data_9NT6
# 
_entry.id   9NT6 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.404 
_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   9NT6         pdb_00009nt6 10.2210/pdb9nt6/pdb 
WWPDB D_1000294110 ?            ?                   
# 
_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       2025-06-18 
_pdbx_audit_revision_history.part_number         ? 
# 
_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                        9NT6 
_pdbx_database_status.recvd_initial_deposition_date   2025-03-18 
_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           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              colin.jackson@anu.edu.au 
_pdbx_contact_author.name_first         Colin 
_pdbx_contact_author.name_last          Jackson 
_pdbx_contact_author.name_mi            J 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-6150-3822 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Georgelin, R.L.' 1 0000-0002-1841-1479 
'Frkic, R.L.'     2 0000-0003-0071-9018 
'Tan, L.'         3 0000-0003-0606-4446 
'Kaczmarski, J.'  4 0000-0001-8549-0122 
'Jackson, C.J.'   5 0000-0001-6150-3822 
# 
_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                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
'Crystal structure of ecLacI transcription factor ancestor 4 bound to Beta-methyl-D-galactoside' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Georgelin, R.L.' 1 0000-0002-1841-1479 
primary 'Frkic, R.L.'     2 0000-0003-0071-9018 
primary 'Tan, L.'         3 0000-0003-0606-4446 
primary 'Kaczmarski, J.'  4 0000-0001-8549-0122 
primary 'Jackson, C.J.'   5 0000-0001-6150-3822 
# 
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 'LacI Transcription Factor'       30166.568 2   ? ? ? ? 
2 non-polymer syn 'methyl beta-D-galactopyranoside' 194.182   2   ? ? ? ? 
3 non-polymer syn 1,2-ETHANEDIOL                    62.068    4   ? ? ? ? 
4 water       nat water                             18.015    409 ? ? ? ? 
# 
_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       
;MKQSHTIGLATTNLALHAPSQIVAAIKSRASQMGFNVVISMVEQGVEACKAAVNSLLAQRVDGLIINVPLENEDAQAVAQ
ACGNVPVLFLDVSPAPVNSVLFDPHEGARLGVEHLVALGHQRIALLTGPLTSVSARLRFEGWRQTLAQHQLQPIAVLHGD
WSALSGYQQTMQMLNEGLPTALLVANDQMALGALRALSESGLRVPAQVSVVGYDDTEDSACFIPPLTTIKQDFRLLGQTS
VNRLVQLLQNPSAQSPQLLPVTLVKRKTTAPPENLYFQGLE
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MKQSHTIGLATTNLALHAPSQIVAAIKSRASQMGFNVVISMVEQGVEACKAAVNSLLAQRVDGLIINVPLENEDAQAVAQ
ACGNVPVLFLDVSPAPVNSVLFDPHEGARLGVEHLVALGHQRIALLTGPLTSVSARLRFEGWRQTLAQHQLQPIAVLHGD
WSALSGYQQTMQMLNEGLPTALLVANDQMALGALRALSESGLRVPAQVSVVGYDDTEDSACFIPPLTTIKQDFRLLGQTS
VNRLVQLLQNPSAQSPQLLPVTLVKRKTTAPPENLYFQGLE
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'methyl beta-D-galactopyranoside' MBG 
3 1,2-ETHANEDIOL                    EDO 
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   LYS n 
1 3   GLN n 
1 4   SER n 
1 5   HIS n 
1 6   THR n 
1 7   ILE n 
1 8   GLY n 
1 9   LEU n 
1 10  ALA n 
1 11  THR n 
1 12  THR n 
1 13  ASN n 
1 14  LEU n 
1 15  ALA n 
1 16  LEU n 
1 17  HIS n 
1 18  ALA n 
1 19  PRO n 
1 20  SER n 
1 21  GLN n 
1 22  ILE n 
1 23  VAL n 
1 24  ALA n 
1 25  ALA n 
1 26  ILE n 
1 27  LYS n 
1 28  SER n 
1 29  ARG n 
1 30  ALA n 
1 31  SER n 
1 32  GLN n 
1 33  MET n 
1 34  GLY n 
1 35  PHE n 
1 36  ASN n 
1 37  VAL n 
1 38  VAL n 
1 39  ILE n 
1 40  SER n 
1 41  MET n 
1 42  VAL n 
1 43  GLU n 
1 44  GLN n 
1 45  GLY n 
1 46  VAL n 
1 47  GLU n 
1 48  ALA n 
1 49  CYS n 
1 50  LYS n 
1 51  ALA n 
1 52  ALA n 
1 53  VAL n 
1 54  ASN n 
1 55  SER n 
1 56  LEU n 
1 57  LEU n 
1 58  ALA n 
1 59  GLN n 
1 60  ARG n 
1 61  VAL n 
1 62  ASP n 
1 63  GLY n 
1 64  LEU n 
1 65  ILE n 
1 66  ILE n 
1 67  ASN n 
1 68  VAL n 
1 69  PRO n 
1 70  LEU n 
1 71  GLU n 
1 72  ASN n 
1 73  GLU n 
1 74  ASP n 
1 75  ALA n 
1 76  GLN n 
1 77  ALA n 
1 78  VAL n 
1 79  ALA n 
1 80  GLN n 
1 81  ALA n 
1 82  CYS n 
1 83  GLY n 
1 84  ASN n 
1 85  VAL n 
1 86  PRO n 
1 87  VAL n 
1 88  LEU n 
1 89  PHE n 
1 90  LEU n 
1 91  ASP n 
1 92  VAL n 
1 93  SER n 
1 94  PRO n 
1 95  ALA n 
1 96  PRO n 
1 97  VAL n 
1 98  ASN n 
1 99  SER n 
1 100 VAL n 
1 101 LEU n 
1 102 PHE n 
1 103 ASP n 
1 104 PRO n 
1 105 HIS n 
1 106 GLU n 
1 107 GLY n 
1 108 ALA n 
1 109 ARG n 
1 110 LEU n 
1 111 GLY n 
1 112 VAL n 
1 113 GLU n 
1 114 HIS n 
1 115 LEU n 
1 116 VAL n 
1 117 ALA n 
1 118 LEU n 
1 119 GLY n 
1 120 HIS n 
1 121 GLN n 
1 122 ARG n 
1 123 ILE n 
1 124 ALA n 
1 125 LEU n 
1 126 LEU n 
1 127 THR n 
1 128 GLY n 
1 129 PRO n 
1 130 LEU n 
1 131 THR n 
1 132 SER n 
1 133 VAL n 
1 134 SER n 
1 135 ALA n 
1 136 ARG n 
1 137 LEU n 
1 138 ARG n 
1 139 PHE n 
1 140 GLU n 
1 141 GLY n 
1 142 TRP n 
1 143 ARG n 
1 144 GLN n 
1 145 THR n 
1 146 LEU n 
1 147 ALA n 
1 148 GLN n 
1 149 HIS n 
1 150 GLN n 
1 151 LEU n 
1 152 GLN n 
1 153 PRO n 
1 154 ILE n 
1 155 ALA n 
1 156 VAL n 
1 157 LEU n 
1 158 HIS n 
1 159 GLY n 
1 160 ASP n 
1 161 TRP n 
1 162 SER n 
1 163 ALA n 
1 164 LEU n 
1 165 SER n 
1 166 GLY n 
1 167 TYR n 
1 168 GLN n 
1 169 GLN n 
1 170 THR n 
1 171 MET n 
1 172 GLN n 
1 173 MET n 
1 174 LEU n 
1 175 ASN n 
1 176 GLU n 
1 177 GLY n 
1 178 LEU n 
1 179 PRO n 
1 180 THR n 
1 181 ALA n 
1 182 LEU n 
1 183 LEU n 
1 184 VAL n 
1 185 ALA n 
1 186 ASN n 
1 187 ASP n 
1 188 GLN n 
1 189 MET n 
1 190 ALA n 
1 191 LEU n 
1 192 GLY n 
1 193 ALA n 
1 194 LEU n 
1 195 ARG n 
1 196 ALA n 
1 197 LEU n 
1 198 SER n 
1 199 GLU n 
1 200 SER n 
1 201 GLY n 
1 202 LEU n 
1 203 ARG n 
1 204 VAL n 
1 205 PRO n 
1 206 ALA n 
1 207 GLN n 
1 208 VAL n 
1 209 SER n 
1 210 VAL n 
1 211 VAL n 
1 212 GLY n 
1 213 TYR n 
1 214 ASP n 
1 215 ASP n 
1 216 THR n 
1 217 GLU n 
1 218 ASP n 
1 219 SER n 
1 220 ALA n 
1 221 CYS n 
1 222 PHE n 
1 223 ILE n 
1 224 PRO n 
1 225 PRO n 
1 226 LEU n 
1 227 THR n 
1 228 THR n 
1 229 ILE n 
1 230 LYS n 
1 231 GLN n 
1 232 ASP n 
1 233 PHE n 
1 234 ARG n 
1 235 LEU n 
1 236 LEU n 
1 237 GLY n 
1 238 GLN n 
1 239 THR n 
1 240 SER n 
1 241 VAL n 
1 242 ASN n 
1 243 ARG n 
1 244 LEU n 
1 245 VAL n 
1 246 GLN n 
1 247 LEU n 
1 248 LEU n 
1 249 GLN n 
1 250 ASN n 
1 251 PRO n 
1 252 SER n 
1 253 ALA n 
1 254 GLN n 
1 255 SER n 
1 256 PRO n 
1 257 GLN n 
1 258 LEU n 
1 259 LEU n 
1 260 PRO n 
1 261 VAL n 
1 262 THR n 
1 263 LEU n 
1 264 VAL n 
1 265 LYS n 
1 266 ARG n 
1 267 LYS n 
1 268 THR n 
1 269 THR n 
1 270 ALA n 
1 271 PRO n 
1 272 PRO n 
1 273 GLU n 
1 274 ASN n 
1 275 LEU n 
1 276 TYR n 
1 277 PHE n 
1 278 GLN n 
1 279 GLY n 
1 280 LEU n 
1 281 GLU 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                   281 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     562 
_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 
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 
EDO non-polymer         . 1,2-ETHANEDIOL                    'ETHYLENE GLYCOL' 'C2 H6 O2'       62.068  
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 
MBG D-saccharide        n 'methyl beta-D-galactopyranoside' 
'METHYL-BETA-GALACTOSE; methyl beta-D-galactoside; methyl D-galactoside; methyl galactoside' 'C7 H14 O6'      194.182 
MET 'L-peptide linking' y METHIONINE                        ? 'C5 H11 N O2 S'  149.211 
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_chem_comp_identifier.comp_id 
_pdbx_chem_comp_identifier.type 
_pdbx_chem_comp_identifier.program 
_pdbx_chem_comp_identifier.program_version 
_pdbx_chem_comp_identifier.identifier 
MBG 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 'DGalp[1Me]b'                
MBG 'COMMON NAME'                         GMML     1.0 1-methyl-b-D-galactopyranose 
MBG 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 b-methyl-galactoside         
# 
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   58  ?   ?   ?   A . n 
A 1 2   LYS 2   59  ?   ?   ?   A . n 
A 1 3   GLN 3   60  ?   ?   ?   A . n 
A 1 4   SER 4   61  61  SER SER A . n 
A 1 5   HIS 5   62  62  HIS HIS A . n 
A 1 6   THR 6   63  63  THR THR A . n 
A 1 7   ILE 7   64  64  ILE ILE A . n 
A 1 8   GLY 8   65  65  GLY GLY A . n 
A 1 9   LEU 9   66  66  LEU LEU A . n 
A 1 10  ALA 10  67  67  ALA ALA A . n 
A 1 11  THR 11  68  68  THR THR A . n 
A 1 12  THR 12  69  69  THR THR A . n 
A 1 13  ASN 13  70  70  ASN ASN A . n 
A 1 14  LEU 14  71  71  LEU LEU A . n 
A 1 15  ALA 15  72  72  ALA ALA A . n 
A 1 16  LEU 16  73  73  LEU LEU A . n 
A 1 17  HIS 17  74  74  HIS HIS A . n 
A 1 18  ALA 18  75  75  ALA ALA A . n 
A 1 19  PRO 19  76  76  PRO PRO A . n 
A 1 20  SER 20  77  77  SER SER A . n 
A 1 21  GLN 21  78  78  GLN GLN A . n 
A 1 22  ILE 22  79  79  ILE ILE A . n 
A 1 23  VAL 23  80  80  VAL VAL A . n 
A 1 24  ALA 24  81  81  ALA ALA A . n 
A 1 25  ALA 25  82  82  ALA ALA A . n 
A 1 26  ILE 26  83  83  ILE ILE A . n 
A 1 27  LYS 27  84  84  LYS LYS A . n 
A 1 28  SER 28  85  85  SER SER A . n 
A 1 29  ARG 29  86  86  ARG ARG A . n 
A 1 30  ALA 30  87  87  ALA ALA A . n 
A 1 31  SER 31  88  88  SER SER A . n 
A 1 32  GLN 32  89  89  GLN GLN A . n 
A 1 33  MET 33  90  90  MET MET A . n 
A 1 34  GLY 34  91  91  GLY GLY A . n 
A 1 35  PHE 35  92  92  PHE PHE A . n 
A 1 36  ASN 36  93  93  ASN ASN A . n 
A 1 37  VAL 37  94  94  VAL VAL A . n 
A 1 38  VAL 38  95  95  VAL VAL A . n 
A 1 39  ILE 39  96  96  ILE ILE A . n 
A 1 40  SER 40  97  97  SER SER A . n 
A 1 41  MET 41  98  98  MET MET A . n 
A 1 42  VAL 42  99  99  VAL VAL A . n 
A 1 43  GLU 43  100 100 GLU GLU A . n 
A 1 44  GLN 44  101 101 GLN GLN A . n 
A 1 45  GLY 45  102 102 GLY GLY A . n 
A 1 46  VAL 46  103 103 VAL VAL A . n 
A 1 47  GLU 47  104 104 GLU GLU A . n 
A 1 48  ALA 48  105 105 ALA ALA A . n 
A 1 49  CYS 49  106 106 CYS CYS A . n 
A 1 50  LYS 50  107 107 LYS LYS A . n 
A 1 51  ALA 51  108 108 ALA ALA A . n 
A 1 52  ALA 52  109 109 ALA ALA A . n 
A 1 53  VAL 53  110 110 VAL VAL A . n 
A 1 54  ASN 54  111 111 ASN ASN A . n 
A 1 55  SER 55  112 112 SER SER A . n 
A 1 56  LEU 56  113 113 LEU LEU A . n 
A 1 57  LEU 57  114 114 LEU LEU A . n 
A 1 58  ALA 58  115 115 ALA ALA A . n 
A 1 59  GLN 59  116 116 GLN GLN A . n 
A 1 60  ARG 60  117 117 ARG ARG A . n 
A 1 61  VAL 61  118 118 VAL VAL A . n 
A 1 62  ASP 62  119 119 ASP ASP A . n 
A 1 63  GLY 63  120 120 GLY GLY A . n 
A 1 64  LEU 64  121 121 LEU LEU A . n 
A 1 65  ILE 65  122 122 ILE ILE A . n 
A 1 66  ILE 66  123 123 ILE ILE A . n 
A 1 67  ASN 67  124 124 ASN ASN A . n 
A 1 68  VAL 68  125 125 VAL VAL A . n 
A 1 69  PRO 69  126 126 PRO PRO A . n 
A 1 70  LEU 70  127 127 LEU LEU A . n 
A 1 71  GLU 71  128 128 GLU GLU A . n 
A 1 72  ASN 72  129 129 ASN ASN A . n 
A 1 73  GLU 73  130 130 GLU GLU A . n 
A 1 74  ASP 74  131 131 ASP ASP A . n 
A 1 75  ALA 75  132 132 ALA ALA A . n 
A 1 76  GLN 76  133 133 GLN GLN A . n 
A 1 77  ALA 77  134 134 ALA ALA A . n 
A 1 78  VAL 78  135 135 VAL VAL A . n 
A 1 79  ALA 79  136 136 ALA ALA A . n 
A 1 80  GLN 80  137 137 GLN GLN A . n 
A 1 81  ALA 81  138 138 ALA ALA A . n 
A 1 82  CYS 82  139 139 CYS CYS A . n 
A 1 83  GLY 83  140 140 GLY GLY A . n 
A 1 84  ASN 84  141 141 ASN ASN A . n 
A 1 85  VAL 85  142 142 VAL VAL A . n 
A 1 86  PRO 86  143 143 PRO PRO A . n 
A 1 87  VAL 87  144 144 VAL VAL A . n 
A 1 88  LEU 88  145 145 LEU LEU A . n 
A 1 89  PHE 89  146 146 PHE PHE A . n 
A 1 90  LEU 90  147 147 LEU LEU A . n 
A 1 91  ASP 91  148 148 ASP ASP A . n 
A 1 92  VAL 92  149 149 VAL VAL A . n 
A 1 93  SER 93  150 150 SER SER A . n 
A 1 94  PRO 94  151 151 PRO PRO A . n 
A 1 95  ALA 95  152 152 ALA ALA A . n 
A 1 96  PRO 96  153 153 PRO PRO A . n 
A 1 97  VAL 97  154 154 VAL VAL A . n 
A 1 98  ASN 98  155 155 ASN ASN A . n 
A 1 99  SER 99  156 156 SER SER A . n 
A 1 100 VAL 100 157 157 VAL VAL A . n 
A 1 101 LEU 101 158 158 LEU LEU A . n 
A 1 102 PHE 102 159 159 PHE PHE A . n 
A 1 103 ASP 103 160 160 ASP ASP A . n 
A 1 104 PRO 104 161 161 PRO PRO A . n 
A 1 105 HIS 105 162 162 HIS HIS A . n 
A 1 106 GLU 106 163 163 GLU GLU A . n 
A 1 107 GLY 107 164 164 GLY GLY A . n 
A 1 108 ALA 108 165 165 ALA ALA A . n 
A 1 109 ARG 109 166 166 ARG ARG A . n 
A 1 110 LEU 110 167 167 LEU LEU A . n 
A 1 111 GLY 111 168 168 GLY GLY A . n 
A 1 112 VAL 112 169 169 VAL VAL A . n 
A 1 113 GLU 113 170 170 GLU GLU A . n 
A 1 114 HIS 114 171 171 HIS HIS A . n 
A 1 115 LEU 115 172 172 LEU LEU A . n 
A 1 116 VAL 116 173 173 VAL VAL A . n 
A 1 117 ALA 117 174 174 ALA ALA A . n 
A 1 118 LEU 118 175 175 LEU LEU A . n 
A 1 119 GLY 119 176 176 GLY GLY A . n 
A 1 120 HIS 120 177 177 HIS HIS A . n 
A 1 121 GLN 121 178 178 GLN GLN A . n 
A 1 122 ARG 122 179 179 ARG ARG A . n 
A 1 123 ILE 123 180 180 ILE ILE A . n 
A 1 124 ALA 124 181 181 ALA ALA A . n 
A 1 125 LEU 125 182 182 LEU LEU A . n 
A 1 126 LEU 126 183 183 LEU LEU A . n 
A 1 127 THR 127 184 184 THR THR A . n 
A 1 128 GLY 128 185 185 GLY GLY A . n 
A 1 129 PRO 129 186 186 PRO PRO A . n 
A 1 130 LEU 130 187 187 LEU LEU A . n 
A 1 131 THR 131 188 188 THR THR A . n 
A 1 132 SER 132 189 189 SER SER A . n 
A 1 133 VAL 133 190 190 VAL VAL A . n 
A 1 134 SER 134 191 191 SER SER A . n 
A 1 135 ALA 135 192 192 ALA ALA A . n 
A 1 136 ARG 136 193 193 ARG ARG A . n 
A 1 137 LEU 137 194 194 LEU LEU A . n 
A 1 138 ARG 138 195 195 ARG ARG A . n 
A 1 139 PHE 139 196 196 PHE PHE A . n 
A 1 140 GLU 140 197 197 GLU GLU A . n 
A 1 141 GLY 141 198 198 GLY GLY A . n 
A 1 142 TRP 142 199 199 TRP TRP A . n 
A 1 143 ARG 143 200 200 ARG ARG A . n 
A 1 144 GLN 144 201 201 GLN GLN A . n 
A 1 145 THR 145 202 202 THR THR A . n 
A 1 146 LEU 146 203 203 LEU LEU A . n 
A 1 147 ALA 147 204 204 ALA ALA A . n 
A 1 148 GLN 148 205 205 GLN GLN A . n 
A 1 149 HIS 149 206 206 HIS HIS A . n 
A 1 150 GLN 150 207 207 GLN GLN A . n 
A 1 151 LEU 151 208 208 LEU LEU A . n 
A 1 152 GLN 152 209 209 GLN GLN A . n 
A 1 153 PRO 153 210 210 PRO PRO A . n 
A 1 154 ILE 154 211 211 ILE ILE A . n 
A 1 155 ALA 155 212 212 ALA ALA A . n 
A 1 156 VAL 156 213 213 VAL VAL A . n 
A 1 157 LEU 157 214 214 LEU LEU A . n 
A 1 158 HIS 158 215 215 HIS HIS A . n 
A 1 159 GLY 159 216 216 GLY GLY A . n 
A 1 160 ASP 160 217 217 ASP ASP A . n 
A 1 161 TRP 161 218 218 TRP TRP A . n 
A 1 162 SER 162 219 219 SER SER A . n 
A 1 163 ALA 163 220 220 ALA ALA A . n 
A 1 164 LEU 164 221 221 LEU LEU A . n 
A 1 165 SER 165 222 222 SER SER A . n 
A 1 166 GLY 166 223 223 GLY GLY A . n 
A 1 167 TYR 167 224 224 TYR TYR A . n 
A 1 168 GLN 168 225 225 GLN GLN A . n 
A 1 169 GLN 169 226 226 GLN GLN A . n 
A 1 170 THR 170 227 227 THR THR A . n 
A 1 171 MET 171 228 228 MET MET A . n 
A 1 172 GLN 172 229 229 GLN GLN A . n 
A 1 173 MET 173 230 230 MET MET A . n 
A 1 174 LEU 174 231 231 LEU LEU A . n 
A 1 175 ASN 175 232 232 ASN ASN A . n 
A 1 176 GLU 176 233 233 GLU GLU A . n 
A 1 177 GLY 177 234 234 GLY GLY A . n 
A 1 178 LEU 178 235 235 LEU LEU A . n 
A 1 179 PRO 179 236 236 PRO PRO A . n 
A 1 180 THR 180 237 237 THR THR A . n 
A 1 181 ALA 181 238 238 ALA ALA A . n 
A 1 182 LEU 182 239 239 LEU LEU A . n 
A 1 183 LEU 183 240 240 LEU LEU A . n 
A 1 184 VAL 184 241 241 VAL VAL A . n 
A 1 185 ALA 185 242 242 ALA ALA A . n 
A 1 186 ASN 186 243 243 ASN ASN A . n 
A 1 187 ASP 187 244 244 ASP ASP A . n 
A 1 188 GLN 188 245 245 GLN GLN A . n 
A 1 189 MET 189 246 246 MET MET A . n 
A 1 190 ALA 190 247 247 ALA ALA A . n 
A 1 191 LEU 191 248 248 LEU LEU A . n 
A 1 192 GLY 192 249 249 GLY GLY A . n 
A 1 193 ALA 193 250 250 ALA ALA A . n 
A 1 194 LEU 194 251 251 LEU LEU A . n 
A 1 195 ARG 195 252 252 ARG ARG A . n 
A 1 196 ALA 196 253 253 ALA ALA A . n 
A 1 197 LEU 197 254 254 LEU LEU A . n 
A 1 198 SER 198 255 255 SER SER A . n 
A 1 199 GLU 199 256 256 GLU GLU A . n 
A 1 200 SER 200 257 257 SER SER A . n 
A 1 201 GLY 201 258 258 GLY GLY A . n 
A 1 202 LEU 202 259 259 LEU LEU A . n 
A 1 203 ARG 203 260 260 ARG ARG A . n 
A 1 204 VAL 204 261 261 VAL VAL A . n 
A 1 205 PRO 205 262 262 PRO PRO A . n 
A 1 206 ALA 206 263 263 ALA ALA A . n 
A 1 207 GLN 207 264 264 GLN GLN A . n 
A 1 208 VAL 208 265 265 VAL VAL A . n 
A 1 209 SER 209 266 266 SER SER A . n 
A 1 210 VAL 210 267 267 VAL VAL A . n 
A 1 211 VAL 211 268 268 VAL VAL A . n 
A 1 212 GLY 212 269 269 GLY GLY A . n 
A 1 213 TYR 213 270 270 TYR TYR A . n 
A 1 214 ASP 214 271 271 ASP ASP A . n 
A 1 215 ASP 215 272 272 ASP ASP A . n 
A 1 216 THR 216 273 273 THR THR A . n 
A 1 217 GLU 217 274 274 GLU GLU A . n 
A 1 218 ASP 218 275 275 ASP ASP A . n 
A 1 219 SER 219 276 276 SER SER A . n 
A 1 220 ALA 220 277 277 ALA ALA A . n 
A 1 221 CYS 221 278 278 CYS CYS A . n 
A 1 222 PHE 222 279 279 PHE PHE A . n 
A 1 223 ILE 223 280 280 ILE ILE A . n 
A 1 224 PRO 224 281 281 PRO PRO A . n 
A 1 225 PRO 225 282 282 PRO PRO A . n 
A 1 226 LEU 226 283 283 LEU LEU A . n 
A 1 227 THR 227 284 284 THR THR A . n 
A 1 228 THR 228 285 285 THR THR A . n 
A 1 229 ILE 229 286 286 ILE ILE A . n 
A 1 230 LYS 230 287 287 LYS LYS A . n 
A 1 231 GLN 231 288 288 GLN GLN A . n 
A 1 232 ASP 232 289 289 ASP ASP A . n 
A 1 233 PHE 233 290 290 PHE PHE A . n 
A 1 234 ARG 234 291 291 ARG ARG A . n 
A 1 235 LEU 235 292 292 LEU LEU A . n 
A 1 236 LEU 236 293 293 LEU LEU A . n 
A 1 237 GLY 237 294 294 GLY GLY A . n 
A 1 238 GLN 238 295 295 GLN GLN A . n 
A 1 239 THR 239 296 296 THR THR A . n 
A 1 240 SER 240 297 297 SER SER A . n 
A 1 241 VAL 241 298 298 VAL VAL A . n 
A 1 242 ASN 242 299 299 ASN ASN A . n 
A 1 243 ARG 243 300 300 ARG ARG A . n 
A 1 244 LEU 244 301 301 LEU LEU A . n 
A 1 245 VAL 245 302 302 VAL VAL A . n 
A 1 246 GLN 246 303 303 GLN GLN A . n 
A 1 247 LEU 247 304 304 LEU LEU A . n 
A 1 248 LEU 248 305 305 LEU LEU A . n 
A 1 249 GLN 249 306 306 GLN GLN A . n 
A 1 250 ASN 250 307 307 ASN ASN A . n 
A 1 251 PRO 251 308 308 PRO PRO A . n 
A 1 252 SER 252 309 309 SER SER A . n 
A 1 253 ALA 253 310 310 ALA ALA A . n 
A 1 254 GLN 254 311 311 GLN GLN A . n 
A 1 255 SER 255 312 312 SER SER A . n 
A 1 256 PRO 256 313 313 PRO PRO A . n 
A 1 257 GLN 257 314 314 GLN GLN A . n 
A 1 258 LEU 258 315 315 LEU LEU A . n 
A 1 259 LEU 259 316 316 LEU LEU A . n 
A 1 260 PRO 260 317 317 PRO PRO A . n 
A 1 261 VAL 261 318 318 VAL VAL A . n 
A 1 262 THR 262 319 319 THR THR A . n 
A 1 263 LEU 263 320 320 LEU LEU A . n 
A 1 264 VAL 264 321 321 VAL VAL A . n 
A 1 265 LYS 265 322 322 LYS LYS A . n 
A 1 266 ARG 266 323 323 ARG ARG A . n 
A 1 267 LYS 267 324 324 LYS LYS A . n 
A 1 268 THR 268 325 325 THR THR A . n 
A 1 269 THR 269 326 326 THR THR A . n 
A 1 270 ALA 270 327 327 ALA ALA A . n 
A 1 271 PRO 271 328 328 PRO PRO A . n 
A 1 272 PRO 272 329 329 PRO PRO A . n 
A 1 273 GLU 273 330 330 GLU GLU A . n 
A 1 274 ASN 274 331 331 ASN ASN A . n 
A 1 275 LEU 275 332 ?   ?   ?   A . n 
A 1 276 TYR 276 333 ?   ?   ?   A . n 
A 1 277 PHE 277 334 ?   ?   ?   A . n 
A 1 278 GLN 278 335 ?   ?   ?   A . n 
A 1 279 GLY 279 336 ?   ?   ?   A . n 
A 1 280 LEU 280 337 ?   ?   ?   A . n 
A 1 281 GLU 281 338 ?   ?   ?   A . n 
B 1 1   MET 1   58  ?   ?   ?   B . n 
B 1 2   LYS 2   59  59  LYS LYS B . n 
B 1 3   GLN 3   60  60  GLN GLN B . n 
B 1 4   SER 4   61  61  SER SER B . n 
B 1 5   HIS 5   62  62  HIS HIS B . n 
B 1 6   THR 6   63  63  THR THR B . n 
B 1 7   ILE 7   64  64  ILE ILE B . n 
B 1 8   GLY 8   65  65  GLY GLY B . n 
B 1 9   LEU 9   66  66  LEU LEU B . n 
B 1 10  ALA 10  67  67  ALA ALA B . n 
B 1 11  THR 11  68  68  THR THR B . n 
B 1 12  THR 12  69  69  THR THR B . n 
B 1 13  ASN 13  70  70  ASN ASN B . n 
B 1 14  LEU 14  71  71  LEU LEU B . n 
B 1 15  ALA 15  72  72  ALA ALA B . n 
B 1 16  LEU 16  73  73  LEU LEU B . n 
B 1 17  HIS 17  74  74  HIS HIS B . n 
B 1 18  ALA 18  75  75  ALA ALA B . n 
B 1 19  PRO 19  76  76  PRO PRO B . n 
B 1 20  SER 20  77  77  SER SER B . n 
B 1 21  GLN 21  78  78  GLN GLN B . n 
B 1 22  ILE 22  79  79  ILE ILE B . n 
B 1 23  VAL 23  80  80  VAL VAL B . n 
B 1 24  ALA 24  81  81  ALA ALA B . n 
B 1 25  ALA 25  82  82  ALA ALA B . n 
B 1 26  ILE 26  83  83  ILE ILE B . n 
B 1 27  LYS 27  84  84  LYS LYS B . n 
B 1 28  SER 28  85  85  SER SER B . n 
B 1 29  ARG 29  86  86  ARG ARG B . n 
B 1 30  ALA 30  87  87  ALA ALA B . n 
B 1 31  SER 31  88  88  SER SER B . n 
B 1 32  GLN 32  89  89  GLN GLN B . n 
B 1 33  MET 33  90  90  MET MET B . n 
B 1 34  GLY 34  91  91  GLY GLY B . n 
B 1 35  PHE 35  92  92  PHE PHE B . n 
B 1 36  ASN 36  93  93  ASN ASN B . n 
B 1 37  VAL 37  94  94  VAL VAL B . n 
B 1 38  VAL 38  95  95  VAL VAL B . n 
B 1 39  ILE 39  96  96  ILE ILE B . n 
B 1 40  SER 40  97  97  SER SER B . n 
B 1 41  MET 41  98  98  MET MET B . n 
B 1 42  VAL 42  99  99  VAL VAL B . n 
B 1 43  GLU 43  100 100 GLU GLU B . n 
B 1 44  GLN 44  101 101 GLN GLN B . n 
B 1 45  GLY 45  102 102 GLY GLY B . n 
B 1 46  VAL 46  103 103 VAL VAL B . n 
B 1 47  GLU 47  104 104 GLU GLU B . n 
B 1 48  ALA 48  105 105 ALA ALA B . n 
B 1 49  CYS 49  106 106 CYS CYS B . n 
B 1 50  LYS 50  107 107 LYS LYS B . n 
B 1 51  ALA 51  108 108 ALA ALA B . n 
B 1 52  ALA 52  109 109 ALA ALA B . n 
B 1 53  VAL 53  110 110 VAL VAL B . n 
B 1 54  ASN 54  111 111 ASN ASN B . n 
B 1 55  SER 55  112 112 SER SER B . n 
B 1 56  LEU 56  113 113 LEU LEU B . n 
B 1 57  LEU 57  114 114 LEU LEU B . n 
B 1 58  ALA 58  115 115 ALA ALA B . n 
B 1 59  GLN 59  116 116 GLN GLN B . n 
B 1 60  ARG 60  117 117 ARG ARG B . n 
B 1 61  VAL 61  118 118 VAL VAL B . n 
B 1 62  ASP 62  119 119 ASP ASP B . n 
B 1 63  GLY 63  120 120 GLY GLY B . n 
B 1 64  LEU 64  121 121 LEU LEU B . n 
B 1 65  ILE 65  122 122 ILE ILE B . n 
B 1 66  ILE 66  123 123 ILE ILE B . n 
B 1 67  ASN 67  124 124 ASN ASN B . n 
B 1 68  VAL 68  125 125 VAL VAL B . n 
B 1 69  PRO 69  126 126 PRO PRO B . n 
B 1 70  LEU 70  127 127 LEU LEU B . n 
B 1 71  GLU 71  128 128 GLU GLU B . n 
B 1 72  ASN 72  129 129 ASN ASN B . n 
B 1 73  GLU 73  130 130 GLU GLU B . n 
B 1 74  ASP 74  131 131 ASP ASP B . n 
B 1 75  ALA 75  132 132 ALA ALA B . n 
B 1 76  GLN 76  133 133 GLN GLN B . n 
B 1 77  ALA 77  134 134 ALA ALA B . n 
B 1 78  VAL 78  135 135 VAL VAL B . n 
B 1 79  ALA 79  136 136 ALA ALA B . n 
B 1 80  GLN 80  137 137 GLN GLN B . n 
B 1 81  ALA 81  138 138 ALA ALA B . n 
B 1 82  CYS 82  139 139 CYS CYS B . n 
B 1 83  GLY 83  140 140 GLY GLY B . n 
B 1 84  ASN 84  141 141 ASN ASN B . n 
B 1 85  VAL 85  142 142 VAL VAL B . n 
B 1 86  PRO 86  143 143 PRO PRO B . n 
B 1 87  VAL 87  144 144 VAL VAL B . n 
B 1 88  LEU 88  145 145 LEU LEU B . n 
B 1 89  PHE 89  146 146 PHE PHE B . n 
B 1 90  LEU 90  147 147 LEU LEU B . n 
B 1 91  ASP 91  148 148 ASP ASP B . n 
B 1 92  VAL 92  149 149 VAL VAL B . n 
B 1 93  SER 93  150 150 SER SER B . n 
B 1 94  PRO 94  151 151 PRO PRO B . n 
B 1 95  ALA 95  152 152 ALA ALA B . n 
B 1 96  PRO 96  153 153 PRO PRO B . n 
B 1 97  VAL 97  154 154 VAL VAL B . n 
B 1 98  ASN 98  155 155 ASN ASN B . n 
B 1 99  SER 99  156 156 SER SER B . n 
B 1 100 VAL 100 157 157 VAL VAL B . n 
B 1 101 LEU 101 158 158 LEU LEU B . n 
B 1 102 PHE 102 159 159 PHE PHE B . n 
B 1 103 ASP 103 160 160 ASP ASP B . n 
B 1 104 PRO 104 161 161 PRO PRO B . n 
B 1 105 HIS 105 162 162 HIS HIS B . n 
B 1 106 GLU 106 163 163 GLU GLU B . n 
B 1 107 GLY 107 164 164 GLY GLY B . n 
B 1 108 ALA 108 165 165 ALA ALA B . n 
B 1 109 ARG 109 166 166 ARG ARG B . n 
B 1 110 LEU 110 167 167 LEU LEU B . n 
B 1 111 GLY 111 168 168 GLY GLY B . n 
B 1 112 VAL 112 169 169 VAL VAL B . n 
B 1 113 GLU 113 170 170 GLU GLU B . n 
B 1 114 HIS 114 171 171 HIS HIS B . n 
B 1 115 LEU 115 172 172 LEU LEU B . n 
B 1 116 VAL 116 173 173 VAL VAL B . n 
B 1 117 ALA 117 174 174 ALA ALA B . n 
B 1 118 LEU 118 175 175 LEU LEU B . n 
B 1 119 GLY 119 176 176 GLY GLY B . n 
B 1 120 HIS 120 177 177 HIS HIS B . n 
B 1 121 GLN 121 178 178 GLN GLN B . n 
B 1 122 ARG 122 179 179 ARG ARG B . n 
B 1 123 ILE 123 180 180 ILE ILE B . n 
B 1 124 ALA 124 181 181 ALA ALA B . n 
B 1 125 LEU 125 182 182 LEU LEU B . n 
B 1 126 LEU 126 183 183 LEU LEU B . n 
B 1 127 THR 127 184 184 THR THR B . n 
B 1 128 GLY 128 185 185 GLY GLY B . n 
B 1 129 PRO 129 186 186 PRO PRO B . n 
B 1 130 LEU 130 187 187 LEU LEU B . n 
B 1 131 THR 131 188 188 THR THR B . n 
B 1 132 SER 132 189 189 SER SER B . n 
B 1 133 VAL 133 190 190 VAL VAL B . n 
B 1 134 SER 134 191 191 SER SER B . n 
B 1 135 ALA 135 192 192 ALA ALA B . n 
B 1 136 ARG 136 193 193 ARG ARG B . n 
B 1 137 LEU 137 194 194 LEU LEU B . n 
B 1 138 ARG 138 195 195 ARG ARG B . n 
B 1 139 PHE 139 196 196 PHE PHE B . n 
B 1 140 GLU 140 197 197 GLU GLU B . n 
B 1 141 GLY 141 198 198 GLY GLY B . n 
B 1 142 TRP 142 199 199 TRP TRP B . n 
B 1 143 ARG 143 200 200 ARG ARG B . n 
B 1 144 GLN 144 201 201 GLN GLN B . n 
B 1 145 THR 145 202 202 THR THR B . n 
B 1 146 LEU 146 203 203 LEU LEU B . n 
B 1 147 ALA 147 204 204 ALA ALA B . n 
B 1 148 GLN 148 205 205 GLN GLN B . n 
B 1 149 HIS 149 206 206 HIS HIS B . n 
B 1 150 GLN 150 207 207 GLN GLN B . n 
B 1 151 LEU 151 208 208 LEU LEU B . n 
B 1 152 GLN 152 209 209 GLN GLN B . n 
B 1 153 PRO 153 210 210 PRO PRO B . n 
B 1 154 ILE 154 211 211 ILE ILE B . n 
B 1 155 ALA 155 212 212 ALA ALA B . n 
B 1 156 VAL 156 213 213 VAL VAL B . n 
B 1 157 LEU 157 214 214 LEU LEU B . n 
B 1 158 HIS 158 215 215 HIS HIS B . n 
B 1 159 GLY 159 216 216 GLY GLY B . n 
B 1 160 ASP 160 217 217 ASP ASP B . n 
B 1 161 TRP 161 218 218 TRP TRP B . n 
B 1 162 SER 162 219 219 SER SER B . n 
B 1 163 ALA 163 220 220 ALA ALA B . n 
B 1 164 LEU 164 221 221 LEU LEU B . n 
B 1 165 SER 165 222 222 SER SER B . n 
B 1 166 GLY 166 223 223 GLY GLY B . n 
B 1 167 TYR 167 224 224 TYR TYR B . n 
B 1 168 GLN 168 225 225 GLN GLN B . n 
B 1 169 GLN 169 226 226 GLN GLN B . n 
B 1 170 THR 170 227 227 THR THR B . n 
B 1 171 MET 171 228 228 MET MET B . n 
B 1 172 GLN 172 229 229 GLN GLN B . n 
B 1 173 MET 173 230 230 MET MET B . n 
B 1 174 LEU 174 231 231 LEU LEU B . n 
B 1 175 ASN 175 232 232 ASN ASN B . n 
B 1 176 GLU 176 233 233 GLU GLU B . n 
B 1 177 GLY 177 234 234 GLY GLY B . n 
B 1 178 LEU 178 235 235 LEU LEU B . n 
B 1 179 PRO 179 236 236 PRO PRO B . n 
B 1 180 THR 180 237 237 THR THR B . n 
B 1 181 ALA 181 238 238 ALA ALA B . n 
B 1 182 LEU 182 239 239 LEU LEU B . n 
B 1 183 LEU 183 240 240 LEU LEU B . n 
B 1 184 VAL 184 241 241 VAL VAL B . n 
B 1 185 ALA 185 242 242 ALA ALA B . n 
B 1 186 ASN 186 243 243 ASN ASN B . n 
B 1 187 ASP 187 244 244 ASP ASP B . n 
B 1 188 GLN 188 245 245 GLN GLN B . n 
B 1 189 MET 189 246 246 MET MET B . n 
B 1 190 ALA 190 247 247 ALA ALA B . n 
B 1 191 LEU 191 248 248 LEU LEU B . n 
B 1 192 GLY 192 249 249 GLY GLY B . n 
B 1 193 ALA 193 250 250 ALA ALA B . n 
B 1 194 LEU 194 251 251 LEU LEU B . n 
B 1 195 ARG 195 252 252 ARG ARG B . n 
B 1 196 ALA 196 253 253 ALA ALA B . n 
B 1 197 LEU 197 254 254 LEU LEU B . n 
B 1 198 SER 198 255 255 SER SER B . n 
B 1 199 GLU 199 256 256 GLU GLU B . n 
B 1 200 SER 200 257 257 SER SER B . n 
B 1 201 GLY 201 258 258 GLY GLY B . n 
B 1 202 LEU 202 259 259 LEU LEU B . n 
B 1 203 ARG 203 260 260 ARG ARG B . n 
B 1 204 VAL 204 261 261 VAL VAL B . n 
B 1 205 PRO 205 262 262 PRO PRO B . n 
B 1 206 ALA 206 263 263 ALA ALA B . n 
B 1 207 GLN 207 264 264 GLN GLN B . n 
B 1 208 VAL 208 265 265 VAL VAL B . n 
B 1 209 SER 209 266 266 SER SER B . n 
B 1 210 VAL 210 267 267 VAL VAL B . n 
B 1 211 VAL 211 268 268 VAL VAL B . n 
B 1 212 GLY 212 269 269 GLY GLY B . n 
B 1 213 TYR 213 270 270 TYR TYR B . n 
B 1 214 ASP 214 271 271 ASP ASP B . n 
B 1 215 ASP 215 272 272 ASP ASP B . n 
B 1 216 THR 216 273 273 THR THR B . n 
B 1 217 GLU 217 274 274 GLU GLU B . n 
B 1 218 ASP 218 275 275 ASP ASP B . n 
B 1 219 SER 219 276 276 SER SER B . n 
B 1 220 ALA 220 277 277 ALA ALA B . n 
B 1 221 CYS 221 278 278 CYS CYS B . n 
B 1 222 PHE 222 279 279 PHE PHE B . n 
B 1 223 ILE 223 280 280 ILE ILE B . n 
B 1 224 PRO 224 281 281 PRO PRO B . n 
B 1 225 PRO 225 282 282 PRO PRO B . n 
B 1 226 LEU 226 283 283 LEU LEU B . n 
B 1 227 THR 227 284 284 THR THR B . n 
B 1 228 THR 228 285 285 THR THR B . n 
B 1 229 ILE 229 286 286 ILE ILE B . n 
B 1 230 LYS 230 287 287 LYS LYS B . n 
B 1 231 GLN 231 288 288 GLN GLN B . n 
B 1 232 ASP 232 289 289 ASP ASP B . n 
B 1 233 PHE 233 290 290 PHE PHE B . n 
B 1 234 ARG 234 291 291 ARG ARG B . n 
B 1 235 LEU 235 292 292 LEU LEU B . n 
B 1 236 LEU 236 293 293 LEU LEU B . n 
B 1 237 GLY 237 294 294 GLY GLY B . n 
B 1 238 GLN 238 295 295 GLN GLN B . n 
B 1 239 THR 239 296 296 THR THR B . n 
B 1 240 SER 240 297 297 SER SER B . n 
B 1 241 VAL 241 298 298 VAL VAL B . n 
B 1 242 ASN 242 299 299 ASN ASN B . n 
B 1 243 ARG 243 300 300 ARG ARG B . n 
B 1 244 LEU 244 301 301 LEU LEU B . n 
B 1 245 VAL 245 302 302 VAL VAL B . n 
B 1 246 GLN 246 303 303 GLN GLN B . n 
B 1 247 LEU 247 304 304 LEU LEU B . n 
B 1 248 LEU 248 305 305 LEU LEU B . n 
B 1 249 GLN 249 306 306 GLN GLN B . n 
B 1 250 ASN 250 307 307 ASN ASN B . n 
B 1 251 PRO 251 308 308 PRO PRO B . n 
B 1 252 SER 252 309 309 SER SER B . n 
B 1 253 ALA 253 310 310 ALA ALA B . n 
B 1 254 GLN 254 311 311 GLN GLN B . n 
B 1 255 SER 255 312 312 SER SER B . n 
B 1 256 PRO 256 313 313 PRO PRO B . n 
B 1 257 GLN 257 314 314 GLN GLN B . n 
B 1 258 LEU 258 315 315 LEU LEU B . n 
B 1 259 LEU 259 316 316 LEU LEU B . n 
B 1 260 PRO 260 317 317 PRO PRO B . n 
B 1 261 VAL 261 318 318 VAL VAL B . n 
B 1 262 THR 262 319 319 THR THR B . n 
B 1 263 LEU 263 320 320 LEU LEU B . n 
B 1 264 VAL 264 321 321 VAL VAL B . n 
B 1 265 LYS 265 322 322 LYS LYS B . n 
B 1 266 ARG 266 323 323 ARG ARG B . n 
B 1 267 LYS 267 324 324 LYS LYS B . n 
B 1 268 THR 268 325 325 THR THR B . n 
B 1 269 THR 269 326 326 THR THR B . n 
B 1 270 ALA 270 327 327 ALA ALA B . n 
B 1 271 PRO 271 328 328 PRO PRO B . n 
B 1 272 PRO 272 329 329 PRO PRO B . n 
B 1 273 GLU 273 330 330 GLU GLU B . n 
B 1 274 ASN 274 331 331 ASN ASN B . n 
B 1 275 LEU 275 332 332 LEU LEU B . n 
B 1 276 TYR 276 333 333 TYR TYR B . n 
B 1 277 PHE 277 334 334 PHE PHE B . n 
B 1 278 GLN 278 335 335 GLN GLN B . n 
B 1 279 GLY 279 336 ?   ?   ?   B . n 
B 1 280 LEU 280 337 ?   ?   ?   B . n 
B 1 281 GLU 281 338 ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        MBG 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   MBG 
_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 
C 2 MBG 1   401 401 MBG MBG A . 
D 3 EDO 1   402 402 EDO EDO A . 
E 3 EDO 1   403 403 EDO EDO A . 
F 2 MBG 1   401 703 MBG MBG B . 
G 3 EDO 1   402 704 EDO EDO B . 
H 3 EDO 1   403 705 EDO EDO B . 
I 4 HOH 1   501 386 HOH HOH A . 
I 4 HOH 2   502 218 HOH HOH A . 
I 4 HOH 3   503 406 HOH HOH A . 
I 4 HOH 4   504 265 HOH HOH A . 
I 4 HOH 5   505 327 HOH HOH A . 
I 4 HOH 6   506 383 HOH HOH A . 
I 4 HOH 7   507 252 HOH HOH A . 
I 4 HOH 8   508 390 HOH HOH A . 
I 4 HOH 9   509 310 HOH HOH A . 
I 4 HOH 10  510 398 HOH HOH A . 
I 4 HOH 11  511 114 HOH HOH A . 
I 4 HOH 12  512 284 HOH HOH A . 
I 4 HOH 13  513 341 HOH HOH A . 
I 4 HOH 14  514 378 HOH HOH A . 
I 4 HOH 15  515 74  HOH HOH A . 
I 4 HOH 16  516 98  HOH HOH A . 
I 4 HOH 17  517 178 HOH HOH A . 
I 4 HOH 18  518 263 HOH HOH A . 
I 4 HOH 19  519 334 HOH HOH A . 
I 4 HOH 20  520 335 HOH HOH A . 
I 4 HOH 21  521 95  HOH HOH A . 
I 4 HOH 22  522 69  HOH HOH A . 
I 4 HOH 23  523 213 HOH HOH A . 
I 4 HOH 24  524 121 HOH HOH A . 
I 4 HOH 25  525 70  HOH HOH A . 
I 4 HOH 26  526 204 HOH HOH A . 
I 4 HOH 27  527 318 HOH HOH A . 
I 4 HOH 28  528 345 HOH HOH A . 
I 4 HOH 29  529 56  HOH HOH A . 
I 4 HOH 30  530 169 HOH HOH A . 
I 4 HOH 31  531 187 HOH HOH A . 
I 4 HOH 32  532 184 HOH HOH A . 
I 4 HOH 33  533 232 HOH HOH A . 
I 4 HOH 34  534 106 HOH HOH A . 
I 4 HOH 35  535 93  HOH HOH A . 
I 4 HOH 36  536 315 HOH HOH A . 
I 4 HOH 37  537 227 HOH HOH A . 
I 4 HOH 38  538 115 HOH HOH A . 
I 4 HOH 39  539 283 HOH HOH A . 
I 4 HOH 40  540 152 HOH HOH A . 
I 4 HOH 41  541 6   HOH HOH A . 
I 4 HOH 42  542 369 HOH HOH A . 
I 4 HOH 43  543 163 HOH HOH A . 
I 4 HOH 44  544 217 HOH HOH A . 
I 4 HOH 45  545 314 HOH HOH A . 
I 4 HOH 46  546 255 HOH HOH A . 
I 4 HOH 47  547 268 HOH HOH A . 
I 4 HOH 48  548 205 HOH HOH A . 
I 4 HOH 49  549 259 HOH HOH A . 
I 4 HOH 50  550 149 HOH HOH A . 
I 4 HOH 51  551 123 HOH HOH A . 
I 4 HOH 52  552 57  HOH HOH A . 
I 4 HOH 53  553 351 HOH HOH A . 
I 4 HOH 54  554 207 HOH HOH A . 
I 4 HOH 55  555 87  HOH HOH A . 
I 4 HOH 56  556 333 HOH HOH A . 
I 4 HOH 57  557 181 HOH HOH A . 
I 4 HOH 58  558 60  HOH HOH A . 
I 4 HOH 59  559 167 HOH HOH A . 
I 4 HOH 60  560 212 HOH HOH A . 
I 4 HOH 61  561 309 HOH HOH A . 
I 4 HOH 62  562 326 HOH HOH A . 
I 4 HOH 63  563 370 HOH HOH A . 
I 4 HOH 64  564 162 HOH HOH A . 
I 4 HOH 65  565 101 HOH HOH A . 
I 4 HOH 66  566 7   HOH HOH A . 
I 4 HOH 67  567 96  HOH HOH A . 
I 4 HOH 68  568 11  HOH HOH A . 
I 4 HOH 69  569 377 HOH HOH A . 
I 4 HOH 70  570 311 HOH HOH A . 
I 4 HOH 71  571 8   HOH HOH A . 
I 4 HOH 72  572 45  HOH HOH A . 
I 4 HOH 73  573 332 HOH HOH A . 
I 4 HOH 74  574 274 HOH HOH A . 
I 4 HOH 75  575 381 HOH HOH A . 
I 4 HOH 76  576 84  HOH HOH A . 
I 4 HOH 77  577 191 HOH HOH A . 
I 4 HOH 78  578 343 HOH HOH A . 
I 4 HOH 79  579 34  HOH HOH A . 
I 4 HOH 80  580 153 HOH HOH A . 
I 4 HOH 81  581 17  HOH HOH A . 
I 4 HOH 82  582 253 HOH HOH A . 
I 4 HOH 83  583 391 HOH HOH A . 
I 4 HOH 84  584 389 HOH HOH A . 
I 4 HOH 85  585 233 HOH HOH A . 
I 4 HOH 86  586 342 HOH HOH A . 
I 4 HOH 87  587 339 HOH HOH A . 
I 4 HOH 88  588 62  HOH HOH A . 
I 4 HOH 89  589 281 HOH HOH A . 
I 4 HOH 90  590 244 HOH HOH A . 
I 4 HOH 91  591 33  HOH HOH A . 
I 4 HOH 92  592 260 HOH HOH A . 
I 4 HOH 93  593 30  HOH HOH A . 
I 4 HOH 94  594 304 HOH HOH A . 
I 4 HOH 95  595 120 HOH HOH A . 
I 4 HOH 96  596 172 HOH HOH A . 
I 4 HOH 97  597 68  HOH HOH A . 
I 4 HOH 98  598 376 HOH HOH A . 
I 4 HOH 99  599 2   HOH HOH A . 
I 4 HOH 100 600 245 HOH HOH A . 
I 4 HOH 101 601 175 HOH HOH A . 
I 4 HOH 102 602 340 HOH HOH A . 
I 4 HOH 103 603 12  HOH HOH A . 
I 4 HOH 104 604 356 HOH HOH A . 
I 4 HOH 105 605 412 HOH HOH A . 
I 4 HOH 106 606 366 HOH HOH A . 
I 4 HOH 107 607 224 HOH HOH A . 
I 4 HOH 108 608 28  HOH HOH A . 
I 4 HOH 109 609 82  HOH HOH A . 
I 4 HOH 110 610 180 HOH HOH A . 
I 4 HOH 111 611 357 HOH HOH A . 
I 4 HOH 112 612 346 HOH HOH A . 
I 4 HOH 113 613 53  HOH HOH A . 
I 4 HOH 114 614 23  HOH HOH A . 
I 4 HOH 115 615 198 HOH HOH A . 
I 4 HOH 116 616 367 HOH HOH A . 
I 4 HOH 117 617 358 HOH HOH A . 
I 4 HOH 118 618 246 HOH HOH A . 
I 4 HOH 119 619 81  HOH HOH A . 
I 4 HOH 120 620 55  HOH HOH A . 
I 4 HOH 121 621 155 HOH HOH A . 
I 4 HOH 122 622 307 HOH HOH A . 
I 4 HOH 123 623 132 HOH HOH A . 
I 4 HOH 124 624 165 HOH HOH A . 
I 4 HOH 125 625 141 HOH HOH A . 
I 4 HOH 126 626 77  HOH HOH A . 
I 4 HOH 127 627 312 HOH HOH A . 
I 4 HOH 128 628 199 HOH HOH A . 
I 4 HOH 129 629 59  HOH HOH A . 
I 4 HOH 130 630 16  HOH HOH A . 
I 4 HOH 131 631 9   HOH HOH A . 
I 4 HOH 132 632 143 HOH HOH A . 
I 4 HOH 133 633 176 HOH HOH A . 
I 4 HOH 134 634 286 HOH HOH A . 
I 4 HOH 135 635 24  HOH HOH A . 
I 4 HOH 136 636 410 HOH HOH A . 
I 4 HOH 137 637 211 HOH HOH A . 
I 4 HOH 138 638 324 HOH HOH A . 
I 4 HOH 139 639 282 HOH HOH A . 
I 4 HOH 140 640 19  HOH HOH A . 
I 4 HOH 141 641 285 HOH HOH A . 
I 4 HOH 142 642 126 HOH HOH A . 
I 4 HOH 143 643 365 HOH HOH A . 
I 4 HOH 144 644 206 HOH HOH A . 
I 4 HOH 145 645 135 HOH HOH A . 
I 4 HOH 146 646 393 HOH HOH A . 
I 4 HOH 147 647 105 HOH HOH A . 
I 4 HOH 148 648 145 HOH HOH A . 
I 4 HOH 149 649 147 HOH HOH A . 
I 4 HOH 150 650 58  HOH HOH A . 
I 4 HOH 151 651 408 HOH HOH A . 
I 4 HOH 152 652 387 HOH HOH A . 
I 4 HOH 153 653 1   HOH HOH A . 
I 4 HOH 154 654 125 HOH HOH A . 
I 4 HOH 155 655 305 HOH HOH A . 
I 4 HOH 156 656 209 HOH HOH A . 
I 4 HOH 157 657 183 HOH HOH A . 
I 4 HOH 158 658 5   HOH HOH A . 
I 4 HOH 159 659 177 HOH HOH A . 
I 4 HOH 160 660 146 HOH HOH A . 
I 4 HOH 161 661 174 HOH HOH A . 
I 4 HOH 162 662 374 HOH HOH A . 
I 4 HOH 163 663 192 HOH HOH A . 
I 4 HOH 164 664 223 HOH HOH A . 
I 4 HOH 165 665 272 HOH HOH A . 
I 4 HOH 166 666 140 HOH HOH A . 
I 4 HOH 167 667 214 HOH HOH A . 
I 4 HOH 168 668 20  HOH HOH A . 
I 4 HOH 169 669 94  HOH HOH A . 
I 4 HOH 170 670 250 HOH HOH A . 
I 4 HOH 171 671 371 HOH HOH A . 
I 4 HOH 172 672 320 HOH HOH A . 
I 4 HOH 173 673 157 HOH HOH A . 
I 4 HOH 174 674 273 HOH HOH A . 
I 4 HOH 175 675 384 HOH HOH A . 
I 4 HOH 176 676 42  HOH HOH A . 
I 4 HOH 177 677 248 HOH HOH A . 
I 4 HOH 178 678 73  HOH HOH A . 
I 4 HOH 179 679 79  HOH HOH A . 
I 4 HOH 180 680 257 HOH HOH A . 
I 4 HOH 181 681 221 HOH HOH A . 
I 4 HOH 182 682 388 HOH HOH A . 
I 4 HOH 183 683 338 HOH HOH A . 
I 4 HOH 184 684 215 HOH HOH A . 
I 4 HOH 185 685 236 HOH HOH A . 
I 4 HOH 186 686 230 HOH HOH A . 
I 4 HOH 187 687 293 HOH HOH A . 
I 4 HOH 188 688 156 HOH HOH A . 
I 4 HOH 189 689 234 HOH HOH A . 
I 4 HOH 190 690 373 HOH HOH A . 
I 4 HOH 191 691 26  HOH HOH A . 
I 4 HOH 192 692 317 HOH HOH A . 
I 4 HOH 193 693 401 HOH HOH A . 
I 4 HOH 194 694 63  HOH HOH A . 
I 4 HOH 195 695 111 HOH HOH A . 
I 4 HOH 196 696 118 HOH HOH A . 
I 4 HOH 197 697 242 HOH HOH A . 
I 4 HOH 198 698 296 HOH HOH A . 
I 4 HOH 199 699 116 HOH HOH A . 
I 4 HOH 200 700 226 HOH HOH A . 
I 4 HOH 201 701 197 HOH HOH A . 
I 4 HOH 202 702 301 HOH HOH A . 
I 4 HOH 203 703 109 HOH HOH A . 
I 4 HOH 204 704 288 HOH HOH A . 
I 4 HOH 205 705 66  HOH HOH A . 
I 4 HOH 206 706 195 HOH HOH A . 
I 4 HOH 207 707 380 HOH HOH A . 
I 4 HOH 208 708 355 HOH HOH A . 
I 4 HOH 209 709 396 HOH HOH A . 
I 4 HOH 210 710 239 HOH HOH A . 
I 4 HOH 211 711 249 HOH HOH A . 
I 4 HOH 212 712 394 HOH HOH A . 
I 4 HOH 213 713 348 HOH HOH A . 
I 4 HOH 214 714 300 HOH HOH A . 
I 4 HOH 215 715 185 HOH HOH A . 
I 4 HOH 216 716 362 HOH HOH A . 
I 4 HOH 217 717 51  HOH HOH A . 
I 4 HOH 218 718 38  HOH HOH A . 
I 4 HOH 219 719 368 HOH HOH A . 
I 4 HOH 220 720 397 HOH HOH A . 
I 4 HOH 221 721 269 HOH HOH A . 
I 4 HOH 222 722 210 HOH HOH A . 
I 4 HOH 223 723 347 HOH HOH A . 
I 4 HOH 224 724 266 HOH HOH A . 
I 4 HOH 225 725 112 HOH HOH A . 
I 4 HOH 226 726 319 HOH HOH A . 
I 4 HOH 227 727 258 HOH HOH A . 
I 4 HOH 228 728 298 HOH HOH A . 
I 4 HOH 229 729 350 HOH HOH A . 
I 4 HOH 230 730 99  HOH HOH A . 
I 4 HOH 231 731 154 HOH HOH A . 
I 4 HOH 232 732 290 HOH HOH A . 
I 4 HOH 233 733 166 HOH HOH A . 
I 4 HOH 234 734 349 HOH HOH A . 
J 4 HOH 1   501 267 HOH HOH B . 
J 4 HOH 2   502 360 HOH HOH B . 
J 4 HOH 3   503 352 HOH HOH B . 
J 4 HOH 4   504 203 HOH HOH B . 
J 4 HOH 5   505 164 HOH HOH B . 
J 4 HOH 6   506 67  HOH HOH B . 
J 4 HOH 7   507 278 HOH HOH B . 
J 4 HOH 8   508 76  HOH HOH B . 
J 4 HOH 9   509 117 HOH HOH B . 
J 4 HOH 10  510 219 HOH HOH B . 
J 4 HOH 11  511 316 HOH HOH B . 
J 4 HOH 12  512 142 HOH HOH B . 
J 4 HOH 13  513 323 HOH HOH B . 
J 4 HOH 14  514 322 HOH HOH B . 
J 4 HOH 15  515 90  HOH HOH B . 
J 4 HOH 16  516 372 HOH HOH B . 
J 4 HOH 17  517 102 HOH HOH B . 
J 4 HOH 18  518 294 HOH HOH B . 
J 4 HOH 19  519 337 HOH HOH B . 
J 4 HOH 20  520 256 HOH HOH B . 
J 4 HOH 21  521 48  HOH HOH B . 
J 4 HOH 22  522 231 HOH HOH B . 
J 4 HOH 23  523 280 HOH HOH B . 
J 4 HOH 24  524 100 HOH HOH B . 
J 4 HOH 25  525 129 HOH HOH B . 
J 4 HOH 26  526 193 HOH HOH B . 
J 4 HOH 27  527 138 HOH HOH B . 
J 4 HOH 28  528 276 HOH HOH B . 
J 4 HOH 29  529 22  HOH HOH B . 
J 4 HOH 30  530 61  HOH HOH B . 
J 4 HOH 31  531 150 HOH HOH B . 
J 4 HOH 32  532 97  HOH HOH B . 
J 4 HOH 33  533 85  HOH HOH B . 
J 4 HOH 34  534 21  HOH HOH B . 
J 4 HOH 35  535 395 HOH HOH B . 
J 4 HOH 36  536 262 HOH HOH B . 
J 4 HOH 37  537 124 HOH HOH B . 
J 4 HOH 38  538 113 HOH HOH B . 
J 4 HOH 39  539 131 HOH HOH B . 
J 4 HOH 40  540 72  HOH HOH B . 
J 4 HOH 41  541 161 HOH HOH B . 
J 4 HOH 42  542 37  HOH HOH B . 
J 4 HOH 43  543 44  HOH HOH B . 
J 4 HOH 44  544 54  HOH HOH B . 
J 4 HOH 45  545 306 HOH HOH B . 
J 4 HOH 46  546 196 HOH HOH B . 
J 4 HOH 47  547 308 HOH HOH B . 
J 4 HOH 48  548 216 HOH HOH B . 
J 4 HOH 49  549 208 HOH HOH B . 
J 4 HOH 50  550 139 HOH HOH B . 
J 4 HOH 51  551 271 HOH HOH B . 
J 4 HOH 52  552 65  HOH HOH B . 
J 4 HOH 53  553 15  HOH HOH B . 
J 4 HOH 54  554 4   HOH HOH B . 
J 4 HOH 55  555 49  HOH HOH B . 
J 4 HOH 56  556 188 HOH HOH B . 
J 4 HOH 57  557 171 HOH HOH B . 
J 4 HOH 58  558 41  HOH HOH B . 
J 4 HOH 59  559 240 HOH HOH B . 
J 4 HOH 60  560 130 HOH HOH B . 
J 4 HOH 61  561 18  HOH HOH B . 
J 4 HOH 62  562 89  HOH HOH B . 
J 4 HOH 63  563 222 HOH HOH B . 
J 4 HOH 64  564 303 HOH HOH B . 
J 4 HOH 65  565 243 HOH HOH B . 
J 4 HOH 66  566 127 HOH HOH B . 
J 4 HOH 67  567 122 HOH HOH B . 
J 4 HOH 68  568 31  HOH HOH B . 
J 4 HOH 69  569 194 HOH HOH B . 
J 4 HOH 70  570 3   HOH HOH B . 
J 4 HOH 71  571 133 HOH HOH B . 
J 4 HOH 72  572 32  HOH HOH B . 
J 4 HOH 73  573 186 HOH HOH B . 
J 4 HOH 74  574 411 HOH HOH B . 
J 4 HOH 75  575 64  HOH HOH B . 
J 4 HOH 76  576 25  HOH HOH B . 
J 4 HOH 77  577 247 HOH HOH B . 
J 4 HOH 78  578 238 HOH HOH B . 
J 4 HOH 79  579 361 HOH HOH B . 
J 4 HOH 80  580 363 HOH HOH B . 
J 4 HOH 81  581 75  HOH HOH B . 
J 4 HOH 82  582 235 HOH HOH B . 
J 4 HOH 83  583 287 HOH HOH B . 
J 4 HOH 84  584 50  HOH HOH B . 
J 4 HOH 85  585 43  HOH HOH B . 
J 4 HOH 86  586 329 HOH HOH B . 
J 4 HOH 87  587 14  HOH HOH B . 
J 4 HOH 88  588 354 HOH HOH B . 
J 4 HOH 89  589 375 HOH HOH B . 
J 4 HOH 90  590 289 HOH HOH B . 
J 4 HOH 91  591 83  HOH HOH B . 
J 4 HOH 92  592 104 HOH HOH B . 
J 4 HOH 93  593 404 HOH HOH B . 
J 4 HOH 94  594 40  HOH HOH B . 
J 4 HOH 95  595 86  HOH HOH B . 
J 4 HOH 96  596 344 HOH HOH B . 
J 4 HOH 97  597 168 HOH HOH B . 
J 4 HOH 98  598 47  HOH HOH B . 
J 4 HOH 99  599 27  HOH HOH B . 
J 4 HOH 100 600 225 HOH HOH B . 
J 4 HOH 101 601 35  HOH HOH B . 
J 4 HOH 102 602 128 HOH HOH B . 
J 4 HOH 103 603 279 HOH HOH B . 
J 4 HOH 104 604 330 HOH HOH B . 
J 4 HOH 105 605 80  HOH HOH B . 
J 4 HOH 106 606 179 HOH HOH B . 
J 4 HOH 107 607 13  HOH HOH B . 
J 4 HOH 108 608 173 HOH HOH B . 
J 4 HOH 109 609 136 HOH HOH B . 
J 4 HOH 110 610 336 HOH HOH B . 
J 4 HOH 111 611 137 HOH HOH B . 
J 4 HOH 112 612 10  HOH HOH B . 
J 4 HOH 113 613 189 HOH HOH B . 
J 4 HOH 114 614 110 HOH HOH B . 
J 4 HOH 115 615 91  HOH HOH B . 
J 4 HOH 116 616 160 HOH HOH B . 
J 4 HOH 117 617 182 HOH HOH B . 
J 4 HOH 118 618 254 HOH HOH B . 
J 4 HOH 119 619 88  HOH HOH B . 
J 4 HOH 120 620 119 HOH HOH B . 
J 4 HOH 121 621 264 HOH HOH B . 
J 4 HOH 122 622 39  HOH HOH B . 
J 4 HOH 123 623 36  HOH HOH B . 
J 4 HOH 124 624 144 HOH HOH B . 
J 4 HOH 125 625 328 HOH HOH B . 
J 4 HOH 126 626 364 HOH HOH B . 
J 4 HOH 127 627 353 HOH HOH B . 
J 4 HOH 128 628 261 HOH HOH B . 
J 4 HOH 129 629 400 HOH HOH B . 
J 4 HOH 130 630 277 HOH HOH B . 
J 4 HOH 131 631 201 HOH HOH B . 
J 4 HOH 132 632 134 HOH HOH B . 
J 4 HOH 133 633 29  HOH HOH B . 
J 4 HOH 134 634 103 HOH HOH B . 
J 4 HOH 135 635 190 HOH HOH B . 
J 4 HOH 136 636 409 HOH HOH B . 
J 4 HOH 137 637 46  HOH HOH B . 
J 4 HOH 138 638 202 HOH HOH B . 
J 4 HOH 139 639 229 HOH HOH B . 
J 4 HOH 140 640 71  HOH HOH B . 
J 4 HOH 141 641 228 HOH HOH B . 
J 4 HOH 142 642 313 HOH HOH B . 
J 4 HOH 143 643 379 HOH HOH B . 
J 4 HOH 144 644 92  HOH HOH B . 
J 4 HOH 145 645 220 HOH HOH B . 
J 4 HOH 146 646 399 HOH HOH B . 
J 4 HOH 147 647 270 HOH HOH B . 
J 4 HOH 148 648 385 HOH HOH B . 
J 4 HOH 149 649 151 HOH HOH B . 
J 4 HOH 150 650 407 HOH HOH B . 
J 4 HOH 151 651 402 HOH HOH B . 
J 4 HOH 152 652 108 HOH HOH B . 
J 4 HOH 153 653 403 HOH HOH B . 
J 4 HOH 154 654 78  HOH HOH B . 
J 4 HOH 155 655 170 HOH HOH B . 
J 4 HOH 156 656 159 HOH HOH B . 
J 4 HOH 157 657 52  HOH HOH B . 
J 4 HOH 158 658 237 HOH HOH B . 
J 4 HOH 159 659 241 HOH HOH B . 
J 4 HOH 160 660 297 HOH HOH B . 
J 4 HOH 161 661 325 HOH HOH B . 
J 4 HOH 162 662 295 HOH HOH B . 
J 4 HOH 163 663 292 HOH HOH B . 
J 4 HOH 164 664 331 HOH HOH B . 
J 4 HOH 165 665 158 HOH HOH B . 
J 4 HOH 166 666 359 HOH HOH B . 
J 4 HOH 167 667 251 HOH HOH B . 
J 4 HOH 168 668 302 HOH HOH B . 
J 4 HOH 169 669 200 HOH HOH B . 
J 4 HOH 170 670 299 HOH HOH B . 
J 4 HOH 171 671 275 HOH HOH B . 
J 4 HOH 172 672 148 HOH HOH B . 
J 4 HOH 173 673 382 HOH HOH B . 
J 4 HOH 174 674 107 HOH HOH B . 
J 4 HOH 175 675 291 HOH HOH B . 
# 
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 B LYS 59 ? CG ? B LYS 2 CG 
2 1 Y 1 B LYS 59 ? CD ? B LYS 2 CD 
3 1 Y 1 B LYS 59 ? CE ? B LYS 2 CE 
4 1 Y 1 B LYS 59 ? NZ ? B LYS 2 NZ 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? '(1.20.1_4487: ???)' 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .                    2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9NT6 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     36.467 
_cell.length_a_esd                 ? 
_cell.length_b                     108.336 
_cell.length_b_esd                 ? 
_cell.length_c                     119.601 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_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                         9NT6 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_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                   9NT6 
_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             1.96 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          37.18 
_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, HANGING 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    '21 % PEG 3350, 0.1M HEPES pH 7.1' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291 
# 
_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 EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2020-10-01 
_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   0.9537 
_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                        'AUSTRALIAN SYNCHROTRON BEAMLINE MX2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9537 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   MX2 
_diffrn_source.pdbx_synchrotron_site       'Australian Synchrotron' 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9NT6 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.50 
_reflns.d_resolution_low                               49.34 
_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                                     76948 
_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                           99.9 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                12.8 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          10.8 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.82 
_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                                0.146 
_reflns.pdbx_Rpim_I_all                                0.041 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       986424 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.998 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.140 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.50 
_reflns_shell.d_res_low                                     1.53 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           40988 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             3714 
_reflns_shell.percent_possible_obs                          98.3 
_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                               11.0 
_reflns_shell.pdbx_chi_squared                              0.57 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     1.4 
_reflns_shell.pdbx_Rrim_I_all                               1.853 
_reflns_shell.pdbx_Rpim_I_all                               0.552 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.653 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  1.767 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9NT6 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.50 
_refine.ls_d_res_low                             49.34 
_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                     76788 
_refine.ls_number_reflns_R_free                  3845 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.78 
_refine.ls_percent_reflns_R_free                 5.01 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1772 
_refine.ls_R_factor_R_free                       0.2078 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1756 
_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.correlation_coeff_I_to_Fcsqd_work        ? 
_refine.correlation_coeff_I_to_Fcsqd_free        ? 
_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                          1.34 
_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               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 18.92 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.17 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        4114 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         42 
_refine_hist.number_atoms_solvent             409 
_refine_hist.number_atoms_total               4565 
_refine_hist.d_res_high                       1.50 
_refine_hist.d_res_low                        49.34 
# 
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' ? 0.007 ? ?   ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.988 ? ?   ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 6.352 ? 619 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.059 ? 738 ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.010 ? 799 ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.correlation_coeff_Fo_to_Fc 
_refine_ls_shell.correlation_coeff_Fo_to_Fc_free 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_work 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_free 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.50 1.52  . . 131 2633 98.00  . . . . 0.2415 . . . . . . . . . . . . . . . 0.2804 
'X-RAY DIFFRACTION' 1.52 1.54  . . 137 2629 100.00 . . . . 0.2324 . . . . . . . . . . . . . . . 0.2582 
'X-RAY DIFFRACTION' 1.54 1.56  . . 158 2639 100.00 . . . . 0.2295 . . . . . . . . . . . . . . . 0.2311 
'X-RAY DIFFRACTION' 1.56 1.58  . . 156 2688 100.00 . . . . 0.2204 . . . . . . . . . . . . . . . 0.2784 
'X-RAY DIFFRACTION' 1.58 1.61  . . 143 2629 100.00 . . . . 0.2183 . . . . . . . . . . . . . . . 0.2171 
'X-RAY DIFFRACTION' 1.61 1.63  . . 141 2662 100.00 . . . . 0.2096 . . . . . . . . . . . . . . . 0.2557 
'X-RAY DIFFRACTION' 1.63 1.66  . . 142 2691 99.00  . . . . 0.2039 . . . . . . . . . . . . . . . 0.2391 
'X-RAY DIFFRACTION' 1.66 1.69  . . 124 2665 100.00 . . . . 0.2349 . . . . . . . . . . . . . . . 0.2969 
'X-RAY DIFFRACTION' 1.69 1.72  . . 148 2662 100.00 . . . . 0.2313 . . . . . . . . . . . . . . . 0.2584 
'X-RAY DIFFRACTION' 1.72 1.75  . . 138 2673 100.00 . . . . 0.2215 . . . . . . . . . . . . . . . 0.2685 
'X-RAY DIFFRACTION' 1.75 1.79  . . 147 2671 100.00 . . . . 0.2112 . . . . . . . . . . . . . . . 0.2252 
'X-RAY DIFFRACTION' 1.79 1.82  . . 147 2686 100.00 . . . . 0.1950 . . . . . . . . . . . . . . . 0.2585 
'X-RAY DIFFRACTION' 1.82 1.87  . . 146 2666 100.00 . . . . 0.1889 . . . . . . . . . . . . . . . 0.2328 
'X-RAY DIFFRACTION' 1.87 1.91  . . 130 2690 100.00 . . . . 0.1815 . . . . . . . . . . . . . . . 0.2194 
'X-RAY DIFFRACTION' 1.91 1.97  . . 130 2687 100.00 . . . . 0.1786 . . . . . . . . . . . . . . . 0.2097 
'X-RAY DIFFRACTION' 1.97 2.02  . . 153 2713 100.00 . . . . 0.1799 . . . . . . . . . . . . . . . 0.2204 
'X-RAY DIFFRACTION' 2.02 2.09  . . 147 2657 100.00 . . . . 0.1902 . . . . . . . . . . . . . . . 0.2337 
'X-RAY DIFFRACTION' 2.09 2.16  . . 134 2728 100.00 . . . . 0.1844 . . . . . . . . . . . . . . . 0.2112 
'X-RAY DIFFRACTION' 2.16 2.25  . . 171 2657 100.00 . . . . 0.1715 . . . . . . . . . . . . . . . 0.2001 
'X-RAY DIFFRACTION' 2.25 2.35  . . 128 2715 100.00 . . . . 0.1690 . . . . . . . . . . . . . . . 0.2089 
'X-RAY DIFFRACTION' 2.35 2.48  . . 153 2724 100.00 . . . . 0.1734 . . . . . . . . . . . . . . . 0.2047 
'X-RAY DIFFRACTION' 2.48 2.63  . . 145 2722 100.00 . . . . 0.1759 . . . . . . . . . . . . . . . 0.2145 
'X-RAY DIFFRACTION' 2.63 2.83  . . 126 2752 100.00 . . . . 0.1780 . . . . . . . . . . . . . . . 0.1901 
'X-RAY DIFFRACTION' 2.83 3.12  . . 139 2762 100.00 . . . . 0.1733 . . . . . . . . . . . . . . . 0.2312 
'X-RAY DIFFRACTION' 3.12 3.57  . . 134 2776 100.00 . . . . 0.1601 . . . . . . . . . . . . . . . 0.1957 
'X-RAY DIFFRACTION' 3.57 4.50  . . 143 2816 100.00 . . . . 0.1374 . . . . . . . . . . . . . . . 0.1738 
'X-RAY DIFFRACTION' 4.50 49.34 . . 154 2950 100.00 . . . . 0.1528 . . . . . . . . . . . . . . . 0.1486 
# 
_struct.entry_id                     9NT6 
_struct.title                        
'Crystal structure of ecLacI transcription factor ancestor 4 bound to Beta-methyl-D-galactoside' 
_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        9NT6 
_struct_keywords.text            
'Ancestral sequence reconstruction, transcription factor, LacI, BMDG, Beta-methyl-D-galactoside, TRANSCRIPTION' 
_struct_keywords.pdbx_keywords   TRANSCRIPTION 
# 
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 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 3 ? 
F N N 2 ? 
G N N 3 ? 
H N N 3 ? 
I N N 4 ? 
J N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    PDB 
_struct_ref.db_code                    9NT6 
_struct_ref.pdbx_db_accession          9NT6 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   ? 
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9NT6 A 1 ? 281 ? 9NT6 58 ? 338 ? 58 338 
2 1 9NT6 B 1 ? 281 ? 9NT6 58 ? 338 ? 58 338 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 4390  ? 
1 MORE         -9    ? 
1 'SSA (A^2)'  21520 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 LEU A 16  ? GLY A 34  ? LEU A 73  GLY A 91  1 ? 19 
HELX_P HELX_P2  AA2 GLY A 45  ? GLN A 59  ? GLY A 102 GLN A 116 1 ? 15 
HELX_P HELX_P3  AA3 ASN A 72  ? GLY A 83  ? ASN A 129 GLY A 140 1 ? 12 
HELX_P HELX_P4  AA4 HIS A 105 ? LEU A 118 ? HIS A 162 LEU A 175 1 ? 14 
HELX_P HELX_P5  AA5 SER A 132 ? HIS A 149 ? SER A 189 HIS A 206 1 ? 18 
HELX_P HELX_P6  AA6 SER A 162 ? GLY A 177 ? SER A 219 GLY A 234 1 ? 16 
HELX_P HELX_P7  AA7 ASN A 186 ? SER A 200 ? ASN A 243 SER A 257 1 ? 15 
HELX_P HELX_P8  AA8 THR A 216 ? PHE A 222 ? THR A 273 PHE A 279 5 ? 7  
HELX_P HELX_P9  AA9 ASP A 232 ? ASN A 250 ? ASP A 289 ASN A 307 1 ? 19 
HELX_P HELX_P10 AB1 LEU B 16  ? MET B 33  ? LEU B 73  MET B 90  1 ? 18 
HELX_P HELX_P11 AB2 GLY B 45  ? GLN B 59  ? GLY B 102 GLN B 116 1 ? 15 
HELX_P HELX_P12 AB3 GLU B 71  ? CYS B 82  ? GLU B 128 CYS B 139 1 ? 12 
HELX_P HELX_P13 AB4 ASP B 103 ? GLY B 119 ? ASP B 160 GLY B 176 1 ? 17 
HELX_P HELX_P14 AB5 SER B 132 ? HIS B 149 ? SER B 189 HIS B 206 1 ? 18 
HELX_P HELX_P15 AB6 SER B 162 ? GLY B 177 ? SER B 219 GLY B 234 1 ? 16 
HELX_P HELX_P16 AB7 ASN B 186 ? SER B 200 ? ASN B 243 SER B 257 1 ? 15 
HELX_P HELX_P17 AB8 THR B 216 ? PHE B 222 ? THR B 273 PHE B 279 5 ? 7  
HELX_P HELX_P18 AB9 ASP B 232 ? ASN B 250 ? ASP B 289 ASN B 307 1 ? 19 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 SER 93  A . ? SER 150 A PRO 94  A ? PRO 151 A 1 -6.01  
2 VAL 204 A . ? VAL 261 A PRO 205 A ? PRO 262 A 1 4.48   
3 ILE 223 A . ? ILE 280 A PRO 224 A ? PRO 281 A 1 -10.45 
4 VAL 204 B . ? VAL 261 B PRO 205 B ? PRO 262 B 1 4.75   
5 ILE 223 B . ? ILE 280 B PRO 224 B ? PRO 281 B 1 -7.50  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 2 ? 
AA3 ? 2 ? 
AA4 ? 6 ? 
AA5 ? 4 ? 
AA6 ? 2 ? 
AA7 ? 6 ? 
# 
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      
AA2 1 2 ? parallel      
AA3 1 2 ? parallel      
AA4 1 2 ? parallel      
AA4 2 3 ? parallel      
AA4 3 4 ? parallel      
AA4 4 5 ? parallel      
AA4 5 6 ? anti-parallel 
AA5 1 2 ? parallel      
AA5 2 3 ? parallel      
AA5 3 4 ? parallel      
AA6 1 2 ? parallel      
AA7 1 2 ? parallel      
AA7 2 3 ? parallel      
AA7 3 4 ? parallel      
AA7 4 5 ? parallel      
AA7 5 6 ? 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 ASN A 36  ? MET A 41  ? ASN A 93  MET A 98  
AA1 2 THR A 6   ? THR A 11  ? THR A 63  THR A 68  
AA1 3 GLY A 63  ? ASN A 67  ? GLY A 120 ASN A 124 
AA1 4 VAL A 87  ? PHE A 89  ? VAL A 144 PHE A 146 
AA2 1 LEU A 70  ? GLU A 71  ? LEU A 127 GLU A 128 
AA2 2 VAL A 92  ? SER A 93  ? VAL A 149 SER A 150 
AA3 1 VAL A 100 ? PHE A 102 ? VAL A 157 PHE A 159 
AA3 2 GLN A 257 ? LEU A 259 ? GLN A 314 LEU A 316 
AA4 1 ALA A 155 ? HIS A 158 ? ALA A 212 HIS A 215 
AA4 2 ILE A 123 ? THR A 127 ? ILE A 180 THR A 184 
AA4 3 ALA A 181 ? VAL A 184 ? ALA A 238 VAL A 241 
AA4 4 SER A 209 ? ASP A 214 ? SER A 266 ASP A 271 
AA4 5 THR A 228 ? LYS A 230 ? THR A 285 LYS A 287 
AA4 6 THR A 262 ? VAL A 264 ? THR A 319 VAL A 321 
AA5 1 ASN B 36  ? MET B 41  ? ASN B 93  MET B 98  
AA5 2 THR B 6   ? THR B 11  ? THR B 63  THR B 68  
AA5 3 GLY B 63  ? ASN B 67  ? GLY B 120 ASN B 124 
AA5 4 VAL B 87  ? PHE B 89  ? VAL B 144 PHE B 146 
AA6 1 SER B 99  ? PHE B 102 ? SER B 156 PHE B 159 
AA6 2 PRO B 256 ? LEU B 259 ? PRO B 313 LEU B 316 
AA7 1 ALA B 155 ? HIS B 158 ? ALA B 212 HIS B 215 
AA7 2 ILE B 123 ? THR B 127 ? ILE B 180 THR B 184 
AA7 3 ALA B 181 ? VAL B 184 ? ALA B 238 VAL B 241 
AA7 4 SER B 209 ? ASP B 214 ? SER B 266 ASP B 271 
AA7 5 THR B 228 ? LYS B 230 ? THR B 285 LYS B 287 
AA7 6 THR B 262 ? VAL B 264 ? THR B 319 VAL B 321 
# 
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 ASN A 36  ? O ASN A 93  N ILE A 7   ? N ILE A 64  
AA1 2 3 N ALA A 10  ? N ALA A 67  O ASN A 67  ? O ASN A 124 
AA1 3 4 N ILE A 66  ? N ILE A 123 O LEU A 88  ? O LEU A 145 
AA2 1 2 N LEU A 70  ? N LEU A 127 O SER A 93  ? O SER A 150 
AA3 1 2 N LEU A 101 ? N LEU A 158 O LEU A 259 ? O LEU A 316 
AA4 1 2 O LEU A 157 ? O LEU A 214 N THR A 127 ? N THR A 184 
AA4 2 3 N ALA A 124 ? N ALA A 181 O ALA A 181 ? O ALA A 238 
AA4 3 4 N VAL A 184 ? N VAL A 241 O VAL A 211 ? O VAL A 268 
AA4 4 5 N ASP A 214 ? N ASP A 271 O ILE A 229 ? O ILE A 286 
AA4 5 6 N THR A 228 ? N THR A 285 O VAL A 264 ? O VAL A 321 
AA5 1 2 O SER B 40  ? O SER B 97  N LEU B 9   ? N LEU B 66  
AA5 2 3 N ALA B 10  ? N ALA B 67  O ASN B 67  ? O ASN B 124 
AA5 3 4 N ILE B 66  ? N ILE B 123 O LEU B 88  ? O LEU B 145 
AA6 1 2 N LEU B 101 ? N LEU B 158 O GLN B 257 ? O GLN B 314 
AA7 1 2 O LEU B 157 ? O LEU B 214 N THR B 127 ? N THR B 184 
AA7 2 3 N LEU B 126 ? N LEU B 183 O LEU B 183 ? O LEU B 240 
AA7 3 4 N VAL B 184 ? N VAL B 241 O VAL B 211 ? O VAL B 268 
AA7 4 5 N ASP B 214 ? N ASP B 271 O ILE B 229 ? O ILE B 286 
AA7 5 6 N THR B 228 ? N THR B 285 O VAL B 264 ? O VAL B 321 
# 
_pdbx_entry_details.entry_id                   9NT6 
_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 ASN A 70  ? ? -32.76  112.70  
2  1 ASN A 124 ? ? -105.59 75.40   
3  1 ASP A 148 ? ? -156.84 68.35   
4  1 ASN A 155 ? ? 85.14   -30.63  
5  1 TRP A 218 ? ? 85.62   -10.01  
6  1 ASP A 271 ? ? 130.85  -44.94  
7  1 PRO A 308 ? ? -64.29  7.04    
8  1 ARG A 323 ? ? -120.83 -114.74 
9  1 ASN B 70  ? ? -38.18  110.36  
10 1 ASN B 124 ? ? -107.79 73.29   
11 1 ASP B 148 ? ? -151.55 77.51   
12 1 TRP B 218 ? ? 85.12   -9.08   
13 1 ASP B 271 ? ? 136.22  -43.54  
14 1 ARG B 323 ? ? -119.51 -112.49 
# 
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 26.7114 -8.9020  -31.4298 0.1124 ? -0.0087 ? -0.0142 ? 0.0601 ? 0.0175  ? 0.1229 ? 3.3257 ? 
-0.6897 ? -2.5292 ? 2.0750 ? 1.2424  ? 7.5557 ? 0.0121  ? -0.0160 ? 0.0697  ? -0.0623 ? -0.0453 ? -0.1568 ? 0.0100  ? 0.2686  ? 
0.0223  ? 
2  'X-RAY DIFFRACTION' ? refined 17.1250 -15.3706 -36.1905 0.2028 ? -0.0178 ? -0.0411 ? 0.1825 ? -0.0457 ? 0.1828 ? 1.2306 ? 
-0.2670 ? -0.6571 ? 2.1232 ? -1.7829 ? 3.1938 ? 0.0528  ? 0.1554  ? -0.0441 ? -0.1894 ? 0.0375  ? 0.2214  ? 0.3300  ? -0.2534 ? 
-0.0902 ? 
3  'X-RAY DIFFRACTION' ? refined 14.4509 -20.5907 -7.2238  0.0735 ? -0.0348 ? 0.0118  ? 0.0446 ? 0.0018  ? 0.1225 ? 2.4579 ? 
-0.6138 ? 1.1016  ? 3.1862 ? -1.4947 ? 5.4496 ? -0.0695 ? -0.0366 ? -0.2113 ? -0.0158 ? 0.0636  ? 0.0136  ? 0.1843  ? -0.0639 ? 
0.0113  ? 
4  'X-RAY DIFFRACTION' ? refined 10.4729 -23.5896 -13.5251 0.1332 ? -0.0389 ? 0.0027  ? 0.1496 ? -0.0271 ? 0.1792 ? 2.0450 ? 
0.2190  ? -0.5439 ? 5.7747 ? -4.8944 ? 8.7663 ? -0.0249 ? 0.2214  ? -0.1757 ? -0.4965 ? 0.2025  ? 0.3048  ? 0.4599  ? -0.4440 ? 
-0.1885 ? 
5  'X-RAY DIFFRACTION' ? refined 12.4258 -9.4843  -5.8748  0.0807 ? 0.0129  ? 0.0070  ? 0.0970 ? 0.0039  ? 0.1073 ? 1.0491 ? 
-0.1340 ? 0.2821  ? 1.0485 ? -0.1800 ? 1.0512 ? -0.0404 ? -0.0778 ? 0.0081  ? 0.0635  ? 0.0671  ? 0.1203  ? -0.0198 ? -0.1071 ? 
-0.0268 ? 
6  'X-RAY DIFFRACTION' ? refined 28.0524 -15.6642 -23.9747 0.0865 ? 0.0175  ? -0.0072 ? 0.1302 ? 0.0030  ? 0.1031 ? 0.4750 ? 
-0.8802 ? -1.9073 ? 2.6374 ? 3.4585  ? 7.8903 ? -0.0190 ? 0.0279  ? -0.0118 ? -0.2005 ? -0.0071 ? -0.0235 ? -0.0070 ? 0.1762  ? 
-0.0141 ? 
7  'X-RAY DIFFRACTION' ? refined 24.0980 -20.7724 -14.5220 0.1490 ? -0.0061 ? 0.0041  ? 0.1287 ? -0.0082 ? 0.1344 ? 1.0487 ? 
-0.3033 ? -0.5376 ? 1.5759 ? 1.7025  ? 6.6135 ? -0.0112 ? 0.1942  ? -0.1346 ? -0.0034 ? -0.0229 ? 0.0078  ? 0.5535  ? -0.2308 ? 
0.0858  ? 
8  'X-RAY DIFFRACTION' ? refined 20.0079 3.0671   -34.1945 0.1655 ? 0.0466  ? -0.0109 ? 0.1145 ? -0.0096 ? 0.1547 ? 2.7096 ? 
0.3781  ? -0.3131 ? 3.2924 ? 0.7992  ? 6.5938 ? 0.2169  ? 0.2577  ? -0.0532 ? -0.2735 ? -0.0784 ? 0.0117  ? -0.3282 ? -0.2693 ? 
-0.1002 ? 
9  'X-RAY DIFFRACTION' ? refined 29.7560 8.9452   -41.2524 0.5204 ? -0.0534 ? 0.2649  ? 0.3392 ? -0.0945 ? 0.6941 ? 2.4042 ? 
2.2478  ? -0.4853 ? 3.5868 ? -0.5635 ? 3.6756 ? 0.2498  ? 0.4081  ? -0.2153 ? -0.5350 ? 0.3307  ? -1.4649 ? -0.8788 ? 0.6230  ? 
-0.3113 ? 
10 'X-RAY DIFFRACTION' ? refined 25.2823 20.5994  -21.0460 0.2907 ? -0.0428 ? 0.0290  ? 0.1667 ? 0.0155  ? 0.2567 ? 0.4825 ? 
0.6332  ? 1.7085  ? 2.0769 ? 1.5881  ? 6.1003 ? -0.1011 ? 0.1628  ? 0.0133  ? -0.5781 ? 0.1894  ? -0.2764 ? -0.4879 ? 0.3484  ? 
-0.1059 ? 
11 'X-RAY DIFFRACTION' ? refined 31.2438 12.3001  -8.6026  0.1112 ? 0.0011  ? -0.0073 ? 0.1190 ? -0.0116 ? 0.1357 ? 1.0077 ? 
0.1996  ? 0.1684  ? 1.8464 ? 0.3931  ? 0.8652 ? -0.0539 ? 0.0104  ? 0.0186  ? -0.0348 ? 0.0865  ? -0.1436 ? -0.0559 ? 0.1088  ? 
-0.0236 ? 
12 'X-RAY DIFFRACTION' ? refined 18.1135 15.3510  -19.9510 0.1780 ? 0.0351  ? -0.0211 ? 0.1374 ? 0.0100  ? 0.1566 ? 1.3305 ? 
-0.6728 ? 0.5528  ? 1.5633 ? 0.3217  ? 4.6121 ? 0.0964  ? 0.2511  ? 0.0653  ? -0.3608 ? -0.1414 ? 0.0642  ? -0.4032 ? 0.0093  ? 
0.0593  ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1  'X-RAY DIFFRACTION' 1  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 61 through 90 )
;
2  'X-RAY DIFFRACTION' 2  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 91 through 162 )
;
3  'X-RAY DIFFRACTION' 3  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 163 through 189 )
;
4  'X-RAY DIFFRACTION' 4  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 190 through 206 )
;
5  'X-RAY DIFFRACTION' 5  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 207 through 278 )
;
6  'X-RAY DIFFRACTION' 6  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 279 through 306 )
;
7  'X-RAY DIFFRACTION' 7  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 307 through 331 )
;
8  'X-RAY DIFFRACTION' 8  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 59 through 102 )
;
9  'X-RAY DIFFRACTION' 9  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 103 through 146 )
;
10 'X-RAY DIFFRACTION' 10 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 147 through 175 )
;
11 'X-RAY DIFFRACTION' 11 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 176 through 278 )
;
12 'X-RAY DIFFRACTION' 12 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 279 through 335 )
;
# 
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 58  ? A MET 1   
2  1 Y 1 A LYS 59  ? A LYS 2   
3  1 Y 1 A GLN 60  ? A GLN 3   
4  1 Y 1 A LEU 332 ? A LEU 275 
5  1 Y 1 A TYR 333 ? A TYR 276 
6  1 Y 1 A PHE 334 ? A PHE 277 
7  1 Y 1 A GLN 335 ? A GLN 278 
8  1 Y 1 A GLY 336 ? A GLY 279 
9  1 Y 1 A LEU 337 ? A LEU 280 
10 1 Y 1 A GLU 338 ? A GLU 281 
11 1 Y 1 B MET 58  ? B MET 1   
12 1 Y 1 B GLY 336 ? B GLY 279 
13 1 Y 1 B LEU 337 ? B LEU 280 
14 1 Y 1 B GLU 338 ? B GLU 281 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
EDO C1   C N N 88  
EDO O1   O N N 89  
EDO C2   C N N 90  
EDO O2   O N N 91  
EDO H11  H N N 92  
EDO H12  H N N 93  
EDO HO1  H N N 94  
EDO H21  H N N 95  
EDO H22  H N N 96  
EDO HO2  H N N 97  
GLN N    N N N 98  
GLN CA   C N S 99  
GLN C    C N N 100 
GLN O    O N N 101 
GLN CB   C N N 102 
GLN CG   C N N 103 
GLN CD   C N N 104 
GLN OE1  O N N 105 
GLN NE2  N N N 106 
GLN OXT  O N N 107 
GLN H    H N N 108 
GLN H2   H N N 109 
GLN HA   H N N 110 
GLN HB2  H N N 111 
GLN HB3  H N N 112 
GLN HG2  H N N 113 
GLN HG3  H N N 114 
GLN HE21 H N N 115 
GLN HE22 H N N 116 
GLN HXT  H N N 117 
GLU N    N N N 118 
GLU CA   C N S 119 
GLU C    C N N 120 
GLU O    O N N 121 
GLU CB   C N N 122 
GLU CG   C N N 123 
GLU CD   C N N 124 
GLU OE1  O N N 125 
GLU OE2  O N N 126 
GLU OXT  O N N 127 
GLU H    H N N 128 
GLU H2   H N N 129 
GLU HA   H N N 130 
GLU HB2  H N N 131 
GLU HB3  H N N 132 
GLU HG2  H N N 133 
GLU HG3  H N N 134 
GLU HE2  H N N 135 
GLU HXT  H N N 136 
GLY N    N N N 137 
GLY CA   C N N 138 
GLY C    C N N 139 
GLY O    O N N 140 
GLY OXT  O N N 141 
GLY H    H N N 142 
GLY H2   H N N 143 
GLY HA2  H N N 144 
GLY HA3  H N N 145 
GLY HXT  H N N 146 
HIS N    N N N 147 
HIS CA   C N S 148 
HIS C    C N N 149 
HIS O    O N N 150 
HIS CB   C N N 151 
HIS CG   C Y N 152 
HIS ND1  N Y N 153 
HIS CD2  C Y N 154 
HIS CE1  C Y N 155 
HIS NE2  N Y N 156 
HIS OXT  O N N 157 
HIS H    H N N 158 
HIS H2   H N N 159 
HIS HA   H N N 160 
HIS HB2  H N N 161 
HIS HB3  H N N 162 
HIS HD1  H N N 163 
HIS HD2  H N N 164 
HIS HE1  H N N 165 
HIS HE2  H N N 166 
HIS HXT  H N N 167 
HOH O    O N N 168 
HOH H1   H N N 169 
HOH H2   H N N 170 
ILE N    N N N 171 
ILE CA   C N S 172 
ILE C    C N N 173 
ILE O    O N N 174 
ILE CB   C N S 175 
ILE CG1  C N N 176 
ILE CG2  C N N 177 
ILE CD1  C N N 178 
ILE OXT  O N N 179 
ILE H    H N N 180 
ILE H2   H N N 181 
ILE HA   H N N 182 
ILE HB   H N N 183 
ILE HG12 H N N 184 
ILE HG13 H N N 185 
ILE HG21 H N N 186 
ILE HG22 H N N 187 
ILE HG23 H N N 188 
ILE HD11 H N N 189 
ILE HD12 H N N 190 
ILE HD13 H N N 191 
ILE HXT  H N N 192 
LEU N    N N N 193 
LEU CA   C N S 194 
LEU C    C N N 195 
LEU O    O N N 196 
LEU CB   C N N 197 
LEU CG   C N N 198 
LEU CD1  C N N 199 
LEU CD2  C N N 200 
LEU OXT  O N N 201 
LEU H    H N N 202 
LEU H2   H N N 203 
LEU HA   H N N 204 
LEU HB2  H N N 205 
LEU HB3  H N N 206 
LEU HG   H N N 207 
LEU HD11 H N N 208 
LEU HD12 H N N 209 
LEU HD13 H N N 210 
LEU HD21 H N N 211 
LEU HD22 H N N 212 
LEU HD23 H N N 213 
LEU HXT  H N N 214 
LYS N    N N N 215 
LYS CA   C N S 216 
LYS C    C N N 217 
LYS O    O N N 218 
LYS CB   C N N 219 
LYS CG   C N N 220 
LYS CD   C N N 221 
LYS CE   C N N 222 
LYS NZ   N N N 223 
LYS OXT  O N N 224 
LYS H    H N N 225 
LYS H2   H N N 226 
LYS HA   H N N 227 
LYS HB2  H N N 228 
LYS HB3  H N N 229 
LYS HG2  H N N 230 
LYS HG3  H N N 231 
LYS HD2  H N N 232 
LYS HD3  H N N 233 
LYS HE2  H N N 234 
LYS HE3  H N N 235 
LYS HZ1  H N N 236 
LYS HZ2  H N N 237 
LYS HZ3  H N N 238 
LYS HXT  H N N 239 
MBG C1   C N R 240 
MBG C2   C N R 241 
MBG C3   C N S 242 
MBG C4   C N R 243 
MBG C5   C N R 244 
MBG C6   C N N 245 
MBG C7   C N N 246 
MBG O1   O N N 247 
MBG O2   O N N 248 
MBG O3   O N N 249 
MBG O4   O N N 250 
MBG O5   O N N 251 
MBG O6   O N N 252 
MBG H1   H N N 253 
MBG H2   H N N 254 
MBG H3   H N N 255 
MBG H4   H N N 256 
MBG H5   H N N 257 
MBG H61  H N N 258 
MBG H62  H N N 259 
MBG H71  H N N 260 
MBG H72  H N N 261 
MBG H73  H N N 262 
MBG HO2  H N N 263 
MBG HO3  H N N 264 
MBG HO4  H N N 265 
MBG HO6  H N N 266 
MET N    N N N 267 
MET CA   C N S 268 
MET C    C N N 269 
MET O    O N N 270 
MET CB   C N N 271 
MET CG   C N N 272 
MET SD   S N N 273 
MET CE   C N N 274 
MET OXT  O N N 275 
MET H    H N N 276 
MET H2   H N N 277 
MET HA   H N N 278 
MET HB2  H N N 279 
MET HB3  H N N 280 
MET HG2  H N N 281 
MET HG3  H N N 282 
MET HE1  H N N 283 
MET HE2  H N N 284 
MET HE3  H N N 285 
MET HXT  H N N 286 
PHE N    N N N 287 
PHE CA   C N S 288 
PHE C    C N N 289 
PHE O    O N N 290 
PHE CB   C N N 291 
PHE CG   C Y N 292 
PHE CD1  C Y N 293 
PHE CD2  C Y N 294 
PHE CE1  C Y N 295 
PHE CE2  C Y N 296 
PHE CZ   C Y N 297 
PHE OXT  O N N 298 
PHE H    H N N 299 
PHE H2   H N N 300 
PHE HA   H N N 301 
PHE HB2  H N N 302 
PHE HB3  H N N 303 
PHE HD1  H N N 304 
PHE HD2  H N N 305 
PHE HE1  H N N 306 
PHE HE2  H N N 307 
PHE HZ   H N N 308 
PHE HXT  H N N 309 
PRO N    N N N 310 
PRO CA   C N S 311 
PRO C    C N N 312 
PRO O    O N N 313 
PRO CB   C N N 314 
PRO CG   C N N 315 
PRO CD   C N N 316 
PRO OXT  O N N 317 
PRO H    H N N 318 
PRO HA   H N N 319 
PRO HB2  H N N 320 
PRO HB3  H N N 321 
PRO HG2  H N N 322 
PRO HG3  H N N 323 
PRO HD2  H N N 324 
PRO HD3  H N N 325 
PRO HXT  H N N 326 
SER N    N N N 327 
SER CA   C N S 328 
SER C    C N N 329 
SER O    O N N 330 
SER CB   C N N 331 
SER OG   O N N 332 
SER OXT  O N N 333 
SER H    H N N 334 
SER H2   H N N 335 
SER HA   H N N 336 
SER HB2  H N N 337 
SER HB3  H N N 338 
SER HG   H N N 339 
SER HXT  H N N 340 
THR N    N N N 341 
THR CA   C N S 342 
THR C    C N N 343 
THR O    O N N 344 
THR CB   C N R 345 
THR OG1  O N N 346 
THR CG2  C N N 347 
THR OXT  O N N 348 
THR H    H N N 349 
THR H2   H N N 350 
THR HA   H N N 351 
THR HB   H N N 352 
THR HG1  H N N 353 
THR HG21 H N N 354 
THR HG22 H N N 355 
THR HG23 H N N 356 
THR HXT  H N N 357 
TRP N    N N N 358 
TRP CA   C N S 359 
TRP C    C N N 360 
TRP O    O N N 361 
TRP CB   C N N 362 
TRP CG   C Y N 363 
TRP CD1  C Y N 364 
TRP CD2  C Y N 365 
TRP NE1  N Y N 366 
TRP CE2  C Y N 367 
TRP CE3  C Y N 368 
TRP CZ2  C Y N 369 
TRP CZ3  C Y N 370 
TRP CH2  C Y N 371 
TRP OXT  O N N 372 
TRP H    H N N 373 
TRP H2   H N N 374 
TRP HA   H N N 375 
TRP HB2  H N N 376 
TRP HB3  H N N 377 
TRP HD1  H N N 378 
TRP HE1  H N N 379 
TRP HE3  H N N 380 
TRP HZ2  H N N 381 
TRP HZ3  H N N 382 
TRP HH2  H N N 383 
TRP HXT  H N N 384 
TYR N    N N N 385 
TYR CA   C N S 386 
TYR C    C N N 387 
TYR O    O N N 388 
TYR CB   C N N 389 
TYR CG   C Y N 390 
TYR CD1  C Y N 391 
TYR CD2  C Y N 392 
TYR CE1  C Y N 393 
TYR CE2  C Y N 394 
TYR CZ   C Y N 395 
TYR OH   O N N 396 
TYR OXT  O N N 397 
TYR H    H N N 398 
TYR H2   H N N 399 
TYR HA   H N N 400 
TYR HB2  H N N 401 
TYR HB3  H N N 402 
TYR HD1  H N N 403 
TYR HD2  H N N 404 
TYR HE1  H N N 405 
TYR HE2  H N N 406 
TYR HH   H N N 407 
TYR HXT  H N N 408 
VAL N    N N N 409 
VAL CA   C N S 410 
VAL C    C N N 411 
VAL O    O N N 412 
VAL CB   C N N 413 
VAL CG1  C N N 414 
VAL CG2  C N N 415 
VAL OXT  O N N 416 
VAL H    H N N 417 
VAL H2   H N N 418 
VAL HA   H N N 419 
VAL HB   H N N 420 
VAL HG11 H N N 421 
VAL HG12 H N N 422 
VAL HG13 H N N 423 
VAL HG21 H N N 424 
VAL HG22 H N N 425 
VAL HG23 H N N 426 
VAL HXT  H N N 427 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
EDO C1  O1   sing N N 83  
EDO C1  C2   sing N N 84  
EDO C1  H11  sing N N 85  
EDO C1  H12  sing N N 86  
EDO O1  HO1  sing N N 87  
EDO C2  O2   sing N N 88  
EDO C2  H21  sing N N 89  
EDO C2  H22  sing N N 90  
EDO O2  HO2  sing N N 91  
GLN N   CA   sing N N 92  
GLN N   H    sing N N 93  
GLN N   H2   sing N N 94  
GLN CA  C    sing N N 95  
GLN CA  CB   sing N N 96  
GLN CA  HA   sing N N 97  
GLN C   O    doub N N 98  
GLN C   OXT  sing N N 99  
GLN CB  CG   sing N N 100 
GLN CB  HB2  sing N N 101 
GLN CB  HB3  sing N N 102 
GLN CG  CD   sing N N 103 
GLN CG  HG2  sing N N 104 
GLN CG  HG3  sing N N 105 
GLN CD  OE1  doub N N 106 
GLN CD  NE2  sing N N 107 
GLN NE2 HE21 sing N N 108 
GLN NE2 HE22 sing N N 109 
GLN OXT HXT  sing N N 110 
GLU N   CA   sing N N 111 
GLU N   H    sing N N 112 
GLU N   H2   sing N N 113 
GLU CA  C    sing N N 114 
GLU CA  CB   sing N N 115 
GLU CA  HA   sing N N 116 
GLU C   O    doub N N 117 
GLU C   OXT  sing N N 118 
GLU CB  CG   sing N N 119 
GLU CB  HB2  sing N N 120 
GLU CB  HB3  sing N N 121 
GLU CG  CD   sing N N 122 
GLU CG  HG2  sing N N 123 
GLU CG  HG3  sing N N 124 
GLU CD  OE1  doub N N 125 
GLU CD  OE2  sing N N 126 
GLU OE2 HE2  sing N N 127 
GLU OXT HXT  sing N N 128 
GLY N   CA   sing N N 129 
GLY N   H    sing N N 130 
GLY N   H2   sing N N 131 
GLY CA  C    sing N N 132 
GLY CA  HA2  sing N N 133 
GLY CA  HA3  sing N N 134 
GLY C   O    doub N N 135 
GLY C   OXT  sing N N 136 
GLY OXT HXT  sing N N 137 
HIS N   CA   sing N N 138 
HIS N   H    sing N N 139 
HIS N   H2   sing N N 140 
HIS CA  C    sing N N 141 
HIS CA  CB   sing N N 142 
HIS CA  HA   sing N N 143 
HIS C   O    doub N N 144 
HIS C   OXT  sing N N 145 
HIS CB  CG   sing N N 146 
HIS CB  HB2  sing N N 147 
HIS CB  HB3  sing N N 148 
HIS CG  ND1  sing Y N 149 
HIS CG  CD2  doub Y N 150 
HIS ND1 CE1  doub Y N 151 
HIS ND1 HD1  sing N N 152 
HIS CD2 NE2  sing Y N 153 
HIS CD2 HD2  sing N N 154 
HIS CE1 NE2  sing Y N 155 
HIS CE1 HE1  sing N N 156 
HIS NE2 HE2  sing N N 157 
HIS OXT HXT  sing N N 158 
HOH O   H1   sing N N 159 
HOH O   H2   sing N N 160 
ILE N   CA   sing N N 161 
ILE N   H    sing N N 162 
ILE N   H2   sing N N 163 
ILE CA  C    sing N N 164 
ILE CA  CB   sing N N 165 
ILE CA  HA   sing N N 166 
ILE C   O    doub N N 167 
ILE C   OXT  sing N N 168 
ILE CB  CG1  sing N N 169 
ILE CB  CG2  sing N N 170 
ILE CB  HB   sing N N 171 
ILE CG1 CD1  sing N N 172 
ILE CG1 HG12 sing N N 173 
ILE CG1 HG13 sing N N 174 
ILE CG2 HG21 sing N N 175 
ILE CG2 HG22 sing N N 176 
ILE CG2 HG23 sing N N 177 
ILE CD1 HD11 sing N N 178 
ILE CD1 HD12 sing N N 179 
ILE CD1 HD13 sing N N 180 
ILE OXT HXT  sing N N 181 
LEU N   CA   sing N N 182 
LEU N   H    sing N N 183 
LEU N   H2   sing N N 184 
LEU CA  C    sing N N 185 
LEU CA  CB   sing N N 186 
LEU CA  HA   sing N N 187 
LEU C   O    doub N N 188 
LEU C   OXT  sing N N 189 
LEU CB  CG   sing N N 190 
LEU CB  HB2  sing N N 191 
LEU CB  HB3  sing N N 192 
LEU CG  CD1  sing N N 193 
LEU CG  CD2  sing N N 194 
LEU CG  HG   sing N N 195 
LEU CD1 HD11 sing N N 196 
LEU CD1 HD12 sing N N 197 
LEU CD1 HD13 sing N N 198 
LEU CD2 HD21 sing N N 199 
LEU CD2 HD22 sing N N 200 
LEU CD2 HD23 sing N N 201 
LEU OXT HXT  sing N N 202 
LYS N   CA   sing N N 203 
LYS N   H    sing N N 204 
LYS N   H2   sing N N 205 
LYS CA  C    sing N N 206 
LYS CA  CB   sing N N 207 
LYS CA  HA   sing N N 208 
LYS C   O    doub N N 209 
LYS C   OXT  sing N N 210 
LYS CB  CG   sing N N 211 
LYS CB  HB2  sing N N 212 
LYS CB  HB3  sing N N 213 
LYS CG  CD   sing N N 214 
LYS CG  HG2  sing N N 215 
LYS CG  HG3  sing N N 216 
LYS CD  CE   sing N N 217 
LYS CD  HD2  sing N N 218 
LYS CD  HD3  sing N N 219 
LYS CE  NZ   sing N N 220 
LYS CE  HE2  sing N N 221 
LYS CE  HE3  sing N N 222 
LYS NZ  HZ1  sing N N 223 
LYS NZ  HZ2  sing N N 224 
LYS NZ  HZ3  sing N N 225 
LYS OXT HXT  sing N N 226 
MBG C1  C2   sing N N 227 
MBG C1  O1   sing N N 228 
MBG C1  O5   sing N N 229 
MBG C1  H1   sing N N 230 
MBG C2  C3   sing N N 231 
MBG C2  O2   sing N N 232 
MBG C2  H2   sing N N 233 
MBG C3  C4   sing N N 234 
MBG C3  O3   sing N N 235 
MBG C3  H3   sing N N 236 
MBG C4  C5   sing N N 237 
MBG C4  O4   sing N N 238 
MBG C4  H4   sing N N 239 
MBG C5  C6   sing N N 240 
MBG C5  O5   sing N N 241 
MBG C5  H5   sing N N 242 
MBG C6  O6   sing N N 243 
MBG C6  H61  sing N N 244 
MBG C6  H62  sing N N 245 
MBG C7  O1   sing N N 246 
MBG C7  H71  sing N N 247 
MBG C7  H72  sing N N 248 
MBG C7  H73  sing N N 249 
MBG O2  HO2  sing N N 250 
MBG O3  HO3  sing N N 251 
MBG O4  HO4  sing N N 252 
MBG O6  HO6  sing N N 253 
MET N   CA   sing N N 254 
MET N   H    sing N N 255 
MET N   H2   sing N N 256 
MET CA  C    sing N N 257 
MET CA  CB   sing N N 258 
MET CA  HA   sing N N 259 
MET C   O    doub N N 260 
MET C   OXT  sing N N 261 
MET CB  CG   sing N N 262 
MET CB  HB2  sing N N 263 
MET CB  HB3  sing N N 264 
MET CG  SD   sing N N 265 
MET CG  HG2  sing N N 266 
MET CG  HG3  sing N N 267 
MET SD  CE   sing N N 268 
MET CE  HE1  sing N N 269 
MET CE  HE2  sing N N 270 
MET CE  HE3  sing N N 271 
MET OXT HXT  sing N N 272 
PHE N   CA   sing N N 273 
PHE N   H    sing N N 274 
PHE N   H2   sing N N 275 
PHE CA  C    sing N N 276 
PHE CA  CB   sing N N 277 
PHE CA  HA   sing N N 278 
PHE C   O    doub N N 279 
PHE C   OXT  sing N N 280 
PHE CB  CG   sing N N 281 
PHE CB  HB2  sing N N 282 
PHE CB  HB3  sing N N 283 
PHE CG  CD1  doub Y N 284 
PHE CG  CD2  sing Y N 285 
PHE CD1 CE1  sing Y N 286 
PHE CD1 HD1  sing N N 287 
PHE CD2 CE2  doub Y N 288 
PHE CD2 HD2  sing N N 289 
PHE CE1 CZ   doub Y N 290 
PHE CE1 HE1  sing N N 291 
PHE CE2 CZ   sing Y N 292 
PHE CE2 HE2  sing N N 293 
PHE CZ  HZ   sing N N 294 
PHE OXT HXT  sing N N 295 
PRO N   CA   sing N N 296 
PRO N   CD   sing N N 297 
PRO N   H    sing N N 298 
PRO CA  C    sing N N 299 
PRO CA  CB   sing N N 300 
PRO CA  HA   sing N N 301 
PRO C   O    doub N N 302 
PRO C   OXT  sing N N 303 
PRO CB  CG   sing N N 304 
PRO CB  HB2  sing N N 305 
PRO CB  HB3  sing N N 306 
PRO CG  CD   sing N N 307 
PRO CG  HG2  sing N N 308 
PRO CG  HG3  sing N N 309 
PRO CD  HD2  sing N N 310 
PRO CD  HD3  sing N N 311 
PRO OXT HXT  sing N N 312 
SER N   CA   sing N N 313 
SER N   H    sing N N 314 
SER N   H2   sing N N 315 
SER CA  C    sing N N 316 
SER CA  CB   sing N N 317 
SER CA  HA   sing N N 318 
SER C   O    doub N N 319 
SER C   OXT  sing N N 320 
SER CB  OG   sing N N 321 
SER CB  HB2  sing N N 322 
SER CB  HB3  sing N N 323 
SER OG  HG   sing N N 324 
SER OXT HXT  sing N N 325 
THR N   CA   sing N N 326 
THR N   H    sing N N 327 
THR N   H2   sing N N 328 
THR CA  C    sing N N 329 
THR CA  CB   sing N N 330 
THR CA  HA   sing N N 331 
THR C   O    doub N N 332 
THR C   OXT  sing N N 333 
THR CB  OG1  sing N N 334 
THR CB  CG2  sing N N 335 
THR CB  HB   sing N N 336 
THR OG1 HG1  sing N N 337 
THR CG2 HG21 sing N N 338 
THR CG2 HG22 sing N N 339 
THR CG2 HG23 sing N N 340 
THR OXT HXT  sing N N 341 
TRP N   CA   sing N N 342 
TRP N   H    sing N N 343 
TRP N   H2   sing N N 344 
TRP CA  C    sing N N 345 
TRP CA  CB   sing N N 346 
TRP CA  HA   sing N N 347 
TRP C   O    doub N N 348 
TRP C   OXT  sing N N 349 
TRP CB  CG   sing N N 350 
TRP CB  HB2  sing N N 351 
TRP CB  HB3  sing N N 352 
TRP CG  CD1  doub Y N 353 
TRP CG  CD2  sing Y N 354 
TRP CD1 NE1  sing Y N 355 
TRP CD1 HD1  sing N N 356 
TRP CD2 CE2  doub Y N 357 
TRP CD2 CE3  sing Y N 358 
TRP NE1 CE2  sing Y N 359 
TRP NE1 HE1  sing N N 360 
TRP CE2 CZ2  sing Y N 361 
TRP CE3 CZ3  doub Y N 362 
TRP CE3 HE3  sing N N 363 
TRP CZ2 CH2  doub Y N 364 
TRP CZ2 HZ2  sing N N 365 
TRP CZ3 CH2  sing Y N 366 
TRP CZ3 HZ3  sing N N 367 
TRP CH2 HH2  sing N N 368 
TRP OXT HXT  sing N N 369 
TYR N   CA   sing N N 370 
TYR N   H    sing N N 371 
TYR N   H2   sing N N 372 
TYR CA  C    sing N N 373 
TYR CA  CB   sing N N 374 
TYR CA  HA   sing N N 375 
TYR C   O    doub N N 376 
TYR C   OXT  sing N N 377 
TYR CB  CG   sing N N 378 
TYR CB  HB2  sing N N 379 
TYR CB  HB3  sing N N 380 
TYR CG  CD1  doub Y N 381 
TYR CG  CD2  sing Y N 382 
TYR CD1 CE1  sing Y N 383 
TYR CD1 HD1  sing N N 384 
TYR CD2 CE2  doub Y N 385 
TYR CD2 HD2  sing N N 386 
TYR CE1 CZ   doub Y N 387 
TYR CE1 HE1  sing N N 388 
TYR CE2 CZ   sing Y N 389 
TYR CE2 HE2  sing N N 390 
TYR CZ  OH   sing N N 391 
TYR OH  HH   sing N N 392 
TYR OXT HXT  sing N N 393 
VAL N   CA   sing N N 394 
VAL N   H    sing N N 395 
VAL N   H2   sing N N 396 
VAL CA  C    sing N N 397 
VAL CA  CB   sing N N 398 
VAL CA  HA   sing N N 399 
VAL C   O    doub N N 400 
VAL C   OXT  sing N N 401 
VAL CB  CG1  sing N N 402 
VAL CB  CG2  sing N N 403 
VAL CB  HB   sing N N 404 
VAL CG1 HG11 sing N N 405 
VAL CG1 HG12 sing N N 406 
VAL CG1 HG13 sing N N 407 
VAL CG2 HG21 sing N N 408 
VAL CG2 HG22 sing N N 409 
VAL CG2 HG23 sing N N 410 
VAL OXT HXT  sing N N 411 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Australian Research Council (ARC)' Australia CE200100012 1 
'Australian Research Council (ARC)' Australia CE200100029 2 
# 
_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   2P9H 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9NT6 
_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]   0.027422 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_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]   0.009231 
_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]   0.008361 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . SER A 1 4   ? 33.871 -7.672  -46.511 1.00 57.47  ?  61  SER A N   1 
ATOM   2    C CA  . SER A 1 4   ? 33.949 -8.903  -47.289 1.00 49.54  ?  61  SER A CA  1 
ATOM   3    C C   . SER A 1 4   ? 32.958 -9.976  -46.802 1.00 40.92  ?  61  SER A C   1 
ATOM   4    O O   . SER A 1 4   ? 32.461 -10.763 -47.612 1.00 33.93  ?  61  SER A O   1 
ATOM   5    C CB  . SER A 1 4   ? 35.373 -9.453  -47.265 1.00 50.98  ?  61  SER A CB  1 
ATOM   6    O OG  . SER A 1 4   ? 35.509 -10.526 -48.177 1.00 42.83  ?  61  SER A OG  1 
ATOM   7    N N   . HIS A 1 5   ? 32.680 -10.023 -45.494 1.00 28.11  ?  62  HIS A N   1 
ATOM   8    C CA  . HIS A 1 5   ? 31.582 -10.827 -44.969 1.00 21.04  ?  62  HIS A CA  1 
ATOM   9    C C   . HIS A 1 5   ? 30.864 -10.033 -43.895 1.00 24.50  ?  62  HIS A C   1 
ATOM   10   O O   . HIS A 1 5   ? 31.499 -9.299  -43.137 1.00 20.89  ?  62  HIS A O   1 
ATOM   11   C CB  . HIS A 1 5   ? 32.076 -12.151 -44.374 1.00 22.93  ?  62  HIS A CB  1 
ATOM   12   C CG  . HIS A 1 5   ? 32.691 -13.065 -45.389 1.00 27.38  ?  62  HIS A CG  1 
ATOM   13   N ND1 . HIS A 1 5   ? 31.990 -13.555 -46.469 1.00 30.96  ?  62  HIS A ND1 1 
ATOM   14   C CD2 . HIS A 1 5   ? 33.940 -13.579 -45.484 1.00 38.98  ?  62  HIS A CD2 1 
ATOM   15   C CE1 . HIS A 1 5   ? 32.784 -14.327 -47.192 1.00 34.44  ?  62  HIS A CE1 1 
ATOM   16   N NE2 . HIS A 1 5   ? 33.970 -14.363 -46.612 1.00 35.21  ?  62  HIS A NE2 1 
ATOM   17   N N   . THR A 1 6   ? 29.542 -10.191 -43.824 1.00 18.41  ?  63  THR A N   1 
ATOM   18   C CA  . THR A 1 6   ? 28.724 -9.479  -42.849 1.00 18.23  ?  63  THR A CA  1 
ATOM   19   C C   . THR A 1 6   ? 27.724 -10.442 -42.232 1.00 17.28  ?  63  THR A C   1 
ATOM   20   O O   . THR A 1 6   ? 27.105 -11.234 -42.946 1.00 20.67  ?  63  THR A O   1 
ATOM   21   C CB  . THR A 1 6   ? 27.968 -8.298  -43.488 1.00 18.41  ?  63  THR A CB  1 
ATOM   22   O OG1 . THR A 1 6   ? 28.903 -7.396  -44.089 1.00 25.18  ?  63  THR A OG1 1 
ATOM   23   C CG2 . THR A 1 6   ? 27.145 -7.566  -42.417 1.00 20.49  ?  63  THR A CG2 1 
ATOM   24   N N   . ILE A 1 7   ? 27.588 -10.387 -40.896 1.00 15.52  ?  64  ILE A N   1 
ATOM   25   C CA  . ILE A 1 7   ? 26.586 -11.129 -40.139 1.00 16.92  ?  64  ILE A CA  1 
ATOM   26   C C   . ILE A 1 7   ? 25.433 -10.189 -39.831 1.00 16.37  ?  64  ILE A C   1 
ATOM   27   O O   . ILE A 1 7   ? 25.651 -9.041  -39.444 1.00 17.62  ?  64  ILE A O   1 
ATOM   28   C CB  . ILE A 1 7   ? 27.214 -11.678 -38.841 1.00 17.51  ?  64  ILE A CB  1 
ATOM   29   C CG1 . ILE A 1 7   ? 28.236 -12.744 -39.181 1.00 18.80  ?  64  ILE A CG1 1 
ATOM   30   C CG2 . ILE A 1 7   ? 26.159 -12.243 -37.911 1.00 22.86  ?  64  ILE A CG2 1 
ATOM   31   C CD1 . ILE A 1 7   ? 29.055 -13.170 -37.958 1.00 22.47  ?  64  ILE A CD1 1 
ATOM   32   N N   . GLY A 1 8   ? 24.200 -10.658 -40.025 1.00 16.76  ?  65  GLY A N   1 
ATOM   33   C CA  . GLY A 1 8   ? 23.022 -9.907  -39.610 1.00 13.87  ?  65  GLY A CA  1 
ATOM   34   C C   . GLY A 1 8   ? 22.535 -10.443 -38.278 1.00 15.18  ?  65  GLY A C   1 
ATOM   35   O O   . GLY A 1 8   ? 22.396 -11.653 -38.099 1.00 17.15  ?  65  GLY A O   1 
ATOM   36   N N   . LEU A 1 9   ? 22.289 -9.537  -37.338 1.00 15.15  ?  66  LEU A N   1 
ATOM   37   C CA  . LEU A 1 9   ? 21.828 -9.906  -36.004 1.00 14.12  ?  66  LEU A CA  1 
ATOM   38   C C   . LEU A 1 9   ? 20.469 -9.259  -35.766 1.00 14.42  ?  66  LEU A C   1 
ATOM   39   O O   . LEU A 1 9   ? 20.364 -8.030  -35.776 1.00 17.48  ?  66  LEU A O   1 
ATOM   40   C CB  . LEU A 1 9   ? 22.829 -9.469  -34.919 1.00 15.51  ?  66  LEU A CB  1 
ATOM   41   C CG  . LEU A 1 9   ? 22.449 -9.614  -33.444 1.00 19.79  ?  66  LEU A CG  1 
ATOM   42   C CD1 . LEU A 1 9   ? 22.025 -11.028 -33.068 1.00 21.52  ?  66  LEU A CD1 1 
ATOM   43   C CD2 . LEU A 1 9   ? 23.643 -9.185  -32.575 1.00 19.54  ?  66  LEU A CD2 1 
ATOM   44   N N   . ALA A 1 10  ? 19.434 -10.077 -35.562 1.00 12.82  ?  67  ALA A N   1 
ATOM   45   C CA  . ALA A 1 10  ? 18.125 -9.592  -35.139 1.00 15.03  ?  67  ALA A CA  1 
ATOM   46   C C   . ALA A 1 10  ? 18.047 -9.700  -33.629 1.00 14.67  ?  67  ALA A C   1 
ATOM   47   O O   . ALA A 1 10  ? 18.317 -10.770 -33.079 1.00 18.10  ?  67  ALA A O   1 
ATOM   48   C CB  . ALA A 1 10  ? 17.004 -10.417 -35.752 1.00 17.79  ?  67  ALA A CB  1 
ATOM   49   N N   . THR A 1 11  ? 17.657 -8.620  -32.957 1.00 14.15  ?  68  THR A N   1 
ATOM   50   C CA  . THR A 1 11  ? 17.665 -8.612  -31.494 1.00 15.47  ?  68  THR A CA  1 
ATOM   51   C C   . THR A 1 11  ? 16.402 -7.963  -30.950 1.00 15.21  ?  68  THR A C   1 
ATOM   52   O O   . THR A 1 11  ? 15.848 -7.051  -31.563 1.00 15.30  ?  68  THR A O   1 
ATOM   53   C CB  . THR A 1 11  ? 18.889 -7.874  -30.937 1.00 13.32  ?  68  THR A CB  1 
ATOM   54   O OG1 . THR A 1 11  ? 18.835 -7.857  -29.496 1.00 18.12  ?  68  THR A OG1 1 
ATOM   55   C CG2 . THR A 1 11  ? 18.998 -6.459  -31.491 1.00 14.93  ?  68  THR A CG2 1 
ATOM   56   N N   . THR A 1 12  ? 15.972 -8.418  -29.771 1.00 16.28  ?  69  THR A N   1 
ATOM   57   C CA  . THR A 1 12  ? 14.900 -7.741  -29.059 1.00 14.53  ?  69  THR A CA  1 
ATOM   58   C C   . THR A 1 12  ? 15.440 -6.451  -28.428 1.00 16.43  ?  69  THR A C   1 
ATOM   59   O O   . THR A 1 12  ? 16.641 -6.155  -28.491 1.00 17.30  ?  69  THR A O   1 
ATOM   60   C CB  . THR A 1 12  ? 14.312 -8.654  -27.998 1.00 21.08  ?  69  THR A CB  1 
ATOM   61   O OG1 . THR A 1 12  ? 13.253 -7.971  -27.323 1.00 39.00  ?  69  THR A OG1 1 
ATOM   62   C CG2 . THR A 1 12  ? 15.378 -8.963  -27.018 1.00 14.31  ?  69  THR A CG2 1 
ATOM   63   N N   . ASN A 1 13  ? 14.522 -5.677  -27.845 1.00 18.79  ?  70  ASN A N   1 
ATOM   64   C CA  . ASN A 1 13  ? 14.768 -4.375  -27.233 1.00 23.55  ?  70  ASN A CA  1 
ATOM   65   C C   . ASN A 1 13  ? 16.143 -4.234  -26.586 1.00 20.73  ?  70  ASN A C   1 
ATOM   66   O O   . ASN A 1 13  ? 16.427 -4.871  -25.570 1.00 19.11  ?  70  ASN A O   1 
ATOM   67   C CB  . ASN A 1 13  ? 13.686 -4.122  -26.184 1.00 23.73  ?  70  ASN A CB  1 
ATOM   68   C CG  . ASN A 1 13  ? 13.907 -2.844  -25.431 1.00 29.49  ?  70  ASN A CG  1 
ATOM   69   O OD1 . ASN A 1 13  ? 14.495 -1.897  -25.964 1.00 27.30  ?  70  ASN A OD1 1 
ATOM   70   N ND2 . ASN A 1 13  ? 13.418 -2.791  -24.186 1.00 28.78  ?  70  ASN A ND2 1 
ATOM   71   N N   . LEU A 1 14  ? 16.999 -3.382  -27.149 1.00 16.23  ?  71  LEU A N   1 
ATOM   72   C CA  . LEU A 1 14  ? 18.359 -3.213  -26.633 1.00 16.11  ?  71  LEU A CA  1 
ATOM   73   C C   . LEU A 1 14  ? 18.393 -2.441  -25.328 1.00 21.02  ?  71  LEU A C   1 
ATOM   74   O O   . LEU A 1 14  ? 19.454 -2.400  -24.690 1.00 20.87  ?  71  LEU A O   1 
ATOM   75   C CB  . LEU A 1 14  ? 19.232 -2.484  -27.667 1.00 17.87  ?  71  LEU A CB  1 
ATOM   76   C CG  . LEU A 1 14  ? 19.588 -3.411  -28.827 1.00 21.95  ?  71  LEU A CG  1 
ATOM   77   C CD1 . LEU A 1 14  ? 20.300 -2.650  -29.954 1.00 26.05  ?  71  LEU A CD1 1 
ATOM   78   C CD2 . LEU A 1 14  ? 20.439 -4.593  -28.352 1.00 19.32  ?  71  LEU A CD2 1 
ATOM   79   N N   . ALA A 1 15  ? 17.277 -1.830  -24.927 1.00 15.46  ?  72  ALA A N   1 
ATOM   80   C CA  . ALA A 1 15  ? 17.210 -1.167  -23.634 1.00 19.07  ?  72  ALA A CA  1 
ATOM   81   C C   . ALA A 1 15  ? 17.228 -2.155  -22.480 1.00 17.46  ?  72  ALA A C   1 
ATOM   82   O O   . ALA A 1 15  ? 17.394 -1.729  -21.329 1.00 19.86  ?  72  ALA A O   1 
ATOM   83   C CB  . ALA A 1 15  ? 15.970 -0.286  -23.552 1.00 24.69  ?  72  ALA A CB  1 
ATOM   84   N N   . LEU A 1 16  ? 17.055 -3.447  -22.742 1.00 14.96  ?  73  LEU A N   1 
ATOM   85   C CA  . LEU A 1 16  ? 17.330 -4.448  -21.720 1.00 14.43  ?  73  LEU A CA  1 
ATOM   86   C C   . LEU A 1 16  ? 18.802 -4.829  -21.797 1.00 13.87  ?  73  LEU A C   1 
ATOM   87   O O   . LEU A 1 16  ? 19.384 -4.920  -22.884 1.00 14.69  ?  73  LEU A O   1 
ATOM   88   C CB  . LEU A 1 16  ? 16.441 -5.678  -21.886 1.00 12.96  ?  73  LEU A CB  1 
ATOM   89   C CG  . LEU A 1 16  ? 14.937 -5.402  -21.672 1.00 13.84  ?  73  LEU A CG  1 
ATOM   90   C CD1 . LEU A 1 16  ? 14.122 -6.688  -21.778 1.00 18.15  ?  73  LEU A CD1 1 
ATOM   91   C CD2 . LEU A 1 16  ? 14.690 -4.735  -20.345 1.00 17.79  ?  73  LEU A CD2 1 
ATOM   92   N N   . HIS A 1 17  ? 19.404 -5.043  -20.631 1.00 12.37  ?  74  HIS A N   1 
ATOM   93   C CA  . HIS A 1 17  ? 20.853 -5.103  -20.548 1.00 11.62  ?  74  HIS A CA  1 
ATOM   94   C C   . HIS A 1 17  ? 21.416 -6.390  -21.125 1.00 13.50  ?  74  HIS A C   1 
ATOM   95   O O   . HIS A 1 17  ? 22.477 -6.363  -21.761 1.00 12.76  ?  74  HIS A O   1 
ATOM   96   C CB  . HIS A 1 17  ? 21.264 -4.913  -19.092 1.00 12.96  ?  74  HIS A CB  1 
ATOM   97   C CG  . HIS A 1 17  ? 20.808 -3.610  -18.520 1.00 13.27  ?  74  HIS A CG  1 
ATOM   98   N ND1 . HIS A 1 17  ? 20.471 -2.526  -19.309 1.00 14.46  ?  74  HIS A ND1 1 
ATOM   99   C CD2 . HIS A 1 17  ? 20.650 -3.209  -17.238 1.00 14.02  ?  74  HIS A CD2 1 
ATOM   100  C CE1 . HIS A 1 17  ? 20.112 -1.524  -18.531 1.00 14.48  ?  74  HIS A CE1 1 
ATOM   101  N NE2 . HIS A 1 17  ? 20.213 -1.906  -17.268 1.00 16.13  ?  74  HIS A NE2 1 
ATOM   102  N N   . ALA A 1 18  ? 20.744 -7.522  -20.913 1.00 12.76  ?  75  ALA A N   1 
ATOM   103  C CA  . ALA A 1 18  ? 21.285 -8.786  -21.414 1.00 11.27  ?  75  ALA A CA  1 
ATOM   104  C C   . ALA A 1 18  ? 21.368 -8.793  -22.936 1.00 12.51  ?  75  ALA A C   1 
ATOM   105  O O   . ALA A 1 18  ? 22.454 -9.106  -23.461 1.00 11.63  ?  75  ALA A O   1 
ATOM   106  C CB  . ALA A 1 18  ? 20.477 -9.964  -20.850 1.00 13.05  ?  75  ALA A CB  1 
ATOM   107  N N   . PRO A 1 19  ? 20.333 -8.410  -23.699 1.00 12.99  ?  76  PRO A N   1 
ATOM   108  C CA  . PRO A 1 19  ? 20.524 -8.398  -25.165 1.00 14.13  ?  76  PRO A CA  1 
ATOM   109  C C   . PRO A 1 19  ? 21.610 -7.436  -25.616 1.00 14.88  ?  76  PRO A C   1 
ATOM   110  O O   . PRO A 1 19  ? 22.313 -7.714  -26.603 1.00 13.00  ?  76  PRO A O   1 
ATOM   111  C CB  . PRO A 1 19  ? 19.141 -8.005  -25.720 1.00 14.81  ?  76  PRO A CB  1 
ATOM   112  C CG  . PRO A 1 19  ? 18.283 -7.635  -24.532 1.00 20.09  ?  76  PRO A CG  1 
ATOM   113  C CD  . PRO A 1 19  ? 18.915 -8.221  -23.313 1.00 13.92  ?  76  PRO A CD  1 
ATOM   114  N N   . SER A 1 20  ? 21.773 -6.311  -24.939 1.00 12.23  ?  77  SER A N   1 
ATOM   115  C CA  . SER A 1 20  ? 22.842 -5.395  -25.305 1.00 10.84  ?  77  SER A CA  1 
ATOM   116  C C   . SER A 1 20  ? 24.217 -6.018  -25.073 1.00 14.18  ?  77  SER A C   1 
ATOM   117  O O   . SER A 1 20  ? 25.125 -5.845  -25.894 1.00 14.12  ?  77  SER A O   1 
ATOM   118  C CB  . SER A 1 20  ? 22.692 -4.088  -24.547 1.00 16.62  ?  77  SER A CB  1 
ATOM   119  O OG  . SER A 1 20  ? 21.760 -3.262  -25.211 1.00 28.82  ?  77  SER A OG  1 
ATOM   120  N N   . GLN A 1 21  ? 24.405 -6.755  -23.972 1.00 13.88  ?  78  GLN A N   1 
ATOM   121  C CA  . GLN A 1 21  ? 25.684 -7.417  -23.772 1.00 10.85  ?  78  GLN A CA  1 
ATOM   122  C C   . GLN A 1 21  ? 25.896 -8.523  -24.795 1.00 14.09  ?  78  GLN A C   1 
ATOM   123  O O   . GLN A 1 21  ? 27.035 -8.783  -25.191 1.00 13.45  ?  78  GLN A O   1 
ATOM   124  C CB  . GLN A 1 21  ? 25.791 -7.974  -22.342 1.00 10.28  ?  78  GLN A CB  1 
ATOM   125  C CG  . GLN A 1 21  ? 26.044 -6.860  -21.308 1.00 13.25  ?  78  GLN A CG  1 
ATOM   126  C CD  . GLN A 1 21  ? 26.331 -7.343  -19.894 1.00 14.94  ?  78  GLN A CD  1 
ATOM   127  O OE1 . GLN A 1 21  ? 25.676 -6.890  -18.965 1.00 13.83  ?  78  GLN A OE1 1 
ATOM   128  N NE2 . GLN A 1 21  ? 27.327 -8.206  -19.712 1.00 14.60  ?  78  GLN A NE2 1 
ATOM   129  N N   . ILE A 1 22  ? 24.820 -9.168  -25.229 1.00 12.27  ?  79  ILE A N   1 
ATOM   130  C CA  . ILE A 1 22  ? 24.941 -10.208 -26.252 1.00 10.80  ?  79  ILE A CA  1 
ATOM   131  C C   . ILE A 1 22  ? 25.358 -9.600  -27.583 1.00 13.57  ?  79  ILE A C   1 
ATOM   132  O O   . ILE A 1 22  ? 26.268 -10.116 -28.244 1.00 14.13  ?  79  ILE A O   1 
ATOM   133  C CB  . ILE A 1 22  ? 23.630 -10.996 -26.358 1.00 11.09  ?  79  ILE A CB  1 
ATOM   134  C CG1 . ILE A 1 22  ? 23.477 -11.851 -25.105 1.00 13.70  ?  79  ILE A CG1 1 
ATOM   135  C CG2 . ILE A 1 22  ? 23.593 -11.850 -27.649 1.00 14.84  ?  79  ILE A CG2 1 
ATOM   136  C CD1 . ILE A 1 22  ? 22.106 -12.505 -24.921 1.00 15.54  ?  79  ILE A CD1 1 
ATOM   137  N N   . VAL A 1 23  ? 24.750 -8.470  -27.976 1.00 13.21  ?  80  VAL A N   1 
ATOM   138  C CA  . VAL A 1 23  ? 25.185 -7.778  -29.198 1.00 11.71  ?  80  VAL A CA  1 
ATOM   139  C C   . VAL A 1 23  ? 26.668 -7.439  -29.114 1.00 15.33  ?  80  VAL A C   1 
ATOM   140  O O   . VAL A 1 23  ? 27.439 -7.685  -30.049 1.00 14.84  ?  80  VAL A O   1 
ATOM   141  C CB  . VAL A 1 23  ? 24.354 -6.500  -29.439 1.00 16.14  ?  80  VAL A CB  1 
ATOM   142  C CG1 . VAL A 1 23  ? 24.981 -5.666  -30.563 1.00 21.48  ?  80  VAL A CG1 1 
ATOM   143  C CG2 . VAL A 1 23  ? 22.921 -6.855  -29.773 1.00 20.89  ?  80  VAL A CG2 1 
ATOM   144  N N   . ALA A 1 24  ? 27.103 -6.885  -27.984 1.00 13.53  ?  81  ALA A N   1 
ATOM   145  C CA  . ALA A 1 24  ? 28.510 -6.512  -27.862 1.00 15.65  ?  81  ALA A CA  1 
ATOM   146  C C   . ALA A 1 24  ? 29.430 -7.728  -27.995 1.00 13.77  ?  81  ALA A C   1 
ATOM   147  O O   . ALA A 1 24  ? 30.517 -7.635  -28.587 1.00 15.44  ?  81  ALA A O   1 
ATOM   148  C CB  . ALA A 1 24  ? 28.756 -5.799  -26.531 1.00 17.66  ?  81  ALA A CB  1 
ATOM   149  N N   . ALA A 1 25  ? 29.012 -8.876  -27.454 1.00 14.23  ?  82  ALA A N   1 
ATOM   150  C CA  . ALA A 1 25  ? 29.857 -10.068 -27.472 1.00 12.94  ?  82  ALA A CA  1 
ATOM   151  C C   . ALA A 1 25  ? 29.931 -10.662 -28.870 1.00 14.51  ?  82  ALA A C   1 
ATOM   152  O O   . ALA A 1 25  ? 30.975 -11.195 -29.273 1.00 16.15  ?  82  ALA A O   1 
ATOM   153  C CB  . ALA A 1 25  ? 29.310 -11.111 -26.489 1.00 14.21  ?  82  ALA A CB  1 
ATOM   154  N N   . ILE A 1 26  ? 28.826 -10.594 -29.608 1.00 14.21  ?  83  ILE A N   1 
ATOM   155  C CA  . ILE A 1 26  ? 28.815 -11.061 -30.991 1.00 13.03  ?  83  ILE A CA  1 
ATOM   156  C C   . ILE A 1 26  ? 29.683 -10.166 -31.866 1.00 14.74  ?  83  ILE A C   1 
ATOM   157  O O   . ILE A 1 26  ? 30.488 -10.651 -32.682 1.00 15.04  ?  83  ILE A O   1 
ATOM   158  C CB  . ILE A 1 26  ? 27.366 -11.120 -31.495 1.00 12.56  ?  83  ILE A CB  1 
ATOM   159  C CG1 . ILE A 1 26  ? 26.626 -12.267 -30.819 1.00 12.94  ?  83  ILE A CG1 1 
ATOM   160  C CG2 . ILE A 1 26  ? 27.330 -11.239 -33.039 1.00 14.56  ?  83  ILE A CG2 1 
ATOM   161  C CD1 . ILE A 1 26  ? 25.105 -12.288 -31.093 1.00 14.74  ?  83  ILE A CD1 1 
ATOM   162  N N   . LYS A 1 27  ? 29.546 -8.849  -31.710 1.00 14.07  ?  84  LYS A N   1 
ATOM   163  C CA  . LYS A 1 27  ? 30.397 -7.926  -32.460 1.00 16.45  ?  84  LYS A CA  1 
ATOM   164  C C   . LYS A 1 27  ? 31.880 -8.169  -32.176 1.00 15.75  ?  84  LYS A C   1 
ATOM   165  O O   . LYS A 1 27  ? 32.707 -8.136  -33.090 1.00 16.42  ?  84  LYS A O   1 
ATOM   166  C CB  . LYS A 1 27  ? 30.003 -6.477  -32.130 1.00 19.03  ?  84  LYS A CB  1 
ATOM   167  C CG  . LYS A 1 27  ? 30.734 -5.413  -32.953 1.00 25.58  ?  84  LYS A CG  1 
ATOM   168  C CD  . LYS A 1 27  ? 31.934 -4.856  -32.212 1.00 35.02  ?  84  LYS A CD  1 
ATOM   169  C CE  . LYS A 1 27  ? 32.519 -3.651  -32.927 1.00 42.20  ?  84  LYS A CE  1 
ATOM   170  N NZ  . LYS A 1 27  ? 32.452 -3.854  -34.390 1.00 36.49  ?  84  LYS A NZ  1 
ATOM   171  N N   . SER A 1 28  ? 32.244 -8.416  -30.912 1.00 16.65  ?  85  SER A N   1 
ATOM   172  C CA  . SER A 1 28  ? 33.647 -8.637  -30.589 1.00 18.55  ?  85  SER A CA  1 
ATOM   173  C C   . SER A 1 28  ? 34.224 -9.842  -31.334 1.00 15.57  ?  85  SER A C   1 
ATOM   174  O O   . SER A 1 28  ? 35.327 -9.770  -31.889 1.00 20.47  ?  85  SER A O   1 
ATOM   175  C CB  . SER A 1 28  ? 33.797 -8.825  -29.085 1.00 20.43  ?  85  SER A CB  1 
ATOM   176  O OG  . SER A 1 28  ? 35.153 -9.045  -28.767 1.00 26.76  ?  85  SER A OG  1 
ATOM   177  N N   . ARG A 1 29  ? 33.524 -10.986 -31.294 1.00 16.50  ?  86  ARG A N   1 
ATOM   178  C CA  . ARG A 1 29  ? 34.053 -12.179 -31.943 1.00 16.62  ?  86  ARG A CA  1 
ATOM   179  C C   . ARG A 1 29  ? 34.032 -12.004 -33.447 1.00 15.72  ?  86  ARG A C   1 
ATOM   180  O O   . ARG A 1 29  ? 34.984 -12.394 -34.141 1.00 18.60  ?  86  ARG A O   1 
ATOM   181  C CB  . ARG A 1 29  ? 33.246 -13.420 -31.548 1.00 16.78  ?  86  ARG A CB  1 
ATOM   182  C CG  . ARG A 1 29  ? 33.768 -14.720 -32.199 1.00 16.38  ?  86  ARG A CG  1 
ATOM   183  C CD  . ARG A 1 29  ? 35.203 -15.034 -31.803 1.00 21.07  ?  86  ARG A CD  1 
ATOM   184  N NE  . ARG A 1 29  ? 35.670 -16.284 -32.396 1.00 24.18  ?  86  ARG A NE  1 
ATOM   185  C CZ  . ARG A 1 29  ? 36.945 -16.605 -32.573 1.00 35.09  ?  86  ARG A CZ  1 
ATOM   186  N NH1 . ARG A 1 29  ? 37.919 -15.773 -32.243 1.00 33.50  ?  86  ARG A NH1 1 
ATOM   187  N NH2 . ARG A 1 29  ? 37.252 -17.796 -33.087 1.00 35.07  ?  86  ARG A NH2 1 
ATOM   188  N N   . ALA A 1 30  ? 32.977 -11.378 -33.963 1.00 15.99  ?  87  ALA A N   1 
ATOM   189  C CA  . ALA A 1 30  ? 32.886 -11.181 -35.400 1.00 16.36  ?  87  ALA A CA  1 
ATOM   190  C C   . ALA A 1 30  ? 34.038 -10.328 -35.896 1.00 16.49  ?  87  ALA A C   1 
ATOM   191  O O   . ALA A 1 30  ? 34.669 -10.650 -36.906 1.00 17.09  ?  87  ALA A O   1 
ATOM   192  C CB  . ALA A 1 30  ? 31.542 -10.542 -35.740 1.00 16.04  ?  87  ALA A CB  1 
ATOM   193  N N   . SER A 1 31  ? 34.343 -9.246  -35.185 1.00 16.09  ?  88  SER A N   1 
ATOM   194  C CA  . SER A 1 31  ? 35.470 -8.405  -35.583 1.00 17.04  ?  88  SER A CA  1 
ATOM   195  C C   . SER A 1 31  ? 36.791 -9.168  -35.540 1.00 21.22  ?  88  SER A C   1 
ATOM   196  O O   . SER A 1 31  ? 37.634 -9.016  -36.433 1.00 24.65  ?  88  SER A O   1 
ATOM   197  C CB  . SER A 1 31  ? 35.533 -7.172  -34.686 1.00 24.47  ?  88  SER A CB  1 
ATOM   198  O OG  . SER A 1 31  ? 34.478 -6.287  -35.021 1.00 27.48  ?  88  SER A OG  1 
ATOM   199  N N   . GLN A 1 32  ? 36.987 -10.012 -34.526 1.00 20.89  ?  89  GLN A N   1 
ATOM   200  C CA  . GLN A 1 32  ? 38.242 -10.759 -34.445 1.00 23.28  ?  89  GLN A CA  1 
ATOM   201  C C   . GLN A 1 32  ? 38.405 -11.702 -35.624 1.00 22.80  ?  89  GLN A C   1 
ATOM   202  O O   . GLN A 1 32  ? 39.534 -12.017 -36.019 1.00 30.00  ?  89  GLN A O   1 
ATOM   203  C CB  . GLN A 1 32  ? 38.308 -11.555 -33.148 1.00 27.63  ?  89  GLN A CB  1 
ATOM   204  C CG  . GLN A 1 32  ? 38.479 -10.725 -31.923 1.00 31.29  ?  89  GLN A CG  1 
ATOM   205  C CD  . GLN A 1 32  ? 38.613 -11.587 -30.699 1.00 51.17  ?  89  GLN A CD  1 
ATOM   206  O OE1 . GLN A 1 32  ? 37.887 -12.571 -30.537 1.00 44.09  ?  89  GLN A OE1 1 
ATOM   207  N NE2 . GLN A 1 32  ? 39.559 -11.244 -29.839 1.00 55.69  ?  89  GLN A NE2 1 
ATOM   208  N N   A MET A 1 33  ? 37.303 -12.166 -36.201 0.49 22.36  ?  90  MET A N   1 
ATOM   209  N N   B MET A 1 33  ? 37.292 -12.155 -36.199 0.51 22.37  ?  90  MET A N   1 
ATOM   210  C CA  A MET A 1 33  ? 37.393 -13.059 -37.344 0.49 26.25  ?  90  MET A CA  1 
ATOM   211  C CA  B MET A 1 33  ? 37.274 -13.061 -37.338 0.51 26.15  ?  90  MET A CA  1 
ATOM   212  C C   A MET A 1 33  ? 37.535 -12.303 -38.655 0.49 28.26  ?  90  MET A C   1 
ATOM   213  C C   B MET A 1 33  ? 37.064 -12.325 -38.655 0.51 28.33  ?  90  MET A C   1 
ATOM   214  O O   A MET A 1 33  ? 37.905 -12.907 -39.666 0.49 29.89  ?  90  MET A O   1 
ATOM   215  O O   B MET A 1 33  ? 36.705 -12.953 -39.659 0.51 27.42  ?  90  MET A O   1 
ATOM   216  C CB  A MET A 1 33  ? 36.160 -13.955 -37.414 0.49 24.58  ?  90  MET A CB  1 
ATOM   217  C CB  B MET A 1 33  ? 36.186 -14.118 -37.151 0.51 24.50  ?  90  MET A CB  1 
ATOM   218  C CG  A MET A 1 33  ? 35.967 -14.885 -36.226 0.49 25.42  ?  90  MET A CG  1 
ATOM   219  C CG  B MET A 1 33  ? 36.374 -15.019 -35.943 0.51 22.28  ?  90  MET A CG  1 
ATOM   220  S SD  A MET A 1 33  ? 37.135 -16.252 -36.171 0.49 32.71  ?  90  MET A SD  1 
ATOM   221  S SD  B MET A 1 33  ? 34.991 -16.165 -35.777 0.51 28.88  ?  90  MET A SD  1 
ATOM   222  C CE  A MET A 1 33  ? 36.005 -17.635 -36.011 0.49 34.84  ?  90  MET A CE  1 
ATOM   223  C CE  B MET A 1 33  ? 35.498 -17.479 -36.880 0.51 31.37  ?  90  MET A CE  1 
ATOM   224  N N   . GLY A 1 34  ? 37.254 -11.008 -38.659 1.00 24.17  ?  91  GLY A N   1 
ATOM   225  C CA  . GLY A 1 34  ? 37.215 -10.234 -39.878 1.00 28.56  ?  91  GLY A CA  1 
ATOM   226  C C   . GLY A 1 34  ? 35.843 -9.984  -40.463 1.00 25.95  ?  91  GLY A C   1 
ATOM   227  O O   . GLY A 1 34  ? 35.745 -9.708  -41.664 1.00 33.09  ?  91  GLY A O   1 
ATOM   228  N N   A PHE A 1 35  ? 34.774 -10.045 -39.670 0.67 21.63  ?  92  PHE A N   1 
ATOM   229  N N   B PHE A 1 35  ? 34.795 -10.095 -39.647 0.33 21.72  ?  92  PHE A N   1 
ATOM   230  C CA  A PHE A 1 35  ? 33.424 -9.906  -40.200 0.67 22.49  ?  92  PHE A CA  1 
ATOM   231  C CA  B PHE A 1 35  ? 33.413 -9.846  -40.020 0.33 22.63  ?  92  PHE A CA  1 
ATOM   232  C C   A PHE A 1 35  ? 32.735 -8.697  -39.578 0.67 21.66  ?  92  PHE A C   1 
ATOM   233  C C   B PHE A 1 35  ? 33.038 -8.395  -39.774 0.33 22.03  ?  92  PHE A C   1 
ATOM   234  O O   A PHE A 1 35  ? 32.941 -8.396  -38.397 0.67 20.49  ?  92  PHE A O   1 
ATOM   235  O O   B PHE A 1 35  ? 33.695 -7.665  -39.027 0.33 23.83  ?  92  PHE A O   1 
ATOM   236  C CB  A PHE A 1 35  ? 32.579 -11.165 -39.935 0.67 22.59  ?  92  PHE A CB  1 
ATOM   237  C CB  B PHE A 1 35  ? 32.444 -10.693 -39.193 0.33 22.89  ?  92  PHE A CB  1 
ATOM   238  C CG  A PHE A 1 35  ? 33.288 -12.454 -40.249 0.67 23.32  ?  92  PHE A CG  1 
ATOM   239  C CG  B PHE A 1 35  ? 32.208 -12.071 -39.713 0.33 24.05  ?  92  PHE A CG  1 
ATOM   240  C CD1 A PHE A 1 35  ? 34.134 -12.553 -41.349 0.67 28.96  ?  92  PHE A CD1 1 
ATOM   241  C CD1 B PHE A 1 35  ? 31.312 -12.303 -40.742 0.33 26.07  ?  92  PHE A CD1 1 
ATOM   242  C CD2 A PHE A 1 35  ? 33.113 -13.568 -39.449 0.67 27.73  ?  92  PHE A CD2 1 
ATOM   243  C CD2 B PHE A 1 35  ? 32.835 -13.147 -39.118 0.33 24.91  ?  92  PHE A CD2 1 
ATOM   244  C CE1 A PHE A 1 35  ? 34.793 -13.735 -41.640 0.67 36.53  ?  92  PHE A CE1 1 
ATOM   245  C CE1 B PHE A 1 35  ? 31.082 -13.584 -41.193 0.33 22.59  ?  92  PHE A CE1 1 
ATOM   246  C CE2 A PHE A 1 35  ? 33.770 -14.755 -39.736 0.67 32.91  ?  92  PHE A CE2 1 
ATOM   247  C CE2 B PHE A 1 35  ? 32.614 -14.420 -39.563 0.33 30.04  ?  92  PHE A CE2 1 
ATOM   248  C CZ  A PHE A 1 35  ? 34.608 -14.839 -40.831 0.67 34.62  ?  92  PHE A CZ  1 
ATOM   249  C CZ  B PHE A 1 35  ? 31.731 -14.643 -40.595 0.33 24.69  ?  92  PHE A CZ  1 
ATOM   250  N N   . ASN A 1 36  ? 31.933 -8.004  -40.387 1.00 17.97  ?  93  ASN A N   1 
ATOM   251  C CA  . ASN A 1 36  ? 31.104 -6.892  -39.951 1.00 19.44  ?  93  ASN A CA  1 
ATOM   252  C C   . ASN A 1 36  ? 29.805 -7.453  -39.385 1.00 17.96  ?  93  ASN A C   1 
ATOM   253  O O   . ASN A 1 36  ? 29.413 -8.575  -39.715 1.00 18.60  ?  93  ASN A O   1 
ATOM   254  C CB  . ASN A 1 36  ? 30.786 -5.963  -41.118 1.00 23.47  ?  93  ASN A CB  1 
ATOM   255  C CG  . ASN A 1 36  ? 31.923 -5.057  -41.433 1.00 41.94  ?  93  ASN A CG  1 
ATOM   256  O OD1 . ASN A 1 36  ? 32.690 -4.692  -40.543 1.00 43.55  ?  93  ASN A OD1 1 
ATOM   257  N ND2 . ASN A 1 36  ? 32.057 -4.688  -42.703 1.00 51.26  ?  93  ASN A ND2 1 
ATOM   258  N N   . VAL A 1 37  ? 29.135 -6.679  -38.526 1.00 19.40  ?  94  VAL A N   1 
ATOM   259  C CA  . VAL A 1 37  ? 27.831 -7.068  -37.986 1.00 17.00  ?  94  VAL A CA  1 
ATOM   260  C C   . VAL A 1 37  ? 26.862 -5.929  -38.237 1.00 17.84  ?  94  VAL A C   1 
ATOM   261  O O   . VAL A 1 37  ? 27.181 -4.770  -37.950 1.00 21.62  ?  94  VAL A O   1 
ATOM   262  C CB  . VAL A 1 37  ? 27.869 -7.385  -36.474 1.00 16.02  ?  94  VAL A CB  1 
ATOM   263  C CG1 . VAL A 1 37  ? 26.461 -7.757  -35.942 1.00 19.54  ?  94  VAL A CG1 1 
ATOM   264  C CG2 . VAL A 1 37  ? 28.857 -8.497  -36.155 1.00 15.36  ?  94  VAL A CG2 1 
ATOM   265  N N   A VAL A 1 38  ? 25.690 -6.234  -38.793 0.76 14.59  ?  95  VAL A N   1 
ATOM   266  N N   B VAL A 1 38  ? 25.685 -6.276  -38.756 0.24 14.58  ?  95  VAL A N   1 
ATOM   267  C CA  A VAL A 1 38  ? 24.630 -5.235  -38.885 0.76 14.62  ?  95  VAL A CA  1 
ATOM   268  C CA  B VAL A 1 38  ? 24.559 -5.374  -38.969 0.24 14.57  ?  95  VAL A CA  1 
ATOM   269  C C   A VAL A 1 38  ? 23.434 -5.742  -38.097 0.76 15.03  ?  95  VAL A C   1 
ATOM   270  C C   B VAL A 1 38  ? 23.438 -5.800  -38.031 0.24 14.99  ?  95  VAL A C   1 
ATOM   271  O O   A VAL A 1 38  ? 23.091 -6.928  -38.155 0.76 13.90  ?  95  VAL A O   1 
ATOM   272  O O   B VAL A 1 38  ? 23.131 -6.994  -37.938 0.24 14.03  ?  95  VAL A O   1 
ATOM   273  C CB  A VAL A 1 38  ? 24.247 -4.883  -40.339 0.76 17.01  ?  95  VAL A CB  1 
ATOM   274  C CB  B VAL A 1 38  ? 24.101 -5.423  -40.435 0.24 16.39  ?  95  VAL A CB  1 
ATOM   275  C CG1 A VAL A 1 38  ? 25.402 -4.134  -41.017 0.76 18.35  ?  95  VAL A CG1 1 
ATOM   276  C CG1 B VAL A 1 38  ? 22.761 -4.795  -40.581 0.24 19.40  ?  95  VAL A CG1 1 
ATOM   277  C CG2 A VAL A 1 38  ? 23.814 -6.104  -41.133 0.76 14.73  ?  95  VAL A CG2 1 
ATOM   278  C CG2 B VAL A 1 38  ? 25.108 -4.715  -41.329 0.24 19.75  ?  95  VAL A CG2 1 
ATOM   279  N N   . ILE A 1 39  ? 22.820 -4.839  -37.337 1.00 15.29  ?  96  ILE A N   1 
ATOM   280  C CA  . ILE A 1 39  ? 21.849 -5.172  -36.296 1.00 14.23  ?  96  ILE A CA  1 
ATOM   281  C C   . ILE A 1 39  ? 20.487 -4.586  -36.653 1.00 14.58  ?  96  ILE A C   1 
ATOM   282  O O   . ILE A 1 39  ? 20.394 -3.442  -37.116 1.00 15.69  ?  96  ILE A O   1 
ATOM   283  C CB  . ILE A 1 39  ? 22.334 -4.663  -34.920 1.00 14.56  ?  96  ILE A CB  1 
ATOM   284  C CG1 . ILE A 1 39  ? 23.726 -5.243  -34.619 1.00 15.34  ?  96  ILE A CG1 1 
ATOM   285  C CG2 . ILE A 1 39  ? 21.305 -4.949  -33.824 1.00 17.81  ?  96  ILE A CG2 1 
ATOM   286  C CD1 . ILE A 1 39  ? 24.605 -4.295  -33.840 1.00 20.27  ?  96  ILE A CD1 1 
ATOM   287  N N   . SER A 1 40  ? 19.433 -5.373  -36.435 1.00 14.38  ?  97  SER A N   1 
ATOM   288  C CA  . SER A 1 40  ? 18.045 -4.932  -36.591 1.00 14.91  ?  97  SER A CA  1 
ATOM   289  C C   . SER A 1 40  ? 17.325 -5.219  -35.281 1.00 16.54  ?  97  SER A C   1 
ATOM   290  O O   . SER A 1 40  ? 17.366 -6.352  -34.802 1.00 16.11  ?  97  SER A O   1 
ATOM   291  C CB  . SER A 1 40  ? 17.369 -5.659  -37.781 1.00 18.06  ?  97  SER A CB  1 
ATOM   292  O OG  . SER A 1 40  ? 16.034 -5.199  -38.019 1.00 23.39  ?  97  SER A OG  1 
ATOM   293  N N   . MET A 1 41  ? 16.689 -4.202  -34.699 1.00 15.91  ?  98  MET A N   1 
ATOM   294  C CA  . MET A 1 41  ? 15.924 -4.334  -33.457 1.00 17.32  ?  98  MET A CA  1 
ATOM   295  C C   . MET A 1 41  ? 14.468 -4.659  -33.750 1.00 20.17  ?  98  MET A C   1 
ATOM   296  O O   . MET A 1 41  ? 13.832 -3.989  -34.564 1.00 22.06  ?  98  MET A O   1 
ATOM   297  C CB  . MET A 1 41  ? 15.950 -3.047  -32.637 1.00 19.02  ?  98  MET A CB  1 
ATOM   298  C CG  . MET A 1 41  ? 15.647 -3.264  -31.133 1.00 17.56  ?  98  MET A CG  1 
ATOM   299  S SD  . MET A 1 41  ? 15.971 -1.835  -30.081 1.00 23.31  ?  98  MET A SD  1 
ATOM   300  C CE  . MET A 1 41  ? 14.305 -1.180  -30.016 1.00 26.81  ?  98  MET A CE  1 
ATOM   301  N N   . VAL A 1 42  ? 13.921 -5.619  -33.005 1.00 19.33  ?  99  VAL A N   1 
ATOM   302  C CA  . VAL A 1 42  ? 12.626 -6.231  -33.273 1.00 20.49  ?  99  VAL A CA  1 
ATOM   303  C C   . VAL A 1 42  ? 11.714 -6.059  -32.062 1.00 30.33  ?  99  VAL A C   1 
ATOM   304  O O   . VAL A 1 42  ? 12.164 -6.200  -30.922 1.00 28.43  ?  99  VAL A O   1 
ATOM   305  C CB  . VAL A 1 42  ? 12.804 -7.730  -33.602 1.00 25.45  ?  99  VAL A CB  1 
ATOM   306  C CG1 . VAL A 1 42  ? 11.623 -8.252  -34.355 1.00 36.56  ?  99  VAL A CG1 1 
ATOM   307  C CG2 . VAL A 1 42  ? 14.068 -7.955  -34.413 1.00 28.73  ?  99  VAL A CG2 1 
ATOM   308  N N   . GLU A 1 43  ? 10.437 -5.753  -32.307 1.00 25.78  ?  100 GLU A N   1 
ATOM   309  C CA  . GLU A 1 43  ? 9.396  -5.936  -31.301 1.00 27.93  ?  100 GLU A CA  1 
ATOM   310  C C   . GLU A 1 43  ? 8.963  -7.401  -31.282 1.00 28.73  ?  100 GLU A C   1 
ATOM   311  O O   . GLU A 1 43  ? 9.467  -8.231  -32.041 1.00 34.26  ?  100 GLU A O   1 
ATOM   312  C CB  . GLU A 1 43  ? 8.184  -5.047  -31.577 1.00 33.72  ?  100 GLU A CB  1 
ATOM   313  C CG  . GLU A 1 43  ? 8.500  -3.599  -31.907 1.00 45.11  ?  100 GLU A CG  1 
ATOM   314  C CD  . GLU A 1 43  ? 9.208  -2.888  -30.774 1.00 64.18  ?  100 GLU A CD  1 
ATOM   315  O OE1 . GLU A 1 43  ? 8.795  -3.075  -29.609 1.00 66.65  ?  100 GLU A OE1 1 
ATOM   316  O OE2 . GLU A 1 43  ? 10.169 -2.134  -31.050 1.00 67.61  -1 100 GLU A OE2 1 
ATOM   317  N N   . GLN A 1 44  ? 7.986  -7.727  -30.441 1.00 28.79  ?  101 GLN A N   1 
ATOM   318  C CA  . GLN A 1 44  ? 7.619  -9.124  -30.257 1.00 34.86  ?  101 GLN A CA  1 
ATOM   319  C C   . GLN A 1 44  ? 6.799  -9.627  -31.439 1.00 30.53  ?  101 GLN A C   1 
ATOM   320  O O   . GLN A 1 44  ? 6.099  -8.860  -32.102 1.00 29.90  ?  101 GLN A O   1 
ATOM   321  C CB  . GLN A 1 44  ? 6.834  -9.311  -28.954 1.00 40.40  ?  101 GLN A CB  1 
