data_8ZU4
# 
_entry.id   8ZU4 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_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   8ZU4         pdb_00008zu4 10.2210/pdb8zu4/pdb 
WWPDB D_1300048205 ?            ?                   
# 
_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       2025-06-11 
_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                        8ZU4 
_pdbx_database_status.recvd_initial_deposition_date   2024-06-07 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBC 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 3 
_pdbx_contact_author.email              feixu@jiangnan.edu.cn 
_pdbx_contact_author.name_first         Fei 
_pdbx_contact_author.name_last          Xu 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-1077-0431 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Xu, F.'  1 0000-0003-1077-0431 
'Fan, S.' 2 0000-0001-9272-2438 
# 
_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 Methyl parathion hydrolase mutant A127L/I145L/Q272D/S279A/S304P' 
_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 'Xu, F.'  1 0000-0003-1077-0431 
primary 'Fan, S.' 2 0000-0001-9272-2438 
primary 'Li, Y.'  3 0009-0008-9986-7187 
# 
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 'Methyl parathion hydrolase' 31383.578 2   ? 'A127L,I145L,Q272D, S279A,S304P' ? ? 
2 non-polymer syn 'ZINC ION'                   65.409    4   ? ?                                ? ? 
3 water       nat water                        18.015    644 ? ?                                ? ? 
# 
_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       
;AAPQVRTSAPGYYRMLLGDFEITALSDGTVALPVDKRLNQPAPKTQSALAKSFQKAPLETSVTGYLVNTGSKLVLVDTGA
AGLFGPTLGRLLANLKAAGYQPEQVDEIYLTHMHPDHVGGLMVGEQLAFPNAVVRADQKEADFWLSQTNLDKAPDDESKG
FFKGAMASLNPYVKAGKFKPFSGNTDLVPGIKALASHGHTPGHTTYVVESQGQKLALLGDLILVAAVQFDDPSVTTDLDS
DSKAVAVERKKAFADAAKGGYLIAASHLPFPGIGHIRAEGKGYRFVPVNYSVVNAA
;
_entity_poly.pdbx_seq_one_letter_code_can   
;AAPQVRTSAPGYYRMLLGDFEITALSDGTVALPVDKRLNQPAPKTQSALAKSFQKAPLETSVTGYLVNTGSKLVLVDTGA
AGLFGPTLGRLLANLKAAGYQPEQVDEIYLTHMHPDHVGGLMVGEQLAFPNAVVRADQKEADFWLSQTNLDKAPDDESKG
FFKGAMASLNPYVKAGKFKPFSGNTDLVPGIKALASHGHTPGHTTYVVESQGQKLALLGDLILVAAVQFDDPSVTTDLDS
DSKAVAVERKKAFADAAKGGYLIAASHLPFPGIGHIRAEGKGYRFVPVNYSVVNAA
;
_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 'ZINC ION' ZN  
3 water      HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   ALA n 
1 2   ALA n 
1 3   PRO n 
1 4   GLN n 
1 5   VAL n 
1 6   ARG n 
1 7   THR n 
1 8   SER n 
1 9   ALA n 
1 10  PRO n 
1 11  GLY n 
1 12  TYR n 
1 13  TYR n 
1 14  ARG n 
1 15  MET n 
1 16  LEU n 
1 17  LEU n 
1 18  GLY n 
1 19  ASP n 
1 20  PHE n 
1 21  GLU n 
1 22  ILE n 
1 23  THR n 
1 24  ALA n 
1 25  LEU n 
1 26  SER n 
1 27  ASP n 
1 28  GLY n 
1 29  THR n 
1 30  VAL n 
1 31  ALA n 
1 32  LEU n 
1 33  PRO n 
1 34  VAL n 
1 35  ASP n 
1 36  LYS n 
1 37  ARG n 
1 38  LEU n 
1 39  ASN n 
1 40  GLN n 
1 41  PRO n 
1 42  ALA n 
1 43  PRO n 
1 44  LYS n 
1 45  THR n 
1 46  GLN n 
1 47  SER n 
1 48  ALA n 
1 49  LEU n 
1 50  ALA n 
1 51  LYS n 
1 52  SER n 
1 53  PHE n 
1 54  GLN n 
1 55  LYS n 
1 56  ALA n 
1 57  PRO n 
1 58  LEU n 
1 59  GLU n 
1 60  THR n 
1 61  SER n 
1 62  VAL n 
1 63  THR n 
1 64  GLY n 
1 65  TYR n 
1 66  LEU n 
1 67  VAL n 
1 68  ASN n 
1 69  THR n 
1 70  GLY n 
1 71  SER n 
1 72  LYS n 
1 73  LEU n 
1 74  VAL n 
1 75  LEU n 
1 76  VAL n 
1 77  ASP n 
1 78  THR n 
1 79  GLY n 
1 80  ALA n 
1 81  ALA n 
1 82  GLY n 
1 83  LEU n 
1 84  PHE n 
1 85  GLY n 
1 86  PRO n 
1 87  THR n 
1 88  LEU n 
1 89  GLY n 
1 90  ARG n 
1 91  LEU n 
1 92  LEU n 
1 93  ALA n 
1 94  ASN n 
1 95  LEU n 
1 96  LYS n 
1 97  ALA n 
1 98  ALA n 
1 99  GLY n 
1 100 TYR n 
1 101 GLN n 
1 102 PRO n 
1 103 GLU n 
1 104 GLN n 
1 105 VAL n 
1 106 ASP n 
1 107 GLU n 
1 108 ILE n 
1 109 TYR n 
1 110 LEU n 
1 111 THR n 
1 112 HIS n 
1 113 MET n 
1 114 HIS n 
1 115 PRO n 
1 116 ASP n 
1 117 HIS n 
1 118 VAL n 
1 119 GLY n 
1 120 GLY n 
1 121 LEU n 
1 122 MET n 
1 123 VAL n 
1 124 GLY n 
1 125 GLU n 
1 126 GLN n 
1 127 LEU n 
