data_9CD1
# 
_entry.id   9CD1 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_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   9CD1         pdb_00009cd1 10.2210/pdb9cd1/pdb 
WWPDB D_1000285074 ?            ?                   
# 
_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       2025-02-12 
# 
_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                        9CD1 
_pdbx_database_status.recvd_initial_deposition_date   2024-06-23 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_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           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              peizhou@biochem.duke.edu 
_pdbx_contact_author.name_first         Pei 
_pdbx_contact_author.name_last          Zhou 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-7823-3416 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Cochrane, C.S.' 1 ? 
'Zhou, P.'       2 ? 
# 
_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                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Jacs Au' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2691-3704 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            4 
_citation.language                  ? 
_citation.page_first                4383 
_citation.page_last                 4393 
_citation.title                     
'Design and Evaluation of Pyridinyl Sulfonyl Piperazine LpxH Inhibitors with Potent Antibiotic Activity Against Enterobacterales.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/jacsau.4c00731 
_citation.pdbx_database_id_PubMed   39610720 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Ennis, A.F.'    1  ?                   
primary 'Cochrane, C.S.' 2  ?                   
primary 'Dome, P.A.'     3  ?                   
primary 'Jeong, P.'      4  ?                   
primary 'Yu, J.'         5  0000-0001-8487-5565 
primary 'Lee, H.'        6  ?                   
primary 'Williams, C.S.' 7  ?                   
primary 'Ha, Y.'         8  0000-0001-5684-8420 
primary 'Yang, W.'       9  0000-0001-5576-2828 
primary 'Zhou, P.'       10 0000-0002-7823-3416 
primary 'Hong, J.'       11 0000-0002-5253-0949 
# 
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 'UDP-2,3-diacylglucosamine hydrolase' 29627.680 1   3.6.1.54 ? ? ? 
2 non-polymer syn 
'N-(4-{4-[6-chloro-4-(trifluoromethyl)pyridin-2-yl]piperazine-1-sulfonyl}phenyl)-2-[(methanesulfonyl)(methyl)amino]benzamide' 
632.075   1   ?        ? ? ? 
3 non-polymer syn 'MANGANESE (II) ION' 54.938    2   ?        ? ? ? 
4 water       nat water 18.015    129 ?        ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'UDP-2,3-diacylglucosamine diphosphatase' 
# 
_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       
;MATLFIADLHLQTEEPAITAGFLRFLQGEARQADALYILGDLFEAWIGDDDPNPLHQQIASAIKAVVDAGVPCYFIHGNR
DFLVGQRFARQSGMILLAEEERLDLYGREVLIMHGDTLCTDDQGYLAFRAKVHTPWIQRLFLALPLFIRHRIAARMRADS
KAANSSKSMEIMDVNPQAVVDAMERHHVQWLIHGHTHRPAVHELQANGQPAWRVVLGAWHSEGSMVKVTPDDVELIHFPF
LEENLYFQSHHHHHHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MATLFIADLHLQTEEPAITAGFLRFLQGEARQADALYILGDLFEAWIGDDDPNPLHQQIASAIKAVVDAGVPCYFIHGNR
DFLVGQRFARQSGMILLAEEERLDLYGREVLIMHGDTLCTDDQGYLAFRAKVHTPWIQRLFLALPLFIRHRIAARMRADS
KAANSSKSMEIMDVNPQAVVDAMERHHVQWLIHGHTHRPAVHELQANGQPAWRVVLGAWHSEGSMVKVTPDDVELIHFPF
LEENLYFQSHHHHHHHHHH
;
_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 'N-(4-{4-[6-chloro-4-(trifluoromethyl)pyridin-2-yl]piperazine-1-sulfonyl}phenyl)-2-[(methanesulfonyl)(methyl)amino]benzamide' 
A1AVW 
3 'MANGANESE (II) ION'                                                                                                          MN 
4 water                                                                                                                         
HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   ALA n 
1 3   THR n 
1 4   LEU n 
1 5   PHE n 
1 6   ILE n 
1 7   ALA n 
1 8   ASP n 
1 9   LEU n 
1 10  HIS n 
1 11  LEU n 
1 12  GLN n 
1 13  THR n 
1 14  GLU n 
1 15  GLU n 
1 16  PRO n 
1 17  ALA n 
1 18  ILE n 
1 19  THR n 
1 20  ALA n 
1 21  GLY n 
1 22  PHE n 
1 23  LEU n 
1 24  ARG n 
1 25  PHE n 
1 26  LEU n 
1 27  GLN n 
1 28  GLY n 
1 29  GLU n 
1 30  ALA n 
1 31  ARG n 
1 32  GLN n 
1 33  ALA n 
1 34  ASP n 
1 35  ALA n 
1 36  LEU n 
1 37  TYR n 
1 38  ILE n 
1 39  LEU n 
1 40  GLY n 
1 41  ASP n 
1 42  LEU n 
1 43  PHE n 
1 44  GLU n 
1 45  ALA n 
1 46  TRP n 
1 47  ILE n 
1 48  GLY n 
1 49  ASP n 
1 50  ASP n 
1 51  ASP n 
1 52  PRO n 
1 53  ASN n 
1 54  PRO n 
1 55  LEU n 
1 56  HIS n 
1 57  GLN n 
1 58  GLN n 
1 59  ILE n 
1 60  ALA n 
1 61  SER n 
1 62  ALA n 
1 63  ILE n 
1 64  LYS n 
1 65  ALA n 
1 66  VAL n 
1 67  VAL n 
1 68  ASP n 
1 69  ALA n 
1 70  GLY n 
1 71  VAL n 
1 72  PRO n 
1 73  CYS n 
1 74  TYR n 
1 75  PHE n 
1 76  ILE n 
1 77  HIS n 
1 78  GLY n 
1 79  ASN n 
1 80  ARG n 
1 81  ASP n 
1 82  PHE n 
1 83  LEU n 
1 84  VAL n 
1 85  GLY n 
1 86  GLN n 
1 87  ARG n 
1 88  PHE n 
1 89  ALA n 
1 90  ARG n 
1 91  GLN n 
1 92  SER n 
1 93  GLY n 
1 94  MET n 
1 95  ILE n 
1 96  LEU n 
1 97  LEU n 
1 98  ALA n 
1 99  GLU n 
1 100 GLU n 
1 101 GLU n 
1 102 ARG n 
1 103 LEU n 
1 104 ASP n 
1 105 LEU n 
1 106 TYR n 
1 107 GLY n 
1 108 ARG n 
1 109 GLU n 
1 110 VAL n 
1 111 LEU n 
1 112 ILE n 
1 113 MET n 
1 114 HIS n 
1 115 GLY n 
1 116 ASP n 
1 117 THR n 
1 118 LEU n 
1 119 CYS n 
1 120 THR n 
1 121 ASP n 
1 122 ASP n 
1 123 GLN n 
1 124 GLY n 
1 125 TYR n 
1 126 LEU n 
1 127 ALA n 
1 128 PHE n 
1 129 ARG n 
1 130 ALA n 
1 131 LYS n 
1 132 VAL n 
1 133 HIS n 
1 134 THR n 
1 135 PRO n 
1 136 TRP n 
1 137 ILE n 
1 138 GLN n 
1 139 ARG n 
1 140 LEU n 
1 141 PHE n 
1 142 LEU n 
1 143 ALA n 
1 144 LEU n 
1 145 PRO n 
1 146 LEU n 
1 147 PHE n 
1 148 ILE n 
1 149 ARG n 
1 150 HIS n 
1 151 ARG n 
1 152 ILE n 
1 153 ALA n 
1 154 ALA n 
1 155 ARG n 
1 156 MET n 
1 157 ARG n 
1 158 ALA n 
1 159 ASP n 
1 160 SER n 
1 161 LYS n 
1 162 ALA n 
1 163 ALA n 
1 164 ASN n 
1 165 SER n 
1 166 SER n 
1 167 LYS n 
1 168 SER n 
1 169 MET n 
1 170 GLU n 
1 171 ILE n 
1 172 MET n 
1 173 ASP n 
1 174 VAL n 
1 175 ASN n 
1 176 PRO n 
1 177 GLN n 
1 178 ALA n 
1 179 VAL n 
1 180 VAL n 
1 181 ASP n 
1 182 ALA n 
1 183 MET n 
1 184 GLU n 
1 185 ARG n 
1 186 HIS n 
1 187 HIS n 
1 188 VAL n 
1 189 GLN n 
1 190 TRP n 
1 191 LEU n 
1 192 ILE n 
1 193 HIS n 
1 194 GLY n 
1 195 HIS n 
1 196 THR n 
1 197 HIS n 
1 198 ARG n 
1 199 PRO n 
1 200 ALA n 
1 201 VAL n 
1 202 HIS n 
1 203 GLU n 
1 204 LEU n 
1 205 GLN n 
1 206 ALA n 
1 207 ASN n 
1 208 GLY n 
1 209 GLN n 
1 210 PRO n 
1 211 ALA n 
1 212 TRP n 
1 213 ARG n 
1 214 VAL n 
1 215 VAL n 
1 216 LEU n 
1 217 GLY n 
1 218 ALA n 
1 219 TRP n 
1 220 HIS n 
1 221 SER n 
1 222 GLU n 
1 223 GLY n 
1 224 SER n 
1 225 MET n 
1 226 VAL n 
1 227 LYS n 
1 228 VAL n 
1 229 THR n 
1 230 PRO n 
1 231 ASP n 
1 232 ASP n 
1 233 VAL n 
1 234 GLU n 
1 235 LEU n 
1 236 ILE n 
1 237 HIS n 
1 238 PHE n 
1 239 PRO n 
1 240 PHE n 
1 241 LEU n 
1 242 GLU n 
1 243 GLU n 
1 244 ASN n 
1 245 LEU n 
1 246 TYR n 
1 247 PHE n 
1 248 GLN n 
1 249 SER n 
1 250 HIS n 
1 251 HIS n 
1 252 HIS n 
1 253 HIS n 
1 254 HIS n 
1 255 HIS n 
1 256 HIS n 
1 257 HIS n 
1 258 HIS n 
1 259 HIS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   259 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'lpxH_1, lpxH, C3483_19950, NCTC9128_00880, SAMEA104305404_03891' 
_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      'Klebsiella pneumoniae' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     573 
_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      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_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                   ? 
# 
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 
A1AVW non-polymer         . 
'N-(4-{4-[6-chloro-4-(trifluoromethyl)pyridin-2-yl]piperazine-1-sulfonyl}phenyl)-2-[(methanesulfonyl)(methyl)amino]benzamide' ? 
'C25 H25 Cl F3 N5 O5 S2' 632.075 
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 
CYS   'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S'           121.158 
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  
HIS   'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1'         156.162 
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 
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 
MN    non-polymer         . 'MANGANESE (II) ION' ? 'Mn 2'                   54.938  
PHE   'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2'            165.189 
PRO   'L-peptide linking' y PROLINE ? 'C5 H9 N O2'             115.130 
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   MET 1   1   ?   ?   ?   A . n 
A 1 2   ALA 2   2   2   ALA ALA A . n 
A 1 3   THR 3   3   3   THR THR A . n 
A 1 4   LEU 4   4   4   LEU LEU A . n 
A 1 5   PHE 5   5   5   PHE PHE A . n 
A 1 6   ILE 6   6   6   ILE ILE A . n 
A 1 7   ALA 7   7   7   ALA ALA A . n 
A 1 8   ASP 8   8   8   ASP ASP A . n 
A 1 9   LEU 9   9   9   LEU LEU A . n 
A 1 10  HIS 10  10  10  HIS HIS A . n 
A 1 11  LEU 11  11  11  LEU LEU A . n 
A 1 12  GLN 12  12  12  GLN GLN A . n 
A 1 13  THR 13  13  13  THR THR A . n 
A 1 14  GLU 14  14  14  GLU GLU A . n 
A 1 15  GLU 15  15  15  GLU GLU A . n 
A 1 16  PRO 16  16  16  PRO PRO A . n 
A 1 17  ALA 17  17  17  ALA ALA A . n 
A 1 18  ILE 18  18  18  ILE ILE A . n 
A 1 19  THR 19  19  19  THR THR A . n 
A 1 20  ALA 20  20  20  ALA ALA A . n 
A 1 21  GLY 21  21  21  GLY GLY A . n 
A 1 22  PHE 22  22  22  PHE PHE A . n 
A 1 23  LEU 23  23  23  LEU LEU A . n 
A 1 24  ARG 24  24  24  ARG ARG A . n 
A 1 25  PHE 25  25  25  PHE PHE A . n 
A 1 26  LEU 26  26  26  LEU LEU A . n 
A 1 27  GLN 27  27  27  GLN GLN A . n 
A 1 28  GLY 28  28  28  GLY GLY A . n 
A 1 29  GLU 29  29  29  GLU GLU A . n 
A 1 30  ALA 30  30  30  ALA ALA A . n 
A 1 31  ARG 31  31  31  ARG ARG A . n 
A 1 32  GLN 32  32  32  GLN GLN A . n 
A 1 33  ALA 33  33  33  ALA ALA A . n 
A 1 34  ASP 34  34  34  ASP ASP A . n 
A 1 35  ALA 35  35  35  ALA ALA A . n 
A 1 36  LEU 36  36  36  LEU LEU A . n 
A 1 37  TYR 37  37  37  TYR TYR A . n 
A 1 38  ILE 38  38  38  ILE ILE A . n 
A 1 39  LEU 39  39  39  LEU LEU A . n 
A 1 40  GLY 40  40  40  GLY GLY A . n 
A 1 41  ASP 41  41  41  ASP ASP A . n 
A 1 42  LEU 42  42  42  LEU LEU A . n 
A 1 43  PHE 43  43  43  PHE PHE A . n 
A 1 44  GLU 44  44  44  GLU GLU A . n 
A 1 45  ALA 45  45  45  ALA ALA A . n 
A 1 46  TRP 46  46  46  TRP TRP A . n 
A 1 47  ILE 47  47  47  ILE ILE A . n 
A 1 48  GLY 48  48  48  GLY GLY A . n 
A 1 49  ASP 49  49  49  ASP ASP A . n 
A 1 50  ASP 50  50  50  ASP ASP A . n 
A 1 51  ASP 51  51  51  ASP ASP A . n 
A 1 52  PRO 52  52  52  PRO PRO A . n 
A 1 53  ASN 53  53  53  ASN ASN A . n 
A 1 54  PRO 54  54  54  PRO PRO A . n 
A 1 55  LEU 55  55  55  LEU LEU A . n 
A 1 56  HIS 56  56  56  HIS HIS A . n 
A 1 57  GLN 57  57  57  GLN GLN A . n 
A 1 58  GLN 58  58  58  GLN GLN A . n 
A 1 59  ILE 59  59  59  ILE ILE A . n 
A 1 60  ALA 60  60  60  ALA ALA A . n 
A 1 61  SER 61  61  61  SER SER A . n 
A 1 62  ALA 62  62  62  ALA ALA A . n 
A 1 63  ILE 63  63  63  ILE ILE A . n 
A 1 64  LYS 64  64  64  LYS LYS A . n 
A 1 65  ALA 65  65  65  ALA ALA A . n 
A 1 66  VAL 66  66  66  VAL VAL A . n 
A 1 67  VAL 67  67  67  VAL VAL A . n 
A 1 68  ASP 68  68  68  ASP ASP A . n 
A 1 69  ALA 69  69  69  ALA ALA A . n 
A 1 70  GLY 70  70  70  GLY GLY A . n 
A 1 71  VAL 71  71  71  VAL VAL A . n 
A 1 72  PRO 72  72  72  PRO PRO A . n 
A 1 73  CYS 73  73  73  CYS CYS A . n 
A 1 74  TYR 74  74  74  TYR TYR A . n 
A 1 75  PHE 75  75  75  PHE PHE A . n 
A 1 76  ILE 76  76  76  ILE ILE A . n 
A 1 77  HIS 77  77  77  HIS HIS A . n 
A 1 78  GLY 78  78  78  GLY GLY A . n 
A 1 79  ASN 79  79  79  ASN ASN A . n 
A 1 80  ARG 80  80  80  ARG ARG A . n 
A 1 81  ASP 81  81  81  ASP ASP A . n 
A 1 82  PHE 82  82  82  PHE PHE A . n 
A 1 83  LEU 83  83  83  LEU LEU A . n 
A 1 84  VAL 84  84  84  VAL VAL A . n 
A 1 85  GLY 85  85  85  GLY GLY A . n 
A 1 86  GLN 86  86  86  GLN GLN A . n 
A 1 87  ARG 87  87  87  ARG ARG A . n 
A 1 88  PHE 88  88  88  PHE PHE A . n 
A 1 89  ALA 89  89  89  ALA ALA A . n 
A 1 90  ARG 90  90  90  ARG ARG A . n 
A 1 91  GLN 91  91  91  GLN GLN A . n 
A 1 92  SER 92  92  92  SER SER A . n 
A 1 93  GLY 93  93  93  GLY GLY A . n 
A 1 94  MET 94  94  94  MET MET A . n 
A 1 95  ILE 95  95  95  ILE ILE A . n 
A 1 96  LEU 96  96  96  LEU LEU A . n 
A 1 97  LEU 97  97  97  LEU LEU A . n 
A 1 98  ALA 98  98  98  ALA ALA A . n 
A 1 99  GLU 99  99  99  GLU GLU A . n 
A 1 100 GLU 100 100 100 GLU GLU A . n 
A 1 101 GLU 101 101 101 GLU GLU A . n 
A 1 102 ARG 102 102 102 ARG ARG A . n 
A 1 103 LEU 103 103 103 LEU LEU A . n 
A 1 104 ASP 104 104 104 ASP ASP A . n 
A 1 105 LEU 105 105 105 LEU LEU A . n 
A 1 106 TYR 106 106 106 TYR TYR A . n 
A 1 107 GLY 107 107 107 GLY GLY A . n 
A 1 108 ARG 108 108 108 ARG ARG A . n 
A 1 109 GLU 109 109 109 GLU GLU A . n 
A 1 110 VAL 110 110 110 VAL VAL A . n 
A 1 111 LEU 111 111 111 LEU LEU A . n 
A 1 112 ILE 112 112 112 ILE ILE A . n 
A 1 113 MET 113 113 113 MET MET A . n 
A 1 114 HIS 114 114 114 HIS HIS A . n 
A 1 115 GLY 115 115 115 GLY GLY A . n 
A 1 116 ASP 116 116 116 ASP ASP A . n 
A 1 117 THR 117 117 117 THR THR A . n 
A 1 118 LEU 118 118 118 LEU LEU A . n 
A 1 119 CYS 119 119 119 CYS CYS A . n 
A 1 120 THR 120 120 120 THR THR A . n 
A 1 121 ASP 121 121 121 ASP ASP A . n 
A 1 122 ASP 122 122 122 ASP ASP A . n 
A 1 123 GLN 123 123 123 GLN GLN A . n 
A 1 124 GLY 124 124 124 GLY GLY A . n 
A 1 125 TYR 125 125 125 TYR TYR A . n 
A 1 126 LEU 126 126 126 LEU LEU A . n 
A 1 127 ALA 127 127 127 ALA ALA A . n 
A 1 128 PHE 128 128 128 PHE PHE A . n 
A 1 129 ARG 129 129 129 ARG ARG A . n 
A 1 130 ALA 130 130 130 ALA ALA A . n 
A 1 131 LYS 131 131 131 LYS LYS A . n 
A 1 132 VAL 132 132 132 VAL VAL A . n 
A 1 133 HIS 133 133 133 HIS HIS A . n 
A 1 134 THR 134 134 134 THR THR A . n 
A 1 135 PRO 135 135 135 PRO PRO A . n 
A 1 136 TRP 136 136 136 TRP TRP A . n 
A 1 137 ILE 137 137 137 ILE ILE A . n 
A 1 138 GLN 138 138 138 GLN GLN A . n 
A 1 139 ARG 139 139 139 ARG ARG A . n 
A 1 140 LEU 140 140 140 LEU LEU A . n 
A 1 141 PHE 141 141 141 PHE PHE A . n 
A 1 142 LEU 142 142 142 LEU LEU A . n 
A 1 143 ALA 143 143 143 ALA ALA A . n 
A 1 144 LEU 144 144 144 LEU LEU A . n 
A 1 145 PRO 145 145 145 PRO PRO A . n 
A 1 146 LEU 146 146 146 LEU LEU A . n 
A 1 147 PHE 147 147 147 PHE PHE A . n 
A 1 148 ILE 148 148 148 ILE ILE A . n 
A 1 149 ARG 149 149 149 ARG ARG A . n 
A 1 150 HIS 150 150 150 HIS HIS A . n 
A 1 151 ARG 151 151 151 ARG ARG A . n 
A 1 152 ILE 152 152 152 ILE ILE A . n 
A 1 153 ALA 153 153 153 ALA ALA A . n 
A 1 154 ALA 154 154 154 ALA ALA A . n 
A 1 155 ARG 155 155 155 ARG ARG A . n 
A 1 156 MET 156 156 156 MET MET A . n 
A 1 157 ARG 157 157 157 ARG ARG A . n 
A 1 158 ALA 158 158 158 ALA ALA A . n 
A 1 159 ASP 159 159 159 ASP ASP A . n 
A 1 160 SER 160 160 160 SER SER A . n 
A 1 161 LYS 161 161 ?   ?   ?   A . n 
A 1 162 ALA 162 162 ?   ?   ?   A . n 
A 1 163 ALA 163 163 ?   ?   ?   A . n 
A 1 164 ASN 164 164 ?   ?   ?   A . n 
A 1 165 SER 165 165 ?   ?   ?   A . n 
A 1 166 SER 166 166 ?   ?   ?   A . n 
A 1 167 LYS 167 167 ?   ?   ?   A . n 
A 1 168 SER 168 168 ?   ?   ?   A . n 
A 1 169 MET 169 169 ?   ?   ?   A . n 
A 1 170 GLU 170 170 ?   ?   ?   A . n 
A 1 171 ILE 171 171 171 ILE ILE A . n 
A 1 172 MET 172 172 172 MET MET A . n 
A 1 173 ASP 173 173 173 ASP ASP A . n 
A 1 174 VAL 174 174 174 VAL VAL A . n 
A 1 175 ASN 175 175 175 ASN ASN A . n 
A 1 176 PRO 176 176 176 PRO PRO A . n 
A 1 177 GLN 177 177 177 GLN GLN A . n 
A 1 178 ALA 178 178 178 ALA ALA A . n 
A 1 179 VAL 179 179 179 VAL VAL A . n 
A 1 180 VAL 180 180 180 VAL VAL A . n 
A 1 181 ASP 181 181 181 ASP ASP A . n 
A 1 182 ALA 182 182 182 ALA ALA A . n 
A 1 183 MET 183 183 183 MET MET A . n 
A 1 184 GLU 184 184 184 GLU GLU A . n 
A 1 185 ARG 185 185 185 ARG ARG A . n 
A 1 186 HIS 186 186 186 HIS HIS A . n 
A 1 187 HIS 187 187 187 HIS HIS A . n 
A 1 188 VAL 188 188 188 VAL VAL A . n 
A 1 189 GLN 189 189 189 GLN GLN A . n 
A 1 190 TRP 190 190 190 TRP TRP A . n 
A 1 191 LEU 191 191 191 LEU LEU A . n 
A 1 192 ILE 192 192 192 ILE ILE A . n 
A 1 193 HIS 193 193 193 HIS HIS A . n 
A 1 194 GLY 194 194 194 GLY GLY A . n 
A 1 195 HIS 195 195 195 HIS HIS A . n 
A 1 196 THR 196 196 196 THR THR A . n 
A 1 197 HIS 197 197 197 HIS HIS A . n 
A 1 198 ARG 198 198 198 ARG ARG A . n 
A 1 199 PRO 199 199 199 PRO PRO A . n 
A 1 200 ALA 200 200 200 ALA ALA A . n 
A 1 201 VAL 201 201 201 VAL VAL A . n 
A 1 202 HIS 202 202 202 HIS HIS A . n 
A 1 203 GLU 203 203 203 GLU GLU A . n 
A 1 204 LEU 204 204 204 LEU LEU A . n 
A 1 205 GLN 205 205 205 GLN GLN A . n 
A 1 206 ALA 206 206 206 ALA ALA A . n 
A 1 207 ASN 207 207 207 ASN ASN A . n 
A 1 208 GLY 208 208 208 GLY GLY A . n 
A 1 209 GLN 209 209 209 GLN GLN A . n 
A 1 210 PRO 210 210 210 PRO PRO A . n 
A 1 211 ALA 211 211 211 ALA ALA A . n 
A 1 212 TRP 212 212 212 TRP TRP A . n 
A 1 213 ARG 213 213 213 ARG ARG A . n 
A 1 214 VAL 214 214 214 VAL VAL A . n 
A 1 215 VAL 215 215 215 VAL VAL A . n 
A 1 216 LEU 216 216 216 LEU LEU A . n 
A 1 217 GLY 217 217 217 GLY GLY A . n 
A 1 218 ALA 218 218 218 ALA ALA A . n 
A 1 219 TRP 219 219 219 TRP TRP A . n 
A 1 220 HIS 220 220 220 HIS HIS A . n 
A 1 221 SER 221 221 221 SER SER A . n 
A 1 222 GLU 222 222 222 GLU GLU A . n 
A 1 223 GLY 223 223 223 GLY GLY A . n 
A 1 224 SER 224 224 224 SER SER A . n 
A 1 225 MET 225 225 225 MET MET A . n 
A 1 226 VAL 226 226 226 VAL VAL A . n 
A 1 227 LYS 227 227 227 LYS LYS A . n 
A 1 228 VAL 228 228 228 VAL VAL A . n 
A 1 229 THR 229 229 229 THR THR A . n 
A 1 230 PRO 230 230 230 PRO PRO A . n 
A 1 231 ASP 231 231 231 ASP ASP A . n 
A 1 232 ASP 232 232 232 ASP ASP A . n 
A 1 233 VAL 233 233 233 VAL VAL A . n 
A 1 234 GLU 234 234 234 GLU GLU A . n 
A 1 235 LEU 235 235 235 LEU LEU A . n 
A 1 236 ILE 236 236 236 ILE ILE A . n 
A 1 237 HIS 237 237 237 HIS HIS A . n 
A 1 238 PHE 238 238 238 PHE PHE A . n 
A 1 239 PRO 239 239 239 PRO PRO A . n 
A 1 240 PHE 240 240 240 PHE PHE A . n 
A 1 241 LEU 241 241 241 LEU LEU A . n 
A 1 242 GLU 242 242 242 GLU GLU A . n 
A 1 243 GLU 243 243 243 GLU GLU A . n 
A 1 244 ASN 244 244 244 ASN ASN A . n 
A 1 245 LEU 245 245 245 LEU LEU A . n 
A 1 246 TYR 246 246 246 TYR TYR A . n 
A 1 247 PHE 247 247 247 PHE PHE A . n 
A 1 248 GLN 248 248 ?   ?   ?   A . n 
A 1 249 SER 249 249 ?   ?   ?   A . n 
A 1 250 HIS 250 250 250 HIS HIS A . n 
A 1 251 HIS 251 251 251 HIS HIS A . n 
A 1 252 HIS 252 252 252 HIS HIS A . n 
A 1 253 HIS 253 253 ?   ?   ?   A . n 
A 1 254 HIS 254 254 ?   ?   ?   A . n 
A 1 255 HIS 255 255 ?   ?   ?   A . n 
A 1 256 HIS 256 256 ?   ?   ?   A . n 
A 1 257 HIS 257 257 ?   ?   ?   A . n 
A 1 258 HIS 258 258 ?   ?   ?   A . n 
A 1 259 HIS 259 259 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1AVW 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1AVW 
_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 A1AVW 1   301 301 A1AVW LIG A . 
C 3 MN    1   302 1   MN    MN  A . 
D 3 MN    1   303 2   MN    MN  A . 
E 4 HOH   1   401 100 HOH   HOH A . 
E 4 HOH   2   402 89  HOH   HOH A . 
E 4 HOH   3   403 28  HOH   HOH A . 
E 4 HOH   4   404 139 HOH   HOH A . 
E 4 HOH   5   405 38  HOH   HOH A . 
E 4 HOH   6   406 105 HOH   HOH A . 
E 4 HOH   7   407 78  HOH   HOH A . 
E 4 HOH   8   408 19  HOH   HOH A . 
E 4 HOH   9   409 14  HOH   HOH A . 
E 4 HOH   10  410 57  HOH   HOH A . 
E 4 HOH   11  411 47  HOH   HOH A . 
E 4 HOH   12  412 140 HOH   HOH A . 
E 4 HOH   13  413 143 HOH   HOH A . 
E 4 HOH   14  414 138 HOH   HOH A . 
E 4 HOH   15  415 44  HOH   HOH A . 
E 4 HOH   16  416 110 HOH   HOH A . 
E 4 HOH   17  417 51  HOH   HOH A . 
E 4 HOH   18  418 7   HOH   HOH A . 
E 4 HOH   19  419 17  HOH   HOH A . 
E 4 HOH   20  420 36  HOH   HOH A . 
E 4 HOH   21  421 11  HOH   HOH A . 
E 4 HOH   22  422 12  HOH   HOH A . 
E 4 HOH   23  423 85  HOH   HOH A . 
E 4 HOH   24  424 52  HOH   HOH A . 
E 4 HOH   25  425 56  HOH   HOH A . 
E 4 HOH   26  426 27  HOH   HOH A . 
E 4 HOH   27  427 20  HOH   HOH A . 
E 4 HOH   28  428 82  HOH   HOH A . 
E 4 HOH   29  429 43  HOH   HOH A . 
E 4 HOH   30  430 66  HOH   HOH A . 
E 4 HOH   31  431 33  HOH   HOH A . 
E 4 HOH   32  432 24  HOH   HOH A . 
E 4 HOH   33  433 8   HOH   HOH A . 
E 4 HOH   34  434 45  HOH   HOH A . 
E 4 HOH   35  435 23  HOH   HOH A . 
E 4 HOH   36  436 123 HOH   HOH A . 
E 4 HOH   37  437 40  HOH   HOH A . 
E 4 HOH   38  438 6   HOH   HOH A . 
E 4 HOH   39  439 72  HOH   HOH A . 
E 4 HOH   40  440 31  HOH   HOH A . 
E 4 HOH   41  441 76  HOH   HOH A . 
E 4 HOH   42  442 5   HOH   HOH A . 
E 4 HOH   43  443 41  HOH   HOH A . 
E 4 HOH   44  444 58  HOH   HOH A . 
E 4 HOH   45  445 29  HOH   HOH A . 
E 4 HOH   46  446 13  HOH   HOH A . 
E 4 HOH   47  447 90  HOH   HOH A . 
E 4 HOH   48  448 80  HOH   HOH A . 
E 4 HOH   49  449 9   HOH   HOH A . 
E 4 HOH   50  450 106 HOH   HOH A . 
E 4 HOH   51  451 34  HOH   HOH A . 
E 4 HOH   52  452 42  HOH   HOH A . 
E 4 HOH   53  453 73  HOH   HOH A . 
E 4 HOH   54  454 26  HOH   HOH A . 
E 4 HOH   55  455 69  HOH   HOH A . 
E 4 HOH   56  456 88  HOH   HOH A . 
E 4 HOH   57  457 2   HOH   HOH A . 
E 4 HOH   58  458 119 HOH   HOH A . 
E 4 HOH   59  459 86  HOH   HOH A . 
E 4 HOH   60  460 22  HOH   HOH A . 
E 4 HOH   61  461 77  HOH   HOH A . 
E 4 HOH   62  462 18  HOH   HOH A . 
E 4 HOH   63  463 50  HOH   HOH A . 
E 4 HOH   64  464 21  HOH   HOH A . 
E 4 HOH   65  465 141 HOH   HOH A . 
E 4 HOH   66  466 83  HOH   HOH A . 
E 4 HOH   67  467 37  HOH   HOH A . 
E 4 HOH   68  468 15  HOH   HOH A . 
E 4 HOH   69  469 130 HOH   HOH A . 
E 4 HOH   70  470 54  HOH   HOH A . 
E 4 HOH   71  471 4   HOH   HOH A . 
E 4 HOH   72  472 63  HOH   HOH A . 
E 4 HOH   73  473 10  HOH   HOH A . 
E 4 HOH   74  474 61  HOH   HOH A . 
E 4 HOH   75  475 35  HOH   HOH A . 
E 4 HOH   76  476 128 HOH   HOH A . 
E 4 HOH   77  477 135 HOH   HOH A . 
E 4 HOH   78  478 16  HOH   HOH A . 
E 4 HOH   79  479 67  HOH   HOH A . 
E 4 HOH   80  480 39  HOH   HOH A . 
E 4 HOH   81  481 75  HOH   HOH A . 
E 4 HOH   82  482 94  HOH   HOH A . 
E 4 HOH   83  483 32  HOH   HOH A . 
E 4 HOH   84  484 127 HOH   HOH A . 
E 4 HOH   85  485 132 HOH   HOH A . 
E 4 HOH   86  486 65  HOH   HOH A . 
E 4 HOH   87  487 60  HOH   HOH A . 
E 4 HOH   88  488 142 HOH   HOH A . 
E 4 HOH   89  489 71  HOH   HOH A . 
E 4 HOH   90  490 55  HOH   HOH A . 
E 4 HOH   91  491 46  HOH   HOH A . 
E 4 HOH   92  492 137 HOH   HOH A . 
E 4 HOH   93  493 62  HOH   HOH A . 
E 4 HOH   94  494 64  HOH   HOH A . 
E 4 HOH   95  495 79  HOH   HOH A . 
E 4 HOH   96  496 97  HOH   HOH A . 
E 4 HOH   97  497 129 HOH   HOH A . 
E 4 HOH   98  498 1   HOH   HOH A . 
E 4 HOH   99  499 114 HOH   HOH A . 
E 4 HOH   100 500 25  HOH   HOH A . 
E 4 HOH   101 501 93  HOH   HOH A . 
E 4 HOH   102 502 111 HOH   HOH A . 
E 4 HOH   103 503 103 HOH   HOH A . 
E 4 HOH   104 504 101 HOH   HOH A . 
E 4 HOH   105 505 125 HOH   HOH A . 
E 4 HOH   106 506 134 HOH   HOH A . 
E 4 HOH   107 507 84  HOH   HOH A . 
E 4 HOH   108 508 95  HOH   HOH A . 
E 4 HOH   109 509 92  HOH   HOH A . 
E 4 HOH   110 510 104 HOH   HOH A . 
E 4 HOH   111 511 131 HOH   HOH A . 
E 4 HOH   112 512 124 HOH   HOH A . 
E 4 HOH   113 513 87  HOH   HOH A . 
E 4 HOH   114 514 49  HOH   HOH A . 
E 4 HOH   115 515 99  HOH   HOH A . 
E 4 HOH   116 516 30  HOH   HOH A . 
E 4 HOH   117 517 70  HOH   HOH A . 
E 4 HOH   118 518 112 HOH   HOH A . 
E 4 HOH   119 519 3   HOH   HOH A . 
E 4 HOH   120 520 109 HOH   HOH A . 
E 4 HOH   121 521 115 HOH   HOH A . 
E 4 HOH   122 522 53  HOH   HOH A . 
E 4 HOH   123 523 113 HOH   HOH A . 
E 4 HOH   124 524 91  HOH   HOH A . 
E 4 HOH   125 525 116 HOH   HOH A . 
E 4 HOH   126 526 120 HOH   HOH A . 
E 4 HOH   127 527 133 HOH   HOH A . 
E 4 HOH   128 528 108 HOH   HOH A . 
E 4 HOH   129 529 96  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 109 ? CD  ? A GLU 109 CD  
2  1 Y 1 A GLU 109 ? OE1 ? A GLU 109 OE1 
3  1 Y 1 A GLU 109 ? OE2 ? A GLU 109 OE2 
4  1 Y 1 A GLN 123 ? CG  ? A GLN 123 CG  
5  1 Y 1 A GLN 123 ? CD  ? A GLN 123 CD  
6  1 Y 1 A GLN 123 ? OE1 ? A GLN 123 OE1 
7  1 Y 1 A GLN 123 ? NE2 ? A GLN 123 NE2 
8  1 Y 1 A LYS 131 ? CG  ? A LYS 131 CG  
9  1 Y 1 A LYS 131 ? CD  ? A LYS 131 CD  
10 1 Y 1 A LYS 131 ? CE  ? A LYS 131 CE  
11 1 Y 1 A LYS 131 ? NZ  ? A LYS 131 NZ  
12 1 Y 1 A LEU 241 ? CG  ? A LEU 241 CG  
13 1 Y 1 A LEU 241 ? CD1 ? A LEU 241 CD1 
14 1 Y 1 A LEU 241 ? CD2 ? A LEU 241 CD2 
15 1 Y 1 A GLU 242 ? CG  ? A GLU 242 CG  
16 1 Y 1 A GLU 242 ? CD  ? A GLU 242 CD  
17 1 Y 1 A GLU 242 ? OE1 ? A GLU 242 OE1 
18 1 Y 1 A GLU 242 ? OE2 ? A GLU 242 OE2 
19 1 Y 1 A LEU 245 ? CD1 ? A LEU 245 CD1 
20 1 Y 1 A LEU 245 ? CD2 ? A LEU 245 CD2 
21 1 Y 1 A HIS 252 ? CG  ? A HIS 252 CG  
22 1 Y 1 A HIS 252 ? ND1 ? A HIS 252 ND1 
23 1 Y 1 A HIS 252 ? CD2 ? A HIS 252 CD2 
24 1 Y 1 A HIS 252 ? CE1 ? A HIS 252 CE1 
25 1 Y 1 A HIS 252 ? NE2 ? A HIS 252 NE2 
# 
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 ? ? ? 1.19.2_4158 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .           2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XSCALE ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .           4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  120.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9CD1 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     106.160 
_cell.length_a_esd                 ? 
_cell.length_b                     106.160 
_cell.length_b_esd                 ? 
_cell.length_c                     53.550 
_cell.length_c_esd                 ? 
_cell.volume                       522651.170 
_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                         9CD1 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                154 
_symmetry.space_group_name_Hall            
;P 32 2"
;
_symmetry.space_group_name_H-M             'P 32 2 1' 
_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                   9CD1 
_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             2.94 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          58.16 
_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          'VAPOR DIFFUSION, SITTING DROP' 
_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    
;0.91 mg/mL of LpxH, 
0.1 mM LPH-107, 
10 mM MES (pH 6.0), 
100 mM NaCl, 
0.5 mM DTT, 
2.5% glycerol, 
0.8% DMSO, 
0.05 M sodium acetate pH 4.5, 
and 16 % v/v PEG 400
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS3 2M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-03-29 
_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   0.976480 
_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                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'ALS BEAMLINE 5.0.3' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.976480 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   5.0.3 
_diffrn_source.pdbx_synchrotron_site       ALS 
# 
_reflns.B_iso_Wilson_estimate                          26.68 
_reflns.entry_id                                       9CD1 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.0 
_reflns.d_resolution_low                               46.27 
_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                                     23763 
_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                           99.93 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                10.2 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          16.52 
_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                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_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                                    2.000 
_reflns_shell.d_res_low                                     2.072 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           3.09 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2345 
_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                               10.6 
_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                                  0.858 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          99.96 
_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                               31.87 
_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                                 9CD1 
_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                             46.27 
_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                     23762 
_refine.ls_number_reflns_R_free                  1189 
_refine.ls_number_reflns_R_work                  22573 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.95 
_refine.ls_percent_reflns_R_free                 5.00 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1949 
_refine.ls_R_factor_R_free                       0.2096 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1941 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.36 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_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             1.1100 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 20.3972 
_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                            0.1756 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.00 
_refine_hist.d_res_low                        46.27 
_refine_hist.number_atoms_solvent             129 
_refine_hist.number_atoms_total               2073 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        1901 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         43 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.0020  ? 2039 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.5696  ? 2787 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0419  ? 293  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0036  ? 365  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 13.0937 ? 310  ? f_dihedral_angle_d ? ? 
# 
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 2.09  . . 147 2799 99.97  . . . . 0.2216 . . . . . . . . . . . 0.2452 
'X-RAY DIFFRACTION' 2.09 2.20  . . 146 2767 99.93  . . . . 0.2013 . . . . . . . . . . . 0.1958 
'X-RAY DIFFRACTION' 2.20 2.34  . . 148 2809 100.00 . . . . 0.1871 . . . . . . . . . . . 0.2140 
'X-RAY DIFFRACTION' 2.34 2.52  . . 147 2797 100.00 . . . . 0.1967 . . . . . . . . . . . 0.2333 
'X-RAY DIFFRACTION' 2.52 2.77  . . 148 2811 99.97  . . . . 0.1878 . . . . . . . . . . . 0.2004 
'X-RAY DIFFRACTION' 2.77 3.17  . . 148 2813 100.00 . . . . 0.2000 . . . . . . . . . . . 0.2324 
'X-RAY DIFFRACTION' 3.17 4.00  . . 150 2838 100.00 . . . . 0.1793 . . . . . . . . . . . 0.1997 
'X-RAY DIFFRACTION' 4.00 46.27 . . 155 2939 99.77  . . . . 0.1999 . . . . . . . . . . . 0.2005 
# 
_struct.entry_id                     9CD1 
_struct.title                        'Crystal structure of the Klebsiella pneumoniae LpxH / JH-LPH-107 complex' 
_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        9CD1 
_struct_keywords.text            'LpxH, lipid A, antibiotic' 
_struct_keywords.pdbx_keywords   ANTIBIOTIC 
# 
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 3 ? 
D N N 3 ? 
E N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A0A1S0WIC1_KLEPN 
_struct_ref.pdbx_db_accession          A0A1S0WIC1 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MATLFIADLHLQTEEPAITAGFLRFLQGEARQADALYILGDLFEAWIGDDDPNPLHQQIASAIKAVVDAGVPCYFIHGNR
DFLVGQRFARQSGMILLAEEERLDLYGREVLIMHGDTLCTDDQGYLAFRAKVHTPWIQRLFLALPLFIRHRIAARMRADS
KAANSSKSMEIMDVNPQAVVDAMERHHVQWLIHGHTHRPAVHELQANGQPAWRVVLGAWHSEGSMVKVTPDDVELIHFPF

;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9CD1 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 240 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             A0A1S0WIC1 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  240 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       240 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9CD1 LEU A 241 ? UNP A0A1S0WIC1 ? ? 'expression tag' 241 1  
1 9CD1 GLU A 242 ? UNP A0A1S0WIC1 ? ? 'expression tag' 242 2  
1 9CD1 GLU A 243 ? UNP A0A1S0WIC1 ? ? 'expression tag' 243 3  
1 9CD1 ASN A 244 ? UNP A0A1S0WIC1 ? ? 'expression tag' 244 4  
1 9CD1 LEU A 245 ? UNP A0A1S0WIC1 ? ? 'expression tag' 245 5  
1 9CD1 TYR A 246 ? UNP A0A1S0WIC1 ? ? 'expression tag' 246 6  
1 9CD1 PHE A 247 ? UNP A0A1S0WIC1 ? ? 'expression tag' 247 7  
1 9CD1 GLN A 248 ? UNP A0A1S0WIC1 ? ? 'expression tag' 248 8  
1 9CD1 SER A 249 ? UNP A0A1S0WIC1 ? ? 'expression tag' 249 9  
1 9CD1 HIS A 250 ? UNP A0A1S0WIC1 ? ? 'expression tag' 250 10 
1 9CD1 HIS A 251 ? UNP A0A1S0WIC1 ? ? 'expression tag' 251 11 
1 9CD1 HIS A 252 ? UNP A0A1S0WIC1 ? ? 'expression tag' 252 12 
1 9CD1 HIS A 253 ? UNP A0A1S0WIC1 ? ? 'expression tag' 253 13 
1 9CD1 HIS A 254 ? UNP A0A1S0WIC1 ? ? 'expression tag' 254 14 
1 9CD1 HIS A 255 ? UNP A0A1S0WIC1 ? ? 'expression tag' 255 15 
1 9CD1 HIS A 256 ? UNP A0A1S0WIC1 ? ? 'expression tag' 256 16 
1 9CD1 HIS A 257 ? UNP A0A1S0WIC1 ? ? 'expression tag' 257 17 
1 9CD1 HIS A 258 ? UNP A0A1S0WIC1 ? ? 'expression tag' 258 18 
1 9CD1 HIS A 259 ? UNP A0A1S0WIC1 ? ? 'expression tag' 259 19 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_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 
# 
_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]         1.0 
_pdbx_struct_oper_list.matrix[1][2]         0.0 
_pdbx_struct_oper_list.matrix[1][3]         0.0 
_pdbx_struct_oper_list.vector[1]            0.0 
_pdbx_struct_oper_list.matrix[2][1]         0.0 
_pdbx_struct_oper_list.matrix[2][2]         1.0 
_pdbx_struct_oper_list.matrix[2][3]         0.0 
_pdbx_struct_oper_list.vector[2]            0.0 
_pdbx_struct_oper_list.matrix[3][1]         0.0 
_pdbx_struct_oper_list.matrix[3][2]         0.0 
_pdbx_struct_oper_list.matrix[3][3]         1.0 
_pdbx_struct_oper_list.vector[3]            0.0 
# 
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 15  ? GLY A 28  ? GLU A 15  GLY A 28  1 ? 14 
HELX_P HELX_P2 AA2 GLU A 29  ? ALA A 33  ? GLU A 29  ALA A 33  5 ? 5  
HELX_P HELX_P3 AA3 ASN A 53  ? ALA A 69  ? ASN A 53  ALA A 69  1 ? 17 
HELX_P HELX_P4 AA4 GLY A 85  ? GLY A 93  ? GLY A 85  GLY A 93  1 ? 9  
HELX_P HELX_P5 AA5 GLY A 115 ? CYS A 119 ? GLY A 115 CYS A 119 5 ? 5  
HELX_P HELX_P6 AA6 ASP A 122 ? HIS A 133 ? ASP A 122 HIS A 133 1 ? 12 
HELX_P HELX_P7 AA7 THR A 134 ? LEU A 144 ? THR A 134 LEU A 144 1 ? 11 
HELX_P HELX_P8 AA8 PRO A 145 ? SER A 160 ? PRO A 145 SER A 160 1 ? 16 
HELX_P HELX_P9 AA9 ASN A 175 ? HIS A 186 ? ASN A 175 HIS A 186 1 ? 12 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_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 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_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 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1  metalc ? ? A ASP 8   OD1 ? ? ? 1_555 C MN  . MN ? ? A ASP 8   A MN  302 1_555 ? ? ? ? ? ? ? 1.994 ? ? 
metalc2  metalc ? ? A HIS 10  NE2 ? ? ? 1_555 C MN  . MN ? ? A HIS 10  A MN  302 1_555 ? ? ? ? ? ? ? 2.212 ? ? 
metalc3  metalc ? ? A ASP 41  OD2 ? ? ? 1_555 C MN  . MN ? ? A ASP 41  A MN  302 1_555 ? ? ? ? ? ? ? 2.306 ? ? 
metalc4  metalc ? ? A ASP 41  OD2 ? ? ? 1_555 D MN  . MN ? ? A ASP 41  A MN  303 1_555 ? ? ? ? ? ? ? 2.191 ? ? 
metalc5  metalc ? ? A ASN 79  OD1 ? ? ? 1_555 D MN  . MN ? ? A ASN 79  A MN  303 1_555 ? ? ? ? ? ? ? 1.971 ? ? 
metalc6  metalc ? ? A HIS 114 NE2 ? ? ? 1_555 D MN  . MN ? ? A HIS 114 A MN  303 1_555 ? ? ? ? ? ? ? 2.251 ? ? 
metalc7  metalc ? ? A HIS 195 ND1 ? ? ? 1_555 D MN  . MN ? ? A HIS 195 A MN  303 1_555 ? ? ? ? ? ? ? 2.375 ? ? 
metalc8  metalc ? ? A HIS 197 NE2 ? ? ? 1_555 C MN  . MN ? ? A HIS 197 A MN  302 1_555 ? ? ? ? ? ? ? 2.279 ? ? 
metalc9  metalc ? ? C MN  .   MN  ? ? ? 1_555 E HOH . O  ? ? A MN  302 A HOH 413 1_555 ? ? ? ? ? ? ? 1.972 ? ? 
metalc10 metalc ? ? D MN  .   MN  ? ? ? 1_555 E HOH . O  ? ? A MN  303 A HOH 413 1_555 ? ? ? ? ? ? ? 2.114 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  OD1 ? A ASP 8   ? A ASP 8   ? 1_555 MN ? C MN . ? A MN 302 ? 1_555 NE2 ? A HIS 10  ? A HIS 10  ? 1_555 118.2 ? 
2  OD1 ? A ASP 8   ? A ASP 8   ? 1_555 MN ? C MN . ? A MN 302 ? 1_555 OD2 ? A ASP 41  ? A ASP 41  ? 1_555 87.2  ? 
3  NE2 ? A HIS 10  ? A HIS 10  ? 1_555 MN ? C MN . ? A MN 302 ? 1_555 OD2 ? A ASP 41  ? A ASP 41  ? 1_555 102.9 ? 
4  OD1 ? A ASP 8   ? A ASP 8   ? 1_555 MN ? C MN . ? A MN 302 ? 1_555 NE2 ? A HIS 197 ? A HIS 197 ? 1_555 93.8  ? 
5  NE2 ? A HIS 10  ? A HIS 10  ? 1_555 MN ? C MN . ? A MN 302 ? 1_555 NE2 ? A HIS 197 ? A HIS 197 ? 1_555 88.7  ? 
6  OD2 ? A ASP 41  ? A ASP 41  ? 1_555 MN ? C MN . ? A MN 302 ? 1_555 NE2 ? A HIS 197 ? A HIS 197 ? 1_555 166.2 ? 
7  OD1 ? A ASP 8   ? A ASP 8   ? 1_555 MN ? C MN . ? A MN 302 ? 1_555 O   ? E HOH .   ? A HOH 413 ? 1_555 102.8 ? 
8  NE2 ? A HIS 10  ? A HIS 10  ? 1_555 MN ? C MN . ? A MN 302 ? 1_555 O   ? E HOH .   ? A HOH 413 ? 1_555 138.8 ? 
9  OD2 ? A ASP 41  ? A ASP 41  ? 1_555 MN ? C MN . ? A MN 302 ? 1_555 O   ? E HOH .   ? A HOH 413 ? 1_555 73.6  ? 
10 NE2 ? A HIS 197 ? A HIS 197 ? 1_555 MN ? C MN . ? A MN 302 ? 1_555 O   ? E HOH .   ? A HOH 413 ? 1_555 92.8  ? 
11 OD2 ? A ASP 41  ? A ASP 41  ? 1_555 MN ? D MN . ? A MN 303 ? 1_555 OD1 ? A ASN 79  ? A ASN 79  ? 1_555 103.1 ? 
12 OD2 ? A ASP 41  ? A ASP 41  ? 1_555 MN ? D MN . ? A MN 303 ? 1_555 NE2 ? A HIS 114 ? A HIS 114 ? 1_555 94.8  ? 
13 OD1 ? A ASN 79  ? A ASN 79  ? 1_555 MN ? D MN . ? A MN 303 ? 1_555 NE2 ? A HIS 114 ? A HIS 114 ? 1_555 92.5  ? 
14 OD2 ? A ASP 41  ? A ASP 41  ? 1_555 MN ? D MN . ? A MN 303 ? 1_555 ND1 ? A HIS 195 ? A HIS 195 ? 1_555 165.7 ? 
15 OD1 ? A ASN 79  ? A ASN 79  ? 1_555 MN ? D MN . ? A MN 303 ? 1_555 ND1 ? A HIS 195 ? A HIS 195 ? 1_555 90.1  ? 
16 NE2 ? A HIS 114 ? A HIS 114 ? 1_555 MN ? D MN . ? A MN 303 ? 1_555 ND1 ? A HIS 195 ? A HIS 195 ? 1_555 90.1  ? 
17 OD2 ? A ASP 41  ? A ASP 41  ? 1_555 MN ? D MN . ? A MN 303 ? 1_555 O   ? E HOH .   ? A HOH 413 ? 1_555 73.5  ? 
18 OD1 ? A ASN 79  ? A ASN 79  ? 1_555 MN ? D MN . ? A MN 303 ? 1_555 O   ? E HOH .   ? A HOH 413 ? 1_555 134.3 ? 
19 NE2 ? A HIS 114 ? A HIS 114 ? 1_555 MN ? D MN . ? A MN 303 ? 1_555 O   ? E HOH .   ? A HOH 413 ? 1_555 133.0 ? 
20 ND1 ? A HIS 195 ? A HIS 195 ? 1_555 MN ? D MN . ? A MN 303 ? 1_555 O   ? E HOH .   ? A HOH 413 ? 1_555 93.3  ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 6 ? 
AA2 ? 5 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel      
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? parallel      
AA2 3 4 ? parallel      
AA2 4 5 ? 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 ILE A 95  ? LEU A 96  ? ILE A 95  LEU A 96  
AA1 2 CYS A 73  ? PHE A 75  ? CYS A 73  PHE A 75  
AA1 3 ALA A 35  ? ILE A 38  ? ALA A 35  ILE A 38  
AA1 4 THR A 3   ? ILE A 6   ? THR A 3   ILE A 6   
AA1 5 GLY A 223 ? VAL A 228 ? GLY A 223 VAL A 228 
AA1 6 VAL A 233 ? PHE A 238 ? VAL A 233 PHE A 238 
AA2 1 GLU A 101 ? LEU A 105 ? GLU A 101 LEU A 105 
AA2 2 ARG A 108 ? ILE A 112 ? ARG A 108 ILE A 112 
AA2 3 TRP A 190 ? HIS A 193 ? TRP A 190 HIS A 193 
AA2 4 GLN A 209 ? VAL A 215 ? GLN A 209 VAL A 215 
AA2 5 ALA A 200 ? ALA A 206 ? ALA A 200 ALA A 206 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O ILE A 95  ? O ILE A 95  N PHE A 75  ? N PHE A 75  
AA1 2 3 O TYR A 74  ? O TYR A 74  N LEU A 36  ? N LEU A 36  
AA1 3 4 O TYR A 37  ? O TYR A 37  N LEU A 4   ? N LEU A 4   
AA1 4 5 N THR A 3   ? N THR A 3   O VAL A 228 ? O VAL A 228 
AA1 5 6 N GLY A 223 ? N GLY A 223 O PHE A 238 ? O PHE A 238 
AA2 1 2 N LEU A 103 ? N LEU A 103 O VAL A 110 ? O VAL A 110 
AA2 2 3 N LEU A 111 ? N LEU A 111 O ILE A 192 ? O ILE A 192 
AA2 3 4 N LEU A 191 ? N LEU A 191 O VAL A 214 ? O VAL A 214 
AA2 4 5 O ALA A 211 ? O ALA A 211 N LEU A 204 ? N LEU A 204 
# 
_pdbx_entry_details.entry_id                   9CD1 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 LEU A 39  ? ? -92.17 45.15  
2 1 CYS A 119 ? ? -94.06 58.33  
3 1 HIS A 195 ? ? 69.97  -47.65 
4 1 HIS A 220 ? ? -91.68 -67.44 
5 1 HIS A 220 ? ? -91.68 -66.74 
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 A HOH 507 ? E HOH . 
2 1 A HOH 513 ? E HOH . 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z          
2 -y,x-y,z+2/3   
3 -x+y,-x,z+1/3  
4 x-y,-y,-z+1/3  
5 -x,-x+y,-z+2/3 
6 y,x,-z         
# 
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 -36.6736200271 -31.0798661215 -1.04698605113 0.219409849309 ? 0.0151306658346  ? 0.0159850415257   
? 0.17858330981  ? -0.0409087212492 ? 0.203168186386 ? 1.74387826124 ? -0.12530564419  ? 0.410019710085   ? 1.7012422993  ? 
-1.50125209923  ? 2.63860198274  ? 0.00457452214837  ? 0.0846094360382  ? -0.197938163809  ? -0.33491865282  ? -0.0580123442326 ? 
-0.0997313196641 ? 0.311394969497   ? -0.0300536072882 ? 0.0625190929541  ? 
2 'X-RAY DIFFRACTION' ? refined -42.5407556249 -23.6642630826 4.00311343852  0.18608621756  ? 0.0220524584273  ? -0.019529512199   
? 0.178054577994 ? -0.0140162835564 ? 0.173595012295 ? 1.28864149561 ? -0.644222657296 ? -0.183059545932  ? 1.49679995067 ? 
-0.118584211267 ? 0.553031612178 ? -0.0153856087673  ? -0.0634503313205 ? -0.0484443502492 ? 0.0192124285178 ? 0.0427912260661  ? 
0.0807717903957  ? -0.0461822438187 ? -0.08743476501   ? -0.0290814905976 ? 
3 'X-RAY DIFFRACTION' ? refined -32.5391652628 -25.5389882262 12.8372710782  0.197798653542 ? 0.0149750857825  ? -0.00367265875686 
? 0.214343209226 ? -0.0304783555413 ? 0.165344764444 ? 2.65775711788 ? 0.218920222372  ? -0.400917773526  ? 2.72816200096 ? 
-0.672299089354 ? 2.44399996266  ? 0.000633364355647 ? -0.366304449385  ? 0.0642118253505  ? 0.256360123316  ? -0.0246694496586 ? 
-0.225152495139  ? -0.0507363022048 ? 0.197793295053   ? 0.0689066172108  ? 
4 'X-RAY DIFFRACTION' ? refined -38.1200754795 -7.27904732342 11.9989399584  0.346371039408 ? 0.0986642143096  ? -0.0795740354378  
? 0.287188803437 ? -0.100081843023  ? 0.314025962517 ? 3.97114953904 ? -2.20787810779  ? 0.502780911956   ? 1.82748213248 ? 
0.286561632186  ? 1.76880747394  ? -0.428805553765   ? -0.851204853597  ? 0.686536442513   ? 0.413250774192  ? 0.383179061401   ? 
-0.43359647529   ? 0.068876706903   ? 0.0766036142428  ? -0.0104797656843 ? 
5 'X-RAY DIFFRACTION' ? refined -42.5040134979 -5.09422340502 -1.00113745624 0.492413606541 ? -0.0238877006329 ? 0.0359689140482   
? 0.197111333508 ? -0.0482552668065 ? 0.406915286405 ? 3.3150927391  ? 1.05484254824   ? -2.96107209593   ? 6.42441156665 ? 
-1.20484207796  ? 8.17675039434  ? -0.539685181695   ? 0.524527567031   ? 0.210879301061   ? -1.48350441527  ? 0.00714801641708 ? 
-0.849639449611  ? -0.578980798195  ? 0.0827480779602  ? 0.403562081634   ? 
6 'X-RAY DIFFRACTION' ? refined -18.2403417436 -19.111319826  13.2937684267  0.289792993484 ? -0.0246647655056 ? -0.0740491780426  
? 0.320290515355 ? -0.0875630600794 ? 0.437265940809 ? 5.78523562295 ? -1.81914892566  ? -0.0778880608037 ? 4.56442348769 ? 
0.2010587391    ? 1.68988018022  ? -0.174515016721   ? -0.270388821026  ? 1.0506421546     ? 0.40316942505   ? 0.0853581285694  ? 
-0.422069394655  ? -0.272192116963  ? 0.446661530878   ? 0.150217999738   ? 
7 'X-RAY DIFFRACTION' ? refined -21.0683307957 -28.7459892531 6.8262238374   0.164989998004 ? 0.00446890960306 ? -0.00652212044366 
? 0.167430981876 ? -0.0122542246313 ? 0.212016280794 ? 3.9619574318  ? -0.345335839248 ? -0.133906020901  ? 2.26761195817 ? 
0.841759979056  ? 2.5641819293   ? -0.00507613586193 ? -0.0714439033883 ? 0.0980187543575  ? 0.0346170766747 ? 0.052944672312   ? 
-0.296136545941  ? 0.00752418087695 ? 0.103319828436   ? -0.0479899496848 ? 
8 'X-RAY DIFFRACTION' ? refined -26.6257478817 -39.2166880278 -10.3750553409 0.340237919172 ? 0.089861110679   ? -0.0374518917625  
? 0.329044230046 ? -0.0426496948825 ? 0.352817758919 ? 1.23329669414 ? -0.570702010629 ? -0.329430005996  ? 1.36971915839 ? 
1.77035046141   ? 3.81569729166  ? 0.246533750858    ? 0.479656558295   ? -0.194045990526  ? -0.449617520407 ? -0.302734691906  ? 
0.100598597491   ? -0.0487797399189 ? 0.117335985387   ? 0.062807823817   ? 
# 
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 A 1   A 2   ? A 37  A 38  ? ? 
;chain 'A' and (resid 2 through 38 )
;
2 'X-RAY DIFFRACTION' 2 A 38  A 39  ? A 84  A 85  ? ? 
;chain 'A' and (resid 39 through 85 )
;
3 'X-RAY DIFFRACTION' 3 A 85  A 86  ? A 121 A 122 ? ? 
;chain 'A' and (resid 86 through 122 )
;
4 'X-RAY DIFFRACTION' 4 A 122 A 123 ? A 144 A 145 ? ? 
;chain 'A' and (resid 123 through 145 )
;
5 'X-RAY DIFFRACTION' 5 A 145 A 146 ? A 158 A 159 ? ? 
;chain 'A' and (resid 146 through 159 )
;
6 'X-RAY DIFFRACTION' 6 A 159 A 160 ? A 174 A 185 ? ? 
;chain 'A' and (resid 160 through 185 )
;
7 'X-RAY DIFFRACTION' 7 A 175 A 186 ? A 217 A 228 ? ? 
;chain 'A' and (resid 186 through 228 )
;
8 'X-RAY DIFFRACTION' 8 A 218 A 229 ? A 239 A 252 ? ? 
;chain 'A' and (resid 229 through 252 )
;
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 526 ? 6.08 . 
2 1 O ? A HOH 527 ? 7.27 . 
3 1 O ? A HOH 528 ? 7.27 . 
4 1 O ? A HOH 529 ? 7.86 . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET 1   ? A MET 1   
2  1 Y 1 A LYS 161 ? A LYS 161 
3  1 Y 1 A ALA 162 ? A ALA 162 
4  1 Y 1 A ALA 163 ? A ALA 163 
5  1 Y 1 A ASN 164 ? A ASN 164 
6  1 Y 1 A SER 165 ? A SER 165 
7  1 Y 1 A SER 166 ? A SER 166 
8  1 Y 1 A LYS 167 ? A LYS 167 
9  1 Y 1 A SER 168 ? A SER 168 
10 1 Y 1 A MET 169 ? A MET 169 
11 1 Y 1 A GLU 170 ? A GLU 170 
12 1 Y 1 A GLN 248 ? A GLN 248 
13 1 Y 1 A SER 249 ? A SER 249 
14 1 Y 1 A HIS 253 ? A HIS 253 
15 1 Y 1 A HIS 254 ? A HIS 254 
16 1 Y 1 A HIS 255 ? A HIS 255 
17 1 Y 1 A HIS 256 ? A HIS 256 
18 1 Y 1 A HIS 257 ? A HIS 257 
19 1 Y 1 A HIS 258 ? A HIS 258 
20 1 Y 1 A HIS 259 ? A HIS 259 
# 
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 
A1AVW C10  C  N N 1   
A1AVW C15  C  Y N 2   
A1AVW C17  C  Y N 3   
A1AVW C21  C  N N 4   
A1AVW C24  C  Y N 5   
A1AVW C26  C  N N 6   
A1AVW C02  C  Y N 7   
A1AVW C04  C  Y N 8   
A1AVW C06  C  N N 9   
A1AVW C07  C  N N 10  
A1AVW C09  C  N N 11  
A1AVW C14  C  Y N 12  
A1AVW C16  C  Y N 13  
A1AVW C18  C  Y N 14  
A1AVW C19  C  Y N 15  
A1AVW C23  C  Y N 16  
A1AVW C30  C  N N 17  
A1AVW C31  C  Y N 18  
A1AVW C32  C  Y N 19  
A1AVW C33  C  Y N 20  
A1AVW C34  C  Y N 21  
A1AVW C35  C  Y N 22  
A1AVW C36  C  Y N 23  
A1AVW C37  C  Y N 24  
A1AVW C38  C  N N 25  
A1AVW F39  F  N N 26  
A1AVW F40  F  N N 27  
A1AVW F41  F  N N 28  
A1AVW N03  N  Y N 29  
A1AVW N05  N  N N 30  
A1AVW N08  N  N N 31  
A1AVW N20  N  N N 32  
A1AVW N25  N  N N 33  
A1AVW O12  O  N N 34  
A1AVW O13  O  N N 35  
A1AVW O22  O  N N 36  
A1AVW O28  O  N N 37  
A1AVW O29  O  N N 38  
A1AVW S11  S  N N 39  
A1AVW S27  S  N N 40  
A1AVW CL01 CL N N 41  
A1AVW H102 H  N N 42  
A1AVW H101 H  N N 43  
A1AVW H151 H  N N 44  
A1AVW H262 H  N N 45  
A1AVW H263 H  N N 46  
A1AVW H261 H  N N 47  
A1AVW H062 H  N N 48  
A1AVW H061 H  N N 49  
A1AVW H072 H  N N 50  
A1AVW H071 H  N N 51  
A1AVW H091 H  N N 52  
A1AVW H092 H  N N 53  
A1AVW H161 H  N N 54  
A1AVW H181 H  N N 55  
A1AVW H191 H  N N 56  
A1AVW H301 H  N N 57  
A1AVW H303 H  N N 58  
A1AVW H302 H  N N 59  
A1AVW H311 H  N N 60  
A1AVW H321 H  N N 61  
A1AVW H331 H  N N 62  
A1AVW H341 H  N N 63  
A1AVW H351 H  N N 64  
A1AVW H371 H  N N 65  
A1AVW H201 H  N N 66  
ALA   N    N  N N 67  
ALA   CA   C  N S 68  
ALA   C    C  N N 69  
ALA   O    O  N N 70  
ALA   CB   C  N N 71  
ALA   OXT  O  N N 72  
ALA   H    H  N N 73  
ALA   H2   H  N N 74  
ALA   HA   H  N N 75  
ALA   HB1  H  N N 76  
ALA   HB2  H  N N 77  
ALA   HB3  H  N N 78  
ALA   HXT  H  N N 79  
ARG   N    N  N N 80  
ARG   CA   C  N S 81  
ARG   C    C  N N 82  
ARG   O    O  N N 83  
ARG   CB   C  N N 84  
ARG   CG   C  N N 85  
ARG   CD   C  N N 86  
ARG   NE   N  N N 87  
ARG   CZ   C  N N 88  
ARG   NH1  N  N N 89  
ARG   NH2  N  N N 90  
ARG   OXT  O  N N 91  
ARG   H    H  N N 92  
ARG   H2   H  N N 93  
ARG   HA   H  N N 94  
ARG   HB2  H  N N 95  
ARG   HB3  H  N N 96  
ARG   HG2  H  N N 97  
ARG   HG3  H  N N 98  
ARG   HD2  H  N N 99  
ARG   HD3  H  N N 100 
ARG   HE   H  N N 101 
ARG   HH11 H  N N 102 
ARG   HH12 H  N N 103 
ARG   HH21 H  N N 104 
ARG   HH22 H  N N 105 
ARG   HXT  H  N N 106 
ASN   N    N  N N 107 
ASN   CA   C  N S 108 
ASN   C    C  N N 109 
ASN   O    O  N N 110 
ASN   CB   C  N N 111 
ASN   CG   C  N N 112 
ASN   OD1  O  N N 113 
ASN   ND2  N  N N 114 
ASN   OXT  O  N N 115 
ASN   H    H  N N 116 
ASN   H2   H  N N 117 
ASN   HA   H  N N 118 
ASN   HB2  H  N N 119 
ASN   HB3  H  N N 120 
ASN   HD21 H  N N 121 
ASN   HD22 H  N N 122 
ASN   HXT  H  N N 123 
ASP   N    N  N N 124 
ASP   CA   C  N S 125 
ASP   C    C  N N 126 
ASP   O    O  N N 127 
ASP   CB   C  N N 128 
ASP   CG   C  N N 129 
ASP   OD1  O  N N 130 
ASP   OD2  O  N N 131 
ASP   OXT  O  N N 132 
ASP   H    H  N N 133 
ASP   H2   H  N N 134 
ASP   HA   H  N N 135 
ASP   HB2  H  N N 136 
ASP   HB3  H  N N 137 
ASP   HD2  H  N N 138 
ASP   HXT  H  N N 139 
CYS   N    N  N N 140 
CYS   CA   C  N R 141 
CYS   C    C  N N 142 
CYS   O    O  N N 143 
CYS   CB   C  N N 144 
CYS   SG   S  N N 145 
CYS   OXT  O  N N 146 
CYS   H    H  N N 147 
CYS   H2   H  N N 148 
CYS   HA   H  N N 149 
CYS   HB2  H  N N 150 
CYS   HB3  H  N N 151 
CYS   HG   H  N N 152 
CYS   HXT  H  N N 153 
GLN   N    N  N N 154 
GLN   CA   C  N S 155 
GLN   C    C  N N 156 
GLN   O    O  N N 157 
GLN   CB   C  N N 158 
GLN   CG   C  N N 159 
GLN   CD   C  N N 160 
GLN   OE1  O  N N 161 
GLN   NE2  N  N N 162 
GLN   OXT  O  N N 163 
GLN   H    H  N N 164 
GLN   H2   H  N N 165 
GLN   HA   H  N N 166 
GLN   HB2  H  N N 167 
GLN   HB3  H  N N 168 
GLN   HG2  H  N N 169 
GLN   HG3  H  N N 170 
GLN   HE21 H  N N 171 
GLN   HE22 H  N N 172 
GLN   HXT  H  N N 173 
GLU   N    N  N N 174 
GLU   CA   C  N S 175 
GLU   C    C  N N 176 
GLU   O    O  N N 177 
GLU   CB   C  N N 178 
GLU   CG   C  N N 179 
GLU   CD   C  N N 180 
GLU   OE1  O  N N 181 
GLU   OE2  O  N N 182 
GLU   OXT  O  N N 183 
GLU   H    H  N N 184 
GLU   H2   H  N N 185 
GLU   HA   H  N N 186 
GLU   HB2  H  N N 187 
GLU   HB3  H  N N 188 
GLU   HG2  H  N N 189 
GLU   HG3  H  N N 190 
GLU   HE2  H  N N 191 
GLU   HXT  H  N N 192 
GLY   N    N  N N 193 
GLY   CA   C  N N 194 
GLY   C    C  N N 195 
GLY   O    O  N N 196 
GLY   OXT  O  N N 197 
GLY   H    H  N N 198 
GLY   H2   H  N N 199 
GLY   HA2  H  N N 200 
GLY   HA3  H  N N 201 
GLY   HXT  H  N N 202 
HIS   N    N  N N 203 
HIS   CA   C  N S 204 
HIS   C    C  N N 205 
HIS   O    O  N N 206 
HIS   CB   C  N N 207 
HIS   CG   C  Y N 208 
HIS   ND1  N  Y N 209 
HIS   CD2  C  Y N 210 
HIS   CE1  C  Y N 211 
HIS   NE2  N  Y N 212 
HIS   OXT  O  N N 213 
HIS   H    H  N N 214 
HIS   H2   H  N N 215 
HIS   HA   H  N N 216 
HIS   HB2  H  N N 217 
HIS   HB3  H  N N 218 
HIS   HD1  H  N N 219 
HIS   HD2  H  N N 220 
HIS   HE1  H  N N 221 
HIS   HE2  H  N N 222 
HIS   HXT  H  N N 223 
HOH   O    O  N N 224 
HOH   H1   H  N N 225 
HOH   H2   H  N N 226 
ILE   N    N  N N 227 
ILE   CA   C  N S 228 
ILE   C    C  N N 229 
ILE   O    O  N N 230 
ILE   CB   C  N S 231 
ILE   CG1  C  N N 232 
ILE   CG2  C  N N 233 
ILE   CD1  C  N N 234 
ILE   OXT  O  N N 235 
ILE   H    H  N N 236 
ILE   H2   H  N N 237 
ILE   HA   H  N N 238 
ILE   HB   H  N N 239 
ILE   HG12 H  N N 240 
ILE   HG13 H  N N 241 
ILE   HG21 H  N N 242 
ILE   HG22 H  N N 243 
ILE   HG23 H  N N 244 
ILE   HD11 H  N N 245 
ILE   HD12 H  N N 246 
ILE   HD13 H  N N 247 
ILE   HXT  H  N N 248 
LEU   N    N  N N 249 
LEU   CA   C  N S 250 
LEU   C    C  N N 251 
LEU   O    O  N N 252 
LEU   CB   C  N N 253 
LEU   CG   C  N N 254 
LEU   CD1  C  N N 255 
LEU   CD2  C  N N 256 
LEU   OXT  O  N N 257 
LEU   H    H  N N 258 
LEU   H2   H  N N 259 
LEU   HA   H  N N 260 
LEU   HB2  H  N N 261 
LEU   HB3  H  N N 262 
LEU   HG   H  N N 263 
LEU   HD11 H  N N 264 
LEU   HD12 H  N N 265 
LEU   HD13 H  N N 266 
LEU   HD21 H  N N 267 
LEU   HD22 H  N N 268 
LEU   HD23 H  N N 269 
LEU   HXT  H  N N 270 
LYS   N    N  N N 271 
LYS   CA   C  N S 272 
LYS   C    C  N N 273 
LYS   O    O  N N 274 
LYS   CB   C  N N 275 
LYS   CG   C  N N 276 
LYS   CD   C  N N 277 
LYS   CE   C  N N 278 
LYS   NZ   N  N N 279 
LYS   OXT  O  N N 280 
LYS   H    H  N N 281 
LYS   H2   H  N N 282 
LYS   HA   H  N N 283 
LYS   HB2  H  N N 284 
LYS   HB3  H  N N 285 
LYS   HG2  H  N N 286 
LYS   HG3  H  N N 287 
LYS   HD2  H  N N 288 
LYS   HD3  H  N N 289 
LYS   HE2  H  N N 290 
LYS   HE3  H  N N 291 
LYS   HZ1  H  N N 292 
LYS   HZ2  H  N N 293 
LYS   HZ3  H  N N 294 
LYS   HXT  H  N N 295 
MET   N    N  N N 296 
MET   CA   C  N S 297 
MET   C    C  N N 298 
MET   O    O  N N 299 
MET   CB   C  N N 300 
MET   CG   C  N N 301 
MET   SD   S  N N 302 
MET   CE   C  N N 303 
MET   OXT  O  N N 304 
MET   H    H  N N 305 
MET   H2   H  N N 306 
MET   HA   H  N N 307 
MET   HB2  H  N N 308 
MET   HB3  H  N N 309 
MET   HG2  H  N N 310 
MET   HG3  H  N N 311 
MET   HE1  H  N N 312 
MET   HE2  H  N N 313 
MET   HE3  H  N N 314 
MET   HXT  H  N N 315 
MN    MN   MN N N 316 
PHE   N    N  N N 317 
PHE   CA   C  N S 318 
PHE   C    C  N N 319 
PHE   O    O  N N 320 
PHE   CB   C  N N 321 
PHE   CG   C  Y N 322 
PHE   CD1  C  Y N 323 
PHE   CD2  C  Y N 324 
PHE   CE1  C  Y N 325 
PHE   CE2  C  Y N 326 
PHE   CZ   C  Y N 327 
PHE   OXT  O  N N 328 
PHE   H    H  N N 329 
PHE   H2   H  N N 330 
PHE   HA   H  N N 331 
PHE   HB2  H  N N 332 
PHE   HB3  H  N N 333 
PHE   HD1  H  N N 334 
PHE   HD2  H  N N 335 
PHE   HE1  H  N N 336 
PHE   HE2  H  N N 337 
PHE   HZ   H  N N 338 
PHE   HXT  H  N N 339 
PRO   N    N  N N 340 
PRO   CA   C  N S 341 
PRO   C    C  N N 342 
PRO   O    O  N N 343 
PRO   CB   C  N N 344 
PRO   CG   C  N N 345 
PRO   CD   C  N N 346 
PRO   OXT  O  N N 347 
PRO   H    H  N N 348 
PRO   HA   H  N N 349 
PRO   HB2  H  N N 350 
PRO   HB3  H  N N 351 
PRO   HG2  H  N N 352 
PRO   HG3  H  N N 353 
PRO   HD2  H  N N 354 
PRO   HD3  H  N N 355 
PRO   HXT  H  N N 356 
SER   N    N  N N 357 
SER   CA   C  N S 358 
SER   C    C  N N 359 
SER   O    O  N N 360 
SER   CB   C  N N 361 
SER   OG   O  N N 362 
SER   OXT  O  N N 363 
SER   H    H  N N 364 
SER   H2   H  N N 365 
SER   HA   H  N N 366 
SER   HB2  H  N N 367 
SER   HB3  H  N N 368 
SER   HG   H  N N 369 
SER   HXT  H  N N 370 
THR   N    N  N N 371 
THR   CA   C  N S 372 
THR   C    C  N N 373 
THR   O    O  N N 374 
THR   CB   C  N R 375 
THR   OG1  O  N N 376 
THR   CG2  C  N N 377 
THR   OXT  O  N N 378 
THR   H    H  N N 379 
THR   H2   H  N N 380 
THR   HA   H  N N 381 
THR   HB   H  N N 382 
THR   HG1  H  N N 383 
THR   HG21 H  N N 384 
THR   HG22 H  N N 385 
THR   HG23 H  N N 386 
THR   HXT  H  N N 387 
TRP   N    N  N N 388 
TRP   CA   C  N S 389 
TRP   C    C  N N 390 
TRP   O    O  N N 391 
TRP   CB   C  N N 392 
TRP   CG   C  Y N 393 
TRP   CD1  C  Y N 394 
TRP   CD2  C  Y N 395 
TRP   NE1  N  Y N 396 
TRP   CE2  C  Y N 397 
TRP   CE3  C  Y N 398 
TRP   CZ2  C  Y N 399 
TRP   CZ3  C  Y N 400 
TRP   CH2  C  Y N 401 
TRP   OXT  O  N N 402 
TRP   H    H  N N 403 
TRP   H2   H  N N 404 
TRP   HA   H  N N 405 
TRP   HB2  H  N N 406 
TRP   HB3  H  N N 407 
TRP   HD1  H  N N 408 
TRP   HE1  H  N N 409 
TRP   HE3  H  N N 410 
TRP   HZ2  H  N N 411 
TRP   HZ3  H  N N 412 
TRP   HH2  H  N N 413 
TRP   HXT  H  N N 414 
TYR   N    N  N N 415 
TYR   CA   C  N S 416 
TYR   C    C  N N 417 
TYR   O    O  N N 418 
TYR   CB   C  N N 419 
TYR   CG   C  Y N 420 
TYR   CD1  C  Y N 421 
TYR   CD2  C  Y N 422 
TYR   CE1  C  Y N 423 
TYR   CE2  C  Y N 424 
TYR   CZ   C  Y N 425 
TYR   OH   O  N N 426 
TYR   OXT  O  N N 427 
TYR   H    H  N N 428 
TYR   H2   H  N N 429 
TYR   HA   H  N N 430 
TYR   HB2  H  N N 431 
TYR   HB3  H  N N 432 
TYR   HD1  H  N N 433 
TYR   HD2  H  N N 434 
TYR   HE1  H  N N 435 
TYR   HE2  H  N N 436 
TYR   HH   H  N N 437 
TYR   HXT  H  N N 438 
VAL   N    N  N N 439 
VAL   CA   C  N S 440 
VAL   C    C  N N 441 
VAL   O    O  N N 442 
VAL   CB   C  N N 443 
VAL   CG1  C  N N 444 
VAL   CG2  C  N N 445 
VAL   OXT  O  N N 446 
VAL   H    H  N N 447 
VAL   H2   H  N N 448 
VAL   HA   H  N N 449 
VAL   HB   H  N N 450 
VAL   HG11 H  N N 451 
VAL   HG12 H  N N 452 
VAL   HG13 H  N N 453 
VAL   HG21 H  N N 454 
VAL   HG22 H  N N 455 
VAL   HG23 H  N N 456 
VAL   HXT  H  N N 457 
# 
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 
A1AVW C02 CL01 sing N N 1   
A1AVW N03 C02  doub Y N 2   
A1AVW C04 N03  sing Y N 3   
A1AVW C06 N05  sing N N 4   
A1AVW C07 C06  sing N N 5   
A1AVW N08 C07  sing N N 6   
A1AVW C10 C09  sing N N 7   
A1AVW C09 N08  sing N N 8   
A1AVW S11 N08  sing N N 9   
A1AVW O12 S11  doub N N 10  
A1AVW O13 S11  doub N N 11  
A1AVW C14 S11  sing N N 12  
A1AVW C15 C14  doub Y N 13  
A1AVW C16 C15  sing Y N 14  
A1AVW C17 C16  doub Y N 15  
A1AVW C19 C18  doub Y N 16  
A1AVW C18 C17  sing Y N 17  
A1AVW N20 C17  sing N N 18  
A1AVW C21 N20  sing N N 19  
A1AVW O22 C21  doub N N 20  
A1AVW C23 C21  sing N N 21  
A1AVW C24 C23  doub Y N 22  
A1AVW C26 N25  sing N N 23  
A1AVW S27 N25  sing N N 24  
A1AVW O28 S27  doub N N 25  
A1AVW O29 S27  doub N N 26  
A1AVW C30 S27  sing N N 27  
A1AVW N25 C24  sing N N 28  
A1AVW C31 C24  sing Y N 29  
A1AVW C32 C31  doub Y N 30  
A1AVW C33 C32  sing Y N 31  
A1AVW C34 C33  doub Y N 32  
A1AVW N05 C04  sing N N 33  
A1AVW C35 C04  doub Y N 34  
A1AVW C36 C35  sing Y N 35  
A1AVW C37 C36  doub Y N 36  
A1AVW C38 C36  sing N N 37  
A1AVW F39 C38  sing N N 38  
A1AVW F40 C38  sing N N 39  
A1AVW F41 C38  sing N N 40  
A1AVW C02 C37  sing Y N 41  
A1AVW N05 C10  sing N N 42  
A1AVW C14 C19  sing Y N 43  
A1AVW C23 C34  sing Y N 44  
A1AVW C10 H102 sing N N 45  
A1AVW C10 H101 sing N N 46  
A1AVW C15 H151 sing N N 47  
A1AVW C26 H262 sing N N 48  
A1AVW C26 H263 sing N N 49  
A1AVW C26 H261 sing N N 50  
A1AVW C06 H062 sing N N 51  
A1AVW C06 H061 sing N N 52  
A1AVW C07 H072 sing N N 53  
A1AVW C07 H071 sing N N 54  
A1AVW C09 H091 sing N N 55  
A1AVW C09 H092 sing N N 56  
A1AVW C16 H161 sing N N 57  
A1AVW C18 H181 sing N N 58  
A1AVW C19 H191 sing N N 59  
A1AVW C30 H301 sing N N 60  
A1AVW C30 H303 sing N N 61  
A1AVW C30 H302 sing N N 62  
A1AVW C31 H311 sing N N 63  
A1AVW C32 H321 sing N N 64  
A1AVW C33 H331 sing N N 65  
A1AVW C34 H341 sing N N 66  
A1AVW C35 H351 sing N N 67  
A1AVW C37 H371 sing N N 68  
A1AVW N20 H201 sing N N 69  
ALA   N   CA   sing N N 70  
ALA   N   H    sing N N 71  
ALA   N   H2   sing N N 72  
ALA   CA  C    sing N N 73  
ALA   CA  CB   sing N N 74  
ALA   CA  HA   sing N N 75  
ALA   C   O    doub N N 76  
ALA   C   OXT  sing N N 77  
ALA   CB  HB1  sing N N 78  
ALA   CB  HB2  sing N N 79  
ALA   CB  HB3  sing N N 80  
ALA   OXT HXT  sing N N 81  
ARG   N   CA   sing N N 82  
ARG   N   H    sing N N 83  
ARG   N   H2   sing N N 84  
ARG   CA  C    sing N N 85  
ARG   CA  CB   sing N N 86  
ARG   CA  HA   sing N N 87  
ARG   C   O    doub N N 88  
ARG   C   OXT  sing N N 89  
ARG   CB  CG   sing N N 90  
ARG   CB  HB2  sing N N 91  
ARG   CB  HB3  sing N N 92  
ARG   CG  CD   sing N N 93  
ARG   CG  HG2  sing N N 94  
ARG   CG  HG3  sing N N 95  
ARG   CD  NE   sing N N 96  
ARG   CD  HD2  sing N N 97  
ARG   CD  HD3  sing N N 98  
ARG   NE  CZ   sing N N 99  
ARG   NE  HE   sing N N 100 
ARG   CZ  NH1  sing N N 101 
ARG   CZ  NH2  doub N N 102 
ARG   NH1 HH11 sing N N 103 
ARG   NH1 HH12 sing N N 104 
ARG   NH2 HH21 sing N N 105 
ARG   NH2 HH22 sing N N 106 
ARG   OXT HXT  sing N N 107 
ASN   N   CA   sing N N 108 
ASN   N   H    sing N N 109 
ASN   N   H2   sing N N 110 
ASN   CA  C    sing N N 111 
ASN   CA  CB   sing N N 112 
ASN   CA  HA   sing N N 113 
ASN   C   O    doub N N 114 
ASN   C   OXT  sing N N 115 
ASN   CB  CG   sing N N 116 
ASN   CB  HB2  sing N N 117 
ASN   CB  HB3  sing N N 118 
ASN   CG  OD1  doub N N 119 
ASN   CG  ND2  sing N N 120 
ASN   ND2 HD21 sing N N 121 
ASN   ND2 HD22 sing N N 122 
ASN   OXT HXT  sing N N 123 
ASP   N   CA   sing N N 124 
ASP   N   H    sing N N 125 
ASP   N   H2   sing N N 126 
ASP   CA  C    sing N N 127 
ASP   CA  CB   sing N N 128 
ASP   CA  HA   sing N N 129 
ASP   C   O    doub N N 130 
ASP   C   OXT  sing N N 131 
ASP   CB  CG   sing N N 132 
ASP   CB  HB2  sing N N 133 
ASP   CB  HB3  sing N N 134 
ASP   CG  OD1  doub N N 135 
ASP   CG  OD2  sing N N 136 
ASP   OD2 HD2  sing N N 137 
ASP   OXT HXT  sing N N 138 
CYS   N   CA   sing N N 139 
CYS   N   H    sing N N 140 
CYS   N   H2   sing N N 141 
CYS   CA  C    sing N N 142 
CYS   CA  CB   sing N N 143 
CYS   CA  HA   sing N N 144 
CYS   C   O    doub N N 145 
CYS   C   OXT  sing N N 146 
CYS   CB  SG   sing N N 147 
CYS   CB  HB2  sing N N 148 
CYS   CB  HB3  sing N N 149 
CYS   SG  HG   sing N N 150 
CYS   OXT HXT  sing N N 151 
GLN   N   CA   sing N N 152 
GLN   N   H    sing N N 153 
GLN   N   H2   sing N N 154 
GLN   CA  C    sing N N 155 
GLN   CA  CB   sing N N 156 
GLN   CA  HA   sing N N 157 
GLN   C   O    doub N N 158 
GLN   C   OXT  sing N N 159 
GLN   CB  CG   sing N N 160 
GLN   CB  HB2  sing N N 161 
GLN   CB  HB3  sing N N 162 
GLN   CG  CD   sing N N 163 
GLN   CG  HG2  sing N N 164 
GLN   CG  HG3  sing N N 165 
GLN   CD  OE1  doub N N 166 
GLN   CD  NE2  sing N N 167 
GLN   NE2 HE21 sing N N 168 
GLN   NE2 HE22 sing N N 169 
GLN   OXT HXT  sing N N 170 
GLU   N   CA   sing N N 171 
GLU   N   H    sing N N 172 
GLU   N   H2   sing N N 173 
GLU   CA  C    sing N N 174 
GLU   CA  CB   sing N N 175 
GLU   CA  HA   sing N N 176 
GLU   C   O    doub N N 177 
GLU   C   OXT  sing N N 178 
GLU   CB  CG   sing N N 179 
GLU   CB  HB2  sing N N 180 
GLU   CB  HB3  sing N N 181 
GLU   CG  CD   sing N N 182 
GLU   CG  HG2  sing N N 183 
GLU   CG  HG3  sing N N 184 
GLU   CD  OE1  doub N N 185 
GLU   CD  OE2  sing N N 186 
GLU   OE2 HE2  sing N N 187 
GLU   OXT HXT  sing N N 188 
GLY   N   CA   sing N N 189 
GLY   N   H    sing N N 190 
GLY   N   H2   sing N N 191 
GLY   CA  C    sing N N 192 
GLY   CA  HA2  sing N N 193 
GLY   CA  HA3  sing N N 194 
GLY   C   O    doub N N 195 
GLY   C   OXT  sing N N 196 
GLY   OXT HXT  sing N N 197 
HIS   N   CA   sing N N 198 
HIS   N   H    sing N N 199 
HIS   N   H2   sing N N 200 
HIS   CA  C    sing N N 201 
HIS   CA  CB   sing N N 202 
HIS   CA  HA   sing N N 203 
HIS   C   O    doub N N 204 
HIS   C   OXT  sing N N 205 
HIS   CB  CG   sing N N 206 
HIS   CB  HB2  sing N N 207 
HIS   CB  HB3  sing N N 208 
HIS   CG  ND1  sing Y N 209 
HIS   CG  CD2  doub Y N 210 
HIS   ND1 CE1  doub Y N 211 
HIS   ND1 HD1  sing N N 212 
HIS   CD2 NE2  sing Y N 213 
HIS   CD2 HD2  sing N N 214 
HIS   CE1 NE2  sing Y N 215 
HIS   CE1 HE1  sing N N 216 
HIS   NE2 HE2  sing N N 217 
HIS   OXT HXT  sing N N 218 
HOH   O   H1   sing N N 219 
HOH   O   H2   sing N N 220 
ILE   N   CA   sing N N 221 
ILE   N   H    sing N N 222 
ILE   N   H2   sing N N 223 
ILE   CA  C    sing N N 224 
ILE   CA  CB   sing N N 225 
ILE   CA  HA   sing N N 226 
ILE   C   O    doub N N 227 
ILE   C   OXT  sing N N 228 
ILE   CB  CG1  sing N N 229 
ILE   CB  CG2  sing N N 230 
ILE   CB  HB   sing N N 231 
ILE   CG1 CD1  sing N N 232 
ILE   CG1 HG12 sing N N 233 
ILE   CG1 HG13 sing N N 234 
ILE   CG2 HG21 sing N N 235 
ILE   CG2 HG22 sing N N 236 
ILE   CG2 HG23 sing N N 237 
ILE   CD1 HD11 sing N N 238 
ILE   CD1 HD12 sing N N 239 
ILE   CD1 HD13 sing N N 240 
ILE   OXT HXT  sing N N 241 
LEU   N   CA   sing N N 242 
LEU   N   H    sing N N 243 
LEU   N   H2   sing N N 244 
LEU   CA  C    sing N N 245 
LEU   CA  CB   sing N N 246 
LEU   CA  HA   sing N N 247 
LEU   C   O    doub N N 248 
LEU   C   OXT  sing N N 249 
LEU   CB  CG   sing N N 250 
LEU   CB  HB2  sing N N 251 
LEU   CB  HB3  sing N N 252 
LEU   CG  CD1  sing N N 253 
LEU   CG  CD2  sing N N 254 
LEU   CG  HG   sing N N 255 
LEU   CD1 HD11 sing N N 256 
LEU   CD1 HD12 sing N N 257 
LEU   CD1 HD13 sing N N 258 
LEU   CD2 HD21 sing N N 259 
LEU   CD2 HD22 sing N N 260 
LEU   CD2 HD23 sing N N 261 
LEU   OXT HXT  sing N N 262 
LYS   N   CA   sing N N 263 
LYS   N   H    sing N N 264 
LYS   N   H2   sing N N 265 
LYS   CA  C    sing N N 266 
LYS   CA  CB   sing N N 267 
LYS   CA  HA   sing N N 268 
LYS   C   O    doub N N 269 
LYS   C   OXT  sing N N 270 
LYS   CB  CG   sing N N 271 
LYS   CB  HB2  sing N N 272 
LYS   CB  HB3  sing N N 273 
LYS   CG  CD   sing N N 274 
LYS   CG  HG2  sing N N 275 
LYS   CG  HG3  sing N N 276 
LYS   CD  CE   sing N N 277 
LYS   CD  HD2  sing N N 278 
LYS   CD  HD3  sing N N 279 
LYS   CE  NZ   sing N N 280 
LYS   CE  HE2  sing N N 281 
LYS   CE  HE3  sing N N 282 
LYS   NZ  HZ1  sing N N 283 
LYS   NZ  HZ2  sing N N 284 
LYS   NZ  HZ3  sing N N 285 
LYS   OXT HXT  sing N N 286 
MET   N   CA   sing N N 287 
MET   N   H    sing N N 288 
MET   N   H2   sing N N 289 
MET   CA  C    sing N N 290 
MET   CA  CB   sing N N 291 
MET   CA  HA   sing N N 292 
MET   C   O    doub N N 293 
MET   C   OXT  sing N N 294 
MET   CB  CG   sing N N 295 
MET   CB  HB2  sing N N 296 
MET   CB  HB3  sing N N 297 
MET   CG  SD   sing N N 298 
MET   CG  HG2  sing N N 299 
MET   CG  HG3  sing N N 300 
MET   SD  CE   sing N N 301 
MET   CE  HE1  sing N N 302 
MET   CE  HE2  sing N N 303 
MET   CE  HE3  sing N N 304 
MET   OXT HXT  sing N N 305 
PHE   N   CA   sing N N 306 
PHE   N   H    sing N N 307 
PHE   N   H2   sing N N 308 
PHE   CA  C    sing N N 309 
PHE   CA  CB   sing N N 310 
PHE   CA  HA   sing N N 311 
PHE   C   O    doub N N 312 
PHE   C   OXT  sing N N 313 
PHE   CB  CG   sing N N 314 
PHE   CB  HB2  sing N N 315 
PHE   CB  HB3  sing N N 316 
PHE   CG  CD1  doub Y N 317 
PHE   CG  CD2  sing Y N 318 
PHE   CD1 CE1  sing Y N 319 
PHE   CD1 HD1  sing N N 320 
PHE   CD2 CE2  doub Y N 321 
PHE   CD2 HD2  sing N N 322 
PHE   CE1 CZ   doub Y N 323 
PHE   CE1 HE1  sing N N 324 
PHE   CE2 CZ   sing Y N 325 
PHE   CE2 HE2  sing N N 326 
PHE   CZ  HZ   sing N N 327 
PHE   OXT HXT  sing N N 328 
PRO   N   CA   sing N N 329 
PRO   N   CD   sing N N 330 
PRO   N   H    sing N N 331 
PRO   CA  C    sing N N 332 
PRO   CA  CB   sing N N 333 
PRO   CA  HA   sing N N 334 
PRO   C   O    doub N N 335 
PRO   C   OXT  sing N N 336 
PRO   CB  CG   sing N N 337 
PRO   CB  HB2  sing N N 338 
PRO   CB  HB3  sing N N 339 
PRO   CG  CD   sing N N 340 
PRO   CG  HG2  sing N N 341 
PRO   CG  HG3  sing N N 342 
PRO   CD  HD2  sing N N 343 
PRO   CD  HD3  sing N N 344 
PRO   OXT HXT  sing N N 345 
SER   N   CA   sing N N 346 
SER   N   H    sing N N 347 
SER   N   H2   sing N N 348 
SER   CA  C    sing N N 349 
SER   CA  CB   sing N N 350 
SER   CA  HA   sing N N 351 
SER   C   O    doub N N 352 
SER   C   OXT  sing N N 353 
SER   CB  OG   sing N N 354 
SER   CB  HB2  sing N N 355 
SER   CB  HB3  sing N N 356 
SER   OG  HG   sing N N 357 
SER   OXT HXT  sing N N 358 
THR   N   CA   sing N N 359 
THR   N   H    sing N N 360 
THR   N   H2   sing N N 361 
THR   CA  C    sing N N 362 
THR   CA  CB   sing N N 363 
THR   CA  HA   sing N N 364 
THR   C   O    doub N N 365 
THR   C   OXT  sing N N 366 
THR   CB  OG1  sing N N 367 
THR   CB  CG2  sing N N 368 
THR   CB  HB   sing N N 369 
THR   OG1 HG1  sing N N 370 
THR   CG2 HG21 sing N N 371 
THR   CG2 HG22 sing N N 372 
THR   CG2 HG23 sing N N 373 
THR   OXT HXT  sing N N 374 
TRP   N   CA   sing N N 375 
TRP   N   H    sing N N 376 
TRP   N   H2   sing N N 377 
TRP   CA  C    sing N N 378 
TRP   CA  CB   sing N N 379 
TRP   CA  HA   sing N N 380 
TRP   C   O    doub N N 381 
TRP   C   OXT  sing N N 382 
TRP   CB  CG   sing N N 383 
TRP   CB  HB2  sing N N 384 
TRP   CB  HB3  sing N N 385 
TRP   CG  CD1  doub Y N 386 
TRP   CG  CD2  sing Y N 387 
TRP   CD1 NE1  sing Y N 388 
TRP   CD1 HD1  sing N N 389 
TRP   CD2 CE2  doub Y N 390 
TRP   CD2 CE3  sing Y N 391 
TRP   NE1 CE2  sing Y N 392 
TRP   NE1 HE1  sing N N 393 
TRP   CE2 CZ2  sing Y N 394 
TRP   CE3 CZ3  doub Y N 395 
TRP   CE3 HE3  sing N N 396 
TRP   CZ2 CH2  doub Y N 397 
TRP   CZ2 HZ2  sing N N 398 
TRP   CZ3 CH2  sing Y N 399 
TRP   CZ3 HZ3  sing N N 400 
TRP   CH2 HH2  sing N N 401 
TRP   OXT HXT  sing N N 402 
TYR   N   CA   sing N N 403 
TYR   N   H    sing N N 404 
TYR   N   H2   sing N N 405 
TYR   CA  C    sing N N 406 
TYR   CA  CB   sing N N 407 
TYR   CA  HA   sing N N 408 
TYR   C   O    doub N N 409 
TYR   C   OXT  sing N N 410 
TYR   CB  CG   sing N N 411 
TYR   CB  HB2  sing N N 412 
TYR   CB  HB3  sing N N 413 
TYR   CG  CD1  doub Y N 414 
TYR   CG  CD2  sing Y N 415 
TYR   CD1 CE1  sing Y N 416 
TYR   CD1 HD1  sing N N 417 
TYR   CD2 CE2  doub Y N 418 
TYR   CD2 HD2  sing N N 419 
TYR   CE1 CZ   doub Y N 420 
TYR   CE1 HE1  sing N N 421 
TYR   CE2 CZ   sing Y N 422 
TYR   CE2 HE2  sing N N 423 
TYR   CZ  OH   sing N N 424 
TYR   OH  HH   sing N N 425 
TYR   OXT HXT  sing N N 426 
VAL   N   CA   sing N N 427 
VAL   N   H    sing N N 428 
VAL   N   H2   sing N N 429 
VAL   CA  C    sing N N 430 
VAL   CA  CB   sing N N 431 
VAL   CA  HA   sing N N 432 
VAL   C   O    doub N N 433 
VAL   C   OXT  sing N N 434 
VAL   CB  CG1  sing N N 435 
VAL   CB  CG2  sing N N 436 
VAL   CB  HB   sing N N 437 
VAL   CG1 HG11 sing N N 438 
VAL   CG1 HG12 sing N N 439 
VAL   CG1 HG13 sing N N 440 
VAL   CG2 HG21 sing N N 441 
VAL   CG2 HG22 sing N N 442 
VAL   CG2 HG23 sing N N 443 
VAL   OXT HXT  sing N N 444 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           ? 
