0.2129 -0.0168 -0.0253 0.0166  118 MET A C   
1782 O O   . MET A 115 ? 0.1394 0.1293 0.2146 -0.0166 -0.0241 0.0200  118 MET A O   
1783 C CB  . MET A 115 ? 0.1195 0.1332 0.2183 -0.0182 -0.0212 0.0082  118 MET A CB  
1784 C CG  . MET A 115 ? 0.1419 0.1516 0.2382 -0.0198 -0.0175 0.0090  118 MET A CG  
1785 S SD  . MET A 115 ? 0.1783 0.1990 0.2819 -0.0204 -0.0163 0.0028  118 MET A SD  
1786 C CE  . MET A 115 ? 0.1730 0.1971 0.2677 -0.0196 -0.0181 0.0057  118 MET A CE  
1796 N N   . ILE A 116 ? 0.1251 0.1305 0.2062 -0.0171 -0.0268 0.0163  119 ILE A N   
1797 C CA  . ILE A 116 ? 0.1294 0.1298 0.2010 -0.0172 -0.0276 0.0190  119 ILE A CA  
1798 C C   . ILE A 116 ? 0.1599 0.1534 0.2263 -0.0152 -0.0330 0.0209  119 ILE A C   
1799 O O   . ILE A 116 ? 0.1477 0.1325 0.2026 -0.0145 -0.0337 0.0234  119 ILE A O   
1800 C CB  . ILE A 116 ? 0.1605 0.1678 0.2336 -0.0180 -0.0274 0.0180  119 ILE A CB  
1801 C CG1 . ILE A 116 ? 0.1402 0.1538 0.2167 -0.0188 -0.0238 0.0162  119 ILE A CG1 
1802 C CG2 . ILE A 116 ? 0.2209 0.2230 0.2858 -0.0183 -0.0282 0.0196  119 ILE A CG2 
1803 C CD1 . ILE A 116 ? 0.1905 0.2004 0.2650 -0.0196 -0.0204 0.0161  119 ILE A CD1 
1815 N N   . GLY A 117 ? 0.1537 0.1513 0.2285 -0.0138 -0.0371 0.0193  120 GLY A N   
1816 C CA  . GLY A 117 ? 0.2076 0.2001 0.2800 -0.0111 -0.0440 0.0200  120 GLY A CA  
1817 C C   . GLY A 117 ? 0.2846 0.2652 0.3469 -0.0086 -0.0455 0.0238  120 GLY A C   
1818 O O   . GLY A 117 ? 0.2691 0.2411 0.3185 -0.0065 -0.0496 0.0262  120 GLY A O   
1822 N N   . THR A 118 ? 0.2184 0.1972 0.2856 -0.0087 -0.0420 0.0245  121 THR A N   
1823 C CA  . THR A 118 ? 0.1746 0.1401 0.2324 -0.0065 -0.0417 0.0292  121 THR A CA  
1824 C C   . THR A 118 ? 0.1807 0.1377 0.2237 -0.0082 -0.0357 0.0326  121 THR A C   
1825 O O   . THR A 118 ? 0.1983 0.1419 0.2262 -0.0058 -0.0361 0.0375  121 THR A O   
1826 C CB  . THR A 118 ? 0.1700 0.1357 0.2396 -0.0067 -0.0383 0.0283  121 THR A CB  
1827 O OG1 . THR A 118 ? 0.1584 0.1322 0.2358 -0.0106 -0.0315 0.0246  121 THR A OG1 
1828 C CG2 . THR A 118 ? 0.1793 0.1515 0.2629 -0.0043 -0.0441 0.0250  121 THR A CG2 
1836 N N   . GLY A 119 ? 0.2016 0.1656 0.2483 -0.0118 -0.0299 0.0300  122 GLY A N   
1837 C CA  . GLY A 119 ? 0.1777 0.1350 0.2128 -0.0135 -0.0238 0.0321  122 GLY A CA  
1838 C C   . GLY A 119 ? 0.2041 0.1556 0.2235 -0.0116 -0.0280 0.0337  122 GLY A C   
1839 O O   . GLY A 119 ? 0.2717 0.2117 0.2753 -0.0111 -0.0243 0.0371  122 GLY A O   
1843 N N   . LEU A 120 ? 0.1893 0.1482 0.2128 -0.0107 -0.0351 0.0307  123 LEU A N   
1844 C CA  . LEU A 120 ? 0.2261 0.1805 0.2369 -0.0088 -0.0404 0.0305  123 LEU A CA  
1845 C C   . LEU A 120 ? 0.2108 0.1533 0.2076 -0.0041 -0.0467 0.0340  123 LEU A C   
1846 O O   . LEU A 120 ? 0.2600 0.1923 0.2375 -0.0022 -0.0475 0.0359  123 LEU A O   
1847 C CB  . LEU A 120 ? 0.1793 0.1448 0.2021 -0.0092 -0.0461 0.0258  123 LEU A CB  
1848 C CG  . LEU A 120 ? 0.2506 0.2134 0.2655 -0.0072 -0.0536 0.0235  123 LEU A CG  
1849 C CD1 . LEU A 120 ? 0.2656 0.2229 0.2667 -0.0084 -0.0491 0.0233  123 LEU A CD1 
1850 C CD2 . LEU A 120 ? 0.3224 0.2965 0.3545 -0.0083 -0.0578 0.0187  123 LEU A CD2 
1862 N N   . VAL A 121 ? 0.2386 0.1819 0.2440 -0.0016 -0.0515 0.0348  124 VAL A N   
1863 C CA  . VAL A 121 ? 0.2304 0.1618 0.2230 0.0039  -0.0588 0.0387  124 VAL A CA  
1864 C C   . VAL A 121 ? 0.2497 0.1649 0.2229 0.0046  -0.0513 0.0456  124 VAL A C   
1865 O O   . VAL A 121 ? 0.2727 0.1749 0.2239 0.0087  -0.0550 0.0495  124 VAL A O   
1866 C CB  . VAL A 121 ? 0.2507 0.1865 0.2598 0.0064  -0.0645 0.0380  124 VAL A CB  
1867 C CG1 . VAL A 121 ? 0.2481 0.1696 0.2438 0.0129  -0.0715 0.0433  124 VAL A CG1 
1868 C CG2 . VAL A 121 ? 0.2105 0.1606 0.2373 0.0062  -0.0716 0.0312  124 VAL A CG2 
1878 N N   . GLY A 122 ? 0.2423 0.1580 0.2236 0.0006  -0.0406 0.0469  125 GLY A N   
1879 C CA  . GLY A 122 ? 0.2819 0.1824 0.2481 0.0002  -0.0311 0.0530  125 GLY A CA  
1880 C C   . GLY A 122 ? 0.2709 0.1658 0.2190 -0.0011 -0.0258 0.0534  125 GLY A C   
1881 O O   . GLY A 122 ? 0.3044 0.1834 0.2318 0.0004  -0.0202 0.0592  125 GLY A O   
1885 N N   . ALA A 123 ? 0.2555 0.1625 0.2106 -0.0038 -0.0268 0.0474  126 ALA A N   
1886 C CA  . ALA A 123 ? 0.3593 0.2619 0.2993 -0.0050 -0.0218 0.0464  126 ALA A CA  
1887 C C   . ALA A 123 ? 0.3524 0.2453 0.2688 0.0002  -0.0303 0.0475  126 ALA A C   
1888 O O   . ALA A 123 ? 0.3070 0.1893 0.2025 0.0006  -0.0249 0.0490  126 ALA A O   
1889 C CB  . ALA A 123 ? 0.3012 0.2190 0.2570 -0.0087 -0.0211 0.0398  126 ALA A CB  
1895 N N   . LEU A 124 ? 0.2860 0.1824 0.2055 0.0042  -0.0435 0.0460  127 LEU A N   
1896 C CA  . LEU A 124 ? 0.3287 0.2178 0.2284 0.0098  -0.0544 0.0453  127 LEU A CA  
1897 C C   . LEU A 124 ? 0.3378 0.2123 0.2206 0.0163  -0.0604 0.0522  127 LEU A C   
1898 O O   . LEU A 124 ? 0.3965 0.2640 0.2609 0.0222  -0.0713 0.0518  127 LEU A O   
1899 C CB  . LEU A 124 ? 0.2909 0.1945 0.2076 0.0103  -0.0663 0.0375  127 LEU A CB  
1900 C CG  . LEU A 124 ? 0.3438 0.2605 0.2763 0.0048  -0.0618 0.0312  127 LEU A CG  
1901 C CD1 . LEU A 124 ? 0.3965 0.3262 0.3486 0.0050  -0.0721 0.0245  127 LEU A CD1 
1902 C CD2 . LEU A 124 ? 0.2826 0.1928 0.1967 0.0041  -0.0573 0.0292  127 LEU A CD2 
1914 N N   . THR A 125 ? 0.2427 0.1939 0.1575 -0.0069 -0.0078 -0.0139 128 THR A N   
1915 C CA  . THR A 125 ? 0.2334 0.2142 0.1499 -0.0056 -0.0032 -0.0003 128 THR A CA  
1916 C C   . THR A 125 ? 0.3722 0.3637 0.2660 0.0061  0.0048  -0.0033 128 THR A C   
1917 O O   . THR A 125 ? 0.3706 0.3609 0.2636 0.0171  0.0163  -0.0080 128 THR A O   
1918 C CB  . THR A 125 ? 0.2353 0.2259 0.1787 -0.0032 0.0065  0.0155  128 THR A CB  
1919 O OG1 . THR A 125 ? 0.2488 0.2380 0.2084 -0.0119 -0.0002 0.0183  128 THR A OG1 
1920 C CG2 . THR A 125 ? 0.2139 0.2245 0.1551 0.0021  0.0109  0.0309  128 THR A CG2 
1928 N N   . LYS A 126 ? 0.3231 0.3319 0.1985 0.0043  -0.0011 0.0006  129 LYS A N   
1929 C CA  . LYS A 126 ? 0.4433 0.4661 0.2900 0.0143  0.0053  -0.0019 129 LYS A CA  
1930 C C   . LYS A 126 ? 0.3588 0.4058 0.2138 0.0199  0.0192  0.0216  129 LYS A C   
1931 O O   . LYS A 126 ? 0.4407 0.5037 0.2764 0.0282  0.0301  0.0236  129 LYS A O   
1932 C CB  . LYS A 126 ? 0.4480 0.4764 0.2644 0.0079  -0.0113 -0.0100 129 LYS A CB  
1933 C CG  . LYS A 126 ? 0.6008 0.6023 0.4110 -0.0065 -0.0305 -0.0278 129 LYS A CG  
1934 C CD  . LYS A 126 ? 0.7371 0.7505 0.5217 -0.0187 -0.0501 -0.0325 129 LYS A CD  
1935 C CE  . LYS A 126 ? 0.8935 0.8703 0.6369 -0.0218 -0.0636 -0.0617 129 LYS A CE  
1936 N NZ  . LYS A 126 ? 1.2388 1.2248 0.9575 -0.0400 -0.0875 -0.0674 129 LYS A NZ  
1950 N N   . VAL A 127 ? 0.3347 0.3831 0.2146 0.0159  0.0186  0.0396  130 VAL A N   
1951 C CA  . VAL A 127 ? 0.3240 0.3808 0.2112 0.0190  0.0292  0.0628  130 VAL A CA  
1952 C C   . VAL A 127 ? 0.3108 0.3583 0.2196 0.0173  0.0416  0.0642  130 VAL A C   
1953 O O   . VAL A 127 ? 0.3060 0.3368 0.2373 0.0135  0.0388  0.0597  130 VAL A O   
1954 C CB  . VAL A 127 ? 0.4449 0.4998 0.3450 0.0198  0.0213  0.0791  130 VAL A CB  
1955 C CG1 . VAL A 127 ? 0.3277 0.3757 0.2317 0.0222  0.0296  0.1033  130 VAL A CG1 
1956 C CG2 . VAL A 127 ? 0.4065 0.4820 0.2891 0.0216  0.0077  0.0799  130 VAL A CG2 
1966 N N   . TYR A 128 ? 0.4039 0.4686 0.3058 0.0191  0.0550  0.0719  131 TYR A N   
1967 C CA  . TYR A 128 ? 0.2749 0.3436 0.1985 0.0166  0.0660  0.0716  131 TYR A CA  
1968 C C   . TYR A 128 ? 0.3059 0.3538 0.2570 0.0063  0.0634  0.0839  131 TYR A C   
1969 O O   . TYR A 128 ? 0.2470 0.2851 0.2182 0.0038  0.0620  0.0743  131 TYR A O   
1970 C CB  . TYR A 128 ? 0.3212 0.4243 0.2353 0.0179  0.0819  0.0843  131 TYR A CB  
1971 C CG  . TYR A 128 ? 0.5372 0.6598 0.4765 0.0158  0.0937  0.0848  131 TYR A CG  
1972 C CD1 . TYR A 128 ? 0.4745 0.6032 0.4176 0.0292  0.0956  0.0615  131 TYR A CD1 
1973 C CD2 . TYR A 128 ? 0.5021 0.6342 0.4621 -0.0002 0.0993  0.1078  131 TYR A CD2 
1974 C CE1 . TYR A 128 ? 0.4109 0.5660 0.3804 0.0302  0.1053  0.0633  131 TYR A CE1 
1975 C CE2 . TYR A 128 ? 0.5290 0.6843 0.5158 -0.0048 0.1058  0.1072  131 TYR A CE2 
1976 C CZ  . TYR A 128 ? 0.4900 0.6654 0.4831 0.0119  0.1118  0.0881  131 TYR A CZ  
1977 O OH  . TYR A 128 ? 0.5244 0.7283 0.5466 0.0096  0.1162  0.0884  131 TYR A OH  
1987 N N   A SER A 129 ? 0.2443 0.2818 0.1929 0.0016  0.0613  0.1047  132 SER A N   
1988 N N   B SER A 129 ? 0.2443 0.2817 0.1928 0.0016  0.0613  0.1046  132 SER A N   
1989 C CA  A SER A 129 ? 0.3035 0.3128 0.2711 -0.0068 0.0577  0.1142  132 SER A CA  
1990 C CA  B SER A 129 ? 0.3035 0.3128 0.2712 -0.0068 0.0578  0.1142  132 SER A CA  
1991 C C   A SER A 129 ? 0.2735 0.2620 0.2516 -0.0021 0.0478  0.0979  132 SER A C   
1992 C C   B SER A 129 ? 0.2738 0.2622 0.2519 -0.0021 0.0478  0.0979  132 SER A C   
1993 O O   A SER A 129 ? 0.3420 0.3123 0.3362 -0.0081 0.0459  0.0949  132 SER A O   
1994 O O   B SER A 129 ? 0.3416 0.3116 0.3357 -0.0081 0.0459  0.0950  132 SER A O   
1995 C CB  A SER A 129 ? 0.3361 0.3274 0.2930 -0.0085 0.0534  0.1349  132 SER A CB  
1996 C CB  B SER A 129 ? 0.3360 0.3275 0.2930 -0.0087 0.0535  0.1350  132 SER A CB  
1997 O OG  A SER A 129 ? 0.3246 0.3059 0.2716 0.0049  0.0442  0.1354  132 SER A OG  
1998 O OG  B SER A 129 ? 0.3399 0.3489 0.2893 -0.0176 0.0604  0.1468  132 SER A OG  
2009 N N   . TYR A 130 ? 0.2629 0.2576 0.2312 0.0065  0.0408  0.0881  133 TYR A N   
2010 C CA  . TYR A 130 ? 0.1945 0.1795 0.1732 0.0089  0.0329  0.0759  133 TYR A CA  
2011 C C   . TYR A 130 ? 0.2044 0.1877 0.1940 0.0036  0.0336  0.0601  133 TYR A C   
2012 O O   . TYR A 130 ? 0.2471 0.2205 0.2469 0.0024  0.0290  0.0537  133 TYR A O   
2013 C CB  . TYR A 130 ? 0.1950 0.1965 0.1637 0.0144  0.0244  0.0722  133 TYR A CB  
2014 C CG  . TYR A 130 ? 0.3354 0.3423 0.2959 0.0239  0.0206  0.0883  133 TYR A CG  
2015 C CD1 . TYR A 130 ? 0.4191 0.4037 0.3800 0.0285  0.0234  0.1044  133 TYR A CD1 
2016 C CD2 . TYR A 130 ? 0.3737 0.4059 0.3250 0.0279  0.0117  0.0885  133 TYR A CD2 
2017 C CE1 . TYR A 130 ? 0.5483 0.5323 0.4997 0.0409  0.0183  0.1208  133 TYR A CE1 
2018 C CE2 . TYR A 130 ? 0.4520 0.4935 0.3969 0.0397  0.0067  0.1049  133 TYR A CE2 
2019 C CZ  . TYR A 130 ? 0.6225 0.6382 0.5669 0.0483  0.0103  0.1213  133 TYR A CZ  
2020 O OH  . TYR A 130 ? 0.6472 0.6667 0.5833 0.0636  0.0037  0.1393  133 TYR A OH  