ATOM   322  C CG  . GLN A 1 44  ? 7.582  -8.875  -27.683 1.00 46.41  ?  101 GLN A CG  1 
ATOM   323  C CD  . GLN A 1 44  ? 8.917  -9.596  -27.456 1.00 56.40  ?  101 GLN A CD  1 
ATOM   324  O OE1 . GLN A 1 44  ? 9.204  -10.634 -28.059 1.00 54.95  ?  101 GLN A OE1 1 
ATOM   325  N NE2 . GLN A 1 44  ? 9.740  -9.035  -26.579 1.00 37.04  ?  101 GLN A NE2 1 
ATOM   326  N N   . GLY A 1 45  ? 6.910  -10.918 -31.710 1.00 34.78  ?  102 GLY A N   1 
ATOM   327  C CA  . GLY A 1 45  ? 6.023  -11.544 -32.668 1.00 28.76  ?  102 GLY A CA  1 
ATOM   328  C C   . GLY A 1 45  ? 6.742  -11.990 -33.931 1.00 25.72  ?  102 GLY A C   1 
ATOM   329  O O   . GLY A 1 45  ? 7.766  -11.423 -34.337 1.00 23.48  ?  102 GLY A O   1 
ATOM   330  N N   . VAL A 1 46  ? 6.171  -13.004 -34.588 1.00 24.31  ?  103 VAL A N   1 
ATOM   331  C CA  . VAL A 1 46  ? 6.827  -13.585 -35.755 1.00 26.16  ?  103 VAL A CA  1 
ATOM   332  C C   . VAL A 1 46  ? 6.837  -12.597 -36.924 1.00 26.51  ?  103 VAL A C   1 
ATOM   333  O O   . VAL A 1 46  ? 7.809  -12.536 -37.686 1.00 23.31  ?  103 VAL A O   1 
ATOM   334  C CB  . VAL A 1 46  ? 6.165  -14.928 -36.126 1.00 32.11  ?  103 VAL A CB  1 
ATOM   335  C CG1 . VAL A 1 46  ? 4.676  -14.764 -36.328 1.00 40.79  ?  103 VAL A CG1 1 
ATOM   336  C CG2 . VAL A 1 46  ? 6.810  -15.526 -37.370 1.00 42.00  ?  103 VAL A CG2 1 
ATOM   337  N N   . GLU A 1 47  ? 5.777  -11.793 -37.084 1.00 24.76  ?  104 GLU A N   1 
ATOM   338  C CA  . GLU A 1 47  ? 5.781  -10.822 -38.178 1.00 25.05  ?  104 GLU A CA  1 
ATOM   339  C C   . GLU A 1 47  ? 6.919  -9.819  -38.037 1.00 23.92  ?  104 GLU A C   1 
ATOM   340  O O   . GLU A 1 47  ? 7.590  -9.486  -39.022 1.00 22.87  ?  104 GLU A O   1 
ATOM   341  C CB  . GLU A 1 47  ? 4.449  -10.080 -38.257 1.00 29.42  ?  104 GLU A CB  1 
ATOM   342  C CG  . GLU A 1 47  ? 4.445  -9.124  -39.435 1.00 32.89  ?  104 GLU A CG  1 
ATOM   343  C CD  . GLU A 1 47  ? 4.469  -9.880  -40.751 1.00 54.03  ?  104 GLU A CD  1 
ATOM   344  O OE1 . GLU A 1 47  ? 3.724  -10.880 -40.871 1.00 44.40  ?  104 GLU A OE1 1 
ATOM   345  O OE2 . GLU A 1 47  ? 5.247  -9.488  -41.650 1.00 61.04  -1 104 GLU A OE2 1 
ATOM   346  N N   . ALA A 1 48  ? 7.134  -9.309  -36.829 1.00 22.70  ?  105 ALA A N   1 
ATOM   347  C CA  . ALA A 1 48  ? 8.204  -8.345  -36.631 1.00 21.40  ?  105 ALA A CA  1 
ATOM   348  C C   . ALA A 1 48  ? 9.558  -8.989  -36.879 1.00 21.42  ?  105 ALA A C   1 
ATOM   349  O O   . ALA A 1 48  ? 10.475 -8.354  -37.417 1.00 22.86  ?  105 ALA A O   1 
ATOM   350  C CB  . ALA A 1 48  ? 8.128  -7.774  -35.220 1.00 21.57  ?  105 ALA A CB  1 
ATOM   351  N N   A CYS A 1 49  ? 9.702  -10.255 -36.511 0.73 19.63  ?  106 CYS A N   1 
ATOM   352  N N   B CYS A 1 49  ? 9.708  -10.250 -36.475 0.27 19.61  ?  106 CYS A N   1 
ATOM   353  C CA  A CYS A 1 49  ? 10.978 -10.918 -36.742 0.73 19.81  ?  106 CYS A CA  1 
ATOM   354  C CA  B CYS A 1 49  ? 10.939 -10.980 -36.755 0.27 20.12  ?  106 CYS A CA  1 
ATOM   355  C C   A CYS A 1 49  ? 11.195 -11.190 -38.230 0.73 20.66  ?  106 CYS A C   1 
ATOM   356  C C   B CYS A 1 49  ? 11.165 -11.107 -38.246 0.27 20.71  ?  106 CYS A C   1 
ATOM   357  O O   A CYS A 1 49  ? 12.322 -11.084 -38.719 0.73 21.15  ?  106 CYS A O   1 
ATOM   358  O O   B CYS A 1 49  ? 12.264 -10.847 -38.748 0.27 20.75  ?  106 CYS A O   1 
ATOM   359  C CB  A CYS A 1 49  ? 11.053 -12.210 -35.922 0.73 20.34  ?  106 CYS A CB  1 
ATOM   360  C CB  B CYS A 1 49  ? 10.873 -12.368 -36.135 0.27 20.51  ?  106 CYS A CB  1 
ATOM   361  S SG  A CYS A 1 49  ? 12.747 -12.842 -35.684 0.73 20.63  ?  106 CYS A SG  1 
ATOM   362  S SG  B CYS A 1 49  ? 11.094 -12.331 -34.409 0.27 19.64  ?  106 CYS A SG  1 
ATOM   363  N N   . LYS A 1 50  ? 10.134 -11.541 -38.962 1.00 20.35  ?  107 LYS A N   1 
ATOM   364  C CA  . LYS A 1 50  ? 10.245 -11.718 -40.406 1.00 20.76  ?  107 LYS A CA  1 
ATOM   365  C C   . LYS A 1 50  ? 10.654 -10.414 -41.073 1.00 24.52  ?  107 LYS A C   1 
ATOM   366  O O   . LYS A 1 50  ? 11.510 -10.404 -41.966 1.00 23.56  ?  107 LYS A O   1 
ATOM   367  C CB  . LYS A 1 50  ? 8.905  -12.201 -40.959 1.00 22.68  ?  107 LYS A CB  1 
ATOM   368  C CG  . LYS A 1 50  ? 8.607  -13.672 -40.693 1.00 26.66  ?  107 LYS A CG  1 
ATOM   369  C CD  . LYS A 1 50  ? 7.177  -14.001 -41.087 1.00 37.51  ?  107 LYS A CD  1 
ATOM   370  C CE  . LYS A 1 50  ? 7.134  -15.066 -42.152 1.00 45.29  ?  107 LYS A CE  1 
ATOM   371  N NZ  . LYS A 1 50  ? 5.730  -15.436 -42.477 1.00 46.36  ?  107 LYS A NZ  1 
ATOM   372  N N   . ALA A 1 51  ? 10.071 -9.294  -40.627 1.00 21.96  ?  108 ALA A N   1 
ATOM   373  C CA  . ALA A 1 51  ? 10.436 -7.996  -41.184 1.00 23.93  ?  108 ALA A CA  1 
ATOM   374  C C   . ALA A 1 51  ? 11.908 -7.679  -40.938 1.00 23.12  ?  108 ALA A C   1 
ATOM   375  O O   . ALA A 1 51  ? 12.587 -7.147  -41.821 1.00 21.95  ?  108 ALA A O   1 
ATOM   376  C CB  . ALA A 1 51  ? 9.541  -6.905  -40.598 1.00 23.91  ?  108 ALA A CB  1 
ATOM   377  N N   . ALA A 1 52  ? 12.425 -8.011  -39.750 1.00 20.87  ?  109 ALA A N   1 
ATOM   378  C CA  . ALA A 1 52  ? 13.844 -7.794  -39.490 1.00 17.84  ?  109 ALA A CA  1 
ATOM   379  C C   . ALA A 1 52  ? 14.708 -8.666  -40.388 1.00 20.25  ?  109 ALA A C   1 
ATOM   380  O O   . ALA A 1 52  ? 15.721 -8.201  -40.923 1.00 18.75  ?  109 ALA A O   1 
ATOM   381  C CB  . ALA A 1 52  ? 14.165 -8.073  -38.024 1.00 19.07  ?  109 ALA A CB  1 
ATOM   382  N N   . VAL A 1 53  ? 14.329 -9.933  -40.554 1.00 16.96  ?  110 VAL A N   1 
ATOM   383  C CA  . VAL A 1 53  ? 15.083 -10.825 -41.430 1.00 17.36  ?  110 VAL A CA  1 
ATOM   384  C C   . VAL A 1 53  ? 15.105 -10.272 -42.849 1.00 19.49  ?  110 VAL A C   1 
ATOM   385  O O   . VAL A 1 53  ? 16.153 -10.264 -43.508 1.00 20.58  ?  110 VAL A O   1 
ATOM   386  C CB  . VAL A 1 53  ? 14.497 -12.249 -41.364 1.00 21.65  ?  110 VAL A CB  1 
ATOM   387  C CG1 . VAL A 1 53  ? 14.926 -13.086 -42.577 1.00 25.60  ?  110 VAL A CG1 1 
ATOM   388  C CG2 . VAL A 1 53  ? 14.905 -12.916 -40.052 1.00 23.03  ?  110 VAL A CG2 1 
ATOM   389  N N   . ASN A 1 54  ? 13.969 -9.751  -43.322 1.00 19.55  ?  111 ASN A N   1 
ATOM   390  C CA  . ASN A 1 54  ? 13.938 -9.183  -44.668 1.00 21.70  ?  111 ASN A CA  1 
ATOM   391  C C   . ASN A 1 54  ? 14.813 -7.936  -44.769 1.00 18.93  ?  111 ASN A C   1 
ATOM   392  O O   . ASN A 1 54  ? 15.486 -7.727  -45.792 1.00 23.95  ?  111 ASN A O   1 
ATOM   393  C CB  . ASN A 1 54  ? 12.502 -8.871  -45.068 1.00 24.75  ?  111 ASN A CB  1 
ATOM   394  C CG  . ASN A 1 54  ? 11.723 -10.118 -45.453 1.00 28.77  ?  111 ASN A CG  1 
ATOM   395  O OD1 . ASN A 1 54  ? 12.294 -11.096 -45.937 1.00 32.11  ?  111 ASN A OD1 1 
ATOM   396  N ND2 . ASN A 1 54  ? 10.411 -10.091 -45.231 1.00 34.06  ?  111 ASN A ND2 1 
ATOM   397  N N   . SER A 1 55  ? 14.831 -7.105  -43.723 1.00 18.08  ?  112 SER A N   1 
ATOM   398  C CA  . SER A 1 55  ? 15.731 -5.953  -43.728 1.00 19.90  ?  112 SER A CA  1 
ATOM   399  C C   . SER A 1 55  ? 17.184 -6.397  -43.799 1.00 20.22  ?  112 SER A C   1 
ATOM   400  O O   . SER A 1 55  ? 17.989 -5.817  -44.539 1.00 24.67  ?  112 SER A O   1 
ATOM   401  C CB  . SER A 1 55  ? 15.510 -5.104  -42.479 1.00 20.98  ?  112 SER A CB  1 
ATOM   402  O OG  . SER A 1 55  ? 16.408 -3.993  -42.456 1.00 24.23  ?  112 SER A OG  1 
ATOM   403  N N   . LEU A 1 56  ? 17.546 -7.417  -43.020 1.00 18.81  ?  113 LEU A N   1 
ATOM   404  C CA  . LEU A 1 56  ? 18.931 -7.876  -43.005 1.00 19.29  ?  113 LEU A CA  1 
ATOM   405  C C   . LEU A 1 56  ? 19.326 -8.539  -44.322 1.00 17.99  ?  113 LEU A C   1 
ATOM   406  O O   . LEU A 1 56  ? 20.466 -8.373  -44.786 1.00 21.41  ?  113 LEU A O   1 
ATOM   407  C CB  . LEU A 1 56  ? 19.135 -8.824  -41.824 1.00 16.70  ?  113 LEU A CB  1 
ATOM   408  C CG  . LEU A 1 56  ? 19.022 -8.134  -40.462 1.00 16.20  ?  113 LEU A CG  1 
ATOM   409  C CD1 . LEU A 1 56  ? 18.883 -9.177  -39.370 1.00 16.78  ?  113 LEU A CD1 1 
ATOM   410  C CD2 . LEU A 1 56  ? 20.215 -7.208  -40.177 1.00 16.13  ?  113 LEU A CD2 1 
ATOM   411  N N   . LEU A 1 57  ? 18.414 -9.306  -44.938 1.00 19.15  ?  114 LEU A N   1 
ATOM   412  C CA  . LEU A 1 57  ? 18.710 -9.873  -46.250 1.00 20.91  ?  114 LEU A CA  1 
ATOM   413  C C   . LEU A 1 57  ? 18.900 -8.775  -47.292 1.00 23.58  ?  114 LEU A C   1 
ATOM   414  O O   . LEU A 1 57  ? 19.714 -8.929  -48.212 1.00 24.07  ?  114 LEU A O   1 
ATOM   415  C CB  . LEU A 1 57  ? 17.598 -10.836 -46.686 1.00 20.36  ?  114 LEU A CB  1 
ATOM   416  C CG  . LEU A 1 57  ? 17.413 -12.108 -45.840 1.00 24.19  ?  114 LEU A CG  1 
ATOM   417  C CD1 . LEU A 1 57  ? 16.193 -12.918 -46.298 1.00 27.39  ?  114 LEU A CD1 1 
ATOM   418  C CD2 . LEU A 1 57  ? 18.665 -12.978 -45.825 1.00 26.94  ?  114 LEU A CD2 1 
ATOM   419  N N   . ALA A 1 58  ? 18.179 -7.656  -47.161 1.00 21.66  ?  115 ALA A N   1 
ATOM   420  C CA  . ALA A 1 58  ? 18.390 -6.535  -48.068 1.00 26.54  ?  115 ALA A CA  1 
ATOM   421  C C   . ALA A 1 58  ? 19.750 -5.875  -47.880 1.00 24.81  ?  115 ALA A C   1 
ATOM   422  O O   . ALA A 1 58  ? 20.200 -5.141  -48.771 1.00 24.93  ?  115 ALA A O   1 
ATOM   423  C CB  . ALA A 1 58  ? 17.294 -5.486  -47.891 1.00 22.14  ?  115 ALA A CB  1 
ATOM   424  N N   . GLN A 1 59  ? 20.395 -6.085  -46.738 1.00 23.38  ?  116 GLN A N   1 
ATOM   425  C CA  . GLN A 1 59  ? 21.782 -5.682  -46.557 1.00 21.10  ?  116 GLN A CA  1 
ATOM   426  C C   . GLN A 1 59  ? 22.768 -6.707  -47.109 1.00 25.46  ?  116 GLN A C   1 
ATOM   427  O O   . GLN A 1 59  ? 23.984 -6.511  -46.969 1.00 25.06  ?  116 GLN A O   1 
ATOM   428  C CB  . GLN A 1 59  ? 22.067 -5.419  -45.070 1.00 21.49  ?  116 GLN A CB  1 
ATOM   429  C CG  . GLN A 1 59  ? 21.204 -4.345  -44.431 1.00 20.34  ?  116 GLN A CG  1 
ATOM   430  C CD  . GLN A 1 59  ? 21.482 -2.983  -45.018 1.00 32.85  ?  116 GLN A CD  1 
ATOM   431  O OE1 . GLN A 1 59  ? 22.632 -2.521  -45.028 1.00 30.40  ?  116 GLN A OE1 1 
ATOM   432  N NE2 . GLN A 1 59  ? 20.438 -2.337  -45.529 1.00 30.69  ?  116 GLN A NE2 1 
ATOM   433  N N   . ARG A 1 60  ? 22.272 -7.782  -47.738 1.00 21.66  ?  117 ARG A N   1 
ATOM   434  C CA  . ARG A 1 60  ? 23.104 -8.795  -48.392 1.00 25.23  ?  117 ARG A CA  1 
ATOM   435  C C   . ARG A 1 60  ? 23.997 -9.533  -47.390 1.00 23.89  ?  117 ARG A C   1 
ATOM   436  O O   . ARG A 1 60  ? 25.158 -9.843  -47.682 1.00 24.77  ?  117 ARG A O   1 
ATOM   437  C CB  . ARG A 1 60  ? 23.963 -8.182  -49.506 1.00 23.27  ?  117 ARG A CB  1 
ATOM   438  C CG  . ARG A 1 60  ? 23.264 -7.129  -50.370 1.00 31.26  ?  117 ARG A CG  1 
ATOM   439  C CD  . ARG A 1 60  ? 22.305 -7.745  -51.323 1.00 30.59  ?  117 ARG A CD  1 
ATOM   440  N NE  . ARG A 1 60  ? 21.780 -6.814  -52.318 1.00 28.68  ?  117 ARG A NE  1 
ATOM   441  C CZ  . ARG A 1 60  ? 20.769 -7.123  -53.114 1.00 28.06  ?  117 ARG A CZ  1 
ATOM   442  N NH1 . ARG A 1 60  ? 20.172 -8.302  -53.036 1.00 30.72  ?  117 ARG A NH1 1 
ATOM   443  N NH2 . ARG A 1 60  ? 20.337 -6.227  -54.000 1.00 26.05  ?  117 ARG A NH2 1 
ATOM   444  N N   . VAL A 1 61  ? 23.467 -9.832  -46.197 1.00 22.00  ?  118 VAL A N   1 
ATOM   445  C CA  . VAL A 1 61  ? 24.324 -10.468 -45.181 1.00 18.52  ?  118 VAL A CA  1 
ATOM   446  C C   . VAL A 1 61  ? 24.622 -11.918 -45.563 1.00 19.48  ?  118 VAL A C   1 
ATOM   447  O O   . VAL A 1 61  ? 23.894 -12.564 -46.329 1.00 23.97  ?  118 VAL A O   1 
ATOM   448  C CB  . VAL A 1 61  ? 23.709 -10.385 -43.771 1.00 18.09  ?  118 VAL A CB  1 
ATOM   449  C CG1 . VAL A 1 61  ? 23.483 -8.921  -43.365 1.00 18.23  ?  118 VAL A CG1 1 
ATOM   450  C CG2 . VAL A 1 61  ? 22.410 -11.163 -43.704 1.00 21.66  ?  118 VAL A CG2 1 
ATOM   451  N N   . ASP A 1 62  ? 25.742 -12.428 -45.026 1.00 18.98  ?  119 ASP A N   1 
ATOM   452  C CA  . ASP A 1 62  ? 26.168 -13.795 -45.296 1.00 19.45  ?  119 ASP A CA  1 
ATOM   453  C C   . ASP A 1 62  ? 25.461 -14.816 -44.408 1.00 19.97  ?  119 ASP A C   1 
ATOM   454  O O   . ASP A 1 62  ? 25.279 -15.968 -44.821 1.00 21.66  ?  119 ASP A O   1 
ATOM   455  C CB  . ASP A 1 62  ? 27.681 -13.905 -45.099 1.00 21.06  ?  119 ASP A CB  1 
ATOM   456  C CG  . ASP A 1 62  ? 28.469 -13.036 -46.089 1.00 27.10  ?  119 ASP A CG  1 
ATOM   457  O OD1 . ASP A 1 62  ? 28.602 -11.815 -45.862 1.00 30.77  ?  119 ASP A OD1 1 
ATOM   458  O OD2 . ASP A 1 62  ? 28.956 -13.577 -47.103 1.00 45.13  -1 119 ASP A OD2 1 
ATOM   459  N N   . GLY A 1 63  ? 25.061 -14.418 -43.204 1.00 18.63  ?  120 GLY A N   1 
ATOM   460  C CA  . GLY A 1 63  ? 24.480 -15.338 -42.238 1.00 18.98  ?  120 GLY A CA  1 
ATOM   461  C C   . GLY A 1 63  ? 23.708 -14.533 -41.216 1.00 16.20  ?  120 GLY A C   1 
ATOM   462  O O   . GLY A 1 63  ? 23.903 -13.319 -41.100 1.00 16.92  ?  120 GLY A O   1 
ATOM   463  N N   . LEU A 1 64  ? 22.816 -15.211 -40.476 1.00 15.67  ?  121 LEU A N   1 
ATOM   464  C CA  . LEU A 1 64  ? 21.918 -14.556 -39.519 1.00 14.99  ?  121 LEU A CA  1 
ATOM   465  C C   . LEU A 1 64  ? 21.999 -15.179 -38.131 1.00 16.08  ?  121 LEU A C   1 
ATOM   466  O O   . LEU A 1 64  ? 22.056 -16.405 -37.992 1.00 18.25  ?  121 LEU A O   1 
ATOM   467  C CB  . LEU A 1 64  ? 20.473 -14.634 -40.000 1.00 17.07  ?  121 LEU A CB  1 
ATOM   468  C CG  . LEU A 1 64  ? 20.204 -13.904 -41.320 1.00 18.19  ?  121 LEU A CG  1 
ATOM   469  C CD1 . LEU A 1 64  ? 18.995 -14.469 -42.055 1.00 22.51  ?  121 LEU A CD1 1 
ATOM   470  C CD2 . LEU A 1 64  ? 19.953 -12.446 -40.984 1.00 20.56  ?  121 LEU A CD2 1 
ATOM   471  N N   . ILE A 1 65  ? 21.975 -14.326 -37.109 1.00 16.54  ?  122 ILE A N   1 
ATOM   472  C CA  . ILE A 1 65  ? 21.795 -14.750 -35.721 1.00 16.92  ?  122 ILE A CA  1 
ATOM   473  C C   . ILE A 1 65  ? 20.556 -14.048 -35.185 1.00 18.74  ?  122 ILE A C   1 
ATOM   474  O O   . ILE A 1 65  ? 20.425 -12.830 -35.333 1.00 16.37  ?  122 ILE A O   1 
ATOM   475  C CB  . ILE A 1 65  ? 23.036 -14.429 -34.867 1.00 15.31  ?  122 ILE A CB  1 
ATOM   476  C CG1 . ILE A 1 65  ? 24.263 -15.154 -35.439 1.00 16.07  ?  122 ILE A CG1 1 
ATOM   477  C CG2 . ILE A 1 65  ? 22.777 -14.730 -33.371 1.00 18.54  ?  122 ILE A CG2 1 
ATOM   478  C CD1 . ILE A 1 65  ? 25.580 -14.781 -34.733 1.00 19.30  ?  122 ILE A CD1 1 
ATOM   479  N N   . ILE A 1 66  ? 19.631 -14.815 -34.611 1.00 16.87  ?  123 ILE A N   1 
ATOM   480  C CA  . ILE A 1 66  ? 18.346 -14.300 -34.132 1.00 13.71  ?  123 ILE A CA  1 
ATOM   481  C C   . ILE A 1 66  ? 18.341 -14.381 -32.611 1.00 17.90  ?  123 ILE A C   1 
ATOM   482  O O   . ILE A 1 66  ? 18.194 -15.473 -32.043 1.00 19.14  ?  123 ILE A O   1 
ATOM   483  C CB  . ILE A 1 66  ? 17.162 -15.093 -34.712 1.00 19.75  ?  123 ILE A CB  1 
ATOM   484  C CG1 . ILE A 1 66  ? 17.297 -15.263 -36.223 1.00 24.14  ?  123 ILE A CG1 1 
ATOM   485  C CG2 . ILE A 1 66  ? 15.851 -14.438 -34.339 1.00 18.85  ?  123 ILE A CG2 1 
ATOM   486  C CD1 . ILE A 1 66  ? 17.165 -13.989 -36.995 1.00 24.67  ?  123 ILE A CD1 1 
ATOM   487  N N   . ASN A 1 67  ? 18.447 -13.242 -31.933 1.00 16.36  ?  124 ASN A N   1 
ATOM   488  C CA  . ASN A 1 67  ? 18.244 -13.223 -30.479 1.00 17.21  ?  124 ASN A CA  1 
ATOM   489  C C   . ASN A 1 67  ? 16.889 -12.596 -30.153 1.00 16.27  ?  124 ASN A C   1 
ATOM   490  O O   . ASN A 1 67  ? 16.801 -11.460 -29.663 1.00 17.64  ?  124 ASN A O   1 
ATOM   491  C CB  . ASN A 1 67  ? 19.351 -12.501 -29.760 1.00 16.86  ?  124 ASN A CB  1 
ATOM   492  C CG  . ASN A 1 67  ? 19.195 -12.622 -28.251 1.00 17.31  ?  124 ASN A CG  1 
ATOM   493  O OD1 . ASN A 1 67  ? 18.586 -13.591 -27.782 1.00 20.79  ?  124 ASN A OD1 1 
ATOM   494  N ND2 . ASN A 1 67  ? 19.702 -11.656 -27.496 1.00 20.64  ?  124 ASN A ND2 1 
ATOM   495  N N   . VAL A 1 68  ? 15.834 -13.373 -30.384 1.00 17.22  ?  125 VAL A N   1 
ATOM   496  C CA  . VAL A 1 68  ? 14.442 -12.976 -30.158 1.00 19.86  ?  125 VAL A CA  1 
ATOM   497  C C   . VAL A 1 68  ? 13.726 -14.182 -29.565 1.00 19.44  ?  125 VAL A C   1 
ATOM   498  O O   . VAL A 1 68  ? 13.870 -15.280 -30.120 1.00 20.11  ?  125 VAL A O   1 
ATOM   499  C CB  . VAL A 1 68  ? 13.769 -12.543 -31.469 1.00 22.54  ?  125 VAL A CB  1 
ATOM   500  C CG1 . VAL A 1 68  ? 12.334 -12.160 -31.206 1.00 21.27  ?  125 VAL A CG1 1 
ATOM   501  C CG2 . VAL A 1 68  ? 14.558 -11.419 -32.134 1.00 22.28  ?  125 VAL A CG2 1 
ATOM   502  N N   . PRO A 1 69  ? 12.969 -14.064 -28.467 1.00 21.54  ?  126 PRO A N   1 
ATOM   503  C CA  . PRO A 1 69  ? 12.333 -15.268 -27.889 1.00 21.64  ?  126 PRO A CA  1 
ATOM   504  C C   . PRO A 1 69  ? 11.186 -15.748 -28.769 1.00 23.16  ?  126 PRO A C   1 
ATOM   505  O O   . PRO A 1 69  ? 10.233 -15.011 -29.019 1.00 26.20  ?  126 PRO A O   1 
ATOM   506  C CB  . PRO A 1 69  ? 11.843 -14.794 -26.513 1.00 22.06  ?  126 PRO A CB  1 
ATOM   507  C CG  . PRO A 1 69  ? 11.705 -13.308 -26.646 1.00 26.11  ?  126 PRO A CG  1 
ATOM   508  C CD  . PRO A 1 69  ? 12.736 -12.857 -27.640 1.00 22.97  ?  126 PRO A CD  1 
ATOM   509  N N   . LEU A 1 70  ? 11.278 -16.998 -29.235 1.00 22.15  ?  127 LEU A N   1 
ATOM   510  C CA  . LEU A 1 70  ? 10.314 -17.538 -30.186 1.00 24.71  ?  127 LEU A CA  1 
ATOM   511  C C   . LEU A 1 70  ? 9.933  -18.949 -29.774 1.00 27.90  ?  127 LEU A C   1 
ATOM   512  O O   . LEU A 1 70  ? 10.797 -19.730 -29.370 1.00 23.21  ?  127 LEU A O   1 
ATOM   513  C CB  . LEU A 1 70  ? 10.902 -17.575 -31.608 1.00 22.58  ?  127 LEU A CB  1 
ATOM   514  C CG  . LEU A 1 70  ? 11.303 -16.244 -32.236 1.00 25.56  ?  127 LEU A CG  1 
ATOM   515  C CD1 . LEU A 1 70  ? 12.102 -16.512 -33.493 1.00 27.95  ?  127 LEU A CD1 1 
ATOM   516  C CD2 . LEU A 1 70  ? 10.069 -15.418 -32.542 1.00 26.79  ?  127 LEU A CD2 1 
ATOM   517  N N   . GLU A 1 71  ? 8.648  -19.281 -29.888 1.00 27.90  ?  128 GLU A N   1 
ATOM   518  C CA  . GLU A 1 71  ? 8.280  -20.689 -29.909 1.00 35.63  ?  128 GLU A CA  1 
ATOM   519  C C   . GLU A 1 71  ? 8.815  -21.314 -31.187 1.00 41.79  ?  128 GLU A C   1 
ATOM   520  O O   . GLU A 1 71  ? 8.993  -20.634 -32.201 1.00 37.08  ?  128 GLU A O   1 
ATOM   521  C CB  . GLU A 1 71  ? 6.766  -20.866 -29.818 1.00 38.76  ?  128 GLU A CB  1 
ATOM   522  C CG  . GLU A 1 71  ? 6.116  -19.970 -28.780 1.00 50.46  ?  128 GLU A CG  1 
ATOM   523  C CD  . GLU A 1 71  ? 6.198  -20.538 -27.374 1.00 52.43  ?  128 GLU A CD  1 
ATOM   524  O OE1 . GLU A 1 71  ? 7.009  -21.460 -27.138 1.00 54.98  ?  128 GLU A OE1 1 
ATOM   525  O OE2 . GLU A 1 71  ? 5.460  -20.044 -26.493 1.00 77.71  -1 128 GLU A OE2 1 
ATOM   526  N N   . ASN A 1 72  ? 9.087  -22.621 -31.134 1.00 48.81  ?  129 ASN A N   1 
ATOM   527  C CA  . ASN A 1 72  ? 9.787  -23.249 -32.250 1.00 55.71  ?  129 ASN A CA  1 
ATOM   528  C C   . ASN A 1 72  ? 8.971  -23.181 -33.538 1.00 37.26  ?  129 ASN A C   1 
ATOM   529  O O   . ASN A 1 72  ? 9.548  -23.112 -34.630 1.00 41.04  ?  129 ASN A O   1 
ATOM   530  C CB  . ASN A 1 72  ? 10.145 -24.697 -31.909 1.00 64.14  ?  129 ASN A CB  1 
ATOM   531  C CG  . ASN A 1 72  ? 11.181 -25.282 -32.859 1.00 61.63  ?  129 ASN A CG  1 
ATOM   532  O OD1 . ASN A 1 72  ? 12.127 -24.602 -33.261 1.00 68.87  ?  129 ASN A OD1 1 
ATOM   533  N ND2 . ASN A 1 72  ? 11.007 -26.549 -33.216 1.00 61.75  ?  129 ASN A ND2 1 
ATOM   534  N N   . GLU A 1 73  ? 7.638  -23.153 -33.432 1.00 35.03  ?  130 GLU A N   1 
ATOM   535  C CA  . GLU A 1 73  ? 6.801  -23.018 -34.623 1.00 43.22  ?  130 GLU A CA  1 
ATOM   536  C C   . GLU A 1 73  ? 7.041  -21.676 -35.304 1.00 46.65  ?  130 GLU A C   1 
ATOM   537  O O   . GLU A 1 73  ? 7.157  -21.605 -36.534 1.00 40.61  ?  130 GLU A O   1 
ATOM   538  C CB  . GLU A 1 73  ? 5.324  -23.170 -34.261 1.00 40.31  ?  130 GLU A CB  1 
ATOM   539  C CG  . GLU A 1 73  ? 5.035  -24.257 -33.232 1.00 72.47  ?  130 GLU A CG  1 
ATOM   540  C CD  . GLU A 1 73  ? 5.384  -23.827 -31.801 1.00 80.45  ?  130 GLU A CD  1 
ATOM   541  O OE1 . GLU A 1 73  ? 4.512  -23.234 -31.122 1.00 62.59  ?  130 GLU A OE1 1 
ATOM   542  O OE2 . GLU A 1 73  ? 6.540  -24.056 -31.369 1.00 56.37  -1 130 GLU A OE2 1 
ATOM   543  N N   . ASP A 1 74  ? 7.127  -20.597 -34.522 1.00 38.42  ?  131 ASP A N   1 
ATOM   544  C CA  . ASP A 1 74  ? 7.506  -19.314 -35.104 1.00 33.81  ?  131 ASP A CA  1 
ATOM   545  C C   . ASP A 1 74  ? 8.965  -19.304 -35.542 1.00 38.60  ?  131 ASP A C   1 
ATOM   546  O O   . ASP A 1 74  ? 9.297  -18.677 -36.550 1.00 32.43  ?  131 ASP A O   1 
ATOM   547  C CB  . ASP A 1 74  ? 7.209  -18.172 -34.132 1.00 39.32  ?  131 ASP A CB  1 
ATOM   548  C CG  . ASP A 1 74  ? 5.851  -18.315 -33.455 1.00 49.27  ?  131 ASP A CG  1 
ATOM   549  O OD1 . ASP A 1 74  ? 4.831  -18.397 -34.173 1.00 72.81  ?  131 ASP A OD1 1 
ATOM   550  O OD2 . ASP A 1 74  ? 5.798  -18.343 -32.207 1.00 65.79  -1 131 ASP A OD2 1 
ATOM   551  N N   . ALA A 1 75  ? 9.857  -19.983 -34.806 1.00 30.07  ?  132 ALA A N   1 
ATOM   552  C CA  . ALA A 1 75  ? 11.237 -20.078 -35.273 1.00 37.46  ?  132 ALA A CA  1 
ATOM   553  C C   . ALA A 1 75  ? 11.303 -20.774 -36.626 1.00 30.62  ?  132 ALA A C   1 
ATOM   554  O O   . ALA A 1 75  ? 12.102 -20.388 -37.489 1.00 33.41  ?  132 ALA A O   1 
ATOM   555  C CB  . ALA A 1 75  ? 12.112 -20.803 -34.249 1.00 38.68  ?  132 ALA A CB  1 
ATOM   556  N N   . GLN A 1 76  ? 10.461 -21.798 -36.836 1.00 35.46  ?  133 GLN A N   1 
ATOM   557  C CA  . GLN A 1 76  ? 10.408 -22.446 -38.144 1.00 32.45  ?  133 GLN A CA  1 
ATOM   558  C C   . GLN A 1 76  ? 9.985  -21.459 -39.220 1.00 31.09  ?  133 GLN A C   1 
ATOM   559  O O   . GLN A 1 76  ? 10.538 -21.457 -40.324 1.00 34.27  ?  133 GLN A O   1 
ATOM   560  C CB  . GLN A 1 76  ? 9.452  -23.643 -38.124 1.00 41.83  ?  133 GLN A CB  1 
ATOM   561  C CG  . GLN A 1 76  ? 9.918  -24.835 -37.295 1.00 49.41  ?  133 GLN A CG  1 
ATOM   562  C CD  . GLN A 1 76  ? 8.954  -26.023 -37.373 1.00 56.16  ?  133 GLN A CD  1 
ATOM   563  O OE1 . GLN A 1 76  ? 7.790  -25.880 -37.758 1.00 44.31  ?  133 GLN A OE1 1 
ATOM   564  N NE2 . GLN A 1 76  ? 9.440  -27.200 -36.992 1.00 54.70  ?  133 GLN A NE2 1 
ATOM   565  N N   . ALA A 1 77  ? 9.011  -20.604 -38.914 1.00 31.79  ?  134 ALA A N   1 
ATOM   566  C CA  . ALA A 1 77  ? 8.565  -19.628 -39.906 1.00 30.96  ?  134 ALA A CA  1 
ATOM   567  C C   . ALA A 1 77  ? 9.643  -18.582 -40.168 1.00 29.83  ?  134 ALA A C   1 
ATOM   568  O O   . ALA A 1 77  ? 9.816  -18.135 -41.307 1.00 33.13  ?  134 ALA A O   1 
ATOM   569  C CB  . ALA A 1 77  ? 7.260  -18.973 -39.451 1.00 29.97  ?  134 ALA A CB  1 
ATOM   570  N N   . VAL A 1 78  ? 10.387 -18.188 -39.130 1.00 29.97  ?  135 VAL A N   1 
ATOM   571  C CA  . VAL A 1 78  ? 11.499 -17.267 -39.337 1.00 26.87  ?  135 VAL A CA  1 
ATOM   572  C C   . VAL A 1 78  ? 12.593 -17.939 -40.159 1.00 29.87  ?  135 VAL A C   1 
ATOM   573  O O   . VAL A 1 78  ? 13.151 -17.335 -41.078 1.00 29.10  ?  135 VAL A O   1 
ATOM   574  C CB  . VAL A 1 78  ? 12.028 -16.755 -37.981 1.00 28.27  ?  135 VAL A CB  1 
ATOM   575  C CG1 . VAL A 1 78  ? 13.321 -15.954 -38.156 1.00 23.92  ?  135 VAL A CG1 1 
ATOM   576  C CG2 . VAL A 1 78  ? 10.952 -15.939 -37.269 1.00 27.75  ?  135 VAL A CG2 1 
ATOM   577  N N   . ALA A 1 79  ? 12.912 -19.203 -39.855 1.00 30.13  ?  136 ALA A N   1 
ATOM   578  C CA  . ALA A 1 79  ? 13.914 -19.909 -40.650 1.00 31.23  ?  136 ALA A CA  1 
ATOM   579  C C   . ALA A 1 79  ? 13.483 -20.014 -42.107 1.00 34.77  ?  136 ALA A C   1 
ATOM   580  O O   . ALA A 1 79  ? 14.310 -19.898 -43.022 1.00 31.83  ?  136 ALA A O   1 
ATOM   581  C CB  . ALA A 1 79  ? 14.171 -21.299 -40.067 1.00 32.61  ?  136 ALA A CB  1 
ATOM   582  N N   . GLN A 1 80  ? 12.186 -20.221 -42.340 1.00 35.71  ?  137 GLN A N   1 
ATOM   583  C CA  . GLN A 1 80  ? 11.681 -20.273 -43.705 1.00 39.08  ?  137 GLN A CA  1 
ATOM   584  C C   . GLN A 1 80  ? 11.929 -18.953 -44.428 1.00 37.24  ?  137 GLN A C   1 
ATOM   585  O O   . GLN A 1 80  ? 12.297 -18.945 -45.608 1.00 39.90  ?  137 GLN A O   1 
ATOM   586  C CB  . GLN A 1 80  ? 10.193 -20.632 -43.693 1.00 41.86  ?  137 GLN A CB  1 
ATOM   587  C CG  . GLN A 1 80  ? 9.820  -21.787 -44.614 1.00 61.02  ?  137 GLN A CG  1 
ATOM   588  C CD  . GLN A 1 80  ? 9.515  -21.326 -46.029 1.00 65.77  ?  137 GLN A CD  1 
ATOM   589  O OE1 . GLN A 1 80  ? 9.362  -20.130 -46.280 1.00 76.16  ?  137 GLN A OE1 1 
ATOM   590  N NE2 . GLN A 1 80  ? 9.421  -22.273 -46.959 1.00 55.94  ?  137 GLN A NE2 1 
ATOM   591  N N   . ALA A 1 81  ? 11.785 -17.826 -43.721 1.00 34.06  ?  138 ALA A N   1 
ATOM   592  C CA  . ALA A 1 81  ? 12.004 -16.527 -44.351 1.00 32.23  ?  138 ALA A CA  1 
ATOM   593  C C   . ALA A 1 81  ? 13.479 -16.250 -44.650 1.00 28.93  ?  138 ALA A C   1 
ATOM   594  O O   . ALA A 1 81  ? 13.772 -15.377 -45.478 1.00 38.46  ?  138 ALA A O   1 
ATOM   595  C CB  . ALA A 1 81  ? 11.423 -15.416 -43.474 1.00 35.10  ?  138 ALA A CB  1 
ATOM   596  N N   . CYS A 1 82  ? 14.411 -16.970 -44.012 1.00 33.19  ?  139 CYS A N   1 
ATOM   597  C CA  . CYS A 1 82  ? 15.832 -16.809 -44.315 1.00 38.24  ?  139 CYS A CA  1 
ATOM   598  C C   . CYS A 1 82  ? 16.256 -17.526 -45.590 1.00 37.06  ?  139 CYS A C   1 
ATOM   599  O O   . CYS A 1 82  ? 17.290 -17.177 -46.170 1.00 40.16  ?  139 CYS A O   1 
ATOM   600  C CB  . CYS A 1 82  ? 16.690 -17.319 -43.155 1.00 27.55  ?  139 CYS A CB  1 
ATOM   601  S SG  . CYS A 1 82  ? 16.287 -16.595 -41.565 1.00 31.95  ?  139 CYS A SG  1 
ATOM   602  N N   . GLY A 1 83  ? 15.491 -18.516 -46.036 1.00 45.54  ?  140 GLY A N   1 
ATOM   603  C CA  . GLY A 1 83  ? 15.803 -19.187 -47.282 1.00 41.40  ?  140 GLY A CA  1 
ATOM   604  C C   . GLY A 1 83  ? 17.101 -19.966 -47.252 1.00 37.43  ?  140 GLY A C   1 
ATOM   605  O O   . GLY A 1 83  ? 17.269 -20.880 -46.439 1.00 41.65  ?  140 GLY A O   1 
ATOM   606  N N   A ASN A 1 84  ? 18.025 -19.595 -48.142 0.46 40.80  ?  141 ASN A N   1 
ATOM   607  N N   B ASN A 1 84  ? 18.030 -19.629 -48.143 0.54 40.78  ?  141 ASN A N   1 
ATOM   608  C CA  A ASN A 1 84  ? 19.314 -20.259 -48.288 0.46 47.43  ?  141 ASN A CA  1 
ATOM   609  C CA  B ASN A 1 84  ? 19.302 -20.335 -48.200 0.54 47.42  ?  141 ASN A CA  1 
ATOM   610  C C   A ASN A 1 84  ? 20.389 -19.681 -47.379 0.46 48.80  ?  141 ASN A C   1 
ATOM   611  C C   B ASN A 1 84  ? 20.325 -19.790 -47.215 0.54 48.77  ?  141 ASN A C   1 
ATOM   612  O O   A ASN A 1 84  ? 21.499 -20.222 -47.336 0.46 43.46  ?  141 ASN A O   1 
ATOM   613  O O   B ASN A 1 84  ? 21.329 -20.461 -46.953 0.54 42.46  ?  141 ASN A O   1 
ATOM   614  C CB  A ASN A 1 84  ? 19.782 -20.175 -49.750 0.46 53.02  ?  141 ASN A CB  1 
ATOM   615  C CB  B ASN A 1 84  ? 19.883 -20.274 -49.619 0.54 53.02  ?  141 ASN A CB  1 
ATOM   616  C CG  A ASN A 1 84  ? 20.189 -18.763 -50.159 0.46 49.01  ?  141 ASN A CG  1 
ATOM   617  C CG  B ASN A 1 84  ? 19.220 -21.253 -50.563 0.54 53.24  ?  141 ASN A CG  1 
ATOM   618  O OD1 A ASN A 1 84  ? 21.324 -18.338 -49.934 0.46 46.86  ?  141 ASN A OD1 1 
ATOM   619  O OD1 B ASN A 1 84  ? 18.636 -22.250 -50.134 0.54 48.55  ?  141 ASN A OD1 1 
ATOM   620  N ND2 A ASN A 1 84  ? 19.259 -18.031 -50.761 0.46 51.73  ?  141 ASN A ND2 1 
ATOM   621  N ND2 B ASN A 1 84  ? 19.309 -20.976 -51.860 0.54 52.75  ?  141 ASN A ND2 1 
ATOM   622  N N   . VAL A 1 85  ? 20.089 -18.608 -46.664 1.00 39.12  ?  142 VAL A N   1 
ATOM   623  C CA  . VAL A 1 85  ? 21.076 -17.958 -45.798 1.00 33.20  ?  142 VAL A CA  1 
ATOM   624  C C   . VAL A 1 85  ? 21.102 -18.673 -44.447 1.00 36.89  ?  142 VAL A C   1 
ATOM   625  O O   . VAL A 1 85  ? 20.044 -18.844 -43.819 1.00 29.41  ?  142 VAL A O   1 
ATOM   626  C CB  . VAL A 1 85  ? 20.736 -16.472 -45.646 1.00 34.73  ?  142 VAL A CB  1 
ATOM   627  C CG1 . VAL A 1 85  ? 21.698 -15.768 -44.700 1.00 26.66  ?  142 VAL A CG1 1 
ATOM   628  C CG2 . VAL A 1 85  ? 20.731 -15.795 -47.014 1.00 37.68  ?  142 VAL A CG2 1 
ATOM   629  N N   . PRO A 1 86  ? 22.262 -19.131 -43.974 1.00 24.59  ?  143 PRO A N   1 
ATOM   630  C CA  . PRO A 1 86  ? 22.301 -19.870 -42.707 1.00 21.67  ?  143 PRO A CA  1 
ATOM   631  C C   . PRO A 1 86  ? 21.834 -19.000 -41.546 1.00 24.68  ?  143 PRO A C   1 
ATOM   632  O O   . PRO A 1 86  ? 22.136 -17.809 -41.490 1.00 25.45  ?  143 PRO A O   1 
ATOM   633  C CB  . PRO A 1 86  ? 23.779 -20.252 -42.560 1.00 28.32  ?  143 PRO A CB  1 
ATOM   634  C CG  . PRO A 1 86  ? 24.329 -20.203 -43.965 1.00 38.80  ?  143 PRO A CG  1 
ATOM   635  C CD  . PRO A 1 86  ? 23.551 -19.150 -44.688 1.00 33.17  ?  143 PRO A CD  1 
ATOM   636  N N   . VAL A 1 87  ? 21.106 -19.608 -40.604 1.00 21.09  ?  144 VAL A N   1 
ATOM   637  C CA  . VAL A 1 87  ? 20.533 -18.876 -39.478 1.00 17.97  ?  144 VAL A CA  1 
ATOM   638  C C   . VAL A 1 87  ? 20.689 -19.682 -38.194 1.00 25.21  ?  144 VAL A C   1 
ATOM   639  O O   . VAL A 1 87  ? 20.547 -20.911 -38.189 1.00 26.03  ?  144 VAL A O   1 
ATOM   640  C CB  . VAL A 1 87  ? 19.051 -18.515 -39.739 1.00 20.24  ?  144 VAL A CB  1 
ATOM   641  C CG1 . VAL A 1 87  ? 18.231 -19.764 -39.992 1.00 23.84  ?  144 VAL A CG1 1 
ATOM   642  C CG2 . VAL A 1 87  ? 18.473 -17.693 -38.583 1.00 20.54  ?  144 VAL A CG2 1 
ATOM   643  N N   . LEU A 1 88  ? 20.978 -18.974 -37.107 1.00 20.00  ?  145 LEU A N   1 
ATOM   644  C CA  . LEU A 1 88  ? 21.210 -19.540 -35.785 1.00 21.68  ?  145 LEU A CA  1 
ATOM   645  C C   . LEU A 1 88  ? 20.280 -18.828 -34.803 1.00 19.63  ?  145 LEU A C   1 
ATOM   646  O O   . LEU A 1 88  ? 20.176 -17.595 -34.833 1.00 19.35  ?  145 LEU A O   1 
ATOM   647  C CB  . LEU A 1 88  ? 22.674 -19.310 -35.389 1.00 24.74  ?  145 LEU A CB  1 
ATOM   648  C CG  . LEU A 1 88  ? 23.552 -20.342 -34.731 1.00 40.17  ?  145 LEU A CG  1 
ATOM   649  C CD1 . LEU A 1 88  ? 23.374 -21.588 -35.538 1.00 39.74  ?  145 LEU A CD1 1 
ATOM   650  C CD2 . LEU A 1 88  ? 24.968 -19.853 -34.822 1.00 33.05  ?  145 LEU A CD2 1 
ATOM   651  N N   . PHE A 1 89  ? 19.598 -19.580 -33.940 1.00 16.86  ?  146 PHE A N   1 
ATOM   652  C CA  . PHE A 1 89  ? 18.702 -19.005 -32.942 1.00 15.65  ?  146 PHE A CA  1 
ATOM   653  C C   . PHE A 1 89  ? 19.298 -19.087 -31.539 1.00 17.24  ?  146 PHE A C   1 
ATOM   654  O O   . PHE A 1 89  ? 19.902 -20.105 -31.176 1.00 20.11  ?  146 PHE A O   1 
ATOM   655  C CB  . PHE A 1 89  ? 17.348 -19.727 -32.954 1.00 19.24  ?  146 PHE A CB  1 
ATOM   656  C CG  . PHE A 1 89  ? 16.581 -19.535 -34.229 1.00 20.43  ?  146 PHE A CG  1 
ATOM   657  C CD1 . PHE A 1 89  ? 16.803 -20.364 -35.308 1.00 21.18  ?  146 PHE A CD1 1 
ATOM   658  C CD2 . PHE A 1 89  ? 15.665 -18.509 -34.348 1.00 20.29  ?  146 PHE A CD2 1 
ATOM   659  C CE1 . PHE A 1 89  ? 16.099 -20.178 -36.503 1.00 23.51  ?  146 PHE A CE1 1 
ATOM   660  C CE2 . PHE A 1 89  ? 14.966 -18.318 -35.525 1.00 25.37  ?  146 PHE A CE2 1 
ATOM   661  C CZ  . PHE A 1 89  ? 15.192 -19.146 -36.597 1.00 24.43  ?  146 PHE A CZ  1 
ATOM   662  N N   . LEU A 1 90  ? 19.112 -18.028 -30.739 1.00 16.84  ?  147 LEU A N   1 
ATOM   663  C CA  . LEU A 1 90  ? 19.647 -17.976 -29.380 1.00 14.77  ?  147 LEU A CA  1 
ATOM   664  C C   . LEU A 1 90  ? 18.590 -18.067 -28.292 1.00 21.87  ?  147 LEU A C   1 
ATOM   665  O O   . LEU A 1 90  ? 18.950 -18.031 -27.110 1.00 24.24  ?  147 LEU A O   1 
ATOM   666  C CB  . LEU A 1 90  ? 20.461 -16.685 -29.160 1.00 20.48  ?  147 LEU A CB  1 
ATOM   667  C CG  . LEU A 1 90  ? 21.569 -16.353 -30.177 1.00 19.56  ?  147 LEU A CG  1 
ATOM   668  C CD1 . LEU A 1 90  ? 22.417 -15.173 -29.693 1.00 18.37  ?  147 LEU A CD1 1 
ATOM   669  C CD2 . LEU A 1 90  ? 22.462 -17.526 -30.571 1.00 17.77  ?  147 LEU A CD2 1 
ATOM   670  N N   . ASP A 1 91  ? 17.306 -18.154 -28.639 1.00 20.71  ?  148 ASP A N   1 
ATOM   671  C CA  . ASP A 1 91  ? 16.251 -18.089 -27.618 1.00 23.99  ?  148 ASP A CA  1 
ATOM   672  C C   . ASP A 1 91  ? 14.962 -18.750 -28.094 1.00 22.87  ?  148 ASP A C   1 
ATOM   673  O O   . ASP A 1 91  ? 13.961 -18.062 -28.308 1.00 23.20  ?  148 ASP A O   1 
ATOM   674  C CB  . ASP A 1 91  ? 15.953 -16.631 -27.231 1.00 25.55  ?  148 ASP A CB  1 
ATOM   675  C CG  . ASP A 1 91  ? 15.313 -16.503 -25.842 1.00 30.99  ?  148 ASP A CG  1 
ATOM   676  O OD1 . ASP A 1 91  ? 15.200 -17.532 -25.131 1.00 33.18  -1 148 ASP A OD1 1 
ATOM   677  O OD2 . ASP A 1 91  ? 14.893 -15.371 -25.472 1.00 28.28  ?  148 ASP A OD2 1 
ATOM   678  N N   . VAL A 1 92  ? 14.966 -20.073 -28.256 1.00 25.55  ?  149 VAL A N   1 
ATOM   679  C CA  . VAL A 1 92  ? 13.849 -20.797 -28.859 1.00 23.24  ?  149 VAL A CA  1 
ATOM   680  C C   . VAL A 1 92  ? 13.592 -22.063 -28.048 1.00 25.62  ?  149 VAL A C   1 
ATOM   681  O O   . VAL A 1 92  ? 14.535 -22.697 -27.565 1.00 25.82  ?  149 VAL A O   1 
ATOM   682  C CB  . VAL A 1 92  ? 14.140 -21.146 -30.339 1.00 24.25  ?  149 VAL A CB  1 
ATOM   683  C CG1 . VAL A 1 92  ? 13.067 -22.039 -30.918 1.00 29.41  ?  149 VAL A CG1 1 
ATOM   684  C CG2 . VAL A 1 92  ? 14.232 -19.892 -31.172 1.00 30.93  ?  149 VAL A CG2 1 
ATOM   685  N N   . SER A 1 93  ? 12.311 -22.433 -27.880 1.00 20.88  ?  150 SER A N   1 
ATOM   686  C CA  . SER A 1 93  ? 11.998 -23.726 -27.278 1.00 25.34  ?  150 SER A CA  1 
ATOM   687  C C   . SER A 1 93  ? 10.904 -24.397 -28.102 1.00 35.67  ?  150 SER A C   1 
ATOM   688  O O   . SER A 1 93  ? 9.923  -23.735 -28.475 1.00 33.72  ?  150 SER A O   1 
ATOM   689  C CB  . SER A 1 93  ? 11.562 -23.612 -25.815 1.00 36.20  ?  150 SER A CB  1 
ATOM   690  O OG  . SER A 1 93  ? 11.352 -24.888 -25.231 1.00 37.97  ?  150 SER A OG  1 
ATOM   691  N N   . PRO A 1 94  ? 11.044 -25.694 -28.424 1.00 38.53  ?  151 PRO A N   1 
ATOM   692  C CA  . PRO A 1 94  ? 12.205 -26.564 -28.183 1.00 34.29  ?  151 PRO A CA  1 
ATOM   693  C C   . PRO A 1 94  ? 13.444 -26.032 -28.894 1.00 34.46  ?  151 PRO A C   1 
ATOM   694  O O   . PRO A 1 94  ? 13.316 -25.398 -29.932 1.00 31.63  ?  151 PRO A O   1 
ATOM   695  C CB  . PRO A 1 94  ? 11.757 -27.910 -28.771 1.00 37.39  ?  151 PRO A CB  1 
ATOM   696  C CG  . PRO A 1 94  ? 10.272 -27.896 -28.642 1.00 47.41  ?  151 PRO A CG  1 
ATOM   697  C CD  . PRO A 1 94  ? 9.880  -26.466 -28.901 1.00 46.58  ?  151 PRO A CD  1 
ATOM   698  N N   . ALA A 1 95  ? 14.637 -26.237 -28.358 1.00 28.45  ?  152 ALA A N   1 
ATOM   699  C CA  . ALA A 1 95  ? 15.837 -25.707 -28.989 1.00 25.79  ?  152 ALA A CA  1 
ATOM   700  C C   . ALA A 1 95  ? 16.026 -26.396 -30.331 1.00 36.01  ?  152 ALA A C   1 
ATOM   701  O O   . ALA A 1 95  ? 16.134 -27.626 -30.373 1.00 30.48  ?  152 ALA A O   1 
ATOM   702  C CB  . ALA A 1 95  ? 17.053 -25.919 -28.099 1.00 27.15  ?  152 ALA A CB  1 
ATOM   703  N N   . PRO A 1 96  ? 16.041 -25.670 -31.438 1.00 30.49  ?  153 PRO A N   1 
ATOM   704  C CA  . PRO A 1 96  ? 16.170 -26.314 -32.745 1.00 30.20  ?  153 PRO A CA  1 
ATOM   705  C C   . PRO A 1 96  ? 17.619 -26.681 -33.048 1.00 30.05  ?  153 PRO A C   1 
ATOM   706  O O   . PRO A 1 96  ? 18.564 -26.283 -32.369 1.00 26.38  ?  153 PRO A O   1 
ATOM   707  C CB  . PRO A 1 96  ? 15.647 -25.245 -33.711 1.00 39.69  ?  153 PRO A CB  1 
ATOM   708  C CG  . PRO A 1 96  ? 16.026 -23.969 -33.048 1.00 30.99  ?  153 PRO A CG  1 
ATOM   709  C CD  . PRO A 1 96  ? 15.854 -24.212 -31.556 1.00 33.05  ?  153 PRO A CD  1 
ATOM   710  N N   . VAL A 1 97  ? 17.773 -27.483 -34.097 1.00 27.41  ?  154 VAL A N   1 
ATOM   711  C CA  . VAL A 1 97  ? 19.097 -27.812 -34.600 1.00 31.33  ?  154 VAL A CA  1 
ATOM   712  C C   . VAL A 1 97  ? 19.866 -26.536 -34.935 1.00 33.43  ?  154 VAL A C   1 
ATOM   713  O O   . VAL A 1 97  ? 19.287 -25.526 -35.355 1.00 27.55  ?  154 VAL A O   1 
ATOM   714  C CB  . VAL A 1 97  ? 18.926 -28.765 -35.797 1.00 34.49  ?  154 VAL A CB  1 
ATOM   715  C CG1 . VAL A 1 97  ? 20.233 -29.083 -36.459 1.00 40.08  ?  154 VAL A CG1 1 
ATOM   716  C CG2 . VAL A 1 97  ? 18.277 -30.072 -35.309 1.00 31.42  ?  154 VAL A CG2 1 
ATOM   717  N N   . ASN A 1 98  ? 21.174 -26.559 -34.660 1.00 32.76  ?  155 ASN A N   1 
ATOM   718  C CA  . ASN A 1 98  ? 22.114 -25.476 -34.964 1.00 37.56  ?  155 ASN A CA  1 
ATOM   719  C C   . ASN A 1 98  ? 22.141 -24.408 -33.870 1.00 49.46  ?  155 ASN A C   1 
ATOM   720  O O   . ASN A 1 98  ? 23.196 -23.809 -33.639 1.00 49.89  ?  155 ASN A O   1 
ATOM   721  C CB  . ASN A 1 98  ? 21.828 -24.823 -36.329 1.00 46.01  ?  155 ASN A CB  1 
ATOM   722  C CG  . ASN A 1 98  ? 22.277 -25.689 -37.506 1.00 30.33  ?  155 ASN A CG  1 
ATOM   723  O OD1 . ASN A 1 98  ? 23.153 -26.544 -37.367 1.00 41.35  ?  155 ASN A OD1 1 
ATOM   724  N ND2 . ASN A 1 98  ? 21.684 -25.457 -38.670 1.00 41.20  ?  155 ASN A ND2 1 
ATOM   725  N N   . SER A 1 99  ? 21.019 -24.182 -33.171 1.00 24.48  ?  156 SER A N   1 
ATOM   726  C CA  . SER A 1 99  ? 20.929 -23.158 -32.126 1.00 22.08  ?  156 SER A CA  1 
ATOM   727  C C   . SER A 1 99  ? 22.051 -23.233 -31.093 1.00 21.08  ?  156 SER A C   1 
ATOM   728  O O   . SER A 1 99  ? 22.691 -24.273 -30.914 1.00 23.14  ?  156 SER A O   1 
ATOM   729  C CB  . SER A 1 99  ? 19.579 -23.221 -31.395 1.00 22.20  ?  156 SER A CB  1 
ATOM   730  O OG  . SER A 1 99  ? 19.425 -24.402 -30.614 1.00 26.78  ?  156 SER A OG  1 
ATOM   731  N N   . VAL A 1 100 ? 22.295 -22.102 -30.428 1.00 18.37  ?  157 VAL A N   1 
ATOM   732  C CA  . VAL A 1 100 ? 23.252 -21.983 -29.330 1.00 19.11  ?  157 VAL A CA  1 
ATOM   733  C C   . VAL A 1 100 ? 22.522 -21.232 -28.232 1.00 17.69  ?  157 VAL A C   1 
ATOM   734  O O   . VAL A 1 100 ? 22.100 -20.086 -28.435 1.00 19.06  ?  157 VAL A O   1 
ATOM   735  C CB  . VAL A 1 100 ? 24.531 -21.228 -29.745 1.00 19.40  ?  157 VAL A CB  1 
ATOM   736  C CG1 . VAL A 1 100 ? 25.489 -21.112 -28.569 1.00 20.94  ?  157 VAL A CG1 1 
ATOM   737  C CG2 . VAL A 1 100 ? 25.203 -21.923 -30.925 1.00 23.80  ?  157 VAL A CG2 1 
ATOM   738  N N   A LEU A 1 101 ? 22.317 -21.896 -27.091 0.36 18.32  ?  158 LEU A N   1 
ATOM   739  N N   B LEU A 1 101 ? 22.392 -21.850 -27.061 0.64 18.15  ?  158 LEU A N   1 
ATOM   740  C CA  A LEU A 1 101 ? 21.480 -21.373 -26.018 0.36 20.57  ?  158 LEU A CA  1 
ATOM   741  C CA  B LEU A 1 101 ? 21.587 -21.204 -26.039 0.64 20.09  ?  158 LEU A CA  1 
ATOM   742  C C   A LEU A 1 101 ? 22.158 -21.619 -24.683 0.36 17.00  ?  158 LEU A C   1 
ATOM   743  C C   B LEU A 1 101 ? 22.036 -21.671 -24.671 0.64 16.76  ?  158 LEU A C   1 
ATOM   744  O O   A LEU A 1 101 ? 23.001 -22.506 -24.549 0.36 18.03  ?  158 LEU A O   1 
ATOM   745  O O   B LEU A 1 101 ? 22.603 -22.754 -24.507 0.64 17.32  ?  158 LEU A O   1 
ATOM   746  C CB  A LEU A 1 101 ? 20.089 -22.028 -25.983 0.36 22.57  ?  158 LEU A CB  1 
ATOM   747  C CB  B LEU A 1 101 ? 20.089 -21.475 -26.225 0.64 24.95  ?  158 LEU A CB  1 
ATOM   748  C CG  A LEU A 1 101 ? 18.939 -21.528 -26.859 0.36 29.21  ?  158 LEU A CG  1 
ATOM   749  C CG  B LEU A 1 101 ? 19.609 -22.904 -25.988 0.64 22.77  ?  158 LEU A CG  1 
ATOM   750  C CD1 A LEU A 1 101 ? 19.206 -21.789 -28.305 0.36 28.63  ?  158 LEU A CD1 1 
ATOM   751  C CD1 B LEU A 1 101 ? 18.122 -22.906 -25.683 0.64 30.93  ?  158 LEU A CD1 1 
ATOM   752  C CD2 A LEU A 1 101 ? 17.641 -22.203 -26.450 0.36 32.29  ?  158 LEU A CD2 1 
ATOM   753  C CD2 B LEU A 1 101 ? 19.896 -23.773 -27.203 0.64 31.81  ?  158 LEU A CD2 1 
ATOM   754  N N   . PHE A 1 102 ? 21.768 -20.823 -23.686 1.00 18.97  ?  159 PHE A N   1 
ATOM   755  C CA  . PHE A 1 102 ? 22.038 -21.182 -22.313 1.00 21.64  ?  159 PHE A CA  1 
ATOM   756  C C   . PHE A 1 102 ? 21.046 -22.247 -21.904 1.00 24.04  ?  159 PHE A C   1 
ATOM   757  O O   . PHE A 1 102 ? 19.884 -22.229 -22.333 1.00 27.00  ?  159 PHE A O   1 
ATOM   758  C CB  . PHE A 1 102 ? 21.909 -19.970 -21.397 1.00 20.57  ?  159 PHE A CB  1 
ATOM   759  C CG  . PHE A 1 102 ? 22.910 -18.908 -21.673 1.00 22.90  ?  159 PHE A CG  1 
ATOM   760  C CD1 . PHE A 1 102 ? 24.252 -19.128 -21.407 1.00 22.68  ?  159 PHE A CD1 1 
ATOM   761  C CD2 . PHE A 1 102 ? 22.517 -17.680 -22.171 1.00 20.78  ?  159 PHE A CD2 1 
ATOM   762  C CE1 . PHE A 1 102 ? 25.175 -18.143 -21.664 1.00 19.85  ?  159 PHE A CE1 1 
ATOM   763  C CE2 . PHE A 1 102 ? 23.445 -16.685 -22.422 1.00 24.12  ?  159 PHE A CE2 1 
ATOM   764  C CZ  . PHE A 1 102 ? 24.772 -16.928 -22.175 1.00 19.82  ?  159 PHE A CZ  1 
ATOM   765  N N   . ASP A 1 103 ? 21.521 -23.205 -21.122 1.00 25.32  ?  160 ASP A N   1 
ATOM   766  C CA  . ASP A 1 103 ? 20.655 -24.228 -20.581 1.00 27.39  ?  160 ASP A CA  1 
ATOM   767  C C   . ASP A 1 103 ? 19.450 -23.556 -19.935 1.00 32.01  ?  160 ASP A C   1 
ATOM   768  O O   . ASP A 1 103 ? 19.619 -22.759 -18.999 1.00 32.32  ?  160 ASP A O   1 
ATOM   769  C CB  . ASP A 1 103 ? 21.411 -25.069 -19.561 1.00 28.38  ?  160 ASP A CB  1 
ATOM   770  C CG  . ASP A 1 103 ? 20.623 -26.275 -19.099 1.00 32.50  ?  160 ASP A CG  1 
ATOM   771  O OD1 . ASP A 1 103 ? 19.408 -26.141 -18.819 1.00 31.07  ?  160 ASP A OD1 1 
ATOM   772  O OD2 . ASP A 1 103 ? 21.230 -27.363 -19.007 1.00 36.72  -1 160 ASP A OD2 1 
ATOM   773  N N   . PRO A 1 104 ? 18.234 -23.840 -20.394 1.00 36.41  ?  161 PRO A N   1 
ATOM   774  C CA  . PRO A 1 104 ? 17.094 -23.047 -19.940 1.00 29.73  ?  161 PRO A CA  1 
ATOM   775  C C   . PRO A 1 104 ? 16.561 -23.444 -18.575 1.00 32.40  ?  161 PRO A C   1 
ATOM   776  O O   . PRO A 1 104 ? 15.804 -22.658 -17.997 1.00 32.00  ?  161 PRO A O   1 
ATOM   777  C CB  . PRO A 1 104 ? 16.054 -23.292 -21.037 1.00 41.50  ?  161 PRO A CB  1 
ATOM   778  C CG  . PRO A 1 104 ? 16.327 -24.699 -21.461 1.00 40.77  ?  161 PRO A CG  1 
ATOM   779  C CD  . PRO A 1 104 ? 17.822 -24.919 -21.309 1.00 44.99  ?  161 PRO A CD  1 
ATOM   780  N N   . HIS A 1 105 ? 16.916 -24.621 -18.035 1.00 22.78  ?  162 HIS A N   1 
ATOM   781  C CA  . HIS A 1 105 ? 16.442 -25.038 -16.718 1.00 20.44  ?  162 HIS A CA  1 
ATOM   782  C C   . HIS A 1 105 ? 17.510 -25.112 -15.636 1.00 20.70  ?  162 HIS A C   1 
ATOM   783  O O   . HIS A 1 105 ? 17.158 -25.153 -14.450 1.00 21.44  ?  162 HIS A O   1 
ATOM   784  C CB  . HIS A 1 105 ? 15.762 -26.416 -16.779 1.00 31.03  ?  162 HIS A CB  1 
ATOM   785  C CG  . HIS A 1 105 ? 14.567 -26.465 -17.670 1.00 39.79  ?  162 HIS A CG  1 
ATOM   786  N ND1 . HIS A 1 105 ? 14.644 -26.771 -19.011 1.00 43.33  ?  162 HIS A ND1 1 
ATOM   787  C CD2 . HIS A 1 105 ? 13.260 -26.226 -17.410 1.00 42.11  ?  162 HIS A CD2 1 
ATOM   788  C CE1 . HIS A 1 105 ? 13.432 -26.732 -19.537 1.00 56.72  ?  162 HIS A CE1 1 
ATOM   789  N NE2 . HIS A 1 105 ? 12.574 -26.408 -18.585 1.00 44.62  ?  162 HIS A NE2 1 
ATOM   790  N N   A GLU A 1 106 ? 18.793 -25.144 -16.009 0.43 19.68  ?  163 GLU A N   1 
ATOM   791  N N   B GLU A 1 106 ? 18.794 -25.154 -16.007 0.57 19.67  ?  163 GLU A N   1 
ATOM   792  C CA  A GLU A 1 106 ? 19.851 -25.290 -15.011 0.43 19.89  ?  163 GLU A CA  1 
ATOM   793  C CA  B GLU A 1 106 ? 19.844 -25.295 -15.000 0.57 19.85  ?  163 GLU A CA  1 
ATOM   794  C C   A GLU A 1 106 ? 19.915 -24.081 -14.087 0.43 17.18  ?  163 GLU A C   1 
ATOM   795  C C   B GLU A 1 106 ? 19.900 -24.081 -14.082 0.57 17.14  ?  163 GLU A C   1 
ATOM   796  O O   A GLU A 1 106 ? 20.116 -24.226 -12.877 0.43 16.61  ?  163 GLU A O   1 
ATOM   797  O O   B GLU A 1 106 ? 20.077 -24.223 -12.867 0.57 16.64  ?  163 GLU A O   1 
ATOM   798  C CB  A GLU A 1 106 ? 21.198 -25.515 -15.701 0.43 20.35  ?  163 GLU A CB  1 
ATOM   799  C CB  B GLU A 1 106 ? 21.199 -25.527 -15.673 0.57 20.29  ?  163 GLU A CB  1 
ATOM   800  C CG  A GLU A 1 106 ? 21.664 -26.955 -15.645 0.43 28.21  ?  163 GLU A CG  1 
ATOM   801  C CG  B GLU A 1 106 ? 22.333 -25.620 -14.672 0.57 17.42  ?  163 GLU A CG  1 
ATOM   802  C CD  A GLU A 1 106 ? 21.607 -27.535 -14.238 0.43 26.87  ?  163 GLU A CD  1 
ATOM   803  C CD  B GLU A 1 106 ? 23.694 -25.801 -15.326 0.57 22.30  ?  163 GLU A CD  1 
ATOM   804  O OE1 A GLU A 1 106 ? 22.411 -27.110 -13.380 0.43 31.76  ?  163 GLU A OE1 1 
ATOM   805  O OE1 B GLU A 1 106 ? 23.899 -25.300 -16.460 0.57 25.51  ?  163 GLU A OE1 1 
ATOM   806  O OE2 A GLU A 1 106 ? 20.768 -28.429 -14.001 0.43 32.77  -1 163 GLU A OE2 1 
ATOM   807  O OE2 B GLU A 1 106 ? 24.564 -26.454 -14.705 0.57 26.07  -1 163 GLU A OE2 1 
ATOM   808  N N   . GLY A 1 107 ? 19.740 -22.879 -14.635 1.00 14.82  ?  164 GLY A N   1 
ATOM   809  C CA  . GLY A 1 107 ? 19.737 -21.695 -13.788 1.00 14.14  ?  164 GLY A CA  1 
ATOM   810  C C   . GLY A 1 107 ? 18.631 -21.707 -12.751 1.00 14.08  ?  164 GLY A C   1 
ATOM   811  O O   . GLY A 1 107 ? 18.850 -21.343 -11.596 1.00 13.41  ?  164 GLY A O   1 
ATOM   812  N N   . ALA A 1 108 ? 17.427 -22.121 -13.152 1.00 13.35  ?  165 ALA A N   1 
ATOM   813  C CA  . ALA A 1 108 ? 16.323 -22.211 -12.203 1.00 15.10  ?  165 ALA A CA  1 
ATOM   814  C C   . ALA A 1 108 ? 16.617 -23.231 -11.122 1.00 14.44  ?  165 ALA A C   1 
ATOM   815  O O   . ALA A 1 108 ? 16.320 -22.994 -9.938  1.00 13.95  ?  165 ALA A O   1 
ATOM   816  C CB  . ALA A 1 108 ? 15.032 -22.573 -12.942 1.00 15.16  ?  165 ALA A CB  1 
ATOM   817  N N   . ARG A 1 109 ? 17.184 -24.384 -11.512 1.00 14.30  ?  166 ARG A N   1 
ATOM   818  C CA  . ARG A 1 109 ? 17.511 -25.420 -10.534 1.00 13.57  ?  166 ARG A CA  1 
ATOM   819  C C   . ARG A 1 109 ? 18.577 -24.934 -9.559  1.00 15.88  ?  166 ARG A C   1 
ATOM   820  O O   . ARG A 1 109 ? 18.449 -25.135 -8.347  1.00 15.52  ?  166 ARG A O   1 
ATOM   821  C CB  . ARG A 1 109 ? 17.975 -26.687 -11.243 1.00 14.90  ?  166 ARG A CB  1 
ATOM   822  C CG  . ARG A 1 109 ? 18.554 -27.725 -10.302 1.00 20.91  ?  166 ARG A CG  1 
ATOM   823  C CD  . ARG A 1 109 ? 18.917 -28.952 -11.094 1.00 21.74  ?  166 ARG A CD  1 
ATOM   824  N NE  . ARG A 1 109 ? 20.273 -28.840 -11.621 1.00 36.90  ?  166 ARG A NE  1 
ATOM   825  C CZ  . ARG A 1 109 ? 21.376 -28.819 -10.881 1.00 41.27  ?  166 ARG A CZ  1 
ATOM   826  N NH1 . ARG A 1 109 ? 21.336 -28.975 -9.565  1.00 39.58  ?  166 ARG A NH1 1 
ATOM   827  N NH2 . ARG A 1 109 ? 22.555 -28.659 -11.480 1.00 58.68  ?  166 ARG A NH2 1 
ATOM   828  N N   . LEU A 1 110 ? 19.608 -24.250 -10.056 1.00 13.72  ?  167 LEU A N   1 
ATOM   829  C CA  . LEU A 1 110 ? 20.667 -23.775 -9.168  1.00 14.58  ?  167 LEU A CA  1 
ATOM   830  C C   . LEU A 1 110 ? 20.126 -22.786 -8.152  1.00 15.03  ?  167 LEU A C   1 
ATOM   831  O O   . LEU A 1 110 ? 20.561 -22.783 -6.998  1.00 15.08  ?  167 LEU A O   1 
ATOM   832  C CB  . LEU A 1 110 ? 21.807 -23.125 -9.966  1.00 15.11  ?  167 LEU A CB  1 
ATOM   833  C CG  . LEU A 1 110 ? 22.614 -24.064 -10.844 1.00 14.38  ?  167 LEU A CG  1 
ATOM   834  C CD1 . LEU A 1 110 ? 23.531 -23.212 -11.737 1.00 19.53  ?  167 LEU A CD1 1 
ATOM   835  C CD2 . LEU A 1 110 ? 23.384 -25.091 -10.026 1.00 23.72  ?  167 LEU A CD2 1 
ATOM   836  N N   . GLY A 1 111 ? 19.191 -21.929 -8.564  1.00 13.33  ?  168 GLY A N   1 
ATOM   837  C CA  . GLY A 1 111 ? 18.663 -20.935 -7.635  1.00 12.09  ?  168 GLY A CA  1 
ATOM   838  C C   . GLY A 1 111 ? 17.821 -21.557 -6.534  1.00 12.68  ?  168 GLY A C   1 
ATOM   839  O O   . GLY A 1 111 ? 17.988 -21.234 -5.350  1.00 14.43  ?  168 GLY A O   1 
ATOM   840  N N   . VAL A 1 112 ? 16.920 -22.469 -6.901  1.00 12.15  ?  169 VAL A N   1 
ATOM   841  C CA  . VAL A 1 112 ? 16.124 -23.160 -5.878  1.00 11.74  ?  169 VAL A CA  1 
ATOM   842  C C   . VAL A 1 112 ? 17.031 -23.979 -4.969  1.00 16.48  ?  169 VAL A C   1 
ATOM   843  O O   . VAL A 1 112 ? 16.903 -23.936 -3.741  1.00 14.69  ?  169 VAL A O   1 
ATOM   844  C CB  . VAL A 1 112 ? 15.036 -24.053 -6.498  1.00 13.82  ?  169 VAL A CB  1 
ATOM   845  C CG1 . VAL A 1 112 ? 14.413 -24.946 -5.423  1.00 15.34  ?  169 VAL A CG1 1 
ATOM   846  C CG2 . VAL A 1 112 ? 13.922 -23.204 -7.143  1.00 15.23  ?  169 VAL A CG2 1 
ATOM   847  N N   . GLU A 1 113 ? 17.968 -24.723 -5.549  1.00 13.35  ?  170 GLU A N   1 
ATOM   848  C CA  . GLU A 1 113 ? 18.837 -25.567 -4.729  1.00 15.04  ?  170 GLU A CA  1 
ATOM   849  C C   . GLU A 1 113 ? 19.635 -24.734 -3.728  1.00 14.58  ?  170 GLU A C   1 
ATOM   850  O O   . GLU A 1 113 ? 19.834 -25.158 -2.582  1.00 15.22  ?  170 GLU A O   1 
ATOM   851  C CB  . GLU A 1 113 ? 19.779 -26.370 -5.622  1.00 15.66  ?  170 GLU A CB  1 
ATOM   852  C CG  . GLU A 1 113 ? 19.085 -27.503 -6.325  1.00 17.16  ?  170 GLU A CG  1 
ATOM   853  C CD  . GLU A 1 113 ? 18.539 -28.560 -5.390  1.00 26.28  ?  170 GLU A CD  1 
ATOM   854  O OE1 . GLU A 1 113 ? 19.263 -29.004 -4.464  1.00 29.59  ?  170 GLU A OE1 1 
ATOM   855  O OE2 . GLU A 1 113 ? 17.381 -28.977 -5.603  1.00 30.90  -1 170 GLU A OE2 1 
ATOM   856  N N   . HIS A 1 114 ? 20.117 -23.561 -4.142  1.00 12.25  ?  171 HIS A N   1 
ATOM   857  C CA  . HIS A 1 114 ? 20.892 -22.715 -3.232  1.00 10.72  ?  171 HIS A CA  1 
ATOM   858  C C   . HIS A 1 114 ? 20.039 -22.255 -2.051  1.00 13.05  ?  171 HIS A C   1 
ATOM   859  O O   . HIS A 1 114 ? 20.468 -22.343 -0.894  1.00 14.01  ?  171 HIS A O   1 
ATOM   860  C CB  . HIS A 1 114 ? 21.465 -21.521 -4.002  1.00 14.42  ?  171 HIS A CB  1 
ATOM   861  C CG  . HIS A 1 114 ? 22.130 -20.493 -3.139  1.00 14.54  ?  171 HIS A CG  1 
ATOM   862  N ND1 . HIS A 1 114 ? 23.286 -20.739 -2.432  1.00 16.67  ?  171 HIS A ND1 1 
ATOM   863  C CD2 . HIS A 1 114 ? 21.800 -19.200 -2.888  1.00 12.56  ?  171 HIS A CD2 1 
ATOM   864  C CE1 . HIS A 1 114 ? 23.640 -19.642 -1.779  1.00 16.69  ?  171 HIS A CE1 1 
ATOM   865  N NE2 . HIS A 1 114 ? 22.749 -18.696 -2.036  1.00 14.04  ?  171 HIS A NE2 1 
ATOM   866  N N   . LEU A 1 115 ? 18.829 -21.759 -2.324  1.00 13.93  ?  172 LEU A N   1 
ATOM   867  C CA  . LEU A 1 115 ? 17.979 -21.259 -1.238  1.00 12.34  ?  172 LEU A CA  1 
ATOM   868  C C   . LEU A 1 115 ? 17.545 -22.384 -0.306  1.00 13.56  ?  172 LEU A C   1 
ATOM   869  O O   . LEU A 1 115 ? 17.497 -22.200 0.922   1.00 14.45  ?  172 LEU A O   1 
ATOM   870  C CB  . LEU A 1 115 ? 16.759 -20.539 -1.814  1.00 15.71  ?  172 LEU A CB  1 
ATOM   871  C CG  . LEU A 1 115 ? 17.135 -19.255 -2.544  1.00 14.00  ?  172 LEU A CG  1 
ATOM   872  C CD1 . LEU A 1 115 ? 15.838 -18.742 -3.174  1.00 16.91  ?  172 LEU A CD1 1 
ATOM   873  C CD2 . LEU A 1 115 ? 17.743 -18.208 -1.607  1.00 14.16  ?  172 LEU A CD2 1 
ATOM   874  N N   . VAL A 1 116 ? 17.236 -23.567 -0.855  1.00 13.26  ?  173 VAL A N   1 
ATOM   875  C CA  . VAL A 1 116 ? 16.870 -24.695 -0.005  1.00 16.83  ?  173 VAL A CA  1 
ATOM   876  C C   . VAL A 1 116 ? 18.067 -25.137 0.831   1.00 14.51  ?  173 VAL A C   1 
ATOM   877  O O   . VAL A 1 116 ? 17.924 -25.462 2.023   1.00 16.95  ?  173 VAL A O   1 
ATOM   878  C CB  . VAL A 1 116 ? 16.302 -25.842 -0.864  1.00 16.53  ?  173 VAL A CB  1 
ATOM   879  C CG1 . VAL A 1 116 ? 16.122 -27.096 -0.040  1.00 18.30  ?  173 VAL A CG1 1 
ATOM   880  C CG2 . VAL A 1 116 ? 14.951 -25.440 -1.470  1.00 17.66  ?  173 VAL A CG2 1 
ATOM   881  N N   . ALA A 1 117 ? 19.278 -25.130 0.236   1.00 15.11  ?  174 ALA A N   1 
ATOM   882  C CA  . ALA A 1 117 ? 20.473 -25.505 0.994   1.00 17.16  ?  174 ALA A CA  1 
ATOM   883  C C   . ALA A 1 117 ? 20.704 -24.591 2.192   1.00 15.22  ?  174 ALA A C   1 
ATOM   884  O O   . ALA A 1 117 ? 21.262 -25.035 3.204   1.00 19.21  ?  174 ALA A O   1 
ATOM   885  C CB  . ALA A 1 117 ? 21.703 -25.499 0.075   1.00 16.89  ?  174 ALA A CB  1 
ATOM   886  N N   . LEU A 1 118 ? 20.322 -23.308 2.080   1.00 15.31  ?  175 LEU A N   1 
ATOM   887  C CA  . LEU A 1 118 ? 20.426 -22.330 3.158   1.00 14.68  ?  175 LEU A CA  1 
ATOM   888  C C   . LEU A 1 118 ? 19.325 -22.489 4.186   1.00 17.15  ?  175 LEU A C   1 
ATOM   889  O O   . LEU A 1 118 ? 19.398 -21.867 5.255   1.00 19.75  ?  175 LEU A O   1 
ATOM   890  C CB  . LEU A 1 118 ? 20.363 -20.908 2.598   1.00 14.79  ?  175 LEU A CB  1 
ATOM   891  C CG  . LEU A 1 118 ? 21.595 -20.401 1.862   1.00 17.74  ?  175 LEU A CG  1 
ATOM   892  C CD1 . LEU A 1 118 ? 21.220 -19.069 1.235   1.00 15.72  ?  175 LEU A CD1 1 
ATOM   893  C CD2 . LEU A 1 118 ? 22.759 -20.277 2.803   1.00 23.98  ?  175 LEU A CD2 1 
ATOM   894  N N   . GLY A 1 119 ? 18.321 -23.309 3.900   1.00 15.86  ?  176 GLY A N   1 
ATOM   895  C CA  . GLY A 1 119 ? 17.259 -23.585 4.848   1.00 16.06  ?  176 GLY A CA  1 
ATOM   896  C C   . GLY A 1 119 ? 15.938 -22.915 4.555   1.00 17.01  ?  176 GLY A C   1 
ATOM   897  O O   . GLY A 1 119 ? 15.011 -23.061 5.358   1.00 17.20  ?  176 GLY A O   1 
ATOM   898  N N   . HIS A 1 120 ? 15.811 -22.203 3.433   1.00 14.19  ?  177 HIS A N   1 
ATOM   899  C CA  . HIS A 1 120 ? 14.554 -21.544 3.108   1.00 13.44  ?  177 HIS A CA  1 
ATOM   900  C C   . HIS A 1 120 ? 13.480 -22.543 2.738   1.00 17.43  ?  177 HIS A C   1 
ATOM   901  O O   . HIS A 1 120 ? 13.728 -23.515 2.022   1.00 18.24  ?  177 HIS A O   1 
ATOM   902  C CB  . HIS A 1 120 ? 14.759 -20.579 1.959   1.00 13.52  ?  177 HIS A CB  1 
ATOM   903  C CG  . HIS A 1 120 ? 15.590 -19.407 2.348   1.00 11.90  ?  177 HIS A CG  1 
ATOM   904  N ND1 . HIS A 1 120 ? 15.063 -18.309 2.994   1.00 13.84  ?  177 HIS A ND1 1 
ATOM   905  C CD2 . HIS A 1 120 ? 16.919 -19.176 2.230   1.00 15.74  ?  177 HIS A CD2 1 
ATOM   906  C CE1 . HIS A 1 120 ? 16.028 -17.441 3.239   1.00 16.40  ?  177 HIS A CE1 1 
ATOM   907  N NE2 . HIS A 1 120 ? 17.169 -17.946 2.798   1.00 17.71  ?  177 HIS A NE2 1 
ATOM   908  N N   . GLN A 1 121 ? 12.272 -22.269 3.205   1.00 17.16  ?  178 GLN A N   1 
ATOM   909  C CA  . GLN A 1 121 ? 11.085 -23.027 2.843   1.00 18.81  ?  178 GLN A CA  1 
ATOM   910  C C   . GLN A 1 121 ? 10.002 -22.147 2.253   1.00 22.25  ?  178 GLN A C   1 
ATOM   911  O O   . GLN A 1 121 ? 9.100  -22.672 1.591   1.00 25.50  ?  178 GLN A O   1 
ATOM   912  C CB  . GLN A 1 121 ? 10.497 -23.763 4.059   1.00 22.64  ?  178 GLN A CB  1 
ATOM   913  C CG  . GLN A 1 121 ? 11.423 -24.796 4.649   1.00 25.66  ?  178 GLN A CG  1 
ATOM   914  C CD  . GLN A 1 121 ? 11.136 -25.092 6.116   1.00 60.90  ?  178 GLN A CD  1 
ATOM   915  O OE1 . GLN A 1 121 ? 10.194 -24.556 6.708   1.00 44.22  ?  178 GLN A OE1 1 
ATOM   916  N NE2 . GLN A 1 121 ? 11.966 -25.941 6.714   1.00 63.16  ?  178 GLN A NE2 1 
ATOM   917  N N   . ARG A 1 122 ? 10.055 -20.834 2.486   1.00 17.33  ?  179 ARG A N   1 
ATOM   918  C CA  . ARG A 1 122 ? 9.011  -19.896 2.065   1.00 15.62  ?  179 ARG A CA  1 
ATOM   919  C C   . ARG A 1 122 ? 9.633  -19.043 0.964   1.00 16.33  ?  179 ARG A C   1 
ATOM   920  O O   . ARG A 1 122 ? 10.157 -17.957 1.214   1.00 17.93  ?  179 ARG A O   1 
ATOM   921  C CB  . ARG A 1 122 ? 8.525  -19.044 3.254   1.00 18.31  ?  179 ARG A CB  1 
ATOM   922  C CG  . ARG A 1 122 ? 7.748  -19.859 4.249   1.00 22.73  ?  179 ARG A CG  1 
ATOM   923  C CD  . ARG A 1 122 ? 7.038  -18.970 5.250   1.00 27.69  ?  179 ARG A CD  1 
ATOM   924  N NE  . ARG A 1 122 ? 6.600  -19.776 6.375   1.00 41.07  ?  179 ARG A NE  1 
ATOM   925  C CZ  . ARG A 1 122 ? 5.904  -19.318 7.406   1.00 53.17  ?  179 ARG A CZ  1 
ATOM   926  N NH1 . ARG A 1 122 ? 5.515  -18.055 7.471   1.00 50.74  ?  179 ARG A NH1 1 
ATOM   927  N NH2 . ARG A 1 122 ? 5.585  -20.152 8.391   1.00 48.78  ?  179 ARG A NH2 1 
ATOM   928  N N   . ILE A 1 123 ? 9.571  -19.545 -0.262  1.00 12.60  ?  180 ILE A N   1 
ATOM   929  C CA  . ILE A 1 123 ? 10.302 -18.995 -1.390  1.00 13.28  ?  180 ILE A CA  1 
ATOM   930  C C   . ILE A 1 123 ? 9.292  -18.440 -2.386  1.00 14.75  ?  180 ILE A C   1 
ATOM   931  O O   . ILE A 1 123 ? 8.385  -19.154 -2.828  1.00 17.39  ?  180 ILE A O   1 
ATOM   932  C CB  . ILE A 1 123 ? 11.194 -20.075 -2.032  1.00 14.37  ?  180 ILE A CB  1 
ATOM   933  C CG1 . ILE A 1 123 ? 12.270 -20.531 -1.045  1.00 14.39  ?  180 ILE A CG1 1 
ATOM   934  C CG2 . ILE A 1 123 ? 11.863 -19.563 -3.274  1.00 17.66  ?  180 ILE A CG2 1 
ATOM   935  C CD1 . ILE A 1 123 ? 12.938 -21.817 -1.496  1.00 18.83  ?  180 ILE A CD1 1 
ATOM   936  N N   . ALA A 1 124 ? 9.458  -17.165 -2.748  1.00 14.32  ?  181 ALA A N   1 
ATOM   937  C CA  . ALA A 1 124 ? 8.593  -16.507 -3.711  1.00 13.50  ?  181 ALA A CA  1 
ATOM   938  C C   . ALA A 1 124 ? 9.317  -16.415 -5.043  1.00 11.34  ?  181 ALA A C   1 
ATOM   939  O O   . ALA A 1 124 ? 10.554 -16.419 -5.094  1.00 12.88  ?  181 ALA A O   1 
ATOM   940  C CB  . ALA A 1 124 ? 8.193  -15.115 -3.221  1.00 15.27  ?  181 ALA A CB  1 
ATOM   941  N N   . LEU A 1 125 ? 8.527  -16.370 -6.123  1.00 12.78  ?  182 LEU A N   1 
ATOM   942  C CA  . LEU A 1 125 ? 9.054  -16.302 -7.488  1.00 12.72  ?  182 LEU A CA  1 
ATOM   943  C C   . LEU A 1 125 ? 8.595  -15.016 -8.156  1.00 12.65  ?  182 LEU A C   1 
ATOM   944  O O   . LEU A 1 125 ? 7.406  -14.690 -8.110  1.00 13.77  ?  182 LEU A O   1 
ATOM   945  C CB  . LEU A 1 125 ? 8.545  -17.474 -8.326  1.00 13.52  ?  182 LEU A CB  1 
ATOM   946  C CG  . LEU A 1 125 ? 8.721  -18.867 -7.714  1.00 13.31  ?  182 LEU A CG  1 
ATOM   947  C CD1 . LEU A 1 125 ? 8.157  -19.920 -8.654  1.00 16.82  ?  182 LEU A CD1 1 
ATOM   948  C CD2 . LEU A 1 125 ? 10.178 -19.163 -7.408  1.00 16.45  ?  182 LEU A CD2 1 
ATOM   949  N N   . LEU A 1 126 ? 9.521  -14.317 -8.827  1.00 10.75  ?  183 LEU A N   1 
ATOM   950  C CA  . LEU A 1 126 ? 9.179  -13.120 -9.598  1.00 11.86  ?  183 LEU A CA  1 
ATOM   951  C C   . LEU A 1 126 ? 9.591  -13.420 -11.039 1.00 10.96  ?  183 LEU A C   1 
ATOM   952  O O   . LEU A 1 126 ? 10.779 -13.373 -11.380 1.00 14.08  ?  183 LEU A O   1 
ATOM   953  C CB  . LEU A 1 126 ? 9.867  -11.880 -9.030  1.00 12.18  ?  183 LEU A CB  1 
ATOM   954  C CG  . LEU A 1 126 ? 9.765  -10.574 -9.836  1.00 19.52  ?  183 LEU A CG  1 
ATOM   955  C CD1 . LEU A 1 126 ? 8.387  -10.300 -10.448 1.00 20.94  ?  183 LEU A CD1 1 
ATOM   956  C CD2 . LEU A 1 126 ? 10.248 -9.412  -8.917  1.00 17.32  ?  183 LEU A CD2 1 
ATOM   957  N N   . THR A 1 127 ? 8.602  -13.763 -11.855 1.00 12.36  ?  184 THR A N   1 
ATOM   958  C CA  . THR A 1 127 ? 8.903  -14.230 -13.209 1.00 12.15  ?  184 THR A CA  1 
ATOM   959  C C   . THR A 1 127 ? 9.102  -13.058 -14.163 1.00 13.24  ?  184 THR A C   1 
ATOM   960  O O   . THR A 1 127 ? 8.699  -11.919 -13.910 1.00 13.36  ?  184 THR A O   1 
ATOM   961  C CB  . THR A 1 127 ? 7.787  -15.132 -13.766 1.00 11.93  ?  184 THR A CB  1 
ATOM   962  O OG1 . THR A 1 127 ? 6.659  -14.344 -14.198 1.00 14.68  ?  184 THR A OG1 1 
ATOM   963  C CG2 . THR A 1 127 ? 7.345  -16.182 -12.727 1.00 15.61  ?  184 THR A CG2 1 
ATOM   964  N N   . GLY A 1 128 ? 9.706  -13.360 -15.311 1.00 12.68  ?  185 GLY A N   1 
ATOM   965  C CA  . GLY A 1 128 ? 9.575  -12.484 -16.443 1.00 13.96  ?  185 GLY A CA  1 
ATOM   966  C C   . GLY A 1 128 ? 8.186  -12.599 -17.077 1.00 13.29  ?  185 GLY A C   1 
ATOM   967  O O   . GLY A 1 128 ? 7.329  -13.385 -16.645 1.00 15.40  ?  185 GLY A O   1 
ATOM   968  N N   . PRO A 1 129 ? 7.960  -11.825 -18.131 1.00 14.51  ?  186 PRO A N   1 
ATOM   969  C CA  . PRO A 1 129 ? 6.659  -11.875 -18.805 1.00 16.95  ?  186 PRO A CA  1 
ATOM   970  C C   . PRO A 1 129 ? 6.458  -13.240 -19.449 1.00 16.93  ?  186 PRO A C   1 
ATOM   971  O O   . PRO A 1 129 ? 7.319  -13.728 -20.180 1.00 19.06  ?  186 PRO A O   1 
ATOM   972  C CB  . PRO A 1 129 ? 6.754  -10.751 -19.841 1.00 18.26  ?  186 PRO A CB  1 
ATOM   973  C CG  . PRO A 1 129 ? 8.225  -10.596 -20.080 1.00 19.56  ?  186 PRO A CG  1 
ATOM   974  C CD  . PRO A 1 129 ? 8.909  -10.930 -18.811 1.00 16.86  ?  186 PRO A CD  1 
ATOM   975  N N   . LEU A 1 130 ? 5.322  -13.867 -19.156 1.00 20.20  ?  187 LEU A N   1 
ATOM   976  C CA  . LEU A 1 130 ? 5.144  -15.248 -19.580 1.00 24.04  ?  187 LEU A CA  1 
ATOM   977  C C   . LEU A 1 130 ? 4.980  -15.386 -21.092 1.00 25.69  ?  187 LEU A C   1 
ATOM   978  O O   . LEU A 1 130 ? 5.050  -16.510 -21.601 1.00 28.46  ?  187 LEU A O   1 
ATOM   979  C CB  . LEU A 1 130 ? 3.953  -15.866 -18.834 1.00 21.78  ?  187 LEU A CB  1 
ATOM   980  C CG  . LEU A 1 130 ? 4.200  -16.064 -17.325 1.00 28.75  ?  187 LEU A CG  1 
ATOM   981  C CD1 . LEU A 1 130 ? 3.104  -16.916 -16.715 1.00 34.96  ?  187 LEU A CD1 1 
ATOM   982  C CD2 . LEU A 1 130 ? 5.564  -16.675 -17.014 1.00 24.27  ?  187 LEU A CD2 1 
ATOM   983  N N   . THR A 1 131 ? 4.783  -14.272 -21.812 1.00 21.10  ?  188 THR A N   1 
ATOM   984  C CA  . THR A 1 131 ? 4.896  -14.273 -23.262 1.00 26.12  ?  188 THR A CA  1 
ATOM   985  C C   . THR A 1 131 ? 6.277  -14.689 -23.753 1.00 23.27  ?  188 THR A C   1 
ATOM   986  O O   . THR A 1 131 ? 6.407  -15.068 -24.929 1.00 29.10  ?  188 THR A O   1 
ATOM   987  C CB  . THR A 1 131 ? 4.546  -12.886 -23.811 1.00 31.52  ?  188 THR A CB  1 
ATOM   988  O OG1 . THR A 1 131 ? 5.358  -11.895 -23.160 1.00 30.29  ?  188 THR A OG1 1 
ATOM   989  C CG2 . THR A 1 131 ? 3.065  -12.572 -23.636 1.00 35.45  ?  188 THR A CG2 1 
ATOM   990  N N   . SER A 1 132 ? 7.306  -14.620 -22.909 1.00 23.77  ?  189 SER A N   1 
ATOM   991  C CA  . SER A 1 132 ? 8.671  -14.941 -23.326 1.00 20.24  ?  189 SER A CA  1 
ATOM   992  C C   . SER A 1 132 ? 8.979  -16.392 -22.987 1.00 19.73  ?  189 SER A C   1 
ATOM   993  O O   . SER A 1 132 ? 8.753  -16.826 -21.851 1.00 20.62  ?  189 SER A O   1 
ATOM   994  C CB  . SER A 1 132 ? 9.687  -14.024 -22.640 1.00 25.33  ?  189 SER A CB  1 
ATOM   995  O OG  . SER A 1 132 ? 10.916 -14.711 -22.446 1.00 28.16  ?  189 SER A OG  1 
ATOM   996  N N   A VAL A 1 133 ? 9.479  -17.136 -23.979 0.55 21.36  ?  190 VAL A N   1 
ATOM   997  N N   B VAL A 1 133 ? 9.497  -17.143 -23.968 0.45 21.33  ?  190 VAL A N   1 
ATOM   998  C CA  A VAL A 1 133 ? 9.847  -18.529 -23.747 0.55 22.59  ?  190 VAL A CA  1 
ATOM   999  C CA  B VAL A 1 133 ? 9.828  -18.545 -23.712 0.45 22.56  ?  190 VAL A CA  1 
ATOM   1000 C C   A VAL A 1 133 ? 10.835 -18.648 -22.589 0.55 20.26  ?  190 VAL A C   1 
ATOM   1001 C C   B VAL A 1 133 ? 10.859 -18.674 -22.598 0.45 20.28  ?  190 VAL A C   1 
ATOM   1002 O O   A VAL A 1 133 ? 10.714 -19.544 -21.748 0.55 18.09  ?  190 VAL A O   1 
ATOM   1003 O O   B VAL A 1 133 ? 10.795 -19.613 -21.798 0.45 18.14  ?  190 VAL A O   1 
ATOM   1004 C CB  A VAL A 1 133 ? 10.399 -19.158 -25.041 0.55 25.03  ?  190 VAL A CB  1 
ATOM   1005 C CB  B VAL A 1 133 ? 10.299 -19.253 -25.002 0.45 25.19  ?  190 VAL A CB  1 
ATOM   1006 C CG1 A VAL A 1 133 ? 10.781 -20.571 -24.777 0.55 28.57  ?  190 VAL A CG1 1 
ATOM   1007 C CG1 B VAL A 1 133 ? 9.129  -19.495 -25.930 0.45 31.09  ?  190 VAL A CG1 1 
ATOM   1008 C CG2 A VAL A 1 133 ? 9.350  -19.124 -26.135 0.55 32.47  ?  190 VAL A CG2 1 
ATOM   1009 C CG2 B VAL A 1 133 ? 11.385 -18.461 -25.699 0.45 23.62  ?  190 VAL A CG2 1 
ATOM   1010 N N   . SER A 1 134 ? 11.817 -17.745 -22.507 1.00 19.53  ?  191 SER A N   1 
ATOM   1011 C CA  . SER A 1 134 ? 12.805 -17.854 -21.431 1.00 20.18  ?  191 SER A CA  1 
ATOM   1012 C C   . SER A 1 134 ? 12.153 -17.672 -20.067 1.00 17.31  ?  191 SER A C   1 
ATOM   1013 O O   . SER A 1 134 ? 12.460 -18.404 -19.113 1.00 16.24  ?  191 SER A O   1 
ATOM   1014 C CB  . SER A 1 134 ? 13.928 -16.832 -21.617 1.00 24.62  ?  191 SER A CB  1 
ATOM   1015 O OG  . SER A 1 134 ? 14.985 -17.393 -22.376 1.00 40.70  ?  191 SER A OG  1 
ATOM   1016 N N   . ALA A 1 135 ? 11.256 -16.694 -19.947 1.00 15.07  ?  192 ALA A N   1 
ATOM   1017 C CA  . ALA A 1 135 ? 10.591 -16.493 -18.668 1.00 14.50  ?  192 ALA A CA  1 
ATOM   1018 C C   . ALA A 1 135 ? 9.772  -17.716 -18.282 1.00 15.67  ?  192 ALA A C   1 
ATOM   1019 O O   . ALA A 1 135 ? 9.774  -18.129 -17.112 1.00 14.82  ?  192 ALA A O   1 
ATOM   1020 C CB  . ALA A 1 135 ? 9.695  -15.254 -18.712 1.00 16.82  ?  192 ALA A CB  1 
ATOM   1021 N N   . ARG A 1 136 ? 9.088  -18.324 -19.265 1.00 16.24  ?  193 ARG A N   1 
ATOM   1022 C CA  . ARG A 1 136 ? 8.246  -19.488 -18.994 1.00 17.19  ?  193 ARG A CA  1 
ATOM   1023 C C   . ARG A 1 136 ? 9.084  -20.674 -18.543 1.00 18.38  ?  193 ARG A C   1 
ATOM   1024 O O   . ARG A 1 136 ? 8.730  -21.357 -17.578 1.00 15.91  ?  193 ARG A O   1 
ATOM   1025 C CB  . ARG A 1 136 ? 7.427  -19.854 -20.244 1.00 19.87  ?  193 ARG A CB  1 
ATOM   1026 C CG  . ARG A 1 136 ? 6.542  -21.081 -20.019 1.00 31.69  ?  193 ARG A CG  1 
ATOM   1027 C CD  . ARG A 1 136 ? 5.415  -21.179 -21.046 1.00 37.37  ?  193 ARG A CD  1 
ATOM   1028 N NE  . ARG A 1 136 ? 5.874  -21.180 -22.433 1.00 45.32  ?  193 ARG A NE  1 
ATOM   1029 C CZ  . ARG A 1 136 ? 6.667  -22.098 -22.979 1.00 51.38  ?  193 ARG A CZ  1 
ATOM   1030 N NH1 . ARG A 1 136 ? 7.105  -23.142 -22.290 1.00 51.39  ?  193 ARG A NH1 1 
ATOM   1031 N NH2 . ARG A 1 136 ? 7.023  -21.968 -24.255 1.00 63.73  ?  193 ARG A NH2 1 
ATOM   1032 N N   . LEU A 1 137 ? 10.218 -20.913 -19.213 1.00 16.07  ?  194 LEU A N   1 
ATOM   1033 C CA  . LEU A 1 137 ? 11.056 -22.058 -18.861 1.00 16.96  ?  194 LEU A CA  1 
ATOM   1034 C C   . LEU A 1 137 ? 11.712 -21.891 -17.490 1.00 15.66  ?  194 LEU A C   1 
ATOM   1035 O O   . LEU A 1 137 ? 11.861 -22.873 -16.748 1.00 16.63  ?  194 LEU A O   1 
ATOM   1036 C CB  . LEU A 1 137 ? 12.116 -22.261 -19.938 1.00 20.19  ?  194 LEU A CB  1 
ATOM   1037 C CG  . LEU A 1 137 ? 11.538 -22.849 -21.225 1.00 24.52  ?  194 LEU A CG  1 
ATOM   1038 C CD1 . LEU A 1 137 ? 12.634 -23.007 -22.250 1.00 32.47  ?  194 LEU A CD1 1 
ATOM   1039 C CD2 . LEU A 1 137 ? 10.819 -24.170 -20.950 1.00 32.17  ?  194 LEU A CD2 1 
ATOM   1040 N N   . ARG A 1 138 ? 12.097 -20.664 -17.126 1.00 12.68  ?  195 ARG A N   1 
ATOM   1041 C CA  . ARG A 1 138 ? 12.632 -20.418 -15.784 1.00 13.81  ?  195 ARG A CA  1 
ATOM   1042 C C   . ARG A 1 138 ? 11.575 -20.638 -14.718 1.00 16.03  ?  195 ARG A C   1 
ATOM   1043 O O   . ARG A 1 138 ? 11.853 -21.267 -13.688 1.00 16.01  ?  195 ARG A O   1 
ATOM   1044 C CB  . ARG A 1 138 ? 13.213 -19.009 -15.679 1.00 15.55  ?  195 ARG A CB  1 
ATOM   1045 C CG  . ARG A 1 138 ? 14.483 -18.853 -16.499 1.00 14.60  ?  195 ARG A CG  1 
ATOM   1046 C CD  . ARG A 1 138 ? 14.949 -17.390 -16.598 1.00 13.66  ?  195 ARG A CD  1 
ATOM   1047 N NE  . ARG A 1 138 ? 15.857 -17.237 -17.730 1.00 14.87  ?  195 ARG A NE  1 
ATOM   1048 C CZ  . ARG A 1 138 ? 16.352 -16.075 -18.137 1.00 13.91  ?  195 ARG A CZ  1 
ATOM   1049 N NH1 . ARG A 1 138 ? 16.072 -14.946 -17.499 1.00 14.64  ?  195 ARG A NH1 1 
ATOM   1050 N NH2 . ARG A 1 138 ? 17.132 -16.037 -19.222 1.00 15.22  ?  195 ARG A NH2 1 
ATOM   1051 N N   . PHE A 1 139 ? 10.364 -20.101 -14.938 1.00 14.70  ?  196 PHE A N   1 
ATOM   1052 C CA  . PHE A 1 139 ? 9.220  -20.374 -14.062 1.00 15.59  ?  196 PHE A CA  1 
ATOM   1053 C C   . PHE A 1 139 ? 9.006  -21.872 -13.901 1.00 16.71  ?  196 PHE A C   1 
ATOM   1054 O O   . PHE A 1 139 ? 8.885  -22.373 -12.783 1.00 15.79  ?  196 PHE A O   1 
ATOM   1055 C CB  . PHE A 1 139 ? 7.952  -19.711 -14.628 1.00 16.31  ?  196 PHE A CB  1 
ATOM   1056 C CG  . PHE A 1 139 ? 6.708  -19.836 -13.752 1.00 16.50  ?  196 PHE A CG  1 
ATOM   1057 C CD1 . PHE A 1 139 ? 5.462  -19.573 -14.297 1.00 25.06  ?  196 PHE A CD1 1 
ATOM   1058 C CD2 . PHE A 1 139 ? 6.779  -20.119 -12.394 1.00 19.76  ?  196 PHE A CD2 1 
ATOM   1059 C CE1 . PHE A 1 139 ? 4.306  -19.666 -13.536 1.00 33.03  ?  196 PHE A CE1 1 
ATOM   1060 C CE2 . PHE A 1 139 ? 5.631  -20.220 -11.621 1.00 21.94  ?  196 PHE A CE2 1 
ATOM   1061 C CZ  . PHE A 1 139 ? 4.393  -19.991 -12.189 1.00 35.82  ?  196 PHE A CZ  1 
ATOM   1062 N N   . GLU A 1 140 ? 8.920  -22.600 -15.014 1.00 14.61  ?  197 GLU A N   1 
ATOM   1063 C CA  . GLU A 1 140 ? 8.666  -24.036 -14.931 1.00 16.81  ?  197 GLU A CA  1 
ATOM   1064 C C   . GLU A 1 140 ? 9.794  -24.748 -14.198 1.00 17.56  ?  197 GLU A C   1 
ATOM   1065 O O   . GLU A 1 140 ? 9.547  -25.678 -13.413 1.00 19.03  ?  197 GLU A O   1 
ATOM   1066 C CB  . GLU A 1 140 ? 8.451  -24.599 -16.337 1.00 18.04  ?  197 GLU A CB  1 
ATOM   1067 C CG  . GLU A 1 140 ? 7.086  -24.178 -16.878 1.00 28.40  ?  197 GLU A CG  1 
ATOM   1068 C CD  . GLU A 1 140 ? 6.880  -24.436 -18.366 1.00 43.57  ?  197 GLU A CD  1 
ATOM   1069 O OE1 . GLU A 1 140 ? 7.807  -24.940 -19.042 1.00 42.86  ?  197 GLU A OE1 1 
ATOM   1070 O OE2 . GLU A 1 140 ? 5.773  -24.111 -18.859 1.00 29.19  -1 197 GLU A OE2 1 
ATOM   1071 N N   . GLY A 1 141 ? 11.037 -24.320 -14.428 1.00 15.88  ?  198 GLY A N   1 
ATOM   1072 C CA  . GLY A 1 141 ? 12.157 -24.914 -13.714 1.00 15.67  ?  198 GLY A CA  1 
ATOM   1073 C C   . GLY A 1 141 ? 12.102 -24.663 -12.219 1.00 17.22  ?  198 GLY A C   1 
ATOM   1074 O O   . GLY A 1 141 ? 12.389 -25.557 -11.420 1.00 15.90  ?  198 GLY A O   1 
ATOM   1075 N N   . TRP A 1 142 ? 11.781 -23.430 -11.818 1.00 13.17  ?  199 TRP A N   1 
ATOM   1076 C CA  . TRP A 1 142 ? 11.641 -23.131 -10.396 1.00 12.54  ?  199 TRP A CA  1 
ATOM   1077 C C   . TRP A 1 142 ? 10.580 -24.008 -9.756  1.00 15.59  ?  199 TRP A C   1 
ATOM   1078 O O   . TRP A 1 142 ? 10.795 -24.578 -8.673  1.00 15.79  ?  199 TRP A O   1 
ATOM   1079 C CB  . TRP A 1 142 ? 11.245 -21.673 -10.210 1.00 15.44  ?  199 TRP A CB  1 
ATOM   1080 C CG  . TRP A 1 142 ? 12.334 -20.674 -10.437 1.00 13.87  ?  199 TRP A CG  1 
ATOM   1081 C CD1 . TRP A 1 142 ? 13.685 -20.852 -10.296 1.00 12.20  ?  199 TRP A CD1 1 
ATOM   1082 C CD2 . TRP A 1 142 ? 12.138 -19.308 -10.811 1.00 14.07  ?  199 TRP A CD2 1 
ATOM   1083 N NE1 . TRP A 1 142 ? 14.346 -19.655 -10.573 1.00 13.28  ?  199 TRP A NE1 1 
ATOM   1084 C CE2 . TRP A 1 142 ? 13.404 -18.704 -10.888 1.00 13.07  ?  199 TRP A CE2 1 
ATOM   1085 C CE3 . TRP A 1 142 ? 10.994 -18.536 -11.082 1.00 11.83  ?  199 TRP A CE3 1 
ATOM   1086 C CZ2 . TRP A 1 142 ? 13.571 -17.358 -11.214 1.00 13.15  ?  199 TRP A CZ2 1 
ATOM   1087 C CZ3 . TRP A 1 142 ? 11.152 -17.195 -11.407 1.00 13.16  ?  199 TRP A CZ3 1 
ATOM   1088 C CH2 . TRP A 1 142 ? 12.443 -16.623 -11.478 1.00 14.01  ?  199 TRP A CH2 1 
ATOM   1089 N N   . ARG A 1 143 ? 9.402  -24.076 -10.382 1.00 16.04  ?  200 ARG A N   1 
ATOM   1090 C CA  . ARG A 1 143 ? 8.312  -24.877 -9.832  1.00 17.12  ?  200 ARG A CA  1 
ATOM   1091 C C   . ARG A 1 143 ? 8.729  -26.332 -9.699  1.00 18.77  ?  200 ARG A C   1 
ATOM   1092 O O   . ARG A 1 143 ? 8.444  -26.987 -8.687  1.00 17.35  ?  200 ARG A O   1 
ATOM   1093 C CB  . ARG A 1 143 ? 7.066  -24.765 -10.721 1.00 16.94  ?  200 ARG A CB  1 
ATOM   1094 C CG  . ARG A 1 143 ? 5.829  -25.454 -10.146 1.00 30.54  ?  200 ARG A CG  1 
ATOM   1095 C CD  . ARG A 1 143 ? 4.512  -24.816 -10.654 1.00 46.11  ?  200 ARG A CD  1 
ATOM   1096 N NE  . ARG A 1 143 ? 4.420  -24.565 -12.095 1.00 66.81  ?  200 ARG A NE  1 
ATOM   1097 C CZ  . ARG A 1 143 ? 4.833  -25.376 -13.067 1.00 60.29  ?  200 ARG A CZ  1 
ATOM   1098 N NH1 . ARG A 1 143 ? 5.268  -26.604 -12.821 1.00 53.76  ?  200 ARG A NH1 1 
ATOM   1099 N NH2 . ARG A 1 143 ? 4.771  -24.959 -14.330 1.00 57.71  ?  200 ARG A NH2 1 
ATOM   1100 N N   . GLN A 1 144 ? 9.408  -26.858 -10.715 1.00 16.61  ?  201 GLN A N   1 
ATOM   1101 C CA  . GLN A 1 144 ? 9.712  -28.278 -10.689 1.00 18.66  ?  201 GLN A CA  1 
ATOM   1102 C C   . GLN A 1 144 ? 10.805 -28.588 -9.671  1.00 18.62  ?  201 GLN A C   1 
ATOM   1103 O O   . GLN A 1 144 ? 10.741 -29.623 -9.000  1.00 18.96  ?  201 GLN A O   1 
ATOM   1104 C CB  . GLN A 1 144 ? 10.084 -28.748 -12.095 1.00 23.00  ?  201 GLN A CB  1 
ATOM   1105 C CG  . GLN A 1 144 ? 8.816  -29.124 -12.859 1.00 37.21  ?  201 GLN A CG  1 
ATOM   1106 C CD  . GLN A 1 144 ? 7.689  -29.643 -11.931 1.00 67.30  ?  201 GLN A CD  1 
ATOM   1107 O OE1 . GLN A 1 144 ? 6.714  -28.925 -11.656 1.00 49.45  ?  201 GLN A OE1 1 
ATOM   1108 N NE2 . GLN A 1 144 ? 7.827  -30.880 -11.447 1.00 60.83  ?  201 GLN A NE2 1 
ATOM   1109 N N   . THR A 1 145 ? 11.804 -27.715 -9.533  1.00 15.53  ?  202 THR A N   1 
ATOM   1110 C CA  . THR A 1 145 ? 12.832 -27.958 -8.519  1.00 14.61  ?  202 THR A CA  1 
ATOM   1111 C C   . THR A 1 145 ? 12.262 -27.808 -7.110  1.00 17.14  ?  202 THR A C   1 
ATOM   1112 O O   . THR A 1 145 ? 12.619 -28.578 -6.207  1.00 18.03  ?  202 THR A O   1 
ATOM   1113 C CB  . THR A 1 145 ? 14.031 -27.023 -8.728  1.00 14.11  ?  202 THR A CB  1 
ATOM   1114 O OG1 . THR A 1 145 ? 14.437 -27.083 -10.102 1.00 16.05  ?  202 THR A OG1 1 
ATOM   1115 C CG2 . THR A 1 145 ? 15.200 -27.450 -7.851  1.00 16.36  ?  202 THR A CG2 1 
ATOM   1116 N N   . LEU A 1 146 ? 11.394 -26.822 -6.889  1.00 14.40  ?  203 LEU A N   1 
ATOM   1117 C CA  . LEU A 1 146 ? 10.706 -26.737 -5.597  1.00 14.08  ?  203 LEU A CA  1 
ATOM   1118 C C   . LEU A 1 146 ? 9.928  -28.021 -5.310  1.00 15.74  ?  203 LEU A C   1 
ATOM   1119 O O   . LEU A 1 146 ? 9.907  -28.502 -4.167  1.00 16.89  ?  203 LEU A O   1 
ATOM   1120 C CB  . LEU A 1 146 ? 9.759  -25.522 -5.561  1.00 15.36  ?  203 LEU A CB  1 
ATOM   1121 C CG  . LEU A 1 146 ? 10.459 -24.157 -5.417  1.00 14.90  ?  203 LEU A CG  1 
ATOM   1122 C CD1 . LEU A 1 146 ? 9.469  -23.039 -5.721  1.00 16.95  ?  203 LEU A CD1 1 
ATOM   1123 C CD2 . LEU A 1 146 ? 11.029 -23.991 -4.017  1.00 16.55  ?  203 LEU A CD2 1 
ATOM   1124 N N   . ALA A 1 147 ? 9.274  -28.589 -6.331  1.00 15.60  ?  204 ALA A N   1 
ATOM   1125 C CA  . ALA A 1 147 ? 8.489  -29.803 -6.117  1.00 17.11  ?  204 ALA A CA  1 
ATOM   1126 C C   . ALA A 1 147 ? 9.372  -30.994 -5.763  1.00 21.29  ?  204 ALA A C   1 
ATOM   1127 O O   . ALA A 1 147 ? 8.926  -31.910 -5.065  1.00 19.51  ?  204 ALA A O   1 
ATOM   1128 C CB  . ALA A 1 147 ? 7.648  -30.102 -7.357  1.00 20.04  ?  204 ALA A CB  1 
ATOM   1129 N N   . GLN A 1 148 ? 10.621 -30.995 -6.222  1.00 18.69  ?  205 GLN A N   1 
ATOM   1130 C CA  . GLN A 1 148 ? 11.549 -32.045 -5.821  1.00 19.49  ?  205 GLN A CA  1 
ATOM   1131 C C   . GLN A 1 148 ? 11.859 -31.996 -4.331  1.00 19.17  ?  205 GLN A C   1 
ATOM   1132 O O   . GLN A 1 148 ? 12.344 -32.989 -3.777  1.00 20.91  ?  205 GLN A O   1 
ATOM   1133 C CB  . GLN A 1 148 ? 12.846 -31.951 -6.632  1.00 22.95  ?  205 GLN A CB  1 
ATOM   1134 C CG  . GLN A 1 148 ? 12.691 -32.449 -8.054  1.00 26.39  ?  205 GLN A CG  1 
ATOM   1135 C CD  . GLN A 1 148 ? 13.657 -31.813 -9.016  1.00 47.81  ?  205 GLN A CD  1 
ATOM   1136 O OE1 . GLN A 1 148 ? 14.576 -31.099 -8.611  1.00 44.53  ?  205 GLN A OE1 1 
ATOM   1137 N NE2 . GLN A 1 148 ? 13.472 -32.087 -10.305 1.00 57.85  ?  205 GLN A NE2 1 
ATOM   1138 N N   . HIS A 1 149 ? 11.592 -30.865 -3.678  1.00 16.62  ?  206 HIS A N   1 
ATOM   1139 C CA  . HIS A 1 149 ? 11.725 -30.723 -2.235  1.00 18.28  ?  206 HIS A CA  1 
ATOM   1140 C C   . HIS A 1 149 ? 10.370 -30.647 -1.546  1.00 23.12  ?  206 HIS A C   1 
ATOM   1141 O O   . HIS A 1 149 ? 10.287 -30.238 -0.386  1.00 19.83  ?  206 HIS A O   1 
ATOM   1142 C CB  . HIS A 1 149 ? 12.588 -29.494 -1.909  1.00 15.84  ?  206 HIS A CB  1 
ATOM   1143 C CG  . HIS A 1 149 ? 13.998 -29.611 -2.401  1.00 20.14  ?  206 HIS A CG  1 
ATOM   1144 N ND1 . HIS A 1 149 ? 14.987 -30.247 -1.680  1.00 20.80  ?  206 HIS A ND1 1 
ATOM   1145 C CD2 . HIS A 1 149 ? 14.571 -29.224 -3.565  1.00 20.96  ?  206 HIS A CD2 1 
ATOM   1146 C CE1 . HIS A 1 149 ? 16.112 -30.232 -2.373  1.00 20.96  ?  206 HIS A CE1 1 
ATOM   1147 N NE2 . HIS A 1 149 ? 15.890 -29.610 -3.518  1.00 22.80  ?  206 HIS A NE2 1 
ATOM   1148 N N   . GLN A 1 150 ? 9.307  -31.043 -2.248  1.00 20.20  ?  207 GLN A N   1 
ATOM   1149 C CA  . GLN A 1 150 ? 7.942  -31.096 -1.713  1.00 18.34  ?  207 GLN A CA  1 
ATOM   1150 C C   . GLN A 1 150 ? 7.463  -29.722 -1.248  1.00 18.88  ?  207 GLN A C   1 
ATOM   1151 O O   . GLN A 1 150 ? 6.725  -29.597 -0.260  1.00 20.81  ?  207 GLN A O   1 
ATOM   1152 C CB  . GLN A 1 150 ? 7.839  -32.135 -0.603  1.00 18.17  ?  207 GLN A CB  1 
ATOM   1153 C CG  . GLN A 1 150 ? 8.067  -33.562 -1.113  1.00 21.29  ?  207 GLN A CG  1 
ATOM   1154 C CD  . GLN A 1 150 ? 9.557  -33.897 -1.298  1.00 23.83  ?  207 GLN A CD  1 
ATOM   1155 O OE1 . GLN A 1 150 ? 10.402 -33.514 -0.490  1.00 22.88  ?  207 GLN A OE1 1 
ATOM   1156 N NE2 . GLN A 1 150 ? 9.870  -34.628 -2.362  1.00 27.45  ?  207 GLN A NE2 1 
ATOM   1157 N N   . LEU A 1 151 ? 7.855  -28.692 -2.003  1.00 18.90  ?  208 LEU A N   1 
ATOM   1158 C CA  . LEU A 1 151 ? 7.497  -27.310 -1.732  1.00 15.88  ?  208 LEU A CA  1 
ATOM   1159 C C   . LEU A 1 151 ? 6.699  -26.730 -2.888  1.00 19.16  ?  208 LEU A C   1 
ATOM   1160 O O   . LEU A 1 151 ? 6.886  -27.114 -4.047  1.00 19.07  ?  208 LEU A O   1 
ATOM   1161 C CB  . LEU A 1 151 ? 8.751  -26.425 -1.521  1.00 18.84  ?  208 LEU A CB  1 
ATOM   1162 C CG  . LEU A 1 151 ? 9.614  -26.743 -0.305  1.00 18.39  ?  208 LEU A CG  1 
ATOM   1163 C CD1 . LEU A 1 151 ? 10.891 -25.946 -0.332  1.00 17.95  ?  208 LEU A CD1 1 
ATOM   1164 C CD2 . LEU A 1 151 ? 8.825  -26.425 0.970   1.00 20.93  ?  208 LEU A CD2 1 
ATOM   1165 N N   A GLN A 1 152 ? 5.807  -25.787 -2.555  0.56 18.09  ?  209 GLN A N   1 
ATOM   1166 N N   B GLN A 1 152 ? 5.829  -25.789 -2.560  0.44 18.09  ?  209 GLN A N   1 
ATOM   1167 C CA  A GLN A 1 152 ? 5.169  -24.864 -3.487  0.56 18.46  ?  209 GLN A CA  1 
ATOM   1168 C CA  B GLN A 1 152 ? 5.208  -24.873 -3.502  0.44 18.49  ?  209 GLN A CA  1 
ATOM   1169 C C   A GLN A 1 152 ? 5.767  -23.476 -3.287  0.56 17.22  ?  209 GLN A C   1 
ATOM   1170 C C   B GLN A 1 152 ? 5.772  -23.476 -3.288  0.44 17.26  ?  209 GLN A C   1 
ATOM   1171 O O   A GLN A 1 152 ? 6.166  -23.134 -2.168  0.56 19.91  ?  209 GLN A O   1 
ATOM   1172 O O   B GLN A 1 152 ? 6.150  -23.128 -2.164  0.44 19.91  ?  209 GLN A O   1 
ATOM   1173 C CB  A GLN A 1 152 ? 3.649  -24.774 -3.271  0.56 19.98  ?  209 GLN A CB  1 
ATOM   1174 C CB  B GLN A 1 152 ? 3.685  -24.823 -3.325  0.44 20.09  ?  209 GLN A CB  1 
ATOM   1175 C CG  A GLN A 1 152 ? 2.883  -26.046 -3.554  0.56 19.07  ?  209 GLN A CG  1 
ATOM   1176 C CG  B GLN A 1 152 ? 2.930  -25.912 -4.038  0.44 20.20  ?  209 GLN A CG  1 
ATOM   1177 C CD  A GLN A 1 152 ? 2.521  -26.204 -5.013  0.56 24.48  ?  209 GLN A CD  1 
ATOM   1178 C CD  B GLN A 1 152 ? 1.479  -25.931 -3.639  0.44 20.74  ?  209 GLN A CD  1 
ATOM   1179 O OE1 A GLN A 1 152 ? 2.500  -25.231 -5.770  0.56 25.40  ?  209 GLN A OE1 1 
ATOM   1180 O OE1 B GLN A 1 152 ? 1.078  -25.255 -2.692  0.44 24.19  ?  209 GLN A OE1 1 
ATOM   1181 N NE2 A GLN A 1 152 ? 2.226  -27.436 -5.416  0.56 23.69  ?  209 GLN A NE2 1 
ATOM   1182 N NE2 B GLN A 1 152 ? 0.679  -26.715 -4.351  0.44 22.27  ?  209 GLN A NE2 1 
ATOM   1183 N N   . PRO A 1 153 ? 5.847  -22.648 -4.327  1.00 17.38  ?  210 PRO A N   1 
ATOM   1184 C CA  . PRO A 1 153 ? 6.199  -21.240 -4.099  1.00 16.43  ?  210 PRO A CA  1 
ATOM   1185 C C   . PRO A 1 153 ? 5.148  -20.589 -3.202  1.00 18.86  ?  210 PRO A C   1 
ATOM   1186 O O   . PRO A 1 153 ? 3.949  -20.884 -3.293  1.00 19.26  ?  210 PRO A O   1 
ATOM   1187 C CB  . PRO A 1 153 ? 6.205  -20.629 -5.505  1.00 16.35  ?  210 PRO A CB  1 
ATOM   1188 C CG  . PRO A 1 153 ? 5.347  -21.529 -6.321  1.00 18.23  ?  210 PRO A CG  1 
ATOM   1189 C CD  . PRO A 1 153 ? 5.454  -22.927 -5.715  1.00 17.89  ?  210 PRO A CD  1 
ATOM   1190 N N   . ILE A 1 154 ? 5.613  -19.730 -2.290  1.00 17.51  ?  211 ILE A N   1 
ATOM   1191 C CA  . ILE A 1 154 ? 4.688  -19.031 -1.397  1.00 19.90  ?  211 ILE A CA  1 
ATOM   1192 C C   . ILE A 1 154 ? 3.982  -17.886 -2.112  1.00 19.86  ?  211 ILE A C   1 
ATOM   1193 O O   . ILE A 1 154 ? 2.901  -17.463 -1.688  1.00 21.99  ?  211 ILE A O   1 
ATOM   1194 C CB  . ILE A 1 154 ? 5.437  -18.542 -0.148  1.00 24.12  ?  211 ILE A CB  1 
ATOM   1195 C CG1 . ILE A 1 154 ? 4.475  -18.418 1.027   1.00 27.87  ?  211 ILE A CG1 1 
ATOM   1196 C CG2 . ILE A 1 154 ? 6.181  -17.263 -0.430  1.00 20.09  ?  211 ILE A CG2 1 
ATOM   1197 C CD1 . ILE A 1 154 ? 5.133  -18.049 2.328   1.00 40.47  ?  211 ILE A CD1 1 
ATOM   1198 N N   . ALA A 1 155 ? 4.551  -17.398 -3.210  1.00 16.03  ?  212 ALA A N   1 
ATOM   1199 C CA  . ALA A 1 155 ? 3.927  -16.366 -4.013  1.00 15.91  ?  212 ALA A CA  1 
ATOM   1200 C C   . ALA A 1 155 ? 4.543  -16.461 -5.393  1.00 14.66  ?  212 ALA A C   1 
ATOM   1201 O O   . ALA A 1 155 ? 5.685  -16.912 -5.537  1.00 15.55  ?  212 ALA A O   1 
ATOM   1202 C CB  . ALA A 1 155 ? 4.139  -14.972 -3.416  1.00 24.53  ?  212 ALA A CB  1 
ATOM   1203 N N   . VAL A 1 156 ? 3.762  -16.094 -6.405  1.00 15.25  ?  213 VAL A N   1 
ATOM   1204 C CA  . VAL A 1 156 ? 4.235  -16.032 -7.782  1.00 14.72  ?  213 VAL A CA  1 
ATOM   1205 C C   . VAL A 1 156 ? 3.777  -14.701 -8.367  1.00 16.65  ?  213 VAL A C   1 
ATOM   1206 O O   . VAL A 1 156 ? 2.572  -14.452 -8.490  1.00 18.53  ?  213 VAL A O   1 
ATOM   1207 C CB  . VAL A 1 156 ? 3.719  -17.206 -8.635  1.00 17.02  ?  213 VAL A CB  1 
ATOM   1208 C CG1 . VAL A 1 156 ? 4.259  -17.099 -10.081 1.00 19.58  ?  213 VAL A CG1 1 
ATOM   1209 C CG2 . VAL A 1 156 ? 4.117  -18.538 -8.026  1.00 17.56  ?  213 VAL A CG2 1 
ATOM   1210 N N   . LEU A 1 157 ? 4.738  -13.860 -8.727  1.00 14.50  ?  214 LEU A N   1 
ATOM   1211 C CA  . LEU A 1 157 ? 4.517  -12.523 -9.264  1.00 15.26  ?  214 LEU A CA  1 
ATOM   1212 C C   . LEU A 1 157 ? 5.080  -12.493 -10.679 1.00 16.82  ?  214 LEU A C   1 
ATOM   1213 O O   . LEU A 1 157 ? 5.940  -13.295 -11.019 1.00 13.62  ?  214 LEU A O   1 
ATOM   1214 C CB  . LEU A 1 157 ? 5.208  -11.471 -8.377  1.00 19.39  ?  214 LEU A CB  1 
ATOM   1215 C CG  . LEU A 1 157 ? 4.591  -11.141 -6.994  1.00 22.11  ?  214 LEU A CG  1 
ATOM   1216 C CD1 . LEU A 1 157 ? 3.155  -10.655 -7.115  1.00 22.80  ?  214 LEU A CD1 1 
ATOM   1217 C CD2 . LEU A 1 157 ? 4.676  -12.320 -6.025  1.00 28.20  ?  214 LEU A CD2 1 
ATOM   1218 N N   . HIS A 1 158 ? 4.590  -11.576 -11.512 1.00 15.48  ?  215 HIS A N   1 
ATOM   1219 C CA  . HIS A 1 158 ? 4.976  -11.513 -12.920 1.00 16.61  ?  215 HIS A CA  1 
ATOM   1220 C C   . HIS A 1 158 ? 5.384  -10.093 -13.282 1.00 16.49  ?  215 HIS A C   1 
ATOM   1221 O O   . HIS A 1 158 ? 4.560  -9.171  -13.226 1.00 15.58  ?  215 HIS A O   1 
ATOM   1222 C CB  . HIS A 1 158 ? 3.839  -11.978 -13.836 1.00 15.54  ?  215 HIS A CB  1 
ATOM   1223 C CG  . HIS A 1 158 ? 3.239  -13.290 -13.436 1.00 18.00  ?  215 HIS A CG  1 
ATOM   1224 N ND1 . HIS A 1 158 ? 3.917  -14.487 -13.556 1.00 19.84  ?  215 HIS A ND1 1 
ATOM   1225 C CD2 . HIS A 1 158 ? 2.046  -13.590 -12.872 1.00 22.32  ?  215 HIS A CD2 1 
ATOM   1226 C CE1 . HIS A 1 158 ? 3.148  -15.473 -13.114 1.00 19.25  ?  215 HIS A CE1 1 
ATOM   1227 N NE2 . HIS A 1 158 ? 2.007  -14.955 -12.696 1.00 22.59  ?  215 HIS A NE2 1 
ATOM   1228 N N   . GLY A 1 159 ? 6.639  -9.935  -13.706 1.00 14.08  ?  216 GLY A N   1 
ATOM   1229 C CA  . GLY A 1 159 ? 7.185  -8.664  -14.113 1.00 15.31  ?  216 GLY A CA  1 
ATOM   1230 C C   . GLY A 1 159 ? 7.376  -8.584  -15.616 1.00 15.35  ?  216 GLY A C   1 
ATOM   1231 O O   . GLY A 1 159 ? 6.914  -9.442  -16.367 1.00 17.68  ?  216 GLY A O   1 
ATOM   1232 N N   . ASP A 1 160 ? 8.057  -7.508  -16.049 1.00 12.04  ?  217 ASP A N   1 
ATOM   1233 C CA  . ASP A 1 160 ? 8.210  -7.249  -17.481 1.00 13.01  ?  217 ASP A CA  1 
ATOM   1234 C C   . ASP A 1 160 ? 9.663  -7.077  -17.900 1.00 13.36  ?  217 ASP A C   1 
ATOM   1235 O O   . ASP A 1 160 ? 9.922  -6.549  -18.995 1.00 14.71  ?  217 ASP A O   1 
ATOM   1236 C CB  . ASP A 1 160 ? 7.389  -6.027  -17.911 1.00 13.56  ?  217 ASP A CB  1 
ATOM   1237 C CG  . ASP A 1 160 ? 7.904  -4.721  -17.335 1.00 15.29  ?  217 ASP A CG  1 
ATOM   1238 O OD1 . ASP A 1 160 ? 9.018  -4.682  -16.766 1.00 15.13  ?  217 ASP A OD1 1 
ATOM   1239 O OD2 . ASP A 1 160 ? 7.197  -3.695  -17.489 1.00 21.68  -1 217 ASP A OD2 1 
ATOM   1240 N N   . TRP A 1 161 ? 10.598 -7.538  -17.059 1.00 12.63  ?  218 TRP A N   1 
ATOM   1241 C CA  . TRP A 1 161 ? 12.060 -7.512  -17.175 1.00 12.68  ?  218 TRP A CA  1 
ATOM   1242 C C   . TRP A 1 161 ? 12.664 -6.208  -16.667 1.00 11.63  ?  218 TRP A C   1 
ATOM   1243 O O   . TRP A 1 161 ? 13.882 -6.132  -16.530 1.00 11.19  ?  218 TRP A O   1 
ATOM   1244 C CB  . TRP A 1 161 ? 12.571 -7.758  -18.606 1.00 13.46  ?  218 TRP A CB  1 
ATOM   1245 C CG  . TRP A 1 161 ? 12.245 -9.077  -19.287 1.00 10.72  ?  218 TRP A CG  1 
ATOM   1246 C CD1 . TRP A 1 161 ? 11.659 -9.217  -20.519 1.00 12.03  ?  218 TRP A CD1 1 
ATOM   1247 C CD2 . TRP A 1 161 ? 12.586 -10.389 -18.854 1.00 11.08  ?  218 TRP A CD2 1 
ATOM   1248 N NE1 . TRP A 1 161 ? 11.591 -10.544 -20.864 1.00 14.64  ?  218 TRP A NE1 1 
ATOM   1249 C CE2 . TRP A 1 161 ? 12.170 -11.286 -19.866 1.00 12.71  ?  218 TRP A CE2 1 
ATOM   1250 C CE3 . TRP A 1 161 ? 13.191 -10.905 -17.695 1.00 11.43  ?  218 TRP A CE3 1 
ATOM   1251 C CZ2 . TRP A 1 161 ? 12.326 -12.676 -19.755 1.00 12.53  ?  218 TRP A CZ2 1 
ATOM   1252 C CZ3 . TRP A 1 161 ? 13.380 -12.284 -17.593 1.00 13.19  ?  218 TRP A CZ3 1 
ATOM   1253 C CH2 . TRP A 1 161 ? 12.931 -13.155 -18.618 1.00 13.20  ?  218 TRP A CH2 1 
ATOM   1254 N N   . SER A 1 162 ? 11.853 -5.175  -16.375 1.00 12.78  ?  219 SER A N   1 
ATOM   1255 C CA  . SER A 1 162 ? 12.398 -3.881  -15.964 1.00 10.70  ?  219 SER A CA  1 
ATOM   1256 C C   . SER A 1 162 ? 12.531 -3.780  -14.455 1.00 11.75  ?  219 SER A C   1 
ATOM   1257 O O   . SER A 1 162 ? 11.838 -4.459  -13.702 1.00 12.37  ?  219 SER A O   1 
ATOM   1258 C CB  . SER A 1 162 ? 11.507 -2.743  -16.451 1.00 13.15  ?  219 SER A CB  1 
ATOM   1259 O OG  . SER A 1 162 ? 10.308 -2.685  -15.676 1.00 14.36  ?  219 SER A OG  1 
ATOM   1260 N N   . ALA A 1 163 ? 13.422 -2.882  -14.024 1.00 10.25  ?  220 ALA A N   1 
ATOM   1261 C CA  . ALA A 1 163 ? 13.588 -2.662  -12.585 1.00 11.66  ?  220 ALA A CA  1 
ATOM   1262 C C   . ALA A 1 163 ? 12.291 -2.173  -11.938 1.00 13.38  ?  220 ALA A C   1 
ATOM   1263 O O   . ALA A 1 163 ? 11.925 -2.634  -10.849 1.00 12.33  ?  220 ALA A O   1 
ATOM   1264 C CB  . ALA A 1 163 ? 14.724 -1.662  -12.327 1.00 10.84  ?  220 ALA A CB  1 
ATOM   1265 N N   . LEU A 1 164 ? 11.597 -1.229  -12.576 1.00 10.82  ?  221 LEU A N   1 
ATOM   1266 C CA  . LEU A 1 164 ? 10.364 -0.722  -11.985 1.00 11.09  ?  221 LEU A CA  1 
ATOM   1267 C C   . LEU A 1 164 ? 9.357  -1.845  -11.756 1.00 13.05  ?  221 LEU A C   1 
ATOM   1268 O O   . LEU A 1 164 ? 8.662  -1.863  -10.741 1.00 13.02  ?  221 LEU A O   1 
ATOM   1269 C CB  . LEU A 1 164 ? 9.765  0.364   -12.875 1.00 12.53  ?  221 LEU A CB  1 
ATOM   1270 C CG  . LEU A 1 164 ? 8.511  1.009   -12.308 1.00 15.21  ?  221 LEU A CG  1 
ATOM   1271 C CD1 . LEU A 1 164 ? 8.781  1.636   -10.943 1.00 14.91  ?  221 LEU A CD1 1 
ATOM   1272 C CD2 . LEU A 1 164 ? 8.046  2.071   -13.302 1.00 19.48  ?  221 LEU A CD2 1 
ATOM   1273 N N   A SER A 1 165 ? 9.235  -2.781  -12.704 0.76 12.19  ?  222 SER A N   1 
ATOM   1274 N N   B SER A 1 165 ? 9.267  -2.789  -12.690 0.24 12.31  ?  222 SER A N   1 
ATOM   1275 C CA  A SER A 1 165 ? 8.327  -3.907  -12.489 0.76 12.18  ?  222 SER A CA  1 
ATOM   1276 C CA  B SER A 1 165 ? 8.348  -3.901  -12.501 0.24 12.29  ?  222 SER A CA  1 
ATOM   1277 C C   A SER A 1 165 ? 8.764  -4.775  -11.303 0.76 13.09  ?  222 SER A C   1 
ATOM   1278 C C   B SER A 1 165 ? 8.764  -4.772  -11.316 0.24 13.13  ?  222 SER A C   1 
ATOM   1279 O O   A SER A 1 165 ? 7.923  -5.283  -10.544 0.76 13.77  ?  222 SER A O   1 
ATOM   1280 O O   B SER A 1 165 ? 7.909  -5.275  -10.575 0.24 13.70  ?  222 SER A O   1 
ATOM   1281 C CB  A SER A 1 165 ? 8.204  -4.743  -13.777 0.76 14.47  ?  222 SER A CB  1 
ATOM   1282 C CB  B SER A 1 165 ? 8.268  -4.721  -13.785 0.24 14.35  ?  222 SER A CB  1 
ATOM   1283 O OG  A SER A 1 165 ? 9.269  -5.673  -13.947 0.76 14.25  ?  222 SER A OG  1 
ATOM   1284 O OG  B SER A 1 165 ? 7.303  -5.737  -13.662 0.24 13.34  ?  222 SER A OG  1 
ATOM   1285 N N   . GLY A 1 166 ? 10.070 -4.961  -11.118 1.00 13.38  ?  223 GLY A N   1 
ATOM   1286 C CA  . GLY A 1 166 ? 10.539 -5.663  -9.923  1.00 12.07  ?  223 GLY A CA  1 
ATOM   1287 C C   . GLY A 1 166 ? 10.148 -4.948  -8.644  1.00 12.91  ?  223 GLY A C   1 
ATOM   1288 O O   . GLY A 1 166 ? 9.697  -5.575  -7.679  1.00 13.28  ?  223 GLY A O   1 
ATOM   1289 N N   . TYR A 1 167 ? 10.293 -3.615  -8.620  1.00 12.63  ?  224 TYR A N   1 
ATOM   1290 C CA  . TYR A 1 167 ? 9.818  -2.836  -7.476  1.00 11.59  ?  224 TYR A CA  1 
ATOM   1291 C C   . TYR A 1 167 ? 8.314  -3.029  -7.253  1.00 14.96  ?  224 TYR A C   1 
ATOM   1292 O O   . TYR A 1 167 ? 7.873  -3.326  -6.135  1.00 13.19  ?  224 TYR A O   1 
ATOM   1293 C CB  . TYR A 1 167 ? 10.145 -1.349  -7.688  1.00 12.35  ?  224 TYR A CB  1 
ATOM   1294 C CG  . TYR A 1 167 ? 9.504  -0.476  -6.636  1.00 12.21  ?  224 TYR A CG  1 
ATOM   1295 C CD1 . TYR A 1 167 ? 10.089 -0.344  -5.388  1.00 12.42  ?  224 TYR A CD1 1 
ATOM   1296 C CD2 . TYR A 1 167 ? 8.295  0.191   -6.876  1.00 12.37  ?  224 TYR A CD2 1 
ATOM   1297 C CE1 . TYR A 1 167 ? 9.498  0.432   -4.402  1.00 13.48  ?  224 TYR A CE1 1 
ATOM   1298 C CE2 . TYR A 1 167 ? 7.682  0.964   -5.887  1.00 15.07  ?  224 TYR A CE2 1 
ATOM   1299 C CZ  . TYR A 1 167 ? 8.291  1.082   -4.646  1.00 16.41  ?  224 TYR A CZ  1 
ATOM   1300 O OH  . TYR A 1 167 ? 7.694  1.853   -3.654  1.00 18.05  ?  224 TYR A OH  1 
ATOM   1301 N N   . GLN A 1 168 ? 7.492  -2.828  -8.293  1.00 11.62  ?  225 GLN A N   1 
ATOM   1302 C CA  . GLN A 1 168 ? 6.044  -2.874  -8.070  1.00 12.92  ?  225 GLN A CA  1 
ATOM   1303 C C   . GLN A 1 168 ? 5.587  -4.272  -7.694  1.00 12.78  ?  225 GLN A C   1 
ATOM   1304 O O   . GLN A 1 168 ? 4.726  -4.431  -6.826  1.00 15.45  ?  225 GLN A O   1 
ATOM   1305 C CB  . GLN A 1 168 ? 5.276  -2.388  -9.304  1.00 14.02  ?  225 GLN A CB  1 
ATOM   1306 C CG  . GLN A 1 168 ? 5.513  -0.935  -9.713  1.00 17.51  ?  225 GLN A CG  1 
ATOM   1307 C CD  . GLN A 1 168 ? 5.052  0.135   -8.719  1.00 21.01  ?  225 GLN A CD  1 
ATOM   1308 O OE1 . GLN A 1 168 ? 5.415  1.307   -8.872  1.00 24.33  ?  225 GLN A OE1 1 
ATOM   1309 N NE2 . GLN A 1 168 ? 4.258  -0.244  -7.722  1.00 20.40  ?  225 GLN A NE2 1 
ATOM   1310 N N   . GLN A 1 169 ? 6.136  -5.304  -8.339  1.00 12.72  ?  226 GLN A N   1 
ATOM   1311 C CA  . GLN A 1 169 ? 5.718  -6.666  -8.017  1.00 12.95  ?  226 GLN A CA  1 
ATOM   1312 C C   . GLN A 1 169 ? 6.157  -7.075  -6.619  1.00 13.64  ?  226 GLN A C   1 
ATOM   1313 O O   . GLN A 1 169 ? 5.424  -7.797  -5.926  1.00 14.09  ?  226 GLN A O   1 
ATOM   1314 C CB  . GLN A 1 169 ? 6.262  -7.652  -9.045  1.00 14.08  ?  226 GLN A CB  1 
ATOM   1315 C CG  . GLN A 1 169 ? 5.597  -7.502  -10.415 1.00 14.56  ?  226 GLN A CG  1 
ATOM   1316 C CD  . GLN A 1 169 ? 4.075  -7.608  -10.323 1.00 20.28  ?  226 GLN A CD  1 
ATOM   1317 O OE1 . GLN A 1 169 ? 3.556  -8.622  -9.879  1.00 21.78  ?  226 GLN A OE1 1 
ATOM   1318 N NE2 . GLN A 1 169 ? 3.366  -6.555  -10.719 1.00 20.30  ?  226 GLN A NE2 1 
ATOM   1319 N N   . THR A 1 170 ? 7.334  -6.621  -6.184  1.00 12.26  ?  227 THR A N   1 
ATOM   1320 C CA  . THR A 1 170 ? 7.775  -6.925  -4.824  1.00 12.62  ?  227 THR A CA  1 
ATOM   1321 C C   . THR A 1 170 ? 6.918  -6.196  -3.793  1.00 14.66  ?  227 THR A C   1 
ATOM   1322 O O   . THR A 1 170 ? 6.552  -6.783  -2.765  1.00 13.95  ?  227 THR A O   1 
ATOM   1323 C CB  . THR A 1 170 ? 9.273  -6.600  -4.667  1.00 11.26  ?  227 THR A CB  1 
ATOM   1324 O OG1 . THR A 1 170 ? 10.029 -7.376  -5.608  1.00 13.88  ?  227 THR A OG1 1 
ATOM   1325 C CG2 . THR A 1 170 ? 9.764  -7.001  -3.276  1.00 14.92  ?  227 THR A CG2 1 
ATOM   1326 N N   . MET A 1 171 ? 6.535  -4.940  -4.058  1.00 14.16  ?  228 MET A N   1 
ATOM   1327 C CA  . MET A 1 171 ? 5.600  -4.299  -3.137  1.00 14.33  ?  228 MET A CA  1 
ATOM   1328 C C   . MET A 1 171 ? 4.264  -5.031  -3.090  1.00 13.69  ?  228 MET A C   1 
ATOM   1329 O O   . MET A 1 171 ? 3.689  -5.202  -2.013  1.00 16.76  ?  228 MET A O   1 
ATOM   1330 C CB  . MET A 1 171 ? 5.386  -2.831  -3.481  1.00 14.33  ?  228 MET A CB  1 
ATOM   1331 C CG  . MET A 1 171 ? 6.661  -2.000  -3.412  1.00 16.01  ?  228 MET A CG  1 
ATOM   1332 S SD  . MET A 1 171 ? 7.244  -1.838  -1.703  1.00 17.84  ?  228 MET A SD  1 
ATOM   1333 C CE  . MET A 1 171 ? 5.989  -0.787  -0.961  1.00 22.72  ?  228 MET A CE  1 
ATOM   1334 N N   . GLN A 1 172 ? 3.753  -5.465  -4.248  1.00 15.53  ?  229 GLN A N   1 
ATOM   1335 C CA  . GLN A 1 172 ? 2.531  -6.261  -4.273  1.00 16.80  ?  229 GLN A CA  1 
ATOM   1336 C C   . GLN A 1 172 ? 2.692  -7.543  -3.457  1.00 16.44  ?  229 GLN A C   1 
ATOM   1337 O O   . GLN A 1 172 ? 1.801  -7.907  -2.663  1.00 19.35  ?  229 GLN A O   1 
ATOM   1338 C CB  . GLN A 1 172 ? 2.167  -6.565  -5.735  1.00 17.13  ?  229 GLN A CB  1 
ATOM   1339 C CG  . GLN A 1 172 ? 0.839  -7.258  -5.936  1.00 18.61  ?  229 GLN A CG  1 
ATOM   1340 C CD  . GLN A 1 172 ? 0.531  -7.455  -7.416  1.00 20.75  ?  229 GLN A CD  1 
ATOM   1341 O OE1 . GLN A 1 172 ? 0.579  -6.512  -8.209  1.00 23.50  ?  229 GLN A OE1 1 
ATOM   1342 N NE2 . GLN A 1 172 ? 0.210  -8.682  -7.788  1.00 26.17  ?  229 GLN A NE2 1 
ATOM   1343 N N   . MET A 1 173 ? 3.834  -8.219  -3.598  1.00 16.59  ?  230 MET A N   1 
ATOM   1344 C CA  . MET A 1 173 ? 4.017  -9.482  -2.894  1.00 17.39  ?  230 MET A CA  1 
ATOM   1345 C C   . MET A 1 173 ? 4.021  -9.255  -1.384  1.00 20.97  ?  230 MET A C   1 
ATOM   1346 O O   . MET A 1 173 ? 3.398  -10.017 -0.637  1.00 18.98  ?  230 MET A O   1 
ATOM   1347 C CB  . MET A 1 173 ? 5.303  -10.156 -3.377  1.00 17.96  ?  230 MET A CB  1 
ATOM   1348 C CG  . MET A 1 173 ? 5.907  -11.214 -2.448  1.00 20.09  ?  230 MET A CG  1 
ATOM   1349 S SD  . MET A 1 173 ? 7.619  -11.591 -2.789  1.00 21.60  ?  230 MET A SD  1 
ATOM   1350 C CE  . MET A 1 173 ? 8.488  -10.318 -1.880  1.00 19.36  ?  230 MET A CE  1 
ATOM   1351 N N   . LEU A 1 174 ? 4.611  -8.138  -0.930  1.00 15.31  ?  231 LEU A N   1 
ATOM   1352 C CA  . LEU A 1 174 ? 4.675  -7.848  0.495   1.00 16.82  ?  231 LEU A CA  1 
ATOM   1353 C C   . LEU A 1 174 ? 3.321  -7.433  1.046   1.00 23.36  ?  231 LEU A C   1 
ATOM   1354 O O   . LEU A 1 174 ? 3.088  -7.551  2.254   1.00 23.33  ?  231 LEU A O   1 
ATOM   1355 C CB  . LEU A 1 174 ? 5.720  -6.761  0.767   1.00 15.63  ?  231 LEU A CB  1 
ATOM   1356 C CG  . LEU A 1 174 ? 7.168  -7.138  0.435   1.00 16.56  ?  231 LEU A CG  1 
ATOM   1357 C CD1 . LEU A 1 174 ? 8.049  -5.918  0.586   1.00 18.93  ?  231 LEU A CD1 1 
ATOM   1358 C CD2 . LEU A 1 174 ? 7.680  -8.262  1.315   1.00 19.63  ?  231 LEU A CD2 1 
ATOM   1359 N N   . ASN A 1 175 ? 2.414  -6.977  0.187   1.00 18.44  ?  232 ASN A N   1 
ATOM   1360 C CA  . ASN A 1 175 ? 1.062  -6.679  0.642   1.00 24.20  ?  232 ASN A CA  1 
ATOM   1361 C C   . ASN A 1 175 ? 0.273  -7.941  0.956   1.00 25.56  ?  232 ASN A C   1 
ATOM   1362 O O   . ASN A 1 175 ? -0.737 -7.869  1.671   1.00 31.45  ?  232 ASN A O   1 
ATOM   1363 C CB  . ASN A 1 175 ? 0.332  -5.871  -0.432  1.00 26.59  ?  232 ASN A CB  1 
ATOM   1364 C CG  . ASN A 1 175 ? -0.839 -5.082  0.126   1.00 35.95  ?  232 ASN A CG  1 
ATOM   1365 O OD1 . ASN A 1 175 ? -0.743 -4.488  1.201   1.00 57.89  ?  232 ASN A OD1 1 
ATOM   1366 N ND2 . ASN A 1 175 ? -1.957 -5.086  -0.594  1.00 44.44  ?  232 ASN A ND2 1 
ATOM   1367 N N   . GLU A 1 176 ? 0.694  -9.087  0.416   1.00 25.01  ?  233 GLU A N   1 
ATOM   1368 C CA  . GLU A 1 176 ? -0.036 -10.339 0.526   1.00 27.89  ?  233 GLU A CA  1 
ATOM   1369 C C   . GLU A 1 176 ? 0.634  -11.354 1.437   1.00 32.52  ?  233 GLU A C   1 
ATOM   1370 O O   . GLU A 1 176 ? -0.028 -12.298 1.870   1.00 39.34  ?  233 GLU A O   1 
ATOM   1371 C CB  . GLU A 1 176 ? -0.215 -10.959 -0.870  1.00 32.59  ?  233 GLU A CB  1 
ATOM   1372 C CG  . GLU A 1 176 ? -1.083 -10.130 -1.814  1.00 44.88  ?  233 GLU A CG  1 
ATOM   1373 C CD  . GLU A 1 176 ? -1.098 -10.666 -3.248  1.00 64.03  ?  233 GLU A CD  1 
ATOM   1374 O OE1 . GLU A 1 176 ? -1.503 -9.919  -4.172  1.00 53.84  ?  233 GLU A OE1 1 
ATOM   1375 O OE2 . GLU A 1 176 ? -0.664 -11.819 -3.462  1.00 55.74  -1 233 GLU A OE2 1 
ATOM   1376 N N   . GLY A 1 177 ? 1.917  -11.191 1.733   1.00 31.51  ?  234 GLY A N   1 
ATOM   1377 C CA  . GLY A 1 177 ? 2.616  -12.188 2.519   1.00 29.76  ?  234 GLY A CA  1 
ATOM   1378 C C   . GLY A 1 177 ? 4.059  -11.799 2.732   1.00 25.51  ?  234 GLY A C   1 
ATOM   1379 O O   . GLY A 1 177 ? 4.505  -10.727 2.323   1.00 26.60  ?  234 GLY A O   1 
ATOM   1380 N N   . LEU A 1 178 ? 4.793  -12.697 3.386   1.00 23.97  ?  235 LEU A N   1 
ATOM   1381 C CA  . LEU A 1 178 ? 6.178  -12.428 3.759   1.00 24.11  ?  235 LEU A CA  1 
ATOM   1382 C C   . LEU A 1 178 ? 6.998  -13.676 3.472   1.00 19.74  ?  235 LEU A C   1 
ATOM   1383 O O   . LEU A 1 178 ? 7.028  -14.616 4.285   1.00 23.74  ?  235 LEU A O   1 
ATOM   1384 C CB  . LEU A 1 178 ? 6.287  -12.010 5.222   1.00 34.70  ?  235 LEU A CB  1 
ATOM   1385 C CG  . LEU A 1 178 ? 7.695  -11.588 5.648   1.00 31.54  ?  235 LEU A CG  1 
ATOM   1386 C CD1 . LEU A 1 178 ? 8.244  -10.470 4.785   1.00 30.45  ?  235 LEU A CD1 1 
ATOM   1387 C CD2 . LEU A 1 178 ? 7.700  -11.189 7.125   1.00 39.42  ?  235 LEU A CD2 1 
ATOM   1388 N N   . PRO A 1 179 ? 7.681  -13.724 2.339   1.00 16.57  ?  236 PRO A N   1 
ATOM   1389 C CA  . PRO A 1 179 ? 8.592  -14.834 2.084   1.00 17.60  ?  236 PRO A CA  1 
ATOM   1390 C C   . PRO A 1 179 ? 9.881  -14.601 2.860   1.00 18.30  ?  236 PRO A C   1 
ATOM   1391 O O   . PRO A 1 179 ? 10.149 -13.502 3.341   1.00 19.33  ?  236 PRO A O   1 
ATOM   1392 C CB  . PRO A 1 179 ? 8.831  -14.743 0.576   1.00 18.49  ?  236 PRO A CB  1 
ATOM   1393 C CG  . PRO A 1 179 ? 8.823  -13.291 0.324   1.00 20.08  ?  236 PRO A CG  1 
ATOM   1394 C CD  . PRO A 1 179 ? 7.751  -12.714 1.264   1.00 19.60  ?  236 PRO A CD  1 
ATOM   1395 N N   . THR A 1 180 ? 10.700 -15.646 2.959   1.00 15.13  ?  237 THR A N   1 
ATOM   1396 C CA  . THR A 1 180 ? 12.065 -15.447 3.430   1.00 13.43  ?  237 THR A CA  1 
ATOM   1397 C C   . THR A 1 180 ? 13.071 -15.349 2.292   1.00 14.66  ?  237 THR A C   1 
ATOM   1398 O O   . THR A 1 180 ? 14.203 -14.924 2.533   1.00 15.08  ?  237 THR A O   1 
ATOM   1399 C CB  . THR A 1 180 ? 12.498 -16.560 4.404   1.00 16.04  ?  237 THR A CB  1 
ATOM   1400 O OG1 . THR A 1 180 ? 12.503 -17.845 3.760   1.00 16.87  ?  237 THR A OG1 1 
ATOM   1401 C CG2 . THR A 1 180 ? 11.563 -16.625 5.612   1.00 17.66  ?  237 THR A CG2 1 
ATOM   1402 N N   . ALA A 1 181 ? 12.674 -15.693 1.057   1.00 12.10  ?  238 ALA A N   1 
ATOM   1403 C CA  . ALA A 1 181 ? 13.584 -15.610 -0.078  1.00 11.38  ?  238 ALA A CA  1 
ATOM   1404 C C   . ALA A 1 181 ? 12.777 -15.357 -1.334  1.00 13.63  ?  238 ALA A C   1 
ATOM   1405 O O   . ALA A 1 181 ? 11.613 -15.778 -1.431  1.00 14.46  ?  238 ALA A O   1 
ATOM   1406 C CB  . ALA A 1 181 ? 14.412 -16.893 -0.248  1.00 13.78  ?  238 ALA A CB  1 
ATOM   1407 N N   . LEU A 1 182 ? 13.431 -14.707 -2.308  1.00 11.84  ?  239 LEU A N   1 
ATOM   1408 C CA  . LEU A 1 182 ? 12.834 -14.330 -3.588  1.00 11.99  ?  239 LEU A CA  1 
ATOM   1409 C C   . LEU A 1 182 ? 13.780 -14.737 -4.704  1.00 13.37  ?  239 LEU A C   1 
ATOM   1410 O O   . LEU A 1 182 ? 14.937 -14.306 -4.713  1.00 14.49  ?  239 LEU A O   1 
ATOM   1411 C CB  . LEU A 1 182 ? 12.588 -12.819 -3.623  1.00 12.36  ?  239 LEU A CB  1 
ATOM   1412 C CG  . LEU A 1 182 ? 11.884 -12.257 -4.851  1.00 16.64  ?  239 LEU A CG  1 
ATOM   1413 C CD1 . LEU A 1 182 ? 10.463 -12.840 -5.062  1.00 17.17  ?  239 LEU A CD1 1 
ATOM   1414 C CD2 . LEU A 1 182 ? 11.814 -10.722 -4.711  1.00 17.96  ?  239 LEU A CD2 1 
ATOM   1415 N N   . LEU A 1 183 ? 13.282 -15.531 -5.651  1.00 12.89  ?  240 LEU A N   1 
ATOM   1416 C CA  . LEU A 1 183 ? 13.974 -15.838 -6.897  1.00 11.73  ?  240 LEU A CA  1 
ATOM   1417 C C   . LEU A 1 183 ? 13.435 -14.897 -7.960  1.00 10.98  ?  240 LEU A C   1 
ATOM   1418 O O   . LEU A 1 183 ? 12.216 -14.814 -8.143  1.00 12.42  ?  240 LEU A O   1 
ATOM   1419 C CB  . LEU A 1 183 ? 13.739 -17.292 -7.330  1.00 12.87  ?  240 LEU A CB  1 
ATOM   1420 C CG  . LEU A 1 183 ? 14.476 -18.327 -6.495  1.00 13.62  ?  240 LEU A CG  1 
ATOM   1421 C CD1 . LEU A 1 183 ? 13.891 -19.733 -6.738  1.00 16.09  ?  240 LEU A CD1 1 
ATOM   1422 C CD2 . LEU A 1 183 ? 15.973 -18.308 -6.848  1.00 14.94  ?  240 LEU A CD2 1 
ATOM   1423 N N   . VAL A 1 184 ? 14.333 -14.180 -8.644  1.00 10.54  ?  241 VAL A N   1 
ATOM   1424 C CA  . VAL A 1 184 ? 13.925 -13.170 -9.623  1.00 10.53  ?  241 VAL A CA  1 
ATOM   1425 C C   . VAL A 1 184 ? 14.444 -13.583 -10.997 1.00 12.82  ?  241 VAL A C   1 
ATOM   1426 O O   . VAL A 1 184 ? 15.564 -14.090 -11.128 1.00 13.25  ?  241 VAL A O   1 
ATOM   1427 C CB  . VAL A 1 184 ? 14.450 -11.779 -9.215  1.00 9.54   ?  241 VAL A CB  1 
ATOM   1428 C CG1 . VAL A 1 184 ? 13.848 -10.696 -10.109 1.00 12.85  ?  241 VAL A CG1 1 
ATOM   1429 C CG2 . VAL A 1 184 ? 14.093 -11.502 -7.770  1.00 10.68  ?  241 VAL A CG2 1 
ATOM   1430 N N   . ALA A 1 185 ? 13.631 -13.361 -12.035 1.00 10.84  ?  242 ALA A N   1 
ATOM   1431 C CA  . ALA A 1 185 ? 13.969 -13.893 -13.346 1.00 10.20  ?  242 ALA A CA  1 
ATOM   1432 C C   . ALA A 1 185 ? 15.019 -13.078 -14.086 1.00 12.44  ?  242 ALA A C   1 
ATOM   1433 O O   . ALA A 1 185 ? 15.504 -13.542 -15.116 1.00 11.68  ?  242 ALA A O   1 
ATOM   1434 C CB  . ALA A 1 185 ? 12.721 -13.992 -14.216 1.00 11.92  ?  242 ALA A CB  1 
ATOM   1435 N N   . ASN A 1 186 ? 15.367 -11.873 -13.626 1.00 10.31  ?  243 ASN A N   1 
ATOM   1436 C CA  . ASN A 1 186 ? 16.574 -11.235 -14.154 1.00 10.34  ?  243 ASN A CA  1 
ATOM   1437 C C   . ASN A 1 186 ? 17.113 -10.237 -13.142 1.00 12.60  ?  243 ASN A C   1 
ATOM   1438 O O   . ASN A 1 186 ? 16.498 -9.966  -12.102 1.00 12.00  ?  243 ASN A O   1 
ATOM   1439 C CB  . ASN A 1 186 ? 16.366 -10.608 -15.558 1.00 11.13  ?  243 ASN A CB  1 
ATOM   1440 C CG  . ASN A 1 186 ? 15.652 -9.277  -15.545 1.00 11.55  ?  243 ASN A CG  1 
ATOM   1441 O OD1 . ASN A 1 186 ? 15.030 -8.898  -14.567 1.00 12.55  ?  243 ASN A OD1 1 
ATOM   1442 N ND2 . ASN A 1 186 ? 15.747 -8.554  -16.665 1.00 12.15  ?  243 ASN A ND2 1 
ATOM   1443 N N   . ASP A 1 187 ? 18.303 -9.705  -13.454 1.00 10.38  ?  244 ASP A N   1 
ATOM   1444 C CA  . ASP A 1 187 ? 18.959 -8.807  -12.510 1.00 10.76  ?  244 ASP A CA  1 
ATOM   1445 C C   . ASP A 1 187 ? 18.290 -7.438  -12.475 1.00 9.72   ?  244 ASP A C   1 
ATOM   1446 O O   . ASP A 1 187 ? 18.303 -6.775  -11.426 1.00 10.75  ?  244 ASP A O   1 
ATOM   1447 C CB  . ASP A 1 187 ? 20.425 -8.631  -12.881 1.00 9.87   ?  244 ASP A CB  1 
ATOM   1448 C CG  . ASP A 1 187 ? 21.274 -9.853  -12.579 1.00 12.96  ?  244 ASP A CG  1 
ATOM   1449 O OD1 . ASP A 1 187 ? 20.784 -10.829 -11.982 1.00 13.78  ?  244 ASP A OD1 1 
ATOM   1450 O OD2 . ASP A 1 187 ? 22.470 -9.804  -12.929 1.00 13.14  -1 244 ASP A OD2 1 
ATOM   1451 N N   . GLN A 1 188 ? 17.754 -6.967  -13.610 1.00 10.27  ?  245 GLN A N   1 
ATOM   1452 C CA  . GLN A 1 188 ? 17.122 -5.646  -13.585 1.00 11.46  ?  245 GLN A CA  1 
ATOM   1453 C C   . GLN A 1 188 ? 15.912 -5.650  -12.661 1.00 10.18  ?  245 GLN A C   1 
ATOM   1454 O O   . GLN A 1 188 ? 15.764 -4.762  -11.806 1.00 12.23  ?  245 GLN A O   1 
ATOM   1455 C CB  . GLN A 1 188 ? 16.721 -5.194  -14.989 1.00 11.18  ?  245 GLN A CB  1 
ATOM   1456 C CG  . GLN A 1 188 ? 17.925 -4.914  -15.853 1.00 13.69  ?  245 GLN A CG  1 
ATOM   1457 C CD  . GLN A 1 188 ? 17.533 -4.356  -17.197 1.00 14.01  ?  245 GLN A CD  1 
ATOM   1458 O OE1 . GLN A 1 188 ? 17.566 -5.056  -18.199 1.00 12.42  ?  245 GLN A OE1 1 
ATOM   1459 N NE2 . GLN A 1 188 ? 17.150 -3.087  -17.224 1.00 12.56  ?  245 GLN A NE2 1 
ATOM   1460 N N   . MET A 1 189 ? 15.057 -6.681  -12.762 1.00 10.58  ?  246 MET A N   1 
ATOM   1461 C CA  . MET A 1 189 ? 13.948 -6.776  -11.817 1.00 10.44  ?  246 MET A CA  1 
ATOM   1462 C C   . MET A 1 189 ? 14.453 -6.947  -10.387 1.00 12.08  ?  246 MET A C   1 
ATOM   1463 O O   . MET A 1 189 ? 13.845 -6.422  -9.457  1.00 11.63  ?  246 MET A O   1 
ATOM   1464 C CB  . MET A 1 189 ? 12.996 -7.909  -12.202 1.00 9.43   ?  246 MET A CB  1 
ATOM   1465 C CG  . MET A 1 189 ? 12.203 -7.599  -13.458 1.00 10.06  ?  246 MET A CG  1 
ATOM   1466 S SD  . MET A 1 189 ? 10.934 -8.847  -13.809 1.00 12.87  ?  246 MET A SD  1 
ATOM   1467 C CE  . MET A 1 189 ? 11.892 -10.388 -13.831 1.00 14.78  ?  246 MET A CE  1 
ATOM   1468 N N   . ALA A 1 190 ? 15.562 -7.672  -10.191 1.00 11.39  ?  247 ALA A N   1 
ATOM   1469 C CA  . ALA A 1 190 ? 16.094 -7.850  -8.832  1.00 9.97   ?  247 ALA A CA  1 
ATOM   1470 C C   . ALA A 1 190 ? 16.502 -6.523  -8.201  1.00 10.11  ?  247 ALA A C   1 
ATOM   1471 O O   . ALA A 1 190 ? 16.350 -6.342  -6.989  1.00 10.20  ?  247 ALA A O   1 
ATOM   1472 C CB  . ALA A 1 190 ? 17.278 -8.826  -8.847  1.00 10.89  ?  247 ALA A CB  1 
ATOM   1473 N N   . LEU A 1 191 ? 17.023 -5.593  -8.995  1.00 10.40  ?  248 LEU A N   1 
ATOM   1474 C CA  . LEU A 1 191 ? 17.358 -4.259  -8.497  1.00 11.14  ?  248 LEU A CA  1 
ATOM   1475 C C   . LEU A 1 191 ? 16.122 -3.604  -7.902  1.00 11.35  ?  248 LEU A C   1 
ATOM   1476 O O   . LEU A 1 191 ? 16.159 -3.062  -6.792  1.00 11.04  ?  248 LEU A O   1 
ATOM   1477 C CB  . LEU A 1 191 ? 17.911 -3.404  -9.635  1.00 10.06  ?  248 LEU A CB  1 
ATOM   1478 C CG  . LEU A 1 191 ? 18.223 -1.940  -9.333  1.00 11.77  ?  248 LEU A CG  1 
ATOM   1479 C CD1 . LEU A 1 191 ? 19.441 -1.900  -8.370  1.00 14.09  ?  248 LEU A CD1 1 
ATOM   1480 C CD2 . LEU A 1 191 ? 18.494 -1.124  -10.589 1.00 15.20  ?  248 LEU A CD2 1 
ATOM   1481 N N   . GLY A 1 192 ? 15.006 -3.648  -8.640  1.00 10.41  ?  249 GLY A N   1 
ATOM   1482 C CA  . GLY A 1 192 ? 13.764 -3.092  -8.114  1.00 12.36  ?  249 GLY A CA  1 
ATOM   1483 C C   . GLY A 1 192 ? 13.278 -3.836  -6.886  1.00 11.71  ?  249 GLY A C   1 
ATOM   1484 O O   . GLY A 1 192 ? 12.740 -3.228  -5.959  1.00 11.73  ?  249 GLY A O   1 
ATOM   1485 N N   . ALA A 1 193 ? 13.440 -5.162  -6.871  1.00 10.48  ?  250 ALA A N   1 
ATOM   1486 C CA  . ALA A 1 193 ? 13.080 -5.926  -5.676  1.00 10.66  ?  250 ALA A CA  1 
ATOM   1487 C C   . ALA A 1 193 ? 13.894 -5.482  -4.458  1.00 11.42  ?  250 ALA A C   1 
ATOM   1488 O O   . ALA A 1 193 ? 13.327 -5.306  -3.363  1.00 12.26  ?  250 ALA A O   1 
ATOM   1489 C CB  . ALA A 1 193 ? 13.247 -7.427  -5.963  1.00 12.01  ?  250 ALA A CB  1 
ATOM   1490 N N   . LEU A 1 194 ? 15.210 -5.253  -4.632  1.00 10.59  ?  251 LEU A N   1 
ATOM   1491 C CA  . LEU A 1 194 ? 16.039 -4.783  -3.519  1.00 10.68  ?  251 LEU A CA  1 
ATOM   1492 C C   . LEU A 1 194 ? 15.533 -3.446  -3.006  1.00 11.40  ?  251 LEU A C   1 
ATOM   1493 O O   . LEU A 1 194 ? 15.492 -3.211  -1.791  1.00 12.07  ?  251 LEU A O   1 
ATOM   1494 C CB  . LEU A 1 194 ? 17.517 -4.681  -3.926  1.00 9.96   ?  251 LEU A CB  1 
ATOM   1495 C CG  . LEU A 1 194 ? 18.228 -5.997  -4.198  1.00 11.39  ?  251 LEU A CG  1 
ATOM   1496 C CD1 . LEU A 1 194 ? 19.610 -5.727  -4.800  1.00 12.01  ?  251 LEU A CD1 1 
ATOM   1497 C CD2 . LEU A 1 194 ? 18.350 -6.863  -2.923  1.00 11.88  ?  251 LEU A CD2 1 
ATOM   1498 N N   . ARG A 1 195 ? 15.174 -2.535  -3.910  1.00 10.43  ?  252 ARG A N   1 
ATOM   1499 C CA  . ARG A 1 195 ? 14.662 -1.243  -3.467  1.00 11.12  ?  252 ARG A CA  1 
ATOM   1500 C C   . ARG A 1 195 ? 13.371 -1.401  -2.663  1.00 12.40  ?  252 ARG A C   1 
ATOM   1501 O O   . ARG A 1 195 ? 13.208 -0.779  -1.606  1.00 13.65  ?  252 ARG A O   1 
ATOM   1502 C CB  . ARG A 1 195 ? 14.442 -0.321  -4.673  1.00 11.69  ?  252 ARG A CB  1 
ATOM   1503 C CG  . ARG A 1 195 ? 13.713 0.955   -4.277  1.00 13.69  ?  252 ARG A CG  1 
ATOM   1504 C CD  . ARG A 1 195 ? 13.388 1.851   -5.471  1.00 14.63  ?  252 ARG A CD  1 
ATOM   1505 N NE  . ARG A 1 195 ? 12.421 2.842   -5.006  1.00 15.78  ?  252 ARG A NE  1 
ATOM   1506 C CZ  . ARG A 1 195 ? 11.375 3.279   -5.689  1.00 18.05  ?  252 ARG A CZ  1 
ATOM   1507 N NH1 . ARG A 1 195 ? 11.193 2.957   -6.965  1.00 17.18  ?  252 ARG A NH1 1 
ATOM   1508 N NH2 . ARG A 1 195 ? 10.480 4.051   -5.073  1.00 20.01  ?  252 ARG A NH2 1 
ATOM   1509 N N   . ALA A 1 196 ? 12.445 -2.239  -3.140  1.00 12.52  ?  253 ALA A N   1 
ATOM   1510 C CA  . ALA A 1 196 ? 11.182 -2.428  -2.417  1.00 12.68  ?  253 ALA A CA  1 
ATOM   1511 C C   . ALA A 1 196 ? 11.416 -3.025  -1.035  1.00 13.53  ?  253 ALA A C   1 
ATOM   1512 O O   . ALA A 1 196 ? 10.783 -2.614  -0.057  1.00 13.89  ?  253 ALA A O   1 
ATOM   1513 C CB  . ALA A 1 196 ? 10.244 -3.324  -3.222  1.00 14.12  ?  253 ALA A CB  1 
ATOM   1514 N N   . LEU A 1 197 ? 12.318 -3.995  -0.934  1.00 13.13  ?  254 LEU A N   1 
ATOM   1515 C CA  . LEU A 1 197 ? 12.611 -4.573  0.375   1.00 12.64  ?  254 LEU A CA  1 
ATOM   1516 C C   . LEU A 1 197 ? 13.241 -3.545  1.300   1.00 12.36  ?  254 LEU A C   1 
ATOM   1517 O O   . LEU A 1 197 ? 12.842 -3.423  2.467   1.00 15.14  ?  254 LEU A O   1 
ATOM   1518 C CB  . LEU A 1 197 ? 13.509 -5.789  0.207   1.00 11.67  ?  254 LEU A CB  1 
ATOM   1519 C CG  . LEU A 1 197 ? 12.840 -6.960  -0.499  1.00 13.52  ?  254 LEU A CG  1 
ATOM   1520 C CD1 . LEU A 1 197 ? 13.869 -7.936  -1.060  1.00 13.17  ?  254 LEU A CD1 1 
ATOM   1521 C CD2 . LEU A 1 197 ? 11.880 -7.681  0.429   1.00 14.93  ?  254 LEU A CD2 1 
ATOM   1522 N N   . SER A 1 198 ? 14.208 -2.776  0.781   1.00 13.08  ?  255 SER A N   1 
ATOM   1523 C CA  . SER A 1 198 ? 14.874 -1.762  1.587   1.00 13.25  ?  255 SER A CA  1 
ATOM   1524 C C   . SER A 1 198 ? 13.890 -0.721  2.098   1.00 16.01  ?  255 SER A C   1 
ATOM   1525 O O   . SER A 1 198 ? 13.873 -0.392  3.295   1.00 17.43  ?  255 SER A O   1 
ATOM   1526 C CB  . SER A 1 198 ? 15.985 -1.110  0.767   1.00 15.06  ?  255 SER A CB  1 
ATOM   1527 O OG  . SER A 1 198 ? 16.580 -0.041  1.508   1.00 17.59  ?  255 SER A OG  1 
ATOM   1528 N N   . GLU A 1 199 ? 13.031 -0.207  1.212   1.00 15.59  ?  256 GLU A N   1 
ATOM   1529 C CA  . GLU A 1 199 ? 12.123 0.860   1.612   1.00 15.27  ?  256 GLU A CA  1 
ATOM   1530 C C   . GLU A 1 199 ? 11.020 0.341   2.525   1.00 16.59  ?  256 GLU A C   1 
ATOM   1531 O O   . GLU A 1 199 ? 10.464 1.112   3.316   1.00 20.71  ?  256 GLU A O   1 
ATOM   1532 C CB  . GLU A 1 199 ? 11.565 1.536   0.348   1.00 17.84  ?  256 GLU A CB  1 
ATOM   1533 C CG  . GLU A 1 199 ? 12.679 2.294   -0.423  1.00 21.09  ?  256 GLU A CG  1 
ATOM   1534 C CD  . GLU A 1 199 ? 12.209 3.062   -1.664  1.00 23.35  ?  256 GLU A CD  1 
ATOM   1535 O OE1 . GLU A 1 199 ? 11.019 2.986   -2.037  1.00 23.44  ?  256 GLU A OE1 1 
ATOM   1536 O OE2 . GLU A 1 199 ? 13.063 3.756   -2.263  1.00 21.09  -1 256 GLU A OE2 1 