_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   6PJ3 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'P 32 2 1' 
_space_group.name_Hall        
;P 32 2"
;
_space_group.IT_number        154 
_space_group.crystal_system   trigonal 
_space_group.id               1 
# 
_atom_sites.entry_id                    9CD1 
_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]   0.009420 
_atom_sites.fract_transf_matrix[1][2]   0.005438 
_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]   0.010877 
_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]   0.018674 
_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 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C  ? ? 3.54356  2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
CL ? ? 9.50761  7.44341 ? ? 1.04373  23.83732 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
F  ? ? 4.90428  4.07044 ? ? 12.99538 1.63651  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
MN ? ? 20.23591 4.67902 ? ? 2.76514  44.01191 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N  ? ? 4.01032  2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O  ? ? 4.49882  3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S  ? ? 9.55732  6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
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 2   ? -31.40580 -43.36603 7.98326   1.000 24.39403 ? 2   ALA   A N    1 
ATOM   2    C  CA   . ALA   A 1 2   ? -30.62759 -42.16577 7.69360   1.000 25.86293 ? 2   ALA   A CA   1 
ATOM   3    C  C    . ALA   A 1 2   ? -31.45505 -40.90019 7.90615   1.000 24.86985 ? 2   ALA   A C    1 
ATOM   4    O  O    . ALA   A 1 2   ? -32.67595 -40.91396 7.75233   1.000 25.42843 ? 2   ALA   A O    1 
ATOM   5    C  CB   . ALA   A 1 2   ? -30.09546 -42.21357 6.27465   1.000 24.41135 ? 2   ALA   A CB   1 
ATOM   6    N  N    . THR   A 1 3   ? -30.78179 -39.80946 8.26226   1.000 20.55478 ? 3   THR   A N    1 
ATOM   7    C  CA   . THR   A 1 3   ? -31.41299 -38.51122 8.45503   1.000 19.26386 ? 3   THR   A CA   1 
ATOM   8    C  C    . THR   A 1 3   ? -30.91285 -37.55095 7.38463   1.000 22.34718 ? 3   THR   A C    1 
ATOM   9    O  O    . THR   A 1 3   ? -29.71001 -37.48978 7.10815   1.000 20.65687 ? 3   THR   A O    1 
ATOM   10   C  CB   . THR   A 1 3   ? -31.11165 -37.95348 9.85001   1.000 21.90789 ? 3   THR   A CB   1 
ATOM   11   O  OG1  . THR   A 1 3   ? -31.58217 -38.87383 10.84367  1.000 24.91545 ? 3   THR   A OG1  1 
ATOM   12   C  CG2  . THR   A 1 3   ? -31.78733 -36.59664 10.05269  1.000 19.23499 ? 3   THR   A CG2  1 
ATOM   13   N  N    . LEU   A 1 4   ? -31.83909 -36.80965 6.77964   1.000 20.55296 ? 4   LEU   A N    1 
ATOM   14   C  CA   . LEU   A 1 4   ? -31.54837 -35.96109 5.63181   1.000 19.40879 ? 4   LEU   A CA   1 
ATOM   15   C  C    . LEU   A 1 4   ? -31.58028 -34.49040 6.02417   1.000 22.78729 ? 4   LEU   A C    1 
ATOM   16   O  O    . LEU   A 1 4   ? -32.39033 -34.07553 6.86051   1.000 19.68652 ? 4   LEU   A O    1 
ATOM   17   C  CB   . LEU   A 1 4   ? -32.54782 -36.20572 4.49737   1.000 18.55542 ? 4   LEU   A CB   1 
ATOM   18   C  CG   . LEU   A 1 4   ? -32.66173 -37.63747 3.97635   1.000 24.89501 ? 4   LEU   A CG   1 
ATOM   19   C  CD1  . LEU   A 1 4   ? -33.64468 -37.69338 2.82082   1.000 24.11522 ? 4   LEU   A CD1  1 
ATOM   20   C  CD2  . LEU   A 1 4   ? -31.29878 -38.16415 3.55481   1.000 24.77379 ? 4   LEU   A CD2  1 
ATOM   21   N  N    . PHE   A 1 5   ? -30.70063 -33.70667 5.40149   1.000 20.31260 ? 5   PHE   A N    1 
ATOM   22   C  CA   . PHE   A 1 5   ? -30.61850 -32.26813 5.61394   1.000 18.90939 ? 5   PHE   A CA   1 
ATOM   23   C  C    . PHE   A 1 5   ? -30.56286 -31.57908 4.26104   1.000 20.16177 ? 5   PHE   A C    1 
ATOM   24   O  O    . PHE   A 1 5   ? -29.80750 -31.99922 3.37953   1.000 19.06085 ? 5   PHE   A O    1 
ATOM   25   C  CB   . PHE   A 1 5   ? -29.38601 -31.88843 6.44617   1.000 19.09155 ? 5   PHE   A CB   1 
ATOM   26   C  CG   . PHE   A 1 5   ? -29.37132 -32.49616 7.81749   1.000 21.42853 ? 5   PHE   A CG   1 
ATOM   27   C  CD1  . PHE   A 1 5   ? -28.91168 -33.78947 8.01242   1.000 18.81918 ? 5   PHE   A CD1  1 
ATOM   28   C  CD2  . PHE   A 1 5   ? -29.82290 -31.77704 8.91291   1.000 20.19504 ? 5   PHE   A CD2  1 
ATOM   29   C  CE1  . PHE   A 1 5   ? -28.90657 -34.35758 9.27492   1.000 21.80425 ? 5   PHE   A CE1  1 
ATOM   30   C  CE2  . PHE   A 1 5   ? -29.82018 -32.33951 10.17926  1.000 21.29207 ? 5   PHE   A CE2  1 
ATOM   31   C  CZ   . PHE   A 1 5   ? -29.36116 -33.62969 10.35959  1.000 19.91021 ? 5   PHE   A CZ   1 
ATOM   32   N  N    . ILE   A 1 6   ? -31.37296 -30.53252 4.09472   1.000 17.66068 ? 6   ILE   A N    1 
ATOM   33   C  CA   . ILE   A 1 6   ? -31.35773 -29.70364 2.89696   1.000 19.16288 ? 6   ILE   A CA   1 
ATOM   34   C  C    . ILE   A 1 6   ? -31.50370 -28.25333 3.33015   1.000 16.58353 ? 6   ILE   A C    1 
ATOM   35   O  O    . ILE   A 1 6   ? -31.93700 -27.95568 4.44507   1.000 17.67271 ? 6   ILE   A O    1 
ATOM   36   C  CB   . ILE   A 1 6   ? -32.47689 -30.06740 1.89242   1.000 18.70880 ? 6   ILE   A CB   1 
ATOM   37   C  CG1  . ILE   A 1 6   ? -33.85232 -29.81897 2.51649   1.000 19.23990 ? 6   ILE   A CG1  1 
ATOM   38   C  CG2  . ILE   A 1 6   ? -32.33987 -31.50716 1.40799   1.000 21.66524 ? 6   ILE   A CG2  1 
ATOM   39   C  CD1  . ILE   A 1 6   ? -35.01225 -30.11472 1.58307   1.000 17.70739 ? 6   ILE   A CD1  1 
ATOM   40   N  N    . ALA   A 1 7   ? -31.14657 -27.34672 2.42519   1.000 17.38925 ? 7   ALA   A N    1 
ATOM   41   C  CA   . ALA   A 1 7   ? -31.26506 -25.91748 2.68685   1.000 18.36470 ? 7   ALA   A CA   1 
ATOM   42   C  C    . ALA   A 1 7   ? -31.06123 -25.16335 1.38164   1.000 19.23288 ? 7   ALA   A C    1 
ATOM   43   O  O    . ALA   A 1 7   ? -30.61874 -25.72520 0.37529   1.000 18.42122 ? 7   ALA   A O    1 
ATOM   44   C  CB   . ALA   A 1 7   ? -30.25778 -25.44445 3.74029   1.000 17.77565 ? 7   ALA   A CB   1 
ATOM   45   N  N    . ASP   A 1 8   ? -31.39911 -23.87468 1.41805   1.000 18.59222 ? 8   ASP   A N    1 
ATOM   46   C  CA   . ASP   A 1 8   ? -31.08995 -22.93961 0.33862   1.000 18.95556 ? 8   ASP   A CA   1 
ATOM   47   C  C    . ASP   A 1 8   ? -31.68774 -23.38906 -0.99254  1.000 19.36191 ? 8   ASP   A C    1 
ATOM   48   O  O    . ASP   A 1 8   ? -31.03629 -23.33982 -2.03879  1.000 18.45327 ? 8   ASP   A O    1 
ATOM   49   C  CB   . ASP   A 1 8   ? -29.58014 -22.73119 0.23003   1.000 20.07892 ? 8   ASP   A CB   1 
ATOM   50   C  CG   . ASP   A 1 8   ? -28.99480 -22.13057 1.49166   1.000 21.21559 ? 8   ASP   A CG   1 
ATOM   51   O  OD1  . ASP   A 1 8   ? -29.30144 -20.95508 1.78927   1.000 22.41505 ? 8   ASP   A OD1  1 
ATOM   52   O  OD2  . ASP   A 1 8   ? -28.24554 -22.83854 2.19633   1.000 23.32577 ? 8   ASP   A OD2  1 
ATOM   53   N  N    . LEU   A 1 9   ? -32.94584 -23.83193 -0.94863  1.000 18.71229 ? 9   LEU   A N    1 
ATOM   54   C  CA   . LEU   A 1 9   ? -33.66663 -24.13885 -2.17794  1.000 19.50928 ? 9   LEU   A CA   1 
ATOM   55   C  C    . LEU   A 1 9   ? -34.13496 -22.86904 -2.87950  1.000 21.15698 ? 9   LEU   A C    1 
ATOM   56   O  O    . LEU   A 1 9   ? -34.19523 -22.83166 -4.11444  1.000 20.93142 ? 9   LEU   A O    1 
ATOM   57   C  CB   . LEU   A 1 9   ? -34.85452 -25.05077 -1.87177  1.000 20.19947 ? 9   LEU   A CB   1 
ATOM   58   C  CG   . LEU   A 1 9   ? -34.54464 -26.52819 -1.62168  1.000 24.05242 ? 9   LEU   A CG   1 
ATOM   59   C  CD1  . LEU   A 1 9   ? -34.10571 -26.77278 -0.18295  1.000 21.12650 ? 9   LEU   A CD1  1 
ATOM   60   C  CD2  . LEU   A 1 9   ? -35.76093 -27.37193 -1.95840  1.000 21.35171 ? 9   LEU   A CD2  1 
ATOM   61   N  N    . HIS   A 1 10  ? -34.46114 -21.82729 -2.11283  1.000 19.72412 ? 10  HIS   A N    1 
ATOM   62   C  CA   . HIS   A 1 10  ? -34.88858 -20.53635 -2.65317  1.000 20.99726 ? 10  HIS   A CA   1 
ATOM   63   C  C    . HIS   A 1 10  ? -36.04316 -20.70812 -3.63747  1.000 20.89036 ? 10  HIS   A C    1 
ATOM   64   O  O    . HIS   A 1 10  ? -36.02276 -20.18937 -4.75562  1.000 21.12367 ? 10  HIS   A O    1 
ATOM   65   C  CB   . HIS   A 1 10  ? -33.71411 -19.80162 -3.30557  1.000 22.77878 ? 10  HIS   A CB   1 
ATOM   66   C  CG   . HIS   A 1 10  ? -32.61465 -19.45232 -2.35083  1.000 23.45224 ? 10  HIS   A CG   1 
ATOM   67   N  ND1  . HIS   A 1 10  ? -32.57166 -18.25420 -1.67087  1.000 29.88948 ? 10  HIS   A ND1  1 
ATOM   68   C  CD2  . HIS   A 1 10  ? -31.51814 -20.14493 -1.96149  1.000 25.38934 ? 10  HIS   A CD2  1 
ATOM   69   C  CE1  . HIS   A 1 10  ? -31.49723 -18.22449 -0.90271  1.000 29.55379 ? 10  HIS   A CE1  1 
ATOM   70   N  NE2  . HIS   A 1 10  ? -30.84060 -19.35949 -1.06067  1.000 25.70805 ? 10  HIS   A NE2  1 
ATOM   71   N  N    . LEU   A 1 11  ? -37.05803 -21.45945 -3.21038  1.000 20.07960 ? 11  LEU   A N    1 
ATOM   72   C  CA   . LEU   A 1 11  ? -38.19651 -21.74091 -4.07580  1.000 19.99014 ? 11  LEU   A CA   1 
ATOM   73   C  C    . LEU   A 1 11  ? -38.93219 -20.45706 -4.43839  1.000 24.87118 ? 11  LEU   A C    1 
ATOM   74   O  O    . LEU   A 1 11  ? -39.13944 -19.57853 -3.59679  1.000 21.15398 ? 11  LEU   A O    1 
ATOM   75   C  CB   . LEU   A 1 11  ? -39.16025 -22.71646 -3.39630  1.000 18.92485 ? 11  LEU   A CB   1 
ATOM   76   C  CG   . LEU   A 1 11  ? -38.64933 -24.11778 -3.05199  1.000 23.52553 ? 11  LEU   A CG   1 
ATOM   77   C  CD1  . LEU   A 1 11  ? -39.67742 -24.86264 -2.21196  1.000 19.86371 ? 11  LEU   A CD1  1 
ATOM   78   C  CD2  . LEU   A 1 11  ? -38.30782 -24.90690 -4.30904  1.000 24.34320 ? 11  LEU   A CD2  1 
ATOM   79   N  N    . GLN   A 1 12  ? -39.33211 -20.36000 -5.70420  1.000 21.59823 ? 12  GLN   A N    1 
ATOM   80   C  CA   . GLN   A 1 12  ? -40.07384 -19.21350 -6.20726  1.000 25.84630 ? 12  GLN   A CA   1 
ATOM   81   C  C    . GLN   A 1 12  ? -40.80587 -19.64055 -7.46985  1.000 25.85979 ? 12  GLN   A C    1 
ATOM   82   O  O    . GLN   A 1 12  ? -40.36311 -20.54778 -8.17973  1.000 24.28278 ? 12  GLN   A O    1 
ATOM   83   C  CB   . GLN   A 1 12  ? -39.14813 -18.02572 -6.49358  1.000 26.10386 ? 12  GLN   A CB   1 
ATOM   84   C  CG   . GLN   A 1 12  ? -37.98170 -18.35965 -7.41143  1.000 23.07700 ? 12  GLN   A CG   1 
ATOM   85   C  CD   . GLN   A 1 12  ? -36.98348 -17.22241 -7.52782  1.000 30.51091 ? 12  GLN   A CD   1 
ATOM   86   O  OE1  . GLN   A 1 12  ? -35.79953 -17.39049 -7.23763  1.000 37.34863 ? 12  GLN   A OE1  1 
ATOM   87   N  NE2  . GLN   A 1 12  ? -37.45828 -16.05722 -7.94952  1.000 36.62935 ? 12  GLN   A NE2  1 
ATOM   88   N  N    . THR   A 1 13  ? -41.93058 -18.97469 -7.74463  1.000 26.71551 ? 13  THR   A N    1 
ATOM   89   C  CA   . THR   A 1 13  ? -42.74076 -19.35737 -8.89718  1.000 26.57747 ? 13  THR   A CA   1 
ATOM   90   C  C    . THR   A 1 13  ? -41.99817 -19.14491 -10.21109 1.000 22.76744 ? 13  THR   A C    1 
ATOM   91   O  O    . THR   A 1 13  ? -42.30210 -19.81201 -11.20573 1.000 25.61086 ? 13  THR   A O    1 
ATOM   92   C  CB   . THR   A 1 13  ? -44.05861 -18.58113 -8.90328  1.000 34.31657 ? 13  THR   A CB   1 
ATOM   93   O  OG1  . THR   A 1 13  ? -43.79932 -17.19330 -8.66135  1.000 30.93527 ? 13  THR   A OG1  1 
ATOM   94   C  CG2  . THR   A 1 13  ? -44.99636 -19.11444 -7.82637  1.000 28.63905 ? 13  THR   A CG2  1 
ATOM   95   N  N    . GLU   A 1 14  ? -41.02455 -18.23163 -10.23859 1.000 26.93006 ? 14  GLU   A N    1 
ATOM   96   C  CA   . GLU   A 1 14  ? -40.25153 -17.99390 -11.45245 1.000 28.29902 ? 14  GLU   A CA   1 
ATOM   97   C  C    . GLU   A 1 14  ? -39.24887 -19.10364 -11.74899 1.000 27.23802 ? 14  GLU   A C    1 
ATOM   98   O  O    . GLU   A 1 14  ? -38.64261 -19.09190 -12.82671 1.000 32.99011 ? 14  GLU   A O    1 
ATOM   99   C  CB   . GLU   A 1 14  ? -39.51017 -16.65721 -11.35888 1.000 29.75969 ? 14  GLU   A CB   1 
ATOM   100  C  CG   . GLU   A 1 14  ? -40.40947 -15.42946 -11.36623 1.000 41.64303 ? 14  GLU   A CG   1 
ATOM   101  C  CD   . GLU   A 1 14  ? -40.91881 -15.06581 -9.98296  1.000 48.52355 ? 14  GLU   A CD   1 
ATOM   102  O  OE1  . GLU   A 1 14  ? -41.69342 -14.09185 -9.87133  1.000 53.79670 ? 14  GLU   A OE1  1 
ATOM   103  O  OE2  . GLU   A 1 14  ? -40.54149 -15.74892 -9.00750  1.000 50.02487 ? 14  GLU   A OE2  1 
ATOM   104  N  N    . GLU   A 1 15  ? -39.05342 -20.05265 -10.83128 1.000 24.51097 ? 15  GLU   A N    1 
ATOM   105  C  CA   . GLU   A 1 15  ? -38.11579 -21.16007 -11.01128 1.000 27.27138 ? 15  GLU   A CA   1 
ATOM   106  C  C    . GLU   A 1 15  ? -38.86198 -22.48024 -10.83878 1.000 25.68584 ? 15  GLU   A C    1 
ATOM   107  O  O    . GLU   A 1 15  ? -38.64399 -23.20393 -9.85737  1.000 25.89758 ? 15  GLU   A O    1 
ATOM   108  C  CB   . GLU   A 1 15  ? -36.95288 -21.06730 -10.02356 1.000 27.56367 ? 15  GLU   A CB   1 
ATOM   109  C  CG   . GLU   A 1 15  ? -36.02306 -19.87500 -10.22787 1.000 27.62055 ? 15  GLU   A CG   1 
ATOM   110  C  CD   . GLU   A 1 15  ? -35.30291 -19.90790 -11.56189 1.000 38.92425 ? 15  GLU   A CD   1 
ATOM   111  O  OE1  . GLU   A 1 15  ? -35.06321 -21.01568 -12.08528 1.000 35.38760 ? 15  GLU   A OE1  1 
ATOM   112  O  OE2  . GLU   A 1 15  ? -34.97221 -18.82385 -12.08663 1.000 45.37631 ? 15  GLU   A OE2  1 
ATOM   113  N  N    . PRO   A 1 16  ? -39.74368 -22.83029 -11.77997 1.000 26.53292 ? 16  PRO   A N    1 
ATOM   114  C  CA   . PRO   A 1 16  ? -40.54503 -24.05406 -11.60703 1.000 26.39545 ? 16  PRO   A CA   1 
ATOM   115  C  C    . PRO   A 1 16  ? -39.72090 -25.33046 -11.61766 1.000 28.26005 ? 16  PRO   A C    1 
ATOM   116  O  O    . PRO   A 1 16  ? -40.17199 -26.34217 -11.06606 1.000 28.57067 ? 16  PRO   A O    1 
ATOM   117  C  CB   . PRO   A 1 16  ? -41.52025 -24.00727 -12.79155 1.000 29.04612 ? 16  PRO   A CB   1 
ATOM   118  C  CG   . PRO   A 1 16  ? -40.82860 -23.17101 -13.81740 1.000 29.26339 ? 16  PRO   A CG   1 
ATOM   119  C  CD   . PRO   A 1 16  ? -40.03225 -22.15225 -13.05657 1.000 29.64974 ? 16  PRO   A CD   1 
ATOM   120  N  N    . ALA   A 1 17  ? -38.52953 -25.31845 -12.22197 1.000 27.32243 ? 17  ALA   A N    1 
ATOM   121  C  CA   . ALA   A 1 17  ? -37.71004 -26.52644 -12.26112 1.000 28.54295 ? 17  ALA   A CA   1 
ATOM   122  C  C    . ALA   A 1 17  ? -37.24179 -26.92477 -10.86692 1.000 29.36164 ? 17  ALA   A C    1 
ATOM   123  O  O    . ALA   A 1 17  ? -37.20047 -28.11622 -10.53632 1.000 27.27491 ? 17  ALA   A O    1 
ATOM   124  C  CB   . ALA   A 1 17  ? -36.51452 -26.32381 -13.19157 1.000 27.10090 ? 17  ALA   A CB   1 
ATOM   125  N  N    . ILE   A 1 18  ? -36.88292 -25.94268 -10.03500 1.000 26.49489 ? 18  ILE   A N    1 
ATOM   126  C  CA   . ILE   A 1 18  ? -36.47457 -26.24538 -8.66590  1.000 26.39833 ? 18  ILE   A CA   1 
ATOM   127  C  C    . ILE   A 1 18  ? -37.64869 -26.79885 -7.87022  1.000 29.62107 ? 18  ILE   A C    1 
ATOM   128  O  O    . ILE   A 1 18  ? -37.49604 -27.74888 -7.09204  1.000 25.54000 ? 18  ILE   A O    1 
ATOM   129  C  CB   . ILE   A 1 18  ? -35.87806 -24.99773 -7.99069  1.000 32.21427 ? 18  ILE   A CB   1 
ATOM   130  C  CG1  . ILE   A 1 18  ? -34.78600 -24.38161 -8.86550  1.000 34.10098 ? 18  ILE   A CG1  1 
ATOM   131  C  CG2  . ILE   A 1 18  ? -35.32745 -25.34976 -6.61541  1.000 25.32491 ? 18  ILE   A CG2  1 
ATOM   132  C  CD1  . ILE   A 1 18  ? -34.25312 -23.07351 -8.33023  1.000 34.95547 ? 18  ILE   A CD1  1 
ATOM   133  N  N    . THR   A 1 19  ? -38.83519 -26.20962 -8.04510  1.000 23.33698 ? 19  THR   A N    1 
ATOM   134  C  CA   . THR   A 1 19  ? -40.02890 -26.73460 -7.39075  1.000 26.89240 ? 19  THR   A CA   1 
ATOM   135  C  C    . THR   A 1 19  ? -40.29779 -28.17175 -7.81869  1.000 24.92647 ? 19  THR   A C    1 
ATOM   136  O  O    . THR   A 1 19  ? -40.59806 -29.03044 -6.98156  1.000 24.88252 ? 19  THR   A O    1 
ATOM   137  C  CB   . THR   A 1 19  ? -41.23502 -25.84713 -7.70518  1.000 26.19988 ? 19  THR   A CB   1 
ATOM   138  O  OG1  . THR   A 1 19  ? -41.00757 -24.52734 -7.19631  1.000 25.60855 ? 19  THR   A OG1  1 
ATOM   139  C  CG2  . THR   A 1 19  ? -42.50459 -26.41793 -7.07763  1.000 23.78353 ? 19  THR   A CG2  1 
ATOM   140  N  N    . ALA   A 1 20  ? -40.18010 -28.45417 -9.11938  1.000 25.21976 ? 20  ALA   A N    1 
ATOM   141  C  CA   . ALA   A 1 20  ? -40.37603 -29.81676 -9.60455  1.000 28.49685 ? 20  ALA   A CA   1 
ATOM   142  C  C    . ALA   A 1 20  ? -39.35828 -30.77195 -8.99382  1.000 26.53521 ? 20  ALA   A C    1 
ATOM   143  O  O    . ALA   A 1 20  ? -39.70154 -31.89812 -8.61558  1.000 27.24883 ? 20  ALA   A O    1 
ATOM   144  C  CB   . ALA   A 1 20  ? -40.29436 -29.84755 -11.13096 1.000 26.13262 ? 20  ALA   A CB   1 
ATOM   145  N  N    . GLY   A 1 21  ? -38.10187 -30.33767 -8.88165  1.000 28.77058 ? 21  GLY   A N    1 
ATOM   146  C  CA   . GLY   A 1 21  ? -37.08835 -31.19270 -8.28670  1.000 25.72318 ? 21  GLY   A CA   1 
ATOM   147  C  C    . GLY   A 1 21  ? -37.34846 -31.47123 -6.81938  1.000 24.56935 ? 21  GLY   A C    1 
ATOM   148  O  O    . GLY   A 1 21  ? -37.12044 -32.58404 -6.33836  1.000 23.91584 ? 21  GLY   A O    1 
ATOM   149  N  N    . PHE   A 1 22  ? -37.83763 -30.46659 -6.08974  1.000 20.95775 ? 22  PHE   A N    1 
ATOM   150  C  CA   . PHE   A 1 22  ? -38.11267 -30.65227 -4.66939  1.000 22.81685 ? 22  PHE   A CA   1 
ATOM   151  C  C    . PHE   A 1 22  ? -39.29703 -31.58834 -4.45381  1.000 24.10668 ? 22  PHE   A C    1 
ATOM   152  O  O    . PHE   A 1 22  ? -39.28832 -32.40309 -3.52306  1.000 22.99368 ? 22  PHE   A O    1 
ATOM   153  C  CB   . PHE   A 1 22  ? -38.35551 -29.29560 -4.00485  1.000 19.83488 ? 22  PHE   A CB   1 
ATOM   154  C  CG   . PHE   A 1 22  ? -38.57086 -29.37422 -2.51885  1.000 19.36737 ? 22  PHE   A CG   1 
ATOM   155  C  CD1  . PHE   A 1 22  ? -37.79264 -30.21239 -1.73545  1.000 20.44620 ? 22  PHE   A CD1  1 
ATOM   156  C  CD2  . PHE   A 1 22  ? -39.54107 -28.59625 -1.90225  1.000 21.85184 ? 22  PHE   A CD2  1 
ATOM   157  C  CE1  . PHE   A 1 22  ? -37.98491 -30.28463 -0.36402  1.000 19.45750 ? 22  PHE   A CE1  1 
ATOM   158  C  CE2  . PHE   A 1 22  ? -39.73924 -28.66125 -0.53122  1.000 22.16175 ? 22  PHE   A CE2  1 
ATOM   159  C  CZ   . PHE   A 1 22  ? -38.95962 -29.50747 0.23935   1.000 22.82447 ? 22  PHE   A CZ   1 
ATOM   160  N  N    . LEU   A 1 23  ? -40.32075 -31.49731 -5.30800  1.000 23.15828 ? 23  LEU   A N    1 
ATOM   161  C  CA   . LEU   A 1 23  ? -41.45515 -32.40976 -5.19105  1.000 26.81951 ? 23  LEU   A CA   1 
ATOM   162  C  C    . LEU   A 1 23  ? -41.03948 -33.84858 -5.47801  1.000 26.20889 ? 23  LEU   A C    1 
ATOM   163  O  O    . LEU   A 1 23  ? -41.51675 -34.78219 -4.82237  1.000 27.89961 ? 23  LEU   A O    1 
ATOM   164  C  CB   . LEU   A 1 23  ? -42.58263 -31.98040 -6.13042  1.000 25.99156 ? 23  LEU   A CB   1 
ATOM   165  C  CG   . LEU   A 1 23  ? -43.16138 -30.57503 -5.94620  1.000 31.72155 ? 23  LEU   A CG   1 
ATOM   166  C  CD1  . LEU   A 1 23  ? -44.14117 -30.23949 -7.06473  1.000 31.09189 ? 23  LEU   A CD1  1 
ATOM   167  C  CD2  . LEU   A 1 23  ? -43.81947 -30.43013 -4.58820  1.000 25.68524 ? 23  LEU   A CD2  1 
ATOM   168  N  N    . ARG   A 1 24  ? -40.15734 -34.04975 -6.46101  1.000 25.44773 ? 24  ARG   A N    1 
ATOM   169  C  CA   . ARG   A 1 24  ? -39.64168 -35.39065 -6.72318  1.000 28.32863 ? 24  ARG   A CA   1 
ATOM   170  C  C    . ARG   A 1 24  ? -38.84652 -35.91181 -5.53254  1.000 27.86007 ? 24  ARG   A C    1 
ATOM   171  O  O    . ARG   A 1 24  ? -38.94826 -37.09125 -5.17330  1.000 30.77672 ? 24  ARG   A O    1 
ATOM   172  C  CB   . ARG   A 1 24  ? -38.77596 -35.38670 -7.98425  1.000 32.25258 ? 24  ARG   A CB   1 
ATOM   173  C  CG   . ARG   A 1 24  ? -38.03450 -36.69403 -8.23067  1.000 39.14122 ? 24  ARG   A CG   1 
ATOM   174  C  CD   . ARG   A 1 24  ? -37.41257 -36.73915 -9.61907  1.000 47.41708 ? 24  ARG   A CD   1 
ATOM   175  N  NE   . ARG   A 1 24  ? -35.98367 -36.44676 -9.59115  1.000 47.13361 ? 24  ARG   A NE   1 
ATOM   176  C  CZ   . ARG   A 1 24  ? -35.04453 -37.32748 -9.27217  1.000 55.37584 ? 24  ARG   A CZ   1 
ATOM   177  N  NH1  . ARG   A 1 24  ? -35.34709 -38.57325 -8.94566  1.000 52.01221 ? 24  ARG   A NH1  1 
ATOM   178  N  NH2  . ARG   A 1 24  ? -33.76923 -36.94926 -9.28208  1.000 52.70980 ? 24  ARG   A NH2  1 
ATOM   179  N  N    . PHE   A 1 25  ? -38.04939 -35.04158 -4.90826  1.000 25.70243 ? 25  PHE   A N    1 
ATOM   180  C  CA   . PHE   A 1 25  ? -37.29812 -35.42826 -3.71859  1.000 27.93190 ? 25  PHE   A CA   1 
ATOM   181  C  C    . PHE   A 1 25  ? -38.23302 -35.82746 -2.58245  1.000 28.50115 ? 25  PHE   A C    1 
ATOM   182  O  O    . PHE   A 1 25  ? -38.00149 -36.83236 -1.89974  1.000 26.71476 ? 25  PHE   A O    1 
ATOM   183  C  CB   . PHE   A 1 25  ? -36.38544 -34.27358 -3.29786  1.000 24.57631 ? 25  PHE   A CB   1 
ATOM   184  C  CG   . PHE   A 1 25  ? -35.75789 -34.44575 -1.94384  1.000 22.65860 ? 25  PHE   A CG   1 
ATOM   185  C  CD1  . PHE   A 1 25  ? -34.60442 -35.20027 -1.79102  1.000 28.24082 ? 25  PHE   A CD1  1 
ATOM   186  C  CD2  . PHE   A 1 25  ? -36.30529 -33.83053 -0.82789  1.000 22.86175 ? 25  PHE   A CD2  1 
ATOM   187  C  CE1  . PHE   A 1 25  ? -34.01678 -35.35295 -0.54703  1.000 23.70350 ? 25  PHE   A CE1  1 
ATOM   188  C  CE2  . PHE   A 1 25  ? -35.72464 -33.97944 0.41966   1.000 25.90012 ? 25  PHE   A CE2  1 
ATOM   189  C  CZ   . PHE   A 1 25  ? -34.57740 -34.74142 0.56004   1.000 23.62566 ? 25  PHE   A CZ   1 
ATOM   190  N  N    . LEU   A 1 26  ? -39.29950 -35.05264 -2.36924  1.000 24.05116 ? 26  LEU   A N    1 
ATOM   191  C  CA   . LEU   A 1 26  ? -40.24389 -35.36219 -1.30090  1.000 26.41793 ? 26  LEU   A CA   1 
ATOM   192  C  C    . LEU   A 1 26  ? -40.99325 -36.65854 -1.58326  1.000 26.93558 ? 26  LEU   A C    1 
ATOM   193  O  O    . LEU   A 1 26  ? -41.29975 -37.41939 -0.65843  1.000 27.76792 ? 26  LEU   A O    1 
ATOM   194  C  CB   . LEU   A 1 26  ? -41.22408 -34.20309 -1.12371  1.000 22.35456 ? 26  LEU   A CB   1 
ATOM   195  C  CG   . LEU   A 1 26  ? -40.65602 -32.91129 -0.53076  1.000 20.48675 ? 26  LEU   A CG   1 
ATOM   196  C  CD1  . LEU   A 1 26  ? -41.70620 -31.80791 -0.53842  1.000 21.45065 ? 26  LEU   A CD1  1 
ATOM   197  C  CD2  . LEU   A 1 26  ? -40.13558 -33.14896 0.88066   1.000 18.65733 ? 26  LEU   A CD2  1 
ATOM   198  N  N    . GLN   A 1 27  ? -41.29423 -36.92793 -2.85497  1.000 28.04291 ? 27  GLN   A N    1 
ATOM   199  C  CA   . GLN   A 1 27  ? -42.03525 -38.12762 -3.22153  1.000 31.92067 ? 27  GLN   A CA   1 
ATOM   200  C  C    . GLN   A 1 27  ? -41.17934 -39.38598 -3.18664  1.000 31.59409 ? 27  GLN   A C    1 
ATOM   201  O  O    . GLN   A 1 27  ? -41.72817 -40.48700 -3.07095  1.000 38.36215 ? 27  GLN   A O    1 
ATOM   202  C  CB   . GLN   A 1 27  ? -42.64082 -37.96349 -4.61652  1.000 39.30913 ? 27  GLN   A CB   1 
ATOM   203  C  CG   . GLN   A 1 27  ? -43.99436 -37.27587 -4.63132  1.000 43.72825 ? 27  GLN   A CG   1 
ATOM   204  C  CD   . GLN   A 1 27  ? -44.22675 -36.48469 -5.90305  1.000 52.66339 ? 27  GLN   A CD   1 
ATOM   205  O  OE1  . GLN   A 1 27  ? -44.93100 -35.47464 -5.90055  1.000 54.02279 ? 27  GLN   A OE1  1 
ATOM   206  N  NE2  . GLN   A 1 27  ? -43.63155 -36.93986 -6.99935  1.000 54.51824 ? 27  GLN   A NE2  1 
ATOM   207  N  N    . GLY   A 1 28  ? -39.85826 -39.25339 -3.28156  1.000 29.59447 ? 28  GLY   A N    1 
ATOM   208  C  CA   . GLY   A 1 28  ? -38.99346 -40.41525 -3.34223  1.000 33.03814 ? 28  GLY   A CA   1 
ATOM   209  C  C    . GLY   A 1 28  ? -38.06734 -40.57230 -2.15459  1.000 32.45505 ? 28  GLY   A C    1 
ATOM   210  O  O    . GLY   A 1 28  ? -38.38563 -41.29306 -1.20351  1.000 36.48500 ? 28  GLY   A O    1 
ATOM   211  N  N    . GLU   A 1 29  ? -36.91790 -39.89345 -2.20522  1.000 32.93771 ? 29  GLU   A N    1 
ATOM   212  C  CA   . GLU   A 1 29  ? -35.88663 -40.06383 -1.18392  1.000 36.82293 ? 29  GLU   A CA   1 
ATOM   213  C  C    . GLU   A 1 29  ? -36.41508 -39.76221 0.21296   1.000 31.41823 ? 29  GLU   A C    1 
ATOM   214  O  O    . GLU   A 1 29  ? -36.15046 -40.50986 1.16194   1.000 30.83127 ? 29  GLU   A O    1 
ATOM   215  C  CB   . GLU   A 1 29  ? -34.68685 -39.17083 -1.50333  1.000 34.92930 ? 29  GLU   A CB   1 
ATOM   216  C  CG   . GLU   A 1 29  ? -33.55728 -39.26952 -0.48967  1.000 40.78908 ? 29  GLU   A CG   1 
ATOM   217  C  CD   . GLU   A 1 29  ? -32.61484 -40.42403 -0.76645  1.000 44.66082 ? 29  GLU   A CD   1 
ATOM   218  O  OE1  . GLU   A 1 29  ? -32.39643 -40.74833 -1.95288  1.000 48.22447 ? 29  GLU   A OE1  1 
ATOM   219  O  OE2  . GLU   A 1 29  ? -32.08681 -41.00511 0.20389   1.000 49.87271 ? 29  GLU   A OE2  1 
ATOM   220  N  N    . ALA   A 1 30  ? -37.16159 -38.66443 0.35847   1.000 31.26459 ? 30  ALA   A N    1 
ATOM   221  C  CA   . ALA   A 1 30  ? -37.57147 -38.21261 1.68506   1.000 26.68645 ? 30  ALA   A CA   1 
ATOM   222  C  C    . ALA   A 1 30  ? -38.43409 -39.24311 2.40359   1.000 28.16578 ? 30  ALA   A C    1 
ATOM   223  O  O    . ALA   A 1 30  ? -38.40241 -39.32292 3.63722   1.000 24.42837 ? 30  ALA   A O    1 
ATOM   224  C  CB   . ALA   A 1 30  ? -38.31773 -36.88211 1.57799   1.000 27.35887 ? 30  ALA   A CB   1 
ATOM   225  N  N    . ARG   A 1 31  ? -39.19995 -40.04369 1.65689   1.000 24.50999 ? 31  ARG   A N    1 
ATOM   226  C  CA   . ARG   A 1 31  ? -40.09848 -41.01248 2.27458   1.000 29.77482 ? 31  ARG   A CA   1 
ATOM   227  C  C    . ARG   A 1 31  ? -39.35192 -42.11469 3.01504   1.000 32.38444 ? 31  ARG   A C    1 
ATOM   228  O  O    . ARG   A 1 31  ? -39.92797 -42.74073 3.91063   1.000 27.25077 ? 31  ARG   A O    1 
ATOM   229  C  CB   . ARG   A 1 31  ? -41.01191 -41.63548 1.21718   1.000 30.43358 ? 31  ARG   A CB   1 
ATOM   230  C  CG   . ARG   A 1 31  ? -41.77931 -40.62776 0.37663   1.000 33.18548 ? 31  ARG   A CG   1 
ATOM   231  C  CD   . ARG   A 1 31  ? -42.74792 -39.81396 1.21612   1.000 32.46519 ? 31  ARG   A CD   1 
ATOM   232  N  NE   . ARG   A 1 31  ? -43.52065 -38.89092 0.39340   1.000 37.03645 ? 31  ARG   A NE   1 
ATOM   233  C  CZ   . ARG   A 1 31  ? -44.76898 -39.10455 0.00101   1.000 35.70785 ? 31  ARG   A CZ   1 
ATOM   234  N  NH1  . ARG   A 1 31  ? -45.42859 -40.19495 0.35730   1.000 32.61546 ? 31  ARG   A NH1  1 
ATOM   235  N  NH2  . ARG   A 1 31  ? -45.37002 -38.20271 -0.76958  1.000 33.97663 ? 31  ARG   A NH2  1 
ATOM   236  N  N    . GLN   A 1 32  ? -38.09240 -42.36662 2.66729   1.000 29.80798 ? 32  GLN   A N    1 
ATOM   237  C  CA   . GLN   A 1 32  ? -37.31484 -43.42977 3.28929   1.000 36.72240 ? 32  GLN   A CA   1 
ATOM   238  C  C    . GLN   A 1 32  ? -36.47471 -42.94432 4.46270   1.000 30.93755 ? 32  GLN   A C    1 
ATOM   239  O  O    . GLN   A 1 32  ? -35.81115 -43.76089 5.10972   1.000 30.49409 ? 32  GLN   A O    1 
ATOM   240  C  CB   . GLN   A 1 32  ? -36.40661 -44.09318 2.24796   1.000 39.73421 ? 32  GLN   A CB   1 
ATOM   241  C  CG   . GLN   A 1 32  ? -37.07049 -44.31590 0.89890   1.000 39.71427 ? 32  GLN   A CG   1 
ATOM   242  C  CD   . GLN   A 1 32  ? -38.20442 -45.32025 0.96495   1.000 50.85153 ? 32  GLN   A CD   1 
ATOM   243  O  OE1  . GLN   A 1 32  ? -38.16219 -46.27376 1.74303   1.000 58.12603 ? 32  GLN   A OE1  1 
ATOM   244  N  NE2  . GLN   A 1 32  ? -39.23059 -45.10673 0.14932   1.000 54.51696 ? 32  GLN   A NE2  1 
ATOM   245  N  N    . ALA   A 1 33  ? -36.49605 -41.64910 4.75867   1.000 26.08750 ? 33  ALA   A N    1 
ATOM   246  C  CA   . ALA   A 1 33  ? -35.63235 -41.09043 5.78524   1.000 26.78155 ? 33  ALA   A CA   1 
ATOM   247  C  C    . ALA   A 1 33  ? -36.22503 -41.29000 7.17544   1.000 31.33722 ? 33  ALA   A C    1 
ATOM   248  O  O    . ALA   A 1 33  ? -37.43926 -41.44067 7.34622   1.000 26.30928 ? 33  ALA   A O    1 
ATOM   249  C  CB   . ALA   A 1 33  ? -35.40172 -39.60046 5.53327   1.000 23.89074 ? 33  ALA   A CB   1 
ATOM   250  N  N    . ASP   A 1 34  ? -35.34220 -41.29779 8.17757   1.000 25.05589 ? 34  ASP   A N    1 
ATOM   251  C  CA   . ASP   A 1 34  ? -35.79537 -41.26597 9.56365   1.000 24.49188 ? 34  ASP   A CA   1 
ATOM   252  C  C    . ASP   A 1 34  ? -36.37568 -39.90510 9.92308   1.000 25.42124 ? 34  ASP   A C    1 
ATOM   253  O  O    . ASP   A 1 34  ? -37.26944 -39.81726 10.77244  1.000 26.69221 ? 34  ASP   A O    1 
ATOM   254  C  CB   . ASP   A 1 34  ? -34.63967 -41.60336 10.50690  1.000 24.57646 ? 34  ASP   A CB   1 
ATOM   255  C  CG   . ASP   A 1 34  ? -34.15196 -43.02842 10.34715  1.000 25.56648 ? 34  ASP   A CG   1 
ATOM   256  O  OD1  . ASP   A 1 34  ? -34.99826 -43.93486 10.21259  1.000 28.49402 ? 34  ASP   A OD1  1 
ATOM   257  O  OD2  . ASP   A 1 34  ? -32.92085 -43.24237 10.35972  1.000 29.62101 ? 34  ASP   A OD2  1 
ATOM   258  N  N    . ALA   A 1 35  ? -35.87543 -38.84261 9.29627   1.000 22.54637 ? 35  ALA   A N    1 
ATOM   259  C  CA   . ALA   A 1 35  ? -36.31365 -37.47618 9.54703   1.000 21.51445 ? 35  ALA   A CA   1 
ATOM   260  C  C    . ALA   A 1 35  ? -35.75913 -36.59194 8.44197   1.000 23.24122 ? 35  ALA   A C    1 
ATOM   261  O  O    . ALA   A 1 35  ? -34.76983 -36.93586 7.78790   1.000 20.06637 ? 35  ALA   A O    1 
ATOM   262  C  CB   . ALA   A 1 35  ? -35.85122 -36.96782 10.91754  1.000 21.24736 ? 35  ALA   A CB   1 
ATOM   263  N  N    . LEU   A 1 36  ? -36.40424 -35.44326 8.24849   1.000 19.33391 ? 36  LEU   A N    1 
ATOM   264  C  CA   . LEU   A 1 36  ? -35.97795 -34.45925 7.25993   1.000 20.57842 ? 36  LEU   A CA   1 
ATOM   265  C  C    . LEU   A 1 36  ? -35.83682 -33.10714 7.94186   1.000 21.68511 ? 36  LEU   A C    1 
ATOM   266  O  O    . LEU   A 1 36  ? -36.79358 -32.61129 8.54654   1.000 22.55093 ? 36  LEU   A O    1 
ATOM   267  C  CB   . LEU   A 1 36  ? -36.96996 -34.37384 6.09488   1.000 20.48216 ? 36  LEU   A CB   1 
ATOM   268  C  CG   . LEU   A 1 36  ? -36.72385 -33.24836 5.08554   1.000 22.32293 ? 36  LEU   A CG   1 
ATOM   269  C  CD1  . LEU   A 1 36  ? -35.35026 -33.38396 4.43891   1.000 20.02382 ? 36  LEU   A CD1  1 
ATOM   270  C  CD2  . LEU   A 1 36  ? -37.82011 -33.22291 4.02777   1.000 20.05655 ? 36  LEU   A CD2  1 
ATOM   271  N  N    . TYR   A 1 37  ? -34.64922 -32.51737 7.84646   1.000 19.24061 ? 37  TYR   A N    1 
ATOM   272  C  CA   . TYR   A 1 37  ? -34.37213 -31.19626 8.39253   1.000 18.91582 ? 37  TYR   A CA   1 
ATOM   273  C  C    . TYR   A 1 37  ? -34.13111 -30.21880 7.25272   1.000 18.93979 ? 37  TYR   A C    1 
ATOM   274  O  O    . TYR   A 1 37  ? -33.30828 -30.47801 6.36776   1.000 17.39188 ? 37  TYR   A O    1 
ATOM   275  C  CB   . TYR   A 1 37  ? -33.15548 -31.21971 9.32038   1.000 19.60581 ? 37  TYR   A CB   1 
ATOM   276  C  CG   . TYR   A 1 37  ? -33.37800 -31.93946 10.63106  1.000 21.04073 ? 37  TYR   A CG   1 
ATOM   277  C  CD1  . TYR   A 1 37  ? -33.31614 -33.32542 10.70593  1.000 21.72714 ? 37  TYR   A CD1  1 
ATOM   278  C  CD2  . TYR   A 1 37  ? -33.64004 -31.23108 11.79719  1.000 21.22637 ? 37  TYR   A CD2  1 
ATOM   279  C  CE1  . TYR   A 1 37  ? -33.51800 -33.98687 11.90525  1.000 21.10517 ? 37  TYR   A CE1  1 
ATOM   280  C  CE2  . TYR   A 1 37  ? -33.84253 -31.88279 12.99958  1.000 23.95906 ? 37  TYR   A CE2  1 
ATOM   281  C  CZ   . TYR   A 1 37  ? -33.78043 -33.25971 13.04872  1.000 24.86201 ? 37  TYR   A CZ   1 
ATOM   282  O  OH   . TYR   A 1 37  ? -33.98199 -33.90717 14.24635  1.000 23.76223 ? 37  TYR   A OH   1 
ATOM   283  N  N    . ILE   A 1 38  ? -34.84254 -29.09922 7.28192   1.000 19.76915 ? 38  ILE   A N    1 
ATOM   284  C  CA   . ILE   A 1 38  ? -34.68896 -28.03286 6.30155   1.000 18.29375 ? 38  ILE   A CA   1 
ATOM   285  C  C    . ILE   A 1 38  ? -34.07463 -26.84651 7.03037   1.000 18.84609 ? 38  ILE   A C    1 
ATOM   286  O  O    . ILE   A 1 38  ? -34.74013 -26.18961 7.84075   1.000 18.18311 ? 38  ILE   A O    1 
ATOM   287  C  CB   . ILE   A 1 38  ? -36.02540 -27.66647 5.64436   1.000 19.91607 ? 38  ILE   A CB   1 
ATOM   288  C  CG1  . ILE   A 1 38  ? -36.68909 -28.92335 5.07058   1.000 18.75725 ? 38  ILE   A CG1  1 
ATOM   289  C  CG2  . ILE   A 1 38  ? -35.81956 -26.61149 4.56604   1.000 20.23982 ? 38  ILE   A CG2  1 
ATOM   290  C  CD1  . ILE   A 1 38  ? -37.99695 -28.65715 4.35510   1.000 20.72474 ? 38  ILE   A CD1  1 
ATOM   291  N  N    . LEU   A 1 39  ? -32.80226 -26.57378 6.74700   1.000 16.16833 ? 39  LEU   A N    1 
ATOM   292  C  CA   . LEU   A 1 39  ? -32.01550 -25.59459 7.49707   1.000 15.83038 ? 39  LEU   A CA   1 
ATOM   293  C  C    . LEU   A 1 39  ? -32.06096 -24.19507 6.89435   1.000 18.31778 ? 39  LEU   A C    1 
ATOM   294  O  O    . LEU   A 1 39  ? -31.02409 -23.53696 6.77767   1.000 20.71244 ? 39  LEU   A O    1 
ATOM   295  C  CB   . LEU   A 1 39  ? -30.57515 -26.08515 7.61309   1.000 15.12427 ? 39  LEU   A CB   1 
ATOM   296  C  CG   . LEU   A 1 39  ? -30.37046 -27.47087 8.23134   1.000 20.50418 ? 39  LEU   A CG   1 
ATOM   297  C  CD1  . LEU   A 1 39  ? -28.88637 -27.74470 8.44357   1.000 17.89749 ? 39  LEU   A CD1  1 
ATOM   298  C  CD2  . LEU   A 1 39  ? -31.14378 -27.60124 9.53951   1.000 16.95692 ? 39  LEU   A CD2  1 
ATOM   299  N  N    . GLY   A 1 40  ? -33.23051 -23.70385 6.50500   1.000 18.23430 ? 40  GLY   A N    1 
ATOM   300  C  CA   . GLY   A 1 40  ? -33.35865 -22.30655 6.15052   1.000 17.00206 ? 40  GLY   A CA   1 
ATOM   301  C  C    . GLY   A 1 40  ? -33.29831 -22.06538 4.65119   1.000 19.24706 ? 40  GLY   A C    1 
ATOM   302  O  O    . GLY   A 1 40  ? -32.75637 -22.85947 3.87743   1.000 17.98084 ? 40  GLY   A O    1 
ATOM   303  N  N    . ASP   A 1 41  ? -33.86394 -20.92481 4.24777   1.000 17.44623 ? 41  ASP   A N    1 
ATOM   304  C  CA   . ASP   A 1 41  ? -33.92129 -20.50724 2.84657   1.000 17.87802 ? 41  ASP   A CA   1 
ATOM   305  C  C    . ASP   A 1 41  ? -34.63598 -21.54705 1.98593   1.000 19.92778 ? 41  ASP   A C    1 
ATOM   306  O  O    . ASP   A 1 41  ? -34.23499 -21.82972 0.85431   1.000 18.67757 ? 41  ASP   A O    1 
ATOM   307  C  CB   . ASP   A 1 41  ? -32.52434 -20.20342 2.29923   1.000 18.72148 ? 41  ASP   A CB   1 
ATOM   308  C  CG   . ASP   A 1 41  ? -31.97436 -18.87904 2.80151   1.000 23.81437 ? 41  ASP   A CG   1 
ATOM   309  O  OD1  . ASP   A 1 41  ? -32.63975 -18.22708 3.63552   1.000 21.78538 ? 41  ASP   A OD1  1 
ATOM   310  O  OD2  . ASP   A 1 41  ? -30.86767 -18.49511 2.36671   1.000 21.83973 ? 41  ASP   A OD2  1 
ATOM   311  N  N    . LEU   A 1 42  ? -35.70449 -22.13032 2.53334   1.000 17.73184 ? 42  LEU   A N    1 
ATOM   312  C  CA   . LEU   A 1 42  ? -36.57426 -22.97219 1.71918   1.000 18.80961 ? 42  LEU   A CA   1 
ATOM   313  C  C    . LEU   A 1 42  ? -37.23795 -22.15407 0.61884   1.000 19.81624 ? 42  LEU   A C    1 
ATOM   314  O  O    . LEU   A 1 42  ? -37.33354 -22.60269 -0.52915  1.000 18.70219 ? 42  LEU   A O    1 
ATOM   315  C  CB   . LEU   A 1 42  ? -37.62324 -23.65220 2.60171   1.000 19.25805 ? 42  LEU   A CB   1 
ATOM   316  C  CG   . LEU   A 1 42  ? -38.67943 -24.53325 1.92549   1.000 23.55443 ? 42  LEU   A CG   1 
ATOM   317  C  CD1  . LEU   A 1 42  ? -38.03372 -25.65912 1.12228   1.000 19.74463 ? 42  LEU   A CD1  1 
ATOM   318  C  CD2  . LEU   A 1 42  ? -39.64364 -25.09214 2.96638   1.000 19.31216 ? 42  LEU   A CD2  1 
ATOM   319  N  N    . PHE   A 1 43  ? -37.68015 -20.94270 0.94561   1.000 19.87436 ? 43  PHE   A N    1 
ATOM   320  C  CA   . PHE   A 1 43  ? -38.29017 -20.03246 -0.01001  1.000 19.15907 ? 43  PHE   A CA   1 
ATOM   321  C  C    . PHE   A 1 43  ? -37.37521 -18.83863 -0.25460  1.000 18.11923 ? 43  PHE   A C    1 
ATOM   322  O  O    . PHE   A 1 43  ? -36.62050 -18.42053 0.62834   1.000 16.90268 ? 43  PHE   A O    1 
ATOM   323  C  CB   . PHE   A 1 43  ? -39.65796 -19.54649 0.48746   1.000 20.06004 ? 43  PHE   A CB   1 
ATOM   324  C  CG   . PHE   A 1 43  ? -40.67780 -20.64557 0.62622   1.000 19.64789 ? 43  PHE   A CG   1 
ATOM   325  C  CD1  . PHE   A 1 43  ? -41.45556 -21.02771 -0.45541  1.000 21.84885 ? 43  PHE   A CD1  1 
ATOM   326  C  CD2  . PHE   A 1 43  ? -40.84694 -21.30587 1.83413   1.000 18.83163 ? 43  PHE   A CD2  1 
ATOM   327  C  CE1  . PHE   A 1 43  ? -42.39168 -22.04440 -0.33374  1.000 21.80268 ? 43  PHE   A CE1  1 
ATOM   328  C  CE2  . PHE   A 1 43  ? -41.78079 -22.32436 1.96308   1.000 19.95628 ? 43  PHE   A CE2  1 
ATOM   329  C  CZ   . PHE   A 1 43  ? -42.55412 -22.69361 0.87788   1.000 19.15523 ? 43  PHE   A CZ   1 
ATOM   330  N  N    . GLU   A 1 44  ? -37.45124 -18.29451 -1.47268  1.000 18.62795 ? 44  GLU   A N    1 
ATOM   331  C  CA   . GLU   A 1 44  ? -36.68657 -17.09658 -1.80616  1.000 22.81309 ? 44  GLU   A CA   1 
ATOM   332  C  C    . GLU   A 1 44  ? -37.18069 -15.87950 -1.03117  1.000 25.62941 ? 44  GLU   A C    1 
ATOM   333  O  O    . GLU   A 1 44  ? -36.40414 -14.95188 -0.77013  1.000 21.43500 ? 44  GLU   A O    1 
ATOM   334  C  CB   . GLU   A 1 44  ? -36.75622 -16.84258 -3.31527  1.000 23.86464 ? 44  GLU   A CB   1 
ATOM   335  C  CG   . GLU   A 1 44  ? -36.18154 -15.50857 -3.78949  1.000 27.30685 ? 44  GLU   A CG   1 
ATOM   336  C  CD   . GLU   A 1 44  ? -34.67920 -15.37609 -3.57808  1.000 29.81793 ? 44  GLU   A CD   1 
ATOM   337  O  OE1  . GLU   A 1 44  ? -34.01206 -16.38475 -3.26492  1.000 30.19947 ? 44  GLU   A OE1  1 
ATOM   338  O  OE2  . GLU   A 1 44  ? -34.16249 -14.25024 -3.73052  1.000 28.48367 ? 44  GLU   A OE2  1 
ATOM   339  N  N    . ALA   A 1 45  ? -38.45377 -15.86774 -0.64363  1.000 22.75982 ? 45  ALA   A N    1 
ATOM   340  C  CA   . ALA   A 1 45  ? -39.01582 -14.74580 0.09127   1.000 20.85660 ? 45  ALA   A CA   1 
ATOM   341  C  C    . ALA   A 1 45  ? -40.19896 -15.22745 0.91689   1.000 24.04241 ? 45  ALA   A C    1 
ATOM   342  O  O    . ALA   A 1 45  ? -40.80729 -16.25862 0.62369   1.000 21.29672 ? 45  ALA   A O    1 
ATOM   343  C  CB   . ALA   A 1 45  ? -39.44758 -13.61515 -0.85086  1.000 23.88349 ? 45  ALA   A CB   1 
ATOM   344  N  N    . TRP   A 1 46  ? -40.51927 -14.46317 1.95956   1.000 21.24197 ? 46  TRP   A N    1 
ATOM   345  C  CA   . TRP   A 1 46  ? -41.68656 -14.74420 2.78700   1.000 21.95193 ? 46  TRP   A CA   1 
ATOM   346  C  C    . TRP   A 1 46  ? -42.12278 -13.44843 3.44853   1.000 21.63410 ? 46  TRP   A C    1 
ATOM   347  O  O    . TRP   A 1 46  ? -41.30191 -12.76565 4.06871   1.000 22.56494 ? 46  TRP   A O    1 
ATOM   348  C  CB   . TRP   A 1 46  ? -41.38590 -15.80722 3.85092   1.000 17.20897 ? 46  TRP   A CB   1 
ATOM   349  C  CG   . TRP   A 1 46  ? -42.61580 -16.50437 4.36693   1.000 19.66657 ? 46  TRP   A CG   1 
ATOM   350  C  CD1  . TRP   A 1 46  ? -43.37014 -16.14696 5.44851   1.000 19.02700 ? 46  TRP   A CD1  1 
ATOM   351  C  CD2  . TRP   A 1 46  ? -43.22684 -17.68420 3.82484   1.000 19.73947 ? 46  TRP   A CD2  1 
ATOM   352  N  NE1  . TRP   A 1 46  ? -44.41458 -17.02775 5.60937   1.000 18.55109 ? 46  TRP   A NE1  1 
ATOM   353  C  CE2  . TRP   A 1 46  ? -44.34802 -17.98052 4.62636   1.000 20.27452 ? 46  TRP   A CE2  1 
ATOM   354  C  CE3  . TRP   A 1 46  ? -42.93520 -18.51700 2.73915   1.000 22.26015 ? 46  TRP   A CE3  1 
ATOM   355  C  CZ2  . TRP   A 1 46  ? -45.17778 -19.07517 4.37656   1.000 23.13151 ? 46  TRP   A CZ2  1 
ATOM   356  C  CZ3  . TRP   A 1 46  ? -43.76113 -19.60413 2.49319   1.000 20.80974 ? 46  TRP   A CZ3  1 
ATOM   357  C  CH2  . TRP   A 1 46  ? -44.86806 -19.87257 3.30851   1.000 21.10213 ? 46  TRP   A CH2  1 
ATOM   358  N  N    . ILE   A 1 47  ? -43.40678 -13.11276 3.31276   1.000 21.37122 ? 47  ILE   A N    1 
ATOM   359  C  CA   . ILE   A 1 47  ? -43.96808 -11.90086 3.89091   1.000 19.61844 ? 47  ILE   A CA   1 
ATOM   360  C  C    . ILE   A 1 47  ? -45.08984 -12.20088 4.87761   1.000 21.99285 ? 47  ILE   A C    1 
ATOM   361  O  O    . ILE   A 1 47  ? -45.77444 -11.28208 5.32720   1.000 23.36485 ? 47  ILE   A O    1 
ATOM   362  C  CB   . ILE   A 1 47  ? -44.45010 -10.92885 2.79501   1.000 24.17813 ? 47  ILE   A CB   1 
ATOM   363  C  CG1  . ILE   A 1 47  ? -45.51821 -11.58744 1.91795   1.000 23.90098 ? 47  ILE   A CG1  1 
ATOM   364  C  CG2  . ILE   A 1 47  ? -43.27606 -10.45274 1.95466   1.000 22.20876 ? 47  ILE   A CG2  1 
ATOM   365  C  CD1  . ILE   A 1 47  ? -46.30647 -10.60573 1.08006   1.000 30.54065 ? 47  ILE   A CD1  1 
ATOM   366  N  N    . GLY   A 1 48  ? -45.28898 -13.46326 5.22836   1.000 23.72608 ? 48  GLY   A N    1 
ATOM   367  C  CA   . GLY   A 1 48  ? -46.30055 -13.85245 6.19628   1.000 21.26344 ? 48  GLY   A CA   1 
ATOM   368  C  C    . GLY   A 1 48  ? -47.06437 -15.09165 5.77117   1.000 20.97267 ? 48  GLY   A C    1 
ATOM   369  O  O    . GLY   A 1 48  ? -47.22031 -15.38496 4.58463   1.000 20.53228 ? 48  GLY   A O    1 
ATOM   370  N  N    . ASP   A 1 49  ? -47.56443 -15.83425 6.76361   1.000 20.37906 ? 49  ASP   A N    1 
ATOM   371  C  CA   . ASP   A 1 49  ? -48.28699 -17.07578 6.50203   1.000 22.33244 ? 49  ASP   A CA   1 
ATOM   372  C  C    . ASP   A 1 49  ? -49.66446 -16.85640 5.89087   1.000 27.27390 ? 49  ASP   A C    1 
ATOM   373  O  O    . ASP   A 1 49  ? -50.28035 -17.82830 5.44082   1.000 23.21488 ? 49  ASP   A O    1 
ATOM   374  C  CB   . ASP   A 1 49  ? -48.44748 -17.88535 7.78889   1.000 19.96781 ? 49  ASP   A CB   1 
ATOM   375  C  CG   . ASP   A 1 49  ? -47.13118 -18.39950 8.32829   1.000 22.18434 ? 49  ASP   A CG   1 
ATOM   376  O  OD1  . ASP   A 1 49  ? -46.09729 -18.25693 7.64378   1.000 23.52017 ? 49  ASP   A OD1  1 
ATOM   377  O  OD2  . ASP   A 1 49  ? -47.14130 -18.96411 9.43956   1.000 22.62927 ? 49  ASP   A OD2  1 
ATOM   378  N  N    . ASP   A 1 50  ? -50.17245 -15.62942 5.88259   1.000 22.39270 ? 50  ASP   A N    1 
ATOM   379  C  CA   . ASP   A 1 50  ? -51.46255 -15.34061 5.27328   1.000 22.52279 ? 50  ASP   A CA   1 
ATOM   380  C  C    . ASP   A 1 50  ? -51.35283 -15.05602 3.78005   1.000 22.18291 ? 50  ASP   A C    1 
ATOM   381  O  O    . ASP   A 1 50  ? -52.36889 -14.77169 3.13730   1.000 24.52916 ? 50  ASP   A O    1 
ATOM   382  C  CB   . ASP   A 1 50  ? -52.12810 -14.16442 5.99505   1.000 24.28537 ? 50  ASP   A CB   1 
ATOM   383  C  CG   . ASP   A 1 50  ? -51.25525 -12.92448 6.02338   1.000 28.04593 ? 50  ASP   A CG   1 
ATOM   384  O  OD1  . ASP   A 1 50  ? -50.02147 -13.05037 5.86489   1.000 24.62019 ? 50  ASP   A OD1  1 
ATOM   385  O  OD2  . ASP   A 1 50  ? -51.80416 -11.82128 6.21753   1.000 29.11935 ? 50  ASP   A OD2  1 
ATOM   386  N  N    . ASP   A 1 51  ? -50.15175 -15.13677 3.22307   1.000 22.87983 ? 51  ASP   A N    1 
ATOM   387  C  CA   . ASP   A 1 51  ? -49.91633 -14.93609 1.80082   1.000 22.01265 ? 51  ASP   A CA   1 
ATOM   388  C  C    . ASP   A 1 51  ? -50.60969 -16.03720 1.00280   1.000 23.98850 ? 51  ASP   A C    1 
ATOM   389  O  O    . ASP   A 1 51  ? -50.33391 -17.22274 1.23485   1.000 20.58893 ? 51  ASP   A O    1 
ATOM   390  C  CB   . ASP   A 1 51  ? -48.40608 -14.93899 1.55146   1.000 20.46407 ? 51  ASP   A CB   1 
ATOM   391  C  CG   . ASP   A 1 51  ? -48.02607 -14.60040 0.11974   1.000 22.62401 ? 51  ASP   A CG   1 
ATOM   392  O  OD1  . ASP   A 1 51  ? -48.88799 -14.61606 -0.78315  1.000 21.87639 ? 51  ASP   A OD1  1 
ATOM   393  O  OD2  . ASP   A 1 51  ? -46.83062 -14.31072 -0.09765  1.000 26.59357 ? 51  ASP   A OD2  1 
ATOM   394  N  N    . PRO   A 1 52  ? -51.50648 -15.70342 0.07298   1.000 24.15752 ? 52  PRO   A N    1 
ATOM   395  C  CA   . PRO   A 1 52  ? -52.21880 -16.73669 -0.68891  1.000 23.44058 ? 52  PRO   A CA   1 
ATOM   396  C  C    . PRO   A 1 52  ? -51.44426 -17.31356 -1.86387  1.000 23.93697 ? 52  PRO   A C    1 
ATOM   397  O  O    . PRO   A 1 52  ? -52.03825 -18.04598 -2.66006  1.000 24.76898 ? 52  PRO   A O    1 
ATOM   398  C  CB   . PRO   A 1 52  ? -53.46632 -15.98616 -1.18188  1.000 22.87315 ? 52  PRO   A CB   1 
ATOM   399  C  CG   . PRO   A 1 52  ? -53.00084 -14.57740 -1.33517  1.000 27.33281 ? 52  PRO   A CG   1 
ATOM   400  C  CD   . PRO   A 1 52  ? -52.01431 -14.34985 -0.21637  1.000 25.23586 ? 52  PRO   A CD   1 
ATOM   401  N  N    . ASN   A 1 53  ? -50.15023 -16.99715 -1.99798  1.000 21.93631 ? 53  ASN   A N    1 
ATOM   402  C  CA   . ASN   A 1 53  ? -49.27791 -17.52707 -3.04334  1.000 20.41395 ? 53  ASN   A CA   1 
ATOM   403  C  C    . ASN   A 1 53  ? -49.48759 -19.03256 -3.17898  1.000 19.80257 ? 53  ASN   A C    1 
ATOM   404  O  O    . ASN   A 1 53  ? -49.19577 -19.78690 -2.24223  1.000 19.99817 ? 53  ASN   A O    1 
ATOM   405  C  CB   . ASN   A 1 53  ? -47.81253 -17.20776 -2.72337  1.000 22.92893 ? 53  ASN   A CB   1 
ATOM   406  C  CG   . ASN   A 1 53  ? -46.85495 -17.59753 -3.84622  1.000 27.77897 ? 53  ASN   A CG   1 
ATOM   407  O  OD1  . ASN   A 1 53  ? -47.20964 -18.33764 -4.76371  1.000 25.23509 ? 53  ASN   A OD1  1 
ATOM   408  N  ND2  . ASN   A 1 53  ? -45.62691 -17.09536 -3.76921  1.000 23.43407 ? 53  ASN   A ND2  1 
ATOM   409  N  N    . PRO   A 1 54  ? -50.00021 -19.50176 -4.32135  1.000 22.50894 ? 54  PRO   A N    1 
ATOM   410  C  CA   . PRO   A 1 54  ? -50.31444 -20.93572 -4.45227  1.000 21.78062 ? 54  PRO   A CA   1 
ATOM   411  C  C    . PRO   A 1 54  ? -49.11244 -21.84609 -4.27409  1.000 22.24658 ? 54  PRO   A C    1 
ATOM   412  O  O    . PRO   A 1 54  ? -49.27899 -22.99091 -3.83240  1.000 20.32943 ? 54  PRO   A O    1 
ATOM   413  C  CB   . PRO   A 1 54  ? -50.89200 -21.03465 -5.87069  1.000 25.47664 ? 54  PRO   A CB   1 
ATOM   414  C  CG   . PRO   A 1 54  ? -51.40759 -19.65322 -6.16926  1.000 24.42101 ? 54  PRO   A CG   1 
ATOM   415  C  CD   . PRO   A 1 54  ? -50.43607 -18.72620 -5.49588  1.000 22.95459 ? 54  PRO   A CD   1 
ATOM   416  N  N    . LEU   A 1 55  ? -47.90655 -21.37435 -4.60574  1.000 22.01958 ? 55  LEU   A N    1 
ATOM   417  C  CA   . LEU   A 1 55  ? -46.70713 -22.17505 -4.37620  1.000 24.20220 ? 55  LEU   A CA   1 
ATOM   418  C  C    . LEU   A 1 55  ? -46.58970 -22.58447 -2.91449  1.000 25.09573 ? 55  LEU   A C    1 
ATOM   419  O  O    . LEU   A 1 55  ? -46.17459 -23.70788 -2.60682  1.000 22.13133 ? 55  LEU   A O    1 
ATOM   420  C  CB   . LEU   A 1 55  ? -45.46212 -21.40060 -4.81342  1.000 21.76608 ? 55  LEU   A CB   1 
ATOM   421  C  CG   . LEU   A 1 55  ? -44.11873 -22.06537 -4.49230  1.000 25.11310 ? 55  LEU   A CG   1 
ATOM   422  C  CD1  . LEU   A 1 55  ? -43.94086 -23.35529 -5.29066  1.000 23.38739 ? 55  LEU   A CD1  1 
ATOM   423  C  CD2  . LEU   A 1 55  ? -42.96501 -21.10099 -4.73780  1.000 25.18221 ? 55  LEU   A CD2  1 
ATOM   424  N  N    . HIS   A 1 56  ? -46.96410 -21.68608 -1.99941  1.000 20.85939 ? 56  HIS   A N    1 
ATOM   425  C  CA   . HIS   A 1 56  ? -46.89264 -21.99723 -0.57513  1.000 20.08471 ? 56  HIS   A CA   1 
ATOM   426  C  C    . HIS   A 1 56  ? -47.79395 -23.17239 -0.22200  1.000 21.97687 ? 56  HIS   A C    1 
ATOM   427  O  O    . HIS   A 1 56  ? -47.40471 -24.05255 0.55319   1.000 21.68622 ? 56  HIS   A O    1 
ATOM   428  C  CB   . HIS   A 1 56  ? -47.27990 -20.77052 0.25218   1.000 20.26175 ? 56  HIS   A CB   1 
ATOM   429  C  CG   . HIS   A 1 56  ? -46.34281 -19.61296 0.09861   1.000 21.74116 ? 56  HIS   A CG   1 
ATOM   430  N  ND1  . HIS   A 1 56  ? -46.46545 -18.45544 0.83660   1.000 21.40282 ? 56  HIS   A ND1  1 
ATOM   431  C  CD2  . HIS   A 1 56  ? -45.27263 -19.43123 -0.71093  1.000 20.03901 ? 56  HIS   A CD2  1 
ATOM   432  C  CE1  . HIS   A 1 56  ? -45.51171 -17.61027 0.48815   1.000 21.84049 ? 56  HIS   A CE1  1 
ATOM   433  N  NE2  . HIS   A 1 56  ? -44.77361 -18.17828 -0.44865  1.000 19.54164 ? 56  HIS   A NE2  1 
ATOM   434  N  N    . GLN   A 1 57  ? -49.00619 -23.20196 -0.77868  1.000 22.10884 ? 57  GLN   A N    1 
ATOM   435  C  CA   . GLN   A 1 57  ? -49.92963 -24.28493 -0.46436  1.000 24.52533 ? 57  GLN   A CA   1 
ATOM   436  C  C    . GLN   A 1 57  ? -49.50108 -25.58924 -1.12341  1.000 23.66570 ? 57  GLN   A C    1 
ATOM   437  O  O    . GLN   A 1 57  ? -49.71160 -26.66684 -0.55580  1.000 23.50124 ? 57  GLN   A O    1 
ATOM   438  C  CB   . GLN   A 1 57  ? -51.34991 -23.90999 -0.89222  1.000 25.79435 ? 57  GLN   A CB   1 
ATOM   439  C  CG   . GLN   A 1 57  ? -52.10486 -23.00695 0.08933   1.000 33.76849 ? 57  GLN   A CG   1 
ATOM   440  C  CD   . GLN   A 1 57  ? -51.21923 -21.97761 0.77668   1.000 44.11358 ? 57  GLN   A CD   1 
ATOM   441  O  OE1  . GLN   A 1 57  ? -50.83614 -22.14367 1.93617   1.000 42.71762 ? 57  GLN   A OE1  1 
ATOM   442  N  NE2  . GLN   A 1 57  ? -50.89897 -20.90079 0.06363   1.000 42.07020 ? 57  GLN   A NE2  1 
ATOM   443  N  N    . GLN   A 1 58  ? -48.90306 -25.51266 -2.31531  1.000 23.25422 ? 58  GLN   A N    1 
ATOM   444  C  CA   . GLN   A 1 58  ? -48.40228 -26.71462 -2.97389  1.000 26.16023 ? 58  GLN   A CA   1 
ATOM   445  C  C    . GLN   A 1 58  ? -47.23409 -27.31962 -2.20471  1.000 25.52273 ? 58  GLN   A C    1 
ATOM   446  O  O    . GLN   A 1 58  ? -47.15784 -28.54332 -2.04124  1.000 21.16762 ? 58  GLN   A O    1 
ATOM   447  C  CB   . GLN   A 1 58  ? -47.99011 -26.39128 -4.41021  1.000 26.87813 ? 58  GLN   A CB   1 
ATOM   448  C  CG   . GLN   A 1 58  ? -49.13009 -25.88699 -5.28518  1.000 34.80497 ? 58  GLN   A CG   1 
ATOM   449  C  CD   . GLN   A 1 58  ? -48.64275 -25.27514 -6.58557  1.000 35.78061 ? 58  GLN   A CD   1 
ATOM   450  O  OE1  . GLN   A 1 58  ? -47.43935 -25.15358 -6.81535  1.000 39.59242 ? 58  GLN   A OE1  1 
ATOM   451  N  NE2  . GLN   A 1 58  ? -49.57847 -24.89451 -7.44819  1.000 36.77731 ? 58  GLN   A NE2  1 
ATOM   452  N  N    . ILE   A 1 59  ? -46.31364 -26.47942 -1.72668  1.000 20.35986 ? 59  ILE   A N    1 
ATOM   453  C  CA   . ILE   A 1 59  ? -45.18569 -26.98127 -0.94735  1.000 22.95855 ? 59  ILE   A CA   1 
ATOM   454  C  C    . ILE   A 1 59  ? -45.66426 -27.55351 0.38154   1.000 21.02474 ? 59  ILE   A C    1 
ATOM   455  O  O    . ILE   A 1 59  ? -45.18845 -28.60520 0.82591   1.000 21.86934 ? 59  ILE   A O    1 
ATOM   456  C  CB   . ILE   A 1 59  ? -44.14090 -25.86894 -0.74364  1.000 22.76070 ? 59  ILE   A CB   1 
ATOM   457  C  CG1  . ILE   A 1 59  ? -43.49628 -25.49470 -2.08045  1.000 18.83947 ? 59  ILE   A CG1  1 
ATOM   458  C  CG2  . ILE   A 1 59  ? -43.07732 -26.30840 0.25274   1.000 20.94657 ? 59  ILE   A CG2  1 
ATOM   459  C  CD1  . ILE   A 1 59  ? -42.93143 -26.68241 -2.84262  1.000 20.38437 ? 59  ILE   A CD1  1 
ATOM   460  N  N    . ALA   A 1 60  ? -46.61524 -26.87710 1.03330   1.000 21.60005 ? 60  ALA   A N    1 
ATOM   461  C  CA   . ALA   A 1 60  ? -47.11850 -27.35472 2.31765   1.000 22.09744 ? 60  ALA   A CA   1 
ATOM   462  C  C    . ALA   A 1 60  ? -47.76856 -28.72608 2.18411   1.000 23.49512 ? 60  ALA   A C    1 
ATOM   463  O  O    . ALA   A 1 60  ? -47.55452 -29.60618 3.02498   1.000 20.98502 ? 60  ALA   A O    1 
ATOM   464  C  CB   . ALA   A 1 60  ? -48.10866 -26.34743 2.90457   1.000 19.34643 ? 60  ALA   A CB   1 
ATOM   465  N  N    A SER   A 1 61  ? -48.56817 -28.92389 1.13188   0.425 23.03999 ? 61  SER   A N    1 
ATOM   466  N  N    B SER   A 1 61  ? -48.56227 -28.92841 1.12936   0.261 23.20985 ? 61  SER   A N    1 
ATOM   467  N  N    C SER   A 1 61  ? -48.56724 -28.92643 1.13231   0.314 23.04913 ? 61  SER   A N    1 
ATOM   468  C  CA   A SER   A 1 61  ? -49.22289 -30.21280 0.93153   0.425 24.19183 ? 61  SER   A CA   1 
ATOM   469  C  CA   B SER   A 1 61  ? -49.22252 -30.21642 0.94109   0.261 23.95650 ? 61  SER   A CA   1 
ATOM   470  C  CA   C SER   A 1 61  ? -49.22400 -30.21527 0.94111   0.314 23.94007 ? 61  SER   A CA   1 
ATOM   471  C  C    A SER   A 1 61  ? -48.20549 -31.31263 0.65649   0.425 24.07332 ? 61  SER   A C    1 
ATOM   472  C  C    B SER   A 1 61  ? -48.21459 -31.31915 0.64025   0.261 24.06729 ? 61  SER   A C    1 
ATOM   473  C  C    C SER   A 1 61  ? -48.22188 -31.31878 0.62886   0.314 24.07148 ? 61  SER   A C    1 
ATOM   474  O  O    A SER   A 1 61  ? -48.36538 -32.44731 1.12206   0.425 22.62535 ? 61  SER   A O    1 
ATOM   475  O  O    B SER   A 1 61  ? -48.39202 -32.46398 1.07278   0.261 22.76084 ? 61  SER   A O    1 
ATOM   476  O  O    C SER   A 1 61  ? -48.41622 -32.46625 1.04593   0.314 23.10346 ? 61  SER   A O    1 
ATOM   477  C  CB   A SER   A 1 61  ? -50.23023 -30.11834 -0.21530  0.425 25.76961 ? 61  SER   A CB   1 
ATOM   478  C  CB   B SER   A 1 61  ? -50.25863 -30.11608 -0.17795  0.261 25.85763 ? 61  SER   A CB   1 
ATOM   479  C  CB   C SER   A 1 61  ? -50.26485 -30.11417 -0.17351  0.314 25.63407 ? 61  SER   A CB   1 
ATOM   480  O  OG   A SER   A 1 61  ? -51.14762 -29.05792 -0.01246  0.425 22.18799 ? 61  SER   A OG   1 
ATOM   481  O  OG   B SER   A 1 61  ? -50.85170 -31.37635 -0.43813  0.261 25.40887 ? 61  SER   A OG   1 
ATOM   482  O  OG   C SER   A 1 61  ? -49.65096 -30.15789 -1.44961  0.314 25.98823 ? 61  SER   A OG   1 
ATOM   483  N  N    . ALA   A 1 62  ? -47.15037 -30.99584 -0.09798  1.000 24.36010 ? 62  ALA   A N    1 
ATOM   484  C  CA   . ALA   A 1 62  ? -46.15080 -32.00608 -0.42907  1.000 25.15452 ? 62  ALA   A CA   1 
ATOM   485  C  C    . ALA   A 1 62  ? -45.34092 -32.40860 0.79568   1.000 23.82208 ? 62  ALA   A C    1 
ATOM   486  O  O    . ALA   A 1 62  ? -45.03888 -33.59333 0.98505   1.000 23.19348 ? 62  ALA   A O    1 
ATOM   487  C  CB   . ALA   A 1 62  ? -45.23109 -31.49130 -1.53279  1.000 23.90873 ? 62  ALA   A CB   1 
ATOM   488  N  N    . ILE   A 1 63  ? -44.97362 -31.43780 1.63378   1.000 19.60625 ? 63  ILE   A N    1 
ATOM   489  C  CA   . ILE   A 1 63  ? -44.27354 -31.76126 2.87193   1.000 21.40853 ? 63  ILE   A CA   1 
ATOM   490  C  C    . ILE   A 1 63  ? -45.19511 -32.51998 3.81772   1.000 22.23275 ? 63  ILE   A C    1 
ATOM   491  O  O    . ILE   A 1 63  ? -44.77647 -33.47585 4.48294   1.000 21.59772 ? 63  ILE   A O    1 
ATOM   492  C  CB   . ILE   A 1 63  ? -43.72004 -30.48095 3.52348   1.000 19.73704 ? 63  ILE   A CB   1 
ATOM   493  C  CG1  . ILE   A 1 63  ? -42.67454 -29.82310 2.61776   1.000 20.88069 ? 63  ILE   A CG1  1 
ATOM   494  C  CG2  . ILE   A 1 63  ? -43.12881 -30.78937 4.89293   1.000 21.96177 ? 63  ILE   A CG2  1 
ATOM   495  C  CD1  . ILE   A 1 63  ? -42.15218 -28.50362 3.15253   1.000 20.61174 ? 63  ILE   A CD1  1 
ATOM   496  N  N    . LYS   A 1 64  ? -46.46691 -32.11559 3.88300   1.000 20.42576 ? 64  LYS   A N    1 
ATOM   497  C  CA   . LYS   A 1 64  ? -47.42031 -32.79347 4.75499   1.000 24.61859 ? 64  LYS   A CA   1 
ATOM   498  C  C    . LYS   A 1 64  ? -47.58473 -34.25893 4.37339   1.000 25.39059 ? 64  LYS   A C    1 
ATOM   499  O  O    . LYS   A 1 64  ? -47.80169 -35.10672 5.24656   1.000 23.30579 ? 64  LYS   A O    1 
ATOM   500  C  CB   . LYS   A 1 64  ? -48.76849 -32.07164 4.71066   1.000 21.98794 ? 64  LYS   A CB   1 
ATOM   501  C  CG   . LYS   A 1 64  ? -49.85702 -32.70654 5.56240   1.000 28.65537 ? 64  LYS   A CG   1 
ATOM   502  C  CD   . LYS   A 1 64  ? -49.49389 -32.65155 7.03636   1.000 29.14462 ? 64  LYS   A CD   1 
ATOM   503  C  CE   . LYS   A 1 64  ? -50.71162 -32.34842 7.89087   1.000 36.46052 ? 64  LYS   A CE   1 
ATOM   504  N  NZ   . LYS   A 1 64  ? -51.25066 -33.57969 8.52510   1.000 34.44822 ? 64  LYS   A NZ   1 
ATOM   505  N  N    . ALA   A 1 65  ? -47.47765 -34.57769 3.08052   1.000 22.32790 ? 65  ALA   A N    1 
ATOM   506  C  CA   . ALA   A 1 65  ? -47.56087 -35.97103 2.65326   1.000 22.76178 ? 65  ALA   A CA   1 
ATOM   507  C  C    . ALA   A 1 65  ? -46.38140 -36.78145 3.17834   1.000 24.39988 ? 65  ALA   A C    1 
ATOM   508  O  O    . ALA   A 1 65  ? -46.53496 -37.95541 3.53769   1.000 23.93059 ? 65  ALA   A O    1 
ATOM   509  C  CB   . ALA   A 1 65  ? -47.63199 -36.04850 1.12856   1.000 25.30260 ? 65  ALA   A CB   1 
ATOM   510  N  N    . VAL   A 1 66  ? -45.19278 -36.17564 3.22196   1.000 22.15578 ? 66  VAL   A N    1 
ATOM   511  C  CA   . VAL   A 1 66  ? -44.04055 -36.84789 3.81557   1.000 21.19751 ? 66  VAL   A CA   1 
ATOM   512  C  C    . VAL   A 1 66  ? -44.25731 -37.04714 5.31020   1.000 23.62644 ? 66  VAL   A C    1 
ATOM   513  O  O    . VAL   A 1 66  ? -43.96355 -38.11682 5.85969   1.000 23.12798 ? 66  VAL   A O    1 
ATOM   514  C  CB   . VAL   A 1 66  ? -42.75443 -36.05012 3.53055   1.000 23.43115 ? 66  VAL   A CB   1 
ATOM   515  C  CG1  . VAL   A 1 66  ? -41.57217 -36.64583 4.28967   1.000 24.03355 ? 66  VAL   A CG1  1 
ATOM   516  C  CG2  . VAL   A 1 66  ? -42.47440 -36.00968 2.03551   1.000 25.24682 ? 66  VAL   A CG2  1 
ATOM   517  N  N    . VAL   A 1 67  ? -44.77573 -36.02079 5.98899   1.000 22.81140 ? 67  VAL   A N    1 
ATOM   518  C  CA   . VAL   A 1 67  ? -45.06494 -36.12740 7.41739   1.000 21.96324 ? 67  VAL   A CA   1 
ATOM   519  C  C    . VAL   A 1 67  ? -46.09160 -37.22662 7.66852   1.000 25.38770 ? 67  VAL   A C    1 
ATOM   520  O  O    . VAL   A 1 67  ? -45.92886 -38.06034 8.56859   1.000 23.60322 ? 67  VAL   A O    1 
ATOM   521  C  CB   . VAL   A 1 67  ? -45.54014 -34.76909 7.96818   1.000 24.17863 ? 67  VAL   A CB   1 
ATOM   522  C  CG1  . VAL   A 1 67  ? -46.07977 -34.91871 9.38370   1.000 27.24916 ? 67  VAL   A CG1  1 
ATOM   523  C  CG2  . VAL   A 1 67  ? -44.40365 -33.74547 7.92720   1.000 20.83363 ? 67  VAL   A CG2  1 
ATOM   524  N  N    . ASP   A 1 68  ? -47.16057 -37.25314 6.86441   1.000 22.96504 ? 68  ASP   A N    1 
ATOM   525  C  CA   . ASP   A 1 68  ? -48.18351 -38.28408 7.02609   1.000 26.89549 ? 68  ASP   A CA   1 
ATOM   526  C  C    . ASP   A 1 68  ? -47.63337 -39.67690 6.74822   1.000 27.88464 ? 68  ASP   A C    1 
ATOM   527  O  O    . ASP   A 1 68  ? -48.16335 -40.66442 7.26927   1.000 26.85942 ? 68  ASP   A O    1 
ATOM   528  C  CB   . ASP   A 1 68  ? -49.37671 -38.00079 6.11135   1.000 28.00854 ? 68  ASP   A CB   1 
ATOM   529  C  CG   . ASP   A 1 68  ? -50.19701 -36.81093 6.57182   1.000 26.90357 ? 68  ASP   A CG   1 
ATOM   530  O  OD1  . ASP   A 1 68  ? -50.07251 -36.42094 7.75102   1.000 30.98121 ? 68  ASP   A OD1  1 
ATOM   531  O  OD2  . ASP   A 1 68  ? -50.97640 -36.27454 5.75658   1.000 29.68442 ? 68  ASP   A OD2  1 