2030 N N   . ARG A 131 ? 0.2086 0.2030 0.1945 0.0030  0.0391  0.0543  134 ARG A N   
2031 C CA  . ARG A 131 ? 0.2198 0.2103 0.2154 0.0023  0.0383  0.0408  134 ARG A CA  
2032 C C   . ARG A 131 ? 0.2204 0.2022 0.2365 -0.0040 0.0390  0.0446  134 ARG A C   
2033 O O   . ARG A 131 ? 0.2873 0.2607 0.3113 -0.0052 0.0338  0.0359  134 ARG A O   
2034 C CB  . ARG A 131 ? 0.2122 0.2186 0.2000 0.0093  0.0456  0.0341  134 ARG A CB  
2035 C CG  . ARG A 131 ? 0.2549 0.2629 0.2157 0.0159  0.0419  0.0234  134 ARG A CG  
2036 C CD  . ARG A 131 ? 0.3359 0.3611 0.2839 0.0283  0.0517  0.0152  134 ARG A CD  
2037 N NE  . ARG A 131 ? 0.3106 0.3248 0.2646 0.0374  0.0499  -0.0001 134 ARG A NE  
2038 C CZ  . ARG A 131 ? 0.4333 0.4185 0.3706 0.0418  0.0383  -0.0179 134 ARG A CZ  
2039 N NH1 . ARG A 131 ? 0.4026 0.3717 0.3179 0.0345  0.0269  -0.0235 134 ARG A NH1 
2040 N NH2 . ARG A 131 ? 0.3295 0.3007 0.2723 0.0527  0.0361  -0.0287 134 ARG A NH2 
2054 N N   . PHE A 132 ? 0.1635 0.1448 0.1858 -0.0100 0.0435  0.0584  135 PHE A N   
2055 C CA  . PHE A 132 ? 0.1614 0.1318 0.2001 -0.0197 0.0414  0.0611  135 PHE A CA  
2056 C C   . PHE A 132 ? 0.2914 0.2335 0.3270 -0.0192 0.0335  0.0585  135 PHE A C   
2057 O O   . PHE A 132 ? 0.2431 0.1727 0.2868 -0.0256 0.0289  0.0542  135 PHE A O   
2058 C CB  . PHE A 132 ? 0.2267 0.2055 0.2721 -0.0312 0.0476  0.0781  135 PHE A CB  
2059 C CG  . PHE A 132 ? 0.2467 0.2650 0.2963 -0.0291 0.0584  0.0812  135 PHE A CG  
2060 C CD1 . PHE A 132 ? 0.2388 0.2817 0.3068 -0.0281 0.0607  0.0742  135 PHE A CD1 
2061 C CD2 . PHE A 132 ? 0.2335 0.2681 0.2668 -0.0250 0.0665  0.0906  135 PHE A CD2 
2062 C CE1 . PHE A 132 ? 0.3308 0.4153 0.4024 -0.0201 0.0723  0.0753  135 PHE A CE1 
2063 C CE2 . PHE A 132 ? 0.3265 0.4018 0.3597 -0.0194 0.0784  0.0914  135 PHE A CE2 
2064 C CZ  . PHE A 132 ? 0.3950 0.4961 0.4481 -0.0155 0.0821  0.0829  135 PHE A CZ  
2074 N N   . VAL A 133 ? 0.2227 0.1584 0.2458 -0.0101 0.0316  0.0603  136 VAL A N   
2075 C CA  . VAL A 133 ? 0.2777 0.1965 0.2978 -0.0032 0.0261  0.0551  136 VAL A CA  
2076 C C   . VAL A 133 ? 0.1892 0.1181 0.2138 -0.0036 0.0231  0.0423  136 VAL A C   
2077 O O   . VAL A 133 ? 0.3344 0.2520 0.3602 -0.0042 0.0199  0.0359  136 VAL A O   
2078 C CB  . VAL A 133 ? 0.3082 0.2307 0.3179 0.0100  0.0249  0.0616  136 VAL A CB  
2079 C CG1 . VAL A 133 ? 0.2179 0.1383 0.2269 0.0220  0.0214  0.0543  136 VAL A CG1 
2080 C CG2 . VAL A 133 ? 0.3708 0.2733 0.3726 0.0112  0.0257  0.0775  136 VAL A CG2 
2090 N N   . TRP A 134 ? 0.1647 0.1117 0.1881 -0.0044 0.0228  0.0387  137 TRP A N   
2091 C CA  . TRP A 134 ? 0.1722 0.1235 0.1975 -0.0080 0.0182  0.0306  137 TRP A CA  
2092 C C   . TRP A 134 ? 0.1911 0.1350 0.2247 -0.0132 0.0171  0.0267  137 TRP A C   
2093 O O   . TRP A 134 ? 0.1947 0.1358 0.2289 -0.0159 0.0127  0.0229  137 TRP A O   
2094 C CB  . TRP A 134 ? 0.1524 0.1133 0.1706 -0.0102 0.0150  0.0277  137 TRP A CB  
2095 C CG  . TRP A 134 ? 0.2613 0.2375 0.2735 -0.0078 0.0128  0.0320  137 TRP A CG  
2096 C CD1 . TRP A 134 ? 0.1548 0.1393 0.1578 -0.0046 0.0131  0.0354  137 TRP A CD1 
2097 C CD2 . TRP A 134 ? 0.1737 0.1668 0.1895 -0.0075 0.0097  0.0345  137 TRP A CD2 
2098 N NE1 . TRP A 134 ? 0.2260 0.2308 0.2281 -0.0027 0.0083  0.0402  137 TRP A NE1 
2099 C CE2 . TRP A 134 ? 0.1939 0.2073 0.2060 -0.0039 0.0070  0.0400  137 TRP A CE2 
2100 C CE3 . TRP A 134 ? 0.1713 0.1708 0.1927 -0.0091 0.0095  0.0335  137 TRP A CE3 
2101 C CZ2 . TRP A 134 ? 0.1340 0.1783 0.1527 -0.0013 0.0040  0.0450  137 TRP A CZ2 
2102 C CZ3 . TRP A 134 ? 0.1971 0.2273 0.2226 -0.0063 0.0087  0.0381  137 TRP A CZ3 
2103 C CH2 . TRP A 134 ? 0.1699 0.2244 0.1965 -0.0021 0.0060  0.0440  137 TRP A CH2 
2114 N N   . TRP A 135 ? 0.1824 0.1297 0.2227 -0.0145 0.0209  0.0291  138 TRP A N   
2115 C CA  . TRP A 135 ? 0.2134 0.1630 0.2662 -0.0187 0.0189  0.0274  138 TRP A CA  
2116 C C   . TRP A 135 ? 0.2463 0.1830 0.3012 -0.0253 0.0143  0.0271  138 TRP A C   
2117 O O   . TRP A 135 ? 0.2333 0.1696 0.2914 -0.0284 0.0080  0.0228  138 TRP A O   
2118 C CB  . TRP A 135 ? 0.1856 0.1535 0.2490 -0.0191 0.0257  0.0329  138 TRP A CB  
2119 C CG  . TRP A 135 ? 0.1796 0.1614 0.2615 -0.0237 0.0231  0.0336  138 TRP A CG  
2120 C CD1 . TRP A 135 ? 0.1829 0.1792 0.2732 -0.0150 0.0213  0.0289  138 TRP A CD1 
2121 C CD2 . TRP A 135 ? 0.1693 0.1519 0.2635 -0.0380 0.0196  0.0396  138 TRP A CD2 
2122 N NE1 . TRP A 135 ? 0.1766 0.1917 0.2872 -0.0219 0.0175  0.0330  138 TRP A NE1 
2123 C CE2 . TRP A 135 ? 0.2241 0.2311 0.3371 -0.0389 0.0158  0.0392  138 TRP A CE2 
2124 C CE3 . TRP A 135 ? 0.4532 0.4144 0.5421 -0.0499 0.0174  0.0449  138 TRP A CE3 
2125 C CZ2 . TRP A 135 ? 0.2113 0.2286 0.3405 -0.0554 0.0092  0.0445  138 TRP A CZ2 
2126 C CZ3 . TRP A 135 ? 0.4337 0.3959 0.5277 -0.0639 0.0102  0.0456  138 TRP A CZ3 
2127 C CH2 . TRP A 135 ? 0.3740 0.3660 0.4923 -0.0699 0.0060  0.0472  138 TRP A CH2 
2138 N N   . ALA A 136 ? 0.1833 0.1055 0.2324 -0.0264 0.0157  0.0311  139 ALA A N   
2139 C CA  . ALA A 136 ? 0.2419 0.1446 0.2827 -0.0303 0.0091  0.0261  139 ALA A CA  
2140 C C   . ALA A 136 ? 0.3128 0.2090 0.3456 -0.0234 0.0065  0.0176  139 ALA A C   
2141 O O   . ALA A 136 ? 0.2636 0.1525 0.2924 -0.0276 0.0002  0.0105  139 ALA A O   
2142 C CB  . ALA A 136 ? 0.2362 0.1161 0.2657 -0.0296 0.0093  0.0314  139 ALA A CB  
2148 N N   . ILE A 137 ? 0.1631 0.0700 0.1900 -0.0132 0.0105  0.0181  140 ILE A N   
2149 C CA  . ILE A 137 ? 0.2060 0.1218 0.2239 -0.0073 0.0097  0.0122  140 ILE A CA  
2150 C C   . ILE A 137 ? 0.1965 0.1237 0.2172 -0.0160 0.0054  0.0114  140 ILE A C   
2151 O O   . ILE A 137 ? 0.2419 0.1708 0.2536 -0.0163 0.0025  0.0068  140 ILE A O   
2152 C CB  . ILE A 137 ? 0.2537 0.1897 0.2702 0.0018  0.0141  0.0164  140 ILE A CB  
2153 C CG1 . ILE A 137 ? 0.2866 0.2099 0.2977 0.0160  0.0167  0.0180  140 ILE A CG1 
2154 C CG2 . ILE A 137 ? 0.1458 0.1051 0.1575 0.0037  0.0148  0.0143  140 ILE A CG2 
2155 C CD1 . ILE A 137 ? 0.3551 0.3022 0.3696 0.0233  0.0190  0.0259  140 ILE A CD1 
2167 N N   . SER A 138 ? 0.2112 0.1444 0.2409 -0.0209 0.0045  0.0157  141 SER A N   
2168 C CA  . SER A 138 ? 0.2357 0.1718 0.2667 -0.0261 -0.0016 0.0165  141 SER A CA  
2169 C C   . SER A 138 ? 0.1665 0.0988 0.2012 -0.0298 -0.0074 0.0139  141 SER A C   
2170 O O   . SER A 138 ? 0.2018 0.1364 0.2297 -0.0325 -0.0137 0.0139  141 SER A O   
2171 C CB  . SER A 138 ? 0.2413 0.1768 0.2779 -0.0251 -0.0022 0.0186  141 SER A CB  
2172 O OG  . SER A 138 ? 0.2322 0.1623 0.2677 -0.0265 -0.0100 0.0201  141 SER A OG  
2178 N N   . THR A 139 ? 0.1751 0.1042 0.2200 -0.0323 -0.0066 0.0134  142 THR A N   
2179 C CA  . THR A 139 ? 0.1755 0.1059 0.2269 -0.0401 -0.0148 0.0117  142 THR A CA  
2180 C C   . THR A 139 ? 0.2162 0.1323 0.2489 -0.0424 -0.0201 0.0033  142 THR A C   
2181 O O   . THR A 139 ? 0.2951 0.2150 0.3240 -0.0477 -0.0297 0.0004  142 THR A O   
2182 C CB  . THR A 139 ? 0.2906 0.2250 0.3584 -0.0475 -0.0129 0.0160  142 THR A CB  
2183 O OG1 . THR A 139 ? 0.2469 0.2029 0.3302 -0.0420 -0.0072 0.0220  142 THR A OG1 
2184 C CG2 . THR A 139 ? 0.3650 0.3032 0.4401 -0.0609 -0.0238 0.0147  142 THR A CG2 
2192 N N   . ALA A 140 ? 0.1924 0.0929 0.2111 -0.0357 -0.0147 -0.0015 143 ALA A N   
2193 C CA  . ALA A 140 ? 0.2651 0.1509 0.2609 -0.0315 -0.0183 -0.0131 143 ALA A CA  
2194 C C   . ALA A 140 ? 0.2322 0.1385 0.2161 -0.0282 -0.0185 -0.0134 143 ALA A C   
2195 O O   . ALA A 140 ? 0.2961 0.1994 0.2614 -0.0288 -0.0247 -0.0220 143 ALA A O   
2196 C CB  . ALA A 140 ? 0.3469 0.2147 0.3307 -0.0179 -0.0114 -0.0177 143 ALA A CB  
2202 N N   . ALA A 141 ? 0.1897 0.1156 0.1811 -0.0266 -0.0130 -0.0035 144 ALA A N   
2203 C CA  . ALA A 141 ? 0.1791 0.1238 0.1597 -0.0285 -0.0141 0.0016  144 ALA A CA  
2204 C C   . ALA A 141 ? 0.2176 0.1625 0.1998 -0.0370 -0.0256 0.0059  144 ALA A C   
2205 O O   . ALA A 141 ? 0.2370 0.1912 0.2022 -0.0393 -0.0301 0.0073  144 ALA A O   
2206 C CB  . ALA A 141 ? 0.1630 0.1221 0.1510 -0.0302 -0.0088 0.0128  144 ALA A CB  
2212 N N   . MET A 142 ? 0.2566 0.1965 0.2588 -0.0400 -0.0302 0.0091  145 MET A N   
2213 C CA  . MET A 142 ? 0.2432 0.1889 0.2509 -0.0440 -0.0421 0.0136  145 MET A CA  
2214 C C   . MET A 142 ? 0.2195 0.1647 0.2170 -0.0498 -0.0513 0.0045  145 MET A C   
2215 O O   . MET A 142 ? 0.2624 0.2165 0.2491 -0.0526 -0.0618 0.0072  145 MET A O   
2216 C CB  . MET A 142 ? 0.3521 0.3018 0.3860 -0.0415 -0.0429 0.0179  145 MET A CB  
2217 C CG  . MET A 142 ? 0.3153 0.2775 0.3594 -0.0397 -0.0552 0.0246  145 MET A CG  
2218 S SD  . MET A 142 ? 0.3436 0.3268 0.4222 -0.0340 -0.0544 0.0268  145 MET A SD  
2219 C CE  . MET A 142 ? 0.2536 0.2439 0.3402 -0.0509 -0.0550 0.0203  145 MET A CE  
2229 N N   . LEU A 143 ? 0.2385 0.1697 0.2361 -0.0526 -0.0495 -0.0059 146 LEU A N   
2230 C CA  . LEU A 143 ? 0.2681 0.1894 0.2511 -0.0609 -0.0611 -0.0175 146 LEU A CA  
2231 C C   . LEU A 143 ? 0.2932 0.2128 0.2408 -0.0548 -0.0619 -0.0264 146 LEU A C   
2232 O O   . LEU A 143 ? 0.3423 0.2630 0.2727 -0.0611 -0.0749 -0.0334 146 LEU A O   
2233 C CB  . LEU A 143 ? 0.2509 0.1452 0.2354 -0.0659 -0.0600 -0.0260 146 LEU A CB  
2234 C CG  . LEU A 143 ? 0.4686 0.3720 0.4863 -0.0773 -0.0611 -0.0158 146 LEU A CG  
2235 C CD1 . LEU A 143 ? 0.3350 0.2122 0.3503 -0.0798 -0.0551 -0.0188 146 LEU A CD1 
2236 C CD2 . LEU A 143 ? 0.4515 0.3765 0.4837 -0.0927 -0.0772 -0.0131 146 LEU A CD2 
2248 N N   . TYR A 144 ? 0.3067 0.2297 0.2428 -0.0429 -0.0482 -0.0259 147 TYR A N   
2249 C CA  . TYR A 144 ? 0.3071 0.2423 0.2114 -0.0359 -0.0457 -0.0312 147 TYR A CA  
2250 C C   . TYR A 144 ? 0.2773 0.2354 0.1773 -0.0432 -0.0534 -0.0167 147 TYR A C   
2251 O O   . TYR A 144 ? 0.3125 0.2785 0.1849 -0.0442 -0.0605 -0.0219 147 TYR A O   
2252 C CB  . TYR A 144 ? 0.4347 0.3826 0.3354 -0.0228 -0.0287 -0.0292 147 TYR A CB  
2253 C CG  . TYR A 144 ? 0.3630 0.3374 0.2338 -0.0151 -0.0225 -0.0312 147 TYR A CG  
2254 C CD1 . TYR A 144 ? 0.4905 0.4570 0.3302 0.0000  -0.0198 -0.0525 147 TYR A CD1 
2255 C CD2 . TYR A 144 ? 0.3981 0.4043 0.2691 -0.0230 -0.0198 -0.0115 147 TYR A CD2 
2256 C CE1 . TYR A 144 ? 0.4395 0.4386 0.2498 0.0098  -0.0117 -0.0549 147 TYR A CE1 
2257 C CE2 . TYR A 144 ? 0.4922 0.5310 0.3359 -0.0184 -0.0126 -0.0097 147 TYR A CE2 