ATOM   1537 N N   . SER A 1 200 ? 10.732 -0.956  2.469   1.00 16.24  ?  257 SER A N   1 
ATOM   1538 C CA  . SER A 1 200 ? 9.817  -1.603  3.404   1.00 17.95  ?  257 SER A CA  1 
ATOM   1539 C C   . SER A 1 200 ? 10.469 -1.968  4.733   1.00 19.57  ?  257 SER A C   1 
ATOM   1540 O O   . SER A 1 200 ? 9.783  -2.498  5.616   1.00 25.05  ?  257 SER A O   1 
ATOM   1541 C CB  . SER A 1 200 ? 9.240  -2.864  2.761   1.00 20.65  ?  257 SER A CB  1 
ATOM   1542 O OG  . SER A 1 200 ? 8.546  -2.526  1.574   1.00 19.95  ?  257 SER A OG  1 
ATOM   1543 N N   . GLY A 1 201 ? 11.770 -1.747  4.885   1.00 18.40  ?  258 GLY A N   1 
ATOM   1544 C CA  . GLY A 1 201 ? 12.425 -2.066  6.143   1.00 18.11  ?  258 GLY A CA  1 
ATOM   1545 C C   . GLY A 1 201 ? 12.774 -3.523  6.327   1.00 20.61  ?  258 GLY A C   1 
ATOM   1546 O O   . GLY A 1 201 ? 13.040 -3.945  7.456   1.00 23.11  ?  258 GLY A O   1 
ATOM   1547 N N   . LEU A 1 202 ? 12.782 -4.308  5.260   1.00 19.39  ?  259 LEU A N   1 
ATOM   1548 C CA  . LEU A 1 202 ? 13.197 -5.706  5.310   1.00 17.46  ?  259 LEU A CA  1 
ATOM   1549 C C   . LEU A 1 202 ? 14.660 -5.801  4.898   1.00 19.35  ?  259 LEU A C   1 
ATOM   1550 O O   . LEU A 1 202 ? 14.999 -5.567  3.728   1.00 20.11  ?  259 LEU A O   1 
ATOM   1551 C CB  . LEU A 1 202 ? 12.306 -6.555  4.409   1.00 17.16  ?  259 LEU A CB  1 
ATOM   1552 C CG  . LEU A 1 202 ? 10.894 -6.677  4.975   1.00 19.34  ?  259 LEU A CG  1 
ATOM   1553 C CD1 . LEU A 1 202 ? 9.950  -7.177  3.914   1.00 22.66  ?  259 LEU A CD1 1 
ATOM   1554 C CD2 . LEU A 1 202 ? 10.945 -7.668  6.135   1.00 20.15  ?  259 LEU A CD2 1 
ATOM   1555 N N   . ARG A 1 203 ? 15.519 -6.172  5.846   1.00 17.34  ?  260 ARG A N   1 
ATOM   1556 C CA  . ARG A 1 203 ? 16.951 -6.228  5.571   1.00 17.43  ?  260 ARG A CA  1 
ATOM   1557 C C   . ARG A 1 203 ? 17.303 -7.402  4.658   1.00 15.02  ?  260 ARG A C   1 
ATOM   1558 O O   . ARG A 1 203 ? 16.835 -8.526  4.842   1.00 15.52  ?  260 ARG A O   1 
ATOM   1559 C CB  . ARG A 1 203 ? 17.749 -6.335  6.864   1.00 16.23  ?  260 ARG A CB  1 
ATOM   1560 C CG  . ARG A 1 203 ? 17.698 -5.055  7.714   1.00 23.29  ?  260 ARG A CG  1 
ATOM   1561 C CD  . ARG A 1 203 ? 18.609 -5.130  8.955   1.00 33.69  ?  260 ARG A CD  1 
ATOM   1562 N NE  . ARG A 1 203 ? 18.691 -6.469  9.531   1.00 53.06  ?  260 ARG A NE  1 
ATOM   1563 C CZ  . ARG A 1 203 ? 17.697 -7.085  10.163  1.00 61.34  ?  260 ARG A CZ  1 
ATOM   1564 N NH1 . ARG A 1 203 ? 16.536 -6.484  10.382  1.00 61.99  ?  260 ARG A NH1 1 
ATOM   1565 N NH2 . ARG A 1 203 ? 17.877 -8.332  10.595  1.00 47.86  ?  260 ARG A NH2 1 
ATOM   1566 N N   . VAL A 1 204 ? 18.144 -7.136  3.668   1.00 13.57  ?  261 VAL A N   1 
ATOM   1567 C CA  . VAL A 1 204 ? 18.655 -8.143  2.741   1.00 13.85  ?  261 VAL A CA  1 
ATOM   1568 C C   . VAL A 1 204 ? 20.143 -8.320  3.022   1.00 15.87  ?  261 VAL A C   1 
ATOM   1569 O O   . VAL A 1 204 ? 20.897 -7.341  2.973   1.00 16.41  ?  261 VAL A O   1 
ATOM   1570 C CB  . VAL A 1 204 ? 18.430 -7.742  1.279   1.00 12.42  ?  261 VAL A CB  1 
ATOM   1571 C CG1 . VAL A 1 204 ? 19.175 -8.730  0.340   1.00 14.13  ?  261 VAL A CG1 1 
ATOM   1572 C CG2 . VAL A 1 204 ? 16.937 -7.683  0.932   1.00 14.23  ?  261 VAL A CG2 1 
ATOM   1573 N N   . PRO A 1 205 ? 20.618 -9.536  3.312   1.00 14.45  ?  262 PRO A N   1 
ATOM   1574 C CA  . PRO A 1 205 ? 19.894 -10.806 3.317   1.00 11.63  ?  262 PRO A CA  1 
ATOM   1575 C C   . PRO A 1 205 ? 19.401 -11.272 4.671   1.00 15.19  ?  262 PRO A C   1 
ATOM   1576 O O   . PRO A 1 205 ? 18.865 -12.373 4.741   1.00 19.54  ?  262 PRO A O   1 
ATOM   1577 C CB  . PRO A 1 205 ? 20.949 -11.792 2.796   1.00 13.39  ?  262 PRO A CB  1 
ATOM   1578 C CG  . PRO A 1 205 ? 22.191 -11.308 3.426   1.00 14.61  ?  262 PRO A CG  1 
ATOM   1579 C CD  . PRO A 1 205 ? 22.068 -9.768  3.418   1.00 15.05  ?  262 PRO A CD  1 
ATOM   1580 N N   . ALA A 1 206 ? 19.536 -10.495 5.748   1.00 14.89  ?  263 ALA A N   1 
ATOM   1581 C CA  . ALA A 1 206 ? 19.239 -11.034 7.077   1.00 17.63  ?  263 ALA A CA  1 
ATOM   1582 C C   . ALA A 1 206 ? 17.773 -11.453 7.224   1.00 19.37  ?  263 ALA A C   1 
ATOM   1583 O O   . ALA A 1 206 ? 17.477 -12.455 7.892   1.00 21.19  ?  263 ALA A O   1 
ATOM   1584 C CB  . ALA A 1 206 ? 19.618 -10.020 8.144   1.00 19.50  ?  263 ALA A CB  1 
ATOM   1585 N N   . GLN A 1 207 ? 16.844 -10.727 6.583   1.00 15.66  ?  264 GLN A N   1 
ATOM   1586 C CA  . GLN A 1 207 ? 15.419 -11.033 6.660   1.00 14.43  ?  264 GLN A CA  1 
ATOM   1587 C C   . GLN A 1 207 ? 14.847 -11.609 5.375   1.00 18.30  ?  264 GLN A C   1 
ATOM   1588 O O   . GLN A 1 207 ? 13.937 -12.443 5.433   1.00 15.75  ?  264 GLN A O   1 
ATOM   1589 C CB  . GLN A 1 207 ? 14.627 -9.777  7.045   1.00 16.12  ?  264 GLN A CB  1 
ATOM   1590 C CG  . GLN A 1 207 ? 14.955 -9.327  8.450   1.00 20.54  ?  264 GLN A CG  1 
ATOM   1591 C CD  . GLN A 1 207 ? 14.197 -8.099  8.877   1.00 28.11  ?  264 GLN A CD  1 
ATOM   1592 O OE1 . GLN A 1 207 ? 14.395 -7.020  8.330   1.00 21.59  ?  264 GLN A OE1 1 
ATOM   1593 N NE2 . GLN A 1 207 ? 13.331 -8.251  9.869   1.00 30.94  ?  264 GLN A NE2 1 
ATOM   1594 N N   . VAL A 1 208 ? 15.328 -11.171 4.215   1.00 13.99  ?  265 VAL A N   1 
ATOM   1595 C CA  . VAL A 1 208 ? 14.898 -11.735 2.937   1.00 14.67  ?  265 VAL A CA  1 
ATOM   1596 C C   . VAL A 1 208 ? 16.125 -11.917 2.059   1.00 14.04  ?  265 VAL A C   1 
ATOM   1597 O O   . VAL A 1 208 ? 16.919 -10.981 1.902   1.00 13.64  ?  265 VAL A O   1 
ATOM   1598 C CB  . VAL A 1 208 ? 13.853 -10.854 2.216   1.00 12.51  ?  265 VAL A CB  1 
ATOM   1599 C CG1 . VAL A 1 208 ? 13.471 -11.474 0.908   1.00 15.65  ?  265 VAL A CG1 1 
ATOM   1600 C CG2 . VAL A 1 208 ? 12.614 -10.669 3.104   1.00 14.07  ?  265 VAL A CG2 1 
ATOM   1601 N N   . SER A 1 209 ? 16.300 -13.125 1.511   1.00 12.09  ?  266 SER A N   1 
ATOM   1602 C CA  . SER A 1 209 ? 17.340 -13.403 0.539   1.00 10.94  ?  266 SER A CA  1 
ATOM   1603 C C   . SER A 1 209 ? 16.790 -13.166 -0.863  1.00 11.45  ?  266 SER A C   1 
ATOM   1604 O O   . SER A 1 209 ? 15.607 -13.391 -1.122  1.00 13.85  ?  266 SER A O   1 
ATOM   1605 C CB  . SER A 1 209 ? 17.818 -14.857 0.645   1.00 11.29  ?  266 SER A CB  1 
ATOM   1606 O OG  . SER A 1 209 ? 18.593 -15.066 1.828   1.00 12.57  ?  266 SER A OG  1 
ATOM   1607 N N   . VAL A 1 210 ? 17.665 -12.707 -1.771  1.00 10.88  ?  267 VAL A N   1 
ATOM   1608 C CA  . VAL A 1 210 ? 17.280 -12.411 -3.156  1.00 10.74  ?  267 VAL A CA  1 
ATOM   1609 C C   . VAL A 1 210 ? 18.312 -13.028 -4.100  1.00 11.40  ?  267 VAL A C   1 
ATOM   1610 O O   . VAL A 1 210 ? 19.520 -12.879 -3.879  1.00 12.04  ?  267 VAL A O   1 
ATOM   1611 C CB  . VAL A 1 210 ? 17.202 -10.892 -3.402  1.00 11.17  ?  267 VAL A CB  1 
ATOM   1612 C CG1 . VAL A 1 210 ? 16.824 -10.626 -4.855  1.00 11.23  ?  267 VAL A CG1 1 
ATOM   1613 C CG2 . VAL A 1 210 ? 16.218 -10.231 -2.433  1.00 13.43  ?  267 VAL A CG2 1 
ATOM   1614 N N   . VAL A 1 211 ? 17.846 -13.720 -5.154  1.00 11.22  ?  268 VAL A N   1 
ATOM   1615 C CA  . VAL A 1 211 ? 18.715 -14.252 -6.211  1.00 11.85  ?  268 VAL A CA  1 
ATOM   1616 C C   . VAL A 1 211 ? 18.232 -13.705 -7.546  1.00 10.56  ?  268 VAL A C   1 
ATOM   1617 O O   . VAL A 1 211 ? 17.046 -13.796 -7.857  1.00 12.55  ?  268 VAL A O   1 
ATOM   1618 C CB  . VAL A 1 211 ? 18.717 -15.792 -6.238  1.00 10.73  ?  268 VAL A CB  1 
ATOM   1619 C CG1 . VAL A 1 211 ? 19.683 -16.323 -7.331  1.00 14.36  ?  268 VAL A CG1 1 
ATOM   1620 C CG2 . VAL A 1 211 ? 19.092 -16.359 -4.869  1.00 15.28  ?  268 VAL A CG2 1 
ATOM   1621 N N   . GLY A 1 212 ? 19.146 -13.132 -8.327  1.00 9.33   ?  269 GLY A N   1 
ATOM   1622 C CA  . GLY A 1 212 ? 18.819 -12.642 -9.658  1.00 11.24  ?  269 GLY A CA  1 
ATOM   1623 C C   . GLY A 1 212 ? 19.141 -13.652 -10.744 1.00 12.59  ?  269 GLY A C   1 
ATOM   1624 O O   . GLY A 1 212 ? 19.332 -14.852 -10.498 1.00 12.47  ?  269 GLY A O   1 
ATOM   1625 N N   . TYR A 1 213 ? 19.196 -13.151 -11.974 1.00 11.36  ?  270 TYR A N   1 
ATOM   1626 C CA  . TYR A 1 213 ? 19.467 -14.006 -13.131 1.00 11.17  ?  270 TYR A CA  1 
ATOM   1627 C C   . TYR A 1 213 ? 20.077 -13.144 -14.219 1.00 13.30  ?  270 TYR A C   1 
ATOM   1628 O O   . TYR A 1 213 ? 19.460 -12.147 -14.609 1.00 13.57  ?  270 TYR A O   1 
ATOM   1629 C CB  . TYR A 1 213 ? 18.177 -14.671 -13.603 1.00 12.13  ?  270 TYR A CB  1 
ATOM   1630 C CG  . TYR A 1 213 ? 18.341 -16.006 -14.315 1.00 10.70  ?  270 TYR A CG  1 
ATOM   1631 C CD1 . TYR A 1 213 ? 18.871 -16.091 -15.608 1.00 11.39  ?  270 TYR A CD1 1 
ATOM   1632 C CD2 . TYR A 1 213 ? 17.845 -17.165 -13.728 1.00 14.11  ?  270 TYR A CD2 1 
ATOM   1633 C CE1 . TYR A 1 213 ? 18.976 -17.330 -16.262 1.00 13.54  ?  270 TYR A CE1 1 
ATOM   1634 C CE2 . TYR A 1 213 ? 17.939 -18.408 -14.380 1.00 13.35  ?  270 TYR A CE2 1 
ATOM   1635 C CZ  . TYR A 1 213 ? 18.482 -18.481 -15.639 1.00 15.39  ?  270 TYR A CZ  1 
ATOM   1636 O OH  . TYR A 1 213 ? 18.563 -19.732 -16.267 1.00 16.20  ?  270 TYR A OH  1 
ATOM   1637 N N   . ASP A 1 214 ? 21.273 -13.526 -14.696 1.00 12.42  ?  271 ASP A N   1 
ATOM   1638 C CA  . ASP A 1 214 ? 22.016 -12.985 -15.851 1.00 11.61  ?  271 ASP A CA  1 
ATOM   1639 C C   . ASP A 1 214 ? 23.445 -12.695 -15.447 1.00 13.03  ?  271 ASP A C   1 
ATOM   1640 O O   . ASP A 1 214 ? 24.367 -12.987 -16.210 1.00 11.97  ?  271 ASP A O   1 
ATOM   1641 C CB  . ASP A 1 214 ? 21.467 -11.672 -16.442 1.00 13.72  ?  271 ASP A CB  1 
ATOM   1642 C CG  . ASP A 1 214 ? 20.252 -11.874 -17.324 1.00 14.51  ?  271 ASP A CG  1 
ATOM   1643 O OD1 . ASP A 1 214 ? 19.984 -13.006 -17.795 1.00 14.03  ?  271 ASP A OD1 1 
ATOM   1644 O OD2 . ASP A 1 214 ? 19.521 -10.878 -17.527 1.00 13.65  -1 271 ASP A OD2 1 
ATOM   1645 N N   . ASP A 1 215 ? 23.628 -12.071 -14.285 1.00 11.49  ?  272 ASP A N   1 
ATOM   1646 C CA  . ASP A 1 215 ? 24.874 -11.366 -13.942 1.00 10.84  ?  272 ASP A CA  1 
ATOM   1647 C C   . ASP A 1 215 ? 25.231 -10.357 -15.035 1.00 10.20  ?  272 ASP A C   1 
ATOM   1648 O O   . ASP A 1 215 ? 26.335 -10.342 -15.590 1.00 12.79  ?  272 ASP A O   1 
ATOM   1649 C CB  . ASP A 1 215 ? 26.045 -12.339 -13.679 1.00 10.44  ?  272 ASP A CB  1 
ATOM   1650 C CG  . ASP A 1 215 ? 27.188 -11.691 -12.888 1.00 13.66  ?  272 ASP A CG  1 
ATOM   1651 O OD1 . ASP A 1 215 ? 26.920 -10.741 -12.131 1.00 15.32  ?  272 ASP A OD1 1 
ATOM   1652 O OD2 . ASP A 1 215 ? 28.345 -12.138 -13.059 1.00 19.19  -1 272 ASP A OD2 1 
ATOM   1653 N N   . THR A 1 216 ? 24.276 -9.467  -15.305 1.00 11.87  ?  273 THR A N   1 
ATOM   1654 C CA  . THR A 1 216 ? 24.603 -8.328  -16.149 1.00 12.15  ?  273 THR A CA  1 
ATOM   1655 C C   . THR A 1 216 ? 25.561 -7.397  -15.389 1.00 11.36  ?  273 THR A C   1 
ATOM   1656 O O   . THR A 1 216 ? 25.737 -7.498  -14.167 1.00 13.05  ?  273 THR A O   1 
ATOM   1657 C CB  . THR A 1 216 ? 23.327 -7.608  -16.665 1.00 11.28  ?  273 THR A CB  1 
ATOM   1658 O OG1 . THR A 1 216 ? 22.295 -7.587  -15.683 1.00 12.86  ?  273 THR A OG1 1 
ATOM   1659 C CG2 . THR A 1 216 ? 22.765 -8.351  -17.936 1.00 11.67  ?  273 THR A CG2 1 
ATOM   1660 N N   . GLU A 1 217 ? 26.239 -6.535  -16.139 1.00 10.21  ?  274 GLU A N   1 
ATOM   1661 C CA  . GLU A 1 217 ? 27.476 -5.908  -15.657 1.00 12.82  ?  274 GLU A CA  1 
ATOM   1662 C C   . GLU A 1 217 ? 27.288 -5.114  -14.363 1.00 13.16  ?  274 GLU A C   1 
ATOM   1663 O O   . GLU A 1 217 ? 28.166 -5.145  -13.487 1.00 13.11  ?  274 GLU A O   1 
ATOM   1664 C CB  . GLU A 1 217 ? 28.054 -5.002  -16.750 1.00 14.53  ?  274 GLU A CB  1 
ATOM   1665 C CG  . GLU A 1 217 ? 29.522 -4.711  -16.599 1.00 14.52  ?  274 GLU A CG  1 
ATOM   1666 C CD  . GLU A 1 217 ? 30.419 -5.822  -17.144 1.00 19.22  ?  274 GLU A CD  1 
ATOM   1667 O OE1 . GLU A 1 217 ? 30.207 -6.277  -18.290 1.00 25.61  ?  274 GLU A OE1 1 
ATOM   1668 O OE2 . GLU A 1 217 ? 31.376 -6.199  -16.442 1.00 27.15  -1 274 GLU A OE2 1 
ATOM   1669 N N   . ASP A 1 218 ? 26.181 -4.372  -14.233 1.00 11.27  ?  275 ASP A N   1 
ATOM   1670 C CA  . ASP A 1 218 ? 25.992 -3.540  -13.037 1.00 11.42  ?  275 ASP A CA  1 
ATOM   1671 C C   . ASP A 1 218 ? 25.813 -4.332  -11.738 1.00 12.82  ?  275 ASP A C   1 
ATOM   1672 O O   . ASP A 1 218 ? 25.988 -3.737  -10.668 1.00 11.85  ?  275 ASP A O   1 
ATOM   1673 C CB  . ASP A 1 218 ? 24.739 -2.646  -13.130 1.00 13.89  ?  275 ASP A CB  1 
ATOM   1674 C CG  . ASP A 1 218 ? 24.778 -1.599  -14.256 1.00 15.52  ?  275 ASP A CG  1 
ATOM   1675 O OD1 . ASP A 1 218 ? 25.853 -1.132  -14.713 1.00 15.90  ?  275 ASP A OD1 1 
ATOM   1676 O OD2 . ASP A 1 218 ? 23.662 -1.196  -14.650 1.00 17.01  -1 275 ASP A OD2 1 
ATOM   1677 N N   . SER A 1 219 ? 25.439 -5.627  -11.798 1.00 11.31  ?  276 SER A N   1 
ATOM   1678 C CA  . SER A 1 219 ? 24.879 -6.325  -10.633 1.00 13.38  ?  276 SER A CA  1 
ATOM   1679 C C   . SER A 1 219 ? 25.870 -6.471  -9.485  1.00 12.59  ?  276 SER A C   1 
ATOM   1680 O O   . SER A 1 219 ? 25.460 -6.484  -8.308  1.00 10.98  ?  276 SER A O   1 
ATOM   1681 C CB  . SER A 1 219 ? 24.340 -7.683  -11.083 1.00 11.62  ?  276 SER A CB  1 
ATOM   1682 O OG  . SER A 1 219 ? 23.315 -7.444  -12.054 1.00 14.74  ?  276 SER A OG  1 
ATOM   1683 N N   . ALA A 1 220 ? 27.163 -6.557  -9.787  1.00 11.57  ?  277 ALA A N   1 
ATOM   1684 C CA  . ALA A 1 220 ? 28.169 -6.591  -8.733  1.00 9.96   ?  277 ALA A CA  1 
ATOM   1685 C C   . ALA A 1 220 ? 28.233 -5.295  -7.944  1.00 11.94  ?  277 ALA A C   1 
ATOM   1686 O O   . ALA A 1 220 ? 28.885 -5.254  -6.893  1.00 13.15  ?  277 ALA A O   1 
ATOM   1687 C CB  . ALA A 1 220 ? 29.543 -6.900  -9.333  1.00 12.68  ?  277 ALA A CB  1 
ATOM   1688 N N   . CYS A 1 221 ? 27.588 -4.230  -8.412  1.00 11.08  ?  278 CYS A N   1 
ATOM   1689 C CA  . CYS A 1 221 ? 27.587 -2.960  -7.700  1.00 10.17  ?  278 CYS A CA  1 
ATOM   1690 C C   . CYS A 1 221 ? 26.207 -2.572  -7.170  1.00 10.10  ?  278 CYS A C   1 
ATOM   1691 O O   . CYS A 1 221 ? 26.018 -1.421  -6.759  1.00 12.56  ?  278 CYS A O   1 
ATOM   1692 C CB  . CYS A 1 221 ? 28.143 -1.853  -8.600  1.00 14.10  ?  278 CYS A CB  1 
ATOM   1693 S SG  . CYS A 1 221 ? 29.922 -1.973  -8.878  1.00 15.91  ?  278 CYS A SG  1 
ATOM   1694 N N   . PHE A 1 222 ? 25.238 -3.492  -7.163  1.00 11.09  ?  279 PHE A N   1 
ATOM   1695 C CA  . PHE A 1 222 ? 24.027 -3.237  -6.404  1.00 9.58   ?  279 PHE A CA  1 
ATOM   1696 C C   . PHE A 1 222 ? 24.352 -3.184  -4.905  1.00 11.07  ?  279 PHE A C   1 
ATOM   1697 O O   . PHE A 1 222 ? 25.433 -3.579  -4.460  1.00 13.83  ?  279 PHE A O   1 
ATOM   1698 C CB  . PHE A 1 222 ? 22.996 -4.336  -6.658  1.00 11.56  ?  279 PHE A CB  1 
ATOM   1699 C CG  . PHE A 1 222 ? 22.445 -4.400  -8.082  1.00 9.70   ?  279 PHE A CG  1 
ATOM   1700 C CD1 . PHE A 1 222 ? 22.816 -3.502  -9.112  1.00 10.64  ?  279 PHE A CD1 1 
ATOM   1701 C CD2 . PHE A 1 222 ? 21.519 -5.398  -8.381  1.00 10.61  ?  279 PHE A CD2 1 
ATOM   1702 C CE1 . PHE A 1 222 ? 22.249 -3.623  -10.400 1.00 12.65  ?  279 PHE A CE1 1 
ATOM   1703 C CE2 . PHE A 1 222 ? 20.961 -5.512  -9.658  1.00 11.29  ?  279 PHE A CE2 1 
ATOM   1704 C CZ  . PHE A 1 222 ? 21.334 -4.630  -10.667 1.00 12.26  ?  279 PHE A CZ  1 
ATOM   1705 N N   . ILE A 1 223 ? 23.390 -2.683  -4.128  1.00 13.21  ?  280 ILE A N   1 
ATOM   1706 C CA  . ILE A 1 223 ? 23.463 -2.693  -2.668  1.00 12.33  ?  280 ILE A CA  1 
ATOM   1707 C C   . ILE A 1 223 ? 22.404 -3.655  -2.136  1.00 15.98  ?  280 ILE A C   1 
ATOM   1708 O O   . ILE A 1 223 ? 21.199 -3.364  -2.240  1.00 14.30  ?  280 ILE A O   1 
ATOM   1709 C CB  . ILE A 1 223 ? 23.253 -1.297  -2.069  1.00 12.23  ?  280 ILE A CB  1 
ATOM   1710 C CG1 . ILE A 1 223 ? 24.389 -0.371  -2.506  1.00 15.32  ?  280 ILE A CG1 1 
ATOM   1711 C CG2 . ILE A 1 223 ? 23.195 -1.405  -0.523  1.00 16.10  ?  280 ILE A CG2 1 
ATOM   1712 C CD1 . ILE A 1 223 ? 24.136 1.105   -2.162  1.00 14.27  ?  280 ILE A CD1 1 
ATOM   1713 N N   . PRO A 1 224 ? 22.784 -4.815  -1.586  1.00 13.27  ?  281 PRO A N   1 
ATOM   1714 C CA  . PRO A 1 224 ? 24.127 -5.410  -1.604  1.00 13.30  ?  281 PRO A CA  1 
ATOM   1715 C C   . PRO A 1 224 ? 24.448 -6.003  -2.976  1.00 12.11  ?  281 PRO A C   1 
ATOM   1716 O O   . PRO A 1 224 ? 23.554 -6.240  -3.794  1.00 12.45  ?  281 PRO A O   1 
ATOM   1717 C CB  . PRO A 1 224 ? 24.033 -6.514  -0.528  1.00 13.87  ?  281 PRO A CB  1 
ATOM   1718 C CG  . PRO A 1 224 ? 22.637 -6.442  0.070   1.00 16.06  ?  281 PRO A CG  1 
ATOM   1719 C CD  . PRO A 1 224 ? 21.812 -5.735  -0.969  1.00 13.84  ?  281 PRO A CD  1 
ATOM   1720 N N   . PRO A 1 225 ? 25.727 -6.270  -3.239  1.00 11.67  ?  282 PRO A N   1 
ATOM   1721 C CA  . PRO A 1 225 ? 26.089 -6.947  -4.497  1.00 11.42  ?  282 PRO A CA  1 
ATOM   1722 C C   . PRO A 1 225 ? 25.287 -8.235  -4.666  1.00 10.67  ?  282 PRO A C   1 
ATOM   1723 O O   . PRO A 1 225 ? 25.133 -9.019  -3.725  1.00 10.71  ?  282 PRO A O   1 
ATOM   1724 C CB  . PRO A 1 225 ? 27.586 -7.207  -4.324  1.00 12.65  ?  282 PRO A CB  1 
ATOM   1725 C CG  . PRO A 1 225 ? 28.069 -5.980  -3.496  1.00 12.58  ?  282 PRO A CG  1 
ATOM   1726 C CD  . PRO A 1 225 ? 26.911 -5.747  -2.519  1.00 13.39  ?  282 PRO A CD  1 
ATOM   1727 N N   . LEU A 1 226 ? 24.800 -8.463  -5.886  1.00 9.56   ?  283 LEU A N   1 
ATOM   1728 C CA  . LEU A 1 226 ? 23.688 -9.396  -6.095  1.00 9.68   ?  283 LEU A CA  1 
ATOM   1729 C C   . LEU A 1 226 ? 24.189 -10.814 -6.360  1.00 10.15  ?  283 LEU A C   1 
ATOM   1730 O O   . LEU A 1 226 ? 24.983 -11.034 -7.283  1.00 12.17  ?  283 LEU A O   1 
ATOM   1731 C CB  . LEU A 1 226 ? 22.854 -8.909  -7.273  1.00 11.46  ?  283 LEU A CB  1 
ATOM   1732 C CG  . LEU A 1 226 ? 21.669 -9.775  -7.636  1.00 10.36  ?  283 LEU A CG  1 
ATOM   1733 C CD1 . LEU A 1 226 ? 20.573 -9.763  -6.576  1.00 12.94  ?  283 LEU A CD1 1 
ATOM   1734 C CD2 . LEU A 1 226 ? 21.120 -9.267  -8.991  1.00 13.86  ?  283 LEU A CD2 1 
ATOM   1735 N N   . THR A 1 227 ? 23.730 -11.770 -5.553  1.00 10.89  ?  284 THR A N   1 
ATOM   1736 C CA  . THR A 1 227 ? 23.871 -13.189 -5.874  1.00 11.19  ?  284 THR A CA  1 
ATOM   1737 C C   . THR A 1 227 ? 22.926 -13.513 -7.026  1.00 12.64  ?  284 THR A C   1 
ATOM   1738 O O   . THR A 1 227 ? 21.764 -13.099 -7.005  1.00 10.87  ?  284 THR A O   1 
ATOM   1739 C CB  . THR A 1 227 ? 23.523 -14.007 -4.631  1.00 12.43  ?  284 THR A CB  1 
ATOM   1740 O OG1 . THR A 1 227 ? 24.426 -13.647 -3.577  1.00 14.94  ?  284 THR A OG1 1 
ATOM   1741 C CG2 . THR A 1 227 ? 23.569 -15.513 -4.866  1.00 12.83  ?  284 THR A CG2 1 
ATOM   1742 N N   . THR A 1 228 ? 23.427 -14.233 -8.028  1.00 11.30  ?  285 THR A N   1 
ATOM   1743 C CA  . THR A 1 228 ? 22.696 -14.322 -9.287  1.00 10.73  ?  285 THR A CA  1 
ATOM   1744 C C   . THR A 1 228 ? 23.190 -15.520 -10.080 1.00 14.49  ?  285 THR A C   1 
ATOM   1745 O O   . THR A 1 228 ? 24.256 -16.087 -9.804  1.00 14.35  ?  285 THR A O   1 
ATOM   1746 C CB  . THR A 1 228 ? 22.838 -13.015 -10.077 1.00 11.84  ?  285 THR A CB  1 
ATOM   1747 O OG1 . THR A 1 228 ? 22.087 -13.094 -11.279 1.00 13.62  ?  285 THR A OG1 1 
ATOM   1748 C CG2 . THR A 1 228 ? 24.280 -12.728 -10.437 1.00 12.88  ?  285 THR A CG2 1 
ATOM   1749 N N   . ILE A 1 229 ? 22.381 -15.924 -11.054 1.00 12.06  ?  286 ILE A N   1 
ATOM   1750 C CA  . ILE A 1 229 ? 22.788 -16.927 -12.040 1.00 10.67  ?  286 ILE A CA  1 
ATOM   1751 C C   . ILE A 1 229 ? 23.530 -16.236 -13.173 1.00 12.79  ?  286 ILE A C   1 
ATOM   1752 O O   . ILE A 1 229 ? 22.947 -15.415 -13.893 1.00 14.28  ?  286 ILE A O   1 
ATOM   1753 C CB  . ILE A 1 229 ? 21.574 -17.684 -12.597 1.00 11.13  ?  286 ILE A CB  1 
ATOM   1754 C CG1 . ILE A 1 229 ? 20.730 -18.304 -11.480 1.00 14.00  ?  286 ILE A CG1 1 
ATOM   1755 C CG2 . ILE A 1 229 ? 22.017 -18.691 -13.666 1.00 12.54  ?  286 ILE A CG2 1 
ATOM   1756 C CD1 . ILE A 1 229 ? 21.490 -19.308 -10.557 1.00 15.32  ?  286 ILE A CD1 1 
ATOM   1757 N N   . LYS A 1 230 ? 24.786 -16.612 -13.386 1.00 13.40  ?  287 LYS A N   1 
ATOM   1758 C CA  . LYS A 1 230 ? 25.572 -15.995 -14.445 1.00 11.98  ?  287 LYS A CA  1 
ATOM   1759 C C   . LYS A 1 230 ? 25.320 -16.705 -15.764 1.00 15.58  ?  287 LYS A C   1 
ATOM   1760 O O   . LYS A 1 230 ? 25.493 -17.926 -15.869 1.00 15.16  ?  287 LYS A O   1 
ATOM   1761 C CB  . LYS A 1 230 ? 27.062 -16.019 -14.128 1.00 13.65  ?  287 LYS A CB  1 
ATOM   1762 C CG  . LYS A 1 230 ? 27.931 -15.592 -15.334 1.00 14.02  ?  287 LYS A CG  1 
ATOM   1763 C CD  . LYS A 1 230 ? 29.376 -15.306 -14.906 1.00 18.22  ?  287 LYS A CD  1 
ATOM   1764 C CE  . LYS A 1 230 ? 30.013 -14.257 -15.857 1.00 32.75  ?  287 LYS A CE  1 
ATOM   1765 N NZ  . LYS A 1 230 ? 29.482 -12.821 -15.666 1.00 21.36  ?  287 LYS A NZ  1 
ATOM   1766 N N   . GLN A 1 231 ? 24.894 -15.939 -16.749 1.00 13.11  ?  288 GLN A N   1 
ATOM   1767 C CA  . GLN A 1 231 ? 24.896 -16.356 -18.155 1.00 13.00  ?  288 GLN A CA  1 
ATOM   1768 C C   . GLN A 1 231 ? 26.092 -15.670 -18.805 1.00 15.40  ?  288 GLN A C   1 
ATOM   1769 O O   . GLN A 1 231 ? 26.145 -14.437 -18.873 1.00 15.00  ?  288 GLN A O   1 
ATOM   1770 C CB  . GLN A 1 231 ? 23.592 -15.958 -18.836 1.00 13.41  ?  288 GLN A CB  1 
ATOM   1771 C CG  . GLN A 1 231 ? 22.385 -16.601 -18.155 1.00 17.95  ?  288 GLN A CG  1 
ATOM   1772 C CD  . GLN A 1 231 ? 21.160 -16.584 -19.034 1.00 17.39  ?  288 GLN A CD  1 
ATOM   1773 O OE1 . GLN A 1 231 ? 20.685 -17.628 -19.466 1.00 22.46  ?  288 GLN A OE1 1 
ATOM   1774 N NE2 . GLN A 1 231 ? 20.648 -15.392 -19.325 1.00 18.17  ?  288 GLN A NE2 1 
ATOM   1775 N N   . ASP A 1 232 ? 27.084 -16.451 -19.240 1.00 13.37  ?  289 ASP A N   1 
ATOM   1776 C CA  . ASP A 1 232 ? 28.300 -15.864 -19.813 1.00 12.30  ?  289 ASP A CA  1 
ATOM   1777 C C   . ASP A 1 232 ? 28.004 -15.375 -21.234 1.00 13.04  ?  289 ASP A C   1 
ATOM   1778 O O   . ASP A 1 232 ? 28.083 -16.125 -22.213 1.00 15.47  ?  289 ASP A O   1 
ATOM   1779 C CB  . ASP A 1 232 ? 29.438 -16.883 -19.786 1.00 15.14  ?  289 ASP A CB  1 
ATOM   1780 C CG  . ASP A 1 232 ? 30.765 -16.296 -20.227 1.00 20.61  ?  289 ASP A CG  1 
ATOM   1781 O OD1 . ASP A 1 232 ? 30.786 -15.174 -20.763 1.00 18.57  ?  289 ASP A OD1 1 
ATOM   1782 O OD2 . ASP A 1 232 ? 31.802 -16.961 -20.026 1.00 25.12  -1 289 ASP A OD2 1 
ATOM   1783 N N   . PHE A 1 233 ? 27.665 -14.090 -21.346 1.00 12.74  ?  290 PHE A N   1 
ATOM   1784 C CA  . PHE A 1 233 ? 27.303 -13.553 -22.657 1.00 12.17  ?  290 PHE A CA  1 
ATOM   1785 C C   . PHE A 1 233 ? 28.511 -13.470 -23.587 1.00 12.90  ?  290 PHE A C   1 
ATOM   1786 O O   . PHE A 1 233 ? 28.352 -13.571 -24.813 1.00 14.27  ?  290 PHE A O   1 
ATOM   1787 C CB  . PHE A 1 233 ? 26.636 -12.182 -22.510 1.00 14.67  ?  290 PHE A CB  1 
ATOM   1788 C CG  . PHE A 1 233 ? 25.421 -12.199 -21.626 1.00 13.58  ?  290 PHE A CG  1 
ATOM   1789 C CD1 . PHE A 1 233 ? 24.337 -12.994 -21.944 1.00 15.03  ?  290 PHE A CD1 1 
ATOM   1790 C CD2 . PHE A 1 233 ? 25.390 -11.437 -20.451 1.00 13.72  ?  290 PHE A CD2 1 
ATOM   1791 C CE1 . PHE A 1 233 ? 23.213 -13.017 -21.125 1.00 15.88  ?  290 PHE A CE1 1 
ATOM   1792 C CE2 . PHE A 1 233 ? 24.284 -11.451 -19.627 1.00 14.56  ?  290 PHE A CE2 1 
ATOM   1793 C CZ  . PHE A 1 233 ? 23.178 -12.224 -19.961 1.00 15.34  ?  290 PHE A CZ  1 
ATOM   1794 N N   A ARG A 1 234 ? 29.718 -13.274 -23.046 0.54 13.58  ?  291 ARG A N   1 
ATOM   1795 N N   B ARG A 1 234 ? 29.718 -13.281 -23.046 0.46 13.54  ?  291 ARG A N   1 
ATOM   1796 C CA  A ARG A 1 234 ? 30.920 -13.331 -23.874 0.54 15.29  ?  291 ARG A CA  1 
ATOM   1797 C CA  B ARG A 1 234 ? 30.919 -13.321 -23.880 0.46 15.34  ?  291 ARG A CA  1 
ATOM   1798 C C   A ARG A 1 234 ? 31.029 -14.677 -24.568 0.54 13.38  ?  291 ARG A C   1 
ATOM   1799 C C   B ARG A 1 234 ? 31.070 -14.675 -24.557 0.46 13.40  ?  291 ARG A C   1 
ATOM   1800 O O   A ARG A 1 234 ? 31.294 -14.751 -25.777 0.54 15.34  ?  291 ARG A O   1 
ATOM   1801 O O   B ARG A 1 234 ? 31.391 -14.751 -25.752 0.46 15.32  ?  291 ARG A O   1 
ATOM   1802 C CB  A ARG A 1 234 ? 32.170 -13.080 -23.031 0.54 17.67  ?  291 ARG A CB  1 
ATOM   1803 C CB  B ARG A 1 234 ? 32.155 -12.998 -23.037 0.46 17.79  ?  291 ARG A CB  1 
ATOM   1804 C CG  A ARG A 1 234 ? 32.066 -11.868 -22.127 0.54 21.45  ?  291 ARG A CG  1 
ATOM   1805 C CG  B ARG A 1 234 ? 32.064 -11.629 -22.370 0.46 20.13  ?  291 ARG A CG  1 
ATOM   1806 C CD  A ARG A 1 234 ? 33.019 -10.781 -22.555 0.54 36.04  ?  291 ARG A CD  1 
ATOM   1807 C CD  B ARG A 1 234 ? 33.375 -11.193 -21.736 0.46 24.43  ?  291 ARG A CD  1 
ATOM   1808 N NE  A ARG A 1 234 ? 32.345 -9.701  -23.262 0.54 40.56  ?  291 ARG A NE  1 
ATOM   1809 N NE  B ARG A 1 234 ? 33.855 -12.166 -20.763 0.46 32.66  ?  291 ARG A NE  1 
ATOM   1810 C CZ  A ARG A 1 234 ? 32.481 -9.433  -24.554 0.54 28.15  ?  291 ARG A CZ  1 
ATOM   1811 C CZ  B ARG A 1 234 ? 34.896 -11.976 -19.965 0.46 36.61  ?  291 ARG A CZ  1 
ATOM   1812 N NH1 A ARG A 1 234 ? 33.221 -10.194 -25.351 0.54 24.62  ?  291 ARG A NH1 1 
ATOM   1813 N NH1 B ARG A 1 234 ? 35.584 -10.846 -19.983 0.46 38.47  ?  291 ARG A NH1 1 
ATOM   1814 N NH2 A ARG A 1 234 ? 31.857 -8.379  -25.058 0.54 14.83  ?  291 ARG A NH2 1 
ATOM   1815 N NH2 B ARG A 1 234 ? 35.258 -12.945 -19.130 0.46 33.70  ?  291 ARG A NH2 1 
ATOM   1816 N N   . LEU A 1 235 ? 30.847 -15.755 -23.809 1.00 15.38  ?  292 LEU A N   1 
ATOM   1817 C CA  . LEU A 1 235 ? 30.896 -17.091 -24.393 1.00 13.74  ?  292 LEU A CA  1 
ATOM   1818 C C   . LEU A 1 235 ? 29.753 -17.307 -25.387 1.00 15.56  ?  292 LEU A C   1 
ATOM   1819 O O   . LEU A 1 235 ? 29.947 -17.961 -26.418 1.00 15.28  ?  292 LEU A O   1 
ATOM   1820 C CB  . LEU A 1 235 ? 30.833 -18.133 -23.277 1.00 16.04  ?  292 LEU A CB  1 
ATOM   1821 C CG  . LEU A 1 235 ? 30.936 -19.593 -23.719 1.00 18.18  ?  292 LEU A CG  1 
ATOM   1822 C CD1 . LEU A 1 235 ? 32.268 -19.857 -24.350 1.00 21.57  ?  292 LEU A CD1 1 
ATOM   1823 C CD2 . LEU A 1 235 ? 30.718 -20.465 -22.498 1.00 23.43  ?  292 LEU A CD2 1 
ATOM   1824 N N   . LEU A 1 236 ? 28.552 -16.796 -25.095 1.00 13.99  ?  293 LEU A N   1 
ATOM   1825 C CA  . LEU A 1 236 ? 27.473 -16.940 -26.069 1.00 12.98  ?  293 LEU A CA  1 
ATOM   1826 C C   . LEU A 1 236 ? 27.836 -16.264 -27.387 1.00 14.36  ?  293 LEU A C   1 
ATOM   1827 O O   . LEU A 1 236 ? 27.603 -16.821 -28.466 1.00 16.66  ?  293 LEU A O   1 
ATOM   1828 C CB  . LEU A 1 236 ? 26.157 -16.359 -25.521 1.00 11.89  ?  293 LEU A CB  1 
ATOM   1829 C CG  . LEU A 1 236 ? 24.929 -16.537 -26.435 1.00 14.87  ?  293 LEU A CG  1 
ATOM   1830 C CD1 . LEU A 1 236 ? 24.553 -18.008 -26.527 1.00 20.26  ?  293 LEU A CD1 1 
ATOM   1831 C CD2 . LEU A 1 236 ? 23.735 -15.724 -25.953 1.00 18.28  ?  293 LEU A CD2 1 
ATOM   1832 N N   . GLY A 1 237 ? 28.407 -15.059 -27.323 1.00 14.98  ?  294 GLY A N   1 
ATOM   1833 C CA  . GLY A 1 237 ? 28.762 -14.362 -28.554 1.00 13.92  ?  294 GLY A CA  1 
ATOM   1834 C C   . GLY A 1 237 ? 29.843 -15.094 -29.319 1.00 18.37  ?  294 GLY A C   1 
ATOM   1835 O O   . GLY A 1 237 ? 29.765 -15.223 -30.542 1.00 18.59  ?  294 GLY A O   1 
ATOM   1836 N N   A GLN A 1 238 ? 30.844 -15.607 -28.605 0.60 15.27  ?  295 GLN A N   1 
ATOM   1837 N N   B GLN A 1 238 ? 30.865 -15.578 -28.610 0.40 15.28  ?  295 GLN A N   1 
ATOM   1838 C CA  A GLN A 1 238 ? 31.944 -16.326 -29.236 0.60 15.21  ?  295 GLN A CA  1 
ATOM   1839 C CA  B GLN A 1 238 ? 31.943 -16.330 -29.244 0.40 15.20  ?  295 GLN A CA  1 
ATOM   1840 C C   A GLN A 1 238 ? 31.450 -17.612 -29.891 0.60 17.19  ?  295 GLN A C   1 
ATOM   1841 C C   B GLN A 1 238 ? 31.413 -17.593 -29.910 0.40 17.21  ?  295 GLN A C   1 
ATOM   1842 O O   A GLN A 1 238 ? 31.748 -17.881 -31.060 0.60 18.62  ?  295 GLN A O   1 
ATOM   1843 O O   B GLN A 1 238 ? 31.665 -17.840 -31.095 0.40 18.46  ?  295 GLN A O   1 
ATOM   1844 C CB  A GLN A 1 238 ? 33.017 -16.610 -28.180 0.60 19.70  ?  295 GLN A CB  1 
ATOM   1845 C CB  B GLN A 1 238 ? 33.005 -16.680 -28.199 0.40 19.76  ?  295 GLN A CB  1 
ATOM   1846 C CG  A GLN A 1 238 ? 34.052 -17.647 -28.539 0.60 22.12  ?  295 GLN A CG  1 
ATOM   1847 C CG  B GLN A 1 238 ? 33.977 -15.552 -27.891 0.40 24.12  ?  295 GLN A CG  1 
ATOM   1848 C CD  A GLN A 1 238 ? 34.877 -18.050 -27.322 0.60 27.44  ?  295 GLN A CD  1 
ATOM   1849 C CD  B GLN A 1 238 ? 34.279 -15.436 -26.411 0.40 23.67  ?  295 GLN A CD  1 
ATOM   1850 O OE1 A GLN A 1 238 ? 34.885 -17.346 -26.313 0.60 41.02  ?  295 GLN A OE1 1 
ATOM   1851 O OE1 B GLN A 1 238 ? 34.425 -16.441 -25.715 0.40 31.96  ?  295 GLN A OE1 1 
ATOM   1852 N NE2 A GLN A 1 238 ? 35.571 -19.179 -27.414 0.60 36.22  ?  295 GLN A NE2 1 
ATOM   1853 N NE2 B GLN A 1 238 ? 34.402 -14.202 -25.925 0.40 24.86  ?  295 GLN A NE2 1 
ATOM   1854 N N   . THR A 1 239 ? 30.658 -18.394 -29.157 1.00 15.49  ?  296 THR A N   1 
ATOM   1855 C CA  . THR A 1 239 ? 30.161 -19.673 -29.663 1.00 15.06  ?  296 THR A CA  1 
ATOM   1856 C C   . THR A 1 239 ? 29.177 -19.495 -30.810 1.00 20.65  ?  296 THR A C   1 
ATOM   1857 O O   . THR A 1 239 ? 29.199 -20.270 -31.775 1.00 17.92  ?  296 THR A O   1 
ATOM   1858 C CB  . THR A 1 239 ? 29.498 -20.442 -28.517 1.00 17.44  ?  296 THR A CB  1 
ATOM   1859 O OG1 . THR A 1 239 ? 30.418 -20.554 -27.418 1.00 19.29  ?  296 THR A OG1 1 
ATOM   1860 C CG2 . THR A 1 239 ? 29.086 -21.839 -28.984 1.00 22.49  ?  296 THR A CG2 1 
ATOM   1861 N N   . SER A 1 240 ? 28.258 -18.529 -30.704 1.00 16.54  ?  297 SER A N   1 
ATOM   1862 C CA  . SER A 1 240 ? 27.311 -18.334 -31.796 1.00 15.49  ?  297 SER A CA  1 
ATOM   1863 C C   . SER A 1 240 ? 28.015 -17.908 -33.085 1.00 16.27  ?  297 SER A C   1 
ATOM   1864 O O   . SER A 1 240 ? 27.674 -18.392 -34.170 1.00 16.05  ?  297 SER A O   1 
ATOM   1865 C CB  . SER A 1 240 ? 26.219 -17.337 -31.391 1.00 19.33  ?  297 SER A CB  1 
ATOM   1866 O OG  . SER A 1 240 ? 26.743 -16.049 -31.156 1.00 23.37  ?  297 SER A OG  1 
ATOM   1867 N N   . VAL A 1 241 ? 28.959 -16.970 -33.012 1.00 13.56  ?  298 VAL A N   1 
ATOM   1868 C CA  . VAL A 1 241 ? 29.682 -16.587 -34.221 1.00 13.43  ?  298 VAL A CA  1 
ATOM   1869 C C   . VAL A 1 241 ? 30.470 -17.776 -34.762 1.00 18.12  ?  298 VAL A C   1 
ATOM   1870 O O   . VAL A 1 241 ? 30.508 -18.017 -35.974 1.00 18.64  ?  298 VAL A O   1 
ATOM   1871 C CB  . VAL A 1 241 ? 30.591 -15.366 -33.951 1.00 16.45  ?  298 VAL A CB  1 
ATOM   1872 C CG1 . VAL A 1 241 ? 31.521 -15.114 -35.125 1.00 18.12  ?  298 VAL A CG1 1 
ATOM   1873 C CG2 . VAL A 1 241 ? 29.741 -14.128 -33.717 1.00 17.50  ?  298 VAL A CG2 1 
ATOM   1874 N N   . ASN A 1 242 ? 31.090 -18.555 -33.873 1.00 16.40  ?  299 ASN A N   1 
ATOM   1875 C CA  . ASN A 1 242 ? 31.866 -19.696 -34.338 1.00 15.74  ?  299 ASN A CA  1 
ATOM   1876 C C   . ASN A 1 242 ? 30.977 -20.728 -35.009 1.00 17.10  ?  299 ASN A C   1 
ATOM   1877 O O   . ASN A 1 242 ? 31.356 -21.302 -36.045 1.00 16.67  ?  299 ASN A O   1 
ATOM   1878 C CB  . ASN A 1 242 ? 32.620 -20.329 -33.168 1.00 17.36  ?  299 ASN A CB  1 
ATOM   1879 C CG  . ASN A 1 242 ? 33.811 -19.494 -32.718 1.00 23.01  ?  299 ASN A CG  1 
ATOM   1880 O OD1 . ASN A 1 242 ? 34.231 -18.566 -33.408 1.00 22.80  ?  299 ASN A OD1 1 
ATOM   1881 N ND2 . ASN A 1 242 ? 34.367 -19.840 -31.560 1.00 21.16  ?  299 ASN A ND2 1 
ATOM   1882 N N   . ARG A 1 243 ? 29.796 -20.977 -34.443 1.00 16.45  ?  300 ARG A N   1 
ATOM   1883 C CA  . ARG A 1 243 ? 28.883 -21.945 -35.052 1.00 14.90  ?  300 ARG A CA  1 
ATOM   1884 C C   . ARG A 1 243 ? 28.360 -21.440 -36.393 1.00 19.10  ?  300 ARG A C   1 
ATOM   1885 O O   . ARG A 1 243 ? 28.252 -22.212 -37.355 1.00 19.37  ?  300 ARG A O   1 
ATOM   1886 C CB  . ARG A 1 243 ? 27.726 -22.254 -34.104 1.00 19.26  ?  300 ARG A CB  1 
ATOM   1887 C CG  . ARG A 1 243 ? 26.637 -23.100 -34.724 1.00 29.47  ?  300 ARG A CG  1 
ATOM   1888 C CD  . ARG A 1 243 ? 27.085 -24.551 -34.897 1.00 42.19  ?  300 ARG A CD  1 
ATOM   1889 N NE  . ARG A 1 243 ? 26.934 -25.333 -33.673 1.00 58.03  ?  300 ARG A NE  1 
ATOM   1890 C CZ  . ARG A 1 243 ? 27.855 -25.462 -32.726 1.00 65.42  ?  300 ARG A CZ  1 
ATOM   1891 N NH1 . ARG A 1 243 ? 29.056 -24.916 -32.845 1.00 50.39  ?  300 ARG A NH1 1 
ATOM   1892 N NH2 . ARG A 1 243 ? 27.567 -26.170 -31.636 1.00 56.48  ?  300 ARG A NH2 1 
ATOM   1893 N N   . LEU A 1 244 ? 28.039 -20.145 -36.493 1.00 18.67  ?  301 LEU A N   1 
ATOM   1894 C CA  . LEU A 1 244 ? 27.594 -19.618 -37.782 1.00 17.95  ?  301 LEU A CA  1 
ATOM   1895 C C   . LEU A 1 244 ? 28.681 -19.770 -38.845 1.00 17.11  ?  301 LEU A C   1 
ATOM   1896 O O   . LEU A 1 244 ? 28.391 -20.154 -39.982 1.00 18.89  ?  301 LEU A O   1 
ATOM   1897 C CB  . LEU A 1 244 ? 27.168 -18.155 -37.632 1.00 20.57  ?  301 LEU A CB  1 
ATOM   1898 C CG  . LEU A 1 244 ? 26.532 -17.520 -38.868 1.00 21.52  ?  301 LEU A CG  1 
ATOM   1899 C CD1 . LEU A 1 244 ? 25.269 -18.261 -39.312 1.00 24.27  ?  301 LEU A CD1 1 
ATOM   1900 C CD2 . LEU A 1 244 ? 26.237 -16.068 -38.578 1.00 23.52  ?  301 LEU A CD2 1 
ATOM   1901 N N   . VAL A 1 245 ? 29.943 -19.513 -38.482 1.00 18.38  ?  302 VAL A N   1 
ATOM   1902 C CA  . VAL A 1 245 ? 31.047 -19.707 -39.423 1.00 20.18  ?  302 VAL A CA  1 
ATOM   1903 C C   . VAL A 1 245 ? 31.157 -21.173 -39.832 1.00 21.54  ?  302 VAL A C   1 
ATOM   1904 O O   . VAL A 1 245 ? 31.332 -21.496 -41.017 1.00 22.18  ?  302 VAL A O   1 
ATOM   1905 C CB  . VAL A 1 245 ? 32.369 -19.194 -38.821 1.00 27.57  ?  302 VAL A CB  1 
ATOM   1906 C CG1 . VAL A 1 245 ? 33.548 -19.613 -39.705 1.00 27.54  ?  302 VAL A CG1 1 
ATOM   1907 C CG2 . VAL A 1 245 ? 32.326 -17.691 -38.700 1.00 25.11  ?  302 VAL A CG2 1 
ATOM   1908 N N   . GLN A 1 246 ? 31.031 -22.088 -38.871 1.00 20.80  ?  303 GLN A N   1 
ATOM   1909 C CA  . GLN A 1 246 ? 31.068 -23.505 -39.224 1.00 20.40  ?  303 GLN A CA  1 
ATOM   1910 C C   . GLN A 1 246 ? 29.943 -23.868 -40.193 1.00 20.22  ?  303 GLN A C   1 
ATOM   1911 O O   . GLN A 1 246 ? 30.153 -24.653 -41.135 1.00 21.16  ?  303 GLN A O   1 
ATOM   1912 C CB  . GLN A 1 246 ? 30.990 -24.366 -37.965 1.00 21.03  ?  303 GLN A CB  1 
ATOM   1913 C CG  . GLN A 1 246 ? 32.169 -24.216 -37.054 1.00 27.89  ?  303 GLN A CG  1 
ATOM   1914 C CD  . GLN A 1 246 ? 31.876 -24.742 -35.667 1.00 40.67  ?  303 GLN A CD  1 
ATOM   1915 O OE1 . GLN A 1 246 ? 30.931 -25.513 -35.471 1.00 36.02  ?  303 GLN A OE1 1 
ATOM   1916 N NE2 . GLN A 1 246 ? 32.675 -24.315 -34.689 1.00 42.28  ?  303 GLN A NE2 1 
ATOM   1917 N N   . LEU A 1 247 ? 28.750 -23.292 -40.006 1.00 20.22  ?  304 LEU A N   1 
ATOM   1918 C CA  . LEU A 1 247 ? 27.649 -23.557 -40.937 1.00 18.84  ?  304 LEU A CA  1 
ATOM   1919 C C   . LEU A 1 247 ? 27.916 -22.985 -42.324 1.00 24.47  ?  304 LEU A C   1 
ATOM   1920 O O   . LEU A 1 247 ? 27.522 -23.581 -43.326 1.00 25.08  ?  304 LEU A O   1 
ATOM   1921 C CB  . LEU A 1 247 ? 26.340 -22.991 -40.392 1.00 20.85  ?  304 LEU A CB  1 
ATOM   1922 C CG  . LEU A 1 247 ? 25.828 -23.726 -39.168 1.00 25.51  ?  304 LEU A CG  1 
ATOM   1923 C CD1 . LEU A 1 247 ? 24.598 -23.007 -38.685 1.00 27.10  ?  304 LEU A CD1 1 
ATOM   1924 C CD2 . LEU A 1 247 ? 25.531 -25.181 -39.525 1.00 29.25  ?  304 LEU A CD2 1 
ATOM   1925 N N   . LEU A 1 248 ? 28.533 -21.810 -42.403 1.00 23.73  ?  305 LEU A N   1 
ATOM   1926 C CA  . LEU A 1 248 ? 28.844 -21.241 -43.705 1.00 22.57  ?  305 LEU A CA  1 
ATOM   1927 C C   . LEU A 1 248 ? 29.888 -22.076 -44.436 1.00 22.70  ?  305 LEU A C   1 
ATOM   1928 O O   . LEU A 1 248 ? 29.834 -22.203 -45.667 1.00 23.03  ?  305 LEU A O   1 
ATOM   1929 C CB  . LEU A 1 248 ? 29.317 -19.796 -43.529 1.00 22.24  ?  305 LEU A CB  1 
ATOM   1930 C CG  . LEU A 1 248 ? 28.191 -18.796 -43.259 1.00 24.81  ?  305 LEU A CG  1 
ATOM   1931 C CD1 . LEU A 1 248 ? 28.688 -17.590 -42.478 1.00 26.42  ?  305 LEU A CD1 1 
ATOM   1932 C CD2 . LEU A 1 248 ? 27.572 -18.374 -44.583 1.00 25.51  ?  305 LEU A CD2 1 
ATOM   1933 N N   . GLN A 1 249 ? 30.826 -22.669 -43.691 1.00 25.29  ?  306 GLN A N   1 
ATOM   1934 C CA  . GLN A 1 249 ? 31.902 -23.452 -44.294 1.00 26.08  ?  306 GLN A CA  1 
ATOM   1935 C C   . GLN A 1 249 ? 31.439 -24.851 -44.679 1.00 27.20  ?  306 GLN A C   1 
ATOM   1936 O O   . GLN A 1 249 ? 31.852 -25.376 -45.726 1.00 26.51  ?  306 GLN A O   1 
ATOM   1937 C CB  . GLN A 1 249 ? 33.094 -23.527 -43.341 1.00 23.45  ?  306 GLN A CB  1 
ATOM   1938 C CG  . GLN A 1 249 ? 33.767 -22.189 -43.107 1.00 28.67  ?  306 GLN A CG  1 
ATOM   1939 C CD  . GLN A 1 249 ? 34.881 -22.253 -42.086 1.00 32.24  ?  306 GLN A CD  1 
ATOM   1940 O OE1 . GLN A 1 249 ? 34.793 -22.978 -41.097 1.00 35.90  ?  306 GLN A OE1 1 
ATOM   1941 N NE2 . GLN A 1 249 ? 35.937 -21.484 -42.321 1.00 47.47  ?  306 GLN A NE2 1 
ATOM   1942 N N   . ASN A 1 250 ? 30.584 -25.457 -43.863 1.00 34.40  ?  307 ASN A N   1 
ATOM   1943 C CA  . ASN A 1 250 ? 30.078 -26.808 -44.108 1.00 38.49  ?  307 ASN A CA  1 
ATOM   1944 C C   . ASN A 1 250 ? 28.651 -26.872 -43.600 1.00 34.30  ?  307 ASN A C   1 
ATOM   1945 O O   . ASN A 1 250 ? 28.417 -26.939 -42.388 1.00 33.58  ?  307 ASN A O   1 
ATOM   1946 C CB  . ASN A 1 250 ? 30.954 -27.862 -43.436 1.00 38.33  ?  307 ASN A CB  1 
ATOM   1947 C CG  . ASN A 1 250 ? 32.357 -27.909 -44.029 1.00 44.32  ?  307 ASN A CG  1 
ATOM   1948 O OD1 . ASN A 1 250 ? 33.330 -27.524 -43.376 1.00 49.22  ?  307 ASN A OD1 1 
ATOM   1949 N ND2 . ASN A 1 250 ? 32.460 -28.363 -45.277 1.00 45.71  ?  307 ASN A ND2 1 
ATOM   1950 N N   . PRO A 1 251 ? 27.673 -26.838 -44.488 1.00 39.00  ?  308 PRO A N   1 
ATOM   1951 C CA  . PRO A 1 251 ? 26.276 -26.695 -44.047 1.00 44.36  ?  308 PRO A CA  1 
ATOM   1952 C C   . PRO A 1 251 ? 25.718 -27.844 -43.212 1.00 54.41  ?  308 PRO A C   1 
ATOM   1953 O O   . PRO A 1 251 ? 24.519 -27.843 -42.918 1.00 49.29  ?  308 PRO A O   1 
ATOM   1954 C CB  . PRO A 1 251 ? 25.513 -26.573 -45.370 1.00 54.10  ?  308 PRO A CB  1 
ATOM   1955 C CG  . PRO A 1 251 ? 26.498 -26.024 -46.338 1.00 58.72  ?  308 PRO A CG  1 
ATOM   1956 C CD  . PRO A 1 251 ? 27.876 -26.380 -45.871 1.00 42.71  ?  308 PRO A CD  1 
ATOM   1957 N N   . SER A 1 252 ? 26.547 -28.811 -42.820 1.00 55.41  ?  309 SER A N   1 
ATOM   1958 C CA  . SER A 1 252 ? 26.072 -29.933 -42.011 1.00 59.54  ?  309 SER A CA  1 
ATOM   1959 C C   . SER A 1 252 ? 25.411 -29.445 -40.721 1.00 57.82  ?  309 SER A C   1 
ATOM   1960 O O   . SER A 1 252 ? 26.052 -28.795 -39.887 1.00 53.35  ?  309 SER A O   1 
ATOM   1961 C CB  . SER A 1 252 ? 27.228 -30.876 -41.690 1.00 56.62  ?  309 SER A CB  1 
ATOM   1962 O OG  . SER A 1 252 ? 27.675 -31.537 -42.863 1.00 67.83  ?  309 SER A OG  1 
ATOM   1963 N N   . ALA A 1 253 ? 24.127 -29.774 -40.566 1.00 42.04  ?  310 ALA A N   1 
ATOM   1964 C CA  . ALA A 1 253 ? 23.364 -29.373 -39.389 1.00 37.26  ?  310 ALA A CA  1 
ATOM   1965 C C   . ALA A 1 253 ? 23.913 -30.032 -38.125 1.00 38.10  ?  310 ALA A C   1 
ATOM   1966 O O   . ALA A 1 253 ? 24.311 -31.200 -38.129 1.00 50.18  ?  310 ALA A O   1 
ATOM   1967 C CB  . ALA A 1 253 ? 21.889 -29.734 -39.578 1.00 40.21  ?  310 ALA A CB  1 
ATOM   1968 N N   . GLN A 1 254 ? 23.922 -29.280 -37.033 1.00 40.79  ?  311 GLN A N   1 
ATOM   1969 C CA  . GLN A 1 254 ? 24.510 -29.726 -35.780 1.00 47.19  ?  311 GLN A CA  1 
ATOM   1970 C C   . GLN A 1 254 ? 23.453 -29.722 -34.683 1.00 40.61  ?  311 GLN A C   1 
ATOM   1971 O O   . GLN A 1 254 ? 22.533 -28.900 -34.700 1.00 38.74  ?  311 GLN A O   1 
ATOM   1972 C CB  . GLN A 1 254 ? 25.669 -28.813 -35.379 1.00 49.90  ?  311 GLN A CB  1 
ATOM   1973 C CG  . GLN A 1 254 ? 26.639 -28.496 -36.517 1.00 50.26  ?  311 GLN A CG  1 
ATOM   1974 C CD  . GLN A 1 254 ? 27.914 -27.848 -36.018 1.00 65.97  ?  311 GLN A CD  1 
ATOM   1975 O OE1 . GLN A 1 254 ? 28.316 -28.046 -34.868 1.00 63.66  ?  311 GLN A OE1 1 
ATOM   1976 N NE2 . GLN A 1 254 ? 28.540 -27.040 -36.869 1.00 52.71  ?  311 GLN A NE2 1 
ATOM   1977 N N   . SER A 1 255 ? 23.592 -30.635 -33.718 1.00 41.91  ?  312 SER A N   1 
ATOM   1978 C CA  . SER A 1 255 ? 22.685 -30.639 -32.576 1.00 37.70  ?  312 SER A CA  1 
ATOM   1979 C C   . SER A 1 255 ? 22.737 -29.291 -31.855 1.00 35.38  ?  312 SER A C   1 
ATOM   1980 O O   . SER A 1 255 ? 23.752 -28.587 -31.910 1.00 38.22  ?  312 SER A O   1 
ATOM   1981 C CB  . SER A 1 255 ? 23.027 -31.755 -31.583 1.00 36.75  ?  312 SER A CB  1 
ATOM   1982 O OG  . SER A 1 255 ? 23.320 -32.980 -32.233 1.00 43.94  ?  312 SER A OG  1 
ATOM   1983 N N   . PRO A 1 256 ? 21.650 -28.902 -31.184 1.00 36.86  ?  313 PRO A N   1 
ATOM   1984 C CA  . PRO A 1 256 ? 21.692 -27.676 -30.383 1.00 31.24  ?  313 PRO A CA  1 
ATOM   1985 C C   . PRO A 1 256 ? 22.829 -27.752 -29.384 1.00 34.94  ?  313 PRO A C   1 
ATOM   1986 O O   . PRO A 1 256 ? 23.107 -28.805 -28.811 1.00 31.78  ?  313 PRO A O   1 
ATOM   1987 C CB  . PRO A 1 256 ? 20.333 -27.645 -29.671 1.00 36.26  ?  313 PRO A CB  1 
ATOM   1988 C CG  . PRO A 1 256 ? 19.493 -28.667 -30.317 1.00 34.94  ?  313 PRO A CG  1 
ATOM   1989 C CD  . PRO A 1 256 ? 20.351 -29.594 -31.118 1.00 43.46  ?  313 PRO A CD  1 
ATOM   1990 N N   . GLN A 1 257 ? 23.498 -26.631 -29.187 1.00 25.99  ?  314 GLN A N   1 
ATOM   1991 C CA  . GLN A 1 257 ? 24.552 -26.547 -28.192 1.00 23.38  ?  314 GLN A CA  1 
ATOM   1992 C C   . GLN A 1 257 ? 23.995 -25.803 -26.992 1.00 25.21  ?  314 GLN A C   1 
ATOM   1993 O O   . GLN A 1 257 ? 23.491 -24.680 -27.140 1.00 25.95  ?  314 GLN A O   1 
ATOM   1994 C CB  . GLN A 1 257 ? 25.791 -25.836 -28.729 1.00 32.06  ?  314 GLN A CB  1 
ATOM   1995 C CG  . GLN A 1 257 ? 26.860 -25.706 -27.661 1.00 38.68  ?  314 GLN A CG  1 
ATOM   1996 C CD  . GLN A 1 257 ? 28.185 -25.259 -28.214 1.00 43.94  ?  314 GLN A CD  1 
ATOM   1997 O OE1 . GLN A 1 257 ? 28.295 -24.942 -29.397 1.00 42.44  ?  314 GLN A OE1 1 
ATOM   1998 N NE2 . GLN A 1 257 ? 29.204 -25.218 -27.356 1.00 35.05  ?  314 GLN A NE2 1 
ATOM   1999 N N   . LEU A 1 258 ? 24.058 -26.441 -25.821 1.00 24.25  ?  315 LEU A N   1 
ATOM   2000 C CA  . LEU A 1 258 ? 23.579 -25.859 -24.573 1.00 24.03  ?  315 LEU A CA  1 
ATOM   2001 C C   . LEU A 1 258 ? 24.768 -25.364 -23.773 1.00 20.16  ?  315 LEU A C   1 
ATOM   2002 O O   . LEU A 1 258 ? 25.639 -26.155 -23.404 1.00 27.24  ?  315 LEU A O   1 
ATOM   2003 C CB  . LEU A 1 258 ? 22.798 -26.866 -23.731 1.00 29.38  ?  315 LEU A CB  1 
ATOM   2004 C CG  . LEU A 1 258 ? 21.423 -27.330 -24.198 1.00 45.17  ?  315 LEU A CG  1 
ATOM   2005 C CD1 . LEU A 1 258 ? 20.748 -28.112 -23.073 1.00 42.82  ?  315 LEU A CD1 1 
ATOM   2006 C CD2 . LEU A 1 258 ? 20.579 -26.150 -24.603 1.00 32.43  ?  315 LEU A CD2 1 
ATOM   2007 N N   . LEU A 1 259 ? 24.791 -24.064 -23.487 1.00 17.31  ?  316 LEU A N   1 
ATOM   2008 C CA  . LEU A 1 259 ? 25.869 -23.543 -22.673 1.00 18.05  ?  316 LEU A CA  1 
ATOM   2009 C C   . LEU A 1 259 ? 25.490 -23.614 -21.190 1.00 16.50  ?  316 LEU A C   1 
ATOM   2010 O O   . LEU A 1 259 ? 24.330 -23.372 -20.820 1.00 22.54  ?  316 LEU A O   1 
ATOM   2011 C CB  . LEU A 1 259 ? 26.176 -22.095 -23.055 1.00 18.13  ?  316 LEU A CB  1 
ATOM   2012 C CG  . LEU A 1 259 ? 26.597 -21.813 -24.489 1.00 22.71  ?  316 LEU A CG  1 
ATOM   2013 C CD1 . LEU A 1 259 ? 26.990 -20.343 -24.612 1.00 22.13  ?  316 LEU A CD1 1 
ATOM   2014 C CD2 . LEU A 1 259 ? 27.740 -22.711 -24.891 1.00 29.00  ?  316 LEU A CD2 1 
ATOM   2015 N N   . PRO A 1 260 ? 26.443 -23.949 -20.330 1.00 17.84  ?  317 PRO A N   1 
ATOM   2016 C CA  . PRO A 1 260 ? 26.149 -24.051 -18.900 1.00 18.21  ?  317 PRO A CA  1 
ATOM   2017 C C   . PRO A 1 260 ? 26.021 -22.675 -18.266 1.00 21.01  ?  317 PRO A C   1 
ATOM   2018 O O   . PRO A 1 260 ? 26.517 -21.671 -18.782 1.00 19.68  ?  317 PRO A O   1 
ATOM   2019 C CB  . PRO A 1 260 ? 27.369 -24.790 -18.347 1.00 25.81  ?  317 PRO A CB  1 
ATOM   2020 C CG  . PRO A 1 260 ? 28.483 -24.350 -19.256 1.00 31.77  ?  317 PRO A CG  1 
ATOM   2021 C CD  . PRO A 1 260 ? 27.854 -24.243 -20.636 1.00 21.66  ?  317 PRO A CD  1 
ATOM   2022 N N   . VAL A 1 261 ? 25.340 -22.653 -17.123 1.00 16.63  ?  318 VAL A N   1 
ATOM   2023 C CA  . VAL A 1 261 ? 25.262 -21.444 -16.314 1.00 15.83  ?  318 VAL A CA  1 
ATOM   2024 C C   . VAL A 1 261 ? 25.769 -21.789 -14.918 1.00 16.68  ?  318 VAL A C   1 
ATOM   2025 O O   . VAL A 1 261 ? 25.895 -22.961 -14.550 1.00 20.39  ?  318 VAL A O   1 
ATOM   2026 C CB  . VAL A 1 261 ? 23.837 -20.849 -16.277 1.00 17.71  ?  318 VAL A CB  1 
ATOM   2027 C CG1 . VAL A 1 261 ? 23.394 -20.471 -17.698 1.00 17.51  ?  318 VAL A CG1 1 
ATOM   2028 C CG2 . VAL A 1 261 ? 22.872 -21.824 -15.664 1.00 18.78  ?  318 VAL A CG2 1 
ATOM   2029 N N   . THR A 1 262 ? 26.111 -20.757 -14.153 1.00 15.05  ?  319 THR A N   1 
ATOM   2030 C CA  . THR A 1 262 ? 26.658 -20.954 -12.819 1.00 15.14  ?  319 THR A CA  1 
ATOM   2031 C C   . THR A 1 262 ? 26.004 -20.000 -11.830 1.00 13.71  ?  319 THR A C   1 
ATOM   2032 O O   . THR A 1 262 ? 25.446 -18.970 -12.200 1.00 15.39  ?  319 THR A O   1 
ATOM   2033 C CB  . THR A 1 262 ? 28.168 -20.719 -12.775 1.00 17.30  ?  319 THR A CB  1 
ATOM   2034 O OG1 . THR A 1 262 ? 28.451 -19.394 -13.251 1.00 21.22  ?  319 THR A OG1 1 
ATOM   2035 C CG2 . THR A 1 262 ? 28.891 -21.750 -13.647 1.00 19.05  ?  319 THR A CG2 1 
ATOM   2036 N N   . LEU A 1 263 ? 26.106 -20.349 -10.550 1.00 13.01  ?  320 LEU A N   1 
ATOM   2037 C CA  . LEU A 1 263 ? 25.675 -19.472 -9.470  1.00 11.19  ?  320 LEU A CA  1 
ATOM   2038 C C   . LEU A 1 263 ? 26.867 -18.633 -9.030  1.00 14.55  ?  320 LEU A C   1 
ATOM   2039 O O   . LEU A 1 263 ? 27.939 -19.179 -8.776  1.00 15.31  ?  320 LEU A O   1 
ATOM   2040 C CB  . LEU A 1 263 ? 25.142 -20.304 -8.301  1.00 16.05  ?  320 LEU A CB  1 
ATOM   2041 C CG  . LEU A 1 263 ? 24.825 -19.531 -7.019  1.00 15.37  ?  320 LEU A CG  1 
ATOM   2042 C CD1 . LEU A 1 263 ? 23.597 -18.687 -7.281  1.00 17.40  ?  320 LEU A CD1 1 
ATOM   2043 C CD2 . LEU A 1 263 ? 24.621 -20.516 -5.860  1.00 19.20  ?  320 LEU A CD2 1 
ATOM   2044 N N   . VAL A 1 264 ? 26.694 -17.315 -9.008  1.00 13.19  ?  321 VAL A N   1 
ATOM   2045 C CA  . VAL A 1 264 ? 27.695 -16.392 -8.470  1.00 12.28  ?  321 VAL A CA  1 
ATOM   2046 C C   . VAL A 1 264 ? 27.193 -15.916 -7.119  1.00 12.24  ?  321 VAL A C   1 
ATOM   2047 O O   . VAL A 1 264 ? 26.189 -15.192 -7.042  1.00 12.56  ?  321 VAL A O   1 
ATOM   2048 C CB  . VAL A 1 264 ? 27.950 -15.210 -9.413  1.00 15.05  ?  321 VAL A CB  1 
ATOM   2049 C CG1 . VAL A 1 264 ? 28.985 -14.273 -8.804  1.00 13.44  ?  321 VAL A CG1 1 
ATOM   2050 C CG2 . VAL A 1 264 ? 28.428 -15.720 -10.782 1.00 18.52  ?  321 VAL A CG2 1 
ATOM   2051 N N   . LYS A 1 265 ? 27.890 -16.320 -6.054  1.00 12.43  ?  322 LYS A N   1 
ATOM   2052 C CA  . LYS A 1 265 ? 27.526 -15.958 -4.697  1.00 12.37  ?  322 LYS A CA  1 
ATOM   2053 C C   . LYS A 1 265 ? 28.133 -14.607 -4.364  1.00 13.39  ?  322 LYS A C   1 
ATOM   2054 O O   . LYS A 1 265 ? 29.357 -14.438 -4.417  1.00 15.59  ?  322 LYS A O   1 
ATOM   2055 C CB  . LYS A 1 265 ? 28.032 -17.020 -3.727  1.00 16.84  ?  322 LYS A CB  1 
ATOM   2056 C CG  . LYS A 1 265 ? 27.356 -18.381 -3.884  1.00 17.31  ?  322 LYS A CG  1 
ATOM   2057 C CD  . LYS A 1 265 ? 27.965 -19.327 -2.834  1.00 23.59  ?  322 LYS A CD  1 
ATOM   2058 C CE  . LYS A 1 265 ? 27.895 -20.768 -3.230  1.00 31.52  ?  322 LYS A CE  1 
ATOM   2059 N NZ  . LYS A 1 265 ? 28.670 -21.634 -2.269  1.00 24.63  ?  322 LYS A NZ  1 
ATOM   2060 N N   . ARG A 1 266 ? 27.275 -13.639 -4.041  1.00 13.01  ?  323 ARG A N   1 
ATOM   2061 C CA  . ARG A 1 266 ? 27.751 -12.345 -3.579  1.00 11.43  ?  323 ARG A CA  1 
ATOM   2062 C C   . ARG A 1 266 ? 27.187 -12.098 -2.191  1.00 11.60  ?  323 ARG A C   1 
ATOM   2063 O O   . ARG A 1 266 ? 27.525 -12.845 -1.265  1.00 14.77  ?  323 ARG A O   1 
ATOM   2064 C CB  . ARG A 1 266 ? 27.368 -11.235 -4.563  1.00 11.02  ?  323 ARG A CB  1 
ATOM   2065 C CG  . ARG A 1 266 ? 28.068 -11.434 -5.926  1.00 13.86  ?  323 ARG A CG  1 
ATOM   2066 C CD  . ARG A 1 266 ? 28.218 -10.128 -6.711  1.00 13.45  ?  323 ARG A CD  1 
ATOM   2067 N NE  . ARG A 1 266 ? 28.943 -10.306 -7.975  1.00 13.59  ?  323 ARG A NE  1 
ATOM   2068 C CZ  . ARG A 1 266 ? 28.356 -10.450 -9.160  1.00 13.48  ?  323 ARG A CZ  1 
ATOM   2069 N NH1 . ARG A 1 266 ? 27.032 -10.478 -9.285  1.00 13.13  ?  323 ARG A NH1 1 
ATOM   2070 N NH2 . ARG A 1 266 ? 29.119 -10.553 -10.254 1.00 13.15  ?  323 ARG A NH2 1 
ATOM   2071 N N   . LYS A 1 267 ? 26.319 -11.082 -2.032  1.00 9.57   ?  324 LYS A N   1 
ATOM   2072 C CA  . LYS A 1 267 ? 25.947 -10.602 -0.703  1.00 11.56  ?  324 LYS A CA  1 
ATOM   2073 C C   . LYS A 1 267 ? 24.449 -10.545 -0.444  1.00 14.16  ?  324 LYS A C   1 
ATOM   2074 O O   . LYS A 1 267 ? 24.040 -9.917  0.541   1.00 14.32  ?  324 LYS A O   1 
ATOM   2075 C CB  . LYS A 1 267 ? 26.545 -9.213  -0.479  1.00 12.59  ?  324 LYS A CB  1 
ATOM   2076 C CG  . LYS A 1 267 ? 28.063 -9.159  -0.611  1.00 13.11  ?  324 LYS A CG  1 
ATOM   2077 C CD  . LYS A 1 267 ? 28.723 -9.798  0.592   1.00 18.01  ?  324 LYS A CD  1 
ATOM   2078 C CE  . LYS A 1 267 ? 30.245 -9.716  0.473   1.00 23.99  ?  324 LYS A CE  1 
ATOM   2079 N NZ  . LYS A 1 267 ? 30.917 -10.898 1.099   1.00 41.94  ?  324 LYS A NZ  1 
ATOM   2080 N N   . THR A 1 268 ? 23.605 -11.193 -1.258  1.00 11.96  ?  325 THR A N   1 
ATOM   2081 C CA  . THR A 1 268 ? 22.169 -11.098 -1.041  1.00 11.99  ?  325 THR A CA  1 
ATOM   2082 C C   . THR A 1 268 ? 21.499 -12.391 -0.561  1.00 11.18  ?  325 THR A C   1 
ATOM   2083 O O   . THR A 1 268 ? 20.260 -12.443 -0.542  1.00 11.73  ?  325 THR A O   1 
ATOM   2084 C CB  . THR A 1 268 ? 21.469 -10.588 -2.306  1.00 11.68  ?  325 THR A CB  1 
ATOM   2085 O OG1 . THR A 1 268 ? 21.760 -11.444 -3.420  1.00 11.34  ?  325 THR A OG1 1 
ATOM   2086 C CG2 . THR A 1 268 ? 21.939 -9.150  -2.657  1.00 12.16  ?  325 THR A CG2 1 
ATOM   2087 N N   . THR A 1 269 ? 22.250 -13.418 -0.136  1.00 12.51  ?  326 THR A N   1 
ATOM   2088 C CA  . THR A 1 269 ? 21.594 -14.581 0.467   1.00 14.04  ?  326 THR A CA  1 
ATOM   2089 C C   . THR A 1 269 ? 22.227 -14.991 1.798   1.00 13.22  ?  326 THR A C   1 
ATOM   2090 O O   . THR A 1 269 ? 23.402 -14.739 2.077   1.00 15.68  ?  326 THR A O   1 
ATOM   2091 C CB  . THR A 1 269 ? 21.544 -15.817 -0.486  1.00 13.42  ?  326 THR A CB  1 
ATOM   2092 O OG1 . THR A 1 269 ? 22.836 -16.393 -0.606  1.00 16.40  ?  326 THR A OG1 1 
ATOM   2093 C CG2 . THR A 1 269 ? 21.004 -15.474 -1.879  1.00 11.69  ?  326 THR A CG2 1 
ATOM   2094 N N   . ALA A 1 270 ? 21.406 -15.626 2.623   1.00 13.02  ?  327 ALA A N   1 
ATOM   2095 C CA  . ALA A 1 270 ? 21.776 -16.065 3.963   1.00 14.31  ?  327 ALA A CA  1 
ATOM   2096 C C   . ALA A 1 270 ? 20.698 -17.029 4.420   1.00 14.45  ?  327 ALA A C   1 
ATOM   2097 O O   . ALA A 1 270 ? 19.631 -17.075 3.813   1.00 15.99  ?  327 ALA A O   1 
ATOM   2098 C CB  . ALA A 1 270 ? 21.870 -14.867 4.935   1.00 17.75  ?  327 ALA A CB  1 
ATOM   2099 N N   . PRO A 1 271 ? 20.923 -17.801 5.485   1.00 15.33  ?  328 PRO A N   1 
ATOM   2100 C CA  . PRO A 1 271 ? 19.836 -18.613 6.013   1.00 16.18  ?  328 PRO A CA  1 
ATOM   2101 C C   . PRO A 1 271 ? 18.660 -17.749 6.440   1.00 17.45  ?  328 PRO A C   1 
ATOM   2102 O O   . PRO A 1 271 ? 18.822 -16.544 6.710   1.00 19.05  ?  328 PRO A O   1 
ATOM   2103 C CB  . PRO A 1 271 ? 20.470 -19.323 7.224   1.00 20.35  ?  328 PRO A CB  1 
ATOM   2104 C CG  . PRO A 1 271 ? 21.925 -19.294 6.959   1.00 22.25  ?  328 PRO A CG  1 
ATOM   2105 C CD  . PRO A 1 271 ? 22.185 -18.018 6.224   1.00 19.36  ?  328 PRO A CD  1 
ATOM   2106 N N   . PRO A 1 272 ? 17.464 -18.317 6.495   1.00 18.58  ?  329 PRO A N   1 
ATOM   2107 C CA  . PRO A 1 272 ? 16.301 -17.554 6.961   1.00 19.60  ?  329 PRO A CA  1 
ATOM   2108 C C   . PRO A 1 272 ? 16.437 -17.104 8.399   1.00 32.95  ?  329 PRO A C   1 
ATOM   2109 O O   . PRO A 1 272 ? 17.092 -17.751 9.221   1.00 26.57  ?  329 PRO A O   1 
ATOM   2110 C CB  . PRO A 1 272 ? 15.137 -18.535 6.799   1.00 23.38  ?  329 PRO A CB  1 
ATOM   2111 C CG  . PRO A 1 272 ? 15.763 -19.880 6.747   1.00 25.86  ?  329 PRO A CG  1 
ATOM   2112 C CD  . PRO A 1 272 ? 17.116 -19.705 6.148   1.00 19.51  ?  329 PRO A CD  1 
ATOM   2113 N N   . GLU A 1 273 ? 15.799 -15.973 8.687   1.00 31.60  ?  330 GLU A N   1 
ATOM   2114 C CA  . GLU A 1 273 ? 15.642 -15.516 10.056  1.00 49.59  ?  330 GLU A CA  1 
ATOM   2115 C C   . GLU A 1 273 ? 14.956 -16.615 10.855  1.00 41.51  ?  330 GLU A C   1 
ATOM   2116 O O   . GLU A 1 273 ? 13.863 -17.058 10.494  1.00 49.25  ?  330 GLU A O   1 
ATOM   2117 C CB  . GLU A 1 273 ? 14.823 -14.226 10.075  1.00 55.54  ?  330 GLU A CB  1 
ATOM   2118 C CG  . GLU A 1 273 ? 15.074 -13.310 11.257  1.00 54.30  ?  330 GLU A CG  1 
ATOM   2119 C CD  . GLU A 1 273 ? 14.386 -11.961 11.087  1.00 47.41  ?  330 GLU A CD  1 
ATOM   2120 O OE1 . GLU A 1 273 ? 13.375 -11.898 10.350  1.00 49.51  ?  330 GLU A OE1 1 
ATOM   2121 O OE2 . GLU A 1 273 ? 14.862 -10.965 11.670  1.00 58.18  -1 330 GLU A OE2 1 
ATOM   2122 N N   . ASN A 1 274 ? 15.618 -17.087 11.904  1.00 56.56  ?  331 ASN A N   1 
ATOM   2123 C CA  . ASN A 1 274 ? 15.169 -18.280 12.614  1.00 69.89  ?  331 ASN A CA  1 
ATOM   2124 C C   . ASN A 1 274 ? 14.291 -17.924 13.809  1.00 72.04  ?  331 ASN A C   1 
ATOM   2125 O O   . ASN A 1 274 ? 13.433 -17.045 13.722  1.00 71.37  ?  331 ASN A O   1 
ATOM   2126 C CB  . ASN A 1 274 ? 16.375 -19.109 13.069  1.00 70.09  ?  331 ASN A CB  1 
ATOM   2127 C CG  . ASN A 1 274 ? 15.997 -20.522 13.471  1.00 84.78  ?  331 ASN A CG  1 
ATOM   2128 O OD1 . ASN A 1 274 ? 15.961 -20.856 14.656  1.00 91.82  ?  331 ASN A OD1 1 
ATOM   2129 N ND2 . ASN A 1 274 ? 15.716 -21.362 12.480  1.00 75.21  ?  331 ASN A ND2 1 
ATOM   2130 N N   . LYS B 1 2   ? 17.756 5.510   -55.693 1.00 61.06  ?  59  LYS B N   1 
ATOM   2131 C CA  . LYS B 1 2   ? 16.392 5.242   -55.249 1.00 46.94  ?  59  LYS B CA  1 
ATOM   2132 C C   . LYS B 1 2   ? 16.316 5.132   -53.730 1.00 73.59  ?  59  LYS B C   1 
ATOM   2133 O O   . LYS B 1 2   ? 17.165 4.496   -53.103 1.00 74.51  ?  59  LYS B O   1 
ATOM   2134 C CB  . LYS B 1 2   ? 15.858 3.960   -55.893 1.00 49.60  ?  59  LYS B CB  1 
ATOM   2135 N N   . GLN B 1 3   ? 15.288 5.751   -53.150 1.00 80.58  ?  60  GLN B N   1 
ATOM   2136 C CA  . GLN B 1 3   ? 15.085 5.695   -51.708 1.00 81.73  ?  60  GLN B CA  1 
ATOM   2137 C C   . GLN B 1 3   ? 14.800 4.262   -51.262 1.00 88.27  ?  60  GLN B C   1 
ATOM   2138 O O   . GLN B 1 3   ? 14.131 3.498   -51.964 1.00 96.74  ?  60  GLN B O   1 
ATOM   2139 C CB  . GLN B 1 3   ? 13.929 6.617   -51.314 1.00 79.29  ?  60  GLN B CB  1 
ATOM   2140 C CG  . GLN B 1 3   ? 14.259 8.103   -51.419 1.00 95.05  ?  60  GLN B CG  1 
ATOM   2141 C CD  . GLN B 1 3   ? 13.754 8.910   -50.234 1.00 105.18 ?  60  GLN B CD  1 
ATOM   2142 O OE1 . GLN B 1 3   ? 12.549 9.135   -50.088 1.00 102.90 ?  60  GLN B OE1 1 
ATOM   2143 N NE2 . GLN B 1 3   ? 14.674 9.348   -49.380 1.00 87.13  ?  60  GLN B NE2 1 
ATOM   2144 N N   . SER B 1 4   ? 15.320 3.894   -50.082 1.00 49.67  ?  61  SER B N   1 
ATOM   2145 C CA  . SER B 1 4   ? 15.121 2.557   -49.536 1.00 54.32  ?  61  SER B CA  1 
ATOM   2146 C C   . SER B 1 4   ? 14.320 2.531   -48.241 1.00 54.64  ?  61  SER B C   1 
ATOM   2147 O O   . SER B 1 4   ? 13.987 1.436   -47.770 1.00 50.80  ?  61  SER B O   1 
ATOM   2148 C CB  . SER B 1 4   ? 16.472 1.872   -49.279 1.00 46.54  ?  61  SER B CB  1 
ATOM   2149 O OG  . SER B 1 4   ? 17.261 2.645   -48.389 1.00 48.51  ?  61  SER B OG  1 
ATOM   2150 N N   . HIS B 1 5   ? 14.021 3.690   -47.647 1.00 40.57  ?  62  HIS B N   1 
ATOM   2151 C CA  . HIS B 1 5   ? 13.298 3.777   -46.378 1.00 38.34  ?  62  HIS B CA  1 
ATOM   2152 C C   . HIS B 1 5   ? 14.076 3.079   -45.267 1.00 32.56  ?  62  HIS B C   1 
ATOM   2153 O O   . HIS B 1 5   ? 13.504 2.400   -44.411 1.00 35.90  ?  62  HIS B O   1 
ATOM   2154 C CB  . HIS B 1 5   ? 11.883 3.213   -46.510 1.00 53.06  ?  62  HIS B CB  1 
ATOM   2155 C CG  . HIS B 1 5   ? 10.989 4.052   -47.367 1.00 63.46  ?  62  HIS B CG  1 
ATOM   2156 N ND1 . HIS B 1 5   ? 10.438 5.238   -46.931 1.00 61.04  ?  62  HIS B ND1 1 
ATOM   2157 C CD2 . HIS B 1 5   ? 10.590 3.901   -48.653 1.00 60.62  ?  62  HIS B CD2 1 
ATOM   2158 C CE1 . HIS B 1 5   ? 9.714  5.767   -47.901 1.00 57.31  ?  62  HIS B CE1 1 
ATOM   2159 N NE2 . HIS B 1 5   ? 9.792  4.977   -48.958 1.00 57.38  ?  62  HIS B NE2 1 
ATOM   2160 N N   . THR B 1 6   ? 15.396 3.262   -45.278 1.00 32.00  ?  63  THR B N   1 
ATOM   2161 C CA  . THR B 1 6   ? 16.281 2.649   -44.294 1.00 27.94  ?  63  THR B CA  1 
ATOM   2162 C C   . THR B 1 6   ? 17.251 3.707   -43.795 1.00 29.87  ?  63  THR B C   1 
ATOM   2163 O O   . THR B 1 6   ? 17.892 4.392   -44.595 1.00 32.75  ?  63  THR B O   1 
ATOM   2164 C CB  . THR B 1 6   ? 17.043 1.454   -44.894 1.00 28.13  ?  63  THR B CB  1 
ATOM   2165 O OG1 . THR B 1 6   ? 16.110 0.441   -45.279 1.00 34.59  ?  63  THR B OG1 1 
ATOM   2166 C CG2 . THR B 1 6   ? 17.993 0.844   -43.862 1.00 27.42  ?  63  THR B CG2 1 
ATOM   2167 N N   . ILE B 1 7   ? 17.339 3.856   -42.478 1.00 25.06  ?  64  ILE B N   1 
ATOM   2168 C CA  . ILE B 1 7   ? 18.257 4.788   -41.840 1.00 23.97  ?  64  ILE B CA  1 
ATOM   2169 C C   . ILE B 1 7   ? 19.377 3.948   -41.229 1.00 27.97  ?  64  ILE B C   1 
ATOM   2170 O O   . ILE B 1 7   ? 19.110 2.900   -40.624 1.00 23.64  ?  64  ILE B O   1 
ATOM   2171 C CB  . ILE B 1 7   ? 17.540 5.626   -40.764 1.00 27.53  ?  64  ILE B CB  1 
ATOM   2172 C CG1 . ILE B 1 7   ? 16.749 6.774   -41.395 1.00 27.14  ?  64  ILE B CG1 1 
ATOM   2173 C CG2 . ILE B 1 7   ? 18.532 6.238   -39.792 1.00 26.85  ?  64  ILE B CG2 1 
ATOM   2174 C CD1 . ILE B 1 7   ? 15.565 7.204   -40.539 1.00 37.90  ?  64  ILE B CD1 1 
ATOM   2175 N N   . GLY B 1 8   ? 20.622 4.375   -41.420 1.00 23.18  ?  65  GLY B N   1 
ATOM   2176 C CA  . GLY B 1 8   ? 21.774 3.715   -40.813 1.00 20.71  ?  65  GLY B CA  1 
ATOM   2177 C C   . GLY B 1 8   ? 22.204 4.440   -39.544 1.00 23.02  ?  65  GLY B C   1 
ATOM   2178 O O   . GLY B 1 8   ? 22.248 5.665   -39.505 1.00 23.65  ?  65  GLY B O   1 
ATOM   2179 N N   . LEU B 1 9   ? 22.523 3.669   -38.509 1.00 19.95  ?  66  LEU B N   1 
ATOM   2180 C CA  . LEU B 1 9   ? 22.890 4.218   -37.204 1.00 20.90  ?  66  LEU B CA  1 
ATOM   2181 C C   . LEU B 1 9   ? 24.217 3.615   -36.760 1.00 25.49  ?  66  LEU B C   1 
ATOM   2182 O O   . LEU B 1 9   ? 24.296 2.413   -36.508 1.00 23.73  ?  66  LEU B O   1 
ATOM   2183 C CB  . LEU B 1 9   ? 21.792 3.948   -36.165 1.00 19.36  ?  66  LEU B CB  1 
ATOM   2184 C CG  . LEU B 1 9   ? 22.095 4.197   -34.693 1.00 23.97  ?  66  LEU B CG  1 
ATOM   2185 C CD1 . LEU B 1 9   ? 22.594 5.618   -34.442 1.00 30.32  ?  66  LEU B CD1 1 
ATOM   2186 C CD2 . LEU B 1 9   ? 20.808 3.933   -33.899 1.00 24.91  ?  66  LEU B CD2 1 
ATOM   2187 N N   . ALA B 1 10  ? 25.261 4.439   -36.675 1.00 17.70  ?  67  ALA B N   1 
ATOM   2188 C CA  . ALA B 1 10  ? 26.539 4.023   -36.110 1.00 21.70  ?  67  ALA B CA  1 
ATOM   2189 C C   . ALA B 1 10  ? 26.551 4.410   -34.640 1.00 25.34  ?  67  ALA B C   1 
ATOM   2190 O O   . ALA B 1 10  ? 26.254 5.560   -34.299 1.00 25.15  ?  67  ALA B O   1 
ATOM   2191 C CB  . ALA B 1 10  ? 27.720 4.672   -36.837 1.00 18.82  ?  67  ALA B CB  1 
ATOM   2192 N N   . THR B 1 11  ? 26.892 3.460   -33.773 1.00 21.51  ?  68  THR B N   1 
ATOM   2193 C CA  . THR B 1 11  ? 26.761 3.676   -32.337 1.00 20.16  ?  68  THR B CA  1 
ATOM   2194 C C   . THR B 1 11  ? 27.974 3.131   -31.604 1.00 24.62  ?  68  THR B C   1 
ATOM   2195 O O   . THR B 1 11  ? 28.571 2.121   -31.992 1.00 27.89  ?  68  THR B O   1 
ATOM   2196 C CB  . THR B 1 11  ? 25.466 3.041   -31.774 1.00 21.58  ?  68  THR B CB  1 
ATOM   2197 O OG1 . THR B 1 11  ? 25.380 3.262   -30.356 1.00 22.74  ?  68  THR B OG1 1 
ATOM   2198 C CG2 . THR B 1 11  ? 25.439 1.536   -32.031 1.00 23.28  ?  68  THR B CG2 1 
ATOM   2199 N N   . THR B 1 12  ? 28.340 3.830   -30.538 1.00 22.49  ?  69  THR B N   1 
ATOM   2200 C CA  . THR B 1 12  ? 29.339 3.345   -29.607 1.00 23.28  ?  69  THR B CA  1 
ATOM   2201 C C   . THR B 1 12  ? 28.766 2.176   -28.798 1.00 27.35  ?  69  THR B C   1 
ATOM   2202 O O   . THR B 1 12  ? 27.596 1.804   -28.934 1.00 25.34  ?  69  THR B O   1 
ATOM   2203 C CB  . THR B 1 12  ? 29.768 4.490   -28.696 1.00 26.29  ?  69  THR B CB  1 
ATOM   2204 O OG1 . THR B 1 12  ? 30.841 4.077   -27.843 1.00 33.56  ?  69  THR B OG1 1 
ATOM   2205 C CG2 . THR B 1 12  ? 28.585 4.927   -27.850 1.00 23.03  ?  69  THR B CG2 1 
ATOM   2206 N N   . ASN B 1 13  ? 29.602 1.620   -27.917 1.00 30.98  ?  70  ASN B N   1 
ATOM   2207 C CA  . ASN B 1 13  ? 29.323 0.425   -27.113 1.00 33.32  ?  70  ASN B CA  1 
ATOM   2208 C C   . ASN B 1 13  ? 27.886 0.321   -26.598 1.00 27.43  ?  70  ASN B C   1 
ATOM   2209 O O   . ASN B 1 13  ? 27.468 1.083   -25.720 1.00 22.92  ?  70  ASN B O   1 
ATOM   2210 C CB  . ASN B 1 13  ? 30.320 0.375   -25.943 1.00 29.47  ?  70  ASN B CB  1 
ATOM   2211 C CG  . ASN B 1 13  ? 30.160 -0.860  -25.070 1.00 39.00  ?  70  ASN B CG  1 
ATOM   2212 O OD1 . ASN B 1 13  ? 29.589 -1.865  -25.493 1.00 30.47  ?  70  ASN B OD1 1 
ATOM   2213 N ND2 . ASN B 1 13  ? 30.698 -0.797  -23.847 1.00 30.59  ?  70  ASN B ND2 1 
ATOM   2214 N N   . LEU B 1 14  ? 27.116 -0.634  -27.133 1.00 24.34  ?  71  LEU B N   1 
ATOM   2215 C CA  . LEU B 1 14  ? 25.733 -0.807  -26.702 1.00 24.00  ?  71  LEU B CA  1 
ATOM   2216 C C   . LEU B 1 14  ? 25.615 -1.401  -25.309 1.00 23.69  ?  71  LEU B C   1 
ATOM   2217 O O   . LEU B 1 14  ? 24.513 -1.406  -24.750 1.00 23.24  ?  71  LEU B O   1 
ATOM   2218 C CB  . LEU B 1 14  ? 24.971 -1.689  -27.695 1.00 21.75  ?  71  LEU B CB  1 
ATOM   2219 C CG  . LEU B 1 14  ? 24.724 -0.953  -29.003 1.00 20.68  ?  71  LEU B CG  1 
ATOM   2220 C CD1 . LEU B 1 14  ? 24.224 -1.920  -30.065 1.00 25.99  ?  71  LEU B CD1 1 
ATOM   2221 C CD2 . LEU B 1 14  ? 23.734 0.160   -28.767 1.00 23.49  ?  71  LEU B CD2 1 
ATOM   2222 N N   . ALA B 1 15  ? 26.711 -1.888  -24.738 1.00 19.98  ?  72  ALA B N   1 
ATOM   2223 C CA  . ALA B 1 15  ? 26.683 -2.337  -23.354 1.00 26.76  ?  72  ALA B CA  1 
ATOM   2224 C C   . ALA B 1 15  ? 26.597 -1.184  -22.368 1.00 25.95  ?  72  ALA B C   1 
ATOM   2225 O O   . ALA B 1 15  ? 26.354 -1.422  -21.183 1.00 23.75  ?  72  ALA B O   1 
ATOM   2226 C CB  . ALA B 1 15  ? 27.911 -3.196  -23.050 1.00 31.58  ?  72  ALA B CB  1 
ATOM   2227 N N   . LEU B 1 16  ? 26.805 0.053   -22.804 1.00 19.05  ?  73  LEU B N   1 
ATOM   2228 C CA  . LEU B 1 16  ? 26.475 1.188   -21.959 1.00 15.13  ?  73  LEU B CA  1 
ATOM   2229 C C   . LEU B 1 16  ? 24.996 1.529   -22.141 1.00 16.47  ?  73  LEU B C   1 
ATOM   2230 O O   . LEU B 1 16  ? 24.445 1.419   -23.247 1.00 15.41  ?  73  LEU B O   1 
ATOM   2231 C CB  . LEU B 1 16  ? 27.359 2.383   -22.306 1.00 15.26  ?  73  LEU B CB  1 
ATOM   2232 C CG  . LEU B 1 16  ? 28.840 2.206   -21.958 1.00 17.14  ?  73  LEU B CG  1 
ATOM   2233 C CD1 . LEU B 1 16  ? 29.615 3.459   -22.288 1.00 19.06  ?  73  LEU B CD1 1 
ATOM   2234 C CD2 . LEU B 1 16  ? 29.006 1.843   -20.491 1.00 18.59  ?  73  LEU B CD2 1 
ATOM   2235 N N   . HIS B 1 17  ? 24.341 1.934   -21.040 1.00 14.40  ?  74  HIS B N   1 
ATOM   2236 C CA  . HIS B 1 17  ? 22.878 2.023   -21.052 1.00 13.68  ?  74  HIS B CA  1 
ATOM   2237 C C   . HIS B 1 17  ? 22.358 3.183   -21.895 1.00 14.45  ?  74  HIS B C   1 
ATOM   2238 O O   . HIS B 1 17  ? 21.342 3.031   -22.592 1.00 15.44  ?  74  HIS B O   1 
ATOM   2239 C CB  . HIS B 1 17  ? 22.353 2.126   -19.628 1.00 14.56  ?  74  HIS B CB  1 
ATOM   2240 C CG  . HIS B 1 17  ? 22.711 0.945   -18.783 1.00 15.69  ?  74  HIS B CG  1 
ATOM   2241 N ND1 . HIS B 1 17  ? 23.108 -0.260  -19.321 1.00 17.20  ?  74  HIS B ND1 1 
ATOM   2242 C CD2 . HIS B 1 17  ? 22.741 0.789   -17.439 1.00 17.23  ?  74  HIS B CD2 1 
ATOM   2243 C CE1 . HIS B 1 17  ? 23.364 -1.108  -18.339 1.00 17.65  ?  74  HIS B CE1 1 
ATOM   2244 N NE2 . HIS B 1 17  ? 23.155 -0.495  -17.187 1.00 18.19  ?  74  HIS B NE2 1 
ATOM   2245 N N   . ALA B 1 18  ? 23.004 4.343   -21.834 1.00 14.79  ?  75  ALA B N   1 
ATOM   2246 C CA  . ALA B 1 18  ? 22.530 5.478   -22.632 1.00 14.41  ?  75  ALA B CA  1 
ATOM   2247 C C   . ALA B 1 18  ? 22.552 5.188   -24.136 1.00 15.01  ?  75  ALA B C   1 
ATOM   2248 O O   . ALA B 1 18  ? 21.516 5.409   -24.796 1.00 14.64  ?  75  ALA B O   1 
ATOM   2249 C CB  . ALA B 1 18  ? 23.315 6.738   -22.249 1.00 16.00  ?  75  ALA B CB  1 
ATOM   2250 N N   . PRO B 1 19  ? 23.648 4.698   -24.740 1.00 14.52  ?  76  PRO B N   1 
ATOM   2251 C CA  . PRO B 1 19  ? 23.586 4.406   -26.189 1.00 15.22  ?  76  PRO B CA  1 
ATOM   2252 C C   . PRO B 1 19  ? 22.493 3.414   -26.565 1.00 15.64  ?  76  PRO B C   1 
ATOM   2253 O O   . PRO B 1 19  ? 21.889 3.550   -27.632 1.00 14.29  ?  76  PRO B O   1 
ATOM   2254 C CB  . PRO B 1 19  ? 24.983 3.847   -26.508 1.00 18.15  ?  76  PRO B CB  1 
ATOM   2255 C CG  . PRO B 1 19  ? 25.867 4.261   -25.412 1.00 21.46  ?  76  PRO B CG  1 
ATOM   2256 C CD  . PRO B 1 19  ? 25.014 4.576   -24.201 1.00 16.80  ?  76  PRO B CD  1 
ATOM   2257 N N   A SER B 1 20  ? 22.219 2.418   -25.726 0.75 13.84  ?  77  SER B N   1 
ATOM   2258 N N   B SER B 1 20  ? 22.218 2.419   -25.718 0.25 13.80  ?  77  SER B N   1 
ATOM   2259 C CA  A SER B 1 20  ? 21.166 1.469   -26.055 0.75 13.46  ?  77  SER B CA  1 
ATOM   2260 C CA  B SER B 1 20  ? 21.171 1.456   -26.040 0.25 13.47  ?  77  SER B CA  1 
ATOM   2261 C C   A SER B 1 20  ? 19.793 2.116   -25.979 0.75 15.81  ?  77  SER B C   1 
ATOM   2262 C C   B SER B 1 20  ? 19.788 2.092   -25.963 0.25 15.80  ?  77  SER B C   1 
ATOM   2263 O O   A SER B 1 20  ? 18.911 1.805   -26.787 0.75 16.20  ?  77  SER B O   1 
ATOM   2264 O O   B SER B 1 20  ? 18.902 1.754   -26.756 0.25 16.30  ?  77  SER B O   1 
ATOM   2265 C CB  A SER B 1 20  ? 21.249 0.265   -25.130 0.75 15.72  ?  77  SER B CB  1 
ATOM   2266 C CB  B SER B 1 20  ? 21.258 0.246   -25.111 0.25 15.71  ?  77  SER B CB  1 
ATOM   2267 O OG  A SER B 1 20  ? 22.157 -0.673  -25.668 0.75 22.19  ?  77  SER B OG  1 
ATOM   2268 O OG  B SER B 1 20  ? 21.348 0.645   -23.758 0.25 17.21  ?  77  SER B OG  1 
ATOM   2269 N N   . GLN B 1 21  ? 19.573 3.003   -25.009 1.00 15.70  ?  78  GLN B N   1 
ATOM   2270 C CA  . GLN B 1 21  ? 18.297 3.708   -24.966 1.00 15.09  ?  78  GLN B CA  1 
ATOM   2271 C C   . GLN B 1 21  ? 18.151 4.632   -26.160 1.00 15.94  ?  78  GLN B C   1 
ATOM   2272 O O   . GLN B 1 21  ? 17.033 4.822   -26.647 1.00 16.27  ?  78  GLN B O   1 
ATOM   2273 C CB  . GLN B 1 21  ? 18.132 4.498   -23.654 1.00 16.42  ?  78  GLN B CB  1 
ATOM   2274 C CG  . GLN B 1 21  ? 17.728 3.576   -22.503 1.00 14.12  ?  78  GLN B CG  1 
ATOM   2275 C CD  . GLN B 1 21  ? 17.328 4.284   -21.221 1.00 16.50  ?  78  GLN B CD  1 
ATOM   2276 O OE1 . GLN B 1 21  ? 17.863 3.979   -20.157 1.00 15.42  ?  78  GLN B OE1 1 
ATOM   2277 N NE2 . GLN B 1 21  ? 16.339 5.181   -21.300 1.00 17.56  ?  78  GLN B NE2 1 
ATOM   2278 N N   . ILE B 1 22  ? 19.259 5.187   -26.655 1.00 14.06  ?  79  ILE B N   1 
ATOM   2279 C CA  . ILE B 1 22  ? 19.201 6.035   -27.842 1.00 15.90  ?  79  ILE B CA  1 
ATOM   2280 C C   . ILE B 1 22  ? 18.832 5.202   -29.074 1.00 17.44  ?  79  ILE B C   1 
ATOM   2281 O O   . ILE B 1 22  ? 17.959 5.604   -29.858 1.00 16.76  ?  79  ILE B O   1 
ATOM   2282 C CB  . ILE B 1 22  ? 20.528 6.800   -28.023 1.00 15.65  ?  79  ILE B CB  1 
ATOM   2283 C CG1 . ILE B 1 22  ? 20.647 7.892   -26.945 1.00 16.73  ?  79  ILE B CG1 1 
ATOM   2284 C CG2 . ILE B 1 22  ? 20.604 7.408   -29.422 1.00 20.33  ?  79  ILE B CG2 1 
ATOM   2285 C CD1 . ILE B 1 22  ? 22.046 8.501   -26.817 1.00 17.70  ?  79  ILE B CD1 1 
ATOM   2286 N N   . VAL B 1 23  ? 19.423 4.003   -29.231 1.00 15.30  ?  80  VAL B N   1 
ATOM   2287 C CA  . VAL B 1 23  ? 19.040 3.122   -30.344 1.00 13.07  ?  80  VAL B CA  1 
ATOM   2288 C C   . VAL B 1 23  ? 17.548 2.815   -30.292 1.00 17.37  ?  80  VAL B C   1 
ATOM   2289 O O   . VAL B 1 23  ? 16.824 2.922   -31.300 1.00 16.54  ?  80  VAL B O   1 
ATOM   2290 C CB  . VAL B 1 23  ? 19.858 1.817   -30.332 1.00 14.45  ?  80  VAL B CB  1 
ATOM   2291 C CG1 . VAL B 1 23  ? 19.263 0.830   -31.372 1.00 18.67  ?  80  VAL B CG1 1 
ATOM   2292 C CG2 . VAL B 1 23  ? 21.341 2.100   -30.612 1.00 21.54  ?  80  VAL B CG2 1 
ATOM   2293 N N   . ALA B 1 24  ? 17.055 2.443   -29.106 1.00 17.03  ?  81  ALA B N   1 
ATOM   2294 C CA  . ALA B 1 24  ? 15.647 2.116   -28.955 1.00 18.91  ?  81  ALA B CA  1 
ATOM   2295 C C   . ALA B 1 24  ? 14.759 3.294   -29.341 1.00 20.74  ?  81  ALA B C   1 
ATOM   2296 O O   . ALA B 1 24  ? 13.755 3.120   -30.035 1.00 20.88  ?  81  ALA B O   1 
ATOM   2297 C CB  . ALA B 1 24  ? 15.378 1.665   -27.523 1.00 16.73  ?  81  ALA B CB  1 
ATOM   2298 N N   . ALA B 1 25  ? 15.130 4.510   -28.932 1.00 17.41  ?  82  ALA B N   1 
ATOM   2299 C CA  . ALA B 1 25  ? 14.289 5.665   -29.226 1.00 19.48  ?  82  ALA B CA  1 
ATOM   2300 C C   . ALA B 1 25  ? 14.333 6.035   -30.704 1.00 19.90  ?  82  ALA B C   1 
ATOM   2301 O O   . ALA B 1 25  ? 13.333 6.501   -31.252 1.00 22.95  ?  82  ALA B O   1 
ATOM   2302 C CB  . ALA B 1 25  ? 14.716 6.856   -28.365 1.00 22.11  ?  82  ALA B CB  1 
ATOM   2303 N N   . ILE B 1 26  ? 15.479 5.847   -31.357 1.00 17.98  ?  83  ILE B N   1 
ATOM   2304 C CA  . ILE B 1 26  ? 15.579 6.106   -32.793 1.00 18.28  ?  83  ILE B CA  1 
ATOM   2305 C C   . ILE B 1 26  ? 14.746 5.102   -33.592 1.00 22.17  ?  83  ILE B C   1 
ATOM   2306 O O   . ILE B 1 26  ? 13.986 5.479   -34.500 1.00 22.96  ?  83  ILE B O   1 
ATOM   2307 C CB  . ILE B 1 26  ? 17.056 6.099   -33.219 1.00 16.17  ?  83  ILE B CB  1 
ATOM   2308 C CG1 . ILE B 1 26  ? 17.732 7.376   -32.700 1.00 19.17  ?  83  ILE B CG1 1 
ATOM   2309 C CG2 . ILE B 1 26  ? 17.182 5.938   -34.745 1.00 19.83  ?  83  ILE B CG2 1 
ATOM   2310 C CD1 . ILE B 1 26  ? 19.207 7.442   -32.917 1.00 19.53  ?  83  ILE B CD1 1 
ATOM   2311 N N   . LYS B 1 27  ? 14.866 3.816   -33.257 1.00 19.73  ?  84  LYS B N   1 
ATOM   2312 C CA  . LYS B 1 27  ? 14.054 2.788   -33.903 1.00 18.96  ?  84  LYS B CA  1 
ATOM   2313 C C   . LYS B 1 27  ? 12.565 3.085   -33.762 1.00 24.71  ?  84  LYS B C   1 
ATOM   2314 O O   . LYS B 1 27  ? 11.808 2.975   -34.737 1.00 24.91  ?  84  LYS B O   1 
ATOM   2315 C CB  . LYS B 1 27  ? 14.402 1.417   -33.309 1.00 18.65  ?  84  LYS B CB  1 
ATOM   2316 C CG  . LYS B 1 27  ? 13.855 0.217   -34.090 1.00 24.35  ?  84  LYS B CG  1 
ATOM   2317 C CD  . LYS B 1 27  ? 12.542 -0.272  -33.526 1.00 24.45  ?  84  LYS B CD  1 
ATOM   2318 C CE  . LYS B 1 27  ? 12.010 -1.425  -34.365 1.00 28.69  ?  84  LYS B CE  1 
ATOM   2319 N NZ  . LYS B 1 27  ? 10.646 -1.794  -33.934 1.00 46.88  ?  84  LYS B NZ  1 
ATOM   2320 N N   . SER B 1 28  ? 12.128 3.490   -32.563 1.00 22.02  ?  85  SER B N   1 
ATOM   2321 C CA  . SER B 1 28  ? 10.713 3.754   -32.334 1.00 25.57  ?  85  SER B CA  1 
ATOM   2322 C C   . SER B 1 28  ? 10.195 4.856   -33.254 1.00 23.55  ?  85  SER B C   1 
ATOM   2323 O O   . SER B 1 28  ? 9.171  4.681   -33.930 1.00 29.53  ?  85  SER B O   1 
ATOM   2324 C CB  . SER B 1 28  ? 10.492 4.120   -30.871 1.00 26.31  ?  85  SER B CB  1 
ATOM   2325 O OG  . SER B 1 28  ? 9.140  4.454   -30.636 1.00 37.91  ?  85  SER B OG  1 
ATOM   2326 N N   . ARG B 1 29  ? 10.881 6.004   -33.300 1.00 26.93  ?  86  ARG B N   1 
ATOM   2327 C CA  . ARG B 1 29  ? 10.411 7.081   -34.171 1.00 27.57  ?  86  ARG B CA  1 
ATOM   2328 C C   . ARG B 1 29  ? 10.527 6.689   -35.641 1.00 27.45  ?  86  ARG B C   1 
ATOM   2329 O O   . ARG B 1 29  ? 9.637  7.001   -36.447 1.00 30.91  ?  86  ARG B O   1 
ATOM   2330 C CB  . ARG B 1 29  ? 11.183 8.378   -33.915 1.00 29.15  ?  86  ARG B CB  1 
ATOM   2331 C CG  . ARG B 1 29  ? 10.697 9.564   -34.769 1.00 32.58  ?  86  ARG B CG  1 
ATOM   2332 C CD  . ARG B 1 29  ? 9.261  9.959   -34.406 1.00 36.94  ?  86  ARG B CD  1 
ATOM   2333 N NE  . ARG B 1 29  ? 8.783  11.097  -35.183 1.00 38.95  ?  86  ARG B NE  1 
ATOM   2334 C CZ  . ARG B 1 29  ? 7.522  11.515  -35.216 1.00 49.26  ?  86  ARG B CZ  1 
ATOM   2335 N NH1 . ARG B 1 29  ? 6.567  10.892  -34.546 1.00 44.89  ?  86  ARG B NH1 1 
ATOM   2336 N NH2 . ARG B 1 29  ? 7.210  12.583  -35.943 1.00 44.34  ?  86  ARG B NH2 1 
ATOM   2337 N N   . ALA B 1 30  ? 11.618 6.008   -36.011 1.00 27.46  ?  87  ALA B N   1 
ATOM   2338 C CA  . ALA B 1 30  ? 11.788 5.598   -37.401 1.00 26.42  ?  87  ALA B CA  1 
ATOM   2339 C C   . ALA B 1 30  ? 10.628 4.721   -37.852 1.00 27.55  ?  87  ALA B C   1 
ATOM   2340 O O   . ALA B 1 30  ? 10.072 4.922   -38.942 1.00 32.15  ?  87  ALA B O   1 
ATOM   2341 C CB  . ALA B 1 30  ? 13.118 4.871   -37.583 1.00 24.33  ?  87  ALA B CB  1 
ATOM   2342 N N   . SER B 1 31  ? 10.223 3.768   -37.005 1.00 28.30  ?  88  SER B N   1 
ATOM   2343 C CA  . SER B 1 31  ? 9.100  2.895   -37.340 1.00 31.05  ?  88  SER B CA  1 
ATOM   2344 C C   . SER B 1 31  ? 7.815  3.689   -37.531 1.00 33.12  ?  88  SER B C   1 
ATOM   2345 O O   . SER B 1 31  ? 7.007  3.372   -38.411 1.00 38.67  ?  88  SER B O   1 
ATOM   2346 C CB  . SER B 1 31  ? 8.904  1.849   -36.249 1.00 30.34  ?  88  SER B CB  1 
ATOM   2347 O OG  . SER B 1 31  ? 9.965  0.919   -36.246 1.00 33.32  ?  88  SER B OG  1 
ATOM   2348 N N   . GLN B 1 32  ? 7.599  4.716   -36.704 1.00 35.67  ?  89  GLN B N   1 
ATOM   2349 C CA  . GLN B 1 32  ? 6.411  5.548   -36.859 1.00 34.43  ?  89  GLN B CA  1 
ATOM   2350 C C   . GLN B 1 32  ? 6.447  6.343   -38.154 1.00 39.26  ?  89  GLN B C   1 
ATOM   2351 O O   . GLN B 1 32  ? 5.390  6.720   -38.681 1.00 40.23  ?  89  GLN B O   1 
ATOM   2352 C CB  . GLN B 1 32  ? 6.266  6.500   -35.675 1.00 41.43  ?  89  GLN B CB  1 
ATOM   2353 C CG  . GLN B 1 32  ? 5.828  5.838   -34.394 1.00 46.33  ?  89  GLN B CG  1 
ATOM   2354 C CD  . GLN B 1 32  ? 6.028  6.735   -33.196 1.00 62.89  ?  89  GLN B CD  1 
ATOM   2355 O OE1 . GLN B 1 32  ? 6.836  7.667   -33.228 1.00 61.18  ?  89  GLN B OE1 1 
ATOM   2356 N NE2 . GLN B 1 32  ? 5.267  6.484   -32.140 1.00 57.55  ?  89  GLN B NE2 1 
ATOM   2357 N N   . MET B 1 33  ? 7.637  6.628   -38.664 1.00 37.45  ?  90  MET B N   1 
ATOM   2358 C CA  . MET B 1 33  ? 7.802  7.371   -39.902 1.00 39.59  ?  90  MET B CA  1 
ATOM   2359 C C   . MET B 1 33  ? 7.965  6.466   -41.119 1.00 41.47  ?  90  MET B C   1 
ATOM   2360 O O   . MET B 1 33  ? 8.197  6.972   -42.225 1.00 41.06  ?  90  MET B O   1 
ATOM   2361 C CB  . MET B 1 33  ? 9.006  8.315   -39.784 1.00 48.24  ?  90  MET B CB  1 
ATOM   2362 C CG  . MET B 1 33  ? 8.875  9.421   -38.725 1.00 37.48  ?  90  MET B CG  1 
ATOM   2363 S SD  . MET B 1 33  ? 7.436  10.495  -38.919 1.00 49.98  ?  90  MET B SD  1 
ATOM   2364 C CE  . MET B 1 33  ? 6.248  9.737   -37.806 1.00 58.63  ?  90  MET B CE  1 
ATOM   2365 N N   . GLY B 1 34  ? 7.850  5.150   -40.947 1.00 40.07  ?  91  GLY B N   1 
ATOM   2366 C CA  . GLY B 1 34  ? 7.952  4.234   -42.067 1.00 35.62  ?  91  GLY B CA  1 
ATOM   2367 C C   . GLY B 1 34  ? 9.356  3.846   -42.465 1.00 35.26  ?  91  GLY B C   1 
ATOM   2368 O O   . GLY B 1 34  ? 9.567  3.416   -43.602 1.00 40.19  ?  91  GLY B O   1 
ATOM   2369 N N   . PHE B 1 35  ? 10.323 3.967   -41.558 1.00 30.43  ?  92  PHE B N   1 
ATOM   2370 C CA  . PHE B 1 35  ? 11.723 3.680   -41.840 1.00 32.17  ?  92  PHE B CA  1 
ATOM   2371 C C   . PHE B 1 35  ? 12.196 2.488   -41.020 1.00 29.96  ?  92  PHE B C   1 
ATOM   2372 O O   . PHE B 1 35  ? 11.860 2.368   -39.839 1.00 32.87  ?  92  PHE B O   1 
ATOM   2373 C CB  . PHE B 1 35  ? 12.595 4.896   -41.516 1.00 32.42  ?  92  PHE B CB  1 
ATOM   2374 C CG  . PHE B 1 35  ? 12.569 5.946   -42.574 1.00 34.00  ?  92  PHE B CG  1 
ATOM   2375 C CD1 . PHE B 1 35  ? 11.642 6.967   -42.521 1.00 34.04  ?  92  PHE B CD1 1 
ATOM   2376 C CD2 . PHE B 1 35  ? 13.489 5.931   -43.600 1.00 33.36  ?  92  PHE B CD2 1 
ATOM   2377 C CE1 . PHE B 1 35  ? 11.607 7.936   -43.498 1.00 42.40  ?  92  PHE B CE1 1 
ATOM   2378 C CE2 . PHE B 1 35  ? 13.461 6.901   -44.584 1.00 38.08  ?  92  PHE B CE2 1 
ATOM   2379 C CZ  . PHE B 1 35  ? 12.522 7.904   -44.526 1.00 35.75  ?  92  PHE B CZ  1 
ATOM   2380 N N   . ASN B 1 36  ? 12.959 1.602   -41.659 1.00 27.06  ?  93  ASN B N   1 
ATOM   2381 C CA  . ASN B 1 36  ? 13.759 0.603   -40.959 1.00 24.69  ?  93  ASN B CA  1 
ATOM   2382 C C   . ASN B 1 36  ? 15.054 1.247   -40.480 1.00 23.77  ?  93  ASN B C   1 
ATOM   2383 O O   . ASN B 1 36  ? 15.514 2.239   -41.054 1.00 24.25  ?  93  ASN B O   1 
ATOM   2384 C CB  . ASN B 1 36  ? 14.065 -0.585  -41.879 1.00 27.96  ?  93  ASN B CB  1 
ATOM   2385 C CG  . ASN B 1 36  ? 12.843 -1.458  -42.137 1.00 43.78  ?  93  ASN B CG  1 
ATOM   2386 O OD1 . ASN B 1 36  ? 12.049 -1.716  -41.232 1.00 56.22  ?  93  ASN B OD1 1 
ATOM   2387 N ND2 . ASN B 1 36  ? 12.699 -1.932  -43.371 1.00 51.03  ?  93  ASN B ND2 1 
ATOM   2388 N N   . VAL B 1 37  ? 15.638 0.696   -39.407 1.00 19.01  ?  94  VAL B N   1 
ATOM   2389 C CA  . VAL B 1 37  ? 16.930 1.150   -38.902 1.00 21.48  ?  94  VAL B CA  1 
ATOM   2390 C C   . VAL B 1 37  ? 17.900 -0.019  -38.937 1.00 19.77  ?  94  VAL B C   1 
ATOM   2391 O O   . VAL B 1 37  ? 17.582 -1.115  -38.456 1.00 19.19  ?  94  VAL B O   1 
ATOM   2392 C CB  . VAL B 1 37  ? 16.839 1.715   -37.471 1.00 17.33  ?  94  VAL B CB  1 
ATOM   2393 C CG1 . VAL B 1 37  ? 18.183 2.204   -36.998 1.00 18.51  ?  94  VAL B CG1 1 
ATOM   2394 C CG2 . VAL B 1 37  ? 15.866 2.864   -37.436 1.00 18.52  ?  94  VAL B CG2 1 
ATOM   2395 N N   . VAL B 1 38  ? 19.076 0.217   -39.506 1.00 17.26  ?  95  VAL B N   1 
ATOM   2396 C CA  . VAL B 1 38  ? 20.167 -0.747  -39.543 1.00 17.58  ?  95  VAL B CA  1 
ATOM   2397 C C   . VAL B 1 38  ? 21.290 -0.184  -38.687 1.00 22.23  ?  95  VAL B C   1 
ATOM   2398 O O   . VAL B 1 38  ? 21.736 0.947   -38.905 1.00 20.48  ?  95  VAL B O   1 
ATOM   2399 C CB  . VAL B 1 38  ? 20.608 -1.019  -40.987 1.00 21.26  ?  95  VAL B CB  1 
ATOM   2400 C CG1 . VAL B 1 38  ? 21.929 -1.713  -41.014 1.00 30.25  ?  95  VAL B CG1 1 
ATOM   2401 C CG2 . VAL B 1 38  ? 19.558 -1.900  -41.677 1.00 23.30  ?  95  VAL B CG2 1 
ATOM   2402 N N   . ILE B 1 39  ? 21.737 -0.960  -37.696 1.00 16.65  ?  96  ILE B N   1 
ATOM   2403 C CA  . ILE B 1 39  ? 22.618 -0.472  -36.644 1.00 17.06  ?  96  ILE B CA  1 
ATOM   2404 C C   . ILE B 1 39  ? 23.997 -1.096  -36.810 1.00 17.10  ?  96  ILE B C   1 
ATOM   2405 O O   . ILE B 1 39  ? 24.123 -2.299  -37.032 1.00 17.97  ?  96  ILE B O   1 
ATOM   2406 C CB  . ILE B 1 39  ? 22.039 -0.791  -35.248 1.00 16.59  ?  96  ILE B CB  1 
ATOM   2407 C CG1 . ILE B 1 39  ? 20.654 -0.168  -35.078 1.00 16.91  ?  96  ILE B CG1 1 
ATOM   2408 C CG2 . ILE B 1 39  ? 22.987 -0.359  -34.138 1.00 19.41  ?  96  ILE B CG2 1 
ATOM   2409 C CD1 . ILE B 1 39  ? 19.717 -1.084  -34.352 1.00 19.88  ?  96  ILE B CD1 1 
ATOM   2410 N N   . SER B 1 40  ? 25.035 -0.275  -36.690 1.00 18.61  ?  97  SER B N   1 
ATOM   2411 C CA  . SER B 1 40  ? 26.408 -0.762  -36.681 1.00 18.83  ?  97  SER B CA  1 
ATOM   2412 C C   . SER B 1 40  ? 27.082 -0.280  -35.404 1.00 23.62  ?  97  SER B C   1 
ATOM   2413 O O   . SER B 1 40  ? 27.083 0.922   -35.121 1.00 24.59  ?  97  SER B O   1 
ATOM   2414 C CB  . SER B 1 40  ? 27.173 -0.259  -37.898 1.00 22.28  ?  97  SER B CB  1 
ATOM   2415 O OG  . SER B 1 40  ? 28.509 -0.713  -37.891 1.00 33.47  ?  97  SER B OG  1 
ATOM   2416 N N   A MET B 1 41  ? 27.661 -1.199  -34.642 0.95 23.01  ?  98  MET B N   1 
ATOM   2417 N N   B MET B 1 41  ? 27.616 -1.226  -34.632 0.05 23.28  ?  98  MET B N   1 
ATOM   2418 C CA  A MET B 1 41  ? 28.370 -0.846  -33.418 0.95 26.62  ?  98  MET B CA  1 
ATOM   2419 C CA  B MET B 1 41  ? 28.432 -0.926  -33.464 0.05 26.87  ?  98  MET B CA  1 
ATOM   2420 C C   A MET B 1 41  ? 29.859 -0.721  -33.726 0.95 29.82  ?  98  MET B C   1 
ATOM   2421 C C   B MET B 1 41  ? 29.864 -0.643  -33.890 0.05 30.05  ?  98  MET B C   1 
ATOM   2422 O O   A MET B 1 41  ? 30.440 -1.597  -34.369 0.95 29.81  ?  98  MET B O   1 
ATOM   2423 O O   B MET B 1 41  ? 30.429 -1.361  -34.721 0.05 30.14  ?  98  MET B O   1 
ATOM   2424 C CB  A MET B 1 41  ? 28.072 -1.872  -32.314 0.95 26.52  ?  98  MET B CB  1 
ATOM   2425 C CB  B MET B 1 41  ? 28.428 -2.104  -32.489 0.05 27.11  ?  98  MET B CB  1 
ATOM   2426 C CG  A MET B 1 41  ? 28.872 -1.710  -31.005 0.95 34.57  ?  98  MET B CG  1 
ATOM   2427 C CG  B MET B 1 41  ? 29.222 -1.859  -31.214 0.05 32.90  ?  98  MET B CG  1 
ATOM   2428 S SD  A MET B 1 41  ? 28.285 -2.752  -29.632 0.95 28.76  ?  98  MET B SD  1 
ATOM   2429 S SD  B MET B 1 41  ? 29.251 -3.288  -30.113 0.05 28.00  ?  98  MET B SD  1 
ATOM   2430 C CE  A MET B 1 41  ? 29.669 -2.619  -28.503 0.95 45.74  ?  98  MET B CE  1 
ATOM   2431 C CE  B MET B 1 41  ? 27.623 -3.202  -29.388 0.05 26.46  ?  98  MET B CE  1 
ATOM   2432 N N   . VAL B 1 42  ? 30.459 0.404   -33.317 1.00 35.37  ?  99  VAL B N   1 
ATOM   2433 C CA  . VAL B 1 42  ? 31.838 0.745   -33.647 1.00 43.87  ?  99  VAL B CA  1 
ATOM   2434 C C   . VAL B 1 42  ? 32.625 1.065   -32.381 1.00 56.02  ?  99  VAL B C   1 
ATOM   2435 O O   . VAL B 1 42  ? 32.068 1.403   -31.334 1.00 48.16  ?  99  VAL B O   1 
ATOM   2436 C CB  . VAL B 1 42  ? 31.944 1.933   -34.641 1.00 40.76  ?  99  VAL B CB  1 
ATOM   2437 C CG1 . VAL B 1 42  ? 30.966 1.798   -35.802 1.00 49.77  ?  99  VAL B CG1 1 
ATOM   2438 C CG2 . VAL B 1 42  ? 31.723 3.233   -33.920 1.00 45.23  ?  99  VAL B CG2 1 
ATOM   2439 N N   . GLU B 1 43  ? 33.946 0.941   -32.492 1.00 62.39  ?  100 GLU B N   1 
ATOM   2440 C CA  . GLU B 1 43  ? 34.862 1.444   -31.482 1.00 77.98  ?  100 GLU B CA  1 
ATOM   2441 C C   . GLU B 1 43  ? 35.407 2.800   -31.930 1.00 81.07  ?  100 GLU B C   1 
ATOM   2442 O O   . GLU B 1 43  ? 35.137 3.274   -33.038 1.00 68.58  ?  100 GLU B O   1 
ATOM   2443 C CB  . GLU B 1 43  ? 35.987 0.440   -31.213 1.00 76.18  ?  100 GLU B CB  1 
ATOM   2444 C CG  . GLU B 1 43  ? 35.530 -1.011  -31.078 1.00 62.07  ?  100 GLU B CG  1 
ATOM   2445 C CD  . GLU B 1 43  ? 34.331 -1.179  -30.155 1.00 101.35 ?  100 GLU B CD  1 
ATOM   2446 O OE1 . GLU B 1 43  ? 34.284 -0.516  -29.094 1.00 110.13 ?  100 GLU B OE1 1 
ATOM   2447 O OE2 . GLU B 1 43  ? 33.430 -1.977  -30.492 1.00 101.67 -1 100 GLU B OE2 1 
ATOM   2448 N N   . GLN B 1 44  ? 36.183 3.431   -31.054 1.00 75.38  ?  101 GLN B N   1 
ATOM   2449 C CA  . GLN B 1 44  ? 36.627 4.795   -31.297 1.00 73.83  ?  101 GLN B CA  1 
ATOM   2450 C C   . GLN B 1 44  ? 37.548 4.878   -32.509 1.00 69.23  ?  101 GLN B C   1 
ATOM   2451 O O   . GLN B 1 44  ? 38.320 3.959   -32.799 1.00 77.56  ?  101 GLN B O   1 
ATOM   2452 C CB  . GLN B 1 44  ? 37.344 5.349   -30.066 1.00 78.54  ?  101 GLN B CB  1 
ATOM   2453 C CG  . GLN B 1 44  ? 36.596 5.147   -28.755 1.00 80.58  ?  101 GLN B CG  1 
ATOM   2454 C CD  . GLN B 1 44  ? 35.558 6.229   -28.500 1.00 87.87  ?  101 GLN B CD  1 
ATOM   2455 O OE1 . GLN B 1 44  ? 35.729 7.068   -27.615 1.00 82.98  ?  101 GLN B OE1 1 
ATOM   2456 N NE2 . GLN B 1 44  ? 34.468 6.204   -29.263 1.00 80.09  ?  101 GLN B NE2 1 
ATOM   2457 N N   . GLY B 1 45  ? 37.452 5.995   -33.221 1.00 50.78  ?  102 GLY B N   1 
ATOM   2458 C CA  . GLY B 1 45  ? 38.375 6.301   -34.301 1.00 61.09  ?  102 GLY B CA  1 
ATOM   2459 C C   . GLY B 1 45  ? 37.679 6.654   -35.598 1.00 55.91  ?  102 GLY B C   1 
ATOM   2460 O O   . GLY B 1 45  ? 36.592 6.158   -35.903 1.00 65.91  ?  102 GLY B O   1 
ATOM   2461 N N   . VAL B 1 46  ? 38.318 7.533   -36.376 1.00 68.02  ?  103 VAL B N   1 
ATOM   2462 C CA  . VAL B 1 46  ? 37.789 7.899   -37.689 1.00 61.58  ?  103 VAL B CA  1 
ATOM   2463 C C   . VAL B 1 46  ? 37.677 6.674   -38.583 1.00 60.18  ?  103 VAL B C   1 
ATOM   2464 O O   . VAL B 1 46  ? 36.681 6.497   -39.294 1.00 58.14  ?  103 VAL B O   1 
ATOM   2465 C CB  . VAL B 1 46  ? 38.671 8.976   -38.345 1.00 72.89  ?  103 VAL B CB  1 
ATOM   2466 C CG1 . VAL B 1 46  ? 38.069 9.414   -39.672 1.00 66.71  ?  103 VAL B CG1 1 
ATOM   2467 C CG2 . VAL B 1 46  ? 38.842 10.146  -37.423 1.00 74.05  ?  103 VAL B CG2 1 
ATOM   2468 N N   . GLU B 1 47  ? 38.703 5.816   -38.575 1.00 66.49  ?  104 GLU B N   1 
ATOM   2469 C CA  . GLU B 1 47  ? 38.700 4.658   -39.463 1.00 78.37  ?  104 GLU B CA  1 
ATOM   2470 C C   . GLU B 1 47  ? 37.562 3.705   -39.124 1.00 71.60  ?  104 GLU B C   1 
ATOM   2471 O O   . GLU B 1 47  ? 36.892 3.182   -40.023 1.00 75.49  ?  104 GLU B O   1 
ATOM   2472 C CB  . GLU B 1 47  ? 40.043 3.930   -39.393 1.00 67.85  ?  104 GLU B CB  1 
ATOM   2473 C CG  . GLU B 1 47  ? 40.463 3.280   -40.703 1.00 74.03  ?  104 GLU B CG  1 
ATOM   2474 C CD  . GLU B 1 47  ? 40.707 4.294   -41.811 1.00 94.46  ?  104 GLU B CD  1 
ATOM   2475 O OE1 . GLU B 1 47  ? 41.167 5.419   -41.509 1.00 85.61  ?  104 GLU B OE1 1 
ATOM   2476 O OE2 . GLU B 1 47  ? 40.443 3.965   -42.987 1.00 108.13 -1 104 GLU B OE2 1 
ATOM   2477 N N   . ALA B 1 48  ? 37.325 3.467   -37.832 1.00 56.00  ?  105 ALA B N   1 
ATOM   2478 C CA  . ALA B 1 48  ? 36.219 2.600   -37.447 1.00 54.17  ?  105 ALA B CA  1 
ATOM   2479 C C   . ALA B 1 48  ? 34.876 3.195   -37.849 1.00 60.79  ?  105 ALA B C   1 
ATOM   2480 O O   . ALA B 1 48  ? 33.956 2.456   -38.212 1.00 46.79  ?  105 ALA B O   1 
ATOM   2481 C CB  . ALA B 1 48  ? 36.258 2.331   -35.944 1.00 60.84  ?  105 ALA B CB  1 
ATOM   2482 N N   . CYS B 1 49  ? 34.746 4.524   -37.805 1.00 61.66  ?  106 CYS B N   1 
ATOM   2483 C CA  . CYS B 1 49  ? 33.502 5.175   -38.208 1.00 46.09  ?  106 CYS B CA  1 
ATOM   2484 C C   . CYS B 1 49  ? 33.353 5.215   -39.723 1.00 57.02  ?  106 CYS B C   1 
ATOM   2485 O O   . CYS B 1 49  ? 32.254 4.998   -40.244 1.00 54.37  ?  106 CYS B O   1 
ATOM   2486 C CB  . CYS B 1 49  ? 33.448 6.595   -37.654 1.00 48.04  ?  106 CYS B CB  1 
ATOM   2487 S SG  . CYS B 1 49  ? 33.112 6.702   -35.895 1.00 54.87  ?  106 CYS B SG  1 
ATOM   2488 N N   . LYS B 1 50  ? 34.443 5.513   -40.438 1.00 55.17  ?  107 LYS B N   1 
ATOM   2489 C CA  . LYS B 1 50  ? 34.390 5.575   -41.897 1.00 60.44  ?  107 LYS B CA  1 
ATOM   2490 C C   . LYS B 1 50  ? 34.061 4.215   -42.498 1.00 62.30  ?  107 LYS B C   1 
ATOM   2491 O O   . LYS B 1 50  ? 33.314 4.126   -43.480 1.00 60.09  ?  107 LYS B O   1 
ATOM   2492 C CB  . LYS B 1 50  ? 35.717 6.096   -42.461 1.00 59.61  ?  107 LYS B CB  1 
ATOM   2493 C CG  . LYS B 1 50  ? 35.923 7.596   -42.283 1.00 58.01  ?  107 LYS B CG  1 
ATOM   2494 C CD  . LYS B 1 50  ? 37.113 8.115   -43.084 1.00 70.54  ?  107 LYS B CD  1 
ATOM   2495 C CE  . LYS B 1 50  ? 38.382 7.337   -42.790 1.00 77.70  ?  107 LYS B CE  1 
ATOM   2496 N NZ  . LYS B 1 50  ? 39.595 8.101   -43.188 1.00 68.17  ?  107 LYS B NZ  1 
ATOM   2497 N N   . ALA B 1 51  ? 34.617 3.143   -41.929 1.00 59.38  ?  108 ALA B N   1 
ATOM   2498 C CA  . ALA B 1 51  ? 34.294 1.806   -42.414 1.00 63.25  ?  108 ALA B CA  1 
ATOM   2499 C C   . ALA B 1 51  ? 32.815 1.495   -42.216 1.00 59.89  ?  108 ALA B C   1 
ATOM   2500 O O   . ALA B 1 51  ? 32.181 0.878   -43.081 1.00 56.64  ?  108 ALA B O   1 
ATOM   2501 C CB  . ALA B 1 51  ? 35.166 0.766   -41.711 1.00 63.63  ?  108 ALA B CB  1 
ATOM   2502 N N   . ALA B 1 52  ? 32.245 1.929   -41.088 1.00 51.94  ?  109 ALA B N   1 
ATOM   2503 C CA  . ALA B 1 52  ? 30.825 1.705   -40.844 1.00 46.25  ?  109 ALA B CA  1 
ATOM   2504 C C   . ALA B 1 52  ? 29.961 2.464   -41.845 1.00 50.87  ?  109 ALA B C   1 
ATOM   2505 O O   . ALA B 1 52  ? 28.936 1.947   -42.306 1.00 62.59  ?  109 ALA B O   1 
ATOM   2506 C CB  . ALA B 1 52  ? 30.473 2.104   -39.413 1.00 46.11  ?  109 ALA B CB  1 
ATOM   2507 N N   . VAL B 1 53  ? 30.366 3.683   -42.203 1.00 52.61  ?  110 VAL B N   1 
ATOM   2508 C CA  . VAL B 1 53  ? 29.571 4.499   -43.116 1.00 43.43  ?  110 VAL B CA  1 
ATOM   2509 C C   . VAL B 1 53  ? 29.556 3.889   -44.517 1.00 49.55  ?  110 VAL B C   1 
ATOM   2510 O O   . VAL B 1 53  ? 28.492 3.719   -45.125 1.00 53.12  ?  110 VAL B O   1 
ATOM   2511 C CB  . VAL B 1 53  ? 30.101 5.945   -43.135 1.00 48.09  ?  110 VAL B CB  1 
ATOM   2512 C CG1 . VAL B 1 53  ? 29.629 6.673   -44.385 1.00 52.73  ?  110 VAL B CG1 1 
ATOM   2513 C CG2 . VAL B 1 53  ? 29.664 6.684   -41.881 1.00 45.29  ?  110 VAL B CG2 1 
ATOM   2514 N N   . ASN B 1 54  ? 30.733 3.562   -45.056 1.00 50.43  ?  111 ASN B N   1 
ATOM   2515 C CA  . ASN B 1 54  ? 30.805 3.101   -46.442 1.00 68.55  ?  111 ASN B CA  1 
ATOM   2516 C C   . ASN B 1 54  ? 29.979 1.838   -46.662 1.00 61.48  ?  111 ASN B C   1 
ATOM   2517 O O   . ASN B 1 54  ? 29.330 1.689   -47.704 1.00 63.91  ?  111 ASN B O   1 
ATOM   2518 C CB  . ASN B 1 54  ? 32.259 2.867   -46.860 1.00 68.17  ?  111 ASN B CB  1 
ATOM   2519 C CG  . ASN B 1 54  ? 33.126 4.102   -46.695 1.00 64.56  ?  111 ASN B CG  1 
ATOM   2520 O OD1 . ASN B 1 54  ? 34.168 4.057   -46.046 1.00 76.49  ?  111 ASN B OD1 1 
ATOM   2521 N ND2 . ASN B 1 54  ? 32.705 5.210   -47.296 1.00 60.53  ?  111 ASN B ND2 1 
ATOM   2522 N N   . SER B 1 55  ? 29.987 0.920   -45.695 1.00 44.77  ?  112 SER B N   1 
ATOM   2523 C CA  . SER B 1 55  ? 29.211 -0.307  -45.848 1.00 51.55  ?  112 SER B CA  1 
ATOM   2524 C C   . SER B 1 55  ? 27.721 -0.003  -45.958 1.00 50.88  ?  112 SER B C   1 
ATOM   2525 O O   . SER B 1 55  ? 27.025 -0.547  -46.823 1.00 44.79  ?  112 SER B O   1 
ATOM   2526 C CB  . SER B 1 55  ? 29.489 -1.247  -44.678 1.00 52.65  ?  112 SER B CB  1 
ATOM   2527 O OG  . SER B 1 55  ? 29.176 -0.608  -43.457 1.00 53.19  ?  112 SER B OG  1 
ATOM   2528 N N   . LEU B 1 56  ? 27.214 0.879   -45.095 1.00 48.31  ?  113 LEU B N   1 
ATOM   2529 C CA  . LEU B 1 56  ? 25.806 1.240   -45.175 1.00 41.81  ?  113 LEU B CA  1 
ATOM   2530 C C   . LEU B 1 56  ? 25.488 1.937   -46.493 1.00 52.08  ?  113 LEU B C   1 
ATOM   2531 O O   . LEU B 1 56  ? 24.460 1.657   -47.122 1.00 54.23  ?  113 LEU B O   1 
ATOM   2532 C CB  . LEU B 1 56  ? 25.425 2.118   -43.984 1.00 45.05  ?  113 LEU B CB  1 
ATOM   2533 C CG  . LEU B 1 56  ? 25.699 1.432   -42.645 1.00 42.19  ?  113 LEU B CG  1 
ATOM   2534 C CD1 . LEU B 1 56  ? 25.766 2.420   -41.501 1.00 37.49  ?  113 LEU B CD1 1 
ATOM   2535 C CD2 . LEU B 1 56  ? 24.640 0.384   -42.393 1.00 43.39  ?  113 LEU B CD2 1 
ATOM   2536 N N   . LEU B 1 57  ? 26.366 2.836   -46.936 1.00 44.53  ?  114 LEU B N   1 
ATOM   2537 C CA  . LEU B 1 57  ? 26.132 3.522   -48.200 1.00 62.29  ?  114 LEU B CA  1 
ATOM   2538 C C   . LEU B 1 57  ? 26.152 2.549   -49.373 1.00 56.81  ?  114 LEU B C   1 
ATOM   2539 O O   . LEU B 1 57  ? 25.449 2.759   -50.368 1.00 50.58  ?  114 LEU B O   1 
ATOM   2540 C CB  . LEU B 1 57  ? 27.168 4.632   -48.391 1.00 57.04  ?  114 LEU B CB  1 
ATOM   2541 C CG  . LEU B 1 57  ? 27.196 5.769   -47.358 1.00 52.32  ?  114 LEU B CG  1 
ATOM   2542 C CD1 . LEU B 1 57  ? 27.608 7.073   -48.013 1.00 70.35  ?  114 LEU B CD1 1 
ATOM   2543 C CD2 . LEU B 1 57  ? 25.851 5.934   -46.671 1.00 49.77  ?  114 LEU B CD2 1 
ATOM   2544 N N   . ALA B 1 58  ? 26.936 1.473   -49.266 1.00 45.37  ?  115 ALA B N   1 
ATOM   2545 C CA  . ALA B 1 58  ? 26.954 0.457   -50.316 1.00 46.15  ?  115 ALA B CA  1 
ATOM   2546 C C   . ALA B 1 58  ? 25.613 -0.255  -50.441 1.00 47.77  ?  115 ALA B C   1 
ATOM   2547 O O   . ALA B 1 58  ? 25.281 -0.764  -51.518 1.00 50.34  ?  115 ALA B O   1 
ATOM   2548 C CB  . ALA B 1 58  ? 28.060 -0.562  -50.046 1.00 48.04  ?  115 ALA B CB  1 
ATOM   2549 N N   . GLN B 1 59  ? 24.831 -0.308  -49.362 1.00 40.93  ?  116 GLN B N   1 
ATOM   2550 C CA  . GLN B 1 59  ? 23.534 -0.966  -49.387 1.00 42.43  ?  116 GLN B CA  1 
ATOM   2551 C C   . GLN B 1 59  ? 22.374 0.030   -49.439 1.00 48.98  ?  116 GLN B C   1 
ATOM   2552 O O   . GLN B 1 59  ? 21.251 -0.312  -49.051 1.00 50.66  ?  116 GLN B O   1 
ATOM   2553 C CB  . GLN B 1 59  ? 23.402 -1.895  -48.183 1.00 39.23  ?  116 GLN B CB  1 
ATOM   2554 C CG  . GLN B 1 59  ? 24.382 -3.072  -48.195 1.00 39.03  ?  116 GLN B CG  1 
ATOM   2555 C CD  . GLN B 1 59  ? 24.448 -3.815  -49.522 1.00 44.12  ?  116 GLN B CD  1 
ATOM   2556 O OE1 . GLN B 1 59  ? 23.462 -3.917  -50.256 1.00 44.02  ?  116 GLN B OE1 1 
ATOM   2557 N NE2 . GLN B 1 59  ? 25.622 -4.345  -49.828 1.00 44.76  ?  116 GLN B NE2 1 
ATOM   2558 N N   . ARG B 1 60  ? 22.637 1.259   -49.888 1.00 49.10  ?  117 ARG B N   1 
ATOM   2559 C CA  . ARG B 1 60  ? 21.602 2.220   -50.280 1.00 41.39  ?  117 ARG B CA  1 
ATOM   2560 C C   . ARG B 1 60  ? 20.764 2.695   -49.090 1.00 41.55  ?  117 ARG B C   1 
ATOM   2561 O O   . ARG B 1 60  ? 19.541 2.780   -49.191 1.00 68.48  ?  117 ARG B O   1 
ATOM   2562 C CB  . ARG B 1 60  ? 20.682 1.644   -51.366 1.00 58.82  ?  117 ARG B CB  1 
ATOM   2563 C CG  . ARG B 1 60  ? 21.372 1.252   -52.675 1.00 49.57  ?  117 ARG B CG  1 
ATOM   2564 C CD  . ARG B 1 60  ? 20.704 0.014   -53.295 1.00 60.25  ?  117 ARG B CD  1 
ATOM   2565 N NE  . ARG B 1 60  ? 20.750 -1.137  -52.398 1.00 59.08  ?  117 ARG B NE  1 
ATOM   2566 C CZ  . ARG B 1 60  ? 20.093 -2.276  -52.587 1.00 55.79  ?  117 ARG B CZ  1 
ATOM   2567 N NH1 . ARG B 1 60  ? 19.376 -2.491  -53.682 1.00 50.14  ?  117 ARG B NH1 1 
ATOM   2568 N NH2 . ARG B 1 60  ? 20.161 -3.227  -51.658 1.00 50.58  ?  117 ARG B NH2 1 
ATOM   2569 N N   . VAL B 1 61  ? 21.404 3.008   -47.958 1.00 45.81  ?  118 VAL B N   1 
ATOM   2570 C CA  . VAL B 1 61  ? 20.662 3.626   -46.858 1.00 38.13  ?  118 VAL B CA  1 
ATOM   2571 C C   . VAL B 1 61  ? 20.451 5.099   -47.182 1.00 38.42  ?  118 VAL B C   1 
ATOM   2572 O O   . VAL B 1 61  ? 21.287 5.746   -47.822 1.00 40.72  ?  118 VAL B O   1 
ATOM   2573 C CB  . VAL B 1 61  ? 21.364 3.444   -45.493 1.00 47.26  ?  118 VAL B CB  1 
ATOM   2574 C CG1 . VAL B 1 61  ? 21.761 1.987   -45.275 1.00 49.75  ?  118 VAL B CG1 1 
ATOM   2575 C CG2 . VAL B 1 61  ? 22.562 4.371   -45.355 1.00 43.84  ?  118 VAL B CG2 1 
ATOM   2576 N N   . ASP B 1 62  ? 19.317 5.639   -46.735 1.00 35.47  ?  119 ASP B N   1 
ATOM   2577 C CA  . ASP B 1 62  ? 18.934 6.994   -47.134 1.00 32.55  ?  119 ASP B CA  1 
ATOM   2578 C C   . ASP B 1 62  ? 19.644 8.074   -46.327 1.00 35.78  ?  119 ASP B C   1 
ATOM   2579 O O   . ASP B 1 62  ? 19.803 9.201   -46.811 1.00 42.47  ?  119 ASP B O   1 
ATOM   2580 C CB  . ASP B 1 62  ? 17.421 7.168   -47.000 1.00 31.58  ?  119 ASP B CB  1 
ATOM   2581 C CG  . ASP B 1 62  ? 16.639 6.186   -47.853 1.00 50.50  ?  119 ASP B CG  1 
ATOM   2582 O OD1 . ASP B 1 62  ? 17.115 5.838   -48.958 1.00 56.81  -1 119 ASP B OD1 1 
ATOM   2583 O OD2 . ASP B 1 62  ? 15.544 5.767   -47.420 1.00 55.97  ?  119 ASP B OD2 1 
ATOM   2584 N N   . GLY B 1 63  ? 20.063 7.764   -45.110 1.00 32.60  ?  120 GLY B N   1 
ATOM   2585 C CA  . GLY B 1 63  ? 20.658 8.757   -44.242 1.00 32.30  ?  120 GLY B CA  1 
ATOM   2586 C C   . GLY B 1 63  ? 21.246 8.088   -43.024 1.00 32.19  ?  120 GLY B C   1 
ATOM   2587 O O   . GLY B 1 63  ? 20.913 6.942   -42.702 1.00 31.19  ?  120 GLY B O   1 
ATOM   2588 N N   . LEU B 1 64  ? 22.134 8.818   -42.355 1.00 34.23  ?  121 LEU B N   1 
ATOM   2589 C CA  . LEU B 1 64  ? 22.945 8.268   -41.281 1.00 30.00  ?  121 LEU B CA  1 
ATOM   2590 C C   . LEU B 1 64  ? 22.802 9.092   -40.014 1.00 33.20  ?  121 LEU B C   1 
ATOM   2591 O O   . LEU B 1 64  ? 22.623 10.312  -40.055 1.00 33.00  ?  121 LEU B O   1 
ATOM   2592 C CB  . LEU B 1 64  ? 24.429 8.182   -41.679 1.00 32.14  ?  121 LEU B CB  1 
ATOM   2593 C CG  . LEU B 1 64  ? 24.723 7.351   -42.930 1.00 35.82  ?  121 LEU B CG  1 
ATOM   2594 C CD1 . LEU B 1 64  ? 26.005 7.802   -43.604 1.00 50.89  ?  121 LEU B CD1 1 
ATOM   2595 C CD2 . LEU B 1 64  ? 24.802 5.883   -42.549 1.00 33.51  ?  121 LEU B CD2 1 
ATOM   2596 N N   . ILE B 1 65  ? 22.879 8.403   -38.882 1.00 29.87  ?  122 ILE B N   1 
ATOM   2597 C CA  . ILE B 1 65  ? 22.935 9.029   -37.567 1.00 27.86  ?  122 ILE B CA  1 
ATOM   2598 C C   . ILE B 1 65  ? 24.151 8.452   -36.859 1.00 28.49  ?  122 ILE B C   1 
ATOM   2599 O O   . ILE B 1 65  ? 24.287 7.229   -36.776 1.00 27.73  ?  122 ILE B O   1 
ATOM   2600 C CB  . ILE B 1 65  ? 21.650 8.773   -36.754 1.00 27.68  ?  122 ILE B CB  1 
ATOM   2601 C CG1 . ILE B 1 65  ? 20.442 9.424   -37.428 1.00 27.68  ?  122 ILE B CG1 1 
ATOM   2602 C CG2 . ILE B 1 65  ? 21.812 9.275   -35.322 1.00 27.91  ?  122 ILE B CG2 1 
ATOM   2603 C CD1 . ILE B 1 65  ? 19.104 9.075   -36.768 1.00 28.72  ?  122 ILE B CD1 1 
ATOM   2604 N N   . ILE B 1 66  ? 25.049 9.316   -36.391 1.00 30.21  ?  123 ILE B N   1 
ATOM   2605 C CA  . ILE B 1 66  ? 26.318 8.905   -35.787 1.00 32.04  ?  123 ILE B CA  1 
ATOM   2606 C C   . ILE B 1 66  ? 26.285 9.226   -34.299 1.00 31.28  ?  123 ILE B C   1 
ATOM   2607 O O   . ILE B 1 66  ? 26.443 10.393  -33.909 1.00 32.47  ?  123 ILE B O   1 
ATOM   2608 C CB  . ILE B 1 66  ? 27.524 9.592   -36.448 1.00 34.26  ?  123 ILE B CB  1 
ATOM   2609 C CG1 . ILE B 1 66  ? 27.400 9.570   -37.970 1.00 36.41  ?  123 ILE B CG1 1 
ATOM   2610 C CG2 . ILE B 1 66  ? 28.818 8.954   -35.977 1.00 36.26  ?  123 ILE B CG2 1 
ATOM   2611 C CD1 . ILE B 1 66  ? 27.714 8.222   -38.598 1.00 34.73  ?  123 ILE B CD1 1 
ATOM   2612 N N   . ASN B 1 67  ? 26.152 8.203   -33.459 1.00 30.76  ?  124 ASN B N   1 
ATOM   2613 C CA  . ASN B 1 67  ? 26.267 8.387   -32.015 1.00 30.31  ?  124 ASN B CA  1 
ATOM   2614 C C   . ASN B 1 67  ? 27.583 7.783   -31.526 1.00 33.14  ?  124 ASN B C   1 
ATOM   2615 O O   . ASN B 1 67  ? 27.627 6.732   -30.881 1.00 33.37  ?  124 ASN B O   1 
ATOM   2616 C CB  . ASN B 1 67  ? 25.063 7.784   -31.273 1.00 29.45  ?  124 ASN B CB  1 
ATOM   2617 C CG  . ASN B 1 67  ? 25.106 8.096   -29.791 1.00 28.49  ?  124 ASN B CG  1 
ATOM   2618 O OD1 . ASN B 1 67  ? 25.717 9.096   -29.389 1.00 34.98  ?  124 ASN B OD1 1 
ATOM   2619 N ND2 . ASN B 1 67  ? 24.507 7.243   -28.972 1.00 28.18  ?  124 ASN B ND2 1 
ATOM   2620 N N   . VAL B 1 68  ? 28.673 8.474   -31.839 1.00 34.57  ?  125 VAL B N   1 
ATOM   2621 C CA  . VAL B 1 68  ? 30.010 8.104   -31.384 1.00 39.59  ?  125 VAL B CA  1 
ATOM   2622 C C   . VAL B 1 68  ? 30.715 9.371   -30.911 1.00 43.10  ?  125 VAL B C   1 
ATOM   2623 O O   . VAL B 1 68  ? 30.662 10.390  -31.615 1.00 40.04  ?  125 VAL B O   1 
ATOM   2624 C CB  . VAL B 1 68  ? 30.807 7.411   -32.501 1.00 38.79  ?  125 VAL B CB  1 
ATOM   2625 C CG1 . VAL B 1 68  ? 32.189 7.017   -32.003 1.00 45.99  ?  125 VAL B CG1 1 
ATOM   2626 C CG2 . VAL B 1 68  ? 30.048 6.203   -33.035 1.00 36.12  ?  125 VAL B CG2 1 
ATOM   2627 N N   . PRO B 1 69  ? 31.377 9.370   -29.748 1.00 41.20  ?  126 PRO B N   1 
ATOM   2628 C CA  . PRO B 1 69  ? 32.107 10.576  -29.309 1.00 45.52  ?  126 PRO B CA  1 
ATOM   2629 C C   . PRO B 1 69  ? 33.247 10.897  -30.263 1.00 46.20  ?  126 PRO B C   1 
ATOM   2630 O O   . PRO B 1 69  ? 34.106 10.055  -30.537 1.00 53.91  ?  126 PRO B O   1 
ATOM   2631 C CB  . PRO B 1 69  ? 32.631 10.199  -27.916 1.00 49.06  ?  126 PRO B CB  1 
ATOM   2632 C CG  . PRO B 1 69  ? 32.427 8.728   -27.765 1.00 51.10  ?  126 PRO B CG  1 
ATOM   2633 C CD  . PRO B 1 69  ? 31.357 8.311   -28.722 1.00 52.56  ?  126 PRO B CD  1 
ATOM   2634 N N   . LEU B 1 70  ? 33.242 12.126  -30.783 1.00 47.10  ?  127 LEU B N   1 
ATOM   2635 C CA  . LEU B 1 70  ? 34.246 12.566  -31.745 1.00 49.81  ?  127 LEU B CA  1 
ATOM   2636 C C   . LEU B 1 70  ? 34.654 14.007  -31.486 1.00 57.78  ?  127 LEU B C   1 
ATOM   2637 O O   . LEU B 1 70  ? 33.807 14.874  -31.254 1.00 51.07  ?  127 LEU B O   1 
ATOM   2638 C CB  . LEU B 1 70  ? 33.738 12.442  -33.186 1.00 48.32  ?  127 LEU B CB  1 
ATOM   2639 C CG  . LEU B 1 70  ? 33.347 11.039  -33.644 1.00 46.56  ?  127 LEU B CG  1 
ATOM   2640 C CD1 . LEU B 1 70  ? 32.493 11.120  -34.899 1.00 44.62  ?  127 LEU B CD1 1 
ATOM   2641 C CD2 . LEU B 1 70  ? 34.589 10.190  -33.877 1.00 50.34  ?  127 LEU B CD2 1 
ATOM   2642 N N   . GLU B 1 71  ? 35.960 14.260  -31.550 1.00 57.25  ?  128 GLU B N   1 
ATOM   2643 C CA  . GLU B 1 71  ? 36.454 15.627  -31.509 1.00 62.19  ?  128 GLU B CA  1 
ATOM   2644 C C   . GLU B 1 71  ? 36.139 16.332  -32.830 1.00 60.58  ?  128 GLU B C   1 
ATOM   2645 O O   . GLU B 1 71  ? 35.656 15.723  -33.792 1.00 58.39  ?  128 GLU B O   1 
ATOM   2646 C CB  . GLU B 1 71  ? 37.958 15.648  -31.224 1.00 72.87  ?  128 GLU B CB  1 
ATOM   2647 C CG  . GLU B 1 71  ? 38.357 15.416  -29.752 1.00 71.24  ?  128 GLU B CG  1 
ATOM   2648 C CD  . GLU B 1 71  ? 37.286 15.835  -28.741 1.00 84.80  ?  128 GLU B CD  1 
ATOM   2649 O OE1 . GLU B 1 71  ? 37.078 17.055  -28.544 1.00 79.55  ?  128 GLU B OE1 1 
ATOM   2650 O OE2 . GLU B 1 71  ? 36.658 14.941  -28.130 1.00 79.21  -1 128 GLU B OE2 1 
ATOM   2651 N N   . ASN B 1 72  ? 36.413 17.639  -32.863 1.00 60.35  ?  129 ASN B N   1 
ATOM   2652 C CA  . ASN B 1 72  ? 36.125 18.448  -34.044 1.00 66.12  ?  129 ASN B CA  1 
ATOM   2653 C C   . ASN B 1 72  ? 36.669 17.816  -35.318 1.00 61.31  ?  129 ASN B C   1 
ATOM   2654 O O   . ASN B 1 72  ? 35.905 17.428  -36.210 1.00 62.98  ?  129 ASN B O   1 
ATOM   2655 C CB  . ASN B 1 72  ? 36.704 19.849  -33.869 1.00 80.13  ?  129 ASN B CB  1 
ATOM   2656 C CG  . ASN B 1 72  ? 36.321 20.778  -35.003 1.00 88.62  ?  129 ASN B CG  1 
ATOM   2657 O OD1 . ASN B 1 72  ? 35.155 20.863  -35.377 1.00 96.30  ?  129 ASN B OD1 1 
ATOM   2658 N ND2 . ASN B 1 72  ? 37.306 21.473  -35.563 1.00 87.60  ?  129 ASN B ND2 1 
ATOM   2659 N N   . GLU B 1 73  ? 37.995 17.704  -35.411 1.00 64.54  ?  130 GLU B N   1 
ATOM   2660 C CA  . GLU B 1 73  ? 38.633 17.251  -36.645 1.00 71.99  ?  130 GLU B CA  1 
ATOM   2661 C C   . GLU B 1 73  ? 38.141 15.867  -37.043 1.00 63.28  ?  130 GLU B C   1 
ATOM   2662 O O   . GLU B 1 73  ? 37.811 15.622  -38.208 1.00 62.61  ?  130 GLU B O   1 
ATOM   2663 C CB  . GLU B 1 73  ? 40.154 17.250  -36.475 1.00 70.15  ?  130 GLU B CB  1 
ATOM   2664 C CG  . GLU B 1 73  ? 40.723 18.548  -35.928 1.00 76.97  ?  130 GLU B CG  1 
ATOM   2665 C CD  . GLU B 1 73  ? 42.065 18.898  -36.549 1.00 96.61  ?  130 GLU B CD  1 
ATOM   2666 O OE1 . GLU B 1 73  ? 42.153 18.937  -37.795 1.00 100.24 ?  130 GLU B OE1 1 
ATOM   2667 O OE2 . GLU B 1 73  ? 43.034 19.130  -35.793 1.00 98.70  -1 130 GLU B OE2 1 
ATOM   2668 N N   . ASP B 1 74  ? 38.075 14.951  -36.078 1.00 61.92  ?  131 ASP B N   1 
ATOM   2669 C CA  . ASP B 1 74  ? 37.642 13.595  -36.381 1.00 60.34  ?  131 ASP B CA  1 
ATOM   2670 C C   . ASP B 1 74  ? 36.175 13.557  -36.805 1.00 65.85  ?  131 ASP B C   1 
ATOM   2671 O O   . ASP B 1 74  ? 35.795 12.729  -37.639 1.00 55.45  ?  131 ASP B O   1 
ATOM   2672 C CB  . ASP B 1 74  ? 37.904 12.704  -35.167 1.00 65.35  ?  131 ASP B CB  1 
ATOM   2673 C CG  . ASP B 1 74  ? 39.379 12.346  -35.021 1.00 66.88  ?  131 ASP B CG  1 
ATOM   2674 O OD1 . ASP B 1 74  ? 40.166 12.675  -35.933 1.00 77.04  -1 131 ASP B OD1 1 
ATOM   2675 O OD2 . ASP B 1 74  ? 39.755 11.742  -33.995 1.00 73.82  ?  131 ASP B OD2 1 
ATOM   2676 N N   . ALA B 1 75  ? 35.339 14.453  -36.266 1.00 54.48  ?  132 ALA B N   1 
ATOM   2677 C CA  . ALA B 1 75  ? 33.944 14.514  -36.702 1.00 51.96  ?  132 ALA B CA  1 
ATOM   2678 C C   . ALA B 1 75  ? 33.824 15.055  -38.123 1.00 52.34  ?  132 ALA B C   1 
ATOM   2679 O O   . ALA B 1 75  ? 32.945 14.624  -38.881 1.00 50.38  ?  132 ALA B O   1 
ATOM   2680 C CB  . ALA B 1 75  ? 33.121 15.370  -35.737 1.00 52.11  ?  132 ALA B CB  1 
ATOM   2681 N N   . GLN B 1 76  ? 34.692 15.995  -38.498 1.00 55.51  ?  133 GLN B N   1 
ATOM   2682 C CA  . GLN B 1 76  ? 34.704 16.497  -39.868 1.00 56.89  ?  133 GLN B CA  1 
ATOM   2683 C C   . GLN B 1 76  ? 35.107 15.406  -40.852 1.00 58.54  ?  133 GLN B C   1 
ATOM   2684 O O   . GLN B 1 76  ? 34.581 15.341  -41.970 1.00 58.30  ?  133 GLN B O   1 
ATOM   2685 C CB  . GLN B 1 76  ? 35.654 17.688  -39.975 1.00 60.56  ?  133 GLN B CB  1 
ATOM   2686 C CG  . GLN B 1 76  ? 35.279 18.876  -39.101 1.00 60.79  ?  133 GLN B CG  1 
ATOM   2687 C CD  . GLN B 1 76  ? 36.020 20.146  -39.496 1.00 70.22  ?  133 GLN B CD  1 
ATOM   2688 O OE1 . GLN B 1 76  ? 36.144 20.469  -40.679 1.00 65.97  ?  133 GLN B OE1 1 
ATOM   2689 N NE2 . GLN B 1 76  ? 36.511 20.878  -38.500 1.00 66.24  ?  133 GLN B NE2 1 
ATOM   2690 N N   . ALA B 1 77  ? 36.050 14.550  -40.459 1.00 58.37  ?  134 ALA B N   1 
ATOM   2691 C CA  . ALA B 1 77  ? 36.497 13.485  -41.349 1.00 59.21  ?  134 ALA B CA  1 
ATOM   2692 C C   . ALA B 1 77  ? 35.400 12.451  -41.565 1.00 56.39  ?  134 ALA B C   1 
ATOM   2693 O O   . ALA B 1 77  ? 35.267 11.900  -42.665 1.00 56.09  ?  134 ALA B O   1 
ATOM   2694 C CB  . ALA B 1 77  ? 37.754 12.824  -40.788 1.00 62.84  ?  134 ALA B CB  1 
ATOM   2695 N N   . VAL B 1 78  ? 34.609 12.170  -40.529 1.00 52.93  ?  135 VAL B N   1 
ATOM   2696 C CA  . VAL B 1 78  ? 33.508 11.223  -40.682 1.00 49.79  ?  135 VAL B CA  1 
ATOM   2697 C C   . VAL B 1 78  ? 32.426 11.823  -41.572 1.00 48.58  ?  135 VAL B C   1 
ATOM   2698 O O   . VAL B 1 78  ? 31.941 11.178  -42.509 1.00 47.91  ?  135 VAL B O   1 
ATOM   2699 C CB  . VAL B 1 78  ? 32.953 10.813  -39.304 1.00 50.55  ?  135 VAL B CB  1 
ATOM   2700 C CG1 . VAL B 1 78  ? 31.606 10.103  -39.447 1.00 43.97  ?  135 VAL B CG1 1 
ATOM   2701 C CG2 . VAL B 1 78  ? 33.960 9.948   -38.561 1.00 53.06  ?  135 VAL B CG2 1 
ATOM   2702 N N   . ALA B 1 79  ? 32.056 13.079  -41.304 1.00 48.67  ?  136 ALA B N   1 
ATOM   2703 C CA  . ALA B 1 79  ? 31.082 13.778  -42.137 1.00 51.64  ?  136 ALA B CA  1 
ATOM   2704 C C   . ALA B 1 79  ? 31.492 13.752  -43.603 1.00 51.98  ?  136 ALA B C   1 
ATOM   2705 O O   . ALA B 1 79  ? 30.659 13.515  -44.485 1.00 52.11  ?  136 ALA B O   1 
ATOM   2706 C CB  . ALA B 1 79  ? 30.924 15.223  -41.653 1.00 49.03  ?  136 ALA B CB  1 
ATOM   2707 N N   . GLN B 1 80  ? 32.778 13.982  -43.873 1.00 53.40  ?  137 GLN B N   1 
ATOM   2708 C CA  . GLN B 1 80  ? 33.275 14.010  -45.244 1.00 55.99  ?  137 GLN B CA  1 
ATOM   2709 C C   . GLN B 1 80  ? 33.059 12.674  -45.947 1.00 62.66  ?  137 GLN B C   1 
ATOM   2710 O O   . GLN B 1 80  ? 32.722 12.633  -47.137 1.00 63.67  ?  137 GLN B O   1 
ATOM   2711 C CB  . GLN B 1 80  ? 34.757 14.380  -45.233 1.00 73.18  ?  137 GLN B CB  1 
ATOM   2712 C CG  . GLN B 1 80  ? 35.422 14.388  -46.592 1.00 67.06  ?  137 GLN B CG  1 
ATOM   2713 C CD  . GLN B 1 80  ? 36.830 14.943  -46.533 1.00 85.10  ?  137 GLN B CD  1 
ATOM   2714 O OE1 . GLN B 1 80  ? 37.186 15.834  -47.297 1.00 86.33  ?  137 GLN B OE1 1 
ATOM   2715 N NE2 . GLN B 1 80  ? 37.641 14.411  -45.625 1.00 89.44  ?  137 GLN B NE2 1 
ATOM   2716 N N   . ALA B 1 81  ? 33.244 11.568  -45.225 1.00 63.10  ?  138 ALA B N   1 
ATOM   2717 C CA  . ALA B 1 81  ? 33.132 10.252  -45.844 1.00 54.86  ?  138 ALA B CA  1 
ATOM   2718 C C   . ALA B 1 81  ? 31.710 9.947   -46.305 1.00 71.07  ?  138 ALA B C   1 
ATOM   2719 O O   . ALA B 1 81  ? 31.523 9.177   -47.255 1.00 69.33  ?  138 ALA B O   1 
ATOM   2720 C CB  . ALA B 1 81  ? 33.611 9.176   -44.872 1.00 68.80  ?  138 ALA B CB  1 
ATOM   2721 N N   . CYS B 1 82  ? 30.696 10.532  -45.659 1.00 63.74  ?  139 CYS B N   1 
ATOM   2722 C CA  . CYS B 1 82  ? 29.317 10.227  -46.037 1.00 72.36  ?  139 CYS B CA  1 
ATOM   2723 C C   . CYS B 1 82  ? 28.926 10.783  -47.399 1.00 52.98  ?  139 CYS B C   1 
ATOM   2724 O O   . CYS B 1 82  ? 27.792 10.552  -47.831 1.00 54.09  ?  139 CYS B O   1 
ATOM   2725 C CB  . CYS B 1 82  ? 28.340 10.743  -44.976 1.00 50.31  ?  139 CYS B CB  1 
ATOM   2726 S SG  . CYS B 1 82  ? 28.759 10.257  -43.296 1.00 54.72  ?  139 CYS B SG  1 
ATOM   2727 N N   . GLY B 1 83  ? 29.814 11.495  -48.076 1.00 51.18  ?  140 GLY B N   1 
ATOM   2728 C CA  . GLY B 1 83  ? 29.486 12.028  -49.388 1.00 52.77  ?  140 GLY B CA  1 
ATOM   2729 C C   . GLY B 1 83  ? 28.299 12.967  -49.313 1.00 56.59  ?  140 GLY B C   1 
ATOM   2730 O O   . GLY B 1 83  ? 28.307 13.965  -48.579 1.00 57.62  ?  140 GLY B O   1 
ATOM   2731 N N   . ASN B 1 84  ? 27.248 12.641  -50.066 1.00 51.46  ?  141 ASN B N   1 
ATOM   2732 C CA  . ASN B 1 84  ? 26.038 13.451  -50.115 1.00 52.79  ?  141 ASN B CA  1 
ATOM   2733 C C   . ASN B 1 84  ? 24.866 12.815  -49.377 1.00 57.01  ?  141 ASN B C   1 
ATOM   2734 O O   . ASN B 1 84  ? 23.740 13.320  -49.469 1.00 46.67  ?  141 ASN B O   1 
ATOM   2735 C CB  . ASN B 1 84  ? 25.656 13.734  -51.567 1.00 60.79  ?  141 ASN B CB  1 
ATOM   2736 C CG  . ASN B 1 84  ? 26.565 14.763  -52.211 1.00 71.91  ?  141 ASN B CG  1 
ATOM   2737 O OD1 . ASN B 1 84  ? 27.765 14.805  -51.933 1.00 79.00  ?  141 ASN B OD1 1 
ATOM   2738 N ND2 . ASN B 1 84  ? 25.998 15.609  -53.063 1.00 79.66  ?  141 ASN B ND2 1 
ATOM   2739 N N   . VAL B 1 85  ? 25.096 11.732  -48.648 1.00 51.45  ?  142 VAL B N   1 
ATOM   2740 C CA  . VAL B 1 85  ? 24.047 11.167  -47.796 1.00 42.79  ?  142 VAL B CA  1 
ATOM   2741 C C   . VAL B 1 85  ? 23.916 12.033  -46.546 1.00 42.91  ?  142 VAL B C   1 
ATOM   2742 O O   . VAL B 1 85  ? 24.936 12.345  -45.909 1.00 46.65  ?  142 VAL B O   1 
ATOM   2743 C CB  . VAL B 1 85  ? 24.369 9.719   -47.434 1.00 47.76  ?  142 VAL B CB  1 
ATOM   2744 C CG1 . VAL B 1 85  ? 23.347 9.171   -46.451 1.00 41.17  ?  142 VAL B CG1 1 
ATOM   2745 C CG2 . VAL B 1 85  ? 24.406 8.865   -48.688 1.00 54.97  ?  142 VAL B CG2 1 
ATOM   2746 N N   . PRO B 1 86  ? 22.708 12.464  -46.190 1.00 39.47  ?  143 PRO B N   1 
ATOM   2747 C CA  . PRO B 1 86  ? 22.532 13.237  -44.954 1.00 41.21  ?  143 PRO B CA  1 
ATOM   2748 C C   . PRO B 1 86  ? 23.079 12.480  -43.753 1.00 43.95  ?  143 PRO B C   1 
ATOM   2749 O O   . PRO B 1 86  ? 22.852 11.279  -43.604 1.00 38.22  ?  143 PRO B O   1 
ATOM   2750 C CB  . PRO B 1 86  ? 21.011 13.401  -44.862 1.00 43.34  ?  143 PRO B CB  1 
ATOM   2751 C CG  . PRO B 1 86  ? 20.549 13.330  -46.280 1.00 47.57  ?  143 PRO B CG  1 