1 128 ALA n 
1 129 PHE n 
1 130 PRO n 
1 131 ASN n 
1 132 ALA n 
1 133 VAL n 
1 134 VAL n 
1 135 ARG n 
1 136 ALA n 
1 137 ASP n 
1 138 GLN n 
1 139 LYS n 
1 140 GLU n 
1 141 ALA n 
1 142 ASP n 
1 143 PHE n 
1 144 TRP n 
1 145 LEU n 
1 146 SER n 
1 147 GLN n 
1 148 THR n 
1 149 ASN n 
1 150 LEU n 
1 151 ASP n 
1 152 LYS n 
1 153 ALA n 
1 154 PRO n 
1 155 ASP n 
1 156 ASP n 
1 157 GLU n 
1 158 SER n 
1 159 LYS n 
1 160 GLY n 
1 161 PHE n 
1 162 PHE n 
1 163 LYS n 
1 164 GLY n 
1 165 ALA n 
1 166 MET n 
1 167 ALA n 
1 168 SER n 
1 169 LEU n 
1 170 ASN n 
1 171 PRO n 
1 172 TYR n 
1 173 VAL n 
1 174 LYS n 
1 175 ALA n 
1 176 GLY n 
1 177 LYS n 
1 178 PHE n 
1 179 LYS n 
1 180 PRO n 
1 181 PHE n 
1 182 SER n 
1 183 GLY n 
1 184 ASN n 
1 185 THR n 
1 186 ASP n 
1 187 LEU n 
1 188 VAL n 
1 189 PRO n 
1 190 GLY n 
1 191 ILE n 
1 192 LYS n 
1 193 ALA n 
1 194 LEU n 
1 195 ALA n 
1 196 SER n 
1 197 HIS n 
1 198 GLY n 
1 199 HIS n 
1 200 THR n 
1 201 PRO n 
1 202 GLY n 
1 203 HIS n 
1 204 THR n 
1 205 THR n 
1 206 TYR n 
1 207 VAL n 
1 208 VAL n 
1 209 GLU n 
1 210 SER n 
1 211 GLN n 
1 212 GLY n 
1 213 GLN n 
1 214 LYS n 
1 215 LEU n 
1 216 ALA n 
1 217 LEU n 
1 218 LEU n 
1 219 GLY n 
1 220 ASP n 
1 221 LEU n 
1 222 ILE n 
1 223 LEU n 
1 224 VAL n 
1 225 ALA n 
1 226 ALA n 
1 227 VAL n 
1 228 GLN n 
1 229 PHE n 
1 230 ASP n 
1 231 ASP n 
1 232 PRO n 
1 233 SER n 
1 234 VAL n 
1 235 THR n 
1 236 THR n 
1 237 ASP n 
1 238 LEU n 
1 239 ASP n 
1 240 SER n 
1 241 ASP n 
1 242 SER n 
1 243 LYS n 
1 244 ALA n 
1 245 VAL n 
1 246 ALA n 
1 247 VAL n 
1 248 GLU n 
1 249 ARG n 
1 250 LYS n 
1 251 LYS n 
1 252 ALA n 
1 253 PHE n 
1 254 ALA n 
1 255 ASP n 
1 256 ALA n 
1 257 ALA n 
1 258 LYS n 
1 259 GLY n 
1 260 GLY n 
1 261 TYR n 
1 262 LEU n 
1 263 ILE n 
1 264 ALA n 
1 265 ALA n 
1 266 SER n 
1 267 HIS n 
1 268 LEU n 
1 269 PRO n 
1 270 PHE n 
1 271 PRO n 
1 272 GLY n 
1 273 ILE n 
1 274 GLY n 
1 275 HIS n 
1 276 ILE n 
1 277 ARG n 
1 278 ALA n 
1 279 GLU n 
1 280 GLY n 
1 281 LYS n 
1 282 GLY n 
1 283 TYR n 
1 284 ARG n 
1 285 PHE n 
1 286 VAL n 
1 287 PRO n 
1 288 VAL n 
1 289 ASN n 
1 290 TYR n 
1 291 SER n 
1 292 VAL n 
1 293 VAL n 
1 294 ASN n 
1 295 ALA n 
1 296 ALA 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                   296 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 mpd 
_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      'Pseudomonas sp. WBC-3' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     165468 
_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 
GLN 'L-peptide linking' y GLUTAMINE       ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE       ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER           ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE      ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ? 'C5 H11 N O2 S'  149.211 
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 
ZN  non-polymer         . 'ZINC ION'      ? 'Zn 2'           65.409  
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   ALA 1   36  36  ALA ALA A . n 
A 1 2   ALA 2   37  37  ALA ALA A . n 
A 1 3   PRO 3   38  38  PRO PRO A . n 
A 1 4   GLN 4   39  39  GLN GLN A . n 
A 1 5   VAL 5   40  40  VAL VAL A . n 
A 1 6   ARG 6   41  41  ARG ARG A . n 
A 1 7   THR 7   42  42  THR THR A . n 
A 1 8   SER 8   43  43  SER SER A . n 
A 1 9   ALA 9   44  44  ALA ALA A . n 
A 1 10  PRO 10  45  45  PRO PRO A . n 
A 1 11  GLY 11  46  46  GLY GLY A . n 
A 1 12  TYR 12  47  47  TYR TYR A . n 
A 1 13  TYR 13  48  48  TYR TYR A . n 
A 1 14  ARG 14  49  49  ARG ARG A . n 
A 1 15  MET 15  50  50  MET MET A . n 
A 1 16  LEU 16  51  51  LEU LEU A . n 
A 1 17  LEU 17  52  52  LEU LEU A . n 
A 1 18  GLY 18  53  53  GLY GLY A . n 
A 1 19  ASP 19  54  54  ASP ASP A . n 
A 1 20  PHE 20  55  55  PHE PHE A . n 
A 1 21  GLU 21  56  56  GLU GLU A . n 
A 1 22  ILE 22  57  57  ILE ILE A . n 
A 1 23  THR 23  58  58  THR THR A . n 
A 1 24  ALA 24  59  59  ALA ALA A . n 
A 1 25  LEU 25  60  60  LEU LEU A . n 
A 1 26  SER 26  61  61  SER SER A . n 
A 1 27  ASP 27  62  62  ASP ASP A . n 