ATOM   532  N  N    . ALA   A 1 69  ? -46.58142 -39.77942 5.93751   1.000 24.55734 ? 69  ALA   A N    1 
ATOM   533  C  CA   . ALA   A 1 69  ? -45.95365 -41.06397 5.65995   1.000 28.95738 ? 69  ALA   A CA   1 
ATOM   534  C  C    . ALA   A 1 69  ? -45.05691 -41.54327 6.79501   1.000 30.52038 ? 69  ALA   A C    1 
ATOM   535  O  O    . ALA   A 1 69  ? -44.44203 -42.60772 6.66811   1.000 31.24486 ? 69  ALA   A O    1 
ATOM   536  C  CB   . ALA   A 1 69  ? -45.14893 -40.98678 4.35944   1.000 28.13517 ? 69  ALA   A CB   1 
ATOM   537  N  N    . GLY   A 1 70  ? -44.96471 -40.79310 7.88922   1.000 25.93550 ? 70  GLY   A N    1 
ATOM   538  C  CA   . GLY   A 1 70  ? -44.20990 -41.21161 9.05014   1.000 23.62465 ? 70  GLY   A CA   1 
ATOM   539  C  C    . GLY   A 1 70  ? -42.84655 -40.58049 9.21782   1.000 26.50073 ? 70  GLY   A C    1 
ATOM   540  O  O    . GLY   A 1 70  ? -42.09885 -41.00178 10.10731  1.000 25.19523 ? 70  GLY   A O    1 
ATOM   541  N  N    . VAL   A 1 71  ? -42.49901 -39.58714 8.40592   1.000 20.05666 ? 71  VAL   A N    1 
ATOM   542  C  CA   . VAL   A 1 71  ? -41.18501 -38.95824 8.44155   1.000 19.88652 ? 71  VAL   A CA   1 
ATOM   543  C  C    . VAL   A 1 71  ? -41.34077 -37.58094 9.08268   1.000 20.13496 ? 71  VAL   A C    1 
ATOM   544  O  O    . VAL   A 1 71  ? -41.88196 -36.66185 8.44941   1.000 20.17899 ? 71  VAL   A O    1 
ATOM   545  C  CB   . VAL   A 1 71  ? -40.56783 -38.85181 7.03999   1.000 23.25171 ? 71  VAL   A CB   1 
ATOM   546  C  CG1  . VAL   A 1 71  ? -39.19944 -38.17306 7.10590   1.000 20.36487 ? 71  VAL   A CG1  1 
ATOM   547  C  CG2  . VAL   A 1 71  ? -40.46858 -40.22927 6.39202   1.000 23.76878 ? 71  VAL   A CG2  1 
ATOM   548  N  N    . PRO   A 1 72  ? -40.89060 -37.38581 10.32159  1.000 21.09715 ? 72  PRO   A N    1 
ATOM   549  C  CA   . PRO   A 1 72  ? -40.96593 -36.05168 10.92719  1.000 24.48460 ? 72  PRO   A CA   1 
ATOM   550  C  C    . PRO   A 1 72  ? -40.08805 -35.06220 10.17396  1.000 23.18023 ? 72  PRO   A C    1 
ATOM   551  O  O    . PRO   A 1 72  ? -38.97239 -35.38269 9.75847   1.000 19.88104 ? 72  PRO   A O    1 
ATOM   552  C  CB   . PRO   A 1 72  ? -40.46920 -36.27908 12.36000  1.000 24.63102 ? 72  PRO   A CB   1 
ATOM   553  C  CG   . PRO   A 1 72  ? -39.68275 -37.55282 12.30548  1.000 23.37052 ? 72  PRO   A CG   1 
ATOM   554  C  CD   . PRO   A 1 72  ? -40.31381 -38.38849 11.23445  1.000 19.84790 ? 72  PRO   A CD   1 
ATOM   555  N  N    . CYS   A 1 73  ? -40.61312 -33.85335 9.98729   1.000 20.48904 ? 73  CYS   A N    1 
ATOM   556  C  CA   . CYS   A 1 73  ? -39.95355 -32.81122 9.21215   1.000 21.04018 ? 73  CYS   A CA   1 
ATOM   557  C  C    . CYS   A 1 73  ? -39.76408 -31.58022 10.08825  1.000 23.81998 ? 73  CYS   A C    1 
ATOM   558  O  O    . CYS   A 1 73  ? -40.69709 -31.15937 10.78172  1.000 20.26065 ? 73  CYS   A O    1 
ATOM   559  C  CB   . CYS   A 1 73  ? -40.77026 -32.46320 7.96342   1.000 20.99766 ? 73  CYS   A CB   1 
ATOM   560  S  SG   . CYS   A 1 73  ? -40.73960 -33.73336 6.66774   1.000 21.14124 ? 73  CYS   A SG   1 
ATOM   561  N  N    . TYR   A 1 74  ? -38.56082 -31.00327 10.04959  1.000 20.97527 ? 74  TYR   A N    1 
ATOM   562  C  CA   . TYR   A 1 74  ? -38.19133 -29.88438 10.90631  1.000 20.07223 ? 74  TYR   A CA   1 
ATOM   563  C  C    . TYR   A 1 74  ? -37.68353 -28.72148 10.06336  1.000 21.31425 ? 74  TYR   A C    1 
ATOM   564  O  O    . TYR   A 1 74  ? -37.16935 -28.91242 8.95780   1.000 20.32124 ? 74  TYR   A O    1 
ATOM   565  C  CB   . TYR   A 1 74  ? -37.11487 -30.29452 11.92222  1.000 20.02887 ? 74  TYR   A CB   1 
ATOM   566  C  CG   . TYR   A 1 74  ? -37.48736 -31.49351 12.76677  1.000 21.60538 ? 74  TYR   A CG   1 
ATOM   567  C  CD1  . TYR   A 1 74  ? -37.19806 -32.78402 12.34028  1.000 21.06241 ? 74  TYR   A CD1  1 
ATOM   568  C  CD2  . TYR   A 1 74  ? -38.11873 -31.33560 13.99480  1.000 23.42029 ? 74  TYR   A CD2  1 
ATOM   569  C  CE1  . TYR   A 1 74  ? -37.53226 -33.88619 13.10858  1.000 23.05471 ? 74  TYR   A CE1  1 
ATOM   570  C  CE2  . TYR   A 1 74  ? -38.45692 -32.43366 14.77239  1.000 23.03549 ? 74  TYR   A CE2  1 
ATOM   571  C  CZ   . TYR   A 1 74  ? -38.16038 -33.70551 14.32314  1.000 22.56610 ? 74  TYR   A CZ   1 
ATOM   572  O  OH   . TYR   A 1 74  ? -38.49118 -34.80218 15.08696  1.000 24.91685 ? 74  TYR   A OH   1 
ATOM   573  N  N    . PHE   A 1 75  ? -37.81545 -27.51057 10.60547  1.000 19.54892 ? 75  PHE   A N    1 
ATOM   574  C  CA   . PHE   A 1 75  ? -37.46083 -26.29709 9.87943   1.000 19.15235 ? 75  PHE   A CA   1 
ATOM   575  C  C    . PHE   A 1 75  ? -36.73587 -25.32358 10.79441  1.000 20.55925 ? 75  PHE   A C    1 
ATOM   576  O  O    . PHE   A 1 75  ? -37.22495 -25.00322 11.88209  1.000 19.80232 ? 75  PHE   A O    1 
ATOM   577  C  CB   . PHE   A 1 75  ? -38.70668 -25.62103 9.29041   1.000 18.62099 ? 75  PHE   A CB   1 
ATOM   578  C  CG   . PHE   A 1 75  ? -38.40727 -24.38155 8.48792   1.000 18.96122 ? 75  PHE   A CG   1 
ATOM   579  C  CD1  . PHE   A 1 75  ? -37.87674 -24.47580 7.21059   1.000 22.00452 ? 75  PHE   A CD1  1 
ATOM   580  C  CD2  . PHE   A 1 75  ? -38.66674 -23.12237 9.00848   1.000 21.39801 ? 75  PHE   A CD2  1 
ATOM   581  C  CE1  . PHE   A 1 75  ? -37.60428 -23.33449 6.46692   1.000 20.25577 ? 75  PHE   A CE1  1 
ATOM   582  C  CE2  . PHE   A 1 75  ? -38.39835 -21.97912 8.27197   1.000 23.09266 ? 75  PHE   A CE2  1 
ATOM   583  C  CZ   . PHE   A 1 75  ? -37.86648 -22.08588 6.99840   1.000 18.99044 ? 75  PHE   A CZ   1 
ATOM   584  N  N    . ILE   A 1 76  ? -35.57290 -24.85949 10.34670  1.000 18.33928 ? 76  ILE   A N    1 
ATOM   585  C  CA   . ILE   A 1 76  ? -34.87523 -23.72760 10.94414  1.000 20.35665 ? 76  ILE   A CA   1 
ATOM   586  C  C    . ILE   A 1 76  ? -34.93628 -22.58783 9.93966   1.000 21.46527 ? 76  ILE   A C    1 
ATOM   587  O  O    . ILE   A 1 76  ? -34.77641 -22.81074 8.73540   1.000 20.58514 ? 76  ILE   A O    1 
ATOM   588  C  CB   . ILE   A 1 76  ? -33.41639 -24.07493 11.30921  1.000 20.20432 ? 76  ILE   A CB   1 
ATOM   589  C  CG1  . ILE   A 1 76  ? -33.37492 -25.03336 12.50153  1.000 19.72515 ? 76  ILE   A CG1  1 
ATOM   590  C  CG2  . ILE   A 1 76  ? -32.60353 -22.81269 11.60924  1.000 22.06520 ? 76  ILE   A CG2  1 
ATOM   591  C  CD1  . ILE   A 1 76  ? -31.97234 -25.35299 12.98247  1.000 22.22410 ? 76  ILE   A CD1  1 
ATOM   592  N  N    . HIS   A 1 77  ? -35.19189 -21.37600 10.42705  1.000 18.21724 ? 77  HIS   A N    1 
ATOM   593  C  CA   . HIS   A 1 77  ? -35.36215 -20.23364 9.53968   1.000 19.76569 ? 77  HIS   A CA   1 
ATOM   594  C  C    . HIS   A 1 77  ? -34.04608 -19.83528 8.87971   1.000 19.84752 ? 77  HIS   A C    1 
ATOM   595  O  O    . HIS   A 1 77  ? -32.96519 -19.96309 9.46107   1.000 20.64954 ? 77  HIS   A O    1 
ATOM   596  C  CB   . HIS   A 1 77  ? -35.92081 -19.03285 10.30585  1.000 19.39252 ? 77  HIS   A CB   1 
ATOM   597  C  CG   . HIS   A 1 77  ? -37.34205 -19.19710 10.74564  1.000 24.66836 ? 77  HIS   A CG   1 
ATOM   598  N  ND1  . HIS   A 1 77  ? -37.68720 -19.78181 11.94496  1.000 25.30179 ? 77  HIS   A ND1  1 
ATOM   599  C  CD2  . HIS   A 1 77  ? -38.50628 -18.84657 10.14898  1.000 22.26069 ? 77  HIS   A CD2  1 
ATOM   600  C  CE1  . HIS   A 1 77  ? -39.00282 -19.78617 12.06732  1.000 25.94236 ? 77  HIS   A CE1  1 
ATOM   601  N  NE2  . HIS   A 1 77  ? -39.52371 -19.22521 10.99077  1.000 25.57530 ? 77  HIS   A NE2  1 
ATOM   602  N  N    . GLY   A 1 78  ? -34.15365 -19.33755 7.64590   1.000 19.72326 ? 78  GLY   A N    1 
ATOM   603  C  CA   . GLY   A 1 78  ? -33.05770 -18.67254 6.97998   1.000 18.66519 ? 78  GLY   A CA   1 
ATOM   604  C  C    . GLY   A 1 78  ? -33.24898 -17.16103 6.97209   1.000 22.23190 ? 78  GLY   A C    1 
ATOM   605  O  O    . GLY   A 1 78  ? -34.19983 -16.61697 7.52715   1.000 21.88017 ? 78  GLY   A O    1 
ATOM   606  N  N    . ASN   A 1 79  ? -32.30906 -16.47626 6.31740   1.000 23.98433 ? 79  ASN   A N    1 
ATOM   607  C  CA   . ASN   A 1 79  ? -32.42386 -15.02655 6.20666   1.000 23.08253 ? 79  ASN   A CA   1 
ATOM   608  C  C    . ASN   A 1 79  ? -33.47831 -14.60530 5.19274   1.000 24.52625 ? 79  ASN   A C    1 
ATOM   609  O  O    . ASN   A 1 79  ? -33.96129 -13.46959 5.25702   1.000 24.09995 ? 79  ASN   A O    1 
ATOM   610  C  CB   . ASN   A 1 79  ? -31.07645 -14.40566 5.83752   1.000 24.67936 ? 79  ASN   A CB   1 
ATOM   611  C  CG   . ASN   A 1 79  ? -30.49315 -14.99151 4.57323   1.000 24.55490 ? 79  ASN   A CG   1 
ATOM   612  O  OD1  . ASN   A 1 79  ? -30.13227 -16.16573 4.53055   1.000 24.02081 ? 79  ASN   A OD1  1 
ATOM   613  N  ND2  . ASN   A 1 79  ? -30.39974 -14.17477 3.53092   1.000 24.48564 ? 79  ASN   A ND2  1 
ATOM   614  N  N    . ARG   A 1 80  ? -33.84688 -15.48884 4.26301   1.000 19.45238 ? 80  ARG   A N    1 
ATOM   615  C  CA   . ARG   A 1 80  ? -34.87138 -15.14877 3.28155   1.000 24.70504 ? 80  ARG   A CA   1 
ATOM   616  C  C    . ARG   A 1 80  ? -36.27808 -15.38694 3.82193   1.000 23.01095 ? 80  ARG   A C    1 
ATOM   617  O  O    . ARG   A 1 80  ? -37.19245 -14.60618 3.53536   1.000 25.69997 ? 80  ARG   A O    1 
ATOM   618  C  CB   . ARG   A 1 80  ? -34.65530 -15.94634 1.99108   1.000 21.15791 ? 80  ARG   A CB   1 
ATOM   619  C  CG   . ARG   A 1 80  ? -33.27295 -15.78346 1.37363   1.000 24.03140 ? 80  ARG   A CG   1 
ATOM   620  C  CD   . ARG   A 1 80  ? -32.96979 -14.32268 1.05366   1.000 24.66238 ? 80  ARG   A CD   1 
ATOM   621  N  NE   . ARG   A 1 80  ? -33.91188 -13.75760 0.09362   1.000 25.63557 ? 80  ARG   A NE   1 
ATOM   622  C  CZ   . ARG   A 1 80  ? -33.74942 -12.59290 -0.51990  1.000 28.06976 ? 80  ARG   A CZ   1 
ATOM   623  N  NH1  . ARG   A 1 80  ? -32.69336 -11.83087 -0.28818  1.000 24.94171 ? 80  ARG   A NH1  1 
ATOM   624  N  NH2  . ARG   A 1 80  ? -34.66833 -12.18367 -1.39026  1.000 31.05788 ? 80  ARG   A NH2  1 
ATOM   625  N  N    . ASP   A 1 81  ? -36.47369 -16.44482 4.60654   1.000 22.31312 ? 81  ASP   A N    1 
ATOM   626  C  CA   . ASP   A 1 81  ? -37.80342 -16.86330 5.03575   1.000 21.32981 ? 81  ASP   A CA   1 
ATOM   627  C  C    . ASP   A 1 81  ? -37.93092 -16.87519 6.55706   1.000 21.46793 ? 81  ASP   A C    1 
ATOM   628  O  O    . ASP   A 1 81  ? -38.52125 -17.78630 7.14167   1.000 22.74741 ? 81  ASP   A O    1 
ATOM   629  C  CB   . ASP   A 1 81  ? -38.15226 -18.23295 4.45371   1.000 19.58169 ? 81  ASP   A CB   1 
ATOM   630  C  CG   . ASP   A 1 81  ? -37.01787 -19.24128 4.58887   1.000 21.55124 ? 81  ASP   A CG   1 
ATOM   631  O  OD1  . ASP   A 1 81  ? -36.03575 -18.95713 5.30626   1.000 20.51987 ? 81  ASP   A OD1  1 
ATOM   632  O  OD2  . ASP   A 1 81  ? -37.11310 -20.32813 3.97804   1.000 20.32899 ? 81  ASP   A OD2  1 
ATOM   633  N  N    . PHE   A 1 82  ? -37.39795 -15.84650 7.22018   1.000 19.97674 ? 82  PHE   A N    1 
ATOM   634  C  CA   . PHE   A 1 82  ? -37.48180 -15.77304 8.67519   1.000 20.44062 ? 82  PHE   A CA   1 
ATOM   635  C  C    . PHE   A 1 82  ? -38.90010 -15.53380 9.18339   1.000 21.88128 ? 82  PHE   A C    1 
ATOM   636  O  O    . PHE   A 1 82  ? -39.14494 -15.70827 10.38179  1.000 21.45573 ? 82  PHE   A O    1 
ATOM   637  C  CB   . PHE   A 1 82  ? -36.54967 -14.67755 9.20588   1.000 23.06278 ? 82  PHE   A CB   1 
ATOM   638  C  CG   . PHE   A 1 82  ? -36.81981 -13.31292 8.62996   1.000 24.93154 ? 82  PHE   A CG   1 
ATOM   639  C  CD1  . PHE   A 1 82  ? -36.20986 -12.91051 7.45251   1.000 24.94875 ? 82  PHE   A CD1  1 
ATOM   640  C  CD2  . PHE   A 1 82  ? -37.68022 -12.43286 9.26574   1.000 23.78377 ? 82  PHE   A CD2  1 
ATOM   641  C  CE1  . PHE   A 1 82  ? -36.45490 -11.65897 6.91824   1.000 26.36709 ? 82  PHE   A CE1  1 
ATOM   642  C  CE2  . PHE   A 1 82  ? -37.92944 -11.17813 8.73513   1.000 25.34413 ? 82  PHE   A CE2  1 
ATOM   643  C  CZ   . PHE   A 1 82  ? -37.31715 -10.79200 7.56066   1.000 25.08791 ? 82  PHE   A CZ   1 
ATOM   644  N  N    . LEU   A 1 83  ? -39.83727 -15.15273 8.31994   1.000 18.60557 ? 83  LEU   A N    1 
ATOM   645  C  CA   . LEU   A 1 83  ? -41.20427 -14.89792 8.75508   1.000 19.60898 ? 83  LEU   A CA   1 
ATOM   646  C  C    . LEU   A 1 83  ? -42.10515 -16.12399 8.66307   1.000 21.40550 ? 83  LEU   A C    1 
ATOM   647  O  O    . LEU   A 1 83  ? -43.30649 -16.00778 8.92841   1.000 23.65358 ? 83  LEU   A O    1 
ATOM   648  C  CB   . LEU   A 1 83  ? -41.81354 -13.75127 7.94492   1.000 17.13760 ? 83  LEU   A CB   1 
ATOM   649  C  CG   . LEU   A 1 83  ? -41.24569 -12.36597 8.25908   1.000 19.85163 ? 83  LEU   A CG   1 
ATOM   650  C  CD1  . LEU   A 1 83  ? -41.94971 -11.29236 7.44576   1.000 21.42790 ? 83  LEU   A CD1  1 
ATOM   651  C  CD2  . LEU   A 1 83  ? -41.34691 -12.07045 9.75053   1.000 25.60654 ? 83  LEU   A CD2  1 
ATOM   652  N  N    . VAL   A 1 84  ? -41.56428 -17.28608 8.29141   1.000 18.21725 ? 84  VAL   A N    1 
ATOM   653  C  CA   . VAL   A 1 84  ? -42.35312 -18.51471 8.30002   1.000 19.29927 ? 84  VAL   A CA   1 
ATOM   654  C  C    . VAL   A 1 84  ? -42.81567 -18.78420 9.72428   1.000 21.96548 ? 84  VAL   A C    1 
ATOM   655  O  O    . VAL   A 1 84  ? -41.99962 -18.88353 10.64873  1.000 22.12430 ? 84  VAL   A O    1 
ATOM   656  C  CB   . VAL   A 1 84  ? -41.53834 -19.68660 7.74154   1.000 21.46765 ? 84  VAL   A CB   1 
ATOM   657  C  CG1  . VAL   A 1 84  ? -42.24464 -21.00677 8.02257   1.000 18.70577 ? 84  VAL   A CG1  1 
ATOM   658  C  CG2  . VAL   A 1 84  ? -41.30328 -19.51222 6.24817   1.000 16.72693 ? 84  VAL   A CG2  1 
ATOM   659  N  N    . GLY   A 1 85  ? -44.12887 -18.89383 9.91257   1.000 19.01007 ? 85  GLY   A N    1 
ATOM   660  C  CA   . GLY   A 1 85  ? -44.67218 -19.01338 11.25177  1.000 23.74681 ? 85  GLY   A CA   1 
ATOM   661  C  C    . GLY   A 1 85  ? -45.44281 -20.28806 11.53050  1.000 28.03673 ? 85  GLY   A C    1 
ATOM   662  O  O    . GLY   A 1 85  ? -45.35100 -21.26535 10.78091  1.000 23.74609 ? 85  GLY   A O    1 
ATOM   663  N  N    . GLN   A 1 86  ? -46.22700 -20.27368 12.61112  1.000 26.34496 ? 86  GLN   A N    1 
ATOM   664  C  CA   . GLN   A 1 86  ? -46.88108 -21.49099 13.07724  1.000 28.74363 ? 86  GLN   A CA   1 
ATOM   665  C  C    . GLN   A 1 86  ? -48.04677 -21.89780 12.18582  1.000 28.54860 ? 86  GLN   A C    1 
ATOM   666  O  O    . GLN   A 1 86  ? -48.39352 -23.08280 12.13314  1.000 24.18045 ? 86  GLN   A O    1 
ATOM   667  C  CB   . GLN   A 1 86  ? -47.35327 -21.30823 14.51842  1.000 31.78922 ? 86  GLN   A CB   1 
ATOM   668  C  CG   . GLN   A 1 86  ? -46.36327 -21.81718 15.54619  1.000 38.72461 ? 86  GLN   A CG   1 
ATOM   669  C  CD   . GLN   A 1 86  ? -46.05213 -23.29081 15.37025  1.000 36.28656 ? 86  GLN   A CD   1 
ATOM   670  O  OE1  . GLN   A 1 86  ? -44.89053 -23.69472 15.37752  1.000 38.12872 ? 86  GLN   A OE1  1 
ATOM   671  N  NE2  . GLN   A 1 86  ? -47.09187 -24.10259 15.21129  1.000 49.77936 ? 86  GLN   A NE2  1 
ATOM   672  N  N    . ARG   A 1 87  ? -48.66972 -20.94313 11.49170  1.000 25.31036 ? 87  ARG   A N    1 
ATOM   673  C  CA   . ARG   A 1 87  ? -49.73465 -21.29435 10.55743  1.000 26.26682 ? 87  ARG   A CA   1 
ATOM   674  C  C    . ARG   A 1 87  ? -49.20407 -22.17669 9.43349   1.000 25.51747 ? 87  ARG   A C    1 
ATOM   675  O  O    . ARG   A 1 87  ? -49.80879 -23.20043 9.09435   1.000 23.67952 ? 87  ARG   A O    1 
ATOM   676  C  CB   . ARG   A 1 87  ? -50.38381 -20.02949 9.99443   1.000 28.18975 ? 87  ARG   A CB   1 
ATOM   677  C  CG   . ARG   A 1 87  ? -51.46036 -20.29733 8.95352   1.000 30.12520 ? 87  ARG   A CG   1 
ATOM   678  C  CD   . ARG   A 1 87  ? -52.47499 -19.16688 8.90490   1.000 36.11766 ? 87  ARG   A CD   1 
ATOM   679  N  NE   . ARG   A 1 87  ? -53.44003 -19.34440 7.82686   1.000 44.69994 ? 87  ARG   A NE   1 
ATOM   680  C  CZ   . ARG   A 1 87  ? -54.08588 -18.35239 7.22913   1.000 47.44016 ? 87  ARG   A CZ   1 
ATOM   681  N  NH1  . ARG   A 1 87  ? -53.90560 -17.09266 7.59135   1.000 37.73035 ? 87  ARG   A NH1  1 
ATOM   682  N  NH2  . ARG   A 1 87  ? -54.93357 -18.63113 6.24289   1.000 49.82819 ? 87  ARG   A NH2  1 
ATOM   683  N  N    . PHE   A 1 88  ? -48.06713 -21.79707 8.84392   1.000 21.94730 ? 88  PHE   A N    1 
ATOM   684  C  CA   . PHE   A 1 88  ? -47.47534 -22.63020 7.80255   1.000 22.47515 ? 88  PHE   A CA   1 
ATOM   685  C  C    . PHE   A 1 88  ? -46.93836 -23.93647 8.36888   1.000 24.37095 ? 88  PHE   A C    1 
ATOM   686  O  O    . PHE   A 1 88  ? -46.97098 -24.96563 7.68371   1.000 21.53047 ? 88  PHE   A O    1 
ATOM   687  C  CB   . PHE   A 1 88  ? -46.35940 -21.87969 7.07597   1.000 24.21247 ? 88  PHE   A CB   1 
ATOM   688  C  CG   . PHE   A 1 88  ? -45.76484 -22.65360 5.93432   1.000 20.80516 ? 88  PHE   A CG   1 
ATOM   689  C  CD1  . PHE   A 1 88  ? -46.41966 -22.72561 4.71552   1.000 20.95102 ? 88  PHE   A CD1  1 
ATOM   690  C  CD2  . PHE   A 1 88  ? -44.56178 -23.32308 6.08463   1.000 19.97475 ? 88  PHE   A CD2  1 
ATOM   691  C  CE1  . PHE   A 1 88  ? -45.88082 -23.44498 3.66543   1.000 24.99368 ? 88  PHE   A CE1  1 
ATOM   692  C  CE2  . PHE   A 1 88  ? -44.01725 -24.04341 5.03871   1.000 20.48002 ? 88  PHE   A CE2  1 
ATOM   693  C  CZ   . PHE   A 1 88  ? -44.67742 -24.10425 3.82719   1.000 22.14446 ? 88  PHE   A CZ   1 
ATOM   694  N  N    . ALA   A 1 89  ? -46.43234 -23.91474 9.60494   1.000 20.43025 ? 89  ALA   A N    1 
ATOM   695  C  CA   . ALA   A 1 89  ? -45.98807 -25.15200 10.23660  1.000 25.75715 ? 89  ALA   A CA   1 
ATOM   696  C  C    . ALA   A 1 89  ? -47.13470 -26.14633 10.34752  1.000 23.58307 ? 89  ALA   A C    1 
ATOM   697  O  O    . ALA   A 1 89  ? -46.95895 -27.34089 10.08104  1.000 24.53446 ? 89  ALA   A O    1 
ATOM   698  C  CB   . ALA   A 1 89  ? -45.39353 -24.85918 11.61425  1.000 20.35496 ? 89  ALA   A CB   1 
ATOM   699  N  N    . ARG   A 1 90  ? -48.32322 -25.66485 10.72081  1.000 24.48355 ? 90  ARG   A N    1 
ATOM   700  C  CA   . ARG   A 1 90  ? -49.48279 -26.54338 10.83502  1.000 24.51181 ? 90  ARG   A CA   1 
ATOM   701  C  C    . ARG   A 1 90  ? -49.93335 -27.05286 9.47116   1.000 28.42788 ? 90  ARG   A C    1 
ATOM   702  O  O    . ARG   A 1 90  ? -50.28160 -28.23116 9.32939   1.000 26.88881 ? 90  ARG   A O    1 
ATOM   703  C  CB   . ARG   A 1 90  ? -50.62976 -25.81141 11.53125  1.000 27.22563 ? 90  ARG   A CB   1 
ATOM   704  C  CG   . ARG   A 1 90  ? -50.38964 -25.52358 13.00121  1.000 33.55878 ? 90  ARG   A CG   1 
ATOM   705  C  CD   . ARG   A 1 90  ? -51.68007 -25.11287 13.69113  1.000 43.83388 ? 90  ARG   A CD   1 
ATOM   706  N  NE   . ARG   A 1 90  ? -52.13524 -23.79787 13.25605  1.000 49.72308 ? 90  ARG   A NE   1 
ATOM   707  C  CZ   . ARG   A 1 90  ? -51.93524 -22.67295 13.92913  1.000 51.13088 ? 90  ARG   A CZ   1 
ATOM   708  N  NH1  . ARG   A 1 90  ? -51.29062 -22.66333 15.08460  1.000 51.03278 ? 90  ARG   A NH1  1 
ATOM   709  N  NH2  . ARG   A 1 90  ? -52.39464 -21.52869 13.43077  1.000 45.64857 ? 90  ARG   A NH2  1 
ATOM   710  N  N    . GLN   A 1 91  ? -49.94959 -26.17729 8.46072   1.000 25.31981 ? 91  GLN   A N    1 
ATOM   711  C  CA   . GLN   A 1 91  ? -50.36576 -26.59287 7.12359   1.000 29.57746 ? 91  GLN   A CA   1 
ATOM   712  C  C    . GLN   A 1 91  ? -49.42702 -27.64854 6.55193   1.000 24.19573 ? 91  GLN   A C    1 
ATOM   713  O  O    . GLN   A 1 91  ? -49.86681 -28.56866 5.85223   1.000 23.64250 ? 91  GLN   A O    1 
ATOM   714  C  CB   . GLN   A 1 91  ? -50.42938 -25.38315 6.18872   1.000 28.12635 ? 91  GLN   A CB   1 
ATOM   715  C  CG   . GLN   A 1 91  ? -51.40188 -24.29604 6.61292   1.000 34.49984 ? 91  GLN   A CG   1 
ATOM   716  C  CD   . GLN   A 1 91  ? -51.46554 -23.15639 5.61249   1.000 43.69366 ? 91  GLN   A CD   1 
ATOM   717  O  OE1  . GLN   A 1 91  ? -50.46886 -22.82164 4.97149   1.000 42.26281 ? 91  GLN   A OE1  1 
ATOM   718  N  NE2  . GLN   A 1 91  ? -52.64076 -22.55384 5.47459   1.000 47.49640 ? 91  GLN   A NE2  1 
ATOM   719  N  N    . SER   A 1 92  ? -48.13168 -27.53064 6.83484   1.000 21.57123 ? 92  SER   A N    1 
ATOM   720  C  CA   . SER   A 1 92  ? -47.12752 -28.42654 6.27896   1.000 20.86571 ? 92  SER   A CA   1 
ATOM   721  C  C    . SER   A 1 92  ? -46.82405 -29.62099 7.17147   1.000 25.86723 ? 92  SER   A C    1 
ATOM   722  O  O    . SER   A 1 92  ? -46.20790 -30.58394 6.70268   1.000 24.93306 ? 92  SER   A O    1 
ATOM   723  C  CB   . SER   A 1 92  ? -45.82715 -27.66012 6.01988   1.000 20.08048 ? 92  SER   A CB   1 
ATOM   724  O  OG   . SER   A 1 92  ? -45.31439 -27.11695 7.22505   1.000 22.70147 ? 92  SER   A OG   1 
ATOM   725  N  N    . GLY   A 1 93  ? -47.22822 -29.58427 8.43709   1.000 23.69947 ? 93  GLY   A N    1 
ATOM   726  C  CA   . GLY   A 1 93  ? -46.83219 -30.60597 9.37836   1.000 22.56047 ? 93  GLY   A CA   1 
ATOM   727  C  C    . GLY   A 1 93  ? -45.41362 -30.48558 9.88980   1.000 23.04094 ? 93  GLY   A C    1 
ATOM   728  O  O    . GLY   A 1 93  ? -44.95561 -31.38489 10.60555  1.000 22.21914 ? 93  GLY   A O    1 
ATOM   729  N  N    . MET   A 1 94  ? -44.70159 -29.41328 9.55101   1.000 19.65558 ? 94  MET   A N    1 
ATOM   730  C  CA   . MET   A 1 94  ? -43.33435 -29.24337 10.01822  1.000 20.76556 ? 94  MET   A CA   1 
ATOM   731  C  C    . MET   A 1 94  ? -43.30848 -28.70911 11.44290  1.000 25.50427 ? 94  MET   A C    1 
ATOM   732  O  O    . MET   A 1 94  ? -44.23873 -28.03764 11.89875  1.000 24.69885 ? 94  MET   A O    1 
ATOM   733  C  CB   . MET   A 1 94  ? -42.55294 -28.28625 9.11522   1.000 24.71225 ? 94  MET   A CB   1 
ATOM   734  C  CG   . MET   A 1 94  ? -41.99021 -28.91068 7.85365   1.000 27.56941 ? 94  MET   A CG   1 
ATOM   735  S  SD   . MET   A 1 94  ? -40.91719 -27.78329 6.93701   1.000 26.46621 ? 94  MET   A SD   1 
ATOM   736  C  CE   . MET   A 1 94  ? -41.87929 -26.27369 6.96745   1.000 24.59880 ? 94  MET   A CE   1 
ATOM   737  N  N    . ILE   A 1 95  ? -42.21462 -29.00306 12.13775  1.000 20.31550 ? 95  ILE   A N    1 
ATOM   738  C  CA   . ILE   A 1 95  ? -41.95229 -28.47997 13.47125  1.000 22.71198 ? 95  ILE   A CA   1 
ATOM   739  C  C    . ILE   A 1 95  ? -40.89581 -27.39134 13.35488  1.000 23.10411 ? 95  ILE   A C    1 
ATOM   740  O  O    . ILE   A 1 95  ? -39.83116 -27.61018 12.76374  1.000 21.88018 ? 95  ILE   A O    1 
ATOM   741  C  CB   . ILE   A 1 95  ? -41.49472 -29.59622 14.42534  1.000 23.61248 ? 95  ILE   A CB   1 
ATOM   742  C  CG1  . ILE   A 1 95  ? -42.64007 -30.57689 14.68731  1.000 27.48527 ? 95  ILE   A CG1  1 
ATOM   743  C  CG2  . ILE   A 1 95  ? -40.97759 -29.01018 15.72679  1.000 19.23790 ? 95  ILE   A CG2  1 
ATOM   744  C  CD1  . ILE   A 1 95  ? -42.18176 -31.99066 14.97639  1.000 34.07400 ? 95  ILE   A CD1  1 
ATOM   745  N  N    . LEU   A 1 96  ? -41.18669 -26.21866 13.91273  1.000 19.76961 ? 96  LEU   A N    1 
ATOM   746  C  CA   . LEU   A 1 96  ? -40.25190 -25.10252 13.86314  1.000 19.01675 ? 96  LEU   A CA   1 
ATOM   747  C  C    . LEU   A 1 96  ? -39.22264 -25.23175 14.97966  1.000 21.99292 ? 96  LEU   A C    1 
ATOM   748  O  O    . LEU   A 1 96  ? -39.57900 -25.42856 16.14568  1.000 23.05155 ? 96  LEU   A O    1 
ATOM   749  C  CB   . LEU   A 1 96  ? -40.99721 -23.77298 13.98839  1.000 22.53833 ? 96  LEU   A CB   1 
ATOM   750  C  CG   . LEU   A 1 96  ? -42.18082 -23.50552 13.05391  1.000 25.22710 ? 96  LEU   A CG   1 
ATOM   751  C  CD1  . LEU   A 1 96  ? -42.77068 -22.12705 13.32868  1.000 24.90312 ? 96  LEU   A CD1  1 
ATOM   752  C  CD2  . LEU   A 1 96  ? -41.77434 -23.63328 11.59358  1.000 25.28741 ? 96  LEU   A CD2  1 
ATOM   753  N  N    . LEU   A 1 97  ? -37.94879 -25.10831 14.62548  1.000 19.65083 ? 97  LEU   A N    1 
ATOM   754  C  CA   . LEU   A 1 97  ? -36.85645 -25.19980 15.58245  1.000 22.16268 ? 97  LEU   A CA   1 
ATOM   755  C  C    . LEU   A 1 97  ? -36.20586 -23.83495 15.77296  1.000 24.33009 ? 97  LEU   A C    1 
ATOM   756  O  O    . LEU   A 1 97  ? -36.44414 -22.89000 15.01615  1.000 24.03090 ? 97  LEU   A O    1 
ATOM   757  C  CB   . LEU   A 1 97  ? -35.81494 -26.22735 15.12268  1.000 17.96892 ? 97  LEU   A CB   1 
ATOM   758  C  CG   . LEU   A 1 97  ? -36.29887 -27.66673 14.93042  1.000 21.11674 ? 97  LEU   A CG   1 
ATOM   759  C  CD1  . LEU   A 1 97  ? -35.14198 -28.56943 14.51204  1.000 20.38073 ? 97  LEU   A CD1  1 
ATOM   760  C  CD2  . LEU   A 1 97  ? -36.96777 -28.18887 16.19566  1.000 22.22286 ? 97  LEU   A CD2  1 
ATOM   761  N  N    . ALA   A 1 98  ? -35.36777 -23.74359 16.80282  1.000 24.21623 ? 98  ALA   A N    1 
ATOM   762  C  CA   . ALA   A 1 98  ? -34.65156 -22.50952 17.08027  1.000 22.39863 ? 98  ALA   A CA   1 
ATOM   763  C  C    . ALA   A 1 98  ? -33.52081 -22.31186 16.07016  1.000 26.17021 ? 98  ALA   A C    1 
ATOM   764  O  O    . ALA   A 1 98  ? -33.21294 -23.18745 15.25620  1.000 25.09269 ? 98  ALA   A O    1 
ATOM   765  C  CB   . ALA   A 1 98  ? -34.10242 -22.51932 18.50655  1.000 26.90110 ? 98  ALA   A CB   1 
ATOM   766  N  N    . GLU   A 1 99  ? -32.88899 -21.13577 16.13186  1.000 27.07869 ? 99  GLU   A N    1 
ATOM   767  C  CA   . GLU   A 1 99  ? -31.81641 -20.83323 15.18908  1.000 27.68401 ? 99  GLU   A CA   1 
ATOM   768  C  C    . GLU   A 1 99  ? -30.61212 -21.74740 15.37517  1.000 24.44061 ? 99  GLU   A C    1 
ATOM   769  O  O    . GLU   A 1 99  ? -29.83317 -21.92387 14.43382  1.000 27.07298 ? 99  GLU   A O    1 
ATOM   770  C  CB   . GLU   A 1 99  ? -31.38324 -19.37047 15.31319  1.000 27.51166 ? 99  GLU   A CB   1 
ATOM   771  C  CG   . GLU   A 1 99  ? -30.78596 -18.99243 16.65554  1.000 30.21893 ? 99  GLU   A CG   1 
ATOM   772  C  CD   . GLU   A 1 99  ? -30.29824 -17.55478 16.68297  1.000 41.57948 ? 99  GLU   A CD   1 
ATOM   773  O  OE1  . GLU   A 1 99  ? -31.13757 -16.63833 16.56457  1.000 44.71742 ? 99  GLU   A OE1  1 
ATOM   774  O  OE2  . GLU   A 1 99  ? -29.07520 -17.33998 16.81749  1.000 45.67336 ? 99  GLU   A OE2  1 
ATOM   775  N  N    . GLU   A 1 100 ? -30.43812 -22.32267 16.56372  1.000 26.16982 ? 100 GLU   A N    1 
ATOM   776  C  CA   . GLU   A 1 100 ? -29.42219 -23.33352 16.82278  1.000 27.88715 ? 100 GLU   A CA   1 
ATOM   777  C  C    . GLU   A 1 100 ? -30.07303 -24.50416 17.54310  1.000 25.70515 ? 100 GLU   A C    1 
ATOM   778  O  O    . GLU   A 1 100 ? -30.85954 -24.30640 18.47357  1.000 27.01555 ? 100 GLU   A O    1 
ATOM   779  C  CB   . GLU   A 1 100 ? -28.27109 -22.78537 17.68003  1.000 30.99134 ? 100 GLU   A CB   1 
ATOM   780  C  CG   . GLU   A 1 100 ? -27.38759 -21.75730 16.99693  1.000 33.29535 ? 100 GLU   A CG   1 
ATOM   781  C  CD   . GLU   A 1 100 ? -26.30788 -21.22292 17.92118  1.000 35.23123 ? 100 GLU   A CD   1 
ATOM   782  O  OE1  . GLU   A 1 100 ? -26.26402 -21.64643 19.09634  1.000 38.98593 ? 100 GLU   A OE1  1 
ATOM   783  O  OE2  . GLU   A 1 100 ? -25.50211 -20.37996 17.47510  1.000 38.24883 ? 100 GLU   A OE2  1 
ATOM   784  N  N    . GLU   A 1 101 ? -29.75218 -25.72112 17.10775  1.000 24.22864 ? 101 GLU   A N    1 
ATOM   785  C  CA   . GLU   A 1 101 ? -30.21775 -26.92786 17.77603  1.000 26.29477 ? 101 GLU   A CA   1 
ATOM   786  C  C    . GLU   A 1 101 ? -29.09355 -27.95188 17.80523  1.000 27.00235 ? 101 GLU   A C    1 
ATOM   787  O  O    . GLU   A 1 101 ? -28.27842 -28.02867 16.88254  1.000 28.20801 ? 101 GLU   A O    1 
ATOM   788  C  CB   . GLU   A 1 101 ? -31.45185 -27.53921 17.08956  1.000 26.60901 ? 101 GLU   A CB   1 
ATOM   789  C  CG   . GLU   A 1 101 ? -32.68161 -26.64006 17.03918  1.000 26.34885 ? 101 GLU   A CG   1 
ATOM   790  C  CD   . GLU   A 1 101 ? -33.41415 -26.53860 18.36982  1.000 27.73303 ? 101 GLU   A CD   1 
ATOM   791  O  OE1  . GLU   A 1 101 ? -32.96513 -27.14789 19.36392  1.000 32.61030 ? 101 GLU   A OE1  1 
ATOM   792  O  OE2  . GLU   A 1 101 ? -34.45807 -25.85410 18.41491  1.000 28.47123 ? 101 GLU   A OE2  1 
ATOM   793  N  N    . ARG   A 1 102 ? -29.05620 -28.73477 18.87925  1.000 26.71645 ? 102 ARG   A N    1 
ATOM   794  C  CA   . ARG   A 1 102 ? -28.11182 -29.83471 19.02910  1.000 28.98129 ? 102 ARG   A CA   1 
ATOM   795  C  C    . ARG   A 1 102 ? -28.87721 -31.14487 18.90357  1.000 32.78257 ? 102 ARG   A C    1 
ATOM   796  O  O    . ARG   A 1 102 ? -29.83907 -31.37852 19.64316  1.000 35.28485 ? 102 ARG   A O    1 
ATOM   797  C  CB   . ARG   A 1 102 ? -27.38297 -29.75892 20.37047  1.000 30.82689 ? 102 ARG   A CB   1 
ATOM   798  C  CG   . ARG   A 1 102 ? -26.17741 -30.68087 20.46552  1.000 34.72278 ? 102 ARG   A CG   1 
ATOM   799  C  CD   . ARG   A 1 102 ? -26.05299 -31.27764 21.85375  1.000 43.10303 ? 102 ARG   A CD   1 
ATOM   800  N  NE   . ARG   A 1 102 ? -25.65586 -30.27937 22.83875  1.000 51.68664 ? 102 ARG   A NE   1 
ATOM   801  C  CZ   . ARG   A 1 102 ? -25.10511 -30.56215 24.01117  1.000 59.51393 ? 102 ARG   A CZ   1 
ATOM   802  N  NH1  . ARG   A 1 102 ? -24.86612 -31.81001 24.37937  1.000 57.80747 ? 102 ARG   A NH1  1 
ATOM   803  N  NH2  . ARG   A 1 102 ? -24.78534 -29.56784 24.83459  1.000 72.19503 ? 102 ARG   A NH2  1 
ATOM   804  N  N    . LEU   A 1 103 ? -28.45648 -31.98843 17.96768  1.000 29.35763 ? 103 LEU   A N    1 
ATOM   805  C  CA   . LEU   A 1 103 ? -29.13347 -33.24043 17.67539  1.000 26.61716 ? 103 LEU   A CA   1 
ATOM   806  C  C    . LEU   A 1 103 ? -28.24778 -34.41642 18.06076  1.000 30.76322 ? 103 LEU   A C    1 
ATOM   807  O  O    . LEU   A 1 103 ? -27.01743 -34.32419 18.03366  1.000 30.15675 ? 103 LEU   A O    1 
ATOM   808  C  CB   . LEU   A 1 103 ? -29.48496 -33.34364 16.18923  1.000 26.48195 ? 103 LEU   A CB   1 
ATOM   809  C  CG   . LEU   A 1 103 ? -30.26080 -32.18934 15.55373  1.000 29.41108 ? 103 LEU   A CG   1 
ATOM   810  C  CD1  . LEU   A 1 103 ? -30.42521 -32.43694 14.06072  1.000 24.64776 ? 103 LEU   A CD1  1 
ATOM   811  C  CD2  . LEU   A 1 103 ? -31.60887 -31.97887 16.23368  1.000 26.00101 ? 103 LEU   A CD2  1 
ATOM   812  N  N    . ASP   A 1 104 ? -28.88423 -35.52608 18.42244  1.000 28.10497 ? 104 ASP   A N    1 
ATOM   813  C  CA   . ASP   A 1 104 ? -28.20599 -36.81212 18.52715  1.000 31.44510 ? 104 ASP   A CA   1 
ATOM   814  C  C    . ASP   A 1 104 ? -28.56681 -37.61808 17.28744  1.000 33.11234 ? 104 ASP   A C    1 
ATOM   815  O  O    . ASP   A 1 104 ? -29.71587 -38.04272 17.12721  1.000 34.15587 ? 104 ASP   A O    1 
ATOM   816  C  CB   . ASP   A 1 104 ? -28.59384 -37.56291 19.79773  1.000 38.88152 ? 104 ASP   A CB   1 
ATOM   817  C  CG   . ASP   A 1 104 ? -27.79550 -38.84605 19.97663  1.000 41.65345 ? 104 ASP   A CG   1 
ATOM   818  O  OD1  . ASP   A 1 104 ? -26.70835 -38.79695 20.59079  1.000 48.29458 ? 104 ASP   A OD1  1 
ATOM   819  O  OD2  . ASP   A 1 104 ? -28.24811 -39.90359 19.48668  1.000 45.72105 ? 104 ASP   A OD2  1 
ATOM   820  N  N    . LEU   A 1 105 ? -27.59330 -37.81259 16.40771  1.000 29.22237 ? 105 LEU   A N    1 
ATOM   821  C  CA   . LEU   A 1 105 ? -27.77821 -38.58115 15.18227  1.000 30.73856 ? 105 LEU   A CA   1 
ATOM   822  C  C    . LEU   A 1 105 ? -26.97054 -39.86609 15.32287  1.000 30.51678 ? 105 LEU   A C    1 
ATOM   823  O  O    . LEU   A 1 105 ? -25.76367 -39.88174 15.06363  1.000 30.02854 ? 105 LEU   A O    1 
ATOM   824  C  CB   . LEU   A 1 105 ? -27.35371 -37.77396 13.95870  1.000 25.96877 ? 105 LEU   A CB   1 
ATOM   825  C  CG   . LEU   A 1 105 ? -28.12369 -36.47202 13.71910  1.000 30.51068 ? 105 LEU   A CG   1 
ATOM   826  C  CD1  . LEU   A 1 105 ? -27.49263 -35.67568 12.58549  1.000 27.88398 ? 105 LEU   A CD1  1 
ATOM   827  C  CD2  . LEU   A 1 105 ? -29.59937 -36.74749 13.43810  1.000 24.83078 ? 105 LEU   A CD2  1 
ATOM   828  N  N    . TYR   A 1 106 ? -27.64287 -40.93478 15.75556  1.000 30.65600 ? 106 TYR   A N    1 
ATOM   829  C  CA   . TYR   A 1 106 ? -27.04386 -42.26660 15.85340  1.000 33.43837 ? 106 TYR   A CA   1 
ATOM   830  C  C    . TYR   A 1 106 ? -25.78898 -42.25574 16.72316  1.000 36.82946 ? 106 TYR   A C    1 
ATOM   831  O  O    . TYR   A 1 106 ? -24.81322 -42.96034 16.45695  1.000 33.85900 ? 106 TYR   A O    1 
ATOM   832  C  CB   . TYR   A 1 106 ? -26.75516 -42.82962 14.46088  1.000 31.12081 ? 106 TYR   A CB   1 
ATOM   833  C  CG   . TYR   A 1 106 ? -27.86705 -42.52700 13.48475  1.000 31.01340 ? 106 TYR   A CG   1 
ATOM   834  C  CD1  . TYR   A 1 106 ? -29.06319 -43.23099 13.53098  1.000 34.16122 ? 106 TYR   A CD1  1 
ATOM   835  C  CD2  . TYR   A 1 106 ? -27.73556 -41.51997 12.53839  1.000 27.72549 ? 106 TYR   A CD2  1 
ATOM   836  C  CE1  . TYR   A 1 106 ? -30.09364 -42.95004 12.65371  1.000 27.92213 ? 106 TYR   A CE1  1 
ATOM   837  C  CE2  . TYR   A 1 106 ? -28.76149 -41.23012 11.65560  1.000 26.52319 ? 106 TYR   A CE2  1 
ATOM   838  C  CZ   . TYR   A 1 106 ? -29.93763 -41.94882 11.71766  1.000 25.51449 ? 106 TYR   A CZ   1 
ATOM   839  O  OH   . TYR   A 1 106 ? -30.96009 -41.66358 10.84109  1.000 27.57032 ? 106 TYR   A OH   1 
ATOM   840  N  N    . GLY   A 1 107 ? -25.82171 -41.45190 17.78645  1.000 34.22715 ? 107 GLY   A N    1 
ATOM   841  C  CA   . GLY   A 1 107 ? -24.71460 -41.32160 18.70451  1.000 36.42785 ? 107 GLY   A CA   1 
ATOM   842  C  C    . GLY   A 1 107 ? -23.88719 -40.06628 18.52005  1.000 44.94113 ? 107 GLY   A C    1 
ATOM   843  O  O    . GLY   A 1 107 ? -23.21168 -39.64267 19.46540  1.000 51.55248 ? 107 GLY   A O    1 
ATOM   844  N  N    . ARG   A 1 108 ? -23.91687 -39.46660 17.33224  1.000 38.93549 ? 108 ARG   A N    1 
ATOM   845  C  CA   . ARG   A 1 108 ? -23.18677 -38.23188 17.08347  1.000 39.98674 ? 108 ARG   A CA   1 
ATOM   846  C  C    . ARG   A 1 108 ? -23.94948 -37.04925 17.66344  1.000 35.02039 ? 108 ARG   A C    1 
ATOM   847  O  O    . ARG   A 1 108 ? -25.16198 -36.92661 17.46578  1.000 36.15219 ? 108 ARG   A O    1 
ATOM   848  C  CB   . ARG   A 1 108 ? -22.98908 -38.00833 15.58529  1.000 39.47246 ? 108 ARG   A CB   1 
ATOM   849  C  CG   . ARG   A 1 108 ? -21.85961 -38.77779 14.93409  1.000 44.58587 ? 108 ARG   A CG   1 
ATOM   850  C  CD   . ARG   A 1 108 ? -21.68997 -38.29634 13.49439  1.000 40.12390 ? 108 ARG   A CD   1 
ATOM   851  N  NE   . ARG   A 1 108 ? -21.37502 -39.36862 12.55717  1.000 48.82700 ? 108 ARG   A NE   1 
ATOM   852  C  CZ   . ARG   A 1 108 ? -22.23889 -40.28849 12.14842  1.000 43.11487 ? 108 ARG   A CZ   1 
ATOM   853  N  NH1  . ARG   A 1 108 ? -23.48896 -40.30672 12.58268  1.000 36.61108 ? 108 ARG   A NH1  1 
ATOM   854  N  NH2  . ARG   A 1 108 ? -21.84002 -41.21061 11.27727  1.000 38.97394 ? 108 ARG   A NH2  1 
ATOM   855  N  N    . GLU   A 1 109 ? -23.23829 -36.17074 18.36191  1.000 36.07275 ? 109 GLU   A N    1 
ATOM   856  C  CA   . GLU   A 1 109 ? -23.78235 -34.87606 18.75038  1.000 38.33985 ? 109 GLU   A CA   1 
ATOM   857  C  C    . GLU   A 1 109 ? -23.52442 -33.89150 17.61569  1.000 33.84194 ? 109 GLU   A C    1 
ATOM   858  O  O    . GLU   A 1 109 ? -22.36703 -33.61387 17.28132  1.000 35.35918 ? 109 GLU   A O    1 
ATOM   859  C  CB   . GLU   A 1 109 ? -23.15317 -34.38782 20.05427  1.000 41.63736 ? 109 GLU   A CB   1 
ATOM   860  C  CG   . GLU   A 1 109 ? -23.86661 -34.87166 21.30874  1.000 46.33529 ? 109 GLU   A CG   1 
ATOM   861  N  N    . VAL   A 1 110 ? -24.59700 -33.37671 17.01561  1.000 29.15058 ? 110 VAL   A N    1 
ATOM   862  C  CA   . VAL   A 1 110 ? -24.50472 -32.55971 15.81128  1.000 27.73008 ? 110 VAL   A CA   1 
ATOM   863  C  C    . VAL   A 1 110 ? -25.25846 -31.25464 16.02668  1.000 30.17684 ? 110 VAL   A C    1 
ATOM   864  O  O    . VAL   A 1 110 ? -26.43250 -31.26424 16.41361  1.000 30.73575 ? 110 VAL   A O    1 
ATOM   865  C  CB   . VAL   A 1 110 ? -25.05489 -33.29931 14.57647  1.000 23.48596 ? 110 VAL   A CB   1 
ATOM   866  C  CG1  . VAL   A 1 110 ? -24.83364 -32.46756 13.32408  1.000 23.53709 ? 110 VAL   A CG1  1 
ATOM   867  C  CG2  . VAL   A 1 110 ? -24.39772 -34.66888 14.43767  1.000 27.81143 ? 110 VAL   A CG2  1 
ATOM   868  N  N    . LEU   A 1 111 ? -24.58509 -30.13807 15.76320  1.000 26.32660 ? 111 LEU   A N    1 
ATOM   869  C  CA   . LEU   A 1 111 ? -25.19639 -28.81729 15.80902  1.000 26.52735 ? 111 LEU   A CA   1 
ATOM   870  C  C    . LEU   A 1 111 ? -25.68573 -28.42427 14.42063  1.000 26.54931 ? 111 LEU   A C    1 
ATOM   871  O  O    . LEU   A 1 111 ? -24.98509 -28.62561 13.42487  1.000 25.94906 ? 111 LEU   A O    1 
ATOM   872  C  CB   . LEU   A 1 111 ? -24.18749 -27.78981 16.32594  1.000 26.57929 ? 111 LEU   A CB   1 
ATOM   873  C  CG   . LEU   A 1 111 ? -24.50648 -26.29595 16.26345  1.000 28.01915 ? 111 LEU   A CG   1 
ATOM   874  C  CD1  . LEU   A 1 111 ? -25.70322 -25.94899 17.13503  1.000 29.51662 ? 111 LEU   A CD1  1 
ATOM   875  C  CD2  . LEU   A 1 111 ? -23.28064 -25.50328 16.68984  1.000 31.07819 ? 111 LEU   A CD2  1 
ATOM   876  N  N    . ILE   A 1 112 ? -26.89690 -27.86953 14.35488  1.000 20.08319 ? 112 ILE   A N    1 
ATOM   877  C  CA   . ILE   A 1 112 ? -27.47313 -27.42573 13.09148  1.000 21.67024 ? 112 ILE   A CA   1 
ATOM   878  C  C    . ILE   A 1 112 ? -27.93317 -25.98016 13.21827  1.000 25.34605 ? 112 ILE   A C    1 
ATOM   879  O  O    . ILE   A 1 112 ? -28.36812 -25.53213 14.28435  1.000 23.96217 ? 112 ILE   A O    1 
ATOM   880  C  CB   . ILE   A 1 112 ? -28.64553 -28.32283 12.62952  1.000 21.89151 ? 112 ILE   A CB   1 
ATOM   881  C  CG1  . ILE   A 1 112 ? -29.74696 -28.36286 13.69036  1.000 23.08140 ? 112 ILE   A CG1  1 
ATOM   882  C  CG2  . ILE   A 1 112 ? -28.14991 -29.72247 12.29178  1.000 21.99099 ? 112 ILE   A CG2  1 
ATOM   883  C  CD1  . ILE   A 1 112 ? -31.04083 -28.97355 13.20163  1.000 19.51930 ? 112 ILE   A CD1  1 
ATOM   884  N  N    . MET   A 1 113 ? -27.83560 -25.25371 12.10850  1.000 21.10789 ? 113 MET   A N    1 
ATOM   885  C  CA   . MET   A 1 113 ? -28.22564 -23.85180 12.01755  1.000 21.29565 ? 113 MET   A CA   1 
ATOM   886  C  C    . MET   A 1 113 ? -28.25355 -23.48940 10.54091  1.000 23.79308 ? 113 MET   A C    1 
ATOM   887  O  O    . MET   A 1 113 ? -27.75775 -24.23692 9.69403   1.000 20.99346 ? 113 MET   A O    1 
ATOM   888  C  CB   . MET   A 1 113 ? -27.26266 -22.93928 12.78210  1.000 21.11371 ? 113 MET   A CB   1 
ATOM   889  C  CG   . MET   A 1 113 ? -25.83049 -22.99760 12.27458  1.000 25.85641 ? 113 MET   A CG   1 
ATOM   890  S  SD   . MET   A 1 113 ? -24.72080 -21.90447 13.18360  1.000 33.98616 ? 113 MET   A SD   1 
ATOM   891  C  CE   . MET   A 1 113 ? -24.55101 -22.81118 14.71085  1.000 23.03577 ? 113 MET   A CE   1 
ATOM   892  N  N    . HIS   A 1 114 ? -28.84018 -22.33021 10.23500  1.000 21.46848 ? 114 HIS   A N    1 
ATOM   893  C  CA   . HIS   A 1 114 ? -28.80493 -21.86564 8.85305   1.000 19.13473 ? 114 HIS   A CA   1 
ATOM   894  C  C    . HIS   A 1 114 ? -27.38826 -21.48531 8.44126   1.000 20.03502 ? 114 HIS   A C    1 
ATOM   895  O  O    . HIS   A 1 114 ? -26.96992 -21.75822 7.31057   1.000 19.56537 ? 114 HIS   A O    1 
ATOM   896  C  CB   . HIS   A 1 114 ? -29.75350 -20.68604 8.64944   1.000 19.62560 ? 114 HIS   A CB   1 
ATOM   897  C  CG   . HIS   A 1 114 ? -29.78367 -20.18928 7.23771   1.000 23.12301 ? 114 HIS   A CG   1 
ATOM   898  N  ND1  . HIS   A 1 114 ? -30.11799 -20.99928 6.17339   1.000 19.70905 ? 114 HIS   A ND1  1 
ATOM   899  C  CD2  . HIS   A 1 114 ? -29.49015 -18.97712 6.71030   1.000 23.16105 ? 114 HIS   A CD2  1 
ATOM   900  C  CE1  . HIS   A 1 114 ? -30.04392 -20.30325 5.05280   1.000 21.13325 ? 114 HIS   A CE1  1 
ATOM   901  N  NE2  . HIS   A 1 114 ? -29.66481 -19.07319 5.35074   1.000 19.72449 ? 114 HIS   A NE2  1 
ATOM   902  N  N    . GLY   A 1 115 ? -26.63421 -20.86350 9.34425   1.000 19.73830 ? 115 GLY   A N    1 
ATOM   903  C  CA   . GLY   A 1 115 ? -25.25217 -20.50753 9.09509   1.000 21.58179 ? 115 GLY   A CA   1 
ATOM   904  C  C    . GLY   A 1 115 ? -24.99096 -19.02533 8.94673   1.000 23.40196 ? 115 GLY   A C    1 
ATOM   905  O  O    . GLY   A 1 115 ? -23.82177 -18.61917 8.97586   1.000 25.64813 ? 115 GLY   A O    1 
ATOM   906  N  N    . ASP   A 1 116 ? -26.02983 -18.19904 8.79049   1.000 22.28948 ? 116 ASP   A N    1 
ATOM   907  C  CA   . ASP   A 1 116 ? -25.79449 -16.77039 8.60783   1.000 24.72200 ? 116 ASP   A CA   1 
ATOM   908  C  C    . ASP   A 1 116 ? -25.24991 -16.12247 9.87526   1.000 23.82563 ? 116 ASP   A C    1 
ATOM   909  O  O    . ASP   A 1 116 ? -24.53056 -15.12058 9.79491   1.000 27.86722 ? 116 ASP   A O    1 
ATOM   910  C  CB   . ASP   A 1 116 ? -27.07619 -16.06470 8.16120   1.000 26.43643 ? 116 ASP   A CB   1 
ATOM   911  C  CG   . ASP   A 1 116 ? -28.21934 -16.25205 9.13809   1.000 27.16776 ? 116 ASP   A CG   1 
ATOM   912  O  OD1  . ASP   A 1 116 ? -28.54460 -17.40950 9.47309   1.000 24.62743 ? 116 ASP   A OD1  1 
ATOM   913  O  OD2  . ASP   A 1 116 ? -28.78712 -15.23182 9.58222   1.000 25.33217 ? 116 ASP   A OD2  1 
ATOM   914  N  N    . THR   A 1 117 ? -25.57187 -16.67395 11.04795  1.000 25.03577 ? 117 THR   A N    1 
ATOM   915  C  CA   . THR   A 1 117 ? -25.04665 -16.12925 12.29564  1.000 24.98563 ? 117 THR   A CA   1 
ATOM   916  C  C    . THR   A 1 117 ? -23.55640 -16.39155 12.47140  1.000 30.09302 ? 117 THR   A C    1 
ATOM   917  O  O    . THR   A 1 117 ? -22.94681 -15.81668 13.37977  1.000 30.05343 ? 117 THR   A O    1 
ATOM   918  C  CB   . THR   A 1 117 ? -25.81444 -16.70065 13.49106  1.000 31.78159 ? 117 THR   A CB   1 
ATOM   919  O  OG1  . THR   A 1 117 ? -25.66145 -18.12565 13.52461  1.000 28.41129 ? 117 THR   A OG1  1 
ATOM   920  C  CG2  . THR   A 1 117 ? -27.29570 -16.35253 13.39192  1.000 30.44159 ? 117 THR   A CG2  1 
ATOM   921  N  N    . LEU   A 1 118 ? -22.95971 -17.24335 11.63766  1.000 25.33294 ? 118 LEU   A N    1 
ATOM   922  C  CA   . LEU   A 1 118 ? -21.51740 -17.44395 11.65774  1.000 28.47290 ? 118 LEU   A CA   1 
ATOM   923  C  C    . LEU   A 1 118 ? -20.77446 -16.40689 10.82891  1.000 32.65718 ? 118 LEU   A C    1 
ATOM   924  O  O    . LEU   A 1 118 ? -19.53900 -16.38297 10.85308  1.000 32.15366 ? 118 LEU   A O    1 
ATOM   925  C  CB   . LEU   A 1 118 ? -21.17407 -18.84570 11.14832  1.000 29.42446 ? 118 LEU   A CB   1 
ATOM   926  C  CG   . LEU   A 1 118 ? -21.83628 -20.01792 11.87334  1.000 27.25232 ? 118 LEU   A CG   1 
ATOM   927  C  CD1  . LEU   A 1 118 ? -21.59874 -21.32051 11.12070  1.000 28.04202 ? 118 LEU   A CD1  1 
ATOM   928  C  CD2  . LEU   A 1 118 ? -21.31899 -20.11713 13.30003  1.000 31.81738 ? 118 LEU   A CD2  1 
ATOM   929  N  N    . CYS   A 1 119 ? -21.49497 -15.55367 10.10544  1.000 29.50560 ? 119 CYS   A N    1 
ATOM   930  C  CA   . CYS   A 1 119 ? -20.88321 -14.57998 9.20344   1.000 35.16187 ? 119 CYS   A CA   1 
ATOM   931  C  C    . CYS   A 1 119 ? -20.69784 -13.24076 9.92012   1.000 41.01802 ? 119 CYS   A C    1 
ATOM   932  O  O    . CYS   A 1 119 ? -21.19086 -12.19294 9.50183   1.000 41.33092 ? 119 CYS   A O    1 
ATOM   933  C  CB   . CYS   A 1 119 ? -21.73198 -14.43182 7.94595   1.000 33.44048 ? 119 CYS   A CB   1 
ATOM   934  S  SG   . CYS   A 1 119 ? -21.82907 -15.93346 6.92998   1.000 33.62325 ? 119 CYS   A SG   1 
ATOM   935  N  N    . THR   A 1 120 ? -19.94907 -13.29794 11.02311  1.000 39.40676 ? 120 THR   A N    1 
ATOM   936  C  CA   . THR   A 1 120 ? -19.80789 -12.16830 11.93548  1.000 44.07683 ? 120 THR   A CA   1 
ATOM   937  C  C    . THR   A 1 120 ? -18.95672 -11.03355 11.37671  1.000 44.92822 ? 120 THR   A C    1 
ATOM   938  O  O    . THR   A 1 120 ? -18.82023 -10.00908 12.05439  1.000 49.11406 ? 120 THR   A O    1 
ATOM   939  C  CB   . THR   A 1 120 ? -19.21687 -12.64286 13.26444  1.000 40.18608 ? 120 THR   A CB   1 
ATOM   940  O  OG1  . THR   A 1 120 ? -17.92454 -13.21502 13.03441  1.000 39.24427 ? 120 THR   A OG1  1 
ATOM   941  C  CG2  . THR   A 1 120 ? -20.12014 -13.68657 13.90382  1.000 41.48321 ? 120 THR   A CG2  1 
ATOM   942  N  N    . ASP   A 1 121 ? -18.38087 -11.17720 10.18192  1.000 44.72443 ? 121 ASP   A N    1 
ATOM   943  C  CA   . ASP   A 1 121 ? -17.65032 -10.07318 9.57249   1.000 47.84881 ? 121 ASP   A CA   1 
ATOM   944  C  C    . ASP   A 1 121 ? -18.55643 -9.13205  8.78929   1.000 48.90741 ? 121 ASP   A C    1 
ATOM   945  O  O    . ASP   A 1 121 ? -18.19447 -7.96674  8.59285   1.000 49.16247 ? 121 ASP   A O    1 
ATOM   946  C  CB   . ASP   A 1 121 ? -16.55015 -10.60960 8.65429   1.000 47.66482 ? 121 ASP   A CB   1 
ATOM   947  C  CG   . ASP   A 1 121 ? -15.52135 -11.43459 9.39891   1.000 58.41535 ? 121 ASP   A CG   1 
ATOM   948  O  OD1  . ASP   A 1 121 ? -15.05131 -10.97887 10.46269  1.000 50.88395 ? 121 ASP   A OD1  1 
ATOM   949  O  OD2  . ASP   A 1 121 ? -15.18892 -12.54315 8.92654   1.000 58.29952 ? 121 ASP   A OD2  1 
ATOM   950  N  N    . ASP   A 1 122 ? -19.72186 -9.60636  8.34533   1.000 47.35857 ? 122 ASP   A N    1 
ATOM   951  C  CA   . ASP   A 1 122 ? -20.66620 -8.79022  7.58169   1.000 46.23775 ? 122 ASP   A CA   1 
ATOM   952  C  C    . ASP   A 1 122 ? -21.53555 -8.00971  8.56522   1.000 48.83951 ? 122 ASP   A C    1 
ATOM   953  O  O    . ASP   A 1 122 ? -22.65989 -8.39180  8.90197   1.000 40.40147 ? 122 ASP   A O    1 
ATOM   954  C  CB   . ASP   A 1 122 ? -21.50293 -9.66525  6.65455   1.000 48.54502 ? 122 ASP   A CB   1 
ATOM   955  C  CG   . ASP   A 1 122 ? -22.22028 -8.86651  5.58040   1.000 47.62301 ? 122 ASP   A CG   1 
ATOM   956  O  OD1  . ASP   A 1 122 ? -22.44467 -7.65398  5.77920   1.000 51.60995 ? 122 ASP   A OD1  1 
ATOM   957  O  OD2  . ASP   A 1 122 ? -22.55767 -9.45394  4.53083   1.000 41.81114 ? 122 ASP   A OD2  1 
ATOM   958  N  N    . GLN   A 1 123 ? -20.99068 -6.88384  9.03385   1.000 48.84478 ? 123 GLN   A N    1 
ATOM   959  C  CA   . GLN   A 1 123 ? -21.72841 -6.03501  9.96357   1.000 46.93886 ? 123 GLN   A CA   1 
ATOM   960  C  C    . GLN   A 1 123 ? -22.96252 -5.42602  9.31148   1.000 45.66621 ? 123 GLN   A C    1 
ATOM   961  O  O    . GLN   A 1 123 ? -23.94020 -5.12061  10.00405  1.000 42.93335 ? 123 GLN   A O    1 
ATOM   962  C  CB   . GLN   A 1 123 ? -20.81721 -4.93418  10.50786  1.000 51.81274 ? 123 GLN   A CB   1 
ATOM   963  N  N    . GLY   A 1 124 ? -22.93900 -5.24352  7.99005   1.000 49.01176 ? 124 GLY   A N    1 
ATOM   964  C  CA   . GLY   A 1 124 ? -24.10647 -4.71036  7.30854   1.000 41.36929 ? 124 GLY   A CA   1 
ATOM   965  C  C    . GLY   A 1 124 ? -25.28209 -5.66815  7.32936   1.000 47.88060 ? 124 GLY   A C    1 
ATOM   966  O  O    . GLY   A 1 124 ? -26.42482 -5.25742  7.55202   1.000 39.79336 ? 124 GLY   A O    1 
ATOM   967  N  N    . TYR   A 1 125 ? -25.02373 -6.95712  7.09626   1.000 46.92803 ? 125 TYR   A N    1 
ATOM   968  C  CA   . TYR   A 1 125 ? -26.10386 -7.93414  7.17331   1.000 43.21874 ? 125 TYR   A CA   1 
ATOM   969  C  C    . TYR   A 1 125 ? -26.54916 -8.15001  8.61335   1.000 38.47123 ? 125 TYR   A C    1 
ATOM   970  O  O    . TYR   A 1 125 ? -27.74642 -8.30570  8.88104   1.000 38.82525 ? 125 TYR   A O    1 
ATOM   971  C  CB   . TYR   A 1 125 ? -25.68143 -9.26704  6.55849   1.000 39.75215 ? 125 TYR   A CB   1 
ATOM   972  C  CG   . TYR   A 1 125 ? -26.61596 -10.37849 6.97121   1.000 33.00109 ? 125 TYR   A CG   1 
ATOM   973  C  CD1  . TYR   A 1 125 ? -27.90541 -10.44490 6.46184   1.000 32.35015 ? 125 TYR   A CD1  1 
ATOM   974  C  CD2  . TYR   A 1 125 ? -26.22984 -11.32993 7.90703   1.000 30.21615 ? 125 TYR   A CD2  1 
ATOM   975  C  CE1  . TYR   A 1 125 ? -28.77569 -11.44230 6.85007   1.000 29.32583 ? 125 TYR   A CE1  1 
ATOM   976  C  CE2  . TYR   A 1 125 ? -27.09383 -12.32971 8.30308   1.000 31.01003 ? 125 TYR   A CE2  1 
ATOM   977  C  CZ   . TYR   A 1 125 ? -28.36518 -12.38108 7.77066   1.000 28.15038 ? 125 TYR   A CZ   1 
ATOM   978  O  OH   . TYR   A 1 125 ? -29.22991 -13.37474 8.16141   1.000 28.70558 ? 125 TYR   A OH   1 
ATOM   979  N  N    . LEU   A 1 126 ? -25.59791 -8.17751  9.55126   1.000 39.79480 ? 126 LEU   A N    1 
ATOM   980  C  CA   . LEU   A 1 126 ? -25.94226 -8.41528  10.94936  1.000 41.70922 ? 126 LEU   A CA   1 
ATOM   981  C  C    . LEU   A 1 126 ? -26.86117 -7.32495  11.48391  1.000 41.50353 ? 126 LEU   A C    1 
ATOM   982  O  O    . LEU   A 1 126 ? -27.74625 -7.59622  12.30402  1.000 42.71811 ? 126 LEU   A O    1 
ATOM   983  C  CB   . LEU   A 1 126 ? -24.67235 -8.51241  11.79459  1.000 42.53847 ? 126 LEU   A CB   1 
ATOM   984  C  CG   . LEU   A 1 126 ? -23.85973 -9.80291  11.66745  1.000 46.05375 ? 126 LEU   A CG   1 
ATOM   985  C  CD1  . LEU   A 1 126 ? -22.68856 -9.79468  12.63774  1.000 49.87419 ? 126 LEU   A CD1  1 
ATOM   986  C  CD2  . LEU   A 1 126 ? -24.73921 -11.02320 11.89640  1.000 47.72230 ? 126 LEU   A CD2  1 
ATOM   987  N  N    . ALA   A 1 127 ? -26.66756 -6.08416  11.02889  1.000 38.13392 ? 127 ALA   A N    1 
ATOM   988  C  CA   . ALA   A 1 127 ? -27.57370 -5.00685  11.41221  1.000 41.97006 ? 127 ALA   A CA   1 
ATOM   989  C  C    . ALA   A 1 127 ? -28.96856 -5.23612  10.84378  1.000 38.66576 ? 127 ALA   A C    1 
ATOM   990  O  O    . ALA   A 1 127 ? -29.97008 -5.02948  11.53889  1.000 35.67193 ? 127 ALA   A O    1 
ATOM   991  C  CB   . ALA   A 1 127 ? -27.01522 -3.66145  10.95026  1.000 39.49822 ? 127 ALA   A CB   1 
ATOM   992  N  N    . PHE   A 1 128 ? -29.05209 -5.66307  9.58142   1.000 38.64548 ? 128 PHE   A N    1 
ATOM   993  C  CA   . PHE   A 1 128 ? -30.33881 -6.03816  9.00365   1.000 35.18328 ? 128 PHE   A CA   1 
ATOM   994  C  C    . PHE   A 1 128 ? -30.98922 -7.16135  9.80134   1.000 31.77395 ? 128 PHE   A C    1 
ATOM   995  O  O    . PHE   A 1 128 ? -32.17973 -7.09743  10.12900  1.000 33.83770 ? 128 PHE   A O    1 
ATOM   996  C  CB   . PHE   A 1 128 ? -30.15183 -6.45094  7.54196   1.000 38.41382 ? 128 PHE   A CB   1 
ATOM   997  C  CG   . PHE   A 1 128 ? -31.39094 -7.02241  6.90242   1.000 36.81550 ? 128 PHE   A CG   1 
ATOM   998  C  CD1  . PHE   A 1 128 ? -32.30495 -6.19605  6.27047   1.000 38.82972 ? 128 PHE   A CD1  1 
ATOM   999  C  CD2  . PHE   A 1 128 ? -31.63114 -8.38953  6.91814   1.000 33.58533 ? 128 PHE   A CD2  1 
ATOM   1000 C  CE1  . PHE   A 1 128 ? -33.44101 -6.71902  5.67657   1.000 32.86842 ? 128 PHE   A CE1  1 
ATOM   1001 C  CE2  . PHE   A 1 128 ? -32.76554 -8.91885  6.32725   1.000 32.12627 ? 128 PHE   A CE2  1 
ATOM   1002 C  CZ   . PHE   A 1 128 ? -33.67118 -8.08290  5.70500   1.000 33.51808 ? 128 PHE   A CZ   1 
ATOM   1003 N  N    . ARG   A 1 129 ? -30.21763 -8.20445  10.12053  1.000 30.41733 ? 129 ARG   A N    1 
ATOM   1004 C  CA   . ARG   A 1 129 ? -30.77364 -9.34776  10.83790  1.000 30.49368 ? 129 ARG   A CA   1 
ATOM   1005 C  C    . ARG   A 1 129 ? -31.29866 -8.94497  12.21030  1.000 35.95530 ? 129 ARG   A C    1 
ATOM   1006 O  O    . ARG   A 1 129 ? -32.35688 -9.41905  12.63923  1.000 31.40308 ? 129 ARG   A O    1 
ATOM   1007 C  CB   . ARG   A 1 129 ? -29.72216 -10.44854 10.97444  1.000 32.22547 ? 129 ARG   A CB   1 
ATOM   1008 C  CG   . ARG   A 1 129 ? -30.26368 -11.73494 11.57719  1.000 33.14936 ? 129 ARG   A CG   1 
ATOM   1009 C  CD   . ARG   A 1 129 ? -29.14834 -12.71091 11.91690  1.000 29.71162 ? 129 ARG   A CD   1 
ATOM   1010 N  NE   . ARG   A 1 129 ? -29.66024 -14.05764 12.14252  1.000 32.85665 ? 129 ARG   A NE   1 
ATOM   1011 C  CZ   . ARG   A 1 129 ? -30.26375 -14.45559 13.25440  1.000 36.72263 ? 129 ARG   A CZ   1 
ATOM   1012 N  NH1  . ARG   A 1 129 ? -30.44869 -13.63297 14.27383  1.000 38.37871 ? 129 ARG   A NH1  1 
ATOM   1013 N  NH2  . ARG   A 1 129 ? -30.69093 -15.71165 13.34655  1.000 38.10635 ? 129 ARG   A NH2  1 
ATOM   1014 N  N    . ALA   A 1 130 ? -30.56915 -8.07733  12.91799  1.000 35.42112 ? 130 ALA   A N    1 
ATOM   1015 C  CA   . ALA   A 1 130 ? -31.02157 -7.63482  14.23344  1.000 38.60303 ? 130 ALA   A CA   1 
ATOM   1016 C  C    . ALA   A 1 130 ? -32.34434 -6.88579  14.13790  1.000 36.02355 ? 130 ALA   A C    1 
ATOM   1017 O  O    . ALA   A 1 130 ? -33.20448 -7.01442  15.01702  1.000 39.98100 ? 130 ALA   A O    1 
ATOM   1018 C  CB   . ALA   A 1 130 ? -29.95666 -6.75692  14.89189  1.000 36.65890 ? 130 ALA   A CB   1 
ATOM   1019 N  N    . LYS   A 1 131 ? -32.52696 -6.10186  13.07376  1.000 34.32171 ? 131 LYS   A N    1 
ATOM   1020 C  CA   . LYS   A 1 131 ? -33.76035 -5.33910  12.91141  1.000 36.57633 ? 131 LYS   A CA   1 
ATOM   1021 C  C    . LYS   A 1 131 ? -34.94146 -6.25883  12.62393  1.000 35.38340 ? 131 LYS   A C    1 
ATOM   1022 O  O    . LYS   A 1 131 ? -35.94515 -6.24465  13.34538  1.000 35.96908 ? 131 LYS   A O    1 
ATOM   1023 C  CB   . LYS   A 1 131 ? -33.59457 -4.30541  11.79520  1.000 40.20788 ? 131 LYS   A CB   1 
ATOM   1024 N  N    . VAL   A 1 132 ? -34.83657 -7.07724  11.57270  1.000 33.36662 ? 132 VAL   A N    1 
ATOM   1025 C  CA   . VAL   A 1 132 ? -35.95708 -7.91722  11.16057  1.000 33.08559 ? 132 VAL   A CA   1 
ATOM   1026 C  C    . VAL   A 1 132 ? -36.23664 -9.06035  12.12220  1.000 31.23566 ? 132 VAL   A C    1 
ATOM   1027 O  O    . VAL   A 1 132 ? -37.25390 -9.74357  11.96998  1.000 31.02518 ? 132 VAL   A O    1 
ATOM   1028 C  CB   . VAL   A 1 132 ? -35.73448 -8.49437  9.74772   1.000 31.67726 ? 132 VAL   A CB   1 
ATOM   1029 C  CG1  . VAL   A 1 132 ? -35.64297 -7.37332  8.72190   1.000 26.71230 ? 132 VAL   A CG1  1 
ATOM   1030 C  CG2  . VAL   A 1 132 ? -34.49268 -9.37952  9.71491   1.000 32.00322 ? 132 VAL   A CG2  1 
ATOM   1031 N  N    . HIS   A 1 133 ? -35.36305 -9.30116  13.09724  1.000 33.45627 ? 133 HIS   A N    1 
ATOM   1032 C  CA   . HIS   A 1 133 ? -35.63509 -10.27340 14.14643  1.000 30.63720 ? 133 HIS   A CA   1 
ATOM   1033 C  C    . HIS   A 1 133 ? -36.12812 -9.62272  15.43071  1.000 36.44901 ? 133 HIS   A C    1 
ATOM   1034 O  O    . HIS   A 1 133 ? -36.33628 -10.32339 16.42617  1.000 35.60302 ? 133 HIS   A O    1 
ATOM   1035 C  CB   . HIS   A 1 133 ? -34.38898 -11.12008 14.43138  1.000 35.63760 ? 133 HIS   A CB   1 
ATOM   1036 C  CG   . HIS   A 1 133 ? -34.28008 -12.33734 13.56635  1.000 33.09813 ? 133 HIS   A CG   1 
ATOM   1037 N  ND1  . HIS   A 1 133 ? -33.76629 -12.29903 12.28791  1.000 35.53046 ? 133 HIS   A ND1  1 
ATOM   1038 C  CD2  . HIS   A 1 133 ? -34.63349 -13.62513 13.79089  1.000 33.46801 ? 133 HIS   A CD2  1 
ATOM   1039 C  CE1  . HIS   A 1 133 ? -33.80204 -13.51139 11.76434  1.000 27.02822 ? 133 HIS   A CE1  1 
ATOM   1040 N  NE2  . HIS   A 1 133 ? -34.32343 -14.33464 12.65601  1.000 34.46400 ? 133 HIS   A NE2  1 
ATOM   1041 N  N    . THR   A 1 134 ? -36.32016 -8.30932  15.43160  1.000 32.83960 ? 134 THR   A N    1 
ATOM   1042 C  CA   . THR   A 1 134 ? -36.90452 -7.63775  16.58440  1.000 38.24465 ? 134 THR   A CA   1 
ATOM   1043 C  C    . THR   A 1 134 ? -38.40438 -7.91051  16.62165  1.000 38.19718 ? 134 THR   A C    1 
ATOM   1044 O  O    . THR   A 1 134 ? -39.09291 -7.67447  15.62424  1.000 35.09124 ? 134 THR   A O    1 
ATOM   1045 C  CB   . THR   A 1 134 ? -36.64310 -6.13580  16.52205  1.000 38.31252 ? 134 THR   A CB   1 
ATOM   1046 O  OG1  . THR   A 1 134 ? -35.23529 -5.90212  16.38834  1.000 39.06719 ? 134 THR   A OG1  1 
ATOM   1047 C  CG2  . THR   A 1 134 ? -37.14569 -5.45093  17.78456  1.000 39.93046 ? 134 THR   A CG2  1 
ATOM   1048 N  N    . PRO   A 1 135 ? -38.93968 -8.40496  17.74295  1.000 39.48369 ? 135 PRO   A N    1 
ATOM   1049 C  CA   . PRO   A 1 135 ? -40.35170 -8.83139  17.75347  1.000 41.74072 ? 135 PRO   A CA   1 
ATOM   1050 C  C    . PRO   A 1 135 ? -41.34082 -7.74289  17.36383  1.000 39.00864 ? 135 PRO   A C    1 
ATOM   1051 O  O    . PRO   A 1 135 ? -42.27584 -8.01975  16.60238  1.000 34.41998 ? 135 PRO   A O    1 
ATOM   1052 C  CB   . PRO   A 1 135 ? -40.55641 -9.29587  19.20233  1.000 42.52947 ? 135 PRO   A CB   1 
ATOM   1053 C  CG   . PRO   A 1 135 ? -39.19058 -9.70010  19.66144  1.000 46.22498 ? 135 PRO   A CG   1 
ATOM   1054 C  CD   . PRO   A 1 135 ? -38.25073 -8.73157  19.00348  1.000 40.19882 ? 135 PRO   A CD   1 
ATOM   1055 N  N    . TRP   A 1 136 ? -41.17267 -6.51188  17.85629  1.000 36.72304 ? 136 TRP   A N    1 
ATOM   1056 C  CA   . TRP   A 1 136 ? -42.14034 -5.47138  17.51734  1.000 39.00920 ? 136 TRP   A CA   1 
ATOM   1057 C  C    . TRP   A 1 136 ? -42.01397 -5.03624  16.06228  1.000 36.24070 ? 136 TRP   A C    1 
ATOM   1058 O  O    . TRP   A 1 136 ? -42.99972 -4.59050  15.46390  1.000 35.02834 ? 136 TRP   A O    1 
ATOM   1059 C  CB   . TRP   A 1 136 ? -42.00295 -4.27472  18.46614  1.000 38.91882 ? 136 TRP   A CB   1 
ATOM   1060 C  CG   . TRP   A 1 136 ? -40.78929 -3.40474  18.27044  1.000 42.04669 ? 136 TRP   A CG   1 
ATOM   1061 C  CD1  . TRP   A 1 136 ? -39.63365 -3.44174  18.99529  1.000 45.23188 ? 136 TRP   A CD1  1 
ATOM   1062 C  CD2  . TRP   A 1 136 ? -40.63093 -2.34002  17.32019  1.000 43.23096 ? 136 TRP   A CD2  1 
ATOM   1063 N  NE1  . TRP   A 1 136 ? -38.75809 -2.48390  18.54303  1.000 40.87350 ? 136 TRP   A NE1  1 
ATOM   1064 C  CE2  . TRP   A 1 136 ? -39.34627 -1.79359  17.51602  1.000 42.61255 ? 136 TRP   A CE2  1 
ATOM   1065 C  CE3  . TRP   A 1 136 ? -41.44544 -1.80402  16.31713  1.000 39.38455 ? 136 TRP   A CE3  1 
ATOM   1066 C  CZ2  . TRP   A 1 136 ? -38.85752 -0.73855  16.74640  1.000 44.07994 ? 136 TRP   A CZ2  1 
ATOM   1067 C  CZ3  . TRP   A 1 136 ? -40.95746 -0.75652  15.55323  1.000 41.85418 ? 136 TRP   A CZ3  1 
ATOM   1068 C  CH2  . TRP   A 1 136 ? -39.67627 -0.23518  15.77282  1.000 38.60752 ? 136 TRP   A CH2  1 
ATOM   1069 N  N    . ILE   A 1 137 ? -40.82526 -5.16753  15.47205  1.000 31.45773 ? 137 ILE   A N    1 
ATOM   1070 C  CA   . ILE   A 1 137 ? -40.67668 -4.86921  14.05124  1.000 33.48129 ? 137 ILE   A CA   1 
ATOM   1071 C  C    . ILE   A 1 137 ? -41.38756 -5.92259  13.20793  1.000 35.53542 ? 137 ILE   A C    1 
ATOM   1072 O  O    . ILE   A 1 137 ? -42.04803 -5.59862  12.21287  1.000 28.20194 ? 137 ILE   A O    1 
ATOM   1073 C  CB   . ILE   A 1 137 ? -39.18615 -4.75032  13.68455  1.000 37.16799 ? 137 ILE   A CB   1 
ATOM   1074 C  CG1  . ILE   A 1 137 ? -38.54695 -3.57877  14.43650  1.000 39.74634 ? 137 ILE   A CG1  1 