ATOM   2752 C CD  . PRO B 1 86  ? 21.442 12.299  -46.926 1.00 39.23  ?  143 PRO B CD  1 
ATOM   2753 N N   . VAL B 1 87  ? 23.806 13.195  -42.892 1.00 39.31  ?  144 VAL B N   1 
ATOM   2754 C CA  . VAL B 1 87  ? 24.420 12.609  -41.704 1.00 39.13  ?  144 VAL B CA  1 
ATOM   2755 C C   . VAL B 1 87  ? 24.294 13.577  -40.530 1.00 39.19  ?  144 VAL B C   1 
ATOM   2756 O O   . VAL B 1 87  ? 24.520 14.786  -40.674 1.00 39.91  ?  144 VAL B O   1 
ATOM   2757 C CB  . VAL B 1 87  ? 25.895 12.216  -41.963 1.00 40.19  ?  144 VAL B CB  1 
ATOM   2758 C CG1 . VAL B 1 87  ? 26.723 13.418  -42.417 1.00 42.08  ?  144 VAL B CG1 1 
ATOM   2759 C CG2 . VAL B 1 87  ? 26.495 11.601  -40.714 1.00 40.75  ?  144 VAL B CG2 1 
ATOM   2760 N N   . LEU B 1 88  ? 23.926 13.029  -39.365 1.00 37.89  ?  145 LEU B N   1 
ATOM   2761 C CA  . LEU B 1 88  ? 23.718 13.756  -38.116 1.00 34.57  ?  145 LEU B CA  1 
ATOM   2762 C C   . LEU B 1 88  ? 24.595 13.163  -37.022 1.00 35.97  ?  145 LEU B C   1 
ATOM   2763 O O   . LEU B 1 88  ? 24.730 11.940  -36.933 1.00 32.63  ?  145 LEU B O   1 
ATOM   2764 C CB  . LEU B 1 88  ? 22.262 13.659  -37.650 1.00 43.23  ?  145 LEU B CB  1 
ATOM   2765 C CG  . LEU B 1 88  ? 21.124 14.103  -38.556 1.00 41.32  ?  145 LEU B CG  1 
ATOM   2766 C CD1 . LEU B 1 88  ? 19.832 14.084  -37.776 1.00 41.95  ?  145 LEU B CD1 1 
ATOM   2767 C CD2 . LEU B 1 88  ? 21.397 15.500  -39.070 1.00 53.35  ?  145 LEU B CD2 1 
ATOM   2768 N N   . PHE B 1 89  ? 25.142 14.019  -36.156 1.00 36.32  ?  146 PHE B N   1 
ATOM   2769 C CA  . PHE B 1 89  ? 25.995 13.587  -35.053 1.00 36.65  ?  146 PHE B CA  1 
ATOM   2770 C C   . PHE B 1 89  ? 25.331 13.871  -33.712 1.00 38.06  ?  146 PHE B C   1 
ATOM   2771 O O   . PHE B 1 89  ? 24.730 14.932  -33.519 1.00 35.49  ?  146 PHE B O   1 
ATOM   2772 C CB  . PHE B 1 89  ? 27.357 14.281  -35.094 1.00 38.40  ?  146 PHE B CB  1 
ATOM   2773 C CG  . PHE B 1 89  ? 28.187 13.914  -36.291 1.00 39.59  ?  146 PHE B CG  1 
ATOM   2774 C CD1 . PHE B 1 89  ? 27.912 14.461  -37.534 1.00 40.34  ?  146 PHE B CD1 1 
ATOM   2775 C CD2 . PHE B 1 89  ? 29.215 12.982  -36.183 1.00 40.21  ?  146 PHE B CD2 1 
ATOM   2776 C CE1 . PHE B 1 89  ? 28.675 14.115  -38.639 1.00 45.66  ?  146 PHE B CE1 1 
ATOM   2777 C CE2 . PHE B 1 89  ? 29.973 12.627  -37.287 1.00 41.65  ?  146 PHE B CE2 1 
ATOM   2778 C CZ  . PHE B 1 89  ? 29.702 13.190  -38.513 1.00 44.22  ?  146 PHE B CZ  1 
ATOM   2779 N N   . LEU B 1 90  ? 25.468 12.934  -32.774 1.00 31.09  ?  147 LEU B N   1 
ATOM   2780 C CA  . LEU B 1 90  ? 24.845 13.048  -31.465 1.00 28.10  ?  147 LEU B CA  1 
ATOM   2781 C C   . LEU B 1 90  ? 25.842 13.254  -30.335 1.00 26.91  ?  147 LEU B C   1 
ATOM   2782 O O   . LEU B 1 90  ? 25.419 13.444  -29.189 1.00 37.39  ?  147 LEU B O   1 
ATOM   2783 C CB  . LEU B 1 90  ? 24.019 11.793  -31.168 1.00 30.14  ?  147 LEU B CB  1 
ATOM   2784 C CG  . LEU B 1 90  ? 22.914 11.424  -32.157 1.00 27.87  ?  147 LEU B CG  1 
ATOM   2785 C CD1 . LEU B 1 90  ? 22.084 10.296  -31.563 1.00 28.08  ?  147 LEU B CD1 1 
ATOM   2786 C CD2 . LEU B 1 90  ? 22.051 12.617  -32.503 1.00 33.20  ?  147 LEU B CD2 1 
ATOM   2787 N N   . ASP B 1 91  ? 27.147 13.222  -30.609 1.00 34.47  ?  148 ASP B N   1 
ATOM   2788 C CA  . ASP B 1 91  ? 28.133 13.341  -29.536 1.00 42.23  ?  148 ASP B CA  1 
ATOM   2789 C C   . ASP B 1 91  ? 29.427 13.967  -30.058 1.00 36.52  ?  148 ASP B C   1 
ATOM   2790 O O   . ASP B 1 91  ? 30.424 13.274  -30.296 1.00 38.53  ?  148 ASP B O   1 
ATOM   2791 C CB  . ASP B 1 91  ? 28.378 11.966  -28.903 1.00 38.49  ?  148 ASP B CB  1 
ATOM   2792 C CG  . ASP B 1 91  ? 29.029 12.053  -27.535 1.00 57.00  ?  148 ASP B CG  1 
ATOM   2793 O OD1 . ASP B 1 91  ? 29.495 11.012  -27.024 1.00 51.04  ?  148 ASP B OD1 1 
ATOM   2794 O OD2 . ASP B 1 91  ? 29.081 13.168  -26.975 1.00 63.54  -1 148 ASP B OD2 1 
ATOM   2795 N N   . VAL B 1 92  ? 29.415 15.290  -30.238 1.00 43.50  ?  149 VAL B N   1 
ATOM   2796 C CA  . VAL B 1 92  ? 30.534 16.013  -30.834 1.00 44.56  ?  149 VAL B CA  1 
ATOM   2797 C C   . VAL B 1 92  ? 30.823 17.295  -30.063 1.00 55.79  ?  149 VAL B C   1 
ATOM   2798 O O   . VAL B 1 92  ? 29.948 17.868  -29.406 1.00 45.63  ?  149 VAL B O   1 
ATOM   2799 C CB  . VAL B 1 92  ? 30.275 16.346  -32.320 1.00 45.42  ?  149 VAL B CB  1 
ATOM   2800 C CG1 . VAL B 1 92  ? 30.379 15.109  -33.179 1.00 42.84  ?  149 VAL B CG1 1 
ATOM   2801 C CG2 . VAL B 1 92  ? 28.899 16.968  -32.472 1.00 41.76  ?  149 VAL B CG2 1 
ATOM   2802 N N   . SER B 1 93  ? 32.076 17.739  -30.154 1.00 68.96  ?  150 SER B N   1 
ATOM   2803 C CA  . SER B 1 93  ? 32.461 19.067  -29.718 1.00 66.84  ?  150 SER B CA  1 
ATOM   2804 C C   . SER B 1 93  ? 31.978 20.072  -30.759 1.00 73.72  ?  150 SER B C   1 
ATOM   2805 O O   . SER B 1 93  ? 31.498 19.682  -31.828 1.00 72.69  ?  150 SER B O   1 
ATOM   2806 C CB  . SER B 1 93  ? 33.979 19.139  -29.531 1.00 71.01  ?  150 SER B CB  1 
ATOM   2807 O OG  . SER B 1 93  ? 34.671 18.802  -30.724 1.00 66.74  ?  150 SER B OG  1 
ATOM   2808 N N   . PRO B 1 94  ? 32.063 21.386  -30.465 1.00 70.45  ?  151 PRO B N   1 
ATOM   2809 C CA  . PRO B 1 94  ? 31.783 22.386  -31.505 1.00 61.41  ?  151 PRO B CA  1 
ATOM   2810 C C   . PRO B 1 94  ? 32.438 22.038  -32.831 1.00 63.49  ?  151 PRO B C   1 
ATOM   2811 O O   . PRO B 1 94  ? 33.668 21.981  -32.932 1.00 65.74  ?  151 PRO B O   1 
ATOM   2812 C CB  . PRO B 1 94  ? 32.363 23.670  -30.903 1.00 66.14  ?  151 PRO B CB  1 
ATOM   2813 C CG  . PRO B 1 94  ? 32.111 23.499  -29.443 1.00 61.57  ?  151 PRO B CG  1 
ATOM   2814 C CD  . PRO B 1 94  ? 32.338 22.027  -29.163 1.00 73.38  ?  151 PRO B CD  1 
ATOM   2815 N N   . ALA B 1 95  ? 31.617 21.774  -33.844 1.00 70.14  ?  152 ALA B N   1 
ATOM   2816 C CA  . ALA B 1 95  ? 32.102 21.270  -35.120 1.00 86.74  ?  152 ALA B CA  1 
ATOM   2817 C C   . ALA B 1 95  ? 31.223 21.807  -36.236 1.00 72.96  ?  152 ALA B C   1 
ATOM   2818 O O   . ALA B 1 95  ? 30.032 22.059  -36.017 1.00 77.91  ?  152 ALA B O   1 
ATOM   2819 C CB  . ALA B 1 95  ? 32.113 19.733  -35.149 1.00 74.54  ?  152 ALA B CB  1 
ATOM   2820 N N   . PRO B 1 96  ? 31.779 22.004  -37.442 1.00 68.88  ?  153 PRO B N   1 
ATOM   2821 C CA  . PRO B 1 96  ? 30.963 22.383  -38.611 1.00 63.34  ?  153 PRO B CA  1 
ATOM   2822 C C   . PRO B 1 96  ? 30.220 21.193  -39.215 1.00 66.43  ?  153 PRO B C   1 
ATOM   2823 O O   . PRO B 1 96  ? 30.342 20.880  -40.403 1.00 59.25  ?  153 PRO B O   1 
ATOM   2824 C CB  . PRO B 1 96  ? 32.016 22.972  -39.559 1.00 68.77  ?  153 PRO B CB  1 
ATOM   2825 C CG  . PRO B 1 96  ? 33.239 22.169  -39.268 1.00 66.52  ?  153 PRO B CG  1 
ATOM   2826 C CD  . PRO B 1 96  ? 33.218 21.970  -37.766 1.00 68.66  ?  153 PRO B CD  1 
ATOM   2827 N N   . VAL B 1 97  ? 29.434 20.511  -38.375 1.00 60.91  ?  154 VAL B N   1 
ATOM   2828 C CA  . VAL B 1 97  ? 28.657 19.341  -38.765 1.00 65.82  ?  154 VAL B CA  1 
ATOM   2829 C C   . VAL B 1 97  ? 27.225 19.525  -38.273 1.00 61.22  ?  154 VAL B C   1 
ATOM   2830 O O   . VAL B 1 97  ? 26.938 20.372  -37.421 1.00 50.89  ?  154 VAL B O   1 
ATOM   2831 C CB  . VAL B 1 97  ? 29.247 18.019  -38.206 1.00 58.82  ?  154 VAL B CB  1 
ATOM   2832 C CG1 . VAL B 1 97  ? 30.709 17.843  -38.624 1.00 59.71  ?  154 VAL B CG1 1 
ATOM   2833 C CG2 . VAL B 1 97  ? 29.104 17.961  -36.675 1.00 43.46  ?  154 VAL B CG2 1 
ATOM   2834 N N   . ASN B 1 98  ? 26.319 18.713  -38.825 1.00 46.62  ?  155 ASN B N   1 
ATOM   2835 C CA  . ASN B 1 98  ? 24.968 18.631  -38.280 1.00 44.60  ?  155 ASN B CA  1 
ATOM   2836 C C   . ASN B 1 98  ? 24.992 17.879  -36.959 1.00 50.14  ?  155 ASN B C   1 
ATOM   2837 O O   . ASN B 1 98  ? 25.518 16.764  -36.876 1.00 42.53  ?  155 ASN B O   1 
ATOM   2838 C CB  . ASN B 1 98  ? 24.014 17.925  -39.242 1.00 41.09  ?  155 ASN B CB  1 
ATOM   2839 C CG  . ASN B 1 98  ? 23.710 18.738  -40.463 1.00 45.58  ?  155 ASN B CG  1 
ATOM   2840 O OD1 . ASN B 1 98  ? 23.260 19.878  -40.360 1.00 51.51  ?  155 ASN B OD1 1 
ATOM   2841 N ND2 . ASN B 1 98  ? 23.903 18.145  -41.634 1.00 44.95  ?  155 ASN B ND2 1 
ATOM   2842 N N   . SER B 1 99  ? 24.411 18.474  -35.926 1.00 37.02  ?  156 SER B N   1 
ATOM   2843 C CA  . SER B 1 99  ? 24.356 17.810  -34.638 1.00 32.10  ?  156 SER B CA  1 
ATOM   2844 C C   . SER B 1 99  ? 23.015 18.081  -33.977 1.00 34.70  ?  156 SER B C   1 
ATOM   2845 O O   . SER B 1 99  ? 22.416 19.144  -34.166 1.00 42.00  ?  156 SER B O   1 
ATOM   2846 C CB  . SER B 1 99  ? 25.514 18.246  -33.719 1.00 40.15  ?  156 SER B CB  1 
ATOM   2847 O OG  . SER B 1 99  ? 25.495 19.644  -33.470 1.00 41.23  ?  156 SER B OG  1 
ATOM   2848 N N   . VAL B 1 100 ? 22.540 17.084  -33.240 1.00 33.03  ?  157 VAL B N   1 
ATOM   2849 C CA  . VAL B 1 100 ? 21.423 17.211  -32.320 1.00 35.66  ?  157 VAL B CA  1 
ATOM   2850 C C   . VAL B 1 100 ? 21.965 16.759  -30.974 1.00 37.02  ?  157 VAL B C   1 
ATOM   2851 O O   . VAL B 1 100 ? 22.310 15.580  -30.795 1.00 33.70  ?  157 VAL B O   1 
ATOM   2852 C CB  . VAL B 1 100 ? 20.211 16.377  -32.750 1.00 34.69  ?  157 VAL B CB  1 
ATOM   2853 C CG1 . VAL B 1 100 ? 19.088 16.523  -31.733 1.00 30.36  ?  157 VAL B CG1 1 
ATOM   2854 C CG2 . VAL B 1 100 ? 19.752 16.783  -34.130 1.00 38.24  ?  157 VAL B CG2 1 
ATOM   2855 N N   . LEU B 1 101 ? 22.066 17.695  -30.038 1.00 30.91  ?  158 LEU B N   1 
ATOM   2856 C CA  . LEU B 1 101 ? 22.828 17.515  -28.818 1.00 29.86  ?  158 LEU B CA  1 
ATOM   2857 C C   . LEU B 1 101 ? 21.979 17.932  -27.632 1.00 35.09  ?  158 LEU B C   1 
ATOM   2858 O O   . LEU B 1 101 ? 21.206 18.892  -27.716 1.00 30.37  ?  158 LEU B O   1 
ATOM   2859 C CB  . LEU B 1 101 ? 24.113 18.363  -28.832 1.00 39.40  ?  158 LEU B CB  1 
ATOM   2860 C CG  . LEU B 1 101 ? 25.255 17.948  -29.764 1.00 47.97  ?  158 LEU B CG  1 
ATOM   2861 C CD1 . LEU B 1 101 ? 26.472 18.842  -29.564 1.00 45.92  ?  158 LEU B CD1 1 
ATOM   2862 C CD2 . LEU B 1 101 ? 25.624 16.500  -29.572 1.00 45.78  ?  158 LEU B CD2 1 
ATOM   2863 N N   . PHE B 1 102 ? 22.125 17.215  -26.529 1.00 30.91  ?  159 PHE B N   1 
ATOM   2864 C CA  . PHE B 1 102 ? 21.743 17.779  -25.253 1.00 28.11  ?  159 PHE B CA  1 
ATOM   2865 C C   . PHE B 1 102 ? 22.823 18.766  -24.861 1.00 35.63  ?  159 PHE B C   1 
ATOM   2866 O O   . PHE B 1 102 ? 24.004 18.539  -25.130 1.00 42.15  ?  159 PHE B O   1 
ATOM   2867 C CB  . PHE B 1 102 ? 21.603 16.687  -24.200 1.00 22.11  ?  159 PHE B CB  1 
ATOM   2868 C CG  . PHE B 1 102 ? 20.418 15.821  -24.413 1.00 29.59  ?  159 PHE B CG  1 
ATOM   2869 C CD1 . PHE B 1 102 ? 19.140 16.314  -24.206 1.00 30.19  ?  159 PHE B CD1 1 
ATOM   2870 C CD2 . PHE B 1 102 ? 20.575 14.520  -24.838 1.00 30.48  ?  159 PHE B CD2 1 
ATOM   2871 C CE1 . PHE B 1 102 ? 18.039 15.512  -24.421 1.00 29.77  ?  159 PHE B CE1 1 
ATOM   2872 C CE2 . PHE B 1 102 ? 19.474 13.708  -25.040 1.00 29.42  ?  159 PHE B CE2 1 
ATOM   2873 C CZ  . PHE B 1 102 ? 18.206 14.219  -24.834 1.00 28.12  ?  159 PHE B CZ  1 
ATOM   2874 N N   . ASP B 1 103 ? 22.413 19.875  -24.257 1.00 34.86  ?  160 ASP B N   1 
ATOM   2875 C CA  . ASP B 1 103 ? 23.316 20.968  -23.941 1.00 31.31  ?  160 ASP B CA  1 
ATOM   2876 C C   . ASP B 1 103 ? 24.386 20.483  -22.962 1.00 39.79  ?  160 ASP B C   1 
ATOM   2877 O O   . ASP B 1 103 ? 24.087 20.213  -21.790 1.00 36.58  ?  160 ASP B O   1 
ATOM   2878 C CB  . ASP B 1 103 ? 22.502 22.136  -23.376 1.00 33.79  ?  160 ASP B CB  1 
ATOM   2879 C CG  . ASP B 1 103 ? 23.354 23.326  -22.968 1.00 35.59  ?  160 ASP B CG  1 
ATOM   2880 O OD1 . ASP B 1 103 ? 24.592 23.203  -22.817 1.00 43.00  ?  160 ASP B OD1 1 
ATOM   2881 O OD2 . ASP B 1 103 ? 22.756 24.413  -22.802 1.00 60.69  -1 160 ASP B OD2 1 
ATOM   2882 N N   . PRO B 1 104 ? 25.646 20.377  -23.399 1.00 39.60  ?  161 PRO B N   1 
ATOM   2883 C CA  . PRO B 1 104 ? 26.652 19.717  -22.546 1.00 34.11  ?  161 PRO B CA  1 
ATOM   2884 C C   . PRO B 1 104 ? 26.982 20.519  -21.304 1.00 37.49  ?  161 PRO B C   1 
ATOM   2885 O O   . PRO B 1 104 ? 27.250 19.949  -20.237 1.00 40.94  ?  161 PRO B O   1 
ATOM   2886 C CB  . PRO B 1 104 ? 27.875 19.592  -23.464 1.00 45.51  ?  161 PRO B CB  1 
ATOM   2887 C CG  . PRO B 1 104 ? 27.404 19.862  -24.839 1.00 54.84  ?  161 PRO B CG  1 
ATOM   2888 C CD  . PRO B 1 104 ? 26.123 20.627  -24.768 1.00 45.54  ?  161 PRO B CD  1 
ATOM   2889 N N   . HIS B 1 105 ? 26.977 21.843  -21.422 1.00 26.99  ?  162 HIS B N   1 
ATOM   2890 C CA  . HIS B 1 105 ? 27.317 22.711  -20.305 1.00 27.78  ?  162 HIS B CA  1 
ATOM   2891 C C   . HIS B 1 105 ? 26.165 22.846  -19.320 1.00 28.85  ?  162 HIS B C   1 
ATOM   2892 O O   . HIS B 1 105 ? 26.401 23.032  -18.121 1.00 23.93  ?  162 HIS B O   1 
ATOM   2893 C CB  . HIS B 1 105 ? 27.721 24.089  -20.843 1.00 33.40  ?  162 HIS B CB  1 
ATOM   2894 C CG  . HIS B 1 105 ? 27.833 25.148  -19.790 1.00 38.57  ?  162 HIS B CG  1 
ATOM   2895 N ND1 . HIS B 1 105 ? 29.014 25.427  -19.139 1.00 50.44  ?  162 HIS B ND1 1 
ATOM   2896 C CD2 . HIS B 1 105 ? 26.913 26.005  -19.285 1.00 38.66  ?  162 HIS B CD2 1 
ATOM   2897 C CE1 . HIS B 1 105 ? 28.815 26.405  -18.272 1.00 47.15  ?  162 HIS B CE1 1 
ATOM   2898 N NE2 . HIS B 1 105 ? 27.548 26.773  -18.340 1.00 43.11  ?  162 HIS B NE2 1 
ATOM   2899 N N   . GLU B 1 106 ? 24.919 22.758  -19.796 1.00 21.67  ?  163 GLU B N   1 
ATOM   2900 C CA  . GLU B 1 106 ? 23.789 23.034  -18.916 1.00 22.60  ?  163 GLU B CA  1 
ATOM   2901 C C   . GLU B 1 106 ? 23.617 21.936  -17.877 1.00 17.94  ?  163 GLU B C   1 
ATOM   2902 O O   . GLU B 1 106 ? 23.254 22.212  -16.725 1.00 17.06  ?  163 GLU B O   1 
ATOM   2903 C CB  . GLU B 1 106 ? 22.506 23.211  -19.739 1.00 23.40  ?  163 GLU B CB  1 
ATOM   2904 C CG  . GLU B 1 106 ? 21.243 23.471  -18.917 1.00 23.99  ?  163 GLU B CG  1 
ATOM   2905 C CD  . GLU B 1 106 ? 21.242 24.805  -18.160 1.00 30.69  ?  163 GLU B CD  1 
ATOM   2906 O OE1 . GLU B 1 106 ? 22.188 25.616  -18.314 1.00 32.25  ?  163 GLU B OE1 1 
ATOM   2907 O OE2 . GLU B 1 106 ? 20.281 25.035  -17.394 1.00 34.37  -1 163 GLU B OE2 1 
ATOM   2908 N N   . GLY B 1 107 ? 23.867 20.686  -18.262 1.00 17.89  ?  164 GLY B N   1 
ATOM   2909 C CA  . GLY B 1 107 ? 23.741 19.599  -17.305 1.00 18.58  ?  164 GLY B CA  1 
ATOM   2910 C C   . GLY B 1 107 ? 24.730 19.735  -16.166 1.00 17.90  ?  164 GLY B C   1 
ATOM   2911 O O   . GLY B 1 107 ? 24.389 19.509  -15.000 1.00 16.95  ?  164 GLY B O   1 
ATOM   2912 N N   . ALA B 1 108 ? 25.960 20.120  -16.491 1.00 16.59  ?  165 ALA B N   1 
ATOM   2913 C CA  . ALA B 1 108 ? 26.966 20.383  -15.464 1.00 18.73  ?  165 ALA B CA  1 
ATOM   2914 C C   . ALA B 1 108 ? 26.554 21.553  -14.583 1.00 16.37  ?  165 ALA B C   1 
ATOM   2915 O O   . ALA B 1 108 ? 26.647 21.486  -13.347 1.00 17.15  ?  165 ALA B O   1 
ATOM   2916 C CB  . ALA B 1 108 ? 28.318 20.662  -16.130 1.00 17.90  ?  165 ALA B CB  1 
ATOM   2917 N N   . ARG B 1 109 ? 26.089 22.635  -15.201 1.00 16.73  ?  166 ARG B N   1 
ATOM   2918 C CA  . ARG B 1 109 ? 25.662 23.807  -14.441 1.00 16.82  ?  166 ARG B CA  1 
ATOM   2919 C C   . ARG B 1 109 ? 24.535 23.467  -13.474 1.00 16.10  ?  166 ARG B C   1 
ATOM   2920 O O   . ARG B 1 109 ? 24.579 23.857  -12.302 1.00 17.24  ?  166 ARG B O   1 
ATOM   2921 C CB  . ARG B 1 109 ? 25.233 24.912  -15.405 1.00 17.94  ?  166 ARG B CB  1 
ATOM   2922 C CG  . ARG B 1 109 ? 24.999 26.242  -14.718 1.00 21.29  ?  166 ARG B CG  1 
ATOM   2923 C CD  . ARG B 1 109 ? 24.348 27.246  -15.680 1.00 26.10  ?  166 ARG B CD  1 
ATOM   2924 N NE  . ARG B 1 109 ? 22.932 26.931  -15.850 1.00 28.60  ?  166 ARG B NE  1 
ATOM   2925 C CZ  . ARG B 1 109 ? 22.004 27.206  -14.940 1.00 32.31  ?  166 ARG B CZ  1 
ATOM   2926 N NH1 . ARG B 1 109 ? 22.299 27.871  -13.832 1.00 32.90  ?  166 ARG B NH1 1 
ATOM   2927 N NH2 . ARG B 1 109 ? 20.753 26.800  -15.142 1.00 33.39  ?  166 ARG B NH2 1 
ATOM   2928 N N   . LEU B 1 110 ? 23.537 22.707  -13.932 1.00 15.39  ?  167 LEU B N   1 
ATOM   2929 C CA  . LEU B 1 110 ? 22.404 22.348  -13.073 1.00 14.86  ?  167 LEU B CA  1 
ATOM   2930 C C   . LEU B 1 110 ? 22.867 21.565  -11.854 1.00 14.17  ?  167 LEU B C   1 
ATOM   2931 O O   . LEU B 1 110 ? 22.379 21.789  -10.741 1.00 16.09  ?  167 LEU B O   1 
ATOM   2932 C CB  . LEU B 1 110 ? 21.380 21.504  -13.839 1.00 15.72  ?  167 LEU B CB  1 
ATOM   2933 C CG  . LEU B 1 110 ? 20.520 22.260  -14.847 1.00 18.69  ?  167 LEU B CG  1 
ATOM   2934 C CD1 . LEU B 1 110 ? 19.691 21.270  -15.685 1.00 19.10  ?  167 LEU B CD1 1 
ATOM   2935 C CD2 . LEU B 1 110 ? 19.615 23.295  -14.170 1.00 20.16  ?  167 LEU B CD2 1 
ATOM   2936 N N   . GLY B 1 111 ? 23.797 20.635  -12.054 1.00 14.29  ?  168 GLY B N   1 
ATOM   2937 C CA  . GLY B 1 111 ? 24.263 19.833  -10.937 1.00 15.99  ?  168 GLY B CA  1 
ATOM   2938 C C   . GLY B 1 111 ? 24.981 20.650  -9.883  1.00 15.90  ?  168 GLY B C   1 
ATOM   2939 O O   . GLY B 1 111 ? 24.729 20.490  -8.684  1.00 14.94  ?  168 GLY B O   1 
ATOM   2940 N N   . VAL B 1 112 ? 25.909 21.507  -10.308 1.00 14.53  ?  169 VAL B N   1 
ATOM   2941 C CA  . VAL B 1 112 ? 26.621 22.346  -9.343  1.00 14.52  ?  169 VAL B CA  1 
ATOM   2942 C C   . VAL B 1 112 ? 25.643 23.284  -8.642  1.00 16.23  ?  169 VAL B C   1 
ATOM   2943 O O   . VAL B 1 112 ? 25.665 23.436  -7.414  1.00 16.18  ?  169 VAL B O   1 
ATOM   2944 C CB  . VAL B 1 112 ? 27.761 23.121  -10.026 1.00 15.59  ?  169 VAL B CB  1 
ATOM   2945 C CG1 . VAL B 1 112 ? 28.338 24.173  -9.055  1.00 16.06  ?  169 VAL B CG1 1 
ATOM   2946 C CG2 . VAL B 1 112 ? 28.861 22.189  -10.507 1.00 16.14  ?  169 VAL B CG2 1 
ATOM   2947 N N   . GLU B 1 113 ? 24.757 23.916  -9.403  1.00 16.33  ?  170 GLU B N   1 
ATOM   2948 C CA  . GLU B 1 113 ? 23.863 24.887  -8.779  1.00 15.83  ?  170 GLU B CA  1 
ATOM   2949 C C   . GLU B 1 113 ? 22.961 24.230  -7.747  1.00 16.26  ?  170 GLU B C   1 
ATOM   2950 O O   . GLU B 1 113 ? 22.688 24.818  -6.697  1.00 17.61  ?  170 GLU B O   1 
ATOM   2951 C CB  . GLU B 1 113 ? 23.026 25.599  -9.841  1.00 17.51  ?  170 GLU B CB  1 
ATOM   2952 C CG  . GLU B 1 113 ? 23.818 26.535  -10.744 1.00 19.34  ?  170 GLU B CG  1 
ATOM   2953 C CD  . GLU B 1 113 ? 24.305 27.776  -10.041 1.00 25.77  ?  170 GLU B CD  1 
ATOM   2954 O OE1 . GLU B 1 113 ? 23.632 28.247  -9.091  1.00 29.99  ?  170 GLU B OE1 1 
ATOM   2955 O OE2 . GLU B 1 113 ? 25.376 28.280  -10.439 1.00 30.05  -1 170 GLU B OE2 1 
ATOM   2956 N N   . HIS B 1 114 ? 22.487 23.010  -8.036  1.00 15.65  ?  171 HIS B N   1 
ATOM   2957 C CA  . HIS B 1 114 ? 21.662 22.274  -7.084  1.00 14.58  ?  171 HIS B CA  1 
ATOM   2958 C C   . HIS B 1 114 ? 22.411 22.034  -5.780  1.00 16.53  ?  171 HIS B C   1 
ATOM   2959 O O   . HIS B 1 114 ? 21.888 22.299  -4.689  1.00 16.30  ?  171 HIS B O   1 
ATOM   2960 C CB  . HIS B 1 114 ? 21.213 20.961  -7.741  1.00 13.98  ?  171 HIS B CB  1 
ATOM   2961 C CG  . HIS B 1 114 ? 20.442 20.044  -6.838  1.00 17.84  ?  171 HIS B CG  1 
ATOM   2962 N ND1 . HIS B 1 114 ? 19.155 20.307  -6.416  1.00 26.80  ?  171 HIS B ND1 1 
ATOM   2963 C CD2 . HIS B 1 114 ? 20.777 18.847  -6.293  1.00 17.69  ?  171 HIS B CD2 1 
ATOM   2964 C CE1 . HIS B 1 114 ? 18.732 19.314  -5.650  1.00 23.18  ?  171 HIS B CE1 1 
ATOM   2965 N NE2 . HIS B 1 114 ? 19.694 18.409  -5.571  1.00 18.46  ?  171 HIS B NE2 1 
ATOM   2966 N N   . LEU B 1 115 ? 23.653 21.550  -5.868  1.00 13.24  ?  172 LEU B N   1 
ATOM   2967 C CA  . LEU B 1 115 ? 24.395 21.246  -4.651  1.00 14.06  ?  172 LEU B CA  1 
ATOM   2968 C C   . LEU B 1 115 ? 24.776 22.517  -3.907  1.00 17.90  ?  172 LEU B C   1 
ATOM   2969 O O   . LEU B 1 115 ? 24.730 22.554  -2.670  1.00 17.14  ?  172 LEU B O   1 
ATOM   2970 C CB  . LEU B 1 115 ? 25.646 20.441  -4.990  1.00 15.01  ?  172 LEU B CB  1 
ATOM   2971 C CG  . LEU B 1 115 ? 25.299 19.049  -5.513  1.00 13.20  ?  172 LEU B CG  1 
ATOM   2972 C CD1 . LEU B 1 115 ? 26.631 18.488  -5.986  1.00 15.64  ?  172 LEU B CD1 1 
ATOM   2973 C CD2 . LEU B 1 115 ? 24.601 18.170  -4.455  1.00 14.83  ?  172 LEU B CD2 1 
ATOM   2974 N N   . VAL B 1 116 ? 25.196 23.555  -4.635  1.00 15.89  ?  173 VAL B N   1 
ATOM   2975 C CA  . VAL B 1 116 ? 25.577 24.803  -3.979  1.00 15.28  ?  173 VAL B CA  1 
ATOM   2976 C C   . VAL B 1 116 ? 24.381 25.430  -3.284  1.00 16.68  ?  173 VAL B C   1 
ATOM   2977 O O   . VAL B 1 116 ? 24.508 25.943  -2.159  1.00 19.44  ?  173 VAL B O   1 
ATOM   2978 C CB  . VAL B 1 116 ? 26.216 25.762  -4.998  1.00 17.32  ?  173 VAL B CB  1 
ATOM   2979 C CG1 . VAL B 1 116 ? 26.263 27.174  -4.435  1.00 19.34  ?  173 VAL B CG1 1 
ATOM   2980 C CG2 . VAL B 1 116 ? 27.619 25.273  -5.315  1.00 17.24  ?  173 VAL B CG2 1 
ATOM   2981 N N   . ALA B 1 117 ? 23.196 25.360  -3.911  1.00 17.29  ?  174 ALA B N   1 
ATOM   2982 C CA  . ALA B 1 117 ? 21.993 25.936  -3.309  1.00 16.91  ?  174 ALA B CA  1 
ATOM   2983 C C   . ALA B 1 117 ? 21.619 25.208  -2.024  1.00 21.05  ?  174 ALA B C   1 
ATOM   2984 O O   . ALA B 1 117 ? 21.060 25.819  -1.105  1.00 22.96  ?  174 ALA B O   1 
ATOM   2985 C CB  . ALA B 1 117 ? 20.836 25.907  -4.300  1.00 21.71  ?  174 ALA B CB  1 
ATOM   2986 N N   . LEU B 1 118 ? 21.906 23.909  -1.946  1.00 14.97  ?  175 LEU B N   1 
ATOM   2987 C CA  . LEU B 1 118 ? 21.646 23.149  -0.737  1.00 14.58  ?  175 LEU B CA  1 
ATOM   2988 C C   . LEU B 1 118 ? 22.645 23.469  0.373   1.00 19.07  ?  175 LEU B C   1 
ATOM   2989 O O   . LEU B 1 118 ? 22.423 23.083  1.527   1.00 18.59  ?  175 LEU B O   1 
ATOM   2990 C CB  . LEU B 1 118 ? 21.671 21.650  -1.063  1.00 17.71  ?  175 LEU B CB  1 
ATOM   2991 C CG  . LEU B 1 118 ? 20.454 21.107  -1.800  1.00 16.64  ?  175 LEU B CG  1 
ATOM   2992 C CD1 . LEU B 1 118 ? 20.749 19.707  -2.349  1.00 19.27  ?  175 LEU B CD1 1 
ATOM   2993 C CD2 . LEU B 1 118 ? 19.209 21.069  -0.903  1.00 18.39  ?  175 LEU B CD2 1 
ATOM   2994 N N   . GLY B 1 119 ? 23.755 24.126  0.054   1.00 16.81  ?  176 GLY B N   1 
ATOM   2995 C CA  . GLY B 1 119 ? 24.737 24.511  1.056   1.00 15.64  ?  176 GLY B CA  1 
ATOM   2996 C C   . GLY B 1 119 ? 26.089 23.823  0.942   1.00 17.44  ?  176 GLY B C   1 
ATOM   2997 O O   . GLY B 1 119 ? 26.971 24.096  1.770   1.00 16.57  ?  176 GLY B O   1 
ATOM   2998 N N   . HIS B 1 120 ? 26.294 22.955  -0.044  1.00 15.78  ?  177 HIS B N   1 
ATOM   2999 C CA  . HIS B 1 120 ? 27.550 22.224  -0.133  1.00 13.02  ?  177 HIS B CA  1 
ATOM   3000 C C   . HIS B 1 120 ? 28.691 23.137  -0.556  1.00 15.91  ?  177 HIS B C   1 
ATOM   3001 O O   . HIS B 1 120 ? 28.536 23.985  -1.445  1.00 17.75  ?  177 HIS B O   1 
ATOM   3002 C CB  . HIS B 1 120 ? 27.425 21.088  -1.143  1.00 15.12  ?  177 HIS B CB  1 
ATOM   3003 C CG  . HIS B 1 120 ? 26.545 19.983  -0.674  1.00 13.45  ?  177 HIS B CG  1 
ATOM   3004 N ND1 . HIS B 1 120 ? 27.002 18.948  0.115   1.00 13.15  ?  177 HIS B ND1 1 
ATOM   3005 C CD2 . HIS B 1 120 ? 25.219 19.768  -0.859  1.00 14.46  ?  177 HIS B CD2 1 
ATOM   3006 C CE1 . HIS B 1 120 ? 25.987 18.142  0.401   1.00 13.24  ?  177 HIS B CE1 1 
ATOM   3007 N NE2 . HIS B 1 120 ? 24.897 18.619  -0.177  1.00 13.35  ?  177 HIS B NE2 1 
ATOM   3008 N N   . GLN B 1 121 ? 29.855 22.908  0.057   1.00 17.11  ?  178 GLN B N   1 
ATOM   3009 C CA  . GLN B 1 121 ? 31.097 23.581  -0.294  1.00 16.05  ?  178 GLN B CA  1 
ATOM   3010 C C   . GLN B 1 121 ? 32.241 22.630  -0.616  1.00 16.20  ?  178 GLN B C   1 
ATOM   3011 O O   . GLN B 1 121 ? 33.209 23.062  -1.250  1.00 23.36  ?  178 GLN B O   1 
ATOM   3012 C CB  . GLN B 1 121 ? 31.527 24.519  0.847   1.00 23.02  ?  178 GLN B CB  1 
ATOM   3013 C CG  . GLN B 1 121 ? 30.515 25.632  1.106   1.00 25.94  ?  178 GLN B CG  1 
ATOM   3014 C CD  . GLN B 1 121 ? 30.672 26.301  2.461   1.00 49.30  ?  178 GLN B CD  1 
ATOM   3015 O OE1 . GLN B 1 121 ? 31.433 25.845  3.312   1.00 52.58  ?  178 GLN B OE1 1 
ATOM   3016 N NE2 . GLN B 1 121 ? 29.950 27.399  2.661   1.00 55.75  ?  178 GLN B NE2 1 
ATOM   3017 N N   A ARG B 1 122 ? 32.142 21.356  -0.238  0.56 17.23  ?  179 ARG B N   1 
ATOM   3018 N N   B ARG B 1 122 ? 32.156 21.365  -0.216  0.44 17.26  ?  179 ARG B N   1 
ATOM   3019 C CA  A ARG B 1 122 ? 33.180 20.343  -0.441  0.56 15.49  ?  179 ARG B CA  1 
ATOM   3020 C CA  B ARG B 1 122 ? 33.192 20.363  -0.456  0.44 15.48  ?  179 ARG B CA  1 
ATOM   3021 C C   A ARG B 1 122 ? 32.632 19.323  -1.443  0.56 17.49  ?  179 ARG B C   1 
ATOM   3022 C C   B ARG B 1 122 ? 32.612 19.348  -1.440  0.44 17.51  ?  179 ARG B C   1 
ATOM   3023 O O   A ARG B 1 122 ? 32.063 18.295  -1.069  0.56 17.14  ?  179 ARG B O   1 
ATOM   3024 O O   B ARG B 1 122 ? 32.002 18.349  -1.052  0.44 17.03  ?  179 ARG B O   1 
ATOM   3025 C CB  A ARG B 1 122 ? 33.562 19.686  0.893   0.56 20.02  ?  179 ARG B CB  1 
ATOM   3026 C CB  B ARG B 1 122 ? 33.637 19.708  0.853   0.44 20.05  ?  179 ARG B CB  1 
ATOM   3027 C CG  A ARG B 1 122 ? 34.103 20.687  1.920   0.56 21.55  ?  179 ARG B CG  1 
ATOM   3028 C CG  B ARG B 1 122 ? 34.270 20.696  1.834   0.44 21.56  ?  179 ARG B CG  1 
ATOM   3029 C CD  A ARG B 1 122 ? 33.774 20.336  3.383   0.56 29.25  ?  179 ARG B CD  1 
ATOM   3030 C CD  B ARG B 1 122 ? 34.476 20.094  3.225   0.44 22.54  ?  179 ARG B CD  1 
ATOM   3031 N NE  A ARG B 1 122 ? 33.948 18.923  3.698   0.56 23.95  ?  179 ARG B NE  1 
ATOM   3032 N NE  B ARG B 1 122 ? 35.261 18.868  3.166   0.44 28.39  ?  179 ARG B NE  1 
ATOM   3033 C CZ  A ARG B 1 122 ? 33.396 18.317  4.742   0.56 21.39  ?  179 ARG B CZ  1 
ATOM   3034 C CZ  B ARG B 1 122 ? 36.584 18.835  3.094   0.44 31.60  ?  179 ARG B CZ  1 
ATOM   3035 N NH1 A ARG B 1 122 ? 32.663 18.981  5.619   0.56 22.85  ?  179 ARG B NH1 1 
ATOM   3036 N NH1 B ARG B 1 122 ? 37.301 19.947  3.037   0.44 34.78  ?  179 ARG B NH1 1 
ATOM   3037 N NH2 A ARG B 1 122 ? 33.578 17.007  4.902   0.56 18.09  ?  179 ARG B NH2 1 
ATOM   3038 N NH2 B ARG B 1 122 ? 37.202 17.658  3.072   0.44 30.96  ?  179 ARG B NH2 1 
ATOM   3039 N N   . ILE B 1 123 ? 32.786 19.628  -2.726  1.00 14.14  ?  180 ILE B N   1 
ATOM   3040 C CA  . ILE B 1 123 ? 32.164 18.863  -3.801  1.00 13.95  ?  180 ILE B CA  1 
ATOM   3041 C C   . ILE B 1 123 ? 33.254 18.150  -4.591  1.00 15.30  ?  180 ILE B C   1 
ATOM   3042 O O   . ILE B 1 123 ? 34.213 18.780  -5.048  1.00 15.48  ?  180 ILE B O   1 
ATOM   3043 C CB  . ILE B 1 123 ? 31.321 19.788  -4.703  1.00 13.91  ?  180 ILE B CB  1 
ATOM   3044 C CG1 . ILE B 1 123 ? 30.174 20.424  -3.898  1.00 14.31  ?  180 ILE B CG1 1 
ATOM   3045 C CG2 . ILE B 1 123 ? 30.779 19.030  -5.899  1.00 14.66  ?  180 ILE B CG2 1 
ATOM   3046 C CD1 . ILE B 1 123 ? 29.506 21.633  -4.558  1.00 16.47  ?  180 ILE B CD1 1 
ATOM   3047 N N   . ALA B 1 124 ? 33.099 16.844  -4.774  1.00 14.29  ?  181 ALA B N   1 
ATOM   3048 C CA  . ALA B 1 124 ? 34.028 16.089  -5.609  1.00 12.14  ?  181 ALA B CA  1 
ATOM   3049 C C   . ALA B 1 124 ? 33.406 15.782  -6.965  1.00 13.38  ?  181 ALA B C   1 
ATOM   3050 O O   . ALA B 1 124 ? 32.186 15.755  -7.118  1.00 13.39  ?  181 ALA B O   1 
ATOM   3051 C CB  . ALA B 1 124 ? 34.432 14.794  -4.913  1.00 14.27  ?  181 ALA B CB  1 
ATOM   3052 N N   . LEU B 1 125 ? 34.267 15.563  -7.951  1.00 12.39  ?  182 LEU B N   1 
ATOM   3053 C CA  . LEU B 1 125 ? 33.842 15.294  -9.323  1.00 11.91  ?  182 LEU B CA  1 
ATOM   3054 C C   . LEU B 1 125 ? 34.350 13.941  -9.778  1.00 14.73  ?  182 LEU B C   1 
ATOM   3055 O O   . LEU B 1 125 ? 35.537 13.637  -9.641  1.00 14.34  ?  182 LEU B O   1 
ATOM   3056 C CB  . LEU B 1 125 ? 34.365 16.361  -10.294 1.00 12.36  ?  182 LEU B CB  1 
ATOM   3057 C CG  . LEU B 1 125 ? 34.150 17.812  -9.895  1.00 11.96  ?  182 LEU B CG  1 
ATOM   3058 C CD1 . LEU B 1 125 ? 34.838 18.699  -10.947 1.00 16.57  ?  182 LEU B CD1 1 
ATOM   3059 C CD2 . LEU B 1 125 ? 32.661 18.115  -9.772  1.00 14.02  ?  182 LEU B CD2 1 
ATOM   3060 N N   . LEU B 1 126 ? 33.460 13.145  -10.345 1.00 12.99  ?  183 LEU B N   1 
ATOM   3061 C CA  . LEU B 1 126 ? 33.833 11.845  -10.910 1.00 14.98  ?  183 LEU B CA  1 
ATOM   3062 C C   . LEU B 1 126 ? 33.497 11.910  -12.399 1.00 14.07  ?  183 LEU B C   1 
ATOM   3063 O O   . LEU B 1 126 ? 32.328 11.784  -12.778 1.00 13.28  ?  183 LEU B O   1 
ATOM   3064 C CB  . LEU B 1 126 ? 33.086 10.713  -10.183 1.00 14.01  ?  183 LEU B CB  1 
ATOM   3065 C CG  . LEU B 1 126 ? 33.195 9.306   -10.799 1.00 18.90  ?  183 LEU B CG  1 
ATOM   3066 C CD1 . LEU B 1 126 ? 34.611 8.946   -11.176 1.00 19.05  ?  183 LEU B CD1 1 
ATOM   3067 C CD2 . LEU B 1 126 ? 32.611 8.277   -9.816  1.00 18.77  ?  183 LEU B CD2 1 
ATOM   3068 N N   . THR B 1 127 ? 34.516 12.129  -13.237 1.00 14.54  ?  184 THR B N   1 
ATOM   3069 C CA  . THR B 1 127 ? 34.307 12.345  -14.668 1.00 14.25  ?  184 THR B CA  1 
ATOM   3070 C C   . THR B 1 127 ? 34.195 11.017  -15.414 1.00 15.60  ?  184 THR B C   1 
ATOM   3071 O O   . THR B 1 127 ? 34.551 9.948   -14.916 1.00 14.01  ?  184 THR B O   1 
ATOM   3072 C CB  . THR B 1 127 ? 35.445 13.171  -15.292 1.00 15.11  ?  184 THR B CB  1 
ATOM   3073 O OG1 . THR B 1 127 ? 36.597 12.346  -15.535 1.00 16.83  ?  184 THR B OG1 1 
ATOM   3074 C CG2 . THR B 1 127 ? 35.892 14.327  -14.385 1.00 14.90  ?  184 THR B CG2 1 
ATOM   3075 N N   . GLY B 1 128 ? 33.713 11.096  -16.645 1.00 15.14  ?  185 GLY B N   1 
ATOM   3076 C CA  . GLY B 1 128 ? 33.907 10.013  -17.578 1.00 15.59  ?  185 GLY B CA  1 
ATOM   3077 C C   . GLY B 1 128 ? 35.329 10.011  -18.116 1.00 17.57  ?  185 GLY B C   1 
ATOM   3078 O O   . GLY B 1 128 ? 36.189 10.812  -17.715 1.00 18.53  ?  185 GLY B O   1 
ATOM   3079 N N   . PRO B 1 129 ? 35.598 9.100   -19.047 1.00 17.43  ?  186 PRO B N   1 
ATOM   3080 C CA  . PRO B 1 129 ? 36.936 9.030   -19.637 1.00 21.33  ?  186 PRO B CA  1 
ATOM   3081 C C   . PRO B 1 129 ? 37.234 10.290  -20.433 1.00 25.61  ?  186 PRO B C   1 
ATOM   3082 O O   . PRO B 1 129 ? 36.427 10.728  -21.258 1.00 24.69  ?  186 PRO B O   1 
ATOM   3083 C CB  . PRO B 1 129 ? 36.862 7.791   -20.539 1.00 20.66  ?  186 PRO B CB  1 
ATOM   3084 C CG  . PRO B 1 129 ? 35.418 7.585   -20.799 1.00 19.71  ?  186 PRO B CG  1 
ATOM   3085 C CD  . PRO B 1 129 ? 34.679 8.089   -19.606 1.00 17.66  ?  186 PRO B CD  1 
ATOM   3086 N N   . LEU B 1 130 ? 38.410 10.863  -20.191 1.00 25.63  ?  187 LEU B N   1 
ATOM   3087 C CA  . LEU B 1 130 ? 38.716 12.144  -20.809 1.00 30.33  ?  187 LEU B CA  1 
ATOM   3088 C C   . LEU B 1 130 ? 38.958 12.031  -22.312 1.00 32.94  ?  187 LEU B C   1 
ATOM   3089 O O   . LEU B 1 130 ? 39.044 13.061  -22.985 1.00 32.05  ?  187 LEU B O   1 
ATOM   3090 C CB  . LEU B 1 130 ? 39.909 12.777  -20.101 1.00 33.21  ?  187 LEU B CB  1 
ATOM   3091 C CG  . LEU B 1 130 ? 39.572 13.284  -18.688 1.00 32.45  ?  187 LEU B CG  1 
ATOM   3092 C CD1 . LEU B 1 130 ? 40.708 14.117  -18.130 1.00 37.31  ?  187 LEU B CD1 1 
ATOM   3093 C CD2 . LEU B 1 130 ? 38.245 14.048  -18.609 1.00 31.38  ?  187 LEU B CD2 1 
ATOM   3094 N N   . THR B 1 131 ? 39.032 10.816  -22.856 1.00 29.71  ?  188 THR B N   1 
ATOM   3095 C CA  . THR B 1 131 ? 38.996 10.649  -24.305 1.00 28.49  ?  188 THR B CA  1 
ATOM   3096 C C   . THR B 1 131 ? 37.638 11.007  -24.902 1.00 34.12  ?  188 THR B C   1 
ATOM   3097 O O   . THR B 1 131 ? 37.545 11.182  -26.122 1.00 36.95  ?  188 THR B O   1 
ATOM   3098 C CB  . THR B 1 131 ? 39.363 9.206   -24.683 1.00 31.52  ?  188 THR B CB  1 
ATOM   3099 O OG1 . THR B 1 131 ? 38.537 8.287   -23.948 1.00 31.73  ?  188 THR B OG1 1 
ATOM   3100 C CG2 . THR B 1 131 ? 40.818 8.935   -24.368 1.00 37.57  ?  188 THR B CG2 1 
ATOM   3101 N N   . SER B 1 132 ? 36.596 11.131  -24.078 1.00 25.93  ?  189 SER B N   1 
ATOM   3102 C CA  . SER B 1 132 ? 35.244 11.425  -24.542 1.00 25.91  ?  189 SER B CA  1 
ATOM   3103 C C   . SER B 1 132 ? 34.987 12.921  -24.485 1.00 26.21  ?  189 SER B C   1 
ATOM   3104 O O   . SER B 1 132 ? 35.137 13.535  -23.421 1.00 24.46  ?  189 SER B O   1 
ATOM   3105 C CB  . SER B 1 132 ? 34.206 10.709  -23.679 1.00 26.09  ?  189 SER B CB  1 
ATOM   3106 O OG  . SER B 1 132 ? 32.944 11.362  -23.780 1.00 26.98  ?  189 SER B OG  1 
ATOM   3107 N N   . VAL B 1 133 ? 34.566 13.496  -25.620 1.00 26.04  ?  190 VAL B N   1 
ATOM   3108 C CA  . VAL B 1 133 ? 34.231 14.919  -25.648 1.00 26.17  ?  190 VAL B CA  1 
ATOM   3109 C C   . VAL B 1 133 ? 33.151 15.241  -24.621 1.00 24.67  ?  190 VAL B C   1 
ATOM   3110 O O   . VAL B 1 133 ? 33.228 16.256  -23.916 1.00 25.16  ?  190 VAL B O   1 
ATOM   3111 C CB  . VAL B 1 133 ? 33.802 15.348  -27.062 1.00 32.81  ?  190 VAL B CB  1 
ATOM   3112 C CG1 . VAL B 1 133 ? 32.804 14.357  -27.651 1.00 43.52  ?  190 VAL B CG1 1 
ATOM   3113 C CG2 . VAL B 1 133 ? 33.216 16.743  -27.023 1.00 29.32  ?  190 VAL B CG2 1 
ATOM   3114 N N   . SER B 1 134 ? 32.127 14.391  -24.524 1.00 25.31  ?  191 SER B N   1 
ATOM   3115 C CA  . SER B 1 134 ? 31.060 14.601  -23.548 1.00 23.78  ?  191 SER B CA  1 
ATOM   3116 C C   . SER B 1 134 ? 31.608 14.653  -22.129 1.00 23.35  ?  191 SER B C   1 
ATOM   3117 O O   . SER B 1 134 ? 31.224 15.515  -21.324 1.00 22.16  ?  191 SER B O   1 
ATOM   3118 C CB  . SER B 1 134 ? 30.029 13.478  -23.663 1.00 27.14  ?  191 SER B CB  1 
ATOM   3119 O OG  . SER B 1 134 ? 29.047 13.796  -24.629 1.00 42.13  ?  191 SER B OG  1 
ATOM   3120 N N   . ALA B 1 135 ? 32.473 13.704  -21.782 1.00 19.21  ?  192 ALA B N   1 
ATOM   3121 C CA  . ALA B 1 135 ? 33.021 13.710  -20.429 1.00 16.75  ?  192 ALA B CA  1 
ATOM   3122 C C   . ALA B 1 135 ? 33.853 14.963  -20.174 1.00 20.46  ?  192 ALA B C   1 
ATOM   3123 O O   . ALA B 1 135 ? 33.813 15.527  -19.070 1.00 18.13  ?  192 ALA B O   1 
ATOM   3124 C CB  . ALA B 1 135 ? 33.858 12.457  -20.189 1.00 19.48  ?  192 ALA B CB  1 
ATOM   3125 N N   . ARG B 1 136 ? 34.625 15.397  -21.175 1.00 19.51  ?  193 ARG B N   1 
ATOM   3126 C CA  . ARG B 1 136 ? 35.452 16.588  -21.005 1.00 18.91  ?  193 ARG B CA  1 
ATOM   3127 C C   . ARG B 1 136 ? 34.600 17.833  -20.821 1.00 21.45  ?  193 ARG B C   1 
ATOM   3128 O O   . ARG B 1 136 ? 34.859 18.649  -19.924 1.00 20.65  ?  193 ARG B O   1 
ATOM   3129 C CB  . ARG B 1 136 ? 36.398 16.739  -22.195 1.00 20.63  ?  193 ARG B CB  1 
ATOM   3130 C CG  . ARG B 1 136 ? 37.229 18.012  -22.155 1.00 29.64  ?  193 ARG B CG  1 
ATOM   3131 C CD  . ARG B 1 136 ? 38.167 18.132  -23.373 1.00 34.27  ?  193 ARG B CD  1 
ATOM   3132 N NE  . ARG B 1 136 ? 37.463 18.230  -24.652 1.00 39.27  ?  193 ARG B NE  1 
ATOM   3133 C CZ  . ARG B 1 136 ? 36.909 19.342  -25.122 1.00 46.66  ?  193 ARG B CZ  1 
ATOM   3134 N NH1 . ARG B 1 136 ? 36.920 20.469  -24.425 1.00 38.99  ?  193 ARG B NH1 1 
ATOM   3135 N NH2 . ARG B 1 136 ? 36.326 19.324  -26.319 1.00 40.80  ?  193 ARG B NH2 1 
ATOM   3136 N N   . LEU B 1 137 ? 33.557 17.986  -21.632 1.00 20.00  ?  194 LEU B N   1 
ATOM   3137 C CA  . LEU B 1 137 ? 32.731 19.184  -21.522 1.00 21.11  ?  194 LEU B CA  1 
ATOM   3138 C C   . LEU B 1 137 ? 31.925 19.206  -20.227 1.00 18.06  ?  194 LEU B C   1 
ATOM   3139 O O   . LEU B 1 137 ? 31.704 20.291  -19.666 1.00 18.59  ?  194 LEU B O   1 
ATOM   3140 C CB  . LEU B 1 137 ? 31.801 19.302  -22.726 1.00 23.30  ?  194 LEU B CB  1 
ATOM   3141 C CG  . LEU B 1 137 ? 32.509 19.654  -24.032 1.00 29.96  ?  194 LEU B CG  1 
ATOM   3142 C CD1 . LEU B 1 137 ? 31.512 19.660  -25.179 1.00 30.45  ?  194 LEU B CD1 1 
ATOM   3143 C CD2 . LEU B 1 137 ? 33.243 20.997  -23.923 1.00 28.26  ?  194 LEU B CD2 1 
ATOM   3144 N N   . ARG B 1 138 ? 31.477 18.042  -19.734 1.00 16.55  ?  195 ARG B N   1 
ATOM   3145 C CA  . ARG B 1 138 ? 30.819 18.004  -18.430 1.00 14.07  ?  195 ARG B CA  1 
ATOM   3146 C C   . ARG B 1 138 ? 31.794 18.407  -17.331 1.00 18.03  ?  195 ARG B C   1 
ATOM   3147 O O   . ARG B 1 138 ? 31.456 19.212  -16.454 1.00 15.65  ?  195 ARG B O   1 
ATOM   3148 C CB  . ARG B 1 138 ? 30.231 16.615  -18.148 1.00 15.38  ?  195 ARG B CB  1 
ATOM   3149 C CG  . ARG B 1 138 ? 29.020 16.317  -19.006 1.00 18.07  ?  195 ARG B CG  1 
ATOM   3150 C CD  . ARG B 1 138 ? 28.618 14.844  -18.932 1.00 16.15  ?  195 ARG B CD  1 
ATOM   3151 N NE  . ARG B 1 138 ? 27.781 14.503  -20.069 1.00 16.32  ?  195 ARG B NE  1 
ATOM   3152 C CZ  . ARG B 1 138 ? 27.277 13.300  -20.287 1.00 16.95  ?  195 ARG B CZ  1 
ATOM   3153 N NH1 . ARG B 1 138 ? 27.463 12.308  -19.430 1.00 16.57  ?  195 ARG B NH1 1 
ATOM   3154 N NH2 . ARG B 1 138 ? 26.602 13.076  -21.412 1.00 17.43  ?  195 ARG B NH2 1 
ATOM   3155 N N   . PHE B 1 139 ? 33.018 17.864  -17.371 1.00 14.25  ?  196 PHE B N   1 
ATOM   3156 C CA  . PHE B 1 139 ? 34.032 18.257  -16.393 1.00 16.34  ?  196 PHE B CA  1 
ATOM   3157 C C   . PHE B 1 139 ? 34.277 19.761  -16.416 1.00 16.80  ?  196 PHE B C   1 
ATOM   3158 O O   . PHE B 1 139 ? 34.296 20.409  -15.360 1.00 15.92  ?  196 PHE B O   1 
ATOM   3159 C CB  . PHE B 1 139 ? 35.347 17.508  -16.634 1.00 15.47  ?  196 PHE B CB  1 
ATOM   3160 C CG  . PHE B 1 139 ? 36.493 18.080  -15.854 1.00 18.09  ?  196 PHE B CG  1 
ATOM   3161 C CD1 . PHE B 1 139 ? 36.498 18.096  -14.463 1.00 17.69  ?  196 PHE B CD1 1 
ATOM   3162 C CD2 . PHE B 1 139 ? 37.514 18.714  -16.525 1.00 23.78  ?  196 PHE B CD2 1 
ATOM   3163 C CE1 . PHE B 1 139 ? 37.557 18.682  -13.753 1.00 21.01  ?  196 PHE B CE1 1 
ATOM   3164 C CE2 . PHE B 1 139 ? 38.561 19.310  -15.834 1.00 26.82  ?  196 PHE B CE2 1 
ATOM   3165 C CZ  . PHE B 1 139 ? 38.583 19.289  -14.447 1.00 23.97  ?  196 PHE B CZ  1 
ATOM   3166 N N   . GLU B 1 140 ? 34.468 20.329  -17.610 1.00 16.81  ?  197 GLU B N   1 
ATOM   3167 C CA  . GLU B 1 140 ? 34.761 21.759  -17.704 1.00 17.19  ?  197 GLU B CA  1 
ATOM   3168 C C   . GLU B 1 140 ? 33.588 22.586  -17.197 1.00 19.30  ?  197 GLU B C   1 
ATOM   3169 O O   . GLU B 1 140 ? 33.786 23.600  -16.519 1.00 19.76  ?  197 GLU B O   1 
ATOM   3170 C CB  . GLU B 1 140 ? 35.119 22.143  -19.142 1.00 21.16  ?  197 GLU B CB  1 
ATOM   3171 C CG  . GLU B 1 140 ? 36.506 21.624  -19.594 1.00 23.81  ?  197 GLU B CG  1 
ATOM   3172 C CD  . GLU B 1 140 ? 36.723 21.746  -21.103 1.00 42.32  ?  197 GLU B CD  1 
ATOM   3173 O OE1 . GLU B 1 140 ? 35.939 22.460  -21.773 1.00 43.49  ?  197 GLU B OE1 1 
ATOM   3174 O OE2 . GLU B 1 140 ? 37.689 21.140  -21.619 1.00 39.13  -1 197 GLU B OE2 1 
ATOM   3175 N N   . GLY B 1 141 ? 32.358 22.159  -17.508 1.00 18.13  ?  198 GLY B N   1 
ATOM   3176 C CA  . GLY B 1 141 ? 31.184 22.839  -16.972 1.00 16.86  ?  198 GLY B CA  1 
ATOM   3177 C C   . GLY B 1 141 ? 31.116 22.798  -15.457 1.00 15.26  ?  198 GLY B C   1 
ATOM   3178 O O   . GLY B 1 141 ? 30.753 23.794  -14.816 1.00 16.59  ?  198 GLY B O   1 
ATOM   3179 N N   . TRP B 1 142 ? 31.448 21.643  -14.861 1.00 14.54  ?  199 TRP B N   1 
ATOM   3180 C CA  . TRP B 1 142 ? 31.462 21.557  -13.401 1.00 12.81  ?  199 TRP B CA  1 
ATOM   3181 C C   . TRP B 1 142 ? 32.489 22.508  -12.816 1.00 14.55  ?  199 TRP B C   1 
ATOM   3182 O O   . TRP B 1 142 ? 32.194 23.264  -11.882 1.00 13.78  ?  199 TRP B O   1 
ATOM   3183 C CB  . TRP B 1 142 ? 31.806 20.143  -12.951 1.00 14.82  ?  199 TRP B CB  1 
ATOM   3184 C CG  . TRP B 1 142 ? 30.741 19.126  -13.111 1.00 13.65  ?  199 TRP B CG  1 
ATOM   3185 C CD1 . TRP B 1 142 ? 29.389 19.319  -13.132 1.00 12.72  ?  199 TRP B CD1 1 
ATOM   3186 C CD2 . TRP B 1 142 ? 30.956 17.724  -13.283 1.00 12.51  ?  199 TRP B CD2 1 
ATOM   3187 N NE1 . TRP B 1 142 ? 28.735 18.106  -13.273 1.00 14.04  ?  199 TRP B NE1 1 
ATOM   3188 C CE2 . TRP B 1 142 ? 29.686 17.118  -13.386 1.00 12.98  ?  199 TRP B CE2 1 
ATOM   3189 C CE3 . TRP B 1 142 ? 32.107 16.913  -13.343 1.00 13.27  ?  199 TRP B CE3 1 
ATOM   3190 C CZ2 . TRP B 1 142 ? 29.532 15.731  -13.534 1.00 13.81  ?  199 TRP B CZ2 1 
ATOM   3191 C CZ3 . TRP B 1 142 ? 31.955 15.545  -13.500 1.00 13.13  ?  199 TRP B CZ3 1 
ATOM   3192 C CH2 . TRP B 1 142 ? 30.672 14.970  -13.575 1.00 14.18  ?  199 TRP B CH2 1 
ATOM   3193 N N   . ARG B 1 143 ? 33.717 22.456  -13.336 1.00 15.35  ?  200 ARG B N   1 
ATOM   3194 C CA  . ARG B 1 143 ? 34.780 23.296  -12.805 1.00 14.69  ?  200 ARG B CA  1 
ATOM   3195 C C   . ARG B 1 143 ? 34.429 24.772  -12.943 1.00 16.13  ?  200 ARG B C   1 
ATOM   3196 O O   . ARG B 1 143 ? 34.649 25.557  -12.015 1.00 15.99  ?  200 ARG B O   1 
ATOM   3197 C CB  . ARG B 1 143 ? 36.089 22.961  -13.517 1.00 18.44  ?  200 ARG B CB  1 
ATOM   3198 C CG  . ARG B 1 143 ? 37.305 23.686  -12.978 1.00 21.17  ?  200 ARG B CG  1 
ATOM   3199 C CD  . ARG B 1 143 ? 38.547 23.293  -13.782 1.00 27.92  ?  200 ARG B CD  1 
ATOM   3200 N NE  . ARG B 1 143 ? 38.413 23.600  -15.200 1.00 42.05  ?  200 ARG B NE  1 
ATOM   3201 C CZ  . ARG B 1 143 ? 39.206 23.122  -16.151 1.00 53.30  ?  200 ARG B CZ  1 
ATOM   3202 N NH1 . ARG B 1 143 ? 40.207 22.300  -15.869 1.00 41.95  ?  200 ARG B NH1 1 
ATOM   3203 N NH2 . ARG B 1 143 ? 38.993 23.482  -17.416 1.00 33.47  ?  200 ARG B NH2 1 
ATOM   3204 N N   . GLN B 1 144 ? 33.893 25.175  -14.109 1.00 15.30  ?  201 GLN B N   1 
ATOM   3205 C CA  . GLN B 1 144 ? 33.553 26.578  -14.332 1.00 15.75  ?  201 GLN B CA  1 
ATOM   3206 C C   . GLN B 1 144 ? 32.432 27.033  -13.410 1.00 17.37  ?  201 GLN B C   1 
ATOM   3207 O O   . GLN B 1 144 ? 32.478 28.143  -12.873 1.00 17.26  ?  201 GLN B O   1 
ATOM   3208 C CB  . GLN B 1 144 ? 33.147 26.799  -15.794 1.00 19.71  ?  201 GLN B CB  1 
ATOM   3209 C CG  . GLN B 1 144 ? 32.776 28.257  -16.084 1.00 27.96  ?  201 GLN B CG  1 
ATOM   3210 C CD  . GLN B 1 144 ? 31.924 28.412  -17.325 1.00 39.50  ?  201 GLN B CD  1 
ATOM   3211 O OE1 . GLN B 1 144 ? 31.464 27.429  -17.901 1.00 54.44  ?  201 GLN B OE1 1 
ATOM   3212 N NE2 . GLN B 1 144 ? 31.708 29.654  -17.742 1.00 46.52  ?  201 GLN B NE2 1 
ATOM   3213 N N   . THR B 1 145 ? 31.397 26.215  -13.245 1.00 15.20  ?  202 THR B N   1 
ATOM   3214 C CA  . THR B 1 145 ? 30.285 26.632  -12.396 1.00 14.36  ?  202 THR B CA  1 
ATOM   3215 C C   . THR B 1 145 ? 30.700 26.691  -10.931 1.00 15.56  ?  202 THR B C   1 
ATOM   3216 O O   . THR B 1 145 ? 30.288 27.603  -10.200 1.00 16.84  ?  202 THR B O   1 
ATOM   3217 C CB  . THR B 1 145 ? 29.086 25.699  -12.592 1.00 15.19  ?  202 THR B CB  1 
ATOM   3218 O OG1 . THR B 1 145 ? 28.783 25.623  -13.990 1.00 17.45  ?  202 THR B OG1 1 
ATOM   3219 C CG2 . THR B 1 145 ? 27.856 26.237  -11.887 1.00 14.77  ?  202 THR B CG2 1 
ATOM   3220 N N   . LEU B 1 146 ? 31.530 25.745  -10.483 1.00 14.47  ?  203 LEU B N   1 
ATOM   3221 C CA  . LEU B 1 146 ? 32.081 25.833  -9.133  1.00 13.55  ?  203 LEU B CA  1 
ATOM   3222 C C   . LEU B 1 146 ? 32.873 27.121  -8.952  1.00 17.60  ?  203 LEU B C   1 
ATOM   3223 O O   . LEU B 1 146 ? 32.750 27.788  -7.914  1.00 17.51  ?  203 LEU B O   1 
ATOM   3224 C CB  . LEU B 1 146 ? 32.977 24.617  -8.849  1.00 13.18  ?  203 LEU B CB  1 
ATOM   3225 C CG  . LEU B 1 146 ? 32.221 23.311  -8.597  1.00 14.43  ?  203 LEU B CG  1 
ATOM   3226 C CD1 . LEU B 1 146 ? 33.204 22.148  -8.672  1.00 16.52  ?  203 LEU B CD1 1 
ATOM   3227 C CD2 . LEU B 1 146 ? 31.553 23.326  -7.229  1.00 16.99  ?  203 LEU B CD2 1 
ATOM   3228 N N   . ALA B 1 147 ? 33.709 27.476  -9.946  1.00 15.32  ?  204 ALA B N   1 
ATOM   3229 C CA  . ALA B 1 147 ? 34.513 28.697  -9.852  1.00 15.84  ?  204 ALA B CA  1 
ATOM   3230 C C   . ALA B 1 147 ? 33.655 29.959  -9.787  1.00 16.29  ?  204 ALA B C   1 
ATOM   3231 O O   . ALA B 1 147 ? 34.056 30.943  -9.158  1.00 18.42  ?  204 ALA B O   1 
ATOM   3232 C CB  . ALA B 1 147 ? 35.478 28.780  -11.038 1.00 16.50  ?  204 ALA B CB  1 
ATOM   3233 N N   . GLN B 1 148 ? 32.478 29.961  -10.424 1.00 17.76  ?  205 GLN B N   1 
ATOM   3234 C CA  . GLN B 1 148 ? 31.576 31.104  -10.294 1.00 17.56  ?  205 GLN B CA  1 
ATOM   3235 C C   . GLN B 1 148 ? 31.045 31.275  -8.876  1.00 18.06  ?  205 GLN B C   1 
ATOM   3236 O O   . GLN B 1 148 ? 30.564 32.367  -8.535  1.00 21.35  ?  205 GLN B O   1 
ATOM   3237 C CB  . GLN B 1 148 ? 30.402 30.980  -11.275 1.00 18.81  ?  205 GLN B CB  1 
ATOM   3238 C CG  . GLN B 1 148 ? 30.787 31.306  -12.705 1.00 28.40  ?  205 GLN B CG  1 
ATOM   3239 C CD  . GLN B 1 148 ? 29.892 30.668  -13.752 1.00 43.78  ?  205 GLN B CD  1 
ATOM   3240 O OE1 . GLN B 1 148 ? 28.755 30.281  -13.473 1.00 43.24  ?  205 GLN B OE1 1 
ATOM   3241 N NE2 . GLN B 1 148 ? 30.377 30.630  -14.988 1.00 40.45  ?  205 GLN B NE2 1 
ATOM   3242 N N   . HIS B 1 149 ? 31.125 30.227  -8.051  1.00 17.61  ?  206 HIS B N   1 
ATOM   3243 C CA  . HIS B 1 149 ? 30.802 30.282  -6.630  1.00 18.34  ?  206 HIS B CA  1 
ATOM   3244 C C   . HIS B 1 149 ? 32.047 30.295  -5.751  1.00 19.95  ?  206 HIS B C   1 
ATOM   3245 O O   . HIS B 1 149 ? 31.952 30.056  -4.538  1.00 19.83  ?  206 HIS B O   1 
ATOM   3246 C CB  . HIS B 1 149 ? 29.888 29.103  -6.264  1.00 17.01  ?  206 HIS B CB  1 
ATOM   3247 C CG  . HIS B 1 149 ? 28.542 29.208  -6.896  1.00 18.04  ?  206 HIS B CG  1 
ATOM   3248 N ND1 . HIS B 1 149 ? 27.532 29.969  -6.349  1.00 21.36  ?  206 HIS B ND1 1 
ATOM   3249 C CD2 . HIS B 1 149 ? 28.050 28.695  -8.046  1.00 20.70  ?  206 HIS B CD2 1 
ATOM   3250 C CE1 . HIS B 1 149 ? 26.464 29.893  -7.123  1.00 22.28  ?  206 HIS B CE1 1 
ATOM   3251 N NE2 . HIS B 1 149 ? 26.753 29.133  -8.161  1.00 26.21  ?  206 HIS B NE2 1 
ATOM   3252 N N   A GLN B 1 150 ? 33.210 30.593  -6.336  0.51 16.11  ?  207 GLN B N   1 
ATOM   3253 N N   B GLN B 1 150 ? 33.211 30.571  -6.342  0.49 16.13  ?  207 GLN B N   1 
ATOM   3254 C CA  A GLN B 1 150 ? 34.481 30.651  -5.605  0.51 17.04  ?  207 GLN B CA  1 
ATOM   3255 C CA  B GLN B 1 150 ? 34.481 30.647  -5.615  0.49 17.04  ?  207 GLN B CA  1 
ATOM   3256 C C   A GLN B 1 150 ? 34.781 29.334  -4.885  0.51 19.19  ?  207 GLN B C   1 
ATOM   3257 C C   B GLN B 1 150 ? 34.791 29.335  -4.892  0.49 19.20  ?  207 GLN B C   1 
ATOM   3258 O O   A GLN B 1 150 ? 35.267 29.322  -3.750  0.51 18.71  ?  207 GLN B O   1 
ATOM   3259 O O   B GLN B 1 150 ? 35.287 29.328  -3.762  0.49 18.69  ?  207 GLN B O   1 
ATOM   3260 C CB  A GLN B 1 150 ? 34.505 31.837  -4.630  0.51 18.67  ?  207 GLN B CB  1 
ATOM   3261 C CB  B GLN B 1 150 ? 34.496 31.835  -4.644  0.49 18.69  ?  207 GLN B CB  1 
ATOM   3262 C CG  A GLN B 1 150 ? 34.323 33.191  -5.321  0.51 21.33  ?  207 GLN B CG  1 
ATOM   3263 C CG  B GLN B 1 150 ? 34.378 33.198  -5.335  0.49 21.30  ?  207 GLN B CG  1 
ATOM   3264 C CD  A GLN B 1 150 ? 34.628 34.372  -4.419  0.51 24.88  ?  207 GLN B CD  1 
ATOM   3265 C CD  B GLN B 1 150 ? 32.953 33.503  -5.787  0.49 20.97  ?  207 GLN B CD  1 
ATOM   3266 O OE1 A GLN B 1 150 ? 34.491 34.291  -3.199  0.51 37.87  ?  207 GLN B OE1 1 
ATOM   3267 O OE1 B GLN B 1 150 ? 32.014 33.442  -4.993  0.49 24.82  ?  207 GLN B OE1 1 
ATOM   3268 N NE2 A GLN B 1 150 ? 35.047 35.479  -5.020  0.51 33.10  ?  207 GLN B NE2 1 
ATOM   3269 N NE2 B GLN B 1 150 ? 32.791 33.842  -7.062  0.49 22.25  ?  207 GLN B NE2 1 
ATOM   3270 N N   . LEU B 1 151 ? 34.530 28.211  -5.567  1.00 17.16  ?  208 LEU B N   1 
ATOM   3271 C CA  . LEU B 1 151 ? 34.866 26.887  -5.049  1.00 15.09  ?  208 LEU B CA  1 
ATOM   3272 C C   . LEU B 1 151 ? 35.769 26.150  -6.028  1.00 16.14  ?  208 LEU B C   1 
ATOM   3273 O O   . LEU B 1 151 ? 35.638 26.299  -7.251  1.00 17.59  ?  208 LEU B O   1 
ATOM   3274 C CB  . LEU B 1 151 ? 33.610 26.042  -4.810  1.00 14.77  ?  208 LEU B CB  1 
ATOM   3275 C CG  . LEU B 1 151 ? 32.591 26.597  -3.810  1.00 16.81  ?  208 LEU B CG  1 
ATOM   3276 C CD1 . LEU B 1 151 ? 31.299 25.805  -3.935  1.00 22.11  ?  208 LEU B CD1 1 
ATOM   3277 C CD2 . LEU B 1 151 ? 33.137 26.579  -2.372  1.00 18.38  ?  208 LEU B CD2 1 
ATOM   3278 N N   . GLN B 1 152 ? 36.681 25.338  -5.476  1.00 17.05  ?  209 GLN B N   1 
ATOM   3279 C CA  . GLN B 1 152 ? 37.398 24.338  -6.259  1.00 16.95  ?  209 GLN B CA  1 
ATOM   3280 C C   . GLN B 1 152 ? 36.878 22.955  -5.888  1.00 18.07  ?  209 GLN B C   1 
ATOM   3281 O O   . GLN B 1 152 ? 36.482 22.734  -4.738  1.00 17.48  ?  209 GLN B O   1 
ATOM   3282 C CB  . GLN B 1 152 ? 38.908 24.383  -6.013  1.00 20.14  ?  209 GLN B CB  1 
ATOM   3283 C CG  . GLN B 1 152 ? 39.541 25.689  -6.448  1.00 24.15  ?  209 GLN B CG  1 
ATOM   3284 C CD  . GLN B 1 152 ? 40.997 25.782  -6.070  1.00 37.90  ?  209 GLN B CD  1 
ATOM   3285 O OE1 . GLN B 1 152 ? 41.338 25.854  -4.889  1.00 43.68  ?  209 GLN B OE1 1 
ATOM   3286 N NE2 . GLN B 1 152 ? 41.869 25.818  -7.074  1.00 36.93  ?  209 GLN B NE2 1 
ATOM   3287 N N   . PRO B 1 153 ? 36.856 22.008  -6.824  1.00 16.65  ?  210 PRO B N   1 
ATOM   3288 C CA  . PRO B 1 153 ? 36.492 20.637  -6.453  1.00 14.29  ?  210 PRO B CA  1 
ATOM   3289 C C   . PRO B 1 153 ? 37.488 20.099  -5.429  1.00 17.64  ?  210 PRO B C   1 
ATOM   3290 O O   . PRO B 1 153 ? 38.687 20.366  -5.508  1.00 19.11  ?  210 PRO B O   1 
ATOM   3291 C CB  . PRO B 1 153 ? 36.575 19.873  -7.778  1.00 18.51  ?  210 PRO B CB  1 
ATOM   3292 C CG  . PRO B 1 153 ? 37.549 20.634  -8.600  1.00 18.60  ?  210 PRO B CG  1 
ATOM   3293 C CD  . PRO B 1 153 ? 37.341 22.104  -8.215  1.00 17.26  ?  210 PRO B CD  1 
ATOM   3294 N N   A ILE B 1 154 ? 36.970 19.336  -4.459  0.63 15.72  ?  211 ILE B N   1 
ATOM   3295 N N   B ILE B 1 154 ? 36.983 19.336  -4.456  0.37 15.57  ?  211 ILE B N   1 
ATOM   3296 C CA  A ILE B 1 154 ? 37.830 18.765  -3.428  0.63 18.51  ?  211 ILE B CA  1 
ATOM   3297 C CA  B ILE B 1 154 ? 37.885 18.790  -3.447  0.37 18.65  ?  211 ILE B CA  1 
ATOM   3298 C C   A ILE B 1 154 ? 38.601 17.558  -3.947  0.63 20.09  ?  211 ILE B C   1 
ATOM   3299 C C   B ILE B 1 154 ? 38.625 17.561  -3.960  0.37 20.04  ?  211 ILE B C   1 
ATOM   3300 O O   A ILE B 1 154 ? 39.671 17.236  -3.415  0.63 20.83  ?  211 ILE B O   1 
ATOM   3301 O O   B ILE B 1 154 ? 39.686 17.216  -3.425  0.37 20.84  ?  211 ILE B O   1 
ATOM   3302 C CB  A ILE B 1 154 ? 37.004 18.414  -2.176  0.63 22.58  ?  211 ILE B CB  1 
ATOM   3303 C CB  B ILE B 1 154 ? 37.124 18.489  -2.144  0.37 22.48  ?  211 ILE B CB  1 
ATOM   3304 C CG1 A ILE B 1 154 ? 37.929 18.108  -0.994  0.63 24.00  ?  211 ILE B CG1 1 
ATOM   3305 C CG1 B ILE B 1 154 ? 36.116 17.351  -2.337  0.37 22.26  ?  211 ILE B CG1 1 
ATOM   3306 C CG2 A ILE B 1 154 ? 36.045 17.257  -2.449  0.63 22.42  ?  211 ILE B CG2 1 
ATOM   3307 C CG2 B ILE B 1 154 ? 36.453 19.752  -1.632  0.37 23.17  ?  211 ILE B CG2 1 
ATOM   3308 C CD1 A ILE B 1 154 ? 37.209 17.975  0.321   0.63 27.29  ?  211 ILE B CD1 1 
ATOM   3309 C CD1 B ILE B 1 154 ? 36.620 15.999  -1.864  0.37 26.70  ?  211 ILE B CD1 1 
ATOM   3310 N N   . ALA B 1 155 ? 38.092 16.897  -4.984  1.00 16.03  ?  212 ALA B N   1 
ATOM   3311 C CA  . ALA B 1 155 ? 38.763 15.790  -5.642  1.00 17.19  ?  212 ALA B CA  1 
ATOM   3312 C C   . ALA B 1 155 ? 38.221 15.717  -7.060  1.00 15.84  ?  212 ALA B C   1 
ATOM   3313 O O   . ALA B 1 155 ? 37.085 16.121  -7.328  1.00 16.51  ?  212 ALA B O   1 
ATOM   3314 C CB  . ALA B 1 155 ? 38.542 14.458  -4.916  1.00 20.96  ?  212 ALA B CB  1 
ATOM   3315 N N   . VAL B 1 156 ? 39.052 15.227  -7.973  1.00 15.87  ?  213 VAL B N   1 
ATOM   3316 C CA  . VAL B 1 156 ? 38.632 14.996  -9.352  1.00 14.21  ?  213 VAL B CA  1 
ATOM   3317 C C   . VAL B 1 156 ? 39.180 13.631  -9.739  1.00 15.87  ?  213 VAL B C   1 
ATOM   3318 O O   . VAL B 1 156 ? 40.398 13.441  -9.775  1.00 18.65  ?  213 VAL B O   1 
ATOM   3319 C CB  . VAL B 1 156 ? 39.161 16.069  -10.321 1.00 16.83  ?  213 VAL B CB  1 
ATOM   3320 C CG1 . VAL B 1 156 ? 38.711 15.756  -11.736 1.00 19.66  ?  213 VAL B CG1 1 
ATOM   3321 C CG2 . VAL B 1 156 ? 38.730 17.491  -9.904  1.00 17.82  ?  213 VAL B CG2 1 
ATOM   3322 N N   . LEU B 1 157 ? 38.295 12.679  -10.009 1.00 16.23  ?  214 LEU B N   1 
ATOM   3323 C CA  . LEU B 1 157 ? 38.712 11.360  -10.448 1.00 16.81  ?  214 LEU B CA  1 
ATOM   3324 C C   . LEU B 1 157 ? 38.032 11.055  -11.776 1.00 17.68  ?  214 LEU B C   1 
ATOM   3325 O O   . LEU B 1 157 ? 37.081 11.725  -12.180 1.00 15.56  ?  214 LEU B O   1 
ATOM   3326 C CB  . LEU B 1 157 ? 38.389 10.283  -9.393  1.00 25.10  ?  214 LEU B CB  1 
ATOM   3327 C CG  . LEU B 1 157 ? 39.187 10.441  -8.098  1.00 36.64  ?  214 LEU B CG  1 
ATOM   3328 C CD1 . LEU B 1 157 ? 38.364 11.177  -7.066  1.00 35.80  ?  214 LEU B CD1 1 
ATOM   3329 C CD2 . LEU B 1 157 ? 39.672 9.110   -7.564  1.00 30.37  ?  214 LEU B CD2 1 
ATOM   3330 N N   . HIS B 1 158 ? 38.553 10.056  -12.472 1.00 16.61  ?  215 HIS B N   1 
ATOM   3331 C CA  . HIS B 1 158 ? 38.102 9.740   -13.822 1.00 15.09  ?  215 HIS B CA  1 
ATOM   3332 C C   . HIS B 1 158 ? 37.714 8.271   -13.895 1.00 16.45  ?  215 HIS B C   1 
ATOM   3333 O O   . HIS B 1 158 ? 38.543 7.395   -13.616 1.00 18.56  ?  215 HIS B O   1 
ATOM   3334 C CB  . HIS B 1 158 ? 39.202 10.054  -14.858 1.00 19.69  ?  215 HIS B CB  1 
ATOM   3335 C CG  . HIS B 1 158 ? 39.887 11.371  -14.628 1.00 21.15  ?  215 HIS B CG  1 
ATOM   3336 N ND1 . HIS B 1 158 ? 39.262 12.580  -14.858 1.00 19.85  ?  215 HIS B ND1 1 
ATOM   3337 C CD2 . HIS B 1 158 ? 41.123 11.670  -14.161 1.00 25.48  ?  215 HIS B CD2 1 
ATOM   3338 C CE1 . HIS B 1 158 ? 40.086 13.566  -14.544 1.00 22.23  ?  215 HIS B CE1 1 
ATOM   3339 N NE2 . HIS B 1 158 ? 41.223 13.041  -14.123 1.00 24.96  ?  215 HIS B NE2 1 
ATOM   3340 N N   . GLY B 1 159 ? 36.478 7.999   -14.322 1.00 16.91  ?  216 GLY B N   1 
ATOM   3341 C CA  . GLY B 1 159 ? 35.999 6.654   -14.544 1.00 13.54  ?  216 GLY B CA  1 
ATOM   3342 C C   . GLY B 1 159 ? 35.915 6.309   -16.020 1.00 15.74  ?  216 GLY B C   1 
ATOM   3343 O O   . GLY B 1 159 ? 36.438 7.017   -16.882 1.00 19.68  ?  216 GLY B O   1 
ATOM   3344 N N   . ASP B 1 160 ? 35.270 5.166   -16.305 1.00 14.12  ?  217 ASP B N   1 
ATOM   3345 C CA  . ASP B 1 160 ? 35.176 4.673   -17.682 1.00 13.96  ?  217 ASP B CA  1 
ATOM   3346 C C   . ASP B 1 160 ? 33.736 4.452   -18.142 1.00 15.64  ?  217 ASP B C   1 
ATOM   3347 O O   . ASP B 1 160 ? 33.518 3.743   -19.134 1.00 17.43  ?  217 ASP B O   1 
ATOM   3348 C CB  . ASP B 1 160 ? 36.005 3.388   -17.864 1.00 15.11  ?  217 ASP B CB  1 
ATOM   3349 C CG  . ASP B 1 160 ? 35.426 2.181   -17.157 1.00 18.43  ?  217 ASP B CG  1 
ATOM   3350 O OD1 . ASP B 1 160 ? 34.292 2.236   -16.641 1.00 16.65  ?  217 ASP B OD1 1 
ATOM   3351 O OD2 . ASP B 1 160 ? 36.142 1.154   -17.120 1.00 21.72  -1 217 ASP B OD2 1 
ATOM   3352 N N   . TRP B 1 161 ? 32.758 5.043   -17.443 1.00 12.46  ?  218 TRP B N   1 
ATOM   3353 C CA  . TRP B 1 161 ? 31.306 5.004   -17.633 1.00 12.53  ?  218 TRP B CA  1 
ATOM   3354 C C   . TRP B 1 161 ? 30.664 3.792   -16.964 1.00 13.48  ?  218 TRP B C   1 
ATOM   3355 O O   . TRP B 1 161 ? 29.439 3.737   -16.899 1.00 14.14  ?  218 TRP B O   1 
ATOM   3356 C CB  . TRP B 1 161 ? 30.856 5.009   -19.110 1.00 14.19  ?  218 TRP B CB  1 
ATOM   3357 C CG  . TRP B 1 161 ? 31.273 6.196   -19.988 1.00 15.46  ?  218 TRP B CG  1 
ATOM   3358 C CD1 . TRP B 1 161 ? 31.942 6.118   -21.178 1.00 15.97  ?  218 TRP B CD1 1 
ATOM   3359 C CD2 . TRP B 1 161 ? 30.963 7.594   -19.796 1.00 15.08  ?  218 TRP B CD2 1 
ATOM   3360 N NE1 . TRP B 1 161 ? 32.086 7.371   -21.737 1.00 16.17  ?  218 TRP B NE1 1 
ATOM   3361 C CE2 . TRP B 1 161 ? 31.501 8.292   -20.908 1.00 13.84  ?  218 TRP B CE2 1 
ATOM   3362 C CE3 . TRP B 1 161 ? 30.275 8.319   -18.801 1.00 11.90  ?  218 TRP B CE3 1 
ATOM   3363 C CZ2 . TRP B 1 161 ? 31.397 9.683   -21.041 1.00 16.17  ?  218 TRP B CZ2 1 
ATOM   3364 C CZ3 . TRP B 1 161 ? 30.158 9.695   -18.938 1.00 14.59  ?  218 TRP B CZ3 1 
ATOM   3365 C CH2 . TRP B 1 161 ? 30.720 10.365  -20.052 1.00 16.61  ?  218 TRP B CH2 1 
ATOM   3366 N N   . SER B 1 162 ? 31.439 2.822   -16.457 1.00 14.29  ?  219 SER B N   1 
ATOM   3367 C CA  . SER B 1 162 ? 30.845 1.618   -15.884 1.00 12.76  ?  219 SER B CA  1 
ATOM   3368 C C   . SER B 1 162 ? 30.607 1.779   -14.388 1.00 12.31  ?  219 SER B C   1 
ATOM   3369 O O   . SER B 1 162 ? 31.252 2.585   -13.710 1.00 13.44  ?  219 SER B O   1 
ATOM   3370 C CB  . SER B 1 162 ? 31.746 0.408   -16.113 1.00 15.08  ?  219 SER B CB  1 
ATOM   3371 O OG  . SER B 1 162 ? 32.925 0.441   -15.289 1.00 14.95  ?  219 SER B OG  1 
ATOM   3372 N N   . ALA B 1 163 ? 29.700 0.949   -13.859 1.00 11.01  ?  220 ALA B N   1 
ATOM   3373 C CA  . ALA B 1 163 ? 29.444 0.977   -12.418 1.00 12.37  ?  220 ALA B CA  1 
ATOM   3374 C C   . ALA B 1 163 ? 30.689 0.625   -11.602 1.00 12.18  ?  220 ALA B C   1 
ATOM   3375 O O   . ALA B 1 163 ? 30.993 1.293   -10.601 1.00 12.02  ?  220 ALA B O   1 
ATOM   3376 C CB  . ALA B 1 163 ? 28.282 0.031   -12.062 1.00 11.89  ?  220 ALA B CB  1 
ATOM   3377 N N   . LEU B 1 164 ? 31.429 -0.408  -12.010 1.00 12.51  ?  221 LEU B N   1 
ATOM   3378 C CA  . LEU B 1 164 ? 32.597 -0.819  -11.231 1.00 12.19  ?  221 LEU B CA  1 
ATOM   3379 C C   . LEU B 1 164 ? 33.629 0.304   -11.154 1.00 14.63  ?  221 LEU B C   1 
ATOM   3380 O O   . LEU B 1 164 ? 34.297 0.490   -10.125 1.00 13.10  ?  221 LEU B O   1 
ATOM   3381 C CB  . LEU B 1 164 ? 33.204 -2.077  -11.842 1.00 12.82  ?  221 LEU B CB  1 
ATOM   3382 C CG  . LEU B 1 164 ? 34.395 -2.606  -11.057 1.00 14.00  ?  221 LEU B CG  1 
ATOM   3383 C CD1 . LEU B 1 164 ? 33.959 -2.981  -9.637  1.00 18.35  ?  221 LEU B CD1 1 
ATOM   3384 C CD2 . LEU B 1 164 ? 34.985 -3.786  -11.796 1.00 19.41  ?  221 LEU B CD2 1 
ATOM   3385 N N   A SER B 1 165 ? 33.759 1.071   -12.231 0.43 12.51  ?  222 SER B N   1 
ATOM   3386 N N   B SER B 1 165 ? 33.776 1.070   -12.236 0.57 12.50  ?  222 SER B N   1 
ATOM   3387 C CA  A SER B 1 165 ? 34.688 2.194   -12.222 0.43 14.69  ?  222 SER B CA  1 
ATOM   3388 C CA  B SER B 1 165 ? 34.705 2.200   -12.199 0.57 14.66  ?  222 SER B CA  1 
ATOM   3389 C C   A SER B 1 165 ? 34.224 3.282   -11.258 0.43 14.25  ?  222 SER B C   1 
ATOM   3390 C C   B SER B 1 165 ? 34.223 3.277   -11.236 0.57 14.28  ?  222 SER B C   1 
ATOM   3391 O O   A SER B 1 165 ? 35.049 3.921   -10.591 0.43 14.19  ?  222 SER B O   1 
ATOM   3392 O O   B SER B 1 165 ? 35.038 3.912   -10.552 0.57 14.15  ?  222 SER B O   1 
ATOM   3393 C CB  A SER B 1 165 ? 34.837 2.724   -13.646 0.43 16.55  ?  222 SER B CB  1 
ATOM   3394 C CB  B SER B 1 165 ? 34.906 2.769   -13.608 0.57 16.58  ?  222 SER B CB  1 
ATOM   3395 O OG  A SER B 1 165 ? 35.809 3.735   -13.730 0.43 16.97  ?  222 SER B OG  1 
ATOM   3396 O OG  B SER B 1 165 ? 33.874 3.682   -13.959 0.57 15.30  ?  222 SER B OG  1 
ATOM   3397 N N   . GLY B 1 166 ? 32.908 3.497   -11.162 1.00 13.40  ?  223 GLY B N   1 
ATOM   3398 C CA  . GLY B 1 166 ? 32.383 4.408   -10.154 1.00 13.97  ?  223 GLY B CA  1 
ATOM   3399 C C   . GLY B 1 166 ? 32.687 3.952   -8.736  1.00 15.30  ?  223 GLY B C   1 
ATOM   3400 O O   . GLY B 1 166 ? 33.030 4.766   -7.869  1.00 14.05  ?  223 GLY B O   1 
ATOM   3401 N N   . TYR B 1 167 ? 32.535 2.649   -8.473  1.00 12.23  ?  224 TYR B N   1 
ATOM   3402 C CA  . TYR B 1 167 ? 32.927 2.096   -7.173  1.00 12.64  ?  224 TYR B CA  1 
ATOM   3403 C C   . TYR B 1 167 ? 34.420 2.310   -6.909  1.00 15.52  ?  224 TYR B C   1 
ATOM   3404 O O   . TYR B 1 167 ? 34.811 2.798   -5.838  1.00 13.81  ?  224 TYR B O   1 
ATOM   3405 C CB  . TYR B 1 167 ? 32.567 0.601   -7.112  1.00 13.03  ?  224 TYR B CB  1 
ATOM   3406 C CG  . TYR B 1 167 ? 33.143 -0.073  -5.895  1.00 12.43  ?  224 TYR B CG  1 
ATOM   3407 C CD1 . TYR B 1 167 ? 32.497 0.021   -4.659  1.00 12.85  ?  224 TYR B CD1 1 
ATOM   3408 C CD2 . TYR B 1 167 ? 34.325 -0.784  -5.969  1.00 13.67  ?  224 TYR B CD2 1 
ATOM   3409 C CE1 . TYR B 1 167 ? 33.029 -0.568  -3.536  1.00 12.67  ?  224 TYR B CE1 1 
ATOM   3410 C CE2 . TYR B 1 167 ? 34.865 -1.391  -4.844  1.00 14.45  ?  224 TYR B CE2 1 
ATOM   3411 C CZ  . TYR B 1 167 ? 34.221 -1.259  -3.626  1.00 14.55  ?  224 TYR B CZ  1 
ATOM   3412 O OH  . TYR B 1 167 ? 34.792 -1.850  -2.519  1.00 17.49  ?  224 TYR B OH  1 
ATOM   3413 N N   . GLN B 1 168 ? 35.275 1.924   -7.865  1.00 12.83  ?  225 GLN B N   1 
ATOM   3414 C CA  . GLN B 1 168 ? 36.716 1.970   -7.626  1.00 12.66  ?  225 GLN B CA  1 
ATOM   3415 C C   . GLN B 1 168 ? 37.197 3.401   -7.437  1.00 14.54  ?  225 GLN B C   1 
ATOM   3416 O O   . GLN B 1 168 ? 38.020 3.664   -6.558  1.00 15.54  ?  225 GLN B O   1 
ATOM   3417 C CB  . GLN B 1 168 ? 37.466 1.293   -8.767  1.00 13.32  ?  225 GLN B CB  1 
ATOM   3418 C CG  . GLN B 1 168 ? 37.225 -0.205  -8.828  1.00 14.32  ?  225 GLN B CG  1 
ATOM   3419 C CD  . GLN B 1 168 ? 37.814 -0.837  -10.051 1.00 18.75  ?  225 GLN B CD  1 
ATOM   3420 O OE1 . GLN B 1 168 ? 38.219 -0.144  -10.995 1.00 21.11  ?  225 GLN B OE1 1 
ATOM   3421 N NE2 . GLN B 1 168 ? 37.873 -2.172  -10.058 1.00 16.34  ?  225 GLN B NE2 1 
ATOM   3422 N N   . GLN B 1 169 ? 36.705 4.335   -8.249  1.00 14.51  ?  226 GLN B N   1 
ATOM   3423 C CA  . GLN B 1 169 ? 37.170 5.715   -8.114  1.00 14.59  ?  226 GLN B CA  1 
ATOM   3424 C C   . GLN B 1 169 ? 36.634 6.357   -6.848  1.00 15.89  ?  226 GLN B C   1 
ATOM   3425 O O   . GLN B 1 169 ? 37.321 7.180   -6.225  1.00 15.77  ?  226 GLN B O   1 
ATOM   3426 C CB  . GLN B 1 169 ? 36.772 6.540   -9.346  1.00 16.27  ?  226 GLN B CB  1 
ATOM   3427 C CG  . GLN B 1 169 ? 37.443 6.095   -10.647 1.00 16.88  ?  226 GLN B CG  1 
ATOM   3428 C CD  . GLN B 1 169 ? 38.953 5.912   -10.518 1.00 20.80  ?  226 GLN B CD  1 
ATOM   3429 O OE1 . GLN B 1 169 ? 39.651 6.809   -10.070 1.00 22.74  ?  226 GLN B OE1 1 
ATOM   3430 N NE2 . GLN B 1 169 ? 39.450 4.744   -10.903 1.00 26.19  ?  226 GLN B NE2 1 
ATOM   3431 N N   . THR B 1 170 ? 35.422 6.002   -6.441  1.00 13.76  ?  227 THR B N   1 
ATOM   3432 C CA  . THR B 1 170 ? 34.898 6.569   -5.203  1.00 14.32  ?  227 THR B CA  1 
ATOM   3433 C C   . THR B 1 170 ? 35.663 6.040   -3.995  1.00 14.90  ?  227 THR B C   1 
ATOM   3434 O O   . THR B 1 170 ? 35.973 6.790   -3.072  1.00 14.80  ?  227 THR B O   1 
ATOM   3435 C CB  . THR B 1 170 ? 33.388 6.302   -5.085  1.00 12.65  ?  227 THR B CB  1 
ATOM   3436 O OG1 . THR B 1 170 ? 32.693 6.941   -6.168  1.00 13.54  ?  227 THR B OG1 1 
ATOM   3437 C CG2 . THR B 1 170 ? 32.833 6.915   -3.821  1.00 14.52  ?  227 THR B CG2 1 
ATOM   3438 N N   . MET B 1 171 ? 36.005 4.759   -3.988  1.00 14.12  ?  228 MET B N   1 
ATOM   3439 C CA  . MET B 1 171 ? 36.851 4.221   -2.929  1.00 14.83  ?  228 MET B CA  1 
ATOM   3440 C C   . MET B 1 171 ? 38.185 4.967   -2.860  1.00 16.82  ?  228 MET B C   1 
ATOM   3441 O O   . MET B 1 171 ? 38.683 5.284   -1.765  1.00 17.08  ?  228 MET B O   1 
ATOM   3442 C CB  . MET B 1 171 ? 37.065 2.741   -3.246  1.00 15.80  ?  228 MET B CB  1 
ATOM   3443 C CG  . MET B 1 171 ? 36.017 1.758   -2.717  1.00 17.85  ?  228 MET B CG  1 
ATOM   3444 S SD  . MET B 1 171 ? 35.102 2.048   -1.209  1.00 17.29  ?  228 MET B SD  1 
ATOM   3445 C CE  . MET B 1 171 ? 36.122 0.996   -0.187  1.00 22.41  ?  228 MET B CE  1 
ATOM   3446 N N   . GLN B 1 172 ? 38.786 5.253   -4.022  1.00 15.23  ?  229 GLN B N   1 
ATOM   3447 C CA  . GLN B 1 172 ? 40.052 5.984   -4.027  1.00 17.38  ?  229 GLN B CA  1 
ATOM   3448 C C   . GLN B 1 172 ? 39.873 7.395   -3.480  1.00 19.28  ?  229 GLN B C   1 
ATOM   3449 O O   . GLN B 1 172 ? 40.727 7.894   -2.724  1.00 19.33  ?  229 GLN B O   1 
ATOM   3450 C CB  . GLN B 1 172 ? 40.640 6.011   -5.444  1.00 22.07  ?  229 GLN B CB  1 
ATOM   3451 C CG  . GLN B 1 172 ? 42.080 6.495   -5.497  1.00 24.99  ?  229 GLN B CG  1 
ATOM   3452 C CD  . GLN B 1 172 ? 43.015 5.558   -4.748  1.00 26.97  ?  229 GLN B CD  1 
ATOM   3453 O OE1 . GLN B 1 172 ? 43.264 4.435   -5.187  1.00 37.55  ?  229 GLN B OE1 1 
ATOM   3454 N NE2 . GLN B 1 172 ? 43.507 6.000   -3.597  1.00 28.02  ?  229 GLN B NE2 1 
ATOM   3455 N N   A MET B 1 173 ? 38.765 8.045   -3.852  0.54 17.77  ?  230 MET B N   1 
ATOM   3456 N N   B MET B 1 173 ? 38.783 8.065   -3.860  0.46 17.78  ?  230 MET B N   1 
ATOM   3457 C CA  A MET B 1 173 ? 38.443 9.388   -3.375  0.54 18.31  ?  230 MET B CA  1 
ATOM   3458 C CA  B MET B 1 173 ? 38.511 9.401   -3.335  0.46 18.33  ?  230 MET B CA  1 
ATOM   3459 C C   A MET B 1 173 ? 38.364 9.442   -1.855  0.54 21.21  ?  230 MET B C   1 
ATOM   3460 C C   B MET B 1 173 ? 38.470 9.397   -1.816  0.46 21.43  ?  230 MET B C   1 
ATOM   3461 O O   A MET B 1 173 ? 38.849 10.397  -1.235  0.54 22.01  ?  230 MET B O   1 
ATOM   3462 O O   B MET B 1 173 ? 39.071 10.259  -1.161  0.46 21.68  ?  230 MET B O   1 
ATOM   3463 C CB  A MET B 1 173 ? 37.118 9.828   -4.000  0.54 21.00  ?  230 MET B CB  1 
ATOM   3464 C CB  B MET B 1 173 ? 37.189 9.921   -3.884  0.46 21.18  ?  230 MET B CB  1 
ATOM   3465 C CG  A MET B 1 173 ? 36.662 11.223  -3.657  0.54 25.79  ?  230 MET B CG  1 
ATOM   3466 C CG  B MET B 1 173 ? 36.658 11.120  -3.117  0.46 22.91  ?  230 MET B CG  1 
ATOM   3467 S SD  A MET B 1 173 ? 34.927 11.383  -4.139  0.54 28.17  ?  230 MET B SD  1 
ATOM   3468 S SD  B MET B 1 173 ? 35.002 11.475  -3.692  0.46 28.96  ?  230 MET B SD  1 
ATOM   3469 C CE  A MET B 1 173 ? 34.140 10.362  -2.888  0.54 28.86  ?  230 MET B CE  1 
ATOM   3470 C CE  B MET B 1 173 ? 35.252 11.140  -5.430  0.46 17.71  ?  230 MET B CE  1 
ATOM   3471 N N   . LEU B 1 174 ? 37.776 8.415   -1.238  1.00 17.04  ?  231 LEU B N   1 
ATOM   3472 C CA  . LEU B 1 174 ? 37.593 8.370   0.203   1.00 19.50  ?  231 LEU B CA  1 
ATOM   3473 C C   . LEU B 1 174 ? 38.885 8.086   0.949   1.00 24.46  ?  231 LEU B C   1 
ATOM   3474 O O   . LEU B 1 174 ? 38.906 8.216   2.176   1.00 27.13  ?  231 LEU B O   1 
ATOM   3475 C CB  . LEU B 1 174 ? 36.541 7.322   0.561   1.00 20.34  ?  231 LEU B CB  1 
ATOM   3476 C CG  . LEU B 1 174 ? 35.141 7.618   0.027   1.00 19.75  ?  231 LEU B CG  1 
ATOM   3477 C CD1 . LEU B 1 174 ? 34.211 6.434   0.288   1.00 22.71  ?  231 LEU B CD1 1 
ATOM   3478 C CD2 . LEU B 1 174 ? 34.600 8.884   0.682   1.00 20.92  ?  231 LEU B CD2 1 
ATOM   3479 N N   . ASN B 1 175 ? 39.949 7.688   0.248   1.00 24.82  ?  232 ASN B N   1 
ATOM   3480 C CA  . ASN B 1 175 ? 41.255 7.557   0.879   1.00 25.74  ?  232 ASN B CA  1 
ATOM   3481 C C   . ASN B 1 175 ? 41.950 8.898   1.030   1.00 32.34  ?  232 ASN B C   1 
ATOM   3482 O O   . ASN B 1 175 ? 42.880 9.016   1.838   1.00 34.78  ?  232 ASN B O   1 
ATOM   3483 C CB  . ASN B 1 175 ? 42.150 6.624   0.068   1.00 28.35  ?  232 ASN B CB  1 
ATOM   3484 C CG  . ASN B 1 175 ? 41.842 5.177   0.310   1.00 34.53  ?  232 ASN B CG  1 
ATOM   3485 O OD1 . ASN B 1 175 ? 41.529 4.776   1.430   1.00 49.30  ?  232 ASN B OD1 1 
ATOM   3486 N ND2 . ASN B 1 175 ? 41.955 4.367   -0.737  1.00 43.77  ?  232 ASN B ND2 1 
ATOM   3487 N N   . GLU B 1 176 ? 41.528 9.905   0.270   1.00 31.35  ?  233 GLU B N   1 
ATOM   3488 C CA  . GLU B 1 176 ? 42.228 11.177  0.220   1.00 45.93  ?  233 GLU B CA  1 
ATOM   3489 C C   . GLU B 1 176 ? 41.472 12.305  0.895   1.00 43.44  ?  233 GLU B C   1 
ATOM   3490 O O   . GLU B 1 176 ? 42.057 13.367  1.125   1.00 47.76  ?  233 GLU B O   1 
ATOM   3491 C CB  . GLU B 1 176 ? 42.519 11.582  -1.238  1.00 45.28  ?  233 GLU B CB  1 
ATOM   3492 C CG  . GLU B 1 176 ? 43.589 10.769  -2.000  1.00 55.60  ?  233 GLU B CG  1 
ATOM   3493 C CD  . GLU B 1 176 ? 44.682 10.158  -1.121  1.00 64.08  ?  233 GLU B CD  1 
ATOM   3494 O OE1 . GLU B 1 176 ? 45.264 10.882  -0.277  1.00 52.93  ?  233 GLU B OE1 1 
ATOM   3495 O OE2 . GLU B 1 176 ? 44.978 8.952   -1.301  1.00 63.54  -1 233 GLU B OE2 1 
ATOM   3496 N N   . GLY B 1 177 ? 40.200 12.119  1.209   1.00 35.28  ?  234 GLY B N   1 
ATOM   3497 C CA  . GLY B 1 177 ? 39.427 13.236  1.712   1.00 45.76  ?  234 GLY B CA  1 
ATOM   3498 C C   . GLY B 1 177 ? 37.991 12.828  1.920   1.00 40.19  ?  234 GLY B C   1 
ATOM   3499 O O   . GLY B 1 177 ? 37.602 11.672  1.711   1.00 31.98  ?  234 GLY B O   1 
ATOM   3500 N N   . LEU B 1 178 ? 37.197 13.796  2.359   1.00 27.04  ?  235 LEU B N   1 
ATOM   3501 C CA  . LEU B 1 178 ? 35.800 13.528  2.677   1.00 23.30  ?  235 LEU B CA  1 
ATOM   3502 C C   . LEU B 1 178 ? 34.957 14.645  2.097   1.00 20.68  ?  235 LEU B C   1 
ATOM   3503 O O   . LEU B 1 178 ? 34.770 15.694  2.723   1.00 22.21  ?  235 LEU B O   1 
ATOM   3504 C CB  . LEU B 1 178 ? 35.586 13.390  4.186   1.00 29.99  ?  235 LEU B CB  1 
ATOM   3505 C CG  . LEU B 1 178 ? 34.172 12.927  4.556   1.00 31.50  ?  235 LEU B CG  1 
ATOM   3506 C CD1 . LEU B 1 178 ? 33.910 11.513  4.039   1.00 31.67  ?  235 LEU B CD1 1 
ATOM   3507 C CD2 . LEU B 1 178 ? 33.941 13.012  6.061   1.00 43.23  ?  235 LEU B CD2 1 
ATOM   3508 N N   . PRO B 1 179 ? 34.434 14.459  0.891   1.00 17.06  ?  236 PRO B N   1 
ATOM   3509 C CA  . PRO B 1 179 ? 33.472 15.419  0.359   1.00 17.39  ?  236 PRO B CA  1 
ATOM   3510 C C   . PRO B 1 179 ? 32.134 15.270  1.061   1.00 16.61  ?  236 PRO B C   1 
ATOM   3511 O O   . PRO B 1 179 ? 31.844 14.247  1.694   1.00 16.46  ?  236 PRO B O   1 
ATOM   3512 C CB  . PRO B 1 179 ? 33.352 15.015  -1.111  1.00 18.80  ?  236 PRO B CB  1 
ATOM   3513 C CG  . PRO B 1 179 ? 33.584 13.568  -1.086  1.00 23.38  ?  236 PRO B CG  1 
ATOM   3514 C CD  . PRO B 1 179 ? 34.604 13.298  -0.003  1.00 20.96  ?  236 PRO B CD  1 
ATOM   3515 N N   . THR B 1 180 ? 31.309 16.309  0.931   1.00 16.35  ?  237 THR B N   1 
ATOM   3516 C CA  . THR B 1 180 ? 29.911 16.197  1.313   1.00 15.83  ?  237 THR B CA  1 
ATOM   3517 C C   . THR B 1 180 ? 29.012 15.937  0.114   1.00 12.36  ?  237 THR B C   1 
ATOM   3518 O O   . THR B 1 180 ? 27.844 15.596  0.305   1.00 13.73  ?  237 THR B O   1 
ATOM   3519 C CB  . THR B 1 180 ? 29.428 17.451  2.072   1.00 13.96  ?  237 THR B CB  1 
ATOM   3520 O OG1 . THR B 1 180 ? 29.485 18.614  1.224   1.00 15.63  ?  237 THR B OG1 1 
ATOM   3521 C CG2 . THR B 1 180 ? 30.280 17.702  3.327   1.00 17.73  ?  237 THR B CG2 1 
ATOM   3522 N N   . ALA B 1 181 ? 29.534 16.052  -1.110  1.00 12.76  ?  238 ALA B N   1 
ATOM   3523 C CA  . ALA B 1 181 ? 28.726 15.759  -2.282  1.00 11.85  ?  238 ALA B CA  1 
ATOM   3524 C C   . ALA B 1 181 ? 29.630 15.321  -3.423  1.00 13.89  ?  238 ALA B C   1 
ATOM   3525 O O   . ALA B 1 181 ? 30.795 15.719  -3.501  1.00 14.07  ?  238 ALA B O   1 
ATOM   3526 C CB  . ALA B 1 181 ? 27.888 16.965  -2.723  1.00 12.45  ?  238 ALA B CB  1 
ATOM   3527 N N   . LEU B 1 182 ? 29.083 14.478  -4.294  1.00 13.15  ?  239 LEU B N   1 
ATOM   3528 C CA  . LEU B 1 182 ? 29.791 13.947  -5.456  1.00 11.73  ?  239 LEU B CA  1 
ATOM   3529 C C   . LEU B 1 182 ? 28.926 14.185  -6.689  1.00 11.17  ?  239 LEU B C   1 
ATOM   3530 O O   . LEU B 1 182 ? 27.766 13.739  -6.723  1.00 13.99  ?  239 LEU B O   1 
ATOM   3531 C CB  . LEU B 1 182 ? 30.062 12.453  -5.261  1.00 11.48  ?  239 LEU B CB  1 
ATOM   3532 C CG  . LEU B 1 182 ? 30.822 11.677  -6.303  1.00 20.09  ?  239 LEU B CG  1 
ATOM   3533 C CD1 . LEU B 1 182 ? 32.196 12.289  -6.536  1.00 20.67  ?  239 LEU B CD1 1 
ATOM   3534 C CD2 . LEU B 1 182 ? 30.934 10.238  -5.795  1.00 16.71  ?  239 LEU B CD2 1 
ATOM   3535 N N   . LEU B 1 183 ? 29.497 14.858  -7.701  1.00 11.51  ?  240 LEU B N   1 
ATOM   3536 C CA  . LEU B 1 183 ? 28.893 14.946  -9.034  1.00 11.64  ?  240 LEU B CA  1 
ATOM   3537 C C   . LEU B 1 183 ? 29.496 13.847  -9.897  1.00 10.86  ?  240 LEU B C   1 
ATOM   3538 O O   . LEU B 1 183 ? 30.724 13.732  -9.988  1.00 13.46  ?  240 LEU B O   1 
ATOM   3539 C CB  . LEU B 1 183 ? 29.156 16.313  -9.663  1.00 13.30  ?  240 LEU B CB  1 
ATOM   3540 C CG  . LEU B 1 183 ? 28.420 17.488  -9.031  1.00 13.16  ?  240 LEU B CG  1 
ATOM   3541 C CD1 . LEU B 1 183 ? 29.040 18.804  -9.432  1.00 15.11  ?  240 LEU B CD1 1 
ATOM   3542 C CD2 . LEU B 1 183 ? 26.955 17.461  -9.427  1.00 15.65  ?  240 LEU B CD2 1 
ATOM   3543 N N   . VAL B 1 184 ? 28.639 13.023  -10.509 1.00 11.42  ?  241 VAL B N   1 
ATOM   3544 C CA  . VAL B 1 184 ? 29.098 11.863  -11.274 1.00 13.84  ?  241 VAL B CA  1 
ATOM   3545 C C   . VAL B 1 184 ? 28.644 12.032  -12.715 1.00 12.10  ?  241 VAL B C   1 
ATOM   3546 O O   . VAL B 1 184 ? 27.532 12.499  -12.980 1.00 13.57  ?  241 VAL B O   1 
ATOM   3547 C CB  . VAL B 1 184 ? 28.567 10.546  -10.666 1.00 13.22  ?  241 VAL B CB  1 
ATOM   3548 C CG1 . VAL B 1 184 ? 29.225 9.325   -11.311 1.00 12.85  ?  241 VAL B CG1 1 
ATOM   3549 C CG2 . VAL B 1 184 ? 28.799 10.524  -9.165  1.00 12.09  ?  241 VAL B CG2 1 
ATOM   3550 N N   . ALA B 1 185 ? 29.513 11.666  -13.653 1.00 10.98  ?  242 ALA B N   1 
ATOM   3551 C CA  . ALA B 1 185 ? 29.238 11.977  -15.054 1.00 13.13  ?  242 ALA B CA  1 
ATOM   3552 C C   . ALA B 1 185 ? 28.239 11.036  -15.727 1.00 11.42  ?  242 ALA B C   1 
ATOM   3553 O O   . ALA B 1 185 ? 27.840 11.317  -16.859 1.00 12.68  ?  242 ALA B O   1 
ATOM   3554 C CB  . ALA B 1 185 ? 30.545 11.994  -15.858 1.00 14.10  ?  242 ALA B CB  1 
ATOM   3555 N N   . ASN B 1 186 ? 27.838 9.925   -15.097 1.00 10.95  ?  243 ASN B N   1 
ATOM   3556 C CA  . ASN B 1 186 ? 26.684 9.182   -15.603 1.00 12.61  ?  243 ASN B CA  1 
ATOM   3557 C C   . ASN B 1 186 ? 26.075 8.350   -14.485 1.00 11.13  ?  243 ASN B C   1 
ATOM   3558 O O   . ASN B 1 186 ? 26.610 8.263   -13.369 1.00 11.76  ?  243 ASN B O   1 
ATOM   3559 C CB  . ASN B 1 186 ? 27.035 8.345   -16.864 1.00 12.29  ?  243 ASN B CB  1 
ATOM   3560 C CG  . ASN B 1 186 ? 27.685 7.000   -16.570 1.00 13.36  ?  243 ASN B CG  1 
ATOM   3561 O OD1 . ASN B 1 186 ? 28.254 6.785   -15.514 1.00 12.85  ?  243 ASN B OD1 1 
ATOM   3562 N ND2 . ASN B 1 186 ? 27.627 6.096   -17.547 1.00 12.64  ?  243 ASN B ND2 1 
ATOM   3563 N N   . ASP B 1 187 ? 24.911 7.761   -14.787 1.00 12.13  ?  244 ASP B N   1 
ATOM   3564 C CA  . ASP B 1 187 ? 24.180 7.036   -13.744 1.00 11.37  ?  244 ASP B CA  1 
ATOM   3565 C C   . ASP B 1 187 ? 24.820 5.704   -13.424 1.00 10.85  ?  244 ASP B C   1 
ATOM   3566 O O   . ASP B 1 187 ? 24.740 5.261   -12.282 1.00 11.47  ?  244 ASP B O   1 
ATOM   3567 C CB  . ASP B 1 187 ? 22.727 6.781   -14.138 1.00 13.03  ?  244 ASP B CB  1 
ATOM   3568 C CG  . ASP B 1 187 ? 21.883 8.032   -14.148 1.00 14.43  ?  244 ASP B CG  1 
ATOM   3569 O OD1 . ASP B 1 187 ? 22.361 9.113   -13.767 1.00 13.12  ?  244 ASP B OD1 1 
ATOM   3570 O OD2 . ASP B 1 187 ? 20.715 7.935   -14.574 1.00 13.73  -1 244 ASP B OD2 1 
ATOM   3571 N N   . GLN B 1 188 ? 25.441 5.044   -14.409 1.00 11.31  ?  245 GLN B N   1 
ATOM   3572 C CA  . GLN B 1 188 ? 26.082 3.762   -14.117 1.00 10.41  ?  245 GLN B CA  1 
ATOM   3573 C C   . GLN B 1 188 ? 27.221 3.937   -13.117 1.00 12.35  ?  245 GLN B C   1 
ATOM   3574 O O   . GLN B 1 188 ? 27.292 3.224   -12.104 1.00 12.26  ?  245 GLN B O   1 
ATOM   3575 C CB  . GLN B 1 188 ? 26.572 3.117   -15.405 1.00 13.15  ?  245 GLN B CB  1 
ATOM   3576 C CG  . GLN B 1 188 ? 25.402 2.618   -16.254 1.00 12.12  ?  245 GLN B CG  1 
ATOM   3577 C CD  . GLN B 1 188 ? 25.892 1.854   -17.462 1.00 15.43  ?  245 GLN B CD  1 
ATOM   3578 O OE1 . GLN B 1 188 ? 25.928 2.379   -18.582 1.00 14.47  ?  245 GLN B OE1 1 
ATOM   3579 N NE2 . GLN B 1 188 ? 26.306 0.594   -17.240 1.00 13.47  ?  245 GLN B NE2 1 
ATOM   3580 N N   . MET B 1 189 ? 28.098 4.925   -13.350 1.00 11.44  ?  246 MET B N   1 
ATOM   3581 C CA  . MET B 1 189 ? 29.139 5.191   -12.359 1.00 12.29  ?  246 MET B CA  1 
ATOM   3582 C C   . MET B 1 189 ? 28.536 5.612   -11.028 1.00 10.47  ?  246 MET B C   1 
ATOM   3583 O O   . MET B 1 189 ? 29.069 5.264   -9.967  1.00 12.78  ?  246 MET B O   1 
ATOM   3584 C CB  . MET B 1 189 ? 30.121 6.251   -12.877 1.00 13.08  ?  246 MET B CB  1 
ATOM   3585 C CG  . MET B 1 189 ? 30.920 5.777   -14.080 1.00 11.51  ?  246 MET B CG  1 
ATOM   3586 S SD  . MET B 1 189 ? 32.302 6.903   -14.472 1.00 14.15  ?  246 MET B SD  1 
ATOM   3587 C CE  . MET B 1 189 ? 31.388 8.409   -14.841 1.00 15.09  ?  246 MET B CE  1 
ATOM   3588 N N   . ALA B 1 190 ? 27.408 6.327   -11.048 1.00 11.31  ?  247 ALA B N   1 
ATOM   3589 C CA  . ALA B 1 190 ? 26.789 6.730   -9.785  1.00 10.88  ?  247 ALA B CA  1 
ATOM   3590 C C   . ALA B 1 190 ? 26.321 5.535   -8.968  1.00 10.43  ?  247 ALA B C   1 
ATOM   3591 O O   . ALA B 1 190 ? 26.364 5.572   -7.727  1.00 12.86  ?  247 ALA B O   1 
ATOM   3592 C CB  . ALA B 1 190 ? 25.634 7.699   -10.063 1.00 11.54  ?  247 ALA B CB  1 
ATOM   3593 N N   . LEU B 1 191 ? 25.862 4.473   -9.635  1.00 10.69  ?  248 LEU B N   1 
ATOM   3594 C CA  . LEU B 1 191 ? 25.504 3.257   -8.911  1.00 10.33  ?  248 LEU B CA  1 
ATOM   3595 C C   . LEU B 1 191 ? 26.697 2.720   -8.127  1.00 12.09  ?  248 LEU B C   1 
ATOM   3596 O O   . LEU B 1 191 ? 26.576 2.368   -6.943  1.00 11.63  ?  248 LEU B O   1 
ATOM   3597 C CB  . LEU B 1 191 ? 24.977 2.222   -9.903  1.00 9.65   ?  248 LEU B CB  1 
ATOM   3598 C CG  . LEU B 1 191 ? 24.582 0.872   -9.324  1.00 11.20  ?  248 LEU B CG  1 
ATOM   3599 C CD1 . LEU B 1 191 ? 23.271 0.975   -8.555  1.00 13.81  ?  248 LEU B CD1 1 
ATOM   3600 C CD2 . LEU B 1 191 ? 24.496 -0.150  -10.471 1.00 12.83  ?  248 LEU B CD2 1 
ATOM   3601 N N   . GLY B 1 192 ? 27.867 2.686   -8.765  1.00 11.28  ?  249 GLY B N   1 
ATOM   3602 C CA  . GLY B 1 192 ? 29.062 2.207   -8.092  1.00 11.09  ?  249 GLY B CA  1 
ATOM   3603 C C   . GLY B 1 192 ? 29.479 3.140   -6.973  1.00 11.65  ?  249 GLY B C   1 
ATOM   3604 O O   . GLY B 1 192 ? 29.923 2.680   -5.917  1.00 11.82  ?  249 GLY B O   1 
ATOM   3605 N N   . ALA B 1 193 ? 29.296 4.457   -7.167  1.00 11.37  ?  250 ALA B N   1 
ATOM   3606 C CA  . ALA B 1 193 ? 29.612 5.390   -6.081  1.00 12.51  ?  250 ALA B CA  1 
ATOM   3607 C C   . ALA B 1 193 ? 28.705 5.168   -4.876  1.00 12.24  ?  250 ALA B C   1 
ATOM   3608 O O   . ALA B 1 193 ? 29.179 5.197   -3.728  1.00 12.36  ?  250 ALA B O   1 
ATOM   3609 C CB  . ALA B 1 193 ? 29.508 6.842   -6.577  1.00 12.29  ?  250 ALA B CB  1 
ATOM   3610 N N   . LEU B 1 194 ? 27.399 4.919   -5.102  1.00 11.38  ?  251 LEU B N   1 
ATOM   3611 C CA  . LEU B 1 194 ? 26.511 4.633   -3.980  1.00 10.24  ?  251 LEU B CA  1 
ATOM   3612 C C   . LEU B 1 194 ? 26.989 3.405   -3.213  1.00 11.75  ?  251 LEU B C   1 
ATOM   3613 O O   . LEU B 1 194 ? 26.942 3.369   -1.971  1.00 12.21  ?  251 LEU B O   1 
ATOM   3614 C CB  . LEU B 1 194 ? 25.075 4.430   -4.483  1.00 11.12  ?  251 LEU B CB  1 
ATOM   3615 C CG  . LEU B 1 194 ? 24.352 5.658   -5.028  1.00 10.89  ?  251 LEU B CG  1 
ATOM   3616 C CD1 . LEU B 1 194 ? 22.985 5.244   -5.587  1.00 13.63  ?  251 LEU B CD1 1 
ATOM   3617 C CD2 . LEU B 1 194 ? 24.170 6.741   -3.959  1.00 12.53  ?  251 LEU B CD2 1 
ATOM   3618 N N   . ARG B 1 195 ? 27.424 2.373   -3.932  1.00 11.31  ?  252 ARG B N   1 
ATOM   3619 C CA  . ARG B 1 195 ? 27.899 1.173   -3.260  1.00 11.29  ?  252 ARG B CA  1 
ATOM   3620 C C   . ARG B 1 195 ? 29.131 1.474   -2.419  1.00 11.26  ?  252 ARG B C   1 
ATOM   3621 O O   . ARG B 1 195 ? 29.208 1.077   -1.248  1.00 12.62  ?  252 ARG B O   1 
ATOM   3622 C CB  . ARG B 1 195 ? 28.213 0.071   -4.281  1.00 11.03  ?  252 ARG B CB  1 
ATOM   3623 C CG  . ARG B 1 195 ? 28.826 -1.142  -3.582  1.00 11.96  ?  252 ARG B CG  1 
ATOM   3624 C CD  . ARG B 1 195 ? 29.253 -2.260  -4.547  1.00 13.36  ?  252 ARG B CD  1 
ATOM   3625 N NE  . ARG B 1 195 ? 30.144 -3.165  -3.828  1.00 14.77  ?  252 ARG B NE  1 
ATOM   3626 C CZ  . ARG B 1 195 ? 31.284 -3.627  -4.310  1.00 16.38  ?  252 ARG B CZ  1 
ATOM   3627 N NH1 . ARG B 1 195 ? 31.583 -3.514  -5.597  1.00 15.08  ?  252 ARG B NH1 1 
ATOM   3628 N NH2 . ARG B 1 195 ? 32.168 -4.171  -3.472  1.00 16.17  ?  252 ARG B NH2 1 
ATOM   3629 N N   . ALA B 1 196 ? 30.093 2.202   -2.991  1.00 12.66  ?  253 ALA B N   1 
ATOM   3630 C CA  . ALA B 1 196 ? 31.303 2.546   -2.239  1.00 13.09  ?  253 ALA B CA  1 
ATOM   3631 C C   . ALA B 1 196 ? 30.968 3.333   -0.979  1.00 11.60  ?  253 ALA B C   1 
ATOM   3632 O O   . ALA B 1 196 ? 31.529 3.068   0.101   1.00 14.16  ?  253 ALA B O   1 
ATOM   3633 C CB  . ALA B 1 196 ? 32.261 3.337   -3.130  1.00 15.17  ?  253 ALA B CB  1 
ATOM   3634 N N   . LEU B 1 197 ? 30.057 4.304   -1.092  1.00 13.80  ?  254 LEU B N   1 
ATOM   3635 C CA  . LEU B 1 197 ? 29.680 5.097   0.073   1.00 13.24  ?  254 LEU B CA  1 
ATOM   3636 C C   . LEU B 1 197 ? 29.026 4.226   1.142   1.00 13.37  ?  254 LEU B C   1 
ATOM   3637 O O   . LEU B 1 197 ? 29.398 4.290   2.322   1.00 15.33  ?  254 LEU B O   1 
ATOM   3638 C CB  . LEU B 1 197 ? 28.757 6.249   -0.349  1.00 12.38  ?  254 LEU B CB  1 
ATOM   3639 C CG  . LEU B 1 197 ? 29.497 7.297   -1.179  1.00 13.02  ?  254 LEU B CG  1 
ATOM   3640 C CD1 . LEU B 1 197 ? 28.541 8.205   -1.950  1.00 14.00  ?  254 LEU B CD1 1 
ATOM   3641 C CD2 . LEU B 1 197 ? 30.390 8.131   -0.276  1.00 15.26  ?  254 LEU B CD2 1 
ATOM   3642 N N   . SER B 1 198 ? 28.061 3.391   0.738   1.00 12.80  ?  255 SER B N   1 
ATOM   3643 C CA  . SER B 1 198 ? 27.353 2.509   1.660   1.00 12.43  ?  255 SER B CA  1 
ATOM   3644 C C   . SER B 1 198 ? 28.325 1.581   2.387   1.00 16.05  ?  255 SER B C   1 
ATOM   3645 O O   . SER B 1 198 ? 28.297 1.459   3.625   1.00 18.29  ?  255 SER B O   1 
ATOM   3646 C CB  . SER B 1 198 ? 26.314 1.699   0.872   1.00 14.98  ?  255 SER B CB  1 
ATOM   3647 O OG  . SER B 1 198 ? 25.641 0.768   1.692   1.00 18.51  ?  255 SER B OG  1 
ATOM   3648 N N   . GLU B 1 199 ? 29.219 0.945   1.636   1.00 15.58  ?  256 GLU B N   1 
ATOM   3649 C CA  . GLU B 1 199 ? 30.121 -0.026  2.235   1.00 17.66  ?  256 GLU B CA  1 
ATOM   3650 C C   . GLU B 1 199 ? 31.199 0.648   3.079   1.00 19.13  ?  256 GLU B C   1 
ATOM   3651 O O   . GLU B 1 199 ? 31.771 -0.001  3.960   1.00 23.10  ?  256 GLU B O   1 
ATOM   3652 C CB  . GLU B 1 199 ? 30.704 -0.934  1.138   1.00 19.81  ?  256 GLU B CB  1 
ATOM   3653 C CG  . GLU B 1 199 ? 29.626 -1.827  0.485   1.00 19.35  ?  256 GLU B CG  1 
ATOM   3654 C CD  . GLU B 1 199 ? 30.177 -2.808  -0.541  1.00 18.16  ?  256 GLU B CD  1 
ATOM   3655 O OE1 . GLU B 1 199 ? 31.408 -2.796  -0.809  1.00 20.26  ?  256 GLU B OE1 1 
ATOM   3656 O OE2 . GLU B 1 199 ? 29.357 -3.608  -1.062  1.00 18.40  -1 256 GLU B OE2 1 
ATOM   3657 N N   . SER B 1 200 ? 31.423 1.950   2.901   1.00 17.52  ?  257 SER B N   1 
ATOM   3658 C CA  . SER B 1 200 ? 32.342 2.729   3.725   1.00 15.61  ?  257 SER B CA  1 
ATOM   3659 C C   . SER B 1 200 ? 31.668 3.347   4.945   1.00 19.72  ?  257 SER B C   1 
ATOM   3660 O O   . SER B 1 200 ? 32.322 4.087   5.683   1.00 23.81  ?  257 SER B O   1 
ATOM   3661 C CB  . SER B 1 200 ? 32.997 3.830   2.889   1.00 16.26  ?  257 SER B CB  1 
ATOM   3662 O OG  . SER B 1 200 ? 33.687 3.249   1.782   1.00 19.83  ?  257 SER B OG  1 
ATOM   3663 N N   . GLY B 1 201 ? 30.390 3.064   5.173   1.00 19.81  ?  258 GLY B N   1 
ATOM   3664 C CA  . GLY B 1 201 ? 29.696 3.598   6.327   1.00 16.91  ?  258 GLY B CA  1 
ATOM   3665 C C   . GLY B 1 201 ? 29.243 5.037   6.207   1.00 18.80  ?  258 GLY B C   1 
ATOM   3666 O O   . GLY B 1 201 ? 28.945 5.660   7.228   1.00 19.67  ?  258 GLY B O   1 
ATOM   3667 N N   . LEU B 1 202 ? 29.190 5.586   5.004   1.00 16.58  ?  259 LEU B N   1 
ATOM   3668 C CA  . LEU B 1 202 ? 28.704 6.946   4.769   1.00 15.05  ?  259 LEU B CA  1 
ATOM   3669 C C   . LEU B 1 202 ? 27.284 6.879   4.226   1.00 16.73  ?  259 LEU B C   1 
ATOM   3670 O O   . LEU B 1 202 ? 27.067 6.377   3.119   1.00 20.80  ?  259 LEU B O   1 
ATOM   3671 C CB  . LEU B 1 202 ? 29.612 7.683   3.781   1.00 14.00  ?  259 LEU B CB  1 
ATOM   3672 C CG  . LEU B 1 202 ? 30.966 8.008   4.421   1.00 15.20  ?  259 LEU B CG  1 
ATOM   3673 C CD1 . LEU B 1 202 ? 31.998 8.251   3.341   1.00 19.90  ?  259 LEU B CD1 1 
ATOM   3674 C CD2 . LEU B 1 202 ? 30.842 9.218   5.383   1.00 18.37  ?  259 LEU B CD2 1 
ATOM   3675 N N   . ARG B 1 203 ? 26.337 7.440   4.972   1.00 16.40  ?  260 ARG B N   1 
ATOM   3676 C CA  . ARG B 1 203 ? 24.937 7.397   4.575   1.00 14.79  ?  260 ARG B CA  1 
ATOM   3677 C C   . ARG B 1 203 ? 24.641 8.436   3.493   1.00 16.23  ?  260 ARG B C   1 
ATOM   3678 O O   . ARG B 1 203 ? 25.107 9.578   3.566   1.00 15.90  ?  260 ARG B O   1 
ATOM   3679 C CB  . ARG B 1 203 ? 24.051 7.616   5.802   1.00 14.72  ?  260 ARG B CB  1 
ATOM   3680 C CG  . ARG B 1 203 ? 24.085 6.439   6.751   1.00 20.56  ?  260 ARG B CG  1 
ATOM   3681 C CD  . ARG B 1 203 ? 23.404 6.753   8.078   1.00 25.26  ?  260 ARG B CD  1 
ATOM   3682 N NE  . ARG B 1 203 ? 24.273 7.533   8.950   1.00 29.24  ?  260 ARG B NE  1 
ATOM   3683 C CZ  . ARG B 1 203 ? 24.042 8.785   9.320   1.00 27.78  ?  260 ARG B CZ  1 
ATOM   3684 N NH1 . ARG B 1 203 ? 22.932 9.420   8.969   1.00 30.49  ?  260 ARG B NH1 1 
ATOM   3685 N NH2 . ARG B 1 203 ? 24.940 9.412   10.077  1.00 30.53  ?  260 ARG B NH2 1 
ATOM   3686 N N   . VAL B 1 204 ? 23.902 8.015   2.472   1.00 13.42  ?  261 VAL B N   1 
ATOM   3687 C CA  . VAL B 1 204 ? 23.447 8.859   1.371   1.00 12.71  ?  261 VAL B CA  1 
ATOM   3688 C C   . VAL B 1 204 ? 21.943 9.065   1.530   1.00 13.98  ?  261 VAL B C   1 
ATOM   3689 O O   . VAL B 1 204 ? 21.188 8.080   1.541   1.00 15.10  ?  261 VAL B O   1 
ATOM   3690 C CB  . VAL B 1 204 ? 23.768 8.221   0.012   1.00 12.83  ?  261 VAL B CB  1 
ATOM   3691 C CG1 . VAL B 1 204 ? 23.152 9.044   -1.114  1.00 11.71  ?  261 VAL B CG1 1 
ATOM   3692 C CG2 . VAL B 1 204 ? 25.283 8.109   -0.186  1.00 13.59  ?  261 VAL B CG2 1 
ATOM   3693 N N   . PRO B 1 205 ? 21.450 10.320  1.585   1.00 13.52  ?  262 PRO B N   1 
ATOM   3694 C CA  . PRO B 1 205 ? 22.218 11.566  1.408   1.00 12.09  ?  262 PRO B CA  1 
ATOM   3695 C C   . PRO B 1 205 ? 22.599 12.284  2.688   1.00 16.02  ?  262 PRO B C   1 
ATOM   3696 O O   . PRO B 1 205 ? 23.127 13.400  2.617   1.00 15.71  ?  262 PRO B O   1 
ATOM   3697 C CB  . PRO B 1 205 ? 21.250 12.428  0.576   1.00 13.44  ?  262 PRO B CB  1 
ATOM   3698 C CG  . PRO B 1 205 ? 19.905 12.069  1.159   1.00 16.49  ?  262 PRO B CG  1 
ATOM   3699 C CD  . PRO B 1 205 ? 19.999 10.564  1.480   1.00 15.52  ?  262 PRO B CD  1 
ATOM   3700 N N   . ALA B 1 206 ? 22.360 11.695  3.853   1.00 14.39  ?  263 ALA B N   1 
ATOM   3701 C CA  . ALA B 1 206 ? 22.567 12.440  5.091   1.00 15.04  ?  263 ALA B CA  1 
ATOM   3702 C C   . ALA B 1 206 ? 24.018 12.883  5.258   1.00 17.37  ?  263 ALA B C   1 
ATOM   3703 O O   . ALA B 1 206 ? 24.276 13.988  5.764   1.00 18.14  ?  263 ALA B O   1 
ATOM   3704 C CB  . ALA B 1 206 ? 22.119 11.603  6.286   1.00 16.03  ?  263 ALA B CB  1 
ATOM   3705 N N   . GLN B 1 207 ? 24.981 12.034  4.876   1.00 14.34  ?  264 GLN B N   1 
ATOM   3706 C CA  . GLN B 1 207 ? 26.392 12.373  5.028   1.00 15.25  ?  264 GLN B CA  1 
ATOM   3707 C C   . GLN B 1 207 ? 27.067 12.747  3.723   1.00 14.98  ?  264 GLN B C   1 
ATOM   3708 O O   . GLN B 1 207 ? 27.965 13.592  3.738   1.00 15.24  ?  264 GLN B O   1 
ATOM   3709 C CB  . GLN B 1 207 ? 27.154 11.212  5.695   1.00 13.76  ?  264 GLN B CB  1 
ATOM   3710 C CG  . GLN B 1 207 ? 26.606 10.916  7.103   1.00 16.58  ?  264 GLN B CG  1 
ATOM   3711 C CD  . GLN B 1 207 ? 27.309 9.773   7.798   1.00 21.34  ?  264 GLN B CD  1 
ATOM   3712 O OE1 . GLN B 1 207 ? 27.231 8.636   7.351   1.00 19.86  ?  264 GLN B OE1 1 
ATOM   3713 N NE2 . GLN B 1 207 ? 28.006 10.070  8.893   1.00 23.11  ?  264 GLN B NE2 1 
ATOM   3714 N N   . VAL B 1 208 ? 26.652 12.156  2.598   1.00 14.53  ?  265 VAL B N   1 
ATOM   3715 C CA  . VAL B 1 208 ? 27.165 12.494  1.275   1.00 12.42  ?  265 VAL B CA  1 
ATOM   3716 C C   . VAL B 1 208 ? 26.008 12.499  0.288   1.00 13.52  ?  265 VAL B C   1 
ATOM   3717 O O   . VAL B 1 208 ? 25.253 11.523  0.210   1.00 14.11  ?  265 VAL B O   1 
ATOM   3718 C CB  . VAL B 1 208 ? 28.257 11.510  0.795   1.00 11.34  ?  265 VAL B CB  1 
ATOM   3719 C CG1 . VAL B 1 208 ? 28.737 11.906  -0.602  1.00 14.47  ?  265 VAL B CG1 1 
ATOM   3720 C CG2 . VAL B 1 208 ? 29.426 11.462  1.807   1.00 14.35  ?  265 VAL B CG2 1 
ATOM   3721 N N   . SER B 1 209 ? 25.872 13.584  -0.473  1.00 12.39  ?  266 SER B N   1 
ATOM   3722 C CA  . SER B 1 209 ? 24.918 13.689  -1.584  1.00 10.77  ?  266 SER B CA  1 
ATOM   3723 C C   . SER B 1 209 ? 25.569 13.211  -2.884  1.00 13.33  ?  266 SER B C   1 
ATOM   3724 O O   . SER B 1 209 ? 26.777 13.355  -3.077  1.00 12.86  ?  266 SER B O   1 
ATOM   3725 C CB  . SER B 1 209 ? 24.430 15.128  -1.757  1.00 11.14  ?  266 SER B CB  1 
ATOM   3726 O OG  . SER B 1 209 ? 23.592 15.527  -0.693  1.00 12.91  ?  266 SER B OG  1 
ATOM   3727 N N   . VAL B 1 210 ? 24.748 12.664  -3.788  1.00 11.67  ?  267 VAL B N   1 
ATOM   3728 C CA  . VAL B 1 210 ? 25.237 12.147  -5.072  1.00 10.37  ?  267 VAL B CA  1 
ATOM   3729 C C   . VAL B 1 210 ? 24.278 12.585  -6.172  1.00 12.29  ?  267 VAL B C   1 
ATOM   3730 O O   . VAL B 1 210 ? 23.063 12.444  -6.027  1.00 13.37  ?  267 VAL B O   1 
ATOM   3731 C CB  . VAL B 1 210 ? 25.345 10.605  -5.062  1.00 10.72  ?  267 VAL B CB  1 
ATOM   3732 C CG1 . VAL B 1 210 ? 25.868 10.088  -6.408  1.00 13.29  ?  267 VAL B CG1 1 
ATOM   3733 C CG2 . VAL B 1 210 ? 26.255 10.094  -3.953  1.00 12.25  ?  267 VAL B CG2 1 
ATOM   3734 N N   . VAL B 1 211 ? 24.818 13.117  -7.269  1.00 11.34  ?  268 VAL B N   1 
ATOM   3735 C CA  . VAL B 1 211 ? 24.035 13.460  -8.462  1.00 10.03  ?  268 VAL B CA  1 
ATOM   3736 C C   . VAL B 1 211 ? 24.620 12.694  -9.644  1.00 11.64  ?  268 VAL B C   1 
ATOM   3737 O O   . VAL B 1 211 ? 25.832 12.722  -9.853  1.00 12.79  ?  268 VAL B O   1 
ATOM   3738 C CB  . VAL B 1 211 ? 24.064 14.976  -8.736  1.00 11.62  ?  268 VAL B CB  1 
ATOM   3739 C CG1 . VAL B 1 211 ? 23.189 15.333  -9.931  1.00 13.37  ?  268 VAL B CG1 1 
ATOM   3740 C CG2 . VAL B 1 211 ? 23.596 15.747  -7.500  1.00 14.73  ?  268 VAL B CG2 1 
ATOM   3741 N N   . GLY B 1 212 ? 23.754 12.008  -10.399 1.00 11.29  ?  269 GLY B N   1 
ATOM   3742 C CA  . GLY B 1 212 ? 24.147 11.299  -11.599 1.00 13.33  ?  269 GLY B CA  1 
ATOM   3743 C C   . GLY B 1 212 ? 23.906 12.119  -12.854 1.00 10.58  ?  269 GLY B C   1 
ATOM   3744 O O   . GLY B 1 212 ? 23.682 13.326  -12.821 1.00 13.24  ?  269 GLY B O   1 
ATOM   3745 N N   . TYR B 1 213 ? 23.984 11.435  -13.997 1.00 11.96  ?  270 TYR B N   1 
ATOM   3746 C CA  . TYR B 1 213 ? 23.783 12.090  -15.288 1.00 12.39  ?  270 TYR B CA  1 
ATOM   3747 C C   . TYR B 1 213 ? 23.263 11.052  -16.270 1.00 14.10  ?  270 TYR B C   1 
ATOM   3748 O O   . TYR B 1 213 ? 23.934 10.033  -16.482 1.00 13.83  ?  270 TYR B O   1 
ATOM   3749 C CB  . TYR B 1 213 ? 25.096 12.697  -15.789 1.00 12.54  ?  270 TYR B CB  1 
ATOM   3750 C CG  . TYR B 1 213 ? 25.003 13.879  -16.718 1.00 12.84  ?  270 TYR B CG  1 
ATOM   3751 C CD1 . TYR B 1 213 ? 24.551 13.736  -18.027 1.00 15.11  ?  270 TYR B CD1 1 
ATOM   3752 C CD2 . TYR B 1 213 ? 25.477 15.114  -16.310 1.00 15.59  ?  270 TYR B CD2 1 
ATOM   3753 C CE1 . TYR B 1 213 ? 24.506 14.830  -18.885 1.00 18.14  ?  270 TYR B CE1 1 
ATOM   3754 C CE2 . TYR B 1 213 ? 25.451 16.198  -17.156 1.00 17.00  ?  270 TYR B CE2 1 
ATOM   3755 C CZ  . TYR B 1 213 ? 24.968 16.056  -18.429 1.00 19.19  ?  270 TYR B CZ  1 
ATOM   3756 O OH  . TYR B 1 213 ? 24.962 17.161  -19.252 1.00 19.36  ?  270 TYR B OH  1 
ATOM   3757 N N   . ASP B 1 214 ? 22.066 11.308  -16.836 1.00 12.80  ?  271 ASP B N   1 
ATOM   3758 C CA  . ASP B 1 214 ? 21.410 10.607  -17.952 1.00 13.56  ?  271 ASP B CA  1 
ATOM   3759 C C   . ASP B 1 214 ? 19.936 10.384  -17.640 1.00 13.38  ?  271 ASP B C   1 
ATOM   3760 O O   . ASP B 1 214 ? 19.080 10.533  -18.519 1.00 15.37  ?  271 ASP B O   1 
ATOM   3761 C CB  . ASP B 1 214 ? 21.992 9.209   -18.257 1.00 12.39  ?  271 ASP B CB  1 
ATOM   3762 C CG  . ASP B 1 214 ? 23.284 9.255   -19.076 1.00 16.09  ?  271 ASP B CG  1 
ATOM   3763 O OD1 . ASP B 1 214 ? 23.566 10.283  -19.724 1.00 17.35  -1 271 ASP B OD1 1 
ATOM   3764 O OD2 . ASP B 1 214 ? 24.026 8.255   -19.072 1.00 14.20  ?  271 ASP B OD2 1 
ATOM   3765 N N   . ASP B 1 215 ? 19.652 9.967   -16.407 1.00 14.16  ?  272 ASP B N   1 
ATOM   3766 C CA  . ASP B 1 215 ? 18.387 9.327   -16.041 1.00 13.38  ?  272 ASP B CA  1 
ATOM   3767 C C   . ASP B 1 215 ? 18.079 8.130   -16.949 1.00 13.26  ?  272 ASP B C   1 
ATOM   3768 O O   . ASP B 1 215 ? 17.005 8.010   -17.560 1.00 17.24  ?  272 ASP B O   1 
ATOM   3769 C CB  . ASP B 1 215 ? 17.228 10.324  -16.030 1.00 14.89  ?  272 ASP B CB  1 
ATOM   3770 C CG  . ASP B 1 215 ? 16.034 9.800   -15.238 1.00 18.11  ?  272 ASP B CG  1 
ATOM   3771 O OD1 . ASP B 1 215 ? 16.245 8.988   -14.304 1.00 17.83  ?  272 ASP B OD1 1 
ATOM   3772 O OD2 . ASP B 1 215 ? 14.898 10.206  -15.533 1.00 21.60  -1 272 ASP B OD2 1 
ATOM   3773 N N   . THR B 1 216 ? 19.037 7.198   -16.993 1.00 13.11  ?  273 THR B N   1 
ATOM   3774 C CA  . THR B 1 216 ? 18.741 5.922   -17.633 1.00 12.82  ?  273 THR B CA  1 
ATOM   3775 C C   . THR B 1 216 ? 17.723 5.146   -16.784 1.00 11.64  ?  273 THR B C   1 
ATOM   3776 O O   . THR B 1 216 ? 17.483 5.463   -15.620 1.00 13.77  ?  273 THR B O   1 
ATOM   3777 C CB  . THR B 1 216 ? 20.031 5.120   -17.907 1.00 12.76  ?  273 THR B CB  1 
ATOM   3778 O OG1 . THR B 1 216 ? 21.014 5.281   -16.875 1.00 13.68  ?  273 THR B OG1 1 
ATOM   3779 C CG2 . THR B 1 216 ? 20.667 5.631   -19.208 1.00 15.25  ?  273 THR B CG2 1 
ATOM   3780 N N   . GLU B 1 217 ? 17.060 4.173   -17.424 1.00 13.04  ?  274 GLU B N   1 
ATOM   3781 C CA  . GLU B 1 217 ? 15.811 3.625   -16.889 1.00 13.16  ?  274 GLU B CA  1 
ATOM   3782 C C   . GLU B 1 217 ? 15.924 3.094   -15.458 1.00 13.51  ?  274 GLU B C   1 
ATOM   3783 O O   . GLU B 1 217 ? 14.998 3.298   -14.653 1.00 15.27  ?  274 GLU B O   1 
ATOM   3784 C CB  . GLU B 1 217 ? 15.291 2.524   -17.811 1.00 17.44  ?  274 GLU B CB  1 
ATOM   3785 C CG  . GLU B 1 217 ? 13.786 2.262   -17.696 1.00 17.57  ?  274 GLU B CG  1 
ATOM   3786 C CD  . GLU B 1 217 ? 12.941 3.266   -18.481 1.00 30.99  ?  274 GLU B CD  1 
ATOM   3787 O OE1 . GLU B 1 217 ? 13.233 3.519   -19.671 1.00 28.39  ?  274 GLU B OE1 1 
ATOM   3788 O OE2 . GLU B 1 217 ? 11.984 3.821   -17.895 1.00 32.67  -1 274 GLU B OE2 1 
ATOM   3789 N N   . ASP B 1 218 ? 16.999 2.364   -15.142 1.00 14.13  ?  275 ASP B N   1 
ATOM   3790 C CA  . ASP B 1 218 ? 17.124 1.743   -13.824 1.00 14.91  ?  275 ASP B CA  1 
ATOM   3791 C C   . ASP B 1 218 ? 17.238 2.752   -12.685 1.00 16.35  ?  275 ASP B C   1 
ATOM   3792 O O   . ASP B 1 218 ? 16.997 2.371   -11.534 1.00 12.97  ?  275 ASP B O   1 
ATOM   3793 C CB  . ASP B 1 218 ? 18.380 0.864   -13.702 1.00 13.29  ?  275 ASP B CB  1 
ATOM   3794 C CG  . ASP B 1 218 ? 18.399 -0.382  -14.578 1.00 16.62  ?  275 ASP B CG  1 
ATOM   3795 O OD1 . ASP B 1 218 ? 17.370 -0.928  -15.010 1.00 15.17  ?  275 ASP B OD1 1 
ATOM   3796 O OD2 . ASP B 1 218 ? 19.540 -0.902  -14.761 1.00 16.86  -1 275 ASP B OD2 1 
ATOM   3797 N N   . SER B 1 219 ? 17.656 4.001   -12.957 1.00 12.61  ?  276 SER B N   1 
ATOM   3798 C CA  . SER B 1 219 ? 18.119 4.885   -11.879 1.00 13.31  ?  276 SER B CA  1 
ATOM   3799 C C   . SER B 1 219 ? 17.029 5.234   -10.875 1.00 14.83  ?  276 SER B C   1 
ATOM   3800 O O   . SER B 1 219 ? 17.335 5.436   -9.693  1.00 13.92  ?  276 SER B O   1 
ATOM   3801 C CB  . SER B 1 219 ? 18.727 6.165   -12.450 1.00 15.05  ?  276 SER B CB  1 
ATOM   3802 O OG  . SER B 1 219 ? 19.740 5.777   -13.358 1.00 13.92  ?  276 SER B OG  1 
ATOM   3803 N N   . ALA B 1 220 ? 15.768 5.289   -11.302 1.00 13.07  ?  277 ALA B N   1 
ATOM   3804 C CA  . ALA B 1 220 ? 14.684 5.520   -10.345 1.00 13.19  ?  277 ALA B CA  1 
ATOM   3805 C C   . ALA B 1 220 ? 14.560 4.392   -9.334  1.00 15.30  ?  277 ALA B C   1 
ATOM   3806 O O   . ALA B 1 220 ? 13.838 4.543   -8.339  1.00 14.38  ?  277 ALA B O   1 
ATOM   3807 C CB  . ALA B 1 220 ? 13.362 5.686   -11.076 1.00 16.20  ?  277 ALA B CB  1 
ATOM   3808 N N   . CYS B 1 221 ? 15.213 3.254   -9.576  1.00 13.06  ?  278 CYS B N   1 
ATOM   3809 C CA  . CYS B 1 221 ? 15.154 2.137   -8.650  1.00 14.10  ?  278 CYS B CA  1 
ATOM   3810 C C   . CYS B 1 221 ? 16.483 1.841   -7.968  1.00 11.54  ?  278 CYS B C   1 
ATOM   3811 O O   . CYS B 1 221 ? 16.604 0.776   -7.340  1.00 12.77  ?  278 CYS B O   1 
ATOM   3812 C CB  . CYS B 1 221 ? 14.641 0.888   -9.378  1.00 14.27  ?  278 CYS B CB  1 
ATOM   3813 S SG  . CYS B 1 221 ? 12.894 0.941   -9.764  1.00 16.60  ?  278 CYS B SG  1 
ATOM   3814 N N   . PHE B 1 222 ? 17.473 2.746   -8.048  1.00 13.90  ?  279 PHE B N   1 
ATOM   3815 C CA  . PHE B 1 222 ? 18.663 2.617   -7.210  1.00 12.44  ?  279 PHE B CA  1 
ATOM   3816 C C   . PHE B 1 222 ? 18.273 2.783   -5.731  1.00 13.39  ?  279 PHE B C   1 
ATOM   3817 O O   . PHE B 1 222 ? 17.165 3.226   -5.398  1.00 14.83  ?  279 PHE B O   1 
ATOM   3818 C CB  . PHE B 1 222 ? 19.699 3.680   -7.585  1.00 10.90  ?  279 PHE B CB  1 
ATOM   3819 C CG  . PHE B 1 222 ? 20.350 3.493   -8.945  1.00 11.56  ?  279 PHE B CG  1 
ATOM   3820 C CD1 . PHE B 1 222 ? 20.024 2.442   -9.806  1.00 12.06  ?  279 PHE B CD1 1 
ATOM   3821 C CD2 . PHE B 1 222 ? 21.350 4.397   -9.337  1.00 12.44  ?  279 PHE B CD2 1 
ATOM   3822 C CE1 . PHE B 1 222 ? 20.684 2.314   -11.044 1.00 15.83  ?  279 PHE B CE1 1 
ATOM   3823 C CE2 . PHE B 1 222 ? 22.001 4.266   -10.582 1.00 14.38  ?  279 PHE B CE2 1 
ATOM   3824 C CZ  . PHE B 1 222 ? 21.651 3.229   -11.437 1.00 11.82  ?  279 PHE B CZ  1 
ATOM   3825 N N   . ILE B 1 223 ? 19.176 2.391   -4.829  1.00 12.98  ?  280 ILE B N   1 
ATOM   3826 C CA  . ILE B 1 223 ? 18.972 2.626   -3.406  1.00 12.81  ?  280 ILE B CA  1 
ATOM   3827 C C   . ILE B 1 223 ? 20.004 3.661   -2.953  1.00 11.63  ?  280 ILE B C   1 
ATOM   3828 O O   . ILE B 1 223 ? 21.204 3.347   -2.883  1.00 14.77  ?  280 ILE B O   1 
ATOM   3829 C CB  . ILE B 1 223 ? 19.109 1.342   -2.583  1.00 16.69  ?  280 ILE B CB  1 
ATOM   3830 C CG1 . ILE B 1 223 ? 18.013 0.317   -2.873  1.00 16.34  ?  280 ILE B CG1 1 
ATOM   3831 C CG2 . ILE B 1 223 ? 19.045 1.677   -1.115  1.00 15.42  ?  280 ILE B CG2 1 
ATOM   3832 C CD1 . ILE B 1 223 ? 18.363 -1.070  -2.286  1.00 17.00  ?  280 ILE B CD1 1 
ATOM   3833 N N   . PRO B 1 224 ? 19.601 4.897   -2.648  1.00 12.84  ?  281 PRO B N   1 
ATOM   3834 C CA  . PRO B 1 224 ? 18.259 5.452   -2.840  1.00 13.84  ?  281 PRO B CA  1 
ATOM   3835 C C   . PRO B 1 224 ? 18.021 5.839   -4.281  1.00 12.98  ?  281 PRO B C   1 
ATOM   3836 O O   . PRO B 1 224 ? 18.961 5.930   -5.059  1.00 13.67  ?  281 PRO B O   1 
ATOM   3837 C CB  . PRO B 1 224 ? 18.255 6.695   -1.924  1.00 16.75  ?  281 PRO B CB  1 
ATOM   3838 C CG  . PRO B 1 224 ? 19.671 6.820   -1.349  1.00 16.02  ?  281 PRO B CG  1 
ATOM   3839 C CD  . PRO B 1 224 ? 20.545 5.894   -2.119  1.00 13.28  ?  281 PRO B CD  1 
ATOM   3840 N N   . PRO B 1 225 ? 16.770 6.081   -4.658  1.00 13.76  ?  282 PRO B N   1 
ATOM   3841 C CA  . PRO B 1 225 ? 16.493 6.532   -6.031  1.00 13.46  ?  282 PRO B CA  1 
ATOM   3842 C C   . PRO B 1 225 ? 17.322 7.762   -6.393  1.00 15.06  ?  282 PRO B C   1 
ATOM   3843 O O   . PRO B 1 225 ? 17.456 8.705   -5.610  1.00 13.16  ?  282 PRO B O   1 
ATOM   3844 C CB  . PRO B 1 225 ? 14.991 6.823   -5.996  1.00 13.55  ?  282 PRO B CB  1 
ATOM   3845 C CG  . PRO B 1 225 ? 14.466 5.775   -5.039  1.00 13.15  ?  282 PRO B CG  1 
ATOM   3846 C CD  . PRO B 1 225 ? 15.536 5.677   -3.959  1.00 13.56  ?  282 PRO B CD  1 
ATOM   3847 N N   . LEU B 1 226 ? 17.872 7.769   -7.607  1.00 11.32  ?  283 LEU B N   1 
ATOM   3848 C CA  . LEU B 1 226 ? 18.987 8.649   -7.939  1.00 11.08  ?  283 LEU B CA  1 
ATOM   3849 C C   . LEU B 1 226 ? 18.539 10.019  -8.447  1.00 13.53  ?  283 LEU B C   1 
ATOM   3850 O O   . LEU B 1 226 ? 17.787 10.117  -9.414  1.00 14.09  ?  283 LEU B O   1 
ATOM   3851 C CB  . LEU B 1 226 ? 19.887 7.990   -8.997  1.00 13.28  ?  283 LEU B CB  1 
ATOM   3852 C CG  . LEU B 1 226 ? 21.149 8.778   -9.362  1.00 12.22  ?  283 LEU B CG  1 
ATOM   3853 C CD1 . LEU B 1 226 ? 22.140 8.910   -8.229  1.00 15.36  ?  283 LEU B CD1 1 
ATOM   3854 C CD2 . LEU B 1 226 ? 21.830 8.118   -10.555 1.00 13.38  ?  283 LEU B CD2 1 
ATOM   3855 N N   . THR B 1 227 ? 19.032 11.075  -7.797  1.00 12.71  ?  284 THR B N   1 
ATOM   3856 C CA  . THR B 1 227 ? 18.896 12.432  -8.330  1.00 12.43  ?  284 THR B CA  1 
ATOM   3857 C C   . THR B 1 227 ? 19.901 12.594  -9.468  1.00 12.36  ?  284 THR B C   1 
ATOM   3858 O O   . THR B 1 227 ? 21.071 12.213  -9.330  1.00 11.94  ?  284 THR B O   1 
ATOM   3859 C CB  . THR B 1 227 ? 19.148 13.460  -7.218  1.00 13.39  ?  284 THR B CB  1 
ATOM   3860 O OG1 . THR B 1 227 ? 18.119 13.301  -6.230  1.00 14.60  ?  284 THR B OG1 1 
ATOM   3861 C CG2 . THR B 1 227 ? 19.132 14.915  -7.757  1.00 12.28  ?  284 THR B CG2 1 
ATOM   3862 N N   . THR B 1 228 ? 19.442 13.125  -10.608 1.00 12.99  ?  285 THR B N   1 
ATOM   3863 C CA  . THR B 1 228 ? 20.263 13.013  -11.808 1.00 11.65  ?  285 THR B CA  1 
ATOM   3864 C C   . THR B 1 228 ? 19.835 14.042  -12.844 1.00 12.14  ?  285 THR B C   1 
ATOM   3865 O O   . THR B 1 228 ? 18.733 14.577  -12.788 1.00 15.70  ?  285 THR B O   1 
ATOM   3866 C CB  . THR B 1 228 ? 20.171 11.585  -12.371 1.00 16.30  ?  285 THR B CB  1 
ATOM   3867 O OG1 . THR B 1 228 ? 21.027 11.455  -13.512 1.00 14.79  ?  285 THR B OG1 1 
ATOM   3868 C CG2 . THR B 1 228 ? 18.715 11.236  -12.726 1.00 13.86  ?  285 THR B CG2 1 
ATOM   3869 N N   . ILE B 1 229 ? 20.748 14.332  -13.773 1.00 12.83  ?  286 ILE B N   1 
ATOM   3870 C CA  . ILE B 1 229 ? 20.439 15.160  -14.939 1.00 13.88  ?  286 ILE B CA  1 
ATOM   3871 C C   . ILE B 1 229 ? 19.778 14.298  -16.008 1.00 13.67  ?  286 ILE B C   1 
ATOM   3872 O O   . ILE B 1 229 ? 20.426 13.410  -16.578 1.00 16.72  ?  286 ILE B O   1 
ATOM   3873 C CB  . ILE B 1 229 ? 21.707 15.803  -15.511 1.00 14.07  ?  286 ILE B CB  1 
ATOM   3874 C CG1 . ILE B 1 229 ? 22.471 16.637  -14.477 1.00 13.73  ?  286 ILE B CG1 1 
ATOM   3875 C CG2 . ILE B 1 229 ? 21.361 16.626  -16.762 1.00 17.15  ?  286 ILE B CG2 1 
ATOM   3876 C CD1 . ILE B 1 229 ? 21.625 17.713  -13.744 1.00 17.00  ?  286 ILE B CD1 1 
ATOM   3877 N N   . LYS B 1 230 ? 18.523 14.601  -16.341 1.00 14.78  ?  287 LYS B N   1 
ATOM   3878 C CA  . LYS B 1 230 ? 17.810 13.782  -17.318 1.00 15.88  ?  287 LYS B CA  1 
ATOM   3879 C C   . LYS B 1 230 ? 18.150 14.258  -18.720 1.00 17.36  ?  287 LYS B C   1 
ATOM   3880 O O   . LYS B 1 230 ? 17.992 15.447  -19.030 1.00 18.17  ?  287 LYS B O   1 
ATOM   3881 C CB  . LYS B 1 230 ? 16.300 13.835  -17.107 1.00 18.24  ?  287 LYS B CB  1 
ATOM   3882 C CG  . LYS B 1 230 ? 15.533 13.161  -18.260 1.00 17.96  ?  287 LYS B CG  1 
ATOM   3883 C CD  . LYS B 1 230 ? 14.083 12.970  -17.912 1.00 22.27  ?  287 LYS B CD  1 
ATOM   3884 C CE  . LYS B 1 230 ? 13.453 11.930  -18.838 1.00 22.40  ?  287 LYS B CE  1 
ATOM   3885 N NZ  . LYS B 1 230 ? 14.031 10.537  -18.597 1.00 27.49  ?  287 LYS B NZ  1 
ATOM   3886 N N   . GLN B 1 231 ? 18.641 13.334  -19.549 1.00 17.10  ?  288 GLN B N   1 
ATOM   3887 C CA  . GLN B 1 231 ? 18.723 13.508  -20.998 1.00 16.20  ?  288 GLN B CA  1 
ATOM   3888 C C   . GLN B 1 231 ? 17.575 12.680  -21.564 1.00 14.45  ?  288 GLN B C   1 
ATOM   3889 O O   . GLN B 1 231 ? 17.589 11.451  -21.450 1.00 19.95  ?  288 GLN B O   1 
ATOM   3890 C CB  . GLN B 1 231 ? 20.065 13.020  -21.538 1.00 19.28  ?  288 GLN B CB  1 
ATOM   3891 C CG  . GLN B 1 231 ? 21.266 13.780  -20.960 1.00 23.91  ?  288 GLN B CG  1 
ATOM   3892 C CD  . GLN B 1 231 ? 22.537 13.529  -21.720 1.00 27.90  ?  288 GLN B CD  1 
ATOM   3893 O OE1 . GLN B 1 231 ? 23.093 14.449  -22.324 1.00 32.41  ?  288 GLN B OE1 1 
ATOM   3894 N NE2 . GLN B 1 231 ? 23.014 12.280  -21.712 1.00 23.56  ?  288 GLN B NE2 1 
ATOM   3895 N N   . ASP B 1 232 ? 16.561 13.340  -22.111 1.00 16.94  ?  289 ASP B N   1 
ATOM   3896 C CA  . ASP B 1 232 ? 15.363 12.654  -22.614 1.00 18.49  ?  289 ASP B CA  1 
ATOM   3897 C C   . ASP B 1 232 ? 15.687 11.953  -23.932 1.00 20.98  ?  289 ASP B C   1 
ATOM   3898 O O   . ASP B 1 232 ? 15.619 12.553  -25.003 1.00 19.68  ?  289 ASP B O   1 
ATOM   3899 C CB  . ASP B 1 232 ? 14.230 13.659  -22.773 1.00 18.10  ?  289 ASP B CB  1 
ATOM   3900 C CG  . ASP B 1 232 ? 12.903 13.010  -23.147 1.00 27.42  ?  289 ASP B CG  1 
ATOM   3901 O OD1 . ASP B 1 232 ? 12.892 11.882  -23.674 1.00 25.03  ?  289 ASP B OD1 1 
ATOM   3902 O OD2 . ASP B 1 232 ? 11.857 13.640  -22.910 1.00 29.48  -1 289 ASP B OD2 1 
ATOM   3903 N N   . PHE B 1 233 ? 16.013 10.660  -23.862 1.00 17.85  ?  290 PHE B N   1 
ATOM   3904 C CA  . PHE B 1 233 ? 16.455 9.946   -25.051 1.00 16.69  ?  290 PHE B CA  1 
ATOM   3905 C C   . PHE B 1 233 ? 15.305 9.725   -26.014 1.00 20.80  ?  290 PHE B C   1 
ATOM   3906 O O   . PHE B 1 233 ? 15.521 9.621   -27.228 1.00 20.01  ?  290 PHE B O   1 
ATOM   3907 C CB  . PHE B 1 233 ? 17.098 8.612   -24.652 1.00 17.39  ?  290 PHE B CB  1 
ATOM   3908 C CG  . PHE B 1 233 ? 18.288 8.777   -23.737 1.00 16.74  ?  290 PHE B CG  1 
ATOM   3909 C CD1 . PHE B 1 233 ? 19.389 9.525   -24.139 1.00 19.16  ?  290 PHE B CD1 1 
ATOM   3910 C CD2 . PHE B 1 233 ? 18.288 8.213   -22.469 1.00 21.45  ?  290 PHE B CD2 1 
ATOM   3911 C CE1 . PHE B 1 233 ? 20.501 9.684   -23.298 1.00 16.34  ?  290 PHE B CE1 1 
ATOM   3912 C CE2 . PHE B 1 233 ? 19.374 8.382   -21.613 1.00 19.55  ?  290 PHE B CE2 1 
ATOM   3913 C CZ  . PHE B 1 233 ? 20.481 9.105   -22.025 1.00 20.58  ?  290 PHE B CZ  1 
ATOM   3914 N N   . ARG B 1 234 ? 14.083 9.619   -25.492 1.00 17.86  ?  291 ARG B N   1 
ATOM   3915 C CA  . ARG B 1 234 ? 12.912 9.570   -26.358 1.00 24.28  ?  291 ARG B CA  1 
ATOM   3916 C C   . ARG B 1 234 ? 12.857 10.795  -27.256 1.00 23.79  ?  291 ARG B C   1 
ATOM   3917 O O   . ARG B 1 234 ? 12.698 10.683  -28.483 1.00 25.12  ?  291 ARG B O   1 
ATOM   3918 C CB  . ARG B 1 234 ? 11.653 9.454   -25.501 1.00 29.03  ?  291 ARG B CB  1 
ATOM   3919 C CG  . ARG B 1 234 ? 10.645 8.488   -26.059 1.00 46.63  ?  291 ARG B CG  1 
ATOM   3920 C CD  . ARG B 1 234 ? 11.255 7.093   -26.035 1.00 57.18  ?  291 ARG B CD  1 
ATOM   3921 N NE  . ARG B 1 234 ? 10.579 6.169   -26.935 1.00 54.64  ?  291 ARG B NE  1 
ATOM   3922 C CZ  . ARG B 1 234 ? 10.922 4.899   -27.091 1.00 50.35  ?  291 ARG B CZ  1 
ATOM   3923 N NH1 . ARG B 1 234 ? 12.020 4.407   -26.544 1.00 32.07  ?  291 ARG B NH1 1 
ATOM   3924 N NH2 . ARG B 1 234 ? 10.147 4.103   -27.822 1.00 63.05  ?  291 ARG B NH2 1 
ATOM   3925 N N   . LEU B 1 235 ? 13.020 11.981  -26.662 1.00 24.69  ?  292 LEU B N   1 
ATOM   3926 C CA  . LEU B 1 235 ? 12.991 13.199  -27.455 1.00 23.42  ?  292 LEU B CA  1 
ATOM   3927 C C   . LEU B 1 235 ? 14.187 13.270  -28.408 1.00 21.92  ?  292 LEU B C   1 
ATOM   3928 O O   . LEU B 1 235 ? 14.044 13.725  -29.549 1.00 23.38  ?  292 LEU B O   1 
ATOM   3929 C CB  . LEU B 1 235 ? 12.931 14.416  -26.530 1.00 27.78  ?  292 LEU B CB  1 
ATOM   3930 C CG  . LEU B 1 235 ? 13.180 15.806  -27.119 1.00 27.76  ?  292 LEU B CG  1 
ATOM   3931 C CD1 . LEU B 1 235 ? 12.127 16.154  -28.139 1.00 35.09  ?  292 LEU B CD1 1 
ATOM   3932 C CD2 . LEU B 1 235 ? 13.182 16.823  -25.977 1.00 32.70  ?  292 LEU B CD2 1 
ATOM   3933 N N   . LEU B 1 236 ? 15.368 12.808  -27.975 1.00 21.54  ?  293 LEU B N   1 
ATOM   3934 C CA  . LEU B 1 236 ? 16.506 12.790  -28.887 1.00 18.52  ?  293 LEU B CA  1 
ATOM   3935 C C   . LEU B 1 236 ? 16.204 11.920  -30.101 1.00 21.95  ?  293 LEU B C   1 
ATOM   3936 O O   . LEU B 1 236 ? 16.475 12.307  -31.246 1.00 22.47  ?  293 LEU B O   1 
ATOM   3937 C CB  . LEU B 1 236 ? 17.764 12.308  -28.163 1.00 18.96  ?  293 LEU B CB  1 
ATOM   3938 C CG  . LEU B 1 236 ? 19.022 12.207  -29.028 1.00 23.19  ?  293 LEU B CG  1 
ATOM   3939 C CD1 . LEU B 1 236 ? 19.394 13.565  -29.601 1.00 27.09  ?  293 LEU B CD1 1 
ATOM   3940 C CD2 . LEU B 1 236 ? 20.176 11.649  -28.208 1.00 21.60  ?  293 LEU B CD2 1 
ATOM   3941 N N   . GLY B 1 237 ? 15.645 10.731  -29.865 1.00 20.65  ?  294 GLY B N   1 
ATOM   3942 C CA  . GLY B 1 237 ? 15.310 9.856   -30.974 1.00 22.89  ?  294 GLY B CA  1 
ATOM   3943 C C   . GLY B 1 237 ? 14.257 10.463  -31.883 1.00 25.54  ?  294 GLY B C   1 
ATOM   3944 O O   . GLY B 1 237 ? 14.361 10.383  -33.113 1.00 27.84  ?  294 GLY B O   1 
ATOM   3945 N N   . GLN B 1 238 ? 13.233 11.099  -31.302 1.00 23.59  ?  295 GLN B N   1 
ATOM   3946 C CA  . GLN B 1 238 ? 12.238 11.755  -32.152 1.00 28.64  ?  295 GLN B CA  1 
ATOM   3947 C C   . GLN B 1 238 ? 12.855 12.884  -32.964 1.00 32.55  ?  295 GLN B C   1 
ATOM   3948 O O   . GLN B 1 238 ? 12.576 13.019  -34.161 1.00 31.61  ?  295 GLN B O   1 
ATOM   3949 C CB  . GLN B 1 238 ? 11.076 12.300  -31.322 1.00 33.36  ?  295 GLN B CB  1 
ATOM   3950 C CG  . GLN B 1 238 ? 10.477 11.355  -30.320 1.00 53.62  ?  295 GLN B CG  1 
ATOM   3951 C CD  . GLN B 1 238 ? 9.297  11.978  -29.610 1.00 69.85  ?  295 GLN B CD  1 
ATOM   3952 O OE1 . GLN B 1 238 ? 9.441  12.567  -28.535 1.00 61.63  ?  295 GLN B OE1 1 
ATOM   3953 N NE2 . GLN B 1 238 ? 8.121  11.876  -30.222 1.00 63.99  ?  295 GLN B NE2 1 
ATOM   3954 N N   . THR B 1 239 ? 13.701 13.698  -32.329 1.00 31.04  ?  296 THR B N   1 
ATOM   3955 C CA  . THR B 1 239 ? 14.229 14.898  -32.972 1.00 26.39  ?  296 THR B CA  1 
ATOM   3956 C C   . THR B 1 239 ? 15.216 14.546  -34.083 1.00 29.04  ?  296 THR B C   1 
ATOM   3957 O O   . THR B 1 239 ? 15.188 15.155  -35.159 1.00 33.39  ?  296 THR B O   1 
ATOM   3958 C CB  . THR B 1 239 ? 14.896 15.793  -31.920 1.00 34.06  ?  296 THR B CB  1 
ATOM   3959 O OG1 . THR B 1 239 ? 13.934 16.157  -30.922 1.00 31.04  ?  296 THR B OG1 1 
ATOM   3960 C CG2 . THR B 1 239 ? 15.469 17.057  -32.547 1.00 29.53  ?  296 THR B CG2 1 
ATOM   3961 N N   . SER B 1 240 ? 16.101 13.575  -33.838 1.00 26.24  ?  297 SER B N   1 
ATOM   3962 C CA  . SER B 1 240 ? 17.094 13.217  -34.848 1.00 25.07  ?  297 SER B CA  1 
ATOM   3963 C C   . SER B 1 240 ? 16.435 12.588  -36.069 1.00 28.08  ?  297 SER B C   1 
ATOM   3964 O O   . SER B 1 240 ? 16.796 12.904  -37.213 1.00 32.09  ?  297 SER B O   1 
ATOM   3965 C CB  . SER B 1 240 ? 18.137 12.268  -34.257 1.00 29.81  ?  297 SER B CB  1 