A 1 28  GLY 28  63  63  GLY GLY A . n 
A 1 29  THR 29  64  64  THR THR A . n 
A 1 30  VAL 30  65  65  VAL VAL A . n 
A 1 31  ALA 31  66  66  ALA ALA A . n 
A 1 32  LEU 32  67  67  LEU LEU A . n 
A 1 33  PRO 33  68  68  PRO PRO A . n 
A 1 34  VAL 34  69  69  VAL VAL A . n 
A 1 35  ASP 35  70  70  ASP ASP A . n 
A 1 36  LYS 36  71  71  LYS LYS A . n 
A 1 37  ARG 37  72  72  ARG ARG A . n 
A 1 38  LEU 38  73  73  LEU LEU A . n 
A 1 39  ASN 39  74  74  ASN ASN A . n 
A 1 40  GLN 40  75  75  GLN GLN A . n 
A 1 41  PRO 41  76  76  PRO PRO A . n 
A 1 42  ALA 42  77  77  ALA ALA A . n 
A 1 43  PRO 43  78  78  PRO PRO A . n 
A 1 44  LYS 44  79  79  LYS LYS A . n 
A 1 45  THR 45  80  80  THR THR A . n 
A 1 46  GLN 46  81  81  GLN GLN A . n 
A 1 47  SER 47  82  82  SER SER A . n 
A 1 48  ALA 48  83  83  ALA ALA A . n 
A 1 49  LEU 49  84  84  LEU LEU A . n 
A 1 50  ALA 50  85  85  ALA ALA A . n 
A 1 51  LYS 51  86  86  LYS LYS A . n 
A 1 52  SER 52  87  87  SER SER A . n 
A 1 53  PHE 53  88  88  PHE PHE A . n 
A 1 54  GLN 54  89  89  GLN GLN A . n 
A 1 55  LYS 55  90  90  LYS LYS A . n 
A 1 56  ALA 56  91  91  ALA ALA A . n 
A 1 57  PRO 57  92  92  PRO PRO A . n 
A 1 58  LEU 58  93  93  LEU LEU A . n 
A 1 59  GLU 59  94  94  GLU GLU A . n 
A 1 60  THR 60  95  95  THR THR A . n 
A 1 61  SER 61  96  96  SER SER A . n 
A 1 62  VAL 62  97  97  VAL VAL A . n 
A 1 63  THR 63  98  98  THR THR A . n 
A 1 64  GLY 64  99  99  GLY GLY A . n 
A 1 65  TYR 65  100 100 TYR TYR A . n 
A 1 66  LEU 66  101 101 LEU LEU A . n 
A 1 67  VAL 67  102 102 VAL VAL A . n 
A 1 68  ASN 68  103 103 ASN ASN A . n 
A 1 69  THR 69  104 104 THR THR A . n 
A 1 70  GLY 70  105 105 GLY GLY A . n 
A 1 71  SER 71  106 106 SER SER A . n 
A 1 72  LYS 72  107 107 LYS LYS A . n 
A 1 73  LEU 73  108 108 LEU LEU A . n 
A 1 74  VAL 74  109 109 VAL VAL A . n 
A 1 75  LEU 75  110 110 LEU LEU A . n 
A 1 76  VAL 76  111 111 VAL VAL A . n 
A 1 77  ASP 77  112 112 ASP ASP A . n 
A 1 78  THR 78  113 113 THR THR A . n 
A 1 79  GLY 79  114 114 GLY GLY A . n 
A 1 80  ALA 80  115 115 ALA ALA A . n 
A 1 81  ALA 81  116 116 ALA ALA A . n 
A 1 82  GLY 82  117 117 GLY GLY A . n 
A 1 83  LEU 83  118 118 LEU LEU A . n 
A 1 84  PHE 84  119 119 PHE PHE A . n 
A 1 85  GLY 85  120 120 GLY GLY A . n 
A 1 86  PRO 86  121 121 PRO PRO A . n 
A 1 87  THR 87  122 122 THR THR A . n 
A 1 88  LEU 88  123 123 LEU LEU A . n 
A 1 89  GLY 89  124 124 GLY GLY A . n 
A 1 90  ARG 90  125 125 ARG ARG A . n 
A 1 91  LEU 91  126 126 LEU LEU A . n 
A 1 92  LEU 92  127 127 LEU LEU A . n 
A 1 93  ALA 93  128 128 ALA ALA A . n 
A 1 94  ASN 94  129 129 ASN ASN A . n 
A 1 95  LEU 95  130 130 LEU LEU A . n 
A 1 96  LYS 96  131 131 LYS LYS A . n 
A 1 97  ALA 97  132 132 ALA ALA A . n 
A 1 98  ALA 98  133 133 ALA ALA A . n 
A 1 99  GLY 99  134 134 GLY GLY A . n 
A 1 100 TYR 100 135 135 TYR TYR A . n 
A 1 101 GLN 101 136 136 GLN GLN A . n 
A 1 102 PRO 102 137 137 PRO PRO A . n 
A 1 103 GLU 103 138 138 GLU GLU A . n 
A 1 104 GLN 104 139 139 GLN GLN A . n 
A 1 105 VAL 105 140 140 VAL VAL A . n 
A 1 106 ASP 106 141 141 ASP ASP A . n 
A 1 107 GLU 107 142 142 GLU GLU A . n 
A 1 108 ILE 108 143 143 ILE ILE A . n 
A 1 109 TYR 109 144 144 TYR TYR A . n 
A 1 110 LEU 110 145 145 LEU LEU A . n 
A 1 111 THR 111 146 146 THR THR A . n 
A 1 112 HIS 112 147 147 HIS HIS A . n 
A 1 113 MET 113 148 148 MET MET A . n 
A 1 114 HIS 114 149 149 HIS HIS A . n 
A 1 115 PRO 115 150 150 PRO PRO A . n 
A 1 116 ASP 116 151 151 ASP ASP A . n 
A 1 117 HIS 117 152 152 HIS HIS A . n 
A 1 118 VAL 118 153 153 VAL VAL A . n 
A 1 119 GLY 119 154 154 GLY GLY A . n 
A 1 120 GLY 120 155 155 GLY GLY A . n 
A 1 121 LEU 121 156 156 LEU LEU A . n 
A 1 122 MET 122 157 157 MET MET A . n 
A 1 123 VAL 123 158 158 VAL VAL A . n 
A 1 124 GLY 124 159 159 GLY GLY A . n 
A 1 125 GLU 125 160 160 GLU GLU A . n 
A 1 126 GLN 126 161 161 GLN GLN A . n 
A 1 127 LEU 127 162 162 LEU LEU A . n 
A 1 128 ALA 128 163 163 ALA ALA A . n 
A 1 129 PHE 129 164 164 PHE PHE A . n 
A 1 130 PRO 130 165 165 PRO PRO A . n 
A 1 131 ASN 131 166 166 ASN ASN A . n 