2258 C CZ  . TYR A 144 ? 0.6243 0.6644 0.4382 -0.0007 -0.0073 -0.0319 147 TYR A CZ  
2259 O OH  . TYR A 144 ? 0.5335 0.6142 0.3182 0.0067  0.0023  -0.0307 147 TYR A OH  
2269 N N   . ILE A 145 ? 0.3247 0.2901 0.2481 -0.0472 -0.0532 0.0012  148 ILE A N   
2270 C CA  . ILE A 145 ? 0.2622 0.2399 0.1810 -0.0526 -0.0629 0.0177  148 ILE A CA  
2271 C C   . ILE A 145 ? 0.3071 0.2867 0.2243 -0.0572 -0.0805 0.0141  148 ILE A C   
2272 O O   . ILE A 145 ? 0.2982 0.2900 0.1923 -0.0599 -0.0899 0.0191  148 ILE A O   
2273 C CB  . ILE A 145 ? 0.3087 0.2805 0.2512 -0.0531 -0.0621 0.0338  148 ILE A CB  
2274 C CG1 . ILE A 145 ? 0.2956 0.2713 0.2340 -0.0544 -0.0493 0.0409  148 ILE A CG1 
2275 C CG2 . ILE A 145 ? 0.2688 0.2418 0.2091 -0.0552 -0.0767 0.0503  148 ILE A CG2 
2276 C CD1 . ILE A 145 ? 0.2589 0.2195 0.2178 -0.0549 -0.0484 0.0489  148 ILE A CD1 
2288 N N   . LEU A 146 ? 0.3008 0.2737 0.2428 -0.0599 -0.0857 0.0073  149 LEU A N   
2289 C CA  . LEU A 146 ? 0.4333 0.4167 0.3802 -0.0675 -0.1042 0.0054  149 LEU A CA  
2290 C C   . LEU A 146 ? 0.4729 0.4515 0.3840 -0.0732 -0.1125 -0.0114 149 LEU A C   
2291 O O   . LEU A 146 ? 0.4051 0.3984 0.3025 -0.0785 -0.1291 -0.0094 149 LEU A O   
2292 C CB  . LEU A 146 ? 0.4121 0.3966 0.3945 -0.0729 -0.1061 0.0028  149 LEU A CB  
2293 C CG  . LEU A 146 ? 0.3347 0.3282 0.3506 -0.0642 -0.0987 0.0161  149 LEU A CG  
2294 C CD1 . LEU A 146 ? 0.3955 0.4062 0.4456 -0.0711 -0.1022 0.0160  149 LEU A CD1 
2295 C CD2 . LEU A 146 ? 0.3088 0.3132 0.3256 -0.0545 -0.1064 0.0320  149 LEU A CD2 
2307 N N   . TYR A 147 ? 0.4095 0.3660 0.3020 -0.0698 -0.1024 -0.0289 150 TYR A N   
2308 C CA  . TYR A 147 ? 0.4529 0.3971 0.3044 -0.0706 -0.1099 -0.0497 150 TYR A CA  
2309 C C   . TYR A 147 ? 0.4976 0.4650 0.3144 -0.0650 -0.1100 -0.0445 150 TYR A C   
2310 O O   . TYR A 147 ? 0.5047 0.4769 0.2922 -0.0703 -0.1253 -0.0535 150 TYR A O   
2311 C CB  . TYR A 147 ? 0.4319 0.3450 0.2681 -0.0602 -0.0970 -0.0686 150 TYR A CB  
2312 C CG  . TYR A 147 ? 0.6931 0.5910 0.4784 -0.0518 -0.1002 -0.0929 150 TYR A CG  
2313 C CD1 . TYR A 147 ? 0.7409 0.6125 0.5046 -0.0637 -0.1207 -0.1125 150 TYR A CD1 
2314 C CD2 . TYR A 147 ? 0.7008 0.6136 0.4586 -0.0320 -0.0831 -0.0969 150 TYR A CD2 
2315 C CE1 . TYR A 147 ? 0.8810 0.7423 0.6036 -0.0520 -0.1195 -0.1353 150 TYR A CE1 
2316 C CE2 . TYR A 147 ? 0.7999 0.7025 0.5077 -0.0192 -0.0842 -0.1216 150 TYR A CE2 
2317 C CZ  . TYR A 147 ? 1.0091 0.8820 0.6978 -0.0287 -0.1026 -0.1421 150 TYR A CZ  
2318 O OH  . TYR A 147 ? 1.2522 1.1205 0.9026 -0.0159 -0.0985 -0.1643 150 TYR A OH  
2328 N N   . VAL A 148 ? 0.4247 0.4087 0.2428 -0.0568 -0.0941 -0.0287 151 VAL A N   
2329 C CA  . VAL A 148 ? 0.3989 0.4094 0.1840 -0.0546 -0.0922 -0.0186 151 VAL A CA  
2330 C C   . VAL A 148 ? 0.4932 0.5178 0.2785 -0.0642 -0.1120 -0.0013 151 VAL A C   
2331 O O   . VAL A 148 ? 0.5204 0.5607 0.2690 -0.0659 -0.1211 -0.0019 151 VAL A O   
2332 C CB  . VAL A 148 ? 0.4764 0.5035 0.2694 -0.0504 -0.0729 -0.0006 151 VAL A CB  
2333 C CG1 . VAL A 148 ? 0.4198 0.4773 0.1852 -0.0549 -0.0730 0.0197  151 VAL A CG1 
2334 C CG2 . VAL A 148 ? 0.3767 0.4023 0.1630 -0.0367 -0.0543 -0.0179 151 VAL A CG2 
2344 N N   . LEU A 149 ? 0.3780 0.3989 0.2025 -0.0679 -0.1193 0.0143  152 LEU A N   
2345 C CA  . LEU A 149 ? 0.4549 0.4901 0.2834 -0.0716 -0.1388 0.0327  152 LEU A CA  
2346 C C   . LEU A 149 ? 0.5209 0.5651 0.3383 -0.0778 -0.1584 0.0184  152 LEU A C   
2347 O O   . LEU A 149 ? 0.5826 0.6441 0.3955 -0.0758 -0.1695 0.0300  152 LEU A O   
2348 C CB  . LEU A 149 ? 0.4182 0.4476 0.2923 -0.0678 -0.1413 0.0475  152 LEU A CB  
2349 C CG  . LEU A 149 ? 0.5142 0.5298 0.3984 -0.0629 -0.1277 0.0642  152 LEU A CG  
2350 C CD1 . LEU A 149 ? 0.4877 0.4951 0.4099 -0.0547 -0.1333 0.0740  152 LEU A CD1 
2351 C CD2 . LEU A 149 ? 0.4941 0.5148 0.3470 -0.0663 -0.1292 0.0858  152 LEU A CD2 
2363 N N   . PHE A 150 ? 0.6434 0.6724 0.4607 -0.0833 -0.1597 -0.0070 153 PHE A N   
2364 C CA  . PHE A 150 ? 0.5555 0.5889 0.3699 -0.0901 -0.1749 -0.0226 153 PHE A CA  
2365 C C   . PHE A 150 ? 0.5519 0.5772 0.3154 -0.0866 -0.1742 -0.0454 153 PHE A C   
2366 O O   . PHE A 150 ? 0.8141 0.8555 0.5591 -0.0871 -0.1872 -0.0481 153 PHE A O   
2367 C CB  . PHE A 150 ? 0.6810 0.6995 0.5297 -0.1004 -0.1771 -0.0345 153 PHE A CB  
2368 C CG  . PHE A 150 ? 0.6374 0.6813 0.5364 -0.1037 -0.1842 -0.0162 153 PHE A CG  
2369 C CD1 . PHE A 150 ? 0.8164 0.8910 0.7266 -0.1066 -0.2004 -0.0096 153 PHE A CD1 
2370 C CD2 . PHE A 150 ? 0.6060 0.6469 0.5406 -0.1013 -0.1742 -0.0066 153 PHE A CD2 
2371 C CE1 . PHE A 150 ? 0.6149 0.7191 0.5712 -0.1049 -0.2053 0.0062  153 PHE A CE1 
2372 C CE2 . PHE A 150 ? 0.8665 0.9363 0.8458 -0.0995 -0.1784 0.0084  153 PHE A CE2 
2373 C CZ  . PHE A 150 ? 0.6510 0.7537 0.6415 -0.1003 -0.1935 0.0147  153 PHE A CZ  
2383 N N   . PHE A 151 ? 0.7169 0.7184 0.4565 -0.0797 -0.1594 -0.0628 154 PHE A N   
2384 C CA  . PHE A 151 ? 0.7875 0.7800 0.4794 -0.0701 -0.1563 -0.0892 154 PHE A CA  
2385 C C   . PHE A 151 ? 0.9108 0.9236 0.5674 -0.0544 -0.1389 -0.0815 154 PHE A C   
2386 O O   . PHE A 151 ? 1.2259 1.2313 0.8494 -0.0390 -0.1255 -0.1021 154 PHE A O   
2387 C CB  . PHE A 151 ? 0.9834 0.9342 0.6744 -0.0688 -0.1505 -0.1160 154 PHE A CB  
2388 C CG  . PHE A 151 ? 1.0354 0.9681 0.7656 -0.0870 -0.1640 -0.1176 154 PHE A CG  
2389 C CD1 . PHE A 151 ? 0.7552 0.6874 0.5315 -0.0945 -0.1611 -0.0992 154 PHE A CD1 
2390 C CD2 . PHE A 151 ? 1.1749 1.0958 0.8958 -0.0975 -0.1785 -0.1364 154 PHE A CD2 
2391 C CE1 . PHE A 151 ? 0.8094 0.7361 0.6230 -0.1108 -0.1698 -0.0976 154 PHE A CE1 
2392 C CE2 . PHE A 151 ? 1.2192 1.1303 0.9771 -0.1167 -0.1894 -0.1340 154 PHE A CE2 
2393 C CZ  . PHE A 151 ? 1.0941 1.0113 0.8989 -0.1229 -0.1838 -0.1135 154 PHE A CZ  
2403 N N   . GLY A 152 ? 0.6436 0.6926 0.6960 -0.0980 -0.0059 -0.0972 155 GLY A N   
2404 C CA  . GLY A 152 ? 0.8847 0.9543 0.9388 -0.0646 0.0289  -0.0966 155 GLY A CA  
2405 C C   . GLY A 152 ? 0.8402 0.9508 0.8955 -0.0617 0.0459  -0.0880 155 GLY A C   
2406 O O   . GLY A 152 ? 0.9236 1.0380 0.9494 -0.0293 0.0658  -0.0879 155 GLY A O   
2410 N N   . PHE A 153 ? 0.9318 1.0768 1.0167 -0.0883 0.0381  -0.0781 156 PHE A N   
2411 C CA  . PHE A 153 ? 0.9390 1.1183 1.0265 -0.0881 0.0476  -0.0708 156 PHE A CA  
2412 C C   . PHE A 153 ? 1.0290 1.1916 1.0651 -0.0962 0.0344  -0.0836 156 PHE A C   
2413 O O   . PHE A 153 ? 1.1075 1.2737 1.1145 -0.0781 0.0473  -0.0862 156 PHE A O   
2414 C CB  . PHE A 153 ? 0.7181 0.9328 0.8474 -0.1015 0.0364  -0.0604 156 PHE A CB  
2415 C CG  . PHE A 153 ? 0.5200 0.7463 0.7075 -0.0903 0.0372  -0.0476 156 PHE A CG  
2416 C CD1 . PHE A 153 ? 0.4034 0.6201 0.6146 -0.0762 0.0530  -0.0390 156 PHE A CD1 
2417 C CD2 . PHE A 153 ? 0.4671 0.7104 0.6869 -0.0897 0.0142  -0.0436 156 PHE A CD2 
2418 C CE1 . PHE A 153 ? 0.6552 0.8845 0.9363 -0.0702 0.0465  -0.0198 156 PHE A CE1 
2419 C CE2 . PHE A 153 ? 0.4744 0.7154 0.7569 -0.0808 -0.0022 -0.0319 156 PHE A CE2 
2420 C CZ  . PHE A 153 ? 0.6079 0.8447 0.9288 -0.0753 0.0142  -0.0166 156 PHE A CZ  
2430 N N   . THR A 154 ? 0.9556 1.1047 0.9872 -0.1222 0.0063  -0.0848 157 THR A N   
2431 C CA  . THR A 154 ? 1.1943 1.3281 1.1949 -0.1364 -0.0171 -0.0903 157 THR A CA  
2432 C C   . THR A 154 ? 1.2292 1.3040 1.1680 -0.1079 -0.0264 -0.1165 157 THR A C   
2433 O O   . THR A 154 ? 1.2351 1.3016 1.1376 -0.1027 -0.0354 -0.1264 157 THR A O   
2434 C CB  . THR A 154 ? 1.0979 1.2293 1.1258 -0.1692 -0.0512 -0.0719 157 THR A CB  
2435 O OG1 . THR A 154 ? 0.4956 0.6947 0.5639 -0.1784 -0.0390 -0.0447 157 THR A OG1 
2436 C CG2 . THR A 154 ? 1.2603 1.3710 1.2731 -0.1885 -0.0870 -0.0709 157 THR A CG2 
2444 N N   . SER A 155 ? 1.2064 1.2386 1.1239 -0.0807 -0.0264 -0.1300 158 SER A N   
2445 C CA  . SER A 155 ? 1.3350 1.3083 1.1742 -0.0328 -0.0383 -0.1589 158 SER A CA  
2446 C C   . SER A 155 ? 1.4407 1.4578 1.2527 0.0120  0.0084  -0.1526 158 SER A C   
2447 O O   . SER A 155 ? 1.4895 1.4730 1.2238 0.0593  0.0008  -0.1736 158 SER A O   
2448 C CB  . SER A 155 ? 1.5111 1.4318 1.3290 -0.0051 -0.0501 -0.1737 158 SER A CB  
2451 N N   . LYS A 156 ? 1.4596 1.5494 1.3359 0.0021  0.0502  -0.1205 159 LYS A N   
2452 C CA  . LYS A 156 ? 1.4941 1.6390 1.3734 0.0373  0.0927  -0.0961 159 LYS A CA  
2453 C C   . LYS A 156 ? 1.4527 1.6350 1.3516 0.0109  0.0947  -0.0851 159 LYS A C   
2454 O O   . LYS A 156 ? 1.4389 1.6527 1.3182 0.0424  0.1195  -0.0701 159 LYS A O   
2455 C CB  . LYS A 156 ? 1.3685 1.5664 1.3252 0.0430  0.1259  -0.0583 159 LYS A CB  
2456 C CG  . LYS A 156 ? 1.1804 1.4527 1.2008 0.0462  0.1566  -0.0119 159 LYS A CG  
2457 C CD  . LYS A 156 ? 0.9708 1.2903 1.0808 0.0536  0.1784  0.0333  159 LYS A CD  
2458 C CE  . LYS A 156 ? 1.3963 1.7339 1.4723 0.1183  0.2135  0.0512  159 LYS A CE  
2459 N NZ  . LYS A 156 ? 1.0615 1.4669 1.2454 0.1258  0.2387  0.1135  159 LYS A NZ  
2473 N N   . ALA A 157 ? 1.1791 1.3643 1.1130 -0.0392 0.0705  -0.0885 160 ALA A N   
2474 C CA  . ALA A 157 ? 1.0207 1.2382 0.9645 -0.0590 0.0686  -0.0816 160 ALA A CA  
2475 C C   . ALA A 157 ? 1.0807 1.2680 0.9539 -0.0484 0.0531  -0.1033 160 ALA A C   
2476 O O   . ALA A 157 ? 0.9369 1.1512 0.7989 -0.0411 0.0651  -0.0964 160 ALA A O   
2477 C CB  . ALA A 157 ? 0.7393 0.9724 0.7232 -0.0989 0.0467  -0.0789 160 ALA A CB  
2483 N N   . GLU A 158 ? 1.1673 1.2923 0.9956 -0.0468 0.0184  -0.1294 161 GLU A N   
2484 C CA  . GLU A 158 ? 1.1716 1.2515 0.9359 -0.0371 -0.0146 -0.1539 161 GLU A CA  
2485 C C   . GLU A 158 ? 1.2516 1.3246 0.9422 0.0282  0.0079  -0.1644 161 GLU A C   
2486 O O   . GLU A 158 ? 1.5717 1.6179 1.2054 0.0438  -0.0137 -0.1836 161 GLU A O   
2487 C CB  . GLU A 158 ? 1.2485 1.2499 0.9934 -0.0487 -0.0731 -0.1761 161 GLU A CB  
2488 C CG  . GLU A 158 ? 1.2862 1.3082 1.1059 -0.1114 -0.0989 -0.1521 161 GLU A CG  
2489 C CD  . GLU A 158 ? 1.5313 1.4841 1.3594 -0.1264 -0.1550 -0.1583 161 GLU A CD  
2490 O OE1 . GLU A 158 ? 1.7049 1.5755 1.4674 -0.0865 -0.1863 -0.1928 161 GLU A OE1 
2491 O OE2 . GLU A 158 ? 1.3356 1.3173 1.2346 -0.1721 -0.1706 -0.1256 161 GLU A OE2 
2498 N N   . SER A 159 ? 1.3491 1.4527 1.0412 0.0717  0.0512  -0.1467 162 SER A N   
2499 C CA  . SER A 159 ? 1.3918 1.5143 1.0190 0.1470  0.0840  -0.1401 162 SER A CA  
2500 C C   . SER A 159 ? 1.3819 1.5981 1.0700 0.1443  0.1346  -0.0896 162 SER A C   