ATOM   3966 O OG  . SER B 1 240 ? 17.520 11.169  -33.613 1.00 35.46  ?  297 SER B OG  1 
ATOM   3967 N N   . VAL B 1 241 ? 15.463 11.699  -35.853 1.00 27.40  ?  298 VAL B N   1 
ATOM   3968 C CA  . VAL B 1 241 ? 14.791 11.088  -36.994 1.00 27.76  ?  298 VAL B CA  1 
ATOM   3969 C C   . VAL B 1 241 ? 14.027 12.144  -37.788 1.00 34.70  ?  298 VAL B C   1 
ATOM   3970 O O   . VAL B 1 241 ? 14.016 12.122  -39.025 1.00 35.73  ?  298 VAL B O   1 
ATOM   3971 C CB  . VAL B 1 241 ? 13.877 9.941   -36.526 1.00 29.89  ?  298 VAL B CB  1 
ATOM   3972 C CG1 . VAL B 1 241 ? 13.016 9.447   -37.674 1.00 29.32  ?  298 VAL B CG1 1 
ATOM   3973 C CG2 . VAL B 1 241 ? 14.726 8.797   -35.973 1.00 28.65  ?  298 VAL B CG2 1 
ATOM   3974 N N   . ASN B 1 242 ? 13.411 13.105  -37.095 1.00 32.95  ?  299 ASN B N   1 
ATOM   3975 C CA  . ASN B 1 242 ? 12.726 14.178  -37.808 1.00 31.80  ?  299 ASN B CA  1 
ATOM   3976 C C   . ASN B 1 242 ? 13.710 15.075  -38.555 1.00 33.75  ?  299 ASN B C   1 
ATOM   3977 O O   . ASN B 1 242 ? 13.418 15.517  -39.670 1.00 40.66  ?  299 ASN B O   1 
ATOM   3978 C CB  . ASN B 1 242 ? 11.871 14.993  -36.837 1.00 34.96  ?  299 ASN B CB  1 
ATOM   3979 C CG  . ASN B 1 242 ? 10.666 14.209  -36.309 1.00 39.14  ?  299 ASN B CG  1 
ATOM   3980 O OD1 . ASN B 1 242 ? 10.288 13.176  -36.860 1.00 37.77  ?  299 ASN B OD1 1 
ATOM   3981 N ND2 . ASN B 1 242 ? 10.052 14.717  -35.245 1.00 40.75  ?  299 ASN B ND2 1 
ATOM   3982 N N   . ARG B 1 243 ? 14.884 15.351  -37.971 1.00 35.36  ?  300 ARG B N   1 
ATOM   3983 C CA  . ARG B 1 243 ? 15.856 16.193  -38.672 1.00 35.70  ?  300 ARG B CA  1 
ATOM   3984 C C   . ARG B 1 243 ? 16.430 15.486  -39.897 1.00 49.44  ?  300 ARG B C   1 
ATOM   3985 O O   . ARG B 1 243 ? 16.749 16.139  -40.901 1.00 45.10  ?  300 ARG B O   1 
ATOM   3986 C CB  . ARG B 1 243 ? 16.972 16.626  -37.713 1.00 44.69  ?  300 ARG B CB  1 
ATOM   3987 C CG  . ARG B 1 243 ? 18.171 17.322  -38.368 1.00 53.08  ?  300 ARG B CG  1 
ATOM   3988 C CD  . ARG B 1 243 ? 17.827 18.720  -38.903 1.00 66.02  ?  300 ARG B CD  1 
ATOM   3989 N NE  . ARG B 1 243 ? 19.015 19.458  -39.327 1.00 59.88  ?  300 ARG B NE  1 
ATOM   3990 C CZ  . ARG B 1 243 ? 18.995 20.551  -40.083 1.00 81.36  ?  300 ARG B CZ  1 
ATOM   3991 N NH1 . ARG B 1 243 ? 17.859 21.069  -40.522 1.00 70.23  ?  300 ARG B NH1 1 
ATOM   3992 N NH2 . ARG B 1 243 ? 20.145 21.138  -40.409 1.00 74.07  ?  300 ARG B NH2 1 
ATOM   3993 N N   . LEU B 1 244 ? 16.556 14.157  -39.844 1.00 34.26  ?  301 LEU B N   1 
ATOM   3994 C CA  . LEU B 1 244 ? 17.036 13.418  -41.007 1.00 34.96  ?  301 LEU B CA  1 
ATOM   3995 C C   . LEU B 1 244 ? 16.002 13.427  -42.127 1.00 49.59  ?  301 LEU B C   1 
ATOM   3996 O O   . LEU B 1 244 ? 16.350 13.632  -43.298 1.00 40.58  ?  301 LEU B O   1 
ATOM   3997 C CB  . LEU B 1 244 ? 17.406 11.989  -40.601 1.00 33.90  ?  301 LEU B CB  1 
ATOM   3998 C CG  . LEU B 1 244 ? 18.406 11.257  -41.494 1.00 46.10  ?  301 LEU B CG  1 
ATOM   3999 C CD1 . LEU B 1 244 ? 19.671 12.084  -41.671 1.00 46.68  ?  301 LEU B CD1 1 
ATOM   4000 C CD2 . LEU B 1 244 ? 18.736 9.912   -40.869 1.00 43.36  ?  301 LEU B CD2 1 
ATOM   4001 N N   . VAL B 1 245 ? 14.724 13.233  -41.793 1.00 37.63  ?  302 VAL B N   1 
ATOM   4002 C CA  . VAL B 1 245 ? 13.677 13.361  -42.809 1.00 54.53  ?  302 VAL B CA  1 
ATOM   4003 C C   . VAL B 1 245 ? 13.693 14.757  -43.426 1.00 54.49  ?  302 VAL B C   1 
ATOM   4004 O O   . VAL B 1 245 ? 13.539 14.920  -44.646 1.00 52.02  ?  302 VAL B O   1 
ATOM   4005 C CB  . VAL B 1 245 ? 12.299 13.030  -42.209 1.00 49.77  ?  302 VAL B CB  1 
ATOM   4006 C CG1 . VAL B 1 245 ? 11.216 13.225  -43.257 1.00 49.82  ?  302 VAL B CG1 1 
ATOM   4007 C CG2 . VAL B 1 245 ? 12.279 11.610  -41.685 1.00 42.24  ?  302 VAL B CG2 1 
ATOM   4008 N N   . GLN B 1 246 ? 13.876 15.786  -42.594 1.00 49.40  ?  303 GLN B N   1 
ATOM   4009 C CA  . GLN B 1 246 ? 13.933 17.154  -43.103 1.00 55.10  ?  303 GLN B CA  1 
ATOM   4010 C C   . GLN B 1 246 ? 15.153 17.373  -43.993 1.00 66.00  ?  303 GLN B C   1 
ATOM   4011 O O   . GLN B 1 246 ? 15.077 18.132  -44.967 1.00 60.01  ?  303 GLN B O   1 
ATOM   4012 C CB  . GLN B 1 246 ? 13.929 18.146  -41.935 1.00 51.09  ?  303 GLN B CB  1 
ATOM   4013 C CG  . GLN B 1 246 ? 13.789 19.618  -42.317 1.00 74.46  ?  303 GLN B CG  1 
ATOM   4014 C CD  . GLN B 1 246 ? 14.050 20.553  -41.140 1.00 90.50  ?  303 GLN B CD  1 
ATOM   4015 O OE1 . GLN B 1 246 ? 14.364 20.105  -40.033 1.00 83.61  ?  303 GLN B OE1 1 
ATOM   4016 N NE2 . GLN B 1 246 ? 13.926 21.857  -41.377 1.00 71.82  ?  303 GLN B NE2 1 
ATOM   4017 N N   . LEU B 1 247 ? 16.278 16.716  -43.684 1.00 44.64  ?  304 LEU B N   1 
ATOM   4018 C CA  . LEU B 1 247 ? 17.486 16.861  -44.487 1.00 46.26  ?  304 LEU B CA  1 
ATOM   4019 C C   . LEU B 1 247 ? 17.391 16.118  -45.810 1.00 58.61  ?  304 LEU B C   1 
ATOM   4020 O O   . LEU B 1 247 ? 18.064 16.500  -46.777 1.00 56.90  ?  304 LEU B O   1 
ATOM   4021 C CB  . LEU B 1 247 ? 18.701 16.378  -43.693 1.00 50.50  ?  304 LEU B CB  1 
ATOM   4022 C CG  . LEU B 1 247 ? 19.401 17.460  -42.859 1.00 54.25  ?  304 LEU B CG  1 
ATOM   4023 C CD1 . LEU B 1 247 ? 20.627 16.900  -42.181 1.00 54.62  ?  304 LEU B CD1 1 
ATOM   4024 C CD2 . LEU B 1 247 ? 19.772 18.681  -43.701 1.00 61.27  ?  304 LEU B CD2 1 
ATOM   4025 N N   . LEU B 1 248 ? 16.559 15.079  -45.879 1.00 55.75  ?  305 LEU B N   1 
ATOM   4026 C CA  . LEU B 1 248 ? 16.331 14.405  -47.149 1.00 51.74  ?  305 LEU B CA  1 
ATOM   4027 C C   . LEU B 1 248 ? 15.507 15.264  -48.096 1.00 55.08  ?  305 LEU B C   1 
ATOM   4028 O O   . LEU B 1 248 ? 15.679 15.180  -49.317 1.00 66.63  ?  305 LEU B O   1 
ATOM   4029 C CB  . LEU B 1 248 ? 15.628 13.073  -46.921 1.00 53.94  ?  305 LEU B CB  1 
ATOM   4030 C CG  . LEU B 1 248 ? 16.508 11.951  -46.375 1.00 49.58  ?  305 LEU B CG  1 
ATOM   4031 C CD1 . LEU B 1 248 ? 15.641 10.773  -45.952 1.00 52.24  ?  305 LEU B CD1 1 
ATOM   4032 C CD2 . LEU B 1 248 ? 17.579 11.535  -47.380 1.00 46.75  ?  305 LEU B CD2 1 
ATOM   4033 N N   . GLN B 1 249 ? 14.607 16.087  -47.558 1.00 69.27  ?  306 GLN B N   1 
ATOM   4034 C CA  . GLN B 1 249 ? 13.735 16.886  -48.412 1.00 70.96  ?  306 GLN B CA  1 
ATOM   4035 C C   . GLN B 1 249 ? 14.422 18.161  -48.881 1.00 59.17  ?  306 GLN B C   1 
ATOM   4036 O O   . GLN B 1 249 ? 14.331 18.519  -50.059 1.00 66.57  ?  306 GLN B O   1 
ATOM   4037 C CB  . GLN B 1 249 ? 12.443 17.218  -47.671 1.00 64.23  ?  306 GLN B CB  1 
ATOM   4038 C CG  . GLN B 1 249 ? 11.376 16.164  -47.857 1.00 77.42  ?  306 GLN B CG  1 
ATOM   4039 C CD  . GLN B 1 249 ? 10.280 16.608  -48.797 1.00 76.38  ?  306 GLN B CD  1 
ATOM   4040 O OE1 . GLN B 1 249 ? 10.378 17.656  -49.439 1.00 72.67  ?  306 GLN B OE1 1 
ATOM   4041 N NE2 . GLN B 1 249 ? 9.229  15.803  -48.895 1.00 81.86  ?  306 GLN B NE2 1 
ATOM   4042 N N   . ASN B 1 250 ? 15.112 18.856  -47.980 1.00 58.07  ?  307 ASN B N   1 
ATOM   4043 C CA  . ASN B 1 250 ? 15.810 20.097  -48.302 1.00 72.43  ?  307 ASN B CA  1 
ATOM   4044 C C   . ASN B 1 250 ? 17.231 19.989  -47.770 1.00 73.61  ?  307 ASN B C   1 
ATOM   4045 O O   . ASN B 1 250 ? 17.508 20.394  -46.632 1.00 72.67  ?  307 ASN B O   1 
ATOM   4046 C CB  . ASN B 1 250 ? 15.098 21.311  -47.707 1.00 61.37  ?  307 ASN B CB  1 
ATOM   4047 C CG  . ASN B 1 250 ? 14.030 21.863  -48.624 1.00 58.65  ?  307 ASN B CG  1 
ATOM   4048 O OD1 . ASN B 1 250 ? 14.271 22.082  -49.809 1.00 57.72  ?  307 ASN B OD1 1 
ATOM   4049 N ND2 . ASN B 1 250 ? 12.844 22.108  -48.075 1.00 63.70  ?  307 ASN B ND2 1 
ATOM   4050 N N   . PRO B 1 251 ? 18.157 19.420  -48.558 1.00 65.81  ?  308 PRO B N   1 
ATOM   4051 C CA  . PRO B 1 251 ? 19.573 19.430  -48.169 1.00 64.24  ?  308 PRO B CA  1 
ATOM   4052 C C   . PRO B 1 251 ? 20.018 20.811  -47.717 1.00 82.37  ?  308 PRO B C   1 
ATOM   4053 O O   . PRO B 1 251 ? 19.878 21.787  -48.462 1.00 87.68  ?  308 PRO B O   1 
ATOM   4054 C CB  . PRO B 1 251 ? 20.272 19.004  -49.461 1.00 69.56  ?  308 PRO B CB  1 
ATOM   4055 C CG  . PRO B 1 251 ? 19.319 18.005  -50.029 1.00 68.37  ?  308 PRO B CG  1 
ATOM   4056 C CD  . PRO B 1 251 ? 17.938 18.593  -49.760 1.00 70.51  ?  308 PRO B CD  1 
ATOM   4057 N N   . SER B 1 252 ? 20.529 20.913  -46.494 1.00 80.39  ?  309 SER B N   1 
ATOM   4058 C CA  . SER B 1 252 ? 20.768 22.204  -45.871 1.00 86.42  ?  309 SER B CA  1 
ATOM   4059 C C   . SER B 1 252 ? 22.192 22.288  -45.349 1.00 92.69  ?  309 SER B C   1 
ATOM   4060 O O   . SER B 1 252 ? 22.890 21.280  -45.204 1.00 96.38  ?  309 SER B O   1 
ATOM   4061 C CB  . SER B 1 252 ? 19.779 22.461  -44.724 1.00 83.30  ?  309 SER B CB  1 
ATOM   4062 O OG  . SER B 1 252 ? 18.625 23.135  -45.197 1.00 89.28  ?  309 SER B OG  1 
ATOM   4063 N N   . ALA B 1 253 ? 22.611 23.522  -45.066 1.00 88.49  ?  310 ALA B N   1 
ATOM   4064 C CA  . ALA B 1 253 ? 23.893 23.782  -44.427 1.00 89.72  ?  310 ALA B CA  1 
ATOM   4065 C C   . ALA B 1 253 ? 23.953 23.093  -43.067 1.00 76.20  ?  310 ALA B C   1 
ATOM   4066 O O   . ALA B 1 253 ? 22.913 22.756  -42.489 1.00 67.53  ?  310 ALA B O   1 
ATOM   4067 C CB  . ALA B 1 253 ? 24.123 25.289  -44.283 1.00 70.55  ?  310 ALA B CB  1 
ATOM   4068 N N   . GLN B 1 254 ? 25.164 22.871  -42.561 1.00 78.61  ?  311 GLN B N   1 
ATOM   4069 C CA  . GLN B 1 254 ? 25.337 22.232  -41.264 1.00 74.21  ?  311 GLN B CA  1 
ATOM   4070 C C   . GLN B 1 254 ? 24.768 23.121  -40.164 1.00 59.70  ?  311 GLN B C   1 
ATOM   4071 O O   . GLN B 1 254 ? 24.823 24.351  -40.240 1.00 73.23  ?  311 GLN B O   1 
ATOM   4072 C CB  . GLN B 1 254 ? 26.820 21.951  -40.996 1.00 68.92  ?  311 GLN B CB  1 
ATOM   4073 C CG  . GLN B 1 254 ? 27.567 21.278  -42.150 1.00 84.70  ?  311 GLN B CG  1 
ATOM   4074 C CD  . GLN B 1 254 ? 26.743 20.223  -42.868 1.00 91.57  ?  311 GLN B CD  1 
ATOM   4075 O OE1 . GLN B 1 254 ? 26.459 19.156  -42.319 1.00 102.40 ?  311 GLN B OE1 1 
ATOM   4076 N NE2 . GLN B 1 254 ? 26.355 20.518  -44.106 1.00 71.92  ?  311 GLN B NE2 1 
ATOM   4077 N N   . SER B 1 255 ? 24.205 22.489  -39.132 1.00 48.91  ?  312 SER B N   1 
ATOM   4078 C CA  . SER B 1 255 ? 23.653 23.256  -38.027 1.00 58.53  ?  312 SER B CA  1 
ATOM   4079 C C   . SER B 1 255 ? 23.796 22.480  -36.728 1.00 60.41  ?  312 SER B C   1 
ATOM   4080 O O   . SER B 1 255 ? 23.622 21.252  -36.726 1.00 43.87  ?  312 SER B O   1 
ATOM   4081 C CB  . SER B 1 255 ? 22.176 23.606  -38.259 1.00 60.71  ?  312 SER B CB  1 
ATOM   4082 O OG  . SER B 1 255 ? 21.553 24.021  -37.049 1.00 58.48  ?  312 SER B OG  1 
ATOM   4083 N N   . PRO B 1 256 ? 24.130 23.154  -35.619 1.00 57.52  ?  313 PRO B N   1 
ATOM   4084 C CA  . PRO B 1 256 ? 24.062 22.495  -34.311 1.00 49.71  ?  313 PRO B CA  1 
ATOM   4085 C C   . PRO B 1 256 ? 22.758 22.811  -33.588 1.00 54.21  ?  313 PRO B C   1 
ATOM   4086 O O   . PRO B 1 256 ? 22.397 23.980  -33.418 1.00 62.23  ?  313 PRO B O   1 
ATOM   4087 C CB  . PRO B 1 256 ? 25.294 23.055  -33.589 1.00 45.79  ?  313 PRO B CB  1 
ATOM   4088 C CG  . PRO B 1 256 ? 25.495 24.440  -34.203 1.00 54.41  ?  313 PRO B CG  1 
ATOM   4089 C CD  . PRO B 1 256 ? 24.719 24.500  -35.512 1.00 51.27  ?  313 PRO B CD  1 
ATOM   4090 N N   . GLN B 1 257 ? 22.032 21.775  -33.176 1.00 38.74  ?  314 GLN B N   1 
ATOM   4091 C CA  . GLN B 1 257 ? 20.723 21.929  -32.555 1.00 41.87  ?  314 GLN B CA  1 
ATOM   4092 C C   . GLN B 1 257 ? 20.752 21.355  -31.143 1.00 37.68  ?  314 GLN B C   1 
ATOM   4093 O O   . GLN B 1 257 ? 21.299 20.271  -30.915 1.00 36.34  ?  314 GLN B O   1 
ATOM   4094 C CB  . GLN B 1 257 ? 19.643 21.248  -33.407 1.00 45.97  ?  314 GLN B CB  1 
ATOM   4095 C CG  . GLN B 1 257 ? 18.252 21.286  -32.821 1.00 47.21  ?  314 GLN B CG  1 
ATOM   4096 C CD  . GLN B 1 257 ? 17.236 20.603  -33.713 1.00 66.52  ?  314 GLN B CD  1 
ATOM   4097 O OE1 . GLN B 1 257 ? 16.220 20.099  -33.239 1.00 79.13  ?  314 GLN B OE1 1 
ATOM   4098 N NE2 . GLN B 1 257 ? 17.510 20.577  -35.017 1.00 55.31  ?  314 GLN B NE2 1 
ATOM   4099 N N   . LEU B 1 258 ? 20.169 22.089  -30.191 1.00 32.59  ?  315 LEU B N   1 
ATOM   4100 C CA  . LEU B 1 258 ? 20.253 21.762  -28.773 1.00 30.61  ?  315 LEU B CA  1 
ATOM   4101 C C   . LEU B 1 258 ? 18.900 21.325  -28.220 1.00 25.71  ?  315 LEU B C   1 
ATOM   4102 O O   . LEU B 1 258 ? 17.856 21.862  -28.595 1.00 29.51  ?  315 LEU B O   1 
ATOM   4103 C CB  . LEU B 1 258 ? 20.784 22.954  -27.967 1.00 29.60  ?  315 LEU B CB  1 
ATOM   4104 C CG  . LEU B 1 258 ? 22.266 23.310  -28.155 1.00 37.14  ?  315 LEU B CG  1 
ATOM   4105 C CD1 . LEU B 1 258 ? 22.657 24.530  -27.322 1.00 39.07  ?  315 LEU B CD1 1 
ATOM   4106 C CD2 . LEU B 1 258 ? 23.133 22.116  -27.776 1.00 31.98  ?  315 LEU B CD2 1 
ATOM   4107 N N   . LEU B 1 259 ? 18.928 20.336  -27.330 1.00 22.13  ?  316 LEU B N   1 
ATOM   4108 C CA  . LEU B 1 259 ? 17.735 19.883  -26.631 1.00 22.36  ?  316 LEU B CA  1 
ATOM   4109 C C   . LEU B 1 259 ? 17.867 20.210  -25.142 1.00 20.59  ?  316 LEU B C   1 
ATOM   4110 O O   . LEU B 1 259 ? 18.983 20.250  -24.619 1.00 24.41  ?  316 LEU B O   1 
ATOM   4111 C CB  . LEU B 1 259 ? 17.529 18.368  -26.801 1.00 24.43  ?  316 LEU B CB  1 
ATOM   4112 C CG  . LEU B 1 259 ? 17.046 17.935  -28.194 1.00 27.92  ?  316 LEU B CG  1 
ATOM   4113 C CD1 . LEU B 1 259 ? 16.890 16.415  -28.221 1.00 29.03  ?  316 LEU B CD1 1 
ATOM   4114 C CD2 . LEU B 1 259 ? 15.739 18.624  -28.576 1.00 29.11  ?  316 LEU B CD2 1 
ATOM   4115 N N   . PRO B 1 260 ? 16.768 20.478  -24.439 1.00 19.55  ?  317 PRO B N   1 
ATOM   4116 C CA  . PRO B 1 260 ? 16.874 20.788  -23.008 1.00 18.23  ?  317 PRO B CA  1 
ATOM   4117 C C   . PRO B 1 260 ? 17.233 19.578  -22.169 1.00 18.64  ?  317 PRO B C   1 
ATOM   4118 O O   . PRO B 1 260 ? 16.931 18.434  -22.509 1.00 22.99  ?  317 PRO B O   1 
ATOM   4119 C CB  . PRO B 1 260 ? 15.479 21.295  -22.647 1.00 20.48  ?  317 PRO B CB  1 
ATOM   4120 C CG  . PRO B 1 260 ? 14.573 20.718  -23.702 1.00 31.28  ?  317 PRO B CG  1 
ATOM   4121 C CD  . PRO B 1 260 ? 15.390 20.594  -24.942 1.00 27.45  ?  317 PRO B CD  1 
ATOM   4122 N N   . VAL B 1 261 ? 17.923 19.849  -21.070 1.00 19.35  ?  318 VAL B N   1 
ATOM   4123 C CA  . VAL B 1 261 ? 18.116 18.885  -19.997 1.00 19.89  ?  318 VAL B CA  1 
ATOM   4124 C C   . VAL B 1 261 ? 17.458 19.443  -18.746 1.00 19.14  ?  318 VAL B C   1 
ATOM   4125 O O   . VAL B 1 261 ? 17.234 20.649  -18.611 1.00 20.88  ?  318 VAL B O   1 
ATOM   4126 C CB  . VAL B 1 261 ? 19.599 18.558  -19.731 1.00 23.50  ?  318 VAL B CB  1 
ATOM   4127 C CG1 . VAL B 1 261 ? 20.199 17.808  -20.917 1.00 25.51  ?  318 VAL B CG1 1 
ATOM   4128 C CG2 . VAL B 1 261 ? 20.376 19.818  -19.432 1.00 26.83  ?  318 VAL B CG2 1 
ATOM   4129 N N   . THR B 1 262 ? 17.147 18.537  -17.821 1.00 17.65  ?  319 THR B N   1 
ATOM   4130 C CA  . THR B 1 262 ? 16.459 18.878  -16.587 1.00 18.37  ?  319 THR B CA  1 
ATOM   4131 C C   . THR B 1 262 ? 17.119 18.148  -15.431 1.00 16.02  ?  319 THR B C   1 
ATOM   4132 O O   . THR B 1 262 ? 17.737 17.100  -15.615 1.00 19.16  ?  319 THR B O   1 
ATOM   4133 C CB  . THR B 1 262 ? 14.960 18.512  -16.629 1.00 21.86  ?  319 THR B CB  1 
ATOM   4134 O OG1 . THR B 1 262 ? 14.801 17.131  -16.976 1.00 21.16  ?  319 THR B OG1 1 
ATOM   4135 C CG2 . THR B 1 262 ? 14.224 19.372  -17.648 1.00 27.74  ?  319 THR B CG2 1 
ATOM   4136 N N   . LEU B 1 263 ? 16.976 18.706  -14.239 1.00 17.56  ?  320 LEU B N   1 
ATOM   4137 C CA  . LEU B 1 263 ? 17.352 18.023  -13.007 1.00 16.05  ?  320 LEU B CA  1 
ATOM   4138 C C   . LEU B 1 263 ? 16.134 17.278  -12.484 1.00 13.42  ?  320 LEU B C   1 
ATOM   4139 O O   . LEU B 1 263 ? 15.073 17.879  -12.297 1.00 18.13  ?  320 LEU B O   1 
ATOM   4140 C CB  . LEU B 1 263 ? 17.846 19.027  -11.966 1.00 18.38  ?  320 LEU B CB  1 
ATOM   4141 C CG  . LEU B 1 263 ? 18.117 18.436  -10.576 1.00 20.82  ?  320 LEU B CG  1 
ATOM   4142 C CD1 . LEU B 1 263 ? 19.350 17.597  -10.617 1.00 21.84  ?  320 LEU B CD1 1 
ATOM   4143 C CD2 . LEU B 1 263 ? 18.262 19.545  -9.549  1.00 28.93  ?  320 LEU B CD2 1 
ATOM   4144 N N   . VAL B 1 264 ? 16.277 15.965  -12.293 1.00 15.03  ?  321 VAL B N   1 
ATOM   4145 C CA  . VAL B 1 264 ? 15.253 15.127  -11.686 1.00 16.21  ?  321 VAL B CA  1 
ATOM   4146 C C   . VAL B 1 264 ? 15.658 14.888  -10.237 1.00 12.85  ?  321 VAL B C   1 
ATOM   4147 O O   . VAL B 1 264 ? 16.662 14.214  -9.958  1.00 14.00  ?  321 VAL B O   1 
ATOM   4148 C CB  . VAL B 1 264 ? 15.077 13.805  -12.445 1.00 16.74  ?  321 VAL B CB  1 
ATOM   4149 C CG1 . VAL B 1 264 ? 13.981 12.958  -11.768 1.00 14.37  ?  321 VAL B CG1 1 
ATOM   4150 C CG2 . VAL B 1 264 ? 14.678 14.078  -13.893 1.00 22.11  ?  321 VAL B CG2 1 
ATOM   4151 N N   . LYS B 1 265 ? 14.883 15.465  -9.320  1.00 17.41  ?  322 LYS B N   1 
ATOM   4152 C CA  . LYS B 1 265 ? 15.139 15.361  -7.886  1.00 16.46  ?  322 LYS B CA  1 
ATOM   4153 C C   . LYS B 1 265 ? 14.507 14.082  -7.352  1.00 13.14  ?  322 LYS B C   1 
ATOM   4154 O O   . LYS B 1 265 ? 13.280 13.917  -7.400  1.00 17.09  ?  322 LYS B O   1 
ATOM   4155 C CB  . LYS B 1 265 ? 14.556 16.560  -7.148  1.00 20.94  ?  322 LYS B CB  1 
ATOM   4156 C CG  . LYS B 1 265 ? 15.288 17.847  -7.434  1.00 25.29  ?  322 LYS B CG  1 
ATOM   4157 C CD  . LYS B 1 265 ? 14.586 19.018  -6.756  1.00 29.79  ?  322 LYS B CD  1 
ATOM   4158 C CE  . LYS B 1 265 ? 15.437 20.283  -6.779  1.00 34.94  ?  322 LYS B CE  1 
ATOM   4159 N NZ  . LYS B 1 265 ? 14.948 21.292  -5.791  1.00 36.05  ?  322 LYS B NZ  1 
ATOM   4160 N N   . ARG B 1 266 ? 15.353 13.178  -6.851  1.00 13.27  ?  323 ARG B N   1 
ATOM   4161 C CA  . ARG B 1 266 ? 14.840 11.994  -6.189  1.00 15.58  ?  323 ARG B CA  1 
ATOM   4162 C C   . ARG B 1 266 ? 15.326 11.967  -4.743  1.00 13.19  ?  323 ARG B C   1 
ATOM   4163 O O   . ARG B 1 266 ? 14.904 12.805  -3.933  1.00 16.97  ?  323 ARG B O   1 
ATOM   4164 C CB  . ARG B 1 266 ? 15.250 10.736  -6.967  1.00 12.48  ?  323 ARG B CB  1 
ATOM   4165 C CG  . ARG B 1 266 ? 14.584 10.694  -8.353  1.00 14.53  ?  323 ARG B CG  1 
ATOM   4166 C CD  . ARG B 1 266 ? 14.619 9.297   -8.957  1.00 14.12  ?  323 ARG B CD  1 
ATOM   4167 N NE  . ARG B 1 266 ? 13.948 9.265   -10.266 1.00 15.33  ?  323 ARG B NE  1 
ATOM   4168 C CZ  . ARG B 1 266 ? 14.589 9.238   -11.427 1.00 16.01  ?  323 ARG B CZ  1 
ATOM   4169 N NH1 . ARG B 1 266 ? 15.914 9.268   -11.494 1.00 15.46  ?  323 ARG B NH1 1 
ATOM   4170 N NH2 . ARG B 1 266 ? 13.881 9.162   -12.556 1.00 15.90  ?  323 ARG B NH2 1 
ATOM   4171 N N   . LYS B 1 267 ? 16.190 11.013  -4.390  1.00 13.37  ?  324 LYS B N   1 
ATOM   4172 C CA  . LYS B 1 267 ? 16.435 10.719  -2.984  1.00 13.19  ?  324 LYS B CA  1 
ATOM   4173 C C   . LYS B 1 267 ? 17.920 10.711  -2.618  1.00 12.37  ?  324 LYS B C   1 
ATOM   4174 O O   . LYS B 1 267 ? 18.269 10.259  -1.517  1.00 14.83  ?  324 LYS B O   1 
ATOM   4175 C CB  . LYS B 1 267 ? 15.798 9.367   -2.648  1.00 13.87  ?  324 LYS B CB  1 
ATOM   4176 C CG  . LYS B 1 267 ? 14.283 9.345   -2.617  1.00 18.39  ?  324 LYS B CG  1 
ATOM   4177 C CD  . LYS B 1 267 ? 13.666 10.467  -1.805  1.00 23.05  ?  324 LYS B CD  1 
ATOM   4178 C CE  . LYS B 1 267 ? 12.142 10.426  -1.870  1.00 29.68  ?  324 LYS B CE  1 
ATOM   4179 N NZ  . LYS B 1 267 ? 11.578 10.994  -0.616  1.00 46.15  ?  324 LYS B NZ  1 
ATOM   4180 N N   . THR B 1 268 ? 18.802 11.208  -3.481  1.00 10.74  ?  325 THR B N   1 
ATOM   4181 C CA  . THR B 1 268 ? 20.223 11.158  -3.170  1.00 11.91  ?  325 THR B CA  1 
ATOM   4182 C C   . THR B 1 268 ? 20.843 12.516  -2.881  1.00 11.60  ?  325 THR B C   1 
ATOM   4183 O O   . THR B 1 268 ? 22.060 12.579  -2.768  1.00 12.26  ?  325 THR B O   1 
ATOM   4184 C CB  . THR B 1 268 ? 21.024 10.444  -4.274  1.00 11.97  ?  325 THR B CB  1 
ATOM   4185 O OG1 . THR B 1 268 ? 20.813 11.081  -5.547  1.00 12.04  ?  325 THR B OG1 1 
ATOM   4186 C CG2 . THR B 1 268 ? 20.590 8.967   -4.380  1.00 13.37  ?  325 THR B CG2 1 
ATOM   4187 N N   . THR B 1 269 ? 20.058 13.583  -2.708  1.00 13.44  ?  326 THR B N   1 
ATOM   4188 C CA  . THR B 1 269 ? 20.672 14.843  -2.275  1.00 12.24  ?  326 THR B CA  1 
ATOM   4189 C C   . THR B 1 269 ? 19.926 15.433  -1.090  1.00 13.43  ?  326 THR B C   1 
ATOM   4190 O O   . THR B 1 269 ? 18.732 15.196  -0.873  1.00 16.29  ?  326 THR B O   1 
ATOM   4191 C CB  . THR B 1 269 ? 20.781 15.927  -3.389  1.00 16.06  ?  326 THR B CB  1 
ATOM   4192 O OG1 . THR B 1 269 ? 19.490 16.462  -3.669  1.00 19.61  ?  326 THR B OG1 1 
ATOM   4193 C CG2 . THR B 1 269 ? 21.432 15.379  -4.678  1.00 13.41  ?  326 THR B CG2 1 
ATOM   4194 N N   . ALA B 1 270 ? 20.679 16.216  -0.325  1.00 12.82  ?  327 ALA B N   1 
ATOM   4195 C CA  . ALA B 1 270 ? 20.227 16.838  0.911   1.00 13.69  ?  327 ALA B CA  1 
ATOM   4196 C C   . ALA B 1 270 ? 21.226 17.936  1.257   1.00 14.50  ?  327 ALA B C   1 
ATOM   4197 O O   . ALA B 1 270 ? 22.312 18.004  0.662   1.00 14.66  ?  327 ALA B O   1 
ATOM   4198 C CB  . ALA B 1 270 ? 20.130 15.789  2.042   1.00 13.67  ?  327 ALA B CB  1 
ATOM   4199 N N   . PRO B 1 271 ? 20.922 18.805  2.221   1.00 15.02  ?  328 PRO B N   1 
ATOM   4200 C CA  . PRO B 1 271 ? 21.956 19.756  2.687   1.00 14.02  ?  328 PRO B CA  1 
ATOM   4201 C C   . PRO B 1 271 ? 23.166 19.018  3.230   1.00 15.35  ?  328 PRO B C   1 
ATOM   4202 O O   . PRO B 1 271 ? 23.075 17.837  3.599   1.00 15.99  ?  328 PRO B O   1 
ATOM   4203 C CB  . PRO B 1 271 ? 21.241 20.548  3.791   1.00 16.56  ?  328 PRO B CB  1 
ATOM   4204 C CG  . PRO B 1 271 ? 19.791 20.443  3.461   1.00 18.20  ?  328 PRO B CG  1 
ATOM   4205 C CD  . PRO B 1 271 ? 19.622 19.056  2.866   1.00 17.01  ?  328 PRO B CD  1 
ATOM   4206 N N   . PRO B 1 272 ? 24.318 19.672  3.313   1.00 16.34  ?  329 PRO B N   1 
ATOM   4207 C CA  . PRO B 1 272 ? 25.479 19.007  3.916   1.00 16.29  ?  329 PRO B CA  1 
ATOM   4208 C C   . PRO B 1 272 ? 25.203 18.619  5.363   1.00 19.30  ?  329 PRO B C   1 
ATOM   4209 O O   . PRO B 1 272 ? 24.428 19.274  6.069   1.00 18.46  ?  329 PRO B O   1 
ATOM   4210 C CB  . PRO B 1 272 ? 26.598 20.049  3.806   1.00 18.62  ?  329 PRO B CB  1 
ATOM   4211 C CG  . PRO B 1 272 ? 25.937 21.334  3.508   1.00 20.17  ?  329 PRO B CG  1 
ATOM   4212 C CD  . PRO B 1 272 ? 24.652 21.012  2.802   1.00 15.81  ?  329 PRO B CD  1 
ATOM   4213 N N   . GLU B 1 273 ? 25.861 17.534  5.784   1.00 20.48  ?  330 GLU B N   1 
ATOM   4214 C CA  . GLU B 1 273 ? 25.739 16.951  7.116   1.00 24.18  ?  330 GLU B CA  1 
ATOM   4215 C C   . GLU B 1 273 ? 25.718 18.007  8.202   1.00 24.04  ?  330 GLU B C   1 
ATOM   4216 O O   . GLU B 1 273 ? 26.640 18.825  8.320   1.00 26.32  ?  330 GLU B O   1 
ATOM   4217 C CB  . GLU B 1 273 ? 26.892 15.977  7.368   1.00 26.10  ?  330 GLU B CB  1 
ATOM   4218 C CG  . GLU B 1 273 ? 26.607 14.959  8.468   1.00 32.51  ?  330 GLU B CG  1 
ATOM   4219 C CD  . GLU B 1 273 ? 27.757 13.982  8.672   1.00 32.24  ?  330 GLU B CD  1 
ATOM   4220 O OE1 . GLU B 1 273 ? 28.735 14.037  7.886   1.00 29.57  ?  330 GLU B OE1 1 
ATOM   4221 O OE2 . GLU B 1 273 ? 27.691 13.176  9.635   1.00 37.84  -1 330 GLU B OE2 1 
ATOM   4222 N N   . ASN B 1 274 ? 24.635 17.992  8.966   1.00 25.22  ?  331 ASN B N   1 
ATOM   4223 C CA  . ASN B 1 274 ? 24.461 18.761  10.187  1.00 29.84  ?  331 ASN B CA  1 
ATOM   4224 C C   . ASN B 1 274 ? 24.444 20.268  9.945   1.00 29.10  ?  331 ASN B C   1 
ATOM   4225 O O   . ASN B 1 274 ? 24.568 21.043  10.895  1.00 33.51  ?  331 ASN B O   1 
ATOM   4226 C CB  . ASN B 1 274 ? 25.526 18.376  11.221  1.00 32.47  ?  331 ASN B CB  1 
ATOM   4227 C CG  . ASN B 1 274 ? 25.421 16.907  11.628  1.00 36.97  ?  331 ASN B CG  1 
ATOM   4228 O OD1 . ASN B 1 274 ? 26.427 16.249  11.899  1.00 45.30  ?  331 ASN B OD1 1 
ATOM   4229 N ND2 . ASN B 1 274 ? 24.190 16.378  11.615  1.00 40.63  ?  331 ASN B ND2 1 
ATOM   4230 N N   . LEU B 1 275 ? 24.273 20.714  8.691   1.00 22.54  ?  332 LEU B N   1 
ATOM   4231 C CA  . LEU B 1 275 ? 23.928 22.117  8.471   1.00 19.63  ?  332 LEU B CA  1 
ATOM   4232 C C   . LEU B 1 275 ? 22.625 22.454  9.185   1.00 25.77  ?  332 LEU B C   1 
ATOM   4233 O O   . LEU B 1 275 ? 22.495 23.525  9.795   1.00 29.23  ?  332 LEU B O   1 
ATOM   4234 C CB  . LEU B 1 275 ? 23.813 22.408  6.971   1.00 25.92  ?  332 LEU B CB  1 
ATOM   4235 C CG  . LEU B 1 275 ? 23.620 23.886  6.601   1.00 21.20  ?  332 LEU B CG  1 
ATOM   4236 C CD1 . LEU B 1 275 ? 24.603 24.806  7.339   1.00 25.91  ?  332 LEU B CD1 1 
ATOM   4237 C CD2 . LEU B 1 275 ? 23.626 24.110  5.071   1.00 22.90  ?  332 LEU B CD2 1 
ATOM   4238 N N   . TYR B 1 276 ? 21.656 21.539  9.143   1.00 24.54  ?  333 TYR B N   1 
ATOM   4239 C CA  . TYR B 1 276 ? 20.386 21.745  9.837   1.00 25.00  ?  333 TYR B CA  1 
ATOM   4240 C C   . TYR B 1 276 ? 20.164 20.605  10.829  1.00 29.27  ?  333 TYR B C   1 
ATOM   4241 O O   . TYR B 1 276 ? 19.198 19.846  10.702  1.00 36.39  ?  333 TYR B O   1 
ATOM   4242 C CB  . TYR B 1 276 ? 19.243 21.815  8.825   1.00 25.30  ?  333 TYR B CB  1 
ATOM   4243 C CG  . TYR B 1 276 ? 19.427 22.891  7.779   1.00 23.75  ?  333 TYR B CG  1 
ATOM   4244 C CD1 . TYR B 1 276 ? 19.436 24.241  8.128   1.00 23.11  ?  333 TYR B CD1 1 
ATOM   4245 C CD2 . TYR B 1 276 ? 19.612 22.557  6.441   1.00 19.28  ?  333 TYR B CD2 1 
ATOM   4246 C CE1 . TYR B 1 276 ? 19.598 25.234  7.170   1.00 21.60  ?  333 TYR B CE1 1 
ATOM   4247 C CE2 . TYR B 1 276 ? 19.783 23.544  5.473   1.00 21.93  ?  333 TYR B CE2 1 
ATOM   4248 C CZ  . TYR B 1 276 ? 19.782 24.872  5.850   1.00 20.57  ?  333 TYR B CZ  1 
ATOM   4249 O OH  . TYR B 1 276 ? 19.950 25.844  4.892   1.00 25.60  ?  333 TYR B OH  1 
ATOM   4250 N N   . PHE B 1 277 ? 21.070 20.464  11.794  1.00 27.60  ?  334 PHE B N   1 
ATOM   4251 C CA  . PHE B 1 277 ? 21.021 19.355  12.744  1.00 28.50  ?  334 PHE B CA  1 
ATOM   4252 C C   . PHE B 1 277 ? 19.707 19.344  13.513  1.00 35.80  ?  334 PHE B C   1 
ATOM   4253 O O   . PHE B 1 277 ? 19.343 20.330  14.162  1.00 35.95  ?  334 PHE B O   1 
ATOM   4254 C CB  . PHE B 1 277 ? 22.202 19.447  13.708  1.00 32.11  ?  334 PHE B CB  1 
ATOM   4255 C CG  . PHE B 1 277 ? 22.292 18.300  14.683  1.00 33.99  ?  334 PHE B CG  1 
ATOM   4256 C CD1 . PHE B 1 277 ? 23.246 17.309  14.514  1.00 36.36  ?  334 PHE B CD1 1 
ATOM   4257 C CD2 . PHE B 1 277 ? 21.468 18.253  15.807  1.00 46.27  ?  334 PHE B CD2 1 
ATOM   4258 C CE1 . PHE B 1 277 ? 23.347 16.265  15.418  1.00 33.72  ?  334 PHE B CE1 1 
ATOM   4259 C CE2 . PHE B 1 277 ? 21.562 17.208  16.715  1.00 39.07  ?  334 PHE B CE2 1 
ATOM   4260 C CZ  . PHE B 1 277 ? 22.500 16.219  16.516  1.00 41.59  ?  334 PHE B CZ  1 
ATOM   4261 N N   . GLN B 1 278 ? 19.012 18.214  13.454  1.00 33.96  ?  335 GLN B N   1 
ATOM   4262 C CA  . GLN B 1 278 ? 17.722 18.070  14.109  1.00 49.01  ?  335 GLN B CA  1 
ATOM   4263 C C   . GLN B 1 278 ? 17.625 16.690  14.742  1.00 52.62  ?  335 GLN B C   1 
ATOM   4264 O O   . GLN B 1 278 ? 18.263 15.746  14.267  1.00 56.83  ?  335 GLN B O   1 
ATOM   4265 C CB  . GLN B 1 278 ? 16.591 18.282  13.103  1.00 45.33  ?  335 GLN B CB  1 
ATOM   4266 C CG  . GLN B 1 278 ? 16.438 19.721  12.641  1.00 58.96  ?  335 GLN B CG  1 
ATOM   4267 C CD  . GLN B 1 278 ? 15.629 19.835  11.364  1.00 71.44  ?  335 GLN B CD  1 
ATOM   4268 O OE1 . GLN B 1 278 ? 14.496 19.352  11.286  1.00 84.84  ?  335 GLN B OE1 1 
ATOM   4269 N NE2 . GLN B 1 278 ? 16.206 20.477  10.351  1.00 65.12  ?  335 GLN B NE2 1 
HETATM 4270 C C1  A MBG C 2 .   ? 16.792 -13.005 -21.154 0.51 14.33  ?  401 MBG A C1  1 
HETATM 4271 C C1  B MBG C 2 .   ? 16.962 -12.874 -21.375 0.49 14.01  ?  401 MBG A C1  1 
HETATM 4272 C C2  A MBG C 2 .   ? 17.380 -12.238 -19.986 0.51 13.06  ?  401 MBG A C2  1 
HETATM 4273 C C2  B MBG C 2 .   ? 17.508 -12.197 -20.135 0.49 12.77  ?  401 MBG A C2  1 
HETATM 4274 C C3  A MBG C 2 .   ? 16.464 -11.165 -19.506 0.51 13.42  ?  401 MBG A C3  1 
HETATM 4275 C C3  B MBG C 2 .   ? 16.517 -11.257 -19.533 0.49 13.38  ?  401 MBG A C3  1 
HETATM 4276 C C4  A MBG C 2 .   ? 15.972 -10.257 -20.600 0.51 12.47  ?  401 MBG A C4  1 
HETATM 4277 C C4  B MBG C 2 .   ? 15.882 -10.310 -20.517 0.49 12.47  ?  401 MBG A C4  1 
HETATM 4278 C C5  A MBG C 2 .   ? 15.467 -11.102 -21.779 0.51 13.50  ?  401 MBG A C5  1 
HETATM 4279 C C5  B MBG C 2 .   ? 15.356 -11.105 -21.716 0.49 13.47  ?  401 MBG A C5  1 
HETATM 4280 C C6  A MBG C 2 .   ? 15.025 -10.262 -22.946 0.51 15.90  ?  401 MBG A C6  1 
HETATM 4281 C C6  B MBG C 2 .   ? 14.697 -10.213 -22.734 0.49 15.69  ?  401 MBG A C6  1 
HETATM 4282 C C7  A MBG C 2 .   ? 18.853 -13.613 -22.150 0.51 6.58   ?  401 MBG A C7  1 
HETATM 4283 C C7  B MBG C 2 .   ? 17.324 -14.682 -22.710 0.49 22.96  ?  401 MBG A C7  1 
HETATM 4284 O O1  A MBG C 2 .   ? 17.635 -13.999 -21.558 0.51 20.48  ?  401 MBG A O1  1 
HETATM 4285 O O1  B MBG C 2 .   ? 17.917 -13.633 -21.969 0.49 15.64  ?  401 MBG A O1  1 
HETATM 4286 O O2  A MBG C 2 .   ? 17.599 -13.188 -18.927 0.51 13.33  ?  401 MBG A O2  1 
HETATM 4287 O O2  B MBG C 2 .   ? 17.790 -13.254 -19.197 0.49 12.99  ?  401 MBG A O2  1 
HETATM 4288 O O3  A MBG C 2 .   ? 17.142 -10.355 -18.508 0.51 14.48  ?  401 MBG A O3  1 
HETATM 4289 O O3  B MBG C 2 .   ? 17.139 -10.471 -18.480 0.49 14.50  ?  401 MBG A O3  1 
HETATM 4290 O O4  A MBG C 2 .   ? 17.025 -9.386  -21.036 0.51 12.85  ?  401 MBG A O4  1 
HETATM 4291 O O4  B MBG C 2 .   ? 16.825 -9.332  -20.970 0.49 12.80  ?  401 MBG A O4  1 
HETATM 4292 O O5  A MBG C 2 .   ? 16.498 -12.038 -22.259 0.51 15.14  ?  401 MBG A O5  1 
HETATM 4293 O O5  B MBG C 2 .   ? 16.456 -11.852 -22.346 0.49 14.60  ?  401 MBG A O5  1 
HETATM 4294 O O6  A MBG C 2 .   ? 14.512 -11.122 -23.952 0.51 17.29  ?  401 MBG A O6  1 
HETATM 4295 O O6  B MBG C 2 .   ? 14.177 -10.986 -23.801 0.49 18.37  ?  401 MBG A O6  1 
HETATM 4296 C C1  . EDO D 3 .   ? 22.370 -22.540 9.078   1.00 43.37  ?  402 EDO A C1  1 
HETATM 4297 O O1  . EDO D 3 .   ? 22.014 -23.304 7.916   1.00 38.49  ?  402 EDO A O1  1 
HETATM 4298 C C2  . EDO D 3 .   ? 23.646 -21.749 8.808   1.00 46.60  ?  402 EDO A C2  1 
HETATM 4299 O O2  . EDO D 3 .   ? 23.734 -20.622 9.688   1.00 59.49  ?  402 EDO A O2  1 
HETATM 4300 C C1  . EDO E 3 .   ? 6.897  5.527   -13.659 1.00 45.42  ?  403 EDO A C1  1 
HETATM 4301 O O1  . EDO E 3 .   ? 5.812  4.786   -14.227 1.00 37.95  ?  403 EDO A O1  1 
HETATM 4302 C C2  . EDO E 3 .   ? 6.570  5.857   -12.211 1.00 47.41  ?  403 EDO A C2  1 
HETATM 4303 O O2  . EDO E 3 .   ? 6.536  4.665   -11.426 1.00 35.62  ?  403 EDO A O2  1 
HETATM 4304 C C1  A MBG F 2 .   ? 26.991 9.783   -22.793 0.62 18.07  ?  401 MBG B C1  1 
HETATM 4305 C C1  B MBG F 2 .   ? 26.702 9.553   -23.074 0.38 17.37  ?  401 MBG B C1  1 
HETATM 4306 C C2  A MBG F 2 .   ? 26.310 9.229   -21.551 0.62 14.53  ?  401 MBG B C2  1 
HETATM 4307 C C2  B MBG F 2 .   ? 26.138 9.108   -21.733 0.38 15.28  ?  401 MBG B C2  1 
HETATM 4308 C C3  A MBG F 2 .   ? 27.215 8.263   -20.856 0.62 15.22  ?  401 MBG B C3  1 
HETATM 4309 C C3  B MBG F 2 .   ? 27.132 8.312   -20.949 0.38 15.16  ?  401 MBG B C3  1 
HETATM 4310 C C4  A MBG F 2 .   ? 27.826 7.210   -21.740 0.62 14.92  ?  401 MBG B C4  1 
HETATM 4311 C C4  B MBG F 2 .   ? 27.844 7.244   -21.732 0.38 14.91  ?  401 MBG B C4  1 
HETATM 4312 C C5  A MBG F 2 .   ? 28.383 7.831   -23.022 0.62 18.01  ?  401 MBG B C5  1 
HETATM 4313 C C5  B MBG F 2 .   ? 28.393 7.818   -23.034 0.38 18.09  ?  401 MBG B C5  1 
HETATM 4314 C C6  A MBG F 2 .   ? 28.854 6.798   -24.007 0.62 22.38  ?  401 MBG B C6  1 
HETATM 4315 C C6  B MBG F 2 .   ? 29.075 6.758   -23.851 0.38 21.75  ?  401 MBG B C6  1 
HETATM 4316 C C7  A MBG F 2 .   ? 24.992 10.216  -23.993 0.62 9.66   ?  401 MBG B C7  1 
HETATM 4317 C C7  B MBG F 2 .   ? 26.310 11.169  -24.659 0.38 26.85  ?  401 MBG B C7  1 
HETATM 4318 O O1  A MBG F 2 .   ? 26.203 10.690  -23.444 0.62 23.07  ?  401 MBG B O1  1 
HETATM 4319 O O1  B MBG F 2 .   ? 25.752 10.159  -23.847 0.38 19.50  ?  401 MBG B O1  1 
HETATM 4320 O O2  A MBG F 2 .   ? 25.958 10.316  -20.668 0.62 16.11  ?  401 MBG B O2  1 
HETATM 4321 O O2  B MBG F 2 .   ? 25.770 10.293  -21.001 0.38 13.76  ?  401 MBG B O2  1 
HETATM 4322 O O3  A MBG F 2 .   ? 26.487 7.582   -19.806 0.62 16.33  ?  401 MBG B O3  1 
HETATM 4323 O O3  B MBG F 2 .   ? 26.467 7.673   -19.828 0.38 16.31  ?  401 MBG B O3  1 
HETATM 4324 O O4  A MBG F 2 .   ? 26.810 6.243   -22.078 0.62 15.13  ?  401 MBG B O4  1 
HETATM 4325 O O4  B MBG F 2 .   ? 26.923 6.183   -22.041 0.38 15.29  ?  401 MBG B O4  1 
HETATM 4326 O O5  A MBG F 2 .   ? 27.342 8.626   -23.671 0.62 16.18  ?  401 MBG B O5  1 
HETATM 4327 O O5  B MBG F 2 .   ? 27.285 8.384   -23.806 0.38 16.48  ?  401 MBG B O5  1 
HETATM 4328 O O6  A MBG F 2 .   ? 29.560 7.471   -25.030 0.62 22.03  ?  401 MBG B O6  1 
HETATM 4329 O O6  B MBG F 2 .   ? 29.738 7.376   -24.933 0.38 21.95  ?  401 MBG B O6  1 
HETATM 4330 C C1  . EDO G 3 .   ? 26.761 16.162  -22.425 1.00 37.70  ?  402 EDO B C1  1 
HETATM 4331 O O1  . EDO G 3 .   ? 27.602 15.578  -23.428 1.00 61.84  ?  402 EDO B O1  1 
HETATM 4332 C C2  . EDO G 3 .   ? 25.326 16.241  -22.924 1.00 40.21  ?  402 EDO B C2  1 
HETATM 4333 O O2  . EDO G 3 .   ? 24.441 16.676  -21.870 1.00 31.35  ?  402 EDO B O2  1 
HETATM 4334 C C1  . EDO H 3 .   ? 40.018 21.203  -11.222 1.00 34.10  ?  403 EDO B C1  1 
HETATM 4335 O O1  . EDO H 3 .   ? 40.869 21.332  -12.377 1.00 54.79  ?  403 EDO B O1  1 
HETATM 4336 C C2  . EDO H 3 .   ? 40.486 22.134  -10.101 1.00 55.49  ?  403 EDO B C2  1 
HETATM 4337 O O2  . EDO H 3 .   ? 40.144 23.506  -10.369 1.00 46.55  ?  403 EDO B O2  1 
HETATM 4338 O O   . HOH I 4 .   ? 19.749 -23.209 7.472   1.00 30.29  ?  501 HOH A O   1 
HETATM 4339 O O   . HOH I 4 .   ? 16.028 -11.415 -25.765 1.00 25.73  ?  502 HOH A O   1 
HETATM 4340 O O   . HOH I 4 .   ? 24.776 -21.236 11.744  1.00 84.21  ?  503 HOH A O   1 
HETATM 4341 O O   . HOH I 4 .   ? 6.912  -17.077 -30.480 1.00 33.54  ?  504 HOH A O   1 
HETATM 4342 O O   . HOH I 4 .   ? 1.628  -12.572 -3.591  1.00 32.28  ?  505 HOH A O   1 
HETATM 4343 O O   . HOH I 4 .   ? 31.002 -28.952 -47.138 1.00 38.54  ?  506 HOH A O   1 
HETATM 4344 O O   . HOH I 4 .   ? 23.977 -33.032 -39.705 1.00 37.46  ?  507 HOH A O   1 
HETATM 4345 O O   . HOH I 4 .   ? 12.399 -13.753 -46.704 1.00 42.06  ?  508 HOH A O   1 
HETATM 4346 O O   . HOH I 4 .   ? 16.838 -21.906 -15.893 1.00 23.04  ?  509 HOH A O   1 
HETATM 4347 O O   . HOH I 4 .   ? 16.386 -29.387 -28.668 1.00 39.16  ?  510 HOH A O   1 
HETATM 4348 O O   . HOH I 4 .   ? 8.760  2.207   -1.397  1.00 23.17  ?  511 HOH A O   1 
HETATM 4349 O O   . HOH I 4 .   ? 5.236  2.561   -11.237 1.00 27.85  ?  512 HOH A O   1 
HETATM 4350 O O   . HOH I 4 .   ? 30.612 -18.448 -12.481 1.00 32.49  ?  513 HOH A O   1 
HETATM 4351 O O   . HOH I 4 .   ? -2.403 -7.754  -3.327  1.00 35.09  ?  514 HOH A O   1 
HETATM 4352 O O   . HOH I 4 .   ? 1.896  -10.323 -10.657 1.00 22.32  ?  515 HOH A O   1 
HETATM 4353 O O   . HOH I 4 .   ? 12.288 -9.732  -24.892 1.00 25.28  ?  516 HOH A O   1 
HETATM 4354 O O   . HOH I 4 .   ? 7.360  -15.701 6.532   1.00 40.32  ?  517 HOH A O   1 
HETATM 4355 O O   . HOH I 4 .   ? 29.656 -12.411 -49.239 1.00 35.24  ?  518 HOH A O   1 
HETATM 4356 O O   . HOH I 4 .   ? 24.401 -25.735 -32.509 1.00 33.97  ?  519 HOH A O   1 
HETATM 4357 O O   . HOH I 4 .   ? 16.037 -13.451 -26.782 1.00 32.83  ?  520 HOH A O   1 
HETATM 4358 O O   . HOH I 4 .   ? 19.516 -19.889 -18.673 1.00 24.21  ?  521 HOH A O   1 
HETATM 4359 O O   . HOH I 4 .   ? 11.623 -6.087  -28.053 1.00 33.52  ?  522 HOH A O   1 
HETATM 4360 O O   . HOH I 4 .   ? 32.130 -19.198 -18.749 1.00 27.35  ?  523 HOH A O   1 
HETATM 4361 O O   . HOH I 4 .   ? 28.043 -9.786  -47.395 1.00 30.40  ?  524 HOH A O   1 
HETATM 4362 O O   . HOH I 4 .   ? 24.990 -15.023 -1.435  1.00 22.18  ?  525 HOH A O   1 
HETATM 4363 O O   . HOH I 4 .   ? 1.905  -25.124 -0.220  1.00 29.38  ?  526 HOH A O   1 
HETATM 4364 O O   . HOH I 4 .   ? 23.142 -22.388 5.745   1.00 26.08  ?  527 HOH A O   1 
HETATM 4365 O O   . HOH I 4 .   ? 4.901  -6.201  -14.589 1.00 28.65  ?  528 HOH A O   1 
HETATM 4366 O O   . HOH I 4 .   ? 16.358 0.356   -20.121 1.00 19.22  ?  529 HOH A O   1 
HETATM 4367 O O   . HOH I 4 .   ? 27.162 -19.147 -18.445 1.00 22.00  ?  530 HOH A O   1 
HETATM 4368 O O   . HOH I 4 .   ? 29.747 -14.154 -0.758  1.00 31.95  ?  531 HOH A O   1 
HETATM 4369 O O   . HOH I 4 .   ? 24.175 -27.058 -18.396 1.00 39.21  ?  532 HOH A O   1 
HETATM 4370 O O   . HOH I 4 .   ? 9.739  -31.962 -9.998  1.00 28.28  ?  533 HOH A O   1 
HETATM 4371 O O   . HOH I 4 .   ? 19.344 -27.881 -2.084  1.00 24.15  ?  534 HOH A O   1 
HETATM 4372 O O   . HOH I 4 .   ? 29.186 -4.882  -20.276 1.00 20.17  ?  535 HOH A O   1 
HETATM 4373 O O   . HOH I 4 .   ? 9.905  -26.527 -18.826 1.00 30.18  ?  536 HOH A O   1 
HETATM 4374 O O   . HOH I 4 .   ? 31.265 -8.227  -19.726 1.00 28.58  ?  537 HOH A O   1 
HETATM 4375 O O   . HOH I 4 .   ? 8.303  -22.093 -0.862  1.00 21.55  ?  538 HOH A O   1 
HETATM 4376 O O   . HOH I 4 .   ? 7.704  -11.364 -24.263 1.00 34.63  ?  539 HOH A O   1 
HETATM 4377 O O   . HOH I 4 .   ? 6.029  3.656   -7.814  1.00 27.18  ?  540 HOH A O   1 
HETATM 4378 O O   . HOH I 4 .   ? 28.431 -1.280  -15.303 1.00 14.17  ?  541 HOH A O   1 
HETATM 4379 O O   . HOH I 4 .   ? 3.320  5.393   -14.906 1.00 31.04  ?  542 HOH A O   1 
HETATM 4380 O O   . HOH I 4 .   ? 13.556 -4.666  -37.115 1.00 28.26  ?  543 HOH A O   1 
HETATM 4381 O O   . HOH I 4 .   ? 5.977  -3.106  1.923   1.00 23.40  ?  544 HOH A O   1 
HETATM 4382 O O   . HOH I 4 .   ? 14.586 -30.473 0.941   1.00 31.79  ?  545 HOH A O   1 
HETATM 4383 O O   . HOH I 4 .   ? 30.391 -18.910 -9.783  1.00 31.79  ?  546 HOH A O   1 
HETATM 4384 O O   . HOH I 4 .   ? 18.558 -21.048 -43.627 1.00 35.66  ?  547 HOH A O   1 
HETATM 4385 O O   . HOH I 4 .   ? 30.771 -12.981 -12.338 1.00 27.04  ?  548 HOH A O   1 
HETATM 4386 O O   . HOH I 4 .   ? -2.770 -9.556  -6.496  1.00 29.38  ?  549 HOH A O   1 
HETATM 4387 O O   . HOH I 4 .   ? 6.783  -33.502 -5.263  1.00 26.03  ?  550 HOH A O   1 
HETATM 4388 O O   . HOH I 4 .   ? 28.527 -27.586 -39.790 1.00 38.90  ?  551 HOH A O   1 
HETATM 4389 O O   . HOH I 4 .   ? 22.576 -5.533  -13.985 1.00 17.28  ?  552 HOH A O   1 
HETATM 4390 O O   . HOH I 4 .   ? 14.961 -29.497 -11.144 1.00 38.11  ?  553 HOH A O   1 
HETATM 4391 O O   . HOH I 4 .   ? 33.056 -5.348  -14.530 1.00 28.00  ?  554 HOH A O   1 
HETATM 4392 O O   . HOH I 4 .   ? 16.008 2.570   1.264   1.00 24.79  ?  555 HOH A O   1 
HETATM 4393 O O   . HOH I 4 .   ? 9.872  -10.793 -32.753 1.00 29.58  ?  556 HOH A O   1 
HETATM 4394 O O   . HOH I 4 .   ? 25.607 -17.013 -47.285 1.00 30.01  ?  557 HOH A O   1 
HETATM 4395 O O   . HOH I 4 .   ? 5.668  6.000   -9.248  1.00 25.55  ?  558 HOH A O   1 
HETATM 4396 O O   . HOH I 4 .   ? 25.348 -13.395 0.770   1.00 25.57  ?  559 HOH A O   1 
HETATM 4397 O O   . HOH I 4 .   ? 6.501  -23.171 2.140   1.00 33.80  ?  560 HOH A O   1 
HETATM 4398 O O   . HOH I 4 .   ? 17.636 -14.761 4.424   1.00 15.47  ?  561 HOH A O   1 
HETATM 4399 O O   . HOH I 4 .   ? 32.621 -5.958  -25.994 1.00 29.89  ?  562 HOH A O   1 
HETATM 4400 O O   . HOH I 4 .   ? 13.793 -25.716 -24.389 1.00 39.07  ?  563 HOH A O   1 
HETATM 4401 O O   . HOH I 4 .   ? 23.760 -24.384 4.052   1.00 24.88  ?  564 HOH A O   1 
HETATM 4402 O O   . HOH I 4 .   ? 6.405  -30.861 2.124   1.00 20.42  ?  565 HOH A O   1 
HETATM 4403 O O   . HOH I 4 .   ? 19.546 -8.456  -16.279 1.00 12.90  ?  566 HOH A O   1 
HETATM 4404 O O   . HOH I 4 .   ? 20.865 -9.409  -28.520 1.00 17.94  ?  567 HOH A O   1 
HETATM 4405 O O   . HOH I 4 .   ? 29.951 -4.011  -11.760 1.00 14.40  ?  568 HOH A O   1 
HETATM 4406 O O   . HOH I 4 .   ? 1.867  -8.783  -13.499 1.00 33.62  ?  569 HOH A O   1 
HETATM 4407 O O   . HOH I 4 .   ? 30.679 -8.800  -15.953 1.00 32.22  ?  570 HOH A O   1 
HETATM 4408 O O   . HOH I 4 .   ? 17.105 -4.313  2.510   1.00 16.50  ?  571 HOH A O   1 
HETATM 4409 O O   . HOH I 4 .   ? 29.260 -9.558  -21.105 1.00 46.74  ?  572 HOH A O   1 
HETATM 4410 O O   . HOH I 4 .   ? 19.342 -14.405 8.379   1.00 29.83  ?  573 HOH A O   1 
HETATM 4411 O O   . HOH I 4 .   ? 21.994 -29.100 -4.696  1.00 29.94  ?  574 HOH A O   1 
HETATM 4412 O O   . HOH I 4 .   ? 7.525  4.053   -16.243 1.00 34.87  ?  575 HOH A O   1 
HETATM 4413 O O   . HOH I 4 .   ? 11.746 -20.196 4.963   1.00 19.60  ?  576 HOH A O   1 
HETATM 4414 O O   . HOH I 4 .   ? 0.763  -12.530 -9.261  1.00 26.95  ?  577 HOH A O   1 
HETATM 4415 O O   . HOH I 4 .   ? 19.488 -22.548 -34.767 1.00 24.44  ?  578 HOH A O   1 
HETATM 4416 O O   . HOH I 4 .   ? 3.780  -3.618  0.237   1.00 23.72  ?  579 HOH A O   1 
HETATM 4417 O O   . HOH I 4 .   ? 32.051 -6.886  -36.179 1.00 25.15  ?  580 HOH A O   1 
HETATM 4418 O O   . HOH I 4 .   ? 10.538 -16.355 -15.147 1.00 14.93  ?  581 HOH A O   1 
HETATM 4419 O O   . HOH I 4 .   ? 14.780 -8.472  -48.351 1.00 30.76  ?  582 HOH A O   1 
HETATM 4420 O O   . HOH I 4 .   ? 15.121 -14.908 5.785   1.00 26.74  ?  583 HOH A O   1 
HETATM 4421 O O   . HOH I 4 .   ? 21.551 -11.771 -47.548 1.00 34.66  ?  584 HOH A O   1 
HETATM 4422 O O   . HOH I 4 .   ? 33.812 -24.538 -47.482 1.00 31.01  ?  585 HOH A O   1 
HETATM 4423 O O   . HOH I 4 .   ? 36.748 -18.208 -29.717 1.00 46.50  ?  586 HOH A O   1 
HETATM 4424 O O   . HOH I 4 .   ? 30.115 -7.936  -46.513 1.00 33.77  ?  587 HOH A O   1 
HETATM 4425 O O   . HOH I 4 .   ? 27.197 -12.344 -17.404 1.00 16.73  ?  588 HOH A O   1 
HETATM 4426 O O   . HOH I 4 .   ? 14.858 -7.054  -24.920 1.00 24.01  ?  589 HOH A O   1 
HETATM 4427 O O   . HOH I 4 .   ? 26.090 -29.256 -30.590 1.00 36.91  ?  590 HOH A O   1 
HETATM 4428 O O   . HOH I 4 .   ? 19.844 -3.030  0.157   1.00 17.33  ?  591 HOH A O   1 
HETATM 4429 O O   . HOH I 4 .   ? 8.345  -6.957  -21.241 1.00 30.96  ?  592 HOH A O   1 
HETATM 4430 O O   . HOH I 4 .   ? 27.843 -8.128  -12.306 1.00 14.29  ?  593 HOH A O   1 
HETATM 4431 O O   . HOH I 4 .   ? 2.629  -2.634  -6.531  1.00 19.23  ?  594 HOH A O   1 
HETATM 4432 O O   . HOH I 4 .   ? 20.024 -18.496 -24.590 1.00 26.05  ?  595 HOH A O   1 
HETATM 4433 O O   . HOH I 4 .   ? 19.214 -0.880  1.791   1.00 23.85  ?  596 HOH A O   1 
HETATM 4434 O O   . HOH I 4 .   ? 28.197 -3.837  -35.535 1.00 21.17  ?  597 HOH A O   1 
HETATM 4435 O O   . HOH I 4 .   ? 16.254 -27.054 3.576   1.00 36.44  ?  598 HOH A O   1 
HETATM 4436 O O   . HOH I 4 .   ? 18.405 -7.592  -18.975 1.00 14.21  ?  599 HOH A O   1 
HETATM 4437 O O   . HOH I 4 .   ? 34.122 -21.338 -36.338 1.00 31.25  ?  600 HOH A O   1 
HETATM 4438 O O   . HOH I 4 .   ? 13.690 -26.169 2.865   1.00 34.88  ?  601 HOH A O   1 
HETATM 4439 O O   . HOH I 4 .   ? 34.754 -16.226 -48.529 1.00 36.82  ?  602 HOH A O   1 
HETATM 4440 O O   . HOH I 4 .   ? 24.759 -4.259  -18.815 1.00 16.94  ?  603 HOH A O   1 
HETATM 4441 O O   . HOH I 4 .   ? 15.078 -23.533 -24.958 1.00 34.20  ?  604 HOH A O   1 
HETATM 4442 O O   . HOH I 4 .   ? 29.433 -8.570  -23.685 1.00 15.95  ?  605 HOH A O   1 
HETATM 4443 O O   . HOH I 4 .   ? 4.943  2.319   -3.501  1.00 30.39  ?  606 HOH A O   1 
HETATM 4444 O O   . HOH I 4 .   ? 18.134 -5.618  -55.612 1.00 35.85  ?  607 HOH A O   1 
HETATM 4445 O O   . HOH I 4 .   ? 6.439  -26.396 -6.715  1.00 18.33  ?  608 HOH A O   1 
HETATM 4446 O O   . HOH I 4 .   ? 10.838 -4.220  -20.250 1.00 21.13  ?  609 HOH A O   1 
HETATM 4447 O O   . HOH I 4 .   ? 23.459 -6.481  3.705   1.00 26.80  ?  610 HOH A O   1 
HETATM 4448 O O   . HOH I 4 .   ? 26.985 -23.644 -3.252  1.00 38.17  ?  611 HOH A O   1 
HETATM 4449 O O   . HOH I 4 .   ? 11.761 -5.584  9.335   1.00 38.71  ?  612 HOH A O   1 
HETATM 4450 O O   . HOH I 4 .   ? 28.233 -8.957  -17.118 1.00 16.48  ?  613 HOH A O   1 
HETATM 4451 O O   . HOH I 4 .   ? 17.045 -16.428 -10.097 1.00 13.26  ?  614 HOH A O   1 
HETATM 4452 O O   . HOH I 4 .   ? 4.224  -9.943  -16.994 1.00 27.23  ?  615 HOH A O   1 
HETATM 4453 O O   . HOH I 4 .   ? 34.424 -27.142 -46.869 1.00 36.31  ?  616 HOH A O   1 
HETATM 4454 O O   . HOH I 4 .   ? 33.920 -16.055 -21.631 1.00 32.01  ?  617 HOH A O   1 
HETATM 4455 O O   . HOH I 4 .   ? 28.871 -20.839 -6.712  1.00 27.07  ?  618 HOH A O   1 
HETATM 4456 O O   . HOH I 4 .   ? 11.168 -12.649 5.851   1.00 21.40  ?  619 HOH A O   1 
HETATM 4457 O O   . HOH I 4 .   ? 0.371  -3.775  -7.608  1.00 17.34  ?  620 HOH A O   1 
HETATM 4458 O O   . HOH I 4 .   ? 3.030  -12.752 -1.183  1.00 27.65  ?  621 HOH A O   1 
HETATM 4459 O O   . HOH I 4 .   ? 17.725 -3.074  -45.123 1.00 34.95  ?  622 HOH A O   1 
HETATM 4460 O O   . HOH I 4 .   ? 25.136 -8.207  2.495   1.00 23.35  ?  623 HOH A O   1 
HETATM 4461 O O   . HOH I 4 .   ? 28.748 -18.878 -16.010 1.00 25.48  ?  624 HOH A O   1 
HETATM 4462 O O   . HOH I 4 .   ? 11.509 -5.434  -43.789 1.00 32.99  ?  625 HOH A O   1 
HETATM 4463 O O   . HOH I 4 .   ? 15.926 -16.981 -31.042 1.00 17.92  ?  626 HOH A O   1 
HETATM 4464 O O   . HOH I 4 .   ? -1.613 -24.444 -2.418  1.00 33.66  ?  627 HOH A O   1 
HETATM 4465 O O   . HOH I 4 .   ? 32.186 -5.354  -28.648 1.00 28.22  ?  628 HOH A O   1 
HETATM 4466 O O   . HOH I 4 .   ? 32.714 -12.531 -27.463 1.00 23.57  ?  629 HOH A O   1 
HETATM 4467 O O   . HOH I 4 .   ? 17.487 -4.411  -0.180  1.00 14.47  ?  630 HOH A O   1 
HETATM 4468 O O   . HOH I 4 .   ? 30.872 -6.977  -5.839  1.00 17.01  ?  631 HOH A O   1 
HETATM 4469 O O   . HOH I 4 .   ? 18.016 -1.212  -5.707  1.00 18.48  ?  632 HOH A O   1 
HETATM 4470 O O   . HOH I 4 .   ? 30.551 -4.779  -36.966 1.00 30.27  ?  633 HOH A O   1 
HETATM 4471 O O   . HOH I 4 .   ? 37.082 -7.653  -31.184 1.00 36.38  ?  634 HOH A O   1 
HETATM 4472 O O   . HOH I 4 .   ? 17.130 -19.217 -10.211 1.00 13.37  ?  635 HOH A O   1 
HETATM 4473 O O   . HOH I 4 .   ? 27.620 -21.403 -47.262 1.00 36.83  ?  636 HOH A O   1 
HETATM 4474 O O   . HOH I 4 .   ? 10.826 -5.539  -37.187 1.00 25.59  ?  637 HOH A O   1 
HETATM 4475 O O   . HOH I 4 .   ? 4.930  -8.503  4.216   1.00 38.49  ?  638 HOH A O   1 
HETATM 4476 O O   . HOH I 4 .   ? -0.607 -7.195  -10.715 1.00 33.83  ?  639 HOH A O   1 
HETATM 4477 O O   . HOH I 4 .   ? 20.585 -1.886  -22.097 1.00 16.39  ?  640 HOH A O   1 
HETATM 4478 O O   . HOH I 4 .   ? 17.368 -15.646 -48.599 1.00 43.19  ?  641 HOH A O   1 
HETATM 4479 O O   . HOH I 4 .   ? 4.396  -14.495 -32.888 1.00 29.77  ?  642 HOH A O   1 
HETATM 4480 O O   . HOH I 4 .   ? 21.026 -1.380  -5.149  1.00 21.75  ?  643 HOH A O   1 
HETATM 4481 O O   . HOH I 4 .   ? 13.522 -13.841 -23.337 1.00 28.23  ?  644 HOH A O   1 
HETATM 4482 O O   . HOH I 4 .   ? 31.384 -12.891 -19.095 1.00 26.50  ?  645 HOH A O   1 
HETATM 4483 O O   . HOH I 4 .   ? 31.572 -13.358 -5.934  1.00 37.62  ?  646 HOH A O   1 
HETATM 4484 O O   . HOH I 4 .   ? 5.055  -9.336  -34.808 1.00 27.07  ?  647 HOH A O   1 
HETATM 4485 O O   . HOH I 4 .   ? 9.896  -4.590  -34.912 1.00 28.01  ?  648 HOH A O   1 
HETATM 4486 O O   . HOH I 4 .   ? 23.968 -3.909  -21.325 1.00 22.82  ?  649 HOH A O   1 
HETATM 4487 O O   . HOH I 4 .   ? 22.934 -24.321 -6.320  1.00 19.76  ?  650 HOH A O   1 
HETATM 4488 O O   . HOH I 4 .   ? 0.822  -28.489 -7.743  1.00 38.78  ?  651 HOH A O   1 
HETATM 4489 O O   . HOH I 4 .   ? 32.488 -26.376 -40.823 1.00 31.58  ?  652 HOH A O   1 
HETATM 4490 O O   . HOH I 4 .   ? 12.579 0.329   -14.844 1.00 12.95  ?  653 HOH A O   1 
HETATM 4491 O O   . HOH I 4 .   ? 24.864 -17.554 1.174   1.00 22.77  ?  654 HOH A O   1 
HETATM 4492 O O   . HOH I 4 .   ? 8.706  4.105   -8.028  1.00 27.59  ?  655 HOH A O   1 
HETATM 4493 O O   . HOH I 4 .   ? 8.551  -16.207 -26.612 1.00 28.61  ?  656 HOH A O   1 
HETATM 4494 O O   . HOH I 4 .   ? 12.899 -0.660  -22.220 1.00 25.76  ?  657 HOH A O   1 
HETATM 4495 O O   . HOH I 4 .   ? 24.084 -3.885  -16.250 1.00 15.11  ?  658 HOH A O   1 
HETATM 4496 O O   . HOH I 4 .   ? 7.676  -1.108  -16.152 1.00 28.53  ?  659 HOH A O   1 
HETATM 4497 O O   . HOH I 4 .   ? 28.399 -26.244 -24.450 1.00 31.67  ?  660 HOH A O   1 
HETATM 4498 O O   . HOH I 4 .   ? 11.781 6.413   -2.547  1.00 25.80  ?  661 HOH A O   1 
HETATM 4499 O O   . HOH I 4 .   ? 25.252 -29.162 -25.766 1.00 36.53  ?  662 HOH A O   1 
HETATM 4500 O O   . HOH I 4 .   ? 10.179 -10.767 -23.471 1.00 28.56  ?  663 HOH A O   1 
HETATM 4501 O O   . HOH I 4 .   ? 20.840 -4.434  2.348   1.00 27.39  ?  664 HOH A O   1 
HETATM 4502 O O   . HOH I 4 .   ? 33.111 -22.224 -30.300 1.00 29.50  ?  665 HOH A O   1 
HETATM 4503 O O   . HOH I 4 .   ? 1.130  -15.018 -5.503  1.00 25.05  ?  666 HOH A O   1 
HETATM 4504 O O   . HOH I 4 .   ? 30.469 -17.792 -6.347  1.00 25.06  ?  667 HOH A O   1 
HETATM 4505 O O   . HOH I 4 .   ? 27.183 -23.070 -9.936  1.00 22.61  ?  668 HOH A O   1 
HETATM 4506 O O   . HOH I 4 .   ? 3.237  -12.356 -17.633 1.00 25.45  ?  669 HOH A O   1 
HETATM 4507 O O   . HOH I 4 .   ? 15.691 4.246   -0.910  1.00 25.39  ?  670 HOH A O   1 
HETATM 4508 O O   . HOH I 4 .   ? 19.252 -14.830 -25.125 1.00 37.44  ?  671 HOH A O   1 
HETATM 4509 O O   . HOH I 4 .   ? 21.105 -7.962  6.155   1.00 22.10  ?  672 HOH A O   1 
HETATM 4510 O O   . HOH I 4 .   ? 18.651 -11.506 -24.672 1.00 20.35  ?  673 HOH A O   1 
HETATM 4511 O O   . HOH I 4 .   ? 9.886  -3.915  8.279   1.00 41.55  ?  674 HOH A O   1 
HETATM 4512 O O   . HOH I 4 .   ? 32.006 -9.733  -9.903  1.00 35.37  ?  675 HOH A O   1 
HETATM 4513 O O   . HOH I 4 .   ? 28.864 -11.867 -19.665 1.00 18.67  ?  676 HOH A O   1 
HETATM 4514 O O   . HOH I 4 .   ? 12.898 0.636   -25.374 1.00 31.20  ?  677 HOH A O   1 
HETATM 4515 O O   . HOH I 4 .   ? 4.560  -4.390  -12.514 1.00 24.18  ?  678 HOH A O   1 
HETATM 4516 O O   . HOH I 4 .   ? 5.196  -25.317 0.403   1.00 23.07  ?  679 HOH A O   1 
HETATM 4517 O O   . HOH I 4 .   ? 36.054 -27.213 -44.731 1.00 33.99  ?  680 HOH A O   1 
HETATM 4518 O O   . HOH I 4 .   ? 12.004 -7.066  -24.673 1.00 32.09  ?  681 HOH A O   1 
HETATM 4519 O O   . HOH I 4 .   ? 18.196 -10.287 -51.766 1.00 50.84  ?  682 HOH A O   1 
HETATM 4520 O O   . HOH I 4 .   ? 35.634 -11.728 -24.208 1.00 33.36  ?  683 HOH A O   1 
HETATM 4521 O O   . HOH I 4 .   ? 18.062 -19.810 -22.959 1.00 34.06  ?  684 HOH A O   1 
HETATM 4522 O O   . HOH I 4 .   ? 30.509 -26.223 -48.386 1.00 38.69  ?  685 HOH A O   1 
HETATM 4523 O O   . HOH I 4 .   ? 20.623 -22.617 -41.174 1.00 32.69  ?  686 HOH A O   1 
HETATM 4524 O O   . HOH I 4 .   ? 9.555  5.469   -11.860 1.00 29.68  ?  687 HOH A O   1 
HETATM 4525 O O   . HOH I 4 .   ? 11.322 -4.892  -23.077 1.00 28.41  ?  688 HOH A O   1 
HETATM 4526 O O   . HOH I 4 .   ? 4.181  -27.493 -7.926  1.00 34.97  ?  689 HOH A O   1 
HETATM 4527 O O   . HOH I 4 .   ? 2.099  -19.000 -5.093  1.00 30.40  ?  690 HOH A O   1 
HETATM 4528 O O   . HOH I 4 .   ? 14.780 -1.313  -18.492 1.00 19.27  ?  691 HOH A O   1 
HETATM 4529 O O   . HOH I 4 .   ? 0.722  -6.257  -12.686 1.00 30.21  ?  692 HOH A O   1 
HETATM 4530 O O   . HOH I 4 .   ? 33.347 -5.151  -18.893 1.00 35.53  ?  693 HOH A O   1 
HETATM 4531 O O   . HOH I 4 .   ? 10.212 0.587   -16.375 1.00 20.75  ?  694 HOH A O   1 
HETATM 4532 O O   . HOH I 4 .   ? 2.580  -12.157 -20.094 1.00 33.25  ?  695 HOH A O   1 
HETATM 4533 O O   . HOH I 4 .   ? 23.174 -25.136 -3.671  1.00 24.32  ?  696 HOH A O   1 
HETATM 4534 O O   . HOH I 4 .   ? 1.372  -14.702 -21.288 1.00 35.41  ?  697 HOH A O   1 
HETATM 4535 O O   . HOH I 4 .   ? 6.960  -35.897 -3.902  1.00 29.53  ?  698 HOH A O   1 
HETATM 4536 O O   . HOH I 4 .   ? 23.038 -27.077 -7.069  1.00 26.69  ?  699 HOH A O   1 
HETATM 4537 O O   . HOH I 4 .   ? 11.306 7.532   -5.259  1.00 28.38  ?  700 HOH A O   1 
HETATM 4538 O O   . HOH I 4 .   ? 5.698  -1.911  -13.269 1.00 33.72  ?  701 HOH A O   1 
HETATM 4539 O O   . HOH I 4 .   ? 2.087  -0.668  -4.751  1.00 26.30  ?  702 HOH A O   1 
HETATM 4540 O O   . HOH I 4 .   ? 18.034 -2.387  3.988   1.00 23.83  ?  703 HOH A O   1 
HETATM 4541 O O   . HOH I 4 .   ? 32.196 -12.683 -10.102 1.00 41.09  ?  704 HOH A O   1 
HETATM 4542 O O   . HOH I 4 .   ? 30.481 -8.071  -13.135 1.00 22.23  ?  705 HOH A O   1 
HETATM 4543 O O   . HOH I 4 .   ? 6.107  8.491   -13.580 1.00 40.58  ?  706 HOH A O   1 
HETATM 4544 O O   . HOH I 4 .   ? 22.936 -11.803 6.961   1.00 35.94  ?  707 HOH A O   1 
HETATM 4545 O O   . HOH I 4 .   ? 20.680 -15.744 -23.653 1.00 34.76  ?  708 HOH A O   1 
HETATM 4546 O O   . HOH I 4 .   ? 32.113 -10.324 -12.720 1.00 36.49  ?  709 HOH A O   1 
HETATM 4547 O O   . HOH I 4 .   ? 32.010 -17.250 -3.983  1.00 36.35  ?  710 HOH A O   1 
HETATM 4548 O O   . HOH I 4 .   ? 7.410  -27.271 7.455   1.00 39.22  ?  711 HOH A O   1 
HETATM 4549 O O   . HOH I 4 .   ? 27.345 -22.916 -5.781  1.00 41.77  ?  712 HOH A O   1 
HETATM 4550 O O   . HOH I 4 .   ? 36.720 -24.679 -44.541 1.00 32.62  ?  713 HOH A O   1 
HETATM 4551 O O   . HOH I 4 .   ? -3.295 -6.855  -7.322  1.00 24.53  ?  714 HOH A O   1 
HETATM 4552 O O   . HOH I 4 .   ? 27.142 -25.150 -11.468 1.00 32.59  ?  715 HOH A O   1 
HETATM 4553 O O   . HOH I 4 .   ? 3.011  -22.388 -9.070  1.00 35.18  ?  716 HOH A O   1 
HETATM 4554 O O   . HOH I 4 .   ? 31.847 -5.992  -12.179 1.00 19.15  ?  717 HOH A O   1 
HETATM 4555 O O   . HOH I 4 .   ? 29.523 -5.985  -22.848 1.00 20.57  ?  718 HOH A O   1 
HETATM 4556 O O   . HOH I 4 .   ? 8.660  -37.387 0.285   1.00 33.18  ?  719 HOH A O   1 
HETATM 4557 O O   . HOH I 4 .   ? 26.648 -12.248 2.691   1.00 42.09  ?  720 HOH A O   1 
HETATM 4558 O O   . HOH I 4 .   ? 14.398 3.688   3.062   1.00 30.88  ?  721 HOH A O   1 
HETATM 4559 O O   . HOH I 4 .   ? 10.387 -0.145  -18.984 1.00 25.36  ?  722 HOH A O   1 
HETATM 4560 O O   . HOH I 4 .   ? 2.159  -22.287 0.280   1.00 37.67  ?  723 HOH A O   1 
HETATM 4561 O O   . HOH I 4 .   ? 7.538  7.893   -8.764  1.00 28.67  ?  724 HOH A O   1 
HETATM 4562 O O   . HOH I 4 .   ? -3.314 -7.154  -10.002 1.00 22.86  ?  725 HOH A O   1 
HETATM 4563 O O   . HOH I 4 .   ? 15.202 6.686   0.111   1.00 29.10  ?  726 HOH A O   1 
HETATM 4564 O O   . HOH I 4 .   ? 30.497 -10.322 -3.449  1.00 24.70  ?  727 HOH A O   1 
HETATM 4565 O O   . HOH I 4 .   ? -1.546 -13.179 -10.764 1.00 34.06  ?  728 HOH A O   1 
HETATM 4566 O O   . HOH I 4 .   ? 3.676  -20.286 -17.683 1.00 30.90  ?  729 HOH A O   1 
HETATM 4567 O O   . HOH I 4 .   ? 12.313 -1.915  -19.824 1.00 24.35  ?  730 HOH A O   1 
HETATM 4568 O O   . HOH I 4 .   ? 23.649 -3.641  2.771   1.00 29.60  ?  731 HOH A O   1 
HETATM 4569 O O   . HOH I 4 .   ? 5.404  -26.346 2.723   1.00 35.53  ?  732 HOH A O   1 
HETATM 4570 O O   . HOH I 4 .   ? 25.487 -24.012 -7.329  1.00 28.27  ?  733 HOH A O   1 
HETATM 4571 O O   . HOH I 4 .   ? 1.792  -19.935 -15.641 1.00 39.24  ?  734 HOH A O   1 
HETATM 4572 O O   . HOH J 4 .   ? 35.928 37.668  -4.991  1.00 43.44  ?  501 HOH B O   1 
HETATM 4573 O O   . HOH J 4 .   ? 27.715 20.898  -35.253 1.00 47.99  ?  502 HOH B O   1 
HETATM 4574 O O   . HOH J 4 .   ? 23.291 13.932  -28.243 1.00 34.16  ?  503 HOH B O   1 
HETATM 4575 O O   . HOH J 4 .   ? 27.548 20.758  9.400   1.00 36.93  ?  504 HOH B O   1 
HETATM 4576 O O   . HOH J 4 .   ? 34.523 33.051  -1.151  1.00 29.04  ?  505 HOH B O   1 
HETATM 4577 O O   . HOH J 4 .   ? 19.762 0.768   -21.878 1.00 19.29  ?  506 HOH B O   1 
HETATM 4578 O O   . HOH J 4 .   ? 22.233 25.978  9.701   1.00 37.84  ?  507 HOH B O   1 
HETATM 4579 O O   . HOH J 4 .   ? 17.616 14.554  -4.114  1.00 25.63  ?  508 HOH B O   1 
HETATM 4580 O O   . HOH J 4 .   ? 33.735 -1.721  -0.236  1.00 23.37  ?  509 HOH B O   1 
HETATM 4581 O O   . HOH J 4 .   ? 16.405 16.163  -21.548 1.00 27.77  ?  510 HOH B O   1 
HETATM 4582 O O   . HOH J 4 .   ? 38.282 3.206   -13.864 1.00 34.68  ?  511 HOH B O   1 
HETATM 4583 O O   . HOH J 4 .   ? 28.828 11.794  -32.658 1.00 32.38  ?  512 HOH B O   1 
HETATM 4584 O O   . HOH J 4 .   ? 24.112 26.477  -19.759 1.00 42.36  ?  513 HOH B O   1 
HETATM 4585 O O   . HOH J 4 .   ? 23.235 27.758  -6.589  1.00 28.00  ?  514 HOH B O   1 
HETATM 4586 O O   . HOH J 4 .   ? 14.409 1.871   -21.280 1.00 20.59  ?  515 HOH B O   1 
HETATM 4587 O O   . HOH J 4 .   ? 11.423 1.871   -27.431 1.00 35.82  ?  516 HOH B O   1 
HETATM 4588 O O   . HOH J 4 .   ? 27.265 -3.226  -19.533 1.00 19.28  ?  517 HOH B O   1 
HETATM 4589 O O   . HOH J 4 .   ? 37.266 35.633  -6.388  1.00 30.17  ?  518 HOH B O   1 
HETATM 4590 O O   . HOH J 4 .   ? 21.626 26.455  -33.751 1.00 37.47  ?  519 HOH B O   1 
HETATM 4591 O O   . HOH J 4 .   ? 31.660 5.750   -25.642 1.00 30.78  ?  520 HOH B O   1 
HETATM 4592 O O   . HOH J 4 .   ? 18.768 1.597   -19.525 1.00 18.80  ?  521 HOH B O   1 
HETATM 4593 O O   . HOH J 4 .   ? 16.718 13.592  -1.400  1.00 30.57  ?  522 HOH B O   1 
HETATM 4594 O O   . HOH J 4 .   ? 26.683 14.288  -46.235 1.00 41.61  ?  523 HOH B O   1 
HETATM 4595 O O   . HOH J 4 .   ? 36.227 3.733   2.291   1.00 22.73  ?  524 HOH B O   1 
HETATM 4596 O O   . HOH J 4 .   ? 28.350 -2.879  -39.385 1.00 30.18  ?  525 HOH B O   1 
HETATM 4597 O O   . HOH J 4 .   ? 38.575 2.343   -11.803 1.00 29.05  ?  526 HOH B O   1 
HETATM 4598 O O   . HOH J 4 .   ? 35.876 30.603  -1.524  1.00 29.60  ?  527 HOH B O   1 
HETATM 4599 O O   . HOH J 4 .   ? 16.238 22.451  -16.950 1.00 28.43  ?  528 HOH B O   1 
HETATM 4600 O O   . HOH J 4 .   ? 20.641 3.507   -14.934 1.00 15.62  ?  529 HOH B O   1 
HETATM 4601 O O   . HOH J 4 .   ? 16.326 9.705   -19.875 1.00 19.62  ?  530 HOH B O   1 
HETATM 4602 O O   . HOH J 4 .   ? 39.067 7.281   -17.324 1.00 29.55  ?  531 HOH B O   1 
HETATM 4603 O O   . HOH J 4 .   ? 26.776 15.976  3.451   1.00 20.05  ?  532 HOH B O   1 
HETATM 4604 O O   . HOH J 4 .   ? 38.556 3.848   0.495   1.00 19.75  ?  533 HOH B O   1 
HETATM 4605 O O   . HOH J 4 .   ? 32.829 14.149  -16.984 1.00 17.88  ?  534 HOH B O   1 
HETATM 4606 O O   . HOH J 4 .   ? 27.049 16.709  -40.468 1.00 41.63  ?  535 HOH B O   1 
HETATM 4607 O O   . HOH J 4 .   ? 12.624 17.652  -13.394 1.00 30.68  ?  536 HOH B O   1 
HETATM 4608 O O   . HOH J 4 .   ? 11.545 7.936   -29.831 1.00 29.86  ?  537 HOH B O   1 
HETATM 4609 O O   . HOH J 4 .   ? 20.579 24.817  2.461   1.00 30.02  ?  538 HOH B O   1 
HETATM 4610 O O   . HOH J 4 .   ? 23.348 4.916   -29.712 1.00 20.05  ?  539 HOH B O   1 
HETATM 4611 O O   . HOH J 4 .   ? 34.128 22.071  -3.590  1.00 21.19  ?  540 HOH B O   1 
HETATM 4612 O O   . HOH J 4 .   ? 10.009 3.340   -16.108 1.00 25.84  ?  541 HOH B O   1 
HETATM 4613 O O   . HOH J 4 .   ? 30.145 21.068  2.162   1.00 18.10  ?  542 HOH B O   1 
HETATM 4614 O O   . HOH J 4 .   ? 13.052 2.414   -12.985 1.00 15.29  ?  543 HOH B O   1 
HETATM 4615 O O   . HOH J 4 .   ? 16.303 -3.086  -39.810 1.00 23.35  ?  544 HOH B O   1 
HETATM 4616 O O   . HOH J 4 .   ? 9.239  17.451  -51.892 1.00 38.30  ?  545 HOH B O   1 
HETATM 4617 O O   . HOH J 4 .   ? 30.688 10.061  -24.780 1.00 30.20  ?  546 HOH B O   1 
HETATM 4618 O O   . HOH J 4 .   ? 24.336 15.744  1.972   1.00 14.61  ?  547 HOH B O   1 
HETATM 4619 O O   . HOH J 4 .   ? 27.323 25.251  4.207   1.00 34.37  ?  548 HOH B O   1 
HETATM 4620 O O   . HOH J 4 .   ? 30.638 12.334  6.941   1.00 33.92  ?  549 HOH B O   1 
HETATM 4621 O O   . HOH J 4 .   ? 26.832 6.688   9.352   1.00 28.94  ?  550 HOH B O   1 
HETATM 4622 O O   . HOH J 4 .   ? 35.980 7.641   -24.961 1.00 37.62  ?  551 HOH B O   1 
HETATM 4623 O O   . HOH J 4 .   ? 22.376 16.010  5.500   1.00 19.78  ?  552 HOH B O   1 
HETATM 4624 O O   . HOH J 4 .   ? 14.765 -0.953  -15.834 1.00 13.11  ?  553 HOH B O   1 
HETATM 4625 O O   . HOH J 4 .   ? 23.864 6.050   -17.465 1.00 14.81  ?  554 HOH B O   1 
HETATM 4626 O O   . HOH J 4 .   ? 16.304 -1.751  -36.124 1.00 19.34  ?  555 HOH B O   1 
HETATM 4627 O O   . HOH J 4 .   ? 12.360 11.100  -15.039 1.00 27.66  ?  556 HOH B O   1 
HETATM 4628 O O   . HOH J 4 .   ? 15.247 6.403   -18.908 1.00 19.69  ?  557 HOH B O   1 
HETATM 4629 O O   . HOH J 4 .   ? 32.771 1.217   -19.879 1.00 23.00  ?  558 HOH B O   1 
HETATM 4630 O O   . HOH J 4 .   ? 28.156 27.930  -15.338 1.00 33.30  ?  559 HOH B O   1 
HETATM 4631 O O   . HOH J 4 .   ? 14.532 6.306   -23.034 1.00 24.56  ?  560 HOH B O   1 
HETATM 4632 O O   . HOH J 4 .   ? 15.308 6.414   -14.112 1.00 15.82  ?  561 HOH B O   1 
HETATM 4633 O O   . HOH J 4 .   ? 24.728 0.830   -5.616  1.00 15.19  ?  562 HOH B O   1 
HETATM 4634 O O   . HOH J 4 .   ? 14.568 16.354  -19.608 1.00 28.48  ?  563 HOH B O   1 
HETATM 4635 O O   . HOH J 4 .   ? 28.026 8.078   -27.236 1.00 40.47  ?  564 HOH B O   1 
HETATM 4636 O O   . HOH J 4 .   ? 37.548 -1.762  -2.528  1.00 27.11  ?  565 HOH B O   1 
HETATM 4637 O O   . HOH J 4 .   ? 26.859 -3.791  0.108   1.00 26.49  ?  566 HOH B O   1 
HETATM 4638 O O   . HOH J 4 .   ? 26.192 -1.923  2.011   1.00 24.77  ?  567 HOH B O   1 
HETATM 4639 O O   . HOH J 4 .   ? 25.913 14.957  -12.583 1.00 15.22  ?  568 HOH B O   1 
HETATM 4640 O O   . HOH J 4 .   ? 36.369 24.840  -16.607 1.00 29.07  ?  569 HOH B O   1 
HETATM 4641 O O   . HOH J 4 .   ? 24.965 4.998   1.943   1.00 17.12  ?  570 HOH B O   1 
HETATM 4642 O O   . HOH J 4 .   ? 30.648 13.918  4.394   1.00 22.12  ?  571 HOH B O   1 
HETATM 4643 O O   . HOH J 4 .   ? 21.297 5.298   1.399   1.00 23.36  ?  572 HOH B O   1 
HETATM 4644 O O   . HOH J 4 .   ? 12.556 1.322   -37.331 1.00 25.69  ?  573 HOH B O   1 
HETATM 4645 O O   . HOH J 4 .   ? 11.317 8.672   -9.482  1.00 36.33  ?  574 HOH B O   1 
HETATM 4646 O O   . HOH J 4 .   ? 11.921 6.514   -7.757  1.00 16.90  ?  575 HOH B O   1 
HETATM 4647 O O   . HOH J 4 .   ? 25.144 4.774   -19.828 1.00 15.32  ?  576 HOH B O   1 
HETATM 4648 O O   . HOH J 4 .   ? 12.456 5.258   -21.740 1.00 32.39  ?  577 HOH B O   1 
HETATM 4649 O O   . HOH J 4 .   ? 35.229 3.854   -21.364 1.00 31.32  ?  578 HOH B O   1 
HETATM 4650 O O   . HOH J 4 .   ? 27.667 30.693  -3.632  1.00 31.84  ?  579 HOH B O   1 
HETATM 4651 O O   . HOH J 4 .   ? 12.702 6.509   -17.444 1.00 30.45  ?  580 HOH B O   1 
HETATM 4652 O O   . HOH J 4 .   ? 36.400 25.269  -9.764  1.00 17.70  ?  581 HOH B O   1 
HETATM 4653 O O   . HOH J 4 .   ? 32.973 3.900   -29.908 1.00 52.20  ?  582 HOH B O   1 
HETATM 4654 O O   . HOH J 4 .   ? 40.756 14.945  -2.133  1.00 38.04  ?  583 HOH B O   1 
HETATM 4655 O O   . HOH J 4 .   ? 22.960 1.660   1.692   1.00 27.57  ?  584 HOH B O   1 
HETATM 4656 O O   . HOH J 4 .   ? 21.668 0.899   -14.298 1.00 17.10  ?  585 HOH B O   1 
HETATM 4657 O O   . HOH J 4 .   ? 29.197 3.304   -25.428 1.00 41.89  ?  586 HOH B O   1 
HETATM 4658 O O   . HOH J 4 .   ? 22.429 3.497   -0.334  1.00 16.81  ?  587 HOH B O   1 
HETATM 4659 O O   . HOH J 4 .   ? 38.661 13.210  -1.525  1.00 27.96  ?  588 HOH B O   1 
HETATM 4660 O O   . HOH J 4 .   ? 19.216 22.984  13.169  1.00 38.22  ?  589 HOH B O   1 
HETATM 4661 O O   . HOH J 4 .   ? 21.225 26.427  -24.088 1.00 36.98  ?  590 HOH B O   1 
HETATM 4662 O O   . HOH J 4 .   ? 32.490 1.184   -22.886 1.00 27.51  ?  591 HOH B O   1 
HETATM 4663 O O   . HOH J 4 .   ? 14.555 4.946   -25.266 1.00 24.57  ?  592 HOH B O   1 
HETATM 4664 O O   . HOH J 4 .   ? 14.322 19.911  -10.461 1.00 31.30  ?  593 HOH B O   1 
HETATM 4665 O O   . HOH J 4 .   ? 21.446 -2.857  -13.966 1.00 17.95  ?  594 HOH B O   1 
HETATM 4666 O O   . HOH J 4 .   ? 18.500 7.434   2.210   1.00 25.21  ?  595 HOH B O   1 
HETATM 4667 O O   . HOH J 4 .   ? 17.520 18.608  8.652   1.00 31.57  ?  596 HOH B O   1 
HETATM 4668 O O   . HOH J 4 .   ? 40.303 9.787   -18.355 1.00 34.96  ?  597 HOH B O   1 
HETATM 4669 O O   . HOH J 4 .   ? 39.957 1.799   -5.600  1.00 21.04  ?  598 HOH B O   1 
HETATM 4670 O O   . HOH J 4 .   ? 24.775 4.740   -0.716  1.00 16.37  ?  599 HOH B O   1 
HETATM 4671 O O   . HOH J 4 .   ? 11.985 0.921   -29.592 1.00 30.85  ?  600 HOH B O   1 
HETATM 4672 O O   . HOH J 4 .   ? 37.082 25.430  -2.648  1.00 19.75  ?  601 HOH B O   1 
HETATM 4673 O O   . HOH J 4 .   ? 40.990 8.770   -11.662 1.00 23.77  ?  602 HOH B O   1 
HETATM 4674 O O   . HOH J 4 .   ? 33.541 7.283   -24.199 1.00 26.53  ?  603 HOH B O   1 
HETATM 4675 O O   . HOH J 4 .   ? 19.059 22.730  -4.557  1.00 28.02  ?  604 HOH B O   1 
HETATM 4676 O O   . HOH J 4 .   ? 23.245 -1.340  -21.974 1.00 18.88  ?  605 HOH B O   1 
HETATM 4677 O O   . HOH J 4 .   ? 16.941 8.881   0.631   1.00 24.77  ?  606 HOH B O   1 
HETATM 4678 O O   . HOH J 4 .   ? 25.881 17.685  -13.159 1.00 15.74  ?  607 HOH B O   1 
HETATM 4679 O O   . HOH J 4 .   ? 30.661 -6.180  -0.888  1.00 24.42  ?  608 HOH B O   1 
HETATM 4680 O O   . HOH J 4 .   ? 35.446 12.096  -27.993 1.00 32.81  ?  609 HOH B O   1 
HETATM 4681 O O   . HOH J 4 .   ? 12.464 16.874  -10.054 1.00 29.68  ?  610 HOH B O   1 
HETATM 4682 O O   . HOH J 4 .   ? 26.368 2.951   5.193   1.00 28.62  ?  611 HOH B O   1 
HETATM 4683 O O   . HOH J 4 .   ? 30.561 -2.370  -13.972 1.00 13.78  ?  612 HOH B O   1 
HETATM 4684 O O   . HOH J 4 .   ? 12.188 9.890   -21.672 1.00 36.11  ?  613 HOH B O   1 
HETATM 4685 O O   . HOH J 4 .   ? 15.905 21.415  -14.194 1.00 23.53  ?  614 HOH B O   1 
HETATM 4686 O O   . HOH J 4 .   ? 30.946 -4.206  -24.402 1.00 27.19  ?  615 HOH B O   1 
HETATM 4687 O O   . HOH J 4 .   ? 17.394 17.875  -2.204  1.00 25.65  ?  616 HOH B O   1 
HETATM 4688 O O   . HOH J 4 .   ? 38.818 26.104  -10.201 1.00 31.52  ?  617 HOH B O   1 
HETATM 4689 O O   . HOH J 4 .   ? 41.707 14.668  -6.860  1.00 30.53  ?  618 HOH B O   1 
HETATM 4690 O O   . HOH J 4 .   ? 24.770 29.373  -13.312 1.00 38.64  ?  619 HOH B O   1 
HETATM 4691 O O   . HOH J 4 .   ? 14.744 8.848   -21.921 1.00 25.48  ?  620 HOH B O   1 
HETATM 4692 O O   . HOH J 4 .   ? 34.699 37.221  -2.673  1.00 37.63  ?  621 HOH B O   1 
HETATM 4693 O O   . HOH J 4 .   ? 19.842 23.244  -10.397 1.00 23.67  ?  622 HOH B O   1 
HETATM 4694 O O   . HOH J 4 .   ? 35.547 -1.144  -15.376 1.00 28.85  ?  623 HOH B O   1 
HETATM 4695 O O   . HOH J 4 .   ? 17.937 22.829  -20.498 1.00 26.64  ?  624 HOH B O   1 
HETATM 4696 O O   . HOH J 4 .   ? 14.059 -1.079  -37.627 1.00 23.19  ?  625 HOH B O   1 
HETATM 4697 O O   . HOH J 4 .   ? 21.957 1.379   -5.073  1.00 17.76  ?  626 HOH B O   1 
HETATM 4698 O O   . HOH J 4 .   ? 24.648 10.832  -27.230 1.00 41.66  ?  627 HOH B O   1 
HETATM 4699 O O   . HOH J 4 .   ? 34.130 30.417  -13.844 1.00 33.40  ?  628 HOH B O   1 
HETATM 4700 O O   . HOH J 4 .   ? 16.498 20.425  -3.388  1.00 38.68  ?  629 HOH B O   1 
HETATM 4701 O O   . HOH J 4 .   ? 25.367 7.719   -26.004 1.00 27.24  ?  630 HOH B O   1 
HETATM 4702 O O   . HOH J 4 .   ? 20.727 9.318   4.669   1.00 20.33  ?  631 HOH B O   1 
HETATM 4703 O O   . HOH J 4 .   ? 38.543 -3.757  -12.515 1.00 26.37  ?  632 HOH B O   1 
HETATM 4704 O O   . HOH J 4 .   ? 19.294 1.546   -16.895 1.00 18.49  ?  633 HOH B O   1 
HETATM 4705 O O   . HOH J 4 .   ? 35.003 -5.144  -3.845  1.00 27.10  ?  634 HOH B O   1 
HETATM 4706 O O   . HOH J 4 .   ? 21.651 19.147  7.269   1.00 26.96  ?  635 HOH B O   1 
HETATM 4707 O O   . HOH J 4 .   ? 39.607 3.692   -35.847 1.00 44.75  ?  636 HOH B O   1 
HETATM 4708 O O   . HOH J 4 .   ? 34.392 -4.469  -6.269  1.00 21.29  ?  637 HOH B O   1 
HETATM 4709 O O   . HOH J 4 .   ? 31.054 23.025  -20.912 1.00 35.11  ?  638 HOH B O   1 
HETATM 4710 O O   . HOH J 4 .   ? 34.623 -0.642  -19.154 1.00 36.49  ?  639 HOH B O   1 
HETATM 4711 O O   . HOH J 4 .   ? 28.628 -1.291  -18.100 1.00 18.42  ?  640 HOH B O   1 
HETATM 4712 O O   . HOH J 4 .   ? 38.332 15.268  -25.348 1.00 43.59  ?  641 HOH B O   1 
HETATM 4713 O O   . HOH J 4 .   ? 40.215 1.713   -0.623  1.00 28.35  ?  642 HOH B O   1 
HETATM 4714 O O   . HOH J 4 .   ? 39.826 26.928  -2.294  1.00 36.29  ?  643 HOH B O   1 
HETATM 4715 O O   . HOH J 4 .   ? 20.268 8.534   7.442   1.00 30.76  ?  644 HOH B O   1 
HETATM 4716 O O   . HOH J 4 .   ? 35.355 35.710  -0.441  1.00 29.71  ?  645 HOH B O   1 
HETATM 4717 O O   . HOH J 4 .   ? 22.042 5.639   3.692   1.00 34.77  ?  646 HOH B O   1 
HETATM 4718 O O   . HOH J 4 .   ? 30.773 -2.756  -21.188 1.00 30.59  ?  647 HOH B O   1 
HETATM 4719 O O   . HOH J 4 .   ? 26.141 26.838  -38.418 1.00 39.89  ?  648 HOH B O   1 
HETATM 4720 O O   . HOH J 4 .   ? 33.011 -2.946  -15.302 1.00 21.88  ?  649 HOH B O   1 
HETATM 4721 O O   . HOH J 4 .   ? 23.393 26.893  -37.337 1.00 47.91  ?  650 HOH B O   1 
HETATM 4722 O O   . HOH J 4 .   ? 32.821 -3.168  -22.239 1.00 38.77  ?  651 HOH B O   1 
HETATM 4723 O O   . HOH J 4 .   ? 31.239 -7.697  -3.272  1.00 19.22  ?  652 HOH B O   1 
HETATM 4724 O O   . HOH J 4 .   ? 19.983 25.914  -11.683 1.00 37.14  ?  653 HOH B O   1 
HETATM 4725 O O   . HOH J 4 .   ? 12.747 6.154   -15.016 1.00 23.65  ?  654 HOH B O   1 
HETATM 4726 O O   . HOH J 4 .   ? 18.841 12.593  4.514   1.00 34.11  ?  655 HOH B O   1 
HETATM 4727 O O   . HOH J 4 .   ? 29.899 21.407  4.904   1.00 34.05  ?  656 HOH B O   1 
HETATM 4728 O O   . HOH J 4 .   ? 23.952 3.380   3.798   1.00 23.95  ?  657 HOH B O   1 
HETATM 4729 O O   . HOH J 4 .   ? 14.203 2.469   -23.999 1.00 26.17  ?  658 HOH B O   1 
HETATM 4730 O O   . HOH J 4 .   ? 39.750 24.787  -1.499  1.00 45.47  ?  659 HOH B O   1 
HETATM 4731 O O   . HOH J 4 .   ? 29.898 23.413  -23.472 1.00 46.80  ?  660 HOH B O   1 
HETATM 4732 O O   . HOH J 4 .   ? 23.156 29.313  -4.433  1.00 36.41  ?  661 HOH B O   1 
HETATM 4733 O O   . HOH J 4 .   ? 12.153 4.942   -55.537 1.00 45.19  ?  662 HOH B O   1 
HETATM 4734 O O   . HOH J 4 .   ? 11.188 4.214   -13.731 1.00 19.59  ?  663 HOH B O   1 
HETATM 4735 O O   . HOH J 4 .   ? 32.685 13.286  -51.151 1.00 35.64  ?  664 HOH B O   1 
HETATM 4736 O O   . HOH J 4 .   ? 32.922 -2.606  -18.064 1.00 27.17  ?  665 HOH B O   1 
HETATM 4737 O O   . HOH J 4 .   ? 27.886 -2.697  3.945   1.00 26.74  ?  666 HOH B O   1 
HETATM 4738 O O   . HOH J 4 .   ? 32.712 3.756   -24.007 1.00 38.08  ?  667 HOH B O   1 
HETATM 4739 O O   . HOH J 4 .   ? 10.569 10.605  -7.794  1.00 32.53  ?  668 HOH B O   1 
HETATM 4740 O O   . HOH J 4 .   ? 27.134 -6.160  1.645   1.00 27.06  ?  669 HOH B O   1 
HETATM 4741 O O   . HOH J 4 .   ? 12.032 10.031  -5.775  1.00 29.14  ?  670 HOH B O   1 
HETATM 4742 O O   . HOH J 4 .   ? 18.444 4.514   1.809   1.00 30.25  ?  671 HOH B O   1 
HETATM 4743 O O   . HOH J 4 .   ? 37.916 38.967  -5.643  1.00 29.98  ?  672 HOH B O   1 
HETATM 4744 O O   . HOH J 4 .   ? 27.876 22.819  6.065   1.00 40.34  ?  673 HOH B O   1 
HETATM 4745 O O   . HOH J 4 .   ? 31.036 -1.034  -19.289 1.00 21.08  ?  674 HOH B O   1 
HETATM 4746 O O   . HOH J 4 .   ? 17.154 22.786  -11.759 1.00 33.56  ?  675 HOH B 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   . SER A 4   ? 0.7641 0.7588 0.6607 0.0029  0.1110  0.0606  61  SER A N   
2    C CA  . SER A 4   ? 0.6602 0.6719 0.5500 0.0179  0.1096  0.0510  61  SER A CA  
3    C C   . SER A 4   ? 0.5525 0.5581 0.4443 0.0289  0.0906  0.0389  61  SER A C   
4    O O   . SER A 4   ? 0.4715 0.4755 0.3423 0.0385  0.0881  0.0303  61  SER A O   
5    C CB  . SER A 4   ? 0.6579 0.7060 0.5730 0.0163  0.1220  0.0440  61  SER A CB  
6    O OG  . SER A 4   ? 0.5568 0.6131 0.4574 0.0323  0.1258  0.0355  61  SER A OG  
7    N N   . HIS A 5   ? 0.3839 0.3858 0.2984 0.0248  0.0793  0.0364  62  HIS A N   
8    C CA  . HIS A 5   ? 0.2991 0.2888 0.2116 0.0298  0.0643  0.0268  62  HIS A CA  
9    C C   . HIS A 5   ? 0.3430 0.3220 0.2657 0.0228  0.0538  0.0323  62  HIS A C   
10   O O   . HIS A 5   ? 0.2904 0.2726 0.2309 0.0141  0.0570  0.0382  62  HIS A O   
11   C CB  . HIS A 5   ? 0.3178 0.3099 0.2437 0.0371  0.0648  0.0160  62  HIS A CB  
12   C CG  . HIS A 5   ? 0.3774 0.3735 0.2893 0.0477  0.0765  0.0081  62  HIS A CG  
13   N ND1 . HIS A 5   ? 0.4358 0.4214 0.3190 0.0492  0.0772  -0.0015 62  HIS A ND1 
14   C CD2 . HIS A 5   ? 0.5151 0.5289 0.4371 0.0588  0.0883  0.0068  62  HIS A CD2 
15   C CE1 . HIS A 5   ? 0.4821 0.4708 0.3557 0.0595  0.0902  -0.0086 62  HIS A CE1 
16   N NE2 . HIS A 5   ? 0.4783 0.4840 0.3756 0.0675  0.0974  -0.0028 62  HIS A NE2 
17   N N   . THR A 6   ? 0.2721 0.2432 0.1840 0.0254  0.0420  0.0278  63  THR A N   
18   C CA  . THR A 6   ? 0.2702 0.2331 0.1895 0.0221  0.0324  0.0318  63  THR A CA  
19   C C   . THR A 6   ? 0.2561 0.2203 0.1801 0.0207  0.0217  0.0187  63  THR A C   
20   O O   . THR A 6   ? 0.3014 0.2722 0.2117 0.0214  0.0196  0.0071  63  THR A O   
21   C CB  . THR A 6   ? 0.2824 0.2385 0.1787 0.0295  0.0316  0.0431  63  THR A CB  
22   O OG1 . THR A 6   ? 0.3760 0.3198 0.2609 0.0276  0.0468  0.0562  63  THR A OG1 
23   C CG2 . THR A 6   ? 0.3097 0.2557 0.2131 0.0297  0.0235  0.0464  63  THR A CG2 
24   N N   . ILE A 7   ? 0.2299 0.1881 0.1717 0.0158  0.0167  0.0188  64  ILE A N   
25   C CA  . ILE A 7   ? 0.2473 0.2031 0.1925 0.0112  0.0095  0.0084  64  ILE A CA  
26   C C   . ILE A 7   ? 0.2378 0.2016 0.1826 0.0123  0.0007  0.0112  64  ILE A C   
27   O O   . ILE A 7   ? 0.2550 0.2117 0.2029 0.0153  0.0011  0.0224  64  ILE A O   
28   C CB  . ILE A 7   ? 0.2536 0.1984 0.2135 0.0093  0.0111  0.0089  64  ILE A CB  
29   C CG1 . ILE A 7   ? 0.2735 0.2116 0.2294 0.0161  0.0204  0.0060  64  ILE A CG1 
30   C CG2 . ILE A 7   ? 0.3239 0.2604 0.2844 0.0026  0.0066  0.0013  64  ILE A CG2 
31   C CD1 . ILE A 7   ? 0.3172 0.2520 0.2845 0.0230  0.0218  0.0104  64  ILE A CD1 
32   N N   . GLY A 8   ? 0.2389 0.2192 0.1787 0.0097  -0.0056 -0.0006 65  GLY A N   
33   C CA  . GLY A 8   ? 0.1956 0.1932 0.1381 0.0142  -0.0141 0.0000  65  GLY A CA  
34   C C   . GLY A 8   ? 0.2084 0.2023 0.1659 0.0024  -0.0155 -0.0077 65  GLY A C   
35   O O   . GLY A 8   ? 0.2351 0.2238 0.1927 -0.0111 -0.0114 -0.0204 65  GLY A O   
36   N N   . LEU A 9   ? 0.2066 0.1969 0.1721 0.0073  -0.0186 -0.0001 66  LEU A N   
37   C CA  . LEU A 9   ? 0.1906 0.1781 0.1678 -0.0022 -0.0191 -0.0055 66  LEU A CA  
38   C C   . LEU A 9   ? 0.1835 0.2001 0.1641 0.0041  -0.0255 -0.0094 66  LEU A C   
39   O O   . LEU A 9   ? 0.2245 0.2389 0.2006 0.0206  -0.0277 0.0009  66  LEU A O   
40   C CB  . LEU A 9   ? 0.2143 0.1768 0.1982 -0.0021 -0.0166 0.0043  66  LEU A CB  
41   C CG  . LEU A 9   ? 0.2673 0.2258 0.2588 -0.0080 -0.0173 0.0018  66  LEU A CG  
42   C CD1 . LEU A 9   ? 0.2917 0.2458 0.2803 -0.0200 -0.0124 -0.0075 66  LEU A CD1 
43   C CD2 . LEU A 9   ? 0.2677 0.2110 0.2638 -0.0074 -0.0162 0.0094  66  LEU A CD2 
44   N N   . ALA A 10  ? 0.1525 0.1955 0.1392 -0.0087 -0.0261 -0.0250 67  ALA A N   
45   C CA  . ALA A 10  ? 0.1647 0.2463 0.1600 -0.0039 -0.0312 -0.0313 67  ALA A CA  
46   C C   . ALA A 10  ? 0.1632 0.2272 0.1671 -0.0133 -0.0266 -0.0310 67  ALA A C   
47   O O   . ALA A 10  ? 0.2140 0.2566 0.2170 -0.0324 -0.0189 -0.0363 67  ALA A O   
48   C CB  . ALA A 10  ? 0.1812 0.3139 0.1810 -0.0180 -0.0330 -0.0526 67  ALA A CB  
49   N N   . THR A 11  ? 0.1537 0.2229 0.1611 0.0019  -0.0296 -0.0247 68  THR A N   
50   C CA  . THR A 11  ? 0.1745 0.2264 0.1867 -0.0053 -0.0253 -0.0240 68  THR A CA  
51   C C   . THR A 11  ? 0.1566 0.2447 0.1766 0.0048  -0.0270 -0.0297 68  THR A C   
52   O O   . THR A 11  ? 0.1506 0.2626 0.1681 0.0279  -0.0322 -0.0270 68  THR A O   
53   C CB  . THR A 11  ? 0.1638 0.1728 0.1696 0.0014  -0.0244 -0.0108 68  THR A CB  
54   O OG1 . THR A 11  ? 0.2270 0.2263 0.2351 -0.0045 -0.0215 -0.0119 68  THR A OG1 
55   C CG2 . THR A 11  ? 0.1901 0.1900 0.1870 0.0223  -0.0261 -0.0016 68  THR A CG2 
56   N N   . THR A 12  ? 0.1672 0.2581 0.1933 -0.0093 -0.0213 -0.0361 69  THR A N   
57   C CA  . THR A 12  ? 0.1319 0.2548 0.1654 0.0015  -0.0210 -0.0410 69  THR A CA  
58   C C   . THR A 12  ? 0.1716 0.2582 0.1947 0.0219  -0.0216 -0.0294 69  THR A C   
59   O O   . THR A 12  ? 0.2008 0.2429 0.2137 0.0218  -0.0219 -0.0197 69  THR A O   
60   C CB  . THR A 12  ? 0.2089 0.3431 0.2488 -0.0226 -0.0116 -0.0515 69  THR A CB  
61   O OG1 . THR A 12  ? 0.4204 0.5924 0.4691 -0.0110 -0.0104 -0.0574 69  THR A OG1 
62   C CG2 . THR A 12  ? 0.1459 0.2252 0.1728 -0.0310 -0.0067 -0.0418 69  THR A CG2 
63   N N   . ASN A 13  ? 0.1933 0.3020 0.2186 0.0382  -0.0201 -0.0330 70  ASN A N   
64   C CA  . ASN A 13  ? 0.2699 0.3437 0.2811 0.0584  -0.0173 -0.0263 70  ASN A CA  
65   C C   . ASN A 13  ? 0.2566 0.2741 0.2569 0.0444  -0.0150 -0.0206 70  ASN A C   
66   O O   . ASN A 13  ? 0.2367 0.2496 0.2396 0.0264  -0.0130 -0.0242 70  ASN A O   
67   C CB  . ASN A 13  ? 0.2603 0.3639 0.2775 0.0653  -0.0125 -0.0354 70  ASN A CB  
68   C CG  . ASN A 13  ? 0.3532 0.4151 0.3521 0.0837  -0.0070 -0.0320 70  ASN A CG  
69   O OD1 . ASN A 13  ? 0.3461 0.3647 0.3264 0.0994  -0.0055 -0.0232 70  ASN A OD1 
70   N ND2 . ASN A 13  ? 0.3407 0.4116 0.3410 0.0806  -0.0012 -0.0401 70  ASN A ND2 
71   N N   . LEU A 14  ? 0.2175 0.1955 0.2037 0.0528  -0.0140 -0.0122 71  LEU A N   
72   C CA  . LEU A 14  ? 0.2313 0.1696 0.2110 0.0364  -0.0120 -0.0104 71  LEU A CA  
73   C C   . LEU A 14  ? 0.3037 0.2213 0.2736 0.0354  -0.0067 -0.0172 71  LEU A C   
74   O O   . LEU A 14  ? 0.3088 0.2082 0.2759 0.0187  -0.0065 -0.0202 71  LEU A O   
75   C CB  . LEU A 14  ? 0.2692 0.1736 0.2363 0.0404  -0.0087 -0.0019 71  LEU A CB  
76   C CG  . LEU A 14  ? 0.3120 0.2342 0.2878 0.0352  -0.0140 0.0034  71  LEU A CG  
77   C CD1 . LEU A 14  ? 0.3793 0.2709 0.3397 0.0415  -0.0085 0.0131  71  LEU A CD1 
78   C CD2 . LEU A 14  ? 0.2717 0.2022 0.2602 0.0136  -0.0176 0.0005  71  LEU A CD2 
79   N N   . ALA A 15  ? 0.2324 0.1580 0.1970 0.0538  -0.0025 -0.0213 72  ALA A N   
80   C CA  . ALA A 15  ? 0.2880 0.1953 0.2413 0.0531  0.0037  -0.0302 72  ALA A CA  
81   C C   . ALA A 15  ? 0.2557 0.1889 0.2190 0.0346  0.0003  -0.0364 72  ALA A C   
82   O O   . ALA A 15  ? 0.2939 0.2144 0.2463 0.0298  0.0040  -0.0446 72  ALA A O   
83   C CB  . ALA A 15  ? 0.3612 0.2721 0.3047 0.0829  0.0108  -0.0326 72  ALA A CB  
84   N N   . LEU A 16  ? 0.2086 0.1728 0.1870 0.0242  -0.0044 -0.0329 73  LEU A N   
85   C CA  . LEU A 16  ? 0.1989 0.1720 0.1773 0.0073  -0.0047 -0.0342 73  LEU A CA  
86   C C   . LEU A 16  ? 0.1990 0.1538 0.1743 -0.0042 -0.0102 -0.0288 73  LEU A C   
87   O O   . LEU A 16  ? 0.2097 0.1576 0.1907 -0.0046 -0.0134 -0.0232 73  LEU A O   
88   C CB  . LEU A 16  ? 0.1663 0.1707 0.1555 -0.0006 -0.0017 -0.0341 73  LEU A CB  
89   C CG  . LEU A 16  ? 0.1625 0.2037 0.1598 0.0082  0.0043  -0.0427 73  LEU A CG  
90   C CD1 . LEU A 16  ? 0.2021 0.2769 0.2104 -0.0096 0.0104  -0.0468 73  LEU A CD1 
91   C CD2 . LEU A 16  ? 0.2182 0.2540 0.2039 0.0137  0.0098  -0.0485 73  LEU A CD2 
92   N N   . HIS A 17  ? 0.1839 0.1370 0.1493 -0.0114 -0.0112 -0.0309 74  HIS A N   
93   C CA  . HIS A 17  ? 0.1769 0.1247 0.1399 -0.0183 -0.0175 -0.0292 74  HIS A CA  
94   C C   . HIS A 17  ? 0.1974 0.1505 0.1649 -0.0193 -0.0202 -0.0181 74  HIS A C   
95   O O   . HIS A 17  ? 0.1862 0.1390 0.1597 -0.0210 -0.0246 -0.0156 74  HIS A O   
96   C CB  . HIS A 17  ? 0.1961 0.1512 0.1450 -0.0220 -0.0192 -0.0363 74  HIS A CB  
97   C CG  . HIS A 17  ? 0.2070 0.1500 0.1472 -0.0220 -0.0143 -0.0501 74  HIS A CG  
98   N ND1 . HIS A 17  ? 0.2298 0.1483 0.1714 -0.0175 -0.0087 -0.0541 74  HIS A ND1 
99   C CD2 . HIS A 17  ? 0.2203 0.1672 0.1452 -0.0237 -0.0124 -0.0608 74  HIS A CD2 
100  C CE1 . HIS A 17  ? 0.2402 0.1430 0.1670 -0.0158 -0.0021 -0.0668 74  HIS A CE1 
101  N NE2 . HIS A 17  ? 0.2576 0.1796 0.1756 -0.0212 -0.0047 -0.0726 74  HIS A NE2 
102  N N   . ALA A 18  ? 0.1892 0.1442 0.1515 -0.0194 -0.0150 -0.0125 75  ALA A N   
103  C CA  . ALA A 18  ? 0.1740 0.1213 0.1328 -0.0191 -0.0137 -0.0026 75  ALA A CA  
104  C C   . ALA A 18  ? 0.1858 0.1306 0.1588 -0.0200 -0.0150 -0.0020 75  ALA A C   
105  O O   . ALA A 18  ? 0.1752 0.1170 0.1496 -0.0167 -0.0184 0.0033  75  ALA A O   
106  C CB  . ALA A 18  ? 0.2052 0.1423 0.1483 -0.0234 -0.0021 0.0018  75  ALA A CB  
107  N N   . PRO A 19  ? 0.1861 0.1381 0.1692 -0.0216 -0.0131 -0.0073 76  PRO A N   
108  C CA  . PRO A 19  ? 0.1977 0.1498 0.1895 -0.0201 -0.0154 -0.0059 76  PRO A CA  
109  C C   . PRO A 19  ? 0.2085 0.1533 0.2035 -0.0157 -0.0204 -0.0035 76  PRO A C   
110  O O   . PRO A 19  ? 0.1847 0.1265 0.1828 -0.0154 -0.0213 0.0006  76  PRO A O   
111  C CB  . PRO A 19  ? 0.1968 0.1692 0.1965 -0.0177 -0.0141 -0.0127 76  PRO A CB  
112  C CG  . PRO A 19  ? 0.2608 0.2437 0.2586 -0.0171 -0.0106 -0.0181 76  PRO A CG  
113  C CD  . PRO A 19  ? 0.1919 0.1595 0.1774 -0.0235 -0.0080 -0.0145 76  PRO A CD  
114  N N   . SER A 20  ? 0.1774 0.1175 0.1698 -0.0150 -0.0212 -0.0076 77  SER A N   
115  C CA  . SER A 20  ? 0.1631 0.0926 0.1560 -0.0183 -0.0217 -0.0082 77  SER A CA  
116  C C   . SER A 20  ? 0.1995 0.1422 0.1968 -0.0241 -0.0255 -0.0065 77  SER A C   
117  O O   . SER A 20  ? 0.1963 0.1406 0.1997 -0.0276 -0.0249 -0.0048 77  SER A O   
118  C CB  . SER A 20  ? 0.2441 0.1590 0.2284 -0.0203 -0.0181 -0.0167 77  SER A CB  
119  O OG  . SER A 20  ? 0.4067 0.3040 0.3843 -0.0085 -0.0127 -0.0153 77  SER A OG  
120  N N   . GLN A 21  ? 0.1931 0.1488 0.1856 -0.0224 -0.0287 -0.0062 78  GLN A N   
121  C CA  . GLN A 21  ? 0.1473 0.1230 0.1418 -0.0194 -0.0331 -0.0028 78  GLN A CA  
122  C C   . GLN A 21  ? 0.1899 0.1598 0.1857 -0.0113 -0.0305 0.0068  78  GLN A C   
123  O O   . GLN A 21  ? 0.1741 0.1606 0.1764 -0.0071 -0.0324 0.0090  78  GLN A O   
124  C CB  . GLN A 21  ? 0.1401 0.1292 0.1212 -0.0126 -0.0366 -0.0016 78  GLN A CB  
125  C CG  . GLN A 21  ? 0.1727 0.1782 0.1525 -0.0223 -0.0408 -0.0150 78  GLN A CG  
126  C CD  . GLN A 21  ? 0.1917 0.2202 0.1558 -0.0138 -0.0461 -0.0144 78  GLN A CD  
127  O OE1 . GLN A 21  ? 0.1827 0.2069 0.1357 -0.0175 -0.0450 -0.0212 78  GLN A OE1 
128  N NE2 . GLN A 21  ? 0.1797 0.2348 0.1402 0.0007  -0.0516 -0.0064 78  GLN A NE2 
129  N N   . ILE A 22  ? 0.1755 0.1257 0.1652 -0.0102 -0.0251 0.0098  79  ILE A N   
130  C CA  . ILE A 22  ? 0.1614 0.1005 0.1486 -0.0060 -0.0204 0.0149  79  ILE A CA  
131  C C   . ILE A 22  ? 0.1908 0.1347 0.1899 -0.0084 -0.0214 0.0135  79  ILE A C   
132  O O   . ILE A 22  ? 0.1962 0.1438 0.1970 -0.0029 -0.0199 0.0171  79  ILE A O   
133  C CB  . ILE A 22  ? 0.1742 0.0955 0.1518 -0.0116 -0.0127 0.0131  79  ILE A CB  
134  C CG1 . ILE A 22  ? 0.2183 0.1256 0.1768 -0.0087 -0.0068 0.0181  79  ILE A CG1 
135  C CG2 . ILE A 22  ? 0.2266 0.1356 0.2015 -0.0132 -0.0069 0.0124  79  ILE A CG2 
136  C CD1 . ILE A 22  ? 0.2499 0.1421 0.1985 -0.0217 0.0044  0.0135  79  ILE A CD1 
137  N N   . VAL A 23  ? 0.1852 0.1277 0.1892 -0.0137 -0.0222 0.0096  80  VAL A N   
138  C CA  . VAL A 23  ? 0.1654 0.1062 0.1734 -0.0147 -0.0204 0.0110  80  VAL A CA  
139  C C   . VAL A 23  ? 0.2043 0.1580 0.2201 -0.0192 -0.0202 0.0108  80  VAL A C   
140  O O   . VAL A 23  ? 0.1946 0.1547 0.2144 -0.0182 -0.0172 0.0137  80  VAL A O   
141  C CB  . VAL A 23  ? 0.2268 0.1561 0.2303 -0.0139 -0.0188 0.0096  80  VAL A CB  
142  C CG1 . VAL A 23  ? 0.2995 0.2173 0.2992 -0.0147 -0.0134 0.0138  80  VAL A CG1 
143  C CG2 . VAL A 23  ? 0.2862 0.2210 0.2866 -0.0071 -0.0201 0.0081  80  VAL A CG2 
144  N N   . ALA A 24  ? 0.1770 0.1414 0.1958 -0.0257 -0.0228 0.0053  81  ALA A N   
145  C CA  . ALA A 24  ? 0.1914 0.1820 0.2211 -0.0345 -0.0227 0.0004  81  ALA A CA  
146  C C   . ALA A 24  ? 0.1561 0.1749 0.1921 -0.0216 -0.0256 0.0054  81  ALA A C   
147  O O   . ALA A 24  ? 0.1651 0.2088 0.2129 -0.0249 -0.0228 0.0037  81  ALA A O   
148  C CB  . ALA A 24  ? 0.2120 0.2168 0.2422 -0.0452 -0.0262 -0.0105 81  ALA A CB  
149  N N   . ALA A 25  ? 0.1676 0.1801 0.1929 -0.0058 -0.0284 0.0117  82  ALA A N   
150  C CA  . ALA A 25  ? 0.1467 0.1756 0.1694 0.0134  -0.0284 0.0184  82  ALA A CA  
151  C C   . ALA A 25  ? 0.1724 0.1852 0.1939 0.0186  -0.0211 0.0225  82  ALA A C   
152  O O   . ALA A 25  ? 0.1843 0.2190 0.2104 0.0314  -0.0191 0.0251  82  ALA A O   
153  C CB  . ALA A 25  ? 0.1762 0.1862 0.1775 0.0288  -0.0283 0.0259  82  ALA A CB  
154  N N   . ILE A 26  ? 0.1816 0.1621 0.1962 0.0106  -0.0172 0.0220  83  ILE A N   
155  C CA  . ILE A 26  ? 0.1720 0.1400 0.1830 0.0130  -0.0108 0.0230  83  ILE A CA  
156  C C   . ILE A 26  ? 0.1821 0.1712 0.2067 0.0060  -0.0088 0.0217  83  ILE A C   
157  O O   . ILE A 26  ? 0.1817 0.1815 0.2083 0.0135  -0.0037 0.0231  83  ILE A O   
158  C CB  . ILE A 26  ? 0.1778 0.1203 0.1790 0.0051  -0.0093 0.0199  83  ILE A CB  
159  C CG1 . ILE A 26  ? 0.1954 0.1152 0.1811 0.0075  -0.0055 0.0194  83  ILE A CG1 
160  C CG2 . ILE A 26  ? 0.2056 0.1445 0.2033 0.0046  -0.0048 0.0183  83  ILE A CG2 
161  C CD1 . ILE A 26  ? 0.2228 0.1331 0.2041 -0.0052 -0.0042 0.0119  83  ILE A CD1 
162  N N   . LYS A 27  ? 0.1710 0.1618 0.2017 -0.0088 -0.0098 0.0187  84  LYS A N   
163  C CA  . LYS A 27  ? 0.1946 0.1972 0.2333 -0.0203 -0.0030 0.0174  84  LYS A CA  
164  C C   . LYS A 27  ? 0.1645 0.2130 0.2208 -0.0201 -0.0024 0.0136  84  LYS A C   
165  O O   . LYS A 27  ? 0.1651 0.2308 0.2281 -0.0223 0.0053  0.0137  84  LYS A O   
166  C CB  . LYS A 27  ? 0.2347 0.2189 0.2695 -0.0366 -0.0002 0.0141  84  LYS A CB  
167  C CG  . LYS A 27  ? 0.3196 0.2987 0.3535 -0.0528 0.0127  0.0136  84  LYS A CG  
168  C CD  . LYS A 27  ? 0.4224 0.4349 0.4733 -0.0735 0.0160  0.0019  84  LYS A CD  
169  C CE  . LYS A 27  ? 0.5210 0.5165 0.5659 -0.0977 0.0342  -0.0007 84  LYS A CE  
170  N NZ  . LYS A 27  ? 0.4585 0.4367 0.4914 -0.0881 0.0428  0.0114  84  LYS A NZ  
171  N N   . SER A 28  ? 0.1645 0.2402 0.2280 -0.0157 -0.0105 0.0098  85  SER A N   
172  C CA  . SER A 28  ? 0.1626 0.2976 0.2445 -0.0116 -0.0121 0.0048  85  SER A CA  
173  C C   . SER A 28  ? 0.1213 0.2682 0.2020 0.0136  -0.0084 0.0119  85  SER A C   
174  O O   . SER A 28  ? 0.1634 0.3536 0.2606 0.0128  -0.0031 0.0082  85  SER A O   
175  C CB  . SER A 28  ? 0.1764 0.3403 0.2596 -0.0041 -0.0233 0.0012  85  SER A CB  
176  O OG  . SER A 28  ? 0.2266 0.4617 0.3285 0.0039  -0.0268 -0.0046 85  SER A OG  
177  N N   . ARG A 29  ? 0.1526 0.2618 0.2125 0.0354  -0.0090 0.0207  86  ARG A N   
178  C CA  . ARG A 29  ? 0.1569 0.2658 0.2086 0.0612  -0.0024 0.0263  86  ARG A CA  
179  C C   . ARG A 29  ? 0.1504 0.2448 0.2020 0.0519  0.0072  0.0248  86  ARG A C   
180  O O   . ARG A 29  ? 0.1757 0.2971 0.2338 0.0641  0.0141  0.0245  86  ARG A O   
181  C CB  . ARG A 29  ? 0.1859 0.2435 0.2081 0.0810  -0.0002 0.0340  86  ARG A CB  
182  C CG  . ARG A 29  ? 0.1919 0.2336 0.1969 0.1097  0.0107  0.0391  86  ARG A CG  
183  C CD  . ARG A 29  ? 0.2284 0.3281 0.2440 0.1378  0.0091  0.0421  86  ARG A CD  
184  N NE  . ARG A 29  ? 0.2852 0.3576 0.2760 0.1590  0.0211  0.0450  86  ARG A NE  
185  C CZ  . ARG A 29  ? 0.4070 0.5230 0.4032 0.1770  0.0229  0.0448  86  ARG A CZ  
186  N NH1 . ARG A 29  ? 0.3512 0.5436 0.3782 0.1720  0.0140  0.0393  86  ARG A NH1 
187  N NH2 . ARG A 29  ? 0.4272 0.5098 0.3955 0.1980  0.0346  0.0486  86  ARG A NH2 
188  N N   . ALA A 30  ? 0.1688 0.2265 0.2124 0.0328  0.0080  0.0239  87  ALA A N   
189  C CA  . ALA A 30  ? 0.1797 0.2245 0.2174 0.0265  0.0165  0.0238  87  ALA A CA  
190  C C   . ALA A 30  ? 0.1620 0.2465 0.2181 0.0147  0.0235  0.0215  87  ALA A C   
191  O O   . ALA A 30  ? 0.1655 0.2625 0.2214 0.0208  0.0327  0.0217  87  ALA A O   
192  C CB  . ALA A 30  ? 0.1921 0.2006 0.2167 0.0130  0.0142  0.0243  87  ALA A CB  
193  N N   . SER A 31  ? 0.1452 0.2500 0.2160 -0.0048 0.0214  0.0173  88  SER A N   
194  C CA  . SER A 31  ? 0.1385 0.2821 0.2268 -0.0239 0.0318  0.0117  88  SER A CA  
195  C C   . SER A 31  ? 0.1631 0.3710 0.2722 -0.0084 0.0331  0.0076  88  SER A C   
196  O O   . SER A 31  ? 0.1938 0.4305 0.3124 -0.0142 0.0454  0.0053  88  SER A O   
197  C CB  . SER A 31  ? 0.2275 0.3773 0.3248 -0.0514 0.0311  0.0036  88  SER A CB  
198  O OG  . SER A 31  ? 0.2932 0.3827 0.3683 -0.0633 0.0357  0.0086  88  SER A OG  
199  N N   . GLN A 32  ? 0.1491 0.3817 0.2630 0.0150  0.0219  0.0076  89  GLN A N   
200  C CA  . GLN A 32  ? 0.1515 0.4505 0.2825 0.0388  0.0226  0.0052  89  GLN A CA  
201  C C   . GLN A 32  ? 0.1555 0.4371 0.2735 0.0621  0.0332  0.0112  89  GLN A C   
202  O O   . GLN A 32  ? 0.2243 0.5588 0.3567 0.0749  0.0394  0.0078  89  GLN A O   
203  C CB  . GLN A 32  ? 0.2015 0.5195 0.3290 0.0679  0.0095  0.0085  89  GLN A CB  
204  C CG  . GLN A 32  ? 0.2343 0.5823 0.3724 0.0475  -0.0014 -0.0009 89  GLN A CG  
205  C CD  . GLN A 32  ? 0.4912 0.8421 0.6108 0.0769  -0.0124 0.0043  89  GLN A CD  
206  O OE1 . GLN A 32  ? 0.4266 0.7279 0.5207 0.1029  -0.0125 0.0170  89  GLN A OE1 
207  N NE2 . GLN A 32  ? 0.5282 0.9328 0.6549 0.0720  -0.0187 -0.0057 89  GLN A NE2 
208  N N   A MET A 33  ? 0.1838 0.3928 0.2729 0.0665  0.0353  0.0177  90  MET A N   
209  N N   B MET A 33  ? 0.1840 0.3927 0.2731 0.0661  0.0353  0.0177  90  MET A N   
210  C CA  A MET A 33  ? 0.2458 0.4334 0.3181 0.0853  0.0464  0.0198  90  MET A CA  
211  C CA  B MET A 33  ? 0.2472 0.4290 0.3174 0.0845  0.0459  0.0201  90  MET A CA  
212  C C   A MET A 33  ? 0.2702 0.4594 0.3441 0.0636  0.0578  0.0176  90  MET A C   
213  C C   B MET A 33  ? 0.2814 0.4483 0.3468 0.0616  0.0558  0.0188  90  MET A C   
214  O O   A MET A 33  ? 0.2941 0.4830 0.3586 0.0774  0.0687  0.0170  90  MET A O   
215  O O   B MET A 33  ? 0.2882 0.4220 0.3316 0.0709  0.0630  0.0192  90  MET A O   
216  C CB  A MET A 33  ? 0.2603 0.3745 0.2991 0.0954  0.0453  0.0233  90  MET A CB  
217  C CB  B MET A 33  ? 0.2593 0.3739 0.2975 0.1003  0.0439  0.0241  90  MET A CB  
218  C CG  A MET A 33  ? 0.2812 0.3773 0.3072 0.1192  0.0398  0.0281  90  MET A CG  
219  C CG  B MET A 33  ? 0.2340 0.3480 0.2645 0.1287  0.0391  0.0293  90  MET A CG  
220  S SD  A MET A 33  ? 0.3728 0.4834 0.3865 0.1625  0.0478  0.0320  90  MET A SD  
221  S SD  B MET A 33  ? 0.3621 0.3850 0.3503 0.1356  0.0434  0.0321  90  MET A SD  
222  C CE  A MET A 33  ? 0.4484 0.4622 0.4130 0.1700  0.0545  0.0351  90  MET A CE  
223  C CE  B MET A 33  ? 0.4123 0.4058 0.3738 0.1591  0.0603  0.0297  90  MET A CE  
224  N N   . GLY A 34  ? 0.1930 0.4078 0.3174 0.0622  0.0159  0.1299  91  GLY A N   
225  C CA  . GLY A 34  ? 0.2496 0.4606 0.3750 0.0663  0.0225  0.1323  91  GLY A CA  
226  C C   . GLY A 34  ? 0.2381 0.4099 0.3378 0.0664  0.0223  0.1092  91  GLY A C   
227  O O   . GLY A 34  ? 0.3333 0.4978 0.4262 0.0773  0.0310  0.1111  91  GLY A O   
228  N N   A PHE A 35  ? 0.1959 0.3444 0.2817 0.0549  0.0129  0.0890  92  PHE A N   
229  N N   B PHE A 35  ? 0.1969 0.3457 0.2826 0.0553  0.0130  0.0893  92  PHE A N   
230  C CA  A PHE A 35  ? 0.2247 0.3412 0.2887 0.0558  0.0125  0.0697  92  PHE A CA  
231  C CA  B PHE A 35  ? 0.2258 0.3430 0.2912 0.0532  0.0110  0.0691  92  PHE A CA  
232  C C   A PHE A 35  ? 0.2153 0.3238 0.2839 0.0353  0.0024  0.0593  92  PHE A C   
233  C C   B PHE A 35  ? 0.2159 0.3308 0.2904 0.0346  0.0034  0.0643  92  PHE A C   
234  O O   A PHE A 35  ? 0.1955 0.3105 0.2725 0.0198  -0.0063 0.0587  92  PHE A O   
235  O O   B PHE A 35  ? 0.2278 0.3584 0.3192 0.0188  -0.0034 0.0717  92  PHE A O   
236  C CB  A PHE A 35  ? 0.2419 0.3342 0.2822 0.0633  0.0129  0.0557  92  PHE A CB  
237  C CB  B PHE A 35  ? 0.2419 0.3379 0.2901 0.0507  0.0059  0.0527  92  PHE A CB  
238  C CG  A PHE A 35  ? 0.2538 0.3473 0.2849 0.0827  0.0234  0.0653  92  PHE A CG  
239  C CG  B PHE A 35  ? 0.2695 0.3483 0.2959 0.0683  0.0138  0.0492  92  PHE A CG  
240  C CD1 A PHE A 35  ? 0.3221 0.4248 0.3534 0.1001  0.0357  0.0802  92  PHE A CD1 
241  C CD1 B PHE A 35  ? 0.3106 0.3651 0.3149 0.0759  0.0170  0.0386  92  PHE A CD1 
242  C CD2 A PHE A 35  ? 0.3166 0.3999 0.3370 0.0854  0.0228  0.0606  92  PHE A CD2 
243  C CD2 B PHE A 35  ? 0.2788 0.3633 0.3041 0.0762  0.0173  0.0563  92  PHE A CD2 
244  C CE1 A PHE A 35  ? 0.4229 0.5228 0.4421 0.1210  0.0481  0.0901  92  PHE A CE1 
245  C CE1 B PHE A 35  ? 0.2825 0.3147 0.2610 0.0893  0.0231  0.0340  92  PHE A CE1 
246  C CE2 A PHE A 35  ? 0.3872 0.4671 0.3962 0.1052  0.0346  0.0702  92  PHE A CE2 
247  C CE2 B PHE A 35  ? 0.3597 0.4213 0.3603 0.0921  0.0256  0.0526  92  PHE A CE2 
248  C CZ  A PHE A 35  ? 0.4069 0.4941 0.4142 0.1237  0.0477  0.0849  92  PHE A CZ  
249  C CZ  B PHE A 35  ? 0.3098 0.3430 0.2854 0.0975  0.0281  0.0405  92  PHE A CZ  
250  N N   . ASN A 36  ? 0.1763 0.2694 0.2369 0.0364  0.0043  0.0520  93  ASN A N   
251  C CA  . ASN A 36  ? 0.1999 0.2791 0.2598 0.0219  -0.0017 0.0419  93  ASN A CA  
252  C C   . ASN A 36  ? 0.1933 0.2522 0.2369 0.0213  -0.0055 0.0251  93  ASN A C   
253  O O   . ASN A 36  ? 0.2077 0.2601 0.2389 0.0320  -0.0033 0.0204  93  ASN A O   
254  C CB  . ASN A 36  ? 0.2530 0.3267 0.3121 0.0265  0.0037  0.0441  93  ASN A CB  
255  C CG  . ASN A 36  ? 0.4749 0.5660 0.5526 0.0211  0.0062  0.0602  93  ASN A CG  
256  O OD1 . ASN A 36  ? 0.4869 0.5897 0.5781 0.0061  0.0003  0.0665  93  ASN A OD1 
257  N ND2 . ASN A 36  ? 0.5918 0.6858 0.6700 0.0321  0.0145  0.0682  93  ASN A ND2 
258  N N   . VAL A 37  ? 0.2161 0.2630 0.2582 0.0086  -0.0105 0.0167  94  VAL A N   
259  C CA  . VAL A 37  ? 0.1951 0.2257 0.2249 0.0082  -0.0128 0.0032  94  VAL A CA  
260  C C   . VAL A 37  ? 0.2112 0.2285 0.2379 0.0061  -0.0109 -0.0014 94  VAL A C   
261  O O   . VAL A 37  ? 0.2596 0.2718 0.2899 -0.0027 -0.0107 0.0013  94  VAL A O   
262  C CB  . VAL A 37  ? 0.1844 0.2121 0.2120 -0.0019 -0.0185 -0.0016 94  VAL A CB  
263  C CG1 . VAL A 37  ? 0.2378 0.2501 0.2544 -0.0013 -0.0190 -0.0134 94  VAL A CG1 
264  C CG2 . VAL A 37  ? 0.1696 0.2126 0.2014 0.0014  -0.0197 0.0053  94  VAL A CG2 
265  N N   A VAL A 38  ? 0.1745 0.1859 0.1940 0.0139  -0.0095 -0.0071 95  VAL A N   
266  N N   B VAL A 38  ? 0.1744 0.1857 0.1937 0.0138  -0.0097 -0.0073 95  VAL A N   
267  C CA  A VAL A 38  ? 0.1788 0.1802 0.1965 0.0140  -0.0069 -0.0097 95  VAL A CA  
268  C CA  B VAL A 38  ? 0.1781 0.1802 0.1953 0.0150  -0.0071 -0.0100 95  VAL A CA  
269  C C   A VAL A 38  ? 0.1878 0.1831 0.2003 0.0130  -0.0088 -0.0178 95  VAL A C   
270  C C   B VAL A 38  ? 0.1874 0.1825 0.1997 0.0127  -0.0090 -0.0181 95  VAL A C   
271  O O   A VAL A 38  ? 0.1732 0.1726 0.1825 0.0154  -0.0121 -0.0212 95  VAL A O   
272  O O   B VAL A 38  ? 0.1751 0.1738 0.1842 0.0142  -0.0124 -0.0218 95  VAL A O   
273  C CB  A VAL A 38  ? 0.2077 0.2134 0.2252 0.0241  -0.0033 -0.0050 95  VAL A CB  
274  C CB  B VAL A 38  ? 0.1999 0.2077 0.2150 0.0259  -0.0049 -0.0067 95  VAL A CB  
275  C CG1 A VAL A 38  ? 0.2208 0.2315 0.2449 0.0248  0.0006  0.0048  95  VAL A CG1 
276  C CG1 B VAL A 38  ? 0.2397 0.2435 0.2540 0.0289  -0.0033 -0.0082 95  VAL A CG1 
277  C CG2 A VAL A 38  ? 0.1796 0.1909 0.1893 0.0318  -0.0064 -0.0075 95  VAL A CG2 
278  C CG2 B VAL A 38  ? 0.2390 0.2522 0.2593 0.0293  -0.0005 0.0029  95  VAL A CG2 
279  N N   . ILE A 39  ? 0.1959 0.1789 0.2060 0.0096  -0.0056 -0.0200 96  ILE A N   
280  C CA  . ILE A 39  ? 0.1861 0.1628 0.1919 0.0081  -0.0054 -0.0257 96  ILE A CA  
281  C C   . ILE A 39  ? 0.1900 0.1663 0.1976 0.0159  0.0001  -0.0234 96  ILE A C   
282  O O   . ILE A 39  ? 0.2065 0.1761 0.2138 0.0200  0.0060  -0.0189 96  ILE A O   
283  C CB  . ILE A 39  ? 0.1984 0.1592 0.1957 -0.0013 -0.0050 -0.0293 96  ILE A CB  
284  C CG1 . ILE A 39  ? 0.2049 0.1736 0.2042 -0.0091 -0.0117 -0.0282 96  ILE A CG1 
285  C CG2 . ILE A 39  ? 0.2446 0.1972 0.2350 -0.0005 -0.0025 -0.0342 96  ILE A CG2 
286  C CD1 . ILE A 39  ? 0.2738 0.2300 0.2665 -0.0213 -0.0136 -0.0279 96  ILE A CD1 
287  N N   . SER A 40  ? 0.1839 0.1684 0.1943 0.0181  -0.0015 -0.0247 97  SER A N   
288  C CA  . SER A 40  ? 0.1868 0.1773 0.2026 0.0254  0.0036  -0.0196 97  SER A CA  
289  C C   . SER A 40  ? 0.2096 0.1951 0.2235 0.0241  0.0070  -0.0218 97  SER A C   
290  O O   . SER A 40  ? 0.2026 0.1926 0.2168 0.0184  0.0014  -0.0258 97  SER A O   
291  C CB  . SER A 40  ? 0.2169 0.2286 0.2406 0.0281  -0.0031 -0.0157 97  SER A CB  
292  O OG  . SER A 40  ? 0.2769 0.3019 0.3099 0.0350  0.0005  -0.0074 97  SER A OG  
293  N N   . MET A 41  ? 0.2070 0.1808 0.2169 0.0306  0.0177  -0.0184 98  MET A N   
294  C CA  . MET A 41  ? 0.2283 0.1958 0.2341 0.0326  0.0243  -0.0186 98  MET A CA  
295  C C   . MET A 41  ? 0.2505 0.2426 0.2731 0.0400  0.0267  -0.0086 98  MET A C   
296  O O   . MET A 41  ? 0.2678 0.2713 0.2993 0.0490  0.0309  0.0007  98  MET A O   
297  C CB  . MET A 41  ? 0.2659 0.2031 0.2535 0.0376  0.0369  -0.0193 98  MET A CB  
298  C CG  . MET A 41  ? 0.2575 0.1787 0.2309 0.0371  0.0427  -0.0232 98  MET A CG  
299  S SD  . MET A 41  ? 0.3577 0.2310 0.2969 0.0392  0.0554  -0.0283 98  MET A SD  
300  C CE  . MET A 41  ? 0.4005 0.2752 0.3431 0.0610  0.0750  -0.0153 98  MET A CE  
301  N N   . VAL A 42  ? 0.2353 0.2363 0.2628 0.0365  0.0250  -0.0086 99  VAL A N   
302  C CA  . VAL A 42  ? 0.2337 0.2638 0.2809 0.0384  0.0235  0.0017  99  VAL A CA  
303  C C   . VAL A 42  ? 0.3586 0.3871 0.4068 0.0459  0.0362  0.0082  99  VAL A C   
304  O O   . VAL A 42  ? 0.3468 0.3539 0.3793 0.0438  0.0402  0.0008  99  VAL A O   
305  C CB  . VAL A 42  ? 0.2905 0.3331 0.3432 0.0251  0.0089  -0.0031 99  VAL A CB  
306  C CG1 . VAL A 42  ? 0.4144 0.4880 0.4867 0.0227  0.0024  0.0075  99  VAL A CG1 
307  C CG2 . VAL A 42  ? 0.3388 0.3713 0.3813 0.0195  -0.0001 -0.0123 99  VAL A CG2 
308  N N   . GLU A 43  ? 0.2869 0.3396 0.3530 0.0556  0.0430  0.0236  100 GLU A N   
309  C CA  . GLU A 43  ? 0.3083 0.3706 0.3824 0.0622  0.0539  0.0337  100 GLU A CA  
310  C C   . GLU A 43  ? 0.3043 0.3917 0.3957 0.0482  0.0415  0.0357  100 GLU A C   
311  O O   . GLU A 43  ? 0.3720 0.4645 0.4651 0.0344  0.0255  0.0282  100 GLU A O   
312  C CB  . GLU A 43  ? 0.3693 0.4525 0.4593 0.0795  0.0672  0.0532  100 GLU A CB  
313  C CG  . GLU A 43  ? 0.5266 0.5863 0.6011 0.0936  0.0790  0.0536  100 GLU A CG  
314  C CD  . GLU A 43  ? 0.7959 0.8066 0.8363 0.0986  0.0919  0.0419  100 GLU A CD  
315  O OE1 . GLU A 43  ? 0.8327 0.8343 0.8652 0.1035  0.1022  0.0436  100 GLU A OE1 
316  O OE2 . GLU A 43  ? 0.8559 0.8369 0.8763 0.0968  0.0914  0.0318  100 GLU A OE2 
317  N N   . GLN A 44  ? 0.2961 0.3982 0.3996 0.0522  0.0500  0.0470  101 GLN A N   
318  C CA  . GLN A 44  ? 0.3623 0.4826 0.4797 0.0373  0.0395  0.0487  101 GLN A CA  
319  C C   . GLN A 44  ? 0.2857 0.4447 0.4296 0.0275  0.0258  0.0601  101 GLN A C   
320  O O   . GLN A 44  ? 0.2648 0.4474 0.4239 0.0367  0.0289  0.0738  101 GLN A O   
321  C CB  . GLN A 44  ? 0.4291 0.5539 0.5519 0.0443  0.0538  0.0589  101 GLN A CB  
322  C CG  . GLN A 44  ? 0.5292 0.6135 0.6207 0.0529  0.0665  0.0475  101 GLN A CG  
323  C CD  . GLN A 44  ? 0.6715 0.7295 0.7421 0.0392  0.0546  0.0280  101 GLN A CD  
324  O OE1 . GLN A 44  ? 0.6472 0.7148 0.7259 0.0245  0.0393  0.0234  101 GLN A OE1 
325  N NE2 . GLN A 44  ? 0.4474 0.4711 0.4890 0.0445  0.0618  0.0173  101 GLN A NE2 
326  N N   . GLY A 45  ? 0.3371 0.5006 0.4837 0.0086  0.0102  0.0546  102 GLY A N   
327  C CA  . GLY A 45  ? 0.2421 0.4402 0.4107 -0.0049 -0.0045 0.0657  102 GLY A CA  
328  C C   . GLY A 45  ? 0.2116 0.3994 0.3661 -0.0175 -0.0224 0.0530  102 GLY A C   
329  O O   . GLY A 45  ? 0.1976 0.3619 0.3327 -0.0106 -0.0212 0.0409  102 GLY A O   
330  N N   . VAL A 46  ? 0.1851 0.3903 0.3482 -0.0367 -0.0390 0.0567  103 VAL A N   
331  C CA  . VAL A 46  ? 0.2206 0.4099 0.3636 -0.0492 -0.0556 0.0438  103 VAL A CA  
332  C C   . VAL A 46  ? 0.2205 0.4228 0.3638 -0.0405 -0.0587 0.0475  103 VAL A C   
333  O O   . VAL A 46  ? 0.1953 0.3744 0.3158 -0.0394 -0.0633 0.0345  103 VAL A O   
334  C CB  . VAL A 46  ? 0.2919 0.4900 0.4381 -0.0739 -0.0729 0.0462  103 VAL A CB  
335  C CG1 . VAL A 46  ? 0.3740 0.6218 0.5542 -0.0804 -0.0782 0.0692  103 VAL A CG1 
336  C CG2 . VAL A 46  ? 0.4340 0.6095 0.5523 -0.0857 -0.0889 0.0324  103 VAL A CG2 
337  N N   . GLU A 47  ? 0.1770 0.4174 0.3465 -0.0325 -0.0548 0.0671  104 GLU A N   
338  C CA  . GLU A 47  ? 0.1764 0.4293 0.3461 -0.0225 -0.0566 0.0722  104 GLU A CA  
339  C C   . GLU A 47  ? 0.1791 0.3999 0.3298 -0.0044 -0.0426 0.0609  104 GLU A C   
340  O O   . GLU A 47  ? 0.1745 0.3845 0.3101 -0.0021 -0.0476 0.0540  104 GLU A O   
341  C CB  . GLU A 47  ? 0.2050 0.5056 0.4074 -0.0134 -0.0518 0.0980  104 GLU A CB  
342  C CG  . GLU A 47  ? 0.2446 0.5586 0.4464 -0.0028 -0.0541 0.1044  104 GLU A CG  
343  C CD  . GLU A 47  ? 0.5139 0.8345 0.7044 -0.0223 -0.0784 0.0995  104 GLU A CD  
344  O OE1 . GLU A 47  ? 0.3817 0.7232 0.5821 -0.0435 -0.0944 0.1051  104 GLU A OE1 
345  O OE2 . GLU A 47  ? 0.6158 0.9182 0.7850 -0.0172 -0.0812 0.0899  104 GLU A OE2 
346  N N   . ALA A 48  ? 0.1690 0.3742 0.3192 0.0078  -0.0251 0.0598  105 ALA A N   
347  C CA  . ALA A 48  ? 0.1696 0.3429 0.3007 0.0214  -0.0132 0.0495  105 ALA A CA  
348  C C   . ALA A 48  ? 0.1883 0.3304 0.2952 0.0120  -0.0215 0.0299  105 ALA A C   
349  O O   . ALA A 48  ? 0.2168 0.3420 0.3100 0.0180  -0.0197 0.0231  105 ALA A O   
350  C CB  . ALA A 48  ? 0.1769 0.3357 0.3068 0.0335  0.0056  0.0513  105 ALA A CB  
351  N N   A CYS A 49  ? 0.1698 0.3045 0.2716 -0.0019 -0.0297 0.0224  106 CYS A N   
352  N N   B CYS A 49  ? 0.1697 0.3040 0.2715 -0.0017 -0.0293 0.0224  106 CYS A N   
353  C CA  A CYS A 49  ? 0.1893 0.2954 0.2681 -0.0081 -0.0356 0.0063  106 CYS A CA  
354  C CA  B CYS A 49  ? 0.1928 0.2996 0.2720 -0.0089 -0.0362 0.0064  106 CYS A CA  
355  C C   A CYS A 49  ? 0.2026 0.3107 0.2715 -0.0134 -0.0483 0.0036  106 CYS A C   
356  C C   B CYS A 49  ? 0.2027 0.3119 0.2724 -0.0126 -0.0479 0.0042  106 CYS A C   
357  O O   A CYS A 49  ? 0.2213 0.3094 0.2727 -0.0098 -0.0482 -0.0056 106 CYS A O   
358  O O   B CYS A 49  ? 0.2148 0.3054 0.2684 -0.0077 -0.0468 -0.0040 106 CYS A O   
359  C CB  A CYS A 49  ? 0.2014 0.2960 0.2754 -0.0195 -0.0389 0.0003  106 CYS A CB  
360  C CB  B CYS A 49  ? 0.2018 0.3004 0.2771 -0.0222 -0.0419 0.0014  106 CYS A CB  
361  S SG  A CYS A 49  ? 0.2260 0.2842 0.2736 -0.0203 -0.0387 -0.0164 106 CYS A SG  
362  S SG  B CYS A 49  ? 0.1950 0.2805 0.2708 -0.0168 -0.0283 -0.0004 106 CYS A SG  
363  N N   . LYS A 50  ? 0.1872 0.3200 0.2661 -0.0222 -0.0596 0.0124  107 LYS A N   
364  C CA  . LYS A 50  ? 0.1963 0.3305 0.2619 -0.0270 -0.0722 0.0104  107 LYS A CA  
365  C C   . LYS A 50  ? 0.2430 0.3805 0.3082 -0.0111 -0.0651 0.0141  107 LYS A C   
366  O O   . LYS A 50  ? 0.2428 0.3643 0.2882 -0.0087 -0.0682 0.0067  107 LYS A O   
367  C CB  . LYS A 50  ? 0.2059 0.3710 0.2847 -0.0410 -0.0868 0.0219  107 LYS A CB  
368  C CG  . LYS A 50  ? 0.2623 0.4175 0.3333 -0.0618 -0.0982 0.0165  107 LYS A CG  
369  C CD  . LYS A 50  ? 0.3807 0.5731 0.4713 -0.0777 -0.1127 0.0314  107 LYS A CD  
370  C CE  . LYS A 50  ? 0.4931 0.6708 0.5570 -0.0986 -0.1331 0.0235  107 LYS A CE  
371  N NZ  . LYS A 50  ? 0.4891 0.7009 0.5715 -0.1161 -0.1471 0.0381  107 LYS A NZ  
372  N N   . ALA A 51  ? 0.1977 0.3534 0.2832 0.0013  -0.0538 0.0263  108 ALA A N   
373  C CA  . ALA A 51  ? 0.2232 0.3783 0.3077 0.0168  -0.0451 0.0306  108 ALA A CA  
374  C C   . ALA A 51  ? 0.2303 0.3515 0.2968 0.0221  -0.0369 0.0176  108 ALA A C   
375  O O   . ALA A 51  ? 0.2211 0.3351 0.2776 0.0282  -0.0363 0.0163  108 ALA A O   
376  C CB  . ALA A 51  ? 0.2096 0.3835 0.3154 0.0304  -0.0315 0.0461  108 ALA A CB  
377  N N   . ALA A 52  ? 0.2094 0.3117 0.2721 0.0194  -0.0311 0.0094  109 ALA A N   
378  C CA  . ALA A 52  ? 0.1849 0.2601 0.2327 0.0218  -0.0258 -0.0011 109 ALA A CA  
379  C C   . ALA A 52  ? 0.2243 0.2895 0.2556 0.0163  -0.0351 -0.0092 109 ALA A C   
380  O O   . ALA A 52  ? 0.2118 0.2663 0.2342 0.0218  -0.0319 -0.0115 109 ALA A O   
381  C CB  . ALA A 52  ? 0.2060 0.2663 0.2523 0.0189  -0.0198 -0.0071 109 ALA A CB  
382  N N   . VAL A 53  ? 0.1843 0.2505 0.2097 0.0057  -0.0454 -0.0129 110 VAL A N   
383  C CA  . VAL A 53  ? 0.2019 0.2525 0.2054 0.0021  -0.0526 -0.0207 110 VAL A CA  
384  C C   . VAL A 53  ? 0.2291 0.2863 0.2251 0.0080  -0.0559 -0.0166 110 VAL A C   
385  O O   . VAL A 53  ? 0.2530 0.2959 0.2333 0.0139  -0.0535 -0.0204 110 VAL A O   
386  C CB  . VAL A 53  ? 0.2607 0.3064 0.2555 -0.0118 -0.0631 -0.0250 110 VAL A CB  
387  C CG1 . VAL A 53  ? 0.3262 0.3541 0.2924 -0.0152 -0.0715 -0.0316 110 VAL A CG1 
388  C CG2 . VAL A 53  ? 0.2827 0.3143 0.2781 -0.0150 -0.0579 -0.0304 110 VAL A CG2 
389  N N   . ASN A 54  ? 0.2175 0.2991 0.2261 0.0079  -0.0604 -0.0067 111 ASN A N   
390  C CA  . ASN A 54  ? 0.2444 0.3344 0.2457 0.0143  -0.0638 -0.0014 111 ASN A CA  
391  C C   . ASN A 54  ? 0.2101 0.2943 0.2147 0.0287  -0.0506 0.0017  111 ASN A C   
392  O O   . ASN A 54  ? 0.2806 0.3582 0.2710 0.0349  -0.0503 0.0015  111 ASN A O   
393  C CB  . ASN A 54  ? 0.2669 0.3892 0.2841 0.0115  -0.0716 0.0113  111 ASN A CB  
394  C CG  . ASN A 54  ? 0.3190 0.4471 0.3271 -0.0061 -0.0891 0.0092  111 ASN A CG  
395  O OD1 . ASN A 54  ? 0.3788 0.4822 0.3590 -0.0136 -0.0963 -0.0022 111 ASN A OD1 
396  N ND2 . ASN A 54  ? 0.3680 0.5278 0.3985 -0.0130 -0.0956 0.0212  111 ASN A ND2 
397  N N   . SER A 55  ? 0.1941 0.2781 0.2149 0.0336  -0.0393 0.0046  112 SER A N   
398  C CA  . SER A 55  ? 0.2206 0.2936 0.2420 0.0437  -0.0275 0.0066  112 SER A CA  
399  C C   . SER A 55  ? 0.2358 0.2892 0.2433 0.0423  -0.0263 -0.0018 112 SER A C   
400  O O   . SER A 55  ? 0.2954 0.3443 0.2976 0.0491  -0.0217 0.0011  112 SER A O   
401  C CB  . SER A 55  ? 0.2317 0.2999 0.2656 0.0467  -0.0164 0.0090  112 SER A CB  
402  O OG  . SER A 55  ? 0.2788 0.3316 0.3101 0.0530  -0.0061 0.0102  112 SER A OG  
403  N N   . LEU A 56  ? 0.2229 0.2662 0.2255 0.0345  -0.0292 -0.0103 113 LEU A N   
404  C CA  . LEU A 56  ? 0.2376 0.2660 0.2295 0.0350  -0.0268 -0.0154 113 LEU A CA  
405  C C   . LEU A 56  ? 0.2290 0.2528 0.2017 0.0388  -0.0310 -0.0164 113 LEU A C   
406  O O   . LEU A 56  ? 0.2764 0.2940 0.2429 0.0455  -0.0253 -0.0145 113 LEU A O   
407  C CB  . LEU A 56  ? 0.2079 0.2277 0.1991 0.0275  -0.0282 -0.0224 113 LEU A CB  
408  C CG  . LEU A 56  ? 0.1974 0.2165 0.2017 0.0249  -0.0225 -0.0221 113 LEU A CG  
409  C CD1 . LEU A 56  ? 0.2070 0.2208 0.2099 0.0177  -0.0252 -0.0279 113 LEU A CD1 
410  C CD2 . LEU A 56  ? 0.1980 0.2102 0.2047 0.0271  -0.0157 -0.0202 113 LEU A CD2 
411  N N   . LEU A 57  ? 0.2468 0.2727 0.2080 0.0341  -0.0408 -0.0187 114 LEU A N   
412  C CA  . LEU A 57  ? 0.2809 0.2972 0.2166 0.0378  -0.0449 -0.0204 114 LEU A CA  
413  C C   . LEU A 57  ? 0.3112 0.3369 0.2477 0.0485  -0.0406 -0.0119 114 LEU A C   
414  O O   . LEU A 57  ? 0.3272 0.3425 0.2449 0.0567  -0.0373 -0.0114 114 LEU A O   
415  C CB  . LEU A 57  ? 0.2791 0.2944 0.2000 0.0268  -0.0588 -0.0246 114 LEU A CB  
416  C CG  . LEU A 57  ? 0.3347 0.3355 0.2491 0.0153  -0.0633 -0.0330 114 LEU A CG  
417  C CD1 . LEU A 57  ? 0.3787 0.3808 0.2810 0.0007  -0.0788 -0.0353 114 LEU A CD1 
418  C CD2 . LEU A 57  ? 0.3863 0.3591 0.2783 0.0208  -0.0567 -0.0396 114 LEU A CD2 
419  N N   . ALA A 58  ? 0.2741 0.3181 0.2309 0.0504  -0.0389 -0.0039 115 ALA A N   
420  C CA  . ALA A 58  ? 0.3328 0.3842 0.2916 0.0615  -0.0330 0.0055  115 ALA A CA  
421  C C   . ALA A 58  ? 0.3122 0.3543 0.2762 0.0681  -0.0205 0.0081  115 ALA A C   
422  O O   . ALA A 58  ? 0.3140 0.3581 0.2752 0.0775  -0.0147 0.0158  115 ALA A O   
423  C CB  . ALA A 58  ? 0.2639 0.3347 0.2428 0.0637  -0.0318 0.0149  115 ALA A CB  
424  N N   . GLN A 59  ? 0.2940 0.3281 0.2664 0.0627  -0.0169 0.0033  116 GLN A N   
425  C CA  . GLN A 59  ? 0.2656 0.2937 0.2426 0.0658  -0.0079 0.0066  116 GLN A CA  
426  C C   . GLN A 59  ? 0.3290 0.3493 0.2890 0.0704  -0.0070 0.0048  116 GLN A C   
427  O O   . GLN A 59  ? 0.3219 0.3422 0.2880 0.0733  0.0003  0.0100  116 GLN A O   
428  C CB  . GLN A 59  ? 0.2666 0.2911 0.2586 0.0571  -0.0056 0.0036  116 GLN A CB  
429  C CG  . GLN A 59  ? 0.2478 0.2733 0.2519 0.0548  -0.0029 0.0056  116 GLN A CG  
430  C CD  . GLN A 59  ? 0.4047 0.4295 0.4140 0.0610  0.0053  0.0150  116 GLN A CD  
431  O OE1 . GLN A 59  ? 0.3741 0.3942 0.3866 0.0597  0.0103  0.0189  116 GLN A OE1 
432  N NE2 . GLN A 59  ? 0.3747 0.4057 0.3858 0.0676  0.0067  0.0206  116 GLN A NE2 
433  N N   . ARG A 60  ? 0.2909 0.3037 0.2285 0.0711  -0.0139 -0.0012 117 ARG A N   
434  C CA  . ARG A 60  ? 0.3490 0.3473 0.2623 0.0785  -0.0111 -0.0030 117 ARG A CA  
435  C C   . ARG A 60  ? 0.3328 0.3246 0.2505 0.0766  -0.0070 -0.0054 117 ARG A C   
436  O O   . ARG A 60  ? 0.3472 0.3352 0.2586 0.0863  0.0017  0.0000  117 ARG A O   
437  C CB  . ARG A 60  ? 0.3253 0.3260 0.2328 0.0921  -0.0017 0.0072  117 ARG A CB  
438  C CG  . ARG A 60  ? 0.4221 0.4336 0.3320 0.0955  -0.0031 0.0133  117 ARG A CG  
439  C CD  . ARG A 60  ? 0.4250 0.4300 0.3073 0.0956  -0.0132 0.0081  117 ARG A CD  
440  N NE  . ARG A 60  ? 0.3972 0.4142 0.2784 0.1019  -0.0139 0.0164  117 ARG A NE  
441  C CZ  . ARG A 60  ? 0.3955 0.4138 0.2570 0.0996  -0.0254 0.0141  117 ARG A CZ  
442  N NH1 . ARG A 60  ? 0.4400 0.4463 0.2810 0.0893  -0.0373 0.0033  117 ARG A NH1 
443  N NH2 . ARG A 60  ? 0.3653 0.3973 0.2272 0.1067  -0.0255 0.0237  117 ARG A NH2 
444  N N   . VAL A 61  ? 0.3048 0.2972 0.2337 0.0654  -0.0124 -0.0117 118 VAL A N   
445  C CA  . VAL A 61  ? 0.2602 0.2490 0.1945 0.0639  -0.0087 -0.0125 118 VAL A CA  
446  C C   . VAL A 61  ? 0.2886 0.2569 0.1949 0.0697  -0.0075 -0.0171 118 VAL A C   
447  O O   . VAL A 61  ? 0.3590 0.3116 0.2401 0.0691  -0.0130 -0.0236 118 VAL A O   
448  C CB  . VAL A 61  ? 0.2476 0.2409 0.1987 0.0516  -0.0137 -0.0175 118 VAL A CB  
449  C CG1 . VAL A 61  ? 0.2379 0.2440 0.2106 0.0475  -0.0124 -0.0131 118 VAL A CG1 
450  C CG2 . VAL A 61  ? 0.2990 0.2845 0.2394 0.0441  -0.0225 -0.0260 118 VAL A CG2 
451  N N   . ASP A 62  ? 0.2816 0.2489 0.1907 0.0754  -0.0001 -0.0125 119 ASP A N   
452  C CA  . ASP A 62  ? 0.3045 0.2488 0.1858 0.0841  0.0047  -0.0149 119 ASP A CA  
453  C C   . ASP A 62  ? 0.3188 0.2479 0.1923 0.0739  -0.0017 -0.0250 119 ASP A C   
454  O O   . ASP A 62  ? 0.3600 0.2607 0.2021 0.0768  -0.0012 -0.0312 119 ASP A O   