ATOM   1075 C  CG2  . ILE   A 1 137 ? -39.01452 -4.58361  12.18172  1.000 32.44929 ? 137 ILE   A CG2  1 
ATOM   1076 C  CD1  . ILE   A 1 137 ? -37.16521 -3.20477  13.93692  1.000 39.50803 ? 137 ILE   A CD1  1 
ATOM   1077 N  N    . GLN   A 1 138 ? -41.27485 -7.19662  13.59527  1.000 30.04599 ? 138 GLN   A N    1 
ATOM   1078 C  CA   . GLN   A 1 138 ? -41.97179 -8.25610  12.87109  1.000 30.06299 ? 138 GLN   A CA   1 
ATOM   1079 C  C    . GLN   A 1 138 ? -43.48200 -8.10220  12.98239  1.000 31.65812 ? 138 GLN   A C    1 
ATOM   1080 O  O    . GLN   A 1 138 ? -44.20404 -8.25034  11.98905  1.000 29.15226 ? 138 GLN   A O    1 
ATOM   1081 C  CB   . GLN   A 1 138 ? -41.54930 -9.62634  13.39881  1.000 28.37582 ? 138 GLN   A CB   1 
ATOM   1082 C  CG   . GLN   A 1 138 ? -40.11854 -10.01031 13.09336  1.000 32.39829 ? 138 GLN   A CG   1 
ATOM   1083 C  CD   . GLN   A 1 138 ? -39.84782 -11.47691 13.36327  1.000 37.21467 ? 138 GLN   A CD   1 
ATOM   1084 O  OE1  . GLN   A 1 138 ? -40.69650 -12.18391 13.90548  1.000 33.75792 ? 138 GLN   A OE1  1 
ATOM   1085 N  NE2  . GLN   A 1 138 ? -38.66474 -11.94354 12.98014  1.000 27.77768 ? 138 GLN   A NE2  1 
ATOM   1086 N  N    A ARG   A 1 139 ? -43.97783 -7.81162  14.18780  0.523 30.50152 ? 139 ARG   A N    1 
ATOM   1087 N  N    B ARG   A 1 139 ? -43.98101 -7.81201  14.18598  0.477 30.47461 ? 139 ARG   A N    1 
ATOM   1088 C  CA   A ARG   A 1 139 ? -45.41575 -7.65634  14.37893  0.523 31.51159 ? 139 ARG   A CA   1 
ATOM   1089 C  CA   B ARG   A 1 139 ? -45.42102 -7.66695  14.36672  0.477 31.49743 ? 139 ARG   A CA   1 
ATOM   1090 C  C    A ARG   A 1 139 ? -45.95077 -6.47294  13.58420  0.523 30.10854 ? 139 ARG   A C    1 
ATOM   1091 C  C    B ARG   A 1 139 ? -45.96303 -6.46163  13.61005  0.477 30.09348 ? 139 ARG   A C    1 
ATOM   1092 O  O    A ARG   A 1 139 ? -47.06086 -6.52976  13.04148  0.523 31.32522 ? 139 ARG   A O    1 
ATOM   1093 O  O    B ARG   A 1 139 ? -47.09713 -6.49926  13.11878  0.477 31.34288 ? 139 ARG   A O    1 
ATOM   1094 C  CB   A ARG   A 1 139 ? -45.73099 -7.49286  15.86611  0.523 36.42418 ? 139 ARG   A CB   1 
ATOM   1095 C  CB   B ARG   A 1 139 ? -45.75431 -7.56210  15.85496  0.477 36.42321 ? 139 ARG   A CB   1 
ATOM   1096 C  CG   A ARG   A 1 139 ? -45.47646 -8.74210  16.69607  0.523 39.63895 ? 139 ARG   A CG   1 
ATOM   1097 C  CG   B ARG   A 1 139 ? -45.40459 -8.81039  16.65228  0.477 39.61228 ? 139 ARG   A CG   1 
ATOM   1098 C  CD   A ARG   A 1 139 ? -46.11050 -8.63308  18.07537  0.523 43.33931 ? 139 ARG   A CD   1 
ATOM   1099 C  CD   B ARG   A 1 139 ? -46.22887 -8.90891  17.92590  0.477 43.42248 ? 139 ARG   A CD   1 
ATOM   1100 N  NE   A ARG   A 1 139 ? -45.57944 -7.51284  18.84366  0.523 44.50956 ? 139 ARG   A NE   1 
ATOM   1101 N  NE   B ARG   A 1 139 ? -45.59467 -9.76229  18.92402  0.477 45.05933 ? 139 ARG   A NE   1 
ATOM   1102 C  CZ   A ARG   A 1 139 ? -44.50951 -7.57941  19.62453  0.523 47.30675 ? 139 ARG   A CZ   1 
ATOM   1103 C  CZ   B ARG   A 1 139 ? -44.95555 -9.31570  19.99682  0.477 47.47155 ? 139 ARG   A CZ   1 
ATOM   1104 N  NH1  A ARG   A 1 139 ? -43.82203 -8.70159  19.76120  0.523 47.54546 ? 139 ARG   A NH1  1 
ATOM   1105 N  NH1  B ARG   A 1 139 ? -44.84632 -8.02115  20.24806  0.477 47.87944 ? 139 ARG   A NH1  1 
ATOM   1106 N  NH2  A ARG   A 1 139 ? -44.12052 -6.49335  20.28652  0.523 42.92647 ? 139 ARG   A NH2  1 
ATOM   1107 N  NH2  B ARG   A 1 139 ? -44.41384 -10.19008 20.84003  0.477 52.15642 ? 139 ARG   A NH2  1 
ATOM   1108 N  N    . LEU   A 1 140 ? -45.17131 -5.39258  13.49964  1.000 29.60114 ? 140 LEU   A N    1 
ATOM   1109 C  CA   . LEU   A 1 140 ? -45.61199 -4.22015  12.75211  1.000 32.08309 ? 140 LEU   A CA   1 
ATOM   1110 C  C    . LEU   A 1 140 ? -45.67527 -4.51190  11.25839  1.000 30.08448 ? 140 LEU   A C    1 
ATOM   1111 O  O    . LEU   A 1 140 ? -46.63157 -4.11469  10.58185  1.000 24.94559 ? 140 LEU   A O    1 
ATOM   1112 C  CB   . LEU   A 1 140 ? -44.67913 -3.04330  13.03427  1.000 32.76384 ? 140 LEU   A CB   1 
ATOM   1113 C  CG   . LEU   A 1 140 ? -44.81120 -1.80692  12.14337  1.000 40.54984 ? 140 LEU   A CG   1 
ATOM   1114 C  CD1  . LEU   A 1 140 ? -46.13481 -1.10243  12.38894  1.000 29.82363 ? 140 LEU   A CD1  1 
ATOM   1115 C  CD2  . LEU   A 1 140 ? -43.64440 -0.85644  12.37227  1.000 43.95661 ? 140 LEU   A CD2  1 
ATOM   1116 N  N    . PHE   A 1 141 ? -44.67134 -5.21377  10.72873  1.000 26.15240 ? 141 PHE   A N    1 
ATOM   1117 C  CA   . PHE   A 1 141 ? -44.67054 -5.54617  9.30804   1.000 26.94525 ? 141 PHE   A CA   1 
ATOM   1118 C  C    . PHE   A 1 141 ? -45.81512 -6.49134  8.96450   1.000 26.74396 ? 141 PHE   A C    1 
ATOM   1119 O  O    . PHE   A 1 141 ? -46.51499 -6.29780  7.96443   1.000 22.79772 ? 141 PHE   A O    1 
ATOM   1120 C  CB   . PHE   A 1 141 ? -43.32780 -6.16036  8.90994   1.000 26.91600 ? 141 PHE   A CB   1 
ATOM   1121 C  CG   . PHE   A 1 141 ? -43.27328 -6.62414  7.47890   1.000 27.28374 ? 141 PHE   A CG   1 
ATOM   1122 C  CD1  . PHE   A 1 141 ? -43.02326 -5.72619  6.45563   1.000 24.77377 ? 141 PHE   A CD1  1 
ATOM   1123 C  CD2  . PHE   A 1 141 ? -43.46781 -7.95915  7.15797   1.000 25.45160 ? 141 PHE   A CD2  1 
ATOM   1124 C  CE1  . PHE   A 1 141 ? -42.97113 -6.14864  5.13921   1.000 27.35672 ? 141 PHE   A CE1  1 
ATOM   1125 C  CE2  . PHE   A 1 141 ? -43.41699 -8.38781  5.84278   1.000 26.56137 ? 141 PHE   A CE2  1 
ATOM   1126 C  CZ   . PHE   A 1 141 ? -43.16712 -7.48162  4.83294   1.000 25.23164 ? 141 PHE   A CZ   1 
ATOM   1127 N  N    . LEU   A 1 142 ? -46.01872 -7.52610  9.78449   1.000 25.43896 ? 142 LEU   A N    1 
ATOM   1128 C  CA   . LEU   A 1 142 ? -47.07773 -8.49420  9.51959   1.000 25.23615 ? 142 LEU   A CA   1 
ATOM   1129 C  C    . LEU   A 1 142 ? -48.46792 -7.88263  9.63351   1.000 27.09866 ? 142 LEU   A C    1 
ATOM   1130 O  O    . LEU   A 1 142 ? -49.41569 -8.41735  9.04838   1.000 25.04769 ? 142 LEU   A O    1 
ATOM   1131 C  CB   . LEU   A 1 142 ? -46.95514 -9.68573  10.47171  1.000 23.62527 ? 142 LEU   A CB   1 
ATOM   1132 C  CG   . LEU   A 1 142 ? -45.72639 -10.57905 10.27865  1.000 23.74584 ? 142 LEU   A CG   1 
ATOM   1133 C  CD1  . LEU   A 1 142 ? -45.57246 -11.54627 11.44373  1.000 26.57036 ? 142 LEU   A CD1  1 
ATOM   1134 C  CD2  . LEU   A 1 142 ? -45.80457 -11.33359 8.95665   1.000 24.80448 ? 142 LEU   A CD2  1 
ATOM   1135 N  N    . ALA   A 1 143 ? -48.61266 -6.77837  10.36843  1.000 26.59193 ? 143 ALA   A N    1 
ATOM   1136 C  CA   . ALA   A 1 143 ? -49.90396 -6.11343  10.47892  1.000 29.90095 ? 143 ALA   A CA   1 
ATOM   1137 C  C    . ALA   A 1 143 ? -50.25919 -5.31138  9.23423   1.000 31.71675 ? 143 ALA   A C    1 
ATOM   1138 O  O    . ALA   A 1 143 ? -51.43004 -4.95884  9.05486   1.000 32.13988 ? 143 ALA   A O    1 
ATOM   1139 C  CB   . ALA   A 1 143 ? -49.92204 -5.19793  11.70501  1.000 29.36423 ? 143 ALA   A CB   1 
ATOM   1140 N  N    . LEU   A 1 144 ? -49.28375 -5.01920  8.37734   1.000 22.52661 ? 144 LEU   A N    1 
ATOM   1141 C  CA   . LEU   A 1 144 ? -49.54879 -4.25045  7.17332   1.000 23.39959 ? 144 LEU   A CA   1 
ATOM   1142 C  C    . LEU   A 1 144 ? -50.39629 -5.06433  6.19572   1.000 24.97993 ? 144 LEU   A C    1 
ATOM   1143 O  O    . LEU   A 1 144 ? -50.36947 -6.29800  6.21700   1.000 27.33008 ? 144 LEU   A O    1 
ATOM   1144 C  CB   . LEU   A 1 144 ? -48.23933 -3.83750  6.50433   1.000 23.69719 ? 144 LEU   A CB   1 
ATOM   1145 C  CG   . LEU   A 1 144 ? -47.34234 -2.88652  7.29940   1.000 25.77838 ? 144 LEU   A CG   1 
ATOM   1146 C  CD1  . LEU   A 1 144 ? -45.95670 -2.81203  6.67769   1.000 26.89789 ? 144 LEU   A CD1  1 
ATOM   1147 C  CD2  . LEU   A 1 144 ? -47.96791 -1.50190  7.39592   1.000 23.10287 ? 144 LEU   A CD2  1 
ATOM   1148 N  N    . PRO   A 1 145 ? -51.16650 -4.39668  5.33482   1.000 28.48523 ? 145 PRO   A N    1 
ATOM   1149 C  CA   . PRO   A 1 145 ? -51.93202 -5.12865  4.31881   1.000 26.72393 ? 145 PRO   A CA   1 
ATOM   1150 C  C    . PRO   A 1 145 ? -51.01231 -5.93673  3.41481   1.000 27.29471 ? 145 PRO   A C    1 
ATOM   1151 O  O    . PRO   A 1 145 ? -49.84947 -5.58558  3.20230   1.000 24.00628 ? 145 PRO   A O    1 
ATOM   1152 C  CB   . PRO   A 1 145 ? -52.65046 -4.01864  3.54202   1.000 34.82953 ? 145 PRO   A CB   1 
ATOM   1153 C  CG   . PRO   A 1 145 ? -52.68912 -2.84877  4.48224   1.000 30.40317 ? 145 PRO   A CG   1 
ATOM   1154 C  CD   . PRO   A 1 145 ? -51.43682 -2.94756  5.30326   1.000 30.19678 ? 145 PRO   A CD   1 
ATOM   1155 N  N    . LEU   A 1 146 ? -51.55422 -7.03510  2.88091   1.000 29.39593 ? 146 LEU   A N    1 
ATOM   1156 C  CA   . LEU   A 1 146 ? -50.75273 -7.94938  2.07063   1.000 26.10513 ? 146 LEU   A CA   1 
ATOM   1157 C  C    . LEU   A 1 146 ? -50.13548 -7.24022  0.87082   1.000 27.16919 ? 146 LEU   A C    1 
ATOM   1158 O  O    . LEU   A 1 146 ? -48.95137 -7.42651  0.56882   1.000 25.79829 ? 146 LEU   A O    1 
ATOM   1159 C  CB   . LEU   A 1 146 ? -51.60682 -9.13315  1.61303   1.000 24.95007 ? 146 LEU   A CB   1 
ATOM   1160 C  CG   . LEU   A 1 146 ? -51.54506 -10.39702 2.47176   1.000 37.29120 ? 146 LEU   A CG   1 
ATOM   1161 C  CD1  . LEU   A 1 146 ? -52.55052 -11.42586 1.97932   1.000 33.88340 ? 146 LEU   A CD1  1 
ATOM   1162 C  CD2  . LEU   A 1 146 ? -50.13521 -10.97685 2.45995   1.000 28.00584 ? 146 LEU   A CD2  1 
ATOM   1163 N  N    . PHE   A 1 147 ? -50.92296 -6.42174  0.16983   1.000 27.86940 ? 147 PHE   A N    1 
ATOM   1164 C  CA   . PHE   A 1 147 ? -50.39674 -5.76256  -1.02074  1.000 28.89947 ? 147 PHE   A CA   1 
ATOM   1165 C  C    . PHE   A 1 147 ? -49.31025 -4.75271  -0.66945  1.000 28.50105 ? 147 PHE   A C    1 
ATOM   1166 O  O    . PHE   A 1 147 ? -48.42102 -4.49414  -1.48903  1.000 31.87309 ? 147 PHE   A O    1 
ATOM   1167 C  CB   . PHE   A 1 147 ? -51.53256 -5.10180  -1.80633  1.000 32.88014 ? 147 PHE   A CB   1 
ATOM   1168 C  CG   . PHE   A 1 147 ? -52.09067 -3.86059  -1.16263  1.000 40.50862 ? 147 PHE   A CG   1 
ATOM   1169 C  CD1  . PHE   A 1 147 ? -53.05126 -3.94717  -0.16624  1.000 41.25653 ? 147 PHE   A CD1  1 
ATOM   1170 C  CD2  . PHE   A 1 147 ? -51.69004 -2.60519  -1.58814  1.000 43.44367 ? 147 PHE   A CD2  1 
ATOM   1171 C  CE1  . PHE   A 1 147 ? -53.57641 -2.80427  0.41483   1.000 33.16046 ? 147 PHE   A CE1  1 
ATOM   1172 C  CE2  . PHE   A 1 147 ? -52.21527 -1.46185  -1.01307  1.000 43.04197 ? 147 PHE   A CE2  1 
ATOM   1173 C  CZ   . PHE   A 1 147 ? -53.15947 -1.56356  -0.00993  1.000 35.18190 ? 147 PHE   A CZ   1 
ATOM   1174 N  N    . ILE   A 1 148 ? -49.35580 -4.18390  0.53813   1.000 26.19783 ? 148 ILE   A N    1 
ATOM   1175 C  CA   . ILE   A 1 148 ? -48.27608 -3.30873  0.98530   1.000 28.02039 ? 148 ILE   A CA   1 
ATOM   1176 C  C    . ILE   A 1 148 ? -47.01484 -4.11953  1.25507   1.000 30.87283 ? 148 ILE   A C    1 
ATOM   1177 O  O    . ILE   A 1 148 ? -45.91124 -3.72611  0.85837   1.000 26.86033 ? 148 ILE   A O    1 
ATOM   1178 C  CB   . ILE   A 1 148 ? -48.71032 -2.50757  2.22741   1.000 25.13172 ? 148 ILE   A CB   1 
ATOM   1179 C  CG1  . ILE   A 1 148 ? -49.84417 -1.54230  1.87863   1.000 31.20260 ? 148 ILE   A CG1  1 
ATOM   1180 C  CG2  . ILE   A 1 148 ? -47.52465 -1.74602  2.82332   1.000 24.67662 ? 148 ILE   A CG2  1 
ATOM   1181 C  CD1  . ILE   A 1 148 ? -49.42893 -0.43538  0.93988   1.000 35.29989 ? 148 ILE   A CD1  1 
ATOM   1182 N  N    . ARG   A 1 149 ? -47.15807 -5.26599  1.92647   1.000 25.54115 ? 149 ARG   A N    1 
ATOM   1183 C  CA   . ARG   A 1 149 ? -46.00289 -6.11216  2.21440   1.000 28.64977 ? 149 ARG   A CA   1 
ATOM   1184 C  C    . ARG   A 1 149 ? -45.34212 -6.60038  0.93124   1.000 27.55071 ? 149 ARG   A C    1 
ATOM   1185 O  O    . ARG   A 1 149 ? -44.11006 -6.66693  0.84419   1.000 27.93621 ? 149 ARG   A O    1 
ATOM   1186 C  CB   . ARG   A 1 149 ? -46.42637 -7.29828  3.08272   1.000 25.50463 ? 149 ARG   A CB   1 
ATOM   1187 C  CG   . ARG   A 1 149 ? -46.63629 -6.95569  4.55123   1.000 26.66891 ? 149 ARG   A CG   1 
ATOM   1188 C  CD   . ARG   A 1 149 ? -47.08544 -8.17038  5.35367   1.000 28.02901 ? 149 ARG   A CD   1 
ATOM   1189 N  NE   . ARG   A 1 149 ? -48.53736 -8.25665  5.46410   1.000 23.95733 ? 149 ARG   A NE   1 
ATOM   1190 C  CZ   . ARG   A 1 149 ? -49.21312 -9.39117  5.59144   1.000 29.44090 ? 149 ARG   A CZ   1 
ATOM   1191 N  NH1  . ARG   A 1 149 ? -48.59996 -10.56440 5.60952   1.000 23.54159 ? 149 ARG   A NH1  1 
ATOM   1192 N  NH2  . ARG   A 1 149 ? -50.53723 -9.34828  5.70725   1.000 25.35144 ? 149 ARG   A NH2  1 
ATOM   1193 N  N    . HIS   A 1 150 ? -46.14783 -6.94966  -0.07487  1.000 24.70608 ? 150 HIS   A N    1 
ATOM   1194 C  CA   . HIS   A 1 150 ? -45.60001 -7.36755  -1.36173  1.000 27.17784 ? 150 HIS   A CA   1 
ATOM   1195 C  C    . HIS   A 1 150 ? -44.77841 -6.25527  -2.00146  1.000 28.94156 ? 150 HIS   A C    1 
ATOM   1196 O  O    . HIS   A 1 150 ? -43.70039 -6.50853  -2.55333  1.000 30.38789 ? 150 HIS   A O    1 
ATOM   1197 C  CB   . HIS   A 1 150 ? -46.73559 -7.79770  -2.29050  1.000 30.91161 ? 150 HIS   A CB   1 
ATOM   1198 C  CG   . HIS   A 1 150 ? -46.34936 -8.85687  -3.27461  1.000 41.07541 ? 150 HIS   A CG   1 
ATOM   1199 N  ND1  . HIS   A 1 150 ? -46.20954 -10.18294 -2.92576  1.000 51.01484 ? 150 HIS   A ND1  1 
ATOM   1200 C  CD2  . HIS   A 1 150 ? -46.08266 -8.78653  -4.60032  1.000 47.31729 ? 150 HIS   A CD2  1 
ATOM   1201 C  CE1  . HIS   A 1 150 ? -45.86891 -10.88317 -3.99309  1.000 56.54145 ? 150 HIS   A CE1  1 
ATOM   1202 N  NE2  . HIS   A 1 150 ? -45.78539 -10.05948 -5.02239  1.000 53.81043 ? 150 HIS   A NE2  1 
ATOM   1203 N  N    . ARG   A 1 151 ? -45.27207 -5.01542  -1.93642  1.000 29.35973 ? 151 ARG   A N    1 
ATOM   1204 C  CA   . ARG   A 1 151 ? -44.54973 -3.89686  -2.53418  1.000 31.76226 ? 151 ARG   A CA   1 
ATOM   1205 C  C    . ARG   A 1 151 ? -43.25330 -3.61357  -1.78700  1.000 31.99981 ? 151 ARG   A C    1 
ATOM   1206 O  O    . ARG   A 1 151 ? -42.22923 -3.30120  -2.40628  1.000 34.27008 ? 151 ARG   A O    1 
ATOM   1207 C  CB   . ARG   A 1 151 ? -45.43651 -2.65147  -2.56046  1.000 33.23327 ? 151 ARG   A CB   1 
ATOM   1208 C  CG   . ARG   A 1 151 ? -46.39261 -2.59647  -3.74162  1.000 40.80170 ? 151 ARG   A CG   1 
ATOM   1209 C  CD   . ARG   A 1 151 ? -47.70333 -1.92117  -3.36799  1.000 47.30208 ? 151 ARG   A CD   1 
ATOM   1210 N  NE   . ARG   A 1 151 ? -47.67619 -0.48861  -3.63954  1.000 59.79943 ? 151 ARG   A NE   1 
ATOM   1211 C  CZ   . ARG   A 1 151 ? -48.68634 0.33951   -3.40803  1.000 68.80747 ? 151 ARG   A CZ   1 
ATOM   1212 N  NH1  . ARG   A 1 151 ? -49.82962 -0.08915  -2.89821  1.000 64.38107 ? 151 ARG   A NH1  1 
ATOM   1213 N  NH2  . ARG   A 1 151 ? -48.54514 1.63103   -3.69314  1.000 63.35548 ? 151 ARG   A NH2  1 
ATOM   1214 N  N    . ILE   A 1 152 ? -43.27960 -3.71407  -0.45622  1.000 28.47079 ? 152 ILE   A N    1 
ATOM   1215 C  CA   . ILE   A 1 152 ? -42.06617 -3.51463  0.33255   1.000 33.40745 ? 152 ILE   A CA   1 
ATOM   1216 C  C    . ILE   A 1 152 ? -41.03410 -4.58291  -0.00706  1.000 32.03466 ? 152 ILE   A C    1 
ATOM   1217 O  O    . ILE   A 1 152 ? -39.85281 -4.28653  -0.22503  1.000 32.55106 ? 152 ILE   A O    1 
ATOM   1218 C  CB   . ILE   A 1 152 ? -42.39666 -3.51488  1.83596   1.000 30.81665 ? 152 ILE   A CB   1 
ATOM   1219 C  CG1  . ILE   A 1 152 ? -43.24405 -2.29628  2.20520   1.000 27.99813 ? 152 ILE   A CG1  1 
ATOM   1220 C  CG2  . ILE   A 1 152 ? -41.11894 -3.54792  2.66378   1.000 32.45642 ? 152 ILE   A CG2  1 
ATOM   1221 C  CD1  . ILE   A 1 152 ? -43.80056 -2.35666  3.60850   1.000 28.24362 ? 152 ILE   A CD1  1 
ATOM   1222 N  N    . ALA   A 1 153 ? -41.47111 -5.84316  -0.06607  1.000 28.98356 ? 153 ALA   A N    1 
ATOM   1223 C  CA   . ALA   A 1 153 ? -40.54419 -6.94586  -0.30132  1.000 35.49897 ? 153 ALA   A CA   1 
ATOM   1224 C  C    . ALA   A 1 153 ? -39.92368 -6.86884  -1.69039  1.000 40.05791 ? 153 ALA   A C    1 
ATOM   1225 O  O    . ALA   A 1 153 ? -38.73925 -7.17900  -1.86343  1.000 42.36226 ? 153 ALA   A O    1 
ATOM   1226 C  CB   . ALA   A 1 153 ? -41.26094 -8.28067  -0.10631  1.000 31.44885 ? 153 ALA   A CB   1 
ATOM   1227 N  N    . ALA   A 1 154 ? -40.70557 -6.46023  -2.69238  1.000 37.69103 ? 154 ALA   A N    1 
ATOM   1228 C  CA   . ALA   A 1 154 ? -40.16792 -6.34143  -4.04385  1.000 45.29624 ? 154 ALA   A CA   1 
ATOM   1229 C  C    . ALA   A 1 154 ? -39.06693 -5.28956  -4.10932  1.000 46.10000 ? 154 ALA   A C    1 
ATOM   1230 O  O    . ALA   A 1 154 ? -38.06096 -5.47445  -4.80445  1.000 49.40005 ? 154 ALA   A O    1 
ATOM   1231 C  CB   . ALA   A 1 154 ? -41.28996 -6.01119  -5.02774  1.000 39.98850 ? 154 ALA   A CB   1 
ATOM   1232 N  N    . ARG   A 1 155 ? -39.23625 -4.17964  -3.38814  1.000 40.77363 ? 155 ARG   A N    1 
ATOM   1233 C  CA   . ARG   A 1 155 ? -38.20327 -3.14991  -3.35664  1.000 40.53333 ? 155 ARG   A CA   1 
ATOM   1234 C  C    . ARG   A 1 155 ? -37.02135 -3.56875  -2.48869  1.000 48.80906 ? 155 ARG   A C    1 
ATOM   1235 O  O    . ARG   A 1 155 ? -35.86450 -3.31983  -2.84769  1.000 56.21810 ? 155 ARG   A O    1 
ATOM   1236 C  CB   . ARG   A 1 155 ? -38.79541 -1.83095  -2.85483  1.000 43.59052 ? 155 ARG   A CB   1 
ATOM   1237 C  CG   . ARG   A 1 155 ? -37.76214 -0.76476  -2.52747  1.000 49.87881 ? 155 ARG   A CG   1 
ATOM   1238 C  CD   . ARG   A 1 155 ? -36.93173 -0.40754  -3.74979  1.000 59.96920 ? 155 ARG   A CD   1 
ATOM   1239 N  NE   . ARG   A 1 155 ? -37.76231 0.02827   -4.86538  1.000 57.17479 ? 155 ARG   A NE   1 
ATOM   1240 C  CZ   . ARG   A 1 155 ? -38.13240 1.28420   -5.07374  1.000 62.75639 ? 155 ARG   A CZ   1 
ATOM   1241 N  NH1  . ARG   A 1 155 ? -37.74968 2.26048   -4.26657  1.000 50.96041 ? 155 ARG   A NH1  1 
ATOM   1242 N  NH2  . ARG   A 1 155 ? -38.90384 1.56845   -6.11894  1.000 70.00224 ? 155 ARG   A NH2  1 
ATOM   1243 N  N    . MET   A 1 156 ? -37.29195 -4.20962  -1.34921  1.000 41.87780 ? 156 MET   A N    1 
ATOM   1244 C  CA   . MET   A 1 156 ? -36.21871 -4.57270  -0.42996  1.000 46.85955 ? 156 MET   A CA   1 
ATOM   1245 C  C    . MET   A 1 156 ? -35.32230 -5.66444  -1.00043  1.000 56.63555 ? 156 MET   A C    1 
ATOM   1246 O  O    . MET   A 1 156 ? -34.11780 -5.68165  -0.71867  1.000 59.12463 ? 156 MET   A O    1 
ATOM   1247 C  CB   . MET   A 1 156 ? -36.80431 -5.01797  0.90648   1.000 43.33326 ? 156 MET   A CB   1 
ATOM   1248 C  CG   . MET   A 1 156 ? -37.10773 -3.87770  1.85146   1.000 42.97331 ? 156 MET   A CG   1 
ATOM   1249 S  SD   . MET   A 1 156 ? -37.69875 -4.49684  3.42925   1.000 42.17369 ? 156 MET   A SD   1 
ATOM   1250 C  CE   . MET   A 1 156 ? -36.37785 -5.63329  3.84802   1.000 43.61490 ? 156 MET   A CE   1 
ATOM   1251 N  N    . ARG   A 1 157 ? -35.88557 -6.58500  -1.78762  1.000 50.03342 ? 157 ARG   A N    1 
ATOM   1252 C  CA   . ARG   A 1 157 ? -35.07084 -7.61679  -2.42239  1.000 53.94479 ? 157 ARG   A CA   1 
ATOM   1253 C  C    . ARG   A 1 157 ? -34.02476 -6.99511  -3.33831  1.000 58.89268 ? 157 ARG   A C    1 
ATOM   1254 O  O    . ARG   A 1 157 ? -32.85448 -7.39493  -3.32836  1.000 69.34223 ? 157 ARG   A O    1 
ATOM   1255 C  CB   . ARG   A 1 157 ? -35.96327 -8.58617  -3.19846  1.000 52.34588 ? 157 ARG   A CB   1 
ATOM   1256 C  CG   . ARG   A 1 157 ? -36.70367 -9.58540  -2.32511  1.000 41.57027 ? 157 ARG   A CG   1 
ATOM   1257 C  CD   . ARG   A 1 157 ? -37.26982 -10.72765 -3.15176  1.000 50.40201 ? 157 ARG   A CD   1 
ATOM   1258 N  NE   . ARG   A 1 157 ? -38.44256 -10.31346 -3.91214  1.000 51.04782 ? 157 ARG   A NE   1 
ATOM   1259 C  CZ   . ARG   A 1 157 ? -39.66950 -10.23808 -3.41516  1.000 45.77426 ? 157 ARG   A CZ   1 
ATOM   1260 N  NH1  . ARG   A 1 157 ? -39.92524 -10.54885 -2.15511  1.000 44.13861 ? 157 ARG   A NH1  1 
ATOM   1261 N  NH2  . ARG   A 1 157 ? -40.66533 -9.84148  -4.20254  1.000 46.53215 ? 157 ARG   A NH2  1 
ATOM   1262 N  N    . ALA   A 1 158 ? -34.43173 -6.00728  -4.13896  1.000 59.88461 ? 158 ALA   A N    1 
ATOM   1263 C  CA   . ALA   A 1 158 ? -33.47571 -5.29635  -4.97933  1.000 62.57072 ? 158 ALA   A CA   1 
ATOM   1264 C  C    . ALA   A 1 158 ? -32.49129 -4.48757  -4.14496  1.000 66.26318 ? 158 ALA   A C    1 
ATOM   1265 O  O    . ALA   A 1 158 ? -31.34062 -4.29913  -4.55587  1.000 65.44354 ? 158 ALA   A O    1 
ATOM   1266 C  CB   . ALA   A 1 158 ? -34.21458 -4.38800  -5.96169  1.000 60.88437 ? 158 ALA   A CB   1 
ATOM   1267 N  N    . ASP   A 1 159 ? -32.91882 -4.00971  -2.97430  1.000 65.15723 ? 159 ASP   A N    1 
ATOM   1268 C  CA   . ASP   A 1 159 ? -32.02687 -3.23322  -2.11951  1.000 66.09439 ? 159 ASP   A CA   1 
ATOM   1269 C  C    . ASP   A 1 159 ? -30.94273 -4.11442  -1.51055  1.000 67.03186 ? 159 ASP   A C    1 
ATOM   1270 O  O    . ASP   A 1 159 ? -29.75972 -3.75385  -1.51740  1.000 63.32690 ? 159 ASP   A O    1 
ATOM   1271 C  CB   . ASP   A 1 159 ? -32.83048 -2.52972  -1.02539  1.000 64.72143 ? 159 ASP   A CB   1 
ATOM   1272 C  CG   . ASP   A 1 159 ? -33.59820 -1.33005  -1.54623  1.000 73.65613 ? 159 ASP   A CG   1 
ATOM   1273 O  OD1  . ASP   A 1 159 ? -34.42419 -0.77747  -0.78960  1.000 67.80556 ? 159 ASP   A OD1  1 
ATOM   1274 O  OD2  . ASP   A 1 159 ? -33.37565 -0.93864  -2.71170  1.000 73.15577 ? 159 ASP   A OD2  1 
ATOM   1275 N  N    . SER   A 1 160 ? -31.32688 -5.27142  -0.97876  1.000 63.09884 ? 160 SER   A N    1 
ATOM   1276 C  CA   . SER   A 1 160 ? -30.37400 -6.19473  -0.37288  1.000 57.38708 ? 160 SER   A CA   1 
ATOM   1277 C  C    . SER   A 1 160 ? -29.40372 -6.74340  -1.41340  1.000 61.36177 ? 160 SER   A C    1 
ATOM   1278 O  O    . SER   A 1 160 ? -28.20164 -6.83559  -1.16604  1.000 65.47771 ? 160 SER   A O    1 
ATOM   1279 C  CB   . SER   A 1 160 ? -31.10649 -7.34723  0.31973   1.000 51.91649 ? 160 SER   A CB   1 
ATOM   1280 O  OG   . SER   A 1 160 ? -31.83263 -6.89014  1.44726   1.000 49.92069 ? 160 SER   A OG   1 
ATOM   1281 N  N    . ILE   A 1 171 ? -22.69638 -13.66393 -1.35488  1.000 65.86674 ? 171 ILE   A N    1 
ATOM   1282 C  CA   . ILE   A 1 171 ? -22.79807 -14.00559 0.05810   1.000 65.59089 ? 171 ILE   A CA   1 
ATOM   1283 C  C    . ILE   A 1 171 ? -21.40940 -14.20506 0.65244   1.000 68.98721 ? 171 ILE   A C    1 
ATOM   1284 O  O    . ILE   A 1 171 ? -20.61544 -14.99550 0.14108   1.000 66.01669 ? 171 ILE   A O    1 
ATOM   1285 C  CB   . ILE   A 1 171 ? -23.66275 -15.26167 0.26715   1.000 61.08711 ? 171 ILE   A CB   1 
ATOM   1286 C  CG1  . ILE   A 1 171 ? -25.00868 -15.11040 -0.44406  1.000 57.23094 ? 171 ILE   A CG1  1 
ATOM   1287 C  CG2  . ILE   A 1 171 ? -23.86628 -15.52771 1.75182   1.000 49.19271 ? 171 ILE   A CG2  1 
ATOM   1288 C  CD1  . ILE   A 1 171 ? -25.76355 -16.41141 -0.59857  1.000 45.38598 ? 171 ILE   A CD1  1 
ATOM   1289 N  N    . MET   A 1 172 ? -21.11785 -13.48478 1.73320   1.000 68.07403 ? 172 MET   A N    1 
ATOM   1290 C  CA   . MET   A 1 172 ? -19.83729 -13.64012 2.40241   1.000 61.23301 ? 172 MET   A CA   1 
ATOM   1291 C  C    . MET   A 1 172 ? -19.78644 -14.97506 3.14424   1.000 58.03942 ? 172 MET   A C    1 
ATOM   1292 O  O    . MET   A 1 172 ? -20.80188 -15.64614 3.35256   1.000 58.41105 ? 172 MET   A O    1 
ATOM   1293 C  CB   . MET   A 1 172 ? -19.58541 -12.48063 3.36545   1.000 59.00868 ? 172 MET   A CB   1 
ATOM   1294 C  CG   . MET   A 1 172 ? -18.13672 -12.01807 3.39181   1.000 70.57550 ? 172 MET   A CG   1 
ATOM   1295 S  SD   . MET   A 1 172 ? -17.83701 -10.65577 4.53311   1.000 68.97019 ? 172 MET   A SD   1 
ATOM   1296 C  CE   . MET   A 1 172 ? -16.15071 -10.22524 4.10236   1.000 60.68636 ? 172 MET   A CE   1 
ATOM   1297 N  N    . ASP   A 1 173 ? -18.57860 -15.35921 3.54543   1.000 52.76103 ? 173 ASP   A N    1 
ATOM   1298 C  CA   . ASP   A 1 173 ? -18.34188 -16.65026 4.16665   1.000 47.17013 ? 173 ASP   A CA   1 
ATOM   1299 C  C    . ASP   A 1 173 ? -18.31957 -16.51545 5.68795   1.000 40.81694 ? 173 ASP   A C    1 
ATOM   1300 O  O    . ASP   A 1 173 ? -18.39307 -15.41909 6.24986   1.000 40.45065 ? 173 ASP   A O    1 
ATOM   1301 C  CB   . ASP   A 1 173 ? -17.03978 -17.26141 3.64635   1.000 45.78083 ? 173 ASP   A CB   1 
ATOM   1302 C  CG   . ASP   A 1 173 ? -17.08700 -18.77700 3.60117   1.000 42.22640 ? 173 ASP   A CG   1 
ATOM   1303 O  OD1  . ASP   A 1 173 ? -18.04431 -19.35918 4.15395   1.000 35.09694 ? 173 ASP   A OD1  1 
ATOM   1304 O  OD2  . ASP   A 1 173 ? -16.16678 -19.38610 3.01639   1.000 48.99342 ? 173 ASP   A OD2  1 
ATOM   1305 N  N    . VAL   A 1 174 ? -18.20877 -17.65971 6.36070   1.000 36.65646 ? 174 VAL   A N    1 
ATOM   1306 C  CA   . VAL   A 1 174 ? -18.27407 -17.69004 7.81500   1.000 33.56996 ? 174 VAL   A CA   1 
ATOM   1307 C  C    . VAL   A 1 174 ? -16.95600 -17.20563 8.40998   1.000 31.85895 ? 174 VAL   A C    1 
ATOM   1308 O  O    . VAL   A 1 174 ? -15.89663 -17.24668 7.77835   1.000 31.44126 ? 174 VAL   A O    1 
ATOM   1309 C  CB   . VAL   A 1 174 ? -18.62515 -19.10080 8.32162   1.000 33.85673 ? 174 VAL   A CB   1 
ATOM   1310 C  CG1  . VAL   A 1 174 ? -19.87337 -19.62557 7.62243   1.000 31.31355 ? 174 VAL   A CG1  1 
ATOM   1311 C  CG2  . VAL   A 1 174 ? -17.45086 -20.04547 8.11763   1.000 32.75755 ? 174 VAL   A CG2  1 
ATOM   1312 N  N    . ASN   A 1 175 ? -17.03252 -16.73658 9.64725   1.000 33.51128 ? 175 ASN   A N    1 
ATOM   1313 C  CA   . ASN   A 1 175 ? -15.84577 -16.38347 10.41679  1.000 34.34183 ? 175 ASN   A CA   1 
ATOM   1314 C  C    . ASN   A 1 175 ? -15.30703 -17.62759 11.11184  1.000 35.97162 ? 175 ASN   A C    1 
ATOM   1315 O  O    . ASN   A 1 175 ? -16.06943 -18.32203 11.79602  1.000 31.53149 ? 175 ASN   A O    1 
ATOM   1316 C  CB   . ASN   A 1 175 ? -16.17057 -15.31017 11.44793  1.000 34.30517 ? 175 ASN   A CB   1 
ATOM   1317 C  CG   . ASN   A 1 175 ? -14.98076 -14.95347 12.32104  1.000 39.07362 ? 175 ASN   A CG   1 
ATOM   1318 O  OD1  . ASN   A 1 175 ? -14.66590 -15.65495 13.28231  1.000 40.18871 ? 175 ASN   A OD1  1 
ATOM   1319 N  ND2  . ASN   A 1 175 ? -14.31708 -13.85043 11.99235  1.000 42.19638 ? 175 ASN   A ND2  1 
ATOM   1320 N  N    . PRO   A 1 176 ? -14.01701 -17.94498 10.95466  1.000 34.74771 ? 176 PRO   A N    1 
ATOM   1321 C  CA   . PRO   A 1 176 ? -13.49620 -19.19080 11.54711  1.000 34.98740 ? 176 PRO   A CA   1 
ATOM   1322 C  C    . PRO   A 1 176 ? -13.67321 -19.27052 13.05383  1.000 34.43338 ? 176 PRO   A C    1 
ATOM   1323 O  O    . PRO   A 1 176 ? -14.01013 -20.33987 13.57861  1.000 30.47008 ? 176 PRO   A O    1 
ATOM   1324 C  CB   . PRO   A 1 176 ? -12.01274 -19.16688 11.15182  1.000 38.95179 ? 176 PRO   A CB   1 
ATOM   1325 C  CG   . PRO   A 1 176 ? -11.95606 -18.29934 9.93331   1.000 44.47205 ? 176 PRO   A CG   1 
ATOM   1326 C  CD   . PRO   A 1 176 ? -13.00202 -17.24360 10.15017  1.000 36.37903 ? 176 PRO   A CD   1 
ATOM   1327 N  N    . GLN   A 1 177 ? -13.45621 -18.16325 13.76852  1.000 34.59161 ? 177 GLN   A N    1 
ATOM   1328 C  CA   . GLN   A 1 177 ? -13.58993 -18.18649 15.22114  1.000 35.16811 ? 177 GLN   A CA   1 
ATOM   1329 C  C    . GLN   A 1 177 ? -15.04626 -18.31287 15.65051  1.000 38.33279 ? 177 GLN   A C    1 
ATOM   1330 O  O    . GLN   A 1 177 ? -15.33220 -18.92298 16.68712  1.000 38.93146 ? 177 GLN   A O    1 
ATOM   1331 C  CB   . GLN   A 1 177 ? -12.95919 -16.93378 15.82899  1.000 41.48948 ? 177 GLN   A CB   1 
ATOM   1332 C  CG   . GLN   A 1 177 ? -12.89540 -16.95207 17.34773  1.000 50.24369 ? 177 GLN   A CG   1 
ATOM   1333 C  CD   . GLN   A 1 177 ? -12.02223 -18.07385 17.87844  1.000 60.63634 ? 177 GLN   A CD   1 
ATOM   1334 O  OE1  . GLN   A 1 177 ? -10.85968 -18.20645 17.49467  1.000 61.97053 ? 177 GLN   A OE1  1 
ATOM   1335 N  NE2  . GLN   A 1 177 ? -12.58058 -18.88895 18.76675  1.000 52.71313 ? 177 GLN   A NE2  1 
ATOM   1336 N  N    . ALA   A 1 178 ? -15.97689 -17.74940 14.87464  1.000 34.37371 ? 178 ALA   A N    1 
ATOM   1337 C  CA   . ALA   A 1 178 ? -17.39406 -17.93483 15.17355  1.000 35.32019 ? 178 ALA   A CA   1 
ATOM   1338 C  C    . ALA   A 1 178 ? -17.77664 -19.40857 15.12327  1.000 31.46416 ? 178 ALA   A C    1 
ATOM   1339 O  O    . ALA   A 1 178 ? -18.62068 -19.86676 15.90247  1.000 30.75271 ? 178 ALA   A O    1 
ATOM   1340 C  CB   . ALA   A 1 178 ? -18.24982 -17.12713 14.19929  1.000 35.97896 ? 178 ALA   A CB   1 
ATOM   1341 N  N    . VAL   A 1 179 ? -17.15885 -20.16702 14.21529  1.000 31.62269 ? 179 VAL   A N    1 
ATOM   1342 C  CA   . VAL   A 1 179 ? -17.43284 -21.59827 14.11704  1.000 28.46604 ? 179 VAL   A CA   1 
ATOM   1343 C  C    . VAL   A 1 179 ? -16.95976 -22.32043 15.37338  1.000 31.07568 ? 179 VAL   A C    1 
ATOM   1344 O  O    . VAL   A 1 179 ? -17.69861 -23.11375 15.96906  1.000 29.21156 ? 179 VAL   A O    1 
ATOM   1345 C  CB   . VAL   A 1 179 ? -16.77611 -22.18018 12.85188  1.000 31.24846 ? 179 VAL   A CB   1 
ATOM   1346 C  CG1  . VAL   A 1 179 ? -16.76406 -23.70625 12.90116  1.000 30.86715 ? 179 VAL   A CG1  1 
ATOM   1347 C  CG2  . VAL   A 1 179 ? -17.49136 -21.67819 11.60184  1.000 26.26101 ? 179 VAL   A CG2  1 
ATOM   1348 N  N    . VAL   A 1 180 ? -15.71849 -22.05855 15.79209  1.000 30.37497 ? 180 VAL   A N    1 
ATOM   1349 C  CA   . VAL   A 1 180 ? -15.18289 -22.69728 16.99183  1.000 32.03017 ? 180 VAL   A CA   1 
ATOM   1350 C  C    . VAL   A 1 180 ? -16.01722 -22.32904 18.21186  1.000 33.75878 ? 180 VAL   A C    1 
ATOM   1351 O  O    . VAL   A 1 180 ? -16.29459 -23.17511 19.07135  1.000 33.64631 ? 180 VAL   A O    1 
ATOM   1352 C  CB   . VAL   A 1 180 ? -13.70239 -22.31617 17.18316  1.000 35.56998 ? 180 VAL   A CB   1 
ATOM   1353 C  CG1  . VAL   A 1 180 ? -13.18731 -22.81110 18.52831  1.000 34.26522 ? 180 VAL   A CG1  1 
ATOM   1354 C  CG2  . VAL   A 1 180 ? -12.85973 -22.87316 16.04511  1.000 32.95141 ? 180 VAL   A CG2  1 
ATOM   1355 N  N    A ASP   A 1 181 ? -16.43090 -21.06310 18.30617  0.422 33.92007 ? 181 ASP   A N    1 
ATOM   1356 N  N    B ASP   A 1 181 ? -16.43752 -21.06485 18.30234  0.578 33.90184 ? 181 ASP   A N    1 
ATOM   1357 C  CA   A ASP   A 1 181 ? -17.21027 -20.62443 19.45942  0.422 36.41768 ? 181 ASP   A CA   1 
ATOM   1358 C  CA   B ASP   A 1 181 ? -17.21112 -20.62211 19.45831  0.578 36.44175 ? 181 ASP   A CA   1 
ATOM   1359 C  C    A ASP   A 1 181 ? -18.54214 -21.36005 19.54114  0.422 35.20142 ? 181 ASP   A C    1 
ATOM   1360 C  C    B ASP   A 1 181 ? -18.54856 -21.34661 19.54281  0.578 35.17292 ? 181 ASP   A C    1 
ATOM   1361 O  O    A ASP   A 1 181 ? -18.95158 -21.79877 20.62224  0.422 36.69387 ? 181 ASP   A O    1 
ATOM   1362 O  O    B ASP   A 1 181 ? -18.96778 -21.76471 20.62805  0.578 36.70404 ? 181 ASP   A O    1 
ATOM   1363 C  CB   A ASP   A 1 181 ? -17.43633 -19.11457 19.39599  0.422 36.34076 ? 181 ASP   A CB   1 
ATOM   1364 C  CB   B ASP   A 1 181 ? -17.42309 -19.10980 19.39883  0.578 36.33153 ? 181 ASP   A CB   1 
ATOM   1365 C  CG   A ASP   A 1 181 ? -18.51959 -18.64910 20.34802  0.422 39.07670 ? 181 ASP   A CG   1 
ATOM   1366 C  CG   B ASP   A 1 181 ? -16.14122 -18.33215 19.62065  0.578 40.94996 ? 181 ASP   A CG   1 
ATOM   1367 O  OD1  A ASP   A 1 181 ? -18.46184 -19.01367 21.54142  0.422 41.67204 ? 181 ASP   A OD1  1 
ATOM   1368 O  OD1  B ASP   A 1 181 ? -15.11922 -18.95284 19.98369  0.578 41.33525 ? 181 ASP   A OD1  1 
ATOM   1369 O  OD2  A ASP   A 1 181 ? -19.43460 -17.92632 19.90110  0.422 40.03075 ? 181 ASP   A OD2  1 
ATOM   1370 O  OD2  B ASP   A 1 181 ? -16.15668 -17.09796 19.43228  0.578 41.80686 ? 181 ASP   A OD2  1 
ATOM   1371 N  N    . ALA   A 1 182 ? -19.23228 -21.50726 18.40795  1.000 32.65994 ? 182 ALA   A N    1 
ATOM   1372 C  CA   . ALA   A 1 182 ? -20.51807 -22.19771 18.41405  1.000 36.28594 ? 182 ALA   A CA   1 
ATOM   1373 C  C    . ALA   A 1 182 ? -20.34597 -23.68063 18.71530  1.000 34.73783 ? 182 ALA   A C    1 
ATOM   1374 O  O    . ALA   A 1 182 ? -21.14181 -24.26881 19.45696  1.000 30.83250 ? 182 ALA   A O    1 
ATOM   1375 C  CB   . ALA   A 1 182 ? -21.22336 -22.00277 17.07224  1.000 31.93297 ? 182 ALA   A CB   1 
ATOM   1376 N  N    . MET   A 1 183 ? -19.30035 -24.29471 18.16055  1.000 30.43115 ? 183 MET   A N    1 
ATOM   1377 C  CA   . MET   A 1 183 ? -19.10134 -25.72833 18.32166  1.000 30.03448 ? 183 MET   A CA   1 
ATOM   1378 C  C    . MET   A 1 183 ? -18.65396 -26.07371 19.73614  1.000 32.97985 ? 183 MET   A C    1 
ATOM   1379 O  O    . MET   A 1 183 ? -18.88735 -27.19405 20.20510  1.000 32.70919 ? 183 MET   A O    1 
ATOM   1380 C  CB   . MET   A 1 183 ? -18.08720 -26.21136 17.28933  1.000 29.90237 ? 183 MET   A CB   1 
ATOM   1381 C  CG   . MET   A 1 183 ? -18.68311 -26.31965 15.89533  1.000 25.02978 ? 183 MET   A CG   1 
ATOM   1382 S  SD   . MET   A 1 183 ? -17.64961 -27.21796 14.73335  1.000 26.63777 ? 183 MET   A SD   1 
ATOM   1383 C  CE   . MET   A 1 183 ? -18.30622 -28.87406 14.91821  1.000 25.70819 ? 183 MET   A CE   1 
ATOM   1384 N  N    . GLU   A 1 184 ? -18.01802 -25.12891 20.43005  1.000 33.57453 ? 184 GLU   A N    1 
ATOM   1385 C  CA   . GLU   A 1 184 ? -17.63596 -25.33140 21.82042  1.000 35.21899 ? 184 GLU   A CA   1 
ATOM   1386 C  C    . GLU   A 1 184 ? -18.73317 -24.91390 22.78736  1.000 35.75828 ? 184 GLU   A C    1 
ATOM   1387 O  O    . GLU   A 1 184 ? -18.84053 -25.49285 23.87436  1.000 41.05727 ? 184 GLU   A O    1 
ATOM   1388 C  CB   . GLU   A 1 184 ? -16.34213 -24.57078 22.12344  1.000 36.21914 ? 184 GLU   A CB   1 
ATOM   1389 C  CG   . GLU   A 1 184 ? -15.13690 -25.11817 21.37136  1.000 35.51316 ? 184 GLU   A CG   1 
ATOM   1390 C  CD   . GLU   A 1 184 ? -13.81776 -24.56080 21.86685  1.000 43.03473 ? 184 GLU   A CD   1 
ATOM   1391 O  OE1  . GLU   A 1 184 ? -13.80880 -23.43928 22.41612  1.000 44.42356 ? 184 GLU   A OE1  1 
ATOM   1392 O  OE2  . GLU   A 1 184 ? -12.78705 -25.24823 21.69992  1.000 40.82909 ? 184 GLU   A OE2  1 
ATOM   1393 N  N    . ARG   A 1 185 ? -19.54952 -23.92322 22.41556  1.000 36.44147 ? 185 ARG   A N    1 
ATOM   1394 C  CA   . ARG   A 1 185 ? -20.73259 -23.60356 23.20821  1.000 38.26319 ? 185 ARG   A CA   1 
ATOM   1395 C  C    . ARG   A 1 185 ? -21.63364 -24.82235 23.35555  1.000 37.03576 ? 185 ARG   A C    1 
ATOM   1396 O  O    . ARG   A 1 185 ? -22.17068 -25.08268 24.43879  1.000 38.13040 ? 185 ARG   A O    1 
ATOM   1397 C  CB   . ARG   A 1 185 ? -21.50626 -22.45364 22.56170  1.000 38.27493 ? 185 ARG   A CB   1 
ATOM   1398 C  CG   . ARG   A 1 185 ? -21.08439 -21.06640 23.01201  1.000 43.82162 ? 185 ARG   A CG   1 
ATOM   1399 C  CD   . ARG   A 1 185 ? -22.10039 -20.01292 22.58188  1.000 45.72482 ? 185 ARG   A CD   1 
ATOM   1400 N  NE   . ARG   A 1 185 ? -22.16453 -19.86150 21.13217  1.000 41.65971 ? 185 ARG   A NE   1 
ATOM   1401 C  CZ   . ARG   A 1 185 ? -23.19334 -20.23592 20.38342  1.000 41.06393 ? 185 ARG   A CZ   1 
ATOM   1402 N  NH1  . ARG   A 1 185 ? -24.27204 -20.78663 20.91594  1.000 41.33624 ? 185 ARG   A NH1  1 
ATOM   1403 N  NH2  . ARG   A 1 185 ? -23.13800 -20.05458 19.06695  1.000 40.36555 ? 185 ARG   A NH2  1 
ATOM   1404 N  N    . HIS   A 1 186 ? -21.81019 -25.57917 22.27261  1.000 36.20370 ? 186 HIS   A N    1 
ATOM   1405 C  CA   . HIS   A 1 186 ? -22.65211 -26.76604 22.26422  1.000 37.78846 ? 186 HIS   A CA   1 
ATOM   1406 C  C    . HIS   A 1 186 ? -21.86774 -28.04893 22.49843  1.000 38.93188 ? 186 HIS   A C    1 
ATOM   1407 O  O    . HIS   A 1 186 ? -22.48108 -29.11611 22.61421  1.000 36.57282 ? 186 HIS   A O    1 
ATOM   1408 C  CB   . HIS   A 1 186 ? -23.41099 -26.85955 20.93473  1.000 34.45893 ? 186 HIS   A CB   1 
ATOM   1409 C  CG   . HIS   A 1 186 ? -24.43817 -25.78631 20.75252  1.000 36.01670 ? 186 HIS   A CG   1 
ATOM   1410 N  ND1  . HIS   A 1 186 ? -25.76192 -25.95686 21.09670  1.000 37.96735 ? 186 HIS   A ND1  1 
ATOM   1411 C  CD2  . HIS   A 1 186 ? -24.33301 -24.52327 20.27550  1.000 35.59925 ? 186 HIS   A CD2  1 
ATOM   1412 C  CE1  . HIS   A 1 186 ? -26.42893 -24.84701 20.83457  1.000 40.78162 ? 186 HIS   A CE1  1 
ATOM   1413 N  NE2  . HIS   A 1 186 ? -25.58511 -23.96148 20.33587  1.000 36.15927 ? 186 HIS   A NE2  1 
ATOM   1414 N  N    . HIS   A 1 187 ? -20.53822 -27.96316 22.57091  1.000 37.01608 ? 187 HIS   A N    1 
ATOM   1415 C  CA   . HIS   A 1 187 ? -19.67011 -29.10565 22.85035  1.000 36.22206 ? 187 HIS   A CA   1 
ATOM   1416 C  C    . HIS   A 1 187 ? -19.92027 -30.23763 21.85682  1.000 36.55400 ? 187 HIS   A C    1 
ATOM   1417 O  O    . HIS   A 1 187 ? -20.21127 -31.37677 22.22726  1.000 40.73796 ? 187 HIS   A O    1 
ATOM   1418 C  CB   . HIS   A 1 187 ? -19.84548 -29.58414 24.29275  1.000 42.97541 ? 187 HIS   A CB   1 
ATOM   1419 C  CG   . HIS   A 1 187 ? -18.82436 -30.59242 24.72659  1.000 51.07604 ? 187 HIS   A CG   1 
ATOM   1420 N  ND1  . HIS   A 1 187 ? -17.50019 -30.26890 24.93131  1.000 52.60469 ? 187 HIS   A ND1  1 
ATOM   1421 C  CD2  . HIS   A 1 187 ? -18.93661 -31.91242 25.01097  1.000 56.27596 ? 187 HIS   A CD2  1 
ATOM   1422 C  CE1  . HIS   A 1 187 ? -16.83957 -31.34753 25.31431  1.000 50.30677 ? 187 HIS   A CE1  1 
ATOM   1423 N  NE2  . HIS   A 1 187 ? -17.68747 -32.35881 25.36888  1.000 57.62941 ? 187 HIS   A NE2  1 
ATOM   1424 N  N    . VAL   A 1 188 ? -19.80719 -29.90854 20.57129  1.000 29.64495 ? 188 VAL   A N    1 
ATOM   1425 C  CA   . VAL   A 1 188 ? -20.03680 -30.86385 19.49769  1.000 34.60055 ? 188 VAL   A CA   1 
ATOM   1426 C  C    . VAL   A 1 188 ? -18.78659 -30.95049 18.63337  1.000 33.82283 ? 188 VAL   A C    1 
ATOM   1427 O  O    . VAL   A 1 188 ? -17.95110 -30.04363 18.60527  1.000 27.35491 ? 188 VAL   A O    1 
ATOM   1428 C  CB   . VAL   A 1 188 ? -21.25883 -30.49165 18.63210  1.000 32.31323 ? 188 VAL   A CB   1 
ATOM   1429 C  CG1  . VAL   A 1 188 ? -22.54466 -30.60989 19.43506  1.000 32.68720 ? 188 VAL   A CG1  1 
ATOM   1430 C  CG2  . VAL   A 1 188 ? -21.09686 -29.08851 18.06086  1.000 28.53611 ? 188 VAL   A CG2  1 
ATOM   1431 N  N    . GLN   A 1 189 ? -18.66970 -32.06757 17.91826  1.000 29.82189 ? 189 GLN   A N    1 
ATOM   1432 C  CA   . GLN   A 1 189 ? -17.62378 -32.25669 16.92469  1.000 31.83589 ? 189 GLN   A CA   1 
ATOM   1433 C  C    . GLN   A 1 189 ? -18.16324 -32.23174 15.50204  1.000 31.79228 ? 189 GLN   A C    1 
ATOM   1434 O  O    . GLN   A 1 189 ? -17.39217 -32.42646 14.55681  1.000 26.97349 ? 189 GLN   A O    1 
ATOM   1435 C  CB   . GLN   A 1 189 ? -16.88076 -33.57748 17.17268  1.000 30.59804 ? 189 GLN   A CB   1 
ATOM   1436 C  CG   . GLN   A 1 189 ? -16.35537 -33.75414 18.59160  1.000 31.88793 ? 189 GLN   A CG   1 
ATOM   1437 C  CD   . GLN   A 1 189 ? -15.56000 -32.55799 19.08019  1.000 35.31009 ? 189 GLN   A CD   1 
ATOM   1438 O  OE1  . GLN   A 1 189 ? -15.87945 -31.96527 20.11076  1.000 33.65048 ? 189 GLN   A OE1  1 
ATOM   1439 N  NE2  . GLN   A 1 189 ? -14.51643 -32.19840 18.34189  1.000 31.74175 ? 189 GLN   A NE2  1 
ATOM   1440 N  N    . TRP   A 1 190 ? -19.46271 -31.99693 15.32425  1.000 25.61075 ? 190 TRP   A N    1 
ATOM   1441 C  CA   . TRP   A 1 190 ? -20.08387 -31.97281 14.00892  1.000 27.97423 ? 190 TRP   A CA   1 
ATOM   1442 C  C    . TRP   A 1 190 ? -21.03256 -30.78839 13.91929  1.000 25.11057 ? 190 TRP   A C    1 
ATOM   1443 O  O    . TRP   A 1 190 ? -21.77465 -30.50135 14.86322  1.000 27.70181 ? 190 TRP   A O    1 
ATOM   1444 C  CB   . TRP   A 1 190 ? -20.84641 -33.27298 13.71495  1.000 27.18331 ? 190 TRP   A CB   1 
ATOM   1445 C  CG   . TRP   A 1 190 ? -19.95439 -34.42077 13.35521  1.000 30.80508 ? 190 TRP   A CG   1 
ATOM   1446 C  CD1  . TRP   A 1 190 ? -19.46976 -35.37703 14.19793  1.000 31.63456 ? 190 TRP   A CD1  1 
ATOM   1447 C  CD2  . TRP   A 1 190 ? -19.43289 -34.72901 12.05560  1.000 29.29289 ? 190 TRP   A CD2  1 
ATOM   1448 N  NE1  . TRP   A 1 190 ? -18.68089 -36.26340 13.50452  1.000 30.80614 ? 190 TRP   A NE1  1 
ATOM   1449 C  CE2  . TRP   A 1 190 ? -18.64190 -35.88725 12.18739  1.000 32.37876 ? 190 TRP   A CE2  1 
ATOM   1450 C  CE3  . TRP   A 1 190 ? -19.55875 -34.13803 10.79427  1.000 28.65251 ? 190 TRP   A CE3  1 
ATOM   1451 C  CZ2  . TRP   A 1 190 ? -17.97933 -36.46709 11.10588  1.000 33.67974 ? 190 TRP   A CZ2  1 
ATOM   1452 C  CZ3  . TRP   A 1 190 ? -18.90068 -34.71599 9.72156   1.000 31.75962 ? 190 TRP   A CZ3  1 
ATOM   1453 C  CH2  . TRP   A 1 190 ? -18.12080 -35.86802 9.88517   1.000 30.34258 ? 190 TRP   A CH2  1 
ATOM   1454 N  N    . LEU   A 1 191 ? -21.00405 -30.10968 12.77532  1.000 24.86743 ? 191 LEU   A N    1 
ATOM   1455 C  CA   . LEU   A 1 191 ? -21.85769 -28.95787 12.52083  1.000 24.24982 ? 191 LEU   A CA   1 
ATOM   1456 C  C    . LEU   A 1 191 ? -22.31633 -29.00320 11.07196  1.000 23.18686 ? 191 LEU   A C    1 
ATOM   1457 O  O    . LEU   A 1 191 ? -21.49835 -29.19445 10.16768  1.000 25.33209 ? 191 LEU   A O    1 
ATOM   1458 C  CB   . LEU   A 1 191 ? -21.11486 -27.64561 12.81714  1.000 21.93138 ? 191 LEU   A CB   1 
ATOM   1459 C  CG   . LEU   A 1 191 ? -21.59613 -26.35043 12.15654  1.000 24.03255 ? 191 LEU   A CG   1 
ATOM   1460 C  CD1  . LEU   A 1 191 ? -22.97445 -25.93986 12.66938  1.000 23.84933 ? 191 LEU   A CD1  1 
ATOM   1461 C  CD2  . LEU   A 1 191 ? -20.58251 -25.23492 12.38228  1.000 22.67279 ? 191 LEU   A CD2  1 
ATOM   1462 N  N    . ILE   A 1 192 ? -23.62135 -28.84781 10.85659  1.000 21.82036 ? 192 ILE   A N    1 
ATOM   1463 C  CA   . ILE   A 1 192 ? -24.20912 -28.80587 9.52234   1.000 18.95491 ? 192 ILE   A CA   1 
ATOM   1464 C  C    . ILE   A 1 192 ? -24.93793 -27.48007 9.36565   1.000 19.83316 ? 192 ILE   A C    1 
ATOM   1465 O  O    . ILE   A 1 192 ? -25.72766 -27.09496 10.23592  1.000 20.29085 ? 192 ILE   A O    1 
ATOM   1466 C  CB   . ILE   A 1 192 ? -25.17510 -29.98096 9.27906   1.000 20.06808 ? 192 ILE   A CB   1 
ATOM   1467 C  CG1  . ILE   A 1 192 ? -24.48466 -31.31783 9.55021   1.000 18.05212 ? 192 ILE   A CG1  1 
ATOM   1468 C  CG2  . ILE   A 1 192 ? -25.71887 -29.93634 7.85434   1.000 22.22053 ? 192 ILE   A CG2  1 
ATOM   1469 C  CD1  . ILE   A 1 192 ? -25.42822 -32.50745 9.51497   1.000 20.53614 ? 192 ILE   A CD1  1 
ATOM   1470 N  N    . HIS   A 1 193 ? -24.68186 -26.78886 8.25765   1.000 18.35978 ? 193 HIS   A N    1 
ATOM   1471 C  CA   . HIS   A 1 193 ? -25.35831 -25.52982 7.98708   1.000 19.54765 ? 193 HIS   A CA   1 
ATOM   1472 C  C    . HIS   A 1 193 ? -25.38318 -25.28295 6.48647   1.000 21.06456 ? 193 HIS   A C    1 
ATOM   1473 O  O    . HIS   A 1 193 ? -24.79985 -26.03132 5.69800   1.000 21.71513 ? 193 HIS   A O    1 
ATOM   1474 C  CB   . HIS   A 1 193 ? -24.69318 -24.36097 8.73098   1.000 20.92341 ? 193 HIS   A CB   1 
ATOM   1475 C  CG   . HIS   A 1 193 ? -23.36731 -23.94746 8.16780   1.000 19.74200 ? 193 HIS   A CG   1 
ATOM   1476 N  ND1  . HIS   A 1 193 ? -23.24754 -23.12276 7.06930   1.000 22.77117 ? 193 HIS   A ND1  1 
ATOM   1477 C  CD2  . HIS   A 1 193 ? -22.10311 -24.23040 8.56409   1.000 21.34804 ? 193 HIS   A CD2  1 
ATOM   1478 C  CE1  . HIS   A 1 193 ? -21.96794 -22.92163 6.80873   1.000 20.22749 ? 193 HIS   A CE1  1 
ATOM   1479 N  NE2  . HIS   A 1 193 ? -21.25236 -23.58278 7.70081   1.000 21.62483 ? 193 HIS   A NE2  1 
ATOM   1480 N  N    . GLY   A 1 194 ? -26.08849 -24.22389 6.10155   1.000 20.81132 ? 194 GLY   A N    1 
ATOM   1481 C  CA   . GLY   A 1 194 ? -26.12284 -23.78445 4.72285   1.000 19.12205 ? 194 GLY   A CA   1 
ATOM   1482 C  C    . GLY   A 1 194 ? -25.75285 -22.32205 4.58956   1.000 23.15190 ? 194 GLY   A C    1 
ATOM   1483 O  O    . GLY   A 1 194 ? -24.69860 -21.89921 5.07454   1.000 23.09998 ? 194 GLY   A O    1 
ATOM   1484 N  N    . HIS   A 1 195 ? -26.61804 -21.55138 3.92357   1.000 21.48989 ? 195 HIS   A N    1 
ATOM   1485 C  CA   . HIS   A 1 195 ? -26.49764 -20.10398 3.74936   1.000 23.97747 ? 195 HIS   A CA   1 
ATOM   1486 C  C    . HIS   A 1 195 ? -25.35991 -19.67987 2.82332   1.000 23.56468 ? 195 HIS   A C    1 
ATOM   1487 O  O    . HIS   A 1 195 ? -25.56315 -18.83320 1.94758   1.000 23.94775 ? 195 HIS   A O    1 
ATOM   1488 C  CB   . HIS   A 1 195 ? -26.33193 -19.39747 5.09752   1.000 22.65335 ? 195 HIS   A CB   1 
ATOM   1489 C  CG   . HIS   A 1 195 ? -26.15858 -17.91546 4.97547   1.000 24.10515 ? 195 HIS   A CG   1 
ATOM   1490 N  ND1  . HIS   A 1 195 ? -27.18151 -17.07768 4.58646   1.000 23.48448 ? 195 HIS   A ND1  1 
ATOM   1491 C  CD2  . HIS   A 1 195 ? -25.07646 -17.12413 5.16663   1.000 22.98152 ? 195 HIS   A CD2  1 
ATOM   1492 C  CE1  . HIS   A 1 195 ? -26.74107 -15.83238 4.55630   1.000 26.38562 ? 195 HIS   A CE1  1 
ATOM   1493 N  NE2  . HIS   A 1 195 ? -25.46663 -15.83310 4.90386   1.000 24.01745 ? 195 HIS   A NE2  1 
ATOM   1494 N  N    . THR   A 1 196 ? -24.15838 -20.22832 3.01003   1.000 21.57509 ? 196 THR   A N    1 
ATOM   1495 C  CA   . THR   A 1 196 ? -23.01356 -19.75640 2.23748   1.000 25.38026 ? 196 THR   A CA   1 
ATOM   1496 C  C    . THR   A 1 196 ? -22.98937 -20.28625 0.80972   1.000 24.63656 ? 196 THR   A C    1 
ATOM   1497 O  O    . THR   A 1 196 ? -22.22776 -19.75977 -0.00972  1.000 25.14820 ? 196 THR   A O    1 
ATOM   1498 C  CB   . THR   A 1 196 ? -21.70084 -20.12552 2.93576   1.000 29.35063 ? 196 THR   A CB   1 
ATOM   1499 O  OG1  . THR   A 1 196 ? -21.59630 -21.54967 3.04608   1.000 25.18027 ? 196 THR   A OG1  1 
ATOM   1500 C  CG2  . THR   A 1 196 ? -21.63922 -19.50167 4.32475   1.000 27.67654 ? 196 THR   A CG2  1 
ATOM   1501 N  N    . HIS   A 1 197 ? -23.79313 -21.30526 0.49582   1.000 24.49434 ? 197 HIS   A N    1 
ATOM   1502 C  CA   . HIS   A 1 197 ? -23.88823 -21.85983 -0.85655  1.000 23.22662 ? 197 HIS   A CA   1 
ATOM   1503 C  C    . HIS   A 1 197 ? -22.54894 -22.41873 -1.33361  1.000 25.51518 ? 197 HIS   A C    1 
ATOM   1504 O  O    . HIS   A 1 197 ? -22.24967 -22.41073 -2.52993  1.000 24.98730 ? 197 HIS   A O    1 
ATOM   1505 C  CB   . HIS   A 1 197 ? -24.41878 -20.81938 -1.85136  1.000 25.49802 ? 197 HIS   A CB   1 
ATOM   1506 C  CG   . HIS   A 1 197 ? -25.79357 -20.31423 -1.53168  1.000 26.35365 ? 197 HIS   A CG   1 
ATOM   1507 N  ND1  . HIS   A 1 197 ? -26.49759 -19.48748 -2.38153  1.000 28.80334 ? 197 HIS   A ND1  1 
ATOM   1508 C  CD2  . HIS   A 1 197 ? -26.59618 -20.52256 -0.46065  1.000 23.85273 ? 197 HIS   A CD2  1 
ATOM   1509 C  CE1  . HIS   A 1 197 ? -27.67182 -19.20449 -1.84561  1.000 27.68426 ? 197 HIS   A CE1  1 
ATOM   1510 N  NE2  . HIS   A 1 197 ? -27.75704 -19.82074 -0.68018  1.000 27.46845 ? 197 HIS   A NE2  1 
ATOM   1511 N  N    . ARG   A 1 198 ? -21.72930 -22.90577 -0.40384  1.000 21.23220 ? 198 ARG   A N    1 
ATOM   1512 C  CA   . ARG   A 1 198 ? -20.40798 -23.45384 -0.71261  1.000 24.82308 ? 198 ARG   A CA   1 
ATOM   1513 C  C    . ARG   A 1 198 ? -20.32086 -24.85680 -0.12927  1.000 24.18286 ? 198 ARG   A C    1 
ATOM   1514 O  O    . ARG   A 1 198 ? -19.71269 -25.06147 0.92994   1.000 23.89063 ? 198 ARG   A O    1 
ATOM   1515 C  CB   . ARG   A 1 198 ? -19.29219 -22.56821 -0.15543  1.000 26.02609 ? 198 ARG   A CB   1 
ATOM   1516 C  CG   . ARG   A 1 198 ? -19.08022 -21.24733 -0.88062  1.000 30.63981 ? 198 ARG   A CG   1 
ATOM   1517 C  CD   . ARG   A 1 198 ? -18.33625 -20.27559 0.02926   1.000 39.20705 ? 198 ARG   A CD   1 
ATOM   1518 N  NE   . ARG   A 1 198 ? -18.03998 -18.99904 -0.60943  1.000 44.61223 ? 198 ARG   A NE   1 
ATOM   1519 C  CZ   . ARG   A 1 198 ? -18.58323 -17.84199 -0.25573  1.000 51.39095 ? 198 ARG   A CZ   1 
ATOM   1520 N  NH1  . ARG   A 1 198 ? -19.48065 -17.76676 0.71443   1.000 49.98485 ? 198 ARG   A NH1  1 
ATOM   1521 N  NH2  . ARG   A 1 198 ? -18.21760 -16.73237 -0.89116  1.000 57.04524 ? 198 ARG   A NH2  1 
ATOM   1522 N  N    . PRO   A 1 199 ? -20.91358 -25.84830 -0.79421  1.000 25.86313 ? 199 PRO   A N    1 
ATOM   1523 C  CA   . PRO   A 1 199 ? -20.92085 -27.20828 -0.23581  1.000 22.67320 ? 199 PRO   A CA   1 
ATOM   1524 C  C    . PRO   A 1 199 ? -19.50702 -27.74440 -0.05764  1.000 23.74969 ? 199 PRO   A C    1 
ATOM   1525 O  O    . PRO   A 1 199 ? -18.69678 -27.73116 -0.98721  1.000 25.64982 ? 199 PRO   A O    1 
ATOM   1526 C  CB   . PRO   A 1 199 ? -21.71171 -28.01659 -1.27215  1.000 25.57690 ? 199 PRO   A CB   1 
ATOM   1527 C  CG   . PRO   A 1 199 ? -21.67180 -27.20205 -2.52349  1.000 27.23225 ? 199 PRO   A CG   1 
ATOM   1528 C  CD   . PRO   A 1 199 ? -21.61024 -25.77172 -2.08927  1.000 25.12663 ? 199 PRO   A CD   1 
ATOM   1529 N  N    . ALA   A 1 200 ? -19.21734 -28.22004 1.15153   1.000 19.57864 ? 200 ALA   A N    1 
ATOM   1530 C  CA   . ALA   A 1 200 ? -17.86538 -28.62869 1.51219   1.000 24.21439 ? 200 ALA   A CA   1 
ATOM   1531 C  C    . ALA   A 1 200 ? -17.90509 -29.34422 2.85507   1.000 24.77045 ? 200 ALA   A C    1 
ATOM   1532 O  O    . ALA   A 1 200 ? -18.91765 -29.33461 3.56046   1.000 19.88075 ? 200 ALA   A O    1 
ATOM   1533 C  CB   . ALA   A 1 200 ? -16.91529 -27.42910 1.57466   1.000 22.49297 ? 200 ALA   A CB   1 
ATOM   1534 N  N    . VAL   A 1 201 ? -16.77781 -29.96456 3.19715   1.000 23.64455 ? 201 VAL   A N    1 
ATOM   1535 C  CA   . VAL   A 1 201 ? -16.55328 -30.57329 4.50376   1.000 26.44031 ? 201 VAL   A CA   1 
ATOM   1536 C  C    . VAL   A 1 201 ? -15.24390 -30.00635 5.03348   1.000 26.14475 ? 201 VAL   A C    1 
ATOM   1537 O  O    . VAL   A 1 201 ? -14.17012 -30.31709 4.50315   1.000 27.53809 ? 201 VAL   A O    1 
ATOM   1538 C  CB   . VAL   A 1 201 ? -16.49689 -32.10619 4.43879   1.000 26.27464 ? 201 VAL   A CB   1 
ATOM   1539 C  CG1  . VAL   A 1 201 ? -16.18479 -32.68165 5.81344   1.000 26.84890 ? 201 VAL   A CG1  1 
ATOM   1540 C  CG2  . VAL   A 1 201 ? -17.80868 -32.66627 3.91310   1.000 26.84785 ? 201 VAL   A CG2  1 
ATOM   1541 N  N    . HIS   A 1 202 ? -15.32761 -29.17765 6.06966   1.000 27.09958 ? 202 HIS   A N    1 
ATOM   1542 C  CA   . HIS   A 1 202 ? -14.16311 -28.52627 6.65431   1.000 28.53094 ? 202 HIS   A CA   1 
ATOM   1543 C  C    . HIS   A 1 202 ? -13.76743 -29.23492 7.94229   1.000 28.17208 ? 202 HIS   A C    1 
ATOM   1544 O  O    . HIS   A 1 202 ? -14.60439 -29.43255 8.82817   1.000 29.92205 ? 202 HIS   A O    1 
ATOM   1545 C  CB   . HIS   A 1 202 ? -14.45146 -27.05240 6.94666   1.000 25.52946 ? 202 HIS   A CB   1 
ATOM   1546 C  CG   . HIS   A 1 202 ? -14.92055 -26.27461 5.75662   1.000 26.26266 ? 202 HIS   A CG   1 
ATOM   1547 N  ND1  . HIS   A 1 202 ? -14.05970 -25.57792 4.93582   1.000 24.91702 ? 202 HIS   A ND1  1 
ATOM   1548 C  CD2  . HIS   A 1 202 ? -16.16303 -26.07092 5.25788   1.000 26.03308 ? 202 HIS   A CD2  1 
ATOM   1549 C  CE1  . HIS   A 1 202 ? -14.75065 -24.98432 3.97884   1.000 27.63429 ? 202 HIS   A CE1  1 
ATOM   1550 N  NE2  . HIS   A 1 202 ? -16.02933 -25.26753 4.15128   1.000 26.88472 ? 202 HIS   A NE2  1 
ATOM   1551 N  N    . GLU   A 1 203 ? -12.49616 -29.60711 8.04848   1.000 26.90644 ? 203 GLU   A N    1 
ATOM   1552 C  CA   . GLU   A 1 203 ? -11.96500 -30.14667 9.29115   1.000 23.92370 ? 203 GLU   A CA   1 
ATOM   1553 C  C    . GLU   A 1 203 ? -11.36108 -29.02353 10.12233  1.000 30.70851 ? 203 GLU   A C    1 
ATOM   1554 O  O    . GLU   A 1 203 ? -10.66150 -28.15249 9.59780   1.000 31.67475 ? 203 GLU   A O    1 
ATOM   1555 C  CB   . GLU   A 1 203 ? -10.91298 -31.22516 9.02254   1.000 30.11888 ? 203 GLU   A CB   1 
ATOM   1556 C  CG   . GLU   A 1 203 ? -10.34425 -31.85265 10.29064  1.000 32.04826 ? 203 GLU   A CG   1 
ATOM   1557 C  CD   . GLU   A 1 203 ? -9.44930  -33.04662 10.01138  1.000 46.57040 ? 203 GLU   A CD   1 
ATOM   1558 O  OE1  . GLU   A 1 203 ? -9.09626  -33.27095 8.83423   1.000 48.32574 ? 203 GLU   A OE1  1 
ATOM   1559 O  OE2  . GLU   A 1 203 ? -9.08791  -33.75509 10.97439  1.000 47.12326 ? 203 GLU   A OE2  1 
ATOM   1560 N  N    . LEU   A 1 204 ? -11.64531 -29.04510 11.42058  1.000 29.55234 ? 204 LEU   A N    1 
ATOM   1561 C  CA   . LEU   A 1 204 ? -11.10711 -28.06523 12.35371  1.000 34.50595 ? 204 LEU   A CA   1 
ATOM   1562 C  C    . LEU   A 1 204 ? -10.86797 -28.76544 13.68643  1.000 32.51283 ? 204 LEU   A C    1 
ATOM   1563 O  O    . LEU   A 1 204 ? -10.96589 -29.99166 13.78879  1.000 31.43013 ? 204 LEU   A O    1 
ATOM   1564 C  CB   . LEU   A 1 204 ? -12.05564 -26.86607 12.48715  1.000 31.42137 ? 204 LEU   A CB   1 
ATOM   1565 C  CG   . LEU   A 1 204 ? -13.44313 -27.15354 13.06847  1.000 30.75368 ? 204 LEU   A CG   1 
ATOM   1566 C  CD1  . LEU   A 1 204 ? -13.84034 -26.08129 14.07287  1.000 29.90130 ? 204 LEU   A CD1  1 
ATOM   1567 C  CD2  . LEU   A 1 204 ? -14.48603 -27.26666 11.96538  1.000 27.34585 ? 204 LEU   A CD2  1 
ATOM   1568 N  N    . GLN   A 1 205 ? -10.55003 -27.98432 14.71416  1.000 33.80070 ? 205 GLN   A N    1 
ATOM   1569 C  CA   . GLN   A 1 205 ? -10.41562 -28.49635 16.07028  1.000 37.10722 ? 205 GLN   A CA   1 
ATOM   1570 C  C    . GLN   A 1 205 ? -11.35575 -27.73392 16.99003  1.000 35.00765 ? 205 GLN   A C    1 
ATOM   1571 O  O    . GLN   A 1 205 ? -11.38112 -26.49876 16.97644  1.000 37.58229 ? 205 GLN   A O    1 
ATOM   1572 C  CB   . GLN   A 1 205 ? -8.97576  -28.38895 16.57943  1.000 37.55463 ? 205 GLN   A CB   1 
ATOM   1573 C  CG   . GLN   A 1 205 ? -8.68763  -29.32734 17.74368  1.000 47.71011 ? 205 GLN   A CG   1 
ATOM   1574 C  CD   . GLN   A 1 205 ? -7.26148  -29.23227 18.24481  1.000 54.65792 ? 205 GLN   A CD   1 
ATOM   1575 O  OE1  . GLN   A 1 205 ? -6.34850  -29.82423 17.66973  1.000 63.91961 ? 205 GLN   A OE1  1 
ATOM   1576 N  NE2  . GLN   A 1 205 ? -7.06414  -28.49336 19.33071  1.000 53.33183 ? 205 GLN   A NE2  1 
ATOM   1577 N  N    . ALA   A 1 206 ? -12.12817 -28.47449 17.77904  1.000 32.88055 ? 206 ALA   A N    1 
ATOM   1578 C  CA   . ALA   A 1 206 ? -13.03332 -27.89227 18.75689  1.000 36.54939 ? 206 ALA   A CA   1 
ATOM   1579 C  C    . ALA   A 1 206 ? -13.09469 -28.82485 19.95478  1.000 38.28054 ? 206 ALA   A C    1 
ATOM   1580 O  O    . ALA   A 1 206 ? -13.12216 -30.04760 19.79032  1.000 38.36052 ? 206 ALA   A O    1 
ATOM   1581 C  CB   . ALA   A 1 206 ? -14.43376 -27.67157 18.17371  1.000 31.48517 ? 206 ALA   A CB   1 
ATOM   1582 N  N    . ASN   A 1 207 ? -13.10547 -28.24024 21.15424  1.000 38.17672 ? 207 ASN   A N    1 
ATOM   1583 C  CA   . ASN   A 1 207 ? -13.09701 -29.00460 22.40189  1.000 39.91507 ? 207 ASN   A CA   1 
ATOM   1584 C  C    . ASN   A 1 207 ? -11.88048 -29.92604 22.47238  1.000 41.70391 ? 207 ASN   A C    1 
ATOM   1585 O  O    . ASN   A 1 207 ? -11.95794 -31.05415 22.96265  1.000 41.81087 ? 207 ASN   A O    1 
ATOM   1586 C  CB   . ASN   A 1 207 ? -14.39709 -29.79450 22.57525  1.000 41.55577 ? 207 ASN   A CB   1 
ATOM   1587 C  CG   . ASN   A 1 207 ? -15.62346 -28.98010 22.21408  1.000 36.93770 ? 207 ASN   A CG   1 
ATOM   1588 O  OD1  . ASN   A 1 207 ? -15.90030 -27.95124 22.82885  1.000 36.90142 ? 207 ASN   A OD1  1 
ATOM   1589 N  ND2  . ASN   A 1 207 ? -16.36113 -29.43286 21.20683  1.000 33.47621 ? 207 ASN   A ND2  1 
ATOM   1590 N  N    . GLY   A 1 208 ? -10.74789 -29.44096 21.96674  1.000 39.69007 ? 208 GLY   A N    1 
ATOM   1591 C  CA   . GLY   A 1 208 ? -9.51329  -30.20203 22.00636  1.000 42.00035 ? 208 GLY   A CA   1 
ATOM   1592 C  C    . GLY   A 1 208 ? -9.51426  -31.46722 21.18053  1.000 44.13199 ? 208 GLY   A C    1 
ATOM   1593 O  O    . GLY   A 1 208 ? -8.67376  -32.34107 21.40449  1.000 44.53909 ? 208 GLY   A O    1 
ATOM   1594 N  N    . GLN   A 1 209 ? -10.42664 -31.59002 20.22620  1.000 39.38604 ? 209 GLN   A N    1 
ATOM   1595 C  CA   . GLN   A 1 209 ? -10.57976 -32.78687 19.41597  1.000 41.85583 ? 209 GLN   A CA   1 
ATOM   1596 C  C    . GLN   A 1 209 ? -10.90542 -32.37470 17.98929  1.000 40.93350 ? 209 GLN   A C    1 
ATOM   1597 O  O    . GLN   A 1 209 ? -11.38896 -31.26154 17.75484  1.000 38.57135 ? 209 GLN   A O    1 
ATOM   1598 C  CB   . GLN   A 1 209 ? -11.68689 -33.69786 19.96735  1.000 43.55475 ? 209 GLN   A CB   1 
ATOM   1599 C  CG   . GLN   A 1 209 ? -11.34000 -34.39035 21.28110  1.000 46.01483 ? 209 GLN   A CG   1 
ATOM   1600 C  CD   . GLN   A 1 209 ? -10.11983 -35.28620 21.17191  1.000 53.28910 ? 209 GLN   A CD   1 
ATOM   1601 O  OE1  . GLN   A 1 209 ? -9.11746  -35.07738 21.85542  1.000 61.74089 ? 209 GLN   A OE1  1 
ATOM   1602 N  NE2  . GLN   A 1 209 ? -10.20049 -36.29266 20.30932  1.000 57.51611 ? 209 GLN   A NE2  1 
ATOM   1603 N  N    . PRO   A 1 210 ? -10.63900 -33.24344 17.01328  1.000 38.62907 ? 210 PRO   A N    1 
ATOM   1604 C  CA   . PRO   A 1 210 ? -11.03188 -32.93416 15.63317  1.000 35.83206 ? 210 PRO   A CA   1 
ATOM   1605 C  C    . PRO   A 1 210 ? -12.53382 -32.71882 15.52164  1.000 33.10413 ? 210 PRO   A C    1 
ATOM   1606 O  O    . PRO   A 1 210 ? -13.32876 -33.38249 16.19079  1.000 31.00489 ? 210 PRO   A O    1 
ATOM   1607 C  CB   . PRO   A 1 210 ? -10.57764 -34.17037 14.84813  1.000 40.56484 ? 210 PRO   A CB   1 
ATOM   1608 C  CG   . PRO   A 1 210 ? -9.48963  -34.76857 15.68325  1.000 38.84880 ? 210 PRO   A CG   1 
ATOM   1609 C  CD   . PRO   A 1 210 ? -9.88621  -34.50705 17.10340  1.000 39.64812 ? 210 PRO   A CD   1 
ATOM   1610 N  N    . ALA   A 1 211 ? -12.91395 -31.76740 14.67204  1.000 29.56648 ? 211 ALA   A N    1 
ATOM   1611 C  CA   . ALA   A 1 211 ? -14.31067 -31.43533 14.44096  1.000 30.02395 ? 211 ALA   A CA   1 
ATOM   1612 C  C    . ALA   A 1 211 ? -14.50301 -31.12863 12.96327  1.000 30.13509 ? 211 ALA   A C    1 
ATOM   1613 O  O    . ALA   A 1 211 ? -13.54397 -30.85128 12.23835  1.000 26.61215 ? 211 ALA   A O    1 
ATOM   1614 C  CB   . ALA   A 1 211 ? -14.75977 -30.24734 15.30210  1.000 24.89908 ? 211 ALA   A CB   1 
ATOM   1615 N  N    . TRP   A 1 212 ? -15.75871 -31.17886 12.51827  1.000 25.10773 ? 212 TRP   A N    1 
ATOM   1616 C  CA   . TRP   A 1 212 ? -16.06703 -31.02162 11.10404  1.000 25.67226 ? 212 TRP   A CA   1 
ATOM   1617 C  C    . TRP   A 1 212 ? -17.27685 -30.12069 10.91026  1.000 27.18167 ? 212 TRP   A C    1 