2501 O O   . SER A 159 ? 1.3212 1.5871 0.9913 0.2058  0.1775  -0.0576 162 SER A O   
2502 C CB  . SER A 159 ? 1.2126 1.3238 0.8057 0.2085  0.1014  -0.1394 162 SER A CB  
2503 O OG  . SER A 159 ? 1.3943 1.5620 1.0852 0.1806  0.1342  -0.0998 162 SER A OG  
2509 N N   . MET A 160 ? 1.3061 1.5501 1.0668 0.0801  0.1273  -0.0771 163 MET A N   
2510 C CA  . MET A 160 ? 1.1516 1.4698 0.9831 0.0691  0.1580  -0.0305 163 MET A CA  
2511 C C   . MET A 160 ? 0.9157 1.2345 0.7228 0.0499  0.1432  -0.0426 163 MET A C   
2512 O O   . MET A 160 ? 0.9004 1.1680 0.6361 0.0505  0.1130  -0.0827 163 MET A O   
2513 C CB  . MET A 160 ? 1.0083 1.3507 0.9432 0.0219  0.1524  -0.0080 163 MET A CB  
2514 C CG  . MET A 160 ? 1.1981 1.5337 1.1606 0.0334  0.1607  -0.0004 163 MET A CG  
2515 S SD  . MET A 160 ? 1.3811 1.7955 1.4293 0.0689  0.2062  0.0725  163 MET A SD  
2516 C CE  . MET A 160 ? 0.6271 1.0962 0.7772 0.0337  0.1998  0.1208  163 MET A CE  
2526 N N   . ARG A 161 ? 0.8212 1.1950 0.6948 0.0322  0.1575  -0.0054 164 ARG A N   
2527 C CA  . ARG A 161 ? 0.6823 1.0611 0.5382 0.0141  0.1444  -0.0143 164 ARG A CA  
2528 C C   . ARG A 161 ? 0.5429 0.8808 0.3814 -0.0299 0.1029  -0.0548 164 ARG A C   
2529 O O   . ARG A 161 ? 0.6072 0.9371 0.4856 -0.0572 0.0877  -0.0586 164 ARG A O   
2530 C CB  . ARG A 161 ? 0.6163 1.0490 0.5602 -0.0052 0.1514  0.0307  164 ARG A CB  
2531 C CG  . ARG A 161 ? 0.7186 1.1999 0.7520 0.0091  0.1763  0.0899  164 ARG A CG  
2532 C CD  . ARG A 161 ? 0.5828 1.1163 0.7009 -0.0003 0.1778  0.1457  164 ARG A CD  
2533 N NE  . ARG A 161 ? 0.4973 1.0048 0.6399 -0.0434 0.1317  0.1223  164 ARG A NE  
2534 C CZ  . ARG A 161 ? 0.3949 0.9180 0.6333 -0.0644 0.1028  0.1590  164 ARG A CZ  
2535 N NH1 . ARG A 161 ? 0.4687 1.0398 0.8116 -0.0579 0.1135  0.2315  164 ARG A NH1 
2536 N NH2 . ARG A 161 ? 0.3839 0.8745 0.6171 -0.0884 0.0564  0.1265  164 ARG A NH2 
2550 N N   . PRO A 162 ? 0.5806 0.5565 0.3525 -0.0568 -0.1535 -0.0200 165 PRO A N   
2551 C CA  . PRO A 162 ? 0.6176 0.6044 0.4149 -0.0626 -0.1594 -0.0217 165 PRO A CA  
2552 C C   . PRO A 162 ? 0.6642 0.6652 0.4912 -0.0586 -0.1577 -0.0139 165 PRO A C   
2553 O O   . PRO A 162 ? 0.6098 0.6129 0.4548 -0.0621 -0.1562 -0.0164 165 PRO A O   
2554 C CB  . PRO A 162 ? 0.5380 0.5367 0.3337 -0.0657 -0.1702 -0.0213 165 PRO A CB  
2555 C CG  . PRO A 162 ? 0.6810 0.6675 0.4444 -0.0641 -0.1696 -0.0239 165 PRO A CG  
2556 C CD  . PRO A 162 ? 0.6060 0.5842 0.3593 -0.0567 -0.1595 -0.0193 165 PRO A CD  
2564 N N   . GLU A 163 ? 0.4829 0.4925 0.3147 -0.0513 -0.1574 -0.0043 166 GLU A N   
2565 C CA  . GLU A 163 ? 0.5674 0.5880 0.4254 -0.0467 -0.1554 0.0027  166 GLU A CA  
2566 C C   . GLU A 163 ? 0.4772 0.4880 0.3394 -0.0464 -0.1467 0.0010  166 GLU A C   
2567 O O   . GLU A 163 ? 0.4961 0.5144 0.3812 -0.0456 -0.1450 0.0028  166 GLU A O   
2568 C CB  . GLU A 163 ? 0.5674 0.5933 0.4249 -0.0388 -0.1563 0.0129  166 GLU A CB  
2569 C CG  . GLU A 163 ? 0.6949 0.7071 0.5296 -0.0360 -0.1501 0.0161  166 GLU A CG  
2570 C CD  . GLU A 163 ? 0.6699 0.6789 0.4798 -0.0364 -0.1538 0.0160  166 GLU A CD  
2571 O OE1 . GLU A 163 ? 0.8157 0.8262 0.6191 -0.0413 -0.1596 0.0090  166 GLU A OE1 
2572 O OE2 . GLU A 163 ? 0.9904 0.9952 0.7870 -0.0323 -0.1508 0.0231  166 GLU A OE2 
2579 N N   . VAL A 164 ? 0.4811 0.4759 0.3207 -0.0464 -0.1408 -0.0023 167 VAL A N   
2580 C CA  . VAL A 164 ? 0.5110 0.4969 0.3526 -0.0456 -0.1330 -0.0040 167 VAL A CA  
2581 C C   . VAL A 164 ? 0.5189 0.4993 0.3673 -0.0516 -0.1331 -0.0127 167 VAL A C   
2582 O O   . VAL A 164 ? 0.4721 0.4551 0.3393 -0.0513 -0.1294 -0.0121 167 VAL A O   
2583 C CB  . VAL A 164 ? 0.6288 0.6018 0.4455 -0.0419 -0.1239 -0.0049 167 VAL A CB  
2584 C CG1 . VAL A 164 ? 0.6618 0.6266 0.4835 -0.0393 -0.1114 -0.0100 167 VAL A CG1 
2585 C CG2 . VAL A 164 ? 0.6002 0.5792 0.4170 -0.0367 -0.1208 0.0059  167 VAL A CG2 
2595 N N   . ALA A 165 ? 0.3975 0.3695 0.2308 -0.0569 -0.1364 -0.0206 168 ALA A N   
2596 C CA  . ALA A 165 ? 0.5549 0.5180 0.3918 -0.0636 -0.1362 -0.0287 168 ALA A CA  
2597 C C   . ALA A 165 ? 0.4473 0.4285 0.3152 -0.0675 -0.1403 -0.0254 168 ALA A C   
2598 O O   . ALA A 165 ? 0.5067 0.4848 0.3866 -0.0707 -0.1372 -0.0277 168 ALA A O   
2599 C CB  . ALA A 165 ? 0.6163 0.5658 0.4299 -0.0689 -0.1396 -0.0375 168 ALA A CB  
2605 N N   . SER A 166 ? 0.4414 0.4417 0.3216 -0.0665 -0.1466 -0.0199 169 SER A N   
2606 C CA  . SER A 166 ? 0.4475 0.4671 0.3558 -0.0689 -0.1497 -0.0169 169 SER A CA  
2607 C C   . SER A 166 ? 0.4540 0.4810 0.3828 -0.0630 -0.1438 -0.0111 169 SER A C   
2608 O O   . SER A 166 ? 0.4484 0.4822 0.3959 -0.0660 -0.1419 -0.0115 169 SER A O   
2609 C CB  . SER A 166 ? 0.5236 0.5616 0.4377 -0.0675 -0.1579 -0.0126 169 SER A CB  
2610 O OG  . SER A 166 ? 0.8585 0.9145 0.7954 -0.0716 -0.1616 -0.0120 169 SER A OG  
2616 N N   . THR A 167 ? 0.4675 0.4928 0.3925 -0.0550 -0.1408 -0.0055 170 THR A N   
2617 C CA  . THR A 167 ? 0.4082 0.4385 0.3508 -0.0494 -0.1355 -0.0003 170 THR A CA  
2618 C C   . THR A 167 ? 0.3958 0.4138 0.3379 -0.0521 -0.1292 -0.0046 170 THR A C   
2619 O O   . THR A 167 ? 0.4220 0.4464 0.3832 -0.0516 -0.1259 -0.0032 170 THR A O   
2620 C CB  . THR A 167 ? 0.4627 0.4912 0.3989 -0.0415 -0.1340 0.0068  170 THR A CB  
2621 O OG1 . THR A 167 ? 0.4736 0.5124 0.4101 -0.0382 -0.1401 0.0112  170 THR A OG1 
2622 C CG2 . THR A 167 ? 0.4439 0.4753 0.3968 -0.0362 -0.1289 0.0116  170 THR A CG2 
2630 N N   . PHE A 168 ? 0.3970 0.3972 0.3169 -0.0536 -0.1261 -0.0098 171 PHE A N   
2631 C CA  . PHE A 168 ? 0.5283 0.5166 0.4489 -0.0526 -0.1157 -0.0140 171 PHE A CA  
2632 C C   . PHE A 168 ? 0.4108 0.3983 0.3413 -0.0608 -0.1186 -0.0184 171 PHE A C   
2633 O O   . PHE A 168 ? 0.4561 0.4451 0.4017 -0.0598 -0.1125 -0.0173 171 PHE A O   
2634 C CB  . PHE A 168 ? 0.3658 0.3359 0.2605 -0.0503 -0.1098 -0.0193 171 PHE A CB  
2635 C CG  . PHE A 168 ? 0.5377 0.4936 0.4304 -0.0492 -0.1010 -0.0245 171 PHE A CG  
2636 C CD1 . PHE A 168 ? 0.4069 0.3650 0.3107 -0.0423 -0.0909 -0.0208 171 PHE A CD1 
2637 C CD2 . PHE A 168 ? 0.5273 0.4665 0.4060 -0.0554 -0.1034 -0.0329 171 PHE A CD2 
2638 C CE1 . PHE A 168 ? 0.5987 0.5445 0.5007 -0.0401 -0.0832 -0.0247 171 PHE A CE1 
2639 C CE2 . PHE A 168 ? 0.5607 0.4843 0.4362 -0.0532 -0.0953 -0.0371 171 PHE A CE2 
2640 C CZ  . PHE A 168 ? 0.5260 0.4539 0.4138 -0.0449 -0.0852 -0.0327 171 PHE A CZ  
2650 N N   . LYS A 169 ? 0.3872 0.3726 0.3092 -0.0693 -0.1270 -0.0230 172 LYS A N   
2651 C CA  . LYS A 169 ? 0.5017 0.4861 0.4333 -0.0777 -0.1274 -0.0265 172 LYS A CA  
2652 C C   . LYS A 169 ? 0.4992 0.5056 0.4605 -0.0772 -0.1264 -0.0203 172 LYS A C   
2653 O O   . LYS A 169 ? 0.5342 0.5390 0.5059 -0.0816 -0.1230 -0.0212 172 LYS A O   
2654 C CB  . LYS A 169 ? 0.5425 0.5254 0.4639 -0.0853 -0.1340 -0.0311 172 LYS A CB  
2655 C CG  . LYS A 169 ? 0.7373 0.6919 0.6288 -0.0883 -0.1331 -0.0401 172 LYS A CG  
2656 C CD  . LYS A 169 ? 0.9582 0.9098 0.8435 -0.0984 -0.1395 -0.0451 172 LYS A CD  
2657 C CE  . LYS A 169 ? 1.2235 1.1441 1.0768 -0.1000 -0.1379 -0.0546 172 LYS A CE  
2658 N NZ  . LYS A 169 ? 1.1777 1.0812 1.0291 -0.1088 -0.1369 -0.0597 172 LYS A NZ  
2661 N N   . VAL A 170 ? 0.4388 0.4647 0.4126 -0.0712 -0.1287 -0.0141 173 VAL A N   
2662 C CA  . VAL A 170 ? 0.4616 0.5077 0.4613 -0.0685 -0.1269 -0.0087 173 VAL A CA  
2663 C C   . VAL A 170 ? 0.3926 0.4343 0.3995 -0.0633 -0.1196 -0.0063 173 VAL A C   
2664 O O   . VAL A 170 ? 0.3397 0.3872 0.3616 -0.0652 -0.1158 -0.0054 173 VAL A O   
2665 C CB  . VAL A 170 ? 0.4809 0.5455 0.4887 -0.0617 -0.1314 -0.0033 173 VAL A CB  
2666 C CG1 . VAL A 170 ? 0.3904 0.4719 0.4211 -0.0552 -0.1280 0.0022  173 VAL A CG1 
2667 C CG2 . VAL A 170 ? 0.5208 0.5953 0.5277 -0.0677 -0.1392 -0.0052 173 VAL A CG2 
2677 N N   . LEU A 171 ? 0.3304 0.3623 0.3263 -0.0570 -0.1178 -0.0049 174 LEU A N   
2678 C CA  . LEU A 171 ? 0.3169 0.3449 0.3194 -0.0506 -0.1082 -0.0027 174 LEU A CA  
2679 C C   . LEU A 171 ? 0.3451 0.3587 0.3429 -0.0538 -0.1012 -0.0073 174 LEU A C   
2680 O O   . LEU A 171 ? 0.2822 0.2969 0.2908 -0.0512 -0.0946 -0.0056 174 LEU A O   
2681 C CB  . LEU A 171 ? 0.2865 0.3083 0.2782 -0.0428 -0.1045 0.0002  174 LEU A CB  
2682 C CG  . LEU A 171 ? 0.2562 0.2883 0.2516 -0.0379 -0.1101 0.0062  174 LEU A CG  
2683 C CD1 . LEU A 171 ? 0.4445 0.4677 0.4267 -0.0327 -0.1061 0.0093  174 LEU A CD1 
2684 C CD2 . LEU A 171 ? 0.3460 0.3908 0.3620 -0.0338 -0.1096 0.0102  174 LEU A CD2 
2696 N N   . ARG A 172 ? 0.2894 0.2879 0.2696 -0.0588 -0.1027 -0.0132 175 ARG A N   
2697 C CA  . ARG A 172 ? 0.3936 0.3753 0.3676 -0.0610 -0.0966 -0.0175 175 ARG A CA  
2698 C C   . ARG A 172 ? 0.3389 0.3260 0.3274 -0.0695 -0.0987 -0.0173 175 ARG A C   
2699 O O   . ARG A 172 ? 0.4082 0.3890 0.4015 -0.0688 -0.0919 -0.0168 175 ARG A O   
2700 C CB  . ARG A 172 ? 0.4127 0.3741 0.3615 -0.0636 -0.0980 -0.0245 175 ARG A CB  
2701 C CG  . ARG A 172 ? 0.5477 0.4872 0.4864 -0.0655 -0.0927 -0.0297 175 ARG A CG  
2702 C CD  . ARG A 172 ? 0.5838 0.5036 0.4996 -0.0730 -0.0985 -0.0377 175 ARG A CD  
2703 N NE  . ARG A 172 ? 0.6987 0.6278 0.6215 -0.0863 -0.1098 -0.0382 175 ARG A NE  
2704 C CZ  . ARG A 172 ? 0.7227 0.6415 0.6293 -0.0943 -0.1166 -0.0440 175 ARG A CZ  
2705 N NH1 . ARG A 172 ? 0.7061 0.6001 0.5839 -0.0920 -0.1157 -0.0514 175 ARG A NH1 
2706 N NH2 . ARG A 172 ? 0.7071 0.6430 0.6281 -0.1024 -0.1219 -0.0419 175 ARG A NH2 
2720 N N   . ASN A 173 ? 0.3756 0.3759 0.3714 -0.0779 -0.1081 -0.0169 176 ASN A N   
2721 C CA  . ASN A 173 ? 0.3350 0.3450 0.3467 -0.0857 -0.1080 -0.0155 176 ASN A CA  
2722 C C   . ASN A 173 ? 0.2270 0.2539 0.2599 -0.0802 -0.1031 -0.0093 176 ASN A C   
2723 O O   . ASN A 173 ? 0.2955 0.3209 0.3363 -0.0836 -0.0986 -0.0082 176 ASN A O   
2724 C CB  . ASN A 173 ? 0.3855 0.4107 0.4023 -0.0913 -0.1142 -0.0156 176 ASN A CB  
2725 C CG  . ASN A 173 ? 0.5864 0.5936 0.5818 -0.0985 -0.1190 -0.0223 176 ASN A CG  
2726 O OD1 . ASN A 173 ? 0.4023 0.3835 0.3783 -0.0995 -0.1168 -0.0274 176 ASN A OD1 
2727 N ND2 . ASN A 173 ? 0.4989 0.5190 0.4968 -0.1030 -0.1257 -0.0226 176 ASN A ND2 
2734 N N   . VAL A 174 ? 0.2274 0.2688 0.2681 -0.0713 -0.1039 -0.0053 177 VAL A N   
2735 C CA  . VAL A 174 ? 0.2324 0.2868 0.2899 -0.0645 -0.0988 -0.0003 177 VAL A CA  