455  C CB  . ASP A 62  ? 0.3186 0.2726 0.2089 0.0969  0.0169  -0.0021 119 ASP A CB  
456  C CG  . ASP A 62  ? 0.3885 0.3564 0.2847 0.1083  0.0252  0.0101  119 ASP A CG  
457  O OD1 . ASP A 62  ? 0.4180 0.4090 0.3420 0.1016  0.0233  0.0162  119 ASP A OD1 
458  O OD2 . ASP A 62  ? 0.6303 0.5833 0.5009 0.1242  0.0345  0.0140  119 ASP A OD2 
459  N N   . GLY A 63  ? 0.2883 0.2324 0.1869 0.0622  -0.0070 -0.0265 120 GLY A N   
460  C CA  . GLY A 63  ? 0.2977 0.2307 0.1928 0.0532  -0.0114 -0.0336 120 GLY A CA  
461  C C   . GLY A 63  ? 0.2478 0.1989 0.1688 0.0406  -0.0178 -0.0353 120 GLY A C   
462  O O   . GLY A 63  ? 0.2444 0.2136 0.1848 0.0401  -0.0169 -0.0304 120 GLY A O   
463  N N   . LEU A 64  ? 0.2442 0.1877 0.1634 0.0308  -0.0231 -0.0416 121 LEU A N   
464  C CA  . LEU A 64  ? 0.2238 0.1818 0.1638 0.0206  -0.0276 -0.0427 121 LEU A CA  
465  C C   . LEU A 64  ? 0.2370 0.1922 0.1819 0.0162  -0.0264 -0.0439 121 LEU A C   
466  O O   . LEU A 64  ? 0.2751 0.2133 0.2049 0.0161  -0.0258 -0.0466 121 LEU A O   
467  C CB  . LEU A 64  ? 0.2509 0.2093 0.1882 0.0120  -0.0357 -0.0464 121 LEU A CB  
468  C CG  . LEU A 64  ? 0.2642 0.2293 0.1978 0.0156  -0.0383 -0.0442 121 LEU A CG  
469  C CD1 . LEU A 64  ? 0.3243 0.2855 0.2456 0.0066  -0.0486 -0.0475 121 LEU A CD1 
470  C CD2 . LEU A 64  ? 0.2793 0.2650 0.2367 0.0166  -0.0359 -0.0387 121 LEU A CD2 
471  N N   . ILE A 65  ? 0.2324 0.2010 0.1951 0.0127  -0.0256 -0.0419 122 ILE A N   
472  C CA  . ILE A 65  ? 0.2361 0.2035 0.2032 0.0076  -0.0253 -0.0431 122 ILE A CA  
473  C C   . ILE A 65  ? 0.2528 0.2280 0.2313 0.0010  -0.0271 -0.0443 122 ILE A C   
474  O O   . ILE A 65  ? 0.2171 0.2008 0.2043 0.0021  -0.0258 -0.0423 122 ILE A O   
475  C CB  . ILE A 65  ? 0.2115 0.1858 0.1845 0.0102  -0.0221 -0.0385 122 ILE A CB  
476  C CG1 . ILE A 65  ? 0.2249 0.1962 0.1895 0.0196  -0.0184 -0.0336 122 ILE A CG1 
477  C CG2 . ILE A 65  ? 0.2519 0.2253 0.2271 0.0049  -0.0223 -0.0397 122 ILE A CG2 
478  C CD1 . ILE A 65  ? 0.2575 0.2436 0.2322 0.0215  -0.0168 -0.0253 122 ILE A CD1 
479  N N   . ILE A 66  ? 0.2304 0.2020 0.2086 -0.0049 -0.0287 -0.0461 123 ILE A N   
480  C CA  . ILE A 66  ? 0.1831 0.1646 0.1733 -0.0094 -0.0287 -0.0444 123 ILE A CA  
481  C C   . ILE A 66  ? 0.2360 0.2155 0.2285 -0.0106 -0.0244 -0.0441 123 ILE A C   
482  O O   . ILE A 66  ? 0.2555 0.2282 0.2437 -0.0141 -0.0246 -0.0447 123 ILE A O   
483  C CB  . ILE A 66  ? 0.2590 0.2422 0.2493 -0.0167 -0.0347 -0.0440 123 ILE A CB  
484  C CG1 . ILE A 66  ? 0.3195 0.2988 0.2990 -0.0164 -0.0404 -0.0458 123 ILE A CG1 
485  C CG2 . ILE A 66  ? 0.2360 0.2368 0.2436 -0.0192 -0.0337 -0.0382 123 ILE A CG2 
486  C CD1 . ILE A 66  ? 0.3187 0.3122 0.3065 -0.0111 -0.0402 -0.0422 123 ILE A CD1 
487  N N   . ASN A 67  ? 0.2143 0.1966 0.2107 -0.0081 -0.0200 -0.0431 124 ASN A N   
488  C CA  . ASN A 67  ? 0.2270 0.2054 0.2216 -0.0090 -0.0155 -0.0429 124 ASN A CA  
489  C C   . ASN A 67  ? 0.2101 0.1949 0.2131 -0.0075 -0.0102 -0.0390 124 ASN A C   
490  O O   . ASN A 67  ? 0.2299 0.2103 0.2300 -0.0034 -0.0042 -0.0384 124 ASN A O   
491  C CB  . ASN A 67  ? 0.2274 0.1993 0.2138 -0.0084 -0.0143 -0.0446 124 ASN A CB  
492  C CG  . ASN A 67  ? 0.2380 0.2030 0.2166 -0.0096 -0.0107 -0.0451 124 ASN A CG  
493  O OD1 . ASN A 67  ? 0.2814 0.2470 0.2613 -0.0103 -0.0093 -0.0436 124 ASN A OD1 
494  N ND2 . ASN A 67  ? 0.2865 0.2429 0.2548 -0.0107 -0.0093 -0.0469 124 ASN A ND2 
495  N N   . VAL A 68  ? 0.2160 0.2100 0.2282 -0.0110 -0.0119 -0.0353 125 VAL A N   
496  C CA  . VAL A 68  ? 0.2406 0.2481 0.2660 -0.0092 -0.0068 -0.0275 125 VAL A CA  
497  C C   . VAL A 68  ? 0.2320 0.2437 0.2630 -0.0158 -0.0074 -0.0238 125 VAL A C   
498  O O   . VAL A 68  ? 0.2424 0.2509 0.2709 -0.0239 -0.0153 -0.0263 125 VAL A O   
499  C CB  . VAL A 68  ? 0.2650 0.2888 0.3024 -0.0090 -0.0110 -0.0226 125 VAL A CB  
500  C CG1 . VAL A 68  ? 0.2367 0.2802 0.2914 -0.0058 -0.0051 -0.0110 125 VAL A CG1 
501  C CG2 . VAL A 68  ? 0.2658 0.2837 0.2971 -0.0026 -0.0100 -0.0257 125 VAL A CG2 
502  N N   . PRO A 69  ? 0.2555 0.2713 0.2914 -0.0125 0.0015  -0.0177 126 PRO A N   
503  C CA  . PRO A 69  ? 0.2534 0.2732 0.2956 -0.0197 0.0013  -0.0129 126 PRO A CA  
504  C C   . PRO A 69  ? 0.2590 0.3003 0.3207 -0.0289 -0.0055 -0.0044 126 PRO A C   
505  O O   . PRO A 69  ? 0.2848 0.3476 0.3632 -0.0250 -0.0022 0.0055  126 PRO A O   
506  C CB  . PRO A 69  ? 0.2592 0.2786 0.3004 -0.0111 0.0146  -0.0071 126 PRO A CB  
507  C CG  . PRO A 69  ? 0.3106 0.3309 0.3505 -0.0001 0.0218  -0.0057 126 PRO A CG  
508  C CD  . PRO A 69  ? 0.2763 0.2882 0.3081 -0.0015 0.0135  -0.0149 126 PRO A CD  
509  N N   . LEU A 70  ? 0.2497 0.2842 0.3077 -0.0416 -0.0151 -0.0075 127 LEU A N   
510  C CA  . LEU A 70  ? 0.2724 0.3230 0.3435 -0.0549 -0.0254 -0.0013 127 LEU A CA  
511  C C   . LEU A 70  ? 0.3155 0.3584 0.3861 -0.0688 -0.0287 0.0009  127 LEU A C   
512  O O   . LEU A 70  ? 0.2713 0.2877 0.3230 -0.0691 -0.0274 -0.0073 127 LEU A O   
513  C CB  . LEU A 70  ? 0.2527 0.2943 0.3109 -0.0588 -0.0367 -0.0099 127 LEU A CB  
514  C CG  . LEU A 70  ? 0.2881 0.3365 0.3465 -0.0468 -0.0347 -0.0115 127 LEU A CG  
515  C CD1 . LEU A 70  ? 0.3294 0.3627 0.3697 -0.0496 -0.0440 -0.0207 127 LEU A CD1 
516  C CD2 . LEU A 70  ? 0.2851 0.3657 0.3671 -0.0449 -0.0340 0.0018  127 LEU A CD2 
517  N N   . GLU A 71  ? 0.3005 0.3672 0.3924 -0.0807 -0.0329 0.0134  128 GLU A N   
518  C CA  . GLU A 71  ? 0.4029 0.4589 0.4918 -0.0997 -0.0406 0.0145  128 GLU A CA  
519  C C   . GLU A 71  ? 0.4967 0.5290 0.5623 -0.1108 -0.0545 0.0027  128 GLU A C   
520  O O   . GLU A 71  ? 0.4360 0.4746 0.4984 -0.1076 -0.0607 -0.0009 128 GLU A O   
521  C CB  . GLU A 71  ? 0.4206 0.5117 0.5403 -0.1127 -0.0438 0.0328  128 GLU A CB  
522  C CG  . GLU A 71  ? 0.5513 0.6709 0.6949 -0.0972 -0.0281 0.0472  128 GLU A CG  
523  C CD  . GLU A 71  ? 0.5814 0.6886 0.7221 -0.0932 -0.0154 0.0499  128 GLU A CD  
524  O OE1 . GLU A 71  ? 0.6322 0.7064 0.7504 -0.0980 -0.0171 0.0386  128 GLU A OE1 
525  O OE2 . GLU A 71  ? 0.8876 1.0177 1.0474 -0.0832 -0.0023 0.0643  128 GLU A OE2 
526  N N   . ASN A 72  ? 0.6022 0.6038 0.6485 -0.1228 -0.0581 -0.0031 129 ASN A N   
527  C CA  . ASN A 72  ? 0.7112 0.6796 0.7261 -0.1291 -0.0676 -0.0160 129 ASN A CA  
528  C C   . ASN A 72  ? 0.4720 0.4542 0.4894 -0.1456 -0.0840 -0.0138 129 ASN A C   
529  O O   . ASN A 72  ? 0.5336 0.4983 0.5276 -0.1442 -0.0907 -0.0237 129 ASN A O   
530  C CB  . ASN A 72  ? 0.8393 0.7676 0.8301 -0.1381 -0.0663 -0.0213 129 ASN A CB  
531  C CG  . ASN A 72  ? 0.8349 0.7207 0.7863 -0.1359 -0.0695 -0.0354 129 ASN A CG  
532  O OD1 . ASN A 72  ? 0.9303 0.8139 0.8726 -0.1191 -0.0657 -0.0417 129 ASN A OD1 
533  N ND2 . ASN A 72  ? 0.8567 0.7065 0.7830 -0.1526 -0.0754 -0.0395 129 ASN A ND2 
534  N N   . GLU A 73  ? 0.4227 0.4393 0.4689 -0.1603 -0.0905 0.0007  130 GLU A N   
535  C CA  . GLU A 73  ? 0.5176 0.5550 0.5696 -0.1770 -0.1080 0.0057  130 GLU A CA  
536  C C   . GLU A 73  ? 0.5513 0.6111 0.6100 -0.1599 -0.1071 0.0057  130 GLU A C   
537  O O   . GLU A 73  ? 0.4829 0.5362 0.5240 -0.1650 -0.1190 -0.0002 130 GLU A O   
538  C CB  . GLU A 73  ? 0.4559 0.5330 0.5426 -0.1899 -0.1111 0.0249  130 GLU A CB  
539  C CG  . GLU A 73  ? 0.8671 0.9301 0.9564 -0.2002 -0.1056 0.0289  130 GLU A CG  
540  C CD  . GLU A 73  ? 0.9603 1.0306 1.0660 -0.1836 -0.0873 0.0340  130 GLU A CD  
541  O OE1 . GLU A 73  ? 0.7083 0.8204 0.8495 -0.1783 -0.0797 0.0517  130 GLU A OE1 
542  O OE2 . GLU A 73  ? 0.6763 0.7096 0.7560 -0.1700 -0.0776 0.0203  130 GLU A OE2 
543  N N   . ASP A 74  ? 0.4322 0.5148 0.5128 -0.1388 -0.0922 0.0121  131 ASP A N   
544  C CA  . ASP A 74  ? 0.3688 0.4645 0.4515 -0.1213 -0.0889 0.0110  131 ASP A CA  
545  C C   . ASP A 74  ? 0.4532 0.5108 0.5028 -0.1102 -0.0861 -0.0066 131 ASP A C   
546  O O   . ASP A 74  ? 0.3774 0.4366 0.4184 -0.1044 -0.0904 -0.0101 131 ASP A O   
547  C CB  . ASP A 74  ? 0.4208 0.5433 0.5300 -0.1023 -0.0728 0.0220  131 ASP A CB  
548  C CG  . ASP A 74  ? 0.5239 0.6822 0.6660 -0.1099 -0.0709 0.0414  131 ASP A CG  
549  O OD1 . ASP A 74  ? 0.8055 0.9952 0.9659 -0.1238 -0.0834 0.0540  131 ASP A OD1 
550  O OD2 . ASP A 74  ? 0.7309 0.8879 0.8808 -0.1019 -0.0570 0.0456  131 ASP A OD2 
551  N N   . ALA A 75  ? 0.3617 0.3872 0.3935 -0.1062 -0.0782 -0.0158 132 ALA A N   
552  C CA  . ALA A 75  ? 0.4759 0.4690 0.4783 -0.0959 -0.0756 -0.0293 132 ALA A CA  
553  C C   . ALA A 75  ? 0.4057 0.3771 0.3808 -0.1076 -0.0886 -0.0367 132 ALA A C   
554  O O   . ALA A 75  ? 0.4507 0.4107 0.4081 -0.0979 -0.0887 -0.0434 132 ALA A O   
555  C CB  . ALA A 75  ? 0.5048 0.4708 0.4942 -0.0900 -0.0655 -0.0348 132 ALA A CB  
556  N N   . GLN A 76  ? 0.4713 0.4353 0.4406 -0.1293 -0.0998 -0.0351 133 GLN A N   
557  C CA  . GLN A 76  ? 0.4509 0.3918 0.3901 -0.1408 -0.1121 -0.0422 133 GLN A CA  
558  C C   . GLN A 76  ? 0.4213 0.3909 0.3689 -0.1394 -0.1211 -0.0379 133 GLN A C   
559  O O   . GLN A 76  ? 0.4770 0.4276 0.3976 -0.1338 -0.1234 -0.0457 133 GLN A O   
560  C CB  . GLN A 76  ? 0.5731 0.5064 0.5100 -0.1599 -0.1183 -0.0386 133 GLN A CB  
561  C CG  . GLN A 76  ? 0.6871 0.5833 0.6070 -0.1615 -0.1097 -0.0437 133 GLN A CG  
562  C CD  . GLN A 76  ? 0.7773 0.6639 0.6927 -0.1818 -0.1169 -0.0399 133 GLN A CD  
563  O OE1 . GLN A 76  ? 0.6111 0.5274 0.5451 -0.1962 -0.1280 -0.0306 133 GLN A OE1 
564  N NE2 . GLN A 76  ? 0.7808 0.6261 0.6714 -0.1828 -0.1102 -0.0458 133 GLN A NE2 
565  N N   . ALA A 77  ? 0.4020 0.4187 0.3872 -0.1426 -0.1246 -0.0238 134 ALA A N   
566  C CA  . ALA A 77  ? 0.3778 0.4252 0.3733 -0.1394 -0.1321 -0.0170 134 ALA A CA  
567  C C   . ALA A 77  ? 0.3672 0.4095 0.3565 -0.1149 -0.1205 -0.0224 134 ALA A C   
568  O O   . ALA A 77  ? 0.4132 0.4566 0.3892 -0.1115 -0.1267 -0.0242 134 ALA A O   
569  C CB  . ALA A 77  ? 0.3326 0.4335 0.3727 -0.1432 -0.1337 0.0027  134 ALA A CB  
570  N N   . VAL A 78  ? 0.3682 0.4046 0.3658 -0.0985 -0.1040 -0.0244 135 VAL A N   
571  C CA  . VAL A 78  ? 0.3336 0.3627 0.3245 -0.0782 -0.0936 -0.0293 135 VAL A CA  
572  C C   . VAL A 78  ? 0.3970 0.3879 0.3501 -0.0761 -0.0953 -0.0421 135 VAL A C   
573  O O   . VAL A 78  ? 0.3916 0.3805 0.3337 -0.0662 -0.0949 -0.0441 135 VAL A O   
574  C CB  . VAL A 78  ? 0.3460 0.3762 0.3518 -0.0649 -0.0779 -0.0284 135 VAL A CB  
575  C CG1 . VAL A 78  ? 0.2979 0.3167 0.2943 -0.0480 -0.0688 -0.0339 135 VAL A CG1 
576  C CG2 . VAL A 78  ? 0.3170 0.3819 0.3555 -0.0627 -0.0733 -0.0151 135 VAL A CG2 
577  N N   . ALA A 79  ? 0.4182 0.3769 0.3496 -0.0839 -0.0957 -0.0496 136 ALA A N   
578  C CA  . ALA A 79  ? 0.4586 0.3775 0.3505 -0.0796 -0.0950 -0.0604 136 ALA A CA  
579  C C   . ALA A 79  ? 0.5132 0.4258 0.3819 -0.0886 -0.1087 -0.0630 136 ALA A C   
580  O O   . ALA A 79  ? 0.4911 0.3846 0.3336 -0.0775 -0.1059 -0.0684 136 ALA A O   
581  C CB  . ALA A 79  ? 0.4952 0.3779 0.3660 -0.0867 -0.0924 -0.0665 136 ALA A CB  
582  N N   . GLN A 80  ? 0.5149 0.4470 0.3950 -0.1070 -0.1218 -0.0572 137 GLN A N   
583  C CA  . GLN A 80  ? 0.5621 0.4961 0.4267 -0.1132 -0.1322 -0.0570 137 GLN A CA  
584  C C   . GLN A 80  ? 0.5297 0.4860 0.3991 -0.1012 -0.1343 -0.0533 137 GLN A C   
585  O O   . GLN A 80  ? 0.5776 0.5188 0.4195 -0.0963 -0.1366 -0.0578 137 GLN A O   
586  C CB  . GLN A 80  ? 0.5820 0.5416 0.4668 -0.1333 -0.1442 -0.0478 137 GLN A CB  
587  C CG  . GLN A 80  ? 0.8444 0.7760 0.6980 -0.1473 -0.1526 -0.0531 137 GLN A CG  
588  C CD  . GLN A 80  ? 0.9057 0.8471 0.7462 -0.1483 -0.1631 -0.0521 137 GLN A CD  
589  O OE1 . GLN A 80  ? 1.0189 0.9951 0.8796 -0.1401 -0.1652 -0.0445 137 GLN A OE1 
590  N NE2 . GLN A 80  ? 0.8036 0.7134 0.6086 -0.1583 -0.1697 -0.0589 137 GLN A NE2 
591  N N   . ALA A 81  ? 0.4649 0.4571 0.3721 -0.0911 -0.1274 -0.0436 138 ALA A N   
592  C CA  . ALA A 81  ? 0.4307 0.4453 0.3486 -0.0752 -0.1232 -0.0376 138 ALA A CA  
593  C C   . ALA A 81  ? 0.4042 0.3930 0.3019 -0.0560 -0.1102 -0.0452 138 ALA A C   
594  O O   . ALA A 81  ? 0.5225 0.5206 0.4183 -0.0446 -0.1083 -0.0418 138 ALA A O   
595  C CB  . ALA A 81  ? 0.4391 0.4935 0.4009 -0.0675 -0.1153 -0.0246 138 ALA A CB  
596  N N   . CYS A 82  ? 0.4726 0.4316 0.3567 -0.0517 -0.1009 -0.0533 139 CYS A N   
597  C CA  . CYS A 82  ? 0.5494 0.4875 0.4161 -0.0340 -0.0887 -0.0577 139 CYS A CA  
598  C C   . CYS A 82  ? 0.5604 0.4653 0.3824 -0.0330 -0.0927 -0.0651 139 CYS A C   
599  O O   . CYS A 82  ? 0.6073 0.5024 0.4160 -0.0165 -0.0832 -0.0652 139 CYS A O   
600  C CB  . CYS A 82  ? 0.4181 0.3408 0.2879 -0.0283 -0.0771 -0.0608 139 CYS A CB  
601  S SG  . CYS A 82  ? 0.4496 0.4023 0.3622 -0.0291 -0.0714 -0.0539 139 CYS A SG  
602  N N   . GLY A 83  ? 0.6828 0.5684 0.4792 -0.0506 -0.1062 -0.0707 140 GLY A N   
603  C CA  . GLY A 83  ? 0.6557 0.5085 0.4086 -0.0495 -0.1079 -0.0772 140 GLY A CA  
604  C C   . GLY A 83  ? 0.6278 0.4410 0.3533 -0.0345 -0.0918 -0.0827 140 GLY A C   
605  O O   . GLY A 83  ? 0.6873 0.4829 0.4124 -0.0377 -0.0860 -0.0851 140 GLY A O   
606  N N   A ASN A 84  ? 0.6817 0.4831 0.3855 -0.0166 -0.0835 -0.0826 141 ASN A N   
607  N N   B ASN A 84  ? 0.6819 0.4824 0.3852 -0.0167 -0.0834 -0.0827 141 ASN A N   
608  C CA  A ASN A 84  ? 0.7852 0.5532 0.4639 0.0012  -0.0666 -0.0841 141 ASN A CA  
609  C CA  B ASN A 84  ? 0.7851 0.5522 0.4645 0.0005  -0.0664 -0.0843 141 ASN A CA  
610  C C   A ASN A 84  ? 0.7924 0.5715 0.4903 0.0189  -0.0533 -0.0798 141 ASN A C   
611  C C   B ASN A 84  ? 0.7917 0.5701 0.4912 0.0170  -0.0537 -0.0803 141 ASN A C   
612  O O   A ASN A 84  ? 0.7366 0.4947 0.4200 0.0349  -0.0381 -0.0778 141 ASN A O   
613  O O   B ASN A 84  ? 0.7228 0.4799 0.4106 0.0302  -0.0394 -0.0789 141 ASN A O   
614  C CB  A ASN A 84  ? 0.8722 0.6236 0.5187 0.0130  -0.0627 -0.0837 141 ASN A CB  
615  C CB  B ASN A 84  ? 0.8728 0.6219 0.5197 0.0139  -0.0610 -0.0837 141 ASN A CB  
616  C CG  A ASN A 84  ? 0.8085 0.5869 0.4667 0.0277  -0.0602 -0.0776 141 ASN A CG  
617  C CG  B ASN A 84  ? 0.8955 0.6171 0.5102 0.0005  -0.0693 -0.0892 141 ASN A CG  
618  O OD1 A ASN A 84  ? 0.7779 0.5599 0.4426 0.0475  -0.0452 -0.0722 141 ASN A OD1 
619  O OD1 B ASN A 84  ? 0.8426 0.5488 0.4532 -0.0150 -0.0745 -0.0933 141 ASN A OD1 
620  N ND2 A ASN A 84  ? 0.8334 0.6346 0.4975 0.0182  -0.0744 -0.0761 141 ASN A ND2 
621  N ND2 B ASN A 84  ? 0.8999 0.6142 0.4900 0.0064  -0.0706 -0.0891 141 ASN A ND2 
622  N N   . VAL A 85  ? 0.6393 0.4623 0.3849 0.0160  -0.0553 -0.0726 142 VAL A N   
623  C CA  . VAL A 85  ? 0.5463 0.3912 0.3241 0.0291  -0.0422 -0.0646 142 VAL A CA  
624  C C   . VAL A 85  ? 0.5906 0.4308 0.3802 0.0234  -0.0398 -0.0662 142 VAL A C   
625  O O   . VAL A 85  ? 0.4890 0.3368 0.2915 0.0070  -0.0495 -0.0690 142 VAL A O   
626  C CB  . VAL A 85  ? 0.5390 0.4250 0.3554 0.0282  -0.0448 -0.0573 142 VAL A CB  
627  C CG1 . VAL A 85  ? 0.4200 0.3258 0.2671 0.0371  -0.0340 -0.0499 142 VAL A CG1 
628  C CG2 . VAL A 85  ? 0.5793 0.4694 0.3829 0.0352  -0.0463 -0.0544 142 VAL A CG2 
629  N N   . PRO A 86  ? 0.4397 0.2691 0.2255 0.0368  -0.0268 -0.0629 143 PRO A N   
630  C CA  . PRO A 86  ? 0.4017 0.2256 0.1959 0.0324  -0.0243 -0.0635 143 PRO A CA  
631  C C   . PRO A 86  ? 0.4141 0.2737 0.2501 0.0234  -0.0287 -0.0599 143 PRO A C   
632  O O   . PRO A 86  ? 0.4064 0.2938 0.2668 0.0277  -0.0272 -0.0542 143 PRO A O   
633  C CB  . PRO A 86  ? 0.4913 0.3065 0.2781 0.0523  -0.0086 -0.0563 143 PRO A CB  
634  C CG  . PRO A 86  ? 0.6387 0.4379 0.3974 0.0660  -0.0027 -0.0552 143 PRO A CG  
635  C CD  . PRO A 86  ? 0.5574 0.3766 0.3265 0.0575  -0.0134 -0.0571 143 PRO A CD  
636  N N   . VAL A 87  ? 0.3680 0.2238 0.2096 0.0113  -0.0330 -0.0631 144 VAL A N   
637  C CA  . VAL A 87  ? 0.3074 0.1921 0.1831 0.0034  -0.0361 -0.0600 144 VAL A CA  
638  C C   . VAL A 87  ? 0.4007 0.2778 0.2795 0.0016  -0.0319 -0.0596 144 VAL A C   
639  O O   . VAL A 87  ? 0.4278 0.2767 0.2844 -0.0018 -0.0314 -0.0633 144 VAL A O   
640  C CB  . VAL A 87  ? 0.3285 0.2265 0.2140 -0.0113 -0.0475 -0.0616 144 VAL A CB  
641  C CG1 . VAL A 87  ? 0.3896 0.2631 0.2531 -0.0250 -0.0553 -0.0673 144 VAL A CG1 
642  C CG2 . VAL A 87  ? 0.3121 0.2380 0.2304 -0.0156 -0.0473 -0.0570 144 VAL A CG2 
643  N N   . LEU A 88  ? 0.3189 0.2185 0.2225 0.0035  -0.0288 -0.0549 145 LEU A N   
644  C CA  . LEU A 88  ? 0.3390 0.2368 0.2478 0.0032  -0.0247 -0.0528 145 LEU A CA  
645  C C   . LEU A 88  ? 0.2987 0.2168 0.2304 -0.0060 -0.0281 -0.0520 145 LEU A C   
646  O O   . LEU A 88  ? 0.2836 0.2209 0.2308 -0.0054 -0.0291 -0.0503 145 LEU A O   
647  C CB  . LEU A 88  ? 0.3735 0.2796 0.2867 0.0160  -0.0172 -0.0462 145 LEU A CB  
648  C CG  . LEU A 88  ? 0.5761 0.4706 0.4797 0.0244  -0.0098 -0.0416 145 LEU A CG  
649  C CD1 . LEU A 88  ? 0.5921 0.4520 0.4660 0.0269  -0.0069 -0.0458 145 LEU A CD1 
650  C CD2 . LEU A 88  ? 0.4779 0.3890 0.3891 0.0369  -0.0044 -0.0324 145 LEU A CD2 
651  N N   . PHE A 89  ? 0.2654 0.1773 0.1978 -0.0134 -0.0284 -0.0524 146 PHE A N   
652  C CA  . PHE A 89  ? 0.2379 0.1672 0.1896 -0.0197 -0.0290 -0.0501 146 PHE A CA  
653  C C   . PHE A 89  ? 0.2563 0.1875 0.2114 -0.0154 -0.0232 -0.0472 146 PHE A C   
654  O O   . PHE A 89  ? 0.3014 0.2181 0.2447 -0.0121 -0.0198 -0.0463 146 PHE A O   
655  C CB  . PHE A 89  ? 0.2840 0.2097 0.2372 -0.0325 -0.0338 -0.0501 146 PHE A CB  
656  C CG  . PHE A 89  ? 0.2981 0.2278 0.2503 -0.0396 -0.0421 -0.0514 146 PHE A CG  
657  C CD1 . PHE A 89  ? 0.3234 0.2298 0.2515 -0.0425 -0.0466 -0.0564 146 PHE A CD1 
658  C CD2 . PHE A 89  ? 0.2811 0.2365 0.2535 -0.0422 -0.0450 -0.0469 146 PHE A CD2 
659  C CE1 . PHE A 89  ? 0.3531 0.2632 0.2769 -0.0502 -0.0561 -0.0577 146 PHE A CE1 
660  C CE2 . PHE A 89  ? 0.3428 0.3060 0.3152 -0.0485 -0.0537 -0.0463 146 PHE A CE2 
661  C CZ  . PHE A 89  ? 0.3464 0.2876 0.2942 -0.0534 -0.0603 -0.0520 146 PHE A CZ  
662  N N   . LEU A 90  ? 0.2416 0.1885 0.2097 -0.0150 -0.0217 -0.0454 147 LEU A N   
663  C CA  . LEU A 90  ? 0.2149 0.1635 0.1827 -0.0123 -0.0177 -0.0431 147 LEU A CA  
664  C C   . LEU A 90  ? 0.3023 0.2532 0.2755 -0.0165 -0.0146 -0.0412 147 LEU A C   
665  O O   . LEU A 90  ? 0.3337 0.2842 0.3031 -0.0143 -0.0113 -0.0395 147 LEU A O   
666  C CB  . LEU A 90  ? 0.2829 0.2414 0.2540 -0.0089 -0.0179 -0.0428 147 LEU A CB  
667  C CG  . LEU A 90  ? 0.2705 0.2322 0.2406 -0.0043 -0.0199 -0.0420 147 LEU A CG  
668  C CD1 . LEU A 90  ? 0.2512 0.2222 0.2248 -0.0047 -0.0209 -0.0402 147 LEU A CD1 
669  C CD2 . LEU A 90  ? 0.2534 0.2075 0.2143 0.0018  -0.0184 -0.0392 147 LEU A CD2 
670  N N   . ASP A 91  ? 0.2831 0.2385 0.2651 -0.0225 -0.0156 -0.0400 148 ASP A N   
671  C CA  . ASP A 91  ? 0.3196 0.2817 0.3101 -0.0248 -0.0107 -0.0352 148 ASP A CA  
672  C C   . ASP A 91  ? 0.3000 0.2678 0.3012 -0.0342 -0.0136 -0.0311 148 ASP A C   
673  O O   . ASP A 91  ? 0.2936 0.2784 0.3096 -0.0355 -0.0132 -0.0262 148 ASP A O   
674  C CB  . ASP A 91  ? 0.3341 0.3063 0.3303 -0.0195 -0.0063 -0.0341 148 ASP A CB  
675  C CG  . ASP A 91  ? 0.4028 0.3758 0.3990 -0.0168 0.0023  -0.0295 148 ASP A CG  
676  O OD1 . ASP A 91  ? 0.4330 0.4011 0.4265 -0.0192 0.0042  -0.0269 148 ASP A OD1 
677  O OD2 . ASP A 91  ? 0.3672 0.3433 0.3642 -0.0112 0.0084  -0.0278 148 ASP A OD2 
678  N N   . VAL A 92  ? 0.3413 0.2949 0.3347 -0.0412 -0.0163 -0.0317 149 VAL A N   
679  C CA  . VAL A 92  ? 0.3090 0.2646 0.3093 -0.0546 -0.0222 -0.0283 149 VAL A CA  
680  C C   . VAL A 92  ? 0.3453 0.2870 0.3411 -0.0611 -0.0189 -0.0249 149 VAL A C   
681  O O   . VAL A 92  ? 0.3597 0.2819 0.3394 -0.0551 -0.0146 -0.0278 149 VAL A O   
682  C CB  . VAL A 92  ? 0.3304 0.2735 0.3176 -0.0599 -0.0314 -0.0347 149 VAL A CB  
683  C CG1 . VAL A 92  ? 0.3965 0.3363 0.3848 -0.0775 -0.0399 -0.0322 149 VAL A CG1 
684  C CG2 . VAL A 92  ? 0.4073 0.3666 0.4013 -0.0541 -0.0344 -0.0360 149 VAL A CG2 
685  N N   . SER A 93  ? 0.2761 0.2298 0.2874 -0.0730 -0.0204 -0.0167 150 SER A N   
686  C CA  . SER A 93  ? 0.3393 0.2773 0.3462 -0.0822 -0.0182 -0.0128 150 SER A CA  
687  C C   . SER A 93  ? 0.4671 0.4071 0.4809 -0.1031 -0.0287 -0.0089 150 SER A C   
688  O O   . SER A 93  ? 0.4250 0.3952 0.4612 -0.1090 -0.0335 -0.0016 150 SER A O   
689  C CB  . SER A 93  ? 0.4684 0.4191 0.4878 -0.0765 -0.0070 -0.0033 150 SER A CB  
690  O OG  . SER A 93  ? 0.4983 0.4320 0.5123 -0.0846 -0.0039 0.0011  150 SER A OG  
691  N N   . PRO A 94  ? 0.5208 0.4286 0.5145 -0.1151 -0.0327 -0.0128 151 PRO A N   
692  C CA  . PRO A 94  ? 0.4895 0.3590 0.4542 -0.1068 -0.0264 -0.0200 151 PRO A CA  
693  C C   . PRO A 94  ? 0.5006 0.3605 0.4481 -0.0918 -0.0266 -0.0300 151 PRO A C   
694  O O   . PRO A 94  ? 0.4611 0.3307 0.4101 -0.0943 -0.0347 -0.0339 151 PRO A O   
695  C CB  . PRO A 94  ? 0.5459 0.3826 0.4922 -0.1270 -0.0333 -0.0218 151 PRO A CB  
696  C CG  . PRO A 94  ? 0.6542 0.5187 0.6283 -0.1466 -0.0399 -0.0106 151 PRO A CG  
697  C CD  . PRO A 94  ? 0.6205 0.5287 0.6208 -0.1396 -0.0429 -0.0070 151 PRO A CD  
698  N N   . ALA A 95  ? 0.4343 0.2792 0.3674 -0.0760 -0.0177 -0.0322 152 ALA A N   
699  C CA  . ALA A 95  ? 0.4058 0.2471 0.3268 -0.0617 -0.0171 -0.0384 152 ALA A CA  
700  C C   . ALA A 95  ? 0.5541 0.3646 0.4493 -0.0671 -0.0225 -0.0457 152 ALA A C   
701  O O   . ALA A 95  ? 0.5037 0.2786 0.3758 -0.0710 -0.0195 -0.0470 152 ALA A O   
702  C CB  . ALA A 95  ? 0.4280 0.2628 0.3407 -0.0451 -0.0072 -0.0360 152 ALA A CB  
703  N N   . PRO A 96  ? 0.4816 0.3007 0.3762 -0.0673 -0.0296 -0.0504 153 PRO A N   
704  C CA  . PRO A 96  ? 0.4986 0.2855 0.3634 -0.0725 -0.0348 -0.0578 153 PRO A CA  
705  C C   . PRO A 96  ? 0.5139 0.2750 0.3529 -0.0534 -0.0251 -0.0606 153 PRO A C   
706  O O   . PRO A 96  ? 0.4594 0.2349 0.3080 -0.0370 -0.0166 -0.0561 153 PRO A O   
707  C CB  . PRO A 96  ? 0.6061 0.4187 0.4834 -0.0775 -0.0451 -0.0595 153 PRO A CB  
708  C CG  . PRO A 96  ? 0.4748 0.3234 0.3793 -0.0641 -0.0400 -0.0550 153 PRO A CG  
709  C CD  . PRO A 96  ? 0.4935 0.3499 0.4124 -0.0633 -0.0328 -0.0488 153 PRO A CD  
710  N N   . VAL A 97  ? 0.5054 0.2269 0.3093 -0.0559 -0.0263 -0.0672 154 VAL A N   
711  C CA  . VAL A 97  ? 0.5725 0.2686 0.3494 -0.0356 -0.0156 -0.0684 154 VAL A CA  
712  C C   . VAL A 97  ? 0.5815 0.3120 0.3766 -0.0209 -0.0146 -0.0659 154 VAL A C   
713  O O   . VAL A 97  ? 0.4915 0.2500 0.3054 -0.0284 -0.0240 -0.0675 154 VAL A O   
714  C CB  . VAL A 97  ? 0.6334 0.2978 0.3791 -0.0403 -0.0170 -0.0723 154 VAL A CB  
715  C CG1 . VAL A 97  ? 0.7203 0.3628 0.4396 -0.0180 -0.0047 -0.0709 154 VAL A CG1 
716  C CG2 . VAL A 97  ? 0.6071 0.2453 0.3413 -0.0532 -0.0162 -0.0712 154 VAL A CG2 
717  N N   . ASN A 98  ? 0.5735 0.3049 0.3661 -0.0001 -0.0027 -0.0600 155 ASN A N   
718  C CA  . ASN A 98  ? 0.6193 0.3803 0.4273 0.0142  -0.0002 -0.0555 155 ASN A CA  
719  C C   . ASN A 98  ? 0.7428 0.5478 0.5885 0.0129  -0.0030 -0.0500 155 ASN A C   
720  O O   . ASN A 98  ? 0.7372 0.5635 0.5950 0.0254  0.0015  -0.0431 155 ASN A O   
721  C CB  . ASN A 98  ? 0.7285 0.4904 0.5291 0.0108  -0.0074 -0.0615 155 ASN A CB  
722  C CG  . ASN A 98  ? 0.5589 0.2769 0.3164 0.0194  -0.0015 -0.0657 155 ASN A CG  
723  O OD1 . ASN A 98  ? 0.7139 0.4066 0.4507 0.0346  0.0115  -0.0615 155 ASN A OD1 
724  N ND2 . ASN A 98  ? 0.7042 0.4139 0.4472 0.0108  -0.0101 -0.0726 155 ASN A ND2 
725  N N   . SER A 99  ? 0.4166 0.2342 0.2793 -0.0021 -0.0098 -0.0518 156 SER A N   
726  C CA  . SER A 99  ? 0.3650 0.2173 0.2567 -0.0034 -0.0115 -0.0478 156 SER A CA  
727  C C   . SER A 99  ? 0.3477 0.2093 0.2440 0.0086  -0.0043 -0.0402 156 SER A C   
728  O O   . SER A 99  ? 0.3854 0.2278 0.2660 0.0174  0.0030  -0.0362 156 SER A O   
729  C CB  . SER A 99  ? 0.3602 0.2187 0.2645 -0.0180 -0.0158 -0.0485 156 SER A CB  
730  O OG  . SER A 99  ? 0.4279 0.2670 0.3227 -0.0202 -0.0111 -0.0462 156 SER A OG  
731  N N   . VAL A 100 ? 0.2972 0.1874 0.2133 0.0088  -0.0067 -0.0374 157 VAL A N   
732  C CA  . VAL A 100 ? 0.2996 0.2044 0.2220 0.0159  -0.0036 -0.0299 157 VAL A CA  
733  C C   . VAL A 100 ? 0.2725 0.1919 0.2077 0.0071  -0.0071 -0.0314 157 VAL A C   
734  O O   . VAL A 100 ? 0.2823 0.2141 0.2278 0.0020  -0.0113 -0.0349 157 VAL A O   
735  C CB  . VAL A 100 ? 0.2951 0.2182 0.2240 0.0244  -0.0037 -0.0244 157 VAL A CB  
736  C CG1 . VAL A 100 ? 0.3058 0.2477 0.2419 0.0285  -0.0034 -0.0152 157 VAL A CG1 
737  C CG2 . VAL A 100 ? 0.3607 0.2684 0.2751 0.0358  0.0022  -0.0219 157 VAL A CG2 
738  N N   A LEU A 101 ? 0.2829 0.1980 0.2152 0.0067  -0.0039 -0.0281 158 LEU A N   
739  N N   B LEU A 101 ? 0.2803 0.1966 0.2129 0.0071  -0.0040 -0.0278 158 LEU A N   
740  C CA  A LEU A 101 ? 0.3062 0.2296 0.2457 0.0000  -0.0047 -0.0290 158 LEU A CA  
741  C CA  B LEU A 101 ? 0.2991 0.2248 0.2394 0.0003  -0.0052 -0.0291 158 LEU A CA  
742  C C   A LEU A 101 ? 0.2606 0.1894 0.1958 0.0047  -0.0023 -0.0227 158 LEU A C   
743  C C   B LEU A 101 ? 0.2580 0.1856 0.1932 0.0042  -0.0020 -0.0230 158 LEU A C   
744  O O   A LEU A 101 ? 0.2777 0.2018 0.2056 0.0126  0.0009  -0.0165 158 LEU A O   
745  O O   B LEU A 101 ? 0.2709 0.1893 0.1978 0.0109  0.0022  -0.0174 158 LEU A O   
746  C CB  A LEU A 101 ? 0.3351 0.2470 0.2756 -0.0081 -0.0030 -0.0308 158 LEU A CB  
747  C CB  B LEU A 101 ? 0.3619 0.2800 0.3062 -0.0086 -0.0049 -0.0324 158 LEU A CB  
748  C CG  A LEU A 101 ? 0.4148 0.3304 0.3647 -0.0169 -0.0071 -0.0351 158 LEU A CG  
749  C CG  B LEU A 101 ? 0.3433 0.2425 0.2795 -0.0113 -0.0009 -0.0300 158 LEU A CG  
750  C CD1 A LEU A 101 ? 0.4132 0.3187 0.3559 -0.0171 -0.0108 -0.0390 158 LEU A CD1 
751  C CD1 B LEU A 101 ? 0.4421 0.3445 0.3887 -0.0218 -0.0009 -0.0294 158 LEU A CD1 
752  C CD2 A LEU A 101 ? 0.4536 0.3649 0.4083 -0.0260 -0.0054 -0.0325 158 LEU A CD2 
753  C CD2 B LEU A 101 ? 0.4693 0.3472 0.3922 -0.0106 -0.0014 -0.0326 158 LEU A CD2 
754  N N   . PHE A 102 ? 0.2820 0.2195 0.2193 0.0009  -0.0034 -0.0236 159 PHE A N   
755  C CA  . PHE A 102 ? 0.3179 0.2568 0.2474 0.0036  -0.0010 -0.0182 159 PHE A CA  
756  C C   . PHE A 102 ? 0.3536 0.2789 0.2810 0.0026  0.0057  -0.0161 159 PHE A C   
757  O O   . PHE A 102 ? 0.3902 0.3109 0.3248 -0.0037 0.0071  -0.0194 159 PHE A O   
758  C CB  . PHE A 102 ? 0.3032 0.2495 0.2290 -0.0002 -0.0037 -0.0209 159 PHE A CB  
759  C CG  . PHE A 102 ? 0.3288 0.2862 0.2550 -0.0023 -0.0113 -0.0223 159 PHE A CG  
760  C CD1 . PHE A 102 ? 0.3227 0.2923 0.2468 0.0004  -0.0161 -0.0152 159 PHE A CD1 
761  C CD2 . PHE A 102 ? 0.3009 0.2580 0.2305 -0.0072 -0.0133 -0.0289 159 PHE A CD2 
762  C CE1 . PHE A 102 ? 0.2816 0.2641 0.2086 -0.0042 -0.0240 -0.0147 159 PHE A CE1 
763  C CE2 . PHE A 102 ? 0.3406 0.3057 0.2701 -0.0111 -0.0203 -0.0297 159 PHE A CE2 
764  C CZ  . PHE A 102 ? 0.2819 0.2603 0.2110 -0.0107 -0.0262 -0.0226 159 PHE A CZ  
765  N N   . ASP A 103 ? 0.3743 0.2947 0.2932 0.0084  0.0098  -0.0089 160 ASP A N   
766  C CA  . ASP A 103 ? 0.4060 0.3127 0.3221 0.0071  0.0170  -0.0052 160 ASP A CA  
767  C C   . ASP A 103 ? 0.4608 0.3728 0.3826 0.0011  0.0191  -0.0070 160 ASP A C   
768  O O   . ASP A 103 ? 0.4639 0.3845 0.3797 0.0034  0.0186  -0.0069 160 ASP A O   
769  C CB  . ASP A 103 ? 0.4228 0.3274 0.3280 0.0160  0.0215  0.0042  160 ASP A CB  
770  C CG  . ASP A 103 ? 0.4824 0.3689 0.3836 0.0152  0.0303  0.0093  160 ASP A CG  
771  O OD1 . ASP A 103 ? 0.4625 0.3478 0.3702 0.0074  0.0328  0.0080  160 ASP A OD1 
772  O OD2 . ASP A 103 ? 0.5431 0.4169 0.4350 0.0230  0.0356  0.0163  160 ASP A OD2 
773  N N   . PRO A 104 ? 0.5150 0.4219 0.4466 -0.0064 0.0215  -0.0077 161 PRO A N   
774  C CA  . PRO A 104 ? 0.4240 0.3409 0.3645 -0.0098 0.0245  -0.0072 161 PRO A CA  
775  C C   . PRO A 104 ? 0.4598 0.3753 0.3957 -0.0068 0.0335  0.0006  161 PRO A C   
776  O O   . PRO A 104 ? 0.4513 0.3747 0.3899 -0.0054 0.0384  0.0021  161 PRO A O   
777  C CB  . PRO A 104 ? 0.5678 0.4852 0.5236 -0.0198 0.0223  -0.0079 161 PRO A CB  
778  C CG  . PRO A 104 ? 0.5673 0.4655 0.5162 -0.0233 0.0220  -0.0066 161 PRO A CG  
779  C CD  . PRO A 104 ? 0.6283 0.5195 0.5617 -0.0127 0.0216  -0.0077 161 PRO A CD  
780  N N   . HIS A 105 ? 0.3445 0.2490 0.2721 -0.0042 0.0374  0.0065  162 HIS A N   
781  C CA  . HIS A 105 ? 0.3172 0.2202 0.2393 -0.0004 0.0468  0.0152  162 HIS A CA  
782  C C   . HIS A 105 ? 0.3272 0.2293 0.2299 0.0096  0.0475  0.0181  162 HIS A C   
783  O O   . HIS A 105 ? 0.3396 0.2417 0.2334 0.0142  0.0547  0.0241  162 HIS A O   
784  C CB  . HIS A 105 ? 0.4533 0.3438 0.3818 -0.0064 0.0526  0.0228  162 HIS A CB  
785  C CG  . HIS A 105 ? 0.5566 0.4506 0.5046 -0.0194 0.0509  0.0229  162 HIS A CG  
786  N ND1 . HIS A 105 ? 0.6031 0.4887 0.5547 -0.0283 0.0428  0.0167  162 HIS A ND1 
787  C CD2 . HIS A 105 ? 0.5759 0.4833 0.5408 -0.0250 0.0559  0.0300  162 HIS A CD2 
788  C CE1 . HIS A 105 ? 0.7636 0.6580 0.7334 -0.0408 0.0409  0.0195  162 HIS A CE1 
789  N NE2 . HIS A 105 ? 0.6015 0.5115 0.5822 -0.0388 0.0490  0.0286  162 HIS A NE2 
790  N N   A GLU A 106 ? 0.3119 0.1969 0.2390 0.0317  0.0485  -0.0529 163 GLU A N   
791  N N   B GLU A 106 ? 0.3119 0.1966 0.2388 0.0318  0.0485  -0.0530 163 GLU A N   
792  C CA  A GLU A 106 ? 0.2984 0.2061 0.2514 0.0441  0.0557  -0.0441 163 GLU A CA  
793  C CA  B GLU A 106 ? 0.2979 0.2054 0.2510 0.0440  0.0556  -0.0441 163 GLU A CA  
794  C C   A GLU A 106 ? 0.2391 0.1853 0.2282 0.0285  0.0528  -0.0305 163 GLU A C   
795  C C   B GLU A 106 ? 0.2388 0.1846 0.2278 0.0283  0.0526  -0.0305 163 GLU A C   
796  O O   A GLU A 106 ? 0.2237 0.1754 0.2319 0.0278  0.0490  -0.0241 163 GLU A O   
797  O O   B GLU A 106 ? 0.2243 0.1754 0.2324 0.0273  0.0486  -0.0242 163 GLU A O   
798  C CB  A GLU A 106 ? 0.2990 0.2276 0.2466 0.0703  0.0728  -0.0441 163 GLU A CB  
799  C CB  B GLU A 106 ? 0.2982 0.2266 0.2462 0.0703  0.0727  -0.0440 163 GLU A CB  
800  C CG  A GLU A 106 ? 0.4152 0.3129 0.3439 0.0939  0.0741  -0.0518 163 GLU A CG  
801  C CG  B GLU A 106 ? 0.2399 0.2016 0.2203 0.0831  0.0784  -0.0324 163 GLU A CG  
802  C CD  A GLU A 106 ? 0.3970 0.2814 0.3425 0.0926  0.0655  -0.0465 163 GLU A CD  
803  C CD  B GLU A 106 ? 0.2887 0.2855 0.2730 0.1070  0.0937  -0.0285 163 GLU A CD  
804  O OE1 A GLU A 106 ? 0.4353 0.3580 0.4133 0.0982  0.0705  -0.0342 163 GLU A OE1 
805  O OE1 B GLU A 106 ? 0.3270 0.3414 0.3009 0.1067  0.1023  -0.0287 163 GLU A OE1 
806  O OE2 A GLU A 106 ? 0.4923 0.3326 0.4204 0.0835  0.0520  -0.0524 163 GLU A OE2 
807  O OE2 B GLU A 106 ? 0.3276 0.3362 0.3266 0.1218  0.0937  -0.0236 163 GLU A OE2 
808  N N   . GLY A 107 ? 0.2007 0.1681 0.1943 0.0163  0.0531  -0.0261 164 GLY A N   
809  C CA  . GLY A 107 ? 0.1755 0.1672 0.1948 0.0017  0.0477  -0.0152 164 GLY A CA  
810  C C   . GLY A 107 ? 0.1789 0.1535 0.2027 -0.0094 0.0361  -0.0160 164 GLY A C   
811  O O   . GLY A 107 ? 0.1611 0.1464 0.2018 -0.0127 0.0323  -0.0094 164 GLY A O   
812  N N   . ALA A 108 ? 0.1830 0.1333 0.1911 -0.0155 0.0299  -0.0230 165 ALA A N   
813  C CA  . ALA A 108 ? 0.2054 0.1477 0.2207 -0.0256 0.0213  -0.0211 165 ALA A CA  
814  C C   . ALA A 108 ? 0.1990 0.1303 0.2193 -0.0202 0.0215  -0.0189 165 ALA A C   
815  O O   . ALA A 108 ? 0.1864 0.1250 0.2186 -0.0245 0.0186  -0.0124 165 ALA A O   
816  C CB  . ALA A 108 ? 0.2164 0.1417 0.2181 -0.0351 0.0135  -0.0267 165 ALA A CB  
817  N N   . ARG A 109 ? 0.2089 0.1191 0.2154 -0.0088 0.0247  -0.0244 166 ARG A N   
818  C CA  . ARG A 109 ? 0.2048 0.0986 0.2122 -0.0015 0.0240  -0.0211 166 ARG A CA  
819  C C   . ARG A 109 ? 0.2176 0.1403 0.2455 0.0067  0.0274  -0.0122 166 ARG A C   
820  O O   . ARG A 109 ? 0.2112 0.1325 0.2460 0.0045  0.0234  -0.0052 166 ARG A O   
821  C CB  . ARG A 109 ? 0.2413 0.1005 0.2243 0.0137  0.0263  -0.0299 166 ARG A CB  
822  C CG  . ARG A 109 ? 0.3241 0.1644 0.3060 0.0267  0.0260  -0.0253 166 ARG A CG  
823  C CD  . ARG A 109 ? 0.3533 0.1629 0.3098 0.0421  0.0247  -0.0347 166 ARG A CD  
824  N NE  . ARG A 109 ? 0.5389 0.3676 0.4955 0.0685  0.0379  -0.0370 166 ARG A NE  
825  C CZ  . ARG A 109 ? 0.5789 0.4338 0.5554 0.0858  0.0440  -0.0281 166 ARG A CZ  
826  N NH1 . ARG A 109 ? 0.5530 0.4073 0.5434 0.0817  0.0377  -0.0178 166 ARG A NH1 
827  N NH2 . ARG A 109 ? 0.7859 0.6740 0.7698 0.1063  0.0555  -0.0276 166 ARG A NH2 
828  N N   . LEU A 110 ? 0.1773 0.1287 0.2151 0.0140  0.0337  -0.0107 167 LEU A N   
829  C CA  . LEU A 110 ? 0.1707 0.1529 0.2302 0.0182  0.0334  -0.0010 167 LEU A CA  
830  C C   . LEU A 110 ? 0.1713 0.1609 0.2387 0.0027  0.0248  0.0040  167 LEU A C   
831  O O   . LEU A 110 ? 0.1668 0.1641 0.2423 0.0044  0.0197  0.0105  167 LEU A O   
832  C CB  . LEU A 110 ? 0.1612 0.1793 0.2336 0.0235  0.0411  0.0029  167 LEU A CB  
833  C CG  . LEU A 110 ? 0.1537 0.1737 0.2190 0.0463  0.0530  -0.0006 167 LEU A CG  
834  C CD1 . LEU A 110 ? 0.1999 0.2633 0.2788 0.0469  0.0628  0.0061  167 LEU A CD1 
835  C CD2 . LEU A 110 ? 0.2698 0.2893 0.3421 0.0662  0.0530  0.0035  167 LEU A CD2 
836  N N   . GLY A 111 ? 0.1529 0.1389 0.2146 -0.0098 0.0227  0.0009  168 GLY A N   
837  C CA  . GLY A 111 ? 0.1356 0.1246 0.1990 -0.0193 0.0156  0.0041  168 GLY A CA  
838  C C   . GLY A 111 ? 0.1497 0.1246 0.2075 -0.0193 0.0132  0.0057  168 GLY A C   
839  O O   . GLY A 111 ? 0.1708 0.1493 0.2283 -0.0188 0.0087  0.0102  168 GLY A O   
840  N N   . VAL A 112 ? 0.1507 0.1091 0.2019 -0.0211 0.0153  0.0033  169 VAL A N   
841  C CA  . VAL A 112 ? 0.1501 0.0992 0.1967 -0.0235 0.0138  0.0086  169 VAL A CA  
842  C C   . VAL A 112 ? 0.2125 0.1541 0.2594 -0.0148 0.0134  0.0144  169 VAL A C   
843  O O   . VAL A 112 ? 0.1899 0.1340 0.2342 -0.0145 0.0116  0.0215  169 VAL A O   
844  C CB  . VAL A 112 ? 0.1840 0.1214 0.2196 -0.0300 0.0113  0.0069  169 VAL A CB  
845  C CG1 . VAL A 112 ? 0.2078 0.1365 0.2387 -0.0347 0.0103  0.0153  169 VAL A CG1 
846  C CG2 . VAL A 112 ? 0.1974 0.1496 0.2316 -0.0365 0.0085  0.0050  169 VAL A CG2 
847  N N   . GLU A 113 ? 0.1756 0.1092 0.2223 -0.0046 0.0151  0.0119  170 GLU A N   
848  C CA  . GLU A 113 ? 0.1994 0.1267 0.2456 0.0078  0.0135  0.0185  170 GLU A CA  
849  C C   . GLU A 113 ? 0.1813 0.1351 0.2374 0.0102  0.0086  0.0246  170 GLU A C   
850  O O   . GLU A 113 ? 0.1924 0.1418 0.2440 0.0145  0.0043  0.0326  170 GLU A O   
851  C CB  . GLU A 113 ? 0.2107 0.1295 0.2550 0.0242  0.0175  0.0140  170 GLU A CB  
852  C CG  . GLU A 113 ? 0.2504 0.1273 0.2744 0.0238  0.0181  0.0078  170 GLU A CG  
853  C CD  . GLU A 113 ? 0.3806 0.2258 0.3921 0.0199  0.0124  0.0156  170 GLU A CD  
854  O OE1 . GLU A 113 ? 0.4228 0.2662 0.4353 0.0323  0.0108  0.0243  170 GLU A OE1 
855  O OE2 . GLU A 113 ? 0.4478 0.2781 0.4482 0.0031  0.0059  0.0142  170 GLU A OE2 
856  N N   . HIS A 114 ? 0.1402 0.1183 0.2069 0.0059  0.0075  0.0219  171 HIS A N   
857  C CA  . HIS A 114 ? 0.1118 0.1105 0.1852 0.0039  -0.0013 0.0273  171 HIS A CA  
858  C C   . HIS A 114 ? 0.1505 0.1377 0.2075 -0.0023 -0.0064 0.0285  171 HIS A C   
859  O O   . HIS A 114 ? 0.1642 0.1529 0.2151 0.0012  -0.0139 0.0344  171 HIS A O   
860  C CB  . HIS A 114 ? 0.1472 0.1681 0.2327 -0.0043 -0.0030 0.0255  171 HIS A CB  
861  C CG  . HIS A 114 ? 0.1431 0.1779 0.2315 -0.0128 -0.0161 0.0300  171 HIS A CG  
862  N ND1 . HIS A 114 ? 0.1588 0.2147 0.2599 -0.0085 -0.0248 0.0384  171 HIS A ND1 
863  C CD2 . HIS A 114 ? 0.1243 0.1513 0.2016 -0.0255 -0.0243 0.0271  171 HIS A CD2 
864  C CE1 . HIS A 114 ? 0.1586 0.2191 0.2563 -0.0215 -0.0394 0.0402  171 HIS A CE1 
865  N NE2 . HIS A 114 ? 0.1381 0.1769 0.2185 -0.0313 -0.0392 0.0326  171 HIS A NE2 
866  N N   . LEU A 115 ? 0.1678 0.1456 0.2158 -0.0094 -0.0022 0.0235  172 LEU A N   
867  C CA  . LEU A 115 ? 0.1556 0.1269 0.1865 -0.0107 -0.0038 0.0247  172 LEU A CA  
868  C C   . LEU A 115 ? 0.1769 0.1391 0.1991 -0.0066 -0.0004 0.0332  172 LEU A C   
869  O O   . LEU A 115 ? 0.1942 0.1547 0.2001 -0.0031 -0.0036 0.0376  172 LEU A O   
870  C CB  . LEU A 115 ? 0.1999 0.1698 0.2273 -0.0151 0.0014  0.0193  172 LEU A CB  
871  C CG  . LEU A 115 ? 0.1769 0.1492 0.2057 -0.0193 -0.0037 0.0130  172 LEU A CG  
872  C CD1 . LEU A 115 ? 0.2154 0.1860 0.2412 -0.0201 0.0015  0.0093  172 LEU A CD1 
873  C CD2 . LEU A 115 ? 0.1860 0.1524 0.1997 -0.0196 -0.0150 0.0118  172 LEU A CD2 
874  N N   . VAL A 116 ? 0.1746 0.1265 0.2028 -0.0075 0.0051  0.0360  173 VAL A N   
875  C CA  . VAL A 116 ? 0.2276 0.1656 0.2463 -0.0065 0.0070  0.0469  173 VAL A CA  
876  C C   . VAL A 116 ? 0.2007 0.1360 0.2148 0.0043  -0.0002 0.0532  173 VAL A C   
877  O O   . VAL A 116 ? 0.2383 0.1684 0.2371 0.0067  -0.0017 0.0631  173 VAL A O   
878  C CB  . VAL A 116 ? 0.2291 0.1474 0.2514 -0.0128 0.0107  0.0479  173 VAL A CB  
879  C CG1 . VAL A 116 ? 0.2628 0.1589 0.2736 -0.0135 0.0104  0.0612  173 VAL A CG1 
880  C CG2 . VAL A 116 ? 0.2389 0.1659 0.2664 -0.0257 0.0153  0.0452  173 VAL A CG2 
881  N N   . ALA A 117 ? 0.2010 0.1446 0.2285 0.0120  -0.0047 0.0493  174 ALA A N   
882  C CA  . ALA A 117 ? 0.2245 0.1743 0.2532 0.0238  -0.0132 0.0568  174 ALA A CA  
883  C C   . ALA A 117 ? 0.1997 0.1618 0.2169 0.0213  -0.0231 0.0594  174 ALA A C   
884  O O   . ALA A 117 ? 0.2536 0.2147 0.2617 0.0290  -0.0311 0.0687  174 ALA A O   
885  C CB  . ALA A 117 ? 0.2071 0.1765 0.2580 0.0329  -0.0146 0.0535  174 ALA A CB  
886  N N   . LEU A 118 ? 0.1994 0.1691 0.2131 0.0119  -0.0243 0.0510  175 LEU A N   
887  C CA  . LEU A 118 ? 0.1979 0.1686 0.1912 0.0097  -0.0349 0.0499  175 LEU A CA  
888  C C   . LEU A 118 ? 0.2438 0.1997 0.2082 0.0123  -0.0286 0.0537  175 LEU A C   
889  O O   . LEU A 118 ? 0.2871 0.2382 0.2251 0.0148  -0.0368 0.0531  175 LEU A O   
890  C CB  . LEU A 118 ? 0.1978 0.1720 0.1920 0.0003  -0.0388 0.0391  175 LEU A CB  
891  C CG  . LEU A 118 ? 0.2203 0.2145 0.2390 -0.0063 -0.0483 0.0383  175 LEU A CG  
892  C CD1 . LEU A 118 ? 0.1986 0.1861 0.2127 -0.0172 -0.0498 0.0292  175 LEU A CD1 
893  C CD2 . LEU A 118 ? 0.2957 0.3020 0.3134 -0.0069 -0.0666 0.0446  175 LEU A CD2 
894  N N   . GLY A 119 ? 0.2288 0.1779 0.1959 0.0113  -0.0147 0.0586  176 GLY A N   
895  C CA  . GLY A 119 ? 0.2405 0.1843 0.1855 0.0125  -0.0060 0.0669  176 GLY A CA  
896  C C   . GLY A 119 ? 0.2505 0.2020 0.1937 0.0092  0.0059  0.0623  176 GLY A C   
897  O O   . GLY A 119 ? 0.2570 0.2128 0.1839 0.0117  0.0157  0.0709  176 GLY A O   
898  N N   . HIS A 120 ? 0.2075 0.1642 0.1673 0.0050  0.0061  0.0511  177 HIS A N   
899  C CA  . HIS A 120 ? 0.1946 0.1613 0.1546 0.0048  0.0161  0.0476  177 HIS A CA  
900  C C   . HIS A 120 ? 0.2365 0.2129 0.2128 -0.0037 0.0273  0.0582  177 HIS A C   
901  O O   . HIS A 120 ? 0.2444 0.2120 0.2367 -0.0125 0.0253  0.0610  177 HIS A O   
902  C CB  . HIS A 120 ? 0.1916 0.1584 0.1637 0.0020  0.0113  0.0348  177 HIS A CB  
903  C CG  . HIS A 120 ? 0.1809 0.1365 0.1348 0.0061  -0.0010 0.0258  177 HIS A CG  
904  N ND1 . HIS A 120 ? 0.2179 0.1644 0.1437 0.0156  -0.0014 0.0195  177 HIS A ND1 
905  C CD2 . HIS A 120 ? 0.2295 0.1807 0.1877 0.0014  -0.0146 0.0229  177 HIS A CD2 
906  C CE1 . HIS A 120 ? 0.2613 0.1906 0.1713 0.0138  -0.0172 0.0119  177 HIS A CE1 
907  N NE2 . HIS A 120 ? 0.2679 0.2043 0.2005 0.0035  -0.0256 0.0152  177 HIS A NE2 
908  N N   . GLN A 121 ? 0.2288 0.2233 0.1999 -0.0008 0.0386  0.0643  178 GLN A N   
909  C CA  . GLN A 121 ? 0.2370 0.2499 0.2280 -0.0125 0.0482  0.0765  178 GLN A CA  
910  C C   . GLN A 121 ? 0.2676 0.3066 0.2712 -0.0093 0.0546  0.0725  178 GLN A C   
911  O O   . GLN A 121 ? 0.2955 0.3511 0.3222 -0.0221 0.0565  0.0783  178 GLN A O   
912  C CB  . GLN A 121 ? 0.2857 0.3090 0.2655 -0.0136 0.0578  0.0947  178 GLN A CB  
913  C CG  . GLN A 121 ? 0.3372 0.3335 0.3044 -0.0168 0.0507  0.1016  178 GLN A CG  
914  C CD  . GLN A 121 ? 0.7897 0.7912 0.7331 -0.0113 0.0568  0.1128  178 GLN A CD  
915  O OE1 . GLN A 121 ? 0.5719 0.5990 0.5094 -0.0047 0.0677  0.1149  178 GLN A OE1 
916  N NE2 . GLN A 121 ? 0.8311 0.8085 0.7601 -0.0120 0.0496  0.1196  178 GLN A NE2 
917  N N   . ARG A 122 ? 0.2110 0.2500 0.1974 0.0078  0.0546  0.0611  179 ARG A N   
918  C CA  . ARG A 122 ? 0.1795 0.2414 0.1727 0.0176  0.0610  0.0579  179 ARG A CA  
919  C C   . ARG A 122 ? 0.1946 0.2360 0.1899 0.0175  0.0489  0.0418  179 ARG A C   
920  O O   . ARG A 122 ? 0.2298 0.2503 0.2010 0.0299  0.0430  0.0303  179 ARG A O   
921  C CB  . ARG A 122 ? 0.2207 0.2911 0.1840 0.0416  0.0712  0.0578  179 ARG A CB  
922  C CG  . ARG A 122 ? 0.2673 0.3638 0.2327 0.0404  0.0833  0.0745  179 ARG A CG  
923  C CD  . ARG A 122 ? 0.3345 0.4415 0.2761 0.0653  0.0914  0.0714  179 ARG A CD  
924  N NE  . ARG A 122 ? 0.4999 0.6224 0.4383 0.0626  0.0993  0.0850  179 ARG A NE  
925  C CZ  . ARG A 122 ? 0.6544 0.7911 0.5748 0.0818  0.1087  0.0870  179 ARG A CZ  
926  N NH1 . ARG A 122 ? 0.6300 0.7644 0.5335 0.1065  0.1104  0.0760  179 ARG A NH1 
927  N NH2 . ARG A 122 ? 0.5951 0.7458 0.5126 0.0767  0.1165  0.1010  179 ARG A NH2 
928  N N   . ILE A 123 ? 0.1378 0.1824 0.1585 0.0023  0.0443  0.0418  180 ILE A N   
929  C CA  . ILE A 123 ? 0.1519 0.1778 0.1750 -0.0014 0.0338  0.0297  180 ILE A CA  
930  C C   . ILE A 123 ? 0.1597 0.2036 0.1970 -0.0001 0.0345  0.0288  180 ILE A C   
931  O O   . ILE A 123 ? 0.1781 0.2456 0.2371 -0.0102 0.0372  0.0373  180 ILE A O   
932  C CB  . ILE A 123 ? 0.1670 0.1783 0.2008 -0.0162 0.0280  0.0293  180 ILE A CB  
933  C CG1 . ILE A 123 ? 0.1768 0.1726 0.1973 -0.0138 0.0256  0.0311  180 ILE A CG1 
934  C CG2 . ILE A 123 ? 0.2114 0.2112 0.2485 -0.0195 0.0207  0.0194  180 ILE A CG2 
935  C CD1 . ILE A 123 ? 0.2340 0.2174 0.2642 -0.0231 0.0227  0.0338  180 ILE A CD1 
936  N N   . ALA A 124 ? 0.1630 0.1940 0.1873 0.0108  0.0296  0.0195  181 ALA A N   
937  C CA  . ALA A 124 ? 0.1449 0.1891 0.1789 0.0152  0.0282  0.0188  181 ALA A CA  
938  C C   . ALA A 124 ? 0.1223 0.1487 0.1597 0.0030  0.0185  0.0125  181 ALA A C   
939  O O   . ALA A 124 ? 0.1526 0.1559 0.1809 -0.0032 0.0137  0.0073  181 ALA A O   
940  C CB  . ALA A 124 ? 0.1775 0.2137 0.1889 0.0391  0.0296  0.0140  181 ALA A CB  
941  N N   . LEU A 125 ? 0.1306 0.1727 0.1821 -0.0004 0.0157  0.0145  182 LEU A N   
942  C CA  . LEU A 125 ? 0.1346 0.1627 0.1858 -0.0106 0.0078  0.0096  182 LEU A CA  
943  C C   . LEU A 125 ? 0.1378 0.1624 0.1804 0.0005  0.0027  0.0082  182 LEU A C   
944  O O   . LEU A 125 ? 0.1413 0.1895 0.1925 0.0116  0.0040  0.0133  182 LEU A O   
945  C CB  . LEU A 125 ? 0.1342 0.1768 0.2025 -0.0262 0.0052  0.0128  182 LEU A CB  
946  C CG  . LEU A 125 ? 0.1292 0.1717 0.2050 -0.0376 0.0088  0.0164  182 LEU A CG  
947  C CD1 . LEU A 125 ? 0.1728 0.2151 0.2511 -0.0505 0.0030  0.0149  182 LEU A CD1 
948  C CD2 . LEU A 125 ? 0.1818 0.1980 0.2452 -0.0377 0.0101  0.0109  182 LEU A CD2 
949  N N   . LEU A 126 ? 0.1278 0.1256 0.1551 -0.0026 -0.0031 0.0036  183 LEU A N   
950  C CA  . LEU A 126 ? 0.1496 0.1362 0.1648 0.0058  -0.0097 0.0040  183 LEU A CA  
951  C C   . LEU A 126 ? 0.1387 0.1229 0.1549 -0.0084 -0.0142 0.0041  183 LEU A C   
952  O O   . LEU A 126 ? 0.1866 0.1539 0.1945 -0.0180 -0.0143 0.0024  183 LEU A O   
953  C CB  . LEU A 126 ? 0.1741 0.1252 0.1635 0.0138  -0.0137 0.0006  183 LEU A CB  
954  C CG  . LEU A 126 ? 0.2822 0.2074 0.2520 0.0200  -0.0226 0.0021  183 LEU A CG  
955  C CD1 . LEU A 126 ? 0.2915 0.2365 0.2678 0.0352  -0.0241 0.0065  183 LEU A CD1 
956  C CD2 . LEU A 126 ? 0.2785 0.1616 0.2182 0.0291  -0.0284 -0.0022 183 LEU A CD2 
957  N N   . THR A 127 ? 0.1460 0.1509 0.1725 -0.0094 -0.0177 0.0071  184 THR A N   
958  C CA  . THR A 127 ? 0.1460 0.1478 0.1680 -0.0221 -0.0221 0.0057  184 THR A CA  
959  C C   . THR A 127 ? 0.1722 0.1563 0.1746 -0.0183 -0.0282 0.0085  184 THR A C   
960  O O   . THR A 127 ? 0.1796 0.1543 0.1738 -0.0050 -0.0318 0.0120  184 THR A O   
961  C CB  . THR A 127 ? 0.1298 0.1570 0.1665 -0.0288 -0.0279 0.0075  184 THR A CB  
962  O OG1 . THR A 127 ? 0.1577 0.2020 0.1982 -0.0186 -0.0358 0.0137  184 THR A OG1 
963  C CG2 . THR A 127 ? 0.1632 0.2092 0.2206 -0.0338 -0.0230 0.0092  184 THR A CG2 
964  N N   . GLY A 128 ? 0.1712 0.1482 0.1623 -0.0287 -0.0292 0.0075  185 GLY A N   
965  C CA  . GLY A 128 ? 0.1970 0.1637 0.1695 -0.0269 -0.0361 0.0127  185 GLY A CA  
966  C C   . GLY A 128 ? 0.1803 0.1666 0.1579 -0.0222 -0.0466 0.0152  185 GLY A C   
967  O O   . GLY A 128 ? 0.1918 0.2030 0.1905 -0.0231 -0.0484 0.0138  185 GLY A O   
968  N N   . PRO A 129 ? 0.2050 0.1825 0.1639 -0.0189 -0.0548 0.0210  186 PRO A N   
969  C CA  . PRO A 129 ? 0.2268 0.2264 0.1908 -0.0142 -0.0679 0.0249  186 PRO A CA  
970  C C   . PRO A 129 ? 0.2212 0.2345 0.1878 -0.0299 -0.0724 0.0185  186 PRO A C   
971  O O   . PRO A 129 ? 0.2613 0.2568 0.2062 -0.0395 -0.0689 0.0129  186 PRO A O   
972  C CB  . PRO A 129 ? 0.2598 0.2385 0.1956 -0.0083 -0.0753 0.0331  186 PRO A CB  
973  C CG  . PRO A 129 ? 0.2924 0.2433 0.2076 -0.0189 -0.0650 0.0323  186 PRO A CG  
974  C CD  . PRO A 129 ? 0.2528 0.2024 0.1853 -0.0216 -0.0535 0.0263  186 PRO A CD  
975  N N   . LEU A 130 ? 0.2437 0.2883 0.2357 -0.0324 -0.0803 0.0198  187 LEU A N   
976  C CA  . LEU A 130 ? 0.2905 0.3396 0.2834 -0.0509 -0.0869 0.0129  187 LEU A CA  
977  C C   . LEU A 130 ? 0.3244 0.3636 0.2883 -0.0579 -0.1016 0.0107  187 LEU A C   
978  O O   . LEU A 130 ? 0.3672 0.3944 0.3197 -0.0702 -0.1042 0.0014  187 LEU A O   
979  C CB  . LEU A 130 ? 0.2365 0.3243 0.2667 -0.0567 -0.0930 0.0184  187 LEU A CB  
980  C CG  . LEU A 130 ? 0.3151 0.4097 0.3676 -0.0526 -0.0771 0.0191  187 LEU A CG  
981  C CD1 . LEU A 130 ? 0.3725 0.5000 0.4558 -0.0608 -0.0782 0.0248  187 LEU A CD1 
982  C CD2 . LEU A 130 ? 0.2759 0.3350 0.3115 -0.0586 -0.0647 0.0089  187 LEU A CD2 
983  N N   . THR A 131 ? 0.2719 0.3095 0.2203 -0.0467 -0.1079 0.0184  188 THR A N   
984  C CA  . THR A 131 ? 0.3531 0.3745 0.2648 -0.0507 -0.1177 0.0166  188 THR A CA  
985  C C   . THR A 131 ? 0.3399 0.3276 0.2167 -0.0560 -0.1048 0.0073  188 THR A C   
986  O O   . THR A 131 ? 0.4284 0.4026 0.2748 -0.0587 -0.1081 0.0020  188 THR A O   
987  C CB  . THR A 131 ? 0.4252 0.4470 0.3253 -0.0357 -0.1246 0.0294  188 THR A CB  
988  O OG1 . THR A 131 ? 0.4169 0.4194 0.3146 -0.0251 -0.1100 0.0344  188 THR A OG1 
989  C CG2 . THR A 131 ? 0.4517 0.5117 0.3836 -0.0259 -0.1369 0.0374  188 THR A CG2 
990  N N   . SER A 132 ? 0.3465 0.3243 0.2322 -0.0532 -0.0856 0.0054  189 SER A N   
991  C CA  . SER A 132 ? 0.3177 0.2739 0.1775 -0.0547 -0.0702 -0.0004 189 SER A CA  
992  C C   . SER A 132 ? 0.3127 0.2619 0.1751 -0.0612 -0.0658 -0.0141 189 SER A C   
993  O O   . SER A 132 ? 0.3107 0.2691 0.2038 -0.0637 -0.0638 -0.0156 189 SER A O   
994  C CB  . SER A 132 ? 0.3804 0.3324 0.2494 -0.0497 -0.0544 0.0075  189 SER A CB  
995  O OG  . SER A 132 ? 0.4192 0.3655 0.2853 -0.0517 -0.0382 0.0012  189 SER A OG  
996  N N   A VAL A 133 ? 0.3131 0.3200 0.1787 -0.0329 -0.0506 0.0177  190 VAL A N   
997  N N   B VAL A 133 ? 0.3128 0.3193 0.1784 -0.0328 -0.0503 0.0174  190 VAL A N   
998  C CA  A VAL A 133 ? 0.3446 0.3241 0.1894 -0.0448 -0.0493 -0.0010 190 VAL A CA  
999  C CA  B VAL A 133 ? 0.3436 0.3239 0.1897 -0.0450 -0.0495 -0.0009 190 VAL A CA  
1000 C C   A VAL A 133 ? 0.3065 0.2839 0.1796 -0.0317 -0.0250 -0.0106 190 VAL A C   
1001 C C   B VAL A 133 ? 0.3073 0.2837 0.1794 -0.0317 -0.0247 -0.0110 190 VAL A C   
1002 O O   A VAL A 133 ? 0.2742 0.2510 0.1620 -0.0370 -0.0256 -0.0177 190 VAL A O   
1003 O O   B VAL A 133 ? 0.2774 0.2507 0.1613 -0.0370 -0.0247 -0.0189 190 VAL A O   
1004 C CB  A VAL A 133 ? 0.4179 0.3454 0.1878 -0.0517 -0.0486 -0.0129 190 VAL A CB  
1005 C CB  B VAL A 133 ? 0.4196 0.3474 0.1899 -0.0538 -0.0509 -0.0130 190 VAL A CB  
1006 C CG1 A VAL A 133 ? 0.4879 0.3721 0.2255 -0.0579 -0.0425 -0.0310 190 VAL A CG1 
1007 C CG1 B VAL A 133 ? 0.5063 0.4323 0.2426 -0.0793 -0.0858 -0.0040 190 VAL A CG1 
1008 C CG2 A VAL A 133 ? 0.5245 0.4509 0.2584 -0.0724 -0.0801 -0.0023 190 VAL A CG2 
1009 C CG2 B VAL A 133 ? 0.4117 0.3255 0.1603 -0.0357 -0.0277 -0.0120 190 VAL A CG2 
1010 N N   . SER A 134 ? 0.2946 0.2722 0.1754 -0.0182 -0.0062 -0.0077 191 SER A N   
1011 C CA  . SER A 134 ? 0.2929 0.2741 0.1997 -0.0121 0.0111  -0.0117 191 SER A CA  
1012 C C   . SER A 134 ? 0.2375 0.2372 0.1830 -0.0122 0.0060  -0.0095 191 SER A C   
1013 O O   . SER A 134 ? 0.2182 0.2194 0.1796 -0.0132 0.0107  -0.0159 191 SER A O   
1014 C CB  . SER A 134 ? 0.3481 0.3311 0.2564 -0.0069 0.0259  -0.0026 191 SER A CB  
1015 O OG  . SER A 134 ? 0.5623 0.5364 0.4475 -0.0011 0.0425  -0.0030 191 SER A OG  
1016 N N   . ALA A 135 ? 0.2013 0.2128 0.1585 -0.0071 -0.0006 0.0020  192 ALA A N   
1017 C CA  . ALA A 135 ? 0.1808 0.2041 0.1659 -0.0005 0.0010  0.0064  192 ALA A CA  
1018 C C   . ALA A 135 ? 0.1826 0.2264 0.1862 -0.0088 -0.0089 0.0047  192 ALA A C   
1019 O O   . ALA A 135 ? 0.1649 0.2117 0.1865 -0.0076 -0.0030 0.0014  192 ALA A O   
1020 C CB  . ALA A 135 ? 0.2075 0.2357 0.1958 0.0155  0.0018  0.0236  192 ALA A CB  
1021 N N   . ARG A 136 ? 0.1900 0.2437 0.1832 -0.0216 -0.0263 0.0083  193 ARG A N   
1022 C CA  . ARG A 136 ? 0.1928 0.2623 0.1981 -0.0388 -0.0413 0.0105  193 ARG A CA  
1023 C C   . ARG A 136 ? 0.2245 0.2608 0.2130 -0.0463 -0.0340 -0.0088 193 ARG A C   
1024 O O   . ARG A 136 ? 0.1828 0.2286 0.1930 -0.0515 -0.0344 -0.0080 193 ARG A O   
1025 C CB  . ARG A 136 ? 0.2315 0.3084 0.2152 -0.0601 -0.0679 0.0197  193 ARG A CB  
1026 C CG  . ARG A 136 ? 0.3750 0.4639 0.3652 -0.0887 -0.0895 0.0253  193 ARG A CG  
1027 C CD  . ARG A 136 ? 0.4403 0.5568 0.4230 -0.1157 -0.1237 0.0467  193 ARG A CD  
1028 N NE  . ARG A 136 ? 0.5790 0.6482 0.4947 -0.1258 -0.1341 0.0349  193 ARG A NE  
1029 C CZ  . ARG A 136 ? 0.7048 0.6985 0.5488 -0.1376 -0.1320 0.0087  193 ARG A CZ  
1030 N NH1 . ARG A 136 ? 0.7222 0.6778 0.5528 -0.1418 -0.1218 -0.0083 193 ARG A NH1 
1031 N NH2 . ARG A 136 ? 0.8961 0.8475 0.6778 -0.1398 -0.1353 0.0014  193 ARG A NH2 
1032 N N   . LEU A 137 ? 0.2203 0.2192 0.1710 -0.0428 -0.0240 -0.0227 194 LEU A N   
1033 C CA  . LEU A 137 ? 0.2486 0.2149 0.1810 -0.0419 -0.0126 -0.0361 194 LEU A CA  
1034 C C   . LEU A 137 ? 0.2139 0.1973 0.1838 -0.0298 0.0024  -0.0351 194 LEU A C   
1035 O O   . LEU A 137 ? 0.2285 0.2014 0.2018 -0.0313 0.0058  -0.0395 194 LEU A O   
1036 C CB  . LEU A 137 ? 0.3181 0.2465 0.2025 -0.0324 0.0014  -0.0442 194 LEU A CB  
1037 C CG  . LEU A 137 ? 0.4078 0.2941 0.2297 -0.0481 -0.0141 -0.0503 194 LEU A CG  
1038 C CD1 . LEU A 137 ? 0.5417 0.3841 0.3078 -0.0312 0.0076  -0.0572 194 LEU A CD1 
1039 C CD2 . LEU A 137 ? 0.5238 0.3773 0.3213 -0.0702 -0.0302 -0.0570 194 LEU A CD2 
1040 N N   . ARG A 138 ? 0.1629 0.1655 0.1533 -0.0206 0.0093  -0.0283 195 ARG A N   
1041 C CA  . ARG A 138 ? 0.1662 0.1779 0.1806 -0.0162 0.0174  -0.0261 195 ARG A CA  
1042 C C   . ARG A 138 ? 0.1835 0.2072 0.2182 -0.0182 0.0125  -0.0233 195 ARG A C   
1043 O O   . ARG A 138 ? 0.1805 0.2030 0.2250 -0.0187 0.0165  -0.0252 195 ARG A O   
1044 C CB  . ARG A 138 ? 0.1877 0.2007 0.2025 -0.0134 0.0217  -0.0193 195 ARG A CB  
1045 C CG  . ARG A 138 ? 0.1790 0.1918 0.1841 -0.0131 0.0297  -0.0157 195 ARG A CG  
1046 C CD  . ARG A 138 ? 0.1700 0.1795 0.1697 -0.0182 0.0296  -0.0060 195 ARG A CD  
1047 N NE  . ARG A 138 ? 0.1859 0.2022 0.1771 -0.0175 0.0377  0.0015  195 ARG A NE  
1048 C CZ  . ARG A 138 ? 0.1774 0.1907 0.1606 -0.0251 0.0380  0.0128  195 ARG A CZ  
1049 N NH1 . ARG A 138 ? 0.1970 0.1885 0.1706 -0.0342 0.0302  0.0156  195 ARG A NH1 
1050 N NH2 . ARG A 138 ? 0.1922 0.2169 0.1692 -0.0224 0.0486  0.0225  195 ARG A NH2 
1051 N N   . PHE A 139 ? 0.1581 0.1986 0.2017 -0.0169 0.0055  -0.0140 196 PHE A N   
1052 C CA  . PHE A 139 ? 0.1533 0.2172 0.2220 -0.0162 0.0040  -0.0038 196 PHE A CA  
1053 C C   . PHE A 139 ? 0.1667 0.2296 0.2386 -0.0329 -0.0042 -0.0078 196 PHE A C   
1054 O O   . PHE A 139 ? 0.1492 0.2159 0.2350 -0.0326 0.0014  -0.0061 196 PHE A O   
1055 C CB  . PHE A 139 ? 0.1463 0.2426 0.2308 -0.0109 -0.0028 0.0152  196 PHE A CB  
1056 C CG  . PHE A 139 ? 0.1237 0.2595 0.2435 -0.0044 0.0007  0.0358  196 PHE A CG  
1057 C CD1 . PHE A 139 ? 0.2065 0.3914 0.3543 -0.0027 -0.0084 0.0623  196 PHE A CD1 
1058 C CD2 . PHE A 139 ? 0.1648 0.2947 0.2912 0.0025  0.0147  0.0341  196 PHE A CD2 
1059 C CE1 . PHE A 139 ? 0.2768 0.5123 0.4659 0.0064  -0.0018 0.0897  196 PHE A CE1 
1060 C CE2 . PHE A 139 ? 0.1684 0.3382 0.3270 0.0119  0.0227  0.0570  196 PHE A CE2 
1061 C CZ  . PHE A 139 ? 0.3137 0.5400 0.5072 0.0151  0.0161  0.0865  196 PHE A CZ  
1062 N N   . GLU A 140 ? 0.1524 0.2009 0.2018 -0.0489 -0.0177 -0.0126 197 GLU A N   
1063 C CA  . GLU A 140 ? 0.1912 0.2199 0.2275 -0.0687 -0.0272 -0.0166 197 GLU A CA  
1064 C C   . GLU A 140 ? 0.2151 0.2120 0.2400 -0.0590 -0.0115 -0.0290 197 GLU A C   
1065 O O   . GLU A 140 ? 0.2344 0.2240 0.2645 -0.0671 -0.0123 -0.0276 197 GLU A O   
1066 C CB  . GLU A 140 ? 0.2323 0.2295 0.2235 -0.0891 -0.0451 -0.0218 197 GLU A CB  
1067 C CG  . GLU A 140 ? 0.3418 0.3839 0.3534 -0.1073 -0.0688 -0.0008 197 GLU A CG  
1068 C CD  . GLU A 140 ? 0.5616 0.5731 0.5209 -0.1299 -0.0912 -0.0040 197 GLU A CD  
1069 O OE1 . GLU A 140 ? 0.5952 0.5404 0.4930 -0.1275 -0.0838 -0.0252 197 GLU A OE1 
1070 O OE2 . GLU A 140 ? 0.3588 0.4133 0.3368 -0.1459 -0.1134 0.0182  197 GLU A OE2 
1071 N N   . GLY A 141 ? 0.2021 0.1858 0.2153 -0.0420 0.0025  -0.0363 198 GLY A N   
1072 C CA  . GLY A 141 ? 0.2045 0.1737 0.2170 -0.0301 0.0170  -0.0395 198 GLY A CA  
1073 C C   . GLY A 141 ? 0.2054 0.1989 0.2498 -0.0274 0.0199  -0.0328 198 GLY A C   
1074 O O   . GLY A 141 ? 0.1915 0.1750 0.2377 -0.0260 0.0242  -0.0320 198 GLY A O   
1075 N N   . TRP A 142 ? 0.1413 0.1576 0.2016 -0.0246 0.0193  -0.0274 199 TRP A N   
1076 C CA  . TRP A 142 ? 0.1264 0.1510 0.1991 -0.0214 0.0236  -0.0222 199 TRP A CA  
1077 C C   . TRP A 142 ? 0.1582 0.1907 0.2436 -0.0275 0.0219  -0.0168 199 TRP A C   
1078 O O   . TRP A 142 ? 0.1614 0.1893 0.2494 -0.0270 0.0263  -0.0148 199 TRP A O   
1079 C CB  . TRP A 142 ? 0.1630 0.1913 0.2323 -0.0143 0.0265  -0.0178 199 TRP A CB  
1080 C CG  . TRP A 142 ? 0.1530 0.1678 0.2060 -0.0143 0.0269  -0.0196 199 TRP A CG  
1081 C CD1 . TRP A 142 ? 0.1324 0.1468 0.1843 -0.0202 0.0255  -0.0188 199 TRP A CD1 
1082 C CD2 . TRP A 142 ? 0.1652 0.1676 0.2018 -0.0098 0.0282  -0.0172 199 TRP A CD2 
1083 N NE1 . TRP A 142 ? 0.1536 0.1595 0.1913 -0.0259 0.0230  -0.0151 199 TRP A NE1 
1084 C CE2 . TRP A 142 ? 0.1612 0.1514 0.1839 -0.0195 0.0250  -0.0166 199 TRP A CE2 
1085 C CE3 . TRP A 142 ? 0.1380 0.1403 0.1714 0.0027  0.0326  -0.0111 199 TRP A CE3 
1086 C CZ2 . TRP A 142 ? 0.1787 0.1447 0.1761 -0.0216 0.0245  -0.0138 199 TRP A CZ2 
1087 C CZ3 . TRP A 142 ? 0.1723 0.1483 0.1795 0.0082  0.0356  -0.0087 199 TRP A CZ3 
1088 C CH2 . TRP A 142 ? 0.1982 0.1504 0.1835 -0.0063 0.0307  -0.0120 199 TRP A CH2 
1089 N N   . ARG A 143 ? 0.1546 0.2046 0.2503 -0.0356 0.0139  -0.0098 200 ARG A N   
1090 C CA  . ARG A 143 ? 0.1556 0.2243 0.2704 -0.0473 0.0101  0.0026  200 ARG A CA  
1091 C C   . ARG A 143 ? 0.1926 0.2293 0.2911 -0.0611 0.0058  -0.0045 200 ARG A C   
1092 O O   . ARG A 143 ? 0.1706 0.2098 0.2789 -0.0650 0.0096  0.0027  200 ARG A O   
1093 C CB  . ARG A 143 ? 0.1364 0.2387 0.2686 -0.0607 -0.0042 0.0176  200 ARG A CB  
1094 C CG  . ARG A 143 ? 0.2858 0.4254 0.4493 -0.0765 -0.0096 0.0404  200 ARG A CG  
1095 C CD  . ARG A 143 ? 0.4598 0.6467 0.6455 -0.0726 -0.0161 0.0633  200 ARG A CD  
1096 N NE  . ARG A 143 ? 0.7256 0.9133 0.8997 -0.0854 -0.0354 0.0625  200 ARG A NE  
1097 C CZ  . ARG A 143 ? 0.6691 0.8158 0.8058 -0.1111 -0.0545 0.0473  200 ARG A CZ  
1098 N NH1 . ARG A 143 ? 0.6116 0.7114 0.7194 -0.1266 -0.0572 0.0334  200 ARG A NH1 
1099 N NH2 . ARG A 143 ? 0.6430 0.7878 0.7620 -0.1187 -0.0694 0.0469  200 ARG A NH2 
1100 N N   . GLN A 144 ? 0.1883 0.1877 0.2551 -0.0655 0.0010  -0.0174 201 GLN A N   
1101 C CA  . GLN A 144 ? 0.2395 0.1923 0.2772 -0.0748 0.0000  -0.0230 201 GLN A CA  
1102 C C   . GLN A 144 ? 0.2415 0.1841 0.2817 -0.0550 0.0159  -0.0242 201 GLN A C   
1103 O O   . GLN A 144 ? 0.2557 0.1761 0.2886 -0.0599 0.0175  -0.0208 201 GLN A O   
1104 C CB  . GLN A 144 ? 0.3279 0.2302 0.3156 -0.0798 -0.0049 -0.0356 201 GLN A CB  
1105 C CG  . GLN A 144 ? 0.5158 0.4111 0.4871 -0.1147 -0.0297 -0.0306 201 GLN A CG  
1106 C CD  . GLN A 144 ? 0.8744 0.8029 0.8798 -0.1325 -0.0389 -0.0126 201 GLN A CD  
1107 O OE1 . GLN A 144 ? 0.6114 0.6043 0.6630 -0.1354 -0.0441 0.0052  201 GLN A OE1 
1108 N NE2 . GLN A 144 ? 0.8146 0.7006 0.7959 -0.1372 -0.0364 -0.0145 201 GLN A NE2 
1109 N N   . THR A 145 ? 0.1933 0.1533 0.2435 -0.0360 0.0251  -0.0254 202 THR A N   
1110 C CA  . THR A 145 ? 0.1784 0.1408 0.2359 -0.0221 0.0344  -0.0198 202 THR A CA  
1111 C C   . THR A 145 ? 0.1984 0.1798 0.2732 -0.0270 0.0333  -0.0119 202 THR A C   
1112 O O   . THR A 145 ? 0.2130 0.1854 0.2867 -0.0237 0.0370  -0.0057 202 THR A O   
1113 C CB  . THR A 145 ? 0.1624 0.1456 0.2280 -0.0096 0.0390  -0.0169 202 THR A CB  
1114 O OG1 . THR A 145 ? 0.1979 0.1659 0.2459 -0.0027 0.0440  -0.0223 202 THR A OG1 
1115 C CG2 . THR A 145 ? 0.1843 0.1775 0.2599 0.0018  0.0446  -0.0042 202 THR A CG2 
1116 N N   . LEU A 146 ? 0.1523 0.1566 0.2384 -0.0308 0.0314  -0.0098 203 LEU A N   
1117 C CA  . LEU A 146 ? 0.1420 0.1577 0.2354 -0.0308 0.0363  -0.0006 203 LEU A CA  
1118 C C   . LEU A 146 ? 0.1622 0.1735 0.2622 -0.0433 0.0350  0.0070  203 LEU A C   
1119 O O   . LEU A 146 ? 0.1781 0.1865 0.2773 -0.0421 0.0406  0.0147  203 LEU A O   
1120 C CB  . LEU A 146 ? 0.1492 0.1855 0.2490 -0.0249 0.0413  0.0044  203 LEU A CB  
1121 C CG  . LEU A 146 ? 0.1547 0.1783 0.2332 -0.0147 0.0442  -0.0015 203 LEU A CG  
1122 C CD1 . LEU A 146 ? 0.1774 0.2105 0.2561 -0.0034 0.0519  0.0040  203 LEU A CD1 
1123 C CD2 . LEU A 146 ? 0.1906 0.1941 0.2441 -0.0125 0.0479  0.0001  203 LEU A CD2 
1124 N N   . ALA A 147 ? 0.1618 0.1684 0.2624 -0.0594 0.0253  0.0066  204 ALA A N   
1125 C CA  . ALA A 147 ? 0.1845 0.1805 0.2853 -0.0806 0.0192  0.0163  204 ALA A CA  
1126 C C   . ALA A 147 ? 0.2633 0.2094 0.3363 -0.0779 0.0229  0.0111  204 ALA A C   
1127 O O   . ALA A 147 ? 0.2454 0.1792 0.3167 -0.0902 0.0228  0.0214  204 ALA A O   
1128 C CB  . ALA A 147 ? 0.2239 0.2177 0.3199 -0.1066 0.0013  0.0181  204 ALA A CB  
1129 N N   . GLN A 148 ? 0.2457 0.1658 0.2986 -0.0594 0.0283  -0.0003 205 GLN A N   
1130 C CA  . GLN A 148 ? 0.2766 0.1563 0.3075 -0.0465 0.0370  0.0011  205 GLN A CA  
1131 C C   . GLN A 148 ? 0.2586 0.1620 0.3078 -0.0372 0.0428  0.0132  205 GLN A C   
1132 O O   . GLN A 148 ? 0.2948 0.1696 0.3302 -0.0294 0.0484  0.0205  205 GLN A O   
1133 C CB  . GLN A 148 ? 0.3313 0.1946 0.3462 -0.0223 0.0462  -0.0053 205 GLN A CB  
1134 C CG  . GLN A 148 ? 0.4069 0.2173 0.3786 -0.0277 0.0452  -0.0176 205 GLN A CG  
1135 C CD  . GLN A 148 ? 0.6777 0.4948 0.6441 -0.0059 0.0549  -0.0226 205 GLN A CD  
1136 O OE1 . GLN A 148 ? 0.6099 0.4731 0.6088 0.0120  0.0618  -0.0137 205 GLN A OE1 
1137 N NE2 . GLN A 148 ? 0.8363 0.6050 0.7566 -0.0104 0.0543  -0.0346 205 GLN A NE2 
1138 N N   . HIS A 149 ? 0.2049 0.1509 0.2755 -0.0365 0.0422  0.0162  206 HIS A N   
1139 C CA  . HIS A 149 ? 0.2206 0.1799 0.2939 -0.0317 0.0461  0.0266  206 HIS A CA  
1140 C C   . HIS A 149 ? 0.2736 0.2490 0.3559 -0.0426 0.0505  0.0356  206 HIS A C   
1141 O O   . HIS A 149 ? 0.2310 0.2154 0.3069 -0.0365 0.0572  0.0429  206 HIS A O   
1142 C CB  . HIS A 149 ? 0.1839 0.1625 0.2555 -0.0225 0.0437  0.0248  206 HIS A CB  
1143 C CG  . HIS A 149 ? 0.2368 0.2173 0.3109 -0.0121 0.0406  0.0268  206 HIS A CG  
1144 N ND1 . HIS A 149 ? 0.2443 0.2272 0.3189 -0.0030 0.0400  0.0416  206 HIS A ND1 
1145 C CD2 . HIS A 149 ? 0.2434 0.2298 0.3230 -0.0067 0.0404  0.0211  206 HIS A CD2 
1146 C CE1 . HIS A 149 ? 0.2378 0.2348 0.3238 0.0094  0.0408  0.0480  206 HIS A CE1 
1147 N NE2 . HIS A 149 ? 0.2606 0.2579 0.3479 0.0072  0.0421  0.0347  206 HIS A NE2 
1148 N N   . GLN A 150 ? 0.2683 0.1777 0.3214 -0.0466 -0.0136 0.0695  207 GLN A N   
1149 C CA  . GLN A 150 ? 0.2379 0.1579 0.3013 -0.0552 -0.0100 0.0789  207 GLN A CA  
1150 C C   . GLN A 150 ? 0.2368 0.1789 0.3015 -0.0526 -0.0026 0.0797  207 GLN A C   
1151 O O   . GLN A 150 ? 0.2565 0.2096 0.3246 -0.0556 0.0036  0.0888  207 GLN A O   
1152 C CB  . GLN A 150 ? 0.2388 0.1503 0.3013 -0.0591 -0.0087 0.0906  207 GLN A CB  
1153 C CG  . GLN A 150 ? 0.2856 0.1762 0.3472 -0.0615 -0.0160 0.0881  207 GLN A CG  
1154 C CD  . GLN A 150 ? 0.3269 0.2007 0.3780 -0.0530 -0.0203 0.0827  207 GLN A CD  
1155 O OE1 . GLN A 150 ? 0.3169 0.1926 0.3597 -0.0462 -0.0173 0.0853  207 GLN A OE1 
1156 N NE2 . GLN A 150 ? 0.3777 0.2366 0.4285 -0.0525 -0.0272 0.0743  207 GLN A NE2 
1157 N N   . LEU A 151 ? 0.2359 0.1843 0.2980 -0.0471 -0.0031 0.0701  208 LEU A N   
1158 C CA  . LEU A 151 ? 0.1912 0.1580 0.2540 -0.0436 0.0028  0.0689  208 LEU A CA  
1159 C C   . LEU A 151 ? 0.2270 0.2019 0.2992 -0.0465 0.0003  0.0637  208 LEU A C   
1160 O O   . LEU A 151 ? 0.2286 0.1943 0.3016 -0.0481 -0.0064 0.0574  208 LEU A O   
1161 C CB  . LEU A 151 ? 0.2327 0.1999 0.2833 -0.0340 0.0043  0.0626  208 LEU A CB  
1162 C CG  . LEU A 151 ? 0.2323 0.1942 0.2723 -0.0296 0.0066  0.0671  208 LEU A CG  
1163 C CD1 . LEU A 151 ? 0.2301 0.1917 0.2604 -0.0212 0.0060  0.0598  208 LEU A CD1 
1164 C CD2 . LEU A 151 ? 0.2603 0.2344 0.3005 -0.0309 0.0140  0.0758  208 LEU A CD2 
1165 N N   A GLN A 152 ? 0.2053 0.1979 0.2840 -0.0466 0.0056  0.0663  209 GLN A N   
1166 N N   B GLN A 152 ? 0.2054 0.1978 0.2840 -0.0465 0.0056  0.0662  209 GLN A N   
1167 C CA  A GLN A 152 ? 0.2040 0.2073 0.2900 -0.0466 0.0043  0.0612  209 GLN A CA  
1168 C CA  B GLN A 152 ? 0.2047 0.2076 0.2904 -0.0465 0.0041  0.0610  209 GLN A CA  
1169 C C   A GLN A 152 ? 0.1885 0.1991 0.2665 -0.0379 0.0082  0.0561  209 GLN A C   
1170 C C   B GLN A 152 ? 0.1891 0.1996 0.2670 -0.0378 0.0081  0.0561  209 GLN A C   
1171 O O   A GLN A 152 ? 0.2241 0.2375 0.2949 -0.0334 0.0137  0.0588  209 GLN A O   
1172 O O   B GLN A 152 ? 0.2240 0.2376 0.2949 -0.0334 0.0138  0.0588  209 GLN A O   
1173 C CB  A GLN A 152 ? 0.2129 0.2320 0.3144 -0.0527 0.0073  0.0681  209 GLN A CB  
1174 C CB  B GLN A 152 ? 0.2146 0.2327 0.3159 -0.0528 0.0068  0.0678  209 GLN A CB  
1175 C CG  A GLN A 152 ? 0.1993 0.2132 0.3119 -0.0629 0.0028  0.0734  209 GLN A CG  
1176 C CG  B GLN A 152 ? 0.2140 0.2268 0.3267 -0.0626 0.0003  0.0702  209 GLN A CG  
1177 C CD  A GLN A 152 ? 0.2669 0.2771 0.3860 -0.0671 -0.0061 0.0673  209 GLN A CD  
1178 C CD  B GLN A 152 ? 0.2096 0.2392 0.3391 -0.0692 0.0039  0.0786  209 GLN A CD  
1179 O OE1 A GLN A 152 ? 0.2765 0.2933 0.3952 -0.0631 -0.0076 0.0609  209 GLN A OE1 
1180 O OE1 B GLN A 152 ? 0.2477 0.2922 0.3792 -0.0659 0.0124  0.0834  209 GLN A OE1 
1181 N NE2 A GLN A 152 ? 0.2590 0.2578 0.3835 -0.0754 -0.0124 0.0692  209 GLN A NE2 
1182 N NE2 B GLN A 152 ? 0.2261 0.2537 0.3662 -0.0773 -0.0025 0.0792  209 GLN A NE2 
1183 N N   . PRO A 153 ? 0.1897 0.2028 0.2681 -0.0354 0.0051  0.0491  210 PRO A N   
1184 C CA  . PRO A 153 ? 0.1767 0.1976 0.2499 -0.0281 0.0089  0.0453  210 PRO A CA  
1185 C C   . PRO A 153 ? 0.1999 0.2365 0.2801 -0.0274 0.0157  0.0506  210 PRO A C   
1186 O O   . PRO A 153 ? 0.1977 0.2432 0.2907 -0.0327 0.0162  0.0554  210 PRO A O   
1187 C CB  . PRO A 153 ? 0.1752 0.1961 0.2500 -0.0275 0.0037  0.0386  210 PRO A CB  
1188 C CG  . PRO A 153 ? 0.1963 0.2156 0.2807 -0.0350 -0.0016 0.0401  210 PRO A CG  
1189 C CD  . PRO A 153 ? 0.1952 0.2050 0.2795 -0.0397 -0.0020 0.0450  210 PRO A CD  
1190 N N   . ILE A 154 ? 0.1845 0.2246 0.2563 -0.0208 0.0209  0.0497  211 ILE A N   
1191 C CA  . ILE A 154 ? 0.2084 0.2631 0.2848 -0.0185 0.0281  0.0536  211 ILE A CA  
1192 C C   . ILE A 154 ? 0.2018 0.2665 0.2864 -0.0160 0.0277  0.0500  211 ILE A C   
1193 O O   . ILE A 154 ? 0.2211 0.2997 0.3148 -0.0152 0.0327  0.0535  211 ILE A O   
1194 C CB  . ILE A 154 ? 0.2668 0.3202 0.3296 -0.0121 0.0333  0.0532  211 ILE A CB  
1195 C CG1 . ILE A 154 ? 0.3089 0.3754 0.3747 -0.0112 0.0417  0.0596  211 ILE A CG1 
1196 C CG2 . ILE A 154 ? 0.2188 0.2702 0.2743 -0.0054 0.0319  0.0451  211 ILE A CG2 
1197 C CD1 . ILE A 154 ? 0.4739 0.5390 0.5247 -0.0052 0.0466  0.0595  211 ILE A CD1 
1198 N N   . ALA A 155 ? 0.1563 0.2145 0.2382 -0.0145 0.0219  0.0435  212 ALA A N   
1199 C CA  . ALA A 155 ? 0.1499 0.2157 0.2390 -0.0124 0.0202  0.0406  212 ALA A CA  
1200 C C   . ALA A 155 ? 0.1382 0.1944 0.2243 -0.0142 0.0125  0.0356  212 ALA A C   
1201 O O   . ALA A 155 ? 0.1569 0.2012 0.2328 -0.0142 0.0102  0.0327  212 ALA A O   
1202 C CB  . ALA A 155 ? 0.2597 0.3293 0.3430 -0.0043 0.0246  0.0374  212 ALA A CB  
1203 N N   . VAL A 156 ? 0.1409 0.2027 0.2358 -0.0158 0.0085  0.0349  213 VAL A N   
1204 C CA  . VAL A 156 ? 0.1380 0.1922 0.2291 -0.0169 0.0015  0.0301  213 VAL A CA  
1205 C C   . VAL A 156 ? 0.1590 0.2200 0.2537 -0.0128 0.0003  0.0284  213 VAL A C   
1206 O O   . VAL A 156 ? 0.1748 0.2474 0.2820 -0.0136 0.0000  0.0315  213 VAL A O   
1207 C CB  . VAL A 156 ? 0.1659 0.2174 0.2632 -0.0244 -0.0047 0.0312  213 VAL A CB  
1208 C CG1 . VAL A 156 ? 0.2034 0.2468 0.2939 -0.0248 -0.0117 0.0256  213 VAL A CG1 
1209 C CG2 . VAL A 156 ? 0.1765 0.2197 0.2710 -0.0284 -0.0039 0.0334  213 VAL A CG2 
1210 N N   . LEU A 157 ? 0.1374 0.1916 0.2220 -0.0086 -0.0005 0.0241  214 LEU A N   
1211 C CA  . LEU A 157 ? 0.1455 0.2031 0.2312 -0.0043 -0.0018 0.0226  214 LEU A CA  
1212 C C   . LEU A 157 ? 0.1698 0.2200 0.2492 -0.0061 -0.0081 0.0195  214 LEU A C   
1213 O O   . LEU A 157 ? 0.1347 0.1762 0.2063 -0.0086 -0.0098 0.0172  214 LEU A O   
1214 C CB  . LEU A 157 ? 0.2010 0.2562 0.2795 0.0021  0.0031  0.0205  214 LEU A CB  
1215 C CG  . LEU A 157 ? 0.2314 0.2946 0.3141 0.0059  0.0099  0.0227  214 LEU A CG  
1216 C CD1 . LEU A 157 ? 0.2313 0.3074 0.3277 0.0076  0.0105  0.0255  214 LEU A CD1 
1217 C CD2 . LEU A 157 ? 0.3089 0.3724 0.3904 0.0029  0.0136  0.0254  214 LEU A CD2 
1218 N N   . HIS A 158 ? 0.1508 0.2043 0.2331 -0.0043 -0.0116 0.0196  215 HIS A N   
1219 C CA  . HIS A 158 ? 0.1691 0.2170 0.2450 -0.0060 -0.0176 0.0175  215 HIS A CA  
1220 C C   . HIS A 158 ? 0.1700 0.2156 0.2409 -0.0013 -0.0178 0.0168  215 HIS A C   
1221 O O   . HIS A 158 ? 0.1539 0.2057 0.2322 0.0020  -0.0181 0.0189  215 HIS A O   
1222 C CB  . HIS A 158 ? 0.1509 0.2047 0.2350 -0.0101 -0.0240 0.0192  215 HIS A CB  
1223 C CG  . HIS A 158 ? 0.1784 0.2352 0.2703 -0.0155 -0.0244 0.0208  215 HIS A CG  
1224 N ND1 . HIS A 158 ? 0.2071 0.2546 0.2920 -0.0195 -0.0255 0.0184  215 HIS A ND1 
1225 C CD2 . HIS A 158 ? 0.2245 0.2924 0.3310 -0.0175 -0.0234 0.0249  215 HIS A CD2 
1226 C CE1 . HIS A 158 ? 0.1952 0.2464 0.2897 -0.0243 -0.0259 0.0211  215 HIS A CE1 
1227 N NE2 . HIS A 158 ? 0.2287 0.2931 0.3367 -0.0236 -0.0244 0.0254  215 HIS A NE2 
1228 N N   . GLY A 159 ? 0.1463 0.1831 0.2057 -0.0012 -0.0178 0.0142  216 GLY A N   
1229 C CA  . GLY A 159 ? 0.1649 0.1980 0.2189 0.0020  -0.0181 0.0141  216 GLY A CA  
1230 C C   . GLY A 159 ? 0.1686 0.1987 0.2160 -0.0001 -0.0233 0.0141  216 GLY A C   
1231 O O   . GLY A 159 ? 0.1976 0.2290 0.2451 -0.0035 -0.0274 0.0138  216 GLY A O   
1232 N N   . ASP A 160 ? 0.1302 0.1558 0.1714 0.0018  -0.0233 0.0147  217 ASP A N   
1233 C CA  . ASP A 160 ? 0.1458 0.1690 0.1796 0.0003  -0.0278 0.0159  217 ASP A CA  
1234 C C   . ASP A 160 ? 0.1560 0.1730 0.1787 -0.0005 -0.0254 0.0146  217 ASP A C   
1235 O O   . ASP A 160 ? 0.1761 0.1910 0.1917 -0.0011 -0.0278 0.0165  217 ASP A O   
1236 C CB  . ASP A 160 ? 0.1508 0.1759 0.1887 0.0031  -0.0313 0.0199  217 ASP A CB  
1237 C CG  . ASP A 160 ? 0.1742 0.1947 0.2119 0.0066  -0.0283 0.0210  217 ASP A CG  
1238 O OD1 . ASP A 160 ? 0.1753 0.1912 0.2085 0.0061  -0.0241 0.0189  217 ASP A OD1 
1239 O OD2 . ASP A 160 ? 0.2535 0.2745 0.2959 0.0098  -0.0309 0.0241  217 ASP A OD2 
1240 N N   . TRP A 161 ? 0.1478 0.1627 0.1692 -0.0006 -0.0207 0.0118  218 TRP A N   
1241 C CA  . TRP A 161 ? 0.1522 0.1633 0.1661 -0.0012 -0.0175 0.0103  218 TRP A CA  
1242 C C   . TRP A 161 ? 0.1394 0.1481 0.1543 0.0003  -0.0155 0.0120  218 TRP A C   
1243 O O   . TRP A 161 ? 0.1356 0.1424 0.1470 -0.0005 -0.0127 0.0110  218 TRP A O   
1244 C CB  . TRP A 161 ? 0.1657 0.1757 0.1698 -0.0031 -0.0191 0.0102  218 TRP A CB  
1245 C CG  . TRP A 161 ? 0.1324 0.1425 0.1324 -0.0047 -0.0217 0.0072  218 TRP A CG  
1246 C CD1 . TRP A 161 ? 0.1509 0.1612 0.1451 -0.0060 -0.0264 0.0077  218 TRP A CD1 
1247 C CD2 . TRP A 161 ? 0.1375 0.1461 0.1374 -0.0052 -0.0201 0.0030  218 TRP A CD2 
1248 N NE1 . TRP A 161 ? 0.1857 0.1943 0.1761 -0.0074 -0.0281 0.0033  218 TRP A NE1 
1249 C CE2 . TRP A 161 ? 0.1605 0.1676 0.1546 -0.0068 -0.0242 0.0006  218 TRP A CE2 
1250 C CE3 . TRP A 161 ? 0.1409 0.1487 0.1447 -0.0042 -0.0163 0.0012  218 TRP A CE3 
1251 C CZ2 . TRP A 161 ? 0.1599 0.1635 0.1526 -0.0076 -0.0245 -0.0038 218 TRP A CZ2 
1252 C CZ3 . TRP A 161 ? 0.1647 0.1696 0.1669 -0.0048 -0.0163 -0.0024 218 TRP A CZ3 
1253 C CH2 . TRP A 161 ? 0.1674 0.1697 0.1645 -0.0065 -0.0204 -0.0050 218 TRP A CH2 
1254 N N   . SER A 162 ? 0.1524 0.1606 0.1724 0.0025  -0.0170 0.0145  219 SER A N   
1255 C CA  . SER A 162 ? 0.1275 0.1310 0.1479 0.0037  -0.0160 0.0158  219 SER A CA  
1256 C C   . SER A 162 ? 0.1396 0.1424 0.1643 0.0060  -0.0131 0.0129  219 SER A C   
1257 O O   . SER A 162 ? 0.1448 0.1514 0.1737 0.0076  -0.0119 0.0113  219 SER A O   
1258 C CB  . SER A 162 ? 0.1584 0.1600 0.1813 0.0058  -0.0196 0.0196  219 SER A CB  
1259 O OG  . SER A 162 ? 0.1698 0.1747 0.2010 0.0096  -0.0200 0.0190  219 SER A OG  
1260 N N   . ALA A 163 ? 0.1229 0.1204 0.1461 0.0060  -0.0122 0.0126  220 ALA A N   
1261 C CA  . ALA A 163 ? 0.1406 0.1364 0.1661 0.0084  -0.0101 0.0094  220 ALA A CA  
1262 C C   . ALA A 163 ? 0.1605 0.1568 0.1910 0.0132  -0.0104 0.0091  220 ALA A C   
1263 O O   . ALA A 163 ? 0.1456 0.1449 0.1781 0.0155  -0.0078 0.0066  220 ALA A O   
1264 C CB  . ALA A 163 ? 0.1330 0.1223 0.1564 0.0070  -0.0105 0.0090  220 ALA A CB  
1265 N N   . LEU A 164 ? 0.1281 0.1219 0.1609 0.0150  -0.0132 0.0119  221 LEU A N   
1266 C CA  . LEU A 164 ? 0.1290 0.1243 0.1679 0.0205  -0.0131 0.0115  221 LEU A CA  
1267 C C   . LEU A 164 ? 0.1487 0.1543 0.1929 0.0212  -0.0115 0.0115  221 LEU A C   
1268 O O   . LEU A 164 ? 0.1455 0.1550 0.1942 0.0252  -0.0087 0.0098  221 LEU A O   
1269 C CB  . LEU A 164 ? 0.1478 0.1392 0.1889 0.0225  -0.0172 0.0153  221 LEU A CB  
1270 C CG  . LEU A 164 ? 0.1787 0.1718 0.2273 0.0294  -0.0172 0.0148  221 LEU A CG  
1271 C CD1 . LEU A 164 ? 0.1772 0.1645 0.2246 0.0336  -0.0143 0.0100  221 LEU A CD1 
1272 C CD2 . LEU A 164 ? 0.2339 0.2220 0.2842 0.0313  -0.0221 0.0192  221 LEU A CD2 
1273 N N   A SER A 165 ? 0.1363 0.1466 0.1803 0.0173  -0.0132 0.0134  222 SER A N   
1274 N N   B SER A 165 ? 0.1380 0.1481 0.1817 0.0172  -0.0132 0.0134  222 SER A N   
1275 C CA  A SER A 165 ? 0.1313 0.1505 0.1810 0.0167  -0.0123 0.0136  222 SER A CA  
1276 C CA  B SER A 165 ? 0.1327 0.1518 0.1823 0.0167  -0.0123 0.0136  222 SER A CA  
1277 C C   A SER A 165 ? 0.1429 0.1635 0.1912 0.0162  -0.0078 0.0109  222 SER A C   
1278 C C   B SER A 165 ? 0.1433 0.1638 0.1916 0.0162  -0.0078 0.0109  222 SER A C   
1279 O O   A SER A 165 ? 0.1473 0.1745 0.2015 0.0176  -0.0053 0.0111  222 SER A O   
1280 O O   B SER A 165 ? 0.1463 0.1736 0.2006 0.0176  -0.0054 0.0112  222 SER A O   
1281 C CB  A SER A 165 ? 0.1600 0.1817 0.2081 0.0123  -0.0161 0.0153  222 SER A CB  
1282 C CB  B SER A 165 ? 0.1587 0.1801 0.2064 0.0122  -0.0160 0.0153  222 SER A CB  
1283 O OG  A SER A 165 ? 0.1606 0.1795 0.2014 0.0084  -0.0149 0.0133  222 SER A OG  
1284 O OG  B SER A 165 ? 0.1411 0.1703 0.1955 0.0110  -0.0163 0.0158  222 SER A OG  
1285 N N   . GLY A 166 ? 0.1508 0.1659 0.1917 0.0141  -0.0067 0.0088  223 GLY A N   
1286 C CA  . GLY A 166 ? 0.1347 0.1502 0.1736 0.0143  -0.0030 0.0066  223 GLY A CA  
1287 C C   . GLY A 166 ? 0.1449 0.1605 0.1850 0.0191  -0.0001 0.0050  223 GLY A C   
1288 O O   . GLY A 166 ? 0.1476 0.1679 0.1892 0.0204  0.0032  0.0048  223 GLY A O   
1289 N N   . TYR A 167 ? 0.1436 0.1536 0.1825 0.0220  -0.0013 0.0039  224 TYR A N   
1290 C CA  . TYR A 167 ? 0.1307 0.1398 0.1701 0.0277  0.0011  0.0015  224 TYR A CA  
1291 C C   . TYR A 167 ? 0.1674 0.1859 0.2152 0.0313  0.0035  0.0033  224 TYR A C   
1292 O O   . TYR A 167 ? 0.1432 0.1666 0.1914 0.0342  0.0079  0.0022  224 TYR A O   
1293 C CB  . TYR A 167 ? 0.1441 0.1437 0.1815 0.0300  -0.0017 0.0001  224 TYR A CB  
1294 C CG  . TYR A 167 ? 0.1428 0.1405 0.1807 0.0370  0.0005  -0.0031 224 TYR A CG  
1295 C CD1 . TYR A 167 ? 0.1492 0.1428 0.1801 0.0390  0.0026  -0.0077 224 TYR A CD1 
1296 C CD2 . TYR A 167 ? 0.1415 0.1419 0.1866 0.0423  0.0003  -0.0019 224 TYR A CD2 
1297 C CE1 . TYR A 167 ? 0.1637 0.1552 0.1932 0.0460  0.0049  -0.0115 224 TYR A CE1 
1298 C CE2 . TYR A 167 ? 0.1761 0.1751 0.2214 0.0499  0.0030  -0.0055 224 TYR A CE2 
1299 C CZ  . TYR A 167 ? 0.1976 0.1918 0.2343 0.0518  0.0055  -0.0106 224 TYR A CZ  
1300 O OH  . TYR A 167 ? 0.2194 0.2117 0.2546 0.0600  0.0084  -0.0151 224 TYR A OH  
1301 N N   . GLN A 168 ? 0.1215 0.1438 0.1764 0.0312  0.0006  0.0064  225 GLN A N   
1302 C CA  . GLN A 168 ? 0.1311 0.1638 0.1962 0.0350  0.0025  0.0083  225 GLN A CA  
1303 C C   . GLN A 168 ? 0.1246 0.1671 0.1938 0.0316  0.0055  0.0103  225 GLN A C   
1304 O O   . GLN A 168 ? 0.1537 0.2049 0.2286 0.0349  0.0101  0.0109  225 GLN A O   
1305 C CB  . GLN A 168 ? 0.1418 0.1768 0.2141 0.0354  -0.0024 0.0117  225 GLN A CB  
1306 C CG  . GLN A 168 ? 0.1901 0.2153 0.2600 0.0393  -0.0057 0.0111  225 GLN A CG  
1307 C CD  . GLN A 168 ? 0.2345 0.2574 0.3063 0.0476  -0.0028 0.0081  225 GLN A CD  
1308 O OE1 . GLN A 168 ? 0.2813 0.2932 0.3497 0.0505  -0.0054 0.0068  225 GLN A OE1 
1309 N NE2 . GLN A 168 ? 0.2218 0.2546 0.2988 0.0515  0.0026  0.0070  225 GLN A NE2 
1310 N N   . GLN A 169 ? 0.1253 0.1665 0.1917 0.0252  0.0032  0.0114  226 GLN A N   
1311 C CA  . GLN A 169 ? 0.1245 0.1729 0.1948 0.0214  0.0052  0.0135  226 GLN A CA  
1312 C C   . GLN A 169 ? 0.1352 0.1830 0.2001 0.0226  0.0107  0.0122  226 GLN A C   
1313 O O   . GLN A 169 ? 0.1365 0.1924 0.2065 0.0221  0.0145  0.0148  226 GLN A O   
1314 C CB  . GLN A 169 ? 0.1410 0.1858 0.2083 0.0149  0.0010  0.0141  226 GLN A CB  
1315 C CG  . GLN A 169 ? 0.1443 0.1918 0.2170 0.0131  -0.0046 0.0160  226 GLN A CG  
1316 C CD  . GLN A 169 ? 0.2081 0.2678 0.2944 0.0140  -0.0046 0.0193  226 GLN A CD  
1317 O OE1 . GLN A 169 ? 0.2232 0.2892 0.3153 0.0109  -0.0027 0.0211  226 GLN A OE1 
1318 N NE2 . GLN A 169 ? 0.2053 0.2685 0.2975 0.0182  -0.0066 0.0204  226 GLN A NE2 
1319 N N   . THR A 170 ? 0.1242 0.1629 0.1788 0.0239  0.0109  0.0088  227 THR A N   
1320 C CA  . THR A 170 ? 0.1312 0.1690 0.1792 0.0256  0.0152  0.0074  227 THR A CA  
1321 C C   . THR A 170 ? 0.1547 0.1978 0.2045 0.0320  0.0201  0.0065  227 THR A C   
1322 O O   . THR A 170 ? 0.1441 0.1929 0.1930 0.0330  0.0251  0.0080  227 THR A O   
1323 C CB  . THR A 170 ? 0.1210 0.1485 0.1585 0.0251  0.0132  0.0038  227 THR A CB  
1324 O OG1 . THR A 170 ? 0.1555 0.1798 0.1920 0.0198  0.0097  0.0046  227 THR A OG1 
1325 C CG2 . THR A 170 ? 0.1701 0.1967 0.1999 0.0266  0.0165  0.0026  227 THR A CG2 
1326 N N   . MET A 171 ? 0.1481 0.1896 0.2004 0.0368  0.0190  0.0045  228 MET A N   
1327 C CA  . MET A 171 ? 0.1473 0.1948 0.2023 0.0439  0.0240  0.0034  228 MET A CA  
1328 C C   . MET A 171 ? 0.1300 0.1926 0.1973 0.0435  0.0278  0.0083  228 MET A C   
1329 O O   . MET A 171 ? 0.1663 0.2367 0.2339 0.0470  0.0343  0.0089  228 MET A O   
1330 C CB  . MET A 171 ? 0.1486 0.1906 0.2051 0.0497  0.0217  0.0003  228 MET A CB  
1331 C CG  . MET A 171 ? 0.1787 0.2057 0.2240 0.0499  0.0181  -0.0044 228 MET A CG  
1332 S SD  . MET A 171 ? 0.2078 0.2303 0.2399 0.0541  0.0224  -0.0098 228 MET A SD  
1333 C CE  . MET A 171 ? 0.2671 0.2936 0.3024 0.0649  0.0273  -0.0130 228 MET A CE  
1334 N N   . GLN A 172 ? 0.1485 0.2158 0.2258 0.0390  0.0238  0.0120  229 GLN A N   
1335 C CA  . GLN A 172 ? 0.1553 0.2373 0.2458 0.0369  0.0262  0.0171  229 GLN A CA  
1336 C C   . GLN A 172 ? 0.1507 0.2358 0.2383 0.0324  0.0304  0.0199  229 GLN A C   
1337 O O   . GLN A 172 ? 0.1813 0.2784 0.2755 0.0336  0.0365  0.0232  229 GLN A O   
1338 C CB  . GLN A 172 ? 0.1560 0.2398 0.2552 0.0318  0.0193  0.0198  229 GLN A CB  
1339 C CG  . GLN A 172 ? 0.1642 0.2634 0.2794 0.0291  0.0199  0.0250  229 GLN A CG  
1340 C CD  . GLN A 172 ? 0.1889 0.2886 0.3108 0.0244  0.0117  0.0268  229 GLN A CD  
1341 O OE1 . GLN A 172 ? 0.2254 0.3209 0.3467 0.0275  0.0071  0.0253  229 GLN A OE1 
1342 N NE2 . GLN A 172 ? 0.2542 0.3583 0.3818 0.0169  0.0094  0.0299  229 GLN A NE2 
1343 N N   . MET A 173 ? 0.1592 0.2340 0.2370 0.0275  0.0275  0.0189  230 MET A N   
1344 C CA  . MET A 173 ? 0.1699 0.2460 0.2449 0.0231  0.0305  0.0221  230 MET A CA  
1345 C C   . MET A 173 ? 0.2168 0.2955 0.2845 0.0282  0.0378  0.0216  230 MET A C   
1346 O O   . MET A 173 ? 0.1875 0.2750 0.2586 0.0267  0.0430  0.0264  230 MET A O   
1347 C CB  . MET A 173 ? 0.1842 0.2481 0.2502 0.0183  0.0257  0.0206  230 MET A CB  
1348 C CG  . MET A 173 ? 0.2147 0.2754 0.2731 0.0159  0.0283  0.0225  230 MET A CG  
1349 S SD  . MET A 173 ? 0.2426 0.2891 0.2892 0.0138  0.0233  0.0190  230 MET A SD  
1350 C CE  . MET A 173 ? 0.2197 0.2611 0.2548 0.0203  0.0248  0.0137  230 MET A CE  
1351 N N   . LEU A 174 ? 0.1506 0.2225 0.2085 0.0344  0.0382  0.0161  231 LEU A N   
1352 C CA  . LEU A 174 ? 0.1725 0.2456 0.2209 0.0399  0.0443  0.0144  231 LEU A CA  
1353 C C   . LEU A 174 ? 0.2481 0.3349 0.3048 0.0454  0.0513  0.0160  231 LEU A C   
1354 O O   . LEU A 174 ? 0.2480 0.3400 0.2985 0.0489  0.0582  0.0167  231 LEU A O   
1355 C CB  . LEU A 174 ? 0.1659 0.2263 0.2015 0.0444  0.0415  0.0072  231 LEU A CB  
1356 C CG  . LEU A 174 ? 0.1845 0.2331 0.2116 0.0396  0.0357  0.0055  231 LEU A CG  
1357 C CD1 . LEU A 174 ? 0.2212 0.2590 0.2393 0.0434  0.0324  -0.0012 231 LEU A CD1 
1358 C CD2 . LEU A 174 ? 0.2261 0.2745 0.2454 0.0369  0.0377  0.0083  231 LEU A CD2 
1359 N N   . ASN A 175 ? 0.1786 0.2725 0.2494 0.0465  0.0498  0.0170  232 ASN A N   
1360 C CA  . ASN A 175 ? 0.2426 0.3523 0.3244 0.0518  0.0565  0.0193  232 ASN A CA  
1361 C C   . ASN A 175 ? 0.2520 0.3757 0.3434 0.0461  0.0613  0.0272  232 ASN A C   
1362 O O   . ASN A 175 ? 0.3193 0.4579 0.4179 0.0502  0.0692  0.0300  232 ASN A O   
1363 C CB  . ASN A 175 ? 0.2671 0.3806 0.3624 0.0545  0.0524  0.0187  232 ASN A CB  
1364 C CG  . ASN A 175 ? 0.3783 0.5051 0.4825 0.0637  0.0591  0.0182  232 ASN A CG  
1365 O OD1 . ASN A 175 ? 0.6607 0.7846 0.7541 0.0704  0.0642  0.0137  232 ASN A OD1 
1366 N ND2 . ASN A 175 ? 0.4761 0.6146 0.5976 0.0627  0.0573  0.0218  232 ASN A ND2 
1367 N N   . GLU A 176 ? 0.2461 0.3655 0.3385 0.0368  0.0568  0.0310  233 GLU A N   
1368 C CA  . GLU A 176 ? 0.2754 0.4059 0.3785 0.0297  0.0595  0.0390  233 GLU A CA  
1369 C C   . GLU A 176 ? 0.3397 0.4648 0.4310 0.0258  0.0624  0.0421  233 GLU A C   
1370 O O   . GLU A 176 ? 0.4204 0.5552 0.5189 0.0211  0.0668  0.0494  233 GLU A O   
1371 C CB  . GLU A 176 ? 0.3315 0.4607 0.4461 0.0217  0.0511  0.0412  233 GLU A CB  
1372 C CG  . GLU A 176 ? 0.4798 0.6171 0.6084 0.0246  0.0477  0.0401  233 GLU A CG  
1373 C CD  . GLU A 176 ? 0.7212 0.8547 0.8571 0.0171  0.0382  0.0411  233 GLU A CD  
1374 O OE1 . GLU A 176 ? 0.5890 0.7247 0.7321 0.0195  0.0333  0.0394  233 GLU A OE1 
1375 O OE2 . GLU A 176 ? 0.6192 0.7463 0.7523 0.0092  0.0352  0.0433  233 GLU A OE2 
1376 N N   . GLY A 177 ? 0.3376 0.4478 0.4118 0.0275  0.0598  0.0373  234 GLY A N   
1377 C CA  . GLY A 177 ? 0.3212 0.4253 0.3843 0.0239  0.0612  0.0406  234 GLY A CA  
1378 C C   . GLY A 177 ? 0.2781 0.3669 0.3242 0.0266  0.0571  0.0343  234 GLY A C   
1379 O O   . GLY A 177 ? 0.2951 0.3778 0.3378 0.0309  0.0537  0.0276  234 GLY A O   
1380 N N   . LEU A 178 ? 0.2641 0.3465 0.3000 0.0238  0.0572  0.0371  235 LEU A N   
1381 C CA  . LEU A 178 ? 0.2755 0.3452 0.2956 0.0263  0.0534  0.0320  235 LEU A CA  
1382 C C   . LEU A 178 ? 0.2236 0.2846 0.2416 0.0201  0.0486  0.0353  235 LEU A C   
1383 O O   . LEU A 178 ? 0.2759 0.3370 0.2890 0.0181  0.0514  0.0411  235 LEU A O   
1384 C CB  . LEU A 178 ? 0.4138 0.4851 0.4196 0.0325  0.0592  0.0309  235 LEU A CB  
1385 C CG  . LEU A 178 ? 0.3832 0.4422 0.3732 0.0353  0.0544  0.0249  235 LEU A CG  
1386 C CD1 . LEU A 178 ? 0.3711 0.4231 0.3628 0.0373  0.0486  0.0171  235 LEU A CD1 
1387 C CD2 . LEU A 178 ? 0.4874 0.5483 0.4620 0.0415  0.0597  0.0236  235 LEU A CD2 
1388 N N   . PRO A 179 ? 0.1852 0.2382 0.2063 0.0174  0.0417  0.0319  236 PRO A N   
1389 C CA  . PRO A 179 ? 0.2024 0.2461 0.2204 0.0131  0.0371  0.0337  236 PRO A CA  
1390 C C   . PRO A 179 ? 0.2185 0.2547 0.2222 0.0169  0.0353  0.0304  236 PRO A C   
1391 O O   . PRO A 179 ? 0.2338 0.2701 0.2305 0.0219  0.0361  0.0255  236 PRO A O   
1392 C CB  . PRO A 179 ? 0.2125 0.2520 0.2381 0.0104  0.0311  0.0301  236 PRO A CB  
1393 C CG  . PRO A 179 ? 0.2321 0.2735 0.2572 0.0150  0.0310  0.0244  236 PRO A CG  
1394 C CD  . PRO A 179 ? 0.2224 0.2738 0.2485 0.0189  0.0378  0.0261  236 PRO A CD  
1395 N N   . THR A 180 ? 0.1822 0.2110 0.1818 0.0144  0.0321  0.0329  237 THR A N   
1396 C CA  . THR A 180 ? 0.1666 0.1884 0.1551 0.0176  0.0285  0.0293  237 THR A CA  
1397 C C   . THR A 180 ? 0.1833 0.1988 0.1752 0.0165  0.0223  0.0244  237 THR A C   
1398 O O   . THR A 180 ? 0.1920 0.2036 0.1773 0.0191  0.0190  0.0205  237 THR A O   
1399 C CB  . THR A 180 ? 0.2037 0.2216 0.1843 0.0171  0.0286  0.0351  237 THR A CB  
1400 O OG1 . THR A 180 ? 0.2135 0.2265 0.2010 0.0123  0.0262  0.0394  237 THR A OG1 
1401 C CG2 . THR A 180 ? 0.2237 0.2485 0.1989 0.0183  0.0355  0.0406  237 THR A CG2 
1402 N N   . ALA A 181 ? 0.1475 0.1627 0.1495 0.0128  0.0207  0.0245  238 ALA A N   
1403 C CA  . ALA A 181 ? 0.1393 0.1495 0.1436 0.0121  0.0158  0.0200  238 ALA A CA  
1404 C C   . ALA A 181 ? 0.1638 0.1768 0.1774 0.0094  0.0152  0.0189  238 ALA A C   
1405 O O   . ALA A 181 ? 0.1707 0.1878 0.1908 0.0067  0.0173  0.0227  238 ALA A O   
1406 C CB  . ALA A 181 ? 0.1724 0.1755 0.1756 0.0107  0.0126  0.0217  238 ALA A CB  
1407 N N   . LEU A 182 ? 0.1416 0.1525 0.1560 0.0098  0.0121  0.0142  239 LEU A N   
1408 C CA  . LEU A 182 ? 0.1405 0.1533 0.1617 0.0078  0.0107  0.0128  239 LEU A CA  
1409 C C   . LEU A 182 ? 0.1599 0.1675 0.1805 0.0065  0.0069  0.0100  239 LEU A C   
1410 O O   . LEU A 182 ? 0.1762 0.1817 0.1928 0.0084  0.0057  0.0071  239 LEU A O   
1411 C CB  . LEU A 182 ? 0.1439 0.1602 0.1653 0.0105  0.0116  0.0102  239 LEU A CB  
1412 C CG  . LEU A 182 ? 0.1952 0.2140 0.2231 0.0091  0.0099  0.0095  239 LEU A CG  
1413 C CD1 . LEU A 182 ? 0.1972 0.2217 0.2334 0.0066  0.0109  0.0133  239 LEU A CD1 
1414 C CD2 . LEU A 182 ? 0.2118 0.2317 0.2388 0.0127  0.0105  0.0070  239 LEU A CD2 
1415 N N   . LEU A 183 ? 0.1530 0.1590 0.1778 0.0032  0.0051  0.0107  240 LEU A N   
1416 C CA  . LEU A 183 ? 0.1400 0.1418 0.1638 0.0024  0.0019  0.0074  240 LEU A CA  
1417 C C   . LEU A 183 ? 0.1285 0.1338 0.1549 0.0015  0.0007  0.0060  240 LEU A C   
1418 O O   . LEU A 183 ? 0.1437 0.1528 0.1755 -0.0004 0.0005  0.0080  240 LEU A O   
1419 C CB  . LEU A 183 ? 0.1559 0.1521 0.1811 -0.0005 -0.0002 0.0082  240 LEU A CB  
1420 C CG  . LEU A 183 ? 0.1684 0.1587 0.1904 0.0008  -0.0001 0.0096  240 LEU A CG  
1421 C CD1 . LEU A 183 ? 0.2010 0.1847 0.2257 -0.0028 -0.0022 0.0116  240 LEU A CD1 
1422 C CD2 . LEU A 183 ? 0.1875 0.1749 0.2051 0.0043  -0.0011 0.0056  240 LEU A CD2 
1423 N N   . VAL A 184 ? 0.1242 0.1288 0.1473 0.0028  -0.0001 0.0030  241 VAL A N   
1424 C CA  . VAL A 184 ? 0.1228 0.1300 0.1471 0.0023  -0.0013 0.0024  241 VAL A CA  
1425 C C   . VAL A 184 ? 0.1539 0.1583 0.1749 0.0010  -0.0036 0.0001  241 VAL A C   
1426 O O   . VAL A 184 ? 0.1615 0.1631 0.1789 0.0020  -0.0032 -0.0020 241 VAL A O   
1427 C CB  . VAL A 184 ? 0.1103 0.1189 0.1332 0.0046  -0.0001 0.0018  241 VAL A CB  
1428 C CG1 . VAL A 184 ? 0.1510 0.1614 0.1757 0.0042  -0.0015 0.0024  241 VAL A CG1 
1429 C CG2 . VAL A 184 ? 0.1240 0.1342 0.1476 0.0067  0.0023  0.0029  241 VAL A CG2 
1430 N N   . ALA A 185 ? 0.1280 0.1337 0.1501 -0.0009 -0.0060 0.0004  242 ALA A N   
1431 C CA  . ALA A 185 ? 0.1225 0.1252 0.1397 -0.0020 -0.0084 -0.0021 242 ALA A CA  
1432 C C   . ALA A 185 ? 0.1525 0.1559 0.1644 -0.0007 -0.0073 -0.0033 242 ALA A C   
1433 O O   . ALA A 185 ? 0.1453 0.1468 0.1517 -0.0009 -0.0081 -0.0057 242 ALA A O   
1434 C CB  . ALA A 185 ? 0.1433 0.1472 0.1625 -0.0047 -0.0122 -0.0013 242 ALA A CB  
1435 N N   . ASN A 186 ? 0.1241 0.1300 0.1374 0.0004  -0.0056 -0.0017 243 ASN A N   
1436 C CA  . ASN A 186 ? 0.1255 0.1322 0.1351 0.0009  -0.0041 -0.0023 243 ASN A CA  
1437 C C   . ASN A 186 ? 0.1529 0.1606 0.1654 0.0018  -0.0025 -0.0012 243 ASN A C   
1438 O O   . ASN A 186 ? 0.1442 0.1518 0.1601 0.0027  -0.0025 -0.0004 243 ASN A O   
1439 C CB  . ASN A 186 ? 0.1367 0.1441 0.1421 -0.0005 -0.0056 -0.0011 243 ASN A CB  
1440 C CG  . ASN A 186 ? 0.1409 0.1490 0.1489 -0.0009 -0.0070 0.0022  243 ASN A CG  
1441 O OD1 . ASN A 186 ? 0.1517 0.1600 0.1651 0.0001  -0.0070 0.0031  243 ASN A OD1 
1442 N ND2 . ASN A 186 ? 0.1498 0.1581 0.1536 -0.0019 -0.0080 0.0043  243 ASN A ND2 
1443 N N   . ASP A 187 ? 0.1247 0.1339 0.1359 0.0015  -0.0012 -0.0013 244 ASP A N   
1444 C CA  . ASP A 187 ? 0.1284 0.1380 0.1424 0.0018  -0.0006 -0.0009 244 ASP A CA  
1445 C C   . ASP A 187 ? 0.1156 0.1230 0.1308 0.0012  -0.0020 0.0013  244 ASP A C   
1446 O O   . ASP A 187 ? 0.1286 0.1342 0.1458 0.0021  -0.0023 0.0008  244 ASP A O   
1447 C CB  . ASP A 187 ? 0.1160 0.1289 0.1301 0.0009  0.0009  -0.0011 244 ASP A CB  
1448 C CG  . ASP A 187 ? 0.1543 0.1693 0.1688 0.0029  0.0022  -0.0035 244 ASP A CG  
1449 O OD1 . ASP A 187 ? 0.1656 0.1782 0.1797 0.0046  0.0016  -0.0048 244 ASP A OD1 
1450 O OD2 . ASP A 187 ? 0.1546 0.1742 0.1705 0.0027  0.0038  -0.0037 244 ASP A OD2 
1451 N N   . GLN A 188 ? 0.1232 0.1302 0.1366 -0.0001 -0.0031 0.0035  245 GLN A N   
1452 C CA  . GLN A 188 ? 0.1388 0.1429 0.1539 0.0000  -0.0048 0.0058  245 GLN A CA  
1453 C C   . GLN A 188 ? 0.1217 0.1250 0.1402 0.0027  -0.0054 0.0050  245 GLN A C   
1454 O O   . GLN A 188 ? 0.1479 0.1484 0.1683 0.0045  -0.0056 0.0046  245 GLN A O   
1455 C CB  . GLN A 188 ? 0.1363 0.1401 0.1484 -0.0014 -0.0065 0.0090  245 GLN A CB  
1456 C CG  . GLN A 188 ? 0.1688 0.1738 0.1774 -0.0041 -0.0050 0.0107  245 GLN A CG  
1457 C CD  . GLN A 188 ? 0.1747 0.1789 0.1786 -0.0055 -0.0066 0.0148  245 GLN A CD  
1458 O OE1 . GLN A 188 ? 0.1556 0.1625 0.1538 -0.0061 -0.0061 0.0146  245 GLN A OE1 
1459 N NE2 . GLN A 188 ? 0.1572 0.1570 0.1628 -0.0058 -0.0087 0.0183  245 GLN A NE2 
1460 N N   . MET A 189 ? 0.1256 0.1316 0.1450 0.0032  -0.0056 0.0047  246 MET A N   
1461 C CA  . MET A 189 ? 0.1218 0.1292 0.1455 0.0055  -0.0052 0.0046  246 MET A CA  
1462 C C   . MET A 189 ? 0.1429 0.1497 0.1664 0.0071  -0.0028 0.0025  246 MET A C   
1463 O O   . MET A 189 ? 0.1366 0.1433 0.1619 0.0098  -0.0018 0.0021  246 MET A O   
1464 C CB  . MET A 189 ? 0.1072 0.1181 0.1332 0.0044  -0.0060 0.0051  246 MET A CB  
1465 C CG  . MET A 189 ? 0.1144 0.1266 0.1411 0.0034  -0.0094 0.0072  246 MET A CG  
1466 S SD  . MET A 189 ? 0.1471 0.1636 0.1783 0.0015  -0.0118 0.0078  246 MET A SD  
1467 C CE  . MET A 189 ? 0.1742 0.1874 0.2001 -0.0008 -0.0107 0.0047  246 MET A CE  
1468 N N   . ALA A 190 ? 0.1352 0.1417 0.1559 0.0061  -0.0020 0.0010  247 ALA A N   
1469 C CA  . ALA A 190 ? 0.1178 0.1236 0.1373 0.0077  -0.0006 -0.0007 247 ALA A CA  
1470 C C   . ALA A 190 ? 0.1209 0.1237 0.1396 0.0089  -0.0013 -0.0019 247 ALA A C   
1471 O O   . ALA A 190 ? 0.1229 0.1247 0.1401 0.0113  -0.0005 -0.0034 247 ALA A O   
1472 C CB  . ALA A 190 ? 0.1299 0.1362 0.1475 0.0068  -0.0003 -0.0017 247 ALA A CB  
1473 N N   . LEU A 191 ? 0.1252 0.1258 0.1442 0.0071  -0.0028 -0.0013 248 LEU A N   
1474 C CA  . LEU A 191 ? 0.1363 0.1320 0.1550 0.0076  -0.0043 -0.0025 248 LEU A CA  
1475 C C   . LEU A 191 ? 0.1396 0.1329 0.1588 0.0114  -0.0041 -0.0031 248 LEU A C   
1476 O O   . LEU A 191 ? 0.1376 0.1275 0.1546 0.0139  -0.0042 -0.0060 248 LEU A O   
1477 C CB  . LEU A 191 ? 0.1230 0.1166 0.1427 0.0043  -0.0060 -0.0002 248 LEU A CB  
1478 C CG  . LEU A 191 ? 0.1469 0.1334 0.1669 0.0038  -0.0083 -0.0006 248 LEU A CG  
1479 C CD1 . LEU A 191 ? 0.1766 0.1626 0.1962 0.0025  -0.0094 -0.0035 248 LEU A CD1 
1480 C CD2 . LEU A 191 ? 0.1907 0.1748 0.2119 0.0004  -0.0097 0.0034  248 LEU A CD2 
1481 N N   . GLY A 192 ? 0.1260 0.1214 0.1481 0.0122  -0.0039 -0.0008 249 GLY A N   
1482 C CA  . GLY A 192 ? 0.1499 0.1452 0.1744 0.0165  -0.0032 -0.0011 249 GLY A CA  
1483 C C   . GLY A 192 ? 0.1406 0.1400 0.1644 0.0193  0.0000  -0.0027 249 GLY A C   
1484 O O   . GLY A 192 ? 0.1414 0.1397 0.1645 0.0236  0.0015  -0.0048 249 GLY A O   
1485 N N   . ALA A 193 ? 0.1235 0.1275 0.1471 0.0170  0.0014  -0.0016 250 ALA A N   
1486 C CA  . ALA A 193 ? 0.1251 0.1326 0.1473 0.0190  0.0045  -0.0020 250 ALA A CA  
1487 C C   . ALA A 193 ? 0.1384 0.1417 0.1539 0.0211  0.0048  -0.0054 250 ALA A C   
1488 O O   . ALA A 193 ? 0.1495 0.1539 0.1624 0.0249  0.0074  -0.0067 250 ALA A O   
1489 C CB  . ALA A 193 ? 0.1409 0.1516 0.1638 0.0157  0.0049  0.0000  250 ALA A CB  
1490 N N   . LEU A 194 ? 0.1302 0.1294 0.1429 0.0187  0.0020  -0.0070 251 LEU A N   
1491 C CA  . LEU A 194 ? 0.1346 0.1297 0.1414 0.0201  0.0008  -0.0105 251 LEU A CA  
1492 C C   . LEU A 194 ? 0.1462 0.1361 0.1509 0.0238  0.0004  -0.0136 251 LEU A C   
1493 O O   . LEU A 194 ? 0.1574 0.1454 0.1559 0.0272  0.0012  -0.0168 251 LEU A O   
1494 C CB  . LEU A 194 ? 0.1262 0.1193 0.1331 0.0163  -0.0026 -0.0111 251 LEU A CB  
1495 C CG  . LEU A 194 ? 0.1424 0.1400 0.1503 0.0141  -0.0023 -0.0093 251 LEU A CG  
1496 C CD1 . LEU A 194 ? 0.1495 0.1471 0.1598 0.0107  -0.0050 -0.0096 251 LEU A CD1 
1497 C CD2 . LEU A 194 ? 0.1499 0.1488 0.1528 0.0163  -0.0014 -0.0097 251 LEU A CD2 
1498 N N   . ARG A 195 ? 0.1336 0.1203 0.1426 0.0235  -0.0011 -0.0129 252 ARG A N   
1499 C CA  . ARG A 195 ? 0.1450 0.1252 0.1525 0.0277  -0.0018 -0.0160 252 ARG A CA  
1500 C C   . ARG A 195 ? 0.1599 0.1446 0.1668 0.0337  0.0027  -0.0168 252 ARG A C   
1501 O O   . ARG A 195 ? 0.1789 0.1597 0.1800 0.0384  0.0035  -0.0212 252 ARG A O   
1502 C CB  . ARG A 195 ? 0.1519 0.1277 0.1646 0.0265  -0.0044 -0.0138 252 ARG A CB  
1503 C CG  . ARG A 195 ? 0.1798 0.1483 0.1920 0.0320  -0.0050 -0.0168 252 ARG A CG  
1504 C CD  . ARG A 195 ? 0.1916 0.1552 0.2091 0.0313  -0.0079 -0.0136 252 ARG A CD  
1505 N NE  . ARG A 195 ? 0.2077 0.1661 0.2258 0.0385  -0.0076 -0.0164 252 ARG A NE  
1506 C CZ  . ARG A 195 ? 0.2341 0.1935 0.2583 0.0419  -0.0078 -0.0136 252 ARG A CZ  
1507 N NH1 . ARG A 195 ? 0.2199 0.1838 0.2492 0.0382  -0.0093 -0.0078 252 ARG A NH1 
1508 N NH2 . ARG A 195 ? 0.2597 0.2159 0.2846 0.0498  -0.0067 -0.0169 252 ARG A NH2 
1509 N N   . ALA A 196 ? 0.1565 0.1500 0.1693 0.0335  0.0056  -0.0127 253 ALA A N   
1510 C CA  . ALA A 196 ? 0.1556 0.1560 0.1701 0.0386  0.0105  -0.0124 253 ALA A CA  
1511 C C   . ALA A 196 ? 0.1684 0.1708 0.1747 0.0404  0.0138  -0.0142 253 ALA A C   
1512 O O   . ALA A 196 ? 0.1739 0.1775 0.1764 0.0461  0.0173  -0.0168 253 ALA A O   
1513 C CB  . ALA A 196 ? 0.1676 0.1776 0.1912 0.0364  0.0121  -0.0072 253 ALA A CB  
1514 N N   . LEU A 197 ? 0.1643 0.1672 0.1673 0.0360  0.0126  -0.0128 254 LEU A N   
1515 C CA  . LEU A 197 ? 0.1606 0.1647 0.1548 0.0376  0.0150  -0.0137 254 LEU A CA  
1516 C C   . LEU A 197 ? 0.1631 0.1590 0.1473 0.0410  0.0128  -0.0199 254 LEU A C   
1517 O O   . LEU A 197 ? 0.2007 0.1976 0.1770 0.0459  0.0161  -0.0223 254 LEU A O   
1518 C CB  . LEU A 197 ? 0.1482 0.1534 0.1417 0.0326  0.0132  -0.0108 254 LEU A CB  
1519 C CG  . LEU A 197 ? 0.1668 0.1786 0.1681 0.0294  0.0153  -0.0053 254 LEU A CG  
1520 C CD1 . LEU A 197 ? 0.1628 0.1729 0.1646 0.0248  0.0122  -0.0036 254 LEU A CD1 
1521 C CD2 . LEU A 197 ? 0.1829 0.2015 0.1831 0.0313  0.0208  -0.0021 254 LEU A CD2 
1522 N N   . SER A 198 ? 0.1748 0.1628 0.1593 0.0384  0.0072  -0.0226 255 SER A N   
1523 C CA  . SER A 198 ? 0.1828 0.1617 0.1587 0.0406  0.0037  -0.0289 255 SER A CA  
1524 C C   . SER A 198 ? 0.2201 0.1953 0.1930 0.0475  0.0061  -0.0331 255 SER A C   
1525 O O   . SER A 198 ? 0.2427 0.2147 0.2049 0.0522  0.0070  -0.0381 255 SER A O   
1526 C CB  . SER A 198 ? 0.2069 0.1789 0.1866 0.0355  -0.0025 -0.0297 255 SER A CB  
1527 O OG  . SER A 198 ? 0.2447 0.2067 0.2172 0.0369  -0.0068 -0.0360 255 SER A OG  
1528 N N   . GLU A 199 ? 0.2117 0.1874 0.1934 0.0489  0.0072  -0.0314 256 GLU A N   
1529 C CA  . GLU A 199 ? 0.2094 0.1811 0.1897 0.0564  0.0091  -0.0356 256 GLU A CA  
1530 C C   . GLU A 199 ? 0.2237 0.2053 0.2013 0.0625  0.0167  -0.0353 256 GLU A C   
1531 O O   . GLU A 199 ? 0.2788 0.2574 0.2507 0.0700  0.0192  -0.0405 256 GLU A O   
1532 C CB  . GLU A 199 ? 0.2388 0.2086 0.2302 0.0562  0.0073  -0.0330 256 GLU A CB  
1533 C CG  . GLU A 199 ? 0.2836 0.2419 0.2758 0.0507  0.0002  -0.0336 256 GLU A CG  
1534 C CD  . GLU A 199 ? 0.3104 0.2649 0.3117 0.0505  -0.0022 -0.0305 256 GLU A CD  
1535 O OE1 . GLU A 199 ? 0.3071 0.2684 0.3151 0.0545  0.0010  -0.0278 256 GLU A OE1 
1536 O OE2 . GLU A 199 ? 0.2849 0.2298 0.2867 0.0460  -0.0075 -0.0303 256 GLU A OE2 
1537 N N   . SER A 200 ? 0.2142 0.2073 0.1955 0.0594  0.0205  -0.0293 257 SER A N   
1538 C CA  . SER A 200 ? 0.2332 0.2369 0.2119 0.0636  0.0280  -0.0276 257 SER A CA  
1539 C C   . SER A 200 ? 0.2595 0.2611 0.2229 0.0648  0.0289  -0.0303 257 SER A C   
1540 O O   . SER A 200 ? 0.3275 0.3376 0.2865 0.0682  0.0356  -0.0285 257 SER A O   
1541 C CB  . SER A 200 ? 0.2598 0.2754 0.2493 0.0587  0.0309  -0.0195 257 SER A CB  
1542 O OG  . SER A 200 ? 0.2457 0.2640 0.2484 0.0581  0.0297  -0.0171 257 SER A OG  
1543 N N   . GLY A 201 ? 0.2505 0.2424 0.2064 0.0616  0.0224  -0.0338 258 GLY A N   
1544 C CA  . GLY A 201 ? 0.2525 0.2423 0.1934 0.0628  0.0221  -0.0364 258 GLY A CA  
1545 C C   . GLY A 201 ? 0.2819 0.2789 0.2222 0.0582  0.0233  -0.0297 258 GLY A C   
1546 O O   . GLY A 201 ? 0.3176 0.3153 0.2453 0.0601  0.0245  -0.0301 258 GLY A O   
1547 N N   . LEU A 202 ? 0.2609 0.2624 0.2135 0.0525  0.0227  -0.0237 259 LEU A N   
1548 C CA  . LEU A 202 ? 0.2349 0.2408 0.1877 0.0480  0.0228  -0.0177 259 LEU A CA  
1549 C C   . LEU A 202 ? 0.2610 0.2605 0.2136 0.0434  0.0153  -0.0190 259 LEU A C   
1550 O O   . LEU A 202 ? 0.2681 0.2657 0.2303 0.0397  0.0120  -0.0188 259 LEU A O   
1551 C CB  . LEU A 202 ? 0.2240 0.2381 0.1900 0.0447  0.0264  -0.0109 259 LEU A CB  
1552 C CG  . LEU A 202 ? 0.2481 0.2714 0.2154 0.0487  0.0344  -0.0082 259 LEU A CG  
1553 C CD1 . LEU A 202 ? 0.2825 0.3133 0.2652 0.0454  0.0364  -0.0030 259 LEU A CD1 
1554 C CD2 . LEU A 202 ? 0.2604 0.2873 0.2178 0.0489  0.0380  -0.0042 259 LEU A CD2 
1555 N N   . ARG A 203 ? 0.2398 0.2372 0.1818 0.0436  0.0127  -0.0198 260 ARG A N   
1556 C CA  . ARG A 203 ? 0.2422 0.2352 0.1848 0.0398  0.0054  -0.0212 260 ARG A CA  
1557 C C   . ARG A 203 ? 0.2071 0.2040 0.1596 0.0352  0.0049  -0.0153 260 ARG A C   
1558 O O   . ARG A 203 ? 0.2119 0.2131 0.1646 0.0348  0.0085  -0.0099 260 ARG A O   
1559 C CB  . ARG A 203 ? 0.2324 0.2229 0.1613 0.0418  0.0020  -0.0235 260 ARG A CB  
1560 C CG  . ARG A 203 ? 0.3277 0.3118 0.2454 0.0461  0.0003  -0.0313 260 ARG A CG  
1561 C CD  . ARG A 203 ? 0.4653 0.4463 0.3684 0.0475  -0.0048 -0.0342 260 ARG A CD  
1562 N NE  . ARG A 203 ? 0.7105 0.6970 0.6086 0.0476  -0.0029 -0.0276 260 ARG A NE  
1563 C CZ  . ARG A 203 ? 0.8160 0.8073 0.7074 0.0507  0.0045  -0.0234 260 ARG A CZ  
1564 N NH1 . ARG A 203 ? 0.8247 0.8174 0.7134 0.0549  0.0110  -0.0255 260 ARG A NH1 
1565 N NH2 . ARG A 203 ? 0.6452 0.6402 0.5332 0.0498  0.0053  -0.0165 260 ARG A NH2 
1566 N N   . VAL A 204 ? 0.1867 0.1817 0.1472 0.0315  0.0006  -0.0164 261 VAL A N   
1567 C CA  . VAL A 204 ? 0.1866 0.1844 0.1554 0.0278  -0.0004 -0.0124 261 VAL A CA  
1568 C C   . VAL A 204 ? 0.2130 0.2098 0.1803 0.0265  -0.0061 -0.0137 261 VAL A C   
1569 O O   . VAL A 204 ? 0.2206 0.2147 0.1884 0.0254  -0.0105 -0.0178 261 VAL A O   
1570 C CB  . VAL A 204 ? 0.1649 0.1629 0.1443 0.0249  -0.0001 -0.0122 261 VAL A CB  
1571 C CG1 . VAL A 204 ? 0.1834 0.1837 0.1696 0.0216  -0.0016 -0.0093 261 VAL A CG1 
1572 C CG2 . VAL A 204 ? 0.1858 0.1863 0.1686 0.0261  0.0048  -0.0103 261 VAL A CG2 
1573 N N   . PRO A 205 ? 0.1946 0.1935 0.1609 0.0266  -0.0068 -0.0100 262 PRO A N   
1574 C CA  . PRO A 205 ? 0.1581 0.1589 0.1249 0.0268  -0.0027 -0.0045 262 PRO A CA  
1575 C C   . PRO A 205 ? 0.2069 0.2076 0.1626 0.0298  -0.0005 -0.0020 262 PRO A C   
1576 O O   . PRO A 205 ? 0.2615 0.2633 0.2178 0.0293  0.0025  0.0035  262 PRO A O   
1577 C CB  . PRO A 205 ? 0.1783 0.1797 0.1506 0.0255  -0.0059 -0.0025 262 PRO A CB  
1578 C CG  . PRO A 205 ? 0.1949 0.1964 0.1639 0.0263  -0.0115 -0.0055 262 PRO A CG  
1579 C CD  . PRO A 205 ? 0.2014 0.2012 0.1692 0.0257  -0.0125 -0.0108 262 PRO A CD  
1580 N N   . ALA A 206 ? 0.2071 0.2063 0.1522 0.0326  -0.0019 -0.0055 263 ALA A N   
1581 C CA  . ALA A 206 ? 0.2459 0.2454 0.1784 0.0356  0.0000  -0.0025 263 ALA A CA  
1582 C C   . ALA A 206 ? 0.2670 0.2699 0.1991 0.0362  0.0079  0.0020  263 ALA A C   
1583 O O   . ALA A 206 ? 0.2913 0.2956 0.2183 0.0366  0.0105  0.0081  263 ALA A O   
1584 C CB  . ALA A 206 ? 0.2748 0.2716 0.1946 0.0387  -0.0032 -0.0083 263 ALA A CB  
1585 N N   . GLN A 207 ? 0.2172 0.2221 0.1560 0.0361  0.0117  -0.0001 264 GLN A N   
1586 C CA  . GLN A 207 ? 0.1989 0.2092 0.1402 0.0366  0.0192  0.0041  264 GLN A CA  
1587 C C   . GLN A 207 ? 0.2422 0.2550 0.1982 0.0324  0.0206  0.0076  264 GLN A C   
1588 O O   . GLN A 207 ? 0.2072 0.2243 0.1668 0.0309  0.0251  0.0136  264 GLN A O   
1589 C CB  . GLN A 207 ? 0.2211 0.2329 0.1585 0.0409  0.0228  -0.0009 264 GLN A CB  
1590 C CG  . GLN A 207 ? 0.2836 0.2931 0.2040 0.0456  0.0225  -0.0043 264 GLN A CG  
1591 C CD  . GLN A 207 ? 0.3810 0.3907 0.2963 0.0509  0.0262  -0.0102 264 GLN A CD  
1592 O OE1 . GLN A 207 ? 0.2987 0.3037 0.2179 0.0516  0.0229  -0.0164 264 GLN A OE1 
1593 N NE2 . GLN A 207 ? 0.4179 0.4331 0.3244 0.0550  0.0332  -0.0081 264 GLN A NE2 
1594 N N   . VAL A 208 ? 0.1857 0.1960 0.1500 0.0303  0.0167  0.0043  265 VAL A N   
1595 C CA  . VAL A 208 ? 0.1897 0.2015 0.1661 0.0264  0.0170  0.0070  265 VAL A CA  
1596 C C   . VAL A 208 ? 0.1819 0.1896 0.1619 0.0241  0.0115  0.0050  265 VAL A C   
1597 O O   . VAL A 208 ? 0.1780 0.1835 0.1569 0.0248  0.0082  0.0003  265 VAL A O   
1598 C CB  . VAL A 208 ? 0.1587 0.1740 0.1427 0.0267  0.0194  0.0053  265 VAL A CB  
1599 C CG1 . VAL A 208 ? 0.1944 0.2109 0.1893 0.0225  0.0186  0.0078  265 VAL A CG1 
1600 C CG2 . VAL A 208 ? 0.1771 0.1985 0.1589 0.0298  0.0257  0.0072  265 VAL A CG2 
1601 N N   . SER A 209 ? 0.1561 0.1627 0.1406 0.0214  0.0106  0.0085  266 SER A N   
1602 C CA  . SER A 209 ? 0.1409 0.1449 0.1299 0.0198  0.0066  0.0067  266 SER A CA  
1603 C C   . SER A 209 ? 0.1442 0.1492 0.1416 0.0173  0.0070  0.0057  266 SER A C   
1604 O O   . SER A 209 ? 0.1725 0.1798 0.1738 0.0158  0.0096  0.0081  266 SER A O   
1605 C CB  . SER A 209 ? 0.1463 0.1473 0.1352 0.0193  0.0053  0.0103  266 SER A CB  
1606 O OG  . SER A 209 ? 0.1656 0.1653 0.1466 0.0219  0.0034  0.0112  266 SER A OG  
1607 N N   . VAL A 210 ? 0.1363 0.1406 0.1366 0.0165  0.0042  0.0025  267 VAL A N   
1608 C CA  . VAL A 210 ? 0.1323 0.1373 0.1386 0.0143  0.0041  0.0016  267 VAL A CA  
1609 C C   . VAL A 210 ? 0.1405 0.1440 0.1488 0.0132  0.0020  0.0005  267 VAL A C   
1610 O O   . VAL A 210 ? 0.1488 0.1527 0.1561 0.0143  0.0002  -0.0011 267 VAL A O   
1611 C CB  . VAL A 210 ? 0.1373 0.1429 0.1440 0.0147  0.0038  -0.0011 267 VAL A CB  
1612 C CG1 . VAL A 210 ? 0.1362 0.1425 0.1481 0.0124  0.0033  -0.0011 267 VAL A CG1 
1613 C CG2 . VAL A 210 ? 0.1664 0.1732 0.1706 0.0171  0.0062  -0.0010 267 VAL A CG2 
1614 N N   . VAL A 211 ? 0.1374 0.1400 0.1490 0.0113  0.0021  0.0011  268 VAL A N   
1615 C CA  . VAL A 211 ? 0.1453 0.1468 0.1581 0.0110  0.0007  -0.0007 268 VAL A CA  
1616 C C   . VAL A 211 ? 0.1279 0.1306 0.1426 0.0089  0.0006  -0.0018 268 VAL A C   
1617 O O   . VAL A 211 ? 0.1527 0.1552 0.1690 0.0073  0.0008  -0.0004 268 VAL A O   
1618 C CB  . VAL A 211 ? 0.1326 0.1297 0.1452 0.0112  0.0001  0.0003  268 VAL A CB  
1619 C CG1 . VAL A 211 ? 0.1789 0.1746 0.1919 0.0123  -0.0008 -0.0026 268 VAL A CG1 
1620 C CG2 . VAL A 211 ? 0.1917 0.1871 0.2017 0.0133  -0.0001 0.0026  268 VAL A CG2 
1621 N N   . GLY A 212 ? 0.1117 0.1162 0.1265 0.0089  0.0003  -0.0036 269 GLY A N   
1622 C CA  . GLY A 212 ? 0.1356 0.1410 0.1505 0.0071  0.0002  -0.0041 269 GLY A CA  
1623 C C   . GLY A 212 ? 0.1537 0.1576 0.1669 0.0071  -0.0001 -0.0058 269 GLY A C   
1624 O O   . GLY A 212 ? 0.1535 0.1541 0.1661 0.0084  -0.0004 -0.0067 269 GLY A O   
1625 N N   . TYR A 213 ? 0.1383 0.1438 0.1497 0.0059  0.0000  -0.0064 270 TYR A N   
1626 C CA  . TYR A 213 ? 0.1376 0.1415 0.1453 0.0063  0.0000  -0.0089 270 TYR A CA  
1627 C C   . TYR A 213 ? 0.1640 0.1721 0.1692 0.0057  0.0014  -0.0088 270 TYR A C   
1628 O O   . TYR A 213 ? 0.1673 0.1764 0.1721 0.0035  0.0005  -0.0066 270 TYR A O   
1629 C CB  . TYR A 213 ? 0.1517 0.1514 0.1579 0.0046  -0.0025 -0.0091 270 TYR A CB  
1630 C CG  . TYR A 213 ? 0.1365 0.1311 0.1388 0.0055  -0.0036 -0.0127 270 TYR A CG  
1631 C CD1 . TYR A 213 ? 0.1472 0.1422 0.1434 0.0065  -0.0031 -0.0157 270 TYR A CD1 
1632 C CD2 . TYR A 213 ? 0.1812 0.1698 0.1852 0.0053  -0.0054 -0.0129 270 TYR A CD2 
1633 C CE1 . TYR A 213 ? 0.1781 0.1669 0.1695 0.0080  -0.0043 -0.0200 270 TYR A CE1 
1634 C CE2 . TYR A 213 ? 0.1752 0.1567 0.1753 0.0061  -0.0071 -0.0167 270 TYR A CE2 
1635 C CZ  . TYR A 213 ? 0.2033 0.1846 0.1968 0.0078  -0.0068 -0.0208 270 TYR A CZ  
1636 O OH  . TYR A 213 ? 0.2179 0.1909 0.2066 0.0093  -0.0088 -0.0255 270 TYR A OH  
1637 N N   . ASP A 214 ? 0.1524 0.1633 0.1562 0.0077  0.0036  -0.0108 271 ASP A N   
1638 C CA  . ASP A 214 ? 0.1414 0.1574 0.1422 0.0073  0.0061  -0.0107 271 ASP A CA  
1639 C C   . ASP A 214 ? 0.1554 0.1782 0.1614 0.0086  0.0089  -0.0103 271 ASP A C   
1640 O O   . ASP A 214 ? 0.1407 0.1686 0.1455 0.0104  0.0120  -0.0117 271 ASP A O   
1641 C CB  . ASP A 214 ? 0.1683 0.1856 0.1675 0.0039  0.0055  -0.0072 271 ASP A CB  
1642 C CG  . ASP A 214 ? 0.1817 0.1949 0.1749 0.0028  0.0028  -0.0074 271 ASP A CG  
1643 O OD1 . ASP A 214 ? 0.1782 0.1879 0.1669 0.0042  0.0018  -0.0109 271 ASP A OD1 
1644 O OD2 . ASP A 214 ? 0.1709 0.1837 0.1642 0.0006  0.0011  -0.0041 271 ASP A OD2 
1645 N N   . ASP A 215 ? 0.1336 0.1575 0.1456 0.0076  0.0077  -0.0085 272 ASP A N   
1646 C CA  . ASP A 215 ? 0.1209 0.1520 0.1389 0.0069  0.0091  -0.0071 272 ASP A CA  
1647 C C   . ASP A 215 ? 0.1114 0.1474 0.1286 0.0037  0.0114  -0.0043 272 ASP A C   
1648 O O   . ASP A 215 ? 0.1407 0.1848 0.1605 0.0040  0.0148  -0.0039 272 ASP A O   
1649 C CB  . ASP A 215 ? 0.1128 0.1489 0.1348 0.0109  0.0106  -0.0094 272 ASP A CB  
1650 C CG  . ASP A 215 ? 0.1483 0.1917 0.1788 0.0099  0.0102  -0.0079 272 ASP A CG  
1651 O OD1 . ASP A 215 ? 0.1695 0.2109 0.2018 0.0068  0.0076  -0.0061 272 ASP A OD1 
1652 O OD2 . ASP A 215 ? 0.2140 0.2655 0.2496 0.0125  0.0123  -0.0087 272 ASP A OD2 
1653 N N   . THR A 216 ? 0.1352 0.1666 0.1493 0.0008  0.0097  -0.0019 273 THR A N   
1654 C CA  . THR A 216 ? 0.1378 0.1724 0.1515 -0.0028 0.0112  0.0021  273 THR A CA  
1655 C C   . THR A 216 ? 0.1236 0.1621 0.1458 -0.0056 0.0108  0.0042  273 THR A C   
1656 O O   . THR A 216 ? 0.1439 0.1812 0.1707 -0.0046 0.0085  0.0023  273 THR A O   
1657 C CB  . THR A 216 ? 0.1306 0.1588 0.1391 -0.0047 0.0087  0.0046  273 THR A CB  
1658 O OG1 . THR A 216 ? 0.1522 0.1741 0.1622 -0.0038 0.0053  0.0034  273 THR A OG1 
1659 C CG2 . THR A 216 ? 0.1388 0.1664 0.1383 -0.0034 0.0095  0.0035  273 THR A CG2 
1660 N N   . GLU A 217 ? 0.1069 0.1504 0.1309 -0.0092 0.0129  0.0081  274 GLU A N   
1661 C CA  . GLU A 217 ? 0.1345 0.1847 0.1680 -0.0123 0.0133  0.0100  274 GLU A CA  
1662 C C   . GLU A 217 ? 0.1394 0.1832 0.1774 -0.0142 0.0082  0.0095  274 GLU A C   
1663 O O   . GLU A 217 ? 0.1348 0.1830 0.1802 -0.0145 0.0068  0.0082  274 GLU A O   
1664 C CB  . GLU A 217 ? 0.1540 0.2097 0.1885 -0.0170 0.0164  0.0157  274 GLU A CB  
1665 C CG  . GLU A 217 ? 0.1464 0.2135 0.1918 -0.0200 0.0186  0.0178  274 GLU A CG  
1666 C CD  . GLU A 217 ? 0.2011 0.2807 0.2483 -0.0160 0.0242  0.0159  274 GLU A CD  
1667 O OE1 . GLU A 217 ? 0.2842 0.3658 0.3230 -0.0139 0.0285  0.0162  274 GLU A OE1 
1668 O OE2 . GLU A 217 ? 0.2956 0.3833 0.3525 -0.0148 0.0240  0.0142  274 GLU A OE2 
1669 N N   . ASP A 218 ? 0.1203 0.1541 0.1540 -0.0151 0.0053  0.0104  275 ASP A N   
1670 C CA  . ASP A 218 ? 0.1235 0.1503 0.1601 -0.0162 0.0008  0.0092  275 ASP A CA  
1671 C C   . ASP A 218 ? 0.1417 0.1671 0.1781 -0.0121 -0.0012 0.0044  275 ASP A C   
1672 O O   . ASP A 218 ? 0.1300 0.1517 0.1686 -0.0129 -0.0047 0.0028  275 ASP A O   
1673 C CB  . ASP A 218 ? 0.1598 0.1761 0.1918 -0.0164 -0.0016 0.0105  275 ASP A CB  
1674 C CG  . ASP A 218 ? 0.1812 0.1957 0.2127 -0.0207 -0.0011 0.0162  275 ASP A CG  
1675 O OD1 . ASP A 218 ? 0.1828 0.2025 0.2189 -0.0253 0.0003  0.0198  275 ASP A OD1 
1676 O OD2 . ASP A 218 ? 0.2040 0.2115 0.2307 -0.0195 -0.0024 0.0177  275 ASP A OD2 
1677 N N   . SER A 219 ? 0.1232 0.1504 0.1561 -0.0079 0.0007  0.0022  276 SER A N   
1678 C CA  . SER A 219 ? 0.1514 0.1749 0.1821 -0.0042 -0.0011 -0.0010 276 SER A CA  
1679 C C   . SER A 219 ? 0.1390 0.1656 0.1739 -0.0036 -0.0033 -0.0028 276 SER A C   
1680 O O   . SER A 219 ? 0.1209 0.1430 0.1532 -0.0018 -0.0058 -0.0049 276 SER A O   
1681 C CB  . SER A 219 ? 0.1302 0.1542 0.1570 -0.0008 0.0011  -0.0022 276 SER A CB  
1682 O OG  . SER A 219 ? 0.1723 0.1930 0.1949 -0.0016 0.0019  -0.0006 276 SER A OG  
1683 N N   . ALA A 220 ? 0.1210 0.1561 0.1623 -0.0051 -0.0025 -0.0020 277 ALA A N   
1684 C CA  . ALA A 220 ? 0.0974 0.1367 0.1441 -0.0050 -0.0057 -0.0034 277 ALA A CA  
1685 C C   . ALA A 220 ? 0.1238 0.1581 0.1716 -0.0086 -0.0102 -0.0039 277 ALA A C   
1686 O O   . ALA A 220 ? 0.1379 0.1735 0.1881 -0.0085 -0.0142 -0.0058 277 ALA A O   
1687 C CB  . ALA A 220 ? 0.1249 0.1765 0.1805 -0.0059 -0.0036 -0.0020 277 ALA A CB  
1688 N N   . CYS A 221 ? 0.1160 0.1435 0.1616 -0.0116 -0.0103 -0.0024 278 CYS A N   
1689 C CA  . CYS A 221 ? 0.1068 0.1270 0.1527 -0.0147 -0.0150 -0.0035 278 CYS A CA  
1690 C C   . CYS A 221 ? 0.1125 0.1214 0.1500 -0.0116 -0.0159 -0.0057 278 CYS A C   
1691 O O   . CYS A 221 ? 0.1466 0.1473 0.1832 -0.0134 -0.0193 -0.0069 278 CYS A O   
1692 C CB  . CYS A 221 ? 0.1542 0.1752 0.2062 -0.0210 -0.0150 0.0004  278 CYS A CB  
1693 S SG  . CYS A 221 ? 0.1681 0.2038 0.2328 -0.0256 -0.0149 0.0029  278 CYS A SG  
1694 N N   . PHE A 222 ? 0.1541 0.1317 0.1355 -0.0268 -0.0004 0.0054  279 PHE A N   
1695 C CA  . PHE A 222 ? 0.1408 0.1048 0.1183 -0.0150 -0.0030 0.0097  279 PHE A CA  
1696 C C   . PHE A 222 ? 0.1556 0.1269 0.1382 -0.0206 -0.0031 0.0077  279 PHE A C   
1697 O O   . PHE A 222 ? 0.1794 0.1737 0.1721 -0.0280 -0.0046 0.0021  279 PHE A O   
1698 C CB  . PHE A 222 ? 0.1531 0.1343 0.1517 -0.0013 -0.0090 0.0106  279 PHE A CB  
1699 C CG  . PHE A 222 ? 0.1312 0.1112 0.1261 0.0084  -0.0115 0.0100  279 PHE A CG  
1700 C CD1 . PHE A 222 ? 0.1617 0.1151 0.1273 0.0091  -0.0083 0.0117  279 PHE A CD1 
1701 C CD2 . PHE A 222 ? 0.1281 0.1310 0.1439 0.0160  -0.0151 0.0055  279 PHE A CD2 
1702 C CE1 . PHE A 222 ? 0.1908 0.1416 0.1482 0.0234  -0.0125 0.0109  279 PHE A CE1 
1703 C CE2 . PHE A 222 ? 0.1346 0.1448 0.1495 0.0267  -0.0193 0.0018  279 PHE A CE2 
1704 C CZ  . PHE A 222 ? 0.1652 0.1498 0.1508 0.0333  -0.0198 0.0054  279 PHE A CZ  
1705 N N   . ILE A 223 ? 0.1911 0.1456 0.1651 -0.0139 -0.0025 0.0105  280 ILE A N   
1706 C CA  . ILE A 223 ? 0.1787 0.1352 0.1547 -0.0162 -0.0027 0.0096  280 ILE A CA  
1707 C C   . ILE A 223 ? 0.2182 0.1809 0.2081 -0.0057 -0.0043 0.0110  280 ILE A C   
1708 O O   . ILE A 223 ? 0.1987 0.1565 0.1883 0.0020  -0.0027 0.0102  280 ILE A O   
1709 C CB  . ILE A 223 ? 0.1962 0.1230 0.1457 -0.0208 0.0031  0.0102  280 ILE A CB  
1710 C CG1 . ILE A 223 ? 0.2469 0.1605 0.1746 -0.0400 0.0111  0.0047  280 ILE A CG1 
1711 C CG2 . ILE A 223 ? 0.2432 0.1727 0.1958 -0.0213 0.0020  0.0095  280 ILE A CG2 
1712 C CD1 . ILE A 223 ? 0.2636 0.1295 0.1490 -0.0462 0.0217  0.0053  280 ILE A CD1 
1713 N N   . PRO A 224 ? 0.1785 0.1504 0.1753 -0.0042 -0.0056 0.0103  281 PRO A N   
1714 C CA  . PRO A 224 ? 0.1733 0.1611 0.1711 -0.0038 -0.0105 0.0078  281 PRO A CA  
1715 C C   . PRO A 224 ? 0.1501 0.1517 0.1585 -0.0031 -0.0121 0.0074  281 PRO A C   
1716 O O   . PRO A 224 ? 0.1538 0.1512 0.1682 -0.0018 -0.0098 0.0092  281 PRO A O   
1717 C CB  . PRO A 224 ? 0.1884 0.1643 0.1743 0.0066  -0.0100 0.0085  281 PRO A CB  
1718 C CG  . PRO A 224 ? 0.2248 0.1789 0.2066 0.0038  -0.0013 0.0102  281 PRO A CG  
1719 C CD  . PRO A 224 ? 0.1882 0.1521 0.1856 -0.0007 -0.0002 0.0094  281 PRO A CD  
1720 N N   . PRO A 225 ? 0.1358 0.1599 0.1477 -0.0030 -0.0165 0.0022  282 PRO A N   
1721 C CA  . PRO A 225 ? 0.1254 0.1623 0.1463 -0.0011 -0.0176 0.0017  282 PRO A CA  
1722 C C   . PRO A 225 ? 0.1220 0.1436 0.1398 0.0087  -0.0158 0.0064  282 PRO A C   
1723 O O   . PRO A 225 ? 0.1331 0.1383 0.1355 0.0177  -0.0143 0.0074  282 PRO A O   
1724 C CB  . PRO A 225 ? 0.1284 0.1993 0.1530 0.0024  -0.0234 -0.0087 282 PRO A CB  
1725 C CG  . PRO A 225 ? 0.1246 0.2060 0.1474 -0.0109 -0.0220 -0.0170 282 PRO A CG  
1726 C CD  . PRO A 225 ? 0.1505 0.1974 0.1611 -0.0072 -0.0200 -0.0075 282 PRO A CD  