ATOM   1618 O  O    . TRP   A 1 212 ? -18.27161 -30.22909 11.63362  1.000 26.19171 ? 212 TRP   A O    1 
ATOM   1619 C  CB   . TRP   A 1 212 ? -16.31786 -32.37743 10.43379  1.000 27.56813 ? 212 TRP   A CB   1 
ATOM   1620 C  CG   . TRP   A 1 212 ? -15.11118 -33.25801 10.44875  1.000 31.30250 ? 212 TRP   A CG   1 
ATOM   1621 C  CD1  . TRP   A 1 212 ? -14.14233 -33.34051 9.49110   1.000 31.90979 ? 212 TRP   A CD1  1 
ATOM   1622 C  CD2  . TRP   A 1 212 ? -14.73229 -34.17045 11.48415  1.000 30.20660 ? 212 TRP   A CD2  1 
ATOM   1623 N  NE1  . TRP   A 1 212 ? -13.18610 -34.25427 9.86464   1.000 34.62370 ? 212 TRP   A NE1  1 
ATOM   1624 C  CE2  . TRP   A 1 212 ? -13.52588 -34.77741 11.08494  1.000 32.61152 ? 212 TRP   A CE2  1 
ATOM   1625 C  CE3  . TRP   A 1 212 ? -15.29841 -34.53579 12.70936  1.000 33.70631 ? 212 TRP   A CE3  1 
ATOM   1626 C  CZ2  . TRP   A 1 212 ? -12.87643 -35.73068 11.86667  1.000 39.65056 ? 212 TRP   A CZ2  1 
ATOM   1627 C  CZ3  . TRP   A 1 212 ? -14.65048 -35.48231 13.48474  1.000 36.84458 ? 212 TRP   A CZ3  1 
ATOM   1628 C  CH2  . TRP   A 1 212 ? -13.45249 -36.06798 13.06063  1.000 38.04745 ? 212 TRP   A CH2  1 
ATOM   1629 N  N    . ARG   A 1 213 ? -17.17902 -29.23776 9.91825   1.000 23.58779 ? 213 ARG   A N    1 
ATOM   1630 C  CA   . ARG   A 1 213 ? -18.25821 -28.34054 9.52084   1.000 24.35745 ? 213 ARG   A CA   1 
ATOM   1631 C  C    . ARG   A 1 213 ? -18.69303 -28.72597 8.11254   1.000 22.83002 ? 213 ARG   A C    1 
ATOM   1632 O  O    . ARG   A 1 213 ? -17.92732 -28.56614 7.15525   1.000 22.73094 ? 213 ARG   A O    1 
ATOM   1633 C  CB   . ARG   A 1 213 ? -17.80857 -26.88238 9.57674   1.000 23.32894 ? 213 ARG   A CB   1 
ATOM   1634 C  CG   . ARG   A 1 213 ? -18.87455 -25.89368 9.13078   1.000 22.93216 ? 213 ARG   A CG   1 
ATOM   1635 C  CD   . ARG   A 1 213 ? -18.47163 -24.46139 9.43736   1.000 19.84436 ? 213 ARG   A CD   1 
ATOM   1636 N  NE   . ARG   A 1 213 ? -17.25322 -24.06267 8.74143   1.000 24.76654 ? 213 ARG   A NE   1 
ATOM   1637 C  CZ   . ARG   A 1 213 ? -17.22915 -23.50338 7.53917   1.000 27.56677 ? 213 ARG   A CZ   1 
ATOM   1638 N  NH1  . ARG   A 1 213 ? -18.34093 -23.28627 6.85545   1.000 22.99518 ? 213 ARG   A NH1  1 
ATOM   1639 N  NH2  . ARG   A 1 213 ? -16.06112 -23.14962 7.01061   1.000 27.74660 ? 213 ARG   A NH2  1 
ATOM   1640 N  N    . VAL   A 1 214 ? -19.91673 -29.23328 7.99015   1.000 21.48444 ? 214 VAL   A N    1 
ATOM   1641 C  CA   . VAL   A 1 214 ? -20.46462 -29.68811 6.71748   1.000 21.85663 ? 214 VAL   A CA   1 
ATOM   1642 C  C    . VAL   A 1 214 ? -21.40802 -28.61731 6.19188   1.000 22.65053 ? 214 VAL   A C    1 
ATOM   1643 O  O    . VAL   A 1 214 ? -22.30388 -28.15930 6.91242   1.000 23.53702 ? 214 VAL   A O    1 
ATOM   1644 C  CB   . VAL   A 1 214 ? -21.18951 -31.03563 6.87188   1.000 25.43265 ? 214 VAL   A CB   1 
ATOM   1645 C  CG1  . VAL   A 1 214 ? -21.66484 -31.53611 5.51476   1.000 20.17067 ? 214 VAL   A CG1  1 
ATOM   1646 C  CG2  . VAL   A 1 214 ? -20.27546 -32.05773 7.54261   1.000 23.66072 ? 214 VAL   A CG2  1 
ATOM   1647 N  N    . VAL   A 1 215 ? -21.21253 -28.21894 4.93837   1.000 20.71845 ? 215 VAL   A N    1 
ATOM   1648 C  CA   . VAL   A 1 215 ? -21.95112 -27.11588 4.33677   1.000 21.63179 ? 215 VAL   A CA   1 
ATOM   1649 C  C    . VAL   A 1 215 ? -22.80587 -27.66039 3.20224   1.000 23.86238 ? 215 VAL   A C    1 
ATOM   1650 O  O    . VAL   A 1 215 ? -22.31606 -28.41327 2.35191   1.000 19.41527 ? 215 VAL   A O    1 
ATOM   1651 C  CB   . VAL   A 1 215 ? -21.00935 -26.00763 3.83068   1.000 23.57106 ? 215 VAL   A CB   1 
ATOM   1652 C  CG1  . VAL   A 1 215 ? -21.81299 -24.78730 3.39823   1.000 21.29355 ? 215 VAL   A CG1  1 
ATOM   1653 C  CG2  . VAL   A 1 215 ? -19.99623 -25.63168 4.91007   1.000 21.45289 ? 215 VAL   A CG2  1 
ATOM   1654 N  N    . LEU   A 1 216 ? -24.07905 -27.27948 3.19473   1.000 20.98266 ? 216 LEU   A N    1 
ATOM   1655 C  CA   . LEU   A 1 216 ? -24.99634 -27.67812 2.14201   1.000 20.70321 ? 216 LEU   A CA   1 
ATOM   1656 C  C    . LEU   A 1 216 ? -24.84933 -26.76882 0.92603   1.000 23.35527 ? 216 LEU   A C    1 
ATOM   1657 O  O    . LEU   A 1 216 ? -24.32910 -25.65261 1.00662   1.000 20.38256 ? 216 LEU   A O    1 
ATOM   1658 C  CB   . LEU   A 1 216 ? -26.43852 -27.63947 2.64722   1.000 19.68824 ? 216 LEU   A CB   1 
ATOM   1659 C  CG   . LEU   A 1 216 ? -26.86571 -28.76351 3.58976   1.000 21.77823 ? 216 LEU   A CG   1 
ATOM   1660 C  CD1  . LEU   A 1 216 ? -27.96809 -28.28614 4.52417   1.000 19.76842 ? 216 LEU   A CD1  1 
ATOM   1661 C  CD2  . LEU   A 1 216 ? -27.33091 -29.96139 2.77838   1.000 21.99201 ? 216 LEU   A CD2  1 
ATOM   1662 N  N    . GLY   A 1 217 ? -25.32534 -27.26125 -0.21181  1.000 23.91829 ? 217 GLY   A N    1 
ATOM   1663 C  CA   . GLY   A 1 217 ? -25.33549 -26.49499 -1.44016  1.000 21.74833 ? 217 GLY   A CA   1 
ATOM   1664 C  C    . GLY   A 1 217 ? -26.70820 -25.91325 -1.72352  1.000 25.67409 ? 217 GLY   A C    1 
ATOM   1665 O  O    . GLY   A 1 217 ? -27.72583 -26.43134 -1.26890  1.000 21.86856 ? 217 GLY   A O    1 
ATOM   1666 N  N    . ALA   A 1 218 ? -26.72406 -24.81535 -2.47192  1.000 23.07079 ? 218 ALA   A N    1 
ATOM   1667 C  CA   . ALA   A 1 218 ? -27.97769 -24.24183 -2.93064  1.000 25.05682 ? 218 ALA   A CA   1 
ATOM   1668 C  C    . ALA   A 1 218 ? -28.48849 -25.01164 -4.14123  1.000 27.54358 ? 218 ALA   A C    1 
ATOM   1669 O  O    . ALA   A 1 218 ? -27.71624 -25.61857 -4.88884  1.000 28.13854 ? 218 ALA   A O    1 
ATOM   1670 C  CB   . ALA   A 1 218 ? -27.80341 -22.76342 -3.28219  1.000 23.37151 ? 218 ALA   A CB   1 
ATOM   1671 N  N    . TRP   A 1 219 ? -29.80838 -24.98688 -4.32877  1.000 20.85377 ? 219 TRP   A N    1 
ATOM   1672 C  CA   . TRP   A 1 219 ? -30.43692 -25.68318 -5.45151  1.000 26.71288 ? 219 TRP   A CA   1 
ATOM   1673 C  C    . TRP   A 1 219 ? -30.45217 -24.73900 -6.65106  1.000 31.62056 ? 219 TRP   A C    1 
ATOM   1674 O  O    . TRP   A 1 219 ? -31.46814 -24.13836 -7.00492  1.000 31.29148 ? 219 TRP   A O    1 
ATOM   1675 C  CB   . TRP   A 1 219 ? -31.83789 -26.15671 -5.08009  1.000 23.88676 ? 219 TRP   A CB   1 
ATOM   1676 C  CG   . TRP   A 1 219 ? -31.86873 -27.24092 -4.03390  1.000 20.34259 ? 219 TRP   A CG   1 
ATOM   1677 C  CD1  . TRP   A 1 219 ? -31.10404 -27.31765 -2.90495  1.000 22.19335 ? 219 TRP   A CD1  1 
ATOM   1678 C  CD2  . TRP   A 1 219 ? -32.70800 -28.40265 -4.02748  1.000 20.46585 ? 219 TRP   A CD2  1 
ATOM   1679 N  NE1  . TRP   A 1 219 ? -31.41689 -28.45216 -2.19619  1.000 22.36007 ? 219 TRP   A NE1  1 
ATOM   1680 C  CE2  . TRP   A 1 219 ? -32.39840 -29.13595 -2.86410  1.000 22.59736 ? 219 TRP   A CE2  1 
ATOM   1681 C  CE3  . TRP   A 1 219 ? -33.69155 -28.89288 -4.89174  1.000 22.56304 ? 219 TRP   A CE3  1 
ATOM   1682 C  CZ2  . TRP   A 1 219 ? -33.03646 -30.33260 -2.54381  1.000 20.12625 ? 219 TRP   A CZ2  1 
ATOM   1683 C  CZ3  . TRP   A 1 219 ? -34.32490 -30.08233 -4.57169  1.000 25.91537 ? 219 TRP   A CZ3  1 
ATOM   1684 C  CH2  . TRP   A 1 219 ? -33.99483 -30.78764 -3.40811  1.000 20.48861 ? 219 TRP   A CH2  1 
ATOM   1685 N  N    . HIS   A 1 220 ? -29.28761 -24.60727 -7.28540  1.000 33.69852 ? 220 HIS   A N    1 
ATOM   1686 C  CA   . HIS   A 1 220 ? -29.13671 -23.71092 -8.43950  1.000 37.65869 ? 220 HIS   A CA   1 
ATOM   1687 C  C    . HIS   A 1 220 ? -29.40114 -24.47812 -9.73218  1.000 42.01208 ? 220 HIS   A C    1 
ATOM   1688 O  O    . HIS   A 1 220 ? -30.38657 -24.21759 -10.43087 1.000 44.75437 ? 220 HIS   A O    1 
ATOM   1689 C  CB   . HIS   A 1 220 ? -27.74572 -23.07284 -8.43222  1.000 34.93401 ? 220 HIS   A CB   1 
ATOM   1690 C  CG   . HIS   A 1 220 ? -27.52680 -22.08805 -9.53805  1.000 47.83802 ? 220 HIS   A CG   1 
ATOM   1691 N  ND1  . HIS   A 1 220 ? -26.52987 -22.23515 -10.47825 1.000 45.84902 ? 220 HIS   A ND1  1 
ATOM   1692 C  CD2  . HIS   A 1 220 ? -28.17621 -20.94270 -9.85444  1.000 46.01631 ? 220 HIS   A CD2  1 
ATOM   1693 C  CE1  . HIS   A 1 220 ? -26.57457 -21.22325 -11.32636 1.000 49.70824 ? 220 HIS   A CE1  1 
ATOM   1694 N  NE2  . HIS   A 1 220 ? -27.56462 -20.42474 -10.97024 1.000 49.40957 ? 220 HIS   A NE2  1 
ATOM   1695 N  N    A SER   A 1 221 ? -28.51992 -25.42002 -10.06409 0.700 39.89844 ? 221 SER   A N    1 
ATOM   1696 N  N    B SER   A 1 221 ? -28.52864 -25.42809 -10.05580 0.300 39.86244 ? 221 SER   A N    1 
ATOM   1697 C  CA   A SER   A 1 221 ? -28.69648 -26.28646 -11.22166 0.700 39.36671 ? 221 SER   A CA   1 
ATOM   1698 C  CA   B SER   A 1 221 ? -28.69559 -26.28415 -11.22161 0.300 39.35985 ? 221 SER   A CA   1 
ATOM   1699 C  C    A SER   A 1 221 ? -29.04505 -27.71819 -10.85305 0.700 37.30997 ? 221 SER   A C    1 
ATOM   1700 C  C    B SER   A 1 221 ? -29.01672 -27.72750 -10.86980 0.300 37.34634 ? 221 SER   A C    1 
ATOM   1701 O  O    A SER   A 1 221 ? -29.77986 -28.37280 -11.59496 0.700 39.70299 ? 221 SER   A O    1 
ATOM   1702 O  O    B SER   A 1 221 ? -29.71018 -28.39738 -11.63803 0.300 39.61121 ? 221 SER   A O    1 
ATOM   1703 C  CB   A SER   A 1 221 ? -27.42735 -26.29394 -12.08367 0.700 40.07952 ? 221 SER   A CB   1 
ATOM   1704 C  CB   B SER   A 1 221 ? -27.43161 -26.24769 -12.08936 0.300 40.07269 ? 221 SER   A CB   1 
ATOM   1705 O  OG   A SER   A 1 221 ? -26.79155 -25.02697 -12.07074 0.700 36.70522 ? 221 SER   A OG   1 
ATOM   1706 O  OG   B SER   A 1 221 ? -26.30349 -26.66808 -11.34513 0.300 38.03519 ? 221 SER   A OG   1 
ATOM   1707 N  N    . GLU   A 1 222 ? -28.53904 -28.21471 -9.72780  1.000 36.95552 ? 222 GLU   A N    1 
ATOM   1708 C  CA   . GLU   A 1 222 ? -28.83601 -29.55288 -9.24498  1.000 35.18503 ? 222 GLU   A CA   1 
ATOM   1709 C  C    . GLU   A 1 222 ? -29.21595 -29.47302 -7.77353  1.000 31.54731 ? 222 GLU   A C    1 
ATOM   1710 O  O    . GLU   A 1 222 ? -29.05844 -28.43704 -7.12178  1.000 33.49685 ? 222 GLU   A O    1 
ATOM   1711 C  CB   . GLU   A 1 222 ? -27.64167 -30.50024 -9.43008  1.000 35.48476 ? 222 GLU   A CB   1 
ATOM   1712 C  CG   . GLU   A 1 222 ? -27.48422 -31.05893 -10.83185 1.000 39.88103 ? 222 GLU   A CG   1 
ATOM   1713 C  CD   . GLU   A 1 222 ? -26.71205 -32.36455 -10.84352 1.000 46.39740 ? 222 GLU   A CD   1 
ATOM   1714 O  OE1  . GLU   A 1 222 ? -26.06883 -32.68408 -9.82050  1.000 40.55024 ? 222 GLU   A OE1  1 
ATOM   1715 O  OE2  . GLU   A 1 222 ? -26.74438 -33.06909 -11.87357 1.000 48.67120 ? 222 GLU   A OE2  1 
ATOM   1716 N  N    . GLY   A 1 223 ? -29.72108 -30.58489 -7.25060  1.000 23.62727 ? 223 GLY   A N    1 
ATOM   1717 C  CA   . GLY   A 1 223 ? -30.05098 -30.66196 -5.84736  1.000 20.99010 ? 223 GLY   A CA   1 
ATOM   1718 C  C    . GLY   A 1 223 ? -28.85510 -31.02618 -4.98648  1.000 25.65427 ? 223 GLY   A C    1 
ATOM   1719 O  O    . GLY   A 1 223 ? -27.83661 -31.51993 -5.46756  1.000 24.06179 ? 223 GLY   A O    1 
ATOM   1720 N  N    . SER   A 1 224 ? -28.99495 -30.77414 -3.68826  1.000 20.00455 ? 224 SER   A N    1 
ATOM   1721 C  CA   . SER   A 1 224 ? -27.94361 -31.07198 -2.72895  1.000 25.05321 ? 224 SER   A CA   1 
ATOM   1722 C  C    . SER   A 1 224 ? -28.58414 -31.48231 -1.41344  1.000 22.64691 ? 224 SER   A C    1 
ATOM   1723 O  O    . SER   A 1 224 ? -29.59670 -30.90742 -1.00595  1.000 23.05039 ? 224 SER   A O    1 
ATOM   1724 C  CB   . SER   A 1 224 ? -27.02361 -29.86244 -2.51879  1.000 23.72215 ? 224 SER   A CB   1 
ATOM   1725 O  OG   . SER   A 1 224 ? -26.06703 -30.11702 -1.50567  1.000 33.23925 ? 224 SER   A OG   1 
ATOM   1726 N  N    . MET   A 1 225 ? -27.99713 -32.48234 -0.75943  1.000 21.59814 ? 225 MET   A N    1 
ATOM   1727 C  CA   . MET   A 1 225 ? -28.43832 -32.87132 0.57128   1.000 17.03641 ? 225 MET   A CA   1 
ATOM   1728 C  C    . MET   A 1 225 ? -27.25643 -33.43176 1.34505   1.000 21.73936 ? 225 MET   A C    1 
ATOM   1729 O  O    . MET   A 1 225 ? -26.24673 -33.84535 0.76753   1.000 22.18112 ? 225 MET   A O    1 
ATOM   1730 C  CB   . MET   A 1 225 ? -29.55667 -33.92217 0.53844   1.000 18.79110 ? 225 MET   A CB   1 
ATOM   1731 C  CG   . MET   A 1 225 ? -29.10888 -35.28837 0.02441   1.000 20.30718 ? 225 MET   A CG   1 
ATOM   1732 S  SD   . MET   A 1 225 ? -30.42955 -36.51646 0.02751   1.000 26.14493 ? 225 MET   A SD   1 
ATOM   1733 C  CE   . MET   A 1 225 ? -30.42051 -37.05858 -1.68100  1.000 35.97399 ? 225 MET   A CE   1 
ATOM   1734 N  N    . VAL   A 1 226 ? -27.40143 -33.44901 2.66684   1.000 20.20004 ? 226 VAL   A N    1 
ATOM   1735 C  CA   . VAL   A 1 226 ? -26.50493 -34.17745 3.55505   1.000 20.41309 ? 226 VAL   A CA   1 
ATOM   1736 C  C    . VAL   A 1 226 ? -27.28425 -35.33806 4.15300   1.000 20.26260 ? 226 VAL   A C    1 
ATOM   1737 O  O    . VAL   A 1 226 ? -28.38725 -35.14782 4.68082   1.000 20.99269 ? 226 VAL   A O    1 
ATOM   1738 C  CB   . VAL   A 1 226 ? -25.92474 -33.27329 4.65600   1.000 22.48854 ? 226 VAL   A CB   1 
ATOM   1739 C  CG1  . VAL   A 1 226 ? -25.26165 -34.11801 5.73696   1.000 20.01164 ? 226 VAL   A CG1  1 
ATOM   1740 C  CG2  . VAL   A 1 226 ? -24.91996 -32.29949 4.06215   1.000 17.68524 ? 226 VAL   A CG2  1 
ATOM   1741 N  N    . LYS   A 1 227 ? -26.72340 -36.53888 4.05128   1.000 20.27315 ? 227 LYS   A N    1 
ATOM   1742 C  CA   . LYS   A 1 227 ? -27.32564 -37.74319 4.60532   1.000 18.59002 ? 227 LYS   A CA   1 
ATOM   1743 C  C    . LYS   A 1 227 ? -26.42480 -38.26063 5.71760   1.000 24.91517 ? 227 LYS   A C    1 
ATOM   1744 O  O    . LYS   A 1 227 ? -25.23956 -38.52573 5.48810   1.000 26.04754 ? 227 LYS   A O    1 
ATOM   1745 C  CB   . LYS   A 1 227 ? -27.52324 -38.80826 3.52648   1.000 18.25924 ? 227 LYS   A CB   1 
ATOM   1746 C  CG   . LYS   A 1 227 ? -28.04078 -40.13616 4.05400   1.000 22.50997 ? 227 LYS   A CG   1 
ATOM   1747 C  CD   . LYS   A 1 227 ? -28.85457 -40.87037 2.99864   1.000 34.66430 ? 227 LYS   A CD   1 
ATOM   1748 C  CE   . LYS   A 1 227 ? -28.25271 -42.22345 2.67567   1.000 40.17872 ? 227 LYS   A CE   1 
ATOM   1749 N  NZ   . LYS   A 1 227 ? -29.18323 -43.07532 1.88278   1.000 37.38420 ? 227 LYS   A NZ   1 
ATOM   1750 N  N    . VAL   A 1 228 ? -26.98136 -38.38931 6.91876   1.000 26.20107 ? 228 VAL   A N    1 
ATOM   1751 C  CA   . VAL   A 1 228 ? -26.25368 -38.88226 8.08192   1.000 23.97454 ? 228 VAL   A CA   1 
ATOM   1752 C  C    . VAL   A 1 228 ? -26.75734 -40.28012 8.40513   1.000 24.78204 ? 228 VAL   A C    1 
ATOM   1753 O  O    . VAL   A 1 228 ? -27.96555 -40.49104 8.56755   1.000 21.15414 ? 228 VAL   A O    1 
ATOM   1754 C  CB   . VAL   A 1 228 ? -26.41367 -37.94671 9.29303   1.000 24.33837 ? 228 VAL   A CB   1 
ATOM   1755 C  CG1  . VAL   A 1 228 ? -25.66616 -38.50694 10.49642  1.000 22.86985 ? 228 VAL   A CG1  1 
ATOM   1756 C  CG2  . VAL   A 1 228 ? -25.91717 -36.54867 8.95417   1.000 16.84209 ? 228 VAL   A CG2  1 
ATOM   1757 N  N    . THR   A 1 229 ? -25.83186 -41.23201 8.49165   1.000 22.87069 ? 229 THR   A N    1 
ATOM   1758 C  CA   . THR   A 1 229 ? -26.14464 -42.60634 8.85636   1.000 22.56475 ? 229 THR   A CA   1 
ATOM   1759 C  C    . THR   A 1 229 ? -25.39300 -42.94316 10.13903  1.000 25.18494 ? 229 THR   A C    1 
ATOM   1760 O  O    . THR   A 1 229 ? -24.56451 -42.14343 10.59267  1.000 23.96100 ? 229 THR   A O    1 
ATOM   1761 C  CB   . THR   A 1 229 ? -25.75621 -43.57179 7.73148   1.000 28.16368 ? 229 THR   A CB   1 
ATOM   1762 O  OG1  . THR   A 1 229 ? -24.32823 -43.69498 7.67982   1.000 26.55189 ? 229 THR   A OG1  1 
ATOM   1763 C  CG2  . THR   A 1 229 ? -26.27781 -43.07379 6.38350   1.000 26.76234 ? 229 THR   A CG2  1 
ATOM   1764 N  N    . PRO   A 1 230 ? -25.65360 -44.09345 10.76569  1.000 27.12282 ? 230 PRO   A N    1 
ATOM   1765 C  CA   . PRO   A 1 230 ? -24.78740 -44.51965 11.87597  1.000 32.99220 ? 230 PRO   A CA   1 
ATOM   1766 C  C    . PRO   A 1 230 ? -23.33256 -44.69418 11.47403  1.000 31.65423 ? 230 PRO   A C    1 
ATOM   1767 O  O    . PRO   A 1 230 ? -22.46049 -44.68564 12.35128  1.000 33.12816 ? 230 PRO   A O    1 
ATOM   1768 C  CB   . PRO   A 1 230 ? -25.40758 -45.85356 12.32450  1.000 34.93588 ? 230 PRO   A CB   1 
ATOM   1769 C  CG   . PRO   A 1 230 ? -26.41889 -46.21498 11.27169  1.000 33.35785 ? 230 PRO   A CG   1 
ATOM   1770 C  CD   . PRO   A 1 230 ? -26.85857 -44.93247 10.66070  1.000 28.65636 ? 230 PRO   A CD   1 
ATOM   1771 N  N    . ASP   A 1 231 ? -23.03835 -44.82892 10.17765  1.000 29.43387 ? 231 ASP   A N    1 
ATOM   1772 C  CA   . ASP   A 1 231 ? -21.70083 -45.17963 9.72441   1.000 30.73081 ? 231 ASP   A CA   1 
ATOM   1773 C  C    . ASP   A 1 231 ? -20.91986 -44.03814 9.08738   1.000 28.24968 ? 231 ASP   A C    1 
ATOM   1774 O  O    . ASP   A 1 231 ? -19.68623 -44.09705 9.08203   1.000 31.44157 ? 231 ASP   A O    1 
ATOM   1775 C  CB   . ASP   A 1 231 ? -21.76677 -46.34248 8.72220   1.000 29.87353 ? 231 ASP   A CB   1 
ATOM   1776 C  CG   . ASP   A 1 231 ? -22.28820 -47.62152 9.34705   1.000 39.74871 ? 231 ASP   A CG   1 
ATOM   1777 O  OD1  . ASP   A 1 231 ? -22.05430 -47.82919 10.55613  1.000 43.22871 ? 231 ASP   A OD1  1 
ATOM   1778 O  OD2  . ASP   A 1 231 ? -22.92724 -48.42076 8.63084   1.000 52.71984 ? 231 ASP   A OD2  1 
ATOM   1779 N  N    . ASP   A 1 232 ? -21.58044 -43.01448 8.54977   1.000 26.86832 ? 232 ASP   A N    1 
ATOM   1780 C  CA   . ASP   A 1 232 ? -20.85377 -41.97556 7.82854   1.000 23.55329 ? 232 ASP   A CA   1 
ATOM   1781 C  C    . ASP   A 1 232 ? -21.71428 -40.72236 7.70836   1.000 25.75374 ? 232 ASP   A C    1 
ATOM   1782 O  O    . ASP   A 1 232 ? -22.86331 -40.67834 8.15751   1.000 26.83444 ? 232 ASP   A O    1 
ATOM   1783 C  CB   . ASP   A 1 232 ? -20.40829 -42.47389 6.44761   1.000 24.84248 ? 232 ASP   A CB   1 
ATOM   1784 C  CG   . ASP   A 1 232 ? -21.54736 -43.07385 5.63920   1.000 28.23432 ? 232 ASP   A CG   1 
ATOM   1785 O  OD1  . ASP   A 1 232 ? -22.66220 -42.50917 5.64361   1.000 28.28193 ? 232 ASP   A OD1  1 
ATOM   1786 O  OD2  . ASP   A 1 232 ? -21.32017 -44.11080 4.98348   1.000 37.77891 ? 232 ASP   A OD2  1 
ATOM   1787 N  N    . VAL   A 1 233 ? -21.12784 -39.69470 7.09662   1.000 21.94208 ? 233 VAL   A N    1 
ATOM   1788 C  CA   . VAL   A 1 233 ? -21.80616 -38.45316 6.74026   1.000 21.71642 ? 233 VAL   A CA   1 
ATOM   1789 C  C    . VAL   A 1 233 ? -21.56219 -38.21281 5.25775   1.000 25.90930 ? 233 VAL   A C    1 
ATOM   1790 O  O    . VAL   A 1 233 ? -20.41210 -38.23600 4.80441   1.000 25.67605 ? 233 VAL   A O    1 
ATOM   1791 C  CB   . VAL   A 1 233 ? -21.30198 -37.25770 7.57298   1.000 23.75491 ? 233 VAL   A CB   1 
ATOM   1792 C  CG1  . VAL   A 1 233 ? -22.02837 -35.97219 7.17231   1.000 22.74892 ? 233 VAL   A CG1  1 
ATOM   1793 C  CG2  . VAL   A 1 233 ? -21.47273 -37.53274 9.05945   1.000 26.75205 ? 233 VAL   A CG2  1 
ATOM   1794 N  N    . GLU   A 1 234 ? -22.63619 -37.98015 4.50673   1.000 23.76367 ? 234 GLU   A N    1 
ATOM   1795 C  CA   . GLU   A 1 234 ? -22.58655 -37.95574 3.05088   1.000 21.65696 ? 234 GLU   A CA   1 
ATOM   1796 C  C    . GLU   A 1 234 ? -23.10368 -36.62551 2.52074   1.000 23.10447 ? 234 GLU   A C    1 
ATOM   1797 O  O    . GLU   A 1 234 ? -24.22489 -36.21847 2.83962   1.000 25.28641 ? 234 GLU   A O    1 
ATOM   1798 C  CB   . GLU   A 1 234 ? -23.40524 -39.11143 2.46634   1.000 20.51522 ? 234 GLU   A CB   1 
ATOM   1799 C  CG   . GLU   A 1 234 ? -23.16615 -40.44294 3.16632   1.000 20.62202 ? 234 GLU   A CG   1 
ATOM   1800 C  CD   . GLU   A 1 234 ? -24.04797 -41.55565 2.63624   1.000 27.66145 ? 234 GLU   A CD   1 
ATOM   1801 O  OE1  . GLU   A 1 234 ? -24.77882 -41.32186 1.65115   1.000 25.94702 ? 234 GLU   A OE1  1 
ATOM   1802 O  OE2  . GLU   A 1 234 ? -24.00991 -42.66693 3.20514   1.000 29.48588 ? 234 GLU   A OE2  1 
ATOM   1803 N  N    . LEU   A 1 235 ? -22.28703 -35.95811 1.70951   1.000 19.76411 ? 235 LEU   A N    1 
ATOM   1804 C  CA   . LEU   A 1 235 ? -22.69957 -34.77560 0.96241   1.000 22.55691 ? 235 LEU   A CA   1 
ATOM   1805 C  C    . LEU   A 1 235 ? -22.99998 -35.21246 -0.46641  1.000 24.53094 ? 235 LEU   A C    1 
ATOM   1806 O  O    . LEU   A 1 235 ? -22.10092 -35.67095 -1.17990  1.000 23.08246 ? 235 LEU   A O    1 
ATOM   1807 C  CB   . LEU   A 1 235 ? -21.61242 -33.70052 0.99711   1.000 20.28181 ? 235 LEU   A CB   1 
ATOM   1808 C  CG   . LEU   A 1 235 ? -21.81072 -32.40664 0.20317   1.000 20.90892 ? 235 LEU   A CG   1 
ATOM   1809 C  CD1  . LEU   A 1 235 ? -23.05096 -31.65810 0.67301   1.000 22.93247 ? 235 LEU   A CD1  1 
ATOM   1810 C  CD2  . LEU   A 1 235 ? -20.56590 -31.52361 0.30775   1.000 21.58649 ? 235 LEU   A CD2  1 
ATOM   1811 N  N    . ILE   A 1 236 ? -24.25847 -35.07815 -0.87861  1.000 21.74603 ? 236 ILE   A N    1 
ATOM   1812 C  CA   . ILE   A 1 236 ? -24.77149 -35.73547 -2.07528  1.000 20.77010 ? 236 ILE   A CA   1 
ATOM   1813 C  C    . ILE   A 1 236 ? -25.35001 -34.68765 -3.01671  1.000 28.83954 ? 236 ILE   A C    1 
ATOM   1814 O  O    . ILE   A 1 236 ? -26.11998 -33.81912 -2.59092  1.000 24.80190 ? 236 ILE   A O    1 
ATOM   1815 C  CB   . ILE   A 1 236 ? -25.83192 -36.79302 -1.71503  1.000 21.75012 ? 236 ILE   A CB   1 
ATOM   1816 C  CG1  . ILE   A 1 236 ? -25.21652 -37.87885 -0.82620  1.000 20.37522 ? 236 ILE   A CG1  1 
ATOM   1817 C  CG2  . ILE   A 1 236 ? -26.44382 -37.40136 -2.97359  1.000 21.24910 ? 236 ILE   A CG2  1 
ATOM   1818 C  CD1  . ILE   A 1 236 ? -26.22349 -38.87208 -0.28252  1.000 26.38778 ? 236 ILE   A CD1  1 
ATOM   1819 N  N    . HIS   A 1 237 ? -24.98584 -34.77741 -4.29480  1.000 22.17667 ? 237 HIS   A N    1 
ATOM   1820 C  CA   . HIS   A 1 237 ? -25.54582 -33.93263 -5.33989  1.000 26.07186 ? 237 HIS   A CA   1 
ATOM   1821 C  C    . HIS   A 1 237 ? -26.27461 -34.79835 -6.35812  1.000 23.53696 ? 237 HIS   A C    1 
ATOM   1822 O  O    . HIS   A 1 237 ? -25.78055 -35.85926 -6.75286  1.000 23.82995 ? 237 HIS   A O    1 
ATOM   1823 C  CB   . HIS   A 1 237 ? -24.45880 -33.10097 -6.02396  1.000 24.74428 ? 237 HIS   A CB   1 
ATOM   1824 C  CG   . HIS   A 1 237 ? -24.08866 -31.86432 -5.26697  1.000 32.22125 ? 237 HIS   A CG   1 
ATOM   1825 N  ND1  . HIS   A 1 237 ? -23.35762 -31.89775 -4.09894  1.000 32.60212 ? 237 HIS   A ND1  1 
ATOM   1826 C  CD2  . HIS   A 1 237 ? -24.36381 -30.55950 -5.50155  1.000 34.16558 ? 237 HIS   A CD2  1 
ATOM   1827 C  CE1  . HIS   A 1 237 ? -23.19120 -30.66606 -3.65117  1.000 32.29996 ? 237 HIS   A CE1  1 
ATOM   1828 N  NE2  . HIS   A 1 237 ? -23.79196 -29.83523 -4.48403  1.000 38.57330 ? 237 HIS   A NE2  1 
ATOM   1829 N  N    . PHE   A 1 238 ? -27.44858 -34.33688 -6.78179  1.000 23.88050 ? 238 PHE   A N    1 
ATOM   1830 C  CA   . PHE   A 1 238 ? -28.35613 -35.12427 -7.60325  1.000 26.87676 ? 238 PHE   A CA   1 
ATOM   1831 C  C    . PHE   A 1 238 ? -29.14542 -34.18458 -8.50120  1.000 27.25505 ? 238 PHE   A C    1 
ATOM   1832 O  O    . PHE   A 1 238 ? -29.35642 -33.02033 -8.14038  1.000 25.51218 ? 238 PHE   A O    1 
ATOM   1833 C  CB   . PHE   A 1 238 ? -29.30946 -35.95463 -6.72856  1.000 26.12813 ? 238 PHE   A CB   1 
ATOM   1834 C  CG   . PHE   A 1 238 ? -30.10487 -35.12892 -5.75313  1.000 26.98934 ? 238 PHE   A CG   1 
ATOM   1835 C  CD1  . PHE   A 1 238 ? -29.60079 -34.84692 -4.49263  1.000 23.29270 ? 238 PHE   A CD1  1 
ATOM   1836 C  CD2  . PHE   A 1 238 ? -31.35192 -34.62983 -6.09741  1.000 26.42346 ? 238 PHE   A CD2  1 
ATOM   1837 C  CE1  . PHE   A 1 238 ? -30.32386 -34.07833 -3.59329  1.000 24.76414 ? 238 PHE   A CE1  1 
ATOM   1838 C  CE2  . PHE   A 1 238 ? -32.08096 -33.86229 -5.20129  1.000 25.49935 ? 238 PHE   A CE2  1 
ATOM   1839 C  CZ   . PHE   A 1 238 ? -31.56569 -33.58806 -3.94744  1.000 23.87833 ? 238 PHE   A CZ   1 
ATOM   1840 N  N    . PRO   A 1 239 ? -29.59213 -34.65133 -9.66562  1.000 27.38251 ? 239 PRO   A N    1 
ATOM   1841 C  CA   . PRO   A 1 239 ? -30.34992 -33.77737 -10.56777 1.000 32.45483 ? 239 PRO   A CA   1 
ATOM   1842 C  C    . PRO   A 1 239 ? -31.77581 -33.55850 -10.08266 1.000 32.17244 ? 239 PRO   A C    1 
ATOM   1843 O  O    . PRO   A 1 239 ? -32.33974 -34.35564 -9.32978  1.000 33.92381 ? 239 PRO   A O    1 
ATOM   1844 C  CB   . PRO   A 1 239 ? -30.32988 -34.53852 -11.89732 1.000 34.02116 ? 239 PRO   A CB   1 
ATOM   1845 C  CG   . PRO   A 1 239 ? -30.19915 -35.97147 -11.49509 1.000 38.71358 ? 239 PRO   A CG   1 
ATOM   1846 C  CD   . PRO   A 1 239 ? -29.33127 -35.97287 -10.26475 1.000 32.29472 ? 239 PRO   A CD   1 
ATOM   1847 N  N    . PHE   A 1 240 ? -32.35657 -32.44252 -10.53618 1.000 34.79045 ? 240 PHE   A N    1 
ATOM   1848 C  CA   . PHE   A 1 240 ? -33.74145 -32.12264 -10.19680 1.000 34.32759 ? 240 PHE   A CA   1 
ATOM   1849 C  C    . PHE   A 1 240 ? -34.69888 -33.18240 -10.72660 1.000 38.44039 ? 240 PHE   A C    1 
ATOM   1850 O  O    . PHE   A 1 240 ? -35.49403 -33.75392 -9.97166  1.000 35.47624 ? 240 PHE   A O    1 
ATOM   1851 C  CB   . PHE   A 1 240 ? -34.12561 -30.75228 -10.76116 1.000 30.75413 ? 240 PHE   A CB   1 
ATOM   1852 C  CG   . PHE   A 1 240 ? -33.46116 -29.59292 -10.07686 1.000 33.65343 ? 240 PHE   A CG   1 
ATOM   1853 C  CD1  . PHE   A 1 240 ? -32.97778 -29.70925 -8.78549  1.000 30.12304 ? 240 PHE   A CD1  1 
ATOM   1854 C  CD2  . PHE   A 1 240 ? -33.33217 -28.37720 -10.72893 1.000 34.30902 ? 240 PHE   A CD2  1 
ATOM   1855 C  CE1  . PHE   A 1 240 ? -32.37280 -28.63648 -8.16055  1.000 30.52780 ? 240 PHE   A CE1  1 
ATOM   1856 C  CE2  . PHE   A 1 240 ? -32.72719 -27.30212 -10.11018 1.000 35.53683 ? 240 PHE   A CE2  1 
ATOM   1857 C  CZ   . PHE   A 1 240 ? -32.24610 -27.43183 -8.82440  1.000 32.33453 ? 240 PHE   A CZ   1 
ATOM   1858 N  N    . LEU   A 1 241 ? -34.64327 -33.44856 -12.02745 1.000 37.63553 ? 241 LEU   A N    1 
ATOM   1859 C  CA   . LEU   A 1 241 ? -35.60844 -34.30018 -12.70266 1.000 47.36531 ? 241 LEU   A CA   1 
ATOM   1860 C  C    . LEU   A 1 241 ? -34.96837 -35.61579 -13.12446 1.000 54.42952 ? 241 LEU   A C    1 
ATOM   1861 O  O    . LEU   A 1 241 ? -33.74312 -35.76085 -13.15264 1.000 49.28346 ? 241 LEU   A O    1 
ATOM   1862 C  CB   . LEU   A 1 241 ? -36.19658 -33.59111 -13.92773 1.000 48.73793 ? 241 LEU   A CB   1 
ATOM   1863 N  N    . GLU   A 1 242 ? -35.82558 -36.57631 -13.46062 1.000 58.59571 ? 242 GLU   A N    1 
ATOM   1864 C  CA   . GLU   A 1 242 ? -35.38957 -37.90700 -13.87750 1.000 67.24837 ? 242 GLU   A CA   1 
ATOM   1865 C  C    . GLU   A 1 242 ? -34.69450 -37.80291 -15.22814 1.000 68.98212 ? 242 GLU   A C    1 
ATOM   1866 O  O    . GLU   A 1 242 ? -35.34247 -37.65866 -16.26698 1.000 71.14949 ? 242 GLU   A O    1 
ATOM   1867 C  CB   . GLU   A 1 242 ? -36.57904 -38.85820 -13.94270 1.000 68.52968 ? 242 GLU   A CB   1 
ATOM   1868 N  N    . GLU   A 1 243 ? -33.36534 -37.87472 -15.21753 1.000 67.23491 ? 243 GLU   A N    1 
ATOM   1869 C  CA   . GLU   A 1 243 ? -32.56968 -37.82108 -16.44291 1.000 71.22271 ? 243 GLU   A CA   1 
ATOM   1870 C  C    . GLU   A 1 243 ? -32.69006 -39.16627 -17.14720 1.000 71.44951 ? 243 GLU   A C    1 
ATOM   1871 O  O    . GLU   A 1 243 ? -31.91937 -40.09567 -16.90137 1.000 69.17195 ? 243 GLU   A O    1 
ATOM   1872 C  CB   . GLU   A 1 243 ? -31.11856 -37.47899 -16.12922 1.000 73.53393 ? 243 GLU   A CB   1 
ATOM   1873 C  CG   . GLU   A 1 243 ? -30.94978 -36.29687 -15.18909 1.000 71.77566 ? 243 GLU   A CG   1 
ATOM   1874 C  CD   . GLU   A 1 243 ? -30.55868 -35.02636 -15.91644 1.000 71.93296 ? 243 GLU   A CD   1 
ATOM   1875 O  OE1  . GLU   A 1 243 ? -31.40205 -34.48069 -16.65880 1.000 69.74542 ? 243 GLU   A OE1  1 
ATOM   1876 O  OE2  . GLU   A 1 243 ? -29.40722 -34.57363 -15.74587 1.000 75.47059 ? 243 GLU   A OE2  1 
ATOM   1877 N  N    . ASN   A 1 244 ? -33.67730 -39.27011 -18.03467 1.000 72.68577 ? 244 ASN   A N    1 
ATOM   1878 C  CA   . ASN   A 1 244 ? -33.91831 -40.51110 -18.76047 1.000 71.35679 ? 244 ASN   A CA   1 
ATOM   1879 C  C    . ASN   A 1 244 ? -32.75945 -40.79382 -19.70774 1.000 70.29462 ? 244 ASN   A C    1 
ATOM   1880 O  O    . ASN   A 1 244 ? -32.48666 -40.00768 -20.62143 1.000 65.96679 ? 244 ASN   A O    1 
ATOM   1881 C  CB   . ASN   A 1 244 ? -35.23386 -40.42812 -19.53002 1.000 74.11860 ? 244 ASN   A CB   1 
ATOM   1882 C  CG   . ASN   A 1 244 ? -36.42536 -40.20308 -18.62209 1.000 70.00472 ? 244 ASN   A CG   1 
ATOM   1883 O  OD1  . ASN   A 1 244 ? -37.11876 -39.19198 -18.72825 1.000 79.46174 ? 244 ASN   A OD1  1 
ATOM   1884 N  ND2  . ASN   A 1 244 ? -36.66911 -41.14755 -17.72065 1.000 71.00706 ? 244 ASN   A ND2  1 
ATOM   1885 N  N    . LEU   A 1 245 ? -32.07743 -41.91421 -19.48472 1.000 63.42563 ? 245 LEU   A N    1 
ATOM   1886 C  CA   . LEU   A 1 245 ? -30.95361 -42.28641 -20.33058 1.000 62.01286 ? 245 LEU   A CA   1 
ATOM   1887 C  C    . LEU   A 1 245 ? -31.42417 -42.57116 -21.75106 1.000 59.13281 ? 245 LEU   A C    1 
ATOM   1888 O  O    . LEU   A 1 245 ? -32.49798 -43.13975 -21.96795 1.000 46.98486 ? 245 LEU   A O    1 
ATOM   1889 C  CB   . LEU   A 1 245 ? -30.24311 -43.51376 -19.75490 1.000 56.58897 ? 245 LEU   A CB   1 
ATOM   1890 C  CG   . LEU   A 1 245 ? -29.04669 -44.06171 -20.53680 1.000 51.05161 ? 245 LEU   A CG   1 
ATOM   1891 N  N    . TYR   A 1 246 ? -30.61575 -42.15459 -22.72254 1.000 54.71854 ? 246 TYR   A N    1 
ATOM   1892 C  CA   . TYR   A 1 246 ? -30.84659 -42.49838 -24.11635 1.000 51.70699 ? 246 TYR   A CA   1 
ATOM   1893 C  C    . TYR   A 1 246 ? -29.49558 -42.67453 -24.79104 1.000 51.01508 ? 246 TYR   A C    1 
ATOM   1894 O  O    . TYR   A 1 246 ? -28.47412 -42.16610 -24.32108 1.000 58.55934 ? 246 TYR   A O    1 
ATOM   1895 C  CB   . TYR   A 1 246 ? -31.69872 -41.43975 -24.83367 1.000 52.90003 ? 246 TYR   A CB   1 
ATOM   1896 C  CG   . TYR   A 1 246 ? -30.99350 -40.12691 -25.09857 1.000 55.04540 ? 246 TYR   A CG   1 
ATOM   1897 C  CD1  . TYR   A 1 246 ? -31.02156 -39.10122 -24.16319 1.000 61.70650 ? 246 TYR   A CD1  1 
ATOM   1898 C  CD2  . TYR   A 1 246 ? -30.31991 -39.90462 -26.29435 1.000 55.52948 ? 246 TYR   A CD2  1 
ATOM   1899 C  CE1  . TYR   A 1 246 ? -30.38470 -37.89711 -24.40316 1.000 65.38275 ? 246 TYR   A CE1  1 
ATOM   1900 C  CE2  . TYR   A 1 246 ? -29.68025 -38.70455 -26.54235 1.000 65.40617 ? 246 TYR   A CE2  1 
ATOM   1901 C  CZ   . TYR   A 1 246 ? -29.71767 -37.70374 -25.59465 1.000 67.93751 ? 246 TYR   A CZ   1 
ATOM   1902 O  OH   . TYR   A 1 246 ? -29.08263 -36.50681 -25.83706 1.000 66.32332 ? 246 TYR   A OH   1 
ATOM   1903 N  N    . PHE   A 1 247 ? -29.49879 -43.40807 -25.89682 1.000 45.24834 ? 247 PHE   A N    1 
ATOM   1904 C  CA   . PHE   A 1 247 ? -28.25558 -43.74384 -26.57725 1.000 48.44767 ? 247 PHE   A CA   1 
ATOM   1905 C  C    . PHE   A 1 247 ? -28.12639 -43.01178 -27.90749 1.000 53.34673 ? 247 PHE   A C    1 
ATOM   1906 O  O    . PHE   A 1 247 ? -29.11047 -42.50758 -28.44639 1.000 56.46500 ? 247 PHE   A O    1 
ATOM   1907 C  CB   . PHE   A 1 247 ? -28.16568 -45.25325 -26.79827 1.000 46.31044 ? 247 PHE   A CB   1 
ATOM   1908 C  CG   . PHE   A 1 247 ? -28.30558 -46.06052 -25.53842 1.000 44.83911 ? 247 PHE   A CG   1 
ATOM   1909 C  CD1  . PHE   A 1 247 ? -27.52686 -45.77879 -24.42867 1.000 44.36405 ? 247 PHE   A CD1  1 
ATOM   1910 C  CD2  . PHE   A 1 247 ? -29.21008 -47.10870 -25.46816 1.000 45.36380 ? 247 PHE   A CD2  1 
ATOM   1911 C  CE1  . PHE   A 1 247 ? -27.65167 -46.52218 -23.26862 1.000 42.00553 ? 247 PHE   A CE1  1 
ATOM   1912 C  CE2  . PHE   A 1 247 ? -29.33929 -47.85673 -24.31186 1.000 44.28775 ? 247 PHE   A CE2  1 
ATOM   1913 C  CZ   . PHE   A 1 247 ? -28.55908 -47.56319 -23.21079 1.000 42.59426 ? 247 PHE   A CZ   1 
ATOM   1914 N  N    . HIS   A 1 250 ? -22.20533 -42.83990 -30.26384 1.000 63.16728 ? 250 HIS   A N    1 
ATOM   1915 C  CA   . HIS   A 1 250 ? -20.83630 -42.55070 -30.67528 1.000 62.70375 ? 250 HIS   A CA   1 
ATOM   1916 C  C    . HIS   A 1 250 ? -20.29633 -43.63144 -31.60794 1.000 62.35757 ? 250 HIS   A C    1 
ATOM   1917 O  O    . HIS   A 1 250 ? -20.99960 -44.58338 -31.94658 1.000 63.18713 ? 250 HIS   A O    1 
ATOM   1918 C  CB   . HIS   A 1 250 ? -19.92640 -42.41604 -29.45322 1.000 65.59308 ? 250 HIS   A CB   1 
ATOM   1919 C  CG   . HIS   A 1 250 ? -20.33499 -41.32861 -28.50913 1.000 67.81244 ? 250 HIS   A CG   1 
ATOM   1920 N  ND1  . HIS   A 1 250 ? -21.23458 -41.53145 -27.48459 1.000 68.31986 ? 250 HIS   A ND1  1 
ATOM   1921 C  CD2  . HIS   A 1 250 ? -19.96107 -40.02965 -28.42965 1.000 66.82846 ? 250 HIS   A CD2  1 
ATOM   1922 C  CE1  . HIS   A 1 250 ? -21.39968 -40.40363 -26.81679 1.000 60.92340 ? 250 HIS   A CE1  1 
ATOM   1923 N  NE2  . HIS   A 1 250 ? -20.63839 -39.47677 -27.36997 1.000 65.33895 ? 250 HIS   A NE2  1 
ATOM   1924 N  N    . HIS   A 1 251 ? -19.03957 -43.47387 -32.01843 1.000 64.82957 ? 251 HIS   A N    1 
ATOM   1925 C  CA   . HIS   A 1 251 ? -18.37337 -44.43441 -32.88473 1.000 68.18784 ? 251 HIS   A CA   1 
ATOM   1926 C  C    . HIS   A 1 251 ? -16.93342 -44.61001 -32.42397 1.000 68.72068 ? 251 HIS   A C    1 
ATOM   1927 O  O    . HIS   A 1 251 ? -16.37910 -43.76920 -31.71175 1.000 70.45161 ? 251 HIS   A O    1 
ATOM   1928 C  CB   . HIS   A 1 251 ? -18.40987 -43.99570 -34.35589 1.000 68.45687 ? 251 HIS   A CB   1 
ATOM   1929 C  CG   . HIS   A 1 251 ? -19.75637 -44.13301 -34.99604 1.000 71.14846 ? 251 HIS   A CG   1 
ATOM   1930 N  ND1  . HIS   A 1 251 ? -20.79079 -43.25575 -34.75088 1.000 65.34350 ? 251 HIS   A ND1  1 
ATOM   1931 C  CD2  . HIS   A 1 251 ? -20.23634 -45.04361 -35.87611 1.000 72.25590 ? 251 HIS   A CD2  1 
ATOM   1932 C  CE1  . HIS   A 1 251 ? -21.85035 -43.62111 -35.45047 1.000 62.18304 ? 251 HIS   A CE1  1 
ATOM   1933 N  NE2  . HIS   A 1 251 ? -21.54044 -44.70311 -36.14174 1.000 60.89731 ? 251 HIS   A NE2  1 
ATOM   1934 N  N    . HIS   A 1 252 ? -16.33181 -45.71900 -32.84103 1.000 74.07269 ? 252 HIS   A N    1 
ATOM   1935 C  CA   . HIS   A 1 252 ? -14.95545 -46.02710 -32.47132 1.000 77.12575 ? 252 HIS   A CA   1 
ATOM   1936 C  C    . HIS   A 1 252 ? -13.97660 -45.50657 -33.51869 1.000 79.23055 ? 252 HIS   A C    1 
ATOM   1937 O  O    . HIS   A 1 252 ? -13.50993 -46.25913 -34.37415 1.000 76.21590 ? 252 HIS   A O    1 
ATOM   1938 C  CB   . HIS   A 1 252 ? -14.77534 -47.53492 -32.28486 1.000 80.78021 ? 252 HIS   A CB   1 
HETATM 1939 C  C10  . A1AVW B 2 .   ? -39.90217 -9.53425  5.03574   1.000 23.37257 ? 301 A1AVW A C10  1 
HETATM 1940 C  C15  . A1AVW B 2 .   ? -35.59412 -11.24279 2.90606   1.000 22.31925 ? 301 A1AVW A C15  1 
HETATM 1941 C  C17  . A1AVW B 2 .   ? -33.64469 -9.86767  2.50347   1.000 28.33390 ? 301 A1AVW A C17  1 
HETATM 1942 C  C21  . A1AVW B 2 .   ? -31.14185 -10.27720 3.29507   1.000 34.00575 ? 301 A1AVW A C21  1 
HETATM 1943 C  C24  . A1AVW B 2 .   ? -28.57072 -9.98861  2.91349   1.000 33.59730 ? 301 A1AVW A C24  1 
HETATM 1944 C  C26  . A1AVW B 2 .   ? -27.77767 -12.42860 2.89771   1.000 33.80275 ? 301 A1AVW A C26  1 
HETATM 1945 C  C02  . A1AVW B 2 .   ? -39.68274 -7.11475  8.47155   1.000 26.35618 ? 301 A1AVW A C02  1 
HETATM 1946 C  C04  . A1AVW B 2 .   ? -39.60271 -7.26523  6.17629   1.000 23.47233 ? 301 A1AVW A C04  1 
HETATM 1947 C  C06  . A1AVW B 2 .   ? -39.69915 -7.61985  3.62062   1.000 23.18115 ? 301 A1AVW A C06  1 
HETATM 1948 C  C07  . A1AVW B 2 .   ? -38.76008 -8.39688  2.69640   1.000 25.04757 ? 301 A1AVW A C07  1 
HETATM 1949 C  C09  . A1AVW B 2 .   ? -38.92690 -10.31154 4.14988   1.000 21.56605 ? 301 A1AVW A C09  1 
HETATM 1950 C  C14  . A1AVW B 2 .   ? -36.29999 -10.46169 1.98851   1.000 23.51630 ? 301 A1AVW A C14  1 
HETATM 1951 C  C16  . A1AVW B 2 .   ? -34.24389 -10.93903 3.16673   1.000 23.48887 ? 301 A1AVW A C16  1 
HETATM 1952 C  C18  . A1AVW B 2 .   ? -34.36688 -9.08613  1.60520   1.000 29.51539 ? 301 A1AVW A C18  1 
HETATM 1953 C  C19  . A1AVW B 2 .   ? -35.70273 -9.38751  1.34231   1.000 27.68300 ? 301 A1AVW A C19  1 
HETATM 1954 C  C23  . A1AVW B 2 .   ? -29.79063 -9.50749  3.41574   1.000 33.14369 ? 301 A1AVW A C23  1 
HETATM 1955 C  C30  . A1AVW B 2 .   ? -27.84712 -11.11873 -0.60905  1.000 33.94893 ? 301 A1AVW A C30  1 
HETATM 1956 C  C31  . A1AVW B 2 .   ? -27.42037 -9.21294  3.05836   1.000 32.13063 ? 301 A1AVW A C31  1 
HETATM 1957 C  C32  . A1AVW B 2 .   ? -27.47707 -7.96212  3.69152   1.000 35.23389 ? 301 A1AVW A C32  1 
HETATM 1958 C  C33  . A1AVW B 2 .   ? -28.69014 -7.48277  4.18156   1.000 35.30309 ? 301 A1AVW A C33  1 
HETATM 1959 C  C34  . A1AVW B 2 .   ? -29.84206 -8.25554  4.03496   1.000 36.60535 ? 301 A1AVW A C34  1 
HETATM 1960 C  C35  . A1AVW B 2 .   ? -39.57996 -5.87138  6.06140   1.000 24.51639 ? 301 A1AVW A C35  1 
HETATM 1961 C  C36  . A1AVW B 2 .   ? -39.61529 -5.08779  7.21839   1.000 28.21360 ? 301 A1AVW A C36  1 
HETATM 1962 C  C37  . A1AVW B 2 .   ? -39.66909 -5.71595  8.45632   1.000 24.59911 ? 301 A1AVW A C37  1 
HETATM 1963 C  C38  . A1AVW B 2 .   ? -39.59431 -3.55128  7.10828   1.000 31.29776 ? 301 A1AVW A C38  1 
HETATM 1964 F  F39  . A1AVW B 2 .   ? -40.14873 -3.01729  8.23233   1.000 39.32628 ? 301 A1AVW A F39  1 
HETATM 1965 F  F40  . A1AVW B 2 .   ? -40.30698 -3.15465  6.01463   1.000 36.51311 ? 301 A1AVW A F40  1 
HETATM 1966 F  F41  . A1AVW B 2 .   ? -38.30110 -3.12402  6.97731   1.000 35.87653 ? 301 A1AVW A F41  1 
HETATM 1967 N  N03  . A1AVW B 2 .   ? -39.65063 -7.83136  7.35449   1.000 24.36653 ? 301 A1AVW A N03  1 
HETATM 1968 N  N05  . A1AVW B 2 .   ? -39.56928 -8.12590  4.97576   1.000 22.01155 ? 301 A1AVW A N05  1 
HETATM 1969 N  N08  . A1AVW B 2 .   ? -38.95292 -9.84805  2.76756   1.000 24.71850 ? 301 A1AVW A N08  1 
HETATM 1970 N  N20  . A1AVW B 2 .   ? -32.22472 -9.46099  2.73742   1.000 27.89026 ? 301 A1AVW A N20  1 
HETATM 1971 N  N25  . A1AVW B 2 .   ? -28.47089 -11.29910 2.23418   1.000 31.39361 ? 301 A1AVW A N25  1 
HETATM 1972 O  O12  . A1AVW B 2 .   ? -38.40895 -12.21660 1.77727   1.000 24.05209 ? 301 A1AVW A O12  1 
HETATM 1973 O  O13  . A1AVW B 2 .   ? -38.44042 -10.46328 0.25347   1.000 24.55904 ? 301 A1AVW A O13  1 
HETATM 1974 O  O22  . A1AVW B 2 .   ? -31.28776 -11.40715 3.62671   1.000 28.70773 ? 301 A1AVW A O22  1 
HETATM 1975 O  O28  . A1AVW B 2 .   ? -30.30676 -10.63145 0.44091   1.000 29.42379 ? 301 A1AVW A O28  1 
HETATM 1976 O  O29  . A1AVW B 2 .   ? -29.69502 -12.82774 0.43664   1.000 35.91415 ? 301 A1AVW A O29  1 
HETATM 1977 S  S11  . A1AVW B 2 .   ? -38.07262 -10.80433 1.62696   1.000 21.72174 ? 301 A1AVW A S11  1 
HETATM 1978 S  S27  . A1AVW B 2 .   ? -29.13234 -11.48872 0.63852   1.000 34.89511 ? 301 A1AVW A S27  1 
HETATM 1979 CL CL01 . A1AVW B 2 .   ? -39.74788 -7.98961  10.02202  1.000 27.85746 ? 301 A1AVW A CL01 1 
HETATM 1980 MN MN   . MN    C 3 .   ? -29.49713 -19.29891 0.69563   1.000 23.20750 ? 302 MN    A MN   1 
HETATM 1981 MN MN   . MN    D 3 .   ? -29.26583 -17.68645 3.62322   1.000 23.66166 ? 303 MN    A MN   1 
HETATM 1982 O  O    . HOH   E 4 .   ? -31.396   -42.436   -28.552   1.000 34.65436 ? 401 HOH   A O    1 
HETATM 1983 O  O    . HOH   E 4 .   ? -26.49631 -18.59112 16.27303  1.000 44.10984 ? 402 HOH   A O    1 
HETATM 1984 O  O    . HOH   E 4 .   ? -43.72809 -25.77681 15.23069  1.000 28.97689 ? 403 HOH   A O    1 
HETATM 1985 O  O    . HOH   E 4 .   ? -46.50685 -23.22609 -7.89210  1.000 44.30217 ? 404 HOH   A O    1 
HETATM 1986 O  O    . HOH   E 4 .   ? -48.23206 -17.87997 11.29472  1.000 31.83811 ? 405 HOH   A O    1 
HETATM 1987 O  O    . HOH   E 4 .   ? -19.54670 -33.65838 22.67260  1.000 57.70708 ? 406 HOH   A O    1 
HETATM 1988 O  O    . HOH   E 4 .   ? -24.57453 -31.13151 -8.70146  1.000 45.55705 ? 407 HOH   A O    1 
HETATM 1989 O  O    . HOH   E 4 .   ? -42.45780 -17.05345 -1.05799  1.000 29.07754 ? 408 HOH   A O    1 
HETATM 1990 O  O    . HOH   E 4 .   ? -45.38428 -14.65325 -2.11970  1.000 28.17324 ? 409 HOH   A O    1 
HETATM 1991 O  O    . HOH   E 4 .   ? -39.90183 -34.28196 17.13047  1.000 34.41387 ? 410 HOH   A O    1 
HETATM 1992 O  O    . HOH   E 4 .   ? -20.20054 -34.60137 18.20993  1.000 35.77571 ? 411 HOH   A O    1 
HETATM 1993 O  O    . HOH   E 4 .   ? -35.50907 1.52162   -0.39677  1.000 46.16788 ? 412 HOH   A O    1 
HETATM 1994 O  O    . HOH   E 4 .   ? -28.43175 -17.97998 1.70263   1.000 27.13891 ? 413 HOH   A O    1 
HETATM 1995 O  O    . HOH   E 4 .   ? -48.84277 -8.32028  13.67408  1.000 39.49705 ? 414 HOH   A O    1 
HETATM 1996 O  O    . HOH   E 4 .   ? -40.41716 -17.39903 -3.03154  1.000 26.81470 ? 415 HOH   A O    1 
HETATM 1997 O  O    . HOH   E 4 .   ? -32.66988 -9.83356  -2.45796  1.000 46.02347 ? 416 HOH   A O    1 
HETATM 1998 O  O    . HOH   E 4 .   ? -13.42642 -35.82801 17.06689  1.000 37.32277 ? 417 HOH   A O    1 
HETATM 1999 O  O    . HOH   E 4 .   ? -48.30195 -18.29735 2.68018   1.000 24.52759 ? 418 HOH   A O    1 
HETATM 2000 O  O    . HOH   E 4 .   ? -33.95891 -36.51115 14.46710  1.000 27.75767 ? 419 HOH   A O    1 
HETATM 2001 O  O    . HOH   E 4 .   ? -31.81173 -22.01753 -5.51068  1.000 37.14106 ? 420 HOH   A O    1 
HETATM 2002 O  O    . HOH   E 4 .   ? -17.93774 -23.96504 2.51164   1.000 23.85795 ? 421 HOH   A O    1 
HETATM 2003 O  O    . HOH   E 4 .   ? -29.72030 -20.41674 12.27718  1.000 22.82227 ? 422 HOH   A O    1 
HETATM 2004 O  O    . HOH   E 4 .   ? -7.30110  -31.51614 15.88538  1.000 48.54217 ? 423 HOH   A O    1 
HETATM 2005 O  O    . HOH   E 4 .   ? -33.47696 -44.15482 6.27684   1.000 35.81804 ? 424 HOH   A O    1 
HETATM 2006 O  O    . HOH   E 4 .   ? -15.52853 -21.57217 4.35086   1.000 39.66371 ? 425 HOH   A O    1 
HETATM 2007 O  O    . HOH   E 4 .   ? -17.59482 -33.00997 21.82439  1.000 46.89709 ? 426 HOH   A O    1 
HETATM 2008 O  O    . HOH   E 4 .   ? -32.21224 -19.25007 11.90558  1.000 27.32305 ? 427 HOH   A O    1 
HETATM 2009 O  O    . HOH   E 4 .   ? -44.61987 -14.73156 10.85659  1.000 46.72082 ? 428 HOH   A O    1 
HETATM 2010 O  O    . HOH   E 4 .   ? -42.38174 -22.75763 -8.63377  1.000 38.24367 ? 429 HOH   A O    1 
HETATM 2011 O  O    . HOH   E 4 .   ? -44.08030 -21.78660 -11.43811 1.000 34.16782 ? 430 HOH   A O    1 
HETATM 2012 O  O    . HOH   E 4 .   ? -30.56910 -30.82650 -12.34937 1.000 33.55975 ? 431 HOH   A O    1 
HETATM 2013 O  O    . HOH   E 4 .   ? -38.76832 -22.89584 -7.19267  1.000 24.72802 ? 432 HOH   A O    1 
HETATM 2014 O  O    . HOH   E 4 .   ? -19.01773 -21.87049 4.17429   1.000 20.81358 ? 433 HOH   A O    1 
HETATM 2015 O  O    . HOH   E 4 .   ? -54.01192 -19.80631 -2.12768  1.000 36.53427 ? 434 HOH   A O    1 
HETATM 2016 O  O    . HOH   E 4 .   ? -27.16402 -19.32639 11.63100  1.000 26.03040 ? 435 HOH   A O    1 
HETATM 2017 O  O    . HOH   E 4 .   ? -48.42919 -30.49904 -3.83514  1.000 36.80053 ? 436 HOH   A O    1 
HETATM 2018 O  O    . HOH   E 4 .   ? -26.74638 -26.14839 -8.15691  1.000 38.83629 ? 437 HOH   A O    1 
HETATM 2019 O  O    . HOH   E 4 .   ? -25.53836 -23.28250 1.57303   1.000 23.62194 ? 438 HOH   A O    1 
HETATM 2020 O  O    . HOH   E 4 .   ? -52.10126 -15.83370 9.20030   1.000 41.81050 ? 439 HOH   A O    1 
HETATM 2021 O  O    . HOH   E 4 .   ? -50.76462 -33.59615 1.84712   1.000 28.06822 ? 440 HOH   A O    1 
HETATM 2022 O  O    . HOH   E 4 .   ? -27.43707 -9.67993  14.03874  1.000 46.36543 ? 441 HOH   A O    1 
HETATM 2023 O  O    . HOH   E 4 .   ? -35.46774 -20.99849 13.29514  1.000 21.65354 ? 442 HOH   A O    1 
HETATM 2024 O  O    . HOH   E 4 .   ? -30.94150 -17.11005 10.76884  1.000 29.11042 ? 443 HOH   A O    1 
HETATM 2025 O  O    . HOH   E 4 .   ? -20.45591 -18.45016 17.39847  1.000 42.11966 ? 444 HOH   A O    1 
HETATM 2026 O  O    . HOH   E 4 .   ? -33.12396 -38.79647 13.12718  1.000 30.49277 ? 445 HOH   A O    1 
HETATM 2027 O  O    . HOH   E 4 .   ? -42.99733 -33.14964 11.44163  1.000 21.93472 ? 446 HOH   A O    1 
HETATM 2028 O  O    . HOH   E 4 .   ? -21.67630 -34.52440 -3.66742  1.000 30.19809 ? 447 HOH   A O    1 
HETATM 2029 O  O    . HOH   E 4 .   ? -18.17420 -46.29118 8.31358   1.000 39.05367 ? 448 HOH   A O    1 
HETATM 2030 O  O    . HOH   E 4 .   ? -45.24487 -14.93156 2.30376   1.000 22.35979 ? 449 HOH   A O    1 
HETATM 2031 O  O    . HOH   E 4 .   ? -38.66230 -21.22866 14.82099  1.000 31.69405 ? 450 HOH   A O    1 
HETATM 2032 O  O    . HOH   E 4 .   ? -49.00749 -20.23729 4.88563   1.000 26.44040 ? 451 HOH   A O    1 
HETATM 2033 O  O    . HOH   E 4 .   ? -51.69412 -26.82482 1.55315   1.000 35.16931 ? 452 HOH   A O    1 
HETATM 2034 O  O    . HOH   E 4 .   ? -35.03007 -34.24549 -7.13277  1.000 29.24219 ? 453 HOH   A O    1 
HETATM 2035 O  O    . HOH   E 4 .   ? -9.85940  -27.16359 20.59299  1.000 40.25526 ? 454 HOH   A O    1 
HETATM 2036 O  O    . HOH   E 4 .   ? -49.94689 -30.17912 11.32022  1.000 32.72154 ? 455 HOH   A O    1 
HETATM 2037 O  O    . HOH   E 4 .   ? -54.39992 -11.02007 5.50082   1.000 46.01142 ? 456 HOH   A O    1 
HETATM 2038 O  O    . HOH   E 4 .   ? -29.44635 -28.28427 0.21412   1.000 21.32881 ? 457 HOH   A O    1 
HETATM 2039 O  O    . HOH   E 4 .   ? -35.21784 -12.31828 -5.49851  1.000 43.58004 ? 458 HOH   A O    1 
HETATM 2040 O  O    . HOH   E 4 .   ? -44.64002 -42.77256 1.20341   1.000 40.65617 ? 459 HOH   A O    1 
HETATM 2041 O  O    . HOH   E 4 .   ? -44.65735 -35.49062 -1.12124  1.000 26.29452 ? 460 HOH   A O    1 
HETATM 2042 O  O    . HOH   E 4 .   ? -25.35690 -18.83831 -4.88552  1.000 43.51226 ? 461 HOH   A O    1 
HETATM 2043 O  O    . HOH   E 4 .   ? -43.98763 -34.27387 -3.51517  1.000 30.46301 ? 462 HOH   A O    1 
HETATM 2044 O  O    . HOH   E 4 .   ? -17.83231 -25.37787 -2.32603  1.000 28.70322 ? 463 HOH   A O    1 
HETATM 2045 O  O    . HOH   E 4 .   ? -48.62272 -39.65935 2.62072   1.000 34.92176 ? 464 HOH   A O    1 
HETATM 2046 O  O    . HOH   E 4 .   ? -24.77724 -27.15294 -4.56248  1.000 38.51031 ? 465 HOH   A O    1 
HETATM 2047 O  O    . HOH   E 4 .   ? -37.89254 -15.18788 12.91371  1.000 38.87899 ? 466 HOH   A O    1 
HETATM 2048 O  O    . HOH   E 4 .   ? -46.23830 -17.80083 14.07520  1.000 33.42722 ? 467 HOH   A O    1 
HETATM 2049 O  O    . HOH   E 4 .   ? -24.34813 -23.87074 -3.86950  1.000 26.80777 ? 468 HOH   A O    1 
HETATM 2050 O  O    . HOH   E 4 .   ? -39.36680 -43.84239 6.52130   1.000 41.52333 ? 469 HOH   A O    1 
HETATM 2051 O  O    . HOH   E 4 .   ? -17.97525 -13.42758 8.31620   1.000 47.14050 ? 470 HOH   A O    1 
HETATM 2052 O  O    . HOH   E 4 .   ? -39.10837 -13.75376 5.69734   1.000 19.83479 ? 471 HOH   A O    1 
HETATM 2053 O  O    . HOH   E 4 .   ? -37.22688 -39.74182 13.68978  1.000 37.37576 ? 472 HOH   A O    1 
HETATM 2054 O  O    . HOH   E 4 .   ? -29.33236 -45.42461 7.97280   1.000 21.09461 ? 473 HOH   A O    1 
HETATM 2055 O  O    . HOH   E 4 .   ? -36.69670 -37.07858 14.71484  1.000 29.68966 ? 474 HOH   A O    1 
HETATM 2056 O  O    . HOH   E 4 .   ? -30.89454 -28.07897 21.25500  1.000 35.60531 ? 475 HOH   A O    1 
HETATM 2057 O  O    . HOH   E 4 .   ? -51.73744 -29.33821 -3.39228  1.000 45.90431 ? 476 HOH   A O    1 
HETATM 2058 O  O    . HOH   E 4 .   ? -42.40052 -2.33404  -5.20711  1.000 44.26184 ? 477 HOH   A O    1 
HETATM 2059 O  O    . HOH   E 4 .   ? -30.60382 -40.75195 15.88701  1.000 33.02811 ? 478 HOH   A O    1 
HETATM 2060 O  O    . HOH   E 4 .   ? -45.31137 -14.96716 -7.35778  1.000 41.55553 ? 479 HOH   A O    1 
HETATM 2061 O  O    . HOH   E 4 .   ? -13.18652 -22.92529 12.29437  1.000 30.01093 ? 480 HOH   A O    1 
HETATM 2062 O  O    . HOH   E 4 .   ? -32.43087 -36.77136 16.90491  1.000 39.43731 ? 481 HOH   A O    1 
HETATM 2063 O  O    . HOH   E 4 .   ? -26.54280 -43.23177 0.12248   1.000 48.72493 ? 482 HOH   A O    1 
HETATM 2064 O  O    . HOH   E 4 .   ? -29.38681 -15.82760 1.20900   1.000 31.07391 ? 483 HOH   A O    1 
HETATM 2065 O  O    . HOH   E 4 .   ? -41.66853 -14.72515 -6.37712  1.000 49.43332 ? 484 HOH   A O    1 
HETATM 2066 O  O    . HOH   E 4 .   ? -42.36318 -25.57410 17.36133  1.000 46.68619 ? 485 HOH   A O    1 
HETATM 2067 O  O    . HOH   E 4 .   ? -34.32002 -19.06368 17.88233  1.000 36.45830 ? 486 HOH   A O    1 
HETATM 2068 O  O    . HOH   E 4 .   ? -9.45018  -25.13763 14.40826  1.000 42.64264 ? 487 HOH   A O    1 
HETATM 2069 O  O    . HOH   E 4 .   ? -10.93544 -26.54282 23.79052  1.000 54.28805 ? 488 HOH   A O    1 
HETATM 2070 O  O    . HOH   E 4 .   ? -29.35256 -10.81399 14.95575  1.000 38.28402 ? 489 HOH   A O    1 
HETATM 2071 O  O    . HOH   E 4 .   ? -46.31021 -15.30736 9.55504   1.000 34.97418 ? 490 HOH   A O    1 
HETATM 2072 O  O    . HOH   E 4 .   ? -53.93111 -8.32110  4.41338   1.000 35.43174 ? 491 HOH   A O    1 
HETATM 2073 O  O    . HOH   E 4 .   ? -29.35126 -41.31913 -1.47071  1.000 53.85121 ? 492 HOH   A O    1 
HETATM 2074 O  O    . HOH   E 4 .   ? -18.88984 -46.03511 5.47410   1.000 43.64564 ? 493 HOH   A O    1 
HETATM 2075 O  O    . HOH   E 4 .   ? -32.00432 -35.29226 18.79172  1.000 37.62136 ? 494 HOH   A O    1 
HETATM 2076 O  O    . HOH   E 4 .   ? -23.86542 -6.22220  3.35464   1.000 51.37728 ? 495 HOH   A O    1 
HETATM 2077 O  O    . HOH   E 4 .   ? -54.053   -6.787    0.444     1.000 34.32014 ? 496 HOH   A O    1 
HETATM 2078 O  O    . HOH   E 4 .   ? -10.339   -32.999   5.916     1.000 39.88083 ? 497 HOH   A O    1 
HETATM 2079 O  O    . HOH   E 4 .   ? -42.78704 -16.95380 -5.43411  1.000 17.08029 ? 498 HOH   A O    1 
HETATM 2080 O  O    . HOH   E 4 .   ? -32.00103 -39.33917 -12.72009 1.000 57.36537 ? 499 HOH   A O    1 
HETATM 2081 O  O    . HOH   E 4 .   ? -43.12440 -10.55611 -2.03454  1.000 35.40628 ? 500 HOH   A O    1 
HETATM 2082 O  O    . HOH   E 4 .   ? -14.17629 -23.92579 9.62032   1.000 25.32427 ? 501 HOH   A O    1 
HETATM 2083 O  O    . HOH   E 4 .   ? -48.96854 -33.15436 -2.40234  1.000 40.24896 ? 502 HOH   A O    1 
HETATM 2084 O  O    . HOH   E 4 .   ? -46.94450 -32.54007 12.88717  1.000 47.84795 ? 503 HOH   A O    1 
HETATM 2085 O  O    . HOH   E 4 .   ? -18.73675 -40.15146 10.79304  1.000 39.97349 ? 504 HOH   A O    1 
HETATM 2086 O  O    . HOH   E 4 .   ? -32.17324 -43.22444 3.32082   1.000 47.07127 ? 505 HOH   A O    1 
HETATM 2087 O  O    . HOH   E 4 .   ? -43.42651 -12.34326 15.88992  1.000 50.91393 ? 506 HOH   A O    1 
HETATM 2088 O  O    . HOH   E 4 .   ? -19.97707 -34.60130 26.77500  0.50  76.23254 ? 507 HOH   A O    1 
HETATM 2089 O  O    . HOH   E 4 .   ? -25.55039 -42.20433 -29.33056 1.000 46.99597 ? 508 HOH   A O    1 
HETATM 2090 O  O    . HOH   E 4 .   ? -34.51768 -36.78144 -5.81739  1.000 38.14716 ? 509 HOH   A O    1 
HETATM 2091 O  O    . HOH   E 4 .   ? -32.363   -38.112   -4.460    1.000 49.16925 ? 510 HOH   A O    1 
HETATM 2092 O  O    . HOH   E 4 .   ? -52.47037 -31.76765 2.81759   1.000 39.21567 ? 511 HOH   A O    1 
HETATM 2093 O  O    . HOH   E 4 .   ? -41.49111 -44.49741 7.73853   1.000 45.71825 ? 512 HOH   A O    1 
HETATM 2094 O  O    . HOH   E 4 .   ? -24.65384 -42.70171 -26.77500 0.50  42.46348 ? 513 HOH   A O    1 
HETATM 2095 O  O    . HOH   E 4 .   ? -35.93527 -34.44173 17.73962  1.000 41.44747 ? 514 HOH   A O    1 
HETATM 2096 O  O    . HOH   E 4 .   ? -25.72426 -43.31496 -31.35430 1.000 35.24145 ? 515 HOH   A O    1 
HETATM 2097 O  O    . HOH   E 4 .   ? -35.15757 -32.39861 17.49251  1.000 36.61311 ? 516 HOH   A O    1 
HETATM 2098 O  O    . HOH   E 4 .   ? -10.95073 -27.80005 4.28501   1.000 35.46044 ? 517 HOH   A O    1 
HETATM 2099 O  O    . HOH   E 4 .   ? -19.35784 -36.95073 17.81063  1.000 45.71022 ? 518 HOH   A O    1 
HETATM 2100 O  O    . HOH   E 4 .   ? -34.44973 -18.15337 13.86560  1.000 19.80907 ? 519 HOH   A O    1 
HETATM 2101 O  O    . HOH   E 4 .   ? -44.30360 -34.36405 13.42819  1.000 39.41743 ? 520 HOH   A O    1 
HETATM 2102 O  O    . HOH   E 4 .   ? -49.71637 -41.64439 3.46069   1.000 43.23155 ? 521 HOH   A O    1 
HETATM 2103 O  O    . HOH   E 4 .   ? -32.62624 -40.47386 14.80685  1.000 48.19559 ? 522 HOH   A O    1 
HETATM 2104 O  O    . HOH   E 4 .   ? -50.15630 -15.47645 10.31498  1.000 46.45995 ? 523 HOH   A O    1 
HETATM 2105 O  O    . HOH   E 4 .   ? -25.49827 -9.38156  -3.81212  1.000 57.77650 ? 524 HOH   A O    1 
HETATM 2106 O  O    . HOH   E 4 .   ? -10.54124 -23.17978 12.60826  1.000 41.96260 ? 525 HOH   A O    1 
HETATM 2107 O  O    . HOH   E 4 .   ? -23.31371 -6.70756  -4.77150  1.000 56.24905 ? 526 HOH   A O    1 
HETATM 2108 O  O    . HOH   E 4 .   ? -21.62250 -5.41561  -3.90267  1.000 59.27448 ? 527 HOH   A O    1 
HETATM 2109 O  O    . HOH   E 4 .   ? -17.88841 -7.76877  -1.38553  1.000 54.75296 ? 528 HOH   A O    1 
HETATM 2110 O  O    . HOH   E 4 .   ? -15.70820 -8.25907  -0.53638  1.000 53.81403 ? 529 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 2   ? 0.31657 0.20720 0.40309 0.04697  0.03186  0.04412  2   ALA A N   
2    C CA  . ALA A 2   ? 0.32484 0.24055 0.41729 0.05315  0.03718  0.04248  2   ALA A CA  
3    C C   . ALA A 2   ? 0.30503 0.24438 0.39553 0.04046  0.02981  0.03665  2   ALA A C   
4    O O   . ALA A 2   ? 0.31839 0.24984 0.39793 0.02975  0.02340  0.02977  2   ALA A O   
5    C CB  . ALA A 2   ? 0.31865 0.21224 0.39663 0.06575  0.04735  0.03285  2   ALA A CB  
6    N N   . THR A 3   ? 0.23730 0.20515 0.33854 0.04182  0.03035  0.04035  3   THR A N   
7    C CA  . THR A 3   ? 0.21570 0.20272 0.31352 0.03263  0.02430  0.03455  3   THR A CA  
8    C C   . THR A 3   ? 0.25605 0.24423 0.34881 0.03748  0.02923  0.02752  3   THR A C   
9    O O   . THR A 3   ? 0.22972 0.22361 0.33154 0.04662  0.03581  0.03355  3   THR A O   
10   C CB  . THR A 3   ? 0.23542 0.25106 0.34592 0.02804  0.01842  0.04425  3   THR A CB  
11   O OG1 . THR A 3   ? 0.27174 0.28823 0.38670 0.02376  0.01442  0.05238  3   THR A OG1 
12   C CG2 . THR A 3   ? 0.19938 0.22923 0.30224 0.02059  0.01269  0.03681  3   THR A CG2 
13   N N   . LEU A 4   ? 0.23875 0.22371 0.31846 0.03155  0.02618  0.01668  4   LEU A N   
14   C CA  . LEU A 4   ? 0.22743 0.21033 0.29969 0.03521  0.03045  0.00983  4   LEU A CA  
15   C C   . LEU A 4   ? 0.26211 0.26586 0.33785 0.02969  0.02511  0.00952  4   LEU A C   
16   O O   . LEU A 4   ? 0.22021 0.23297 0.29481 0.02245  0.01791  0.00840  4   LEU A O   
17   C CB  . LEU A 4   ? 0.23049 0.19130 0.28323 0.03297  0.03044  -0.00193 4   LEU A CB  
18   C CG  . LEU A 4   ? 0.32413 0.25550 0.36627 0.03679  0.03376  -0.00463 4   LEU A CG  
19   C CD1 . LEU A 4   ? 0.32840 0.23919 0.34868 0.03202  0.03120  -0.01659 4   LEU A CD1 
20   C CD2 . LEU A 4   ? 0.32411 0.24764 0.36955 0.05163  0.04501  -0.00019 4   LEU A CD2 
21   N N   . PHE A 5   ? 0.22755 0.23779 0.30644 0.03364  0.02891  0.01099  5   PHE A N   
22   C CA  . PHE A 5   ? 0.20466 0.22884 0.28497 0.02818  0.02331  0.01066  5   PHE A CA  
23   C C   . PHE A 5   ? 0.22529 0.24350 0.29727 0.03064  0.02755  0.00544  5   PHE A C   
24   O O   . PHE A 5   ? 0.21231 0.22656 0.28536 0.03854  0.03639  0.00815  5   PHE A O   
25   C CB  . PHE A 5   ? 0.19517 0.23818 0.29204 0.02728  0.02078  0.02264  5   PHE A CB  
26   C CG  . PHE A 5   ? 0.21959 0.27074 0.32385 0.02453  0.01586  0.02912  5   PHE A CG  
27   C CD1 . PHE A 5   ? 0.18411 0.23332 0.29761 0.03081  0.02110  0.03677  5   PHE A CD1 
28   C CD2 . PHE A 5   ? 0.20264 0.26199 0.30269 0.01667  0.00632  0.02775  5   PHE A CD2 
29   C CE1 . PHE A 5   ? 0.21670 0.27444 0.33731 0.02799  0.01626  0.04434  5   PHE A CE1 
30   C CE2 . PHE A 5   ? 0.21202 0.28022 0.31676 0.01425  0.00200  0.03432  5   PHE A CE2 
31   C CZ  . PHE A 5   ? 0.19056 0.25922 0.30672 0.01925  0.00665  0.04335  5   PHE A CZ  
32   N N   . ILE A 6   ? 0.19677 0.21456 0.25969 0.02517  0.02196  -0.00135 6   ILE A N   
33   C CA  . ILE A 6   ? 0.21947 0.23368 0.27495 0.02624  0.02437  -0.00476 6   ILE A CA  
34   C C   . ILE A 6   ? 0.18446 0.20552 0.24012 0.02011  0.01630  -0.00494 6   ILE A C   
35   O O   . ILE A 6   ? 0.19711 0.22165 0.25271 0.01602  0.00933  -0.00611 6   ILE A O   
36   C CB  . ILE A 6   ? 0.22434 0.22344 0.26306 0.02690  0.02596  -0.01456 6   ILE A CB  
37   C CG1 . ILE A 6   ? 0.23260 0.23232 0.26611 0.02082  0.01799  -0.01993 6   ILE A CG1 
38   C CG2 . ILE A 6   ? 0.26840 0.25316 0.30163 0.03250  0.03276  -0.01612 6   ILE A CG2 
39   C CD1 . ILE A 6   ? 0.22142 0.21046 0.24092 0.01909  0.01708  -0.02722 6   ILE A CD1 
40   N N   . ALA A 7   ? 0.19523 0.21638 0.24911 0.02005  0.01745  -0.00372 7   ALA A N   
41   C CA  . ALA A 7   ? 0.20803 0.22986 0.25988 0.01442  0.00940  -0.00401 7   ALA A CA  
42   C C   . ALA A 7   ? 0.22100 0.24053 0.26924 0.01518  0.01235  -0.00247 7   ALA A C   
43   O O   . ALA A 7   ? 0.21027 0.23106 0.25859 0.02032  0.02117  0.00013  7   ALA A O   
44   C CB  . ALA A 7   ? 0.19370 0.22473 0.25696 0.00886  0.00290  0.00427  7   ALA A CB  
45   N N   . ASP A 8   ? 0.21615 0.23087 0.25940 0.01084  0.00510  -0.00396 8   ASP A N   
46   C CA  . ASP A 8   ? 0.22162 0.23510 0.26351 0.00964  0.00577  0.00041  8   ASP A CA  
47   C C   . ASP A 8   ? 0.23138 0.24139 0.26290 0.01531  0.01340  -0.00374 8   ASP A C   
48   O O   . ASP A 8   ? 0.21806 0.23260 0.25048 0.01748  0.01982  0.00233  8   ASP A O   
49   C CB  . ASP A 8   ? 0.22646 0.25253 0.28391 0.00632  0.00722  0.01403  8   ASP A CB  
50   C CG  . ASP A 8   ? 0.23753 0.26556 0.30300 -0.00228 -0.00358 0.01875  8   ASP A CG  
51   O OD1 . ASP A 8   ? 0.25911 0.27529 0.31728 -0.00825 -0.01336 0.01631  8   ASP A OD1 
52   O OD2 . ASP A 8   ? 0.25643 0.29605 0.33379 -0.00287 -0.00286 0.02478  8   ASP A OD2 
53   N N   . LEU A 9   ? 0.22900 0.23211 0.24988 0.01729  0.01229  -0.01328 9   LEU A N   
54   C CA  . LEU A 9   ? 0.24498 0.24315 0.25314 0.02020  0.01611  -0.01768 9   LEU A CA  
55   C C   . LEU A 9   ? 0.26863 0.26434 0.27090 0.01886  0.01204  -0.01646 9   LEU A C   
56   O O   . LEU A 9   ? 0.26893 0.26378 0.26259 0.02052  0.01584  -0.01541 9   LEU A O   
57   C CB  . LEU A 9   ? 0.25745 0.25142 0.25862 0.02036  0.01432  -0.02573 9   LEU A CB  
58   C CG  . LEU A 9   ? 0.30688 0.29797 0.30903 0.02217  0.01926  -0.02731 9   LEU A CG  