2736 C C   . VAL A 174 ? 0.2475 0.2867 0.2997 -0.0600 -0.0890 -0.0009 177 VAL A C   
2737 O O   . VAL A 174 ? 0.2563 0.3000 0.3190 -0.0598 -0.0838 0.0013  177 VAL A O   
2738 C CB  . VAL A 174 ? 0.2564 0.3215 0.3174 -0.0547 -0.1012 0.0033  177 VAL A CB  
2739 C CG1 . VAL A 174 ? 0.3164 0.3850 0.3865 -0.0457 -0.0940 0.0068  177 VAL A CG1 
2740 C CG2 . VAL A 174 ? 0.3932 0.4773 0.4631 -0.0548 -0.1060 0.0049  177 VAL A CG2 
2750 N N   . THR A 175 ? 0.3166 0.3392 0.3524 -0.0559 -0.0864 -0.0034 178 THR A N   
2751 C CA  . THR A 175 ? 0.2422 0.2534 0.2738 -0.0507 -0.0778 -0.0031 178 THR A CA  
2752 C C   . THR A 175 ? 0.1775 0.1787 0.2086 -0.0563 -0.0744 -0.0047 178 THR A C   
2753 O O   . THR A 175 ? 0.2779 0.2797 0.3156 -0.0537 -0.0685 -0.0021 178 THR A O   
2754 C CB  . THR A 175 ? 0.4068 0.4051 0.4215 -0.0458 -0.0758 -0.0052 178 THR A CB  
2755 O OG1 . THR A 175 ? 0.2340 0.2407 0.2493 -0.0407 -0.0779 -0.0022 178 THR A OG1 
2756 C CG2 . THR A 175 ? 0.3080 0.2965 0.3190 -0.0405 -0.0674 -0.0048 178 THR A CG2 
2764 N N   . VAL A 176 ? 0.2079 0.1981 0.2295 -0.0645 -0.0784 -0.0089 179 VAL A N   
2765 C CA  . VAL A 176 ? 0.2168 0.1917 0.2340 -0.0703 -0.0754 -0.0104 179 VAL A CA  
2766 C C   . VAL A 176 ? 0.3336 0.3227 0.3687 -0.0758 -0.0744 -0.0059 179 VAL A C   
2767 O O   . VAL A 176 ? 0.2607 0.2426 0.2968 -0.0753 -0.0684 -0.0038 179 VAL A O   
2768 C CB  . VAL A 176 ? 0.4389 0.3969 0.4402 -0.0795 -0.0813 -0.0163 179 VAL A CB  
2769 C CG1 . VAL A 176 ? 0.6310 0.5721 0.6284 -0.0878 -0.0794 -0.0171 179 VAL A CG1 
2770 C CG2 . VAL A 176 ? 0.4081 0.3493 0.3889 -0.0721 -0.0797 -0.0210 179 VAL A CG2 
2780 N N   . VAL A 177 ? 0.2967 0.3075 0.3459 -0.0805 -0.0799 -0.0039 180 VAL A N   
2781 C CA  . VAL A 177 ? 0.1835 0.2114 0.2506 -0.0855 -0.0782 0.0007  180 VAL A CA  
2782 C C   . VAL A 177 ? 0.2301 0.2654 0.3052 -0.0750 -0.0705 0.0046  180 VAL A C   
2783 O O   . VAL A 177 ? 0.3622 0.3960 0.4410 -0.0766 -0.0647 0.0073  180 VAL A O   
2784 C CB  . VAL A 177 ? 0.2549 0.3075 0.3359 -0.0901 -0.0850 0.0022  180 VAL A CB  
2785 C CG1 . VAL A 177 ? 0.2254 0.2999 0.3257 -0.0911 -0.0805 0.0074  180 VAL A CG1 
2786 C CG2 . VAL A 177 ? 0.2513 0.2957 0.3223 -0.1000 -0.0903 -0.0020 180 VAL A CG2 
2796 N N   . LEU A 178 ? 0.1680 0.2098 0.2440 -0.0649 -0.0706 0.0050  181 LEU A N   
2797 C CA  . LEU A 178 ? 0.1561 0.2049 0.2389 -0.0560 -0.0646 0.0081  181 LEU A CA  
2798 C C   . LEU A 178 ? 0.2106 0.2428 0.2837 -0.0524 -0.0582 0.0081  181 LEU A C   
2799 O O   . LEU A 178 ? 0.1473 0.1825 0.2251 -0.0505 -0.0528 0.0108  181 LEU A O   
2800 C CB  . LEU A 178 ? 0.1320 0.1878 0.2158 -0.0473 -0.0672 0.0086  181 LEU A CB  
2801 C CG  . LEU A 178 ? 0.3801 0.4559 0.4760 -0.0473 -0.0729 0.0102  181 LEU A CG  
2802 C CD1 . LEU A 178 ? 0.2065 0.2840 0.3007 -0.0373 -0.0747 0.0113  181 LEU A CD1 
2803 C CD2 . LEU A 178 ? 0.2445 0.3386 0.3567 -0.0489 -0.0699 0.0132  181 LEU A CD2 
2815 N N   . TRP A 179 ? 0.1722 0.1880 0.2314 -0.0507 -0.0584 0.0053  182 TRP A N   
2816 C CA  . TRP A 179 ? 0.2737 0.2768 0.3250 -0.0457 -0.0526 0.0060  182 TRP A CA  
2817 C C   . TRP A 179 ? 0.2340 0.2280 0.2842 -0.0507 -0.0492 0.0073  182 TRP A C   
2818 O O   . TRP A 179 ? 0.2580 0.2491 0.3077 -0.0467 -0.0442 0.0102  182 TRP A O   
2819 C CB  . TRP A 179 ? 0.1992 0.1891 0.2366 -0.0420 -0.0530 0.0030  182 TRP A CB  
2820 C CG  . TRP A 179 ? 0.2605 0.2575 0.2972 -0.0364 -0.0546 0.0034  182 TRP A CG  
2821 C CD1 . TRP A 179 ? 0.3216 0.3308 0.3649 -0.0366 -0.0590 0.0041  182 TRP A CD1 
2822 C CD2 . TRP A 179 ? 0.2421 0.2347 0.2711 -0.0300 -0.0516 0.0038  182 TRP A CD2 
2823 N NE1 . TRP A 179 ? 0.3988 0.4083 0.4372 -0.0315 -0.0592 0.0050  182 TRP A NE1 
2824 C CE2 . TRP A 179 ? 0.2600 0.2609 0.2904 -0.0281 -0.0546 0.0049  182 TRP A CE2 
2825 C CE3 . TRP A 179 ? 0.2757 0.2592 0.2972 -0.0254 -0.0467 0.0039  182 TRP A CE3 
2826 C CZ2 . TRP A 179 ? 0.2680 0.2686 0.2926 -0.0236 -0.0527 0.0064  182 TRP A CZ2 
2827 C CZ3 . TRP A 179 ? 0.2970 0.2835 0.3146 -0.0199 -0.0446 0.0054  182 TRP A CZ3 
2828 C CH2 . TRP A 179 ? 0.2047 0.1999 0.2239 -0.0200 -0.0476 0.0067  182 TRP A CH2 
2839 N N   A SER A 180 ? 0.2419 0.2305 0.2906 -0.0602 -0.0524 0.0056  183 SER A N   
2840 N N   B SER A 180 ? 0.2419 0.2305 0.2905 -0.0603 -0.0524 0.0056  183 SER A N   
2841 C CA  A SER A 180 ? 0.2173 0.1935 0.2626 -0.0665 -0.0495 0.0074  183 SER A CA  
2842 C CA  B SER A 180 ? 0.2115 0.1877 0.2568 -0.0666 -0.0496 0.0073  183 SER A CA  
2843 C C   A SER A 180 ? 0.2755 0.2662 0.3336 -0.0685 -0.0457 0.0127  183 SER A C   
2844 C C   B SER A 180 ? 0.2747 0.2655 0.3328 -0.0685 -0.0457 0.0127  183 SER A C   
2845 O O   A SER A 180 ? 0.2449 0.2255 0.2994 -0.0713 -0.0417 0.0157  183 SER A O   
2846 O O   B SER A 180 ? 0.2448 0.2254 0.2993 -0.0711 -0.0416 0.0157  183 SER A O   
2847 C CB  A SER A 180 ? 0.2838 0.2503 0.3240 -0.0786 -0.0549 0.0043  183 SER A CB  
2848 C CB  B SER A 180 ? 0.2841 0.2511 0.3246 -0.0787 -0.0550 0.0043  183 SER A CB  
2849 O OG  A SER A 180 ? 0.3441 0.2926 0.3681 -0.0762 -0.0575 -0.0012 183 SER A OG  
2850 O OG  B SER A 180 ? 0.3740 0.3632 0.4290 -0.0861 -0.0597 0.0054  183 SER A OG  
2861 N N   . ALA A 181 ? 0.1594 0.1727 0.2309 -0.0664 -0.0464 0.0141  184 ALA A N   
2862 C CA  . ALA A 181 ? 0.2410 0.2692 0.3235 -0.0668 -0.0417 0.0186  184 ALA A CA  
2863 C C   . ALA A 181 ? 0.1477 0.1722 0.2257 -0.0575 -0.0361 0.0206  184 ALA A C   
2864 O O   . ALA A 181 ? 0.2177 0.2467 0.2985 -0.0584 -0.0312 0.0245  184 ALA A O   
2865 C CB  . ALA A 181 ? 0.1883 0.2413 0.2856 -0.0656 -0.0439 0.0191  184 ALA A CB  
2871 N N   . TYR A 182 ? 0.1404 0.1578 0.2111 -0.0494 -0.0370 0.0184  185 TYR A N   
2872 C CA  . TYR A 182 ? 0.1710 0.1872 0.2381 -0.0417 -0.0331 0.0204  185 TYR A CA  
2873 C C   . TYR A 182 ? 0.2091 0.2133 0.2692 -0.0426 -0.0291 0.0238  185 TYR A C   
2874 O O   . TYR A 182 ? 0.1692 0.1787 0.2304 -0.0411 -0.0252 0.0272  185 TYR A O   
2875 C CB  . TYR A 182 ? 0.1868 0.1988 0.2482 -0.0350 -0.0354 0.0181  185 TYR A CB  
2876 C CG  . TYR A 182 ? 0.1432 0.1665 0.2099 -0.0319 -0.0383 0.0165  185 TYR A CG  
2877 C CD1 . TYR A 182 ? 0.1767 0.2048 0.2472 -0.0344 -0.0428 0.0143  185 TYR A CD1 
2878 C CD2 . TYR A 182 ? 0.1346 0.1620 0.2011 -0.0264 -0.0370 0.0173  185 TYR A CD2 
2879 C CE1 . TYR A 182 ? 0.2623 0.2990 0.3367 -0.0304 -0.0456 0.0136  185 TYR A CE1 
2880 C CE2 . TYR A 182 ? 0.1111 0.1445 0.1803 -0.0231 -0.0397 0.0160  185 TYR A CE2 
2881 C CZ  . TYR A 182 ? 0.2582 0.2962 0.3316 -0.0245 -0.0438 0.0145  185 TYR A CZ  
2882 O OH  . TYR A 182 ? 0.2524 0.2948 0.3275 -0.0202 -0.0467 0.0139  185 TYR A OH  
2892 N N   . PRO A 183 ? 0.1623 0.1491 0.2133 -0.0441 -0.0295 0.0233  186 PRO A N   
2893 C CA  . PRO A 183 ? 0.1684 0.1422 0.2119 -0.0437 -0.0258 0.0275  186 PRO A CA  
2894 C C   . PRO A 183 ? 0.1940 0.1711 0.2415 -0.0519 -0.0229 0.0317  186 PRO A C   
2895 O O   . PRO A 183 ? 0.2490 0.2213 0.2918 -0.0505 -0.0191 0.0366  186 PRO A O   
2896 C CB  . PRO A 183 ? 0.2414 0.1940 0.2737 -0.0437 -0.0272 0.0252  186 PRO A CB  
2897 C CG  . PRO A 183 ? 0.2416 0.1972 0.2760 -0.0473 -0.0318 0.0196  186 PRO A CG  
2898 C CD  . PRO A 183 ? 0.1941 0.1708 0.2390 -0.0443 -0.0332 0.0189  186 PRO A CD  
2906 N N   . VAL A 184 ? 0.2128 0.1996 0.2691 -0.0606 -0.0247 0.0306  187 VAL A N   
2907 C CA  . VAL A 184 ? 0.2029 0.1967 0.2649 -0.0696 -0.0215 0.0353  187 VAL A CA  
2908 C C   . VAL A 184 ? 0.1687 0.1819 0.2379 -0.0646 -0.0169 0.0381  187 VAL A C   
2909 O O   . VAL A 184 ? 0.2952 0.3091 0.3624 -0.0667 -0.0119 0.0434  187 VAL A O   
2910 C CB  . VAL A 184 ? 0.2049 0.2069 0.2760 -0.0810 -0.0253 0.0338  187 VAL A CB  
2911 C CG1 . VAL A 184 ? 0.2454 0.2601 0.3253 -0.0910 -0.0214 0.0397  187 VAL A CG1 
2912 C CG2 . VAL A 184 ? 0.2913 0.2696 0.3511 -0.0868 -0.0299 0.0304  187 VAL A CG2 
2922 N N   . VAL A 185 ? 0.1702 0.1976 0.2458 -0.0578 -0.0186 0.0345  188 VAL A N   
2923 C CA  . VAL A 185 ? 0.2491 0.2913 0.3284 -0.0517 -0.0144 0.0358  188 VAL A CA  
2924 C C   . VAL A 185 ? 0.2025 0.2341 0.2699 -0.0458 -0.0117 0.0380  188 VAL A C   
2925 O O   . VAL A 185 ? 0.1609 0.1978 0.2261 -0.0451 -0.0066 0.0416  188 VAL A O   
2926 C CB  . VAL A 185 ? 0.2594 0.3129 0.3448 -0.0448 -0.0175 0.0311  188 VAL A CB  
2927 C CG1 . VAL A 185 ? 0.1677 0.2304 0.2523 -0.0372 -0.0133 0.0313  188 VAL A CG1 
2928 C CG2 . VAL A 185 ? 0.2424 0.3102 0.3406 -0.0500 -0.0204 0.0301  188 VAL A CG2 
2938 N N   . TRP A 186 ? 0.1480 0.1663 0.2075 -0.0413 -0.0150 0.0362  189 TRP A N   
2939 C CA  . TRP A 186 ? 0.2079 0.2182 0.2573 -0.0358 -0.0137 0.0390  189 TRP A CA  
2940 C C   . TRP A 186 ? 0.1826 0.1845 0.2260 -0.0399 -0.0097 0.0452  189 TRP A C   
2941 O O   . TRP A 186 ? 0.2396 0.2436 0.2773 -0.0374 -0.0066 0.0490  189 TRP A O   
2942 C CB  . TRP A 186 ? 0.2782 0.2779 0.3225 -0.0311 -0.0176 0.0370  189 TRP A CB  
2943 C CG  . TRP A 186 ? 0.2672 0.2654 0.3046 -0.0243 -0.0180 0.0392  189 TRP A CG  
2944 C CD1 . TRP A 186 ? 0.2376 0.2432 0.2752 -0.0199 -0.0206 0.0370  189 TRP A CD1 
2945 C CD2 . TRP A 186 ? 0.2009 0.1898 0.2300 -0.0216 -0.0165 0.0446  189 TRP A CD2 
2946 N NE1 . TRP A 186 ? 0.2514 0.2553 0.2825 -0.0156 -0.0212 0.0405  189 TRP A NE1 
2947 C CE2 . TRP A 186 ? 0.3003 0.2947 0.3264 -0.0157 -0.0188 0.0453  189 TRP A CE2 
2948 C CE3 . TRP A 186 ? 0.2065 0.1822 0.2299 -0.0240 -0.0140 0.0493  189 TRP A CE3 
2949 C CZ2 . TRP A 186 ? 0.3017 0.2920 0.3207 -0.0111 -0.0188 0.0508  189 TRP A CZ2 
2950 C CZ3 . TRP A 186 ? 0.2162 0.1847 0.2310 -0.0186 -0.0136 0.0548  189 TRP A CZ3 
2951 C CH2 . TRP A 186 ? 0.2723 0.2496 0.2857 -0.0117 -0.0161 0.0556  189 TRP A CH2 
2962 N N   . LEU A 187 ? 0.2037 0.1941 0.2464 -0.0468 -0.0100 0.0465  190 LEU A N   
2963 C CA  . LEU A 187 ? 0.1980 0.1748 0.2324 -0.0509 -0.0068 0.0530  190 LEU A CA  
2964 C C   . LEU A 187 ? 0.2725 0.2617 0.3100 -0.0563 -0.0013 0.0579  190 LEU A C   
2965 O O   . LEU A 187 ? 0.3327 0.3166 0.3613 -0.0550 0.0021  0.0639  190 LEU A O   
2966 C CB  . LEU A 187 ? 0.2100 0.1692 0.2417 -0.0585 -0.0089 0.0524  190 LEU A CB  
2967 C CG  . LEU A 187 ? 0.3112 0.2489 0.3313 -0.0629 -0.0064 0.0590  190 LEU A CG  
2968 C CD1 . LEU A 187 ? 0.3563 0.2798 0.3645 -0.0513 -0.0066 0.0616  190 LEU A CD1 
2969 C CD2 . LEU A 187 ? 0.3053 0.2251 0.3223 -0.0727 -0.0091 0.0571  190 LEU A CD2 