1727 N N   . LEU A 226 ? 0.1049 0.1271 0.1311 0.0058  -0.0139 0.0077  283 LEU A N   
1728 C CA  . LEU A 226 ? 0.1111 0.1204 0.1364 0.0066  -0.0081 0.0077  283 LEU A CA  
1729 C C   . LEU A 226 ? 0.1239 0.1247 0.1370 0.0136  -0.0061 0.0078  283 LEU A C   
1730 O O   . LEU A 226 ? 0.1430 0.1581 0.1614 0.0171  -0.0105 0.0078  283 LEU A O   
1731 C CB  . LEU A 226 ? 0.1261 0.1451 0.1643 0.0030  -0.0086 0.0056  283 LEU A CB  
1732 C CG  . LEU A 226 ? 0.1092 0.1309 0.1535 -0.0003 -0.0024 -0.0015 283 LEU A CG  
1733 C CD1 . LEU A 226 ? 0.1433 0.1608 0.1874 -0.0057 0.0056  -0.0082 283 LEU A CD1 
1734 C CD2 . LEU A 226 ? 0.1436 0.1838 0.1992 0.0034  -0.0079 -0.0057 283 LEU A CD2 
1735 N N   . THR A 227 ? 0.1511 0.1218 0.1408 0.0157  0.0028  0.0072  284 THR A N   
1736 C CA  . THR A 227 ? 0.1722 0.1166 0.1363 0.0211  0.0102  0.0069  284 THR A CA  
1737 C C   . THR A 227 ? 0.1825 0.1349 0.1629 0.0058  0.0173  0.0013  284 THR A C   
1738 O O   . THR A 227 ? 0.1506 0.1145 0.1478 -0.0079 0.0227  -0.0059 284 THR A O   
1739 C CB  . THR A 227 ? 0.2194 0.1133 0.1398 0.0244  0.0232  0.0067  284 THR A CB  
1740 O OG1 . THR A 227 ? 0.2568 0.1491 0.1618 0.0432  0.0132  0.0103  284 THR A OG1 
1741 C CG2 . THR A 227 ? 0.2557 0.1011 0.1307 0.0291  0.0365  0.0062  284 THR A CG2 
1742 N N   . THR A 228 ? 0.1669 0.1192 0.1432 0.0101  0.0163  0.0021  285 THR A N   
1743 C CA  . THR A 228 ? 0.1463 0.1178 0.1437 -0.0022 0.0184  -0.0043 285 THR A CA  
1744 C C   . THR A 228 ? 0.2068 0.1596 0.1843 0.0016  0.0230  -0.0036 285 THR A C   
1745 O O   . THR A 228 ? 0.2205 0.1531 0.1715 0.0190  0.0206  0.0027  285 THR A O   
1746 C CB  . THR A 228 ? 0.1372 0.1465 0.1661 0.0001  0.0046  -0.0024 285 THR A CB  
1747 O OG1 . THR A 228 ? 0.1490 0.1761 0.1926 -0.0057 0.0044  -0.0096 285 THR A OG1 
1748 C CG2 . THR A 228 ? 0.1474 0.1659 0.1763 0.0106  -0.0046 0.0044  285 THR A CG2 
1749 N N   . ILE A 229 ? 0.1696 0.1313 0.1575 -0.0124 0.0292  -0.0124 286 ILE A N   
1750 C CA  . ILE A 229 ? 0.1617 0.1094 0.1344 -0.0108 0.0329  -0.0123 286 ILE A CA  
1751 C C   . ILE A 229 ? 0.1680 0.1508 0.1672 -0.0008 0.0168  -0.0068 286 ILE A C   
1752 O O   . ILE A 229 ? 0.1673 0.1813 0.1939 -0.0060 0.0100  -0.0111 286 ILE A O   
1753 C CB  . ILE A 229 ? 0.1690 0.1136 0.1403 -0.0342 0.0486  -0.0281 286 ILE A CB  
1754 C CG1 . ILE A 229 ? 0.2271 0.1351 0.1696 -0.0528 0.0709  -0.0384 286 ILE A CG1 
1755 C CG2 . ILE A 229 ? 0.1989 0.1258 0.1519 -0.0332 0.0527  -0.0277 286 ILE A CG2 
1756 C CD1 . ILE A 229 ? 0.2906 0.1233 0.1679 -0.0413 0.0839  -0.0284 286 ILE A CD1 
1757 N N   . LYS A 230 ? 0.1826 0.1585 0.1682 0.0150  0.0120  0.0005  287 LYS A N   
1758 C CA  . LYS A 230 ? 0.1472 0.1537 0.1542 0.0201  0.0012  0.0032  287 LYS A CA  
1759 C C   . LYS A 230 ? 0.1944 0.1978 0.1998 0.0153  0.0046  0.0003  287 LYS A C   
1760 O O   . LYS A 230 ? 0.2076 0.1824 0.1858 0.0189  0.0129  0.0000  287 LYS A O   
1761 C CB  . LYS A 230 ? 0.1673 0.1838 0.1677 0.0376  -0.0052 0.0061  287 LYS A CB  
1762 C CG  . LYS A 230 ? 0.1562 0.2021 0.1744 0.0376  -0.0106 0.0049  287 LYS A CG  
1763 C CD  . LYS A 230 ? 0.1974 0.2743 0.2205 0.0498  -0.0165 0.0000  287 LYS A CD  
1764 C CE  . LYS A 230 ? 0.3637 0.4716 0.4091 0.0358  -0.0166 -0.0051 287 LYS A CE  
1765 N NZ  . LYS A 230 ? 0.2174 0.3229 0.2714 0.0178  -0.0148 -0.0042 287 LYS A NZ  
1766 N N   . GLN A 231 ? 0.1482 0.1748 0.1752 0.0092  -0.0012 -0.0021 288 GLN A N   
1767 C CA  . GLN A 231 ? 0.1454 0.1755 0.1730 0.0080  -0.0017 -0.0043 288 GLN A CA  
1768 C C   . GLN A 231 ? 0.1699 0.2124 0.2026 0.0153  -0.0080 0.0016  288 GLN A C   
1769 O O   . GLN A 231 ? 0.1591 0.2113 0.1996 0.0137  -0.0124 0.0027  288 GLN A O   
1770 C CB  . GLN A 231 ? 0.1403 0.1879 0.1815 0.0006  -0.0045 -0.0141 288 GLN A CB  
1771 C CG  . GLN A 231 ? 0.1979 0.2449 0.2392 -0.0130 0.0054  -0.0269 288 GLN A CG  
1772 C CD  . GLN A 231 ? 0.1753 0.2535 0.2319 -0.0198 0.0031  -0.0444 288 GLN A CD  
1773 O OE1 . GLN A 231 ? 0.2419 0.3184 0.2930 -0.0338 0.0132  -0.0567 288 GLN A OE1 
1774 N NE2 . GLN A 231 ? 0.1711 0.2772 0.2421 -0.0079 -0.0100 -0.0478 288 GLN A NE2 
1775 N N   . ASP A 232 ? 0.1485 0.1878 0.1719 0.0225  -0.0061 0.0033  289 ASP A N   
1776 C CA  . ASP A 232 ? 0.1262 0.1846 0.1566 0.0252  -0.0085 0.0037  289 ASP A CA  
1777 C C   . ASP A 232 ? 0.1361 0.1923 0.1671 0.0186  -0.0088 0.0036  289 ASP A C   
1778 O O   . ASP A 232 ? 0.1709 0.2213 0.1955 0.0206  -0.0072 0.0032  289 ASP A O   
1779 C CB  . ASP A 232 ? 0.1639 0.2271 0.1842 0.0398  -0.0073 0.0022  289 ASP A CB  
1780 C CG  . ASP A 232 ? 0.2175 0.3149 0.2508 0.0398  -0.0079 -0.0041 289 ASP A CG  
1781 O OD1 . ASP A 232 ? 0.1866 0.2904 0.2288 0.0242  -0.0053 -0.0058 289 ASP A OD1 
1782 O OD2 . ASP A 232 ? 0.2693 0.3860 0.2990 0.0563  -0.0094 -0.0099 289 ASP A OD2 
1783 N N   . PHE A 233 ? 0.1330 0.1871 0.1640 0.0131  -0.0104 0.0039  290 PHE A N   
1784 C CA  . PHE A 233 ? 0.1346 0.1753 0.1525 0.0129  -0.0111 0.0040  290 PHE A CA  
1785 C C   . PHE A 233 ? 0.1471 0.1862 0.1569 0.0081  -0.0040 0.0034  290 PHE A C   
1786 O O   . PHE A 233 ? 0.1737 0.1989 0.1695 0.0103  -0.0036 0.0038  290 PHE A O   
1787 C CB  . PHE A 233 ? 0.1760 0.2015 0.1800 0.0145  -0.0134 0.0047  290 PHE A CB  
1788 C CG  . PHE A 233 ? 0.1554 0.1904 0.1703 0.0198  -0.0200 0.0021  290 PHE A CG  
1789 C CD1 . PHE A 233 ? 0.1663 0.2147 0.1901 0.0240  -0.0249 -0.0050 290 PHE A CD1 
1790 C CD2 . PHE A 233 ? 0.1568 0.1907 0.1738 0.0174  -0.0192 0.0036  290 PHE A CD2 
1791 C CE1 . PHE A 233 ? 0.1676 0.2319 0.2039 0.0246  -0.0278 -0.0126 290 PHE A CE1 
1792 C CE2 . PHE A 233 ? 0.1606 0.2048 0.1880 0.0212  -0.0237 -0.0003 290 PHE A CE2 
1793 C CZ  . PHE A 233 ? 0.1611 0.2226 0.1991 0.0243  -0.0274 -0.0094 290 PHE A CZ  
1794 N N   A ARG A 234 ? 0.1467 0.2044 0.1650 0.0011  0.0020  -0.0007 291 ARG A N   
1795 N N   B ARG A 234 ? 0.1461 0.2040 0.1645 0.0012  0.0020  -0.0007 291 ARG A N   
1796 C CA  A ARG A 234 ? 0.1652 0.2340 0.1817 -0.0059 0.0108  -0.0069 291 ARG A CA  
1797 C CA  B ARG A 234 ? 0.1660 0.2346 0.1824 -0.0061 0.0109  -0.0069 291 ARG A CA  
1798 C C   A ARG A 234 ? 0.1385 0.2121 0.1578 0.0055  0.0079  -0.0054 291 ARG A C   
1799 C C   B ARG A 234 ? 0.1383 0.2128 0.1579 0.0053  0.0081  -0.0057 291 ARG A C   
1800 O O   A ARG A 234 ? 0.1704 0.2338 0.1786 0.0025  0.0129  -0.0061 291 ARG A O   
1801 O O   B ARG A 234 ? 0.1692 0.2348 0.1782 0.0021  0.0134  -0.0067 291 ARG A O   
1802 C CB  A ARG A 234 ? 0.1766 0.2845 0.2102 -0.0134 0.0161  -0.0186 291 ARG A CB  
1803 C CB  B ARG A 234 ? 0.1790 0.2854 0.2116 -0.0145 0.0165  -0.0187 291 ARG A CB  
1804 C CG  A ARG A 234 ? 0.2268 0.3305 0.2577 -0.0263 0.0197  -0.0213 291 ARG A CG  
1805 C CG  B ARG A 234 ? 0.2146 0.3106 0.2395 -0.0303 0.0226  -0.0214 291 ARG A CG  
1806 C CD  A ARG A 234 ? 0.4150 0.5200 0.4343 -0.0522 0.0376  -0.0345 291 ARG A CD  
1807 C CD  B ARG A 234 ? 0.2488 0.3893 0.2900 -0.0456 0.0314  -0.0396 291 ARG A CD  
1808 N NE  A ARG A 234 ? 0.5064 0.5503 0.4843 -0.0619 0.0468  -0.0272 291 ARG A NE  
1809 N NE  B ARG A 234 ? 0.3286 0.5165 0.3958 -0.0263 0.0195  -0.0452 291 ARG A NE  
1810 C CZ  A ARG A 234 ? 0.3712 0.3802 0.3183 -0.0692 0.0583  -0.0271 291 ARG A CZ  
1811 C CZ  B ARG A 234 ? 0.3678 0.5835 0.4397 -0.0272 0.0177  -0.0596 291 ARG A CZ  
1812 N NH1 A ARG A 234 ? 0.3145 0.3473 0.2738 -0.0708 0.0620  -0.0332 291 ARG A NH1 
1813 N NH1 B ARG A 234 ? 0.3915 0.6124 0.4576 -0.0523 0.0295  -0.0744 291 ARG A NH1 
1814 N NH2 A ARG A 234 ? 0.2410 0.1848 0.1374 -0.0717 0.0663  -0.0206 291 ARG A NH2 
1815 N NH2 B ARG A 234 ? 0.3245 0.5574 0.3985 -0.0024 0.0053  -0.0609 291 ARG A NH2 
1816 N N   . LEU A 235 ? 0.1590 0.2401 0.1852 0.0186  0.0019  -0.0036 292 LEU A N   
1817 C CA  . LEU A 235 ? 0.1437 0.2170 0.1615 0.0296  0.0017  -0.0021 292 LEU A CA  
1818 C C   . LEU A 235 ? 0.1789 0.2262 0.1861 0.0254  0.0005  0.0017  292 LEU A C   
1819 O O   . LEU A 235 ? 0.1809 0.2205 0.1791 0.0277  0.0029  0.0016  292 LEU A O   
1820 C CB  . LEU A 235 ? 0.1771 0.2450 0.1873 0.0445  -0.0006 -0.0009 292 LEU A CB  
1821 C CG  . LEU A 235 ? 0.2194 0.2649 0.2063 0.0579  0.0026  0.0005  292 LEU A CG  
1822 C CD1 . LEU A 235 ? 0.2537 0.3239 0.2422 0.0697  0.0034  -0.0050 292 LEU A CD1 
1823 C CD2 . LEU A 235 ? 0.3026 0.3226 0.2650 0.0718  0.0039  0.0024  292 LEU A CD2 
1824 N N   . LEU A 236 ? 0.1613 0.2003 0.1699 0.0210  -0.0039 0.0025  293 LEU A N   
1825 C CA  . LEU A 236 ? 0.1544 0.1832 0.1558 0.0202  -0.0074 0.0001  293 LEU A CA  
1826 C C   . LEU A 236 ? 0.1800 0.1986 0.1672 0.0210  -0.0069 0.0012  293 LEU A C   
1827 O O   . LEU A 236 ? 0.2146 0.2260 0.1923 0.0234  -0.0077 -0.0006 293 LEU A O   
1828 C CB  . LEU A 236 ? 0.1367 0.1711 0.1442 0.0195  -0.0137 -0.0043 293 LEU A CB  
1829 C CG  . LEU A 236 ? 0.1732 0.2141 0.1778 0.0219  -0.0199 -0.0140 293 LEU A CG  
1830 C CD1 . LEU A 236 ? 0.2403 0.2826 0.2469 0.0125  -0.0135 -0.0217 293 LEU A CD1 
1831 C CD2 . LEU A 236 ? 0.2084 0.2660 0.2199 0.0271  -0.0281 -0.0221 293 LEU A CD2 
1832 N N   . GLY A 237 ? 0.1927 0.2047 0.1719 0.0173  -0.0032 0.0031  294 GLY A N   
1833 C CA  . GLY A 237 ? 0.1966 0.1837 0.1486 0.0159  0.0023  0.0037  294 GLY A CA  
1834 C C   . GLY A 237 ? 0.2506 0.2435 0.2039 0.0113  0.0105  0.0022  294 GLY A C   
1835 O O   . GLY A 237 ? 0.2664 0.2400 0.1998 0.0141  0.0118  0.0027  294 GLY A O   
1836 N N   A GLN A 238 ? 0.1944 0.2163 0.1694 0.0079  0.0150  -0.0012 295 GLN A N   
1837 N N   B GLN A 238 ? 0.1947 0.2166 0.1695 0.0076  0.0153  -0.0012 295 GLN A N   
1838 C CA  A GLN A 238 ? 0.1877 0.2244 0.1660 0.0080  0.0221  -0.0057 295 GLN A CA  
1839 C CA  B GLN A 238 ? 0.1876 0.2242 0.1658 0.0080  0.0221  -0.0057 295 GLN A CA  
1840 C C   A GLN A 238 ? 0.2182 0.2441 0.1908 0.0192  0.0169  -0.0018 295 GLN A C   
1841 C C   B GLN A 238 ? 0.2189 0.2439 0.1911 0.0191  0.0168  -0.0017 295 GLN A C   
1842 O O   A GLN A 238 ? 0.2443 0.2592 0.2041 0.0188  0.0214  -0.0023 295 GLN A O   
1843 O O   B GLN A 238 ? 0.2433 0.2562 0.2020 0.0186  0.0210  -0.0020 295 GLN A O   
1844 C CB  A GLN A 238 ? 0.2229 0.3016 0.2242 0.0106  0.0239  -0.0137 295 GLN A CB  
1845 C CB  B GLN A 238 ? 0.2237 0.3021 0.2249 0.0114  0.0236  -0.0135 295 GLN A CB  
1846 C CG  A GLN A 238 ? 0.2432 0.3473 0.2501 0.0220  0.0265  -0.0205 295 GLN A CG  
1847 C CG  B GLN A 238 ? 0.2681 0.3709 0.2773 -0.0061 0.0345  -0.0254 295 GLN A CG  
1848 C CD  A GLN A 238 ? 0.2905 0.4377 0.3145 0.0367  0.0223  -0.0296 295 GLN A CD  
1849 C CD  B GLN A 238 ? 0.2438 0.3814 0.2741 -0.0020 0.0292  -0.0313 295 GLN A CD  
1850 O OE1 A GLN A 238 ? 0.4531 0.6167 0.4889 0.0313  0.0203  -0.0332 295 GLN A OE1 
1851 O OE1 B GLN A 238 ? 0.3394 0.4962 0.3786 0.0190  0.0201  -0.0312 295 GLN A OE1 
1852 N NE2 A GLN A 238 ? 0.3973 0.5612 0.4176 0.0591  0.0201  -0.0341 295 GLN A NE2 
1853 N NE2 B GLN A 238 ? 0.2581 0.3976 0.2888 -0.0209 0.0364  -0.0372 295 GLN A NE2 
1854 N N   . THR A 239 ? 0.1958 0.2198 0.1731 0.0263  0.0101  0.0006  296 THR A N   
1855 C CA  . THR A 239 ? 0.1994 0.2076 0.1653 0.0315  0.0096  0.0012  296 THR A CA  
1856 C C   . THR A 239 ? 0.2786 0.2722 0.2340 0.0273  0.0057  -0.0002 296 THR A C   
1857 O O   . THR A 239 ? 0.2519 0.2341 0.1950 0.0286  0.0079  -0.0013 296 THR A O   
1858 C CB  . THR A 239 ? 0.2323 0.2333 0.1970 0.0337  0.0089  0.0010  296 THR A CB  
1859 O OG1 . THR A 239 ? 0.2507 0.2636 0.2186 0.0441  0.0100  0.0018  296 THR A OG1 
1860 C CG2 . THR A 239 ? 0.3123 0.2872 0.2551 0.0339  0.0146  -0.0010 296 THR A CG2 
1861 N N   . SER A 240 ? 0.2256 0.2203 0.1826 0.0258  -0.0014 -0.0018 297 SER A N   
1862 C CA  . SER A 240 ? 0.2193 0.2065 0.1626 0.0298  -0.0085 -0.0067 297 SER A CA  
1863 C C   . SER A 240 ? 0.2443 0.2101 0.1637 0.0330  -0.0046 -0.0031 297 SER A C   
1864 O O   . SER A 240 ? 0.2489 0.2065 0.1546 0.0371  -0.0074 -0.0065 297 SER A O   
1865 C CB  . SER A 240 ? 0.2649 0.2601 0.2092 0.0358  -0.0187 -0.0112 297 SER A CB  
1866 O OG  . SER A 240 ? 0.3259 0.3049 0.2572 0.0382  -0.0162 -0.0045 297 SER A OG  
1867 N N   . VAL A 241 ? 0.2168 0.1713 0.1272 0.0288  0.0038  0.0013  298 VAL A N   
1868 C CA  . VAL A 241 ? 0.2336 0.1614 0.1154 0.0267  0.0132  0.0025  298 VAL A CA  
1869 C C   . VAL A 241 ? 0.2864 0.2249 0.1773 0.0242  0.0194  0.0016  298 VAL A C   
1870 O O   . VAL A 241 ? 0.3067 0.2254 0.1760 0.0270  0.0214  0.0016  298 VAL A O   
1871 C CB  . VAL A 241 ? 0.2814 0.1945 0.1492 0.0141  0.0275  0.0025  298 VAL A CB  
1872 C CG1 . VAL A 241 ? 0.3214 0.2075 0.1597 0.0046  0.0440  0.0004  298 VAL A CG1 
1873 C CG2 . VAL A 241 ? 0.3141 0.1972 0.1535 0.0211  0.0228  0.0047  298 VAL A CG2 
1874 N N   . ASN A 242 ? 0.2465 0.2129 0.1637 0.0230  0.0218  0.0006  299 ASN A N   
1875 C CA  . ASN A 242 ? 0.2356 0.2085 0.1539 0.0271  0.0273  -0.0008 299 ASN A CA  
1876 C C   . ASN A 242 ? 0.2628 0.2182 0.1688 0.0322  0.0218  0.0001  299 ASN A C   
1877 O O   . ASN A 242 ? 0.2659 0.2095 0.1578 0.0342  0.0264  -0.0002 299 ASN A O   
1878 C CB  . ASN A 242 ? 0.2402 0.2415 0.1779 0.0341  0.0286  -0.0031 299 ASN A CB  
1879 C CG  . ASN A 242 ? 0.2957 0.3293 0.2492 0.0277  0.0363  -0.0108 299 ASN A CG  
1880 O OD1 . ASN A 242 ? 0.2973 0.3257 0.2431 0.0133  0.0460  -0.0150 299 ASN A OD1 
1881 N ND2 . ASN A 242 ? 0.2561 0.3211 0.2266 0.0379  0.0336  -0.0154 299 ASN A ND2 
1882 N N   . ARG A 243 ? 0.2527 0.2086 0.1639 0.0315  0.0137  -0.0018 300 ARG A N   
1883 C CA  . ARG A 243 ? 0.2401 0.1856 0.1406 0.0297  0.0113  -0.0072 300 ARG A CA  
1884 C C   . ARG A 243 ? 0.3012 0.2385 0.1859 0.0325  0.0048  -0.0107 300 ARG A C   
1885 O O   . ARG A 243 ? 0.3129 0.2394 0.1836 0.0322  0.0063  -0.0141 300 ARG A O   
1886 C CB  . ARG A 243 ? 0.2885 0.2435 0.1996 0.0227  0.0079  -0.0144 300 ARG A CB  
1887 C CG  . ARG A 243 ? 0.4209 0.3748 0.3240 0.0136  0.0076  -0.0276 300 ARG A CG  
1888 C CD  . ARG A 243 ? 0.5992 0.5239 0.4801 0.0087  0.0213  -0.0270 300 ARG A CD  
1889 N NE  . ARG A 243 ? 0.8086 0.7159 0.6804 0.0015  0.0323  -0.0285 300 ARG A NE  
1890 C CZ  . ARG A 243 ? 0.9090 0.8027 0.7740 0.0137  0.0368  -0.0178 300 ARG A CZ  
1891 N NH1 . ARG A 243 ? 0.7117 0.6177 0.5853 0.0303  0.0323  -0.0079 300 ARG A NH1 
1892 N NH2 . ARG A 243 ? 0.8109 0.6786 0.6565 0.0089  0.0474  -0.0199 300 ARG A NH2 
1893 N N   . LEU A 244 ? 0.2981 0.2342 0.1770 0.0381  -0.0021 -0.0100 301 LEU A N   
1894 C CA  . LEU A 244 ? 0.3046 0.2229 0.1545 0.0485  -0.0088 -0.0130 301 LEU A CA  
1895 C C   . LEU A 244 ? 0.3104 0.2018 0.1380 0.0471  0.0025  -0.0070 301 LEU A C   
1896 O O   . LEU A 244 ? 0.3440 0.2225 0.1511 0.0528  -0.0007 -0.0105 301 LEU A O   
1897 C CB  . LEU A 244 ? 0.3478 0.2542 0.1794 0.0601  -0.0157 -0.0119 301 LEU A CB  
1898 C CG  . LEU A 244 ? 0.3829 0.2637 0.1709 0.0807  -0.0256 -0.0160 301 LEU A CG  
1899 C CD1 . LEU A 244 ? 0.4027 0.3184 0.2012 0.0902  -0.0421 -0.0327 301 LEU A CD1 
1900 C CD2 . LEU A 244 ? 0.4273 0.2822 0.1843 0.0958  -0.0293 -0.0132 301 LEU A CD2 
1901 N N   . VAL A 245 ? 0.3254 0.2143 0.1586 0.0386  0.0164  -0.0011 302 VAL A N   
1902 C CA  . VAL A 245 ? 0.3589 0.2318 0.1761 0.0344  0.0299  0.0005  302 VAL A CA  
1903 C C   . VAL A 245 ? 0.3715 0.2516 0.1954 0.0367  0.0302  -0.0009 302 VAL A C   
1904 O O   . VAL A 245 ? 0.3938 0.2536 0.1953 0.0387  0.0337  -0.0011 302 VAL A O   
1905 C CB  . VAL A 245 ? 0.4433 0.3305 0.2738 0.0225  0.0454  -0.0005 302 VAL A CB  
1906 C CG1 . VAL A 245 ? 0.4457 0.3319 0.2688 0.0170  0.0606  -0.0040 302 VAL A CG1 
1907 C CG2 . VAL A 245 ? 0.4278 0.2905 0.2357 0.0154  0.0512  -0.0002 302 VAL A CG2 
1908 N N   . GLN A 246 ? 0.3481 0.2479 0.1941 0.0369  0.0282  -0.0017 303 GLN A N   
1909 C CA  . GLN A 246 ? 0.3483 0.2400 0.1867 0.0393  0.0314  -0.0031 303 GLN A CA  
1910 C C   . GLN A 246 ? 0.3563 0.2342 0.1779 0.0373  0.0242  -0.0091 303 GLN A C   
1911 O O   . GLN A 246 ? 0.3799 0.2408 0.1833 0.0380  0.0289  -0.0101 303 GLN A O   
1912 C CB  . GLN A 246 ? 0.3509 0.2490 0.1991 0.0409  0.0331  -0.0033 303 GLN A CB  
1913 C CG  . GLN A 246 ? 0.4267 0.3443 0.2885 0.0493  0.0379  -0.0007 303 GLN A CG  
1914 C CD  . GLN A 246 ? 0.5876 0.5053 0.4523 0.0538  0.0369  -0.0003 303 GLN A CD  
1915 O OE1 . GLN A 246 ? 0.5415 0.4358 0.3912 0.0480  0.0380  -0.0023 303 GLN A OE1 
1916 N NE2 . GLN A 246 ? 0.5941 0.5374 0.4750 0.0622  0.0364  -0.0002 303 GLN A NE2 
1917 N N   . LEU A 247 ? 0.3504 0.2403 0.1777 0.0364  0.0122  -0.0158 304 LEU A N   
1918 C CA  . LEU A 247 ? 0.3363 0.2283 0.1511 0.0372  0.0027  -0.0278 304 LEU A CA  
1919 C C   . LEU A 247 ? 0.4251 0.2946 0.2101 0.0487  -0.0003 -0.0252 304 LEU A C   
1920 O O   . LEU A 247 ? 0.4400 0.3039 0.2089 0.0500  -0.0034 -0.0329 304 LEU A O   
1921 C CB  . LEU A 247 ? 0.3465 0.2691 0.1764 0.0386  -0.0111 -0.0403 304 LEU A CB  
1922 C CG  . LEU A 247 ? 0.3916 0.3330 0.2448 0.0226  -0.0058 -0.0478 304 LEU A CG  
1923 C CD1 . LEU A 247 ? 0.3934 0.3722 0.2642 0.0253  -0.0192 -0.0622 304 LEU A CD1 
1924 C CD2 . LEU A 247 ? 0.4453 0.3778 0.2883 0.0063  0.0045  -0.0589 304 LEU A CD2 
1925 N N   . LEU A 248 ? 0.4263 0.2778 0.1975 0.0555  0.0024  -0.0161 305 LEU A N   
1926 C CA  . LEU A 248 ? 0.4376 0.2527 0.1674 0.0650  0.0045  -0.0132 305 LEU A CA  
1927 C C   . LEU A 248 ? 0.4467 0.2462 0.1694 0.0575  0.0191  -0.0089 305 LEU A C   
1928 O O   . LEU A 248 ? 0.4675 0.2441 0.1633 0.0633  0.0183  -0.0100 305 LEU A O   
1929 C CB  . LEU A 248 ? 0.4505 0.2375 0.1569 0.0680  0.0111  -0.0061 305 LEU A CB  
1930 C CG  . LEU A 248 ? 0.4843 0.2735 0.1847 0.0842  -0.0051 -0.0095 305 LEU A CG  
1931 C CD1 . LEU A 248 ? 0.5137 0.2836 0.2063 0.0793  0.0046  -0.0027 305 LEU A CD1 
1932 C CD2 . LEU A 248 ? 0.5113 0.2757 0.1822 0.1038  -0.0146 -0.0120 305 LEU A CD2 
1933 N N   . GLN A 249 ? 0.4654 0.2810 0.2145 0.0477  0.0310  -0.0051 306 GLN A N   
1934 C CA  . GLN A 249 ? 0.4801 0.2873 0.2233 0.0452  0.0448  -0.0029 306 GLN A CA  
1935 C C   . GLN A 249 ? 0.4970 0.3007 0.2358 0.0464  0.0419  -0.0066 306 GLN A C   
1936 O O   . GLN A 249 ? 0.5020 0.2857 0.2196 0.0481  0.0483  -0.0062 306 GLN A O   
1937 C CB  . GLN A 249 ? 0.4296 0.2623 0.1990 0.0415  0.0563  -0.0015 306 GLN A CB  
1938 C CG  . GLN A 249 ? 0.4941 0.3303 0.2649 0.0329  0.0656  -0.0023 306 GLN A CG  
1939 C CD  . GLN A 249 ? 0.5148 0.3923 0.3177 0.0296  0.0745  -0.0071 306 GLN A CD  
1940 O OE1 . GLN A 249 ? 0.5461 0.4472 0.3708 0.0383  0.0674  -0.0066 306 GLN A OE1 
1941 N NE2 . GLN A 249 ? 0.7052 0.5915 0.5071 0.0167  0.0914  -0.0146 306 GLN A NE2 
1942 N N   . ASN A 250 ? 0.5503 0.5540 0.2025 0.0478  0.0676  -0.1172 307 ASN A N   
1943 C CA  . ASN A 250 ? 0.6100 0.5988 0.2534 0.0490  0.0589  -0.1307 307 ASN A CA  
1944 C C   . ASN A 250 ? 0.5588 0.5422 0.2023 0.0417  0.0437  -0.1300 307 ASN A C   
1945 O O   . ASN A 250 ? 0.5447 0.5259 0.2053 0.0405  0.0397  -0.1286 307 ASN A O   
1946 C CB  . ASN A 250 ? 0.6066 0.5875 0.2622 0.0575  0.0631  -0.1405 307 ASN A CB  
1947 C CG  . ASN A 250 ? 0.6777 0.6717 0.3347 0.0663  0.0770  -0.1439 307 ASN A CG  
1948 O OD1 . ASN A 250 ? 0.7268 0.7385 0.4047 0.0716  0.0852  -0.1409 307 ASN A OD1 
1949 N ND2 . ASN A 250 ? 0.7041 0.6933 0.3394 0.0670  0.0798  -0.1512 307 ASN A ND2 
1950 N N   . PRO A 251 ? 0.6241 0.6086 0.2493 0.0365  0.0349  -0.1317 308 PRO A N   
1951 C CA  . PRO A 251 ? 0.6886 0.6795 0.3175 0.0295  0.0201  -0.1308 308 PRO A CA  
1952 C C   . PRO A 251 ? 0.8196 0.7952 0.4524 0.0193  0.0136  -0.1426 308 PRO A C   
1953 O O   . PRO A 251 ? 0.7501 0.7356 0.3870 0.0108  0.0015  -0.1445 308 PRO A O   
1954 C CB  . PRO A 251 ? 0.8169 0.8151 0.4237 0.0284  0.0126  -0.1329 308 PRO A CB  
1955 C CG  . PRO A 251 ? 0.8805 0.8773 0.4731 0.0357  0.0246  -0.1270 308 PRO A CG  
1956 C CD  . PRO A 251 ? 0.6767 0.6657 0.2805 0.0388  0.0392  -0.1291 308 PRO A CD  
1957 N N   . SER A 252 ? 0.8401 0.7934 0.4719 0.0202  0.0216  -0.1510 309 SER A N   
1958 C CA  . SER A 252 ? 0.9013 0.8312 0.5298 0.0077  0.0181  -0.1625 309 SER A CA  
1959 C C   . SER A 252 ? 0.8730 0.8060 0.5179 0.0046  0.0105  -0.1548 309 SER A C   
1960 O O   . SER A 252 ? 0.8049 0.7497 0.4725 0.0130  0.0158  -0.1460 309 SER A O   
1961 C CB  . SER A 252 ? 0.8684 0.7816 0.5015 0.0198  0.0262  -0.1703 309 SER A CB  
1962 O OG  . SER A 252 ? 1.0190 0.9248 0.6335 0.0241  0.0304  -0.1795 309 SER A OG  
1963 N N   . ALA A 253 ? 0.6699 0.6104 0.3171 -0.0063 -0.0028 -0.1607 310 ALA A N   
1964 C CA  . ALA A 253 ? 0.5949 0.5534 0.2676 -0.0180 -0.0075 -0.1561 310 ALA A CA  
1965 C C   . ALA A 253 ? 0.6141 0.5421 0.2916 -0.0195 -0.0017 -0.1575 310 ALA A C   
1966 O O   . ALA A 253 ? 0.7834 0.6771 0.4460 -0.0200 0.0019  -0.1663 310 ALA A O   
1967 C CB  . ALA A 253 ? 0.6238 0.6027 0.3012 -0.0380 -0.0181 -0.1642 310 ALA A CB  
1968 N N   . GLN A 254 ? 0.6373 0.5770 0.3355 -0.0201 -0.0003 -0.1479 311 GLN A N   
1969 C CA  . GLN A 254 ? 0.7278 0.6362 0.4290 -0.0188 0.0054  -0.1456 311 GLN A CA  
1970 C C   . GLN A 254 ? 0.6377 0.5518 0.3536 -0.0389 0.0008  -0.1438 311 GLN A C   
1971 O O   . GLN A 254 ? 0.5934 0.5501 0.3284 -0.0465 -0.0057 -0.1409 311 GLN A O   
1972 C CB  . GLN A 254 ? 0.7526 0.6713 0.4719 0.0021  0.0120  -0.1326 311 GLN A CB  
1973 C CG  . GLN A 254 ? 0.7562 0.6858 0.4677 0.0193  0.0181  -0.1328 311 GLN A CG  
1974 C CD  . GLN A 254 ? 0.9448 0.8855 0.6763 0.0363  0.0265  -0.1230 311 GLN A CD  
1975 O OE1 . GLN A 254 ? 0.9155 0.8444 0.6590 0.0408  0.0276  -0.1200 311 GLN A OE1 
1976 N NE2 . GLN A 254 ? 0.7682 0.7331 0.5014 0.0440  0.0330  -0.1188 311 GLN A NE2 
1977 N N   . SER A 255 ? 0.6707 0.5437 0.3781 -0.0450 0.0043  -0.1447 312 SER A N   
1978 C CA  . SER A 255 ? 0.6119 0.4884 0.3322 -0.0647 0.0026  -0.1420 312 SER A CA  
1979 C C   . SER A 255 ? 0.5615 0.4733 0.3096 -0.0576 0.0013  -0.1313 312 SER A C   
1980 O O   . SER A 255 ? 0.5903 0.5093 0.3524 -0.0340 0.0039  -0.1203 312 SER A O   
1981 C CB  . SER A 255 ? 0.6252 0.4446 0.3265 -0.0678 0.0082  -0.1409 312 SER A CB  
1982 O OG  . SER A 255 ? 0.7396 0.5186 0.4113 -0.0668 0.0109  -0.1483 312 SER A OG  
1983 N N   . PRO A 256 ? 0.5639 0.5055 0.3311 -0.0744 -0.0028 -0.1306 313 PRO A N   
1984 C CA  . PRO A 256 ? 0.4711 0.4438 0.2722 -0.0623 -0.0047 -0.1155 313 PRO A CA  
1985 C C   . PRO A 256 ? 0.5289 0.4664 0.3322 -0.0481 0.0015  -0.1052 313 PRO A C   
1986 O O   . PRO A 256 ? 0.5123 0.4029 0.2924 -0.0537 0.0058  -0.1098 313 PRO A O   
1987 C CB  . PRO A 256 ? 0.5210 0.5224 0.3345 -0.0855 -0.0086 -0.1209 313 PRO A CB  
1988 C CG  . PRO A 256 ? 0.5093 0.5087 0.3094 -0.1062 -0.0093 -0.1334 313 PRO A CG  
1989 C CD  . PRO A 256 ? 0.6434 0.5952 0.4127 -0.1003 -0.0053 -0.1381 313 PRO A CD  
1990 N N   . GLN A 257 ? 0.4009 0.3590 0.2276 -0.0292 0.0020  -0.0921 314 GLN A N   
1991 C CA  . GLN A 257 ? 0.3718 0.3104 0.2063 -0.0158 0.0066  -0.0837 314 GLN A CA  
1992 C C   . GLN A 257 ? 0.3812 0.3372 0.2393 -0.0211 0.0044  -0.0749 314 GLN A C   
1993 O O   . GLN A 257 ? 0.3728 0.3641 0.2492 -0.0193 0.0009  -0.0687 314 GLN A O   
1994 C CB  . GLN A 257 ? 0.4745 0.4258 0.3178 0.0044  0.0109  -0.0779 314 GLN A CB  
1995 C CG  . GLN A 257 ? 0.5570 0.5006 0.4122 0.0174  0.0147  -0.0721 314 GLN A CG  
1996 C CD  . GLN A 257 ? 0.6162 0.5759 0.4775 0.0333  0.0210  -0.0716 314 GLN A CD  
1997 O OE1 . GLN A 257 ? 0.5946 0.5679 0.4500 0.0339  0.0236  -0.0734 314 GLN A OE1 
1998 N NE2 . GLN A 257 ? 0.4990 0.4612 0.3715 0.0456  0.0238  -0.0703 314 GLN A NE2 
1999 N N   . LEU A 258 ? 0.3807 0.3079 0.2326 -0.0259 0.0063  -0.0745 315 LEU A N   
2000 C CA  . LEU A 258 ? 0.3674 0.3070 0.2387 -0.0312 0.0051  -0.0669 315 LEU A CA  
2001 C C   . LEU A 258 ? 0.3161 0.2501 0.2000 -0.0123 0.0074  -0.0575 315 LEU A C   
2002 O O   . LEU A 258 ? 0.4220 0.3234 0.2895 -0.0020 0.0098  -0.0596 315 LEU A O   
2003 C CB  . LEU A 258 ? 0.4510 0.3619 0.3034 -0.0524 0.0069  -0.0730 315 LEU A CB  
2004 C CG  . LEU A 258 ? 0.6487 0.5749 0.4925 -0.0800 0.0057  -0.0850 315 LEU A CG  
2005 C CD1 . LEU A 258 ? 0.6339 0.5326 0.4605 -0.1045 0.0106  -0.0890 315 LEU A CD1 
2006 C CD2 . LEU A 258 ? 0.4561 0.4457 0.3305 -0.0789 -0.0007 -0.0837 315 LEU A CD2 
2007 N N   . LEU A 259 ? 0.2610 0.2261 0.1705 -0.0069 0.0064  -0.0484 316 LEU A N   
2008 C CA  . LEU A 259 ? 0.2661 0.2312 0.1887 0.0063  0.0089  -0.0417 316 LEU A CA  
2009 C C   . LEU A 259 ? 0.2481 0.2033 0.1757 0.0014  0.0075  -0.0376 316 LEU A C   
2010 O O   . LEU A 259 ? 0.3190 0.2853 0.2520 -0.0116 0.0053  -0.0366 316 LEU A O   
2011 C CB  . LEU A 259 ? 0.2517 0.2454 0.1916 0.0116  0.0105  -0.0344 316 LEU A CB  
2012 C CG  . LEU A 259 ? 0.3093 0.3123 0.2414 0.0157  0.0136  -0.0365 316 LEU A CG  
2013 C CD1 . LEU A 259 ? 0.2942 0.3122 0.2344 0.0181  0.0177  -0.0280 316 LEU A CD1 
2014 C CD2 . LEU A 259 ? 0.3956 0.3880 0.3184 0.0247  0.0177  -0.0441 316 LEU A CD2 
2015 N N   . PRO A 260 ? 0.2716 0.2098 0.1963 0.0130  0.0086  -0.0365 317 PRO A N   
2016 C CA  . PRO A 260 ? 0.2809 0.2056 0.2055 0.0097  0.0075  -0.0324 317 PRO A CA  
2017 C C   . PRO A 260 ? 0.2969 0.2523 0.2491 0.0093  0.0067  -0.0244 317 PRO A C   
2018 O O   . PRO A 260 ? 0.2670 0.2461 0.2344 0.0146  0.0080  -0.0218 317 PRO A O   
2019 C CB  . PRO A 260 ? 0.3904 0.2902 0.3000 0.0289  0.0074  -0.0347 317 PRO A CB  
2020 C CG  . PRO A 260 ? 0.4525 0.3795 0.3753 0.0429  0.0089  -0.0380 317 PRO A CG  
2021 C CD  . PRO A 260 ? 0.3221 0.2579 0.2430 0.0318  0.0105  -0.0404 317 PRO A CD  
2022 N N   . VAL A 261 ? 0.2429 0.1926 0.1963 0.0017  0.0058  -0.0211 318 VAL A N   
2023 C CA  . VAL A 261 ? 0.2185 0.1897 0.1930 0.0034  0.0050  -0.0143 318 VAL A CA  
2024 C C   . VAL A 261 ? 0.2371 0.1901 0.2067 0.0091  0.0045  -0.0121 318 VAL A C   
2025 O O   . VAL A 261 ? 0.3030 0.2231 0.2487 0.0103  0.0047  -0.0149 318 VAL A O   
2026 C CB  . VAL A 261 ? 0.2327 0.2247 0.2156 -0.0081 0.0037  -0.0129 318 VAL A CB  
2027 C CG1 . VAL A 261 ? 0.2233 0.2347 0.2072 -0.0084 0.0023  -0.0154 318 VAL A CG1 
2028 C CG2 . VAL A 261 ? 0.2548 0.2340 0.2247 -0.0239 0.0048  -0.0171 318 VAL A CG2 
2029 N N   . THR A 262 ? 0.2050 0.1748 0.1920 0.0137  0.0039  -0.0074 319 THR A N   
2030 C CA  . THR A 262 ? 0.2112 0.1692 0.1947 0.0211  0.0023  -0.0059 319 THR A CA  
2031 C C   . THR A 262 ? 0.1849 0.1551 0.1811 0.0149  0.0022  -0.0006 319 THR A C   
2032 O O   . THR A 262 ? 0.1952 0.1851 0.2044 0.0102  0.0030  0.0018  319 THR A O   
2033 C CB  . THR A 262 ? 0.2313 0.2029 0.2231 0.0366  0.0012  -0.0092 319 THR A CB  
2034 O OG1 . THR A 262 ? 0.2644 0.2650 0.2770 0.0319  0.0041  -0.0081 319 THR A OG1 
2035 C CG2 . THR A 262 ? 0.2618 0.2229 0.2390 0.0479  0.0011  -0.0159 319 THR A CG2 
2036 N N   . LEU A 263 ? 0.1840 0.1388 0.1714 0.0178  0.0009  0.0011  320 LEU A N   
2037 C CA  . LEU A 263 ? 0.1539 0.1194 0.1518 0.0146  0.0008  0.0052  320 LEU A CA  
2038 C C   . LEU A 263 ? 0.1869 0.1676 0.1982 0.0250  -0.0012 0.0046  320 LEU A C   
2039 O O   . LEU A 263 ? 0.1994 0.1768 0.2053 0.0369  -0.0040 0.0009  320 LEU A O   
2040 C CB  . LEU A 263 ? 0.2310 0.1706 0.2084 0.0101  0.0015  0.0069  320 LEU A CB  
2041 C CG  . LEU A 263 ? 0.2170 0.1653 0.2017 0.0091  0.0014  0.0105  320 LEU A CG  
2042 C CD1 . LEU A 263 ? 0.2291 0.2028 0.2290 -0.0014 0.0039  0.0110  320 LEU A CD1 
2043 C CD2 . LEU A 263 ? 0.2861 0.2010 0.2424 0.0069  0.0028  0.0123  320 LEU A CD2 
2044 N N   . VAL A 264 ? 0.1592 0.1571 0.1849 0.0208  0.0003  0.0067  321 VAL A N   
2045 C CA  . VAL A 264 ? 0.1399 0.1511 0.1755 0.0236  0.0001  0.0047  321 VAL A CA  
2046 C C   . VAL A 264 ? 0.1411 0.1482 0.1759 0.0226  -0.0012 0.0077  321 VAL A C   
2047 O O   . VAL A 264 ? 0.1452 0.1516 0.1804 0.0180  0.0006  0.0114  321 VAL A O   
2048 C CB  . VAL A 264 ? 0.1695 0.1910 0.2114 0.0173  0.0047  0.0044  321 VAL A CB  
2049 C CG1 . VAL A 264 ? 0.1430 0.1763 0.1914 0.0136  0.0066  0.0001  321 VAL A CG1 
2050 C CG2 . VAL A 264 ? 0.2120 0.2386 0.2532 0.0178  0.0069  0.0012  321 VAL A CG2 
2051 N N   . LYS A 265 ? 0.1449 0.1509 0.1765 0.0298  -0.0049 0.0054  322 LYS A N   
2052 C CA  . LYS A 265 ? 0.1469 0.1481 0.1750 0.0298  -0.0063 0.0076  322 LYS A CA  
2053 C C   . LYS A 265 ? 0.1510 0.1677 0.1900 0.0260  -0.0055 0.0043  322 LYS A C   
2054 O O   . LYS A 265 ? 0.1704 0.2051 0.2169 0.0275  -0.0068 -0.0029 322 LYS A O   
2055 C CB  . LYS A 265 ? 0.2128 0.2014 0.2256 0.0412  -0.0113 0.0065  322 LYS A CB  
2056 C CG  . LYS A 265 ? 0.2366 0.1949 0.2262 0.0414  -0.0102 0.0101  322 LYS A CG  
2057 C CD  . LYS A 265 ? 0.3327 0.2676 0.2961 0.0567  -0.0152 0.0098  322 LYS A CD  
2058 C CE  . LYS A 265 ? 0.4565 0.3532 0.3880 0.0623  -0.0147 0.0107  322 LYS A CE  
2059 N NZ  . LYS A 265 ? 0.3889 0.2591 0.2878 0.0836  -0.0209 0.0100  322 LYS A NZ  
2060 N N   . ARG A 266 ? 0.1486 0.1594 0.1863 0.0207  -0.0027 0.0079  323 ARG A N   
2061 C CA  . ARG A 266 ? 0.1273 0.1408 0.1661 0.0156  -0.0010 0.0046  323 ARG A CA  
2062 C C   . ARG A 266 ? 0.1337 0.1406 0.1664 0.0185  -0.0028 0.0062  323 ARG A C   
2063 O O   . ARG A 266 ? 0.1736 0.1833 0.2043 0.0241  -0.0073 0.0049  323 ARG A O   
2064 C CB  . ARG A 266 ? 0.1276 0.1305 0.1604 0.0095  0.0048  0.0068  323 ARG A CB  
2065 C CG  . ARG A 266 ? 0.1603 0.1698 0.1965 0.0048  0.0078  0.0046  323 ARG A CG  
2066 C CD  . ARG A 266 ? 0.1654 0.1584 0.1873 -0.0047 0.0152  0.0048  323 ARG A CD  
2067 N NE  . ARG A 266 ? 0.1642 0.1647 0.1875 -0.0115 0.0197  0.0022  323 ARG A NE  
2068 C CZ  . ARG A 266 ? 0.1684 0.1597 0.1840 -0.0076 0.0211  0.0073  323 ARG A CZ  
2069 N NH1 . ARG A 266 ? 0.1700 0.1505 0.1785 0.0035  0.0175  0.0139  323 ARG A NH1 
2070 N NH2 . ARG A 266 ? 0.1622 0.1602 0.1772 -0.0150 0.0263  0.0041  323 ARG A NH2 
2071 N N   . LYS A 267 ? 0.1139 0.1101 0.1396 0.0175  0.0003  0.0089  324 LYS A N   
2072 C CA  . LYS A 267 ? 0.1430 0.1342 0.1620 0.0199  -0.0005 0.0085  324 LYS A CA  
2073 C C   . LYS A 267 ? 0.1782 0.1676 0.1923 0.0257  0.0013  0.0128  324 LYS A C   
2074 O O   . LYS A 267 ? 0.1841 0.1692 0.1908 0.0290  0.0019  0.0119  324 LYS A O   
2075 C CB  . LYS A 267 ? 0.1624 0.1430 0.1730 0.0137  0.0021  0.0037  324 LYS A CB  
2076 C CG  . LYS A 267 ? 0.1621 0.1561 0.1799 0.0034  0.0016  -0.0046 324 LYS A CG  
2077 C CD  . LYS A 267 ? 0.2159 0.2284 0.2401 0.0076  -0.0051 -0.0097 324 LYS A CD  
2078 C CE  . LYS A 267 ? 0.2790 0.3188 0.3136 -0.0007 -0.0065 -0.0216 324 LYS A CE  
2079 N NZ  . LYS A 267 ? 0.4956 0.5601 0.5377 0.0132  -0.0157 -0.0255 324 LYS A NZ  
2080 N N   . THR A 268 ? 0.1463 0.1438 0.1645 0.0266  0.0023  0.0156  325 THR A N   
2081 C CA  . THR A 268 ? 0.1434 0.1523 0.1600 0.0310  0.0043  0.0162  325 THR A CA  
2082 C C   . THR A 268 ? 0.1289 0.1488 0.1472 0.0236  0.0060  0.0165  325 THR A C   
2083 O O   . THR A 268 ? 0.1284 0.1686 0.1488 0.0231  0.0090  0.0145  325 THR A O   
2084 C CB  . THR A 268 ? 0.1372 0.1531 0.1536 0.0377  0.0046  0.0165  325 THR A CB  
2085 O OG1 . THR A 268 ? 0.1294 0.1491 0.1524 0.0315  0.0039  0.0173  325 THR A OG1 
2086 C CG2 . THR A 268 ? 0.1563 0.1482 0.1577 0.0451  0.0051  0.0170  325 THR A CG2 
2087 N N   . THR A 269 ? 0.1519 0.1585 0.1649 0.0181  0.0049  0.0178  326 THR A N   
2088 C CA  . THR A 269 ? 0.1762 0.1792 0.1782 0.0089  0.0088  0.0187  326 THR A CA  
2089 C C   . THR A 269 ? 0.1781 0.1607 0.1635 0.0109  0.0075  0.0206  326 THR A C   
2090 O O   . THR A 269 ? 0.2120 0.1868 0.1971 0.0196  0.0016  0.0201  326 THR A O   
2091 C CB  . THR A 269 ? 0.1727 0.1677 0.1696 0.0000  0.0102  0.0189  326 THR A CB  
2092 O OG1 . THR A 269 ? 0.2205 0.1933 0.2094 0.0064  0.0055  0.0204  326 THR A OG1 
2093 C CG2 . THR A 269 ? 0.1386 0.1551 0.1505 -0.0007 0.0101  0.0164  326 THR A CG2 
2094 N N   . ALA A 270 ? 0.1826 0.1597 0.1524 0.0018  0.0134  0.0215  327 ALA A N   
2095 C CA  . ALA A 270 ? 0.2146 0.1684 0.1608 0.0037  0.0133  0.0241  327 ALA A CA  
2096 C C   . ALA A 270 ? 0.2273 0.1705 0.1513 -0.0140 0.0236  0.0250  327 ALA A C   
2097 O O   . ALA A 270 ? 0.2351 0.2023 0.1702 -0.0274 0.0301  0.0213  327 ALA A O   
2098 C CB  . ALA A 270 ? 0.2518 0.2180 0.2047 0.0124  0.0110  0.0222  327 ALA A CB  
2099 N N   . PRO A 271 ? 0.2614 0.1700 0.1511 -0.0156 0.0258  0.0290  328 PRO A N   
2100 C CA  . PRO A 271 ? 0.2852 0.1810 0.1484 -0.0379 0.0388  0.0292  328 PRO A CA  
2101 C C   . PRO A 271 ? 0.2792 0.2206 0.1633 -0.0465 0.0461  0.0236  328 PRO A C   
2102 O O   . PRO A 271 ? 0.2835 0.2501 0.1903 -0.0306 0.0402  0.0217  328 PRO A O   
2103 C CB  . PRO A 271 ? 0.3701 0.2154 0.1877 -0.0316 0.0383  0.0355  328 PRO A CB  
2104 C CG  . PRO A 271 ? 0.3981 0.2295 0.2176 -0.0058 0.0239  0.0374  328 PRO A CG  
2105 C CD  . PRO A 271 ? 0.3290 0.2084 0.1982 0.0027  0.0169  0.0324  328 PRO A CD  
2106 N N   . PRO A 272 ? 0.2924 0.2464 0.1673 -0.0717 0.0593  0.0192  329 PRO A N   
2107 C CA  . PRO A 272 ? 0.2815 0.2875 0.1758 -0.0778 0.0667  0.0114  329 PRO A CA  
2108 C C   . PRO A 272 ? 0.4590 0.4551 0.3379 -0.0697 0.0680  0.0140  329 PRO A C   
2109 O O   . PRO A 272 ? 0.4070 0.3533 0.2492 -0.0697 0.0683  0.0214  329 PRO A O   
2110 C CB  . PRO A 272 ? 0.3292 0.3475 0.2115 -0.1110 0.0811  0.0044  329 PRO A CB  
2111 C CG  . PRO A 272 ? 0.3958 0.3472 0.2397 -0.1200 0.0807  0.0105  329 PRO A CG  
2112 C CD  . PRO A 272 ? 0.3255 0.2473 0.1687 -0.0974 0.0692  0.0193  329 PRO A CD  
2113 N N   . GLU A 273 ? 0.4178 0.4608 0.3219 -0.0598 0.0683  0.0074  330 GLU A N   
2114 C CA  . GLU A 273 ? 0.6501 0.6931 0.5408 -0.0552 0.0721  0.0071  330 GLU A CA  
2115 C C   . GLU A 273 ? 0.5644 0.5926 0.4201 -0.0844 0.0885  0.0071  330 GLU A C   
2116 O O   . GLU A 273 ? 0.6478 0.7069 0.5168 -0.1029 0.0951  -0.0012 330 GLU A O   
2117 C CB  . GLU A 273 ? 0.6968 0.7961 0.6173 -0.0408 0.0719  -0.0024 330 GLU A CB  
2118 C CG  . GLU A 273 ? 0.6857 0.7792 0.5985 -0.0236 0.0693  -0.0024 330 GLU A CG  
2119 C CD  . GLU A 273 ? 0.5753 0.7139 0.5123 -0.0026 0.0669  -0.0118 330 GLU A CD  
2120 O OE1 . GLU A 273 ? 0.5790 0.7662 0.5361 -0.0046 0.0710  -0.0202 330 GLU A OE1 
2121 O OE2 . GLU A 273 ? 0.7179 0.8422 0.6505 0.0172  0.0605  -0.0117 330 GLU A OE2 
2122 N N   . ASN A 274 ? 0.7855 0.7617 0.6017 -0.0833 0.0889  0.0154  331 ASN A N   
2123 C CA  . ASN A 274 ? 0.9751 0.9191 0.7612 -0.1032 0.0963  0.0164  331 ASN A CA  
2124 C C   . ASN A 274 ? 0.9944 0.9640 0.7787 -0.1094 0.1052  0.0112  331 ASN A C   
2125 O O   . ASN A 274 ? 0.9550 0.9847 0.7722 -0.1071 0.1083  0.0018  331 ASN A O   
2126 C CB  . ASN A 274 ? 1.0161 0.8874 0.7595 -0.0930 0.0890  0.0273  331 ASN A CB  
2127 C CG  . ASN A 274 ? 1.2295 1.0560 0.9357 -0.1137 0.0964  0.0268  331 ASN A CG  
2128 O OD1 . ASN A 274 ? 1.3387 1.1367 1.0135 -0.1156 0.1003  0.0292  331 ASN A OD1 
2129 N ND2 . ASN A 274 ? 1.1120 0.9286 0.8172 -0.1297 0.0988  0.0228  331 ASN A ND2 
2130 N N   . LYS B 2   ? 1.0193 0.8869 0.4135 0.1224  -0.0550 0.0276  59  LYS B N   
2131 C CA  . LYS B 2   ? 0.8167 0.7208 0.2459 0.1364  -0.0843 0.0249  59  LYS B CA  
2132 C C   . LYS B 2   ? 1.1326 1.0465 0.6168 0.1403  -0.0827 0.0213  59  LYS B C   
2133 O O   . LYS B 2   ? 1.1386 1.0497 0.6427 0.1269  -0.0670 0.0084  59  LYS B O   
2134 C CB  . LYS B 2   ? 0.8364 0.7792 0.2688 0.1246  -0.1013 0.0030  59  LYS B CB  
2135 N N   . GLN B 3   ? 1.2085 1.1358 0.7172 0.1596  -0.0984 0.0319  60  GLN B N   
2136 C CA  . GLN B 3   ? 1.2016 1.1423 0.7616 0.1636  -0.0977 0.0288  60  GLN B CA  
2137 C C   . GLN B 3   ? 1.2561 1.2405 0.8571 0.1485  -0.1076 0.0057  60  GLN B C   
2138 O O   . GLN B 3   ? 1.3529 1.3692 0.9537 0.1413  -0.1246 -0.0059 60  GLN B O   
2139 C CB  . GLN B 3   ? 1.1609 1.1134 0.7383 0.1881  -0.1116 0.0417  60  GLN B CB  
2140 C CG  . GLN B 3   ? 1.3910 1.2884 0.9321 0.2033  -0.0990 0.0630  60  GLN B CG  
2141 C CD  . GLN B 3   ? 1.5107 1.4034 1.0821 0.2205  -0.0971 0.0690  60  GLN B CD  
2142 O OE1 . GLN B 3   ? 1.4633 1.3896 1.0570 0.2399  -0.1137 0.0695  60  GLN B OE1 
2143 N NE2 . GLN B 3   ? 1.2951 1.1484 0.8672 0.2124  -0.0759 0.0721  60  GLN B NE2 
2144 N N   . SER B 4   ? 0.7569 0.7395 0.3907 0.1414  -0.0971 -0.0013 61  SER B N   
2145 C CA  . SER B 4   ? 0.7925 0.8074 0.4640 0.1255  -0.1049 -0.0228 61  SER B CA  
2146 C C   . SER B 4   ? 0.7688 0.8144 0.4928 0.1292  -0.1136 -0.0227 61  SER B C   
2147 O O   . SER B 4   ? 0.7001 0.7733 0.4568 0.1129  -0.1214 -0.0393 61  SER B O   
2148 C CB  . SER B 4   ? 0.7044 0.6934 0.3706 0.1111  -0.0852 -0.0360 61  SER B CB  
2149 O OG  . SER B 4   ? 0.7376 0.6990 0.4066 0.1167  -0.0676 -0.0241 61  SER B OG  
2150 N N   . HIS B 5   ? 0.5909 0.6284 0.3223 0.1478  -0.1101 -0.0054 62  HIS B N   
2151 C CA  . HIS B 5   ? 0.5372 0.6026 0.3169 0.1518  -0.1136 -0.0052 62  HIS B CA  
2152 C C   . HIS B 5   ? 0.4585 0.5169 0.2618 0.1367  -0.1044 -0.0144 62  HIS B C   
2153 O O   . HIS B 5   ? 0.4754 0.5675 0.3211 0.1262  -0.1108 -0.0237 62  HIS B O   
2154 C CB  . HIS B 5   ? 0.6931 0.8171 0.5056 0.1480  -0.1330 -0.0140 62  HIS B CB  
2155 C CG  . HIS B 5   ? 0.8264 0.9627 0.6222 0.1684  -0.1441 -0.0034 62  HIS B CG  
2156 N ND1 . HIS B 5   ? 0.7949 0.9281 0.5963 0.1930  -0.1414 0.0097  62  HIS B ND1 
2157 C CD2 . HIS B 5   ? 0.7954 0.9430 0.5647 0.1690  -0.1581 -0.0043 62  HIS B CD2 
2158 C CE1 . HIS B 5   ? 0.7509 0.8946 0.5319 0.2098  -0.1544 0.0166  62  HIS B CE1 
2159 N NE2 . HIS B 5   ? 0.7549 0.9090 0.5164 0.1951  -0.1654 0.0092  62  HIS B NE2 
2160 N N   . THR B 6   ? 0.4741 0.4877 0.2540 0.1314  -0.0857 -0.0116 63  THR B N   
2161 C CA  . THR B 6   ? 0.4155 0.4175 0.2286 0.1120  -0.0703 -0.0196 63  THR B CA  
2162 C C   . THR B 6   ? 0.4567 0.4192 0.2590 0.1149  -0.0497 -0.0063 63  THR B C   
2163 O O   . THR B 6   ? 0.5172 0.4490 0.2782 0.1184  -0.0391 0.0020  63  THR B O   
2164 C CB  . THR B 6   ? 0.4216 0.4177 0.2296 0.0945  -0.0657 -0.0369 63  THR B CB  
2165 O OG1 . THR B 6   ? 0.4906 0.5176 0.3063 0.0868  -0.0849 -0.0513 63  THR B OG1 
2166 C CG2 . THR B 6   ? 0.4055 0.3895 0.2468 0.0805  -0.0518 -0.0434 63  THR B CG2 
2167 N N   . ILE B 7   ? 0.3847 0.3472 0.2203 0.1107  -0.0439 -0.0045 64  ILE B N   
2168 C CA  . ILE B 7   ? 0.3846 0.3122 0.2139 0.1080  -0.0256 0.0048  64  ILE B CA  
2169 C C   . ILE B 7   ? 0.4253 0.3546 0.2828 0.0877  -0.0151 -0.0059 64  ILE B C   
2170 O O   . ILE B 7   ? 0.3521 0.3039 0.2424 0.0804  -0.0232 -0.0158 64  ILE B O   
2171 C CB  . ILE B 7   ? 0.4262 0.3519 0.2681 0.1199  -0.0273 0.0133  64  ILE B CB  
2172 C CG1 . ILE B 7   ? 0.4390 0.3483 0.2437 0.1464  -0.0332 0.0271  64  ILE B CG1 
2173 C CG2 . ILE B 7   ? 0.4266 0.3217 0.2721 0.1083  -0.0100 0.0165  64  ILE B CG2 
2174 C CD1 . ILE B 7   ? 0.5600 0.4917 0.3883 0.1633  -0.0408 0.0286  64  ILE B CD1 
2175 N N   . GLY B 8   ? 0.3766 0.2836 0.2204 0.0787  0.0023  -0.0040 65  GLY B N   
2176 C CA  . GLY B 8   ? 0.3331 0.2478 0.2061 0.0639  0.0117  -0.0134 65  GLY B CA  
2177 C C   . GLY B 8   ? 0.3604 0.2651 0.2490 0.0566  0.0188  -0.0075 65  GLY B C   
2178 O O   . GLY B 8   ? 0.3857 0.2636 0.2495 0.0569  0.0272  0.0030  65  GLY B O   
2179 N N   . LEU B 9   ? 0.3039 0.2254 0.2286 0.0497  0.0149  -0.0143 66  LEU B N   
2180 C CA  . LEU B 9   ? 0.3129 0.2291 0.2521 0.0416  0.0186  -0.0107 66  LEU B CA  
2181 C C   . LEU B 9   ? 0.3568 0.2897 0.3221 0.0304  0.0233  -0.0186 66  LEU B C   
2182 O O   . LEU B 9   ? 0.3216 0.2705 0.3097 0.0334  0.0145  -0.0258 66  LEU B O   
2183 C CB  . LEU B 9   ? 0.2855 0.2093 0.2407 0.0464  0.0064  -0.0092 66  LEU B CB  
2184 C CG  . LEU B 9   ? 0.3395 0.2614 0.3099 0.0376  0.0076  -0.0081 66  LEU B CG  
2185 C CD1 . LEU B 9   ? 0.4360 0.3313 0.3849 0.0317  0.0200  -0.0029 66  LEU B CD1 
2186 C CD2 . LEU B 9   ? 0.3450 0.2767 0.3248 0.0432  -0.0016 -0.0067 66  LEU B CD2 
2187 N N   . ALA B 10  ? 0.2608 0.1898 0.2219 0.0177  0.0368  -0.0173 67  ALA B N   
2188 C CA  . ALA B 10  ? 0.2925 0.2481 0.2838 0.0078  0.0397  -0.0248 67  ALA B CA  
2189 C C   . ALA B 10  ? 0.3355 0.2889 0.3382 -0.0006 0.0337  -0.0219 67  ALA B C   
2190 O O   . ALA B 10  ? 0.3492 0.2766 0.3297 -0.0083 0.0393  -0.0159 67  ALA B O   
2191 C CB  . ALA B 10  ? 0.2557 0.2195 0.2398 -0.0066 0.0585  -0.0274 67  ALA B CB  
2192 N N   . THR B 11  ? 0.2699 0.2455 0.3018 0.0021  0.0222  -0.0263 68  THR B N   
2193 C CA  . THR B 11  ? 0.2519 0.2247 0.2895 -0.0045 0.0140  -0.0232 68  THR B CA  
2194 C C   . THR B 11  ? 0.2879 0.2930 0.3546 -0.0088 0.0075  -0.0285 68  THR B C   
2195 O O   . THR B 11  ? 0.3146 0.3425 0.4025 0.0023  0.0035  -0.0340 68  THR B O   
2196 C CB  . THR B 11  ? 0.2750 0.2357 0.3095 0.0056  0.0022  -0.0189 68  THR B CB  
2197 O OG1 . THR B 11  ? 0.2903 0.2483 0.3256 -0.0019 -0.0036 -0.0162 68  THR B OG1 
2198 C CG2 . THR B 11  ? 0.2876 0.2587 0.3381 0.0165  -0.0080 -0.0225 68  THR B CG2 
2199 N N   . THR B 12  ? 0.2605 0.2676 0.3265 -0.0235 0.0057  -0.0278 69  THR B N   
2200 C CA  . THR B 12  ? 0.2507 0.2912 0.3424 -0.0265 -0.0059 -0.0315 69  THR B CA  
2201 C C   . THR B 12  ? 0.3033 0.3372 0.3986 -0.0112 -0.0233 -0.0263 69  THR B C   
2202 O O   . THR B 12  ? 0.2919 0.2989 0.3721 -0.0035 -0.0245 -0.0214 69  THR B O   
2203 C CB  . THR B 12  ? 0.2922 0.3322 0.3745 -0.0500 -0.0037 -0.0331 69  THR B CB  
2204 O OG1 . THR B 12  ? 0.3616 0.4435 0.4702 -0.0539 -0.0172 -0.0375 69  THR B OG1 
2205 C CG2 . THR B 12  ? 0.2740 0.2744 0.3269 -0.0510 -0.0062 -0.0273 69  THR B CG2 
2206 N N   . ASN B 13  ? 0.3347 0.3943 0.4483 -0.0086 -0.0375 -0.0270 70  ASN B N   
2207 C CA  . ASN B 13  ? 0.3675 0.4180 0.4807 0.0059  -0.0550 -0.0204 70  ASN B CA  
2208 C C   . ASN B 13  ? 0.3152 0.3264 0.4005 0.0028  -0.0558 -0.0121 70  ASN B C   
2209 O O   . ASN B 13  ? 0.2672 0.2685 0.3350 -0.0107 -0.0545 -0.0095 70  ASN B O   
2210 C CB  . ASN B 13  ? 0.3050 0.3849 0.4300 0.0031  -0.0707 -0.0200 70  ASN B CB  
2211 C CG  . ASN B 13  ? 0.4329 0.4980 0.5507 0.0195  -0.0902 -0.0105 70  ASN B CG  
2212 O OD1 . ASN B 13  ? 0.3364 0.3737 0.4477 0.0343  -0.0918 -0.0066 70  ASN B OD1 
2213 N ND2 . ASN B 13  ? 0.3223 0.4030 0.4370 0.0153  -0.1059 -0.0068 70  ASN B ND2 
2214 N N   . LEU B 14  ? 0.2845 0.2750 0.3653 0.0139  -0.0570 -0.0096 71  LEU B N   
2215 C CA  . LEU B 14  ? 0.2962 0.2597 0.3560 0.0083  -0.0564 -0.0031 71  LEU B CA  
2216 C C   . LEU B 14  ? 0.3007 0.2523 0.3471 0.0049  -0.0688 0.0059  71  LEU B C   
2217 O O   . LEU B 14  ? 0.3064 0.2418 0.3348 -0.0043 -0.0658 0.0111  71  LEU B O   
2218 C CB  . LEU B 14  ? 0.2733 0.2214 0.3318 0.0157  -0.0549 -0.0047 71  LEU B CB  
2219 C CG  . LEU B 14  ? 0.2565 0.2120 0.3172 0.0169  -0.0423 -0.0114 71  LEU B CG  
2220 C CD1 . LEU B 14  ? 0.3277 0.2726 0.3872 0.0242  -0.0435 -0.0160 71  LEU B CD1 
2221 C CD2 . LEU B 14  ? 0.2977 0.2499 0.3451 0.0084  -0.0340 -0.0086 71  LEU B CD2 
2222 N N   . ALA B 15  ? 0.2476 0.2100 0.3015 0.0125  -0.0825 0.0080  72  ALA B N   
2223 C CA  . ALA B 15  ? 0.3444 0.2939 0.3784 0.0092  -0.0957 0.0184  72  ALA B CA  
2224 C C   . ALA B 15  ? 0.3357 0.2945 0.3556 -0.0081 -0.0925 0.0179  72  ALA B C   
2225 O O   . ALA B 15  ? 0.3205 0.2661 0.3160 -0.0145 -0.1004 0.0262  72  ALA B O   
2226 C CB  . ALA B 15  ? 0.3984 0.3585 0.4432 0.0277  -0.1145 0.0215  72  ALA B CB  
2227 N N   . LEU B 16  ? 0.2398 0.2154 0.2686 -0.0169 -0.0806 0.0082  73  LEU B N   
2228 C CA  . LEU B 16  ? 0.1988 0.1696 0.2065 -0.0337 -0.0738 0.0056  73  LEU B CA  
2229 C C   . LEU B 16  ? 0.2285 0.1768 0.2205 -0.0362 -0.0583 0.0063  73  LEU B C   
2230 O O   . LEU B 16  ? 0.2122 0.1578 0.2153 -0.0285 -0.0501 0.0049  73  LEU B O   
2231 C CB  . LEU B 16  ? 0.1908 0.1803 0.2087 -0.0441 -0.0674 -0.0053 73  LEU B CB  
2232 C CG  . LEU B 16  ? 0.1956 0.2223 0.2333 -0.0457 -0.0830 -0.0085 73  LEU B CG  
2233 C CD1 . LEU B 16  ? 0.2114 0.2562 0.2567 -0.0644 -0.0735 -0.0204 73  LEU B CD1 
2234 C CD2 . LEU B 16  ? 0.2201 0.2478 0.2383 -0.0492 -0.1009 -0.0025 73  LEU B CD2 
2235 N N   . HIS B 17  ? 0.2150 0.1516 0.1808 -0.0461 -0.0545 0.0077  74  HIS B N   
2236 C CA  . HIS B 17  ? 0.2130 0.1385 0.1682 -0.0458 -0.0411 0.0088  74  HIS B CA  
2237 C C   . HIS B 17  ? 0.2225 0.1454 0.1811 -0.0408 -0.0252 0.0006  74  HIS B C   
2238 O O   . HIS B 17  ? 0.2314 0.1572 0.1980 -0.0326 -0.0180 0.0013  74  HIS B O   
2239 C CB  . HIS B 17  ? 0.2369 0.1541 0.1623 -0.0567 -0.0389 0.0113  74  HIS B CB  
2240 C CG  . HIS B 17  ? 0.2572 0.1691 0.1699 -0.0608 -0.0546 0.0229  74  HIS B CG  
2241 N ND1 . HIS B 17  ? 0.2725 0.1812 0.1997 -0.0522 -0.0671 0.0308  74  HIS B ND1 
2242 C CD2 . HIS B 17  ? 0.2900 0.1936 0.1710 -0.0711 -0.0599 0.0284  74  HIS B CD2 
2243 C CE1 . HIS B 17  ? 0.2904 0.1854 0.1948 -0.0555 -0.0803 0.0422  74  HIS B CE1 
2244 N NE2 . HIS B 17  ? 0.3074 0.2008 0.1830 -0.0678 -0.0767 0.0417  74  HIS B NE2 
2245 N N   . ALA B 18  ? 0.2323 0.1478 0.1820 -0.0460 -0.0204 -0.0068 75  ALA B N   
2246 C CA  . ALA B 18  ? 0.2343 0.1349 0.1784 -0.0393 -0.0056 -0.0125 75  ALA B CA  
2247 C C   . ALA B 18  ? 0.2326 0.1403 0.1975 -0.0281 -0.0050 -0.0102 75  ALA B C   
2248 O O   . ALA B 18  ? 0.2291 0.1337 0.1934 -0.0154 0.0024  -0.0094 75  ALA B O   
2249 C CB  . ALA B 18  ? 0.2678 0.1488 0.1914 -0.0520 -0.0003 -0.0209 75  ALA B CB  
2250 N N   . PRO B 19  ? 0.2160 0.1368 0.1989 -0.0306 -0.0125 -0.0099 76  PRO B N   
2251 C CA  . PRO B 19  ? 0.2184 0.1444 0.2154 -0.0199 -0.0101 -0.0090 76  PRO B CA  
2252 C C   . PRO B 19  ? 0.2187 0.1514 0.2240 -0.0094 -0.0138 -0.0052 76  PRO B C   
2253 O O   . PRO B 19  ? 0.2015 0.1338 0.2076 0.0002  -0.0094 -0.0055 76  PRO B O   
2254 C CB  . PRO B 19  ? 0.2423 0.1881 0.2593 -0.0237 -0.0174 -0.0111 76  PRO B CB  
2255 C CG  . PRO B 19  ? 0.2831 0.2356 0.2968 -0.0380 -0.0223 -0.0140 76  PRO B CG  
2256 C CD  . PRO B 19  ? 0.2376 0.1728 0.2280 -0.0424 -0.0220 -0.0123 76  PRO B CD  
2257 N N   A SER B 20  ? 0.1934 0.1309 0.2014 -0.0130 -0.0224 -0.0014 77  SER B N   
2258 N N   B SER B 20  ? 0.1930 0.1305 0.2008 -0.0131 -0.0224 -0.0013 77  SER B N   
2259 C CA  A SER B 20  ? 0.1852 0.1274 0.1989 -0.0098 -0.0248 0.0012  77  SER B CA  
2260 C CA  B SER B 20  ? 0.1853 0.1275 0.1990 -0.0100 -0.0249 0.0013  77  SER B CA  
2261 C C   A SER B 20  ? 0.2148 0.1634 0.2226 -0.0068 -0.0152 0.0002  77  SER B C   
2262 C C   B SER B 20  ? 0.2145 0.1632 0.2224 -0.0070 -0.0153 0.0003  77  SER B C   
2263 O O   A SER B 20  ? 0.2125 0.1738 0.2292 -0.0014 -0.0149 -0.0009 77  SER B O   
2264 O O   B SER B 20  ? 0.2137 0.1751 0.2305 -0.0019 -0.0152 -0.0008 77  SER B O   
2265 C CB  A SER B 20  ? 0.2165 0.1535 0.2273 -0.0177 -0.0348 0.0071  77  SER B CB  
2266 C CB  B SER B 20  ? 0.2164 0.1532 0.2272 -0.0178 -0.0350 0.0072  77  SER B CB  
2267 O OG  A SER B 20  ? 0.2965 0.2292 0.3176 -0.0119 -0.0448 0.0073  77  SER B OG  
2268 O OG  B SER B 20  ? 0.2422 0.1750 0.2368 -0.0264 -0.0346 0.0101  77  SER B OG  
2269 N N   . GLN B 21  ? 0.2201 0.1634 0.2133 -0.0092 -0.0076 -0.0009 78  GLN B N   
2270 C CA  . GLN B 21  ? 0.2104 0.1630 0.2000 -0.0001 0.0031  -0.0037 78  GLN B CA  
2271 C C   . GLN B 21  ? 0.2234 0.1703 0.2119 0.0168  0.0075  -0.0058 78  GLN B C   
2272 O O   . GLN B 21  ? 0.2195 0.1842 0.2144 0.0302  0.0104  -0.0068 78  GLN B O   
2273 C CB  . GLN B 21  ? 0.2372 0.1801 0.2064 -0.0039 0.0123  -0.0067 78  GLN B CB  
2274 C CG  . GLN B 21  ? 0.2053 0.1598 0.1713 -0.0186 0.0109  -0.0032 78  GLN B CG  
2275 C CD  . GLN B 21  ? 0.2446 0.1947 0.1877 -0.0220 0.0225  -0.0078 78  GLN B CD  
2276 O OE1 . GLN B 21  ? 0.2406 0.1801 0.1652 -0.0365 0.0186  -0.0052 78  GLN B OE1 
2277 N NE2 . GLN B 21  ? 0.2553 0.2145 0.1975 -0.0066 0.0364  -0.0148 78  GLN B NE2 
2278 N N   . ILE B 22  ? 0.2099 0.1346 0.1896 0.0158  0.0077  -0.0061 79  ILE B N   
2279 C CA  . ILE B 22  ? 0.2411 0.1519 0.2113 0.0296  0.0125  -0.0056 79  ILE B CA  
2280 C C   . ILE B 22  ? 0.2484 0.1800 0.2342 0.0365  0.0049  -0.0038 79  ILE B C   
2281 O O   . ILE B 22  ? 0.2391 0.1766 0.2211 0.0530  0.0054  -0.0027 79  ILE B O   
2282 C CB  . ILE B 22  ? 0.2526 0.1350 0.2072 0.0197  0.0172  -0.0065 79  ILE B CB  
2283 C CG1 . ILE B 22  ? 0.2837 0.1381 0.2141 0.0138  0.0259  -0.0106 79  ILE B CG1 
2284 C CG2 . ILE B 22  ? 0.3217 0.1875 0.2632 0.0299  0.0218  -0.0034 79  ILE B CG2 
2285 C CD1 . ILE B 22  ? 0.3070 0.1404 0.2251 -0.0062 0.0291  -0.0139 79  ILE B CD1 
2286 N N   . VAL B 23  ? 0.2123 0.1551 0.2137 0.0259  -0.0035 -0.0044 80  VAL B N   
2287 C CA  . VAL B 23  ? 0.1755 0.1338 0.1873 0.0301  -0.0107 -0.0056 80  VAL B CA  
2288 C C   . VAL B 23  ? 0.2183 0.2025 0.2392 0.0342  -0.0138 -0.0064 80  VAL B C   
2289 O O   . VAL B 23  ? 0.2026 0.2018 0.2242 0.0452  -0.0171 -0.0075 80  VAL B O   
2290 C CB  . VAL B 23  ? 0.1889 0.1476 0.2126 0.0199  -0.0184 -0.0076 80  VAL B CB  
2291 C CG1 . VAL B 23  ? 0.2368 0.2062 0.2662 0.0217  -0.0255 -0.0116 80  VAL B CG1 
2292 C CG2 . VAL B 23  ? 0.2826 0.2308 0.3048 0.0186  -0.0153 -0.0089 80  VAL B CG2 
2293 N N   . ALA B 24  ? 0.2084 0.2028 0.2360 0.0244  -0.0127 -0.0060 81  ALA B N   
2294 C CA  . ALA B 24  ? 0.2164 0.2449 0.2572 0.0236  -0.0131 -0.0080 81  ALA B CA  
2295 C C   . ALA B 24  ? 0.2345 0.2797 0.2739 0.0461  -0.0082 -0.0090 81  ALA B C   
2296 O O   . ALA B 24  ? 0.2202 0.3003 0.2730 0.0536  -0.0136 -0.0116 81  ALA B O   
2297 C CB  . ALA B 24  ? 0.1869 0.2200 0.2288 0.0074  -0.0087 -0.0065 81  ALA B CB  
2298 N N   . ALA B 25  ? 0.2072 0.2260 0.2284 0.0582  0.0009  -0.0075 82  ALA B N   
2299 C CA  . ALA B 25  ? 0.2339 0.2583 0.2481 0.0848  0.0059  -0.0078 82  ALA B CA  
2300 C C   . ALA B 25  ? 0.2453 0.2617 0.2492 0.1017  -0.0011 -0.0041 82  ALA B C   
2301 O O   . ALA B 25  ? 0.2753 0.3148 0.2819 0.1251  -0.0045 -0.0037 82  ALA B O   
2302 C CB  . ALA B 25  ? 0.2887 0.2736 0.2777 0.0915  0.0185  -0.0083 82  ALA B CB  
2303 N N   . ILE B 26  ? 0.2350 0.2220 0.2263 0.0915  -0.0033 -0.0015 83  ILE B N   
2304 C CA  . ILE B 26  ? 0.2469 0.2249 0.2228 0.1040  -0.0086 0.0023  83  ILE B CA  
2305 C C   . ILE B 26  ? 0.2746 0.2974 0.2703 0.1038  -0.0222 -0.0015 83  ILE B C   
2306 O O   . ILE B 26  ? 0.2815 0.3205 0.2705 0.1237  -0.0297 0.0007  83  ILE B O   
2307 C CB  . ILE B 26  ? 0.2375 0.1798 0.1973 0.0896  -0.0041 0.0040  83  ILE B CB  
2308 C CG1 . ILE B 26  ? 0.2993 0.1964 0.2328 0.0902  0.0088  0.0075  83  ILE B CG1 
2309 C CG2 . ILE B 26  ? 0.2887 0.2301 0.2347 0.0960  -0.0097 0.0061  83  ILE B CG2 
2310 C CD1 . ILE B 26  ? 0.3154 0.1877 0.2389 0.0713  0.0153  0.0075  83  ILE B CD1 
2311 N N   . LYS B 27  ? 0.2308 0.2714 0.2474 0.0812  -0.0266 -0.0072 84  LYS B N   
2312 C CA  . LYS B 27  ? 0.2028 0.2818 0.2359 0.0742  -0.0389 -0.0133 84  LYS B CA  
2313 C C   . LYS B 27  ? 0.2526 0.3823 0.3042 0.0866  -0.0431 -0.0152 84  LYS B C   
2314 O O   . LYS B 27  ? 0.2427 0.4055 0.2983 0.0955  -0.0550 -0.0179 84  LYS B O   
2315 C CB  . LYS B 27  ? 0.1950 0.2720 0.2416 0.0467  -0.0404 -0.0182 84  LYS B CB  
2316 C CG  . LYS B 27  ? 0.2571 0.3561 0.3119 0.0326  -0.0523 -0.0266 84  LYS B CG  
2317 C CD  . LYS B 27  ? 0.2350 0.3803 0.3135 0.0191  -0.0553 -0.0308 84  LYS B CD  
2318 C CE  . LYS B 27  ? 0.2810 0.4452 0.3640 0.0003  -0.0676 -0.0411 84  LYS B CE  
2319 N NZ  . LYS B 27  ? 0.4839 0.7043 0.5929 -0.0158 -0.0701 -0.0463 84  LYS B NZ  
2320 N N   . SER B 28  ? 0.2109 0.3519 0.2738 0.0885  -0.0334 -0.0148 85  SER B N   
2321 C CA  . SER B 28  ? 0.2287 0.4276 0.3151 0.1016  -0.0347 -0.0185 85  SER B CA  
2322 C C   . SER B 28  ? 0.2081 0.4071 0.2794 0.1337  -0.0393 -0.0143 85  SER B C   
2323 O O   . SER B 28  ? 0.2660 0.5065 0.3493 0.1368  -0.0487 -0.0174 85  SER B O   
2324 C CB  . SER B 28  ? 0.2350 0.4366 0.3283 0.0998  -0.0194 -0.0194 85  SER B CB  
2325 O OG  . SER B 28  ? 0.3534 0.6157 0.4713 0.1155  -0.0175 -0.0244 85  SER B OG  
2326 N N   . ARG B 29  ? 0.2809 0.4231 0.3190 0.1502  -0.0312 -0.0067 86  ARG B N   
2327 C CA  . ARG B 29  ? 0.3017 0.4297 0.3161 0.1737  -0.0341 -0.0012 86  ARG B CA  
2328 C C   . ARG B 29  ? 0.3033 0.4341 0.3057 0.1735  -0.0475 0.0008  86  ARG B C   
2329 O O   . ARG B 29  ? 0.3400 0.4948 0.3399 0.1888  -0.0565 0.0015  86  ARG B O   
2330 C CB  . ARG B 29  ? 0.3565 0.4177 0.3334 0.1839  -0.0218 0.0058  86  ARG B CB  
2331 C CG  . ARG B 29  ? 0.4165 0.4574 0.3640 0.2091  -0.0244 0.0123  86  ARG B CG  
2332 C CD  . ARG B 29  ? 0.4507 0.5354 0.4174 0.2301  -0.0266 0.0083  86  ARG B CD  
2333 N NE  . ARG B 29  ? 0.4928 0.5565 0.4305 0.2582  -0.0301 0.0148  86  ARG B NE  
2334 C CZ  . ARG B 29  ? 0.6065 0.7084 0.5568 0.2827  -0.0353 0.0126  86  ARG B CZ  
2335 N NH1 . ARG B 29  ? 0.5148 0.6827 0.5080 0.2803  -0.0365 0.0034  86  ARG B NH1 
2336 N NH2 . ARG B 29  ? 0.5641 0.6383 0.4825 0.3104  -0.0390 0.0198  86  ARG B NH2 
2337 N N   . ALA B 30  ? 0.3141 0.4216 0.3077 0.1578  -0.0492 0.0010  87  ALA B N   
2338 C CA  . ALA B 30  ? 0.3058 0.4143 0.2837 0.1574  -0.0610 0.0013  87  ALA B CA  
2339 C C   . ALA B 30  ? 0.2904 0.4613 0.2952 0.1505  -0.0758 -0.0075 87  ALA B C   
2340 O O   . ALA B 30  ? 0.3483 0.5325 0.3408 0.1614  -0.0859 -0.0063 87  ALA B O   
2341 C CB  . ALA B 30  ? 0.2925 0.3718 0.2603 0.1417  -0.0600 -0.0001 87  ALA B CB  
2342 N N   . SER B 31  ? 0.2754 0.4844 0.3157 0.1302  -0.0765 -0.0162 88  SER B N   
2343 C CA  . SER B 31  ? 0.2825 0.5488 0.3485 0.1155  -0.0879 -0.0256 88  SER B CA  
2344 C C   . SER B 31  ? 0.2936 0.5968 0.3681 0.1369  -0.0906 -0.0239 88  SER B C   
2345 O O   . SER B 31  ? 0.3497 0.6894 0.4300 0.1359  -0.1035 -0.0282 88  SER B O   
2346 C CB  . SER B 31  ? 0.2544 0.5466 0.3519 0.0860  -0.0839 -0.0338 88  SER B CB  
2347 O OG  . SER B 31  ? 0.3046 0.5669 0.3944 0.0646  -0.0860 -0.0380 88  SER B OG  
2348 N N   . GLN B 32  ? 0.3289 0.6231 0.4034 0.1567  -0.0791 -0.0188 89  GLN B N   
2349 C CA  . GLN B 32  ? 0.3003 0.6268 0.3809 0.1818  -0.0818 -0.0180 89  GLN B CA  
2350 C C   . GLN B 32  ? 0.3810 0.6830 0.4279 0.2063  -0.0912 -0.0101 89  GLN B C   
2351 O O   . GLN B 32  ? 0.3787 0.7180 0.4319 0.2248  -0.1007 -0.0106 89  GLN B O   
2352 C CB  . GLN B 32  ? 0.3931 0.7061 0.4747 0.1982  -0.0667 -0.0156 89  GLN B CB  
2353 C CG  . GLN B 32  ? 0.4300 0.7832 0.5471 0.1786  -0.0574 -0.0238 89  GLN B CG  
2354 C CD  . GLN B 32  ? 0.6517 0.9767 0.7613 0.1919  -0.0407 -0.0217 89  GLN B CD  
2355 O OE1 . GLN B 32  ? 0.6622 0.9246 0.7376 0.2068  -0.0352 -0.0143 89  GLN B OE1 
2356 N NE2 . GLN B 32  ? 0.5593 0.9292 0.6980 0.1847  -0.0316 -0.0290 89  GLN B NE2 
2357 N N   . MET B 33  ? 0.3905 0.6317 0.4008 0.2070  -0.0883 -0.0026 90  MET B N   
2358 C CA  . MET B 33  ? 0.4407 0.6511 0.4123 0.2269  -0.0950 0.0062  90  MET B CA  
2359 C C   . MET B 33  ? 0.4623 0.6868 0.4266 0.2132  -0.1093 0.0029  90  MET B C   
2360 O O   . MET B 33  ? 0.4781 0.6757 0.4063 0.2267  -0.1150 0.0105  90  MET B O   
2361 C CB  . MET B 33  ? 0.5898 0.7228 0.5203 0.2334  -0.0808 0.0164  90  MET B CB  
2362 C CG  . MET B 33  ? 0.4639 0.5706 0.3896 0.2484  -0.0672 0.0197  90  MET B CG  
2363 S SD  . MET B 33  ? 0.6146 0.7457 0.5386 0.2856  -0.0737 0.0222  90  MET B SD  
2364 C CE  . MET B 33  ? 0.6770 0.8899 0.6608 0.2789  -0.0746 0.0091  90  MET B CE  
2365 N N   . GLY B 34  ? 0.4224 0.6842 0.4159 0.1854  -0.1149 -0.0085 91  GLY B N   
2366 C CA  . GLY B 34  ? 0.3652 0.6387 0.3494 0.1696  -0.1287 -0.0145 91  GLY B CA  
2367 C C   . GLY B 34  ? 0.3876 0.6108 0.3415 0.1577  -0.1242 -0.0140 91  GLY B C   
2368 O O   . GLY B 34  ? 0.4593 0.6781 0.3897 0.1520  -0.1338 -0.0170 91  GLY B O   
2369 N N   . PHE B 35  ? 0.3387 0.5258 0.2917 0.1535  -0.1099 -0.0112 92  PHE B N   
2370 C CA  . PHE B 35  ? 0.3854 0.5264 0.3106 0.1452  -0.1040 -0.0108 92  PHE B CA  
2371 C C   . PHE B 35  ? 0.3464 0.4949 0.2971 0.1201  -0.1031 -0.0226 92  PHE B C   
2372 O O   . PHE B 35  ? 0.3667 0.5327 0.3495 0.1136  -0.0983 -0.0240 92  PHE B O   
2373 C CB  . PHE B 35  ? 0.4162 0.5017 0.3139 0.1608  -0.0880 0.0030  92  PHE B CB  
2374 C CG  . PHE B 35  ? 0.4597 0.5162 0.3160 0.1800  -0.0875 0.0143  92  PHE B CG  
2375 C CD1 . PHE B 35  ? 0.4585 0.5205 0.3142 0.2012  -0.0886 0.0211  92  PHE B CD1 
2376 C CD2 . PHE B 35  ? 0.4771 0.4985 0.2919 0.1768  -0.0849 0.0180  92  PHE B CD2 
2377 C CE1 . PHE B 35  ? 0.5885 0.6194 0.4032 0.2195  -0.0895 0.0320  92  PHE B CE1 
2378 C CE2 . PHE B 35  ? 0.5605 0.5522 0.3341 0.1920  -0.0838 0.0296  92  PHE B CE2 
2379 C CZ  . PHE B 35  ? 0.5300 0.5246 0.3035 0.2136  -0.0871 0.0370  92  PHE B CZ  
2380 N N   . ASN B 36  ? 0.3215 0.4505 0.2563 0.1032  -0.1040 -0.0318 93  ASN B N   
2381 C CA  . ASN B 36  ? 0.2936 0.4002 0.2443 0.0782  -0.0936 -0.0403 93  ASN B CA  
2382 C C   . ASN B 36  ? 0.3010 0.3611 0.2410 0.0827  -0.0746 -0.0311 93  ASN B C   
2383 O O   . ASN B 36  ? 0.3247 0.3612 0.2355 0.0979  -0.0682 -0.0214 93  ASN B O   
2384 C CB  . ASN B 36  ? 0.3426 0.4411 0.2786 0.0612  -0.0995 -0.0555 93  ASN B CB  
2385 C CG  . ASN B 36  ? 0.5232 0.6662 0.4738 0.0454  -0.1179 -0.0685 93  ASN B CG  
2386 O OD1 . ASN B 36  ? 0.6594 0.8338 0.6428 0.0343  -0.1209 -0.0697 93  ASN B OD1 
2387 N ND2 . ASN B 36  ? 0.6223 0.7696 0.5469 0.0412  -0.1294 -0.0796 93  ASN B ND2 
2388 N N   . VAL B 37  ? 0.2379 0.2849 0.1996 0.0678  -0.0659 -0.0337 94  VAL B N   
2389 C CA  . VAL B 37  ? 0.2823 0.2945 0.2393 0.0678  -0.0502 -0.0280 94  VAL B CA  
2390 C C   . VAL B 37  ? 0.2642 0.2607 0.2264 0.0540  -0.0470 -0.0383 94  VAL B C   
2391 O O   . VAL B 37  ? 0.2496 0.2512 0.2282 0.0412  -0.0535 -0.0457 94  VAL B O   
2392 C CB  . VAL B 37  ? 0.2239 0.2352 0.1995 0.0676  -0.0438 -0.0207 94  VAL B CB  
2393 C CG1 . VAL B 37  ? 0.2509 0.2314 0.2210 0.0644  -0.0300 -0.0165 94  VAL B CG1 
2394 C CG2 . VAL B 37  ? 0.2368 0.2607 0.2062 0.0864  -0.0458 -0.0124 94  VAL B CG2 
2395 N N   . VAL B 38  ? 0.2443 0.2206 0.1909 0.0571  -0.0359 -0.0388 95  VAL B N   
2396 C CA  . VAL B 38  ? 0.2503 0.2142 0.2034 0.0511  -0.0305 -0.0488 95  VAL B CA  
2397 C C   . VAL B 38  ? 0.3074 0.2637 0.2735 0.0504  -0.0185 -0.0425 95  VAL B C   
2398 O O   . VAL B 38  ? 0.2915 0.2423 0.2444 0.0529  -0.0079 -0.0349 95  VAL B O   
2399 C CB  . VAL B 38  ? 0.3076 0.2658 0.2345 0.0550  -0.0265 -0.0582 95  VAL B CB  
2400 C CG1 . VAL B 38  ? 0.4220 0.3706 0.3570 0.0551  -0.0160 -0.0679 95  VAL B CG1 
2401 C CG2 . VAL B 38  ? 0.3344 0.3001 0.2509 0.0508  -0.0416 -0.0690 95  VAL B CG2 
2402 N N   . ILE B 39  ? 0.2300 0.1840 0.2187 0.0456  -0.0208 -0.0452 96  ILE B N   
2403 C CA  . ILE B 39  ? 0.2299 0.1841 0.2341 0.0432  -0.0146 -0.0392 96  ILE B CA  
2404 C C   . ILE B 39  ? 0.2257 0.1827 0.2414 0.0467  -0.0089 -0.0474 96  ILE B C   
2405 O O   . ILE B 39  ? 0.2378 0.1880 0.2570 0.0516  -0.0143 -0.0566 96  ILE B O   
2406 C CB  . ILE B 39  ? 0.2193 0.1727 0.2382 0.0370  -0.0233 -0.0339 96  ILE B CB  
2407 C CG1 . ILE B 39  ? 0.2231 0.1836 0.2358 0.0360  -0.0267 -0.0280 96  ILE B CG1 
2408 C CG2 . ILE B 39  ? 0.2505 0.2051 0.2820 0.0337  -0.0195 -0.0291 96  ILE B CG2 
2409 C CD1 . ILE B 39  ? 0.2558 0.2209 0.2786 0.0271  -0.0361 -0.0288 96  ILE B CD1 
2410 N N   . SER B 40  ? 0.2392 0.2068 0.2609 0.0442  0.0023  -0.0451 97  SER B N   
2411 C CA  . SER B 40  ? 0.2297 0.2144 0.2714 0.0485  0.0078  -0.0532 97  SER B CA  
2412 C C   . SER B 40  ? 0.2790 0.2773 0.3412 0.0415  0.0062  -0.0475 97  SER B C   
2413 O O   . SER B 40  ? 0.2941 0.2916 0.3485 0.0294  0.0129  -0.0407 97  SER B O   
2414 C CB  . SER B 40  ? 0.2727 0.2699 0.3041 0.0477  0.0252  -0.0590 97  SER B CB  
2415 O OG  . SER B 40  ? 0.3965 0.4218 0.4534 0.0532  0.0321  -0.0686 97  SER B OG  
2416 N N   A MET B 41  ? 0.2610 0.2681 0.3451 0.0496  -0.0035 -0.0504 98  MET B N   
2417 N N   B MET B 41  ? 0.2649 0.2709 0.3485 0.0497  -0.0040 -0.0502 98  MET B N   
2418 C CA  A MET B 41  ? 0.2945 0.3196 0.3973 0.0439  -0.0085 -0.0459 98  MET B CA  
2419 C CA  B MET B 41  ? 0.2969 0.3231 0.4009 0.0451  -0.0085 -0.0467 98  MET B CA  
2420 C C   A MET B 41  ? 0.3129 0.3791 0.4409 0.0462  0.0001  -0.0546 98  MET B C   
2421 C C   B MET B 41  ? 0.3163 0.3828 0.4427 0.0454  0.0024  -0.0552 98  MET B C   
2422 O O   A MET B 41  ? 0.3043 0.3836 0.4446 0.0631  0.0020  -0.0644 98  MET B O   
2423 O O   B MET B 41  ? 0.3096 0.3900 0.4457 0.0599  0.0076  -0.0655 98  MET B O   
2424 C CB  A MET B 41  ? 0.2967 0.3069 0.4038 0.0517  -0.0263 -0.0412 98  MET B CB  
2425 C CB  B MET B 41  ? 0.3000 0.3168 0.4132 0.0568  -0.0259 -0.0443 98  MET B CB  
2426 C CG  A MET B 41  ? 0.3865 0.4168 0.5101 0.0492  -0.0358 -0.0367 98  MET B CG  
2427 C CG  B MET B 41  ? 0.3603 0.3991 0.4906 0.0536  -0.0349 -0.0397 98  MET B CG  
2428 S SD  A MET B 41  ? 0.3264 0.3270 0.4392 0.0544  -0.0560 -0.0261 98  MET B SD  
2429 S SD  B MET B 41  ? 0.3044 0.3238 0.4355 0.0705  -0.0567 -0.0335 98  MET B SD  
2430 C CE  A MET B 41  ? 0.5216 0.5596 0.6566 0.0583  -0.0681 -0.0245 98  MET B CE  
2431 C CE  B MET B 41  ? 0.3091 0.2869 0.4094 0.0538  -0.0606 -0.0218 98  MET B CE  
2432 N N   . VAL B 42  ? 0.3739 0.4614 0.5084 0.0280  0.0071  -0.0527 99  VAL B N   
2433 C CA  . VAL B 42  ? 0.4571 0.5927 0.6171 0.0220  0.0184  -0.0616 99  VAL B CA  
2434 C C   . VAL B 42  ? 0.5922 0.7603 0.7759 0.0119  0.0081  -0.0609 99  VAL B C   
2435 O O   . VAL B 42  ? 0.5046 0.6503 0.6750 0.0032  -0.0029 -0.0527 99  VAL B O   
2436 C CB  . VAL B 42  ? 0.4255 0.5579 0.5652 0.0011  0.0411  -0.0621 99  VAL B CB  
2437 C CG1 . VAL B 42  ? 0.5633 0.6581 0.6697 0.0093  0.0478  -0.0599 99  VAL B CG1 
2438 C CG2 . VAL B 42  ? 0.4944 0.6078 0.6163 -0.0242 0.0433  -0.0542 99  VAL B CG2 
2439 N N   . GLU B 43  ? 0.6414 0.8681 0.8611 0.0133  0.0118  -0.0710 100 GLU B N   
2440 C CA  . GLU B 43  ? 0.8155 1.0871 1.0604 -0.0023 0.0039  -0.0731 100 GLU B CA  
2441 C C   . GLU B 43  ? 0.8495 1.1397 1.0909 -0.0383 0.0253  -0.0777 100 GLU B C   
2442 O O   . GLU B 43  ? 0.7063 0.9743 0.9252 -0.0472 0.0461  -0.0777 100 GLU B O   
2443 C CB  . GLU B 43  ? 0.7575 1.0896 1.0475 0.0229  -0.0085 -0.0813 100 GLU B CB  
2444 C CG  . GLU B 43  ? 0.5925 0.8906 0.8751 0.0604  -0.0248 -0.0762 100 GLU B CG  
2445 C CD  . GLU B 43  ? 1.1193 1.3602 1.3715 0.0598  -0.0412 -0.0633 100 GLU B CD  
2446 O OE1 . GLU B 43  ? 1.2320 1.4747 1.4778 0.0409  -0.0503 -0.0572 100 GLU B OE1 
2447 O OE2 . GLU B 43  ? 1.1473 1.3388 1.3769 0.0752  -0.0434 -0.0592 100 GLU B OE2 
2448 N N   . GLN B 44  ? 0.7588 1.0872 1.0181 -0.0612 0.0198  -0.0814 101 GLN B N   
2449 C CA  . GLN B 44  ? 0.7457 1.0716 0.9880 -0.1004 0.0384  -0.0832 101 GLN B CA  
2450 C C   . GLN B 44  ? 0.6724 1.0317 0.9261 -0.1045 0.0593  -0.0897 101 GLN B C   
2451 O O   . GLN B 44  ? 0.7510 1.1577 1.0380 -0.0807 0.0557  -0.0957 101 GLN B O   
2452 C CB  . GLN B 44  ? 0.7982 1.1418 1.0442 -0.1188 0.0242  -0.0833 101 GLN B CB  
2453 C CG  . GLN B 44  ? 0.8370 1.1538 1.0708 -0.1125 0.0016  -0.0772 101 GLN B CG  
2454 C CD  . GLN B 44  ? 0.9684 1.2164 1.1540 -0.1356 0.0099  -0.0724 101 GLN B CD  
2455 O OE1 . GLN B 44  ? 0.9190 1.1501 1.0838 -0.1557 0.0057  -0.0723 101 GLN B OE1 
2456 N NE2 . GLN B 44  ? 0.8955 1.0925 1.0549 -0.1249 0.0208  -0.0659 101 GLN B NE2 
2457 N N   . GLY B 45  ? 0.4609 0.7878 0.6805 -0.1339 0.0814  -0.0875 102 GLY B N   
2458 C CA  . GLY B 45  ? 0.5817 0.9357 0.8039 -0.1459 0.1022  -0.0927 102 GLY B CA  
2459 C C   . GLY B 45  ? 0.5453 0.8519 0.7270 -0.1503 0.1248  -0.0875 102 GLY B C   
2460 O O   . GLY B 45  ? 0.6882 0.9612 0.8549 -0.1309 0.1244  -0.0833 102 GLY B O   
2461 N N   . VAL B 46  ? 0.5500 0.6940 1.3403 -0.1592 0.1461  -0.1688 103 VAL B N   
2462 C CA  . VAL B 46  ? 0.4938 0.6069 1.2392 -0.1589 0.1983  -0.1796 103 VAL B CA  
2463 C C   . VAL B 46  ? 0.4545 0.5913 1.2408 -0.1299 0.2111  -0.1924 103 VAL B C   
2464 O O   . VAL B 46  ? 0.4586 0.5631 1.1873 -0.1155 0.2297  -0.1912 103 VAL B O   
2465 C CB  . VAL B 46  ? 0.6432 0.7525 1.3737 -0.1859 0.2382  -0.1895 103 VAL B CB  
2466 C CG1 . VAL B 46  ? 0.6010 0.6689 1.2648 -0.1866 0.2896  -0.1958 103 VAL B CG1 
2467 C CG2 . VAL B 46  ? 0.6810 0.7645 1.3679 -0.2147 0.2236  -0.1773 103 VAL B CG2 
2468 N N   . GLU B 47  ? 0.4927 0.6755 1.3580 -0.1176 0.1988  -0.2020 104 GLU B N   
2469 C CA  . GLU B 47  ? 0.6310 0.8232 1.5233 -0.0920 0.2126  -0.2159 104 GLU B CA  
2470 C C   . GLU B 47  ? 0.5564 0.7332 1.4308 -0.0664 0.1832  -0.2058 104 GLU B C   
2471 O O   . GLU B 47  ? 0.6236 0.7809 1.4637 -0.0521 0.2042  -0.2126 104 GLU B O   
2472 C CB  . GLU B 47  ? 0.4549 0.6907 1.4325 -0.0852 0.2024  -0.2251 104 GLU B CB  
2473 C CG  . GLU B 47  ? 0.5269 0.7652 1.5207 -0.0760 0.2403  -0.2469 104 GLU B CG  
2474 C CD  . GLU B 47  ? 0.8046 1.0286 1.7558 -0.0991 0.2930  -0.2607 104 GLU B CD  
2475 O OE1 . GLU B 47  ? 0.6929 0.9227 1.6372 -0.1237 0.2999  -0.2569 104 GLU B OE1 
2476 O OE2 . GLU B 47  ? 0.9964 1.1991 1.9129 -0.0953 0.3257  -0.2737 104 GLU B OE2 
2477 N N   . ALA B 48  ? 0.3535 0.5349 1.2392 -0.0622 0.1327  -0.1879 105 ALA B N   
2478 C CA  . ALA B 48  ? 0.3439 0.5085 1.2057 -0.0399 0.1019  -0.1765 105 ALA B CA  
2479 C C   . ALA B 48  ? 0.4731 0.5947 1.2420 -0.0397 0.1199  -0.1690 105 ALA B C   
2480 O O   . ALA B 48  ? 0.3150 0.4176 1.0452 -0.0181 0.1158  -0.1659 105 ALA B O   
2481 C CB  . ALA B 48  ? 0.4239 0.5928 1.2951 -0.0394 0.0442  -0.1562 105 ALA B CB  
2482 N N   . CYS B 49  ? 0.5161 0.6063 1.2203 -0.0612 0.1368  -0.1619 106 CYS B N   
2483 C CA  . CYS B 49  ? 0.3763 0.4094 0.9654 -0.0564 0.1516  -0.1488 106 CYS B CA  
2484 C C   . CYS B 49  ? 0.5304 0.5503 1.0857 -0.0526 0.1998  -0.1604 106 CYS B C   
2485 O O   . CYS B 49  ? 0.5301 0.5201 1.0157 -0.0369 0.2038  -0.1514 106 CYS B O   
2486 C CB  . CYS B 49  ? 0.4314 0.4298 0.9643 -0.0796 0.1553  -0.1375 106 CYS B CB  
2487 S SG  . CYS B 49  ? 0.5232 0.5137 1.0478 -0.0855 0.1009  -0.1196 106 CYS B SG  
2488 N N   . LYS B 50  ? 0.4840 0.5269 1.0854 -0.0696 0.2366  -0.1797 107 LYS B N   
2489 C CA  . LYS B 50  ? 0.5667 0.5964 1.1333 -0.0714 0.2850  -0.1923 107 LYS B CA  
2490 C C   . LYS B 50  ? 0.5789 0.6224 1.1659 -0.0480 0.2851  -0.2032 107 LYS B C   
2491 O O   . LYS B 50  ? 0.5850 0.5984 1.0998 -0.0436 0.3059  -0.2014 107 LYS B O   
2492 C CB  . LYS B 50  ? 0.5288 0.5862 1.1498 -0.0969 0.3245  -0.2130 107 LYS B CB  
2493 C CG  . LYS B 50  ? 0.5348 0.5624 1.1068 -0.1253 0.3389  -0.2037 107 LYS B CG  
2494 C CD  . LYS B 50  ? 0.6812 0.7228 1.2760 -0.1489 0.3764  -0.2222 107 LYS B CD  
2495 C CE  . LYS B 50  ? 0.7177 0.8171 1.4175 -0.1445 0.3601  -0.2385 107 LYS B CE  
2496 N NZ  . LYS B 50  ? 0.5868 0.6996 1.3036 -0.1696 0.3848  -0.2504 107 LYS B NZ  
2497 N N   . ALA B 51  ? 0.5014 0.5823 1.1726 -0.0357 0.2555  -0.2102 108 ALA B N   
2498 C CA  . ALA B 51  ? 0.5531 0.6309 1.2190 -0.0178 0.2436  -0.2136 108 ALA B CA  
2499 C C   . ALA B 51  ? 0.5439 0.5926 1.1390 -0.0008 0.2222  -0.1959 108 ALA B C   
2500 O O   . ALA B 51  ? 0.5260 0.5566 1.0695 0.0052  0.2310  -0.1961 108 ALA B O   
2501 C CB  . ALA B 51  ? 0.5166 0.6284 1.2726 -0.0087 0.2107  -0.2184 108 ALA B CB  
2502 N N   . ALA B 52  ? 0.4494 0.4906 1.0334 0.0045  0.1913  -0.1787 109 ALA B N   
2503 C CA  . ALA B 52  ? 0.4143 0.4239 0.9192 0.0184  0.1661  -0.1578 109 ALA B CA  
2504 C C   . ALA B 52  ? 0.5190 0.4901 0.9237 0.0137  0.1973  -0.1489 109 ALA B C   
2505 O O   . ALA B 52  ? 0.6914 0.6456 1.0410 0.0253  0.1932  -0.1409 109 ALA B O   
2506 C CB  . ALA B 52  ? 0.4173 0.4214 0.9132 0.0173  0.1232  -0.1368 109 ALA B CB  
2507 N N   . VAL B 53  ? 0.5543 0.5108 0.9338 -0.0046 0.2274  -0.1488 110 VAL B N   
2508 C CA  . VAL B 53  ? 0.4831 0.3999 0.7670 -0.0095 0.2545  -0.1362 110 VAL B CA  
2509 C C   . VAL B 53  ? 0.5662 0.4834 0.8333 -0.0110 0.2875  -0.1514 110 VAL B C   
2510 O O   . VAL B 53  ? 0.6427 0.5375 0.8379 -0.0042 0.2878  -0.1384 110 VAL B O   
2511 C CB  . VAL B 53  ? 0.5558 0.4524 0.8188 -0.0308 0.2789  -0.1329 110 VAL B CB  
2512 C CG1 . VAL B 53  ? 0.6545 0.5147 0.8345 -0.0394 0.3161  -0.1255 110 VAL B CG1 
2513 C CG2 . VAL B 53  ? 0.5344 0.4115 0.7749 -0.0291 0.2490  -0.1126 110 VAL B CG2 
2514 N N   . ASN B 54  ? 0.5491 0.4917 0.8753 -0.0236 0.3092  -0.1749 111 ASN B N   
2515 C CA  . ASN B 54  ? 0.7915 0.7276 1.0855 -0.0331 0.3328  -0.1840 111 ASN B CA  
2516 C C   . ASN B 54  ? 0.7080 0.6442 0.9837 -0.0169 0.3131  -0.1823 111 ASN B C   
2517 O O   . ASN B 54  ? 0.7685 0.6835 0.9763 -0.0222 0.3268  -0.1785 111 ASN B O   
2518 C CB  . ASN B 54  ? 0.7540 0.7168 1.1193 -0.0477 0.3535  -0.2089 111 ASN B CB  
2519 C CG  . ASN B 54  ? 0.7018 0.6658 1.0852 -0.0674 0.3745  -0.2127 111 ASN B CG  
2520 O OD1 . ASN B 54  ? 0.8140 0.8110 1.2815 -0.0704 0.3700  -0.2253 111 ASN B OD1 
2521 N ND2 . ASN B 54  ? 0.6901 0.6169 0.9930 -0.0818 0.3958  -0.2002 111 ASN B ND2 
2522 N N   . SER B 55  ? 0.4700 0.4280 0.8029 0.0007  0.2793  -0.1841 112 SER B N   
2523 C CA  . SER B 55  ? 0.5631 0.5180 0.8778 0.0145  0.2601  -0.1829 112 SER B CA  
2524 C C   . SER B 55  ? 0.5939 0.5198 0.8194 0.0215  0.2528  -0.1621 112 SER B C   
2525 O O   . SER B 55  ? 0.5395 0.4511 0.7113 0.0198  0.2608  -0.1622 112 SER B O   
2526 C CB  . SER B 55  ? 0.5445 0.5238 0.9323 0.0303  0.2203  -0.1838 112 SER B CB  
2527 O OG  . SER B 55  ? 0.5486 0.5286 0.9437 0.0373  0.1928  -0.1676 112 SER B OG  
2528 N N   . LEU B 56  ? 0.5711 0.4864 0.7781 0.0285  0.2391  -0.1439 113 LEU B N   
2529 C CA  . LEU B 56  ? 0.5264 0.4180 0.6443 0.0336  0.2240  -0.1147 113 LEU B CA  
2530 C C   . LEU B 56  ? 0.6897 0.5570 0.7323 0.0193  0.2603  -0.1092 113 LEU B C   
2531 O O   . LEU B 56  ? 0.7429 0.5981 0.7194 0.0203  0.2565  -0.0952 113 LEU B O   
2532 C CB  . LEU B 56  ? 0.5724 0.4576 0.6818 0.0404  0.1970  -0.0913 113 LEU B CB  
2533 C CG  . LEU B 56  ? 0.5065 0.4140 0.6824 0.0505  0.1579  -0.0943 113 LEU B CG  
2534 C CD1 . LEU B 56  ? 0.4482 0.3492 0.6271 0.0487  0.1413  -0.0801 113 LEU B CD1 
2535 C CD2 . LEU B 56  ? 0.5284 0.4387 0.6817 0.0641  0.1259  -0.0836 113 LEU B CD2 
2536 N N   . LEU B 57  ? 0.5937 0.4544 0.6437 0.0031  0.2940  -0.1185 114 LEU B N   
2537 C CA  . LEU B 57  ? 0.8508 0.6876 0.8283 -0.0148 0.3185  -0.1083 114 LEU B CA  
2538 C C   . LEU B 57  ? 0.7847 0.6259 0.7477 -0.0253 0.3285  -0.1227 114 LEU B C   
2539 O O   . LEU B 57  ? 0.7366 0.5587 0.6265 -0.0352 0.3339  -0.1085 114 LEU B O   
2540 C CB  . LEU B 57  ? 0.7818 0.6107 0.7748 -0.0333 0.3432  -0.1140 114 LEU B CB  
2541 C CG  . LEU B 57  ? 0.7258 0.5409 0.7212 -0.0291 0.3398  -0.1003 114 LEU B CG  
2542 C CD1 . LEU B 57  ? 0.9770 0.7631 0.9330 -0.0500 0.3647  -0.0932 114 LEU B CD1 
2543 C CD2 . LEU B 57  ? 0.7148 0.5141 0.6621 -0.0078 0.3107  -0.0708 114 LEU B CD2 
2544 N N   . ALA B 58  ? 0.6087 0.4741 0.6411 -0.0234 0.3283  -0.1490 115 ALA B N   
2545 C CA  . ALA B 58  ? 0.6234 0.4880 0.6421 -0.0327 0.3396  -0.1646 115 ALA B CA  
2546 C C   . ALA B 58  ? 0.6670 0.5211 0.6269 -0.0243 0.3209  -0.1520 115 ALA B C   
2547 O O   . ALA B 58  ? 0.7189 0.5615 0.6321 -0.0380 0.3314  -0.1561 115 ALA B O   
2548 C CB  . ALA B 58  ? 0.6085 0.4990 0.7179 -0.0284 0.3407  -0.1923 115 ALA B CB  
2549 N N   . GLN B 59  ? 0.5795 0.4366 0.5389 -0.0040 0.2932  -0.1368 116 GLN B N   
2550 C CA  . GLN B 59  ? 0.6205 0.4690 0.5227 0.0033  0.2747  -0.1234 116 GLN B CA  
2551 C C   . GLN B 59  ? 0.7336 0.5698 0.5578 0.0044  0.2605  -0.0839 116 GLN B C   
2552 O O   . GLN B 59  ? 0.7633 0.6046 0.5568 0.0148  0.2269  -0.0612 116 GLN B O   
2553 C CB  . GLN B 59  ? 0.5550 0.4210 0.5144 0.0234  0.2346  -0.1249 116 GLN B CB  
2554 C CG  . GLN B 59  ? 0.5244 0.4000 0.5586 0.0258  0.2447  -0.1609 116 GLN B CG  
2555 C CD  . GLN B 59  ? 0.6041 0.4684 0.6040 0.0079  0.2683  -0.1771 116 GLN B CD  
2556 O OE1 . GLN B 59  ? 0.6362 0.4830 0.5535 -0.0032 0.2715  -0.1669 116 GLN B OE1 
2557 N NE2 . GLN B 59  ? 0.5877 0.4629 0.6500 0.0036  0.2832  -0.2002 116 GLN B NE2 
2558 N N   . ARG B 60  ? 0.7473 0.5709 0.5475 -0.0058 0.2789  -0.0725 117 ARG B N   
2559 C CA  . ARG B 60  ? 0.6771 0.4880 0.4075 -0.0068 0.2656  -0.0353 117 ARG B CA  
2560 C C   . ARG B 60  ? 0.6813 0.4927 0.4047 0.0167  0.2393  -0.0074 117 ARG B C   
2561 O O   . ARG B 60  ? 1.0333 0.8514 0.7171 0.0231  0.2110  0.0213  117 ARG B O   
2562 C CB  . ARG B 60  ? 0.9149 0.7298 0.5903 -0.0184 0.2532  -0.0246 117 ARG B CB  
2563 C CG  . ARG B 60  ? 0.8023 0.6109 0.4702 -0.0430 0.2790  -0.0482 117 ARG B CG  
2564 C CD  . ARG B 60  ? 0.9457 0.7600 0.5834 -0.0515 0.2684  -0.0531 117 ARG B CD  
2565 N NE  . ARG B 60  ? 0.9173 0.7383 0.5892 -0.0389 0.2617  -0.0713 117 ARG B NE  
2566 C CZ  . ARG B 60  ? 0.8829 0.7059 0.5308 -0.0428 0.2478  -0.0750 117 ARG B CZ  
2567 N NH1 . ARG B 60  ? 0.8292 0.6520 0.4240 -0.0604 0.2398  -0.0631 117 ARG B NH1 
2568 N NH2 . ARG B 60  ? 0.8053 0.6301 0.4866 -0.0289 0.2399  -0.0918 117 ARG B NH2 
2569 N N   . VAL B 61  ? 0.7152 0.5302 0.4953 0.0279  0.2351  -0.0154 118 VAL B N   
2570 C CA  . VAL B 61  ? 0.6197 0.4335 0.3955 0.0471  0.2069  0.0112  118 VAL B CA  
2571 C C   . VAL B 61  ? 0.6485 0.4336 0.3776 0.0456  0.2241  0.0342  118 VAL B C   
2572 O O   . VAL B 61  ? 0.6812 0.4521 0.4139 0.0287  0.2490  0.0230  118 VAL B O   
2573 C CB  . VAL B 61  ? 0.7062 0.5335 0.5560 0.0555  0.1889  -0.0036 118 VAL B CB  
2574 C CG1 . VAL B 61  ? 0.7117 0.5637 0.6149 0.0561  0.1739  -0.0278 118 VAL B CG1 
2575 C CG2 . VAL B 61  ? 0.6560 0.4712 0.5385 0.0446  0.2144  -0.0176 118 VAL B CG2 
2576 N N   . ASP B 62  ? 0.6177 0.4038 0.3263 0.0612  0.1947  0.0632  119 ASP B N   
2577 C CA  . ASP B 62  ? 0.5921 0.3631 0.2814 0.0606  0.1926  0.0800  119 ASP B CA  
2578 C C   . ASP B 62  ? 0.6393 0.3796 0.3405 0.0641  0.2093  0.0780  119 ASP B C   
2579 O O   . ASP B 62  ? 0.7371 0.4546 0.4218 0.0579  0.2208  0.0832  119 ASP B O   
2580 C CB  . ASP B 62  ? 0.5729 0.3689 0.2583 0.0735  0.1570  0.1012  119 ASP B CB  
2581 C CG  . ASP B 62  ? 0.8053 0.6339 0.4797 0.0629  0.1392  0.1044  119 ASP B CG  
2582 O OD1 . ASP B 62  ? 0.8932 0.7189 0.5465 0.0449  0.1555  0.0963  119 ASP B OD1 
2583 O OD2 . ASP B 62  ? 0.8600 0.7179 0.5488 0.0686  0.1101  0.1125  119 ASP B OD2 
2584 N N   . GLY B 63  ? 0.5907 0.3295 0.3182 0.0718  0.2109  0.0711  120 GLY B N   
2585 C CA  . GLY B 63  ? 0.5928 0.3036 0.3308 0.0711  0.2241  0.0697  120 GLY B CA  
2586 C C   . GLY B 63  ? 0.5615 0.2968 0.3647 0.0708  0.2018  0.0486  120 GLY B C   
2587 O O   . GLY B 63  ? 0.5303 0.2970 0.3576 0.0780  0.1759  0.0438  120 GLY B O   
2588 N N   . LEU B 64  ? 0.5842 0.3033 0.4132 0.0599  0.2109  0.0371  121 LEU B N   
2589 C CA  . LEU B 64  ? 0.5007 0.2435 0.3957 0.0532  0.1913  0.0162  121 LEU B CA  
2590 C C   . LEU B 64  ? 0.5513 0.2708 0.4395 0.0549  0.1802  0.0242  121 LEU B C   
2591 O O   . LEU B 64  ? 0.5768 0.2552 0.4221 0.0539  0.1999  0.0363  121 LEU B O   
2592 C CB  . LEU B 64  ? 0.5059 0.2620 0.4533 0.0308  0.2122  -0.0113 121 LEU B CB  
2593 C CG  . LEU B 64  ? 0.5421 0.3191 0.4998 0.0260  0.2293  -0.0252 121 LEU B CG  
2594 C CD1 . LEU B 64  ? 0.7246 0.5005 0.7083 0.0027  0.2651  -0.0460 121 LEU B CD1 
2595 C CD2 . LEU B 64  ? 0.4815 0.2977 0.4939 0.0342  0.2019  -0.0390 121 LEU B CD2 
2596 N N   . ILE B 65  ? 0.4882 0.2308 0.4160 0.0562  0.1486  0.0172  122 ILE B N   
2597 C CA  . ILE B 65  ? 0.4691 0.1930 0.3964 0.0511  0.1360  0.0190  122 ILE B CA  
2598 C C   . ILE B 65  ? 0.4438 0.1968 0.4420 0.0323  0.1181  -0.0027 122 ILE B C   
2599 O O   . ILE B 65  ? 0.4067 0.1975 0.4494 0.0365  0.0949  -0.0104 122 ILE B O   
2600 C CB  . ILE B 65  ? 0.4768 0.2003 0.3747 0.0701  0.1108  0.0367  122 ILE B CB  
2601 C CG1 . ILE B 65  ? 0.5060 0.2050 0.3408 0.0904  0.1281  0.0612  122 ILE B CG1 
2602 C CG2 . ILE B 65  ? 0.4853 0.1908 0.3844 0.0598  0.0972  0.0340  122 ILE B CG2 
2603 C CD1 . ILE B 65  ? 0.5127 0.2441 0.3344 0.1034  0.1010  0.0720  122 ILE B CD1 
2604 N N   . ILE B 66  ? 0.4676 0.2030 0.4774 0.0110  0.1286  -0.0117 123 ILE B N   
2605 C CA  . ILE B 66  ? 0.4564 0.2229 0.5381 -0.0099 0.1128  -0.0303 123 ILE B CA  
2606 C C   . ILE B 66  ? 0.4528 0.2065 0.5291 -0.0216 0.0867  -0.0269 123 ILE B C   
2607 O O   . ILE B 66  ? 0.4926 0.2072 0.5339 -0.0369 0.1022  -0.0258 123 ILE B O   
2608 C CB  . ILE B 66  ? 0.4773 0.2416 0.5829 -0.0323 0.1448  -0.0449 123 ILE B CB  
2609 C CG1 . ILE B 66  ? 0.5118 0.2737 0.5980 -0.0242 0.1782  -0.0459 123 ILE B CG1 
2610 C CG2 . ILE B 66  ? 0.4573 0.2683 0.6519 -0.0499 0.1268  -0.0630 123 ILE B CG2 
2611 C CD1 . ILE B 66  ? 0.4563 0.2652 0.5981 -0.0158 0.1719  -0.0590 123 ILE B CD1 
2612 N N   . ASN B 67  ? 0.4253 0.2088 0.5346 -0.0180 0.0476  -0.0264 124 ASN B N   
2613 C CA  . ASN B 67  ? 0.4226 0.1983 0.5308 -0.0351 0.0195  -0.0248 124 ASN B CA  
2614 C C   . ASN B 67  ? 0.4171 0.2347 0.6074 -0.0561 -0.0058 -0.0375 124 ASN B C   
2615 O O   . ASN B 67  ? 0.3964 0.2450 0.6265 -0.0538 -0.0439 -0.0357 124 ASN B O   
2616 C CB  . ASN B 67  ? 0.4231 0.1971 0.4988 -0.0193 -0.0084 -0.0113 124 ASN B CB  
2617 C CG  . ASN B 67  ? 0.4213 0.1795 0.4815 -0.0405 -0.0328 -0.0098 124 ASN B CG  
2618 O OD1 . ASN B 67  ? 0.5167 0.2484 0.5640 -0.0641 -0.0202 -0.0159 124 ASN B OD1 
2619 N ND2 . ASN B 67  ? 0.4131 0.1858 0.4719 -0.0362 -0.0677 -0.0025 124 ASN B ND2 
2620 N N   . VAL B 68  ? 0.4257 0.2448 0.6431 -0.0773 0.0154  -0.0489 125 VAL B N   
2621 C CA  . VAL B 68  ? 0.4476 0.3093 0.7473 -0.0999 -0.0055 -0.0596 125 VAL B CA  
2622 C C   . VAL B 68  ? 0.5066 0.3427 0.7882 -0.1342 0.0078  -0.0642 125 VAL B C   
2623 O O   . VAL B 68  ? 0.4949 0.2947 0.7317 -0.1381 0.0480  -0.0667 125 VAL B O   
2624 C CB  . VAL B 68  ? 0.3984 0.3042 0.7713 -0.0908 0.0101  -0.0727 125 VAL B CB  
2625 C CG1 . VAL B 68  ? 0.4408 0.3971 0.9095 -0.1113 -0.0122 -0.0820 125 VAL B CG1 
2626 C CG2 . VAL B 68  ? 0.3573 0.2788 0.7364 -0.0589 0.0010  -0.0696 125 VAL B CG2 
2627 N N   . PRO B 69  ? 0.4678 0.3187 0.7787 -0.1620 -0.0250 -0.0645 126 PRO B N   
2628 C CA  . PRO B 69  ? 0.5379 0.3652 0.8266 -0.1988 -0.0125 -0.0694 126 PRO B CA  
2629 C C   . PRO B 69  ? 0.5202 0.3754 0.8598 -0.2100 0.0164  -0.0816 126 PRO B C   
2630 O O   . PRO B 69  ? 0.5694 0.4866 0.9922 -0.2051 0.0038  -0.0867 126 PRO B O   
2631 C CB  . PRO B 69  ? 0.5696 0.4272 0.8672 -0.2174 -0.0573 -0.0624 126 PRO B CB  
2632 C CG  . PRO B 69  ? 0.5635 0.4682 0.9098 -0.1895 -0.0904 -0.0556 126 PRO B CG  
2633 C CD  . PRO B 69  ? 0.5905 0.4761 0.9304 -0.1587 -0.0748 -0.0560 126 PRO B CD  
2634 N N   . LEU B 70  ? 0.5659 0.3739 0.8498 -0.2225 0.0570  -0.0853 127 LEU B N   
2635 C CA  . LEU B 70  ? 0.5825 0.4101 0.9001 -0.2351 0.0893  -0.0964 127 LEU B CA  
2636 C C   . LEU B 70  ? 0.7171 0.5032 0.9752 -0.2637 0.1068  -0.0955 127 LEU B C   
2637 O O   . LEU B 70  ? 0.6823 0.4045 0.8536 -0.2598 0.1196  -0.0880 127 LEU B O   
2638 C CB  . LEU B 70  ? 0.5715 0.3858 0.8787 -0.2110 0.1302  -0.1006 127 LEU B CB  
2639 C CG  . LEU B 70  ? 0.5195 0.3772 0.8723 -0.1757 0.1147  -0.1000 127 LEU B CG  
2640 C CD1 . LEU B 70  ? 0.5226 0.3513 0.8213 -0.1494 0.1497  -0.0965 127 LEU B CD1 
2641 C CD2 . LEU B 70  ? 0.5057 0.4363 0.9708 -0.1822 0.1061  -0.1140 127 LEU B CD2 
2642 N N   . GLU B 71  ? 0.6811 0.5059 0.9882 -0.2893 0.1073  -0.1025 128 GLU B N   
2643 C CA  . GLU B 71  ? 0.7722 0.5608 1.0300 -0.3164 0.1277  -0.1033 128 GLU B CA  
2644 C C   . GLU B 71  ? 0.7802 0.5293 0.9924 -0.3063 0.1794  -0.1080 128 GLU B C   
2645 O O   . GLU B 71  ? 0.7462 0.5014 0.9712 -0.2820 0.1988  -0.1106 128 GLU B O   
2646 C CB  . GLU B 71  ? 0.8657 0.7112 1.1918 -0.3475 0.1118  -0.1076 128 GLU B CB  
2647 C CG  . GLU B 71  ? 0.8324 0.6995 1.1749 -0.3680 0.0595  -0.0965 128 GLU B CG  
2648 C CD  . GLU B 71  ? 1.0510 0.8568 1.3143 -0.3642 0.0434  -0.0870 128 GLU B CD  
2649 O OE1 . GLU B 71  ? 1.0260 0.7760 1.2205 -0.3746 0.0640  -0.0882 128 GLU B OE1 
2650 O OE2 . GLU B 71  ? 0.9752 0.7903 1.2442 -0.3496 0.0122  -0.0797 128 GLU B OE2 
2651 N N   . ASN B 72  ? 0.8105 0.5168 0.9655 -0.3260 0.2006  -0.1079 129 ASN B N   
2652 C CA  . ASN B 72  ? 0.9166 0.5789 1.0168 -0.3187 0.2464  -0.1091 129 ASN B CA  
2653 C C   . ASN B 72  ? 0.8216 0.5279 0.9801 -0.3146 0.2707  -0.1197 129 ASN B C   
2654 O O   . ASN B 72  ? 0.8530 0.5455 0.9943 -0.2893 0.2907  -0.1173 129 ASN B O   
2655 C CB  . ASN B 72  ? 1.1227 0.7479 1.1742 -0.3466 0.2614  -0.1108 129 ASN B CB  
2656 C CG  . ASN B 72  ? 1.2705 0.8420 1.2547 -0.3383 0.3047  -0.1093 129 ASN B CG  
2657 O OD1 . ASN B 72  ? 1.3997 0.9293 1.3298 -0.3085 0.3165  -0.0993 129 ASN B OD1 
2658 N ND2 . ASN B 72  ? 1.2552 0.8301 1.2431 -0.3646 0.3267  -0.1179 129 ASN B ND2 
2659 N N   . GLU B 73  ? 0.8209 0.5826 1.0488 -0.3394 0.2694  -0.1311 130 GLU B N   
2660 C CA  . GLU B 73  ? 0.8836 0.6873 1.1646 -0.3378 0.2981  -0.1443 130 GLU B CA  
2661 C C   . GLU B 73  ? 0.7431 0.5838 1.0774 -0.3074 0.2923  -0.1476 130 GLU B C   
2662 O O   . GLU B 73  ? 0.7403 0.5742 1.0643 -0.2928 0.3239  -0.1523 130 GLU B O   
2663 C CB  . GLU B 73  ? 0.8137 0.6803 1.1712 -0.3664 0.2908  -0.1545 130 GLU B CB  
2664 C CG  . GLU B 73  ? 0.9256 0.7611 1.2378 -0.4004 0.2904  -0.1509 130 GLU B CG  
2665 C CD  . GLU B 73  ? 1.1457 1.0221 1.5029 -0.4272 0.3110  -0.1626 130 GLU B CD  
2666 O OE1 . GLU B 73  ? 1.1939 1.0684 1.5462 -0.4216 0.3492  -0.1725 130 GLU B OE1 
2667 O OE2 . GLU B 73  ? 1.1478 1.0585 1.5436 -0.4549 0.2883  -0.1611 130 GLU B OE2 
2668 N N   . ASP B 74  ? 0.6957 0.5737 1.0831 -0.2983 0.2506  -0.1443 131 ASP B N   
2669 C CA  . ASP B 74  ? 0.6453 0.5595 1.0878 -0.2688 0.2411  -0.1478 131 ASP B CA  
2670 C C   . ASP B 74  ? 0.7589 0.6152 1.1279 -0.2444 0.2548  -0.1380 131 ASP B C   
2671 O O   . ASP B 74  ? 0.6151 0.4870 1.0046 -0.2224 0.2675  -0.1422 131 ASP B O   
2672 C CB  . ASP B 74  ? 0.6714 0.6333 1.1784 -0.2646 0.1882  -0.1431 131 ASP B CB  
2673 C CG  . ASP B 74  ? 0.6355 0.6703 1.2351 -0.2781 0.1751  -0.1510 131 ASP B CG  
2674 O OD1 . ASP B 74  ? 0.7511 0.8037 1.3725 -0.2884 0.2095  -0.1634 131 ASP B OD1 
2675 O OD2 . ASP B 74  ? 0.6954 0.7683 1.3411 -0.2781 0.1303  -0.1432 131 ASP B OD2 
2676 N N   . ALA B 75  ? 0.6673 0.4572 0.9457 -0.2451 0.2518  -0.1235 132 ALA B N   
2677 C CA  . ALA B 75  ? 0.6788 0.4130 0.8823 -0.2185 0.2650  -0.1102 132 ALA B CA  
2678 C C   . ALA B 75  ? 0.7082 0.4138 0.8666 -0.2162 0.3109  -0.1099 132 ALA B C   
2679 O O   . ALA B 75  ? 0.6972 0.3925 0.8245 -0.1882 0.3190  -0.1015 132 ALA B O   
2680 C CB  . ALA B 75  ? 0.7274 0.4035 0.8492 -0.2151 0.2504  -0.0947 132 ALA B CB  
2681 N N   . GLN B 76  ? 0.7544 0.4538 0.9008 -0.2405 0.3336  -0.1169 133 GLN B N   
2682 C CA  . GLN B 76  ? 0.7937 0.4695 0.8982 -0.2415 0.3743  -0.1178 133 GLN B CA  
2683 C C   . GLN B 76  ? 0.7753 0.5048 0.9442 -0.2365 0.3902  -0.1324 133 GLN B C   
2684 O O   . GLN B 76  ? 0.7930 0.5024 0.9197 -0.2247 0.4151  -0.1282 133 GLN B O   
2685 C CB  . GLN B 76  ? 0.8518 0.5131 0.9361 -0.2711 0.3912  -0.1245 133 GLN B CB  
2686 C CG  . GLN B 76  ? 0.8973 0.5011 0.9114 -0.2765 0.3809  -0.1122 133 GLN B CG  
2687 C CD  . GLN B 76  ? 1.0391 0.6141 1.0149 -0.3028 0.4047  -0.1170 133 GLN B CD  
2688 O OE1 . GLN B 76  ? 0.9987 0.5591 0.9489 -0.3049 0.4344  -0.1195 133 GLN B OE1 
2689 N NE2 . GLN B 76  ? 0.9947 0.5592 0.9628 -0.3245 0.3902  -0.1181 133 GLN B NE2 
2690 N N   . ALA B 77  ? 0.7162 0.5159 0.9857 -0.2435 0.3739  -0.1491 134 ALA B N   
2691 C CA  . ALA B 77  ? 0.6865 0.5407 1.0226 -0.2346 0.3887  -0.1659 134 ALA B CA  
2692 C C   . ALA B 77  ? 0.6541 0.5085 0.9799 -0.2003 0.3760  -0.1584 134 ALA B C   
2693 O O   . ALA B 77  ? 0.6480 0.5124 0.9710 -0.1897 0.3995  -0.1659 134 ALA B O   
2694 C CB  . ALA B 77  ? 0.6702 0.6001 1.1173 -0.2420 0.3676  -0.1824 134 ALA B CB  
2695 N N   . VAL B 78  ? 0.6188 0.4622 0.9300 -0.1807 0.3351  -0.1436 135 VAL B N   
2696 C CA  . VAL B 78  ? 0.5862 0.4293 0.8764 -0.1453 0.3162  -0.1342 135 VAL B CA  
2697 C C   . VAL B 78  ? 0.6237 0.4097 0.8124 -0.1345 0.3399  -0.1175 135 VAL B C   
2698 O O   . VAL B 78  ? 0.6187 0.4103 0.7913 -0.1187 0.3508  -0.1178 135 VAL B O   
2699 C CB  . VAL B 78  ? 0.5919 0.4383 0.8904 -0.1309 0.2672  -0.1223 135 VAL B CB  
2700 C CG1 . VAL B 78  ? 0.5280 0.3609 0.7818 -0.0974 0.2504  -0.1079 135 VAL B CG1 
2701 C CG2 . VAL B 78  ? 0.5671 0.4770 0.9721 -0.1370 0.2388  -0.1359 135 VAL B CG2 
2702 N N   . ALA B 79  ? 0.6672 0.3959 0.7859 -0.1443 0.3485  -0.1023 136 ALA B N   
2703 C CA  . ALA B 79  ? 0.7549 0.4271 0.7801 -0.1345 0.3707  -0.0828 136 ALA B CA  
2704 C C   . ALA B 79  ? 0.7608 0.4377 0.7765 -0.1464 0.4096  -0.0920 136 ALA B C   
2705 O O   . ALA B 79  ? 0.7841 0.4460 0.7499 -0.1306 0.4177  -0.0801 136 ALA B O   
2706 C CB  . ALA B 79  ? 0.7639 0.3719 0.7270 -0.1481 0.3804  -0.0692 136 ALA B CB  
2707 N N   . GLN B 80  ? 0.7552 0.4552 0.8185 -0.1767 0.4339  -0.1130 137 GLN B N   
2708 C CA  . GLN B 80  ? 0.7908 0.4956 0.8410 -0.1857 0.4605  -0.1256 137 GLN B CA  
2709 C C   . GLN B 80  ? 0.8525 0.5959 0.9323 -0.1687 0.4589  -0.1355 137 GLN B C   
2710 O O   . GLN B 80  ? 0.8883 0.6133 0.9174 -0.1663 0.4682  -0.1321 137 GLN B O   
2711 C CB  . GLN B 80  ? 0.9803 0.7141 1.0862 -0.2148 0.4746  -0.1486 137 GLN B CB  
2712 C CG  . GLN B 80  ? 0.9027 0.6433 1.0020 -0.2274 0.5008  -0.1643 137 GLN B CG  
2713 C CD  . GLN B 80  ? 1.1083 0.8728 1.2522 -0.2562 0.5154  -0.1834 137 GLN B CD  
2714 O OE1 . GLN B 80  ? 1.1500 0.8842 1.2459 -0.2749 0.5364  -0.1846 137 GLN B OE1 
2715 N NE2 . GLN B 80  ? 1.1130 0.9346 1.3508 -0.2600 0.5012  -0.1969 137 GLN B NE2 
2716 N N   . ALA B 81  ? 0.8134 0.6093 0.9748 -0.1576 0.4429  -0.1473 138 ALA B N   
2717 C CA  . ALA B 81  ? 0.6875 0.5175 0.8795 -0.1401 0.4377  -0.1598 138 ALA B CA  
2718 C C   . ALA B 81  ? 0.9291 0.7282 1.0429 -0.1175 0.4258  -0.1385 138 ALA B C   
2719 O O   . ALA B 81  ? 0.9082 0.7153 1.0106 -0.1123 0.4266  -0.1440 138 ALA B O   
2720 C CB  . ALA B 81  ? 0.8104 0.6980 1.1058 -0.1276 0.4113  -0.1743 138 ALA B CB  
2721 N N   . CYS B 82  ? 0.8668 0.6302 0.9248 -0.1046 0.4092  -0.1125 139 CYS B N   
2722 C CA  . CYS B 82  ? 1.0058 0.7474 0.9962 -0.0819 0.3956  -0.0904 139 CYS B CA  
2723 C C   . CYS B 82  ? 0.7970 0.5042 0.7118 -0.0897 0.4066  -0.0770 139 CYS B C   
2724 O O   . CYS B 82  ? 0.8326 0.5275 0.6949 -0.0734 0.3908  -0.0569 139 CYS B O   
2725 C CB  . CYS B 82  ? 0.7476 0.4615 0.7023 -0.0631 0.3635  -0.0640 139 CYS B CB  
2726 S SG  . CYS B 82  ? 0.7663 0.5134 0.7994 -0.0566 0.3233  -0.0733 139 CYS B SG  
2727 N N   . GLY B 83  ? 0.7796 0.4746 0.6906 -0.1139 0.4299  -0.0878 140 GLY B N   
2728 C CA  . GLY B 83  ? 0.8323 0.4970 0.6757 -0.1219 0.4381  -0.0768 140 GLY B CA  
2729 C C   . GLY B 83  ? 0.9197 0.5399 0.6905 -0.1061 0.4218  -0.0432 140 GLY B C   
2730 O O   . GLY B 83  ? 0.9471 0.5373 0.7051 -0.1052 0.4217  -0.0338 140 GLY B O   
2731 N N   . ASN B 84  ? 0.8704 0.4885 0.5965 -0.0930 0.4063  -0.0253 141 ASN B N   
2732 C CA  . ASN B 84  ? 0.9164 0.5042 0.5851 -0.0745 0.3866  0.0068  141 ASN B CA  
2733 C C   . ASN B 84  ? 0.9642 0.5680 0.6340 -0.0456 0.3570  0.0237  141 ASN B C   
2734 O O   . ASN B 84  ? 0.8493 0.4413 0.4826 -0.0274 0.3367  0.0494  141 ASN B O   
2735 C CB  . ASN B 84  ? 1.0373 0.6161 0.6565 -0.0832 0.3881  0.0179  141 ASN B CB  
2736 C CG  . ASN B 84  ? 1.1938 0.7436 0.7950 -0.1083 0.4137  0.0100  141 ASN B CG  
2737 O OD1 . ASN B 84  ? 1.2703 0.8233 0.9080 -0.1272 0.4359  -0.0145 141 ASN B OD1 
2738 N ND2 . ASN B 84  ? 1.3178 0.8428 0.8661 -0.1092 0.4098  0.0311  141 ASN B ND2 
2739 N N   . VAL B 85  ? 0.8683 0.5028 0.5840 -0.0408 0.3533  0.0093  142 VAL B N   
2740 C CA  . VAL B 85  ? 0.7538 0.4015 0.4705 -0.0145 0.3258  0.0247  142 VAL B CA  
2741 C C   . VAL B 85  ? 0.7636 0.3856 0.4814 -0.0033 0.3206  0.0349  142 VAL B C   
2742 O O   . VAL B 85  ? 0.8027 0.4177 0.5521 -0.0183 0.3387  0.0185  142 VAL B O   
2743 C CB  . VAL B 85  ? 0.7871 0.4750 0.5526 -0.0132 0.3241  0.0042  142 VAL B CB  
2744 C CG1 . VAL B 85  ? 0.7003 0.3995 0.4647 0.0127  0.2963  0.0197  142 VAL B CG1 
2745 C CG2 . VAL B 85  ? 0.8744 0.5819 0.6324 -0.0241 0.3287  -0.0067 142 VAL B CG2 
2746 N N   . PRO B 86  ? 0.7329 0.3446 0.4222 0.0208  0.2962  0.0589  143 PRO B N   
2747 C CA  . PRO B 86  ? 0.7626 0.3505 0.4529 0.0323  0.2907  0.0650  143 PRO B CA  
2748 C C   . PRO B 86  ? 0.7791 0.3809 0.5098 0.0286  0.2916  0.0530  143 PRO B C   
2749 O O   . PRO B 86  ? 0.6860 0.3246 0.4415 0.0360  0.2765  0.0488  143 PRO B O   
2750 C CB  . PRO B 86  ? 0.7922 0.3913 0.4632 0.0606  0.2612  0.0864  143 PRO B CB  
2751 C CG  . PRO B 86  ? 0.8490 0.4608 0.4978 0.0571  0.2577  0.0957  143 PRO B CG  
2752 C CD  . PRO B 86  ? 0.7335 0.3617 0.3952 0.0361  0.2726  0.0785  143 PRO B CD  
2753 N N   . VAL B 87  ? 0.7246 0.3010 0.4678 0.0153  0.3035  0.0453  144 VAL B N   
2754 C CA  . VAL B 87  ? 0.6915 0.2980 0.4971 0.0095  0.2813  0.0254  144 VAL B CA  
2755 C C   . VAL B 87  ? 0.7110 0.2790 0.4992 0.0091  0.2767  0.0317  144 VAL B C   
2756 O O   . VAL B 87  ? 0.7460 0.2712 0.4994 -0.0008 0.2989  0.0352  144 VAL B O   
2757 C CB  . VAL B 87  ? 0.6739 0.3114 0.5417 -0.0171 0.2936  -0.0045 144 VAL B CB  
2758 C CG1 . VAL B 87  ? 0.7169 0.3176 0.5642 -0.0428 0.3291  -0.0090 144 VAL B CG1 
2759 C CG2 . VAL B 87  ? 0.6470 0.3187 0.5826 -0.0220 0.2646  -0.0209 144 VAL B CG2 
2760 N N   . LEU B 88  ? 0.6802 0.2675 0.4918 0.0192  0.2453  0.0305  145 LEU B N   
2761 C CA  . LEU B 88  ? 0.6536 0.2111 0.4489 0.0181  0.2366  0.0336  145 LEU B CA  
2762 C C   . LEU B 88  ? 0.6419 0.2287 0.4960 -0.0009 0.2121  0.0133  145 LEU B C   
2763 O O   . LEU B 88  ? 0.5665 0.2039 0.4694 0.0031  0.1874  0.0052  145 LEU B O   
2764 C CB  . LEU B 88  ? 0.7673 0.3405 0.5348 0.0469  0.2145  0.0506  145 LEU B CB  
2765 C CG  . LEU B 88  ? 0.7550 0.3318 0.4833 0.0706  0.2212  0.0668  145 LEU B CG  
2766 C CD1 . LEU B 88  ? 0.7572 0.3578 0.4789 0.0909  0.1989  0.0742  145 LEU B CD1 
2767 C CD2 . LEU B 88  ? 0.9307 0.4684 0.6279 0.0649  0.2473  0.0660  145 LEU B CD2 
2768 N N   . PHE B 89  ? 0.6589 0.2147 0.5063 -0.0220 0.2161  0.0062  146 PHE B N   
2769 C CA  . PHE B 89  ? 0.6367 0.2199 0.5358 -0.0445 0.1899  -0.0104 146 PHE B CA  
2770 C C   . PHE B 89  ? 0.6722 0.2334 0.5403 -0.0423 0.1701  -0.0042 146 PHE B C   
2771 O O   . PHE B 89  ? 0.6671 0.1993 0.4821 -0.0352 0.1829  0.0043  146 PHE B O   
2772 C CB  . PHE B 89  ? 0.6537 0.2292 0.5760 -0.0799 0.2075  -0.0265 146 PHE B CB  
2773 C CG  . PHE B 89  ? 0.6432 0.2529 0.6080 -0.0868 0.2258  -0.0374 146 PHE B CG  
2774 C CD1 . PHE B 89  ? 0.6764 0.2581 0.5983 -0.0798 0.2603  -0.0296 146 PHE B CD1 
2775 C CD2 . PHE B 89  ? 0.6029 0.2736 0.6514 -0.0996 0.2086  -0.0546 146 PHE B CD2 
2776 C CE1 . PHE B 89  ? 0.7223 0.3340 0.6786 -0.0893 0.2802  -0.0415 146 PHE B CE1 
2777 C CE2 . PHE B 89  ? 0.5967 0.2993 0.6864 -0.1052 0.2298  -0.0671 146 PHE B CE2 
2778 C CZ  . PHE B 89  ? 0.6555 0.3281 0.6966 -0.1015 0.2667  -0.0617 146 PHE B CZ  
2779 N N   . LEU B 90  ? 0.5570 0.3091 0.3151 -0.0354 0.0766  -0.0188 147 LEU B N   
2780 C CA  . LEU B 90  ? 0.5071 0.2683 0.2924 -0.0299 0.0607  -0.0105 147 LEU B CA  
2781 C C   . LEU B 90  ? 0.4643 0.2674 0.2908 -0.0260 0.0675  -0.0192 147 LEU B C   
2782 O O   . LEU B 90  ? 0.5868 0.3985 0.4355 -0.0229 0.0561  -0.0129 147 LEU B O   
2783 C CB  . LEU B 90  ? 0.5395 0.2854 0.3204 -0.0177 0.0412  -0.0067 147 LEU B CB  
2784 C CG  . LEU B 90  ? 0.5363 0.2439 0.2788 -0.0216 0.0305  0.0022  147 LEU B CG  
2785 C CD1 . LEU B 90  ? 0.5427 0.2407 0.2833 -0.0161 0.0101  0.0069  147 LEU B CD1 
2786 C CD2 . LEU B 90  ? 0.6129 0.3067 0.3418 -0.0326 0.0270  0.0132  147 LEU B CD2 
2787 N N   . ASP B 91  ? 0.5461 0.3795 0.3841 -0.0263 0.0855  -0.0349 148 ASP B N   
2788 C CA  . ASP B 91  ? 0.6156 0.4939 0.4950 -0.0211 0.0901  -0.0454 148 ASP B CA  
2789 C C   . ASP B 91  ? 0.5283 0.4444 0.4149 -0.0350 0.1147  -0.0599 148 ASP B C   
2790 O O   . ASP B 91  ? 0.5369 0.4890 0.4380 -0.0232 0.1241  -0.0796 148 ASP B O   
2791 C CB  . ASP B 91  ? 0.5599 0.4470 0.4557 0.0048  0.0768  -0.0554 148 ASP B CB  
2792 C CG  . ASP B 91  ? 0.7692 0.6911 0.7052 0.0129  0.0726  -0.0617 148 ASP B CG  
2793 O OD1 . ASP B 91  ? 0.6873 0.6176 0.6345 0.0351  0.0621  -0.0737 148 ASP B OD1 
2794 O OD2 . ASP B 91  ? 0.8420 0.7780 0.7940 -0.0023 0.0779  -0.0551 148 ASP B OD2 
2795 N N   . VAL B 92  ? 0.6237 0.5322 0.4968 -0.0608 0.1244  -0.0517 149 VAL B N   
2796 C CA  . VAL B 92  ? 0.6285 0.5672 0.4972 -0.0845 0.1488  -0.0631 149 VAL B CA  
2797 C C   . VAL B 92  ? 0.7651 0.7122 0.6426 -0.1059 0.1519  -0.0571 149 VAL B C   
2798 O O   . VAL B 92  ? 0.6497 0.5631 0.5211 -0.1051 0.1360  -0.0410 149 VAL B O   
2799 C CB  . VAL B 92  ? 0.6693 0.5710 0.4855 -0.1039 0.1599  -0.0592 149 VAL B CB  
2800 C CG1 . VAL B 92  ? 0.6381 0.5433 0.4463 -0.0860 0.1629  -0.0708 149 VAL B CG1 
2801 C CG2 . VAL B 92  ? 0.6574 0.4931 0.4362 -0.1086 0.1423  -0.0369 149 VAL B CG2 
2802 N N   . SER B 93  ? 0.9115 0.9067 0.8021 -0.1257 0.1726  -0.0716 150 SER B N   
2803 C CA  . SER B 93  ? 0.8865 0.8827 0.7703 -0.1558 0.1790  -0.0663 150 SER B CA  
2804 C C   . SER B 93  ? 1.0159 0.9512 0.8338 -0.1863 0.1838  -0.0530 150 SER B C   
2805 O O   . SER B 93  ? 1.0243 0.9284 0.8092 -0.1839 0.1850  -0.0508 150 SER B O   
2806 C CB  . SER B 93  ? 0.9018 0.9759 0.8202 -0.1705 0.1998  -0.0881 150 SER B CB  
2807 O OG  . SER B 93  ? 0.8421 0.9463 0.7475 -0.1825 0.2218  -0.1044 150 SER B OG  
2808 N N   . PRO B 94  ? 0.9922 0.9013 0.7833 -0.2148 0.1839  -0.0436 151 PRO B N   
2809 C CA  . PRO B 94  ? 0.9213 0.7682 0.6438 -0.2424 0.1832  -0.0343 151 PRO B CA  
2810 C C   . PRO B 94  ? 0.9470 0.8122 0.6531 -0.2567 0.2001  -0.0473 151 PRO B C   
2811 O O   . PRO B 94  ? 0.9459 0.8735 0.6783 -0.2710 0.2161  -0.0646 151 PRO B O   
2812 C CB  . PRO B 94  ? 0.9847 0.8289 0.6995 -0.2640 0.1774  -0.0334 151 PRO B CB  
2813 C CG  . PRO B 94  ? 0.9059 0.7690 0.6645 -0.2451 0.1689  -0.0285 151 PRO B CG  
2814 C CD  . PRO B 94  ? 1.0151 0.9401 0.8330 -0.2179 0.1768  -0.0409 151 PRO B CD  
2815 N N   . ALA B 95  ? 1.0621 0.8761 0.7270 -0.2511 0.1950  -0.0401 152 ALA B N   
2816 C CA  . ALA B 95  ? 1.2726 1.1006 0.9224 -0.2602 0.2103  -0.0518 152 ALA B CA  
2817 C C   . ALA B 95  ? 1.1472 0.8937 0.7310 -0.2685 0.1968  -0.0398 152 ALA B C   
2818 O O   . ALA B 95  ? 1.2366 0.9258 0.7979 -0.2523 0.1748  -0.0244 152 ALA B O   
2819 C CB  . ALA B 95  ? 1.0923 0.9632 0.7768 -0.2310 0.2210  -0.0628 152 ALA B CB  
2820 N N   . PRO B 96  ? 1.1073 0.8495 0.6606 -0.2922 0.2078  -0.0483 153 PRO B N   
2821 C CA  . PRO B 96  ? 1.0837 0.7490 0.5741 -0.2982 0.1951  -0.0399 153 PRO B CA  
2822 C C   . PRO B 96  ? 1.1272 0.7802 0.6165 -0.2726 0.1938  -0.0371 153 PRO B C   
2823 O O   . PRO B 96  ? 1.0492 0.6900 0.5122 -0.2813 0.2016  -0.0422 153 PRO B O   
2824 C CB  . PRO B 96  ? 1.1581 0.8334 0.6216 -0.3368 0.2106  -0.0523 153 PRO B CB  
2825 C CG  . PRO B 96  ? 1.0771 0.8500 0.6003 -0.3372 0.2355  -0.0698 153 PRO B CG  
2826 C CD  . PRO B 96  ? 1.0743 0.8847 0.6497 -0.3157 0.2309  -0.0675 153 PRO B CD  
2827 N N   . VAL B 97  ? 1.0480 0.7027 0.5635 -0.2417 0.1832  -0.0289 154 VAL B N   
2828 C CA  . VAL B 97  ? 1.1160 0.7566 0.6284 -0.2159 0.1785  -0.0257 154 VAL B CA  
2829 C C   . VAL B 97  ? 1.0778 0.6686 0.5799 -0.1944 0.1490  -0.0083 154 VAL B C   
2830 O O   . VAL B 97  ? 0.9474 0.5293 0.4570 -0.1933 0.1354  -0.0015 154 VAL B O   
2831 C CB  . VAL B 97  ? 0.9894 0.6963 0.5492 -0.1955 0.1955  -0.0396 154 VAL B CB  
2832 C CG1 . VAL B 97  ? 0.9707 0.7443 0.5536 -0.2102 0.2215  -0.0617 154 VAL B CG1 
2833 C CG2 . VAL B 97  ? 0.7649 0.5034 0.3827 -0.1743 0.1808  -0.0368 154 VAL B CG2 
2834 N N   . ASN B 98  ? 0.9070 0.4701 0.3942 -0.1757 0.1372  -0.0031 155 ASN B N   
2835 C CA  . ASN B 98  ? 0.8876 0.4255 0.3814 -0.1512 0.1085  0.0095  155 ASN B CA  
2836 C C   . ASN B 98  ? 0.9202 0.5088 0.4761 -0.1300 0.1054  0.0078  155 ASN B C   
2837 O O   . ASN B 98  ? 0.7999 0.4283 0.3877 -0.1186 0.1146  -0.0030 155 ASN B O   
2838 C CB  . ASN B 98  ? 0.8618 0.3676 0.3320 -0.1377 0.0938  0.0124  155 ASN B CB  
2839 C CG  . ASN B 98  ? 0.9493 0.4100 0.3724 -0.1495 0.0851  0.0104  155 ASN B CG  
2840 O OD1 . ASN B 98  ? 1.0378 0.4751 0.4442 -0.1507 0.0689  0.0126  155 ASN B OD1 
2841 N ND2 . ASN B 98  ? 0.9556 0.3999 0.3525 -0.1563 0.0943  0.0057  155 ASN B ND2 
2842 N N   . SER B 99  ? 0.7477 0.3362 0.3228 -0.1213 0.0889  0.0156  156 SER B N   
2843 C CA  . SER B 99  ? 0.6495 0.2857 0.2845 -0.1015 0.0824  0.0130  156 SER B CA  
2844 C C   . SER B 99  ? 0.6854 0.3068 0.3263 -0.0855 0.0563  0.0237  156 SER B C   
2845 O O   . SER B 99  ? 0.8019 0.3847 0.4091 -0.0889 0.0445  0.0310  156 SER B O   
2846 C CB  . SER B 99  ? 0.7257 0.4046 0.3952 -0.1106 0.0975  0.0054  156 SER B CB  
2847 O OG  . SER B 99  ? 0.7562 0.4087 0.4018 -0.1263 0.0947  0.0123  156 SER B OG  
2848 N N   . VAL B 100 ? 0.6415 0.2927 0.3205 -0.0680 0.0463  0.0232  157 VAL B N   
2849 C CA  . VAL B 100 ? 0.6656 0.3252 0.3643 -0.0544 0.0254  0.0296  157 VAL B CA  
2850 C C   . VAL B 100 ? 0.6510 0.3560 0.3997 -0.0484 0.0293  0.0250  157 VAL B C   
2851 O O   . VAL B 100 ? 0.5961 0.3207 0.3638 -0.0430 0.0324  0.0198  157 VAL B O   
2852 C CB  . VAL B 100 ? 0.6593 0.3100 0.3488 -0.0451 0.0083  0.0337  157 VAL B CB  
2853 C CG1 . VAL B 100 ? 0.5887 0.2620 0.3028 -0.0337 -0.0109 0.0374  157 VAL B CG1 
2854 C CG2 . VAL B 100 ? 0.7371 0.3408 0.3752 -0.0501 0.0036  0.0373  157 VAL B CG2 
2855 N N   . LEU B 101 ? 0.5650 0.2804 0.3292 -0.0487 0.0274  0.0265  158 LEU B N   
2856 C CA  . LEU B 101 ? 0.5250 0.2785 0.3311 -0.0466 0.0337  0.0216  158 LEU B CA  
2857 C C   . LEU B 101 ? 0.5803 0.3464 0.4066 -0.0369 0.0182  0.0264  158 LEU B C   
2858 O O   . LEU B 101 ? 0.5342 0.2796 0.3403 -0.0339 0.0073  0.0311  158 LEU B O   
2859 C CB  . LEU B 101 ? 0.6448 0.4029 0.4492 -0.0618 0.0515  0.0165  158 LEU B CB  
2860 C CG  . LEU B 101 ? 0.7534 0.5200 0.5494 -0.0733 0.0720  0.0068  158 LEU B CG  
2861 C CD1 . LEU B 101 ? 0.7205 0.5041 0.5202 -0.0926 0.0892  0.0008  158 LEU B CD1 
2862 C CD2 . LEU B 101 ? 0.7059 0.5028 0.5308 -0.0586 0.0737  -0.0023 158 LEU B CD2 
2863 N N   . PHE B 102 ? 0.5046 0.3029 0.3671 -0.0307 0.0162  0.0238  159 PHE B N   
2864 C CA  . PHE B 102 ? 0.4559 0.2718 0.3404 -0.0254 0.0078  0.0259  159 PHE B CA  
2865 C C   . PHE B 102 ? 0.5491 0.3660 0.4387 -0.0331 0.0188  0.0233  159 PHE B C   
2866 O O   . PHE B 102 ? 0.6266 0.4527 0.5223 -0.0413 0.0336  0.0171  159 PHE B O   
2867 C CB  . PHE B 102 ? 0.3607 0.2046 0.2748 -0.0203 0.0020  0.0243  159 PHE B CB  
2868 C CG  . PHE B 102 ? 0.4582 0.3022 0.3638 -0.0185 -0.0107 0.0277  159 PHE B CG  
2869 C CD1 . PHE B 102 ? 0.4638 0.3163 0.3668 -0.0149 -0.0233 0.0310  159 PHE B CD1 
2870 C CD2 . PHE B 102 ? 0.4746 0.3112 0.3724 -0.0203 -0.0111 0.0261  159 PHE B CD2 
2871 C CE1 . PHE B 102 ? 0.4581 0.3187 0.3545 -0.0172 -0.0345 0.0329  159 PHE B CE1 
2872 C CE2 . PHE B 102 ? 0.4663 0.3003 0.3510 -0.0236 -0.0235 0.0299  159 PHE B CE2 
2873 C CZ  . PHE B 102 ? 0.4443 0.2939 0.3302 -0.0241 -0.0344 0.0334  159 PHE B CZ  
2874 N N   . ASP B 103 ? 0.5436 0.3525 0.4284 -0.0304 0.0110  0.0266  160 ASP B N   
2875 C CA  . ASP B 103 ? 0.5037 0.3034 0.3824 -0.0410 0.0188  0.0258  160 ASP B CA  
2876 C C   . ASP B 103 ? 0.5851 0.4225 0.5041 -0.0441 0.0282  0.0199  160 ASP B C   
2877 O O   . ASP B 103 ? 0.5284 0.3871 0.4746 -0.0344 0.0202  0.0200  160 ASP B O   
2878 C CB  . ASP B 103 ? 0.5474 0.3268 0.4097 -0.0321 0.0038  0.0297  160 ASP B CB  
2879 C CG  . ASP B 103 ? 0.5813 0.3419 0.4290 -0.0446 0.0084  0.0300  160 ASP B CG  
2880 O OD1 . ASP B 103 ? 0.6640 0.4426 0.5274 -0.0608 0.0239  0.0264  160 ASP B OD1 
2881 O OD2 . ASP B 103 ? 0.9205 0.6476 0.7380 -0.0374 -0.0052 0.0327  160 ASP B OD2 
2882 N N   . PRO B 104 ? 0.5776 0.4266 0.5004 -0.0575 0.0446  0.0133  161 PRO B N   
2883 C CA  . PRO B 104 ? 0.4807 0.3710 0.4445 -0.0552 0.0508  0.0046  161 PRO B CA  
2884 C C   . PRO B 104 ? 0.5146 0.4147 0.4950 -0.0581 0.0476  0.0055  161 PRO B C   
2885 O O   . PRO B 104 ? 0.5385 0.4651 0.5519 -0.0488 0.0431  0.0018  161 PRO B O   
2886 C CB  . PRO B 104 ? 0.6206 0.5269 0.5817 -0.0691 0.0697  -0.0055 161 PRO B CB  
2887 C CG  . PRO B 104 ? 0.7648 0.6357 0.6831 -0.0779 0.0735  -0.0010 161 PRO B CG  
2888 C CD  . PRO B 104 ? 0.6702 0.4997 0.5603 -0.0733 0.0574  0.0115  161 PRO B CD  
2889 N N   . HIS B 105 ? 0.4003 0.2729 0.3523 -0.0712 0.0481  0.0106  162 HIS B N   
2890 C CA  . HIS B 105 ? 0.4070 0.2816 0.3671 -0.0758 0.0446  0.0118  162 HIS B CA  
2891 C C   . HIS B 105 ? 0.4216 0.2879 0.3867 -0.0567 0.0272  0.0176  162 HIS B C   
2892 O O   . HIS B 105 ? 0.3471 0.2283 0.3337 -0.0537 0.0232  0.0167  162 HIS B O   
2893 C CB  . HIS B 105 ? 0.5050 0.3428 0.4212 -0.0990 0.0494  0.0151  162 HIS B CB  
2894 C CG  . HIS B 105 ? 0.5778 0.4006 0.4872 -0.1031 0.0416  0.0184  162 HIS B CG  
2895 N ND1 . HIS B 105 ? 0.7127 0.5618 0.6418 -0.1202 0.0502  0.0133  162 HIS B ND1 
2896 C CD2 . HIS B 105 ? 0.6003 0.3850 0.4836 -0.0913 0.0248  0.0250  162 HIS B CD2 
2897 C CE1 . HIS B 105 ? 0.6854 0.5079 0.5983 -0.1206 0.0392  0.0184  162 HIS B CE1 
2898 N NE2 . HIS B 105 ? 0.6570 0.4396 0.5414 -0.1017 0.0237  0.0250  162 HIS B NE2 
2899 N N   . GLU B 106 ? 0.3436 0.1904 0.2896 -0.0442 0.0168  0.0221  163 GLU B N   
2900 C CA  . GLU B 106 ? 0.3543 0.2008 0.3034 -0.0271 0.0013  0.0248  163 GLU B CA  
2901 C C   . GLU B 106 ? 0.2691 0.1545 0.2581 -0.0188 -0.0013 0.0225  163 GLU B C   
2902 O O   . GLU B 106 ? 0.2503 0.1464 0.2516 -0.0116 -0.0087 0.0225  163 GLU B O   
2903 C CB  . GLU B 106 ? 0.3813 0.2059 0.3018 -0.0153 -0.0100 0.0274  163 GLU B CB  
2904 C CG  . GLU B 106 ? 0.3830 0.2195 0.3092 0.0046  -0.0260 0.0263  163 GLU B CG  
2905 C CD  . GLU B 106 ? 0.4811 0.2954 0.3897 0.0113  -0.0343 0.0256  163 GLU B CD  
2906 O OE1 . GLU B 106 ? 0.5192 0.3011 0.4049 -0.0027 -0.0291 0.0278  163 GLU B OE1 
2907 O OE2 . GLU B 106 ? 0.5198 0.3505 0.4357 0.0296  -0.0464 0.0219  163 GLU B OE2 
2908 N N   . GLY B 107 ? 0.2580 0.1599 0.2617 -0.0202 0.0037  0.0201  164 GLY B N   
2909 C CA  . GLY B 107 ? 0.2498 0.1764 0.2797 -0.0149 -0.0012 0.0183  164 GLY B CA  
2910 C C   . GLY B 107 ? 0.2287 0.1698 0.2818 -0.0171 0.0008  0.0148  164 GLY B C   
2911 O O   . GLY B 107 ? 0.2086 0.1607 0.2747 -0.0128 -0.0070 0.0154  164 GLY B O   
2912 N N   . ALA B 108 ? 0.2100 0.1534 0.2672 -0.0256 0.0113  0.0103  165 ALA B N   
2913 C CA  . ALA B 108 ? 0.2241 0.1842 0.3035 -0.0289 0.0127  0.0059  165 ALA B CA  
2914 C C   . ALA B 108 ? 0.2010 0.1484 0.2725 -0.0298 0.0065  0.0111  165 ALA B C   
2915 O O   . ALA B 108 ? 0.2018 0.1597 0.2901 -0.0258 0.0003  0.0104  165 ALA B O   
2916 C CB  . ALA B 108 ? 0.2076 0.1808 0.2918 -0.0417 0.0266  -0.0017 165 ALA B CB  
2917 N N   . ARG B 109 ? 0.2253 0.1446 0.2659 -0.0336 0.0064  0.0157  166 ARG B N   
2918 C CA  . ARG B 109 ? 0.2383 0.1379 0.2630 -0.0305 -0.0020 0.0192  166 ARG B CA  
2919 C C   . ARG B 109 ? 0.2211 0.1337 0.2570 -0.0140 -0.0133 0.0198  166 ARG B C   
2920 O O   . ARG B 109 ? 0.2314 0.1482 0.2754 -0.0109 -0.0183 0.0193  166 ARG B O   
2921 C CB  . ARG B 109 ? 0.2815 0.1390 0.2611 -0.0332 -0.0046 0.0229  166 ARG B CB  
2922 C CG  . ARG B 109 ? 0.3433 0.1694 0.2962 -0.0297 -0.0150 0.0250  166 ARG B CG  
2923 C CD  . ARG B 109 ? 0.4395 0.2139 0.3383 -0.0259 -0.0237 0.0278  166 ARG B CD  
2924 N NE  . ARG B 109 ? 0.4686 0.2507 0.3673 -0.0013 -0.0352 0.0261  166 ARG B NE  
2925 C CZ  . ARG B 109 ? 0.5103 0.3030 0.4143 0.0203  -0.0478 0.0225  166 ARG B CZ  
2926 N NH1 . ARG B 109 ? 0.5199 0.3065 0.4236 0.0221  -0.0518 0.0215  166 ARG B NH1 
2927 N NH2 . ARG B 109 ? 0.5149 0.3288 0.4250 0.0396  -0.0562 0.0186  166 ARG B NH2 
2928 N N   . LEU B 110 ? 0.2088 0.1311 0.2449 -0.0058 -0.0168 0.0203  167 LEU B N   
2929 C CA  . LEU B 110 ? 0.1920 0.1350 0.2374 0.0047  -0.0257 0.0195  167 LEU B CA  
2930 C C   . LEU B 110 ? 0.1683 0.1315 0.2386 0.0004  -0.0258 0.0182  167 LEU B C   
2931 O O   . LEU B 110 ? 0.1873 0.1615 0.2624 0.0048  -0.0314 0.0171  167 LEU B O   
2932 C CB  . LEU B 110 ? 0.2003 0.1550 0.2421 0.0078  -0.0284 0.0197  167 LEU B CB  
2933 C CG  . LEU B 110 ? 0.2518 0.1905 0.2678 0.0174  -0.0339 0.0196  167 LEU B CG  
2934 C CD1 . LEU B 110 ? 0.2528 0.2051 0.2677 0.0167  -0.0358 0.0199  167 LEU B CD1 
2935 C CD2 . LEU B 110 ? 0.2721 0.2147 0.2794 0.0340  -0.0449 0.0153  167 LEU B CD2 
2936 N N   . GLY B 111 ? 0.1644 0.1311 0.2475 -0.0066 -0.0209 0.0170  168 GLY B N   
2937 C CA  . GLY B 111 ? 0.1766 0.1542 0.2767 -0.0084 -0.0248 0.0150  168 GLY B CA  
2938 C C   . GLY B 111 ? 0.1726 0.1495 0.2819 -0.0093 -0.0257 0.0137  168 GLY B C   
2939 O O   . GLY B 111 ? 0.1571 0.1395 0.2712 -0.0083 -0.0321 0.0138  168 GLY B O   
2940 N N   . VAL B 112 ? 0.1579 0.1274 0.2667 -0.0142 -0.0192 0.0125  169 VAL B N   
2941 C CA  . VAL B 112 ? 0.1569 0.1236 0.2712 -0.0180 -0.0208 0.0116  169 VAL B CA  
2942 C C   . VAL B 112 ? 0.1883 0.1424 0.2859 -0.0113 -0.0275 0.0149  169 VAL B C   
2943 O O   . VAL B 112 ? 0.1848 0.1418 0.2884 -0.0094 -0.0331 0.0143  169 VAL B O   
2944 C CB  . VAL B 112 ? 0.1731 0.1351 0.2842 -0.0307 -0.0119 0.0096  169 VAL B CB  
2945 C CG1 . VAL B 112 ? 0.1829 0.1361 0.2915 -0.0377 -0.0151 0.0100  169 VAL B CG1 
2946 C CG2 . VAL B 112 ? 0.1639 0.1512 0.2983 -0.0345 -0.0053 0.0018  169 VAL B CG2 
2947 N N   . GLU B 113 ? 0.2020 0.1418 0.2765 -0.0052 -0.0285 0.0169  170 GLU B N   
2948 C CA  . GLU B 113 ? 0.2052 0.1342 0.2619 0.0066  -0.0368 0.0165  170 GLU B CA  
2949 C C   . GLU B 113 ? 0.1966 0.1538 0.2674 0.0141  -0.0415 0.0139  170 GLU B C   
2950 O O   . GLU B 113 ? 0.2149 0.1722 0.2818 0.0205  -0.0467 0.0117  170 GLU B O   
2951 C CB  . GLU B 113 ? 0.2433 0.1516 0.2704 0.0165  -0.0406 0.0166  170 GLU B CB  
2952 C CG  . GLU B 113 ? 0.2896 0.1579 0.2875 0.0060  -0.0380 0.0196  170 GLU B CG  
2953 C CD  . GLU B 113 ? 0.3894 0.2256 0.3641 0.0032  -0.0437 0.0203  170 GLU B CD  
2954 O OE1 . GLU B 113 ? 0.4451 0.2801 0.4143 0.0193  -0.0535 0.0173  170 GLU B OE1 
2955 O OE2 . GLU B 113 ? 0.4561 0.2697 0.4162 -0.0167 -0.0382 0.0230  170 GLU B OE2 
2956 N N   . HIS B 114 ? 0.1776 0.1569 0.2601 0.0109  -0.0397 0.0140  171 HIS B N   
2957 C CA  . HIS B 114 ? 0.1528 0.1583 0.2430 0.0100  -0.0432 0.0119  171 HIS B CA  
2958 C C   . HIS B 114 ? 0.1751 0.1782 0.2748 0.0032  -0.0451 0.0121  171 HIS B C   
2959 O O   . HIS B 114 ? 0.1694 0.1830 0.2668 0.0054  -0.0484 0.0096  171 HIS B O   
2960 C CB  . HIS B 114 ? 0.1399 0.1587 0.2326 0.0020  -0.0419 0.0132  171 HIS B CB  
2961 C CG  . HIS B 114 ? 0.1811 0.2225 0.2742 -0.0075 -0.0451 0.0120  171 HIS B CG  
2962 N ND1 . HIS B 114 ? 0.2849 0.3583 0.3753 -0.0049 -0.0466 0.0071  171 HIS B ND1 
2963 C CD2 . HIS B 114 ? 0.1819 0.2173 0.2730 -0.0212 -0.0480 0.0142  171 HIS B CD2 
2964 C CE1 . HIS B 114 ? 0.2350 0.3238 0.3218 -0.0216 -0.0479 0.0071  171 HIS B CE1 
2965 N NE2 . HIS B 114 ? 0.1861 0.2458 0.2693 -0.0318 -0.0500 0.0123  171 HIS B NE2 
2966 N N   . LEU B 115 ? 0.1341 0.1252 0.2439 -0.0038 -0.0437 0.0136  172 LEU B N   
2967 C CA  . LEU B 115 ? 0.1430 0.1303 0.2608 -0.0084 -0.0485 0.0128  172 LEU B CA  
2968 C C   . LEU B 115 ? 0.1958 0.1732 0.3112 -0.0052 -0.0498 0.0123  172 LEU B C   
2969 O O   . LEU B 115 ? 0.1866 0.1638 0.3009 -0.0062 -0.0548 0.0115  172 LEU B O   
2970 C CB  . LEU B 115 ? 0.1525 0.1348 0.2831 -0.0116 -0.0490 0.0110  172 LEU B CB  
2971 C CG  . LEU B 115 ? 0.1313 0.1138 0.2565 -0.0137 -0.0515 0.0110  172 LEU B CG  
2972 C CD1 . LEU B 115 ? 0.1588 0.1385 0.2971 -0.0103 -0.0523 0.0057  172 LEU B CD1 
2973 C CD2 . LEU B 115 ? 0.1581 0.1366 0.2690 -0.0207 -0.0603 0.0124  172 LEU B CD2 
2974 N N   . VAL B 116 ? 0.1769 0.1408 0.2860 -0.0037 -0.0461 0.0130  173 VAL B N   
2975 C CA  . VAL B 116 ? 0.1791 0.1245 0.2772 -0.0031 -0.0493 0.0131  173 VAL B CA  
2976 C C   . VAL B 116 ? 0.2025 0.1473 0.2839 0.0097  -0.0544 0.0111  173 VAL B C   
2977 O O   . VAL B 116 ? 0.2417 0.1787 0.3180 0.0114  -0.0593 0.0099  173 VAL B O   
2978 C CB  . VAL B 116 ? 0.2169 0.1405 0.3006 -0.0090 -0.0452 0.0147  173 VAL B CB  
2979 C CG1 . VAL B 116 ? 0.2617 0.1546 0.3187 -0.0074 -0.0513 0.0155  173 VAL B CG1 
2980 C CG2 . VAL B 116 ? 0.2049 0.1400 0.3100 -0.0233 -0.0395 0.0131  173 VAL B CG2 
2981 N N   . ALA B 117 ? 0.2085 0.1660 0.2823 0.0199  -0.0540 0.0090  174 ALA B N   
2982 C CA  . ALA B 117 ? 0.2042 0.1731 0.2654 0.0357  -0.0591 0.0029  174 ALA B CA  
2983 C C   . ALA B 117 ? 0.2438 0.2396 0.3165 0.0303  -0.0590 0.0003  174 ALA B C   
2984 O O   . ALA B 117 ? 0.2688 0.2713 0.3323 0.0402  -0.0625 -0.0055 174 ALA B O   
2985 C CB  . ALA B 117 ? 0.2613 0.2473 0.3164 0.0477  -0.0597 -0.0010 174 ALA B CB  
2986 N N   . LEU B 118 ? 0.1581 0.1655 0.2453 0.0148  -0.0561 0.0038  175 LEU B N   
2987 C CA  . LEU B 118 ? 0.1479 0.1698 0.2364 0.0045  -0.0574 0.0026  175 LEU B CA  
2988 C C   . LEU B 118 ? 0.2128 0.2114 0.3005 0.0010  -0.0620 0.0042  175 LEU B C   
2989 O O   . LEU B 118 ? 0.2068 0.2106 0.2889 -0.0062 -0.0643 0.0028  175 LEU B O   
2990 C CB  . LEU B 118 ? 0.1842 0.2117 0.2767 -0.0111 -0.0568 0.0061  175 LEU B CB  
2991 C CG  . LEU B 118 ? 0.1620 0.2187 0.2517 -0.0139 -0.0533 0.0040  175 LEU B CG  
2992 C CD1 . LEU B 118 ? 0.1997 0.2458 0.2868 -0.0286 -0.0548 0.0089  175 LEU B CD1 
2993 C CD2 . LEU B 118 ? 0.1742 0.2679 0.2568 -0.0190 -0.0518 -0.0027 175 LEU B CD2 
2994 N N   . GLY B 119 ? 0.2241 0.1776 0.2369 0.0234  -0.0130 -0.0434 176 GLY B N   
2995 C CA  . GLY B 119 ? 0.2135 0.1637 0.2169 0.0217  -0.0146 -0.0482 176 GLY B CA  
2996 C C   . GLY B 119 ? 0.2369 0.1908 0.2351 0.0175  -0.0182 -0.0449 176 GLY B C   
2997 O O   . GLY B 119 ? 0.2287 0.1806 0.2203 0.0160  -0.0211 -0.0490 176 GLY B O   
2998 N N   . HIS B 120 ? 0.2127 0.1722 0.2147 0.0157  -0.0185 -0.0384 177 HIS B N   