A 1 132 ALA 132 167 167 ALA ALA A . n 
A 1 133 VAL 133 168 168 VAL VAL A . n 
A 1 134 VAL 134 169 169 VAL VAL A . n 
A 1 135 ARG 135 170 170 ARG ARG A . n 
A 1 136 ALA 136 171 171 ALA ALA A . n 
A 1 137 ASP 137 172 172 ASP ASP A . n 
A 1 138 GLN 138 173 173 GLN GLN A . n 
A 1 139 LYS 139 174 174 LYS LYS A . n 
A 1 140 GLU 140 175 175 GLU GLU A . n 
A 1 141 ALA 141 176 176 ALA ALA A . n 
A 1 142 ASP 142 177 177 ASP ASP A . n 
A 1 143 PHE 143 178 178 PHE PHE A . n 
A 1 144 TRP 144 179 179 TRP TRP A . n 
A 1 145 LEU 145 180 180 LEU LEU A . n 
A 1 146 SER 146 181 181 SER SER A . n 
A 1 147 GLN 147 182 182 GLN GLN A . n 
A 1 148 THR 148 183 183 THR THR A . n 
A 1 149 ASN 149 184 184 ASN ASN A . n 
A 1 150 LEU 150 185 185 LEU LEU A . n 
A 1 151 ASP 151 186 186 ASP ASP A . n 
A 1 152 LYS 152 187 187 LYS LYS A . n 
A 1 153 ALA 153 188 188 ALA ALA A . n 
A 1 154 PRO 154 189 189 PRO PRO A . n 
A 1 155 ASP 155 190 190 ASP ASP A . n 
A 1 156 ASP 156 191 191 ASP ASP A . n 
A 1 157 GLU 157 192 192 GLU GLU A . n 
A 1 158 SER 158 193 193 SER SER A . n 
A 1 159 LYS 159 194 194 LYS LYS A . n 
A 1 160 GLY 160 195 195 GLY GLY A . n 
A 1 161 PHE 161 196 196 PHE PHE A . n 
A 1 162 PHE 162 197 197 PHE PHE A . n 
A 1 163 LYS 163 198 198 LYS LYS A . n 
A 1 164 GLY 164 199 199 GLY GLY A . n 
A 1 165 ALA 165 200 200 ALA ALA A . n 
A 1 166 MET 166 201 201 MET MET A . n 
A 1 167 ALA 167 202 202 ALA ALA A . n 
A 1 168 SER 168 203 203 SER SER A . n 
A 1 169 LEU 169 204 204 LEU LEU A . n 
A 1 170 ASN 170 205 205 ASN ASN A . n 
A 1 171 PRO 171 206 206 PRO PRO A . n 
A 1 172 TYR 172 207 207 TYR TYR A . n 
A 1 173 VAL 173 208 208 VAL VAL A . n 
A 1 174 LYS 174 209 209 LYS LYS A . n 
A 1 175 ALA 175 210 210 ALA ALA A . n 
A 1 176 GLY 176 211 211 GLY GLY A . n 
A 1 177 LYS 177 212 212 LYS LYS A . n 
A 1 178 PHE 178 213 213 PHE PHE A . n 
A 1 179 LYS 179 214 214 LYS LYS A . n 
A 1 180 PRO 180 215 215 PRO PRO A . n 
A 1 181 PHE 181 216 216 PHE PHE A . n 
A 1 182 SER 182 217 217 SER SER A . n 
A 1 183 GLY 183 218 218 GLY GLY A . n 
A 1 184 ASN 184 219 219 ASN ASN A . n 
A 1 185 THR 185 220 220 THR THR A . n 
A 1 186 ASP 186 221 221 ASP ASP A . n 
A 1 187 LEU 187 222 222 LEU LEU A . n 
A 1 188 VAL 188 223 223 VAL VAL A . n 
A 1 189 PRO 189 224 224 PRO PRO A . n 
A 1 190 GLY 190 225 225 GLY GLY A . n 
A 1 191 ILE 191 226 226 ILE ILE A . n 
A 1 192 LYS 192 227 227 LYS LYS A . n 
A 1 193 ALA 193 228 228 ALA ALA A . n 
A 1 194 LEU 194 229 229 LEU LEU A . n 
A 1 195 ALA 195 230 230 ALA ALA A . n 
A 1 196 SER 196 231 231 SER SER A . n 
A 1 197 HIS 197 232 232 HIS HIS A . n 
A 1 198 GLY 198 233 233 GLY GLY A . n 
A 1 199 HIS 199 234 234 HIS HIS A . n 
A 1 200 THR 200 235 235 THR THR A . n 
A 1 201 PRO 201 236 236 PRO PRO A . n 
A 1 202 GLY 202 237 237 GLY GLY A . n 
A 1 203 HIS 203 238 238 HIS HIS A . n 
A 1 204 THR 204 239 239 THR THR A . n 
A 1 205 THR 205 240 240 THR THR A . n 
A 1 206 TYR 206 241 241 TYR TYR A . n 
A 1 207 VAL 207 242 242 VAL VAL A . n 
A 1 208 VAL 208 243 243 VAL VAL A . n 
A 1 209 GLU 209 244 244 GLU GLU A . n 
A 1 210 SER 210 245 245 SER SER A . n 
A 1 211 GLN 211 246 246 GLN GLN A . n 
A 1 212 GLY 212 247 247 GLY GLY A . n 
A 1 213 GLN 213 248 248 GLN GLN A . n 
A 1 214 LYS 214 249 249 LYS LYS A . n 
A 1 215 LEU 215 250 250 LEU LEU A . n 
A 1 216 ALA 216 251 251 ALA ALA A . n 
A 1 217 LEU 217 252 252 LEU LEU A . n 
A 1 218 LEU 218 253 253 LEU LEU A . n 
A 1 219 GLY 219 254 254 GLY GLY A . n 
A 1 220 ASP 220 255 255 ASP ASP A . n 
A 1 221 LEU 221 256 256 LEU LEU A . n 
A 1 222 ILE 222 257 257 ILE ILE A . n 
A 1 223 LEU 223 258 258 LEU LEU A . n 
A 1 224 VAL 224 259 259 VAL VAL A . n 
A 1 225 ALA 225 260 260 ALA ALA A . n 
A 1 226 ALA 226 261 261 ALA ALA A . n 
A 1 227 VAL 227 262 262 VAL VAL A . n 
A 1 228 GLN 228 263 263 GLN GLN A . n 
A 1 229 PHE 229 264 264 PHE PHE A . n 
A 1 230 ASP 230 265 265 ASP ASP A . n 
A 1 231 ASP 231 266 266 ASP ASP A . n 
A 1 232 PRO 232 267 267 PRO PRO A . n 
A 1 233 SER 233 268 268 SER SER A . n 
A 1 234 VAL 234 269 269 VAL VAL A . n 