2981 N N   . ILE A 188 ? 0.1909 0.1978 0.2408 -0.0618 -0.0002 0.0561  191 ILE A N   
2982 C CA  . ILE A 188 ? 0.2784 0.3008 0.3330 -0.0665 0.0062  0.0609  191 ILE A CA  
2983 C C   . ILE A 188 ? 0.2545 0.2928 0.3094 -0.0573 0.0093  0.0590  191 ILE A C   
2984 O O   . ILE A 188 ? 0.2481 0.2995 0.3044 -0.0589 0.0157  0.0628  191 ILE A O   
2985 C CB  . ILE A 188 ? 0.2505 0.2875 0.3198 -0.0771 0.0063  0.0609  191 ILE A CB  
2986 C CG1 . ILE A 188 ? 0.2613 0.3155 0.3426 -0.0718 0.0028  0.0541  191 ILE A CG1 
2987 C CG2 . ILE A 188 ? 0.4151 0.4332 0.4814 -0.0877 0.0023  0.0618  191 ILE A CG2 
2988 C CD1 . ILE A 188 ? 0.3343 0.4031 0.4307 -0.0816 0.0006  0.0537  191 ILE A CD1 
3000 N N   . GLY A 189 ? 0.2988 0.3354 0.3512 -0.0482 0.0051  0.0534  192 GLY A N   
3001 C CA  . GLY A 189 ? 0.2552 0.3025 0.3057 -0.0401 0.0068  0.0503  192 GLY A CA  
3002 C C   . GLY A 189 ? 0.2606 0.3000 0.2960 -0.0354 0.0082  0.0531  192 GLY A C   
3003 O O   . GLY A 189 ? 0.3109 0.3398 0.3384 -0.0382 0.0093  0.0590  192 GLY A O   
3007 N N   A SER A 190 ? 0.2295 0.2731 0.2599 -0.0281 0.0074  0.0488  193 SER A N   
3008 N N   B SER A 190 ? 0.2295 0.2731 0.2599 -0.0281 0.0073  0.0488  193 SER A N   
3009 C CA  A SER A 190 ? 0.3111 0.3494 0.3263 -0.0241 0.0077  0.0507  193 SER A CA  
3010 C CA  B SER A 190 ? 0.3112 0.3494 0.3264 -0.0242 0.0078  0.0508  193 SER A CA  
3011 C C   A SER A 190 ? 0.2765 0.3018 0.2855 -0.0231 0.0019  0.0531  193 SER A C   
3012 C C   B SER A 190 ? 0.2765 0.3018 0.2854 -0.0231 0.0019  0.0531  193 SER A C   
3013 O O   A SER A 190 ? 0.3466 0.3667 0.3442 -0.0220 0.0022  0.0581  193 SER A O   
3014 O O   B SER A 190 ? 0.3464 0.3666 0.3438 -0.0218 0.0021  0.0579  193 SER A O   
3015 C CB  A SER A 190 ? 0.3184 0.3609 0.3282 -0.0176 0.0068  0.0444  193 SER A CB  
3016 C CB  B SER A 190 ? 0.3180 0.3608 0.3276 -0.0177 0.0072  0.0446  193 SER A CB  
3017 O OG  A SER A 190 ? 0.3549 0.3933 0.3685 -0.0154 -0.0001 0.0392  193 SER A OG  
3018 O OG  B SER A 190 ? 0.3874 0.4418 0.3983 -0.0162 0.0145  0.0439  193 SER A OG  
3029 N N   . GLU A 191 ? 0.2442 0.2654 0.2603 -0.0227 -0.0033 0.0501  194 GLU A N   
3030 C CA  . GLU A 191 ? 0.3149 0.3266 0.3265 -0.0201 -0.0080 0.0524  194 GLU A CA  
3031 C C   . GLU A 191 ? 0.3535 0.3539 0.3620 -0.0226 -0.0060 0.0589  194 GLU A C   
3032 O O   . GLU A 191 ? 0.2778 0.2707 0.2795 -0.0185 -0.0084 0.0630  194 GLU A O   
3033 C CB  . GLU A 191 ? 0.1813 0.1924 0.2005 -0.0186 -0.0128 0.0474  194 GLU A CB  
3034 C CG  . GLU A 191 ? 0.3507 0.3686 0.3703 -0.0160 -0.0162 0.0420  194 GLU A CG  
3035 C CD  . GLU A 191 ? 0.4399 0.4642 0.4667 -0.0172 -0.0145 0.0371  194 GLU A CD  
3036 O OE1 . GLU A 191 ? 0.4673 0.4941 0.5009 -0.0207 -0.0110 0.0381  194 GLU A OE1 
3037 O OE2 . GLU A 191 ? 0.3634 0.3901 0.3892 -0.0147 -0.0169 0.0327  194 GLU A OE2 
3044 N N   . GLY A 192 ? 0.3153 0.3141 0.3286 -0.0292 -0.0020 0.0604  195 GLY A N   
3045 C CA  . GLY A 192 ? 0.2145 0.1983 0.2233 -0.0330 -0.0006 0.0663  195 GLY A CA  
3046 C C   . GLY A 192 ? 0.2297 0.2136 0.2328 -0.0384 0.0053  0.0733  195 GLY A C   
3047 O O   . GLY A 192 ? 0.3150 0.2999 0.3080 -0.0347 0.0067  0.0776  195 GLY A O   
3051 N N   . ALA A 193 ? 0.2587 0.2425 0.2679 -0.0479 0.0086  0.0749  196 ALA A N   
3052 C CA  . ALA A 193 ? 0.3888 0.3723 0.3931 -0.0549 0.0148  0.0829  196 ALA A CA  
3053 C C   . ALA A 193 ? 0.3076 0.3127 0.3145 -0.0545 0.0205  0.0827  196 ALA A C   
3054 O O   . ALA A 193 ? 0.3224 0.3293 0.3224 -0.0583 0.0265  0.0899  196 ALA A O   
3055 C CB  . ALA A 193 ? 0.2911 0.2677 0.3015 -0.0672 0.0159  0.0851  196 ALA A CB  
3061 N N   . GLY A 194 ? 0.2721 0.2923 0.2874 -0.0495 0.0193  0.0750  197 GLY A N   
3062 C CA  . GLY A 194 ? 0.3930 0.4314 0.4087 -0.0468 0.0250  0.0738  197 GLY A CA  
3063 C C   . GLY A 194 ? 0.3190 0.3733 0.3451 -0.0549 0.0323  0.0774  197 GLY A C   
3064 O O   . GLY A 194 ? 0.4614 0.5274 0.4831 -0.0539 0.0397  0.0806  197 GLY A O   
3068 N N   . ILE A 195 ? 0.3732 0.4295 0.4129 -0.0631 0.0304  0.0772  198 ILE A N   
3069 C CA  . ILE A 195 ? 0.3814 0.4569 0.4340 -0.0723 0.0365  0.0812  198 ILE A CA  
3070 C C   . ILE A 195 ? 0.3586 0.4591 0.4248 -0.0660 0.0385  0.0753  198 ILE A C   
3071 O O   . ILE A 195 ? 0.3436 0.4661 0.4172 -0.0673 0.0465  0.0785  198 ILE A O   
3072 C CB  . ILE A 195 ? 0.3651 0.4319 0.4255 -0.0854 0.0325  0.0837  198 ILE A CB  
3073 C CG1 . ILE A 195 ? 0.3292 0.3737 0.3757 -0.0932 0.0340  0.0923  198 ILE A CG1 
3074 C CG2 . ILE A 195 ? 0.4862 0.5790 0.5659 -0.0946 0.0358  0.0853  198 ILE A CG2 
3075 C CD1 . ILE A 195 ? 0.4977 0.5158 0.5399 -0.0983 0.0266  0.0911  198 ILE A CD1 
3087 N N   . VAL A 196 ? 0.2438 0.3415 0.3132 -0.0584 0.0318  0.0672  199 VAL A N   
3088 C CA  . VAL A 196 ? 0.2567 0.3738 0.3370 -0.0505 0.0327  0.0614  199 VAL A CA  
3089 C C   . VAL A 196 ? 0.3273 0.4391 0.3934 -0.0378 0.0338  0.0567  199 VAL A C   
3090 O O   . VAL A 196 ? 0.3086 0.4012 0.3619 -0.0349 0.0285  0.0547  199 VAL A O   
3091 C CB  . VAL A 196 ? 0.4054 0.5215 0.4968 -0.0509 0.0242  0.0559  199 VAL A CB  
3092 C CG1 . VAL A 196 ? 0.5746 0.7154 0.6816 -0.0457 0.0260  0.0531  199 VAL A CG1 
3093 C CG2 . VAL A 196 ? 0.6117 0.7200 0.7083 -0.0642 0.0202  0.0594  199 VAL A CG2 
3103 N N   . PRO A 197 ? 0.3843 0.5121 0.4514 -0.0300 0.0404  0.0547  200 PRO A N   
3104 C CA  . PRO A 197 ? 0.4031 0.5221 0.4536 -0.0188 0.0407  0.0493  200 PRO A CA  
3105 C C   . PRO A 197 ? 0.2445 0.3538 0.2954 -0.0123 0.0323  0.0414  200 PRO A C   
3106 O O   . PRO A 197 ? 0.2805 0.3948 0.3457 -0.0137 0.0278  0.0397  200 PRO A O   
3107 C CB  . PRO A 197 ? 0.3958 0.5346 0.4476 -0.0120 0.0511  0.0492  200 PRO A CB  
3108 C CG  . PRO A 197 ? 0.3215 0.4837 0.3967 -0.0169 0.0538  0.0525  200 PRO A CG  
3109 C CD  . PRO A 197 ? 0.3427 0.4979 0.4254 -0.0310 0.0481  0.0576  200 PRO A CD  
3117 N N   . LEU A 198 ? 0.2631 0.3580 0.2966 -0.0057 0.0299  0.0370  201 LEU A N   
3118 C CA  . LEU A 198 ? 0.2582 0.3406 0.2893 -0.0018 0.0213  0.0307  201 LEU A CA  
3119 C C   . LEU A 198 ? 0.3461 0.4374 0.3876 0.0052  0.0213  0.0259  201 LEU A C   
3120 O O   . LEU A 198 ? 0.2577 0.3445 0.3061 0.0049  0.0144  0.0234  201 LEU A O   
3121 C CB  . LEU A 198 ? 0.2746 0.3419 0.2848 0.0025  0.0189  0.0272  201 LEU A CB  
3122 C CG  . LEU A 198 ? 0.5197 0.5738 0.5248 0.0059  0.0106  0.0209  201 LEU A CG  
3123 C CD1 . LEU A 198 ? 0.3052 0.3546 0.3196 0.0000  0.0031  0.0227  201 LEU A CD1 
3124 C CD2 . LEU A 198 ? 0.2942 0.3349 0.2778 0.0080  0.0082  0.0179  201 LEU A CD2 
3136 N N   A ASN A 199 ? 0.2414 0.3460 0.2839 0.0123  0.0294  0.0250  202 ASN A N   
3137 N N   B ASN A 199 ? 0.2431 0.3475 0.2853 0.0124  0.0294  0.0249  202 ASN A N   
3138 C CA  A ASN A 199 ? 0.2673 0.3801 0.3188 0.0215  0.0296  0.0208  202 ASN A CA  
3139 C CA  B ASN A 199 ? 0.2678 0.3811 0.3193 0.0215  0.0299  0.0209  202 ASN A CA  
3140 C C   A ASN A 199 ? 0.2838 0.4121 0.3581 0.0161  0.0265  0.0240  202 ASN A C   
3141 C C   B ASN A 199 ? 0.2830 0.4108 0.3570 0.0160  0.0263  0.0240  202 ASN A C   
3142 O O   A ASN A 199 ? 0.2186 0.3459 0.2994 0.0206  0.0210  0.0209  202 ASN A O   
3143 O O   B ASN A 199 ? 0.2209 0.3466 0.3008 0.0201  0.0205  0.0208  202 ASN A O   
3144 C CB  A ASN A 199 ? 0.3192 0.4452 0.3675 0.0318  0.0401  0.0196  202 ASN A CB  
3145 C CB  B ASN A 199 ? 0.3184 0.4465 0.3680 0.0310  0.0408  0.0204  202 ASN A CB  
3146 C CG  A ASN A 199 ? 0.3104 0.4567 0.3662 0.0259  0.0493  0.0269  202 ASN A CG  
3147 C CG  B ASN A 199 ? 0.3690 0.5020 0.4236 0.0443  0.0414  0.0154  202 ASN A CG  
3148 O OD1 A ASN A 199 ? 0.4798 0.6467 0.5563 0.0200  0.0508  0.0321  202 ASN A OD1 
3149 O OD1 B ASN A 199 ? 0.4281 0.5519 0.4864 0.0456  0.0332  0.0126  202 ASN A OD1 
3150 N ND2 A ASN A 199 ? 0.5010 0.6417 0.5391 0.0265  0.0553  0.0277  202 ASN A ND2 
3151 N ND2 B ASN A 199 ? 0.4611 0.6085 0.5150 0.0548  0.0516  0.0147  202 ASN A ND2 
3164 N N   . ILE A 200 ? 0.2350 0.3763 0.3202 0.0059  0.0293  0.0305  203 ILE A N   
3165 C CA  . ILE A 200 ? 0.1488 0.3029 0.2537 -0.0014 0.0250  0.0332  203 ILE A CA  
3166 C C   . ILE A 200 ? 0.2031 0.3378 0.3045 -0.0073 0.0150  0.0314  203 ILE A C   
3167 O O   . ILE A 200 ? 0.1442 0.2819 0.2553 -0.0078 0.0088  0.0298  203 ILE A O   
3168 C CB  . ILE A 200 ? 0.5117 0.6831 0.6276 -0.0125 0.0307  0.0408  203 ILE A CB  
3169 C CG1 . ILE A 200 ? 0.3633 0.5585 0.4844 -0.0061 0.0419  0.0432  203 ILE A CG1 
3170 C CG2 . ILE A 200 ? 0.2052 0.3875 0.3394 -0.0222 0.0247  0.0431  203 ILE A CG2 
3171 C CD1 . ILE A 200 ? 0.2865 0.5015 0.4212 0.0054  0.0429  0.0405  203 ILE A CD1 
3183 N N   . GLU A 201 ? 0.2435 0.3594 0.3308 -0.0113 0.0134  0.0320  204 GLU A N   
3184 C CA  . GLU A 201 ? 0.1988 0.2978 0.2823 -0.0152 0.0051  0.0304  204 GLU A CA  
3185 C C   . GLU A 201 ? 0.2090 0.3015 0.2903 -0.0077 -0.0006 0.0248  204 GLU A C   
3186 O O   . GLU A 201 ? 0.2033 0.2931 0.2902 -0.0100 -0.0068 0.0236  204 GLU A O   
3187 C CB  . GLU A 201 ? 0.2018 0.2843 0.2704 -0.0177 0.0049  0.0322  204 GLU A CB  
3188 C CG  . GLU A 201 ? 0.3114 0.3785 0.3762 -0.0198 -0.0026 0.0308  204 GLU A CG  
3189 C CD  . GLU A 201 ? 0.2932 0.3473 0.3448 -0.0202 -0.0032 0.0330  204 GLU A CD  
3190 O OE1 . GLU A 201 ? 0.2847 0.3400 0.3289 -0.0199 0.0018  0.0360  204 GLU A OE1 
3191 O OE2 . GLU A 201 ? 0.4229 0.4667 0.4714 -0.0204 -0.0085 0.0322  204 GLU A OE2 
3198 N N   . THR A 202 ? 0.1720 0.2599 0.2431 0.0011  0.0015  0.0213  205 THR A N   
3199 C CA  . THR A 202 ? 0.1984 0.2769 0.2652 0.0077  -0.0038 0.0165  205 THR A CA  
3200 C C   . THR A 202 ? 0.1903 0.2819 0.2719 0.0110  -0.0056 0.0162  205 THR A C   
3201 O O   . THR A 202 ? 0.1467 0.2314 0.2292 0.0115  -0.0122 0.0146  205 THR A O   
3202 C CB  . THR A 202 ? 0.2240 0.2940 0.2758 0.0163  -0.0007 0.0125  205 THR A CB  
3203 O OG1 . THR A 202 ? 0.1951 0.2553 0.2331 0.0125  0.0001  0.0134  205 THR A OG1 
3204 C CG2 . THR A 202 ? 0.1732 0.2286 0.2177 0.0217  -0.0068 0.0079  205 THR A CG2 
3212 N N   . LEU A 203 ? 0.1436 0.2556 0.2370 0.0133  0.0003  0.0185  206 LEU A N   
3213 C CA  . LEU A 203 ? 0.1659 0.2949 0.2758 0.0161  -0.0019 0.0193  206 LEU A CA  
3214 C C   . LEU A 203 ? 0.1217 0.2510 0.2399 0.0056  -0.0092 0.0212  206 LEU A C   