59   C CD1 . LEU A 9   ? 0.26338 0.26067 0.27866 0.02099  0.01715  -0.02423 9   LEU A CD1 
60   C CD2 . LEU A 9   ? 0.27907 0.26256 0.26964 0.02030  0.01704  -0.03418 9   LEU A CD2 
61   N N   . HIS A 10  ? 0.25057 0.24344 0.25542 0.01661  0.00443  -0.01650 10  HIS A N   
62   C CA  . HIS A 10  ? 0.27020 0.25752 0.27009 0.01628  -0.00014 -0.01450 10  HIS A CA  
63   C C   . HIS A 10  ? 0.27232 0.25986 0.26155 0.01922  0.00078  -0.01798 10  HIS A C   
64   O O   . HIS A 10  ? 0.27712 0.26432 0.26117 0.01932  0.00169  -0.01375 10  HIS A O   
65   C CB  . HIS A 10  ? 0.29044 0.27921 0.29584 0.01284  0.00088  -0.00434 10  HIS A CB  
66   C CG  . HIS A 10  ? 0.29480 0.28450 0.31178 0.00737  -0.00308 0.00134  10  HIS A CG  
67   N ND1 . HIS A 10  ? 0.38034 0.35844 0.39689 0.00273  -0.01286 0.00247  10  HIS A ND1 
68   C CD2 . HIS A 10  ? 0.31198 0.31220 0.34050 0.00551  0.00050  0.00680  10  HIS A CD2 
69   C CE1 . HIS A 10  ? 0.37158 0.35315 0.39818 -0.00375 -0.01650 0.00819  10  HIS A CE1 
70   N NE2 . HIS A 10  ? 0.31449 0.31193 0.35037 -0.00194 -0.00826 0.01188  10  HIS A NE2 
71   N N   . LEU A 11  ? 0.26222 0.25208 0.24863 0.02062  -0.00021 -0.02429 11  LEU A N   
72   C CA  . LEU A 11  ? 0.26321 0.25563 0.24070 0.02120  -0.00131 -0.02641 11  LEU A CA  
73   C C   . LEU A 11  ? 0.32589 0.31785 0.30125 0.02385  -0.00609 -0.02315 11  LEU A C   
74   O O   . LEU A 11  ? 0.27869 0.26708 0.25799 0.02705  -0.00949 -0.02295 11  LEU A O   
75   C CB  . LEU A 11  ? 0.24771 0.24521 0.22614 0.02037  -0.00310 -0.03107 11  LEU A CB  
76   C CG  . LEU A 11  ? 0.30633 0.30174 0.28579 0.01789  0.00071  -0.03407 11  LEU A CG  
77   C CD1 . LEU A 11  ? 0.25670 0.25838 0.23964 0.01590  -0.00267 -0.03609 11  LEU A CD1 
78   C CD2 . LEU A 11  ? 0.32306 0.31129 0.29058 0.01661  0.00471  -0.03579 11  LEU A CD2 
79   N N   . GLN A 12  ? 0.28653 0.28048 0.25363 0.02323  -0.00642 -0.02062 12  GLN A N   
80   C CA  . GLN A 12  ? 0.34066 0.33538 0.30599 0.02629  -0.01092 -0.01572 12  GLN A CA  
81   C C   . GLN A 12  ? 0.34206 0.34345 0.29705 0.02394  -0.01242 -0.01432 12  GLN A C   
82   O O   . GLN A 12  ? 0.32581 0.32559 0.27124 0.02015  -0.00900 -0.01690 12  GLN A O   
83   C CB  . GLN A 12  ? 0.34622 0.33230 0.31331 0.02653  -0.01091 -0.00924 12  GLN A CB  
84   C CG  . GLN A 12  ? 0.30869 0.29570 0.27243 0.02265  -0.00526 -0.00526 12  GLN A CG  
85   C CD  . GLN A 12  ? 0.40277 0.38418 0.37232 0.02071  -0.00600 0.00370  12  GLN A CD  
86   O OE1 . GLN A 12  ? 0.48675 0.46906 0.46327 0.01756  -0.00264 0.00669  12  GLN A OE1 
87   N NE2 . GLN A 12  ? 0.48256 0.45875 0.45044 0.02215  -0.01104 0.00959  12  GLN A NE2 
88   N N   . THR A 13  ? 0.35047 0.35859 0.30600 0.02686  -0.01776 -0.00998 13  THR A N   
89   C CA  . THR A 13  ? 0.34918 0.36575 0.29489 0.02312  -0.02162 -0.00750 13  THR A CA  
90   C C   . THR A 13  ? 0.30684 0.31849 0.23973 0.02077  -0.01921 -0.00403 13  THR A C   
91   O O   . THR A 13  ? 0.34698 0.36094 0.26518 0.01602  -0.02096 -0.00512 13  THR A O   
92   C CB  . THR A 13  ? 0.44106 0.46959 0.39323 0.02788  -0.02779 -0.00060 13  THR A CB  
93   O OG1 . THR A 13  ? 0.39894 0.41973 0.35673 0.03573  -0.02717 0.00439  13  THR A OG1 
94   C CG2 . THR A 13  ? 0.36186 0.40188 0.32442 0.02944  -0.02955 -0.00267 13  THR A CG2 
95   N N   . GLU A 14  ? 0.36055 0.36529 0.29737 0.02338  -0.01568 0.00073  14  GLU A N   
96   C CA  . GLU A 14  ? 0.38180 0.38534 0.30809 0.02165  -0.01205 0.00643  14  GLU A CA  
97   C C   . GLU A 14  ? 0.37251 0.37293 0.28948 0.01966  -0.00385 0.00101  14  GLU A C   
98   O O   . GLU A 14  ? 0.44904 0.45044 0.35399 0.01961  0.00097  0.00522  14  GLU A O   
99   C CB  . GLU A 14  ? 0.39894 0.39713 0.33466 0.02353  -0.01170 0.01571  14  GLU A CB  
100  C CG  . GLU A 14  ? 0.54825 0.54511 0.48888 0.02757  -0.01891 0.02269  14  GLU A CG  
101  C CD  . GLU A 14  ? 0.63385 0.62428 0.58554 0.03269  -0.02207 0.01793  14  GLU A CD  
102  O OE1 . GLU A 14  ? 0.70055 0.68789 0.65559 0.03893  -0.02677 0.02274  14  GLU A OE1 
103  O OE2 . GLU A 14  ? 0.65221 0.64040 0.60811 0.03160  -0.01938 0.00980  14  GLU A OE2 
104  N N   . GLU A 15  ? 0.33757 0.33454 0.25919 0.01929  -0.00143 -0.00732 15  GLU A N   
105  C CA  . GLU A 15  ? 0.37680 0.36893 0.29045 0.01975  0.00702  -0.01237 15  GLU A CA  
106  C C   . GLU A 15  ? 0.36177 0.34847 0.26571 0.01691  0.00438  -0.02254 15  GLU A C   
107  O O   . GLU A 15  ? 0.36282 0.34609 0.27507 0.01701  0.00609  -0.02751 15  GLU A O   
108  C CB  . GLU A 15  ? 0.37496 0.36693 0.30540 0.02162  0.01233  -0.01034 15  GLU A CB  
109  C CG  . GLU A 15  ? 0.37109 0.36725 0.31112 0.02181  0.01422  0.00116  15  GLU A CG  
110  C CD  . GLU A 15  ? 0.51662 0.51759 0.44474 0.02376  0.02213  0.00765  15  GLU A CD  
111  O OE1 . GLU A 15  ? 0.47741 0.47614 0.39102 0.02710  0.02942  0.00185  15  GLU A OE1 
112  O OE2 . GLU A 15  ? 0.59547 0.60124 0.52738 0.02245  0.02130  0.01888  15  GLU A OE2 
113  N N   . PRO A 16  ? 0.37892 0.36433 0.26487 0.01312  -0.00093 -0.02485 16  PRO A N   
114  C CA  . PRO A 16  ? 0.38238 0.36118 0.25934 0.00747  -0.00634 -0.03324 16  PRO A CA  
115  C C   . PRO A 16  ? 0.41563 0.37802 0.28011 0.00916  0.00118  -0.04175 16  PRO A C   
116  O O   . PRO A 16  ? 0.42248 0.37704 0.28604 0.00474  -0.00264 -0.04793 16  PRO A O   
117  C CB  . PRO A 16  ? 0.42163 0.40236 0.27963 0.00174  -0.01483 -0.03205 16  PRO A CB  
118  C CG  . PRO A 16  ? 0.42685 0.40961 0.27542 0.00640  -0.00925 -0.02601 16  PRO A CG  
119  C CD  . PRO A 16  ? 0.42157 0.41124 0.29374 0.01245  -0.00341 -0.01892 16  PRO A CD  
120  N N   . ALA A 17  ? 0.40835 0.36587 0.26391 0.01611  0.01213  -0.04097 17  ALA A N   
121  C CA  . ALA A 17  ? 0.43331 0.37472 0.27647 0.02104  0.02106  -0.04836 17  ALA A CA  
122  C C   . ALA A 17  ? 0.43562 0.37831 0.30168 0.02288  0.02380  -0.04849 17  ALA A C   
123  O O   . ALA A 17  ? 0.41636 0.34419 0.27577 0.02308  0.02500  -0.05566 17  ALA A O   
124  C CB  . ALA A 17  ? 0.41886 0.36052 0.25033 0.03045  0.03403  -0.04467 17  ALA A CB  
125  N N   . ILE A 18  ? 0.38565 0.34398 0.27706 0.02383  0.02401  -0.04044 18  ILE A N   
126  C CA  . ILE A 18  ? 0.37672 0.33773 0.28857 0.02461  0.02512  -0.03994 18  ILE A CA  
127  C C   . ILE A 18  ? 0.41711 0.37592 0.33243 0.01797  0.01580  -0.04488 18  ILE A C   
128  O O   . ILE A 18  ? 0.36590 0.31860 0.28591 0.01782  0.01692  -0.04800 18  ILE A O   
129  C CB  . ILE A 18  ? 0.43837 0.41356 0.37206 0.02543  0.02518  -0.03083 18  ILE A CB  
130  C CG1 . ILE A 18  ? 0.46085 0.44172 0.39311 0.02982  0.03318  -0.02276 18  ILE A CG1 
131  C CG2 . ILE A 18  ? 0.34419 0.32211 0.29593 0.02596  0.02613  -0.03004 18  ILE A CG2 
132  C CD1 . ILE A 18  ? 0.46163 0.45326 0.41326 0.02767  0.03048  -0.01279 18  ILE A CD1 
133  N N   . THR A 19  ? 0.33536 0.30132 0.25002 0.01274  0.00669  -0.04375 19  THR A N   
134  C CA  . THR A 19  ? 0.37798 0.34677 0.29704 0.00618  -0.00196 -0.04578 19  THR A CA  
135  C C   . THR A 19  ? 0.36467 0.31632 0.26610 0.00090  -0.00410 -0.05284 19  THR A C   
136  O O   . THR A 19  ? 0.36300 0.31149 0.27093 -0.00300 -0.00682 -0.05441 19  THR A O   
137  C CB  . THR A 19  ? 0.36403 0.34626 0.28518 0.00299  -0.01047 -0.04117 19  THR A CB  
138  O OG1 . THR A 19  ? 0.34822 0.34071 0.28407 0.00878  -0.00888 -0.03548 19  THR A OG1 
139  C CG2 . THR A 19  ? 0.32841 0.31894 0.25631 -0.00388 -0.01901 -0.04045 19  THR A CG2 
140  N N   . ALA A 20  ? 0.38096 0.31933 0.25795 0.00056  -0.00321 -0.05709 20  ALA A N   
141  C CA  . ALA A 20  ? 0.43800 0.35268 0.29207 -0.00427 -0.00591 -0.06559 20  ALA A CA  
142  C C   . ALA A 20  ? 0.41766 0.31701 0.27355 0.00239  0.00327  -0.06945 20  ALA A C   
143  O O   . ALA A 20  ? 0.43364 0.31715 0.28454 -0.00300 -0.00117 -0.07382 20  ALA A O   
144  C CB  . ALA A 20  ? 0.42298 0.32412 0.24583 -0.00367 -0.00527 -0.07032 20  ALA A CB  
145  N N   . GLY A 21  ? 0.44129 0.34610 0.30576 0.01367  0.01548  -0.06619 21  GLY A N   
146  C CA  . GLY A 21  ? 0.40451 0.29894 0.27391 0.02142  0.02465  -0.06736 21  GLY A CA  
147  C C   . GLY A 21  ? 0.37915 0.28197 0.27240 0.01712  0.02018  -0.06385 21  GLY A C   
148  O O   . GLY A 21  ? 0.37622 0.26412 0.26836 0.01813  0.02175  -0.06642 21  GLY A O   
149  N N   . PHE A 22  ? 0.31915 0.24463 0.23252 0.01311  0.01479  -0.05774 22  PHE A N   
150  C CA  . PHE A 22  ? 0.33259 0.26807 0.26628 0.00991  0.01113  -0.05410 22  PHE A CA  
151  C C   . PHE A 22  ? 0.35296 0.28125 0.28174 -0.00017 0.00167  -0.05648 22  PHE A C   
152  O O   . PHE A 22  ? 0.33686 0.26231 0.27448 -0.00217 0.00086  -0.05493 22  PHE A O   
153  C CB  . PHE A 22  ? 0.28156 0.23946 0.23261 0.00997  0.00838  -0.04823 22  PHE A CB  
154  C CG  . PHE A 22  ? 0.26605 0.23507 0.23475 0.00841  0.00577  -0.04470 22  PHE A CG  
155  C CD1 . PHE A 22  ? 0.27881 0.24333 0.25473 0.01063  0.00988  -0.04344 22  PHE A CD1 
156  C CD2 . PHE A 22  ? 0.28945 0.27415 0.26667 0.00615  -0.00011 -0.04187 22  PHE A CD2 
157  C CE1 . PHE A 22  ? 0.25777 0.23353 0.24799 0.00901  0.00729  -0.03952 22  PHE A CE1 
158  C CE2 . PHE A 22  ? 0.28554 0.28084 0.27567 0.00602  -0.00146 -0.03875 22  PHE A CE2 
159  C CZ  . PHE A 22  ? 0.29336 0.28438 0.28948 0.00668  0.00182  -0.03761 22  PHE A CZ  
160  N N   . LEU A 23  ? 0.34596 0.27247 0.26148 -0.00767 -0.00640 -0.05860 23  LEU A N   
161  C CA  . LEU A 23  ? 0.39567 0.31638 0.30697 -0.01986 -0.01723 -0.05892 23  LEU A CA  
162  C C   . LEU A 23  ? 0.40480 0.29311 0.29791 -0.02149 -0.01644 -0.06583 23  LEU A C   
163  O O   . LEU A 23  ? 0.42688 0.30858 0.32460 -0.02949 -0.02252 -0.06400 23  LEU A O   
164  C CB  . LEU A 23  ? 0.38648 0.31371 0.28737 -0.02836 -0.02722 -0.05824 23  LEU A CB  
165  C CG  . LEU A 23  ? 0.44371 0.40063 0.36093 -0.02581 -0.02875 -0.05077 23  LEU A CG  
166  C CD1 . LEU A 23  ? 0.43828 0.39997 0.34310 -0.03320 -0.03822 -0.04929 23  LEU A CD1 
167  C CD2 . LEU A 23  ? 0.35161 0.33105 0.29326 -0.02715 -0.03113 -0.04305 23  LEU A CD2 
168  N N   . ARG A 24  ? 0.40956 0.27643 0.28091 -0.01326 -0.00864 -0.07319 24  ARG A N   
169  C CA  . ARG A 24  ? 0.46438 0.29619 0.31578 -0.01076 -0.00564 -0.08067 24  ARG A CA  
170  C C   . ARG A 24  ? 0.45151 0.28428 0.32276 -0.00373 0.00162  -0.07618 24  ARG A C   
171  O O   . ARG A 24  ? 0.49758 0.30805 0.36374 -0.00741 -0.00158 -0.07793 24  ARG A O   
172  C CB  . ARG A 24  ? 0.52975 0.34200 0.35369 0.00065  0.00429  -0.08860 24  ARG A CB  
173  C CG  . ARG A 24  ? 0.63692 0.41122 0.43904 0.00903  0.01129  -0.09666 24  ARG A CG  
174  C CD  . ARG A 24  ? 0.76014 0.51337 0.52812 0.02012  0.02037  -0.10556 24  ARG A CD  
175  N NE  . ARG A 24  ? 0.75011 0.51328 0.52747 0.03958  0.03887  -0.10139 24  ARG A NE  
176  C CZ  . ARG A 24  ? 0.86064 0.60632 0.63707 0.05300  0.04991  -0.10223 24  ARG A CZ  
177  N NH1 . ARG A 24  ? 0.83286 0.54576 0.59761 0.04959  0.04458  -0.10816 24  ARG A NH1 
178  N NH2 . ARG A 24  ? 0.81731 0.57943 0.60599 0.07010  0.06635  -0.09541 24  ARG A NH2 
179  N N   . PHE A 25  ? 0.40848 0.26608 0.30202 0.00546  0.01025  -0.06956 25  PHE A N   
180  C CA  . PHE A 25  ? 0.42795 0.29133 0.34201 0.01115  0.01578  -0.06349 25  PHE A CA  
181  C C   . PHE A 25  ? 0.42705 0.29944 0.35642 -0.00020 0.00587  -0.05818 25  PHE A C   
182  O O   . PHE A 25  ? 0.40680 0.26745 0.34080 -0.00019 0.00621  -0.05582 25  PHE A O   
183  C CB  . PHE A 25  ? 0.37000 0.26001 0.30379 0.01961  0.02352  -0.05671 25  PHE A CB  
184  C CG  . PHE A 25  ? 0.33368 0.23649 0.29075 0.02258  0.02607  -0.04877 25  PHE A CG  
185  C CD1 . PHE A 25  ? 0.40671 0.29981 0.36650 0.03299  0.03535  -0.04622 25  PHE A CD1 
186  C CD2 . PHE A 25  ? 0.32271 0.24807 0.29787 0.01615  0.01960  -0.04324 25  PHE A CD2 
187  C CE1 . PHE A 25  ? 0.33738 0.24431 0.31894 0.03504  0.03659  -0.03743 25  PHE A CE1 
188  C CE2 . PHE A 25  ? 0.35120 0.28821 0.34467 0.01829  0.02110  -0.03600 25  PHE A CE2 
189  C CZ  . PHE A 25  ? 0.32390 0.25245 0.32132 0.02684  0.02888  -0.03264 25  PHE A CZ  
190  N N   . LEU A 26  ? 0.36055 0.25495 0.29833 -0.00903 -0.00242 -0.05492 26  LEU A N   
191  C CA  . LEU A 26  ? 0.38072 0.28916 0.33387 -0.01881 -0.01058 -0.04793 26  LEU A CA  
192  C C   . LEU A 26  ? 0.39929 0.28435 0.33979 -0.03073 -0.01980 -0.04954 26  LEU A C   
193  O O   . LEU A 26  ? 0.40577 0.29188 0.35741 -0.03681 -0.02373 -0.04310 26  LEU A O   
194  C CB  . LEU A 26  ? 0.31599 0.25381 0.27957 -0.02271 -0.01572 -0.04353 26  LEU A CB  
195  C CG  . LEU A 26  ? 0.28058 0.23997 0.25785 -0.01307 -0.00928 -0.04083 26  LEU A CG  
196  C CD1 . LEU A 26  ? 0.28346 0.26535 0.26622 -0.01497 -0.01410 -0.03768 26  LEU A CD1 
197  C CD2 . LEU A 26  ? 0.24894 0.21765 0.24230 -0.00994 -0.00604 -0.03529 26  LEU A CD2 
198  N N   . GLN A 27  ? 0.42902 0.29164 0.34484 -0.03517 -0.02425 -0.05758 27  GLN A N   
199  C CA  . GLN A 27  ? 0.49260 0.32810 0.39214 -0.04894 -0.03567 -0.05998 27  GLN A CA  
200  C C   . GLN A 27  ? 0.50571 0.30289 0.39182 -0.04347 -0.03095 -0.06518 27  GLN A C   
201  O O   . GLN A 27  ? 0.60170 0.37573 0.48016 -0.05543 -0.04084 -0.06451 27  GLN A O   
202  C CB  . GLN A 27  ? 0.59922 0.42154 0.47281 -0.05621 -0.04349 -0.06746 27  GLN A CB  
203  C CG  . GLN A 27  ? 0.64071 0.49442 0.52634 -0.06918 -0.05527 -0.05931 27  GLN A CG  
204  C CD  . GLN A 27  ? 0.75925 0.61468 0.62703 -0.06886 -0.05743 -0.06451 27  GLN A CD  
205  O OE1 . GLN A 27  ? 0.76097 0.64869 0.64296 -0.07068 -0.06068 -0.05738 27  GLN A OE1 
206  N NE2 . GLN A 27  ? 0.80528 0.62557 0.64060 -0.06526 -0.05506 -0.07654 27  GLN A NE2 
207  N N   . GLY A 28  ? 0.48345 0.27363 0.36737 -0.02573 -0.01640 -0.06898 28  GLY A N   
208  C CA  . GLY A 28  ? 0.54385 0.29735 0.41409 -0.01683 -0.00998 -0.07356 28  GLY A CA  
209  C C   . GLY A 28  ? 0.52355 0.29048 0.41912 -0.00619 -0.00064 -0.06457 28  GLY A C   
210  O O   . GLY A 28  ? 0.57074 0.33631 0.47921 -0.01334 -0.00626 -0.05720 28  GLY A O   
211  N N   . GLU A 29  ? 0.52210 0.30383 0.42555 0.00991  0.01287  -0.06354 29  GLU A N   
212  C CA  . GLU A 29  ? 0.55970 0.35373 0.48567 0.02073  0.02165  -0.05437 29  GLU A CA  
213  C C   . GLU A 29  ? 0.47177 0.29671 0.42527 0.01095  0.01457  -0.04333 29  GLU A C   
214  O O   . GLU A 29  ? 0.46078 0.28378 0.42689 0.01164  0.01459  -0.03566 29  GLU A O   
215  C CB  . GLU A 29  ? 0.52727 0.33983 0.46006 0.03599  0.03480  -0.05270 29  GLU A CB  
216  C CG  . GLU A 29  ? 0.58763 0.41703 0.54514 0.04632  0.04278  -0.04140 29  GLU A CG  
217  C CD  . GLU A 29  ? 0.64919 0.45016 0.59755 0.06162  0.05314  -0.04170 29  GLU A CD  
218  O OE1 . GLU A 29  ? 0.71197 0.48619 0.63415 0.07043  0.05972  -0.05130 29  GLU A OE1 
219  O OE2 . GLU A 29  ? 0.70790 0.51298 0.67406 0.06596  0.05510  -0.03201 29  GLU A OE2 
220  N N   . ALA A 30  ? 0.45753 0.31095 0.41943 0.00305  0.00904  -0.04194 30  ALA A N   
221  C CA  . ALA A 30  ? 0.38130 0.26604 0.36662 -0.00265 0.00480  -0.03214 30  ALA A CA  
222  C C   . ALA A 30  ? 0.40053 0.27933 0.39031 -0.01433 -0.00402 -0.02606 30  ALA A C   
223  O O   . ALA A 30  ? 0.34084 0.23857 0.34876 -0.01544 -0.00458 -0.01629 30  ALA A O   
224  C CB  . ALA A 30  ? 0.37983 0.29080 0.36888 -0.00705 0.00100  -0.03292 30  ALA A CB  
225  N N   . ARG A 31  ? 0.36872 0.22125 0.34131 -0.02408 -0.01177 -0.03084 31  ARG A N   
226  C CA  . ARG A 31  ? 0.43554 0.28265 0.41311 -0.03816 -0.02207 -0.02319 31  ARG A CA  
227  C C   . ARG A 31  ? 0.47255 0.30190 0.45601 -0.03340 -0.01871 -0.01718 31  ARG A C   
228  O O   . ARG A 31  ? 0.40138 0.23698 0.39705 -0.04349 -0.02549 -0.00642 31  ARG A O   
229  C CB  . ARG A 31  ? 0.46074 0.27946 0.41614 -0.05156 -0.03317 -0.02972 31  ARG A CB  
230  C CG  . ARG A 31  ? 0.49239 0.32753 0.44097 -0.05666 -0.03759 -0.03451 31  ARG A CG  
231  C CD  . ARG A 31  ? 0.46031 0.34062 0.43260 -0.06357 -0.04192 -0.02328 31  ARG A CD  
232  N NE  . ARG A 31  ? 0.51499 0.41045 0.48178 -0.06756 -0.04642 -0.02631 31  ARG A NE  
233  C CZ  . ARG A 31  ? 0.49729 0.39762 0.46183 -0.08356 -0.05935 -0.02201 31  ARG A CZ  
234  N NH1 . ARG A 31  ? 0.46020 0.35138 0.42765 -0.09881 -0.06987 -0.01426 31  ARG A NH1 
235  N NH2 . ARG A 31  ? 0.47162 0.38734 0.43200 -0.08510 -0.06260 -0.02392 31  ARG A NH2 
236  N N   . GLN A 32  ? 0.44893 0.25843 0.42521 -0.01773 -0.00805 -0.02211 32  GLN A N   
237  C CA  . GLN A 32  ? 0.54078 0.33193 0.52257 -0.01063 -0.00396 -0.01568 32  GLN A CA  
238  C C   . GLN A 32  ? 0.44771 0.27265 0.45512 -0.00164 0.00310  -0.00460 32  GLN A C   
239  O O   . GLN A 32  ? 0.44216 0.25831 0.45817 0.00450  0.00627  0.00356  32  GLN A O   
240  C CB  . GLN A 32  ? 0.60051 0.34982 0.55939 0.00361  0.00453  -0.02588 32  GLN A CB  
241  C CG  . GLN A 32  ? 0.62203 0.33786 0.54907 -0.00304 -0.00133 -0.04006 32  GLN A CG  
242  C CD  . GLN A 32  ? 0.77512 0.46461 0.69239 -0.02239 -0.01693 -0.03883 32  GLN A CD  
243  O OE1 . GLN A 32  ? 0.86890 0.54500 0.79462 -0.02525 -0.02002 -0.03009 32  GLN A OE1 
244  N NE2 . GLN A 32  ? 0.82930 0.51239 0.72970 -0.03690 -0.02783 -0.04596 32  GLN A NE2 
245  N N   . ALA A 33  ? 0.37045 0.23182 0.38893 -0.00113 0.00465  -0.00378 33  ALA A N   
246  C CA  . ALA A 33  ? 0.36282 0.25350 0.40125 0.00644  0.00989  0.00519  33  ALA A CA  
247  C C   . ALA A 33  ? 0.40796 0.32064 0.46207 -0.00268 0.00337  0.01727  33  ALA A C   
248  O O   . ALA A 33  ? 0.34328 0.26021 0.39614 -0.01524 -0.00465 0.01900  33  ALA A O   
249  C CB  . ALA A 33  ? 0.31730 0.23271 0.35773 0.00992  0.01292  0.00057  33  ALA A CB  
250  N N   . ASP A 34  ? 0.31788 0.24694 0.38719 0.00372  0.00684  0.02717  34  ASP A N   
251  C CA  . ASP A 34  ? 0.29755 0.25301 0.38002 -0.00330 0.00176  0.03871  34  ASP A CA  
252  C C   . ASP A 34  ? 0.29915 0.28470 0.38204 -0.00674 -0.00037 0.03555  34  ASP A C   
253  O O   . ASP A 34  ? 0.30735 0.31240 0.39444 -0.01413 -0.00494 0.04180  34  ASP A O   
254  C CB  . ASP A 34  ? 0.29074 0.25572 0.38733 0.00441  0.00516  0.05033  34  ASP A CB  
255  C CG  . ASP A 34  ? 0.31269 0.24828 0.41044 0.00915  0.00734  0.05608  34  ASP A CG  
256  O OD1 . ASP A 34  ? 0.35869 0.27350 0.45045 0.00064  0.00210  0.05703  34  ASP A OD1 
257  O OD2 . ASP A 34  ? 0.36250 0.29550 0.46746 0.02144  0.01395  0.06064  34  ASP A OD2 
258  N N   . ALA A 35  ? 0.26311 0.25229 0.34126 -0.00064 0.00336  0.02677  35  ALA A N   
259  C CA  . ALA A 35  ? 0.24328 0.25481 0.31936 -0.00191 0.00166  0.02257  35  ALA A CA  
260  C C   . ALA A 35  ? 0.26992 0.27422 0.33891 0.00383  0.00552  0.01272  35  ALA A C   
261  O O   . ALA A 35  ? 0.23440 0.22460 0.30343 0.01054  0.01080  0.01178  35  ALA A O   
262  C CB  . ALA A 35  ? 0.22933 0.26469 0.31329 -0.00050 0.00046  0.03008  35  ALA A CB  
263  N N   . LEU A 36  ? 0.21880 0.23383 0.28197 0.00218  0.00351  0.00662  36  LEU A N   
264  C CA  . LEU A 36  ? 0.23816 0.24879 0.29494 0.00644  0.00620  -0.00123 36  LEU A CA  
265  C C   . LEU A 36  ? 0.24613 0.27403 0.30377 0.00753  0.00402  -0.00172 36  LEU A C   
266  O O   . LEU A 36  ? 0.25425 0.29377 0.30881 0.00525  0.00067  -0.00238 36  LEU A O   
267  C CB  . LEU A 36  ? 0.24422 0.24436 0.28964 0.00318  0.00482  -0.00894 36  LEU A CB  
268  C CG  . LEU A 36  ? 0.27063 0.26882 0.30872 0.00685  0.00690  -0.01593 36  LEU A CG  
269  C CD1 . LEU A 36  ? 0.24476 0.23272 0.28333 0.01382  0.01359  -0.01593 36  LEU A CD1 
270  C CD2 . LEU A 36  ? 0.24824 0.23876 0.27506 0.00254  0.00401  -0.02186 36  LEU A CD2 
271  N N   . TYR A 37  ? 0.21365 0.24263 0.27477 0.01119  0.00579  -0.00076 37  TYR A N   
272  C CA  . TYR A 37  ? 0.20685 0.24580 0.26606 0.01081  0.00201  -0.00185 37  TYR A CA  
273  C C   . TYR A 37  ? 0.21114 0.24321 0.26527 0.01245  0.00336  -0.00739 37  TYR A C   
274  O O   . TYR A 37  ? 0.19225 0.21843 0.25014 0.01525  0.00816  -0.00575 37  TYR A O   
275  C CB  . TYR A 37  ? 0.20940 0.25749 0.27805 0.01049  -0.00000 0.00652  37  TYR A CB  
276  C CG  . TYR A 37  ? 0.22317 0.28105 0.29524 0.00846  -0.00270 0.01305  37  TYR A CG  
277  C CD1 . TYR A 37  ? 0.23004 0.28505 0.31044 0.00935  0.00044  0.01964  37  TYR A CD1 
278  C CD2 . TYR A 37  ? 0.22449 0.29263 0.28938 0.00611  -0.00842 0.01284  37  TYR A CD2 
279  C CE1 . TYR A 37  ? 0.21751 0.28256 0.30182 0.00699  -0.00224 0.02753  37  TYR A CE1 
280  C CE2 . TYR A 37  ? 0.25491 0.33399 0.32143 0.00452  -0.01045 0.01979  37  TYR A CE2 
281  C CZ  . TYR A 37  ? 0.26265 0.34166 0.34034 0.00448  -0.00745 0.02800  37  TYR A CZ  
282  O OH  . TYR A 37  ? 0.24395 0.33489 0.32401 0.00239  -0.00969 0.03675  37  TYR A OH  
283  N N   . ILE A 38  ? 0.22426 0.25736 0.26952 0.01184  -0.00018 -0.01301 38  ILE A N   
284  C CA  . ILE A 38  ? 0.20941 0.23611 0.24956 0.01282  -0.00014 -0.01706 38  ILE A CA  
285  C C   . ILE A 38  ? 0.21643 0.24482 0.25481 0.01097  -0.00595 -0.01620 38  ILE A C   
286  O O   . ILE A 38  ? 0.21098 0.23970 0.24019 0.01148  -0.01023 -0.02008 38  ILE A O   
287  C CB  . ILE A 38  ? 0.23407 0.25771 0.26495 0.01393  -0.00037 -0.02332 38  ILE A CB  
288  C CG1 . ILE A 38  ? 0.22029 0.24108 0.25132 0.01264  0.00239  -0.02363 38  ILE A CG1 
289  C CG2 . ILE A 38  ? 0.24210 0.25880 0.26811 0.01506  -0.00028 -0.02595 38  ILE A CG2 
290  C CD1 . ILE A 38  ? 0.24753 0.26851 0.27140 0.01190  0.00072  -0.02752 38  ILE A CD1 
291  N N   . LEU A 39  ? 0.20885 0.19765 0.20783 0.01828  -0.02866 -0.01751 39  LEU A N   
292  C CA  . LEU A 39  ? 0.20371 0.19391 0.20387 0.01904  -0.03304 -0.02125 39  LEU A CA  
293  C C   . LEU A 39  ? 0.23575 0.22247 0.23778 0.01730  -0.03238 -0.02489 39  LEU A C   
294  O O   . LEU A 39  ? 0.26347 0.24976 0.27375 0.01587  -0.03414 -0.02762 39  LEU A O   
295  C CB  . LEU A 39  ? 0.19090 0.18358 0.20017 0.01874  -0.03557 -0.02120 39  LEU A CB  
296  C CG  . LEU A 39  ? 0.25825 0.25402 0.26679 0.02108  -0.03627 -0.01698 39  LEU A CG  
297  C CD1 . LEU A 39  ? 0.22072 0.21988 0.23942 0.02140  -0.03985 -0.01742 39  LEU A CD1 
298  C CD2 . LEU A 39  ? 0.21630 0.21432 0.21366 0.02499  -0.03838 -0.01557 39  LEU A CD2 
299  N N   . GLY A 40  ? 0.23743 0.22172 0.23367 0.01748  -0.02972 -0.02464 40  GLY A N   
300  C CA  . GLY A 40  ? 0.22274 0.20340 0.21987 0.01683  -0.02921 -0.02762 40  GLY A CA  
301  C C   . GLY A 40  ? 0.25127 0.22798 0.25206 0.01502  -0.02471 -0.02588 40  GLY A C   
302  O O   . GLY A 40  ? 0.23415 0.21065 0.23839 0.01399  -0.02249 -0.02370 40  GLY A O   
303  N N   . ASP A 41  ? 0.23024 0.20330 0.22934 0.01538  -0.02306 -0.02676 41  ASP A N   
304  C CA  . ASP A 41  ? 0.23687 0.20556 0.23686 0.01499  -0.01855 -0.02449 41  ASP A CA  
305  C C   . ASP A 41  ? 0.26457 0.23393 0.25867 0.01566  -0.01683 -0.02162 41  ASP A C   
306  O O   . ASP A 41  ? 0.24957 0.21630 0.24380 0.01561  -0.01367 -0.01984 41  ASP A O   
307  C CB  . ASP A 41  ? 0.24494 0.21135 0.25505 0.01321  -0.01621 -0.02421 41  ASP A CB  
308  C CG  . ASP A 41  ? 0.30749 0.27150 0.32585 0.01216  -0.01739 -0.02731 41  ASP A CG  
309  O OD1 . ASP A 41  ? 0.28322 0.24690 0.29763 0.01320  -0.02047 -0.03044 41  ASP A OD1 
310  O OD2 . ASP A 41  ? 0.27925 0.24150 0.30906 0.01039  -0.01499 -0.02680 41  ASP A OD2 
311  N N   . LEU A 42  ? 0.23723 0.20998 0.22652 0.01654  -0.01880 -0.02137 42  LEU A N   
312  C CA  . LEU A 42  ? 0.25192 0.22521 0.23755 0.01689  -0.01820 -0.01967 42  LEU A CA  
313  C C   . LEU A 42  ? 0.26712 0.23723 0.24858 0.01848  -0.01674 -0.01895 42  LEU A C   
314  O O   . LEU A 42  ? 0.25477 0.22293 0.23290 0.01909  -0.01587 -0.01821 42  LEU A O   
315  C CB  . LEU A 42  ? 0.25635 0.23431 0.24105 0.01731  -0.02001 -0.01901 42  LEU A CB  
316  C CG  . LEU A 42  ? 0.31035 0.28982 0.29479 0.01711  -0.02047 -0.01795 42  LEU A CG  
317  C CD1 . LEU A 42  ? 0.26237 0.23971 0.24812 0.01574  -0.02018 -0.01824 42  LEU A CD1 
318  C CD2 . LEU A 42  ? 0.25419 0.23858 0.24101 0.01742  -0.02092 -0.01632 42  LEU A CD2 
319  N N   . PHE A 43  ? 0.26840 0.23751 0.24923 0.01979  -0.01655 -0.01927 43  PHE A N   
320  C CA  . PHE A 43  ? 0.26163 0.22752 0.23881 0.02208  -0.01503 -0.01778 43  PHE A CA  
321  C C   . PHE A 43  ? 0.24930 0.20960 0.22955 0.02223  -0.01179 -0.01733 43  PHE A C   
322  O O   . PHE A 43  ? 0.23207 0.19191 0.21824 0.02057  -0.01218 -0.01953 43  PHE A O   
323  C CB  . PHE A 43  ? 0.27254 0.24132 0.24833 0.02404  -0.01661 -0.01777 43  PHE A CB  
324  C CG  . PHE A 43  ? 0.26535 0.23991 0.24127 0.02381  -0.01911 -0.01745 43  PHE A CG  
325  C CD1 . PHE A 43  ? 0.29361 0.26921 0.26734 0.02492  -0.02083 -0.01659 43  PHE A CD1 
326  C CD2 . PHE A 43  ? 0.25264 0.23149 0.23138 0.02275  -0.01982 -0.01793 43  PHE A CD2 
327  C CE1 . PHE A 43  ? 0.29004 0.27105 0.26731 0.02407  -0.02354 -0.01679 43  PHE A CE1 
328  C CE2 . PHE A 43  ? 0.26423 0.24812 0.24590 0.02227  -0.02107 -0.01681 43  PHE A CE2 
329  C CZ  . PHE A 43  ? 0.25345 0.23851 0.23585 0.02246  -0.02310 -0.01653 43  PHE A CZ  
330  N N   . GLU A 44  ? 0.25843 0.21437 0.23497 0.02451  -0.00873 -0.01441 44  GLU A N   
331  C CA  . GLU A 44  ? 0.31199 0.26186 0.29294 0.02496  -0.00429 -0.01263 44  GLU A CA  
332  C C   . GLU A 44  ? 0.34709 0.29522 0.33148 0.02560  -0.00492 -0.01407 44  GLU A C   
333  O O   . GLU A 44  ? 0.29278 0.23646 0.28519 0.02440  -0.00267 -0.01477 44  GLU A O   
334  C CB  . GLU A 44  ? 0.32917 0.27447 0.30310 0.02855  -0.00009 -0.00793 44  GLU A CB  
335  C CG  . GLU A 44  ? 0.37362 0.31182 0.35209 0.02997  0.00597  -0.00419 44  GLU A CG  
336  C CD  . GLU A 44  ? 0.40214 0.33813 0.39267 0.02662  0.00987  -0.00428 44  GLU A CD  
337  O OE1 . GLU A 44  ? 0.40471 0.34458 0.39815 0.02400  0.00825  -0.00657 44  GLU A OE1 
338  O OE2 . GLU A 44  ? 0.38435 0.31476 0.38314 0.02666  0.01466  -0.00181 44  GLU A OE2 
339  N N   . ALA A 45  ? 0.31115 0.26260 0.29101 0.02751  -0.00781 -0.01481 45  ALA A N   
340  C CA  . ALA A 45  ? 0.28695 0.23645 0.26906 0.02900  -0.00792 -0.01642 45  ALA A CA  
341  C C   . ALA A 45  ? 0.32626 0.28212 0.30512 0.03016  -0.01124 -0.01810 45  ALA A C   
342  O O   . ALA A 45  ? 0.29074 0.25196 0.26647 0.03021  -0.01314 -0.01683 45  ALA A O   
343  C CB  . ALA A 45  ? 0.32762 0.27141 0.30844 0.03262  -0.00437 -0.01233 45  ALA A CB  
344  N N   . TRP A 46  ? 0.29062 0.24549 0.27099 0.03127  -0.01154 -0.02111 46  TRP A N   
345  C CA  . TRP A 46  ? 0.29865 0.25905 0.27637 0.03339  -0.01289 -0.02191 46  TRP A CA  
346  C C   . TRP A 46  ? 0.29582 0.25200 0.27419 0.03641  -0.01143 -0.02427 46  TRP A C   
347  O O   . TRP A 46  ? 0.30864 0.25956 0.28917 0.03544  -0.01161 -0.02854 46  TRP A O   
348  C CB  . TRP A 46  ? 0.23732 0.20275 0.21380 0.03151  -0.01505 -0.02421 46  TRP A CB  
349  C CG  . TRP A 46  ? 0.26667 0.23905 0.24152 0.03338  -0.01511 -0.02253 46  TRP A CG  
350  C CD1 . TRP A 46  ? 0.25865 0.23281 0.23149 0.03656  -0.01385 -0.02376 46  TRP A CD1 
351  C CD2 . TRP A 46  ? 0.26508 0.24337 0.24157 0.03230  -0.01600 -0.01931 46  TRP A CD2 
352  N NE1 . TRP A 46  ? 0.24968 0.23105 0.22412 0.03744  -0.01306 -0.02049 46  TRP A NE1 
353  C CE2 . TRP A 46  ? 0.26956 0.25355 0.24724 0.03447  -0.01486 -0.01805 46  TRP A CE2 
354  C CE3 . TRP A 46  ? 0.29649 0.27539 0.27390 0.02994  -0.01750 -0.01773 46  TRP A CE3 
355  C CZ2 . TRP A 46  ? 0.30194 0.29252 0.28443 0.03357  -0.01543 -0.01511 46  TRP A CZ2 
356  C CZ3 . TRP A 46  ? 0.27517 0.25996 0.25555 0.02926  -0.01894 -0.01592 46  TRP A CZ3 
357  C CH2 . TRP A 46  ? 0.27562 0.26634 0.25983 0.03068  -0.01803 -0.01455 46  TRP A CH2 
358  N N   . ILE A 47  ? 0.29199 0.25046 0.26956 0.04017  -0.01030 -0.02195 47  ILE A N   
359  C CA  . ILE A 47  ? 0.27096 0.22530 0.24915 0.04394  -0.00823 -0.02389 47  ILE A CA  
360  C C   . ILE A 47  ? 0.29965 0.26021 0.27577 0.04708  -0.00760 -0.02448 47  ILE A C   
361  O O   . ILE A 47  ? 0.31780 0.27589 0.29407 0.05123  -0.00525 -0.02563 47  ILE A O   
362  C CB  . ILE A 47  ? 0.32938 0.27935 0.30993 0.04696  -0.00603 -0.01973 47  ILE A CB  
363  C CG1 . ILE A 47  ? 0.32358 0.28111 0.30344 0.04886  -0.00739 -0.01451 47  ILE A CG1 
364  C CG2 . ILE A 47  ? 0.30621 0.24851 0.28912 0.04464  -0.00469 -0.01859 47  ILE A CG2 
365  C CD1 . ILE A 47  ? 0.40807 0.36307 0.38926 0.05374  -0.00589 -0.01026 47  ILE A CD1 
366  N N   . GLY A 48  ? 0.31947 0.28764 0.29438 0.04552  -0.00884 -0.02332 48  GLY A N   
367  C CA  . GLY A 48  ? 0.28650 0.26090 0.26052 0.04854  -0.00688 -0.02268 48  GLY A CA  
368  C C   . GLY A 48  ? 0.27816 0.26173 0.25698 0.04717  -0.00755 -0.01795 48  GLY A C   
369  O O   . GLY A 48  ? 0.27075 0.25602 0.25336 0.04547  -0.00989 -0.01536 48  GLY A O   
370  N N   . ASP A 49  ? 0.26877 0.25804 0.24750 0.04827  -0.00539 -0.01686 49  ASP A N   
371  C CA  . ASP A 49  ? 0.28819 0.28600 0.27435 0.04648  -0.00559 -0.01250 49  ASP A CA  
372  C C   . ASP A 49  ? 0.34559 0.34933 0.34137 0.04874  -0.00511 -0.00910 49  ASP A C   
373  O O   . ASP A 49  ? 0.28884 0.29962 0.29360 0.04661  -0.00673 -0.00621 49  ASP A O   
374  C CB  . ASP A 49  ? 0.25749 0.25929 0.24191 0.04763  -0.00200 -0.01101 49  ASP A CB  
375  C CG  . ASP A 49  ? 0.28953 0.28753 0.26585 0.04537  -0.00379 -0.01350 49  ASP A CG  
376  O OD1 . ASP A 49  ? 0.30863 0.30186 0.28317 0.04208  -0.00770 -0.01623 49  ASP A OD1 
377  O OD2 . ASP A 49  ? 0.29585 0.29601 0.26795 0.04737  -0.00093 -0.01214 49  ASP A OD2 
378  N N   . ASP A 50  ? 0.28470 0.28593 0.28018 0.05307  -0.00324 -0.00956 50  ASP A N   
379  C CA  . ASP A 50  ? 0.28097 0.28832 0.28646 0.05588  -0.00336 -0.00614 50  ASP A CA  
380  C C   . ASP A 50  ? 0.27694 0.28254 0.28337 0.05489  -0.00873 -0.00554 50  ASP A C   
381  O O   . ASP A 50  ? 0.30240 0.31310 0.31650 0.05766  -0.01039 -0.00284 50  ASP A O   
382  C CB  . ASP A 50  ? 0.30406 0.30958 0.30909 0.06206  0.00180  -0.00639 50  ASP A CB  
383  C CG  . ASP A 50  ? 0.35870 0.35265 0.35426 0.06351  0.00208  -0.01062 50  ASP A CG  
384  O OD1 . ASP A 50  ? 0.31959 0.30740 0.30847 0.05963  -0.00055 -0.01361 50  ASP A OD1 
385  O OD2 . ASP A 50  ? 0.37304 0.36394 0.36943 0.06856  0.00517  -0.01096 50  ASP A OD2 
386  N N   . ASP A 51  ? 0.29057 0.28943 0.28933 0.05162  -0.01129 -0.00764 51  ASP A N   
387  C CA  . ASP A 51  ? 0.28114 0.27737 0.27787 0.05136  -0.01539 -0.00660 51  ASP A CA  
388  C C   . ASP A 51  ? 0.30121 0.30583 0.30441 0.04968  -0.02053 -0.00510 51  ASP A C   
389  O O   . ASP A 51  ? 0.25653 0.26408 0.26167 0.04553  -0.02168 -0.00618 51  ASP A O   
390  C CB  . ASP A 51  ? 0.26715 0.25491 0.25548 0.04808  -0.01545 -0.00889 51  ASP A CB  
391  C CG  . ASP A 51  ? 0.29747 0.28076 0.28139 0.04889  -0.01769 -0.00712 51  ASP A CG  
392  O OD1 . ASP A 51  ? 0.28607 0.27349 0.27165 0.05160  -0.02096 -0.00461 51  ASP A OD1 
393  O OD2 . ASP A 51  ? 0.35198 0.32766 0.33079 0.04718  -0.01608 -0.00808 51  ASP A OD2 
394  N N   . PRO A 52  ? 0.30073 0.30923 0.30791 0.05296  -0.02421 -0.00292 52  PRO A N   
395  C CA  . PRO A 52  ? 0.28644 0.30324 0.30095 0.05145  -0.03067 -0.00283 52  PRO A CA  
396  C C   . PRO A 52  ? 0.29707 0.30981 0.30262 0.04943  -0.03570 -0.00471 52  PRO A C   
397  O O   . PRO A 52  ? 0.30425 0.32269 0.31417 0.04902  -0.04238 -0.00573 52  PRO A O   
398  C CB  . PRO A 52  ? 0.27491 0.29750 0.29667 0.05689  -0.03326 -0.00002 52  PRO A CB  
399  C CG  . PRO A 52  ? 0.33764 0.35109 0.34980 0.06122  -0.02954 0.00156  52  PRO A CG  
400  C CD  . PRO A 52  ? 0.31536 0.32139 0.32210 0.05872  -0.02284 -0.00055 52  PRO A CD  
401  N N   . ASN A 53  ? 0.27882 0.28196 0.27270 0.04846  -0.03270 -0.00549 53  ASN A N   
402  C CA  . ASN A 53  ? 0.26432 0.26265 0.24867 0.04710  -0.03548 -0.00691 53  ASN A CA  
403  C C   . ASN A 53  ? 0.25297 0.25679 0.24265 0.04302  -0.04022 -0.00990 53  ASN A C   
404  O O   . ASN A 53  ? 0.25319 0.25841 0.24824 0.03884  -0.03772 -0.01105 53  ASN A O   
405  C CB  . ASN A 53  ? 0.30178 0.29092 0.27850 0.04508  -0.02998 -0.00740 53  ASN A CB  
406  C CG  . ASN A 53  ? 0.36843 0.35191 0.33514 0.04475  -0.03097 -0.00791 53  ASN A CG  
407  O OD1 . ASN A 53  ? 0.33631 0.32237 0.30014 0.04544  -0.03622 -0.00913 53  ASN A OD1 
408  N ND2 . ASN A 53  ? 0.31760 0.29326 0.27952 0.04392  -0.02585 -0.00727 53  ASN A ND2 
409  N N   . PRO A 54  ? 0.28674 0.29340 0.27509 0.04448  -0.04732 -0.01137 54  PRO A N   
410  C CA  . PRO A 54  ? 0.27330 0.28492 0.26935 0.04041  -0.05253 -0.01514 54  PRO A CA  
411  C C   . PRO A 54  ? 0.28275 0.28859 0.27393 0.03605  -0.04985 -0.01752 54  PRO A C   
412  O O   . PRO A 54  ? 0.25406 0.26336 0.25501 0.03175  -0.05102 -0.01953 54  PRO A O   
413  C CB  . PRO A 54  ? 0.32114 0.33458 0.31228 0.04407  -0.06142 -0.01729 54  PRO A CB  
414  C CG  . PRO A 54  ? 0.30890 0.32274 0.29625 0.05031  -0.06099 -0.01306 54  PRO A CG  
415  C CD  . PRO A 54  ? 0.29522 0.30108 0.27588 0.05049  -0.05146 -0.00972 54  PRO A CD  
416  N N   . LEU A 55  ? 0.28716 0.28436 0.26512 0.03718  -0.04584 -0.01686 55  LEU A N   
417  C CA  . LEU A 55  ? 0.31750 0.30974 0.29233 0.03343  -0.04275 -0.01863 55  LEU A CA  
418  C C   . LEU A 55  ? 0.32456 0.31966 0.30930 0.02947  -0.03878 -0.01783 55  LEU A C   
419  O O   . LEU A 55  ? 0.28579 0.28083 0.27427 0.02587  -0.03865 -0.01946 55  LEU A O   
420  C CB  . LEU A 55  ? 0.29360 0.27718 0.25623 0.03546  -0.03781 -0.01694 55  LEU A CB  
421  C CG  . LEU A 55  ? 0.33801 0.31699 0.29918 0.03200  -0.03385 -0.01810 55  LEU A CG  
422  C CD1 . LEU A 55  ? 0.31750 0.29538 0.27573 0.03093  -0.03745 -0.02183 55  LEU A CD1 
423  C CD2 . LEU A 55  ? 0.34368 0.31543 0.29770 0.03372  -0.02806 -0.01559 55  LEU A CD2 
424  N N   . HIS A 56  ? 0.26904 0.26622 0.25730 0.03079  -0.03533 -0.01522 56  HIS A N   
425  C CA  . HIS A 56  ? 0.25624 0.25590 0.25099 0.02850  -0.03134 -0.01423 56  HIS A CA  
426  C C   . HIS A 56  ? 0.27369 0.28048 0.28085 0.02600  -0.03323 -0.01410 56  HIS A C   
427  O O   . HIS A 56  ? 0.26868 0.27577 0.27953 0.02321  -0.03082 -0.01361 56  HIS A O   
428  C CB  . HIS A 56  ? 0.25823 0.25846 0.25316 0.03151  -0.02763 -0.01224 56  HIS A CB  
429  C CG  . HIS A 56  ? 0.28256 0.27507 0.26844 0.03327  -0.02510 -0.01247 56  HIS A CG  
430  N ND1 . HIS A 56  ? 0.27913 0.26976 0.26432 0.03583  -0.02176 -0.01192 56  HIS A ND1 
431  C CD2 . HIS A 56  ? 0.26563 0.25154 0.24421 0.03288  -0.02491 -0.01312 56  HIS A CD2 
432  C CE1 . HIS A 56  ? 0.28914 0.27222 0.26847 0.03638  -0.02011 -0.01243 56  HIS A CE1 
433  N NE2 . HIS A 56  ? 0.26215 0.24260 0.23775 0.03466  -0.02152 -0.01262 56  HIS A NE2 
434  N N   . GLN A 57  ? 0.27074 0.28347 0.28582 0.02711  -0.03755 -0.01417 57  GLN A N   
435  C CA  . GLN A 57  ? 0.29367 0.31364 0.32454 0.02432  -0.03922 -0.01390 57  GLN A CA  
436  C C   . GLN A 57  ? 0.28308 0.30062 0.31549 0.02058  -0.04331 -0.01756 57  GLN A C   
437  O O   . GLN A 57  ? 0.27622 0.29635 0.32037 0.01713  -0.04205 -0.01689 57  GLN A O   
438  C CB  . GLN A 57  ? 0.30348 0.33144 0.34515 0.02652  -0.04350 -0.01334 57  GLN A CB  
439  C CG  . GLN A 57  ? 0.40093 0.43372 0.44840 0.02965  -0.03801 -0.00902 57  GLN A CG  
440  C CD  . GLN A 57  ? 0.53895 0.56477 0.57240 0.03215  -0.03183 -0.00780 57  GLN A CD  
441  O OE1 . GLN A 57  ? 0.52196 0.54667 0.55444 0.03148  -0.02596 -0.00623 57  GLN A OE1 
442  N NE2 . GLN A 57  ? 0.51826 0.53916 0.54106 0.03536  -0.03332 -0.00854 57  GLN A NE2 
443  N N   . GLN A 58  ? 0.28367 0.29563 0.30425 0.02169  -0.04755 -0.02118 58  GLN A N   
444  C CA  . GLN A 58  ? 0.32200 0.33015 0.34182 0.01891  -0.05099 -0.02549 58  GLN A CA  
445  C C   . GLN A 58  ? 0.31633 0.31955 0.33387 0.01631  -0.04509 -0.02425 58  GLN A C   
446  O O   . GLN A 58  ? 0.25854 0.26138 0.28435 0.01291  -0.04552 -0.02561 58  GLN A O   
447  C CB  . GLN A 58  ? 0.33797 0.34069 0.34259 0.02219  -0.05566 -0.02919 58  GLN A CB  
448  C CG  . GLN A 58  ? 0.43643 0.44409 0.44191 0.02564  -0.06309 -0.03070 58  GLN A CG  
449  C CD  . GLN A 58  ? 0.45725 0.45879 0.44345 0.03082  -0.06577 -0.03229 58  GLN A CD  
450  O OE1 . GLN A 58  ? 0.51249 0.50609 0.48575 0.03167  -0.06092 -0.03178 58  GLN A OE1 
451  N NE2 . GLN A 58  ? 0.46909 0.47458 0.45370 0.03480  -0.07331 -0.03375 58  GLN A NE2 
452  N N   . ILE A 59  ? 0.25553 0.25493 0.26312 0.01795  -0.03990 -0.02177 59  ILE A N   
453  C CA  . ILE A 59  ? 0.29018 0.28597 0.29616 0.01604  -0.03521 -0.02054 59  ILE A CA  
454  C C   . ILE A 59  ? 0.26032 0.26101 0.27752 0.01429  -0.03192 -0.01702 59  ILE A C   
455  O O   . ILE A 59  ? 0.27004 0.26938 0.29152 0.01202  -0.03018 -0.01628 59  ILE A O   
456  C CB  . ILE A 59  ? 0.29278 0.28414 0.28788 0.01813  -0.03152 -0.01933 59  ILE A CB  
457  C CG1 . ILE A 59  ? 0.24859 0.23412 0.23310 0.01999  -0.03288 -0.02154 59  ILE A CG1 
458  C CG2 . ILE A 59  ? 0.27030 0.25987 0.26570 0.01654  -0.02772 -0.01796 59  ILE A CG2 
459  C CD1 . ILE A 59  ? 0.26995 0.25173 0.25283 0.01856  -0.03449 -0.02468 59  ILE A CD1 
460  N N   . ALA A 60  ? 0.26421 0.27037 0.28612 0.01597  -0.03031 -0.01423 60  ALA A N   
461  C CA  . ALA A 60  ? 0.26587 0.27663 0.29710 0.01549  -0.02573 -0.00989 60  ALA A CA  
462  C C   . ALA A 60  ? 0.27745 0.29120 0.32405 0.01203  -0.02707 -0.00951 60  ALA A C   
463  O O   . ALA A 60  ? 0.24384 0.25753 0.29597 0.01070  -0.02296 -0.00612 60  ALA A O   
464  C CB  . ALA A 60  ? 0.22848 0.24447 0.26213 0.01867  -0.02328 -0.00722 60  ALA A CB  
465  N N   A SER A 61  ? 0.26836 0.28454 0.32251 0.01078  -0.03312 -0.01301 61  SER A N   
466  N N   B SER A 61  ? 0.27053 0.28668 0.32466 0.01077  -0.03312 -0.01303 61  SER A N   
467  N N   C SER A 61  ? 0.26847 0.28465 0.32264 0.01077  -0.03311 -0.01301 61  SER A N   
468  C CA  A SER A 61  ? 0.27635 0.29506 0.34777 0.00694  -0.03549 -0.01393 61  SER A CA  
469  C CA  B SER A 61  ? 0.27335 0.29207 0.34482 0.00694  -0.03543 -0.01388 61  SER A CA  
470  C CA  C SER A 61  ? 0.27313 0.29186 0.34462 0.00694  -0.03543 -0.01388 61  SER A CA  
471  C C   A SER A 61  ? 0.27813 0.28965 0.34690 0.00434  -0.03592 -0.01646 61  SER A C   
472  C C   B SER A 61  ? 0.27801 0.28954 0.34689 0.00431  -0.03603 -0.01654 61  SER A C   
473  C C   C SER A 61  ? 0.27804 0.28959 0.34697 0.00430  -0.03610 -0.01659 61  SER A C   
474  O O   A SER A 61  ? 0.25529 0.26698 0.33739 0.00141  -0.03364 -0.01444 61  SER A O   
475  O O   B SER A 61  ? 0.25689 0.26860 0.33932 0.00132  -0.03396 -0.01470 61  SER A O   
476  O O   C SER A 61  ? 0.26112 0.27291 0.34379 0.00128  -0.03415 -0.01483 61  SER A O   
477  C CB  A SER A 61  ? 0.29244 0.31523 0.37146 0.00656  -0.04385 -0.01870 61  SER A CB  
478  C CB  B SER A 61  ? 0.29332 0.31635 0.37281 0.00655  -0.04367 -0.01850 61  SER A CB  
479  C CB  C SER A 61  ? 0.29044 0.31352 0.37001 0.00656  -0.04366 -0.01847 61  SER A CB  
480  O OG  A SER A 61  ? 0.24386 0.27344 0.32574 0.00957  -0.04350 -0.01609 61  SER A OG  
481  O OG  B SER A 61  ? 0.28087 0.30578 0.37877 0.00230  -0.04717 -0.02082 61  SER A OG  
482  O OG  C SER A 61  ? 0.30109 0.31810 0.36825 0.00702  -0.05014 -0.02498 61  SER A OG  
483  N N   . ALA A 62  ? 0.28934 0.29426 0.34197 0.00566  -0.03805 -0.02035 62  ALA A N   
484  C CA  . ALA A 62  ? 0.30263 0.30056 0.35257 0.00387  -0.03808 -0.02296 62  ALA A CA  
485  C C   . ALA A 62  ? 0.28622 0.28264 0.33626 0.00371  -0.03117 -0.01747 62  ALA A C   
486  O O   . ALA A 62  ? 0.27668 0.27016 0.33441 0.00152  -0.02975 -0.01691 62  ALA A O   
487  C CB  . ALA A 62  ? 0.29461 0.28635 0.32746 0.00617  -0.04071 -0.02758 62  ALA A CB  
488  N N   . ILE A 63  ? 0.23517 0.23321 0.27657 0.00643  -0.02724 -0.01363 63  ILE A N   
489  C CA  . ILE A 63  ? 0.25857 0.25607 0.29879 0.00725  -0.02178 -0.00854 63  ILE A CA  
490  C C   . ILE A 63  ? 0.26284 0.26481 0.31709 0.00643  -0.01778 -0.00291 63  ILE A C   
491  O O   . ILE A 63  ? 0.25395 0.25413 0.31254 0.00602  -0.01417 0.00101  63  ILE A O   
492  C CB  . ILE A 63  ? 0.24145 0.23948 0.26898 0.01060  -0.01984 -0.00722 63  ILE A CB  
493  C CG1 . ILE A 63  ? 0.26127 0.25433 0.27777 0.01111  -0.02240 -0.01163 63  ILE A CG1 
494  C CG2 . ILE A 63  ? 0.27020 0.26867 0.29558 0.01238  -0.01541 -0.00228 63  ILE A CG2 
495  C CD1 . ILE A 63  ? 0.26109 0.25406 0.26801 0.01373  -0.02116 -0.01129 63  ILE A CD1 
496  N N   . LYS A 64  ? 0.23520 0.24313 0.29775 0.00654  -0.01779 -0.00173 64  LYS A N   
497  C CA  . LYS A 64  ? 0.28149 0.29425 0.35966 0.00594  -0.01269 0.00450  64  LYS A CA  
498  C C   . LYS A 64  ? 0.28662 0.29707 0.38104 0.00164  -0.01359 0.00405  64  LYS A C   
499  O O   . LYS A 64  ? 0.25637 0.26757 0.36158 0.00129  -0.00751 0.01066  64  LYS A O   
500  C CB  . LYS A 64  ? 0.24288 0.26304 0.32952 0.00673  -0.01298 0.00520  64  LYS A CB  
501  C CG  . LYS A 64  ? 0.31903 0.34515 0.42459 0.00626  -0.00664 0.01230  64  LYS A CG  
502  C CD  . LYS A 64  ? 0.32807 0.35401 0.42528 0.01058  0.00241  0.02012  64  LYS A CD  
503  C CE  . LYS A 64  ? 0.41486 0.44825 0.52222 0.01338  0.00962  0.02684  64  LYS A CE  
504  N NZ  . LYS A 64  ? 0.38246 0.41774 0.50867 0.01192  0.01681  0.03471  64  LYS A NZ  
505  N N   . ALA A 65  ? 0.24849 0.25546 0.34441 -0.00119 -0.02082 -0.00363 65  ALA A N   
506  C CA  . ALA A 65  ? 0.25025 0.25347 0.36112 -0.00527 -0.02247 -0.00576 65  ALA A CA  
507  C C   . ALA A 65  ? 0.27477 0.27136 0.38095 -0.00478 -0.01795 -0.00263 65  ALA A C   
508  O O   . ALA A 65  ? 0.26454 0.25902 0.38569 -0.00702 -0.01467 0.00073  65  ALA A O   
509  C CB  . ALA A 65  ? 0.28400 0.28410 0.39329 -0.00718 -0.03186 -0.01592 65  ALA A CB  
510  N N   . VAL A 66  ? 0.25378 0.24710 0.34094 -0.00179 -0.01770 -0.00341 66  VAL A N   
511  C CA  . VAL A 66  ? 0.24467 0.23313 0.32762 -0.00052 -0.01369 0.00022  66  VAL A CA  
512  C C   . VAL A 66  ? 0.27300 0.26503 0.35966 0.00186  -0.00631 0.01014  66  VAL A C   
513  O O   . VAL A 66  ? 0.26517 0.25423 0.35935 0.00183  -0.00209 0.01528  66  VAL A O   
514  C CB  . VAL A 66  ? 0.28014 0.26574 0.34439 0.00211  -0.01546 -0.00290 66  VAL A CB  
515  C CG1 . VAL A 66  ? 0.28992 0.27237 0.35087 0.00408  -0.01172 0.00156  66  VAL A CG1 
516  C CG2 . VAL A 66  ? 0.30620 0.28714 0.36593 0.00071  -0.02109 -0.01155 66  VAL A CG2 
517  N N   . VAL A 67  ? 0.26274 0.26066 0.34333 0.00466  -0.00422 0.01323  67  VAL A N   
518  C CA  . VAL A 67  ? 0.25062 0.25194 0.33194 0.00821  0.00332  0.02264  67  VAL A CA  
519  C C   . VAL A 67  ? 0.28622 0.28898 0.38942 0.00571  0.00819  0.02829  67  VAL A C   
520  O O   . VAL A 67  ? 0.26264 0.26393 0.37025 0.00755  0.01477  0.03647  67  VAL A O   
521  C CB  . VAL A 67  ? 0.28037 0.28712 0.35118 0.01191  0.00447  0.02339  67  VAL A CB  
522  C CG1 . VAL A 67  ? 0.31766 0.32807 0.38961 0.01623  0.01307  0.03307  67  VAL A CG1 
523  C CG2 . VAL A 67  ? 0.24537 0.24986 0.29636 0.01448  0.00060  0.01879  67  VAL A CG2 
524  N N   . ASP A 68  ? 0.24952 0.25521 0.36784 0.00162  0.00489  0.02424  68  ASP A N   
525  C CA  . ASP A 68  ? 0.29030 0.29780 0.43380 -0.00166 0.00895  0.02889  68  ASP A CA  
526  C C   . ASP A 68  ? 0.30189 0.30177 0.45583 -0.00479 0.00904  0.02866  68  ASP A C   
527  O O   . ASP A 68  ? 0.28262 0.28213 0.45578 -0.00629 0.01533  0.03567  68  ASP A O   
528  C CB  . ASP A 68  ? 0.29758 0.31032 0.45629 -0.00561 0.00315  0.02293  68  ASP A CB  
529  C CG  . ASP A 68  ? 0.28198 0.30306 0.43717 -0.00230 0.00550  0.02571  68  ASP A CG  
530  O OD1 . ASP A 68  ? 0.33627 0.35914 0.48173 0.00272  0.01346  0.03351  68  ASP A OD1 
531  O OD2 . ASP A 68  ? 0.31346 0.33916 0.47525 -0.00416 -0.00077 0.01999  68  ASP A OD2 
532  N N   . ALA A 69  ? 0.26569 0.25910 0.40827 -0.00553 0.00298  0.02115  69  ALA A N   
533  C CA  . ALA A 69  ? 0.32141 0.30664 0.47219 -0.00772 0.00327  0.02037  69  ALA A CA  
534  C C   . ALA A 69  ? 0.34443 0.32676 0.48844 -0.00338 0.01070  0.02992  69  ALA A C   
535  O O   . ALA A 69  ? 0.35390 0.32911 0.50416 -0.00429 0.01182  0.03048  69  ALA A O   
536  C CB  . ALA A 69  ? 0.31646 0.29579 0.45676 -0.00913 -0.00505 0.00900  69  ALA A CB  
537  N N   . GLY A 70  ? 0.28904 0.27639 0.42000 0.00183  0.01539  0.03708  70  GLY A N   
538  C CA  . GLY A 70  ? 0.26290 0.24849 0.38624 0.00705  0.02180  0.04661  70  GLY A CA  
539  C C   . GLY A 70  ? 0.30716 0.29167 0.40808 0.01122  0.01818  0.04416  70  GLY A C   
540  O O   . GLY A 70  ? 0.29327 0.27624 0.38780 0.01584  0.02187  0.05125  70  GLY A O   
541  N N   . VAL A 71  ? 0.22893 0.21439 0.31874 0.01001  0.01116  0.03481  71  VAL A N   
542  C CA  . VAL A 71  ? 0.23292 0.21749 0.30518 0.01305  0.00743  0.03170  71  VAL A CA  
543  C C   . VAL A 71  ? 0.23905 0.22940 0.29658 0.01660  0.00681  0.03176  71  VAL A C   
544  O O   . VAL A 71  ? 0.23954 0.23218 0.29499 0.01464  0.00353  0.02593  71  VAL A O   
545  C CB  . VAL A 71  ? 0.27741 0.25774 0.34831 0.00958  0.00117  0.02169  71  VAL A CB  
546  C CG1 . VAL A 71  ? 0.24586 0.22603 0.30189 0.01256  -0.00172 0.01932  71  VAL A CG1 
547  C CG2 . VAL A 71  ? 0.28150 0.25509 0.36651 0.00646  0.00172  0.02044  71  VAL A CG2 
548  N N   . PRO A 72  ? 0.25420 0.24665 0.30075 0.02231  0.00952  0.03785  72  PRO A N   
549  C CA  . PRO A 72  ? 0.30067 0.29743 0.33221 0.02599  0.00823  0.03633  72  PRO A CA  
550  C C   . PRO A 72  ? 0.28739 0.28326 0.31009 0.02451  0.00111  0.02723  72  PRO A C   
551  O O   . PRO A 72  ? 0.24674 0.23967 0.26897 0.02370  -0.00203 0.02469  72  PRO A O   
552  C CB  . PRO A 72  ? 0.30569 0.30361 0.32656 0.03298  0.01152  0.04408  72  PRO A CB  
553  C CG  . PRO A 72  ? 0.28867 0.28261 0.31670 0.03277  0.01230  0.04800  72  PRO A CG  
554  C CD  . PRO A 72  ? 0.23891 0.22947 0.28575 0.02627  0.01366  0.04632  72  PRO A CD  
555  N N   . CYS A 73  ? 0.25438 0.25269 0.27142 0.02435  -0.00067 0.02287  73  CYS A N   
556  C CA  . CYS A 73  ? 0.26393 0.26105 0.27445 0.02278  -0.00625 0.01497  73  CYS A CA  
557  C C   . CYS A 73  ? 0.30279 0.30220 0.30006 0.02696  -0.00751 0.01359  73  CYS A C   
558  O O   . CYS A 73  ? 0.25790 0.26005 0.25186 0.02974  -0.00426 0.01614  73  CYS A O   
559  C CB  . CYS A 73  ? 0.26140 0.25806 0.27836 0.01861  -0.00786 0.01019  73  CYS A CB  
560  S SG  . CYS A 73  ? 0.26043 0.25273 0.29011 0.01371  -0.00910 0.00790  73  CYS A SG  
561  N N   . TYR A 74  ? 0.26932 0.26748 0.26016 0.02748  -0.01209 0.00924  74  TYR A N   
562  C CA  . TYR A 74  ? 0.26132 0.26080 0.24053 0.03128  -0.01469 0.00654  74  TYR A CA  
563  C C   . TYR A 74  ? 0.27786 0.27535 0.25663 0.02856  -0.01877 -0.00077 74  TYR A C   
564  O O   . TYR A 74  ? 0.26386 0.25906 0.24919 0.02480  -0.01992 -0.00300 74  TYR A O   
565  C CB  . TYR A 74  ? 0.26245 0.26294 0.23561 0.03534  -0.01711 0.00862  74  TYR A CB  
566  C CG  . TYR A 74  ? 0.28206 0.28376 0.25509 0.03889  -0.01239 0.01724  74  TYR A CG  
567  C CD1 . TYR A 74  ? 0.27229 0.27238 0.25560 0.03677  -0.01047 0.02144  74  TYR A CD1 
568  C CD2 . TYR A 74  ? 0.30786 0.31165 0.27035 0.04491  -0.00913 0.02153  74  TYR A CD2 
569  C CE1 . TYR A 74  ? 0.29695 0.29735 0.28167 0.04010  -0.00537 0.03021  74  TYR A CE1 
570  C CE2 . TYR A 74  ? 0.30276 0.30726 0.26522 0.04878  -0.00349 0.03084  74  TYR A CE2 
571  C CZ  . TYR A 74  ? 0.29342 0.29616 0.26783 0.04613  -0.00162 0.03541  74  TYR A CZ  
572  O OH  . TYR A 74  ? 0.32271 0.32539 0.29863 0.05002  0.00471  0.04549  74  TYR A OH  
573  N N   . PHE A 75  ? 0.25807 0.25584 0.22886 0.03098  -0.02037 -0.00430 75  PHE A N   
574  C CA  . PHE A 75  ? 0.25370 0.24892 0.22508 0.02872  -0.02321 -0.01046 75  PHE A CA  
575  C C   . PHE A 75  ? 0.27406 0.26898 0.23812 0.03162  -0.02751 -0.01511 75  PHE A C   
576  O O   . PHE A 75  ? 0.26725 0.26328 0.22186 0.03618  -0.02715 -0.01504 75  PHE A O   
577  C CB  . PHE A 75  ? 0.24688 0.24153 0.21911 0.02794  -0.02050 -0.01104 75  PHE A CB  
578  C CG  . PHE A 75  ? 0.25206 0.24331 0.22508 0.02614  -0.02243 -0.01609 75  PHE A CG  
579  C CD1 . PHE A 75  ? 0.28945 0.27820 0.26842 0.02257  -0.02288 -0.01704 75  PHE A CD1 
580  C CD2 . PHE A 75  ? 0.28521 0.27506 0.25276 0.02855  -0.02309 -0.01958 75  PHE A CD2 
581  C CE1 . PHE A 75  ? 0.26822 0.25339 0.24802 0.02151  -0.02340 -0.02026 75  PHE A CE1 
582  C CE2 . PHE A 75  ? 0.30724 0.29315 0.27702 0.02698  -0.02412 -0.02341 75  PHE A CE2 
583  C CZ  . PHE A 75  ? 0.25392 0.23762 0.23001 0.02348  -0.02398 -0.02318 75  PHE A CZ  
584  N N   . ILE A 76  ? 0.24486 0.23815 0.21380 0.02918  -0.03146 -0.01935 76  ILE A N   
585  C CA  . ILE A 76  ? 0.27171 0.26392 0.23783 0.03046  -0.03648 -0.02559 76  ILE A CA  
586  C C   . ILE A 76  ? 0.28522 0.27330 0.25706 0.02714  -0.03555 -0.02924 76  ILE A C   
587  O O   . ILE A 76  ? 0.27205 0.25867 0.25142 0.02363  -0.03303 -0.02746 76  ILE A O   
588  C CB  . ILE A 76  ? 0.26757 0.26189 0.23821 0.03036  -0.04204 -0.02725 76  ILE A CB  
589  C CG1 . ILE A 76  ? 0.26305 0.26116 0.22525 0.03533  -0.04358 -0.02353 76  ILE A CG1 
590  C CG2 . ILE A 76  ? 0.29077 0.28359 0.26401 0.02990  -0.04796 -0.03498 76  ILE A CG2 
591  C CD1 . ILE A 76  ? 0.29235 0.29355 0.25851 0.03632  -0.05026 -0.02514 76  ILE A CD1 
592  N N   . HIS A 77  ? 0.24639 0.23196 0.21383 0.02888  -0.03718 -0.03414 77  HIS A N   
593  C CA  . HIS A 77  ? 0.26581 0.24671 0.23849 0.02650  -0.03549 -0.03670 77  HIS A CA  
594  C C   . HIS A 77  ? 0.26362 0.24247 0.24802 0.02265  -0.03761 -0.03921 77  HIS A C   
595  O O   . HIS A 77  ? 0.27180 0.25262 0.26017 0.02239  -0.04258 -0.04208 77  HIS A O   
596  C CB  . HIS A 77  ? 0.26436 0.24219 0.23028 0.02968  -0.03656 -0.04170 77  HIS A CB  
597  C CG  . HIS A 77  ? 0.33378 0.31314 0.29036 0.03359  -0.03245 -0.03865 77  HIS A CG  
598  N ND1 . HIS A 77  ? 0.34416 0.32682 0.29037 0.03822  -0.03261 -0.03742 77  HIS A ND1 
599  C CD2 . HIS A 77  ? 0.30346 0.28190 0.26045 0.03398  -0.02773 -0.03608 77  HIS A CD2 
600  C CE1 . HIS A 77  ? 0.35336 0.33710 0.29523 0.04098  -0.02734 -0.03402 77  HIS A CE1 
601  N NE2 . HIS A 77  ? 0.34705 0.32867 0.29602 0.03832  -0.02484 -0.03345 77  HIS A NE2 
602  N N   . GLY A 78  ? 0.26127 0.23641 0.25172 0.02010  -0.03359 -0.03767 78  GLY A N   
603  C CA  . GLY A 78  ? 0.24494 0.21698 0.24728 0.01697  -0.03357 -0.03941 78  GLY A CA  
604  C C   . GLY A 78  ? 0.29116 0.25741 0.29614 0.01698  -0.03329 -0.04334 78  GLY A C   
605  O O   . GLY A 78  ? 0.28996 0.25461 0.28678 0.01975  -0.03351 -0.04534 78  GLY A O   
606  N N   . ASN A 79  ? 0.31021 0.27297 0.32811 0.01400  -0.03203 -0.04405 79  ASN A N   
607  C CA  . ASN A 79  ? 0.29930 0.25535 0.32238 0.01368  -0.03090 -0.04714 79  ASN A CA  
608  C C   . ASN A 79  ? 0.32071 0.27260 0.33858 0.01524  -0.02441 -0.04210 79  ASN A C   
609  O O   . ASN A 79  ? 0.31700 0.26335 0.33534 0.01644  -0.02328 -0.04410 79  ASN A O   
610  C CB  . ASN A 79  ? 0.31427 0.26776 0.35567 0.00988  -0.03082 -0.04873 79  ASN A CB  
611  C CG  . ASN A 79  ? 0.31022 0.26449 0.35827 0.00809  -0.02463 -0.04177 79  ASN A CG  
612  O OD1 . ASN A 79  ? 0.30222 0.26193 0.34853 0.00795  -0.02536 -0.03954 79  ASN A OD1 
613  N ND2 . ASN A 79  ? 0.30902 0.25723 0.36409 0.00736  -0.01792 -0.03802 79  ASN A ND2 
614  N N   . ARG A 80  ? 0.25730 0.21153 0.27027 0.01562  -0.02065 -0.03601 80  ARG A N   
615  C CA  . ARG A 80  ? 0.32677 0.27798 0.33392 0.01778  -0.01592 -0.03147 80  ARG A CA  
616  C C   . ARG A 80  ? 0.30791 0.26219 0.30422 0.02085  -0.01739 -0.03167 80  ARG A C   
617  O O   . ARG A 80  ? 0.34389 0.29522 0.33736 0.02330  -0.01528 -0.03051 80  ARG A O   
618  C CB  . ARG A 80  ? 0.28201 0.23390 0.28800 0.01741  -0.01199 -0.02586 80  ARG A CB  
619  C CG  . ARG A 80  ? 0.31554 0.26480 0.33274 0.01503  -0.00869 -0.02437 80  ARG A CG  
620  C CD  . ARG A 80  ? 0.32294 0.26510 0.34902 0.01480  -0.00502 -0.02390 80  ARG A CD  
621  N NE  . ARG A 80  ? 0.33931 0.27701 0.35771 0.01822  -0.00049 -0.01912 80  ARG A NE  
622  C CZ  . ARG A 80  ? 0.37053 0.30109 0.39491 0.01912  0.00475  -0.01605 80  ARG A CZ  
623  N NH1 . ARG A 80  ? 0.32693 0.25368 0.36707 0.01616  0.00643  -0.01758 80  ARG A NH1 
624  N NH2 . ARG A 80  ? 0.41245 0.33968 0.42793 0.02322  0.00823  -0.01110 80  ARG A NH2 
625  N N   . ASP A 81  ? 0.29875 0.25898 0.29007 0.02111  -0.02040 -0.03248 81  ASP A N   
626  C CA  . ASP A 81  ? 0.28770 0.25180 0.27094 0.02387  -0.02043 -0.03118 81  ASP A CA  
627  C C   . ASP A 81  ? 0.29029 0.25665 0.26874 0.02591  -0.02338 -0.03512 81  ASP A C   
628  O O   . ASP A 81  ? 0.30655 0.27798 0.27977 0.02744  -0.02352 -0.03325 81  ASP A O   
629  C CB  . ASP A 81  ? 0.26461 0.23343 0.24598 0.02308  -0.01982 -0.02701 81  ASP A CB  
630  C CG  . ASP A 81  ? 0.28783 0.25871 0.27230 0.02064  -0.02140 -0.02710 81  ASP A CG  
631  O OD1 . ASP A 81  ? 0.27384 0.24417 0.26165 0.01984  -0.02383 -0.03035 81  ASP A OD1 
632  O OD2 . ASP A 81  ? 0.27170 0.24477 0.25594 0.01970  -0.02064 -0.02427 81  ASP A OD2 
633  N N   . PHE A 82  ? 0.27228 0.23445 0.25230 0.02636  -0.02560 -0.04066 82  PHE A N   
634  C CA  . PHE A 82  ? 0.28017 0.24360 0.25289 0.02941  -0.02897 -0.04542 82  PHE A CA  
635  C C   . PHE A 82  ? 0.30102 0.26523 0.26513 0.03403  -0.02599 -0.04451 82  PHE A C   
636  O O   . PHE A 82  ? 0.29798 0.26406 0.25318 0.03775  -0.02729 -0.04686 82  PHE A O   
637  C CB  . PHE A 82  ? 0.31364 0.27169 0.29095 0.02873  -0.03315 -0.05309 82  PHE A CB  
638  C CG  . PHE A 82  ? 0.33789 0.28846 0.32093 0.02853  -0.03039 -0.05469 82  PHE A CG  
639  C CD1 . PHE A 82  ? 0.33547 0.28238 0.33010 0.02487  -0.02778 -0.05196 82  PHE A CD1 
640  C CD2 . PHE A 82  ? 0.32674 0.27345 0.30348 0.03264  -0.02958 -0.05837 82  PHE A CD2 
641  C CE1 . PHE A 82  ? 0.35407 0.29349 0.35427 0.02519  -0.02450 -0.05226 82  PHE A CE1 
642  C CE2 . PHE A 82  ? 0.34699 0.28613 0.32984 0.03281  -0.02672 -0.05941 82  PHE A CE2 
643  C CZ  . PHE A 82  ? 0.34102 0.27643 0.33578 0.02903  -0.02421 -0.05605 82  PHE A CZ  
644  N N   . LEU A 83  ? 0.25915 0.22230 0.22547 0.03456  -0.02189 -0.04084 83  LEU A N   
645  C CA  . LEU A 83  ? 0.27314 0.23785 0.23406 0.03908  -0.01865 -0.03953 83  LEU A CA  
646  C C   . LEU A 83  ? 0.29365 0.26609 0.25357 0.03961  -0.01629 -0.03333 83  LEU A C   
647  O O   . LEU A 83  ? 0.32174 0.29685 0.28013 0.04314  -0.01292 -0.03111 83  LEU A O   
648  C CB  . LEU A 83  ? 0.24200 0.20190 0.20725 0.04015  -0.01589 -0.03884 83  LEU A CB  
649  C CG  . LEU A 83  ? 0.27869 0.22983 0.24575 0.04078  -0.01695 -0.04523 83  LEU A CG  
650  C CD1 . LEU A 83  ? 0.29881 0.24502 0.27033 0.04260  -0.01329 -0.04304 83  LEU A CD1 
651  C CD2 . LEU A 83  ? 0.35488 0.30485 0.31320 0.04481  -0.01860 -0.05168 83  LEU A CD2 
652  N N   . VAL A 84  ? 0.25126 0.22722 0.21370 0.03624  -0.01771 -0.03052 84  VAL A N   
653  C CA  . VAL A 84  ? 0.26243 0.24502 0.22584 0.03632  -0.01572 -0.02521 84  VAL A CA  
654  C C   . VAL A 84  ? 0.29762 0.28312 0.25385 0.04068  -0.01373 -0.02482 84  VAL A C   
655  O O   . VAL A 84  ? 0.30222 0.28660 0.25180 0.04199  -0.01603 -0.02767 84  VAL A O   
656  C CB  . VAL A 84  ? 0.28809 0.27233 0.25525 0.03222  -0.01765 -0.02325 84  VAL A CB  
657  C CG1 . VAL A 84  ? 0.25053 0.24068 0.21952 0.03235  -0.01568 -0.01839 84  VAL A CG1 
658  C CG2 . VAL A 84  ? 0.22717 0.20880 0.19957 0.02917  -0.01823 -0.02267 84  VAL A CG2 
659  N N   . GLY A 85  ? 0.25839 0.24793 0.21597 0.04351  -0.00938 -0.02107 85  GLY A N   
660  C CA  . GLY A 85  ? 0.32018 0.31198 0.27011 0.04889  -0.00563 -0.01991 85  GLY A CA  
661  C C   . GLY A 85  ? 0.37075 0.36939 0.32512 0.04933  -0.00127 -0.01267 85  GLY A C   
662  O O   . GLY A 85  ? 0.31262 0.31391 0.27571 0.04479  -0.00247 -0.00948 85  GLY A O   
663  N N   . GLN A 86  ? 0.31234 0.34427 0.34437 0.06218  0.07180  -0.02718 86  GLN A N   
664  C CA  . GLN A 86  ? 0.33576 0.38673 0.36964 0.05740  0.07472  -0.02062 86  GLN A CA  
665  C C   . GLN A 86  ? 0.31650 0.38963 0.37858 0.05666  0.07142  -0.00747 86  GLN A C   
666  O O   . GLN A 86  ? 0.25583 0.34192 0.32100 0.04773  0.06835  -0.00049 86  GLN A O   
667  C CB  . GLN A 86  ? 0.37631 0.43053 0.40101 0.06345  0.09047  -0.02682 86  GLN A CB  
668  C CG  . GLN A 86  ? 0.47839 0.52182 0.47115 0.05742  0.09004  -0.03430 86  GLN A CG  
669  C CD  . GLN A 86  ? 0.44673 0.49707 0.43493 0.04656  0.08158  -0.02496 86  GLN A CD  
670  O OE1 . GLN A 86  ? 0.47943 0.51850 0.45079 0.04081  0.07232  -0.02748 86  GLN A OE1 
671  N NE2 . GLN A 86  ? 0.60571 0.67452 0.61116 0.04370  0.08500  -0.01383 86  GLN A NE2 
672  N N   . ARG A 87  ? 0.26684 0.34450 0.35034 0.06537  0.07122  -0.00327 87  ARG A N   
673  C CA  . ARG A 87  ? 0.26175 0.36345 0.37283 0.06370  0.06441  0.01024  87  ARG A CA  
674  C C   . ARG A 87  ? 0.25592 0.35502 0.35860 0.05035  0.04785  0.01444  87  ARG A C   
675  O O   . ARG A 87  ? 0.22397 0.33982 0.33592 0.04081  0.04199  0.02149  87  ARG A O   
676  C CB  . ARG A 87  ? 0.27685 0.38263 0.41160 0.07719  0.06573  0.01560  87  ARG A CB  
677  C CG  . ARG A 87  ? 0.28215 0.41591 0.44655 0.07562  0.05535  0.03109  87  ARG A CG  
678  C CD  . ARG A 87  ? 0.34290 0.49016 0.53924 0.09292  0.06253  0.03866  87  ARG A CD  
679  N NE  . ARG A 87  ? 0.43209 0.60854 0.65777 0.09137  0.04911  0.05515  87  ARG A NE  
680  C CZ  . ARG A 87  ? 0.45482 0.64089 0.70680 0.10508  0.04675  0.06622  87  ARG A CZ  
681  N NH1 . ARG A 87  ? 0.33801 0.50364 0.59193 0.12203  0.05866  0.06212  87  ARG A NH1 
682  N NH2 . ARG A 87  ? 0.46679 0.68282 0.74363 0.10146  0.03136  0.08204  87  ARG A NH2 
683  N N   . PHE A 88  ? 0.22387 0.30126 0.30878 0.04889  0.04105  0.00958  88  PHE A N   
684  C CA  . PHE A 88  ? 0.23605 0.30860 0.30930 0.03743  0.02821  0.01174  88  PHE A CA  
685  C C   . PHE A 88  ? 0.26706 0.33486 0.32406 0.02771  0.02875  0.00741  88  PHE A C   