A 1 235 THR 235 270 270 THR THR A . n 
A 1 236 THR 236 271 271 THR THR A . n 
A 1 237 ASP 237 272 272 ASP ASP A . n 
A 1 238 LEU 238 273 273 LEU LEU A . n 
A 1 239 ASP 239 274 274 ASP ASP A . n 
A 1 240 SER 240 275 275 SER SER A . n 
A 1 241 ASP 241 276 276 ASP ASP A . n 
A 1 242 SER 242 277 277 SER SER A . n 
A 1 243 LYS 243 278 278 LYS LYS A . n 
A 1 244 ALA 244 279 279 ALA ALA A . n 
A 1 245 VAL 245 280 280 VAL VAL A . n 
A 1 246 ALA 246 281 281 ALA ALA A . n 
A 1 247 VAL 247 282 282 VAL VAL A . n 
A 1 248 GLU 248 283 283 GLU GLU A . n 
A 1 249 ARG 249 284 284 ARG ARG A . n 
A 1 250 LYS 250 285 285 LYS LYS A . n 
A 1 251 LYS 251 286 286 LYS LYS A . n 
A 1 252 ALA 252 287 287 ALA ALA A . n 
A 1 253 PHE 253 288 288 PHE PHE A . n 
A 1 254 ALA 254 289 289 ALA ALA A . n 
A 1 255 ASP 255 290 290 ASP ASP A . n 
A 1 256 ALA 256 291 291 ALA ALA A . n 
A 1 257 ALA 257 292 292 ALA ALA A . n 
A 1 258 LYS 258 293 293 LYS LYS A . n 
A 1 259 GLY 259 294 294 GLY GLY A . n 
A 1 260 GLY 260 295 295 GLY GLY A . n 
A 1 261 TYR 261 296 296 TYR TYR A . n 
A 1 262 LEU 262 297 297 LEU LEU A . n 
A 1 263 ILE 263 298 298 ILE ILE A . n 
A 1 264 ALA 264 299 299 ALA ALA A . n 
A 1 265 ALA 265 300 300 ALA ALA A . n 
A 1 266 SER 266 301 301 SER SER A . n 
A 1 267 HIS 267 302 302 HIS HIS A . n 
A 1 268 LEU 268 303 303 LEU LEU A . n 
A 1 269 PRO 269 304 304 PRO PRO A . n 
A 1 270 PHE 270 305 305 PHE PHE A . n 
A 1 271 PRO 271 306 306 PRO PRO A . n 
A 1 272 GLY 272 307 307 GLY GLY A . n 
A 1 273 ILE 273 308 308 ILE ILE A . n 
A 1 274 GLY 274 309 309 GLY GLY A . n 
A 1 275 HIS 275 310 310 HIS HIS A . n 
A 1 276 ILE 276 311 311 ILE ILE A . n 
A 1 277 ARG 277 312 312 ARG ARG A . n 
A 1 278 ALA 278 313 313 ALA ALA A . n 
A 1 279 GLU 279 314 314 GLU GLU A . n 
A 1 280 GLY 280 315 315 GLY GLY A . n 
A 1 281 LYS 281 316 316 LYS LYS A . n 
A 1 282 GLY 282 317 317 GLY GLY A . n 
A 1 283 TYR 283 318 318 TYR TYR A . n 
A 1 284 ARG 284 319 319 ARG ARG A . n 
A 1 285 PHE 285 320 320 PHE PHE A . n 
A 1 286 VAL 286 321 321 VAL VAL A . n 
A 1 287 PRO 287 322 322 PRO PRO A . n 
A 1 288 VAL 288 323 323 VAL VAL A . n 
A 1 289 ASN 289 324 324 ASN ASN A . n 
A 1 290 TYR 290 325 325 TYR TYR A . n 
A 1 291 SER 291 326 326 SER SER A . n 
A 1 292 VAL 292 327 327 VAL VAL A . n 
A 1 293 VAL 293 328 328 VAL VAL A . n 
A 1 294 ASN 294 329 329 ASN ASN A . n 
A 1 295 ALA 295 330 ?   ?   ?   A . n 
A 1 296 ALA 296 331 ?   ?   ?   A . n 
B 1 1   ALA 1   36  36  ALA ALA B . n 
B 1 2   ALA 2   37  37  ALA ALA B . n 
B 1 3   PRO 3   38  38  PRO PRO B . n 
B 1 4   GLN 4   39  39  GLN GLN B . n 
B 1 5   VAL 5   40  40  VAL VAL B . n 
B 1 6   ARG 6   41  41  ARG ARG B . n 
B 1 7   THR 7   42  42  THR THR B . n 
B 1 8   SER 8   43  43  SER SER B . n 
B 1 9   ALA 9   44  44  ALA ALA B . n 
B 1 10  PRO 10  45  45  PRO PRO B . n 
B 1 11  GLY 11  46  46  GLY GLY B . n 
B 1 12  TYR 12  47  47  TYR TYR B . n 
B 1 13  TYR 13  48  48  TYR TYR B . n 
B 1 14  ARG 14  49  49  ARG ARG B . n 
B 1 15  MET 15  50  50  MET MET B . n 
B 1 16  LEU 16  51  51  LEU LEU B . n 
B 1 17  LEU 17  52  52  LEU LEU B . n 
B 1 18  GLY 18  53  53  GLY GLY B . n 
B 1 19  ASP 19  54  54  ASP ASP B . n 
B 1 20  PHE 20  55  55  PHE PHE B . n 
B 1 21  GLU 21  56  56  GLU GLU B . n 
B 1 22  ILE 22  57  57  ILE ILE B . n 
B 1 23  THR 23  58  58  THR THR B . n 
B 1 24  ALA 24  59  59  ALA ALA B . n 
B 1 25  LEU 25  60  60  LEU LEU B . n 
B 1 26  SER 26  61  61  SER SER B . n 
B 1 27  ASP 27  62  62  ASP ASP B . n 
B 1 28  GLY 28  63  63  GLY GLY B . n 
B 1 29  THR 29  64  64  THR THR B . n 
B 1 30  VAL 30  65  65  VAL VAL B . n 
B 1 31  ALA 31  66  66  ALA ALA B . n 
B 1 32  LEU 32  67  67  LEU LEU B . n 
B 1 33  PRO 33  68  68  PRO PRO B . n 
B 1 34  VAL 34  69  69  VAL VAL B . n 
B 1 35  ASP 35  70  70  ASP ASP B . n 
B 1 36  LYS 36  71  71  LYS LYS B . n 
B 1 37  ARG 37  72  72  ARG ARG B . n 
B 1 38  LEU 38  73  73  LEU LEU B . n 
B 1 39  ASN 39  74  74  ASN ASN B . n 
B 1 40  GLN 40  75  75  GLN GLN B . n 
B 1 41  PRO 41  76  76  PRO PRO B . n 
B 1 42  ALA 42  77  77  ALA ALA B . n 