2999 C CA  . HIS B 120 ? 0.1770 0.1412 0.1765 0.0125  -0.0212 -0.0361 177 HIS B CA  
3000 C C   . HIS B 120 ? 0.2132 0.1742 0.2171 0.0081  -0.0255 -0.0372 177 HIS B C   
3001 O O   . HIS B 120 ? 0.2364 0.1920 0.2459 0.0063  -0.0260 -0.0356 177 HIS B O   
3002 C CB  . HIS B 120 ? 0.2004 0.1707 0.2034 0.0118  -0.0195 -0.0298 177 HIS B CB  
3003 C CG  . HIS B 120 ? 0.1793 0.1535 0.1784 0.0149  -0.0155 -0.0285 177 HIS B CG  
3004 N ND1 . HIS B 120 ? 0.1768 0.1543 0.1686 0.0153  -0.0155 -0.0281 177 HIS B ND1 
3005 C CD2 . HIS B 120 ? 0.1907 0.1658 0.1931 0.0173  -0.0116 -0.0275 177 HIS B CD2 
3006 C CE1 . HIS B 120 ? 0.1782 0.1573 0.1674 0.0174  -0.0108 -0.0265 177 HIS B CE1 
3007 N NE2 . HIS B 120 ? 0.1772 0.1559 0.1740 0.0185  -0.0081 -0.0265 177 HIS B NE2 
3008 N N   . GLN B 121 ? 0.2280 0.1921 0.2298 0.0061  -0.0290 -0.0395 178 GLN B N   
3009 C CA  . GLN B 121 ? 0.2126 0.1762 0.2211 0.0011  -0.0327 -0.0409 178 GLN B CA  
3010 C C   . GLN B 121 ? 0.2096 0.1826 0.2232 -0.0013 -0.0342 -0.0388 178 GLN B C   
3011 O O   . GLN B 121 ? 0.2968 0.2714 0.3192 -0.0063 -0.0352 -0.0389 178 GLN B O   
3012 C CB  . GLN B 121 ? 0.3038 0.2621 0.3088 0.0007  -0.0371 -0.0482 178 GLN B CB  
3013 C CG  . GLN B 121 ? 0.3450 0.2932 0.3475 0.0029  -0.0354 -0.0516 178 GLN B CG  
3014 C CD  . GLN B 121 ? 0.6453 0.5879 0.6401 0.0040  -0.0386 -0.0599 178 GLN B CD  
3015 O OE1 . GLN B 121 ? 0.6877 0.6337 0.6765 0.0036  -0.0426 -0.0627 178 GLN B OE1 
3016 N NE2 . GLN B 121 ? 0.7302 0.6634 0.7248 0.0057  -0.0374 -0.0641 178 GLN B NE2 
3017 N N   A ARG B 122 ? 0.2222 0.2009 0.2314 0.0019  -0.0339 -0.0370 179 ARG B N   
3018 N N   B ARG B 122 ? 0.2227 0.2014 0.2318 0.0019  -0.0340 -0.0371 179 ARG B N   
3019 C CA  A ARG B 122 ? 0.1954 0.1828 0.2103 0.0010  -0.0359 -0.0357 179 ARG B CA  
3020 C CA  B ARG B 122 ? 0.1952 0.1826 0.2103 0.0009  -0.0359 -0.0357 179 ARG B CA  
3021 C C   A ARG B 122 ? 0.2191 0.2100 0.2354 0.0020  -0.0309 -0.0301 179 ARG B C   
3022 C C   B ARG B 122 ? 0.2196 0.2102 0.2357 0.0020  -0.0308 -0.0301 179 ARG B C   
3023 O O   A ARG B 122 ? 0.2164 0.2084 0.2266 0.0057  -0.0299 -0.0280 179 ARG B O   
3024 O O   B ARG B 122 ? 0.2153 0.2068 0.2251 0.0057  -0.0298 -0.0281 179 ARG B O   
3025 C CB  A ARG B 122 ? 0.2549 0.2437 0.2623 0.0043  -0.0413 -0.0381 179 ARG B CB  
3026 C CB  B ARG B 122 ? 0.2548 0.2439 0.2630 0.0040  -0.0414 -0.0382 179 ARG B CB  
3027 C CG  A ARG B 122 ? 0.2767 0.2613 0.2809 0.0032  -0.0473 -0.0445 179 ARG B CG  
3028 C CG  B ARG B 122 ? 0.2758 0.2613 0.2821 0.0027  -0.0477 -0.0445 179 ARG B CG  
3029 C CD  A ARG B 122 ? 0.3814 0.3612 0.3688 0.0072  -0.0508 -0.0468 179 ARG B CD  
3030 C CD  B ARG B 122 ? 0.2929 0.2769 0.2866 0.0063  -0.0538 -0.0467 179 ARG B CD  
3031 N NE  A ARG B 122 ? 0.3146 0.2980 0.2972 0.0103  -0.0528 -0.0430 179 ARG B NE  
3032 N NE  B ARG B 122 ? 0.3628 0.3542 0.3615 0.0078  -0.0577 -0.0440 179 ARG B NE  
3033 C CZ  A ARG B 122 ? 0.2898 0.2678 0.2551 0.0136  -0.0532 -0.0421 179 ARG B CZ  
3034 C CZ  B ARG B 122 ? 0.3968 0.3952 0.4087 0.0060  -0.0643 -0.0466 179 ARG B CZ  
3035 N NH1 A ARG B 122 ? 0.3157 0.2857 0.2668 0.0144  -0.0513 -0.0457 179 ARG B NH1 
3036 N NH1 B ARG B 122 ? 0.4334 0.4329 0.4551 0.0017  -0.0673 -0.0516 179 ARG B NH1 
3037 N NH2 A ARG B 122 ? 0.2485 0.2284 0.2103 0.0160  -0.0551 -0.0377 179 ARG B NH2 
3038 N NH2 B ARG B 122 ? 0.3849 0.3895 0.4020 0.0085  -0.0679 -0.0444 179 ARG B NH2 
3039 N N   . ILE B 123 ? 0.1744 0.1657 0.1973 -0.0017 -0.0277 -0.0278 180 ILE B N   
3040 C CA  . ILE B 123 ? 0.1717 0.1643 0.1942 -0.0014 -0.0232 -0.0231 180 ILE B CA  
3041 C C   . ILE B 123 ? 0.1836 0.1837 0.2143 -0.0041 -0.0217 -0.0226 180 ILE B C   
3042 O O   . ILE B 123 ? 0.1827 0.1846 0.2208 -0.0088 -0.0212 -0.0243 180 ILE B O   
3043 C CB  . ILE B 123 ? 0.1742 0.1593 0.1949 -0.0032 -0.0210 -0.0206 180 ILE B CB  
3044 C CG1 . ILE B 123 ? 0.1831 0.1619 0.1986 0.0005  -0.0220 -0.0221 180 ILE B CG1 
3045 C CG2 . ILE B 123 ? 0.1839 0.1698 0.2033 -0.0035 -0.0177 -0.0162 180 ILE B CG2 
3046 C CD1 . ILE B 123 ? 0.2134 0.1832 0.2292 -0.0007 -0.0221 -0.0208 180 ILE B CD1 
3047 N N   . ALA B 124 ? 0.1694 0.1738 0.1996 -0.0013 -0.0204 -0.0208 181 ALA B N   
3048 C CA  . ALA B 124 ? 0.1371 0.1484 0.1756 -0.0032 -0.0180 -0.0211 181 ALA B CA  
3049 C C   . ALA B 124 ? 0.1549 0.1638 0.1898 -0.0051 -0.0127 -0.0177 181 ALA B C   
3050 O O   . ALA B 124 ? 0.1594 0.1629 0.1865 -0.0033 -0.0124 -0.0149 181 ALA B O   
3051 C CB  . ALA B 124 ? 0.1614 0.1781 0.2026 0.0012  -0.0209 -0.0219 181 ALA B CB  
3052 N N   . LEU B 125 ? 0.1389 0.1521 0.1798 -0.0088 -0.0086 -0.0186 182 LEU B N   
3053 C CA  . LEU B 125 ? 0.1357 0.1458 0.1709 -0.0113 -0.0036 -0.0161 182 LEU B CA  
3054 C C   . LEU B 125 ? 0.1676 0.1843 0.2077 -0.0099 -0.0006 -0.0179 182 LEU B C   
3055 O O   . LEU B 125 ? 0.1561 0.1809 0.2078 -0.0104 0.0005  -0.0217 182 LEU B O   
3056 C CB  . LEU B 125 ? 0.1429 0.1495 0.1771 -0.0183 0.0006  -0.0155 182 LEU B CB  
3057 C CG  . LEU B 125 ? 0.1411 0.1405 0.1728 -0.0205 -0.0023 -0.0145 182 LEU B CG  
3058 C CD1 . LEU B 125 ? 0.2011 0.1965 0.2320 -0.0285 0.0029  -0.0134 182 LEU B CD1 
3059 C CD2 . LEU B 125 ? 0.1735 0.1641 0.1953 -0.0170 -0.0059 -0.0110 182 LEU B CD2 
3060 N N   . LEU B 126 ? 0.1491 0.1625 0.1819 -0.0082 0.0004  -0.0158 183 LEU B N   
3061 C CA  . LEU B 126 ? 0.1717 0.1895 0.2081 -0.0069 0.0035  -0.0179 183 LEU B CA  
3062 C C   . LEU B 126 ? 0.1650 0.1776 0.1918 -0.0113 0.0086  -0.0168 183 LEU B C   
3063 O O   . LEU B 126 ? 0.1605 0.1666 0.1775 -0.0106 0.0066  -0.0137 183 LEU B O   
3064 C CB  . LEU B 126 ? 0.1599 0.1769 0.1953 -0.0012 -0.0003 -0.0167 183 LEU B CB  
3065 C CG  . LEU B 126 ? 0.2207 0.2392 0.2582 0.0005  0.0022  -0.0185 183 LEU B CG  
3066 C CD1 . LEU B 126 ? 0.2161 0.2423 0.2653 -0.0002 0.0060  -0.0235 183 LEU B CD1 
3067 C CD2 . LEU B 126 ? 0.2195 0.2364 0.2573 0.0058  -0.0021 -0.0169 183 LEU B CD2 
3068 N N   . THR B 127 ? 0.1691 0.1847 0.1987 -0.0161 0.0149  -0.0194 184 THR B N   
3069 C CA  . THR B 127 ? 0.1718 0.1809 0.1887 -0.0214 0.0202  -0.0182 184 THR B CA  
3070 C C   . THR B 127 ? 0.1896 0.1994 0.2037 -0.0198 0.0234  -0.0209 184 THR B C   
3071 O O   . THR B 127 ? 0.1636 0.1801 0.1885 -0.0153 0.0229  -0.0244 184 THR B O   
3072 C CB  . THR B 127 ? 0.1813 0.1921 0.2005 -0.0284 0.0276  -0.0199 184 THR B CB  
3073 O OG1 . THR B 127 ? 0.1955 0.2166 0.2273 -0.0287 0.0342  -0.0260 184 THR B OG1 
3074 C CG2 . THR B 127 ? 0.1754 0.1879 0.2030 -0.0298 0.0246  -0.0192 184 THR B CG2 
3075 N N   . GLY B 128 ? 0.1917 0.1934 0.1901 -0.0238 0.0262  -0.0194 185 GLY B N   
3076 C CA  . GLY B 128 ? 0.1987 0.2006 0.1931 -0.0243 0.0314  -0.0236 185 GLY B CA  
3077 C C   . GLY B 128 ? 0.2191 0.2279 0.2205 -0.0285 0.0417  -0.0289 185 GLY B C   
3078 O O   . GLY B 128 ? 0.2262 0.2404 0.2376 -0.0311 0.0443  -0.0294 185 GLY B O   
3079 N N   . PRO B 129 ? 0.2188 0.2275 0.2160 -0.0294 0.0482  -0.0339 186 PRO B N   
3080 C CA  . PRO B 129 ? 0.2631 0.2791 0.2680 -0.0335 0.0598  -0.0402 186 PRO B CA  
3081 C C   . PRO B 129 ? 0.3238 0.3337 0.3153 -0.0425 0.0664  -0.0371 186 PRO B C   
3082 O O   . PRO B 129 ? 0.3244 0.3211 0.2924 -0.0464 0.0652  -0.0323 186 PRO B O   
3083 C CB  . PRO B 129 ? 0.2575 0.2715 0.2559 -0.0324 0.0647  -0.0459 186 PRO B CB  
3084 C CG  . PRO B 129 ? 0.2556 0.2577 0.2356 -0.0309 0.0562  -0.0410 186 PRO B CG  
3085 C CD  . PRO B 129 ? 0.2276 0.2297 0.2135 -0.0269 0.0454  -0.0346 186 PRO B CD  
3086 N N   . LEU B 130 ? 0.3159 0.3350 0.3228 -0.0461 0.0731  -0.0398 187 LEU B N   
3087 C CA  . LEU B 130 ? 0.3814 0.3939 0.3769 -0.0554 0.0792  -0.0361 187 LEU B CA  
3088 C C   . LEU B 130 ? 0.4235 0.4288 0.3992 -0.0629 0.0913  -0.0380 187 LEU B C   
3089 O O   . LEU B 130 ? 0.4209 0.4164 0.3805 -0.0714 0.0964  -0.0334 187 LEU B O   
3090 C CB  . LEU B 130 ? 0.4059 0.4307 0.4252 -0.0578 0.0828  -0.0389 187 LEU B CB  
3091 C CG  . LEU B 130 ? 0.3915 0.4187 0.4227 -0.0525 0.0703  -0.0354 187 LEU B CG  
3092 C CD1 . LEU B 130 ? 0.4433 0.4799 0.4944 -0.0567 0.0732  -0.0379 187 LEU B CD1 
3093 C CD2 . LEU B 130 ? 0.3899 0.4018 0.4007 -0.0522 0.0611  -0.0267 187 LEU B CD2 
3094 N N   . THR B 131 ? 0.3821 0.3901 0.3566 -0.0601 0.0960  -0.0445 188 THR B N   
3095 C CA  . THR B 131 ? 0.3784 0.3762 0.3277 -0.0667 0.1058  -0.0461 188 THR B CA  
3096 C C   . THR B 131 ? 0.4665 0.4454 0.3846 -0.0680 0.0968  -0.0380 188 THR B C   
3097 O O   . THR B 131 ? 0.5152 0.4819 0.4067 -0.0749 0.1033  -0.0370 188 THR B O   
3098 C CB  . THR B 131 ? 0.4120 0.4170 0.3686 -0.0626 0.1121  -0.0562 188 THR B CB  
3099 O OG1 . THR B 131 ? 0.4118 0.4178 0.3758 -0.0529 0.0995  -0.0561 188 THR B OG1 
3100 C CG2 . THR B 131 ? 0.4726 0.4957 0.4591 -0.0625 0.1230  -0.0651 188 THR B CG2 
3101 N N   . SER B 132 ? 0.3629 0.3389 0.2835 -0.0618 0.0821  -0.0323 189 SER B N   
3102 C CA  . SER B 132 ? 0.3760 0.3361 0.2722 -0.0617 0.0717  -0.0252 189 SER B CA  
3103 C C   . SER B 132 ? 0.3865 0.3366 0.2729 -0.0663 0.0677  -0.0163 189 SER B C   
3104 O O   . SER B 132 ? 0.3561 0.3126 0.2606 -0.0639 0.0636  -0.0141 189 SER B O   
3105 C CB  . SER B 132 ? 0.3738 0.3370 0.2804 -0.0524 0.0588  -0.0245 189 SER B CB  
3106 O OG  . SER B 132 ? 0.3943 0.3451 0.2857 -0.0519 0.0473  -0.0168 189 SER B OG  
3107 N N   . VAL B 133 ? 0.3998 0.3328 0.2567 -0.0726 0.0679  -0.0111 190 VAL B N   
3108 C CA  . VAL B 133 ? 0.4096 0.3299 0.2551 -0.0767 0.0628  -0.0019 190 VAL B CA  
3109 C C   . VAL B 133 ? 0.3866 0.3072 0.2434 -0.0688 0.0475  0.0026  190 VAL B C   
3110 O O   . VAL B 133 ? 0.3899 0.3100 0.2561 -0.0690 0.0444  0.0066  190 VAL B O   
3111 C CB  . VAL B 133 ? 0.5128 0.4121 0.3216 -0.0838 0.0630  0.0036  190 VAL B CB  
3112 C CG1 . VAL B 133 ? 0.6551 0.5490 0.4493 -0.0795 0.0552  0.0018  190 VAL B CG1 
3113 C CG2 . VAL B 133 ? 0.4774 0.3615 0.2751 -0.0859 0.0539  0.0140  190 VAL B CG2 
3114 N N   . SER B 134 ? 0.3946 0.3158 0.2513 -0.0621 0.0383  0.0015  191 SER B N   
3115 C CA  . SER B 134 ? 0.3706 0.2935 0.2395 -0.0546 0.0253  0.0047  191 SER B CA  
3116 C C   . SER B 134 ? 0.3510 0.2888 0.2475 -0.0505 0.0266  0.0020  191 SER B C   
3117 O O   . SER B 134 ? 0.3337 0.2704 0.2381 -0.0481 0.0202  0.0057  191 SER B O   
3118 C CB  . SER B 134 ? 0.4131 0.3371 0.2809 -0.0490 0.0177  0.0023  191 SER B CB  
3119 O OG  . SER B 134 ? 0.6157 0.5242 0.4607 -0.0507 0.0092  0.0072  191 SER B OG  
3120 N N   . ALA B 135 ? 0.2891 0.2403 0.2005 -0.0490 0.0341  -0.0050 192 ALA B N   
3121 C CA  . ALA B 135 ? 0.2453 0.2097 0.1814 -0.0449 0.0339  -0.0076 192 ALA B CA  
3122 C C   . ALA B 135 ? 0.2909 0.2550 0.2315 -0.0501 0.0379  -0.0056 192 ALA B C   
3123 O O   . ALA B 135 ? 0.2556 0.2236 0.2095 -0.0470 0.0329  -0.0046 192 ALA B O   
3124 C CB  . ALA B 135 ? 0.2704 0.2481 0.2216 -0.0422 0.0403  -0.0153 192 ALA B CB  
3125 N N   . ARG B 136 ? 0.2843 0.2433 0.2138 -0.0584 0.0474  -0.0055 193 ARG B N   
3126 C CA  . ARG B 136 ? 0.2754 0.2333 0.2096 -0.0647 0.0521  -0.0036 193 ARG B CA  
3127 C C   . ARG B 136 ? 0.3155 0.2596 0.2400 -0.0650 0.0429  0.0043  193 ARG B C   
3128 O O   . ARG B 136 ? 0.3002 0.2467 0.2378 -0.0647 0.0403  0.0049  193 ARG B O   
3129 C CB  . ARG B 136 ? 0.3022 0.2566 0.2249 -0.0744 0.0657  -0.0048 193 ARG B CB  
3130 C CG  . ARG B 136 ? 0.4162 0.3677 0.3423 -0.0827 0.0715  -0.0023 193 ARG B CG  
3131 C CD  . ARG B 136 ? 0.4802 0.4281 0.3940 -0.0935 0.0872  -0.0036 193 ARG B CD  
3132 N NE  . ARG B 136 ? 0.5612 0.4899 0.4408 -0.0978 0.0875  0.0022  193 ARG B NE  
3133 C CZ  . ARG B 136 ? 0.6688 0.5777 0.5265 -0.1026 0.0827  0.0115  193 ARG B CZ  
3134 N NH1 . ARG B 136 ? 0.5699 0.4750 0.4366 -0.1036 0.0776  0.0160  193 ARG B NH1 
3135 N NH2 . ARG B 136 ? 0.6112 0.5025 0.4364 -0.1063 0.0824  0.0163  193 ARG B NH2 
3136 N N   . LEU B 137 ? 0.3094 0.2386 0.2118 -0.0651 0.0370  0.0098  194 LEU B N   
3137 C CA  . LEU B 137 ? 0.3310 0.2461 0.2251 -0.0648 0.0276  0.0171  194 LEU B CA  
3138 C C   . LEU B 137 ? 0.2845 0.2061 0.1958 -0.0557 0.0174  0.0164  194 LEU B C   
3139 O O   . LEU B 137 ? 0.2917 0.2075 0.2071 -0.0552 0.0124  0.0195  194 LEU B O   
3140 C CB  . LEU B 137 ? 0.3737 0.2712 0.2406 -0.0665 0.0222  0.0231  194 LEU B CB  
3141 C CG  . LEU B 137 ? 0.4698 0.3550 0.3133 -0.0770 0.0319  0.0260  194 LEU B CG  
3142 C CD1 . LEU B 137 ? 0.4918 0.3589 0.3063 -0.0778 0.0242  0.0318  194 LEU B CD1 
3143 C CD2 . LEU B 137 ? 0.4507 0.3284 0.2948 -0.0843 0.0364  0.0302  194 LEU B CD2 
3144 N N   . ARG B 138 ? 0.2585 0.1910 0.1794 -0.0488 0.0147  0.0121  195 ARG B N   
3145 C CA  . ARG B 138 ? 0.2193 0.1589 0.1563 -0.0410 0.0073  0.0108  195 ARG B CA  
3146 C C   . ARG B 138 ? 0.2605 0.2095 0.2149 -0.0413 0.0106  0.0074  195 ARG B C   
3147 O O   . ARG B 138 ? 0.2287 0.1759 0.1899 -0.0386 0.0053  0.0084  195 ARG B O   
3148 C CB  . ARG B 138 ? 0.2309 0.1795 0.1738 -0.0349 0.0050  0.0073  195 ARG B CB  
3149 C CG  . ARG B 138 ? 0.2727 0.2123 0.2018 -0.0335 -0.0015 0.0103  195 ARG B CG  
3150 C CD  . ARG B 138 ? 0.2439 0.1917 0.1780 -0.0293 -0.0019 0.0062  195 ARG B CD  
3151 N NE  . ARG B 138 ? 0.2544 0.1931 0.1726 -0.0304 -0.0065 0.0080  195 ARG B NE  
3152 C CZ  . ARG B 138 ? 0.2610 0.2032 0.1798 -0.0279 -0.0081 0.0049  195 ARG B CZ  
3153 N NH1 . ARG B 138 ? 0.2471 0.2009 0.1815 -0.0240 -0.0055 0.0006  195 ARG B NH1 
3154 N NH2 . ARG B 138 ? 0.2757 0.2085 0.1782 -0.0297 -0.0128 0.0062  195 ARG B NH2 
3155 N N   . PHE B 139 ? 0.2066 0.1658 0.1691 -0.0444 0.0191  0.0027  196 PHE B N   
3156 C CA  . PHE B 139 ? 0.2243 0.1926 0.2041 -0.0451 0.0213  -0.0009 196 PHE B CA  
3157 C C   . PHE B 139 ? 0.2342 0.1929 0.2112 -0.0507 0.0210  0.0025  196 PHE B C   
3158 O O   . PHE B 139 ? 0.2191 0.1793 0.2064 -0.0484 0.0164  0.0014  196 PHE B O   
3159 C CB  . PHE B 139 ? 0.2057 0.1862 0.1960 -0.0481 0.0306  -0.0067 196 PHE B CB  
3160 C CG  . PHE B 139 ? 0.2300 0.2191 0.2381 -0.0507 0.0327  -0.0103 196 PHE B CG  
3161 C CD1 . PHE B 139 ? 0.2180 0.2141 0.2400 -0.0450 0.0256  -0.0128 196 PHE B CD1 
3162 C CD2 . PHE B 139 ? 0.3018 0.2905 0.3113 -0.0596 0.0416  -0.0110 196 PHE B CD2 
3163 C CE1 . PHE B 139 ? 0.2523 0.2556 0.2903 -0.0476 0.0261  -0.0165 196 PHE B CE1 
3164 C CE2 . PHE B 139 ? 0.3315 0.3283 0.3592 -0.0627 0.0430  -0.0146 196 PHE B CE2 
3165 C CZ  . PHE B 139 ? 0.2881 0.2923 0.3304 -0.0565 0.0345  -0.0176 196 PHE B CZ  
3166 N N   . GLU B 140 ? 0.2431 0.1905 0.2049 -0.0583 0.0260  0.0066  197 GLU B N   
3167 C CA  . GLU B 140 ? 0.2529 0.1890 0.2112 -0.0647 0.0263  0.0105  197 GLU B CA  
3168 C C   . GLU B 140 ? 0.2847 0.2095 0.2391 -0.0596 0.0153  0.0147  197 GLU B C   
3169 O O   . GLU B 140 ? 0.2892 0.2105 0.2511 -0.0606 0.0127  0.0147  197 GLU B O   
3170 C CB  . GLU B 140 ? 0.3138 0.2375 0.2527 -0.0742 0.0341  0.0151  197 GLU B CB  
3171 C CG  . GLU B 140 ? 0.3411 0.2762 0.2873 -0.0812 0.0477  0.0099  197 GLU B CG  
3172 C CD  . GLU B 140 ? 0.5875 0.5102 0.5103 -0.0902 0.0568  0.0139  197 GLU B CD  
3173 O OE1 . GLU B 140 ? 0.6163 0.5195 0.5166 -0.0925 0.0519  0.0219  197 GLU B OE1 
3174 O OE2 . GLU B 140 ? 0.5428 0.4748 0.4692 -0.0952 0.0690  0.0090  197 GLU B OE2 
3175 N N   . GLY B 141 ? 0.2750 0.1946 0.2193 -0.0540 0.0086  0.0175  198 GLY B N   
3176 C CA  . GLY B 141 ? 0.2615 0.1730 0.2061 -0.0479 -0.0017 0.0202  198 GLY B CA  
3177 C C   . GLY B 141 ? 0.2314 0.1540 0.1945 -0.0416 -0.0048 0.0149  198 GLY B C   
3178 O O   . GLY B 141 ? 0.2490 0.1651 0.2162 -0.0397 -0.0098 0.0153  198 GLY B O   
3179 N N   . TRP B 142 ? 0.2137 0.1518 0.1870 -0.0382 -0.0020 0.0097  199 TRP B N   
3180 C CA  . TRP B 142 ? 0.1838 0.1313 0.1714 -0.0328 -0.0048 0.0048  199 TRP B CA  
3181 C C   . TRP B 142 ? 0.2031 0.1508 0.1990 -0.0371 -0.0032 0.0024  199 TRP B C   
3182 O O   . TRP B 142 ? 0.1926 0.1373 0.1934 -0.0343 -0.0079 0.0007  199 TRP B O   
3183 C CB  . TRP B 142 ? 0.2019 0.1639 0.1972 -0.0294 -0.0023 0.0006  199 TRP B CB  
3184 C CG  . TRP B 142 ? 0.1879 0.1516 0.1793 -0.0241 -0.0048 0.0015  199 TRP B CG  
3185 C CD1 . TRP B 142 ? 0.1797 0.1370 0.1667 -0.0200 -0.0104 0.0042  199 TRP B CD1 
3186 C CD2 . TRP B 142 ? 0.1698 0.1424 0.1632 -0.0225 -0.0017 -0.0007 199 TRP B CD2 
3187 N NE1 . TRP B 142 ? 0.1948 0.1572 0.1814 -0.0164 -0.0110 0.0037  199 TRP B NE1 
3188 C CE2 . TRP B 142 ? 0.1776 0.1484 0.1671 -0.0180 -0.0057 0.0009  199 TRP B CE2 
3189 C CE3 . TRP B 142 ? 0.1741 0.1561 0.1741 -0.0242 0.0038  -0.0045 199 TRP B CE3 
3190 C CZ2 . TRP B 142 ? 0.1858 0.1627 0.1763 -0.0156 -0.0043 -0.0008 199 TRP B CZ2 
3191 C CZ3 . TRP B 142 ? 0.1701 0.1578 0.1711 -0.0211 0.0050  -0.0062 199 TRP B CZ3 
3192 C CH2 . TRP B 142 ? 0.1862 0.1707 0.1819 -0.0171 0.0009  -0.0042 199 TRP B CH2 
3193 N N   . ARG B 143 ? 0.2109 0.1626 0.2096 -0.0441 0.0037  0.0012  200 ARG B N   
3194 C CA  . ARG B 143 ? 0.1984 0.1520 0.2078 -0.0490 0.0053  -0.0018 200 ARG B CA  
3195 C C   . ARG B 143 ? 0.2242 0.1613 0.2272 -0.0524 0.0022  0.0020  200 ARG B C   
3196 O O   . ARG B 143 ? 0.2200 0.1561 0.2314 -0.0521 -0.0014 -0.0011 200 ARG B O   
3197 C CB  . ARG B 143 ? 0.2416 0.2027 0.2562 -0.0566 0.0146  -0.0037 200 ARG B CB  
3198 C CG  . ARG B 143 ? 0.2695 0.2357 0.2994 -0.0623 0.0166  -0.0079 200 ARG B CG  
3199 C CD  . ARG B 143 ? 0.3494 0.3246 0.3866 -0.0698 0.0273  -0.0102 200 ARG B CD  
3200 N NE  . ARG B 143 ? 0.5382 0.5013 0.5582 -0.0770 0.0346  -0.0043 200 ARG B NE  
3201 C CZ  . ARG B 143 ? 0.6791 0.6474 0.6988 -0.0833 0.0456  -0.0055 200 ARG B CZ  
3202 N NH1 . ARG B 143 ? 0.5227 0.5094 0.5618 -0.0828 0.0505  -0.0127 200 ARG B NH1 
3203 N NH2 . ARG B 143 ? 0.4393 0.3936 0.4387 -0.0901 0.0517  0.0005  200 ARG B NH2 
3204 N N   . GLN B 144 ? 0.2237 0.1467 0.2110 -0.0557 0.0028  0.0088  201 GLN B N   
3205 C CA  . GLN B 144 ? 0.2378 0.1427 0.2181 -0.0588 -0.0009 0.0134  201 GLN B CA  
3206 C C   . GLN B 144 ? 0.2587 0.1590 0.2423 -0.0502 -0.0101 0.0123  201 GLN B C   
3207 O O   . GLN B 144 ? 0.2587 0.1506 0.2465 -0.0510 -0.0134 0.0114  201 GLN B O   
3208 C CB  . GLN B 144 ? 0.2997 0.1891 0.2599 -0.0633 0.0004  0.0216  201 GLN B CB  
3209 C CG  . GLN B 144 ? 0.4142 0.2821 0.3659 -0.0664 -0.0045 0.0275  201 GLN B CG  
3210 C CD  . GLN B 144 ? 0.5734 0.4241 0.5035 -0.0670 -0.0082 0.0360  201 GLN B CD  
3211 O OE1 . GLN B 144 ? 0.7637 0.6190 0.6856 -0.0643 -0.0082 0.0369  201 GLN B OE1 
3212 N NE2 . GLN B 144 ? 0.6725 0.5022 0.5928 -0.0706 -0.0123 0.0424  201 GLN B NE2 
3213 N N   . THR B 145 ? 0.2301 0.1354 0.2121 -0.0421 -0.0139 0.0120  202 THR B N   
3214 C CA  . THR B 145 ? 0.2190 0.1210 0.2054 -0.0341 -0.0212 0.0103  202 THR B CA  
3215 C C   . THR B 145 ? 0.2268 0.1384 0.2260 -0.0313 -0.0214 0.0028  202 THR B C   
3216 O O   . THR B 145 ? 0.2441 0.1489 0.2471 -0.0283 -0.0257 0.0004  202 THR B O   
3217 C CB  . THR B 145 ? 0.2292 0.1354 0.2127 -0.0271 -0.0243 0.0115  202 THR B CB  
3218 O OG1 . THR B 145 ? 0.2655 0.1622 0.2354 -0.0302 -0.0251 0.0181  202 THR B OG1 
3219 C CG2 . THR B 145 ? 0.2234 0.1253 0.2124 -0.0194 -0.0310 0.0100  202 THR B CG2 
3220 N N   . LEU B 146 ? 0.2059 0.1324 0.2114 -0.0319 -0.0174 -0.0012 203 LEU B N   
3221 C CA  . LEU B 146 ? 0.1884 0.1227 0.2039 -0.0302 -0.0187 -0.0081 203 LEU B CA  
3222 C C   . LEU B 146 ? 0.2409 0.1672 0.2606 -0.0362 -0.0193 -0.0097 203 LEU B C   
3223 O O   . LEU B 146 ? 0.2393 0.1628 0.2631 -0.0336 -0.0233 -0.0144 203 LEU B O   
3224 C CB  . LEU B 146 ? 0.1763 0.1265 0.1980 -0.0304 -0.0154 -0.0113 203 LEU B CB  
3225 C CG  . LEU B 146 ? 0.1901 0.1484 0.2097 -0.0236 -0.0157 -0.0112 203 LEU B CG  
3226 C CD1 . LEU B 146 ? 0.2104 0.1816 0.2356 -0.0248 -0.0122 -0.0131 203 LEU B CD1 
3227 C CD2 . LEU B 146 ? 0.2217 0.1814 0.2425 -0.0170 -0.0198 -0.0152 203 LEU B CD2 
3228 N N   . ALA B 147 ? 0.2138 0.1361 0.2323 -0.0448 -0.0148 -0.0063 204 ALA B N   
3229 C CA  . ALA B 147 ? 0.2214 0.1356 0.2448 -0.0521 -0.0146 -0.0075 204 ALA B CA  
3230 C C   . ALA B 147 ? 0.2351 0.1308 0.2531 -0.0504 -0.0200 -0.0053 204 ALA B C   
3231 O O   . ALA B 147 ? 0.2619 0.1516 0.2861 -0.0530 -0.0224 -0.0091 204 ALA B O   
3232 C CB  . ALA B 147 ? 0.2308 0.1435 0.2526 -0.0624 -0.0070 -0.0035 204 ALA B CB  
3233 N N   . GLN B 148 ? 0.2603 0.1466 0.2679 -0.0460 -0.0226 0.0003  205 GLN B N   
3234 C CA  . GLN B 148 ? 0.2642 0.1337 0.2693 -0.0426 -0.0289 0.0017  205 GLN B CA  
3235 C C   . GLN B 148 ? 0.2664 0.1400 0.2797 -0.0347 -0.0331 -0.0063 205 GLN B C   
3236 O O   . GLN B 148 ? 0.3120 0.1724 0.3268 -0.0325 -0.0375 -0.0078 205 GLN B O   
3237 C CB  . GLN B 148 ? 0.2869 0.1469 0.2811 -0.0387 -0.0321 0.0090  205 GLN B CB  
3238 C CG  . GLN B 148 ? 0.4169 0.2640 0.3981 -0.0471 -0.0297 0.0177  205 GLN B CG  
3239 C CD  . GLN B 148 ? 0.6170 0.4608 0.5857 -0.0442 -0.0320 0.0242  205 GLN B CD  
3240 O OE1 . GLN B 148 ? 0.6081 0.4553 0.5794 -0.0353 -0.0374 0.0230  205 GLN B OE1 
3241 N NE2 . GLN B 148 ? 0.5822 0.4181 0.5367 -0.0522 -0.0280 0.0310  205 GLN B NE2 
3242 N N   . HIS B 149 ? 0.2537 0.1441 0.2713 -0.0305 -0.0315 -0.0114 206 HIS B N   
3243 C CA  . HIS B 149 ? 0.2596 0.1547 0.2823 -0.0242 -0.0341 -0.0195 206 HIS B CA  
3244 C C   . HIS B 149 ? 0.2754 0.1784 0.3044 -0.0283 -0.0337 -0.0259 206 HIS B C   
3245 O O   . HIS B 149 ? 0.2713 0.1804 0.3016 -0.0236 -0.0356 -0.0326 206 HIS B O   
3246 C CB  . HIS B 149 ? 0.2397 0.1459 0.2607 -0.0165 -0.0333 -0.0202 206 HIS B CB  
3247 C CG  . HIS B 149 ? 0.2560 0.1552 0.2744 -0.0114 -0.0353 -0.0158 206 HIS B CG  
3248 N ND1 . HIS B 149 ? 0.2995 0.1910 0.3211 -0.0053 -0.0385 -0.0192 206 HIS B ND1 
3249 C CD2 . HIS B 149 ? 0.2916 0.1898 0.3052 -0.0115 -0.0352 -0.0090 206 HIS B CD2 
3250 C CE1 . HIS B 149 ? 0.3128 0.2002 0.3337 -0.0015 -0.0408 -0.0144 206 HIS B CE1 
3251 N NE2 . HIS B 149 ? 0.3633 0.2541 0.3784 -0.0054 -0.0394 -0.0081 206 HIS B NE2 
3252 N N   A GLN B 150 ? 0.2257 0.1281 0.2583 -0.0371 -0.0314 -0.0242 207 GLN B N   
3253 N N   B GLN B 150 ? 0.2258 0.1285 0.2585 -0.0371 -0.0314 -0.0241 207 GLN B N   
3254 C CA  A GLN B 150 ? 0.2316 0.1423 0.2735 -0.0418 -0.0319 -0.0305 207 GLN B CA  
3255 C CA  B GLN B 150 ? 0.2316 0.1423 0.2735 -0.0418 -0.0319 -0.0304 207 GLN B CA  
3256 C C   A GLN B 150 ? 0.2522 0.1804 0.2965 -0.0375 -0.0320 -0.0341 207 GLN B C   
3257 C C   B GLN B 150 ? 0.2524 0.1806 0.2967 -0.0376 -0.0320 -0.0341 207 GLN B C   
3258 O O   A GLN B 150 ? 0.2429 0.1766 0.2912 -0.0362 -0.0360 -0.0411 207 GLN B O   
3259 O O   B GLN B 150 ? 0.2427 0.1763 0.2911 -0.0363 -0.0359 -0.0410 207 GLN B O   
3260 C CB  A GLN B 150 ? 0.2546 0.1555 0.2994 -0.0417 -0.0371 -0.0372 207 GLN B CB  
3261 C CB  B GLN B 150 ? 0.2549 0.1557 0.2996 -0.0417 -0.0370 -0.0371 207 GLN B CB  
3262 C CG  A GLN B 150 ? 0.2951 0.1767 0.3387 -0.0464 -0.0376 -0.0336 207 GLN B CG  
3263 C CG  B GLN B 150 ? 0.2946 0.1764 0.3385 -0.0468 -0.0375 -0.0335 207 GLN B CG  
3264 C CD  A GLN B 150 ? 0.3416 0.2135 0.3902 -0.0482 -0.0423 -0.0410 207 GLN B CD  
3265 C CD  B GLN B 150 ? 0.2973 0.1667 0.3328 -0.0403 -0.0390 -0.0288 207 GLN B CD  
3266 O OE1 A GLN B 150 ? 0.5046 0.3809 0.5536 -0.0430 -0.0460 -0.0491 207 GLN B OE1 
3267 O OE1 B GLN B 150 ? 0.3465 0.2160 0.3804 -0.0318 -0.0416 -0.0330 207 GLN B OE1 
3268 N NE2 A GLN B 150 ? 0.4497 0.3071 0.5008 -0.0560 -0.0422 -0.0383 207 GLN B NE2 
3269 N NE2 B GLN B 150 ? 0.3190 0.1774 0.3492 -0.0445 -0.0374 -0.0200 207 GLN B NE2 
3270 N N   . LEU B 151 ? 0.2250 0.1611 0.2660 -0.0356 -0.0282 -0.0294 208 LEU B N   
3271 C CA  . LEU B 151 ? 0.1928 0.1441 0.2363 -0.0319 -0.0281 -0.0316 208 LEU B CA  
3272 C C   . LEU B 151 ? 0.2011 0.1617 0.2503 -0.0370 -0.0229 -0.0288 208 LEU B C   
3273 O O   . LEU B 151 ? 0.2226 0.1778 0.2679 -0.0411 -0.0181 -0.0232 208 LEU B O   
3274 C CB  . LEU B 151 ? 0.1912 0.1439 0.2260 -0.0237 -0.0281 -0.0297 208 LEU B CB  
3275 C CG  . LEU B 151 ? 0.2212 0.1668 0.2507 -0.0178 -0.0314 -0.0333 208 LEU B CG  
3276 C CD1 . LEU B 151 ? 0.2898 0.2369 0.3134 -0.0114 -0.0296 -0.0301 208 LEU B CD1 
3277 C CD2 . LEU B 151 ? 0.2395 0.1893 0.2695 -0.0161 -0.0355 -0.0406 208 LEU B CD2 
3278 N N   . GLN B 152 ? 0.2051 0.1793 0.2633 -0.0365 -0.0240 -0.0329 209 GLN B N   
3279 C CA  . GLN B 152 ? 0.1980 0.1833 0.2627 -0.0387 -0.0189 -0.0315 209 GLN B CA  
3280 C C   . GLN B 152 ? 0.2112 0.2038 0.2716 -0.0309 -0.0201 -0.0309 209 GLN B C   
3281 O O   . GLN B 152 ? 0.2049 0.1978 0.2615 -0.0252 -0.0256 -0.0335 209 GLN B O   
3282 C CB  . GLN B 152 ? 0.2289 0.2251 0.3110 -0.0438 -0.0193 -0.0369 209 GLN B CB  
3283 C CG  . GLN B 152 ? 0.2798 0.2696 0.3684 -0.0531 -0.0168 -0.0374 209 GLN B CG  
3284 C CD  . GLN B 152 ? 0.4431 0.4449 0.5520 -0.0582 -0.0181 -0.0439 209 GLN B CD  
3285 O OE1 . GLN B 152 ? 0.5129 0.5188 0.6278 -0.0552 -0.0266 -0.0497 209 GLN B OE1 
3286 N NE2 . GLN B 152 ? 0.4255 0.4328 0.5451 -0.0662 -0.0097 -0.0432 209 GLN B NE2 
3287 N N   . PRO B 153 ? 0.1919 0.1893 0.2515 -0.0309 -0.0148 -0.0278 210 PRO B N   
3288 C CA  . PRO B 153 ? 0.1604 0.1646 0.2178 -0.0241 -0.0162 -0.0276 210 PRO B CA  
3289 C C   . PRO B 153 ? 0.1958 0.2103 0.2642 -0.0218 -0.0213 -0.0328 210 PRO B C   
3290 O O   . PRO B 153 ? 0.2074 0.2289 0.2897 -0.0263 -0.0211 -0.0364 210 PRO B O   
3291 C CB  . PRO B 153 ? 0.2131 0.2202 0.2701 -0.0263 -0.0091 -0.0246 210 PRO B CB  
3292 C CG  . PRO B 153 ? 0.2116 0.2192 0.2758 -0.0347 -0.0038 -0.0253 210 PRO B CG  
3293 C CD  . PRO B 153 ? 0.1990 0.1962 0.2604 -0.0378 -0.0071 -0.0250 210 PRO B CD  
3294 N N   A ILE B 154 ? 0.1734 0.1884 0.2354 -0.0150 -0.0261 -0.0329 211 ILE B N   
3295 N N   B ILE B 154 ? 0.1714 0.1865 0.2336 -0.0151 -0.0261 -0.0330 211 ILE B N   
3296 C CA  A ILE B 154 ? 0.2038 0.2265 0.2731 -0.0120 -0.0328 -0.0370 211 ILE B CA  
3297 C CA  B ILE B 154 ? 0.2053 0.2282 0.2753 -0.0122 -0.0328 -0.0372 211 ILE B CA  
3298 C C   A ILE B 154 ? 0.2164 0.2496 0.2972 -0.0108 -0.0310 -0.0374 211 ILE B C   
3299 C C   B ILE B 154 ? 0.2157 0.2491 0.2968 -0.0109 -0.0309 -0.0374 211 ILE B C   
3300 O O   A ILE B 154 ? 0.2188 0.2604 0.3123 -0.0098 -0.0363 -0.0415 211 ILE B O   
3301 O O   B ILE B 154 ? 0.2187 0.2605 0.3125 -0.0098 -0.0362 -0.0415 211 ILE B O   
3302 C CB  A ILE B 154 ? 0.2619 0.2790 0.3172 -0.0057 -0.0383 -0.0365 211 ILE B CB  
3303 C CB  B ILE B 154 ? 0.2600 0.2775 0.3165 -0.0061 -0.0387 -0.0370 211 ILE B CB  
3304 C CG1 A ILE B 154 ? 0.2769 0.2986 0.3364 -0.0032 -0.0474 -0.0408 211 ILE B CG1 
3305 C CG1 B ILE B 154 ? 0.2610 0.2767 0.3079 -0.0015 -0.0355 -0.0323 211 ILE B CG1 
3306 C CG2 A ILE B 154 ? 0.2632 0.2789 0.3099 -0.0014 -0.0348 -0.0318 211 ILE B CG2 
3307 C CG2 B ILE B 154 ? 0.2751 0.2828 0.3225 -0.0072 -0.0398 -0.0383 211 ILE B CG2 
3308 C CD1 A ILE B 154 ? 0.3268 0.3410 0.3693 0.0016  -0.0526 -0.0407 211 ILE B CD1 
3309 C CD1 B ILE B 154 ? 0.3145 0.3358 0.3641 0.0029  -0.0394 -0.0322 211 ILE B CD1 
3310 N N   . ALA B 155 ? 0.1663 0.1991 0.2436 -0.0107 -0.0241 -0.0338 212 ALA B N   
3311 C CA  . ALA B 155 ? 0.1745 0.2162 0.2624 -0.0099 -0.0208 -0.0348 212 ALA B CA  
3312 C C   . ALA B 155 ? 0.1606 0.1988 0.2423 -0.0133 -0.0116 -0.0316 212 ALA B C   
3313 O O   . ALA B 155 ? 0.1769 0.2056 0.2446 -0.0136 -0.0103 -0.0275 212 ALA B O   
3314 C CB  . ALA B 155 ? 0.2227 0.2656 0.3079 -0.0024 -0.0259 -0.0340 212 ALA B CB  
3315 N N   . VAL B 156 ? 0.1549 0.2007 0.2475 -0.0159 -0.0055 -0.0339 213 VAL B N   
3316 C CA  . VAL B 156 ? 0.1375 0.1798 0.2224 -0.0191 0.0031  -0.0315 213 VAL B CA  
3317 C C   . VAL B 156 ? 0.1527 0.2034 0.2470 -0.0160 0.0061  -0.0346 213 VAL B C   
3318 O O   . VAL B 156 ? 0.1783 0.2398 0.2906 -0.0171 0.0080  -0.0398 213 VAL B O   
3319 C CB  . VAL B 156 ? 0.1708 0.2117 0.2570 -0.0280 0.0106  -0.0316 213 VAL B CB  
3320 C CG1 . VAL B 156 ? 0.2124 0.2479 0.2866 -0.0312 0.0188  -0.0289 213 VAL B CG1 
3321 C CG2 . VAL B 156 ? 0.1888 0.2203 0.2678 -0.0311 0.0069  -0.0290 213 VAL B CG2 
3322 N N   . LEU B 157 ? 0.1622 0.2082 0.2462 -0.0120 0.0063  -0.0320 214 LEU B N   
3323 C CA  . LEU B 157 ? 0.1651 0.2168 0.2567 -0.0089 0.0092  -0.0351 214 LEU B CA  
3324 C C   . LEU B 157 ? 0.1826 0.2281 0.2611 -0.0117 0.0165  -0.0334 214 LEU B C   
3325 O O   . LEU B 157 ? 0.1640 0.2003 0.2270 -0.0146 0.0169  -0.0288 214 LEU B O   
3326 C CB  . LEU B 157 ? 0.2699 0.3213 0.3625 -0.0008 0.0012  -0.0343 214 LEU B CB  
3327 C CG  . LEU B 157 ? 0.4103 0.4673 0.5147 0.0024  -0.0073 -0.0364 214 LEU B CG  
3328 C CD1 . LEU B 157 ? 0.4066 0.4558 0.4979 0.0032  -0.0136 -0.0324 214 LEU B CD1 
3329 C CD2 . LEU B 157 ? 0.3262 0.3871 0.4406 0.0094  -0.0124 -0.0384 214 LEU B CD2 
3330 N N   . HIS B 158 ? 0.1652 0.2157 0.2504 -0.0108 0.0219  -0.0376 215 HIS B N   
3331 C CA  . HIS B 158 ? 0.1520 0.1969 0.2245 -0.0142 0.0295  -0.0374 215 HIS B CA  
3332 C C   . HIS B 158 ? 0.1695 0.2134 0.2420 -0.0084 0.0280  -0.0390 215 HIS B C   
3333 O O   . HIS B 158 ? 0.1883 0.2400 0.2767 -0.0042 0.0281  -0.0440 215 HIS B O   
3334 C CB  . HIS B 158 ? 0.2061 0.2570 0.2851 -0.0207 0.0405  -0.0424 215 HIS B CB  
3335 C CG  . HIS B 158 ? 0.2212 0.2753 0.3068 -0.0264 0.0421  -0.0420 215 HIS B CG  
3336 N ND1 . HIS B 158 ? 0.2133 0.2573 0.2835 -0.0317 0.0416  -0.0363 215 HIS B ND1 
3337 C CD2 . HIS B 158 ? 0.2650 0.3309 0.3721 -0.0276 0.0432  -0.0469 215 HIS B CD2 
3338 C CE1 . HIS B 158 ? 0.2384 0.2869 0.3193 -0.0363 0.0429  -0.0375 215 HIS B CE1 
3339 N NE2 . HIS B 158 ? 0.2607 0.3232 0.3645 -0.0342 0.0440  -0.0441 215 HIS B NE2 
3340 N N   . GLY B 159 ? 0.1842 0.2183 0.2400 -0.0083 0.0266  -0.0352 216 GLY B N   
3341 C CA  . GLY B 159 ? 0.1431 0.1743 0.1971 -0.0041 0.0257  -0.0367 216 GLY B CA  
3342 C C   . GLY B 159 ? 0.1757 0.2030 0.2193 -0.0081 0.0334  -0.0398 216 GLY B C   
3343 O O   . GLY B 159 ? 0.2270 0.2548 0.2659 -0.0141 0.0408  -0.0414 216 GLY B O   
3344 N N   . ASP B 160 ? 0.1583 0.1807 0.1974 -0.0051 0.0319  -0.0409 217 ASP B N   
3345 C CA  . ASP B 160 ? 0.1615 0.1792 0.1896 -0.0084 0.0384  -0.0450 217 ASP B CA  
3346 C C   . ASP B 160 ? 0.1921 0.1990 0.2030 -0.0092 0.0335  -0.0413 217 ASP B C   
3347 O O   . ASP B 160 ? 0.2196 0.2214 0.2214 -0.0106 0.0366  -0.0452 217 ASP B O   
3348 C CB  . ASP B 160 ? 0.1700 0.1927 0.2115 -0.0044 0.0428  -0.0530 217 ASP B CB  
3349 C CG  . ASP B 160 ? 0.2112 0.2306 0.2583 0.0021  0.0356  -0.0524 217 ASP B CG  
3350 O OD1 . ASP B 160 ? 0.1933 0.2065 0.2327 0.0029  0.0283  -0.0462 217 ASP B OD1 
3351 O OD2 . ASP B 160 ? 0.2473 0.2702 0.3079 0.0064  0.0376  -0.0584 217 ASP B OD2 
3352 N N   . TRP B 161 ? 0.1543 0.1579 0.1613 -0.0085 0.0259  -0.0346 218 TRP B N   
3353 C CA  . TRP B 161 ? 0.1617 0.1572 0.1572 -0.0088 0.0197  -0.0304 218 TRP B CA  
3354 C C   . TRP B 161 ? 0.1716 0.1663 0.1745 -0.0040 0.0150  -0.0306 218 TRP B C   
3355 O O   . TRP B 161 ? 0.1831 0.1730 0.1810 -0.0041 0.0096  -0.0272 218 TRP B O   
3356 C CB  . TRP B 161 ? 0.1914 0.1787 0.1689 -0.0135 0.0215  -0.0319 218 TRP B CB  
3357 C CG  . TRP B 161 ? 0.2132 0.1970 0.1772 -0.0196 0.0261  -0.0304 218 TRP B CG  
3358 C CD1 . TRP B 161 ? 0.2244 0.2053 0.1772 -0.0242 0.0342  -0.0348 218 TRP B CD1 
3359 C CD2 . TRP B 161 ? 0.2112 0.1920 0.1698 -0.0220 0.0228  -0.0242 218 TRP B CD2 
3360 N NE1 . TRP B 161 ? 0.2330 0.2087 0.1725 -0.0300 0.0364  -0.0308 218 TRP B NE1 
3361 C CE2 . TRP B 161 ? 0.2024 0.1776 0.1459 -0.0285 0.0291  -0.0243 218 TRP B CE2 
3362 C CE3 . TRP B 161 ? 0.1688 0.1502 0.1332 -0.0195 0.0158  -0.0188 218 TRP B CE3 
3363 C CZ2 . TRP B 161 ? 0.2368 0.2063 0.1714 -0.0325 0.0276  -0.0185 218 TRP B CZ2 
3364 C CZ3 . TRP B 161 ? 0.2070 0.1834 0.1638 -0.0228 0.0143  -0.0141 218 TRP B CZ3 
3365 C CH2 . TRP B 161 ? 0.2396 0.2097 0.1818 -0.0292 0.0197  -0.0136 218 TRP B CH2 
3366 N N   . SER B 162 ? 0.1762 0.1751 0.1917 0.0000  0.0166  -0.0342 219 SER B N   
3367 C CA  . SER B 162 ? 0.1561 0.1517 0.1769 0.0039  0.0125  -0.0339 219 SER B CA  
3368 C C   . SER B 162 ? 0.1475 0.1450 0.1753 0.0072  0.0075  -0.0285 219 SER B C   
3369 O O   . SER B 162 ? 0.1586 0.1613 0.1908 0.0080  0.0074  -0.0270 219 SER B O   
3370 C CB  . SER B 162 ? 0.1822 0.1788 0.2122 0.0070  0.0159  -0.0404 219 SER B CB  
3371 O OG  . SER B 162 ? 0.1733 0.1773 0.2174 0.0108  0.0165  -0.0415 219 SER B OG  
3372 N N   . ALA B 163 ? 0.1323 0.1249 0.1609 0.0090  0.0038  -0.0260 220 ALA B N   
3373 C CA  . ALA B 163 ? 0.1483 0.1410 0.1808 0.0118  0.0001  -0.0209 220 ALA B CA  
3374 C C   . ALA B 163 ? 0.1416 0.1376 0.1835 0.0162  -0.0007 -0.0220 220 ALA B C   
3375 O O   . ALA B 163 ? 0.1383 0.1371 0.1813 0.0175  -0.0031 -0.0190 220 ALA B O   
3376 C CB  . ALA B 163 ? 0.1446 0.1308 0.1764 0.0119  -0.0024 -0.0182 220 ALA B CB  
3377 N N   . LEU B 164 ? 0.1437 0.1389 0.1926 0.0187  0.0006  -0.0267 221 LEU B N   
3378 C CA  . LEU B 164 ? 0.1350 0.1332 0.1951 0.0238  -0.0018 -0.0279 221 LEU B CA  
3379 C C   . LEU B 164 ? 0.1609 0.1687 0.2263 0.0232  -0.0005 -0.0298 221 LEU B C   
3380 O O   . LEU B 164 ? 0.1382 0.1492 0.2102 0.0265  -0.0049 -0.0284 221 LEU B O   
3381 C CB  . LEU B 164 ? 0.1408 0.1369 0.2096 0.0269  -0.0002 -0.0338 221 LEU B CB  
3382 C CG  . LEU B 164 ? 0.1500 0.1488 0.2330 0.0332  -0.0041 -0.0354 221 LEU B CG  
3383 C CD1 . LEU B 164 ? 0.2090 0.2002 0.2882 0.0362  -0.0117 -0.0277 221 LEU B CD1 
3384 C CD2 . LEU B 164 ? 0.2157 0.2127 0.3089 0.0366  -0.0016 -0.0425 221 LEU B CD2 
3385 N N   A SER B 165 ? 0.1338 0.1457 0.1959 0.0187  0.0053  -0.0330 222 SER B N   
3386 N N   B SER B 165 ? 0.1336 0.1456 0.1958 0.0187  0.0054  -0.0330 222 SER B N   
3387 C CA  A SER B 165 ? 0.1569 0.1773 0.2241 0.0168  0.0075  -0.0346 222 SER B CA  
3388 C CA  B SER B 165 ? 0.1564 0.1769 0.2238 0.0169  0.0074  -0.0346 222 SER B CA  
3389 C C   A SER B 165 ? 0.1533 0.1733 0.2147 0.0157  0.0031  -0.0289 222 SER B C   
3390 C C   B SER B 165 ? 0.1537 0.1737 0.2151 0.0158  0.0030  -0.0288 222 SER B C   
3391 O O   A SER B 165 ? 0.1481 0.1740 0.2169 0.0165  0.0010  -0.0293 222 SER B O   
3392 O O   B SER B 165 ? 0.1477 0.1735 0.2164 0.0166  0.0008  -0.0292 222 SER B O   
3393 C CB  A SER B 165 ? 0.1819 0.2038 0.2433 0.0112  0.0154  -0.0384 222 SER B CB  
3394 C CB  B SER B 165 ? 0.1818 0.2043 0.2440 0.0113  0.0154  -0.0385 222 SER B CB  
3395 O OG  A SER B 165 ? 0.1825 0.2123 0.2501 0.0085  0.0190  -0.0404 222 SER B OG  
3396 O OG  B SER B 165 ? 0.1723 0.1897 0.2194 0.0066  0.0152  -0.0339 222 SER B OG  
3397 N N   . GLY B 166 ? 0.1487 0.1622 0.1982 0.0140  0.0015  -0.0241 223 GLY B N   
3398 C CA  . GLY B 166 ? 0.1579 0.1704 0.2025 0.0138  -0.0023 -0.0194 223 GLY B CA  
3399 C C   . GLY B 166 ? 0.1737 0.1855 0.2220 0.0184  -0.0078 -0.0173 223 GLY B C   
3400 O O   . GLY B 166 ? 0.1571 0.1712 0.2054 0.0188  -0.0108 -0.0162 223 GLY B O   
3401 N N   . TYR B 167 ? 0.1360 0.1431 0.1857 0.0217  -0.0096 -0.0165 224 TYR B N   
3402 C CA  . TYR B 167 ? 0.1416 0.1458 0.1930 0.0262  -0.0156 -0.0140 224 TYR B CA  
3403 C C   . TYR B 167 ? 0.1715 0.1832 0.2351 0.0291  -0.0188 -0.0179 224 TYR B C   
3404 O O   . TYR B 167 ? 0.1499 0.1624 0.2126 0.0307  -0.0243 -0.0163 224 TYR B O   
3405 C CB  . TYR B 167 ? 0.1491 0.1454 0.2006 0.0289  -0.0169 -0.0125 224 TYR B CB  
3406 C CG  . TYR B 167 ? 0.1427 0.1342 0.1954 0.0340  -0.0239 -0.0097 224 TYR B CG  
3407 C CD1 . TYR B 167 ? 0.1545 0.1389 0.1949 0.0340  -0.0271 -0.0035 224 TYR B CD1 
3408 C CD2 . TYR B 167 ? 0.1534 0.1471 0.2190 0.0388  -0.0274 -0.0134 224 TYR B CD2 
3409 C CE1 . TYR B 167 ? 0.1551 0.1331 0.1931 0.0384  -0.0344 -0.0003 224 TYR B CE1 
3410 C CE2 . TYR B 167 ? 0.1649 0.1530 0.2311 0.0439  -0.0357 -0.0103 224 TYR B CE2 
3411 C CZ  . TYR B 167 ? 0.1741 0.1537 0.2250 0.0435  -0.0396 -0.0034 224 TYR B CZ  
3412 O OH  . TYR B 167 ? 0.2147 0.1869 0.2631 0.0485  -0.0487 0.0001  224 TYR B OH  
3413 N N   . GLN B 168 ? 0.1314 0.1489 0.2071 0.0296  -0.0154 -0.0237 225 GLN B N   
3414 C CA  . GLN B 168 ? 0.1210 0.1470 0.2128 0.0327  -0.0184 -0.0282 225 GLN B CA  
3415 C C   . GLN B 168 ? 0.1417 0.1753 0.2355 0.0292  -0.0182 -0.0293 225 GLN B C   
3416 O O   . GLN B 168 ? 0.1503 0.1881 0.2521 0.0318  -0.0247 -0.0302 225 GLN B O   
3417 C CB  . GLN B 168 ? 0.1230 0.1545 0.2286 0.0335  -0.0127 -0.0353 225 GLN B CB  
3418 C CG  . GLN B 168 ? 0.1378 0.1615 0.2448 0.0381  -0.0144 -0.0353 225 GLN B CG  
3419 C CD  . GLN B 168 ? 0.1887 0.2167 0.3071 0.0385  -0.0074 -0.0432 225 GLN B CD  
3420 O OE1 . GLN B 168 ? 0.2150 0.2508 0.3362 0.0341  0.0005  -0.0480 225 GLN B OE1 
3421 N NE2 . GLN B 168 ? 0.1584 0.1802 0.2824 0.0436  -0.0097 -0.0448 225 GLN B NE2 
3422 N N   . GLN B 169 ? 0.1434 0.1780 0.2301 0.0233  -0.0116 -0.0293 226 GLN B N   
3423 C CA  . GLN B 169 ? 0.1418 0.1820 0.2305 0.0194  -0.0111 -0.0303 226 GLN B CA  
3424 C C   . GLN B 169 ? 0.1632 0.1985 0.2420 0.0202  -0.0178 -0.0258 226 GLN B C   
3425 O O   . GLN B 169 ? 0.1584 0.1982 0.2424 0.0197  -0.0216 -0.0273 226 GLN B O   
3426 C CB  . GLN B 169 ? 0.1654 0.2053 0.2473 0.0129  -0.0028 -0.0308 226 GLN B CB  
3427 C CG  . GLN B 169 ? 0.1689 0.2138 0.2587 0.0108  0.0053  -0.0362 226 GLN B CG  
3428 C CD  . GLN B 169 ? 0.2077 0.2639 0.3188 0.0126  0.0057  -0.0425 226 GLN B CD  
3429 O OE1 . GLN B 169 ? 0.2274 0.2899 0.3467 0.0107  0.0039  -0.0437 226 GLN B OE1 
3430 N NE2 . GLN B 169 ? 0.2714 0.3306 0.3931 0.0164  0.0076  -0.0470 226 GLN B NE2 
3431 N N   . THR B 170 ? 0.1438 0.1703 0.2088 0.0213  -0.0189 -0.0209 227 THR B N   
3432 C CA  . THR B 170 ? 0.1560 0.1776 0.2106 0.0220  -0.0238 -0.0173 227 THR B CA  
3433 C C   . THR B 170 ? 0.1625 0.1836 0.2200 0.0269  -0.0323 -0.0171 227 THR B C   
3434 O O   . THR B 170 ? 0.1621 0.1834 0.2167 0.0271  -0.0374 -0.0173 227 THR B O   
3435 C CB  . THR B 170 ? 0.1422 0.1555 0.1831 0.0214  -0.0214 -0.0126 227 THR B CB  
3436 O OG1 . THR B 170 ? 0.1540 0.1678 0.1926 0.0172  -0.0157 -0.0128 227 THR B OG1 
3437 C CG2 . THR B 170 ? 0.1711 0.1797 0.2010 0.0219  -0.0246 -0.0098 227 THR B CG2 
3438 N N   . MET B 171 ? 0.1514 0.1708 0.2144 0.0311  -0.0348 -0.0169 228 MET B N   
3439 C CA  . MET B 171 ? 0.1595 0.1777 0.2264 0.0363  -0.0445 -0.0167 228 MET B CA  
3440 C C   . MET B 171 ? 0.1757 0.2049 0.2584 0.0363  -0.0485 -0.0223 228 MET B C   
3441 O O   . MET B 171 ? 0.1798 0.2083 0.2608 0.0384  -0.0576 -0.0221 228 MET B O   
3442 C CB  . MET B 171 ? 0.1705 0.1856 0.2444 0.0407  -0.0456 -0.0165 228 MET B CB  
3443 C CG  . MET B 171 ? 0.2060 0.2076 0.2647 0.0422  -0.0465 -0.0099 228 MET B CG  
3444 S SD  . MET B 171 ? 0.2107 0.2006 0.2456 0.0415  -0.0504 -0.0027 228 MET B SD  
3445 C CE  . MET B 171 ? 0.2772 0.2602 0.3140 0.0487  -0.0632 -0.0005 228 MET B CE  
3446 N N   . GLN B 172 ? 0.1471 0.1864 0.2452 0.0335  -0.0418 -0.0276 229 GLN B N   
3447 C CA  . GLN B 172 ? 0.1646 0.2155 0.2804 0.0324  -0.0442 -0.0334 229 GLN B CA  
3448 C C   . GLN B 172 ? 0.1914 0.2419 0.2990 0.0281  -0.0457 -0.0328 229 GLN B C   
3449 O O   . GLN B 172 ? 0.1879 0.2431 0.3036 0.0289  -0.0535 -0.0356 229 GLN B O   
3450 C CB  . GLN B 172 ? 0.2154 0.2762 0.3471 0.0291  -0.0341 -0.0390 229 GLN B CB  
3451 C CG  . GLN B 172 ? 0.2397 0.3144 0.3952 0.0282  -0.0356 -0.0459 229 GLN B CG  
3452 C CD  . GLN B 172 ? 0.2580 0.3367 0.4299 0.0360  -0.0462 -0.0485 229 GLN B CD  
3453 O OE1 . GLN B 172 ? 0.3884 0.4682 0.5699 0.0404  -0.0448 -0.0505 229 GLN B OE1 
3454 N NE2 . GLN B 172 ? 0.2702 0.3500 0.4444 0.0379  -0.0577 -0.0484 229 GLN B NE2 
3455 N N   A MET B 173 ? 0.1794 0.2239 0.2718 0.0238  -0.0391 -0.0296 230 MET B N   
3456 N N   B MET B 173 ? 0.1794 0.2241 0.2721 0.0237  -0.0391 -0.0297 230 MET B N   
3457 C CA  A MET B 173 ? 0.1900 0.2321 0.2737 0.0200  -0.0399 -0.0291 230 MET B CA  
3458 C CA  B MET B 173 ? 0.1898 0.2323 0.2742 0.0201  -0.0404 -0.0293 230 MET B CA  
3459 C C   A MET B 173 ? 0.2322 0.2684 0.3054 0.0234  -0.0498 -0.0274 230 MET B C   
3460 C C   B MET B 173 ? 0.2345 0.2711 0.3088 0.0238  -0.0505 -0.0277 230 MET B C   
3461 O O   A MET B 173 ? 0.2413 0.2792 0.3158 0.0218  -0.0547 -0.0301 230 MET B O   
3462 O O   B MET B 173 ? 0.2358 0.2749 0.3130 0.0226  -0.0562 -0.0306 230 MET B O   
3463 C CB  A MET B 173 ? 0.2310 0.2664 0.3005 0.0165  -0.0323 -0.0255 230 MET B CB  
3464 C CB  B MET B 173 ? 0.2332 0.2687 0.3029 0.0165  -0.0330 -0.0257 230 MET B CB  
3465 C CG  A MET B 173 ? 0.2957 0.3275 0.3569 0.0129  -0.0321 -0.0252 230 MET B CG  
3466 C CG  B MET B 173 ? 0.2605 0.2908 0.3191 0.0146  -0.0352 -0.0249 230 MET B CG  
3467 S SD  A MET B 173 ? 0.3340 0.3569 0.3794 0.0116  -0.0258 -0.0204 230 MET B SD  
3468 S SD  B MET B 173 ? 0.3447 0.3670 0.3888 0.0124  -0.0280 -0.0207 230 MET B SD  
3469 C CE  A MET B 173 ? 0.3492 0.3652 0.3822 0.0168  -0.0299 -0.0167 230 MET B CE  
3470 C CE  B MET B 173 ? 0.1976 0.2246 0.2506 0.0091  -0.0203 -0.0214 230 MET B CE  
3471 N N   . LEU B 174 ? 0.1860 0.2140 0.2475 0.0278  -0.0529 -0.0230 231 LEU B N   
3472 C CA  . LEU B 174 ? 0.2249 0.2446 0.2714 0.0307  -0.0613 -0.0205 231 LEU B CA  
3473 C C   . LEU B 174 ? 0.2832 0.3065 0.3396 0.0346  -0.0732 -0.0232 231 LEU B C   
3474 O O   . LEU B 174 ? 0.3238 0.3402 0.3668 0.0366  -0.0818 -0.0219 231 LEU B O   
3475 C CB  . LEU B 174 ? 0.2445 0.2533 0.2750 0.0331  -0.0596 -0.0143 231 LEU B CB  
3476 C CG  . LEU B 174 ? 0.2415 0.2466 0.2622 0.0295  -0.0495 -0.0117 231 LEU B CG  
3477 C CD1 . LEU B 174 ? 0.2859 0.2818 0.2953 0.0314  -0.0474 -0.0061 231 LEU B CD1 
3478 C CD2 . LEU B 174 ? 0.2612 0.2633 0.2703 0.0269  -0.0486 -0.0125 231 LEU B CD2 
3479 N N   . ASN B 175 ? 0.2766 0.3106 0.3560 0.0360  -0.0741 -0.0273 232 ASN B N   
3480 C CA  . ASN B 175 ? 0.2812 0.3213 0.3753 0.0397  -0.0861 -0.0312 232 ASN B CA  
3481 C C   . ASN B 175 ? 0.3590 0.4072 0.4626 0.0353  -0.0886 -0.0369 232 ASN B C   
3482 O O   . ASN B 175 ? 0.3861 0.4376 0.4976 0.0378  -0.1007 -0.0400 232 ASN B O   
3483 C CB  . ASN B 175 ? 0.3029 0.3527 0.4217 0.0430  -0.0855 -0.0347 232 ASN B CB  
3484 C CG  . ASN B 175 ? 0.3864 0.4269 0.4987 0.0492  -0.0891 -0.0299 232 ASN B CG  
3485 O OD1 . ASN B 175 ? 0.5833 0.6119 0.6779 0.0527  -0.0981 -0.0248 232 ASN B OD1 
3486 N ND2 . ASN B 175 ? 0.4974 0.5422 0.6233 0.0505  -0.0821 -0.0317 232 ASN B ND2 
3487 N N   . GLU B 176 ? 0.3457 0.3965 0.4489 0.0289  -0.0782 -0.0382 233 GLU B N   
3488 C CA  . GLU B 176 ? 0.5240 0.5824 0.6389 0.0237  -0.0789 -0.0437 233 GLU B CA  
3489 C C   . GLU B 176 ? 0.5020 0.5512 0.5973 0.0205  -0.0795 -0.0426 233 GLU B C   
3490 O O   . GLU B 176 ? 0.5530 0.6060 0.6557 0.0167  -0.0827 -0.0472 233 GLU B O   
3491 C CB  . GLU B 176 ? 0.5069 0.5749 0.6385 0.0180  -0.0666 -0.0465 233 GLU B CB  
3492 C CG  . GLU B 176 ? 0.6247 0.7055 0.7822 0.0197  -0.0646 -0.0508 233 GLU B CG  
3493 C CD  . GLU B 176 ? 0.7247 0.8119 0.8983 0.0258  -0.0783 -0.0544 233 GLU B CD  
3494 O OE1 . GLU B 176 ? 0.5811 0.6707 0.7591 0.0249  -0.0879 -0.0575 233 GLU B OE1 
3495 O OE2 . GLU B 176 ? 0.7139 0.8036 0.8968 0.0316  -0.0799 -0.0545 233 GLU B OE2 
3496 N N   . GLY B 177 ? 0.4103 0.4478 0.4825 0.0217  -0.0761 -0.0372 234 GLY B N   
3497 C CA  . GLY B 177 ? 0.5510 0.5806 0.6070 0.0187  -0.0745 -0.0373 234 GLY B CA  
3498 C C   . GLY B 177 ? 0.4912 0.5102 0.5258 0.0204  -0.0689 -0.0316 234 GLY B C   
3499 O O   . GLY B 177 ? 0.3889 0.4059 0.4204 0.0234  -0.0668 -0.0274 234 GLY B O   
3500 N N   . LEU B 178 ? 0.3315 0.3436 0.3525 0.0183  -0.0664 -0.0321 235 LEU B N   
3501 C CA  . LEU B 178 ? 0.2934 0.2963 0.2956 0.0196  -0.0607 -0.0279 235 LEU B CA  
3502 C C   . LEU B 178 ? 0.2610 0.2622 0.2625 0.0160  -0.0528 -0.0289 235 LEU B C   
3503 O O   . LEU B 178 ? 0.2841 0.2809 0.2787 0.0148  -0.0541 -0.0323 235 LEU B O   
3504 C CB  . LEU B 178 ? 0.3880 0.3815 0.3698 0.0223  -0.0670 -0.0275 235 LEU B CB  
3505 C CG  . LEU B 178 ? 0.4162 0.4010 0.3797 0.0233  -0.0597 -0.0230 235 LEU B CG  
3506 C CD1 . LEU B 178 ? 0.4173 0.4025 0.3835 0.0253  -0.0569 -0.0173 235 LEU B CD1 
3507 C CD2 . LEU B 178 ? 0.5760 0.5504 0.5163 0.0247  -0.0640 -0.0234 235 LEU B CD2 
3508 N N   . PRO B 179 ? 0.2119 0.2159 0.2204 0.0145  -0.0451 -0.0263 236 PRO B N   
3509 C CA  . PRO B 179 ? 0.2179 0.2185 0.2242 0.0121  -0.0387 -0.0262 236 PRO B CA  
3510 C C   . PRO B 179 ? 0.2153 0.2089 0.2070 0.0144  -0.0353 -0.0243 236 PRO B C   
3511 O O   . PRO B 179 ? 0.2172 0.2083 0.2000 0.0170  -0.0357 -0.0216 236 PRO B O   
3512 C CB  . PRO B 179 ? 0.2311 0.2361 0.2471 0.0102  -0.0331 -0.0235 236 PRO B CB  
3513 C CG  . PRO B 179 ? 0.2880 0.2956 0.3049 0.0132  -0.0342 -0.0211 236 PRO B CG  
3514 C CD  . PRO B 179 ? 0.2570 0.2657 0.2738 0.0155  -0.0425 -0.0233 236 PRO B CD  
3515 N N   . THR B 180 ? 0.2138 0.2037 0.2036 0.0132  -0.0314 -0.0258 237 THR B N   
3516 C CA  . THR B 180 ? 0.2116 0.1971 0.1926 0.0151  -0.0260 -0.0245 237 THR B CA  
3517 C C   . THR B 180 ? 0.1646 0.1522 0.1529 0.0145  -0.0206 -0.0211 237 THR B C   
3518 O O   . THR B 180 ? 0.1836 0.1696 0.1683 0.0160  -0.0160 -0.0197 237 THR B O   
3519 C CB  . THR B 180 ? 0.1919 0.1718 0.1668 0.0153  -0.0253 -0.0293 237 THR B CB  
3520 O OG1 . THR B 180 ? 0.2099 0.1892 0.1946 0.0131  -0.0252 -0.0311 237 THR B OG1 
3521 C CG2 . THR B 180 ? 0.2441 0.2206 0.2090 0.0156  -0.0315 -0.0334 237 THR B CG2 
3522 N N   . ALA B 181 ? 0.1651 0.1562 0.1634 0.0122  -0.0211 -0.0199 238 ALA B N   
3523 C CA  . ALA B 181 ? 0.1517 0.1437 0.1546 0.0115  -0.0173 -0.0167 238 ALA B CA  
3524 C C   . ALA B 181 ? 0.1739 0.1700 0.1837 0.0091  -0.0177 -0.0153 238 ALA B C   
3525 O O   . ALA B 181 ? 0.1740 0.1724 0.1883 0.0070  -0.0200 -0.0173 238 ALA B O   
3526 C CB  . ALA B 181 ? 0.1600 0.1479 0.1650 0.0110  -0.0160 -0.0175 238 ALA B CB  
3527 N N   . LEU B 182 ? 0.1637 0.1611 0.1749 0.0091  -0.0152 -0.0124 239 LEU B N   
3528 C CA  . LEU B 182 ? 0.1429 0.1436 0.1590 0.0068  -0.0142 -0.0116 239 LEU B CA  
3529 C C   . LEU B 182 ? 0.1372 0.1349 0.1524 0.0050  -0.0122 -0.0093 239 LEU B C   
3530 O O   . LEU B 182 ? 0.1738 0.1702 0.1874 0.0068  -0.0115 -0.0077 239 LEU B O   
3531 C CB  . LEU B 182 ? 0.1384 0.1422 0.1554 0.0090  -0.0142 -0.0108 239 LEU B CB  
3532 C CG  . LEU B 182 ? 0.2443 0.2520 0.2670 0.0077  -0.0126 -0.0112 239 LEU B CG  
3533 C CD1 . LEU B 182 ? 0.2478 0.2599 0.2776 0.0052  -0.0130 -0.0143 239 LEU B CD1 
3534 C CD2 . LEU B 182 ? 0.2009 0.2095 0.2243 0.0111  -0.0137 -0.0105 239 LEU B CD2 
3535 N N   . LEU B 183 ? 0.1416 0.1381 0.1577 0.0012  -0.0114 -0.0092 240 LEU B N   
3536 C CA  . LEU B 183 ? 0.1457 0.1382 0.1582 -0.0010 -0.0103 -0.0067 240 LEU B CA  
3537 C C   . LEU B 183 ? 0.1346 0.1307 0.1475 -0.0026 -0.0075 -0.0070 240 LEU B C   
3538 O O   . LEU B 183 ? 0.1646 0.1649 0.1817 -0.0045 -0.0054 -0.0092 240 LEU B O   
3539 C CB  . LEU B 183 ? 0.1696 0.1561 0.1796 -0.0049 -0.0107 -0.0057 240 LEU B CB  
3540 C CG  . LEU B 183 ? 0.1698 0.1506 0.1796 -0.0032 -0.0138 -0.0056 240 LEU B CG  
3541 C CD1 . LEU B 183 ? 0.1971 0.1715 0.2056 -0.0075 -0.0142 -0.0051 240 LEU B CD1 
3542 C CD2 . LEU B 183 ? 0.2032 0.1802 0.2113 -0.0006 -0.0160 -0.0033 240 LEU B CD2 
3543 N N   . VAL B 184 ? 0.1431 0.1378 0.1530 -0.0016 -0.0075 -0.0056 241 VAL B N   
3544 C CA  . VAL B 184 ? 0.1729 0.1701 0.1827 -0.0025 -0.0048 -0.0069 241 VAL B CA  
3545 C C   . VAL B 184 ? 0.1557 0.1472 0.1569 -0.0058 -0.0043 -0.0054 241 VAL B C   
3546 O O   . VAL B 184 ? 0.1774 0.1638 0.1745 -0.0055 -0.0079 -0.0029 241 VAL B O   
3547 C CB  . VAL B 184 ? 0.1633 0.1628 0.1762 0.0013  -0.0055 -0.0071 241 VAL B CB  
3548 C CG1 . VAL B 184 ? 0.1573 0.1591 0.1720 0.0011  -0.0029 -0.0094 241 VAL B CG1 
3549 C CG2 . VAL B 184 ? 0.1468 0.1490 0.1636 0.0045  -0.0070 -0.0074 241 VAL B CG2 
3550 N N   . ALA B 185 ? 0.1422 0.1343 0.1406 -0.0090 0.0000  -0.0072 242 ALA B N   
3551 C CA  . ALA B 185 ? 0.1760 0.1608 0.1622 -0.0132 0.0007  -0.0057 242 ALA B CA  
3552 C C   . ALA B 185 ? 0.1572 0.1388 0.1378 -0.0121 -0.0019 -0.0056 242 ALA B C   
3553 O O   . ALA B 185 ? 0.1797 0.1539 0.1481 -0.0152 -0.0032 -0.0040 242 ALA B O   
3554 C CB  . ALA B 185 ? 0.1887 0.1748 0.1724 -0.0180 0.0079  -0.0083 242 ALA B CB  
3555 N N   . ASN B 186 ? 0.1472 0.1334 0.1356 -0.0083 -0.0030 -0.0072 243 ASN B N   
3556 C CA  . ASN B 186 ? 0.1703 0.1532 0.1555 -0.0075 -0.0067 -0.0070 243 ASN B CA  
3557 C C   . ASN B 186 ? 0.1466 0.1339 0.1424 -0.0035 -0.0082 -0.0071 243 ASN B C   
3558 O O   . ASN B 186 ? 0.1507 0.1425 0.1537 -0.0011 -0.0065 -0.0074 243 ASN B O   
3559 C CB  . ASN B 186 ? 0.1702 0.1500 0.1467 -0.0103 -0.0040 -0.0101 243 ASN B CB  
3560 C CG  . ASN B 186 ? 0.1795 0.1642 0.1638 -0.0082 0.0000  -0.0144 243 ASN B CG  
3561 O OD1 . ASN B 186 ? 0.1676 0.1581 0.1625 -0.0053 0.0014  -0.0148 243 ASN B OD1 
3562 N ND2 . ASN B 186 ? 0.1736 0.1549 0.1517 -0.0096 0.0012  -0.0178 243 ASN B ND2 
3563 N N   . ASP B 187 ? 0.1598 0.1451 0.1560 -0.0031 -0.0118 -0.0068 244 ASP B N   
3564 C CA  . ASP B 187 ? 0.1458 0.1345 0.1518 -0.0003 -0.0124 -0.0064 244 ASP B CA  
3565 C C   . ASP B 187 ? 0.1376 0.1276 0.1471 0.0008  -0.0093 -0.0086 244 ASP B C   
3566 O O   . ASP B 187 ? 0.1428 0.1348 0.1582 0.0031  -0.0083 -0.0074 244 ASP B O   
3567 C CB  . ASP B 187 ? 0.1664 0.1536 0.1751 -0.0008 -0.0171 -0.0059 244 ASP B CB  
3568 C CG  . ASP B 187 ? 0.1839 0.1705 0.1938 -0.0003 -0.0214 -0.0037 244 ASP B CG  
3569 O OD1 . ASP B 187 ? 0.1680 0.1544 0.1761 0.0004  -0.0205 -0.0023 244 ASP B OD1 
3570 O OD2 . ASP B 187 ? 0.1739 0.1600 0.1878 -0.0004 -0.0263 -0.0037 244 ASP B OD2 
3571 N N   . GLN B 188 ? 0.1456 0.1335 0.1505 -0.0007 -0.0076 -0.0118 245 GLN B N   
3572 C CA  . GLN B 188 ? 0.1323 0.1208 0.1423 0.0012  -0.0050 -0.0143 245 GLN B CA  
3573 C C   . GLN B 188 ? 0.1537 0.1464 0.1690 0.0038  -0.0027 -0.0140 245 GLN B C   
3574 O O   . GLN B 188 ? 0.1507 0.1436 0.1716 0.0067  -0.0033 -0.0129 245 GLN B O   
3575 C CB  . GLN B 188 ? 0.1700 0.1555 0.1743 -0.0007 -0.0029 -0.0190 245 GLN B CB  
3576 C CG  . GLN B 188 ? 0.1601 0.1405 0.1598 -0.0029 -0.0067 -0.0200 245 GLN B CG  
3577 C CD  . GLN B 188 ? 0.2058 0.1821 0.1983 -0.0047 -0.0044 -0.0256 245 GLN B CD  
3578 O OE1 . GLN B 188 ? 0.1990 0.1717 0.1790 -0.0079 -0.0043 -0.0270 245 GLN B OE1 
3579 N NE2 . GLN B 188 ? 0.1790 0.1545 0.1783 -0.0025 -0.0022 -0.0291 245 GLN B NE2 
3580 N N   . MET B 189 ? 0.1419 0.1374 0.1552 0.0026  -0.0008 -0.0147 246 MET B N   
3581 C CA  . MET B 189 ? 0.1489 0.1492 0.1688 0.0049  -0.0001 -0.0148 246 MET B CA  
3582 C C   . MET B 189 ? 0.1255 0.1257 0.1465 0.0070  -0.0032 -0.0109 246 MET B C   
3583 O O   . MET B 189 ? 0.1528 0.1546 0.1781 0.0099  -0.0043 -0.0105 246 MET B O   
3584 C CB  . MET B 189 ? 0.1583 0.1616 0.1771 0.0022  0.0028  -0.0164 246 MET B CB  
3585 C CG  . MET B 189 ? 0.1384 0.1425 0.1564 0.0000  0.0080  -0.0211 246 MET B CG  
3586 S SD  . MET B 189 ? 0.1692 0.1786 0.1897 -0.0038 0.0134  -0.0234 246 MET B SD  
3587 C CE  . MET B 189 ? 0.1879 0.1904 0.1952 -0.0081 0.0111  -0.0181 246 MET B CE  
3588 N N   . ALA B 190 ? 0.1381 0.1363 0.1553 0.0056  -0.0047 -0.0084 247 ALA B N   
3589 C CA  . ALA B 190 ? 0.1322 0.1306 0.1504 0.0074  -0.0061 -0.0058 247 ALA B CA  
3590 C C   . ALA B 190 ? 0.1265 0.1231 0.1467 0.0094  -0.0060 -0.0043 247 ALA B C   
3591 O O   . ALA B 190 ? 0.1577 0.1540 0.1770 0.0112  -0.0062 -0.0026 247 ALA B O   
3592 C CB  . ALA B 190 ? 0.1416 0.1387 0.1581 0.0061  -0.0075 -0.0043 247 ALA B CB  
3593 N N   . LEU B 191 ? 0.1301 0.1244 0.1517 0.0086  -0.0057 -0.0050 248 LEU B N   
3594 C CA  . LEU B 191 ? 0.1260 0.1170 0.1495 0.0097  -0.0054 -0.0033 248 LEU B CA  
3595 C C   . LEU B 191 ? 0.1486 0.1385 0.1723 0.0129  -0.0062 -0.0030 248 LEU B C   
3596 O O   . LEU B 191 ? 0.1446 0.1313 0.1660 0.0144  -0.0067 0.0001  248 LEU B O   
3597 C CB  . LEU B 191 ? 0.1177 0.1057 0.1433 0.0080  -0.0055 -0.0050 248 LEU B CB  
3598 C CG  . LEU B 191 ? 0.1383 0.1210 0.1664 0.0084  -0.0050 -0.0033 248 LEU B CG  
3599 C CD1 . LEU B 191 ? 0.1709 0.1534 0.2004 0.0066  -0.0036 0.0000  248 LEU B CD1 
3600 C CD2 . LEU B 191 ? 0.1593 0.1386 0.1895 0.0071  -0.0056 -0.0068 248 LEU B CD2 
3601 N N   . GLY B 192 ? 0.1365 0.1290 0.1631 0.0138  -0.0064 -0.0064 249 GLY B N   
3602 C CA  . GLY B 192 ? 0.1328 0.1256 0.1631 0.0174  -0.0084 -0.0070 249 GLY B CA  
3603 C C   . GLY B 192 ? 0.1399 0.1349 0.1677 0.0186  -0.0106 -0.0053 249 GLY B C   
3604 O O   . GLY B 192 ? 0.1434 0.1356 0.1702 0.0217  -0.0140 -0.0033 249 GLY B O   
3605 N N   . ALA B 193 ? 0.1358 0.1346 0.1616 0.0163  -0.0095 -0.0058 250 ALA B N   
3606 C CA  . ALA B 193 ? 0.1509 0.1508 0.1737 0.0172  -0.0118 -0.0049 250 ALA B CA  
3607 C C   . ALA B 193 ? 0.1519 0.1464 0.1668 0.0181  -0.0122 -0.0011 250 ALA B C   
3608 O O   . ALA B 193 ? 0.1556 0.1480 0.1660 0.0202  -0.0154 0.0001  250 ALA B O   
3609 C CB  . ALA B 193 ? 0.1472 0.1503 0.1694 0.0144  -0.0104 -0.0064 250 ALA B CB  
3610 N N   . LEU B 194 ? 0.1424 0.1345 0.1556 0.0162  -0.0090 0.0007  251 LEU B N   
3611 C CA  . LEU B 194 ? 0.1317 0.1191 0.1383 0.0163  -0.0074 0.0040  251 LEU B CA  
3612 C C   . LEU B 194 ? 0.1543 0.1352 0.1568 0.0184  -0.0096 0.0069  251 LEU B C   
3613 O O   . LEU B 194 ? 0.1651 0.1409 0.1579 0.0192  -0.0102 0.0097  251 LEU B O   
3614 C CB  . LEU B 194 ? 0.1418 0.1292 0.1514 0.0136  -0.0034 0.0048  251 LEU B CB  
3615 C CG  . LEU B 194 ? 0.1362 0.1282 0.1493 0.0122  -0.0023 0.0028  251 LEU B CG  
3616 C CD1 . LEU B 194 ? 0.1687 0.1614 0.1878 0.0099  -0.0001 0.0031  251 LEU B CD1 
3617 C CD2 . LEU B 194 ? 0.1585 0.1509 0.1667 0.0130  -0.0011 0.0025  251 LEU B CD2 
3618 N N   . ARG B 195 ? 0.1473 0.1269 0.1557 0.0193  -0.0109 0.0063  252 ARG B N   
3619 C CA  . ARG B 195 ? 0.1505 0.1224 0.1560 0.0218  -0.0140 0.0093  252 ARG B CA  
3620 C C   . ARG B 195 ? 0.1510 0.1230 0.1537 0.0255  -0.0200 0.0092  252 ARG B C   
3621 O O   . ARG B 195 ? 0.1742 0.1382 0.1668 0.0270  -0.0231 0.0133  252 ARG B O   
3622 C CB  . ARG B 195 ? 0.1447 0.1154 0.1591 0.0226  -0.0144 0.0073  252 ARG B CB  
3623 C CG  . ARG B 195 ? 0.1600 0.1216 0.1727 0.0262  -0.0189 0.0103  252 ARG B CG  
3624 C CD  . ARG B 195 ? 0.1751 0.1347 0.1979 0.0280  -0.0196 0.0072  252 ARG B CD  
3625 N NE  . ARG B 195 ? 0.1952 0.1473 0.2185 0.0329  -0.0259 0.0094  252 ARG B NE  
3626 C CZ  . ARG B 195 ? 0.2110 0.1656 0.2459 0.0373  -0.0294 0.0050  252 ARG B CZ  
3627 N NH1 . ARG B 195 ? 0.1883 0.1510 0.2337 0.0367  -0.0256 -0.0018 252 ARG B NH1 
3628 N NH2 . ARG B 195 ? 0.2099 0.1589 0.2456 0.0427  -0.0369 0.0071  252 ARG B NH2 
3629 N N   . ALA B 196 ? 0.1632 0.1435 0.1743 0.0265  -0.0219 0.0045  253 ALA B N   
3630 C CA  . ALA B 196 ? 0.1679 0.1500 0.1796 0.0297  -0.0285 0.0035  253 ALA B CA  
3631 C C   . ALA B 196 ? 0.1547 0.1332 0.1529 0.0291  -0.0300 0.0058  253 ALA B C   
3632 O O   . ALA B 196 ? 0.1915 0.1645 0.1822 0.0319  -0.0364 0.0080  253 ALA B O   
3633 C CB  . ALA B 196 ? 0.1863 0.1792 0.2107 0.0292  -0.0283 -0.0023 253 ALA B CB  
3634 N N   . LEU B 197 ? 0.1831 0.1640 0.1774 0.0257  -0.0246 0.0052  254 LEU B N   
3635 C CA  . LEU B 197 ? 0.1814 0.1588 0.1629 0.0252  -0.0247 0.0061  254 LEU B CA  
3636 C C   . LEU B 197 ? 0.1915 0.1581 0.1584 0.0253  -0.0238 0.0115  254 LEU B C   
3637 O O   . LEU B 197 ? 0.2228 0.1831 0.1765 0.0268  -0.0283 0.0132  254 LEU B O   
3638 C CB  . LEU B 197 ? 0.1686 0.1505 0.1515 0.0221  -0.0188 0.0039  254 LEU B CB  
3639 C CG  . LEU B 197 ? 0.1706 0.1604 0.1637 0.0214  -0.0203 -0.0006 254 LEU B CG  
3640 C CD1 . LEU B 197 ? 0.1809 0.1736 0.1773 0.0186  -0.0151 -0.0020 254 LEU B CD1 
3641 C CD2 . LEU B 197 ? 0.2002 0.1903 0.1894 0.0224  -0.0257 -0.0030 254 LEU B CD2 
3642 N N   . SER B 198 ? 0.1849 0.1484 0.1530 0.0234  -0.0183 0.0143  255 SER B N   
3643 C CA  . SER B 198 ? 0.1882 0.1409 0.1431 0.0222  -0.0157 0.0199  255 SER B CA  
3644 C C   . SER B 198 ? 0.2400 0.1831 0.1869 0.0257  -0.0238 0.0237  255 SER B C   
3645 O O   . SER B 198 ? 0.2776 0.2108 0.2065 0.0259  -0.0256 0.0277  255 SER B O   
3646 C CB  . SER B 198 ? 0.2181 0.1704 0.1807 0.0192  -0.0094 0.0214  255 SER B CB  
3647 O OG  . SER B 198 ? 0.2702 0.2115 0.2216 0.0172  -0.0060 0.0271  255 SER B OG  
3648 N N   . GLU B 199 ? 0.2289 0.1744 0.1887 0.0288  -0.0292 0.0223  256 GLU B N   
3649 C CA  . GLU B 199 ? 0.2597 0.1960 0.2153 0.0330  -0.0379 0.0258  256 GLU B CA  
3650 C C   . GLU B 199 ? 0.2799 0.2170 0.2300 0.0364  -0.0471 0.0243  256 GLU B C   
3651 O O   . GLU B 199 ? 0.3370 0.2636 0.2771 0.0397  -0.0555 0.0284  256 GLU B O   
3652 C CB  . GLU B 199 ? 0.2800 0.2191 0.2534 0.0357  -0.0401 0.0235  256 GLU B CB  
3653 C CG  . GLU B 199 ? 0.2748 0.2095 0.2507 0.0323  -0.0328 0.0256  256 GLU B CG  
3654 C CD  . GLU B 199 ? 0.2544 0.1897 0.2458 0.0351  -0.0348 0.0228  256 GLU B CD  
3655 O OE1 . GLU B 199 ? 0.2756 0.2162 0.2778 0.0397  -0.0409 0.0188  256 GLU B OE1 
3656 O OE2 . GLU B 199 ? 0.2584 0.1889 0.2519 0.0324  -0.0300 0.0240  256 GLU B OE2 
3657 N N   . SER B 200 ? 0.2545 0.2021 0.2092 0.0353  -0.0462 0.0190  257 SER B N   
3658 C CA  . SER B 200 ? 0.2316 0.1803 0.1811 0.0375  -0.0547 0.0167  257 SER B CA  
3659 C C   . SER B 200 ? 0.2940 0.2347 0.2204 0.0352  -0.0528 0.0188  257 SER B C   
3660 O O   . SER B 200 ? 0.3481 0.2888 0.2677 0.0364  -0.0596 0.0164  257 SER B O   
3661 C CB  . SER B 200 ? 0.2291 0.1925 0.1963 0.0369  -0.0545 0.0094  257 SER B CB  
3662 O OG  . SER B 200 ? 0.2651 0.2359 0.2526 0.0388  -0.0553 0.0068  257 SER B OG  
3663 N N   . GLY B 201 ? 0.3012 0.2355 0.2161 0.0316  -0.0434 0.0227  258 GLY B N   
3664 C CA  . GLY B 201 ? 0.2744 0.2010 0.1671 0.0292  -0.0395 0.0240  258 GLY B CA  
3665 C C   . GLY B 201 ? 0.2945 0.2298 0.1900 0.0269  -0.0337 0.0179  258 GLY B C   
3666 O O   . GLY B 201 ? 0.3133 0.2430 0.1910 0.0257  -0.0322 0.0170  258 GLY B O   
3667 N N   . LEU B 202 ? 0.2554 0.2030 0.1715 0.0262  -0.0306 0.0135  259 LEU B N   
3668 C CA  . LEU B 202 ? 0.2322 0.1870 0.1527 0.0243  -0.0254 0.0082  259 LEU B CA  
3669 C C   . LEU B 202 ? 0.2510 0.2081 0.1765 0.0214  -0.0144 0.0089  259 LEU B C   
3670 O O   . LEU B 202 ? 0.2961 0.2582 0.2360 0.0208  -0.0125 0.0097  259 LEU B O   
3671 C CB  . LEU B 202 ? 0.2092 0.1746 0.1481 0.0251  -0.0299 0.0033  259 LEU B CB  
3672 C CG  . LEU B 202 ? 0.2254 0.1904 0.1618 0.0275  -0.0406 0.0009  259 LEU B CG  
3673 C CD1 . LEU B 202 ? 0.2743 0.2499 0.2319 0.0280  -0.0444 -0.0026 259 LEU B CD1 
3674 C CD2 . LEU B 202 ? 0.2709 0.2329 0.1943 0.0265  -0.0412 -0.0030 259 LEU B CD2 
3675 N N   . ARG B 203 ? 0.2514 0.2056 0.1663 0.0195  -0.0073 0.0078  260 ARG B N   
3676 C CA  . ARG B 203 ? 0.2276 0.1850 0.1493 0.0169  0.0030  0.0079  260 ARG B CA  
3677 C C   . ARG B 203 ? 0.2365 0.2042 0.1761 0.0169  0.0042  0.0030  260 ARG B C   
3678 O O   . ARG B 203 ? 0.2312 0.2012 0.1715 0.0180  0.0011  -0.0013 260 ARG B O   
3679 C CB  . ARG B 203 ? 0.2343 0.1855 0.1394 0.0149  0.0111  0.0077  260 ARG B CB  
3680 C CG  . ARG B 203 ? 0.3187 0.2577 0.2046 0.0136  0.0117  0.0141  260 ARG B CG  
3681 C CD  . ARG B 203 ? 0.3880 0.3193 0.2526 0.0113  0.0198  0.0136  260 ARG B CD  
3682 N NE  . ARG B 203 ? 0.4456 0.3718 0.2936 0.0135  0.0129  0.0104  260 ARG B NE  
3683 C CZ  . ARG B 203 ? 0.4269 0.3559 0.2725 0.0138  0.0159  0.0034  260 ARG B CZ  
3684 N NH1 . ARG B 203 ? 0.4544 0.3912 0.3128 0.0125  0.0262  -0.0010 260 ARG B NH1 
3685 N NH2 . ARG B 203 ? 0.4686 0.3923 0.2992 0.0156  0.0079  0.0004  260 ARG B NH2 
3686 N N   . VAL B 204 ? 0.1945 0.1672 0.1481 0.0156  0.0078  0.0040  261 VAL B N   
3687 C CA  . VAL B 204 ? 0.1777 0.1583 0.1469 0.0155  0.0086  0.0006  261 VAL B CA  
3688 C C   . VAL B 204 ? 0.1913 0.1743 0.1655 0.0140  0.0170  -0.0007 261 VAL B C   
3689 O O   . VAL B 204 ? 0.2050 0.1873 0.1812 0.0119  0.0217  0.0022  261 VAL B O   
3690 C CB  . VAL B 204 ? 0.1741 0.1584 0.1552 0.0152  0.0050  0.0021  261 VAL B CB  
3691 C CG1 . VAL B 204 ? 0.1536 0.1438 0.1475 0.0146  0.0055  -0.0005 261 VAL B CG1 
3692 C CG2 . VAL B 204 ? 0.1843 0.1680 0.1639 0.0168  -0.0022 0.0021  261 VAL B CG2 
3693 N N   . PRO B 205 ? 0.1828 0.1691 0.1617 0.0149  0.0190  -0.0053 262 PRO B N   
3694 C CA  . PRO B 205 ? 0.1644 0.1511 0.1437 0.0168  0.0136  -0.0089 262 PRO B CA  
3695 C C   . PRO B 205 ? 0.2206 0.2022 0.1857 0.0177  0.0141  -0.0122 262 PRO B C   
3696 O O   . PRO B 205 ? 0.2163 0.1978 0.1826 0.0188  0.0101  -0.0159 262 PRO B O   
3697 C CB  . PRO B 205 ? 0.1747 0.1666 0.1693 0.0174  0.0151  -0.0118 262 PRO B CB  
3698 C CG  . PRO B 205 ? 0.2117 0.2055 0.2094 0.0166  0.0239  -0.0126 262 PRO B CG  
3699 C CD  . PRO B 205 ? 0.2029 0.1939 0.1930 0.0142  0.0262  -0.0075 262 PRO B CD  
3700 N N   . ALA B 206 ? 0.2066 0.1830 0.1572 0.0169  0.0188  -0.0109 263 ALA B N   
3701 C CA  . ALA B 206 ? 0.2219 0.1927 0.1568 0.0176  0.0199  -0.0149 263 ALA B CA  
3702 C C   . ALA B 206 ? 0.2547 0.2225 0.1828 0.0188  0.0097  -0.0161 263 ALA B C   
3703 O O   . ALA B 206 ? 0.2668 0.2324 0.1901 0.0197  0.0081  -0.0215 263 ALA B O   
3704 C CB  . ALA B 206 ? 0.2429 0.2066 0.1595 0.0158  0.0267  -0.0124 263 ALA B CB  
3705 N N   . GLN B 207 ? 0.2162 0.1839 0.1448 0.0189  0.0027  -0.0117 264 GLN B N   
3706 C CA  . GLN B 207 ? 0.2291 0.1957 0.1548 0.0200  -0.0072 -0.0131 264 GLN B CA  
3707 C C   . GLN B 207 ? 0.2171 0.1910 0.1610 0.0199  -0.0118 -0.0139 264 GLN B C   
3708 O O   . GLN B 207 ? 0.2194 0.1942 0.1655 0.0199  -0.0175 -0.0174 264 GLN B O   
3709 C CB  . GLN B 207 ? 0.2165 0.1771 0.1294 0.0208  -0.0128 -0.0085 264 GLN B CB  
3710 C CG  . GLN B 207 ? 0.2632 0.2138 0.1528 0.0202  -0.0086 -0.0074 264 GLN B CG  
3711 C CD  . GLN B 207 ? 0.3314 0.2735 0.2059 0.0211  -0.0152 -0.0018 264 GLN B CD  
3712 O OE1 . GLN B 207 ? 0.3112 0.2527 0.1904 0.0210  -0.0148 0.0037  264 GLN B OE1 
3713 N NE2 . GLN B 207 ? 0.3625 0.2970 0.2186 0.0220  -0.0221 -0.0033 264 GLN B NE2 
3714 N N   . VAL B 208 ? 0.2058 0.1844 0.1619 0.0192  -0.0092 -0.0109 265 VAL B N   
3715 C CA  . VAL B 208 ? 0.1722 0.1566 0.1430 0.0184  -0.0119 -0.0114 265 VAL B CA  
3716 C C   . VAL B 208 ? 0.1820 0.1693 0.1623 0.0176  -0.0066 -0.0103 265 VAL B C   
3717 O O   . VAL B 208 ? 0.1895 0.1768 0.1700 0.0174  -0.0029 -0.0073 265 VAL B O   
3718 C CB  . VAL B 208 ? 0.1563 0.1430 0.1315 0.0188  -0.0167 -0.0090 265 VAL B CB  
3719 C CG1 . VAL B 208 ? 0.1895 0.1819 0.1783 0.0172  -0.0175 -0.0100 265 VAL B CG1 
3720 C CG2 . VAL B 208 ? 0.1977 0.1819 0.1655 0.0202  -0.0239 -0.0102 265 VAL B CG2 
3721 N N   . SER B 209 ? 0.1646 0.1536 0.1528 0.0169  -0.0071 -0.0125 266 SER B N   
3722 C CA  . SER B 209 ? 0.1400 0.1313 0.1377 0.0163  -0.0048 -0.0114 266 SER B CA  
3723 C C   . SER B 209 ? 0.1698 0.1636 0.1732 0.0146  -0.0075 -0.0092 266 SER B C   
3724 O O   . SER B 209 ? 0.1635 0.1581 0.1670 0.0137  -0.0106 -0.0099 266 SER B O   
3725 C CB  . SER B 209 ? 0.1439 0.1336 0.1459 0.0168  -0.0049 -0.0145 266 SER B CB  
3726 O OG  . SER B 209 ? 0.1678 0.1559 0.1666 0.0186  -0.0008 -0.0175 266 SER B OG  
3727 N N   . VAL B 210 ? 0.1465 0.1417 0.1551 0.0141  -0.0060 -0.0072 267 VAL B N   
3728 C CA  . VAL B 210 ? 0.1286 0.1252 0.1404 0.0123  -0.0077 -0.0057 267 VAL B CA  
3729 C C   . VAL B 210 ? 0.1516 0.1475 0.1681 0.0115  -0.0084 -0.0050 267 VAL B C   
3730 O O   . VAL B 210 ? 0.1636 0.1604 0.1841 0.0125  -0.0070 -0.0049 267 VAL B O   
3731 C CB  . VAL B 210 ? 0.1328 0.1303 0.1441 0.0125  -0.0067 -0.0039 267 VAL B CB  
3732 C CG1 . VAL B 210 ? 0.1640 0.1627 0.1782 0.0108  -0.0077 -0.0036 267 VAL B CG1 
3733 C CG2 . VAL B 210 ? 0.1541 0.1509 0.1603 0.0140  -0.0076 -0.0038 267 VAL B CG2 
3734 N N   . VAL B 211 ? 0.1402 0.1345 0.1562 0.0094  -0.0106 -0.0046 268 VAL B N   
3735 C CA  . VAL B 211 ? 0.1240 0.1157 0.1413 0.0083  -0.0129 -0.0032 268 VAL B CA  
3736 C C   . VAL B 211 ? 0.1457 0.1371 0.1595 0.0057  -0.0130 -0.0023 268 VAL B C   
3737 O O   . VAL B 211 ? 0.1610 0.1528 0.1720 0.0038  -0.0117 -0.0029 268 VAL B O   
3738 C CB  . VAL B 211 ? 0.1462 0.1329 0.1626 0.0078  -0.0155 -0.0032 268 VAL B CB  
3739 C CG1 . VAL B 211 ? 0.1698 0.1521 0.1862 0.0073  -0.0196 -0.0010 268 VAL B CG1 
3740 C CG2 . VAL B 211 ? 0.1844 0.1711 0.2042 0.0107  -0.0148 -0.0055 268 VAL B CG2 
3741 N N   . GLY B 212 ? 0.1411 0.1321 0.1558 0.0054  -0.0145 -0.0015 269 GLY B N   
3742 C CA  . GLY B 212 ? 0.1691 0.1586 0.1788 0.0028  -0.0147 -0.0014 269 GLY B CA  
3743 C C   . GLY B 212 ? 0.1387 0.1219 0.1416 0.0005  -0.0183 0.0003  269 GLY B C   
3744 O O   . GLY B 212 ? 0.1738 0.1532 0.1760 0.0007  -0.0209 0.0017  269 GLY B O   
3745 N N   . TYR B 213 ? 0.1592 0.1398 0.1555 -0.0019 -0.0189 0.0000  270 TYR B N   
3746 C CA  . TYR B 213 ? 0.1709 0.1435 0.1565 -0.0047 -0.0227 0.0020  270 TYR B CA  
3747 C C   . TYR B 213 ? 0.1948 0.1655 0.1755 -0.0060 -0.0252 0.0009  270 TYR B C   
3748 O O   . TYR B 213 ? 0.1913 0.1642 0.1701 -0.0071 -0.0207 -0.0018 270 TYR B O   
3749 C CB  . TYR B 213 ? 0.1770 0.1461 0.1533 -0.0087 -0.0185 0.0025  270 TYR B CB  
3750 C CG  . TYR B 213 ? 0.1883 0.1469 0.1527 -0.0117 -0.0219 0.0061  270 TYR B CG  
3751 C CD1 . TYR B 213 ? 0.2243 0.1747 0.1751 -0.0142 -0.0258 0.0077  270 TYR B CD1 
3752 C CD2 . TYR B 213 ? 0.2239 0.1795 0.1888 -0.0127 -0.0212 0.0079  270 TYR B CD2 
3753 C CE1 . TYR B 213 ? 0.2713 0.2097 0.2084 -0.0173 -0.0295 0.0121  270 TYR B CE1 
3754 C CE2 . TYR B 213 ? 0.2496 0.1935 0.2027 -0.0159 -0.0242 0.0120  270 TYR B CE2 
3755 C CZ  . TYR B 213 ? 0.2851 0.2202 0.2238 -0.0182 -0.0283 0.0145  270 TYR B CZ  
3756 O OH  . TYR B 213 ? 0.2966 0.2179 0.2211 -0.0216 -0.0319 0.0194  270 TYR B OH  
3757 N N   . ASP B 214 ? 0.1799 0.1465 0.1598 -0.0053 -0.0328 0.0024  271 ASP B N   
3758 C CA  . ASP B 214 ? 0.1932 0.1557 0.1663 -0.0069 -0.0381 0.0015  271 ASP B CA  
3759 C C   . ASP B 214 ? 0.1851 0.1515 0.1720 -0.0040 -0.0448 0.0012  271 ASP B C   
3760 O O   . ASP B 214 ? 0.2130 0.1744 0.1964 -0.0043 -0.0535 0.0019  271 ASP B O   
3761 C CB  . ASP B 214 ? 0.1787 0.1433 0.1488 -0.0087 -0.0330 -0.0023 271 ASP B CB  
3762 C CG  . ASP B 214 ? 0.2322 0.1921 0.1870 -0.0125 -0.0272 -0.0033 271 ASP B CG  
3763 O OD1 . ASP B 214 ? 0.2548 0.2073 0.1971 -0.0151 -0.0283 -0.0004 271 ASP B OD1 
3764 O OD2 . ASP B 214 ? 0.2069 0.1700 0.1627 -0.0130 -0.0212 -0.0071 271 ASP B OD2 
3765 N N   . ASP B 215 ? 0.1868 0.1619 0.1893 -0.0014 -0.0407 -0.0002 272 ASP B N   
3766 C CA  . ASP B 215 ? 0.1699 0.1508 0.1876 0.0002  -0.0436 -0.0018 272 ASP B CA  
3767 C C   . ASP B 215 ? 0.1700 0.1492 0.1845 -0.0024 -0.0468 -0.0043 272 ASP B C   
3768 O O   . ASP B 215 ? 0.2191 0.1977 0.2383 -0.0026 -0.0549 -0.0051 272 ASP B O   
3769 C CB  . ASP B 215 ? 0.1856 0.1672 0.2131 0.0028  -0.0510 -0.0007 272 ASP B CB  
3770 C CG  . ASP B 215 ? 0.2163 0.2072 0.2646 0.0046  -0.0505 -0.0030 272 ASP B CG  
3771 O OD1 . ASP B 215 ? 0.2091 0.2053 0.2630 0.0041  -0.0424 -0.0042 272 ASP B OD1 
3772 O OD2 . ASP B 215 ? 0.2561 0.2488 0.3157 0.0064  -0.0580 -0.0036 272 ASP B OD2 
3773 N N   . THR B 216 ? 0.1706 0.1490 0.1784 -0.0041 -0.0406 -0.0060 273 THR B N   
3774 C CA  . THR B 216 ? 0.1678 0.1447 0.1748 -0.0063 -0.0424 -0.0093 273 THR B CA  
3775 C C   . THR B 216 ? 0.1443 0.1280 0.1700 -0.0055 -0.0420 -0.0103 273 THR B C   
3776 O O   . THR B 216 ? 0.1656 0.1551 0.2024 -0.0035 -0.0380 -0.0087 273 THR B O   
3777 C CB  . THR B 216 ? 0.1714 0.1454 0.1682 -0.0077 -0.0357 -0.0117 273 THR B CB  
3778 O OG1 . THR B 216 ? 0.1806 0.1585 0.1806 -0.0059 -0.0281 -0.0105 273 THR B OG1 
3779 C CG2 . THR B 216 ? 0.2121 0.1781 0.1893 -0.0103 -0.0372 -0.0121 273 THR B CG2 
3780 N N   . GLU B 217 ? 0.1615 0.1438 0.1901 -0.0077 -0.0463 -0.0133 274 GLU B N   
3781 C CA  . GLU B 217 ? 0.1545 0.1430 0.2023 -0.0082 -0.0480 -0.0144 274 GLU B CA  
3782 C C   . GLU B 217 ? 0.1537 0.1473 0.2123 -0.0075 -0.0386 -0.0131 274 GLU B C   
3783 O O   . GLU B 217 ? 0.1687 0.1689 0.2427 -0.0070 -0.0372 -0.0124 274 GLU B O   
3784 C CB  . GLU B 217 ? 0.2098 0.1949 0.2580 -0.0114 -0.0536 -0.0184 274 GLU B CB  
3785 C CG  . GLU B 217 ? 0.2025 0.1940 0.2712 -0.0127 -0.0593 -0.0201 274 GLU B CG  
3786 C CD  . GLU B 217 ? 0.3716 0.3637 0.4424 -0.0114 -0.0709 -0.0201 274 GLU B CD  
3787 O OE1 . GLU B 217 ? 0.3473 0.3311 0.4004 -0.0121 -0.0784 -0.0206 274 GLU B OE1 
3788 O OE2 . GLU B 217 ? 0.3837 0.3842 0.4735 -0.0096 -0.0725 -0.0195 274 GLU B OE2 
3789 N N   . ASP B 218 ? 0.1653 0.1554 0.2161 -0.0076 -0.0324 -0.0130 275 ASP B N   
3790 C CA  . ASP B 218 ? 0.1723 0.1644 0.2300 -0.0072 -0.0248 -0.0112 275 ASP B CA  
3791 C C   . ASP B 218 ? 0.1883 0.1849 0.2480 -0.0046 -0.0204 -0.0081 275 ASP B C   
3792 O O   . ASP B 218 ? 0.1429 0.1414 0.2086 -0.0047 -0.0147 -0.0063 275 ASP B O   
3793 C CB  . ASP B 218 ? 0.1565 0.1431 0.2053 -0.0067 -0.0205 -0.0115 275 ASP B CB  
3794 C CG  . ASP B 218 ? 0.2011 0.1819 0.2484 -0.0090 -0.0227 -0.0153 275 ASP B CG  
3795 O OD1 . ASP B 218 ? 0.1802 0.1609 0.2353 -0.0119 -0.0265 -0.0174 275 ASP B OD1 
3796 O OD2 . ASP B 218 ? 0.2083 0.1846 0.2477 -0.0078 -0.0200 -0.0168 275 ASP B OD2 
3797 N N   . SER B 219 ? 0.1431 0.1400 0.1960 -0.0025 -0.0226 -0.0073 276 SER B N   
3798 C CA  . SER B 219 ? 0.1516 0.1508 0.2032 0.0000  -0.0181 -0.0051 276 SER B CA  
3799 C C   . SER B 219 ? 0.1647 0.1697 0.2289 0.0007  -0.0153 -0.0046 276 SER B C   
3800 O O   . SER B 219 ? 0.1534 0.1593 0.2161 0.0020  -0.0095 -0.0033 276 SER B O   
3801 C CB  . SER B 219 ? 0.1773 0.1745 0.2201 0.0013  -0.0213 -0.0046 276 SER B CB  
3802 O OG  . SER B 219 ? 0.1683 0.1608 0.1997 0.0000  -0.0220 -0.0056 276 SER B OG  
3803 N N   . ALA B 220 ? 0.1370 0.1459 0.2137 -0.0002 -0.0192 -0.0063 277 ALA B N   
3804 C CA  . ALA B 220 ? 0.1312 0.1470 0.2230 0.0001  -0.0148 -0.0068 277 ALA B CA  
3805 C C   . ALA B 220 ? 0.1570 0.1730 0.2515 -0.0025 -0.0065 -0.0058 277 ALA B C   
3806 O O   . ALA B 220 ? 0.1405 0.1615 0.2442 -0.0028 -0.0001 -0.0060 277 ALA B O   
3807 C CB  . ALA B 220 ? 0.1620 0.1832 0.2703 -0.0004 -0.0214 -0.0094 277 ALA B CB  
3808 N N   . CYS B 221 ? 0.1332 0.1433 0.2199 -0.0045 -0.0063 -0.0047 278 CYS B N   
3809 C CA  . CYS B 221 ? 0.1470 0.1544 0.2342 -0.0070 0.0008  -0.0027 278 CYS B CA  
3810 C C   . CYS B 221 ? 0.1222 0.1227 0.1937 -0.0053 0.0038  0.0002  278 CYS B C   
3811 O O   . CYS B 221 ? 0.1403 0.1355 0.2093 -0.0072 0.0079  0.0026  278 CYS B O   
3812 C CB  . CYS B 221 ? 0.1475 0.1528 0.2421 -0.0110 -0.0018 -0.0042 278 CYS B CB  
3813 S SG  . CYS B 221 ? 0.1661 0.1807 0.2840 -0.0141 -0.0041 -0.0076 278 CYS B SG  
3814 N N   . PHE B 222 ? 0.1931 0.1157 0.2195 -0.0161 -0.0147 0.0028  279 PHE B N   
3815 C CA  . PHE B 222 ? 0.1813 0.0958 0.1954 -0.0031 -0.0128 0.0045  279 PHE B CA  
3816 C C   . PHE B 222 ? 0.1915 0.1103 0.2070 -0.0086 -0.0067 0.0108  279 PHE B C   
3817 O O   . PHE B 222 ? 0.1996 0.1348 0.2293 -0.0205 -0.0025 0.0134  279 PHE B O   
3818 C CB  . PHE B 222 ? 0.1505 0.0884 0.1752 0.0095  -0.0122 0.0010  279 PHE B CB  
3819 C CG  . PHE B 222 ? 0.1611 0.0972 0.1808 0.0181  -0.0166 -0.0044 279 PHE B CG  
3820 C CD1 . PHE B 222 ? 0.1805 0.0926 0.1852 0.0172  -0.0221 -0.0074 279 PHE B CD1 
3821 C CD2 . PHE B 222 ? 0.1617 0.1208 0.1900 0.0267  -0.0148 -0.0065 279 PHE B CD2 
3822 C CE1 . PHE B 222 ? 0.2305 0.1427 0.2282 0.0282  -0.0256 -0.0129 279 PHE B CE1 
3823 C CE2 . PHE B 222 ? 0.1870 0.1493 0.2101 0.0353  -0.0170 -0.0107 279 PHE B CE2 
3824 C CZ  . PHE B 222 ? 0.1674 0.1068 0.1750 0.0375  -0.0223 -0.0141 279 PHE B CZ  
3825 N N   . ILE B 223 ? 0.1961 0.1017 0.1953 0.0018  -0.0062 0.0131  280 ILE B N   
3826 C CA  . ILE B 223 ? 0.1930 0.1032 0.1905 -0.0001 -0.0005 0.0186  280 ILE B CA  
3827 C C   . ILE B 223 ? 0.1679 0.1003 0.1737 0.0131  -0.0004 0.0154  280 ILE B C   
3828 O O   . ILE B 223 ? 0.2132 0.1403 0.2078 0.0270  -0.0043 0.0130  280 ILE B O   
3829 C CB  . ILE B 223 ? 0.2641 0.1382 0.2316 0.0004  -0.0007 0.0246  280 ILE B CB  
3830 C CG1 . ILE B 223 ? 0.2719 0.1203 0.2286 -0.0184 -0.0005 0.0290  280 ILE B CG1 
3831 C CG2 . ILE B 223 ? 0.2470 0.1282 0.2108 0.0016  0.0053  0.0302  280 ILE B CG2 
3832 C CD1 . ILE B 223 ? 0.3098 0.1088 0.2274 -0.0160 -0.0029 0.0347  280 ILE B CD1 
3833 N N   . PRO B 224 ? 0.1688 0.1263 0.1927 0.0098  0.0032  0.0145  281 PRO B N   
3834 C CA  . PRO B 224 ? 0.1716 0.1434 0.2109 -0.0016 0.0070  0.0155  281 PRO B CA  
3835 C C   . PRO B 224 ? 0.1537 0.1337 0.2058 -0.0039 0.0034  0.0110  281 PRO B C   
3836 O O   . PRO B 224 ? 0.1636 0.1417 0.2141 0.0032  -0.0005 0.0073  281 PRO B O   
3837 C CB  . PRO B 224 ? 0.1997 0.1903 0.2463 0.0030  0.0103  0.0145  281 PRO B CB  
3838 C CG  . PRO B 224 ? 0.1949 0.1819 0.2320 0.0140  0.0071  0.0124  281 PRO B CG  
3839 C CD  . PRO B 224 ? 0.1673 0.1413 0.1961 0.0189  0.0023  0.0111  281 PRO B CD  
3840 N N   . PRO B 225 ? 0.1554 0.1477 0.2198 -0.0129 0.0049  0.0111  282 PRO B N   
3841 C CA  . PRO B 225 ? 0.1454 0.1460 0.2200 -0.0131 0.0006  0.0067  282 PRO B CA  
3842 C C   . PRO B 225 ? 0.1619 0.1701 0.2400 -0.0035 -0.0006 0.0035  282 PRO B C   
3843 O O   . PRO B 225 ? 0.1345 0.1506 0.2148 0.0003  0.0019  0.0036  282 PRO B O   
3844 C CB  . PRO B 225 ? 0.1351 0.1560 0.2238 -0.0213 0.0027  0.0072  282 PRO B CB  
3845 C CG  . PRO B 225 ? 0.1341 0.1486 0.2167 -0.0324 0.0072  0.0127  282 PRO B CG  
3846 C CD  . PRO B 225 ? 0.1495 0.1487 0.2171 -0.0243 0.0099  0.0157  282 PRO B CD  
3847 N N   . LEU B 226 ? 0.1165 0.1209 0.1929 -0.0006 -0.0045 0.0007  283 LEU B N   
3848 C CA  . LEU B 226 ? 0.1123 0.1207 0.1878 0.0055  -0.0048 -0.0008 283 LEU B CA  
3849 C C   . LEU B 226 ? 0.1391 0.1549 0.2201 0.0057  -0.0051 -0.0017 283 LEU B C   
3850 O O   . LEU B 226 ? 0.1448 0.1622 0.2282 0.0053  -0.0075 -0.0027 283 LEU B O   
3851 C CB  . LEU B 226 ? 0.1444 0.1473 0.2128 0.0096  -0.0074 -0.0028 283 LEU B CB  
3852 C CG  . LEU B 226 ? 0.1275 0.1407 0.1961 0.0133  -0.0063 -0.0037 283 LEU B CG  
3853 C CD1 . LEU B 226 ? 0.1649 0.1852 0.2334 0.0157  -0.0049 -0.0035 283 LEU B CD1 
3854 C CD2 . LEU B 226 ? 0.1445 0.1574 0.2063 0.0190  -0.0078 -0.0058 283 LEU B CD2 
3855 N N   . THR B 227 ? 0.1285 0.1460 0.2085 0.0070  -0.0037 -0.0016 284 THR B N   
3856 C CA  . THR B 227 ? 0.1266 0.1415 0.2041 0.0079  -0.0048 -0.0021 284 THR B CA  
3857 C C   . THR B 227 ? 0.1279 0.1408 0.2009 0.0059  -0.0053 -0.0015 284 THR B C   
3858 O O   . THR B 227 ? 0.1207 0.1392 0.1937 0.0043  -0.0041 -0.0016 284 THR B O   
3859 C CB  . THR B 227 ? 0.1415 0.1525 0.2147 0.0085  -0.0041 -0.0028 284 THR B CB  
3860 O OG1 . THR B 227 ? 0.1542 0.1702 0.2304 0.0123  -0.0025 -0.0032 284 THR B OG1 
3861 C CG2 . THR B 227 ? 0.1351 0.1330 0.1983 0.0088  -0.0063 -0.0031 284 THR B CG2 
3862 N N   . THR B 228 ? 0.1390 0.1470 0.2075 0.0071  -0.0070 -0.0009 285 THR B N   
3863 C CA  . THR B 228 ? 0.1236 0.1323 0.1868 0.0057  -0.0064 0.0003  285 THR B CA  
3864 C C   . THR B 228 ? 0.1370 0.1348 0.1895 0.0069  -0.0079 0.0023  285 THR B C   
3865 O O   . THR B 228 ? 0.1850 0.1764 0.2354 0.0118  -0.0110 0.0017  285 THR B O   
3866 C CB  . THR B 228 ? 0.1803 0.1934 0.2458 0.0092  -0.0077 -0.0018 285 THR B CB  
3867 O OG1 . THR B 228 ? 0.1624 0.1786 0.2210 0.0106  -0.0065 -0.0014 285 THR B OG1 
3868 C CG2 . THR B 228 ? 0.1492 0.1601 0.2175 0.0111  -0.0120 -0.0036 285 THR B CG2 
3869 N N   . ILE B 229 ? 0.1487 0.1459 0.1930 0.0032  -0.0054 0.0051  286 ILE B N   
3870 C CA  . ILE B 229 ? 0.1716 0.1553 0.2006 0.0047  -0.0064 0.0084  286 ILE B CA  
3871 C C   . ILE B 229 ? 0.1677 0.1557 0.1959 0.0128  -0.0098 0.0061  286 ILE B C   
3872 O O   . ILE B 229 ? 0.2028 0.2006 0.2317 0.0134  -0.0079 0.0049  286 ILE B O   
3873 C CB  . ILE B 229 ? 0.1778 0.1605 0.1965 -0.0050 -0.0010 0.0135  286 ILE B CB  
3874 C CG1 . ILE B 229 ? 0.1743 0.1536 0.1937 -0.0167 0.0011  0.0149  286 ILE B CG1 
3875 C CG2 . ILE B 229 ? 0.2301 0.1940 0.2276 -0.0032 -0.0016 0.0184  286 ILE B CG2 
3876 C CD1 . ILE B 229 ? 0.2278 0.1812 0.2370 -0.0149 -0.0034 0.0145  286 ILE B CD1 
3877 N N   . LYS B 230 ? 0.1851 0.1665 0.2098 0.0202  -0.0154 0.0046  287 LYS B N   
3878 C CA  . LYS B 230 ? 0.1972 0.1843 0.2218 0.0265  -0.0206 0.0010  287 LYS B CA  
3879 C C   . LYS B 230 ? 0.2258 0.2033 0.2305 0.0301  -0.0204 0.0044  287 LYS B C   
3880 O O   . LYS B 230 ? 0.2467 0.2082 0.2356 0.0323  -0.0207 0.0089  287 LYS B O   
3881 C CB  . LYS B 230 ? 0.2228 0.2155 0.2548 0.0329  -0.0275 -0.0029 287 LYS B CB  
3882 C CG  . LYS B 230 ? 0.2177 0.2167 0.2478 0.0382  -0.0348 -0.0072 287 LYS B CG  
3883 C CD  . LYS B 230 ? 0.2619 0.2777 0.3063 0.0411  -0.0414 -0.0122 287 LYS B CD  
3884 C CE  . LYS B 230 ? 0.2595 0.2848 0.3067 0.0405  -0.0494 -0.0183 287 LYS B CE  
3885 N NZ  . LYS B 230 ? 0.3233 0.3456 0.3755 0.0301  -0.0476 -0.0205 287 LYS B NZ  
3886 N N   . GLN B 231 ? 0.2214 0.2054 0.2230 0.0315  -0.0199 0.0025  288 GLN B N   
3887 C CA  . GLN B 231 ? 0.2186 0.1964 0.2005 0.0375  -0.0209 0.0042  288 GLN B CA  
3888 C C   . GLN B 231 ? 0.1944 0.1758 0.1786 0.0453  -0.0310 -0.0033 288 GLN B C   
3889 O O   . GLN B 231 ? 0.2590 0.2471 0.2517 0.0443  -0.0335 -0.0093 288 GLN B O   
3890 C CB  . GLN B 231 ? 0.2570 0.2430 0.2327 0.0356  -0.0133 0.0059  288 GLN B CB  
3891 C CG  . GLN B 231 ? 0.3136 0.3041 0.2910 0.0245  -0.0035 0.0127  288 GLN B CG  
3892 C CD  . GLN B 231 ? 0.3616 0.3671 0.3313 0.0234  0.0049  0.0154  288 GLN B CD  
3893 O OE1 . GLN B 231 ? 0.4247 0.4270 0.3797 0.0167  0.0114  0.0233  288 GLN B OE1 
3894 N NE2 . GLN B 231 ? 0.2988 0.3205 0.2758 0.0303  0.0050  0.0092  288 GLN B NE2 
3895 N N   . ASP B 232 ? 0.2307 0.2067 0.2063 0.0529  -0.0380 -0.0036 289 ASP B N   
3896 C CA  . ASP B 232 ? 0.2457 0.2308 0.2261 0.0589  -0.0493 -0.0117 289 ASP B CA  
3897 C C   . ASP B 232 ? 0.2840 0.2655 0.2476 0.0641  -0.0524 -0.0149 289 ASP B C   
3898 O O   . ASP B 232 ? 0.2775 0.2506 0.2197 0.0731  -0.0545 -0.0124 289 ASP B O   
3899 C CB  . ASP B 232 ? 0.2423 0.2273 0.2181 0.0687  -0.0563 -0.0114 289 ASP B CB  
3900 C CG  . ASP B 232 ? 0.3504 0.3544 0.3370 0.0733  -0.0688 -0.0206 289 ASP B CG  
3901 O OD1 . ASP B 232 ? 0.3179 0.3265 0.3065 0.0693  -0.0734 -0.0268 289 ASP B OD1 
3902 O OD2 . ASP B 232 ? 0.3709 0.3860 0.3633 0.0811  -0.0746 -0.0224 289 ASP B OD2 
3903 N N   . PHE B 233 ? 0.2412 0.2260 0.2110 0.0601  -0.0533 -0.0209 290 PHE B N   
3904 C CA  . PHE B 233 ? 0.2348 0.2138 0.1854 0.0670  -0.0558 -0.0250 290 PHE B CA  
3905 C C   . PHE B 233 ? 0.2894 0.2688 0.2320 0.0737  -0.0695 -0.0323 290 PHE B C   
3906 O O   . PHE B 233 ? 0.2892 0.2619 0.2089 0.0833  -0.0723 -0.0342 290 PHE B O   
3907 C CB  . PHE B 233 ? 0.2432 0.2198 0.1979 0.0636  -0.0545 -0.0303 290 PHE B CB  
3908 C CG  . PHE B 233 ? 0.2310 0.2119 0.1934 0.0593  -0.0423 -0.0241 290 PHE B CG  
3909 C CD1 . PHE B 233 ? 0.2635 0.2492 0.2154 0.0621  -0.0319 -0.0168 290 PHE B CD1 
3910 C CD2 . PHE B 233 ? 0.2845 0.2664 0.2642 0.0515  -0.0414 -0.0253 290 PHE B CD2 
3911 C CE1 . PHE B 233 ? 0.2213 0.2170 0.1827 0.0568  -0.0217 -0.0122 290 PHE B CE1 
3912 C CE2 . PHE B 233 ? 0.2560 0.2443 0.2426 0.0489  -0.0317 -0.0205 290 PHE B CE2 
3913 C CZ  . PHE B 233 ? 0.2687 0.2658 0.2476 0.0514  -0.0224 -0.0146 290 PHE B CZ  
3914 N N   . ARG B 234 ? 0.2421 0.2329 0.2035 0.0688  -0.0782 -0.0371 291 ARG B N   
3915 C CA  . ARG B 234 ? 0.3222 0.3209 0.2794 0.0749  -0.0923 -0.0444 291 ARG B CA  
3916 C C   . ARG B 234 ? 0.3250 0.3183 0.2604 0.0898  -0.0927 -0.0388 291 ARG B C   
3917 O O   . ARG B 234 ? 0.3507 0.3390 0.2647 0.1000  -0.1003 -0.0426 291 ARG B O   
3918 C CB  . ARG B 234 ? 0.3657 0.3866 0.3508 0.0664  -0.0992 -0.0489 291 ARG B CB  
3919 C CG  . ARG B 234 ? 0.5830 0.6155 0.5732 0.0613  -0.1143 -0.0606 291 ARG B CG  
3920 C CD  . ARG B 234 ? 0.7249 0.7384 0.7093 0.0505  -0.1146 -0.0656 291 ARG B CD  
3921 N NE  . ARG B 234 ? 0.6959 0.7080 0.6721 0.0474  -0.1302 -0.0775 291 ARG B NE  
3922 C CZ  . ARG B 234 ? 0.6530 0.6427 0.6176 0.0395  -0.1345 -0.0843 291 ARG B CZ  
3923 N NH1 . ARG B 234 ? 0.4313 0.3990 0.3883 0.0384  -0.1242 -0.0802 291 ARG B NH1 
3924 N NH2 . ARG B 234 ? 0.8163 0.8045 0.7749 0.0334  -0.1495 -0.0954 291 ARG B NH2 
3925 N N   . LEU B 235 ? 0.3374 0.3271 0.2736 0.0916  -0.0849 -0.0295 292 LEU B N   
3926 C CA  . LEU B 235 ? 0.3348 0.3106 0.2444 0.1052  -0.0850 -0.0227 292 LEU B CA  
3927 C C   . LEU B 235 ? 0.3314 0.2892 0.2125 0.1076  -0.0765 -0.0164 292 LEU B C   
3928 O O   . LEU B 235 ? 0.3627 0.3098 0.2158 0.1199  -0.0805 -0.0143 292 LEU B O   
3929 C CB  . LEU B 235 ? 0.3913 0.3601 0.3041 0.1055  -0.0791 -0.0148 292 LEU B CB  
3930 C CG  . LEU B 235 ? 0.4113 0.3529 0.2906 0.1161  -0.0762 -0.0046 292 LEU B CG  
3931 C CD1 . LEU B 235 ? 0.5103 0.4520 0.3710 0.1351  -0.0897 -0.0084 292 LEU B CD1 
3932 C CD2 . LEU B 235 ? 0.4759 0.4067 0.3597 0.1136  -0.0710 0.0012  292 LEU B CD2 
3933 N N   . LEU B 236 ? 0.3248 0.2819 0.2118 0.0971  -0.0647 -0.0133 293 LEU B N   
3934 C CA  . LEU B 236 ? 0.2973 0.2464 0.1599 0.0998  -0.0558 -0.0081 293 LEU B CA  
3935 C C   . LEU B 236 ? 0.3461 0.2959 0.1920 0.1109  -0.0653 -0.0170 293 LEU B C   
3936 O O   . LEU B 236 ? 0.3657 0.3064 0.1816 0.1207  -0.0637 -0.0130 293 LEU B O   
3937 C CB  . LEU B 236 ? 0.2959 0.2528 0.1717 0.0889  -0.0432 -0.0057 293 LEU B CB  
3938 C CG  . LEU B 236 ? 0.3557 0.3147 0.2107 0.0918  -0.0322 -0.0009 293 LEU B CG  
3939 C CD1 . LEU B 236 ? 0.4173 0.3640 0.2482 0.0904  -0.0238 0.0123  293 LEU B CD1 
3940 C CD2 . LEU B 236 ? 0.3248 0.2990 0.1971 0.0836  -0.0219 -0.0007 293 LEU B CD2 
3941 N N   . GLY B 237 ? 0.3215 0.2795 0.1837 0.1086  -0.0754 -0.0293 294 GLY B N   
3942 C CA  . GLY B 237 ? 0.3566 0.3117 0.2013 0.1180  -0.0867 -0.0397 294 GLY B CA  
3943 C C   . GLY B 237 ? 0.3956 0.3500 0.2247 0.1296  -0.0992 -0.0417 294 GLY B C   
3944 O O   . GLY B 237 ? 0.4371 0.3838 0.2368 0.1421  -0.1032 -0.0439 294 GLY B O   
3945 N N   . GLN B 238 ? 0.3620 0.3259 0.2085 0.1280  -0.1056 -0.0414 295 GLN B N   
3946 C CA  . GLN B 238 ? 0.4294 0.3947 0.2642 0.1400  -0.1145 -0.0431 295 GLN B CA  
3947 C C   . GLN B 238 ? 0.4970 0.4415 0.2982 0.1506  -0.1049 -0.0310 295 GLN B C   
3948 O O   . GLN B 238 ? 0.4942 0.4323 0.2745 0.1610  -0.1082 -0.0331 295 GLN B O   
3949 C CB  . GLN B 238 ? 0.4746 0.4572 0.3356 0.1376  -0.1196 -0.0447 295 GLN B CB  
3950 C CG  . GLN B 238 ? 0.7118 0.7171 0.6082 0.1233  -0.1258 -0.0535 295 GLN B CG  
3951 C CD  . GLN B 238 ? 0.9020 0.9297 0.8222 0.1231  -0.1284 -0.0544 295 GLN B CD  
3952 O OE1 . GLN B 238 ? 0.7933 0.8228 0.7257 0.1204  -0.1215 -0.0482 295 GLN B OE1 
3953 N NE2 . GLN B 238 ? 0.8200 0.8660 0.7455 0.1270  -0.1379 -0.0624 295 GLN B NE2 
3954 N N   . THR B 239 ? 0.4842 0.4165 0.2788 0.1466  -0.0930 -0.0179 296 THR B N   
3955 C CA  . THR B 239 ? 0.4438 0.3527 0.2062 0.1518  -0.0831 -0.0046 296 THR B CA  
3956 C C   . THR B 239 ? 0.4885 0.3909 0.2239 0.1546  -0.0749 -0.0012 296 THR B C   
3957 O O   . THR B 239 ? 0.5572 0.4456 0.2658 0.1627  -0.0727 0.0035  296 THR B O   
3958 C CB  . THR B 239 ? 0.5444 0.4408 0.3091 0.1416  -0.0718 0.0081  296 THR B CB  
3959 O OG1 . THR B 239 ? 0.4964 0.3990 0.2839 0.1423  -0.0794 0.0043  296 THR B OG1 
3960 C CG2 . THR B 239 ? 0.5091 0.3757 0.2372 0.1426  -0.0616 0.0229  296 THR B CG2 
3961 N N   . SER B 240 ? 0.4470 0.3606 0.1894 0.1486  -0.0695 -0.0040 297 SER B N   
3962 C CA  . SER B 240 ? 0.4406 0.3535 0.1586 0.1529  -0.0598 -0.0016 297 SER B CA  
3963 C C   . SER B 240 ? 0.4820 0.3949 0.1901 0.1653  -0.0706 -0.0131 297 SER B C   
3964 O O   . SER B 240 ? 0.5441 0.4492 0.2259 0.1729  -0.0647 -0.0082 297 SER B O   
3965 C CB  . SER B 240 ? 0.4892 0.4181 0.2255 0.1442  -0.0502 -0.0050 297 SER B CB  
3966 O OG  . SER B 240 ? 0.5490 0.4859 0.3122 0.1418  -0.0622 -0.0191 297 SER B OG  
3967 N N   . VAL B 241 ? 0.4637 0.3850 0.1923 0.1660  -0.0862 -0.0279 298 VAL B N   
3968 C CA  . VAL B 241 ? 0.4717 0.3922 0.1910 0.1762  -0.0973 -0.0392 298 VAL B CA  
3969 C C   . VAL B 241 ? 0.5675 0.4800 0.2710 0.1859  -0.1010 -0.0348 298 VAL B C   
3970 O O   . VAL B 241 ? 0.5906 0.4962 0.2707 0.1972  -0.1023 -0.0362 298 VAL B O   
3971 C CB  . VAL B 241 ? 0.4864 0.4174 0.2319 0.1700  -0.1130 -0.0550 298 VAL B CB  
3972 C CG1 . VAL B 241 ? 0.4823 0.4128 0.2190 0.1786  -0.1261 -0.0660 298 VAL B CG1 
3973 C CG2 . VAL B 241 ? 0.4687 0.3993 0.2207 0.1635  -0.1096 -0.0600 298 VAL B CG2 
3974 N N   . ASN B 242 ? 0.5421 0.4539 0.2559 0.1834  -0.1023 -0.0295 299 ASN B N   
3975 C CA  . ASN B 242 ? 0.5375 0.4380 0.2328 0.1949  -0.1052 -0.0255 299 ASN B CA  
3976 C C   . ASN B 242 ? 0.5817 0.4592 0.2413 0.1983  -0.0910 -0.0103 299 ASN B C   
3977 O O   . ASN B 242 ? 0.6815 0.5474 0.3159 0.2104  -0.0932 -0.0090 299 ASN B O   
3978 C CB  . ASN B 242 ? 0.5702 0.4743 0.2836 0.1931  -0.1093 -0.0242 299 ASN B CB  
3979 C CG  . ASN B 242 ? 0.6024 0.5345 0.3503 0.1902  -0.1237 -0.0390 299 ASN B CG  
3980 O OD1 . ASN B 242 ? 0.5789 0.5232 0.3330 0.1905  -0.1331 -0.0506 299 ASN B OD1 
3981 N ND2 . ASN B 242 ? 0.6121 0.5544 0.3820 0.1865  -0.1250 -0.0385 299 ASN B ND2 
3982 N N   . ARG B 243 ? 0.6051 0.4770 0.2616 0.1865  -0.0761 0.0017  300 ARG B N   
3983 C CA  . ARG B 243 ? 0.6263 0.4796 0.2504 0.1849  -0.0611 0.0173  300 ARG B CA  
3984 C C   . ARG B 243 ? 0.8043 0.6638 0.4102 0.1922  -0.0573 0.0147  300 ARG B C   
3985 O O   . ARG B 243 ? 0.7643 0.6093 0.3400 0.1968  -0.0505 0.0239  300 ARG B O   
3986 C CB  . ARG B 243 ? 0.7395 0.5907 0.3679 0.1673  -0.0456 0.0304  300 ARG B CB  
3987 C CG  . ARG B 243 ? 0.8589 0.6991 0.4589 0.1587  -0.0275 0.0467  300 ARG B CG  
3988 C CD  . ARG B 243 ? 1.0433 0.8508 0.6145 0.1603  -0.0267 0.0579  300 ARG B CD  
3989 N NE  . ARG B 243 ? 0.9770 0.7740 0.5242 0.1453  -0.0086 0.0752  300 ARG B NE  
3990 C CZ  . ARG B 243 ? 1.2693 1.0375 0.7844 0.1450  -0.0052 0.0864  300 ARG B CZ  
3991 N NH1 . ARG B 243 ? 1.1407 0.8861 0.6414 0.1620  -0.0183 0.0819  300 ARG B NH1 
3992 N NH2 . ARG B 243 ? 1.1844 0.9484 0.6814 0.1267  0.0118  0.1024  300 ARG B NH2 
3993 N N   . LEU B 244 ? 0.6004 0.4790 0.2225 0.1939  -0.0619 0.0019  301 LEU B N   
3994 C CA  . LEU B 244 ? 0.6134 0.4966 0.2182 0.2036  -0.0598 -0.0027 301 LEU B CA  
3995 C C   . LEU B 244 ? 0.8067 0.6813 0.3963 0.2192  -0.0735 -0.0106 301 LEU B C   
3996 O O   . LEU B 244 ? 0.7045 0.5717 0.2658 0.2284  -0.0685 -0.0062 301 LEU B O   
3997 C CB  . LEU B 244 ? 0.5880 0.4878 0.2121 0.2025  -0.0625 -0.0153 301 LEU B CB  
3998 C CG  . LEU B 244 ? 0.7454 0.6526 0.3535 0.2104  -0.0539 -0.0170 301 LEU B CG  
3999 C CD1 . LEU B 244 ? 0.7560 0.6688 0.3489 0.2035  -0.0323 0.0004  301 LEU B CD1 
4000 C CD2 . LEU B 244 ? 0.7005 0.6187 0.3282 0.2095  -0.0574 -0.0294 301 LEU B CD2 
4001 N N   . VAL B 245 ? 0.6479 0.5259 0.2560 0.2219  -0.0903 -0.0221 302 VAL B N   
4002 C CA  . VAL B 245 ? 0.8680 0.7412 0.4629 0.2366  -0.1035 -0.0295 302 VAL B CA  
4003 C C   . VAL B 245 ? 0.8842 0.7368 0.4492 0.2437  -0.0968 -0.0157 302 VAL B C   
4004 O O   . VAL B 245 ? 0.8652 0.7083 0.4031 0.2572  -0.0992 -0.0158 302 VAL B O   
4005 C CB  . VAL B 245 ? 0.7931 0.6805 0.4174 0.2352  -0.1211 -0.0429 302 VAL B CB  
4006 C CG1 . VAL B 245 ? 0.7984 0.6851 0.4096 0.2507  -0.1345 -0.0505 302 VAL B CG1 
4007 C CG2 . VAL B 245 ? 0.6842 0.5866 0.3339 0.2259  -0.1282 -0.0560 302 VAL B CG2 
4008 N N   . GLN B 246 ? 0.8226 0.6646 0.3896 0.2347  -0.0889 -0.0036 303 GLN B N   
4009 C CA  . GLN B 246 ? 0.9142 0.7295 0.4497 0.2393  -0.0824 0.0103  303 GLN B CA  
4010 C C   . GLN B 246 ? 1.0663 0.8708 0.5706 0.2365  -0.0665 0.0235  303 GLN B C   
4011 O O   . GLN B 246 ? 1.0083 0.7923 0.4796 0.2455  -0.0647 0.0309  303 GLN B O   
4012 C CB  . GLN B 246 ? 0.8648 0.6676 0.4089 0.2284  -0.0776 0.0196  303 GLN B CB  
4013 C CG  . GLN B 246 ? 1.1830 0.9518 0.6945 0.2333  -0.0739 0.0321  303 GLN B CG  
4014 C CD  . GLN B 246 ? 1.3898 1.1419 0.9069 0.2196  -0.0671 0.0421  303 GLN B CD  
4015 O OE1 . GLN B 246 ? 1.2874 1.0557 0.8335 0.2067  -0.0645 0.0405  303 GLN B OE1 
4016 N NE2 . GLN B 246 ? 1.1749 0.8919 0.6621 0.2228  -0.0646 0.0522  303 GLN B NE2 
4017 N N   . LEU B 247 ? 0.7873 0.6075 0.3012 0.2246  -0.0546 0.0264  304 LEU B N   
4018 C CA  . LEU B 247 ? 0.8167 0.6360 0.3052 0.2203  -0.0379 0.0384  304 LEU B CA  
4019 C C   . LEU B 247 ? 0.9770 0.8020 0.4481 0.2374  -0.0428 0.0297  304 LEU B C   
4020 O O   . LEU B 247 ? 0.9672 0.7861 0.4086 0.2391  -0.0317 0.0400  304 LEU B O   
4021 C CB  . LEU B 247 ? 0.8570 0.6976 0.3641 0.2037  -0.0235 0.0426  304 LEU B CB  
4022 C CG  . LEU B 247 ? 0.9078 0.7389 0.4145 0.1824  -0.0093 0.0599  304 LEU B CG  
4023 C CD1 . LEU B 247 ? 0.8970 0.7556 0.4227 0.1675  0.0051  0.0624  304 LEU B CD1 
4024 C CD2 . LEU B 247 ? 1.0170 0.8241 0.4869 0.1771  0.0010  0.0772  304 LEU B CD2 
4025 N N   . LEU B 248 ? 0.9313 0.7674 0.4193 0.2490  -0.0594 0.0110  305 LEU B N   
4026 C CA  . LEU B 248 ? 0.8862 0.7237 0.3561 0.2662  -0.0667 0.0014  305 LEU B CA  
4027 C C   . LEU B 248 ? 0.9445 0.7618 0.3865 0.2801  -0.0742 0.0041  305 LEU B C   
4028 O O   . LEU B 248 ? 1.1020 0.9139 0.5156 0.2927  -0.0731 0.0046  305 LEU B O   
4029 C CB  . LEU B 248 ? 0.9009 0.7525 0.3961 0.2713  -0.0837 -0.0193 305 LEU B CB  
4030 C CG  . LEU B 248 ? 0.8343 0.7021 0.3476 0.2642  -0.0778 -0.0247 305 LEU B CG  
4031 C CD1 . LEU B 248 ? 0.8573 0.7318 0.3959 0.2647  -0.0964 -0.0440 305 LEU B CD1 
4032 C CD2 . LEU B 248 ? 0.8048 0.6770 0.2944 0.2728  -0.0663 -0.0219 305 LEU B CD2 
4033 N N   . GLN B 249 ? 1.1258 0.9319 0.5742 0.2799  -0.0819 0.0053  306 GLN B N   
4034 C CA  . GLN B 249 ? 1.1622 0.9494 0.5844 0.2961  -0.0906 0.0059  306 GLN B CA  
4035 C C   . GLN B 249 ? 1.0346 0.7940 0.4196 0.2930  -0.0755 0.0265  306 GLN B C   
4036 O O   . GLN B 249 ? 1.1449 0.8891 0.4954 0.3066  -0.0759 0.0300  306 GLN B O   
4037 C CB  . GLN B 249 ? 1.0691 0.8586 0.5130 0.2997  -0.1055 -0.0029 306 GLN B CB  
4038 C CG  . GLN B 249 ? 1.2211 1.0336 0.6868 0.3091  -0.1248 -0.0238 306 GLN B CG  
4039 C CD  . GLN B 249 ? 1.2166 1.0226 0.6628 0.3298  -0.1384 -0.0302 306 GLN B CD  
4040 O OE1 . GLN B 249 ? 1.1897 0.9703 0.6011 0.3397  -0.1331 -0.0190 306 GLN B OE1 
4041 N NE2 . GLN B 249 ? 1.2713 1.1002 0.7387 0.3357  -0.1564 -0.0482 306 GLN B NE2 
4042 N N   . ASN B 250 ? 1.0218 0.7729 0.4118 0.2742  -0.0625 0.0403  307 ASN B N   
4043 C CA  . ASN B 250 ? 1.2245 0.9473 0.5804 0.2654  -0.0478 0.0610  307 ASN B CA  
4044 C C   . ASN B 250 ? 1.2321 0.9680 0.5965 0.2412  -0.0284 0.0733  307 ASN B C   
4045 O O   . ASN B 250 ? 1.2150 0.9487 0.5974 0.2242  -0.0232 0.0792  307 ASN B O   
4046 C CB  . ASN B 250 ? 1.0963 0.7898 0.4458 0.2659  -0.0529 0.0661  307 ASN B CB  
4047 C CG  . ASN B 250 ? 1.0783 0.7503 0.3997 0.2899  -0.0657 0.0615  307 ASN B CG  
4048 O OD1 . ASN B 250 ? 1.0829 0.7412 0.3690 0.2985  -0.0620 0.0678  307 ASN B OD1 
4049 N ND2 . ASN B 250 ? 1.1379 0.8086 0.4740 0.3015  -0.0804 0.0504  307 ASN B ND2 
4050 N N   . PRO B 251 ? 1.1316 0.8843 0.4844 0.2397  -0.0173 0.0763  308 PRO B N   
4051 C CA  . PRO B 251 ? 1.1043 0.8741 0.4625 0.2165  0.0031  0.0889  308 PRO B CA  
4052 C C   . PRO B 251 ? 1.3471 1.0921 0.6907 0.1950  0.0144  0.1088  308 PRO B C   
4053 O O   . PRO B 251 ? 1.4362 1.1512 0.7440 0.1969  0.0163  0.1203  308 PRO B O   
4054 C CB  . PRO B 251 ? 1.1755 0.9584 0.5090 0.2234  0.0123  0.0913  308 PRO B CB  
4055 C CG  . PRO B 251 ? 1.1570 0.9452 0.4954 0.2497  -0.0061 0.0711  308 PRO B CG  
4056 C CD  . PRO B 251 ? 1.1924 0.9550 0.5315 0.2600  -0.0238 0.0656  308 PRO B CD  
4057 N N   . SER B 252 ? 1.3100 1.0647 0.6798 0.1746  0.0212  0.1127  309 SER B N   
4058 C CA  . SER B 252 ? 1.3985 1.1257 0.7592 0.1544  0.0280  0.1286  309 SER B CA  
4059 C C   . SER B 252 ? 1.4661 1.2175 0.8384 0.1245  0.0478  0.1412  309 SER B C   
4060 O O   . SER B 252 ? 1.4921 1.2835 0.8862 0.1215  0.0549  0.1347  309 SER B O   
4061 C CB  . SER B 252 ? 1.3575 1.0679 0.7398 0.1590  0.0138  0.1201  309 SER B CB  
4062 O OG  . SER B 252 ? 1.4521 1.1285 0.8117 0.1785  0.0001  0.1169  309 SER B OG  
4063 N N   . ALA B 253 ? 1.4261 1.1526 0.7834 0.1027  0.0563  0.1584  310 ALA B N   
4064 C CA  . ALA B 253 ? 1.4292 1.1787 0.8010 0.0706  0.0738  0.1710  310 ALA B CA  
4065 C C   . ALA B 253 ? 1.2358 1.0091 0.6505 0.0658  0.0711  0.1599  310 ALA B C   
4066 O O   . ALA B 253 ? 1.1253 0.8860 0.5547 0.0835  0.0552  0.1462  310 ALA B O   
4067 C CB  . ALA B 253 ? 1.2067 0.9177 0.5562 0.0499  0.0794  0.1898  310 ALA B CB  
4068 N N   . GLN B 254 ? 1.2469 1.0579 0.6822 0.0421  0.0865  0.1656  311 GLN B N   
4069 C CA  . GLN B 254 ? 1.1703 1.0047 0.6447 0.0366  0.0856  0.1560  311 GLN B CA  
4070 C C   . GLN B 254 ? 0.9963 0.7941 0.4778 0.0288  0.0775  0.1589  311 GLN B C   
4071 O O   . GLN B 254 ? 1.1857 0.9499 0.6469 0.0156  0.0799  0.1723  311 GLN B O   
4072 C CB  . GLN B 254 ? 1.0804 0.9645 0.5736 0.0116  0.1047  0.1619  311 GLN B CB  
4073 C CG  . GLN B 254 ? 1.2731 1.1912 0.7540 0.0157  0.1159  0.1600  311 GLN B CG  
4074 C CD  . GLN B 254 ? 1.3628 1.2779 0.8384 0.0514  0.1035  0.1432  311 GLN B CD  
4075 O OE1 . GLN B 254 ? 1.4857 1.4172 0.9878 0.0677  0.0957  0.1269  311 GLN B OE1 
4076 N NE2 . GLN B 254 ? 1.1320 1.0270 0.5737 0.0636  0.1008  0.1473  311 GLN B NE2 
4077 N N   . SER B 255 ? 0.8490 0.6512 0.3582 0.0380  0.0674  0.1453  312 SER B N   
4078 C CA  . SER B 255 ? 0.9791 0.7487 0.4961 0.0320  0.0594  0.1456  312 SER B CA  
4079 C C   . SER B 255 ? 0.9819 0.7770 0.5364 0.0281  0.0585  0.1360  312 SER B C   
4080 O O   . SER B 255 ? 0.7574 0.5811 0.3284 0.0438  0.0548  0.1234  312 SER B O   
4081 C CB  . SER B 255 ? 1.0253 0.7555 0.5260 0.0570  0.0409  0.1377  312 SER B CB  
4082 O OG  . SER B 255 ? 0.9989 0.7085 0.5145 0.0565  0.0316  0.1326  312 SER B OG  
4083 N N   . PRO B 256 ? 0.9444 0.7287 0.5123 0.0078  0.0615  0.1410  313 PRO B N   
4084 C CA  . PRO B 256 ? 0.8291 0.6299 0.4297 0.0066  0.0582  0.1311  313 PRO B CA  
4085 C C   . PRO B 256 ? 0.8970 0.6634 0.4994 0.0213  0.0408  0.1227  313 PRO B C   
4086 O O   . PRO B 256 ? 1.0168 0.7443 0.6035 0.0169  0.0363  0.1276  313 PRO B O   
4087 C CB  . PRO B 256 ? 0.7695 0.5845 0.3857 -0.0254 0.0722  0.1407  313 PRO B CB  
4088 C CG  . PRO B 256 ? 0.8996 0.6799 0.4877 -0.0386 0.0757  0.1546  313 PRO B CG  
4089 C CD  . PRO B 256 ? 0.8780 0.6371 0.4328 -0.0165 0.0691  0.1554  313 PRO B CD  
4090 N N   . GLN B 257 ? 0.6894 0.4720 0.3108 0.0403  0.0305  0.1093  314 GLN B N   
4091 C CA  . GLN B 257 ? 0.7334 0.4959 0.3615 0.0567  0.0135  0.0999  314 GLN B CA  
4092 C C   . GLN B 257 ? 0.6634 0.4433 0.3252 0.0512  0.0117  0.0929  314 GLN B C   
4093 O O   . GLN B 257 ? 0.6213 0.4434 0.3158 0.0475  0.0162  0.0851  314 GLN B O   
4094 C CB  . GLN B 257 ? 0.7838 0.5541 0.4086 0.0840  0.0000  0.0886  314 GLN B CB  
4095 C CG  . GLN B 257 ? 0.7972 0.5609 0.4357 0.1010  -0.0172 0.0770  314 GLN B CG  
4096 C CD  . GLN B 257 ? 1.0368 0.8147 0.6759 0.1236  -0.0302 0.0649  314 GLN B CD  
4097 O OE1 . GLN B 257 ? 1.1836 0.9771 0.8458 0.1351  -0.0432 0.0522  314 GLN B OE1 
4098 N NE2 . GLN B 257 ? 0.9039 0.6789 0.5188 0.1285  -0.0265 0.0683  314 GLN B NE2 
4099 N N   . LEU B 258 ? 0.6060 0.3609 0.2712 0.0503  0.0043  0.0919  315 LEU B N   
4100 C CA  . LEU B 258 ? 0.5609 0.3355 0.2665 0.0409  0.0032  0.0838  315 LEU B CA  
4101 C C   . LEU B 258 ? 0.4894 0.2716 0.2158 0.0614  -0.0124 0.0702  315 LEU B C   
4102 O O   . LEU B 258 ? 0.5532 0.3112 0.2570 0.0801  -0.0234 0.0696  315 LEU B O   
4103 C CB  . LEU B 258 ? 0.5631 0.3051 0.2564 0.0206  0.0085  0.0929  315 LEU B CB  
4104 C CG  . LEU B 258 ? 0.6597 0.4061 0.3453 -0.0083 0.0252  0.1050  315 LEU B CG  
4105 C CD1 . LEU B 258 ? 0.6929 0.4137 0.3777 -0.0286 0.0261  0.1083  315 LEU B CD1 
4106 C CD2 . LEU B 258 ? 0.5600 0.3655 0.2896 -0.0168 0.0330  0.0976  315 LEU B CD2 
4107 N N   . LEU B 259 ? 0.4179 0.2361 0.1869 0.0578  -0.0132 0.0597  316 LEU B N   
4108 C CA  . LEU B 259 ? 0.4083 0.2396 0.2018 0.0714  -0.0255 0.0477  316 LEU B CA  
4109 C C   . LEU B 259 ? 0.3790 0.2097 0.1935 0.0607  -0.0236 0.0461  316 LEU B C   
4110 O O   . LEU B 259 ? 0.4229 0.2585 0.2462 0.0418  -0.0135 0.0503  316 LEU B O   
4111 C CB  . LEU B 259 ? 0.4123 0.2818 0.2343 0.0762  -0.0291 0.0363  316 LEU B CB  
4112 C CG  . LEU B 259 ? 0.4623 0.3336 0.2651 0.0915  -0.0360 0.0335  316 LEU B CG  
4113 C CD1 . LEU B 259 ? 0.4569 0.3598 0.2862 0.0932  -0.0404 0.0212  316 LEU B CD1 
4114 C CD2 . LEU B 259 ? 0.4890 0.3437 0.2735 0.1105  -0.0493 0.0318  316 LEU B CD2 
4115 N N   . PRO B 260 ? 0.3645 0.1917 0.1867 0.0729  -0.0333 0.0399  317 PRO B N   
4116 C CA  . PRO B 260 ? 0.3423 0.1685 0.1817 0.0646  -0.0315 0.0379  317 PRO B CA  
4117 C C   . PRO B 260 ? 0.3214 0.1857 0.2010 0.0547  -0.0277 0.0309  317 PRO B C   
4118 O O   . PRO B 260 ? 0.3615 0.2529 0.2592 0.0590  -0.0304 0.0244  317 PRO B O   
4119 C CB  . PRO B 260 ? 0.3747 0.1933 0.2101 0.0854  -0.0430 0.0323  317 PRO B CB  
4120 C CG  . PRO B 260 ? 0.5059 0.3419 0.3406 0.1022  -0.0517 0.0273  317 PRO B CG  
4121 C CD  . PRO B 260 ? 0.4680 0.2939 0.2811 0.0962  -0.0463 0.0345  317 PRO B CD  
4122 N N   . VAL B 261 ? 0.3278 0.1900 0.2175 0.0410  -0.0221 0.0322  318 VAL B N   
4123 C CA  . VAL B 261 ? 0.3133 0.2052 0.2371 0.0347  -0.0200 0.0256  318 VAL B CA  
4124 C C   . VAL B 261 ? 0.3044 0.1888 0.2340 0.0389  -0.0239 0.0221  318 VAL B C   
4125 O O   . VAL B 261 ? 0.3449 0.1979 0.2507 0.0429  -0.0265 0.0253  318 VAL B O   
4126 C CB  . VAL B 261 ? 0.3519 0.2561 0.2849 0.0167  -0.0102 0.0289  318 VAL B CB  
4127 C CG1 . VAL B 261 ? 0.3733 0.2929 0.3033 0.0164  -0.0059 0.0304  318 VAL B CG1 
4128 C CG2 . VAL B 261 ? 0.4089 0.2873 0.3232 0.0027  -0.0057 0.0364  318 VAL B CG2 
4129 N N   . THR B 262 ? 0.2671 0.1782 0.2253 0.0387  -0.0244 0.0154  319 THR B N   
4130 C CA  . THR B 262 ? 0.2732 0.1851 0.2396 0.0442  -0.0270 0.0113  319 THR B CA  
4131 C C   . THR B 262 ? 0.2300 0.1599 0.2189 0.0327  -0.0218 0.0091  319 THR B C   
4132 O O   . THR B 262 ? 0.2592 0.2070 0.2618 0.0254  -0.0184 0.0086  319 THR B O   
4133 C CB  . THR B 262 ? 0.3072 0.2385 0.2848 0.0600  -0.0342 0.0050  319 THR B CB  
4134 O OG1 . THR B 262 ? 0.2819 0.2412 0.2808 0.0558  -0.0345 0.0014  319 THR B OG1 
4135 C CG2 . THR B 262 ? 0.3960 0.3093 0.3487 0.0760  -0.0413 0.0063  319 THR B CG2 
4136 N N   . LEU B 263 ? 0.2515 0.1748 0.2410 0.0335  -0.0220 0.0073  320 LEU B N   
4137 C CA  . LEU B 263 ? 0.2199 0.1608 0.2291 0.0266  -0.0184 0.0045  320 LEU B CA  
4138 C C   . LEU B 263 ? 0.1728 0.1372 0.2000 0.0355  -0.0204 -0.0004 320 LEU B C   
4139 O O   . LEU B 263 ? 0.2342 0.1978 0.2569 0.0481  -0.0241 -0.0028 320 LEU B O   
4140 C CB  . LEU B 263 ? 0.2598 0.1810 0.2577 0.0224  -0.0179 0.0045  320 LEU B CB  
4141 C CG  . LEU B 263 ? 0.2796 0.2175 0.2941 0.0185  -0.0154 0.0011  320 LEU B CG  
4142 C CD1 . LEU B 263 ? 0.2835 0.2365 0.3098 0.0059  -0.0112 0.0027  320 LEU B CD1 
4143 C CD2 . LEU B 263 ? 0.3946 0.3105 0.3940 0.0190  -0.0173 -0.0009 320 LEU B CD2 
4144 N N   . VAL B 264 ? 0.1800 0.1652 0.2257 0.0292  -0.0180 -0.0016 321 VAL B N   
4145 C CA  . VAL B 264 ? 0.1818 0.1893 0.2448 0.0314  -0.0184 -0.0048 321 VAL B CA  
4146 C C   . VAL B 264 ? 0.1360 0.1470 0.2052 0.0268  -0.0137 -0.0048 321 VAL B C   
4147 O O   . VAL B 264 ? 0.1501 0.1600 0.2217 0.0188  -0.0109 -0.0035 321 VAL B O   
4148 C CB  . VAL B 264 ? 0.1811 0.2010 0.2540 0.0263  -0.0199 -0.0060 321 VAL B CB  
4149 C CG1 . VAL B 264 ? 0.1381 0.1799 0.2279 0.0238  -0.0200 -0.0084 321 VAL B CG1 
4150 C CG2 . VAL B 264 ? 0.2530 0.2696 0.3174 0.0324  -0.0254 -0.0067 321 VAL B CG2 
4151 N N   . LYS B 265 ? 0.1921 0.2080 0.2616 0.0342  -0.0134 -0.0067 322 LYS B N   
4152 C CA  . LYS B 265 ? 0.1783 0.1970 0.2503 0.0323  -0.0092 -0.0070 322 LYS B CA  
4153 C C   . LYS B 265 ? 0.1233 0.1646 0.2114 0.0274  -0.0057 -0.0064 322 LYS B C   
4154 O O   . LYS B 265 ? 0.1633 0.2250 0.2610 0.0308  -0.0058 -0.0077 322 LYS B O   
4155 C CB  . LYS B 265 ? 0.2405 0.2532 0.3018 0.0446  -0.0102 -0.0098 322 LYS B CB  
4156 C CG  . LYS B 265 ? 0.3136 0.2943 0.3529 0.0465  -0.0139 -0.0099 322 LYS B CG  
4157 C CD  . LYS B 265 ? 0.3801 0.3486 0.4032 0.0620  -0.0165 -0.0139 322 LYS B CD  
4158 C CE  . LYS B 265 ? 0.4679 0.3956 0.4640 0.0601  -0.0207 -0.0142 322 LYS B CE  
4159 N NZ  . LYS B 265 ? 0.4940 0.4048 0.4707 0.0749  -0.0235 -0.0195 322 LYS B NZ  
4160 N N   . ARG B 266 ? 0.1256 0.1634 0.2151 0.0189  -0.0029 -0.0042 323 ARG B N   
4161 C CA  . ARG B 266 ? 0.1480 0.1982 0.2459 0.0128  0.0008  -0.0023 323 ARG B CA  
4162 C C   . ARG B 266 ? 0.1207 0.1677 0.2129 0.0135  0.0051  -0.0009 323 ARG B C   
4163 O O   . ARG B 266 ? 0.1679 0.2199 0.2571 0.0208  0.0069  -0.0025 323 ARG B O   
4164 C CB  . ARG B 266 ? 0.1106 0.1541 0.2095 0.0044  -0.0010 -0.0010 323 ARG B CB  
4165 C CG  . ARG B 266 ? 0.1331 0.1820 0.2369 0.0039  -0.0060 -0.0033 323 ARG B CG  
4166 C CD  . ARG B 266 ? 0.1301 0.1726 0.2336 -0.0049 -0.0084 -0.0032 323 ARG B CD  
4167 N NE  . ARG B 266 ? 0.1422 0.1908 0.2493 -0.0051 -0.0144 -0.0066 323 ARG B NE  
4168 C CZ  . ARG B 266 ? 0.1577 0.1944 0.2562 -0.0016 -0.0184 -0.0083 323 ARG B CZ  
4169 N NH1 . ARG B 266 ? 0.1587 0.1813 0.2471 0.0018  -0.0164 -0.0070 323 ARG B NH1 
4170 N NH2 . ARG B 266 ? 0.1538 0.1963 0.2540 -0.0012 -0.0246 -0.0117 323 ARG B NH2 
4171 N N   . LYS B 267 ? 0.1274 0.1652 0.2152 0.0084  0.0061  0.0015  324 LYS B N   
4172 C CA  . LYS B 267 ? 0.1278 0.1644 0.2091 0.0093  0.0100  0.0036  324 LYS B CA  
4173 C C   . LYS B 267 ? 0.1244 0.1492 0.1964 0.0117  0.0075  0.0027  324 LYS B C   
4174 O O   . LYS B 267 ? 0.1593 0.1811 0.2232 0.0136  0.0094  0.0045  324 LYS B O   
4175 C CB  . LYS B 267 ? 0.1356 0.1739 0.2175 0.0011  0.0140  0.0085  324 LYS B CB  
4176 C CG  . LYS B 267 ? 0.1820 0.2416 0.2752 -0.0037 0.0180  0.0097  324 LYS B CG  
4177 C CD  . LYS B 267 ? 0.2347 0.3116 0.3296 0.0060  0.0216  0.0076  324 LYS B CD  
4178 C CE  . LYS B 267 ? 0.3035 0.4113 0.4129 0.0030  0.0256  0.0080  324 LYS B CE  
4179 N NZ  . LYS B 267 ? 0.5072 0.6327 0.6138 0.0116  0.0325  0.0082  324 LYS B NZ  
4180 N N   . THR B 268 ? 0.1047 0.1258 0.1774 0.0118  0.0034  0.0001  325 THR B N   
4181 C CA  . THR B 268 ? 0.1219 0.1411 0.1896 0.0131  0.0010  -0.0013 325 THR B CA  
4182 C C   . THR B 268 ? 0.1190 0.1379 0.1840 0.0125  -0.0017 -0.0050 325 THR B C   
4183 O O   . THR B 268 ? 0.1261 0.1496 0.1902 0.0110  -0.0044 -0.0069 325 THR B O   
4184 C CB  . THR B 268 ? 0.1219 0.1415 0.1913 0.0123  -0.0010 -0.0013 325 THR B CB  
4185 O OG1 . THR B 268 ? 0.1211 0.1414 0.1950 0.0092  -0.0019 -0.0021 325 THR B OG1 
4186 C CG2 . THR B 268 ? 0.1438 0.1552 0.2090 0.0130  -0.0002 0.0014  325 THR B CG2 
4187 N N   . THR B 269 ? 0.1451 0.1586 0.2071 0.0141  -0.0017 -0.0066 326 THR B N   
4188 C CA  . THR B 269 ? 0.1357 0.1404 0.1889 0.0126  -0.0055 -0.0106 326 THR B CA  
4189 C C   . THR B 269 ? 0.1558 0.1550 0.1994 0.0204  -0.0051 -0.0132 326 THR B C   
4190 O O   . THR B 269 ? 0.1894 0.1944 0.2349 0.0270  -0.0010 -0.0117 326 THR B O   
4191 C CB  . THR B 269 ? 0.1894 0.1821 0.2387 0.0075  -0.0081 -0.0111 326 THR B CB  
4192 O OG1 . THR B 269 ? 0.2384 0.2231 0.2835 0.0151  -0.0076 -0.0111 326 THR B OG1 
4193 C CG2 . THR B 269 ? 0.1505 0.1510 0.2080 0.0011  -0.0073 -0.0081 326 THR B CG2 
4194 N N   . ALA B 270 ? 0.1545 0.1450 0.1875 0.0191  -0.0095 -0.0177 327 ALA B N   
4195 C CA  . ALA B 270 ? 0.1728 0.1554 0.1919 0.0277  -0.0105 -0.0219 327 ALA B CA  
4196 C C   . ALA B 270 ? 0.1929 0.1590 0.1989 0.0213  -0.0184 -0.0281 327 ALA B C   
4197 O O   . ALA B 270 ? 0.1922 0.1608 0.2039 0.0087  -0.0217 -0.0280 327 ALA B O   
4198 C CB  . ALA B 270 ? 0.1679 0.1640 0.1874 0.0334  -0.0064 -0.0199 327 ALA B CB  
4199 N N   . PRO B 271 ? 0.2111 0.1612 0.1986 0.0289  -0.0219 -0.0340 328 PRO B N   
4200 C CA  . PRO B 271 ? 0.2089 0.1416 0.1821 0.0200  -0.0311 -0.0409 328 PRO B CA  
4201 C C   . PRO B 271 ? 0.2153 0.1696 0.1983 0.0126  -0.0337 -0.0418 328 PRO B C   
4202 O O   . PRO B 271 ? 0.2134 0.1883 0.2061 0.0197  -0.0287 -0.0378 328 PRO B O   
4203 C CB  . PRO B 271 ? 0.2556 0.1687 0.2049 0.0345  -0.0338 -0.0476 328 PRO B CB  
4204 C CG  . PRO B 271 ? 0.2746 0.1913 0.2255 0.0496  -0.0264 -0.0441 328 PRO B CG  
4205 C CD  . PRO B 271 ? 0.2406 0.1877 0.2178 0.0456  -0.0182 -0.0355 328 PRO B CD  
4206 N N   . PRO B 272 ? 0.2304 0.1806 0.2097 -0.0015 -0.0419 -0.0470 329 PRO B N   
4207 C CA  . PRO B 272 ? 0.2178 0.1944 0.2066 -0.0055 -0.0459 -0.0494 329 PRO B CA  
4208 C C   . PRO B 272 ? 0.2593 0.2379 0.2361 0.0099  -0.0471 -0.0528 329 PRO B C   
4209 O O   . PRO B 272 ? 0.2625 0.2194 0.2197 0.0193  -0.0480 -0.0567 329 PRO B O   
4210 C CB  . PRO B 272 ? 0.2504 0.2215 0.2354 -0.0257 -0.0555 -0.0558 329 PRO B CB  
4211 C CG  . PRO B 272 ? 0.2909 0.2208 0.2548 -0.0296 -0.0578 -0.0577 329 PRO B CG  
4212 C CD  . PRO B 272 ? 0.2374 0.1599 0.2033 -0.0159 -0.0484 -0.0505 329 PRO B CD  
4213 N N   . GLU B 273 ? 0.2626 0.2668 0.2485 0.0144  -0.0471 -0.0512 330 GLU B N   
4214 C CA  . GLU B 273 ? 0.3125 0.3205 0.2857 0.0294  -0.0477 -0.0525 330 GLU B CA  
4215 C C   . GLU B 273 ? 0.3242 0.3141 0.2749 0.0319  -0.0558 -0.0622 330 GLU B C   
4216 O O   . GLU B 273 ? 0.3547 0.3428 0.3026 0.0195  -0.0667 -0.0706 330 GLU B O   
4217 C CB  . GLU B 273 ? 0.3248 0.3602 0.3069 0.0315  -0.0519 -0.0526 330 GLU B CB  
4218 C CG  . GLU B 273 ? 0.4101 0.4469 0.3782 0.0494  -0.0491 -0.0491 330 GLU B CG  
4219 C CD  . GLU B 273 ? 0.3971 0.4578 0.3699 0.0556  -0.0546 -0.0493 330 GLU B CD  
4220 O OE1 . GLU B 273 ? 0.3501 0.4324 0.3410 0.0463  -0.0592 -0.0521 330 GLU B OE1 
4221 O OE2 . GLU B 273 ? 0.4743 0.5328 0.4306 0.0709  -0.0542 -0.0466 330 GLU B OE2 
4222 N N   . ASN B 274 ? 0.3490 0.3262 0.2831 0.0473  -0.0502 -0.0611 331 ASN B N   
4223 C CA  . ASN B 274 ? 0.4219 0.3823 0.3296 0.0566  -0.0563 -0.0699 331 ASN B CA  
4224 C C   . ASN B 274 ? 0.4271 0.3578 0.3208 0.0484  -0.0646 -0.0790 331 ASN B C   
4225 O O   . ASN B 274 ? 0.4972 0.4095 0.3664 0.0532  -0.0734 -0.0891 331 ASN B O   
4226 C CB  . ASN B 274 ? 0.4527 0.4274 0.3535 0.0592  -0.0655 -0.0754 331 ASN B CB  
4227 C CG  . ASN B 274 ? 0.5024 0.4960 0.4064 0.0717  -0.0576 -0.0659 331 ASN B CG  
4228 O OD1 . ASN B 274 ? 0.6004 0.6122 0.5085 0.0724  -0.0636 -0.0667 331 ASN B OD1 
4229 N ND2 . ASN B 274 ? 0.5511 0.5403 0.4524 0.0809  -0.0441 -0.0567 331 ASN B ND2 
4230 N N   . LEU B 275 ? 0.3437 0.2647 0.2482 0.0369  -0.0625 -0.0757 332 LEU B N   
4231 C CA  . LEU B 275 ? 0.3266 0.2094 0.2097 0.0340  -0.0685 -0.0823 332 LEU B CA  
4232 C C   . LEU B 275 ? 0.4175 0.2837 0.2778 0.0580  -0.0641 -0.0848 332 LEU B C   
4233 O O   . LEU B 275 ? 0.4822 0.3160 0.3125 0.0642  -0.0725 -0.0949 332 LEU B O   
4234 C CB  . LEU B 275 ? 0.4048 0.2796 0.3006 0.0212  -0.0652 -0.0761 332 LEU B CB  
4235 C CG  . LEU B 275 ? 0.3693 0.1974 0.2388 0.0157  -0.0728 -0.0818 332 LEU B CG  
4236 C CD1 . LEU B 275 ? 0.4440 0.2486 0.2919 0.0019  -0.0874 -0.0932 332 LEU B CD1 
4237 C CD2 . LEU B 275 ? 0.3897 0.2104 0.2701 0.0019  -0.0693 -0.0742 332 LEU B CD2 
4238 N N   . TYR B 276 ? 0.3901 0.2793 0.2630 0.0715  -0.0509 -0.0762 333 TYR B N   
4239 C CA  . TYR B 276 ? 0.4029 0.2885 0.2584 0.0946  -0.0444 -0.0777 333 TYR B CA  
4240 C C   . TYR B 276 ? 0.4462 0.3605 0.3052 0.1045  -0.0358 -0.0725 333 TYR B C   
4241 O O   . TYR B 276 ? 0.5250 0.4613 0.3961 0.1117  -0.0229 -0.0637 333 TYR B O   
4242 C CB  . TYR B 276 ? 0.4021 0.2909 0.2683 0.1006  -0.0359 -0.0718 333 TYR B CB  
4243 C CG  . TYR B 276 ? 0.3957 0.2523 0.2545 0.0920  -0.0438 -0.0750 333 TYR B CG  
4244 C CD1 . TYR B 276 ? 0.4131 0.2273 0.2377 0.0985  -0.0543 -0.0857 333 TYR B CD1 
4245 C CD2 . TYR B 276 ? 0.3289 0.1931 0.2106 0.0773  -0.0411 -0.0672 333 TYR B CD2 
4246 C CE1 . TYR B 276 ? 0.4068 0.1904 0.2235 0.0876  -0.0605 -0.0844 333 TYR B CE1 
4247 C CE2 . TYR B 276 ? 0.3766 0.2088 0.2478 0.0690  -0.0476 -0.0688 333 TYR B CE2 
4248 C CZ  . TYR B 276 ? 0.3860 0.1737 0.2219 0.0744  -0.0577 -0.0783 333 TYR B CZ  
4249 O OH  . TYR B 276 ? 0.4635 0.2207 0.2886 0.0634  -0.0626 -0.0756 333 TYR B OH  
4250 N N   . PHE B 277 ? 0.4289 0.3431 0.2765 0.1035  -0.0432 -0.0775 334 PHE B N   
4251 C CA  . PHE B 277 ? 0.4335 0.3698 0.2795 0.1124  -0.0362 -0.0717 334 PHE B CA  
4252 C C   . PHE B 277 ? 0.5294 0.4712 0.3595 0.1327  -0.0248 -0.0697 334 PHE B C   
4253 O O   . PHE B 277 ? 0.5458 0.4701 0.3501 0.1467  -0.0290 -0.0796 334 PHE B O   
4254 C CB  . PHE B 277 ? 0.4858 0.4180 0.3164 0.1113  -0.0490 -0.0800 334 PHE B CB  
4255 C CG  . PHE B 277 ? 0.5057 0.4560 0.3298 0.1214  -0.0434 -0.0737 334 PHE B CG  
4256 C CD1 . PHE B 277 ? 0.5255 0.4920 0.3639 0.1137  -0.0461 -0.0685 334 PHE B CD1 
4257 C CD2 . PHE B 277 ? 0.6696 0.6193 0.4691 0.1402  -0.0362 -0.0732 334 PHE B CD2 
4258 C CE1 . PHE B 277 ? 0.4929 0.4691 0.3192 0.1246  -0.0422 -0.0622 334 PHE B CE1 
4259 C CE2 . PHE B 277 ? 0.5779 0.5399 0.3665 0.1488  -0.0308 -0.0661 334 PHE B CE2 
4260 C CZ  . PHE B 277 ? 0.6024 0.5747 0.4031 0.1409  -0.0343 -0.0604 334 PHE B CZ  
4261 N N   . GLN B 278 ? 0.4933 0.4597 0.3373 0.1338  -0.0105 -0.0572 335 GLN B N   
4262 C CA  . GLN B 278 ? 0.6821 0.6637 0.5164 0.1496  0.0031  -0.0532 335 GLN B CA  
4263 C C   . GLN B 278 ? 0.7214 0.7219 0.5562 0.1481  0.0141  -0.0408 335 GLN B C   
4264 O O   . GLN B 278 ? 0.7691 0.7717 0.6186 0.1346  0.0133  -0.0333 335 GLN B O   
4265 C CB  . GLN B 278 ? 0.6252 0.6190 0.4783 0.1497  0.0112  -0.0497 335 GLN B CB  
4266 C CG  . GLN B 278 ? 0.8088 0.7793 0.6522 0.1567  0.0014  -0.0610 335 GLN B CG  
4267 C CD  . GLN B 278 ? 0.9563 0.9365 0.8215 0.1536  0.0059  -0.0571 335 GLN B CD  
4268 O OE1 . GLN B 278 ? 1.1112 1.1218 0.9904 0.1569  0.0176  -0.0493 335 GLN B OE1 
4269 N NE2 . GLN B 278 ? 0.8833 0.8389 0.7519 0.1444  -0.0043 -0.0614 335 GLN B NE2 
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