686  O O   . PHE A 88  ? 0.23149 0.30122 0.28535 0.01757  0.02065  0.01038  88  PHE A O   
687  C CB  . PHE A 88  ? 0.26941 0.32154 0.32901 0.03883  0.02373  0.00851  88  PHE A CB  
688  C CG  . PHE A 88  ? 0.23238 0.27947 0.27866 0.02874  0.01308  0.01026  88  PHE A CG  
689  C CD1 . PHE A 88  ? 0.22854 0.28612 0.28138 0.02552  0.00295  0.01908  88  PHE A CD1 
690  C CD2 . PHE A 88  ? 0.23319 0.26582 0.25994 0.02295  0.01334  0.00309  88  PHE A CD2 
691  C CE1 . PHE A 88  ? 0.28776 0.33848 0.32340 0.01609  -0.00551 0.01865  88  PHE A CE1 
692  C CE2 . PHE A 88  ? 0.24590 0.27237 0.25988 0.01524  0.00634  0.00343  88  PHE A CE2 
693  C CZ  . PHE A 88  ? 0.26372 0.29777 0.27990 0.01148  -0.00247 0.01019  88  PHE A CZ  
694  N N   . ALA A 89  ? 0.22373 0.28370 0.26883 0.03065  0.03780  0.00048  89  ALA A N   
695  C CA  . ALA A 89  ? 0.29705 0.35343 0.32817 0.02308  0.03851  -0.00065 89  ALA A CA  
696  C C   . ALA A 89  ? 0.25912 0.33286 0.30406 0.01646  0.03980  0.00753  89  ALA A C   
697  O O   . ALA A 89  ? 0.27449 0.34398 0.31372 0.00659  0.03479  0.00991  89  ALA A O   
698  C CB  . ALA A 89  ? 0.23643 0.28514 0.25182 0.02784  0.04710  -0.00775 89  ALA A CB  
699  N N   . ARG A 90  ? 0.25728 0.35037 0.32261 0.02167  0.04717  0.01207  90  ARG A N   
700  C CA  . ARG A 90  ? 0.24443 0.35844 0.32847 0.01420  0.04900  0.02113  90  ARG A CA  
701  C C   . ARG A 90  ? 0.28719 0.40892 0.38402 0.00412  0.03457  0.02671  90  ARG A C   
702  O O   . ARG A 90  ? 0.26548 0.39086 0.36532 -0.00875 0.03061  0.03072  90  ARG A O   
703  C CB  . ARG A 90  ? 0.26382 0.40012 0.37051 0.02385  0.06190  0.02506  90  ARG A CB  
704  C CG  . ARG A 90  ? 0.35135 0.48176 0.44197 0.03146  0.07803  0.01916  90  ARG A CG  
705  C CD  . ARG A 90  ? 0.46521 0.62059 0.57970 0.03940  0.09374  0.02421  90  ARG A CD  
706  N NE  . ARG A 90  ? 0.53137 0.69247 0.66541 0.05311  0.09588  0.02293  90  ARG A NE  
707  C CZ  . ARG A 90  ? 0.55617 0.70540 0.68117 0.06704  0.10785  0.01338  90  ARG A CZ  
708  N NH1 . ARG A 90  ? 0.57044 0.70362 0.66495 0.06831  0.11773  0.00323  90  ARG A NH1 
709  N NH2 . ARG A 90  ? 0.47868 0.63098 0.62478 0.07983  0.10942  0.01409  90  ARG A NH2 
710  N N   . GLN A 91  ? 0.24532 0.36842 0.34829 0.00903  0.02632  0.02725  91  GLN A N   
711  C CA  . GLN A 91  ? 0.29426 0.42514 0.40440 -0.00084 0.01102  0.03221  91  GLN A CA  
712  C C   . GLN A 91  ? 0.24225 0.35047 0.32661 -0.01253 0.00337  0.02610  91  GLN A C   
713  O O   . GLN A 91  ? 0.23332 0.34533 0.31966 -0.02585 -0.00626 0.02801  91  GLN A O   
714  C CB  . GLN A 91  ? 0.27270 0.40672 0.38925 0.00811  0.00409  0.03543  91  GLN A CB  
715  C CG  . GLN A 91  ? 0.33680 0.49177 0.48227 0.02191  0.01158  0.04234  91  GLN A CG  
716  C CD  . GLN A 91  ? 0.45071 0.60642 0.60303 0.03089  0.00357  0.04822  91  GLN A CD  
717  O OE1 . GLN A 91  ? 0.44752 0.58098 0.57729 0.03082  -0.00140 0.04422  91  GLN A OE1 
718  N NE2 . GLN A 91  ? 0.47902 0.66142 0.66421 0.03915  0.00290  0.05934  91  GLN A NE2 
719  N N   . SER A 92  ? 0.22463 0.30925 0.28573 -0.00784 0.00764  0.01829  92  SER A N   
720  C CA  . SER A 92  ? 0.23053 0.29322 0.26904 -0.01538 0.00270  0.01242  92  SER A CA  
721  C C   . SER A 92  ? 0.29984 0.35236 0.33064 -0.02073 0.00855  0.01117  92  SER A C   
722  O O   . SER A 92  ? 0.29874 0.33345 0.31516 -0.02760 0.00502  0.00741  92  SER A O   
723  C CB  . SER A 92  ? 0.23181 0.27751 0.25365 -0.00733 0.00390  0.00648  92  SER A CB  
724  O OG  . SER A 92  ? 0.26672 0.30918 0.28665 0.00134  0.01337  0.00361  92  SER A OG  
725  N N   . GLY A 93  ? 0.26663 0.32857 0.30527 -0.01705 0.01830  0.01466  93  GLY A N   
726  C CA  . GLY A 93  ? 0.25919 0.31037 0.28764 -0.02033 0.02433  0.01574  93  GLY A CA  
727  C C   . GLY A 93  ? 0.27800 0.31139 0.28606 -0.01279 0.02692  0.01040  93  GLY A C   
728  O O   . GLY A 93  ? 0.27420 0.29746 0.27257 -0.01450 0.03019  0.01284  93  GLY A O   
729  N N   . MET A 94  ? 0.23792 0.26801 0.24090 -0.00497 0.02506  0.00453  94  MET A N   
730  C CA  . MET A 94  ? 0.26133 0.27862 0.24905 0.00076  0.02611  -0.00026 94  MET A CA  
731  C C   . MET A 94  ? 0.32099 0.34412 0.30394 0.00691  0.03334  -0.00080 94  MET A C   
732  O O   . MET A 94  ? 0.30384 0.33939 0.29522 0.01002  0.03919  -0.00010 94  MET A O   
733  C CB  . MET A 94  ? 0.31400 0.32564 0.29931 0.00468  0.02188  -0.00587 94  MET A CB  
734  C CG  . MET A 94  ? 0.35592 0.35619 0.33540 0.00011  0.01642  -0.00743 94  MET A CG  
735  S SD  . MET A 94  ? 0.34530 0.33975 0.32055 0.00469  0.01448  -0.01199 94  MET A SD  
736  C CE  . MET A 94  ? 0.31361 0.31988 0.30115 0.00921  0.01487  -0.00995 94  MET A CE  
737  N N   . ILE A 95  ? 0.26282 0.27742 0.23166 0.00914  0.03292  -0.00220 95  ILE A N   
738  C CA  . ILE A 95  ? 0.29583 0.31385 0.25327 0.01400  0.03738  -0.00451 95  ILE A CA  
739  C C   . ILE A 95  ? 0.30408 0.31696 0.25681 0.01800  0.03322  -0.01342 95  ILE A C   
740  O O   . ILE A 95  ? 0.29100 0.29704 0.24331 0.01724  0.02708  -0.01440 95  ILE A O   
741  C CB  . ILE A 95  ? 0.31272 0.32727 0.25718 0.01269  0.03777  0.00232  95  ILE A CB  
742  C CG1 . ILE A 95  ? 0.35846 0.37753 0.30832 0.00735  0.04390  0.01205  95  ILE A CG1 
743  C CG2 . ILE A 95  ? 0.26215 0.27969 0.18911 0.01701  0.03921  -0.00120 95  ILE A CG2 
744  C CD1 . ILE A 95  ? 0.44773 0.45608 0.39085 0.00413  0.04227  0.02142  95  ILE A CD1 
745  N N   . LEU A 96  ? 0.26176 0.27726 0.21213 0.02205  0.03760  -0.02012 96  LEU A N   
746  C CA  . LEU A 96  ? 0.25576 0.26423 0.20256 0.02385  0.03395  -0.02927 96  LEU A CA  
747  C C   . LEU A 96  ? 0.29964 0.30704 0.22895 0.02296  0.03006  -0.03261 96  LEU A C   
748  O O   . LEU A 96  ? 0.31663 0.32788 0.23134 0.02394  0.03432  -0.03248 96  LEU A O   
749  C CB  . LEU A 96  ? 0.29930 0.30644 0.25062 0.02864  0.04059  -0.03607 96  LEU A CB  
750  C CG  . LEU A 96  ? 0.32505 0.33770 0.29576 0.03136  0.04407  -0.03098 96  LEU A CG  
751  C CD1 . LEU A 96  ? 0.32042 0.32951 0.29628 0.03884  0.05164  -0.03753 96  LEU A CD1 
752  C CD2 . LEU A 96  ? 0.32383 0.33300 0.30397 0.02806  0.03610  -0.02682 96  LEU A CD2 
753  N N   . LEU A 97  ? 0.27051 0.27471 0.20142 0.02090  0.02192  -0.03483 97  LEU A N   
754  C CA  . LEU A 97  ? 0.30560 0.31262 0.22386 0.01932  0.01494  -0.03694 97  LEU A CA  
755  C C   . LEU A 97  ? 0.33524 0.33770 0.25149 0.01671  0.01141  -0.04903 97  LEU A C   
756  O O   . LEU A 97  ? 0.33047 0.32531 0.25728 0.01675  0.01459  -0.05403 97  LEU A O   
757  C CB  . LEU A 97  ? 0.24883 0.25909 0.17481 0.01894  0.00800  -0.02873 97  LEU A CB  
758  C CG  . LEU A 97  ? 0.28852 0.29787 0.21595 0.02063  0.01095  -0.01742 97  LEU A CG  
759  C CD1 . LEU A 97  ? 0.27641 0.28594 0.21202 0.02246  0.00542  -0.01095 97  LEU A CD1 
760  C CD2 . LEU A 97  ? 0.30692 0.31962 0.21783 0.02121  0.01425  -0.01227 97  LEU A CD2 
761  N N   . ALA A 98  ? 0.33709 0.34371 0.23931 0.01369  0.00390  -0.05306 98  ALA A N   
762  C CA  . ALA A 98  ? 0.31673 0.31826 0.21606 0.00834  -0.00139 -0.06571 98  ALA A CA  
763  C C   . ALA A 98  ? 0.35628 0.36043 0.27764 0.00431  -0.00805 -0.06364 98  ALA A C   
764  O O   . ALA A 98  ? 0.33585 0.34623 0.27132 0.00681  -0.00839 -0.05322 98  ALA A O   
765  C CB  . ALA A 98  ? 0.37977 0.38710 0.25525 0.00453  -0.00960 -0.07084 98  ALA A CB  
766  N N   . GLU A 99  ? 0.36890 0.36707 0.29289 -0.00248 -0.01224 -0.07423 99  GLU A N   
767  C CA  . GLU A 99  ? 0.36776 0.36965 0.31445 -0.00755 -0.01674 -0.07174 99  GLU A CA  
768  C C   . GLU A 99  ? 0.31702 0.33907 0.27254 -0.00899 -0.02698 -0.06352 99  GLU A C   
769  O O   . GLU A 99  ? 0.34065 0.36996 0.31803 -0.00965 -0.02714 -0.05716 99  GLU A O   
770  C CB  . GLU A 99  ? 0.36886 0.35894 0.31752 -0.01661 -0.01927 -0.08448 99  GLU A CB  
771  C CG  . GLU A 99  ? 0.40777 0.40094 0.33947 -0.02480 -0.03021 -0.09568 99  GLU A CG  
772  C CD  . GLU A 99  ? 0.55538 0.53350 0.49095 -0.03609 -0.03307 -0.10937 99  GLU A CD  
773  O OE1 . GLU A 99  ? 0.60501 0.55965 0.53440 -0.03397 -0.02324 -0.11800 99  GLU A OE1 
774  O OE2 . GLU A 99  ? 0.59953 0.58929 0.54656 -0.04716 -0.04505 -0.11092 99  GLU A OE2 
775  N N   . GLU A 100 ? 0.34106 0.37300 0.28027 -0.00866 -0.03486 -0.06253 100 GLU A N   
776  C CA  . GLU A 100 ? 0.35311 0.40527 0.30120 -0.00695 -0.04473 -0.05153 100 GLU A CA  
777  C C   . GLU A 100 ? 0.33103 0.38493 0.26072 0.00079  -0.04333 -0.04251 100 GLU A C   
778  O O   . GLU A 100 ? 0.35844 0.40578 0.26225 0.00030  -0.04148 -0.04792 100 GLU A O   
779  C CB  . GLU A 100 ? 0.38755 0.45427 0.33571 -0.01662 -0.06069 -0.05700 100 GLU A CB  
780  C CG  . GLU A 100 ? 0.40800 0.47691 0.38016 -0.02645 -0.06362 -0.06319 100 GLU A CG  
781  C CD  . GLU A 100 ? 0.42716 0.51183 0.39964 -0.03860 -0.08139 -0.06946 100 GLU A CD  
782  O OE1 . GLU A 100 ? 0.47896 0.57277 0.42956 -0.03860 -0.09210 -0.06907 100 GLU A OE1 
783  O OE2 . GLU A 100 ? 0.45686 0.54542 0.45101 -0.04918 -0.08520 -0.07416 100 GLU A OE2 
784  N N   . GLU A 101 ? 0.30555 0.36664 0.24839 0.00807  -0.04268 -0.02865 101 GLU A N   
785  C CA  . GLU A 101 ? 0.33631 0.39795 0.26482 0.01480  -0.04199 -0.01735 101 GLU A CA  
786  C C   . GLU A 101 ? 0.33481 0.41155 0.27960 0.02056  -0.05024 -0.00340 101 GLU A C   
787  O O   . GLU A 101 ? 0.33930 0.42208 0.31039 0.02252  -0.04968 -0.00116 101 GLU A O   
788  C CB  . GLU A 101 ? 0.34596 0.39200 0.27305 0.01954  -0.02791 -0.01383 101 GLU A CB  
789  C CG  . GLU A 101 ? 0.35047 0.38459 0.26607 0.01644  -0.01879 -0.02458 101 GLU A CG  
790  C CD  . GLU A 101 ? 0.37729 0.41105 0.26539 0.01573  -0.01749 -0.02683 101 GLU A CD  
791  O OE1 . GLU A 101 ? 0.44082 0.48324 0.31499 0.01653  -0.02497 -0.01960 101 GLU A OE1 
792  O OE2 . GLU A 101 ? 0.39205 0.41742 0.27231 0.01518  -0.00821 -0.03496 101 GLU A OE2 
793  N N   . ARG A 102 ? 0.33427 0.41741 0.26342 0.02416  -0.05694 0.00702  102 ARG A N   
794  C CA  . ARG A 102 ? 0.35369 0.44980 0.29767 0.03239  -0.06447 0.02351  102 ARG A CA  
795  C C   . ARG A 102 ? 0.40891 0.48910 0.34759 0.04084  -0.05429 0.03594  102 ARG A C   
796  O O   . ARG A 102 ? 0.45197 0.52344 0.36526 0.03948  -0.05064 0.03834  102 ARG A O   
797  C CB  . ARG A 102 ? 0.37475 0.49110 0.30543 0.02999  -0.08239 0.02887  102 ARG A CB  
798  C CG  . ARG A 102 ? 0.40968 0.54565 0.36397 0.03905  -0.09303 0.04653  102 ARG A CG  
799  C CD  . ARG A 102 ? 0.52008 0.66671 0.45092 0.04169  -0.10619 0.06057  102 ARG A CD  
800  N NE  . ARG A 102 ? 0.62966 0.79314 0.54105 0.03014  -0.12278 0.05113  102 ARG A NE  
801  C CZ  . ARG A 102 ? 0.72775 0.91036 0.62315 0.03012  -0.14084 0.06229  102 ARG A CZ  
802  N NH1 . ARG A 102 ? 0.70336 0.89125 0.60181 0.04237  -0.14457 0.08564  102 ARG A NH1 
803  N NH2 . ARG A 102 ? 0.89104 1.08640 0.76564 0.01723  -0.15602 0.04989  102 ARG A NH2 
804  N N   . LEU A 103 ? 0.35921 0.43460 0.32165 0.04896  -0.04861 0.04329  103 LEU A N   
805  C CA  . LEU A 103 ? 0.33187 0.38739 0.29207 0.05555  -0.03834 0.05308  103 LEU A CA  
806  C C   . LEU A 103 ? 0.37860 0.43947 0.35079 0.06713  -0.04407 0.07153  103 LEU A C   
807  O O   . LEU A 103 ? 0.35729 0.43783 0.35070 0.07213  -0.05274 0.07560  103 LEU A O   
808  C CB  . LEU A 103 ? 0.33105 0.36994 0.30521 0.05583  -0.02525 0.04494  103 LEU A CB  
809  C CG  . LEU A 103 ? 0.37161 0.40578 0.34010 0.04644  -0.01967 0.02888  103 LEU A CG  
810  C CD1 . LEU A 103 ? 0.31185 0.33186 0.29279 0.04763  -0.00904 0.02375  103 LEU A CD1 
811  C CD2 . LEU A 103 ? 0.33874 0.36540 0.28377 0.04060  -0.01634 0.02651  103 LEU A CD2 
812  N N   . ASP A 104 ? 0.35438 0.39813 0.31536 0.07148  -0.03892 0.08393  104 ASP A N   
813  C CA  . ASP A 104 ? 0.39347 0.43270 0.36861 0.08453  -0.04006 0.10229  104 ASP A CA  
814  C C   . ASP A 104 ? 0.41960 0.43108 0.40744 0.08854  -0.02463 0.09892  104 ASP A C   
815  O O   . ASP A 104 ? 0.44513 0.43385 0.41879 0.08287  -0.01538 0.09723  104 ASP A O   
816  C CB  . ASP A 104 ? 0.49611 0.53180 0.44941 0.08660  -0.04480 0.12052  104 ASP A CB  
817  C CG  . ASP A 104 ? 0.52716 0.55844 0.49705 0.10182  -0.04744 0.14212  104 ASP A CG  
818  O OD1 . ASP A 104 ? 0.59957 0.65592 0.57948 0.10899  -0.06194 0.15319  104 ASP A OD1 
819  O OD2 . ASP A 104 ? 0.58683 0.58919 0.56117 0.10659  -0.03539 0.14808  104 ASP A OD2 
820  N N   . LEU A 105 ? 0.36062 0.37480 0.37490 0.09747  -0.02159 0.09727  105 LEU A N   
821  C CA  . LEU A 105 ? 0.38568 0.37257 0.40968 0.10206  -0.00669 0.09205  105 LEU A CA  
822  C C   . LEU A 105 ? 0.37998 0.35799 0.42154 0.11890  -0.00497 0.10891  105 LEU A C   
823  O O   . LEU A 105 ? 0.35947 0.35442 0.42706 0.13033  -0.00652 0.11261  105 LEU A O   
824  C CB  . LEU A 105 ? 0.31838 0.31229 0.35602 0.09976  -0.00076 0.07564  105 LEU A CB  
825  C CG  . LEU A 105 ? 0.37871 0.37890 0.40165 0.08469  -0.00182 0.06014  105 LEU A CG  
826  C CD1 . LEU A 105 ? 0.33724 0.34672 0.37551 0.08364  0.00313  0.04821  105 LEU A CD1 
827  C CD2 . LEU A 105 ? 0.32205 0.29714 0.32427 0.07577  0.00556  0.05437  105 LEU A CD2 
828  N N   . TYR A 106 ? 0.39449 0.34640 0.42390 0.12061  -0.00124 0.12029  106 TYR A N   
829  C CA  . TYR A 106 ? 0.43053 0.36490 0.47508 0.13712  0.00258  0.13712  106 TYR A CA  
830  C C   . TYR A 106 ? 0.45666 0.42290 0.51979 0.15055  -0.01121 0.15523  106 TYR A C   
831  O O   . TYR A 106 ? 0.41035 0.37585 0.50029 0.16798  -0.00816 0.16499  106 TYR A O   
832  C CB  . TYR A 106 ? 0.40426 0.31366 0.46452 0.14461  0.01845  0.12558  106 TYR A CB  
833  C CG  . TYR A 106 ? 0.41607 0.30408 0.45822 0.12898  0.02807  0.10465  106 TYR A CG  
834  C CD1 . TYR A 106 ? 0.47276 0.32887 0.49634 0.11942  0.03327  0.10489  106 TYR A CD1 
835  C CD2 . TYR A 106 ? 0.36912 0.27072 0.41359 0.12288  0.03096  0.08625  106 TYR A CD2 
836  C CE1 . TYR A 106 ? 0.40358 0.24449 0.41285 0.10440  0.03955  0.08693  106 TYR A CE1 
837  C CE2 . TYR A 106 ? 0.36527 0.24976 0.39274 0.10901  0.03763  0.06923  106 TYR A CE2 
838  C CZ  . TYR A 106 ? 0.36776 0.22333 0.37834 0.09987  0.04106  0.06943  106 TYR A CZ  
839  O OH  . TYR A 106 ? 0.40294 0.24553 0.39908 0.08553  0.04543  0.05354  106 TYR A OH  
840  N N   . GLY A 107 ? 0.41891 0.41394 0.46763 0.14253  -0.02674 0.15969  107 GLY A N   
841  C CA  . GLY A 107 ? 0.43084 0.46041 0.49284 0.15149  -0.04391 0.17615  107 GLY A CA  
842  C C   . GLY A 107 ? 0.52082 0.58838 0.59837 0.14639  -0.05363 0.16418  107 GLY A C   
843  O O   . GLY A 107 ? 0.59293 0.69342 0.67241 0.14624  -0.07207 0.17388  107 GLY A O   
844  N N   . ARG A 108 ? 0.44265 0.50625 0.53047 0.14120  -0.04233 0.14402  108 ARG A N   
845  C CA  . ARG A 108 ? 0.43989 0.53635 0.54308 0.13426  -0.04963 0.13255  108 ARG A CA  
846  C C   . ARG A 108 ? 0.38473 0.48817 0.45771 0.11532  -0.05810 0.11993  108 ARG A C   
847  O O   . ARG A 108 ? 0.41578 0.49464 0.46320 0.10627  -0.04907 0.10976  108 ARG A O   
848  C CB  . ARG A 108 ? 0.43018 0.51771 0.55188 0.13531  -0.03283 0.11699  108 ARG A CB  
849  C CG  . ARG A 108 ? 0.48062 0.57356 0.63988 0.15406  -0.02439 0.12548  108 ARG A CG  
850  C CD  . ARG A 108 ? 0.42182 0.51001 0.59270 0.15169  -0.00785 0.10784  108 ARG A CD  
851  N NE  . ARG A 108 ? 0.53462 0.59971 0.72088 0.16806  0.01096  0.10878  108 ARG A NE  
852  C CZ  . ARG A 108 ? 0.48338 0.50564 0.64915 0.17036  0.02323  0.10493  108 ARG A CZ  
853  N NH1 . ARG A 108 ? 0.41928 0.42000 0.55178 0.15756  0.01904  0.10181  108 ARG A NH1 
854  N NH2 . ARG A 108 ? 0.43358 0.43400 0.61325 0.18539  0.04082  0.10357  108 ARG A NH2 
855  N N   . GLU A 109 ? 0.38542 0.52242 0.46276 0.10923  -0.07522 0.11998  109 GLU A N   
856  C CA  . GLU A 109 ? 0.42029 0.56322 0.47322 0.09152  -0.08160 0.10387  109 GLU A CA  
857  C C   . GLU A 109 ? 0.35593 0.50279 0.42713 0.08430  -0.07389 0.08625  109 GLU A C   
858  O O   . GLU A 109 ? 0.35605 0.52799 0.45945 0.08684  -0.07853 0.08810  109 GLU A O   
859  C CB  . GLU A 109 ? 0.45454 0.62813 0.49936 0.08631  -0.10440 0.11039  109 GLU A CB  
860  C CG  . GLU A 109 ? 0.52930 0.69470 0.53652 0.08585  -0.11107 0.12126  109 GLU A CG  
861  N N   . VAL A 110 ? 0.31047 0.43414 0.36298 0.07554  -0.06194 0.07095  110 VAL A N   
862  C CA  . VAL A 110 ? 0.28861 0.41004 0.35497 0.06984  -0.05212 0.05651  110 VAL A CA  
863  C C   . VAL A 110 ? 0.32835 0.44559 0.37264 0.05462  -0.05445 0.04092  110 VAL A C   
864  O O   . VAL A 110 ? 0.35068 0.45006 0.36707 0.05096  -0.05106 0.03725  110 VAL A O   
865  C CB  . VAL A 110 ? 0.24328 0.33742 0.31166 0.07639  -0.03329 0.05391  110 VAL A CB  
866  C CG1 . VAL A 110 ? 0.23947 0.33411 0.32073 0.07123  -0.02378 0.04148  110 VAL A CG1 
867  C CG2 . VAL A 110 ? 0.29268 0.38415 0.37988 0.09286  -0.02906 0.06837  110 VAL A CG2 
868  N N   . LEU A 111 ? 0.26938 0.40258 0.32833 0.04606  -0.05904 0.03228  111 LEU A N   
869  C CA  . LEU A 111 ? 0.27990 0.40562 0.32239 0.03253  -0.05941 0.01672  111 LEU A CA  
870  C C   . LEU A 111 ? 0.28419 0.39248 0.33208 0.03106  -0.04364 0.00848  111 LEU A C   
871  O O   . LEU A 111 ? 0.26683 0.38047 0.33865 0.03533  -0.03639 0.01132  111 LEU A O   
872  C CB  . LEU A 111 ? 0.26842 0.41823 0.32323 0.02198  -0.07410 0.01198  111 LEU A CB  
873  C CG  . LEU A 111 ? 0.29251 0.43415 0.33795 0.00739  -0.07450 -0.00476 111 LEU A CG  
874  C CD1 . LEU A 111 ? 0.33039 0.45351 0.33760 0.00349  -0.07492 -0.01356 111 LEU A CD1 
875  C CD2 . LEU A 111 ? 0.31628 0.48362 0.38093 -0.00361 -0.08995 -0.00737 111 LEU A CD2 
876  N N   . ILE A 112 ? 0.21639 0.30499 0.24170 0.02567  -0.03793 -0.00092 112 ILE A N   
877  C CA  . ILE A 112 ? 0.24113 0.31393 0.26831 0.02380  -0.02528 -0.00750 112 ILE A CA  
878  C C   . ILE A 112 ? 0.29277 0.35950 0.31076 0.01342  -0.02663 -0.01932 112 ILE A C   
879  O O   . ILE A 112 ? 0.28170 0.34696 0.28179 0.00922  -0.03305 -0.02464 112 ILE A O   
880  C CB  . ILE A 112 ? 0.25539 0.30803 0.26836 0.02939  -0.01526 -0.00523 112 ILE A CB  
881  C CG1 . ILE A 112 ? 0.28084 0.32635 0.26980 0.02750  -0.01792 -0.00634 112 ILE A CG1 
882  C CG2 . ILE A 112 ? 0.25341 0.30536 0.27678 0.03963  -0.01142 0.00479  112 ILE A CG2 
883  C CD1 . ILE A 112 ? 0.24519 0.27309 0.22336 0.02921  -0.00845 -0.00552 112 ILE A CD1 
884  N N   . MET A 113 ? 0.23721 0.29857 0.26623 0.00984  -0.01940 -0.02318 113 MET A N   
885  C CA  . MET A 113 ? 0.24442 0.29603 0.26868 0.00112  -0.01874 -0.03287 113 MET A CA  
886  C C   . MET A 113 ? 0.27524 0.31889 0.30990 0.00082  -0.00808 -0.03152 113 MET A C   
887  O O   . MET A 113 ? 0.23444 0.28317 0.28005 0.00592  -0.00210 -0.02498 113 MET A O   
888  C CB  . MET A 113 ? 0.23528 0.29912 0.26782 -0.00878 -0.02988 -0.03843 113 MET A CB  
889  C CG  . MET A 113 ? 0.27850 0.36306 0.34087 -0.01126 -0.03218 -0.03235 113 MET A CG  
890  S SD  . MET A 113 ? 0.37174 0.47298 0.44660 -0.02652 -0.04787 -0.03925 113 MET A SD  
891  C CE  . MET A 113 ? 0.23243 0.34994 0.29288 -0.02249 -0.06354 -0.03596 113 MET A CE  
892  N N   . HIS A 114 ? 0.25206 0.28192 0.28172 -0.00453 -0.00504 -0.03746 114 HIS A N   
893  C CA  . HIS A 114 ? 0.22214 0.24503 0.25986 -0.00569 0.00400  -0.03429 114 HIS A CA  
894  C C   . HIS A 114 ? 0.22115 0.25808 0.28200 -0.01166 0.00426  -0.03129 114 HIS A C   
895  O O   . HIS A 114 ? 0.21128 0.25121 0.28091 -0.00943 0.01320  -0.02508 114 HIS A O   
896  C CB  . HIS A 114 ? 0.23737 0.24182 0.26649 -0.00876 0.00679  -0.03883 114 HIS A CB  
897  C CG  . HIS A 114 ? 0.28251 0.27929 0.31676 -0.00971 0.01512  -0.03308 114 HIS A CG  
898  N ND1 . HIS A 114 ? 0.24137 0.23754 0.26995 -0.00404 0.02148  -0.02670 114 HIS A ND1 
899  C CD2 . HIS A 114 ? 0.28301 0.27144 0.32557 -0.01633 0.01809  -0.03221 114 HIS A CD2 
900  C CE1 . HIS A 114 ? 0.26088 0.25038 0.29171 -0.00668 0.02771  -0.02172 114 HIS A CE1 
901  N NE2 . HIS A 114 ? 0.24144 0.22604 0.28197 -0.01384 0.02620  -0.02381 114 HIS A NE2 
902  N N   . GLY A 115 ? 0.21086 0.25756 0.28154 -0.02000 -0.00521 -0.03582 115 GLY A N   
903  C CA  . GLY A 115 ? 0.21912 0.28414 0.31675 -0.02754 -0.00664 -0.03244 115 GLY A CA  
904  C C   . GLY A 115 ? 0.24239 0.29829 0.34849 -0.04098 -0.00699 -0.03712 115 GLY A C   
905  O O   . GLY A 115 ? 0.25696 0.32995 0.38761 -0.05067 -0.01064 -0.03540 115 GLY A O   
906  N N   . ASP A 116 ? 0.24262 0.27239 0.33189 -0.04198 -0.00319 -0.04220 116 ASP A N   
907  C CA  . ASP A 116 ? 0.27524 0.29106 0.37302 -0.05425 -0.00230 -0.04585 116 ASP A CA  
908  C C   . ASP A 116 ? 0.26209 0.28042 0.36276 -0.06654 -0.01564 -0.05752 116 ASP A C   
909  O O   . ASP A 116 ? 0.30873 0.32422 0.42588 -0.08061 -0.01750 -0.05989 116 ASP A O   
910  C CB  . ASP A 116 ? 0.31253 0.29890 0.39303 -0.04985 0.00503  -0.04721 116 ASP A CB  
911  C CG  . ASP A 116 ? 0.33318 0.30846 0.39062 -0.04259 0.00105  -0.05636 116 ASP A CG  
912  O OD1 . ASP A 116 ? 0.30022 0.28739 0.34812 -0.03398 -0.00088 -0.05474 116 ASP A OD1 
913  O OD2 . ASP A 116 ? 0.31983 0.27345 0.36923 -0.04539 0.00109  -0.06503 116 ASP A OD2 
914  N N   . THR A 117 ? 0.28154 0.30463 0.36508 -0.06271 -0.02518 -0.06482 117 THR A N   
915  C CA  . THR A 117 ? 0.28076 0.30726 0.36132 -0.07496 -0.03950 -0.07692 117 THR A CA  
916  C C   . THR A 117 ? 0.32519 0.38449 0.43372 -0.08450 -0.05026 -0.07193 117 THR A C   
917  O O   . THR A 117 ? 0.32220 0.38707 0.43263 -0.09848 -0.06422 -0.08156 117 THR A O   
918  C CB  . THR A 117 ? 0.37760 0.40164 0.42832 -0.06766 -0.04584 -0.08438 117 THR A CB  
919  O OG1 . THR A 117 ? 0.32669 0.37358 0.37923 -0.05659 -0.04749 -0.07315 117 THR A OG1 
920  C CG2 . THR A 117 ? 0.37803 0.37289 0.40572 -0.05873 -0.03470 -0.08956 117 THR A CG2 
921  N N   . LEU A 118 ? 0.25011 0.33182 0.38061 -0.07731 -0.04419 -0.05765 118 LEU A N   
922  C CA  . LEU A 118 ? 0.26703 0.38317 0.43164 -0.08490 -0.05176 -0.05070 118 LEU A CA  
923  C C   . LEU A 118 ? 0.31059 0.42709 0.50315 -0.09926 -0.04555 -0.04811 118 LEU A C   
924  O O   . LEU A 118 ? 0.28292 0.42986 0.50891 -0.10865 -0.05170 -0.04268 118 LEU A O   
925  C CB  . LEU A 118 ? 0.26704 0.40641 0.44455 -0.06896 -0.04553 -0.03668 118 LEU A CB  
926  C CG  . LEU A 118 ? 0.24756 0.38675 0.40115 -0.05443 -0.05019 -0.03573 118 LEU A CG  
927  C CD1 . LEU A 118 ? 0.24913 0.40133 0.41500 -0.03834 -0.03976 -0.02274 118 LEU A CD1 
928  C CD2 . LEU A 118 ? 0.29977 0.45803 0.45112 -0.06056 -0.07092 -0.03945 118 LEU A CD2 
929  N N   . CYS A 119 ? 0.28487 0.36972 0.46648 -0.10116 -0.03358 -0.05028 119 CYS A N   
930  C CA  . CYS A 119 ? 0.34968 0.43077 0.55554 -0.11402 -0.02497 -0.04492 119 CYS A CA  
931  C C   . CYS A 119 ? 0.42941 0.49260 0.63649 -0.13421 -0.03525 -0.05810 119 CYS A C   
932  O O   . CYS A 119 ? 0.44654 0.47703 0.64682 -0.13998 -0.02757 -0.06103 119 CYS A O   
933  C CB  . CYS A 119 ? 0.34033 0.39698 0.53327 -0.10428 -0.00655 -0.03710 119 CYS A CB  
934  S SG  . CYS A 119 ? 0.33734 0.41189 0.52830 -0.08409 0.00669  -0.02352 119 CYS A SG  
935  N N   . THR A 120 ? 0.39892 0.48365 0.61470 -0.14520 -0.05364 -0.06591 120 THR A N   
936  C CA  . THR A 120 ? 0.46595 0.53295 0.67582 -0.16502 -0.06685 -0.08273 120 THR A CA  
937  C C   . THR A 120 ? 0.46724 0.53075 0.70907 -0.18665 -0.06421 -0.08048 120 THR A C   
938  O O   . THR A 120 ? 0.52820 0.57186 0.76605 -0.20541 -0.07439 -0.09557 120 THR A O   
939  C CB  . THR A 120 ? 0.40821 0.50298 0.61570 -0.17129 -0.08946 -0.09079 120 THR A CB  
940  O OG1 . THR A 120 ? 0.36677 0.50879 0.61555 -0.17558 -0.09544 -0.07710 120 THR A OG1 
941  C CG2 . THR A 120 ? 0.43659 0.53025 0.60934 -0.15133 -0.09142 -0.09263 120 THR A CG2 
942  N N   . ASP A 121 ? 0.44890 0.52953 0.72089 -0.18546 -0.05021 -0.06270 121 ASP A N   
943  C CA  . ASP A 121 ? 0.48037 0.55533 0.78233 -0.20618 -0.04469 -0.05813 121 ASP A CA  
944  C C   . ASP A 121 ? 0.51574 0.54241 0.80012 -0.20444 -0.02853 -0.05693 121 ASP A C   
945  O O   . ASP A 121 ? 0.52107 0.52778 0.81910 -0.22321 -0.02666 -0.05782 121 ASP A O   
946  C CB  . ASP A 121 ? 0.44984 0.56754 0.79367 -0.20643 -0.03512 -0.03834 121 ASP A CB  
947  C CG  . ASP A 121 ? 0.56016 0.72885 0.93051 -0.20884 -0.05153 -0.03697 121 ASP A CG  
948  O OD1 . ASP A 121 ? 0.46234 0.63736 0.83366 -0.22548 -0.07173 -0.04871 121 ASP A OD1 
949  O OD2 . ASP A 121 ? 0.54343 0.74403 0.92765 -0.19231 -0.04380 -0.02370 121 ASP A OD2 
950  N N   . ASP A 122 ? 0.51245 0.52017 0.76679 -0.18224 -0.01762 -0.05360 122 ASP A N   
951  C CA  . ASP A 122 ? 0.51802 0.48303 0.75578 -0.17740 -0.00346 -0.04989 122 ASP A CA  
952  C C   . ASP A 122 ? 0.57317 0.49843 0.78408 -0.17944 -0.01118 -0.06967 122 ASP A C   
953  O O   . ASP A 122 ? 0.48110 0.39196 0.66201 -0.16218 -0.01039 -0.07596 122 ASP A O   
954  C CB  . ASP A 122 ? 0.55267 0.51937 0.77244 -0.15388 0.00982  -0.03720 122 ASP A CB  
955  C CG  . ASP A 122 ? 0.55524 0.48811 0.76610 -0.15000 0.02474  -0.02641 122 ASP A CG  
956  O OD1 . ASP A 122 ? 0.61744 0.51587 0.82763 -0.16031 0.02448  -0.03206 122 ASP A OD1 
957  O OD2 . ASP A 122 ? 0.48183 0.42147 0.68534 -0.13656 0.03645  -0.01208 122 ASP A OD2 
958  N N   . GLN A 123 ? 0.42899 0.55034 0.87655 0.07436  -0.15433 -0.16034 123 GLN A N   
959  C CA  . GLN A 123 ? 0.40577 0.51871 0.85898 0.07636  -0.17088 -0.18557 123 GLN A CA  
960  C C   . GLN A 123 ? 0.40144 0.48443 0.84924 0.06173  -0.15595 -0.16704 123 GLN A C   
961  O O   . GLN A 123 ? 0.38009 0.44986 0.80132 0.06761  -0.16402 -0.18041 123 GLN A O   
962  C CB  . GLN A 123 ? 0.43189 0.56891 0.96785 0.07204  -0.19309 -0.21733 123 GLN A CB  
963  N N   . GLY A 124 ? 0.43878 0.51346 0.90998 0.04498  -0.13416 -0.13631 124 GLY A N   
964  C CA  . GLY A 124 ? 0.35382 0.40124 0.81679 0.03342  -0.11960 -0.11745 124 GLY A CA  
965  C C   . GLY A 124 ? 0.47109 0.49741 0.85074 0.04290  -0.11033 -0.10550 124 GLY A C   
966  O O   . GLY A 124 ? 0.38133 0.38907 0.74156 0.04164  -0.11058 -0.10820 124 GLY A O   
967  N N   . TYR A 125 ? 0.47377 0.50287 0.80641 0.05255  -0.10244 -0.09251 125 TYR A N   
968  C CA  . TYR A 125 ? 0.45797 0.46665 0.71749 0.06092  -0.09490 -0.08195 125 TYR A CA  
969  C C   . TYR A 125 ? 0.40927 0.41891 0.63355 0.07593  -0.11137 -0.10519 125 TYR A C   
970  O O   . TYR A 125 ? 0.43284 0.42549 0.61685 0.07826  -0.10754 -0.10173 125 TYR A O   
971  C CB  . TYR A 125 ? 0.42606 0.43537 0.64897 0.06815  -0.08402 -0.06350 125 TYR A CB  
972  C CG  . TYR A 125 ? 0.37006 0.36040 0.52343 0.07894  -0.08170 -0.05853 125 TYR A CG  
973  C CD1 . TYR A 125 ? 0.37870 0.34580 0.50466 0.07250  -0.06979 -0.04411 125 TYR A CD1 
974  C CD2 . TYR A 125 ? 0.34446 0.34084 0.46278 0.09589  -0.09161 -0.06797 125 TYR A CD2 
975  C CE1 . TYR A 125 ? 0.36440 0.31498 0.43487 0.08037  -0.06722 -0.03874 125 TYR A CE1 
976  C CE2 . TYR A 125 ? 0.37998 0.35806 0.44020 0.10479  -0.08795 -0.06004 125 TYR A CE2 
977  C CZ  . TYR A 125 ? 0.35840 0.31372 0.39746 0.09583  -0.07557 -0.04537 125 TYR A CZ  
978  O OH  . TYR A 125 ? 0.38798 0.32597 0.37673 0.10282  -0.07134 -0.03647 125 TYR A OH  
979  N N   . LEU A 126 ? 0.41367 0.44613 0.65222 0.08798  -0.12945 -0.12864 126 LEU A N   
980  C CA  . LEU A 126 ? 0.44818 0.48684 0.64974 0.10721  -0.14515 -0.15028 126 LEU A CA  
981  C C   . LEU A 126 ? 0.44325 0.47644 0.65726 0.10492  -0.15334 -0.16683 126 LEU A C   
982  O O   . LEU A 126 ? 0.47542 0.50488 0.64280 0.11798  -0.15608 -0.17205 126 LEU A O   
983  C CB  . LEU A 126 ? 0.44234 0.51056 0.66336 0.12235  -0.16513 -0.17532 126 LEU A CB  
984  C CG  . LEU A 126 ? 0.49445 0.57007 0.68532 0.13367  -0.16107 -0.16372 126 LEU A CG  
985  C CD1 . LEU A 126 ? 0.52586 0.63352 0.73561 0.15144  -0.18364 -0.19269 126 LEU A CD1 
986  C CD2 . LEU A 126 ? 0.54770 0.60315 0.66238 0.14524  -0.15032 -0.14491 126 LEU A CD2 
987  N N   . ALA A 127 ? 0.37919 0.41239 0.65734 0.08920  -0.15679 -0.17416 127 ALA A N   
988  C CA  . ALA A 127 ? 0.42576 0.45031 0.71861 0.08656  -0.16437 -0.18921 127 ALA A CA  
989  C C   . ALA A 127 ? 0.40663 0.40575 0.65675 0.08010  -0.14529 -0.16499 127 ALA A C   
990  O O   . ALA A 127 ? 0.37951 0.37466 0.60120 0.08871  -0.14989 -0.17522 127 ALA A O   
991  C CB  . ALA A 127 ? 0.36604 0.39223 0.74248 0.06981  -0.17115 -0.19887 127 ALA A CB  
992  N N   . PHE A 128 ? 0.41264 0.39738 0.65833 0.06667  -0.12435 -0.13401 128 PHE A N   
993  C CA  . PHE A 128 ? 0.39013 0.35310 0.59357 0.06214  -0.10722 -0.11210 128 PHE A CA  
994  C C   . PHE A 128 ? 0.36943 0.33130 0.50653 0.07732  -0.10638 -0.11097 128 PHE A C   
995  O O   . PHE A 128 ? 0.40802 0.36120 0.51646 0.07981  -0.10327 -0.11040 128 PHE A O   
996  C CB  . PHE A 128 ? 0.43305 0.38608 0.64042 0.05011  -0.08745 -0.08211 128 PHE A CB  
997  C CG  . PHE A 128 ? 0.43434 0.36746 0.59702 0.04753  -0.07155 -0.06151 128 PHE A CG  
998  C CD1 . PHE A 128 ? 0.46008 0.37961 0.63567 0.03784  -0.06405 -0.05387 128 PHE A CD1 
999  C CD2 . PHE A 128 ? 0.41241 0.34020 0.52348 0.05518  -0.06499 -0.05036 128 PHE A CD2 
1000 C CE1 . PHE A 128 ? 0.40239 0.30658 0.53988 0.03629  -0.05108 -0.03754 128 PHE A CE1 
1001 C CE2 . PHE A 128 ? 0.41110 0.32152 0.48804 0.05205  -0.05222 -0.03398 128 PHE A CE2 
1002 C CZ  . PHE A 128 ? 0.42776 0.32796 0.51781 0.04279  -0.04560 -0.02850 128 PHE A CZ  
1003 N N   . ARG A 129 ? 0.35686 0.32821 0.47066 0.08806  -0.10837 -0.10907 129 ARG A N   
1004 C CA  . ARG A 129 ? 0.37900 0.34743 0.43219 0.10253  -0.10549 -0.10292 129 ARG A CA  
1005 C C   . ARG A 129 ? 0.44948 0.43087 0.48579 0.11831  -0.11856 -0.12440 129 ARG A C   
1006 O O   . ARG A 129 ? 0.40808 0.38328 0.40181 0.12456  -0.11118 -0.11553 129 ARG A O   
1007 C CB  . ARG A 129 ? 0.40394 0.38040 0.44008 0.11327  -0.10740 -0.09857 129 ARG A CB  
1008 C CG  . ARG A 129 ? 0.43829 0.40697 0.41426 0.12707  -0.10167 -0.08591 129 ARG A CG  
1009 C CD  . ARG A 129 ? 0.39670 0.37498 0.35723 0.14182  -0.10735 -0.08579 129 ARG A CD  
1010 N NE  . ARG A 129 ? 0.45919 0.42180 0.36742 0.15080  -0.09761 -0.06561 129 ARG A NE  
1011 C CZ  . ARG A 129 ? 0.51992 0.48562 0.38975 0.16642  -0.09856 -0.06455 129 ARG A CZ  
1012 N NH1 . ARG A 129 ? 0.53321 0.51951 0.40549 0.17767  -0.10994 -0.08499 129 ARG A NH1 
1013 N NH2 . ARG A 129 ? 0.55661 0.50518 0.38608 0.17208  -0.08782 -0.04212 129 ARG A NH2 
1014 N N   . ALA A 130 ? 0.42431 0.42613 0.49541 0.12614  -0.13837 -0.15340 130 ALA A N   
1015 C CA  . ALA A 130 ? 0.46433 0.48278 0.51963 0.14532  -0.15327 -0.17788 130 ALA A CA  
1016 C C   . ALA A 130 ? 0.43589 0.44304 0.48981 0.13846  -0.14794 -0.17747 130 ALA A C   
1017 O O   . ALA A 130 ? 0.49601 0.51127 0.51182 0.15383  -0.14875 -0.18199 130 ALA A O   
1018 C CB  . ALA A 130 ? 0.41621 0.45859 0.51807 0.15440  -0.17850 -0.21347 130 ALA A CB  
1019 N N   . LYS A 131 ? 0.40639 0.39667 0.50101 0.11699  -0.14163 -0.17070 131 LYS A N   
1020 C CA  . LYS A 131 ? 0.43828 0.41722 0.53424 0.11086  -0.13723 -0.17070 131 LYS A CA  
1021 C C   . LYS A 131 ? 0.44474 0.41070 0.48897 0.10876  -0.11709 -0.14395 131 LYS A C   
1022 O O   . LYS A 131 ? 0.46014 0.43235 0.47418 0.11945  -0.11655 -0.14812 131 LYS A O   
1023 C CB  . LYS A 131 ? 0.47049 0.43392 0.62330 0.08985  -0.13455 -0.16685 131 LYS A CB  
1024 N N   . VAL A 132 ? 0.42742 0.37731 0.46305 0.09593  -0.10081 -0.11711 132 VAL A N   
1025 C CA  . VAL A 132 ? 0.44169 0.37735 0.43807 0.09138  -0.08308 -0.09335 132 VAL A CA  
1026 C C   . VAL A 132 ? 0.43210 0.37566 0.37906 0.10686  -0.08010 -0.08691 132 VAL A C   
1027 O O   . VAL A 132 ? 0.44236 0.37627 0.36018 0.10375  -0.06635 -0.06869 132 VAL A O   
1028 C CB  . VAL A 132 ? 0.42797 0.34554 0.43008 0.07617  -0.06901 -0.06974 132 VAL A CB  
1029 C CG1 . VAL A 132 ? 0.35262 0.26259 0.39974 0.06201  -0.06757 -0.06949 132 VAL A CG1 
1030 C CG2 . VAL A 132 ? 0.43195 0.35399 0.43004 0.08109  -0.07101 -0.06543 132 VAL A CG2 
1031 N N   . HIS A 133 ? 0.45702 0.41851 0.39566 0.12399  -0.09233 -0.10031 133 HIS A N   
1032 C CA  . HIS A 133 ? 0.43372 0.40556 0.32480 0.14268  -0.08962 -0.09346 133 HIS A CA  
1033 C C   . HIS A 133 ? 0.50347 0.49981 0.38162 0.16263  -0.10015 -0.11405 133 HIS A C   
1034 O O   . HIS A 133 ? 0.50137 0.51207 0.33931 0.18235  -0.09796 -0.10853 133 HIS A O   
1035 C CB  . HIS A 133 ? 0.49837 0.47612 0.37957 0.15382  -0.09537 -0.09236 133 HIS A CB  
1036 C CG  . HIS A 133 ? 0.47863 0.43405 0.34490 0.14369  -0.08088 -0.06506 133 HIS A CG  
1037 N ND1 . HIS A 133 ? 0.50479 0.44565 0.39956 0.12642  -0.07709 -0.05871 133 HIS A ND1 
1038 C CD2 . HIS A 133 ? 0.49961 0.44493 0.32709 0.14962  -0.06966 -0.04271 133 HIS A CD2 
1039 C CE1 . HIS A 133 ? 0.41031 0.33382 0.28282 0.12354  -0.06605 -0.03696 133 HIS A CE1 
1040 N NE2 . HIS A 133 ? 0.51728 0.44098 0.35121 0.13620  -0.06174 -0.02693 133 HIS A NE2 
1041 N N   . THR A 134 ? 0.44490 0.44689 0.35596 0.15977  -0.11139 -0.13696 134 THR A N   
1042 C CA  . THR A 134 ? 0.50953 0.53529 0.40830 0.18020  -0.12213 -0.15881 134 THR A CA  
1043 C C   . THR A 134 ? 0.52009 0.54297 0.38826 0.17839  -0.10463 -0.13998 134 THR A C   
1044 O O   . THR A 134 ? 0.48233 0.48486 0.36612 0.15751  -0.09378 -0.12783 134 THR A O   
1045 C CB  . THR A 134 ? 0.49252 0.52187 0.44131 0.17724  -0.14117 -0.19065 134 THR A CB  
1046 O OG1 . THR A 134 ? 0.48878 0.52094 0.47466 0.17535  -0.15606 -0.20607 134 THR A OG1 
1047 C CG2 . THR A 134 ? 0.50823 0.56519 0.44376 0.20305  -0.15613 -0.21870 134 THR A CG2 
1048 N N   . PRO A 135 ? 0.54309 0.58835 0.36876 0.20088  -0.10095 -0.13628 135 PRO A N   
1049 C CA  . PRO A 135 ? 0.58083 0.62530 0.37982 0.19752  -0.08108 -0.11329 135 PRO A CA  
1050 C C   . PRO A 135 ? 0.53972 0.58195 0.36048 0.18811  -0.08171 -0.12455 135 PRO A C   
1051 O O   . PRO A 135 ? 0.48695 0.51336 0.30750 0.17030  -0.06518 -0.10380 135 PRO A O   
1052 C CB  . PRO A 135 ? 0.59457 0.67188 0.34948 0.22901  -0.08047 -0.11247 135 PRO A CB  
1053 C CG  . PRO A 135 ? 0.64093 0.72527 0.39014 0.24374  -0.09342 -0.12137 135 PRO A CG  
1054 C CD  . PRO A 135 ? 0.55166 0.62513 0.35058 0.23097  -0.11257 -0.14871 135 PRO A CD  
1055 N N   . TRP A 136 ? 0.49886 0.55628 0.34017 0.20044  -0.10160 -0.15826 136 TRP A N   
1056 C CA  . TRP A 136 ? 0.52232 0.57646 0.38339 0.19361  -0.10280 -0.16905 136 TRP A CA  
1057 C C   . TRP A 136 ? 0.48489 0.50549 0.38660 0.16439  -0.09966 -0.16219 136 TRP A C   
1058 O O   . TRP A 136 ? 0.47001 0.48079 0.38012 0.15340  -0.09197 -0.15678 136 TRP A O   
1059 C CB  . TRP A 136 ? 0.50691 0.58584 0.38599 0.21397  -0.12558 -0.20389 136 TRP A CB  
1060 C CG  . TRP A 136 ? 0.53183 0.60400 0.46175 0.20838  -0.14715 -0.22687 136 TRP A CG  
1061 C CD1 . TRP A 136 ? 0.56280 0.65266 0.50314 0.22216  -0.16269 -0.24070 136 TRP A CD1 
1062 C CD2 . TRP A 136 ? 0.53735 0.58617 0.51906 0.18793  -0.15446 -0.23618 136 TRP A CD2 
1063 N NE1 . TRP A 136 ? 0.49194 0.57192 0.48915 0.21025  -0.17924 -0.25888 136 TRP A NE1 
1064 C CE2 . TRP A 136 ? 0.51366 0.56808 0.53735 0.18861  -0.17360 -0.25422 136 TRP A CE2 
1065 C CE3 . TRP A 136 ? 0.49101 0.51595 0.48947 0.16972  -0.14560 -0.22849 136 TRP A CE3 
1066 C CZ2 . TRP A 136 ? 0.51824 0.55557 0.60103 0.17021  -0.18230 -0.26172 136 TRP A CZ2 
1067 C CZ3 . TRP A 136 ? 0.50980 0.51677 0.56370 0.15273  -0.15433 -0.23479 136 TRP A CZ3 
1068 C CH2 . TRP A 136 ? 0.45252 0.46596 0.54843 0.15240  -0.17163 -0.24992 136 TRP A CH2 
1069 N N   . ILE A 137 ? 0.42123 0.42656 0.34746 0.15330  -0.10471 -0.16120 137 ILE A N   
1070 C CA  . ILE A 137 ? 0.44490 0.42167 0.40557 0.12791  -0.09845 -0.14938 137 ILE A CA  
1071 C C   . ILE A 137 ? 0.48398 0.44501 0.42119 0.11333  -0.07596 -0.11641 137 ILE A C   
1072 O O   . ILE A 137 ? 0.39190 0.33667 0.34297 0.09830  -0.06756 -0.10670 137 ILE A O   
1073 C CB  . ILE A 137 ? 0.48258 0.45271 0.47692 0.12175  -0.10866 -0.15603 137 ILE A CB  
1074 C CG1 . ILE A 137 ? 0.49894 0.48327 0.52797 0.13389  -0.13330 -0.19222 137 ILE A CG1 
1075 C CG2 . ILE A 137 ? 0.42128 0.36566 0.44598 0.09796  -0.09839 -0.13797 137 ILE A CG2 
1076 C CD1 . ILE A 137 ? 0.48192 0.45953 0.55967 0.12363  -0.14341 -0.19974 137 ILE A CD1 
1077 N N   . GLN A 138 ? 0.42440 0.38997 0.32725 0.11882  -0.06689 -0.09953 138 GLN A N   
1078 C CA  . GLN A 138 ? 0.43583 0.38619 0.32023 0.10576  -0.04768 -0.07075 138 GLN A CA  
1079 C C   . GLN A 138 ? 0.45792 0.41469 0.33025 0.10494  -0.03777 -0.06536 138 GLN A C   
1080 O O   . GLN A 138 ? 0.42896 0.37044 0.30825 0.08933  -0.02724 -0.05207 138 GLN A O   
1081 C CB  . GLN A 138 ? 0.42404 0.37699 0.27711 0.11358  -0.04126 -0.05437 138 GLN A CB  
1082 C CG  . GLN A 138 ? 0.47444 0.41914 0.33742 0.11264  -0.04826 -0.05527 138 GLN A CG  
1083 C CD  . GLN A 138 ? 0.54721 0.48723 0.37955 0.11780  -0.03958 -0.03452 138 GLN A CD  
1084 O OE1 . GLN A 138 ? 0.51117 0.45531 0.31617 0.12292  -0.02836 -0.01891 138 GLN A OE1 
1085 N NE2 . GLN A 138 ? 0.42825 0.35982 0.26735 0.11668  -0.04418 -0.03307 138 GLN A NE2 
1086 N N   A ARG A 139 ? 0.44080 0.42332 0.29480 0.12360  -0.04133 -0.07637 139 ARG A N   
1087 N N   B ARG A 139 ? 0.44047 0.42297 0.29446 0.12356  -0.04129 -0.07633 139 ARG A N   
1088 C CA  A ARG A 139 ? 0.45333 0.44758 0.29640 0.12480  -0.03135 -0.07147 139 ARG A CA  
1089 C CA  B ARG A 139 ? 0.45323 0.44723 0.29630 0.12456  -0.03116 -0.07116 139 ARG A CA  
1090 C C   A ARG A 139 ? 0.42905 0.41346 0.30148 0.11484  -0.03637 -0.08444 139 ARG A C   
1091 C C   B ARG A 139 ? 0.42876 0.41378 0.30088 0.11527  -0.03648 -0.08477 139 ARG A C   
1092 O O   A ARG A 139 ? 0.44555 0.42667 0.31800 0.10534  -0.02519 -0.07371 139 ARG A O   
1093 O O   B ARG A 139 ? 0.44548 0.42843 0.31698 0.10657  -0.02545 -0.07460 139 ARG A O   
1094 C CB  A ARG A 139 ? 0.51267 0.54157 0.32971 0.15109  -0.03510 -0.08242 139 ARG A CB  
1095 C CB  B ARG A 139 ? 0.51313 0.54170 0.32909 0.15061  -0.03405 -0.08074 139 ARG A CB  
1096 C CG  A ARG A 139 ? 0.56078 0.60201 0.34331 0.16331  -0.02548 -0.06281 139 ARG A CG  
1097 C CG  B ARG A 139 ? 0.56099 0.60039 0.34371 0.16240  -0.02529 -0.06168 139 ARG A CG  
1098 C CD  A ARG A 139 ? 0.60465 0.68470 0.35734 0.19049  -0.02349 -0.06701 139 ARG A CD  
1099 C CD  B ARG A 139 ? 0.60756 0.68336 0.35893 0.18592  -0.01845 -0.05882 139 ARG A CD  
1100 N NE  A ARG A 139 ? 0.61115 0.71200 0.36800 0.21288  -0.04599 -0.10299 139 ARG A NE  
1101 N NE  B ARG A 139 ? 0.63357 0.72525 0.35323 0.20624  -0.01645 -0.04855 139 ARG A NE  
1102 C CZ  A ARG A 139 ? 0.64515 0.75884 0.39345 0.23187  -0.05971 -0.11607 139 ARG A CZ  
1103 C CZ  B ARG A 139 ? 0.65884 0.77649 0.36837 0.23281  -0.03182 -0.06973 139 ARG A CZ  
1104 N NH1 A ARG A 139 ? 0.65676 0.76479 0.38496 0.23378  -0.05284 -0.09641 139 ARG A NH1 
1105 N NH1 B ARG A 139 ? 0.65245 0.78221 0.38453 0.24138  -0.05139 -0.10308 139 ARG A NH1 
1106 N NH2 A ARG A 139 ? 0.57599 0.70766 0.34736 0.24657  -0.08108 -0.14619 139 ARG A NH2 
1107 N NH2 B ARG A 139 ? 0.72017 0.84920 0.41234 0.24713  -0.02777 -0.05478 139 ARG A NH2 
1108 N N   . LEU A 140 ? 0.41492 0.39443 0.31536 0.11712  -0.05341 -0.10723 140 LEU A N   
1109 C CA  . LEU A 140 ? 0.44027 0.40763 0.37111 0.10883  -0.05841 -0.11781 140 LEU A CA  
1110 C C   . LEU A 140 ? 0.41904 0.35991 0.36412 0.08720  -0.04712 -0.09728 140 LEU A C   
1111 O O   . LEU A 140 ? 0.35390 0.28838 0.30553 0.08035  -0.04125 -0.09310 140 LEU A O   
1112 C CB  . LEU A 140 ? 0.43820 0.40455 0.40212 0.11556  -0.07952 -0.14552 140 LEU A CB  
1113 C CG  . LEU A 140 ? 0.52983 0.47656 0.53431 0.10513  -0.08549 -0.15351 140 LEU A CG  
1114 C CD1 . LEU A 140 ? 0.39291 0.34864 0.39161 0.11317  -0.08591 -0.16330 140 LEU A CD1 
1115 C CD2 . LEU A 140 ? 0.56077 0.50332 0.60606 0.10813  -0.10562 -0.17704 140 LEU A CD2 
1116 N N   . PHE A 141 ? 0.37249 0.30021 0.32097 0.07873  -0.04451 -0.08519 141 PHE A N   
1117 C CA  . PHE A 141 ? 0.38621 0.29256 0.34502 0.06215  -0.03444 -0.06669 141 PHE A CA  
1118 C C   . PHE A 141 ? 0.39166 0.29742 0.32707 0.05649  -0.01965 -0.04900 141 PHE A C   
1119 O O   . PHE A 141 ? 0.34214 0.23821 0.28586 0.04782  -0.01368 -0.04226 141 PHE A O   
1120 C CB  . PHE A 141 ? 0.38687 0.28387 0.35195 0.05756  -0.03523 -0.05891 141 PHE A CB  
1121 C CG  . PHE A 141 ? 0.39554 0.27482 0.36631 0.04468  -0.02496 -0.04021 141 PHE A CG  
1122 C CD1 . PHE A 141 ? 0.35740 0.22599 0.35790 0.03796  -0.02549 -0.03898 141 PHE A CD1 
1123 C CD2 . PHE A 141 ? 0.38193 0.25592 0.32920 0.04111  -0.01512 -0.02380 141 PHE A CD2 
1124 C CE1 . PHE A 141 ? 0.39351 0.25038 0.39554 0.03043  -0.01602 -0.02200 141 PHE A CE1 
1125 C CE2 . PHE A 141 ? 0.39915 0.25943 0.35064 0.03275  -0.00802 -0.01038 141 PHE A CE2 
1126 C CZ  . PHE A 141 ? 0.37615 0.22984 0.35269 0.02868  -0.00829 -0.00962 141 PHE A CZ  
1127 N N   . LEU A 142 ? 0.38050 0.29727 0.28880 0.06197  -0.01374 -0.04092 142 LEU A N   
1128 C CA  . LEU A 142 ? 0.38315 0.29936 0.27635 0.05505  0.00019  -0.02347 142 LEU A CA  
1129 C C   . LEU A 142 ? 0.40185 0.33129 0.29648 0.05626  0.00386  -0.02839 142 LEU A C   
1130 O O   . LEU A 142 ? 0.37688 0.30376 0.27105 0.04714  0.01376  -0.01692 142 LEU A O   
1131 C CB  . LEU A 142 ? 0.36828 0.29331 0.23607 0.06147  0.00662  -0.01106 142 LEU A CB  
1132 C CG  . LEU A 142 ? 0.37627 0.28674 0.23922 0.06003  0.00505  -0.00250 142 LEU A CG  
1133 C CD1 . LEU A 142 ? 0.41715 0.33875 0.25365 0.07134  0.00980  0.00824  142 LEU A CD1 
1134 C CD2 . LEU A 142 ? 0.39444 0.28245 0.26557 0.04510  0.01134  0.01085  142 LEU A CD2 
1135 N N   . ALA A 143 ? 0.38915 0.33373 0.28749 0.06826  -0.00517 -0.04710 143 ALA A N   
1136 C CA  . ALA A 143 ? 0.42577 0.38445 0.32588 0.07165  -0.00292 -0.05389 143 ALA A CA  
1137 C C   . ALA A 143 ? 0.44674 0.38863 0.36972 0.06237  -0.00509 -0.05718 143 ALA A C   
1138 O O   . ALA A 143 ? 0.44861 0.39942 0.37314 0.06268  -0.00125 -0.05915 143 ALA A O   
1139 C CB  . ALA A 143 ? 0.41298 0.39435 0.30838 0.09103  -0.01379 -0.07546 143 ALA A CB  
1140 N N   . LEU A 144 ? 0.33169 0.25187 0.27235 0.05559  -0.01035 -0.05652 144 LEU A N   
1141 C CA  . LEU A 144 ? 0.34106 0.24602 0.30200 0.04938  -0.01100 -0.05604 144 LEU A CA  
1142 C C   . LEU A 144 ? 0.36482 0.26590 0.31840 0.04025  0.00041  -0.04081 144 LEU A C   
1143 O O   . LEU A 144 ? 0.39899 0.30050 0.33893 0.03496  0.00760  -0.02892 144 LEU A O   
1144 C CB  . LEU A 144 ? 0.34389 0.23010 0.32639 0.04506  -0.01659 -0.05455 144 LEU A CB  
1145 C CG  . LEU A 144 ? 0.36334 0.25119 0.36493 0.05241  -0.03060 -0.07250 144 LEU A CG  
1146 C CD1 . LEU A 144 ? 0.37489 0.24805 0.39906 0.04576  -0.03311 -0.06653 144 LEU A CD1 
1147 C CD2 . LEU A 144 ? 0.32315 0.21074 0.34391 0.05866  -0.03898 -0.08823 144 LEU A CD2 
1148 N N   . PRO A 145 ? 0.40703 0.30426 0.37102 0.03946  0.00105  -0.04205 145 PRO A N   
1149 C CA  . PRO A 145 ? 0.38686 0.28194 0.34659 0.03275  0.00912  -0.03120 145 PRO A CA  
1150 C C   . PRO A 145 ? 0.39959 0.27872 0.35876 0.02650  0.01162  -0.01886 145 PRO A C   
1151 O O   . PRO A 145 ? 0.35880 0.22675 0.32658 0.02711  0.00798  -0.01716 145 PRO A O   
1152 C CB  . PRO A 145 ? 0.48618 0.37898 0.45820 0.03712  0.00660  -0.03656 145 PRO A CB  
1153 C CG  . PRO A 145 ? 0.42554 0.32447 0.40518 0.04594  -0.00150 -0.05178 145 PRO A CG  
1154 C CD  . PRO A 145 ? 0.42371 0.31932 0.40431 0.04655  -0.00676 -0.05495 145 PRO A CD  
1155 N N   . LEU A 146 ? 0.37966 0.35525 0.38199 0.07565  -0.13333 -0.12815 146 LEU A N   
1156 C CA  . LEU A 146 ? 0.35638 0.30924 0.32626 0.04494  -0.10742 -0.13316 146 LEU A CA  
1157 C C   . LEU A 146 ? 0.40625 0.30835 0.31771 0.03967  -0.11782 -0.13060 146 LEU A C   
1158 O O   . LEU A 146 ? 0.40783 0.26732 0.30507 0.02804  -0.09149 -0.13084 146 LEU A O   
1159 C CB  . LEU A 146 ? 0.33956 0.31674 0.29168 0.01909  -0.09596 -0.14412 146 LEU A CB  
1160 C CG  . LEU A 146 ? 0.48455 0.46970 0.46264 0.00935  -0.06471 -0.14674 146 LEU A CG  
1161 C CD1 . LEU A 146 ? 0.44715 0.44242 0.39785 -0.01680 -0.06125 -0.15730 146 LEU A CD1 
1162 C CD2 . LEU A 146 ? 0.38540 0.32630 0.35239 0.00288  -0.03041 -0.14107 146 LEU A CD2 
1163 N N   . PHE A 147 ? 0.42680 0.33040 0.30171 0.05011  -0.15304 -0.12300 147 PHE A N   
1164 C CA  . PHE A 147 ? 0.48105 0.33012 0.28689 0.04344  -0.15742 -0.10853 147 PHE A CA  
1165 C C   . PHE A 147 ? 0.48858 0.28865 0.30569 0.05404  -0.14616 -0.09050 147 PHE A C   
1166 O O   . PHE A 147 ? 0.56144 0.31209 0.33750 0.03835  -0.12534 -0.07795 147 PHE A O   
1167 C CB  . PHE A 147 ? 0.53930 0.40686 0.30314 0.05654  -0.19956 -0.09576 147 PHE A CB  
1168 C CG  . PHE A 147 ? 0.62166 0.49803 0.41946 0.09665  -0.22327 -0.07717 147 PHE A CG  
1169 C CD1 . PHE A 147 ? 0.58824 0.52342 0.45590 0.11172  -0.22101 -0.08258 147 PHE A CD1 
1170 C CD2 . PHE A 147 ? 0.69550 0.50893 0.44623 0.11592  -0.23679 -0.05274 147 PHE A CD2 
1171 C CE1 . PHE A 147 ? 0.48014 0.41097 0.36884 0.14295  -0.22790 -0.06990 147 PHE A CE1 
1172 C CE2 . PHE A 147 ? 0.68226 0.49220 0.46094 0.14884  -0.24376 -0.03836 147 PHE A CE2 
1173 C CZ  . PHE A 147 ? 0.54012 0.41027 0.38636 0.16063  -0.23768 -0.04939 147 PHE A CZ  
1174 N N   . ILE A 148 ? 0.43883 0.24944 0.30713 0.07611  -0.15717 -0.09036 148 ILE A N   
1175 C CA  . ILE A 148 ? 0.47273 0.23918 0.35274 0.07623  -0.14612 -0.07789 148 ILE A CA  
1176 C C   . ILE A 148 ? 0.49577 0.26679 0.41047 0.05289  -0.10943 -0.08306 148 ILE A C   
1177 O O   . ILE A 148 ? 0.45899 0.19612 0.36546 0.03684  -0.08881 -0.06996 148 ILE A O   
1178 C CB  . ILE A 148 ? 0.42385 0.19354 0.33750 0.10236  -0.16718 -0.07962 148 ILE A CB  
1179 C CG1 . ILE A 148 ? 0.51528 0.27474 0.39555 0.13188  -0.19635 -0.06755 148 ILE A CG1 
1180 C CG2 . ILE A 148 ? 0.41869 0.17058 0.34832 0.08424  -0.14809 -0.06686 148 ILE A CG2 
1181 C CD1 . ILE A 148 ? 0.61220 0.29864 0.43040 0.13381  -0.19867 -0.04300 148 ILE A CD1 
1182 N N   . ARG A 149 ? 0.39982 0.21489 0.35573 0.05188  -0.09820 -0.09950 149 ARG A N   
1183 C CA  . ARG A 149 ? 0.42324 0.24936 0.41596 0.03780  -0.06147 -0.09873 149 ARG A CA  
1184 C C   . ARG A 149 ? 0.43261 0.22735 0.38684 0.01820  -0.02771 -0.09490 149 ARG A C   
1185 O O   . ARG A 149 ? 0.43205 0.21949 0.40991 0.00854  0.00262  -0.08353 149 ARG A O   
1186 C CB  . ARG A 149 ? 0.35445 0.23440 0.38021 0.03944  -0.04844 -0.10300 149 ARG A CB  
1187 C CG  . ARG A 149 ? 0.34288 0.26403 0.40638 0.04897  -0.06436 -0.09371 149 ARG A CG  
1188 C CD  . ARG A 149 ? 0.34223 0.30007 0.42267 0.04691  -0.05229 -0.09460 149 ARG A CD  
1189 N NE  . ARG A 149 ? 0.28428 0.26473 0.36125 0.05341  -0.06922 -0.10225 149 ARG A NE  
1190 C CZ  . ARG A 149 ? 0.34781 0.34479 0.42603 0.04742  -0.05622 -0.10798 149 ARG A CZ  
1191 N NH1 . ARG A 149 ? 0.28058 0.26356 0.35034 0.03593  -0.02643 -0.10461 149 ARG A NH1 
1192 N NH2 . ARG A 149 ? 0.28428 0.30756 0.37140 0.05623  -0.07231 -0.11722 149 ARG A NH2 
1193 N N   . HIS A 150 ? 0.42094 0.20247 0.31530 0.01013  -0.03071 -0.10264 150 HIS A N   
1194 C CA  . HIS A 150 ? 0.48392 0.22584 0.32287 -0.01148 0.00385  -0.09943 150 HIS A CA  
1195 C C   . HIS A 150 ? 0.52864 0.22858 0.34243 -0.01756 0.00981  -0.07698 150 HIS A C   
1196 O O   . HIS A 150 ? 0.55649 0.23239 0.36572 -0.03222 0.05273  -0.06908 150 HIS A O   
1197 C CB  . HIS A 150 ? 0.55681 0.29286 0.32483 -0.02370 -0.01105 -0.11258 150 HIS A CB  
1198 C CG  . HIS A 150 ? 0.71588 0.41557 0.42923 -0.04992 0.03363  -0.12305 150 HIS A CG  
1199 N ND1 . HIS A 150 ? 0.82836 0.54139 0.56858 -0.05534 0.06732  -0.13722 150 HIS A ND1 
1200 C CD2 . HIS A 150 ? 0.83983 0.48748 0.47053 -0.07053 0.05229  -0.11813 150 HIS A CD2 
1201 C CE1 . HIS A 150 ? 0.92754 0.60549 0.61529 -0.07603 0.10351  -0.13645 150 HIS A CE1 
1202 N NE2 . HIS A 150 ? 0.93484 0.56433 0.54538 -0.08875 0.09827  -0.13127 150 HIS A NE2 
1203 N N   . ARG A 151 ? 0.54411 0.23088 0.34054 -0.00558 -0.02831 -0.06556 151 ARG A N   
1204 C CA  . ARG A 151 ? 0.60282 0.23773 0.36627 -0.01373 -0.02121 -0.04380 151 ARG A CA  
1205 C C   . ARG A 151 ? 0.58050 0.22407 0.41127 -0.02256 0.00137  -0.03611 151 ARG A C   
1206 O O   . ARG A 151 ? 0.62284 0.23652 0.44274 -0.04211 0.03303  -0.02215 151 ARG A O   
1207 C CB  . ARG A 151 ? 0.64224 0.25220 0.36827 0.00615  -0.06471 -0.03211 151 ARG A CB  
1208 C CG  . ARG A 151 ? 0.77256 0.36307 0.41465 0.00969  -0.08468 -0.02631 151 ARG A CG  
1209 C CD  . ARG A 151 ? 0.84872 0.45971 0.48883 0.04303  -0.13429 -0.02183 151 ARG A CD  
1210 N NE  . ARG A 151 ? 1.04205 0.59115 0.63890 0.05959  -0.14775 0.00415  151 ARG A NE  
1211 C CZ  . ARG A 151 ? 1.15923 0.70830 0.74684 0.09591  -0.18446 0.01597  151 ARG A CZ  
1212 N NH1 . ARG A 151 ? 1.06710 0.68588 0.69320 0.11844  -0.21343 0.00419  151 ARG A NH1 
1213 N NH2 . ARG A 151 ? 1.13094 0.60617 0.67011 0.11098  -0.18832 0.04137  151 ARG A NH2 
1214 N N   . ILE A 152 ? 0.49797 0.18593 0.39786 -0.01080 -0.01484 -0.04445 152 ILE A N   
1215 C CA  . ILE A 152 ? 0.53037 0.24113 0.49783 -0.02227 -0.00050 -0.03718 152 ILE A CA  
1216 C C   . ILE A 152 ? 0.49172 0.22967 0.49578 -0.03318 0.04698  -0.03368 152 ILE A C   
1217 O O   . ILE A 152 ? 0.48783 0.22841 0.52055 -0.05129 0.07397  -0.01873 152 ILE A O   
1218 C CB  . ILE A 152 ? 0.46596 0.21748 0.48745 -0.00734 -0.02985 -0.04783 152 ILE A CB  
1219 C CG1 . ILE A 152 ? 0.45415 0.16876 0.44089 0.00478  -0.06775 -0.04898 152 ILE A CG1 
1220 C CG2 . ILE A 152 ? 0.44936 0.24059 0.54325 -0.02176 -0.01820 -0.04021 152 ILE A CG2 
1221 C CD1 . ILE A 152 ? 0.43053 0.19013 0.45247 0.02086  -0.08825 -0.05937 152 ILE A CD1 
1222 N N   . ALA A 153 ? 0.44690 0.20371 0.45064 -0.02240 0.06154  -0.04697 153 ALA A N   
1223 C CA  . ALA A 153 ? 0.51206 0.28726 0.54948 -0.02479 0.11231  -0.04338 153 ALA A CA  
1224 C C   . ALA A 153 ? 0.60176 0.33088 0.58938 -0.04318 0.15460  -0.03354 153 ALA A C   
1225 O O   . ALA A 153 ? 0.61076 0.35620 0.64262 -0.04827 0.19898  -0.02022 153 ALA A O   
1226 C CB  . ALA A 153 ? 0.46022 0.24476 0.48993 -0.01153 0.12203  -0.06194 153 ALA A CB  
1227 N N   . ALA A 154 ? 0.62067 0.29508 0.51634 -0.05200 0.14246  -0.03795 154 ALA A N   
1228 C CA  . ALA A 154 ? 0.75644 0.37658 0.58803 -0.07126 0.18252  -0.02854 154 ALA A CA  
1229 C C   . ALA A 154 ? 0.75815 0.37314 0.62029 -0.08606 0.19609  -0.00619 154 ALA A C   
1230 O O   . ALA A 154 ? 0.80372 0.40519 0.66807 -0.10008 0.24881  0.00488  154 ALA A O   
1231 C CB  . ALA A 154 ? 0.74368 0.31032 0.46537 -0.07723 0.15619  -0.03445 154 ALA A CB  
1232 N N   . ARG A 155 ? 0.68086 0.30325 0.56510 -0.08545 0.15308  -0.00021 155 ARG A N   
1233 C CA  . ARG A 155 ? 0.67060 0.28606 0.58342 -0.10740 0.16456  0.01827  155 ARG A CA  
1234 C C   . ARG A 155 ? 0.71096 0.40480 0.73877 -0.11219 0.18570  0.02462  155 ARG A C   
1235 O O   . ARG A 155 ? 0.78935 0.49457 0.85211 -0.13415 0.22351  0.04059  155 ARG A O   
1236 C CB  . ARG A 155 ? 0.72822 0.31215 0.61587 -0.10704 0.11509  0.02048  155 ARG A CB  
1237 C CG  . ARG A 155 ? 0.79755 0.37626 0.72136 -0.13589 0.12177  0.03456  155 ARG A CG  
1238 C CD  . ARG A 155 ? 0.95462 0.48598 0.83795 -0.16343 0.16936  0.05179  155 ARG A CD  
1239 N NE  . ARG A 155 ? 0.98828 0.43177 0.75233 -0.15680 0.16443  0.05679  155 ARG A NE  
1240 C CZ  . ARG A 155 ? 1.10251 0.47904 0.80290 -0.15918 0.14159  0.06681  155 ARG A CZ  
1241 N NH1 . ARG A 155 ? 0.93741 0.32092 0.67793 -0.17090 0.12381  0.06861  155 ARG A NH1 
1242 N NH2 . ARG A 155 ? 1.25273 0.56050 0.84653 -0.14719 0.13493  0.07487  155 ARG A NH2 
1243 N N   . MET A 156 ? 0.58322 0.33600 0.67194 -0.09174 0.16199  0.01446  156 MET A N   
1244 C CA  . MET A 156 ? 0.58254 0.41764 0.78027 -0.09256 0.17259  0.02445  156 MET A CA  
1245 C C   . MET A 156 ? 0.68310 0.54775 0.92104 -0.08543 0.23436  0.03500  156 MET A C   
1246 O O   . MET A 156 ? 0.66398 0.59286 0.98963 -0.09356 0.25734  0.05341  156 MET A O   
1247 C CB  . MET A 156 ? 0.50954 0.38998 0.74695 -0.06976 0.13245  0.01256  156 MET A CB  
1248 C CG  . MET A 156 ? 0.50550 0.38305 0.74424 -0.08070 0.08054  0.00807  156 MET A CG  
1249 S SD  . MET A 156 ? 0.46396 0.39327 0.74518 -0.05468 0.04197  -0.00498 156 MET A SD  
1250 C CE  . MET A 156 ? 0.41677 0.43837 0.80203 -0.04661 0.07527  0.01408  156 MET A CE  
1251 N N   . ARG A 157 ? 0.63492 0.45527 0.81085 -0.07089 0.26308  0.02380  157 ARG A N   
1252 C CA  . ARG A 157 ? 0.67466 0.50240 0.87260 -0.06222 0.33116  0.03222  157 ARG A CA  
1253 C C   . ARG A 157 ? 0.74211 0.56066 0.93489 -0.08074 0.35986  0.04615  157 ARG A C   
1254 O O   . ARG A 157 ? 0.83556 0.70559 1.09354 -0.06938 0.38324  0.05860  157 ARG A O   
1255 C CB  . ARG A 157 ? 0.70780 0.46847 0.81263 -0.05222 0.35323  0.01178  157 ARG A CB  
1256 C CG  . ARG A 157 ? 0.55910 0.34068 0.67969 -0.02687 0.33453  -0.00394 157 ARG A CG  
1257 C CD  . ARG A 157 ? 0.72039 0.43706 0.75759 -0.02345 0.36285  -0.02288 157 ARG A CD  
1258 N NE  . ARG A 157 ? 0.78443 0.44162 0.71353 -0.04446 0.34234  -0.04205 157 ARG A NE  
1259 C CZ  . ARG A 157 ? 0.72367 0.38683 0.62871 -0.04239 0.28802  -0.05911 157 ARG A CZ  
1260 N NH1 . ARG A 157 ? 0.66334 0.37830 0.63542 -0.02306 0.26177  -0.06248 157 ARG A NH1 
1261 N NH2 . ARG A 157 ? 0.77884 0.39844 0.59073 -0.05927 0.25982  -0.07120 157 ARG A NH2 
1262 N N   . ALA A 158 ? 0.80533 0.55514 0.91488 -0.10720 0.35308  0.04535  158 ALA A N   
1263 C CA  . ALA A 158 ? 0.84613 0.58508 0.94619 -0.12706 0.37716  0.05784  158 ALA A CA  
1264 C C   . ALA A 158 ? 0.83570 0.64843 1.03357 -0.14507 0.35989  0.07445  158 ALA A C   
1265 O O   . ALA A 158 ? 0.80234 0.64653 1.03769 -0.15587 0.38744  0.08717  158 ALA A O   
1266 C CB  . ALA A 158 ? 0.89701 0.54042 0.87589 -0.14742 0.36669  0.05505  158 ALA A CB  
1267 N N   . ASP A 159 ? 0.79929 0.63965 1.03674 -0.15128 0.31303  0.07295  159 ASP A N   
1268 C CA  . ASP A 159 ? 0.76062 0.66976 1.08090 -0.17488 0.28975  0.08461  159 ASP A CA  
1269 C C   . ASP A 159 ? 0.70022 0.71847 1.12822 -0.15581 0.30209  0.09584  159 ASP A C   
1270 O O   . ASP A 159 ? 0.61578 0.69156 1.09880 -0.17488 0.31163  0.11010  159 ASP A O   
1271 C CB  . ASP A 159 ? 0.74705 0.64483 1.06724 -0.18478 0.23279  0.07500  159 ASP A CB  
1272 C CG  . ASP A 159 ? 0.93071 0.72193 1.14596 -0.20415 0.21310  0.06916  159 ASP A CG  
1273 O OD1 . ASP A 159 ? 0.87442 0.64086 1.06103 -0.19809 0.16221  0.05670  159 ASP A OD1 
1274 O OD2 . ASP A 159 ? 0.96376 0.70115 1.11468 -0.21526 0.24139  0.07640  159 ASP A OD2 
1275 N N   . SER A 160 ? 0.69960 0.53785 1.16002 0.07533  -0.08730 0.31219  160 SER A N   
1276 C CA  . SER A 160 ? 0.62998 0.47574 1.07473 0.06192  -0.07976 0.29366  160 SER A CA  
1277 C C   . SER A 160 ? 0.68813 0.55888 1.08446 0.06524  -0.07188 0.32923  160 SER A C   
1278 O O   . SER A 160 ? 0.73767 0.61033 1.13985 0.04974  -0.05685 0.33340  160 SER A O   
1279 C CB  . SER A 160 ? 0.56362 0.41700 0.99197 0.06675  -0.09172 0.25333  160 SER A CB  
1280 O OG  . SER A 160 ? 0.53102 0.36456 1.00118 0.06134  -0.09224 0.21636  160 SER A OG  
1281 N N   . ILE A 171 ? 0.76394 0.80917 0.92953 0.02489  -0.00718 0.25886  171 ILE A N   
1282 C CA  . ILE A 171 ? 0.75793 0.78721 0.94702 0.01151  -0.01521 0.21569  171 ILE A CA  
1283 C C   . ILE A 171 ? 0.79088 0.83046 0.99986 -0.00471 -0.00292 0.20773  171 ILE A C   
1284 O O   . ILE A 171 ? 0.75308 0.82177 0.93348 -0.00103 0.00698  0.21201  171 ILE A O   
1285 C CB  . ILE A 171 ? 0.71126 0.74884 0.86093 0.02230  -0.02900 0.18071  171 ILE A CB  
1286 C CG1 . ILE A 171 ? 0.66879 0.70262 0.80311 0.03951  -0.04374 0.18819  171 ILE A CG1 
1287 C CG2 . ILE A 171 ? 0.55928 0.57875 0.73107 0.01093  -0.03422 0.14225  171 ILE A CG2 
1288 C CD1 . ILE A 171 ? 0.52572 0.57518 0.62357 0.05171  -0.05680 0.15914  171 ILE A CD1 
1289 N N   . MET A 172 ? 0.76984 0.78688 1.02978 -0.02132 -0.00498 0.19375  172 MET A N   
1290 C CA  . MET A 172 ? 0.67136 0.69900 0.95622 -0.03642 0.00125  0.18165  172 MET A CA  
1291 C C   . MET A 172 ? 0.63854 0.67901 0.88768 -0.03327 -0.00598 0.14422  172 MET A C   
1292 O O   . MET A 172 ? 0.65609 0.69074 0.87252 -0.02289 -0.01532 0.12461  172 MET A O   
1293 C CB  . MET A 172 ? 0.63069 0.63076 0.98061 -0.05340 -0.00355 0.17183  172 MET A CB  
1294 C CG  . MET A 172 ? 0.75642 0.76895 1.15618 -0.06981 0.00711  0.18487  172 MET A CG  
1295 S SD  . MET A 172 ? 0.71901 0.69865 1.20290 -0.08992 -0.00340 0.16562  172 MET A SD  
1296 C CE  . MET A 172 ? 0.58523 0.58858 1.13199 -0.10754 0.01304  0.19306  172 MET A CE  
1297 N N   . ASP A 173 ? 0.56158 0.62017 0.82293 -0.04214 -0.00118 0.13612  173 ASP A N   
1298 C CA  . ASP A 173 ? 0.49641 0.56941 0.72643 -0.03788 -0.00614 0.10726  173 ASP A CA  
1299 C C   . ASP A 173 ? 0.41538 0.47088 0.66460 -0.04635 -0.01916 0.07412  173 ASP A C   
1300 O O   . ASP A 173 ? 0.40467 0.43867 0.69360 -0.05620 -0.02487 0.06942  173 ASP A O   
1301 C CB  . ASP A 173 ? 0.46797 0.57518 0.69631 -0.03840 0.00627  0.11842  173 ASP A CB  
1302 C CG  . ASP A 173 ? 0.43273 0.55760 0.61408 -0.02546 0.00506  0.10049  173 ASP A CG  
1303 O OD1 . ASP A 173 ? 0.35585 0.46537 0.51231 -0.01897 -0.00573 0.07822  173 ASP A OD1 
1304 O OD2 . ASP A 173 ? 0.51118 0.66504 0.68530 -0.02154 0.01637  0.10891  173 ASP A OD2 
1305 N N   . VAL A 174 ? 0.36944 0.43432 0.58901 -0.04074 -0.02394 0.05058  174 VAL A N   
1306 C CA  . VAL A 174 ? 0.33400 0.38504 0.55647 -0.04358 -0.03589 0.01981  174 VAL A CA  
1307 C C   . VAL A 174 ? 0.29563 0.35709 0.55777 -0.05598 -0.04177 0.01280  174 VAL A C   
1308 O O   . VAL A 174 ? 0.27524 0.36060 0.55879 -0.06129 -0.03447 0.02978  174 VAL A O   
1309 C CB  . VAL A 174 ? 0.35057 0.40737 0.52846 -0.03165 -0.03739 0.00256  174 VAL A CB  
1310 C CG1 . VAL A 174 ? 0.32990 0.38011 0.47976 -0.02073 -0.03285 0.00830  174 VAL A CG1 
1311 C CG2 . VAL A 174 ? 0.32923 0.41514 0.50027 -0.02975 -0.03420 0.00554  174 VAL A CG2 