B 1 43  PRO 43  78  78  PRO PRO B . n 
B 1 44  LYS 44  79  79  LYS LYS B . n 
B 1 45  THR 45  80  80  THR THR B . n 
B 1 46  GLN 46  81  81  GLN GLN B . n 
B 1 47  SER 47  82  82  SER SER B . n 
B 1 48  ALA 48  83  83  ALA ALA B . n 
B 1 49  LEU 49  84  84  LEU LEU B . n 
B 1 50  ALA 50  85  85  ALA ALA B . n 
B 1 51  LYS 51  86  86  LYS LYS B . n 
B 1 52  SER 52  87  87  SER SER B . n 
B 1 53  PHE 53  88  88  PHE PHE B . n 
B 1 54  GLN 54  89  89  GLN GLN B . n 
B 1 55  LYS 55  90  90  LYS LYS B . n 
B 1 56  ALA 56  91  91  ALA ALA B . n 
B 1 57  PRO 57  92  92  PRO PRO B . n 
B 1 58  LEU 58  93  93  LEU LEU B . n 
B 1 59  GLU 59  94  94  GLU GLU B . n 
B 1 60  THR 60  95  95  THR THR B . n 
B 1 61  SER 61  96  96  SER SER B . n 
B 1 62  VAL 62  97  97  VAL VAL B . n 
B 1 63  THR 63  98  98  THR THR B . n 
B 1 64  GLY 64  99  99  GLY GLY B . n 
B 1 65  TYR 65  100 100 TYR TYR B . n 
B 1 66  LEU 66  101 101 LEU LEU B . n 
B 1 67  VAL 67  102 102 VAL VAL B . n 
B 1 68  ASN 68  103 103 ASN ASN B . n 
B 1 69  THR 69  104 104 THR THR B . n 
B 1 70  GLY 70  105 105 GLY GLY B . n 
B 1 71  SER 71  106 106 SER SER B . n 
B 1 72  LYS 72  107 107 LYS LYS B . n 
B 1 73  LEU 73  108 108 LEU LEU B . n 
B 1 74  VAL 74  109 109 VAL VAL B . n 
B 1 75  LEU 75  110 110 LEU LEU B . n 
B 1 76  VAL 76  111 111 VAL VAL B . n 
B 1 77  ASP 77  112 112 ASP ASP B . n 
B 1 78  THR 78  113 113 THR THR B . n 
B 1 79  GLY 79  114 114 GLY GLY B . n 
B 1 80  ALA 80  115 115 ALA ALA B . n 
B 1 81  ALA 81  116 116 ALA ALA B . n 
B 1 82  GLY 82  117 117 GLY GLY B . n 
B 1 83  LEU 83  118 118 LEU LEU B . n 
B 1 84  PHE 84  119 119 PHE PHE B . n 
B 1 85  GLY 85  120 120 GLY GLY B . n 
B 1 86  PRO 86  121 121 PRO PRO B . n 
B 1 87  THR 87  122 122 THR THR B . n 
B 1 88  LEU 88  123 123 LEU LEU B . n 
B 1 89  GLY 89  124 124 GLY GLY B . n 
B 1 90  ARG 90  125 125 ARG ARG B . n 
B 1 91  LEU 91  126 126 LEU LEU B . n 
B 1 92  LEU 92  127 127 LEU LEU B . n 
B 1 93  ALA 93  128 128 ALA ALA B . n 
B 1 94  ASN 94  129 129 ASN ASN B . n 
B 1 95  LEU 95  130 130 LEU LEU B . n 
B 1 96  LYS 96  131 131 LYS LYS B . n 
B 1 97  ALA 97  132 132 ALA ALA B . n 
B 1 98  ALA 98  133 133 ALA ALA B . n 
B 1 99  GLY 99  134 134 GLY GLY B . n 
B 1 100 TYR 100 135 135 TYR TYR B . n 
B 1 101 GLN 101 136 136 GLN GLN B . n 
B 1 102 PRO 102 137 137 PRO PRO B . n 
B 1 103 GLU 103 138 138 GLU GLU B . n 
B 1 104 GLN 104 139 139 GLN GLN B . n 
B 1 105 VAL 105 140 140 VAL VAL B . n 
B 1 106 ASP 106 141 141 ASP ASP B . n 
B 1 107 GLU 107 142 142 GLU GLU B . n 
B 1 108 ILE 108 143 143 ILE ILE B . n 
B 1 109 TYR 109 144 144 TYR TYR B . n 
B 1 110 LEU 110 145 145 LEU LEU B . n 
B 1 111 THR 111 146 146 THR THR B . n 
B 1 112 HIS 112 147 147 HIS HIS B . n 
B 1 113 MET 113 148 148 MET MET B . n 
B 1 114 HIS 114 149 149 HIS HIS B . n 
B 1 115 PRO 115 150 150 PRO PRO B . n 
B 1 116 ASP 116 151 151 ASP ASP B . n 
B 1 117 HIS 117 152 152 HIS HIS B . n 
B 1 118 VAL 118 153 153 VAL VAL B . n 
B 1 119 GLY 119 154 154 GLY GLY B . n 
B 1 120 GLY 120 155 155 GLY GLY B . n 
B 1 121 LEU 121 156 156 LEU LEU B . n 
B 1 122 MET 122 157 157 MET MET B . n 
B 1 123 VAL 123 158 158 VAL VAL B . n 
B 1 124 GLY 124 159 159 GLY GLY B . n 
B 1 125 GLU 125 160 160 GLU GLU B . n 
B 1 126 GLN 126 161 161 GLN GLN B . n 
B 1 127 LEU 127 162 162 LEU LEU B . n 
B 1 128 ALA 128 163 163 ALA ALA B . n 
B 1 129 PHE 129 164 164 PHE PHE B . n 
B 1 130 PRO 130 165 165 PRO PRO B . n 
B 1 131 ASN 131 166 166 ASN ASN B . n 
B 1 132 ALA 132 167 167 ALA ALA B . n 
B 1 133 VAL 133 168 168 VAL VAL B . n 
B 1 134 VAL 134 169 169 VAL VAL B . n 
B 1 135 ARG 135 170 170 ARG ARG B . n 
B 1 136 ALA 136 171 171 ALA ALA B . n 
B 1 137 ASP 137 172 172 ASP ASP B . n 
B 1 138 GLN 138 173 173 GLN GLN B . n 
B 1 139 LYS 139 174 174 LYS LYS B . n 
B 1 140 GLU 140 175 175 GLU GLU B . n 
B 1 141 ALA 141 176 176 ALA ALA B . n 
B 1 142 ASP 142 177 177 ASP ASP B . n 
B 1 143 PHE 143 178 178 PHE PHE B . n 
B 1 144 TRP 144 179 179 TRP TRP B . n 
B 1 145 LEU 145 180 180 LEU LEU B . n 
B 1 146 SER 146 181 181 SER SER B . n 