3215 O O   . LEU A 203 ? 0.2010 0.3311 0.3240 0.0078  -0.0155 0.0201  206 LEU A O   
3216 C CB  . LEU A 203 ? 0.1343 0.2899 0.2578 0.0184  0.0062  0.0227  206 LEU A CB  
3217 C CG  . LEU A 203 ? 0.3200 0.5004 0.4647 0.0189  0.0038  0.0254  206 LEU A CG  
3218 C CD1 . LEU A 203 ? 0.2015 0.3773 0.3452 0.0315  -0.0010 0.0221  206 LEU A CD1 
3219 C CD2 . LEU A 203 ? 0.3983 0.6082 0.5573 0.0205  0.0130  0.0298  206 LEU A CD2 
3231 N N   . LEU A 204 ? 0.1195 0.2465 0.2375 -0.0055 -0.0084 0.0240  207 LEU A N   
3232 C CA  . LEU A 204 ? 0.1248 0.2494 0.2480 -0.0155 -0.0148 0.0250  207 LEU A CA  
3233 C C   . LEU A 204 ? 0.1986 0.3039 0.3115 -0.0139 -0.0217 0.0216  207 LEU A C   
3234 O O   . LEU A 204 ? 0.1519 0.2584 0.2692 -0.0155 -0.0279 0.0207  207 LEU A O   
3235 C CB  . LEU A 204 ? 0.1907 0.3113 0.3121 -0.0265 -0.0121 0.0285  207 LEU A CB  
3236 C CG  . LEU A 204 ? 0.1705 0.3118 0.3039 -0.0320 -0.0059 0.0333  207 LEU A CG  
3237 C CD1 . LEU A 204 ? 0.2938 0.4245 0.4202 -0.0419 -0.0028 0.0373  207 LEU A CD1 
3238 C CD2 . LEU A 204 ? 0.2469 0.4076 0.3975 -0.0378 -0.0102 0.0348  207 LEU A CD2 
3250 N N   . PHE A 205 ? 0.1758 0.2645 0.2747 -0.0114 -0.0207 0.0201  208 PHE A N   
3251 C CA  . PHE A 205 ? 0.1557 0.2289 0.2458 -0.0106 -0.0265 0.0178  208 PHE A CA  
3252 C C   . PHE A 205 ? 0.1462 0.2200 0.2373 -0.0035 -0.0304 0.0156  208 PHE A C   
3253 O O   . PHE A 205 ? 0.1801 0.2478 0.2695 -0.0048 -0.0360 0.0149  208 PHE A O   
3254 C CB  . PHE A 205 ? 0.1553 0.2149 0.2321 -0.0093 -0.0249 0.0173  208 PHE A CB  
3255 C CG  . PHE A 205 ? 0.1432 0.1965 0.2163 -0.0155 -0.0239 0.0198  208 PHE A CG  
3256 C CD1 . PHE A 205 ? 0.2727 0.3221 0.3481 -0.0208 -0.0270 0.0203  208 PHE A CD1 
3257 C CD2 . PHE A 205 ? 0.3090 0.3588 0.3746 -0.0153 -0.0200 0.0216  208 PHE A CD2 
3258 C CE1 . PHE A 205 ? 0.1178 0.1587 0.1882 -0.0247 -0.0258 0.0226  208 PHE A CE1 
3259 C CE2 . PHE A 205 ? 0.1425 0.1856 0.2041 -0.0195 -0.0192 0.0247  208 PHE A CE2 
3260 C CZ  . PHE A 205 ? 0.2152 0.2532 0.2794 -0.0237 -0.0219 0.0252  208 PHE A CZ  
3270 N N   . MET A 206 ? 0.1188 0.1988 0.2113 0.0047  -0.0271 0.0147  209 MET A N   
3271 C CA  . MET A 206 ? 0.1960 0.2734 0.2875 0.0129  -0.0307 0.0130  209 MET A CA  
3272 C C   . MET A 206 ? 0.1889 0.2793 0.2931 0.0117  -0.0356 0.0147  209 MET A C   
3273 O O   . MET A 206 ? 0.1413 0.2242 0.2420 0.0132  -0.0416 0.0143  209 MET A O   
3274 C CB  . MET A 206 ? 0.1991 0.2802 0.2890 0.0236  -0.0253 0.0115  209 MET A CB  
3275 C CG  . MET A 206 ? 0.1922 0.2630 0.2759 0.0337  -0.0287 0.0094  209 MET A CG  
3276 S SD  . MET A 206 ? 0.4623 0.5557 0.5635 0.0426  -0.0295 0.0117  209 MET A SD  
3277 C CE  . MET A 206 ? 0.1949 0.2963 0.2953 0.0552  -0.0195 0.0100  209 MET A CE  
3287 N N   . VAL A 207 ? 0.1482 0.2586 0.2665 0.0079  -0.0335 0.0171  210 VAL A N   
3288 C CA  . VAL A 207 ? 0.2175 0.3421 0.3480 0.0049  -0.0393 0.0189  210 VAL A CA  
3289 C C   . VAL A 207 ? 0.1179 0.2299 0.2417 -0.0040 -0.0454 0.0181  210 VAL A C   
3290 O O   . VAL A 207 ? 0.1391 0.2515 0.2635 -0.0036 -0.0521 0.0181  210 VAL A O   
3291 C CB  . VAL A 207 ? 0.1834 0.3330 0.3305 -0.0002 -0.0359 0.0221  210 VAL A CB  
3292 C CG1 . VAL A 207 ? 0.1498 0.3126 0.3080 -0.0075 -0.0435 0.0237  210 VAL A CG1 
3293 C CG2 . VAL A 207 ? 0.1124 0.2790 0.2678 0.0112  -0.0298 0.0232  210 VAL A CG2 
3303 N N   . LEU A 208 ? 0.1065 0.2069 0.2230 -0.0113 -0.0431 0.0175  211 LEU A N   
3304 C CA  . LEU A 208 ? 0.1743 0.2620 0.2832 -0.0181 -0.0476 0.0163  211 LEU A CA  
3305 C C   . LEU A 208 ? 0.1467 0.2201 0.2444 -0.0131 -0.0508 0.0149  211 LEU A C   
3306 O O   . LEU A 208 ? 0.2068 0.2770 0.3015 -0.0148 -0.0562 0.0145  211 LEU A O   
3307 C CB  . LEU A 208 ? 0.1631 0.2412 0.2664 -0.0247 -0.0436 0.0166  211 LEU A CB  
3308 C CG  . LEU A 208 ? 0.1970 0.2853 0.3090 -0.0327 -0.0409 0.0188  211 LEU A CG  
3309 C CD1 . LEU A 208 ? 0.2922 0.3669 0.3957 -0.0370 -0.0367 0.0198  211 LEU A CD1 
3310 C CD2 . LEU A 208 ? 0.1969 0.2914 0.3148 -0.0407 -0.0470 0.0185  211 LEU A CD2 
3322 N N   . ASP A 209 ? 0.1582 0.2228 0.2487 -0.0079 -0.0476 0.0144  212 ASP A N   
3323 C CA  . ASP A 209 ? 0.1124 0.1633 0.1921 -0.0053 -0.0505 0.0138  212 ASP A CA  
3324 C C   . ASP A 209 ? 0.1147 0.1672 0.1955 -0.0005 -0.0557 0.0144  212 ASP A C   
3325 O O   . ASP A 209 ? 0.2421 0.2876 0.3167 -0.0023 -0.0600 0.0149  212 ASP A O   
3326 C CB  . ASP A 209 ? 0.1475 0.1895 0.2195 -0.0015 -0.0472 0.0131  212 ASP A CB  
3327 C CG  . ASP A 209 ? 0.1725 0.2101 0.2401 -0.0062 -0.0438 0.0134  212 ASP A CG  
3328 O OD1 . ASP A 209 ? 0.1367 0.1734 0.2044 -0.0112 -0.0444 0.0141  212 ASP A OD1 
3329 O OD2 . ASP A 209 ? 0.1389 0.1734 0.2018 -0.0041 -0.0407 0.0129  212 ASP A OD2 
3334 N N   . VAL A 210 ? 0.1177 0.1797 0.2057 0.0065  -0.0551 0.0148  213 VAL A N   
3335 C CA  . VAL A 210 ? 0.1662 0.2293 0.2549 0.0130  -0.0603 0.0161  213 VAL A CA  
3336 C C   . VAL A 210 ? 0.1980 0.2704 0.2920 0.0078  -0.0662 0.0174  213 VAL A C   
3337 O O   . VAL A 210 ? 0.1390 0.2048 0.2266 0.0090  -0.0716 0.0187  213 VAL A O   
3338 C CB  . VAL A 210 ? 0.2588 0.3328 0.3556 0.0234  -0.0576 0.0165  213 VAL A CB  
3339 C CG1 . VAL A 210 ? 0.3276 0.4047 0.4266 0.0315  -0.0635 0.0187  213 VAL A CG1 
3340 C CG2 . VAL A 210 ? 0.3293 0.3895 0.4160 0.0290  -0.0524 0.0142  213 VAL A CG2 
3350 N N   . SER A 211 ? 0.1164 0.2027 0.2204 0.0012  -0.0654 0.0173  214 SER A N   
3351 C CA  . SER A 211 ? 0.1980 0.2917 0.3051 -0.0053 -0.0718 0.0177  214 SER A CA  
3352 C C   . SER A 211 ? 0.2034 0.2804 0.2963 -0.0107 -0.0740 0.0162  214 SER A C   
3353 O O   . SER A 211 ? 0.1569 0.2329 0.2450 -0.0117 -0.0801 0.0167  214 SER A O   
3354 C CB  . SER A 211 ? 0.2322 0.3409 0.3509 -0.0136 -0.0705 0.0177  214 SER A CB  
3355 O OG  . SER A 211 ? 0.2246 0.3538 0.3585 -0.0087 -0.0683 0.0200  214 SER A OG  
3361 N N   . ALA A 212 ? 0.1963 0.2614 0.2821 -0.0136 -0.0689 0.0147  215 ALA A N   
3362 C CA  . ALA A 212 ? 0.2852 0.3375 0.3591 -0.0180 -0.0694 0.0134  215 ALA A CA  
3363 C C   . ALA A 212 ? 0.3458 0.3879 0.4095 -0.0141 -0.0708 0.0148  215 ALA A C   
3364 O O   . ALA A 212 ? 0.3366 0.3716 0.3908 -0.0167 -0.0719 0.0145  215 ALA A O   
3365 C CB  . ALA A 212 ? 0.1686 0.2141 0.2400 -0.0213 -0.0634 0.0122  215 ALA A CB  
3371 N N   . LYS A 213 ? 0.2414 0.2819 0.3059 -0.0079 -0.0704 0.0164  216 LYS A N   
3372 C CA  . LYS A 213 ? 0.2065 0.2347 0.2603 -0.0056 -0.0717 0.0184  216 LYS A CA  
3373 C C   . LYS A 213 ? 0.3151 0.3437 0.3681 -0.0001 -0.0774 0.0210  216 LYS A C   
3374 O O   . LYS A 213 ? 0.4285 0.4546 0.4745 -0.0021 -0.0815 0.0226  216 LYS A O   
3375 C CB  . LYS A 213 ? 0.2287 0.2492 0.2798 -0.0041 -0.0675 0.0182  216 LYS A CB  
3376 C CG  . LYS A 213 ? 0.2739 0.2937 0.3243 -0.0090 -0.0629 0.0169  216 LYS A CG  
3377 C CD  . LYS A 213 ? 0.2862 0.2999 0.3334 -0.0082 -0.0599 0.0168  216 LYS A CD  
3378 C CE  . LYS A 213 ? 0.2953 0.3109 0.3430 -0.0120 -0.0559 0.0164  216 LYS A CE  
3379 N NZ  . LYS A 213 ? 0.4029 0.4259 0.4574 -0.0132 -0.0540 0.0151  216 LYS A NZ  
3390 N N   . VAL A 214 ? 0.2700 0.3054 0.3313 0.0068  -0.0777 0.0212  217 VAL A N   
3391 C CA  . VAL A 214 ? 0.1838 0.2202 0.2450 0.0143  -0.0830 0.0242  217 VAL A CA  
3392 C C   . VAL A 214 ? 0.1726 0.2251 0.2413 0.0123  -0.0886 0.0251  217 VAL A C   
3393 O O   . VAL A 214 ? 0.1970 0.2468 0.2589 0.0126  -0.0945 0.0277  217 VAL A O   
3394 C CB  . VAL A 214 ? 0.2500 0.2879 0.3167 0.0246  -0.0806 0.0240  217 VAL A CB  
3395 C CG1 . VAL A 214 ? 0.2751 0.3122 0.3409 0.0344  -0.0863 0.0277  217 VAL A CG1 
3396 C CG2 . VAL A 214 ? 0.2408 0.2608 0.2975 0.0250  -0.0759 0.0222  217 VAL A CG2 
3406 N N   . GLY A 215 ? 0.2045 0.2738 0.2864 0.0093  -0.0871 0.0232  218 GLY A N   
3407 C CA  . GLY A 215 ? 0.2656 0.3508 0.3548 0.0050  -0.0932 0.0238  218 GLY A CA  
3408 C C   . GLY A 215 ? 0.2919 0.3682 0.3685 -0.0029 -0.0969 0.0227  218 GLY A C   
3409 O O   . GLY A 215 ? 0.2631 0.3440 0.3367 -0.0033 -0.1043 0.0245  218 GLY A O   
3413 N N   . PHE A 216 ? 0.2092 0.2733 0.2777 -0.0087 -0.0918 0.0198  219 PHE A N   
3414 C CA  . PHE A 216 ? 0.3042 0.3585 0.3587 -0.0143 -0.0935 0.0185  219 PHE A CA  
3415 C C   . PHE A 216 ? 0.2776 0.3237 0.3206 -0.0102 -0.0972 0.0222  219 PHE A C   
3416 O O   . PHE A 216 ? 0.2390 0.2846 0.2730 -0.0127 -0.1024 0.0226  219 PHE A O   
3417 C CB  . PHE A 216 ? 0.2715 0.3150 0.3204 -0.0179 -0.0862 0.0158  219 PHE A CB  
3418 C CG  . PHE A 216 ? 0.2547 0.2885 0.2890 -0.0218 -0.0861 0.0142  219 PHE A CG  
3419 C CD1 . PHE A 216 ? 0.3724 0.3981 0.3955 -0.0197 -0.0854 0.0169  219 PHE A CD1 
3420 C CD2 . PHE A 216 ? 0.2425 0.2746 0.2734 -0.0277 -0.0861 0.0100  219 PHE A CD2 
3421 C CE1 . PHE A 216 ? 0.3155 0.3346 0.3253 -0.0223 -0.0840 0.0156  219 PHE A CE1 
3422 C CE2 . PHE A 216 ? 0.2551 0.2772 0.2709 -0.0296 -0.0850 0.0078  219 PHE A CE2 
3423 C CZ  . PHE A 216 ? 0.2224 0.2395 0.2281 -0.0264 -0.0836 0.0107  219 PHE A CZ  
3433 N N   . GLY A 217 ? 0.2579 0.2962 0.2994 -0.0043 -0.0948 0.0250  220 GLY A N   
3434 C CA  . GLY A 217 ? 0.1683 0.1960 0.1976 -0.0014 -0.0980 0.0294  220 GLY A CA  
3435 C C   . GLY A 217 ? 0.2771 0.3116 0.3075 0.0038  -0.1062 0.0330  220 GLY A C   
3436 O O   . GLY A 217 ? 0.2654 0.2939 0.2836 0.0036  -0.1106 0.0365  220 GLY A O   
3440 N N   . LEU A 218 ? 0.2643 0.3130 0.3094 0.0090  -0.1083 0.0329  221 LEU A N   
3441 C CA  . LEU A 218 ? 0.1973 0.2558 0.2453 0.0153  -0.1154 0.0367  221 LEU A CA  
3442 C C   . LEU A 218 ? 0.3589 0.4256 0.4018 0.0083  -0.1195 0.0352  221 LEU A C   
3443 O O   . LEU A 218 ? 0.3117 0.3783 0.3466 0.0113  -0.1244 0.0386  221 LEU A O   
3444 C CB  . LEU A 218 ? 0.2872 0.3634 0.3537 0.0225  -0.1145 0.0366  221 LEU A CB  
3445 C CG  . LEU A 218 ? 0.3525 0.4193 0.4211 0.0334  -0.1113 0.0383  221 LEU A CG  
3446 C CD1 . LEU A 218 ? 0.3932 0.4803 0.4811 0.0393  -0.1082 0.0371  221 LEU A CD1 
3447 C CD2 . LEU A 218 ? 0.2948 0.3491 0.3528 0.0431  -0.1156 0.0437  221 LEU A CD2 
3459 N N   . ILE A 219 ? 0.3079 0.3800 0.3538 -0.0008 -0.1177 0.0301  222 ILE A N   
3460 C CA  . ILE A 219 ? 0.3067 0.3834 0.3455 -0.0080 -0.1219 0.0275  222 ILE A CA  
3461 C C   . ILE A 219 ? 0.3117 0.3723 0.3296 -0.0103 -0.1232 0.0285  222 ILE A C   
3462 O O   . ILE A 219 ? 0.2922 0.3543 0.3003 -0.0109 -0.1284 0.0295  222 ILE A O   