1312 N N   . ASN A 175 ? 0.31809 0.36328 0.59190 -0.05963 -0.05538 -0.01428 175 ASN A N   
1313 C CA  . ASN A 175 ? 0.31309 0.36925 0.62248 -0.06937 -0.06775 -0.03038 175 ASN A CA  
1314 C C   . ASN A 175 ? 0.33864 0.41525 0.61287 -0.05998 -0.07443 -0.04574 175 ASN A C   
1315 O O   . ASN A 175 ? 0.30123 0.36765 0.52917 -0.04773 -0.07663 -0.06012 175 ASN A O   
1316 C CB  . ASN A 175 ? 0.31297 0.34317 0.64730 -0.07473 -0.08248 -0.05748 175 ASN A CB  
1317 C CG  . ASN A 175 ? 0.35677 0.39937 0.72848 -0.08353 -0.10106 -0.08122 175 ASN A CG  
1318 O OD1 . ASN A 175 ? 0.37752 0.43138 0.71809 -0.07500 -0.11390 -0.10441 175 ASN A OD1 
1319 N ND2 . ASN A 175 ? 0.37339 0.41433 0.81555 -0.10005 -0.10347 -0.07480 175 ASN A ND2 
1320 N N   . PRO A 176 ? 0.30537 0.41119 0.60369 -0.06447 -0.07632 -0.04082 176 PRO A N   
1321 C CA  . PRO A 176 ? 0.31242 0.43808 0.57887 -0.05313 -0.08278 -0.05187 176 PRO A CA  
1322 C C   . PRO A 176 ? 0.31711 0.43214 0.55907 -0.04587 -0.10223 -0.08283 176 PRO A C   
1323 O O   . PRO A 176 ? 0.28306 0.39835 0.47632 -0.03109 -0.10202 -0.08773 176 PRO A O   
1324 C CB  . PRO A 176 ? 0.33528 0.49438 0.65032 -0.06163 -0.08338 -0.04280 176 PRO A CB  
1325 C CG  . PRO A 176 ? 0.39193 0.55112 0.74669 -0.07369 -0.06605 -0.01539 176 PRO A CG  
1326 C CD  . PRO A 176 ? 0.30007 0.42357 0.65860 -0.07880 -0.06952 -0.02083 176 PRO A CD  
1327 N N   . GLN A 177 ? 0.31138 0.41682 0.58613 -0.05471 -0.11868 -0.10399 177 GLN A N   
1328 C CA  . GLN A 177 ? 0.33109 0.42909 0.57604 -0.04487 -0.13839 -0.13650 177 GLN A CA  
1329 C C   . GLN A 177 ? 0.39791 0.46728 0.59129 -0.03319 -0.12890 -0.14251 177 GLN A C   
1330 O O   . GLN A 177 ? 0.42252 0.49001 0.56668 -0.01787 -0.13442 -0.15761 177 GLN A O   
1331 C CB  . GLN A 177 ? 0.39415 0.49016 0.69210 -0.05690 -0.16077 -0.16311 177 GLN A CB  
1332 C CG  . GLN A 177 ? 0.51653 0.61158 0.78092 -0.04422 -0.18562 -0.20119 177 GLN A CG  
1333 C CD  . GLN A 177 ? 0.64737 0.77281 0.88373 -0.03154 -0.19820 -0.20282 177 GLN A CD  
1334 O OE1 . GLN A 177 ? 0.63973 0.79336 0.92151 -0.03958 -0.20588 -0.19575 177 GLN A OE1 
1335 N NE2 . GLN A 177 ? 0.57267 0.69315 0.73704 -0.01064 -0.19888 -0.20990 177 GLN A NE2 
1336 N N   . ALA A 178 ? 0.35075 0.39932 0.55597 -0.03890 -0.11382 -0.12899 178 ALA A N   
1337 C CA  . ALA A 178 ? 0.38408 0.40920 0.54872 -0.02784 -0.10261 -0.13238 178 ALA A CA  
1338 C C   . ALA A 178 ? 0.34871 0.38206 0.46472 -0.01426 -0.09031 -0.11920 178 ALA A C   
1339 O O   . ALA A 178 ? 0.35688 0.37855 0.43303 -0.00153 -0.08461 -0.12785 178 ALA A O   
1340 C CB  . ALA A 178 ? 0.38959 0.39539 0.58206 -0.03556 -0.09068 -0.11669 178 ALA A CB  
1341 N N   . VAL A 179 ? 0.34197 0.39537 0.46418 -0.01625 -0.08448 -0.09829 179 VAL A N   
1342 C CA  . VAL A 179 ? 0.31203 0.37211 0.39744 -0.00388 -0.07412 -0.08762 179 VAL A CA  
1343 C C   . VAL A 179 ? 0.35311 0.42089 0.40673 0.00853  -0.08362 -0.10019 179 VAL A C   
1344 O O   . VAL A 179 ? 0.34541 0.40331 0.36119 0.02152  -0.07498 -0.09960 179 VAL A O   
1345 C CB  . VAL A 179 ? 0.33493 0.41592 0.43645 -0.00735 -0.06688 -0.06694 179 VAL A CB  
1346 C CG1 . VAL A 179 ? 0.33719 0.42669 0.40894 0.00586  -0.06051 -0.06141 179 VAL A CG1 
1347 C CG2 . VAL A 179 ? 0.26966 0.34250 0.38565 -0.01349 -0.05565 -0.05131 179 VAL A CG2 
1348 N N   . VAL A 180 ? 0.33204 0.41880 0.40328 0.00551  -0.10156 -0.11003 180 VAL A N   
1349 C CA  . VAL A 180 ? 0.36014 0.45743 0.39943 0.01977  -0.11504 -0.12146 180 VAL A CA  
1350 C C   . VAL A 180 ? 0.40169 0.47942 0.40156 0.03030  -0.11774 -0.14072 180 VAL A C   
1351 O O   . VAL A 180 ? 0.41667 0.49285 0.36889 0.04779  -0.11431 -0.13910 180 VAL A O   
1352 C CB  . VAL A 180 ? 0.38410 0.50802 0.45938 0.01365  -0.13816 -0.13219 180 VAL A CB  
1353 C CG1 . VAL A 180 ? 0.37582 0.51117 0.41493 0.03080  -0.15800 -0.14740 180 VAL A CG1 
1354 C CG2 . VAL A 180 ? 0.33176 0.47900 0.44124 0.00735  -0.13062 -0.11116 180 VAL A CG2 
1355 N N   A ASP A 181 ? 0.40222 0.46455 0.42204 0.02122  -0.12204 -0.15805 181 ASP A N   
1356 N N   B ASP A 181 ? 0.40204 0.46426 0.42181 0.02122  -0.12190 -0.15794 181 ASP A N   
1357 C CA  A ASP A 181 ? 0.45177 0.49679 0.43514 0.03268  -0.12346 -0.18052 181 ASP A CA  
1358 C CA  B ASP A 181 ? 0.45206 0.49705 0.43551 0.03265  -0.12345 -0.18054 181 ASP A CA  
1359 C C   A ASP A 181 ? 0.45465 0.48300 0.39985 0.04413  -0.09703 -0.16575 181 ASP A C   
1360 C C   B ASP A 181 ? 0.45429 0.48246 0.39966 0.04407  -0.09705 -0.16596 181 ASP A C   
1361 O O   A ASP A 181 ? 0.49126 0.51609 0.38684 0.06183  -0.09221 -0.17179 181 ASP A O   
1362 O O   B ASP A 181 ? 0.49143 0.51581 0.38735 0.06169  -0.09226 -0.17241 181 ASP A O   
1363 C CB  A ASP A 181 ? 0.44304 0.47223 0.46551 0.02016  -0.13145 -0.20212 181 ASP A CB  
1364 C CB  B ASP A 181 ? 0.44277 0.47214 0.46552 0.02009  -0.13172 -0.20229 181 ASP A CB  
1365 C CG  A ASP A 181 ? 0.49629 0.50408 0.48437 0.03250  -0.12525 -0.22377 181 ASP A CG  
1366 C CG  B ASP A 181 ? 0.48239 0.52696 0.54656 0.01002  -0.16010 -0.22347 181 ASP A CG  
1367 O OD1 A ASP A 181 ? 0.54459 0.55781 0.48095 0.05061  -0.13160 -0.23969 181 ASP A OD1 
1368 O OD1 B ASP A 181 ? 0.48183 0.55125 0.53747 0.01542  -0.17561 -0.22483 181 ASP A OD1 
1369 O OD2 A ASP A 181 ? 0.50755 0.49437 0.51906 0.02599  -0.11319 -0.22387 181 ASP A OD2 
1370 O OD2 B ASP A 181 ? 0.48181 0.51350 0.59317 -0.00321 -0.16748 -0.23872 181 ASP A OD2 
1371 N N   . ALA A 182 ? 0.41741 0.43704 0.38648 0.03517  -0.07959 -0.14581 182 ALA A N   
1372 C CA  . ALA A 182 ? 0.47554 0.48114 0.42202 0.04401  -0.05591 -0.13321 182 ALA A CA  
1373 C C   . ALA A 182 ? 0.46336 0.47820 0.37832 0.05677  -0.04746 -0.11607 182 ALA A C   
1374 O O   . ALA A 182 ? 0.42772 0.43344 0.31033 0.07028  -0.03127 -0.11138 182 ALA A O   
1375 C CB  . ALA A 182 ? 0.41090 0.40856 0.39385 0.03223  -0.04513 -0.11865 182 ALA A CB  
1376 N N   . MET A 183 ? 0.39857 0.43145 0.32623 0.05343  -0.05646 -0.10530 183 MET A N   
1377 C CA  . MET A 183 ? 0.39820 0.43780 0.30517 0.06541  -0.04873 -0.08774 183 MET A CA  
1378 C C   . MET A 183 ? 0.44852 0.49381 0.31075 0.08322  -0.05667 -0.09242 183 MET A C   
1379 O O   . MET A 183 ? 0.45489 0.49736 0.29055 0.09760  -0.04417 -0.07542 183 MET A O   
1380 C CB  . MET A 183 ? 0.38039 0.43877 0.31700 0.05820  -0.05589 -0.07763 183 MET A CB  
1381 C CG  . MET A 183 ? 0.31070 0.36424 0.27608 0.04791  -0.04350 -0.06768 183 MET A CG  
1382 S SD  . MET A 183 ? 0.31595 0.39174 0.30443 0.04620  -0.04495 -0.05548 183 MET A SD  
1383 C CE  . MET A 183 ? 0.31325 0.37792 0.28562 0.06062  -0.02939 -0.04329 183 MET A CE  
1384 N N   . GLU A 184 ? 0.45599 0.50920 0.31049 0.08358  -0.07812 -0.11518 184 GLU A N   
1385 C CA  . GLU A 184 ? 0.49107 0.55163 0.29546 0.10343  -0.08958 -0.12385 184 GLU A CA  
1386 C C   . GLU A 184 ? 0.51766 0.56095 0.28004 0.11546  -0.07581 -0.13471 184 GLU A C   
1387 O O   . GLU A 184 ? 0.60234 0.64736 0.31029 0.13720  -0.07095 -0.12911 184 GLU A O   
1388 C CB  . GLU A 184 ? 0.49183 0.57327 0.31106 0.09963  -0.12384 -0.14790 184 GLU A CB  
1389 C CG  . GLU A 184 ? 0.46252 0.56693 0.31989 0.09250  -0.13600 -0.13566 184 GLU A CG  
1390 C CD  . GLU A 184 ? 0.54397 0.67366 0.41749 0.09226  -0.17084 -0.15806 184 GLU A CD  
1391 O OE1 . GLU A 184 ? 0.56177 0.68870 0.43742 0.08880  -0.18758 -0.18770 184 GLU A OE1 
1392 O OE2 . GLU A 184 ? 0.50299 0.65591 0.39242 0.09581  -0.18241 -0.14790 184 GLU A OE2 
1393 N N   . ARG A 185 ? 0.52363 0.55112 0.30987 0.10362  -0.06803 -0.14849 185 ARG A N   
1394 C CA  . ARG A 185 ? 0.56316 0.57426 0.31641 0.11541  -0.04867 -0.15680 185 ARG A CA  
1395 C C   . ARG A 185 ? 0.55759 0.56094 0.28866 0.12701  -0.01673 -0.12632 185 ARG A C   
1396 O O   . ARG A 185 ? 0.58912 0.58897 0.27069 0.14675  -0.00095 -0.12396 185 ARG A O   
1397 C CB  . ARG A 185 ? 0.55457 0.54939 0.35031 0.09980  -0.04377 -0.17150 185 ARG A CB  
1398 C CG  . ARG A 185 ? 0.62248 0.61585 0.42669 0.09640  -0.06724 -0.20856 185 ARG A CG  
1399 C CD  . ARG A 185 ? 0.64163 0.61407 0.48163 0.08685  -0.05644 -0.22025 185 ARG A CD  
1400 N NE  . ARG A 185 ? 0.57209 0.54051 0.47028 0.06617  -0.05451 -0.20162 185 ARG A NE  
1401 C CZ  . ARG A 185 ? 0.56198 0.52111 0.47715 0.06281  -0.03263 -0.18071 185 ARG A CZ  
1402 N NH1 . ARG A 185 ? 0.57655 0.52873 0.46531 0.07610  -0.00836 -0.17431 185 ARG A NH1 
1403 N NH2 . ARG A 185 ? 0.53803 0.49664 0.49904 0.04663  -0.03514 -0.16561 185 ARG A NH2 
1404 N N   . HIS A 186 ? 0.43948 0.59982 0.33627 0.03630  -0.08097 -0.09920 186 HIS A N   
1405 C CA  . HIS A 186 ? 0.47001 0.62269 0.34309 0.03633  -0.07085 -0.07318 186 HIS A CA  
1406 C C   . HIS A 186 ? 0.48967 0.64103 0.34854 0.04159  -0.07914 -0.05054 186 HIS A C   
1407 O O   . HIS A 186 ? 0.46947 0.61230 0.30783 0.04127  -0.07138 -0.02745 186 HIS A O   
1408 C CB  . HIS A 186 ? 0.42941 0.55723 0.32265 0.02988  -0.05758 -0.06449 186 HIS A CB  
1409 C CG  . HIS A 186 ? 0.44572 0.57412 0.34863 0.02727  -0.04837 -0.08115 186 HIS A CG  
1410 N ND1 . HIS A 186 ? 0.47325 0.60903 0.36031 0.02612  -0.03632 -0.07799 186 HIS A ND1 
1411 C CD2 . HIS A 186 ? 0.43381 0.55617 0.36263 0.02627  -0.04936 -0.10088 186 HIS A CD2 
1412 C CE1 . HIS A 186 ? 0.50340 0.63928 0.40684 0.02641  -0.03139 -0.09618 186 HIS A CE1 
1413 N NE2 . HIS A 186 ? 0.44023 0.56542 0.36824 0.02672  -0.03930 -0.10932 186 HIS A NE2 
1414 N N   . HIS A 187 ? 0.45832 0.61781 0.33031 0.04646  -0.09457 -0.05694 187 HIS A N   
1415 C CA  . HIS A 187 ? 0.45123 0.61204 0.31300 0.05491  -0.10545 -0.03756 187 HIS A CA  
1416 C C   . HIS A 187 ? 0.46280 0.59411 0.33198 0.05297  -0.09593 -0.01315 187 HIS A C   
1417 O O   . HIS A 187 ? 0.52646 0.64899 0.37241 0.05667  -0.09376 0.01058  187 HIS A O   
1418 C CB  . HIS A 187 ? 0.54437 0.72577 0.36272 0.06280  -0.11161 -0.02816 187 HIS A CB  
1419 C CG  . HIS A 187 ? 0.64902 0.83505 0.45658 0.07481  -0.12697 -0.00998 187 HIS A CG  
1420 N ND1 . HIS A 187 ? 0.65587 0.86250 0.48037 0.08243  -0.14641 -0.02417 187 HIS A ND1 
1421 C CD2 . HIS A 187 ? 0.72736 0.90006 0.51082 0.08122  -0.12621 0.02136  187 HIS A CD2 
1422 C CE1 . HIS A 187 ? 0.63131 0.83486 0.44526 0.09296  -0.15568 -0.00211 187 HIS A CE1 
1423 N NE2 . HIS A 187 ? 0.74002 0.92320 0.52644 0.09401  -0.14525 0.02634  187 HIS A NE2 
1424 N N   . VAL A 188 ? 0.36975 0.48502 0.27159 0.04677  -0.08981 -0.01942 188 VAL A N   
1425 C CA  . VAL A 188 ? 0.43773 0.52712 0.34981 0.04430  -0.08080 -0.00228 188 VAL A CA  
1426 C C   . VAL A 188 ? 0.41853 0.50487 0.36171 0.04726  -0.08754 -0.00627 188 VAL A C   
1427 O O   . VAL A 188 ? 0.32490 0.42643 0.28804 0.04694  -0.09498 -0.02401 188 VAL A O   
1428 C CB  . VAL A 188 ? 0.41118 0.48649 0.33009 0.03421  -0.06480 -0.00485 188 VAL A CB  
1429 C CG1 . VAL A 188 ? 0.42343 0.50374 0.31479 0.03116  -0.05601 0.00075  188 VAL A CG1 
1430 C CG2 . VAL A 188 ? 0.35390 0.43365 0.29669 0.02980  -0.06419 -0.02632 188 VAL A CG2 
1431 N N   . GLN A 189 ? 0.37222 0.43935 0.32152 0.04950  -0.08388 0.00921  189 GLN A N   
1432 C CA  . GLN A 189 ? 0.38866 0.45252 0.36844 0.05202  -0.08632 0.00537  189 GLN A CA  
1433 C C   . GLN A 189 ? 0.38907 0.43472 0.38417 0.04345  -0.07205 0.00423  189 GLN A C   
1434 O O   . GLN A 189 ? 0.32105 0.36426 0.33956 0.04472  -0.07100 0.00108  189 GLN A O   
1435 C CB  . GLN A 189 ? 0.37539 0.43358 0.35362 0.06442  -0.09504 0.02080  189 GLN A CB  
1436 C CG  . GLN A 189 ? 0.39218 0.46894 0.35048 0.07565  -0.11105 0.02612  189 GLN A CG  
1437 C CD  . GLN A 189 ? 0.42100 0.52946 0.39116 0.07589  -0.12254 0.00420  189 GLN A CD  
1438 O OE1 . GLN A 189 ? 0.40168 0.52678 0.35010 0.07544  -0.12770 -0.00196 189 GLN A OE1 
1439 N NE2 . GLN A 189 ? 0.36052 0.47891 0.36661 0.07580  -0.12583 -0.00922 189 GLN A NE2 
1440 N N   . TRP A 190 ? 0.31810 0.35438 0.30061 0.03545  -0.06127 0.00589  190 TRP A N   
1441 C CA  . TRP A 190 ? 0.34901 0.37133 0.34256 0.02836  -0.04949 0.00486  190 TRP A CA  
1442 C C   . TRP A 190 ? 0.31225 0.33870 0.30313 0.02135  -0.04323 -0.00445 190 TRP A C   
1443 O O   . TRP A 190 ? 0.34851 0.38190 0.32213 0.02063  -0.04310 -0.00513 190 TRP A O   
1444 C CB  . TRP A 190 ? 0.34839 0.35196 0.33249 0.02708  -0.04284 0.01872  190 TRP A CB  
1445 C CG  . TRP A 190 ? 0.39438 0.38715 0.38892 0.03426  -0.04661 0.02558  190 TRP A CG  
1446 C CD1 . TRP A 190 ? 0.40952 0.39706 0.39539 0.04311  -0.05446 0.03812  190 TRP A CD1 
1447 C CD2 . TRP A 190 ? 0.37031 0.35670 0.38598 0.03476  -0.04267 0.01996  190 TRP A CD2 
1448 N NE1 . TRP A 190 ? 0.39678 0.37333 0.40039 0.04995  -0.05613 0.03968  190 TRP A NE1 
1449 C CE2 . TRP A 190 ? 0.41035 0.38758 0.43232 0.04455  -0.04835 0.02724  190 TRP A CE2 
1450 C CE3 . TRP A 190 ? 0.35734 0.34562 0.38570 0.02883  -0.03476 0.00996  190 TRP A CE3 
1451 C CZ2 . TRP A 190 ? 0.42182 0.39334 0.46452 0.04843  -0.04561 0.02163  190 TRP A CZ2 
1452 C CZ3 . TRP A 190 ? 0.39251 0.37672 0.43749 0.03176  -0.03164 0.00595  190 TRP A CZ3 
1453 C CH2 . TRP A 190 ? 0.37436 0.35105 0.42747 0.04138  -0.03668 0.01018  190 TRP A CH2 
1454 N N   . LEU A 191 ? 0.30485 0.32750 0.31250 0.01718  -0.03769 -0.01109 191 LEU A N   
1455 C CA  . LEU A 191 ? 0.29655 0.31961 0.30522 0.01269  -0.03236 -0.01858 191 LEU A CA  
1456 C C   . LEU A 191 ? 0.28399 0.29680 0.30020 0.00940  -0.02404 -0.01554 191 LEU A C   
1457 O O   . LEU A 191 ? 0.30797 0.31790 0.33663 0.00932  -0.02266 -0.01475 191 LEU A O   
1458 C CB  . LEU A 191 ? 0.25988 0.29108 0.28233 0.01202  -0.03710 -0.03172 191 LEU A CB  
1459 C CG  . LEU A 191 ? 0.28505 0.30978 0.31830 0.00821  -0.03145 -0.03857 191 LEU A CG  
1460 C CD1 . LEU A 191 ? 0.28679 0.31242 0.30696 0.00932  -0.02856 -0.04173 191 LEU A CD1 
1461 C CD2 . LEU A 191 ? 0.25992 0.28889 0.31265 0.00564  -0.03589 -0.05095 191 LEU A CD2 
1462 N N   . ILE A 192 ? 0.26992 0.28072 0.27844 0.00728  -0.01867 -0.01463 192 ILE A N   
1463 C CA  . ILE A 192 ? 0.23404 0.23929 0.24687 0.00535  -0.01269 -0.01272 192 ILE A CA  
1464 C C   . ILE A 192 ? 0.24369 0.25039 0.25950 0.00610  -0.01111 -0.01785 192 ILE A C   
1465 O O   . ILE A 192 ? 0.24929 0.26216 0.25951 0.00726  -0.01158 -0.02232 192 ILE A O   
1466 C CB  . ILE A 192 ? 0.25154 0.25471 0.25625 0.00285  -0.00900 -0.00750 192 ILE A CB  
1467 C CG1 . ILE A 192 ? 0.22886 0.22523 0.23181 0.00323  -0.01077 -0.00161 192 ILE A CG1 
1468 C CG2 . ILE A 192 ? 0.27787 0.27986 0.28655 0.00166  -0.00501 -0.00814 192 ILE A CG2 
1469 C CD1 . ILE A 192 ? 0.26414 0.25471 0.26142 -0.00124 -0.00665 0.00340  192 ILE A CD1 
1470 N N   . HIS A 193 ? 0.22407 0.22511 0.24841 0.00621  -0.00865 -0.01668 193 HIS A N   
1471 C CA  . HIS A 193 ? 0.23886 0.23667 0.26719 0.00877  -0.00760 -0.01884 193 HIS A CA  
1472 C C   . HIS A 193 ? 0.25951 0.25161 0.28924 0.00942  -0.00380 -0.01130 193 HIS A C   
1473 O O   . HIS A 193 ? 0.26810 0.26089 0.29609 0.00719  -0.00129 -0.00705 193 HIS A O   
1474 C CB  . HIS A 193 ? 0.25403 0.24783 0.29313 0.00870  -0.01030 -0.02668 193 HIS A CB  
1475 C CG  . HIS A 193 ? 0.23678 0.22404 0.28929 0.00463  -0.00892 -0.02484 193 HIS A CG  
1476 N ND1 . HIS A 193 ? 0.27646 0.25253 0.33621 0.00368  -0.00389 -0.01816 193 HIS A ND1 
1477 C CD2 . HIS A 193 ? 0.25247 0.24495 0.31371 0.00114  -0.01146 -0.02840 193 HIS A CD2 
1478 C CE1 . HIS A 193 ? 0.24024 0.21502 0.31329 -0.00207 -0.00150 -0.01778 193 HIS A CE1 
1479 N NE2 . HIS A 193 ? 0.25315 0.23930 0.32920 -0.00338 -0.00660 -0.02527 193 HIS A NE2 
1480 N N   . GLY A 194 ? 0.25719 0.24438 0.28916 0.01378  -0.00352 -0.00978 194 GLY A N   
1481 C CA  . GLY A 194 ? 0.23839 0.21973 0.26843 0.01593  -0.00056 -0.00000 194 GLY A CA  
1482 C C   . GLY A 194 ? 0.29126 0.25660 0.33181 0.01731  0.00091  0.00364  194 GLY A C   
1483 O O   . GLY A 194 ? 0.28892 0.24745 0.34133 0.01173  0.00225  0.00003  194 GLY A O   
1484 N N   . HIS A 195 ? 0.27310 0.23226 0.31116 0.02488  0.00015  0.01075  195 HIS A N   
1485 C CA  . HIS A 195 ? 0.30800 0.24647 0.35657 0.02807  0.00139  0.01648  195 HIS A CA  
1486 C C   . HIS A 195 ? 0.30638 0.23183 0.35714 0.02146  0.00886  0.02970  195 HIS A C   
1487 O O   . HIS A 195 ? 0.31696 0.22782 0.36512 0.02596  0.01134  0.04434  195 HIS A O   
1488 C CB  . HIS A 195 ? 0.28829 0.21935 0.35308 0.02691  -0.00106 0.00176  195 HIS A CB  
1489 C CG  . HIS A 195 ? 0.31011 0.21553 0.39025 0.02905  0.00046  0.00517  195 HIS A CG  
1490 N ND1 . HIS A 195 ? 0.30571 0.19944 0.38715 0.04118  -0.00198 0.01121  195 HIS A ND1 
1491 C CD2 . HIS A 195 ? 0.29591 0.18394 0.39334 0.02047  0.00416  0.00350  195 HIS A CD2 
1492 C CE1 . HIS A 195 ? 0.34620 0.21221 0.44413 0.04040  0.00049  0.01427  195 HIS A CE1 
1493 N NE2 . HIS A 195 ? 0.31391 0.17615 0.42250 0.02659  0.00472  0.00910  195 HIS A NE2 
1494 N N   . THR A 196 ? 0.27741 0.20864 0.33371 0.01128  0.01292  0.02570  196 THR A N   
1495 C CA  . THR A 196 ? 0.32632 0.24848 0.38954 0.00320  0.02207  0.03640  196 THR A CA  
1496 C C   . THR A 196 ? 0.32049 0.25100 0.36459 0.00441  0.02818  0.05080  196 THR A C   
1497 O O   . THR A 196 ? 0.32890 0.25197 0.37465 -0.00122 0.03783  0.06366  196 THR A O   
1498 C CB  . THR A 196 ? 0.36821 0.29871 0.44827 -0.00725 0.02387  0.02510  196 THR A CB  
1499 O OG1 . THR A 196 ? 0.31185 0.26277 0.38212 -0.00631 0.02133  0.01887  196 THR A OG1 
1500 C CG2 . THR A 196 ? 0.34316 0.26774 0.44068 -0.00872 0.01723  0.00939  196 THR A CG2 
1501 N N   . HIS A 197 ? 0.31908 0.26600 0.34560 0.01068  0.02350  0.04805  197 HIS A N   
1502 C CA  . HIS A 197 ? 0.30593 0.26441 0.31216 0.01299  0.02759  0.05759  197 HIS A CA  
1503 C C   . HIS A 197 ? 0.33095 0.29854 0.33996 0.00413  0.03759  0.05728  197 HIS A C   
1504 O O   . HIS A 197 ? 0.32703 0.30027 0.32210 0.00372  0.04560  0.06825  197 HIS A O   
1505 C CB  . HIS A 197 ? 0.34272 0.28966 0.33643 0.01987  0.02918  0.07676  197 HIS A CB  
1506 C CG  . HIS A 197 ? 0.35571 0.29763 0.34798 0.03165  0.01865  0.07664  197 HIS A CG  
1507 N ND1 . HIS A 197 ? 0.39354 0.32718 0.37368 0.04221  0.01631  0.09363  197 HIS A ND1 
1508 C CD2 . HIS A 197 ? 0.31936 0.26566 0.32127 0.03540  0.01020  0.06179  197 HIS A CD2 
1509 C CE1 . HIS A 197 ? 0.37741 0.31140 0.36306 0.05280  0.00612  0.08753  197 HIS A CE1 
1510 N NE2 . HIS A 197 ? 0.36743 0.30999 0.36625 0.04806  0.00329  0.06777  197 HIS A NE2 
1511 N N   . ARG A 198 ? 0.26944 0.24115 0.29614 -0.00201 0.03715  0.04450  198 ARG A N   
1512 C CA  . ARG A 198 ? 0.30800 0.29146 0.34370 -0.00902 0.04567  0.04130  198 ARG A CA  
1513 C C   . ARG A 198 ? 0.29490 0.29141 0.33253 -0.00690 0.03968  0.02641  198 ARG A C   
1514 O O   . ARG A 198 ? 0.28512 0.28282 0.33980 -0.00938 0.03553  0.01724  198 ARG A O   
1515 C CB  . ARG A 198 ? 0.31706 0.29323 0.37859 -0.01837 0.05058  0.04096  198 ARG A CB  
1516 C CG  . ARG A 198 ? 0.37997 0.34058 0.44363 -0.02356 0.06049  0.05782  198 ARG A CG  
1517 C CD  . ARG A 198 ? 0.48250 0.43087 0.57632 -0.03296 0.06103  0.05258  198 ARG A CD  
1518 N NE  . ARG A 198 ? 0.55512 0.48397 0.65598 -0.04030 0.07198  0.06927  198 ARG A NE  
1519 C CZ  . ARG A 198 ? 0.64762 0.54959 0.75541 -0.03929 0.06880  0.07425  198 ARG A CZ  
1520 N NH1 . ARG A 198 ? 0.63211 0.52719 0.73990 -0.03075 0.05546  0.06237  198 ARG A NH1 
1521 N NH2 . ARG A 198 ? 0.72361 0.60458 0.83927 -0.04698 0.08023  0.09168  198 ARG A NH2 
1522 N N   . PRO A 199 ? 0.31865 0.32462 0.33941 -0.00210 0.03853  0.02365  199 PRO A N   
1523 C CA  . PRO A 199 ? 0.27504 0.28760 0.29884 -0.00019 0.03305  0.01085  199 PRO A CA  
1524 C C   . PRO A 199 ? 0.28013 0.30078 0.32147 -0.00281 0.03745  0.00429  199 PRO A C   
1525 O O   . PRO A 199 ? 0.30018 0.33091 0.34349 -0.00485 0.04748  0.00565  199 PRO A O   
1526 C CB  . PRO A 199 ? 0.31527 0.33633 0.32020 0.00371  0.03319  0.00832  199 PRO A CB  
1527 C CG  . PRO A 199 ? 0.33946 0.36471 0.33052 0.00410  0.04080  0.01965  199 PRO A CG  
1528 C CD  . PRO A 199 ? 0.31516 0.32610 0.31344 0.00195  0.04151  0.03173  199 PRO A CD  
1529 N N   . ALA A 200 ? 0.22379 0.24245 0.27766 -0.00193 0.02991  -0.00267 200 ALA A N   
1530 C CA  . ALA A 200 ? 0.27255 0.30061 0.34688 -0.00237 0.03102  -0.00905 200 ALA A CA  
1531 C C   . ALA A 200 ? 0.27913 0.30359 0.35844 0.00176  0.01960  -0.01431 200 ALA A C   
1532 O O   . ALA A 200 ? 0.22418 0.23929 0.29191 0.00274  0.01296  -0.01243 200 ALA A O   
1533 C CB  . ALA A 200 ? 0.24341 0.27545 0.33577 -0.00936 0.03636  -0.00622 200 ALA A CB  
1534 N N   . VAL A 201 ? 0.25592 0.28986 0.35261 0.00485  0.01774  -0.02028 201 VAL A N   
1535 C CA  . VAL A 201 ? 0.28998 0.32266 0.39197 0.01015  0.00621  -0.02286 201 VAL A CA  
1536 C C   . VAL A 201 ? 0.27303 0.32106 0.39929 0.00899  0.00344  -0.02789 201 VAL A C   
1537 O O   . VAL A 201 ? 0.27956 0.34207 0.42470 0.01063  0.00815  -0.03294 201 VAL A O   
1538 C CB  . VAL A 201 ? 0.28957 0.31821 0.39054 0.01818  0.00376  -0.02529 201 VAL A CB  
1539 C CG1 . VAL A 201 ? 0.29638 0.32279 0.40097 0.02487  -0.00848 -0.02383 201 VAL A CG1 
1540 C CG2 . VAL A 201 ? 0.30798 0.32316 0.38896 0.01699  0.00635  -0.02310 201 VAL A CG2 
1541 N N   . HIS A 202 ? 0.28470 0.33247 0.41249 0.00610  -0.00406 -0.02881 202 HIS A N   
1542 C CA  . HIS A 202 ? 0.28903 0.35332 0.44169 0.00332  -0.00843 -0.03650 202 HIS A CA  
1543 C C   . HIS A 202 ? 0.28116 0.35371 0.43554 0.01247  -0.02354 -0.04012 202 HIS A C   
1544 O O   . HIS A 202 ? 0.31351 0.37634 0.44706 0.01585  -0.03120 -0.03643 202 HIS A O   
1545 C CB  . HIS A 202 ? 0.25184 0.31088 0.40728 -0.00615 -0.00746 -0.03823 202 HIS A CB  
1546 C CG  . HIS A 202 ? 0.26660 0.31393 0.41733 -0.01359 0.00610  -0.03075 202 HIS A CG  
1547 N ND1 . HIS A 202 ? 0.24054 0.29488 0.41131 -0.02236 0.01726  -0.03018 202 HIS A ND1 
1548 C CD2 . HIS A 202 ? 0.27685 0.30737 0.40492 -0.01309 0.01003  -0.02237 202 HIS A CD2 
1549 C CE1 . HIS A 202 ? 0.28431 0.32422 0.44145 -0.02625 0.02741  -0.01957 202 HIS A CE1 
1550 N NE2 . HIS A 202 ? 0.28779 0.31409 0.41962 -0.01987 0.02213  -0.01546 202 HIS A NE2 
1551 N N   . GLU A 203 ? 0.25026 0.34287 0.42920 0.01704  -0.02765 -0.04673 203 GLU A N   
1552 C CA  . GLU A 203 ? 0.20737 0.31184 0.38979 0.02718  -0.04413 -0.04966 203 GLU A CA  
1553 C C   . GLU A 203 ? 0.28164 0.40455 0.48059 0.02107  -0.05232 -0.06094 203 GLU A C   
1554 O O   . GLU A 203 ? 0.28103 0.41620 0.50627 0.01088  -0.04519 -0.06909 203 GLU A O   
1555 C CB  . GLU A 203 ? 0.27441 0.39292 0.47706 0.03861  -0.04690 -0.05198 203 GLU A CB  
1556 C CG  . GLU A 203 ? 0.29398 0.42474 0.49897 0.05224  -0.06591 -0.05223 203 GLU A CG  
1557 C CD  . GLU A 203 ? 0.46863 0.60818 0.69266 0.06712  -0.06940 -0.05272 203 GLU A CD  
1558 O OE1 . GLU A 203 ? 0.48441 0.62677 0.72498 0.06551  -0.05622 -0.05722 203 GLU A OE1 
1559 O OE2 . GLU A 203 ? 0.47465 0.61911 0.69671 0.08155  -0.08545 -0.04869 203 GLU A OE2 
1560 N N   . LEU A 204 ? 0.27144 0.39670 0.45471 0.02648  -0.06666 -0.06187 204 LEU A N   
1561 C CA  . LEU A 204 ? 0.32309 0.46807 0.51990 0.02203  -0.07727 -0.07614 204 LEU A CA  
1562 C C   . LEU A 204 ? 0.29758 0.45682 0.48094 0.03584  -0.09653 -0.07579 204 LEU A C   
1563 O O   . LEU A 204 ? 0.29095 0.44327 0.45998 0.04841  -0.10038 -0.06298 204 LEU A O   
1564 C CB  . LEU A 204 ? 0.29318 0.42274 0.47795 0.01078  -0.07170 -0.07987 204 LEU A CB  
1565 C CG  . LEU A 204 ? 0.30381 0.41472 0.44996 0.01533  -0.07291 -0.07074 204 LEU A CG  
1566 C CD1 . LEU A 204 ? 0.29382 0.40888 0.43341 0.01107  -0.07934 -0.08369 204 LEU A CD1 
1567 C CD2 . LEU A 204 ? 0.27352 0.35911 0.40639 0.01141  -0.05754 -0.05871 204 LEU A CD2 
1568 N N   . GLN A 205 ? 0.30605 0.48469 0.49353 0.03378  -0.10894 -0.08988 205 GLN A N   
1569 C CA  . GLN A 205 ? 0.34905 0.54377 0.51708 0.04685  -0.12813 -0.08947 205 GLN A CA  
1570 C C   . GLN A 205 ? 0.33311 0.52345 0.47357 0.04229  -0.13088 -0.09538 205 GLN A C   
1571 O O   . GLN A 205 ? 0.35981 0.55308 0.51507 0.03008  -0.12769 -0.11229 205 GLN A O   
1572 C CB  . GLN A 205 ? 0.33133 0.56464 0.53094 0.05202  -0.14469 -0.10494 205 GLN A CB  
1573 C CG  . GLN A 205 ? 0.46148 0.71121 0.64008 0.07128  -0.16539 -0.09756 205 GLN A CG  
1574 C CD  . GLN A 205 ? 0.53097 0.81183 0.73395 0.07516  -0.17676 -0.10935 205 GLN A CD  
1575 O OE1 . GLN A 205 ? 0.63652 0.92621 0.86592 0.08112  -0.17587 -0.10715 205 GLN A OE1 
1576 N NE2 . GLN A 205 ? 0.51212 0.80896 0.70529 0.07180  -0.18604 -0.12244 205 GLN A NE2 
1577 N N   . ALA A 206 ? 0.32169 0.50432 0.42330 0.05196  -0.13566 -0.08154 206 ALA A N   
1578 C CA  . ALA A 206 ? 0.37777 0.56112 0.44983 0.04985  -0.13790 -0.08708 206 ALA A CA  
1579 C C   . ALA A 206 ? 0.40744 0.60212 0.44493 0.06446  -0.15162 -0.07468 206 ALA A C   
1580 O O   . ALA A 206 ? 0.41650 0.59841 0.44262 0.07385  -0.15127 -0.05303 206 ALA A O   
1581 C CB  . ALA A 206 ? 0.32905 0.48263 0.38461 0.04168  -0.11979 -0.07889 206 ALA A CB  
1582 N N   . ASN A 207 ? 0.40399 0.62201 0.42454 0.06652  -0.16354 -0.08858 207 ASN A N   
1583 C CA  . ASN A 207 ? 0.43319 0.66668 0.41672 0.08069  -0.17752 -0.07683 207 ASN A CA  
1584 C C   . ASN A 207 ? 0.44834 0.69095 0.44527 0.09282  -0.18923 -0.06577 207 ASN A C   
1585 O O   . ASN A 207 ? 0.46085 0.69639 0.43139 0.10513  -0.19390 -0.04195 207 ASN A O   
1586 C CB  . ASN A 207 ? 0.47580 0.68429 0.41884 0.08235  -0.16532 -0.05188 207 ASN A CB  
1587 C CG  . ASN A 207 ? 0.42422 0.61634 0.36290 0.06872  -0.14734 -0.05988 207 ASN A CG  
1588 O OD1 . ASN A 207 ? 0.42039 0.62806 0.35364 0.06434  -0.14915 -0.08078 207 ASN A OD1 
1589 N ND2 . ASN A 207 ? 0.38913 0.55099 0.33182 0.06293  -0.13074 -0.04503 207 ASN A ND2 
1590 N N   . GLY A 208 ? 0.40366 0.66087 0.44352 0.08878  -0.19267 -0.08257 208 GLY A N   
1591 C CA  . GLY A 208 ? 0.42238 0.69274 0.48069 0.10008  -0.20323 -0.07628 208 GLY A CA  
1592 C C   . GLY A 208 ? 0.45444 0.70467 0.51770 0.11069  -0.20003 -0.05401 208 GLY A C   
1593 O O   . GLY A 208 ? 0.45551 0.71198 0.52479 0.12388  -0.20924 -0.04343 208 GLY A O   
1594 N N   . GLN A 209 ? 0.40340 0.62760 0.46549 0.10521  -0.18626 -0.04717 209 GLN A N   
1595 C CA  . GLN A 209 ? 0.44383 0.63888 0.50762 0.11160  -0.17701 -0.02618 209 GLN A CA  
1596 C C   . GLN A 209 ? 0.43068 0.60636 0.51825 0.09631  -0.15609 -0.03273 209 GLN A C   
1597 O O   . GLN A 209 ? 0.40003 0.57518 0.49033 0.08117  -0.14690 -0.04582 209 GLN A O   
1598 C CB  . GLN A 209 ? 0.48964 0.65692 0.50833 0.11666  -0.17303 -0.00017 209 GLN A CB  
1599 C CG  . GLN A 209 ? 0.52556 0.70669 0.51610 0.13482  -0.19266 0.01459  209 GLN A CG  
1600 C CD  . GLN A 209 ? 0.60821 0.79323 0.62330 0.14870  -0.20189 0.02166  209 GLN A CD  
1601 O OE1 . GLN A 209 ? 0.70272 0.91567 0.72748 0.15323  -0.21457 0.01340  209 GLN A OE1 
1602 N NE2 . GLN A 209 ? 0.66739 0.82423 0.69373 0.15583  -0.19538 0.03560  209 GLN A NE2 
1603 N N   . PRO A 210 ? 0.40107 0.56093 0.50573 0.10093  -0.14861 -0.02428 210 PRO A N   
1604 C CA  . PRO A 210 ? 0.36629 0.50846 0.48671 0.08742  -0.12847 -0.02865 210 PRO A CA  
1605 C C   . PRO A 210 ? 0.35082 0.46610 0.44088 0.07643  -0.11527 -0.02060 210 PRO A C   
1606 O O   . PRO A 210 ? 0.33973 0.43981 0.39850 0.08094  -0.11688 -0.00523 210 PRO A O   
1607 C CB  . PRO A 210 ? 0.42526 0.55516 0.56086 0.09832  -0.12532 -0.01991 210 PRO A CB  
1608 C CG  . PRO A 210 ? 0.39284 0.54473 0.53850 0.11701  -0.14542 -0.01821 210 PRO A CG  
1609 C CD  . PRO A 210 ? 0.41137 0.57111 0.52397 0.12005  -0.15902 -0.01239 210 PRO A CD  
1610 N N   . ALA A 211 ? 0.30398 0.41476 0.40465 0.06202  -0.10190 -0.03042 211 ALA A N   
1611 C CA  . ALA A 211 ? 0.32441 0.41394 0.40242 0.05224  -0.08973 -0.02548 211 ALA A CA  
1612 C C   . ALA A 211 ? 0.32436 0.40220 0.41844 0.04295  -0.07406 -0.02834 211 ALA A C   
1613 O O   . ALA A 211 ? 0.26657 0.35591 0.38866 0.04110  -0.07143 -0.03653 211 ALA A O   
1614 C CB  . ALA A 211 ? 0.25978 0.35972 0.32655 0.04577  -0.09320 -0.03607 211 ALA A CB  
1615 N N   . TRP A 212 ? 0.27345 0.33121 0.34932 0.03713  -0.06346 -0.02147 212 TRP A N   
1616 C CA  . TRP A 212 ? 0.28124 0.32831 0.36587 0.03026  -0.04981 -0.02199 212 TRP A CA  
1617 C C   . TRP A 212 ? 0.30786 0.34561 0.37931 0.02161  -0.04231 -0.02252 212 TRP A C   
1618 O O   . TRP A 212 ? 0.30419 0.33627 0.35470 0.02179  -0.04368 -0.01820 212 TRP A O   
1619 C CB  . TRP A 212 ? 0.31174 0.34372 0.39200 0.03507  -0.04510 -0.01333 212 TRP A CB  
1620 C CG  . TRP A 212 ? 0.35077 0.39013 0.44845 0.04563  -0.05146 -0.01385 212 TRP A CG  
1621 C CD1 . TRP A 212 ? 0.34673 0.39624 0.46945 0.04720  -0.04667 -0.02144 212 TRP A CD1 
1622 C CD2 . TRP A 212 ? 0.33895 0.37782 0.43094 0.05753  -0.06382 -0.00611 212 TRP A CD2 
1623 N NE1 . TRP A 212 ? 0.37432 0.43062 0.51060 0.06022  -0.05578 -0.02093 212 TRP A NE1 
1624 C CE2 . TRP A 212 ? 0.35786 0.40622 0.47500 0.06737  -0.06726 -0.01040 212 TRP A CE2 
1625 C CE3 . TRP A 212 ? 0.39377 0.42605 0.46087 0.06145  -0.07180 0.00511  212 TRP A CE3 
1626 C CZ2 . TRP A 212 ? 0.44593 0.49530 0.56530 0.08263  -0.08024 -0.00331 212 TRP A CZ2 
1627 C CZ3 . TRP A 212 ? 0.43397 0.46644 0.49952 0.07542  -0.08388 0.01430  212 TRP A CZ3 
1628 C CH2 . TRP A 212 ? 0.43784 0.47780 0.52999 0.08667  -0.08892 0.01031  212 TRP A CH2 
1629 N N   . ARG A 213 ? 0.25823 0.29531 0.34268 0.01464  -0.03385 -0.02700 213 ARG A N   
1630 C CA  . ARG A 213 ? 0.27425 0.30136 0.34987 0.00861  -0.02689 -0.02650 213 ARG A CA  
1631 C C   . ARG A 213 ? 0.25879 0.27698 0.33167 0.00697  -0.01669 -0.02046 213 ARG A C   
1632 O O   . ARG A 213 ? 0.25164 0.27373 0.33830 0.00472  -0.01056 -0.02130 213 ARG A O   
1633 C CB  . ARG A 213 ? 0.25452 0.28559 0.34628 0.00246  -0.02635 -0.03512 213 ARG A CB  
1634 C CG  . ARG A 213 ? 0.25603 0.27402 0.34126 -0.00135 -0.01988 -0.03357 213 ARG A CG  
1635 C CD  . ARG A 213 ? 0.21154 0.22857 0.31388 -0.00696 -0.02065 -0.04303 213 ARG A CD  
1636 N NE  . ARG A 213 ? 0.26439 0.28561 0.39101 -0.01360 -0.01574 -0.04414 213 ARG A NE  
1637 C CZ  . ARG A 213 ? 0.30118 0.31221 0.43403 -0.01888 -0.00461 -0.03617 213 ARG A CZ  
1638 N NH1 . ARG A 213 ? 0.25367 0.25003 0.37001 -0.01661 0.00072  -0.02663 213 ARG A NH1 
1639 N NH2 . ARG A 213 ? 0.29335 0.31130 0.44959 -0.02647 0.00140  -0.03727 213 ARG A NH2 
1640 N N   . VAL A 214 ? 0.25053 0.25986 0.30593 0.00763  -0.01460 -0.01544 214 VAL A N   
1641 C CA  . VAL A 214 ? 0.25870 0.26257 0.30918 0.00656  -0.00710 -0.01214 214 VAL A CA  
1642 C C   . VAL A 214 ? 0.27180 0.27250 0.31632 0.00368  -0.00309 -0.01068 214 VAL A C   
1643 O O   . VAL A 214 ? 0.28591 0.28510 0.32329 0.00387  -0.00589 -0.01137 214 VAL A O   
1644 C CB  . VAL A 214 ? 0.30982 0.30715 0.34935 0.00841  -0.00810 -0.00915 214 VAL A CB  
1645 C CG1 . VAL A 214 ? 0.24491 0.23981 0.28168 0.00703  -0.00165 -0.01014 214 VAL A CG1 
1646 C CG2 . VAL A 214 ? 0.28583 0.28220 0.33097 0.01362  -0.01355 -0.00800 214 VAL A CG2 
1647 N N   . VAL A 215 ? 0.24651 0.24729 0.29341 0.00213  0.00362  -0.00826 215 VAL A N   
1648 C CA  . VAL A 215 ? 0.26123 0.25754 0.30314 0.00140  0.00674  -0.00395 215 VAL A CA  
1649 C C   . VAL A 215 ? 0.29320 0.29171 0.32175 0.00324  0.00970  -0.00096 215 VAL A C   
1650 O O   . VAL A 215 ? 0.23569 0.23912 0.26289 0.00310  0.01380  -0.00199 215 VAL A O   
1651 C CB  . VAL A 215 ? 0.28245 0.27653 0.33662 -0.00239 0.01230  -0.00074 215 VAL A CB  
1652 C CG1 . VAL A 215 ? 0.25858 0.24248 0.30800 -0.00149 0.01415  0.00607  215 VAL A CG1 
1653 C CG2 . VAL A 215 ? 0.24884 0.24550 0.32077 -0.00545 0.00836  -0.00776 215 VAL A CG2 
1654 N N   . LEU A 216 ? 0.25983 0.25749 0.27993 0.00561  0.00713  0.00056  216 LEU A N   
1655 C CA  . LEU A 216 ? 0.25804 0.26199 0.26659 0.00779  0.00765  0.00166  216 LEU A CA  
1656 C C   . LEU A 216 ? 0.29381 0.29747 0.29611 0.01013  0.01179  0.01040  216 LEU A C   
1657 O O   . LEU A 216 ? 0.25713 0.25177 0.26555 0.00961  0.01443  0.01700  216 LEU A O   
1658 C CB  . LEU A 216 ? 0.24488 0.25291 0.25027 0.00996  0.00266  -0.00097 216 LEU A CB  
1659 C CG  . LEU A 216 ? 0.26997 0.28056 0.27695 0.00629  0.00075  -0.00716 216 LEU A CG  
1660 C CD1 . LEU A 216 ? 0.24253 0.25776 0.25082 0.00755  -0.00178 -0.00922 216 LEU A CD1 
1661 C CD2 . LEU A 216 ? 0.27184 0.28870 0.27506 0.00382  0.00126  -0.01177 216 LEU A CD2 
1662 N N   . GLY A 217 ? 0.30191 0.31542 0.29146 0.01236  0.01241  0.01050  217 GLY A N   
1663 C CA  . GLY A 217 ? 0.27776 0.29365 0.25493 0.01597  0.01580  0.02106  217 GLY A CA  
1664 C C   . GLY A 217 ? 0.32907 0.34875 0.29768 0.02348  0.00866  0.02542  217 GLY A C   
1665 O O   . GLY A 217 ? 0.27731 0.30499 0.24861 0.02474  0.00208  0.01663  217 GLY A O   
1666 N N   . ALA A 218 ? 0.30085 0.31506 0.26067 0.02866  0.01034  0.03998  218 ALA A N   
1667 C CA  . ALA A 218 ? 0.32719 0.34690 0.27795 0.03896  0.00235  0.04595  218 ALA A CA  
1668 C C   . ALA A 218 ? 0.35758 0.39998 0.28897 0.04249  -0.00101 0.04279  218 ALA A C   
1669 O O   . ALA A 218 ? 0.36631 0.41581 0.28702 0.03823  0.00551  0.04113  218 ALA A O   
1670 C CB  . ALA A 218 ? 0.31279 0.31427 0.26095 0.04471  0.00472  0.06527  218 ALA A CB  
1671 N N   . TRP A 219 ? 0.26902 0.32589 0.19744 0.05071  -0.01156 0.03963  219 TRP A N   
1672 C CA  . TRP A 219 ? 0.34023 0.42303 0.25170 0.05458  -0.01759 0.03336  219 TRP A CA  
1673 C C   . TRP A 219 ? 0.40961 0.49455 0.29728 0.06547  -0.01887 0.05314  219 TRP A C   
1674 O O   . TRP A 219 ? 0.40428 0.49833 0.28633 0.07782  -0.02939 0.05996  219 TRP A O   
1675 C CB  . TRP A 219 ? 0.29415 0.39630 0.21715 0.05716  -0.02875 0.01895  219 TRP A CB  
1676 C CG  . TRP A 219 ? 0.24309 0.34442 0.18541 0.04519  -0.02612 0.00159  219 TRP A CG  
1677 C CD1 . TRP A 219 ? 0.26905 0.34995 0.22424 0.03749  -0.01868 0.00153  219 TRP A CD1 
1678 C CD2 . TRP A 219 ? 0.23516 0.35669 0.18576 0.03939  -0.03103 -0.01700 219 TRP A CD2 
1679 N NE1 . TRP A 219 ? 0.26544 0.35089 0.23326 0.02843  -0.01841 -0.01294 219 TRP A NE1 
1680 C CE2 . TRP A 219 ? 0.26105 0.36958 0.22797 0.02830  -0.02498 -0.02446 219 TRP A CE2 
1681 C CE3 . TRP A 219 ? 0.25352 0.40360 0.20018 0.04206  -0.04032 -0.02839 219 TRP A CE3 
1682 C CZ2 . TRP A 219 ? 0.22204 0.34086 0.20181 0.01882  -0.02610 -0.04043 219 TRP A CZ2 
1683 C CZ3 . TRP A 219 ? 0.28639 0.44908 0.24919 0.03155  -0.04196 -0.04783 219 TRP A CZ3 
1684 C CH2 . TRP A 219 ? 0.21805 0.36301 0.19741 0.01956  -0.03398 -0.05251 219 TRP A CH2 
1685 N N   . HIS A 220 ? 0.44310 0.52053 0.31676 0.06128  -0.00753 0.06354  220 HIS A N   
1686 C CA  . HIS A 220 ? 0.50214 0.57914 0.34958 0.06984  -0.00536 0.08655  220 HIS A CA  
1687 C C   . HIS A 220 ? 0.55609 0.66485 0.37532 0.07379  -0.00897 0.07983  220 HIS A C   
1688 O O   . HIS A 220 ? 0.59060 0.71699 0.39288 0.08631  -0.02116 0.08487  220 HIS A O   
1689 C CB  . HIS A 220 ? 0.47489 0.52890 0.32355 0.06165  0.01094  0.10239  220 HIS A CB  
1690 C CG  . HIS A 220 ? 0.64883 0.69761 0.47119 0.06834  0.01617  0.13024  220 HIS A CG  
1691 N ND1 . HIS A 220 ? 0.62772 0.68460 0.42974 0.06259  0.03026  0.13868  220 HIS A ND1 
1692 C CD2 . HIS A 220 ? 0.63330 0.66915 0.44596 0.08088  0.00987  0.15299  220 HIS A CD2 
1693 C CE1 . HIS A 220 ? 0.68712 0.73602 0.46555 0.07002  0.03326  0.16732  220 HIS A CE1 
1694 N NE2 . HIS A 220 ? 0.68620 0.72035 0.47078 0.08181  0.02028  0.17719  220 HIS A NE2 
1695 N N   A SER A 221 ? 0.52772 0.64588 0.34236 0.06432  0.00083  0.06694  221 SER A N   
1696 N N   B SER A 221 ? 0.52717 0.64539 0.34203 0.06430  0.00072  0.06671  221 SER A N   
1697 C CA  A SER A 221 ? 0.51866 0.66834 0.30876 0.06679  -0.00179 0.05391  221 SER A CA  
1698 C CA  B SER A 221 ? 0.51859 0.66823 0.30868 0.06679  -0.00177 0.05396  221 SER A CA  
1699 C C   A SER A 221 ? 0.48228 0.64587 0.28946 0.05985  -0.00712 0.02186  221 SER A C   
1700 C C   B SER A 221 ? 0.48283 0.64651 0.28965 0.05973  -0.00679 0.02182  221 SER A C   
1701 O O   A SER A 221 ? 0.50758 0.69890 0.30206 0.06366  -0.01672 0.00621  221 SER A O   
1702 O O   B SER A 221 ? 0.50667 0.69821 0.30016 0.06340  -0.01592 0.00606  221 SER A O   
1703 C CB  A SER A 221 ? 0.53330 0.68662 0.30291 0.06258  0.01495  0.06181  221 SER A CB  
1704 C CB  B SER A 221 ? 0.53351 0.68635 0.30272 0.06282  0.01496  0.06282  221 SER A CB  
1705 O OG  A SER A 221 ? 0.49951 0.62987 0.26525 0.06266  0.02518  0.09142  221 SER A OG  
1706 O OG  B SER A 221 ? 0.50467 0.64227 0.29822 0.05080  0.02776  0.05443  221 SER A OG  
1707 N N   . GLU A 222 ? 0.47453 0.61928 0.31033 0.04976  -0.00156 0.01200  222 GLU A N   
1708 C CA  . GLU A 222 ? 0.44395 0.59427 0.29865 0.04238  -0.00533 -0.01460 222 GLU A CA  
1709 C C   . GLU A 222 ? 0.39489 0.52558 0.27819 0.03779  -0.00843 -0.01462 222 GLU A C   
1710 O O   . GLU A 222 ? 0.42347 0.53633 0.31292 0.03988  -0.00653 0.00249  222 GLU A O   
1711 C CB  . GLU A 222 ? 0.44729 0.59575 0.30521 0.03534  0.00643  -0.02790 222 GLU A CB  
1712 C CG  . GLU A 222 ? 0.50243 0.67752 0.33535 0.03851  0.00836  -0.04024 222 GLU A CG  
1713 C CD  . GLU A 222 ? 0.58068 0.75582 0.42638 0.03221  0.01567  -0.06424 222 GLU A CD  
1714 O OE1 . GLU A 222 ? 0.50558 0.65840 0.37674 0.02650  0.02088  -0.06516 222 GLU A OE1 
1715 O OE2 . GLU A 222 ? 0.60700 0.80497 0.43731 0.03412  0.01556  -0.08288 222 GLU A OE2 
1716 N N   . GLY A 223 ? 0.28768 0.42166 0.18839 0.03099  -0.01255 -0.03456 223 GLY A N   
1717 C CA  . GLY A 223 ? 0.25154 0.36959 0.17639 0.02556  -0.01365 -0.03505 223 GLY A CA  
1718 C C   . GLY A 223 ? 0.31396 0.40917 0.25162 0.01889  -0.00407 -0.03396 223 GLY A C   
1719 O O   . GLY A 223 ? 0.29568 0.38923 0.22933 0.01731  0.00310  -0.03828 223 GLY A O   
1720 N N   . SER A 224 ? 0.24206 0.32253 0.19549 0.01601  -0.00443 -0.02906 224 SER A N   
1721 C CA  . SER A 224 ? 0.30833 0.36966 0.27392 0.01114  0.00189  -0.02742 224 SER A CA  
1722 C C   . SER A 224 ? 0.27537 0.32933 0.25578 0.00611  -0.00101 -0.03057 224 SER A C   
1723 O O   . SER A 224 ? 0.27767 0.33768 0.26046 0.00781  -0.00551 -0.02801 224 SER A O   
1724 C CB  . SER A 224 ? 0.29563 0.34598 0.25973 0.01407  0.00676  -0.01221 224 SER A CB  
1725 O OG  . SER A 224 ? 0.41623 0.45270 0.39401 0.01001  0.01040  -0.01235 224 SER A OG  
1726 N N   . MET A 225 ? 0.26288 0.30472 0.25303 0.00077  0.00200  -0.03553 225 MET A N   
1727 C CA  . MET A 225 ? 0.20456 0.23762 0.20513 -0.00426 0.00111  -0.03460 225 MET A CA  
1728 C C   . MET A 225 ? 0.26774 0.28379 0.27447 -0.00528 0.00425  -0.03171 225 MET A C   
1729 O O   . MET A 225 ? 0.27416 0.28678 0.28183 -0.00313 0.00702  -0.03496 225 MET A O   
1730 C CB  . MET A 225 ? 0.22239 0.26158 0.23000 -0.01148 -0.00069 -0.04527 225 MET A CB  
1731 C CG  . MET A 225 ? 0.24251 0.27372 0.25535 -0.01569 0.00138  -0.05650 225 MET A CG  
1732 S SD  . MET A 225 ? 0.31050 0.34583 0.33706 -0.02742 0.00006  -0.07035 225 MET A SD  
1733 C CE  . MET A 225 ? 0.43144 0.48149 0.45392 -0.02598 -0.00275 -0.09019 225 MET A CE  
1734 N N   . VAL A 226 ? 0.24953 0.25771 0.26026 -0.00758 0.00358  -0.02601 226 VAL A N   
1735 C CA  . VAL A 226 ? 0.25553 0.24886 0.27121 -0.00787 0.00423  -0.02242 226 VAL A CA  
1736 C C   . VAL A 226 ? 0.25503 0.24020 0.27466 -0.01488 0.00507  -0.02312 226 VAL A C   
1737 O O   . VAL A 226 ? 0.26231 0.25445 0.28086 -0.01977 0.00560  -0.02160 226 VAL A O   
1738 C CB  . VAL A 226 ? 0.28286 0.27455 0.29706 -0.00458 0.00241  -0.01426 226 VAL A CB  
1739 C CG1 . VAL A 226 ? 0.25470 0.23439 0.27126 -0.00404 0.00081  -0.00928 226 VAL A CG1 
1740 C CG2 . VAL A 226 ? 0.22020 0.21584 0.23592 0.00001  0.00307  -0.01365 226 VAL A CG2 
1741 N N   . LYS A 227 ? 0.25792 0.22824 0.28412 -0.01550 0.00608  -0.02559 227 LYS A N   
1742 C CA  . LYS A 227 ? 0.23944 0.19538 0.27152 -0.02308 0.00805  -0.02414 227 LYS A CA  
1743 C C   . LYS A 227 ? 0.32588 0.26331 0.35747 -0.01879 0.00689  -0.01186 227 LYS A C   
1744 O O   . LYS A 227 ? 0.34110 0.27119 0.37740 -0.01058 0.00474  -0.01294 227 LYS A O   
1745 C CB  . LYS A 227 ? 0.23379 0.18391 0.27607 -0.02706 0.00950  -0.03835 227 LYS A CB  
1746 C CG  . LYS A 227 ? 0.29114 0.22025 0.34389 -0.03627 0.01249  -0.03689 227 LYS A CG  
1747 C CD  . LYS A 227 ? 0.44000 0.37258 0.50451 -0.04501 0.01364  -0.05543 227 LYS A CD  
1748 C CE  . LYS A 227 ? 0.51408 0.42018 0.59235 -0.04483 0.01496  -0.06354 227 LYS A CE  
1749 N NZ  . LYS A 227 ? 0.47365 0.37998 0.56680 -0.05662 0.01626  -0.08299 227 LYS A NZ  
1750 N N   . VAL A 228 ? 0.34570 0.27858 0.37124 -0.02347 0.00826  -0.00014 228 VAL A N   
1751 C CA  . VAL A 228 ? 0.32447 0.24166 0.34479 -0.01870 0.00605  0.01437  228 VAL A CA  
1752 C C   . VAL A 228 ? 0.34085 0.23435 0.36641 -0.02643 0.01051  0.02139  228 VAL A C   
1753 O O   . VAL A 228 ? 0.29371 0.18993 0.32012 -0.03870 0.01672  0.02199  228 VAL A O   
1754 C CB  . VAL A 228 ? 0.32968 0.26022 0.33486 -0.01737 0.00465  0.02385  228 VAL A CB  
1755 C CG1 . VAL A 228 ? 0.31853 0.23584 0.31457 -0.01132 0.00082  0.03949  228 VAL A CG1 
1756 C CG2 . VAL A 228 ? 0.22881 0.17824 0.23287 -0.01099 0.00064  0.01592  228 VAL A CG2 
1757 N N   . THR A 229 ? 0.27336 0.19229 0.40333 -0.01192 -0.00489 0.02085  229 THR A N   
1758 C CA  . THR A 229 ? 0.29019 0.16966 0.39751 -0.01025 -0.00342 0.02004  229 THR A CA  
1759 C C   . THR A 229 ? 0.33186 0.20131 0.42374 -0.00041 -0.00248 0.02732  229 THR A C   
1760 O O   . THR A 229 ? 0.30281 0.20225 0.40535 0.00600  -0.00394 0.03063  229 THR A O   
1761 C CB  . THR A 229 ? 0.37104 0.23516 0.46389 0.00226  -0.00630 0.01452  229 THR A CB  
1762 O OG1 . THR A 229 ? 0.34869 0.22600 0.43416 0.02311  -0.00939 0.01675  229 THR A OG1 
1763 C CG2 . THR A 229 ? 0.34231 0.22417 0.45037 -0.00318 -0.00854 0.00734  229 THR A CG2 
1764 N N   . PRO A 230 ? 0.37972 0.20645 0.44438 0.00099  0.00027  0.02934  230 PRO A N   
1765 C CA  . PRO A 230 ? 0.46585 0.27950 0.50820 0.01715  -0.00056 0.03620  230 PRO A CA  
1766 C C   . PRO A 230 ? 0.44467 0.27663 0.48141 0.04359  -0.00738 0.03454  230 PRO A C   
1767 O O   . PRO A 230 ? 0.46375 0.30398 0.49098 0.05944  -0.01020 0.03780  230 PRO A O   
1768 C CB  . PRO A 230 ? 0.52248 0.27595 0.52898 0.01381  0.00463  0.03810  230 PRO A CB  
1769 C CG  . PRO A 230 ? 0.50481 0.24484 0.51780 -0.00274 0.00753  0.02963  230 PRO A CG  
1770 C CD  . PRO A 230 ? 0.41593 0.20449 0.46839 -0.01509 0.00561  0.02514  230 PRO A CD  
1771 N N   . ASP A 231 ? 0.41087 0.25356 0.45393 0.04944  -0.01027 0.02804  231 ASP A N   
1772 C CA  . ASP A 231 ? 0.42450 0.28323 0.45990 0.07497  -0.01606 0.02404  231 ASP A CA  
1773 C C   . ASP A 231 ? 0.36396 0.28010 0.42930 0.07543  -0.01705 0.01980  231 ASP A C   
1774 O O   . ASP A 231 ? 0.39603 0.33841 0.46019 0.09494  -0.02075 0.01549  231 ASP A O   
1775 C CB  . ASP A 231 ? 0.43152 0.25745 0.44609 0.08458  -0.01810 0.01855  231 ASP A CB  
1776 C CG  . ASP A 231 ? 0.59048 0.35266 0.56713 0.08707  -0.01615 0.02187  231 ASP A CG  
1777 O OD1 . ASP A 231 ? 0.64671 0.39159 0.60419 0.09457  -0.01581 0.02855  231 ASP A OD1 
1778 O OD2 . ASP A 231 ? 0.77061 0.49816 0.73435 0.08119  -0.01441 0.01737  231 ASP A OD2 
1779 N N   . ASP A 232 ? 0.33182 0.26750 0.42155 0.05516  -0.01348 0.01985  232 ASP A N   
1780 C CA  . ASP A 232 ? 0.26750 0.24858 0.37884 0.05391  -0.01229 0.01630  232 ASP A CA  
1781 C C   . ASP A 232 ? 0.28464 0.27744 0.41645 0.03148  -0.00825 0.01928  232 ASP A C   
1782 O O   . ASP A 232 ? 0.30514 0.27689 0.43755 0.01841  -0.00738 0.02242  232 ASP A O   
1783 C CB  . ASP A 232 ? 0.28435 0.26926 0.39029 0.06461  -0.01392 0.00959  232 ASP A CB  
1784 C CG  . ASP A 232 ? 0.34142 0.29253 0.43882 0.05732  -0.01456 0.00824  232 ASP A CG  
1785 O OD1 . ASP A 232 ? 0.34079 0.28549 0.44831 0.03897  -0.01243 0.01048  232 ASP A OD1 
1786 O OD2 . ASP A 232 ? 0.47381 0.40694 0.55468 0.07081  -0.01764 0.00313  232 ASP A OD2 
1787 N N   . VAL A 233 ? 0.22025 0.24652 0.36693 0.02743  -0.00524 0.01736  233 VAL A N   
1788 C CA  . VAL A 233 ? 0.21028 0.24438 0.37047 0.00994  -0.00169 0.01975  233 VAL A CA  
1789 C C   . VAL A 233 ? 0.26114 0.30388 0.41942 0.01132  0.00015  0.01643  233 VAL A C   
1790 O O   . VAL A 233 ? 0.25055 0.31639 0.40863 0.01939  0.00266  0.01247  233 VAL A O   
1791 C CB  . VAL A 233 ? 0.22234 0.28299 0.39725 0.00114  0.00237  0.02174  233 VAL A CB  
1792 C CG1 . VAL A 233 ? 0.20684 0.26768 0.38983 -0.01493 0.00576  0.02443  233 VAL A CG1 
1793 C CG2 . VAL A 233 ? 0.26257 0.31651 0.43737 0.00201  0.00019  0.02465  233 VAL A CG2 
1794 N N   . GLU A 234 ? 0.23998 0.26670 0.39623 0.00421  -0.00107 0.01678  234 GLU A N   
1795 C CA  . GLU A 234 ? 0.21539 0.24328 0.36419 0.00809  -0.00066 0.01358  234 GLU A CA  
1796 C C   . GLU A 234 ? 0.23245 0.26261 0.38281 -0.00263 0.00227  0.01673  234 GLU A C   
1797 O O   . GLU A 234 ? 0.26305 0.28082 0.41689 -0.00988 -0.00079 0.01801  234 GLU A O   
1798 C CB  . GLU A 234 ? 0.21239 0.21569 0.35140 0.01424  -0.00659 0.00857  234 GLU A CB  
1799 C CG  . GLU A 234 ? 0.22179 0.20869 0.35306 0.02335  -0.00940 0.00668  234 GLU A CG  
1800 C CD  . GLU A 234 ? 0.32420 0.28214 0.44467 0.02530  -0.01355 0.00061  234 GLU A CD  
1801 O OE1 . GLU A 234 ? 0.30232 0.25962 0.42394 0.02149  -0.01535 -0.00377 234 GLU A OE1 
1802 O OE2 . GLU A 234 ? 0.35916 0.29336 0.46780 0.03092  -0.01489 -0.00051 234 GLU A OE2 
1803 N N   . LEU A 235 ? 0.18693 0.23175 0.33227 -0.00308 0.00861  0.01726  235 LEU A N   
1804 C CA  . LEU A 235 ? 0.22733 0.26566 0.36407 -0.01023 0.01207  0.02081  235 LEU A CA  
1805 C C   . LEU A 235 ? 0.26063 0.28964 0.38179 -0.00083 0.00925  0.01745  235 LEU A C   
1806 O O   . LEU A 235 ? 0.24037 0.28122 0.35544 0.00581  0.01286  0.01439  235 LEU A O   
1807 C CB  . LEU A 235 ? 0.19282 0.24841 0.32938 -0.01993 0.02345  0.02364  235 LEU A CB  
1808 C CG  . LEU A 235 ? 0.21091 0.25306 0.33048 -0.02801 0.03009  0.02864  235 LEU A CG  
1809 C CD1 . LEU A 235 ? 0.24423 0.26459 0.36251 -0.03184 0.02442  0.03260  235 LEU A CD1 
1810 C CD2 . LEU A 235 ? 0.21344 0.27355 0.33320 -0.04115 0.04420  0.02929  235 LEU A CD2 
1811 N N   . ILE A 236 ? 0.23324 0.24450 0.34851 0.00080  0.00234  0.01631  236 ILE A N   
1812 C CA  . ILE A 236 ? 0.22757 0.23064 0.33096 0.01146  -0.00351 0.01019  236 ILE A CA  
1813 C C   . ILE A 236 ? 0.33948 0.33171 0.42458 0.01337  -0.00401 0.01257  236 ILE A C   
1814 O O   . ILE A 236 ? 0.29114 0.27469 0.37653 0.00902  -0.00644 0.01519  236 ILE A O   
1815 C CB  . ILE A 236 ? 0.23998 0.23363 0.35280 0.01360  -0.01286 0.00233  236 ILE A CB  
1816 C CG1 . ILE A 236 ? 0.21900 0.21420 0.34096 0.01402  -0.01182 0.00132  236 ILE A CG1 
1817 C CG2 . ILE A 236 ? 0.23936 0.22676 0.34125 0.02355  -0.01939 -0.00658 236 ILE A CG2 
1818 C CD1 . ILE A 236 ? 0.29834 0.27801 0.42626 0.01145  -0.01764 -0.00518 236 ILE A CD1 
1819 N N   . HIS A 237 ? 0.26159 0.25298 0.32805 0.02172  -0.00211 0.01133  237 HIS A N   
1820 C CA  . HIS A 237 ? 0.32413 0.30071 0.36577 0.02789  -0.00360 0.01326  237 HIS A CA  
1821 C C   . HIS A 237 ? 0.29500 0.26972 0.32958 0.04199  -0.01384 0.00301  237 HIS A C   
1822 O O   . HIS A 237 ? 0.29457 0.27823 0.33263 0.04695  -0.01404 -0.00275 237 HIS A O   
1823 C CB  . HIS A 237 ? 0.31544 0.28993 0.33480 0.02408  0.00985  0.02136  237 HIS A CB  
1824 C CG  . HIS A 237 ? 0.41283 0.38082 0.43061 0.00975  0.01940  0.03039  237 HIS A CG  
1825 N ND1 . HIS A 237 ? 0.40403 0.38936 0.44534 -0.00258 0.02526  0.03137  237 HIS A ND1 
1826 C CD2 . HIS A 237 ? 0.45368 0.39746 0.44700 0.00657  0.02376  0.03801  237 HIS A CD2 
1827 C CE1 . HIS A 237 ? 0.40605 0.38081 0.44039 -0.01462 0.03325  0.03830  237 HIS A CE1 
1828 N NE2 . HIS A 237 ? 0.50491 0.45173 0.50897 -0.00965 0.03289  0.04293  237 HIS A NE2 
1829 N N   . PHE A 238 ? 0.30631 0.27056 0.33049 0.04968  -0.02298 -0.00082 238 PHE A N   
1830 C CA  . PHE A 238 ? 0.34409 0.31090 0.36620 0.06222  -0.03468 -0.01417 238 PHE A CA  
1831 C C   . PHE A 238 ? 0.36179 0.31677 0.35700 0.07559  -0.04118 -0.01483 238 PHE A C   
1832 O O   . PHE A 238 ? 0.34749 0.28976 0.33209 0.07393  -0.03951 -0.00678 238 PHE A O   
1833 C CB  . PHE A 238 ? 0.32251 0.29727 0.37297 0.05652  -0.04291 -0.02558 238 PHE A CB  
1834 C CG  . PHE A 238 ? 0.33023 0.30389 0.39135 0.04982  -0.04563 -0.02397 238 PHE A CG  
1835 C CD1 . PHE A 238 ? 0.27846 0.25234 0.35421 0.03616  -0.03822 -0.01487 238 PHE A CD1 
1836 C CD2 . PHE A 238 ? 0.32426 0.29926 0.38045 0.05899  -0.05635 -0.03310 238 PHE A CD2 
1837 C CE1 . PHE A 238 ? 0.29403 0.26768 0.37921 0.03053  -0.04069 -0.01403 238 PHE A CE1 
1838 C CE2 . PHE A 238 ? 0.30887 0.28516 0.37484 0.05455  -0.05930 -0.03310 238 PHE A CE2 
1839 C CZ  . PHE A 238 ? 0.28403 0.25875 0.36450 0.03967  -0.05109 -0.02315 238 PHE A CZ  
1840 N N   . PRO A 239 ? 0.36731 0.32450 0.34860 0.09060  -0.04922 -0.02485 239 PRO A N   
1841 C CA  . PRO A 239 ? 0.44568 0.39092 0.39653 0.10778  -0.05702 -0.02627 239 PRO A CA  
1842 C C   . PRO A 239 ? 0.43492 0.38778 0.39971 0.11276  -0.07072 -0.03829 239 PRO A C   
1843 O O   . PRO A 239 ? 0.43998 0.41073 0.43823 0.10349  -0.07531 -0.04990 239 PRO A O   
1844 C CB  . PRO A 239 ? 0.46855 0.41968 0.40443 0.12233  -0.06191 -0.03581 239 PRO A CB  
1845 C CG  . PRO A 239 ? 0.51103 0.48028 0.47964 0.11321  -0.06291 -0.04671 239 PRO A CG  
1846 C CD  . PRO A 239 ? 0.42331 0.39200 0.41174 0.09447  -0.05133 -0.03522 239 PRO A CD  
1847 N N   . PHE A 240 ? 0.48280 0.42061 0.41847 0.12815  -0.07673 -0.03595 240 PHE A N   
1848 C CA  . PHE A 240 ? 0.46995 0.41881 0.41552 0.13755  -0.09127 -0.04973 240 PHE A CA  
1849 C C   . PHE A 240 ? 0.50649 0.48404 0.47003 0.14614  -0.10481 -0.07385 240 PHE A C   
1850 O O   . PHE A 240 ? 0.44941 0.45055 0.44797 0.13654  -0.11021 -0.08886 240 PHE A O   
1851 C CB  . PHE A 240 ? 0.44757 0.37081 0.35013 0.15832  -0.09655 -0.04332 240 PHE A CB  
1852 C CG  . PHE A 240 ? 0.49957 0.39302 0.38609 0.14820  -0.08443 -0.02321 240 PHE A CG  
1853 C CD1 . PHE A 240 ? 0.44146 0.34240 0.36068 0.12423  -0.07484 -0.01709 240 PHE A CD1 
1854 C CD2 . PHE A 240 ? 0.53757 0.39287 0.37315 0.16295  -0.08243 -0.01105 240 PHE A CD2 
1855 C CE1 . PHE A 240 ? 0.45952 0.33524 0.36516 0.11417  -0.06384 -0.00088 240 PHE A CE1 
1856 C CE2 . PHE A 240 ? 0.56884 0.39343 0.38797 0.15144  -0.07012 0.00608  240 PHE A CE2 
1857 C CZ  . PHE A 240 ? 0.51165 0.34889 0.36802 0.12652  -0.06101 0.01031  240 PHE A CZ  
1858 N N   . LEU A 241 ? 0.50491 0.48110 0.44397 0.16304  -0.10958 -0.07893 241 LEU A N   
1859 C CA  . LEU A 241 ? 0.61522 0.61862 0.56583 0.17445  -0.12382 -0.10406 241 LEU A CA  
1860 C C   . LEU A 241 ? 0.69816 0.70899 0.66093 0.16554  -0.11853 -0.10887 241 LEU A C   
1861 O O   . LEU A 241 ? 0.64109 0.63606 0.59539 0.15703  -0.10535 -0.09239 241 LEU A O   
1862 C CB  . LEU A 241 ? 0.64770 0.64588 0.55823 0.20566  -0.13668 -0.10994 241 LEU A CB  
1863 N N   . GLU A 242 ? 0.73567 0.77232 0.71837 0.16788  -0.12912 -0.13371 242 GLU A N   
1864 C CA  . GLU A 242 ? 0.83962 0.88196 0.83355 0.16070  -0.12605 -0.14233 242 GLU A CA  
1865 C C   . GLU A 242 ? 0.87753 0.90879 0.83469 0.17952  -0.12569 -0.13599 242 GLU A C   
1866 O O   . GLU A 242 ? 0.90802 0.94911 0.84622 0.20101  -0.13794 -0.14926 242 GLU A O   
1867 C CB  . GLU A 242 ? 0.83687 0.90826 0.85868 0.15744  -0.13714 -0.17284 242 GLU A CB  
1868 N N   . GLU A 243 ? 0.86496 0.87823 0.81143 0.17211  -0.11157 -0.11686 243 GLU A N   
1869 C CA  . GLU A 243 ? 0.93003 0.93386 0.84225 0.18658  -0.10797 -0.11006 243 GLU A CA  
1870 C C   . GLU A 243 ? 0.92406 0.94375 0.84695 0.19035  -0.11400 -0.12997 243 GLU A C   
1871 O O   . GLU A 243 ? 0.89081 0.90930 0.82812 0.17878  -0.10620 -0.12901 243 GLU A O   
1872 C CB  . GLU A 243 ? 0.96848 0.95494 0.87053 0.17507  -0.08999 -0.08658 243 GLU A CB  
1873 C CG  . GLU A 243 ? 0.95225 0.92330 0.85159 0.16505  -0.08233 -0.06875 243 GLU A CG  
1874 C CD  . GLU A 243 ? 0.97772 0.92472 0.83068 0.17633  -0.07631 -0.05273 243 GLU A CD  
1875 O OE1 . GLU A 243 ? 0.96116 0.90166 0.78719 0.19680  -0.08753 -0.05828 243 GLU A OE1 
1876 O OE2 . GLU A 243 ? 1.03067 0.96465 0.87222 0.16479  -0.05998 -0.03550 243 GLU A OE2 
1877 N N   . ASN A 244 ? 0.93754 0.97223 0.85196 0.20825  -0.12882 -0.14961 244 ASN A N   
1878 C CA  . ASN A 244 ? 0.91210 0.96296 0.83618 0.21225  -0.13584 -0.17191 244 ASN A CA  
1879 C C   . ASN A 244 ? 0.91083 0.95157 0.80848 0.22107  -0.12819 -0.16263 244 ASN A C   
1880 O O   . ASN A 244 ? 0.87149 0.90401 0.73093 0.23913  -0.12796 -0.15316 244 ASN A O   
1881 C CB  . ASN A 244 ? 0.94082 1.01475 0.86060 0.23127  -0.15414 -0.19660 244 ASN A CB  
1882 C CG  . ASN A 244 ? 0.87308 0.96473 0.82205 0.22264  -0.16193 -0.21009 244 ASN A CG  
1883 O OD1 . ASN A 244 ? 0.99585 1.09285 0.93048 0.23854  -0.17105 -0.21098 244 ASN A OD1 
1884 N ND2 . ASN A 244 ? 0.87030 0.96973 0.85791 0.19799  -0.15799 -0.22111 244 ASN A ND2 
1885 N N   . LEU A 245 ? 0.81829 0.85802 0.73357 0.20901  -0.12152 -0.16561 245 LEU A N   
1886 C CA  . LEU A 245 ? 0.80899 0.84405 0.70317 0.21723  -0.11427 -0.15958 245 LEU A CA  
1887 C C   . LEU A 245 ? 0.77558 0.82279 0.64841 0.23927  -0.12582 -0.17718 245 LEU A C   
1888 O O   . LEU A 245 ? 0.61151 0.67442 0.49928 0.24277  -0.13926 -0.20137 245 LEU A O   
1889 C CB  . LEU A 245 ? 0.73367 0.76519 0.65127 0.20314  -0.10751 -0.16271 245 LEU A CB  
1890 C CG  . LEU A 245 ? 0.66931 0.70038 0.57004 0.21190  -0.10053 -0.15990 245 LEU A CG  
1891 N N   . TYR A 246 ? 0.73345 0.77501 0.57059 0.25345  -0.11988 -0.16601 246 TYR A N   
1892 C CA  . TYR A 246 ? 0.69977 0.75191 0.51295 0.27539  -0.12909 -0.18112 246 TYR A CA  
1893 C C   . TYR A 246 ? 0.70031 0.74747 0.49056 0.27949  -0.11615 -0.16976 246 TYR A C   
1894 O O   . TYR A 246 ? 0.80130 0.83750 0.58619 0.26842  -0.10033 -0.14848 246 TYR A O   
1895 C CB  . TYR A 246 ? 0.72586 0.77771 0.50639 0.29691  -0.13965 -0.18184 246 TYR A CB  
1896 C CG  . TYR A 246 ? 0.77559 0.80305 0.51283 0.30299  -0.12754 -0.15440 246 TYR A CG  
1897 C CD1 . TYR A 246 ? 0.86568 0.87573 0.60315 0.29203  -0.12106 -0.13623 246 TYR A CD1 
1898 C CD2 . TYR A 246 ? 0.79871 0.81864 0.49252 0.31874  -0.12170 -0.14742 246 TYR A CD2 
1899 C CE1 . TYR A 246 ? 0.93546 0.91817 0.63062 0.29511  -0.10848 -0.11200 246 TYR A CE1 
1900 C CE2 . TYR A 246 ? 0.94724 0.94028 0.59762 0.32112  -0.10809 -0.12260 246 TYR A CE2 
1901 C CZ  . TYR A 246 ? 0.98584 0.95880 0.63667 0.30869  -0.10134 -0.10511 246 TYR A CZ  
1902 O OH  . TYR A 246 ? 0.99120 0.93252 0.59626 0.30862  -0.08630 -0.08117 246 TYR A OH  
1903 N N   . PHE A 247 ? 0.62748 0.68622 0.40553 0.29510  -0.12283 -0.18616 247 PHE A N   
1904 C CA  . PHE A 247 ? 0.67389 0.73349 0.43341 0.29978  -0.11146 -0.17995 247 PHE A CA  
1905 C C   . PHE A 247 ? 0.75311 0.81076 0.46306 0.32132  -0.11065 -0.17456 247 PHE A C   
1906 O O   . PHE A 247 ? 0.79923 0.85659 0.48959 0.33747  -0.12319 -0.18127 247 PHE A O   
1907 C CB  . PHE A 247 ? 0.63568 0.70688 0.41703 0.30075  -0.11754 -0.20231 247 PHE A CB  
1908 C CG  . PHE A 247 ? 0.60502 0.67082 0.42785 0.28060  -0.11776 -0.20791 247 PHE A CG  
1909 C CD1 . PHE A 247 ? 0.59784 0.65356 0.43422 0.26383  -0.10480 -0.18870 247 PHE A CD1 
1910 C CD2 . PHE A 247 ? 0.60265 0.67234 0.44863 0.27789  -0.13018 -0.23320 247 PHE A CD2 
1911 C CE1 . PHE A 247 ? 0.55996 0.60706 0.42900 0.24717  -0.10491 -0.19291 247 PHE A CE1 
1912 C CE2 . PHE A 247 ? 0.58220 0.64040 0.46014 0.25830  -0.12850 -0.23732 247 PHE A CE2 
1913 C CZ  . PHE A 247 ? 0.56164 0.60726 0.44948 0.24417  -0.11617 -0.21630 247 PHE A CZ  
1914 N N   . HIS A 250 ? 0.89816 0.98319 0.51872 0.31692  -0.03288 -0.13337 250 HIS A N   
1915 C CA  . HIS A 250 ? 0.89439 0.99219 0.49588 0.31027  -0.01076 -0.12418 250 HIS A CA  
1916 C C   . HIS A 250 ? 0.88210 1.00591 0.48129 0.32604  -0.01306 -0.14252 250 HIS A C   
1917 O O   . HIS A 250 ? 0.88741 1.01550 0.49792 0.34178  -0.03188 -0.16182 250 HIS A O   
1918 C CB  . HIS A 250 ? 0.91709 1.02412 0.55103 0.28674  0.00318  -0.11484 250 HIS A CB  
1919 C CG  . HIS A 250 ? 0.95252 1.03526 0.58879 0.26992  0.00728  -0.09690 250 HIS A CG  
1920 N ND1 . HIS A 250 ? 0.95153 1.02389 0.62042 0.26571  -0.00747 -0.09946 250 HIS A ND1 
1921 C CD2 . HIS A 250 ? 0.95503 1.02045 0.56369 0.25554  0.02525  -0.07686 250 HIS A CD2 
1922 C CE1 . HIS A 250 ? 0.86668 0.91883 0.52931 0.25137  0.00000  -0.08203 250 HIS A CE1 
1923 N NE2 . HIS A 250 ? 0.93714 0.98266 0.56279 0.24492  0.01968  -0.06802 250 HIS A NE2 
1924 N N   . HIS A 251 ? 0.91194 1.05455 0.49674 0.32079  0.00683  -0.13793 251 HIS A N   
1925 C CA  . HIS A 251 ? 0.94601 1.11696 0.52786 0.33548  0.00705  -0.15510 251 HIS A CA  
1926 C C   . HIS A 251 ? 0.93598 1.13734 0.53775 0.32212  0.02520  -0.15469 251 HIS A C   
1927 O O   . HIS A 251 ? 0.95654 1.15735 0.56295 0.30072  0.04163  -0.13926 251 HIS A O   
1928 C CB  . HIS A 251 ? 0.96723 1.13424 0.49958 0.34834  0.01191  -0.15220 251 HIS A CB  
1929 C CG  . HIS A 251 ? 1.01154 1.15937 0.53240 0.36645  -0.01033 -0.15859 251 HIS A CG  
1930 N ND1 . HIS A 251 ? 0.95423 1.07226 0.45626 0.36794  -0.01720 -0.14855 251 HIS A ND1 
1931 C CD2 . HIS A 251 ? 1.02018 1.17746 0.54775 0.38398  -0.02765 -0.17516 251 HIS A CD2 
1932 C CE1 . HIS A 251 ? 0.91625 1.03003 0.41639 0.38601  -0.03801 -0.15976 251 HIS A CE1 
1933 N NE2 . HIS A 251 ? 0.88704 1.02427 0.40252 0.39513  -0.04419 -0.17587 251 HIS A NE2 
1934 N N   . HIS A 252 ? 0.99023 1.21984 0.60436 0.33564  0.02142  -0.17354 252 HIS A N   
1935 C CA  . HIS A 252 ? 1.00963 1.27438 0.64641 0.32695  0.03525  -0.17712 252 HIS A CA  
1936 C C   . HIS A 252 ? 1.03773 1.32385 0.64883 0.32017  0.05542  -0.17152 252 HIS A C   
1937 O O   . HIS A 252 ? 0.99203 1.29869 0.60514 0.33120  0.05190  -0.18318 252 HIS A O   
1938 C CB  . HIS A 252 ? 1.03984 1.31805 0.71139 0.34110  0.01793  -0.19681 252 HIS A CB  
# 