B 1 147 GLN 147 182 182 GLN GLN B . n 
B 1 148 THR 148 183 183 THR THR B . n 
B 1 149 ASN 149 184 184 ASN ASN B . n 
B 1 150 LEU 150 185 185 LEU LEU B . n 
B 1 151 ASP 151 186 186 ASP ASP B . n 
B 1 152 LYS 152 187 187 LYS LYS B . n 
B 1 153 ALA 153 188 188 ALA ALA B . n 
B 1 154 PRO 154 189 189 PRO PRO B . n 
B 1 155 ASP 155 190 190 ASP ASP B . n 
B 1 156 ASP 156 191 191 ASP ASP B . n 
B 1 157 GLU 157 192 192 GLU GLU B . n 
B 1 158 SER 158 193 193 SER SER B . n 
B 1 159 LYS 159 194 194 LYS LYS B . n 
B 1 160 GLY 160 195 195 GLY GLY B . n 
B 1 161 PHE 161 196 196 PHE PHE B . n 
B 1 162 PHE 162 197 197 PHE PHE B . n 
B 1 163 LYS 163 198 198 LYS LYS B . n 
B 1 164 GLY 164 199 199 GLY GLY B . n 
B 1 165 ALA 165 200 200 ALA ALA B . n 
B 1 166 MET 166 201 201 MET MET B . n 
B 1 167 ALA 167 202 202 ALA ALA B . n 
B 1 168 SER 168 203 203 SER SER B . n 
B 1 169 LEU 169 204 204 LEU LEU B . n 
B 1 170 ASN 170 205 205 ASN ASN B . n 
B 1 171 PRO 171 206 206 PRO PRO B . n 
B 1 172 TYR 172 207 207 TYR TYR B . n 
B 1 173 VAL 173 208 208 VAL VAL B . n 
B 1 174 LYS 174 209 209 LYS LYS B . n 
B 1 175 ALA 175 210 210 ALA ALA B . n 
B 1 176 GLY 176 211 211 GLY GLY B . n 
B 1 177 LYS 177 212 212 LYS LYS B . n 
B 1 178 PHE 178 213 213 PHE PHE B . n 
B 1 179 LYS 179 214 214 LYS LYS B . n 
B 1 180 PRO 180 215 215 PRO PRO B . n 
B 1 181 PHE 181 216 216 PHE PHE B . n 
B 1 182 SER 182 217 217 SER SER B . n 
B 1 183 GLY 183 218 218 GLY GLY B . n 
B 1 184 ASN 184 219 219 ASN ASN B . n 
B 1 185 THR 185 220 220 THR THR B . n 
B 1 186 ASP 186 221 221 ASP ASP B . n 
B 1 187 LEU 187 222 222 LEU LEU B . n 
B 1 188 VAL 188 223 223 VAL VAL B . n 
B 1 189 PRO 189 224 224 PRO PRO B . n 
B 1 190 GLY 190 225 225 GLY GLY B . n 
B 1 191 ILE 191 226 226 ILE ILE B . n 
B 1 192 LYS 192 227 227 LYS LYS B . n 
B 1 193 ALA 193 228 228 ALA ALA B . n 
B 1 194 LEU 194 229 229 LEU LEU B . n 
B 1 195 ALA 195 230 230 ALA ALA B . n 
B 1 196 SER 196 231 231 SER SER B . n 
B 1 197 HIS 197 232 232 HIS HIS B . n 
B 1 198 GLY 198 233 233 GLY GLY B . n 
B 1 199 HIS 199 234 234 HIS HIS B . n 
B 1 200 THR 200 235 235 THR THR B . n 
B 1 201 PRO 201 236 236 PRO PRO B . n 
B 1 202 GLY 202 237 237 GLY GLY B . n 
B 1 203 HIS 203 238 238 HIS HIS B . n 
B 1 204 THR 204 239 239 THR THR B . n 
B 1 205 THR 205 240 240 THR THR B . n 
B 1 206 TYR 206 241 241 TYR TYR B . n 
B 1 207 VAL 207 242 242 VAL VAL B . n 
B 1 208 VAL 208 243 243 VAL VAL B . n 
B 1 209 GLU 209 244 244 GLU GLU B . n 
B 1 210 SER 210 245 245 SER SER B . n 
B 1 211 GLN 211 246 246 GLN GLN B . n 
B 1 212 GLY 212 247 247 GLY GLY B . n 
B 1 213 GLN 213 248 248 GLN GLN B . n 
B 1 214 LYS 214 249 249 LYS LYS B . n 
B 1 215 LEU 215 250 250 LEU LEU B . n 
B 1 216 ALA 216 251 251 ALA ALA B . n 
B 1 217 LEU 217 252 252 LEU LEU B . n 
B 1 218 LEU 218 253 253 LEU LEU B . n 
B 1 219 GLY 219 254 254 GLY GLY B . n 
B 1 220 ASP 220 255 255 ASP ASP B . n 
B 1 221 LEU 221 256 256 LEU LEU B . n 
B 1 222 ILE 222 257 257 ILE ILE B . n 
B 1 223 LEU 223 258 258 LEU LEU B . n 
B 1 224 VAL 224 259 259 VAL VAL B . n 
B 1 225 ALA 225 260 260 ALA ALA B . n 
B 1 226 ALA 226 261 261 ALA ALA B . n 
B 1 227 VAL 227 262 262 VAL VAL B . n 
B 1 228 GLN 228 263 263 GLN GLN B . n 
B 1 229 PHE 229 264 264 PHE PHE B . n 
B 1 230 ASP 230 265 265 ASP ASP B . n 
B 1 231 ASP 231 266 266 ASP ASP B . n 
B 1 232 PRO 232 267 267 PRO PRO B . n 
B 1 233 SER 233 268 268 SER SER B . n 
B 1 234 VAL 234 269 269 VAL VAL B . n 
B 1 235 THR 235 270 270 THR THR B . n 
B 1 236 THR 236 271 271 THR THR B . n 
B 1 237 ASP 237 272 272 ASP ASP B . n 
B 1 238 LEU 238 273 273 LEU LEU B . n 
B 1 239 ASP 239 274 274 ASP ASP B . n 
B 1 240 SER 240 275 275 SER SER B . n 
B 1 241 ASP 241 276 276 ASP ASP B . n 
B 1 242 SER 242 277 277 SER SER B . n 
B 1 243 LYS 243 278 278 LYS LYS B . n 
B 1 244 ALA 244 279 279 ALA ALA B . n 
B 1 245 VAL 245 280 280 VAL VAL B . n 
B 1 246 ALA 246 281 281 ALA ALA B . n 
B 1 247 VAL 247 282 282 VAL VAL B . n 
B 1 248 GLU 248 283 283 GLU GLU B . n 
B 1 249 ARG 249 284 284 ARG ARG B . n 
B 1 250 LYS 250 285 285 LYS LYS B . n 