3463 C CB  . ILE A 219 ? 0.3257 0.4070 0.3704 -0.0174 -0.1195 0.0216  222 ILE A CB  
3464 C CG1 . ILE A 219 ? 0.3446 0.4452 0.4097 -0.0162 -0.1185 0.0216  222 ILE A CG1 
3465 C CG2 . ILE A 219 ? 0.4105 0.4901 0.4432 -0.0254 -0.1241 0.0179  222 ILE A CG2 
3466 C CD1 . ILE A 219 ? 0.3851 0.4866 0.4571 -0.0245 -0.1140 0.0174  222 ILE A CD1 
3478 N N   . LEU A 220 ? 0.3051 0.3518 0.3160 -0.0115 -0.1185 0.0286  223 LEU A N   
3479 C CA  . LEU A 220 ? 0.3073 0.3414 0.2987 -0.0144 -0.1184 0.0297  223 LEU A CA  
3480 C C   . LEU A 220 ? 0.2765 0.3045 0.2584 -0.0089 -0.1215 0.0368  223 LEU A C   
3481 O O   . LEU A 220 ? 0.3361 0.3622 0.3040 -0.0101 -0.1249 0.0383  223 LEU A O   
3482 C CB  . LEU A 220 ? 0.3658 0.3899 0.3547 -0.0163 -0.1082 0.0276  223 LEU A CB  
3483 C CG  . LEU A 220 ? 0.2233 0.2370 0.1944 -0.0182 -0.1043 0.0293  223 LEU A CG  
3484 C CD1 . LEU A 220 ? 0.3561 0.3692 0.3143 -0.0227 -0.1055 0.0246  223 LEU A CD1 
3485 C CD2 . LEU A 220 ? 0.3362 0.3446 0.3098 -0.0188 -0.0950 0.0291  223 LEU A CD2 
3497 N N   . LEU A 221 ? 0.3571 0.3802 0.3448 -0.0027 -0.1202 0.0410  224 LEU A N   
3498 C CA  . LEU A 221 ? 0.3575 0.3694 0.3338 0.0019  -0.1222 0.0481  224 LEU A CA  
3499 C C   . LEU A 221 ? 0.4361 0.4558 0.4125 0.0078  -0.1283 0.0509  224 LEU A C   
3500 O O   . LEU A 221 ? 0.4820 0.4919 0.4469 0.0115  -0.1304 0.0572  224 LEU A O   
3501 C CB  . LEU A 221 ? 0.3820 0.3828 0.3625 0.0066  -0.1194 0.0511  224 LEU A CB  
3502 C CG  . LEU A 221 ? 0.3284 0.3214 0.3078 0.0006  -0.1103 0.0483  224 LEU A CG  
3503 C CD1 . LEU A 221 ? 0.2208 0.2020 0.2031 0.0046  -0.1076 0.0499  224 LEU A CD1 
3504 C CD2 . LEU A 221 ? 0.3403 0.3261 0.3036 -0.0059 -0.1077 0.0511  224 LEU A CD2 
3516 N N   . ARG A 222 ? 0.5095 0.5414 0.3358 0.1283  -0.0112 0.0893  225 ARG A N   
3517 C CA  . ARG A 222 ? 0.5272 0.6079 0.3691 0.1739  -0.0128 0.1185  225 ARG A CA  
3518 C C   . ARG A 222 ? 0.6058 0.7490 0.4859 0.1533  -0.0466 0.1271  225 ARG A C   
3519 O O   . ARG A 222 ? 0.5373 0.7218 0.4292 0.1844  -0.0536 0.1534  225 ARG A O   
3520 C CB  . ARG A 222 ? 0.5199 0.6779 0.4016 0.2088  -0.0037 0.1386  225 ARG A CB  
3521 C CG  . ARG A 222 ? 0.9252 1.0202 0.7609 0.2402  0.0351  0.1324  225 ARG A CG  
3522 C CD  . ARG A 222 ? 1.0800 1.2538 0.9544 0.2867  0.0494  0.1592  225 ARG A CD  
3523 N NE  . ARG A 222 ? 1.3716 1.5320 1.2313 0.3456  0.0683  0.1864  225 ARG A NE  
3524 C CZ  . ARG A 222 ? 1.3613 1.4281 1.1591 0.3844  0.1052  0.1822  225 ARG A CZ  
3525 N NH1 . ARG A 222 ? 1.3053 1.2794 1.0429 0.3697  0.1266  0.1510  225 ARG A NH1 
3526 N NH2 . ARG A 222 ? 1.4611 1.5249 1.2568 0.4382  0.1197  0.2112  225 ARG A NH2 
3540 N N   . SER A 223 ? 0.4268 0.5762 0.3253 0.1018  -0.0671 0.1064  226 SER A N   
3541 C CA  . SER A 223 ? 0.3844 0.5829 0.3110 0.0793  -0.0974 0.1090  226 SER A CA  
3542 C C   . SER A 223 ? 0.6706 0.7966 0.5452 0.0755  -0.0936 0.1038  226 SER A C   
3543 O O   . SER A 223 ? 0.5929 0.6297 0.4196 0.0719  -0.0729 0.0914  226 SER A O   
3544 C CB  . SER A 223 ? 0.4526 0.6901 0.4259 0.0279  -0.1189 0.0891  226 SER A CB  
3545 O OG  . SER A 223 ? 0.5909 0.8161 0.5615 -0.0016 -0.1350 0.0766  226 SER A OG  
3551 N N   . ARG A 224 ? 0.4695 0.6350 0.3520 0.0744  -0.1150 0.1149  227 ARG A N   
3552 C CA  . ARG A 224 ? 0.6686 0.7774 0.5051 0.0660  -0.1141 0.1106  227 ARG A CA  
3553 C C   . ARG A 224 ? 0.5946 0.6863 0.4369 0.0158  -0.1235 0.0831  227 ARG A C   
3554 O O   . ARG A 224 ? 0.4562 0.5029 0.2621 0.0053  -0.1209 0.0781  227 ARG A O   
3555 C CB  . ARG A 224 ? 0.5837 0.7403 0.4192 0.0859  -0.1327 0.1357  227 ARG A CB  
3556 C CG  . ARG A 224 ? 0.9003 1.0207 0.6976 0.1331  -0.1153 0.1623  227 ARG A CG  
3557 C CD  . ARG A 224 ? 0.8028 0.8535 0.5439 0.1275  -0.1093 0.1604  227 ARG A CD  
3558 N NE  . ARG A 224 ? 1.4341 1.4739 1.1509 0.1696  -0.1029 0.1923  227 ARG A NE  
3559 C CZ  . ARG A 224 ? 1.5670 1.5317 1.2446 0.1998  -0.0768 0.2007  227 ARG A CZ  
3560 N NH1 . ARG A 224 ? 1.0980 0.9857 0.7506 0.1891  -0.0550 0.1780  227 ARG A NH1 
3561 N NH2 . ARG A 224 ? 1.3670 1.3327 1.0436 0.2301  -0.0718 0.2256  227 ARG A NH2 
3575 N N   . ALA A 225 ? 0.5536 0.6812 0.4429 -0.0144 -0.1329 0.0673  228 ALA A N   
3576 C CA  . ALA A 225 ? 0.5512 0.6642 0.4552 -0.0600 -0.1393 0.0429  228 ALA A CA  
3577 C C   . ALA A 225 ? 0.4245 0.4490 0.2929 -0.0759 -0.1169 0.0305  228 ALA A C   
3578 O O   . ALA A 225 ? 0.5855 0.5856 0.4548 -0.1077 -0.1175 0.0159  228 ALA A O   
3579 C CB  . ALA A 225 ? 0.3877 0.5327 0.3634 -0.0686 -0.1294 0.0249  228 ALA A CB  
3585 N N   . ILE A 226 ? 0.4419 0.4161 0.2791 -0.0544 -0.0963 0.0365  229 ILE A N   
3586 C CA  . ILE A 226 ? 0.6062 0.4933 0.4088 -0.0729 -0.0780 0.0267  229 ILE A CA  
3587 C C   . ILE A 226 ? 0.6031 0.4262 0.3522 -0.0634 -0.0675 0.0334  229 ILE A C   
3588 O O   . ILE A 226 ? 0.6030 0.3592 0.3286 -0.0857 -0.0565 0.0272  229 ILE A O   
3589 C CB  . ILE A 226 ? 0.6690 0.5170 0.4498 -0.0567 -0.0609 0.0283  229 ILE A CB  
3590 C CG1 . ILE A 226 ? 0.6009 0.4291 0.3413 -0.0038 -0.0473 0.0465  229 ILE A CG1 
3591 C CG2 . ILE A 226 ? 0.4454 0.3596 0.2785 -0.0684 -0.0704 0.0232  229 ILE A CG2 
3592 C CD1 . ILE A 226 ? 0.6841 0.4636 0.3936 0.0168  -0.0262 0.0457  229 ILE A CD1 
3604 N N   . PHE A 227 ? 0.5801 0.4243 0.3112 -0.0326 -0.0719 0.0490  230 PHE A N   
3605 C CA  . PHE A 227 ? 0.5807 0.3717 0.2620 -0.0228 -0.0636 0.0587  230 PHE A CA  
3606 C C   . PHE A 227 ? 0.5991 0.4194 0.2891 -0.0474 -0.0763 0.0518  230 PHE A C   
3607 O O   . PHE A 227 ? 0.5388 0.4295 0.2666 -0.0573 -0.0954 0.0456  230 PHE A O   
3608 C CB  . PHE A 227 ? 0.6354 0.4294 0.2895 0.0253  -0.0605 0.0833  230 PHE A CB  
3609 C CG  . PHE A 227 ? 0.6462 0.3963 0.2809 0.0553  -0.0420 0.0899  230 PHE A CG  
3610 C CD1 . PHE A 227 ? 0.7562 0.5575 0.4238 0.0742  -0.0430 0.0925  230 PHE A CD1 
3611 C CD2 . PHE A 227 ? 0.8116 0.4672 0.3934 0.0647  -0.0229 0.0938  230 PHE A CD2 
3612 C CE1 . PHE A 227 ? 0.7370 0.4939 0.3812 0.1039  -0.0219 0.0964  230 PHE A CE1 
3613 C CE2 . PHE A 227 ? 0.8253 0.4314 0.3823 0.0926  -0.0046 0.0969  230 PHE A CE2 
3614 C CZ  . PHE A 227 ? 0.7912 0.4470 0.3776 0.1133  -0.0025 0.0970  230 PHE A CZ  
3624 N N   . GLY A 228 ? 0.7886 0.5519 0.4411 -0.0574 -0.0650 0.0531  231 GLY A N   
3625 C CA  . GLY A 228 ? 0.7254 0.5084 0.3753 -0.0767 -0.0717 0.0467  231 GLY A CA  
3626 C C   . GLY A 228 ? 0.8510 0.6734 0.4789 -0.0518 -0.0850 0.0621  231 GLY A C   
3627 O O   . GLY A 228 ? 0.8372 0.6513 0.4412 -0.0173 -0.0833 0.0839  231 GLY A O   
3631 N N   . GLU A 229 ? 0.7506 0.6150 0.3863 -0.0705 -0.0988 0.0513  232 GLU A N   
3632 C CA  . GLU A 229 ? 0.9031 0.8066 0.5142 -0.0548 -0.1157 0.0653  232 GLU A CA  
3633 C C   . GLU A 229 ? 1.0152 0.8671 0.5670 -0.0432 -0.1019 0.0817  232 GLU A C   
3634 O O   . GLU A 229 ? 1.1894 1.0177 0.7211 -0.0635 -0.0918 0.0710  232 GLU A O   
3635 C CB  . GLU A 229 ? 0.9595 0.9138 0.6007 -0.0785 -0.1292 0.0434  232 GLU A CB  
3636 C CG  . GLU A 229 ? 0.8875 0.9111 0.5567 -0.0611 -0.1508 0.0505  232 GLU A CG  
3637 C CD  . GLU A 229 ? 0.8210 0.8700 0.5063 -0.0784 -0.1583 0.0295  232 GLU A CD  
3638 O OE1 . GLU A 229 ? 0.8440 0.8734 0.5436 -0.1030 -0.1466 0.0068  232 GLU A OE1 
3639 O OE2 . GLU A 229 ? 0.6929 0.7753 0.3757 -0.0661 -0.1748 0.0373  232 GLU A OE2 
3646 N N   . ALA A 230 ? 0.7292 0.5655 0.2588 -0.0087 -0.0991 0.1087  233 ALA A N   
3647 C CA  . ALA A 230 ? 1.0862 0.8794 0.5757 0.0050  -0.0848 0.1268  233 ALA A CA  
3648 C C   . ALA A 230 ? 1.1084 0.9454 0.5927 0.0340  -0.0982 0.1548  233 ALA A C   
3649 O O   . ALA A 230 ? 1.0170 0.9050 0.5283 0.0503  -0.1142 0.1652  233 ALA A O   
3650 C CB  . ALA A 230 ? 1.3371 1.0565 0.8166 0.0157  -0.0627 0.1328  233 ALA A CB  
3656 N N   . GLU A 231 ? 1.1303 0.9513 0.5851 0.0378  -0.0918 0.1698  234 GLU A N   
3657 C CA  . GLU A 231 ? 1.3006 1.1606 0.7507 0.0577  -0.1054 0.2005  234 GLU A CA  
3658 C C   . GLU A 231 ? 1.4453 1.2687 0.8996 0.0902  -0.0963 0.2247  234 GLU A C   
3659 O O   . GLU A 231 ? 1.5295 1.3244 0.9639 0.0999  -0.0895 0.2440  234 GLU A O   
3660 C CB  . GLU A 231 ? 0.9772 0.8385 0.3932 0.0458  -0.1034 0.2061  234 GLU A CB  
3661 C CG  . GLU A 231 ? 1.0616 0.9801 0.4736 0.0521  -0.1251 0.2346  234 GLU A CG  
3662 C CD  . GLU A 231 ? 1.0288 1.0143 0.4663 0.0588  -0.1423 0.2184  234 GLU A CD  
3663 O OE1 . GLU A 231 ? 0.9061 0.8837 0.3358 0.0426  -0.1452 0.1837  234 GLU A OE1 
3664 O OE2 . GLU A 231 ? 1.0128 0.9547 0.4239 0.0628  -0.1758 0.2290  234 GLU A OE2 
4118 C C1  . RET S .   ? 0.2696 0.2636 0.3094 -0.0162 -0.0278 0.0281  318 RET A C1  
4119 C C2  . RET S .   ? 0.2710 0.2592 0.3060 -0.0139 -0.0251 0.0330  318 RET A C2  
4120 C C3  . RET S .   ? 0.2699 0.2450 0.3014 -0.0182 -0.0229 0.0342  318 RET A C3  
4121 C C4  . RET S .   ? 0.2344 0.1960 0.2609 -0.0176 -0.0235 0.0311  318 RET A C4  
4122 C C5  . RET S .   ? 0.2970 0.2653 0.3267 -0.0174 -0.0264 0.0261  318 RET A C5  
4123 C C6  . RET S .   ? 0.1953 0.1785 0.2321 -0.0182 -0.0283 0.0250  318 RET A C6  
4124 C C7  . RET S .   ? 0.2037 0.1913 0.2433 -0.0205 -0.0314 0.0207  318 RET A C7  
4125 C C8  . RET S .   ? 0.2053 0.2037 0.2499 -0.0205 -0.0339 0.0194  318 RET A C8  
4126 C C9  . RET S .   ? 0.1817 0.1823 0.2272 -0.0223 -0.0373 0.0161  318 RET A C9  
4127 C C10 . RET S .   ? 0.1554 0.1650 0.2050 -0.0216 -0.0397 0.0158  318 RET A C10 
4128 C C11 . RET S .   ? 0.2076 0.2203 0.2583 -0.0228 -0.0436 0.0137  318 RET A C11 
4129 C C12 . RET S .   ? 0.2008 0.2195 0.2543 -0.0212 -0.0459 0.0139  318 RET A C12 
4130 C C13 . RET S .   ? 0.3559 0.3784 0.4115 -0.0219 -0.0503 0.0127  318 RET A C13 
4131 C C14 . RET S .   ? 0.4674 0.4935 0.5252 -0.0189 -0.0521 0.0135  318 RET A C14 
4132 C C15 . RET S .   ? 0.3325 0.3553 0.3862 -0.0163 -0.0520 0.0149  318 RET A C15 
4133 C C16 . RET S .   ? 0.2474 0.2498 0.2931 -0.0206 -0.0279 0.0269  318 RET A C16 
4134 C C17 . RET S .   ? 0.1837 0.1856 0.2241 -0.0119 -0.0298 0.0280  318 RET A C17 
4135 C C18 . RET S .   ? 0.2671 0.2214 0.2891 -0.0164 -0.0268 0.0225  318 RET A C18 
4136 C C19 . RET S .   ? 0.1877 0.1788 0.2281 -0.0254 -0.0386 0.0130  318 RET A C19 
4137 C C20 . RET S .   ? 0.4548 0.4773 0.5111 -0.0261 -0.0528 0.0106  318 RET A C20 
# 