B 1 251 LYS 251 286 286 LYS LYS B . n 
B 1 252 ALA 252 287 287 ALA ALA B . n 
B 1 253 PHE 253 288 288 PHE PHE B . n 
B 1 254 ALA 254 289 289 ALA ALA B . n 
B 1 255 ASP 255 290 290 ASP ASP B . n 
B 1 256 ALA 256 291 291 ALA ALA B . n 
B 1 257 ALA 257 292 292 ALA ALA B . n 
B 1 258 LYS 258 293 293 LYS LYS B . n 
B 1 259 GLY 259 294 294 GLY GLY B . n 
B 1 260 GLY 260 295 295 GLY GLY B . n 
B 1 261 TYR 261 296 296 TYR TYR B . n 
B 1 262 LEU 262 297 297 LEU LEU B . n 
B 1 263 ILE 263 298 298 ILE ILE B . n 
B 1 264 ALA 264 299 299 ALA ALA B . n 
B 1 265 ALA 265 300 300 ALA ALA B . n 
B 1 266 SER 266 301 301 SER SER B . n 
B 1 267 HIS 267 302 302 HIS HIS B . n 
B 1 268 LEU 268 303 303 LEU LEU B . n 
B 1 269 PRO 269 304 304 PRO PRO B . n 
B 1 270 PHE 270 305 305 PHE PHE B . n 
B 1 271 PRO 271 306 306 PRO PRO B . n 
B 1 272 GLY 272 307 307 GLY GLY B . n 
B 1 273 ILE 273 308 308 ILE ILE B . n 
B 1 274 GLY 274 309 309 GLY GLY B . n 
B 1 275 HIS 275 310 310 HIS HIS B . n 
B 1 276 ILE 276 311 311 ILE ILE B . n 
B 1 277 ARG 277 312 312 ARG ARG B . n 
B 1 278 ALA 278 313 313 ALA ALA B . n 
B 1 279 GLU 279 314 314 GLU GLU B . n 
B 1 280 GLY 280 315 315 GLY GLY B . n 
B 1 281 LYS 281 316 316 LYS LYS B . n 
B 1 282 GLY 282 317 317 GLY GLY B . n 
B 1 283 TYR 283 318 318 TYR TYR B . n 
B 1 284 ARG 284 319 319 ARG ARG B . n 
B 1 285 PHE 285 320 320 PHE PHE B . n 
B 1 286 VAL 286 321 321 VAL VAL B . n 
B 1 287 PRO 287 322 322 PRO PRO B . n 
B 1 288 VAL 288 323 323 VAL VAL B . n 
B 1 289 ASN 289 324 324 ASN ASN B . n 
B 1 290 TYR 290 325 325 TYR TYR B . n 
B 1 291 SER 291 326 326 SER SER B . n 
B 1 292 VAL 292 327 327 VAL VAL B . n 
B 1 293 VAL 293 328 328 VAL VAL B . n 
B 1 294 ASN 294 329 329 ASN ASN B . n 
B 1 295 ALA 295 330 330 ALA ALA B . n 
B 1 296 ALA 296 331 331 ALA ALA B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        ZN 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   ZN 
_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 ZN  1   401 3   ZN  ZN  A . 
D 2 ZN  1   402 4   ZN  ZN  A . 
E 2 ZN  1   401 1   ZN  ZN  B . 
F 2 ZN  1   402 2   ZN  ZN  B . 
G 3 HOH 1   501 535 HOH HOH A . 
G 3 HOH 2   502 524 HOH HOH A . 
G 3 HOH 3   503 320 HOH HOH A . 
G 3 HOH 4   504 569 HOH HOH A . 
G 3 HOH 5   505 333 HOH HOH A . 
G 3 HOH 6   506 522 HOH HOH A . 
G 3 HOH 7   507 43  HOH HOH A . 
G 3 HOH 8   508 281 HOH HOH A . 
G 3 HOH 9   509 291 HOH HOH A . 
G 3 HOH 10  510 62  HOH HOH A . 
G 3 HOH 11  511 69  HOH HOH A . 
G 3 HOH 12  512 201 HOH HOH A . 
G 3 HOH 13  513 10  HOH HOH A . 
G 3 HOH 14  514 146 HOH HOH A . 
G 3 HOH 15  515 52  HOH HOH A . 
G 3 HOH 16  516 149 HOH HOH A . 
G 3 HOH 17  517 317 HOH HOH A . 
G 3 HOH 18  518 116 HOH HOH A . 
G 3 HOH 19  519 182 HOH HOH A . 
G 3 HOH 20  520 305 HOH HOH A . 
G 3 HOH 21  521 270 HOH HOH A . 
G 3 HOH 22  522 29  HOH HOH A . 
G 3 HOH 23  523 229 HOH HOH A . 
G 3 HOH 24  524 169 HOH HOH A . 
G 3 HOH 25  525 85  HOH HOH A . 
G 3 HOH 26  526 322 HOH HOH A . 
G 3 HOH 27  527 511 HOH HOH A . 
G 3 HOH 28  528 277 HOH HOH A . 
G 3 HOH 29  529 3   HOH HOH A . 
G 3 HOH 30  530 32  HOH HOH A . 
G 3 HOH 31  531 35  HOH HOH A . 
G 3 HOH 32  532 92  HOH HOH A . 
G 3 HOH 33  533 274 HOH HOH A . 
G 3 HOH 34  534 618 HOH HOH A . 
G 3 HOH 35  535 444 HOH HOH A . 
G 3 HOH 36  536 599 HOH HOH A . 
G 3 HOH 37  537 213 HOH HOH A . 
G 3 HOH 38  538 25  HOH HOH A . 
G 3 HOH 39  539 411 HOH HOH A . 
G 3 HOH 40  540 525 HOH HOH A . 
G 3 HOH 41  541 8   HOH HOH A . 
G 3 HOH 42  542 397 HOH HOH A . 
G 3 HOH 43  543 300 HOH HOH A . 
G 3 HOH 44  544 20  HOH HOH A . 
G 3 HOH 45  545 353 HOH HOH A . 
G 3 HOH 46  546 414 HOH HOH A . 
G 3 HOH 47  547 79  HOH HOH A . 
G 3 HOH 48  548 207 HOH HOH A . 
G 3 HOH 49  549 15  HOH HOH A . 
G 3 HOH 50  550 555 HOH HOH A . 
G 3 HOH 51  551 243 HOH HOH A . 
G 3 HOH 52  552 128 HOH HOH A . 
G 3 HOH 53  553 60  HOH HOH A . 
G 3 HOH 54  554 71  HOH HOH A . 
G 3 HOH 55  555 119 HOH HOH A . 
G 3 HOH 56  556 600 HOH HOH A . 
G 3 HOH 57  557 319 HOH HOH A . 
G 3 HOH 58  558 87  HOH HOH A . 
G 3 HOH 59  559 218 HOH HOH A . 
G 3 HOH 60  560 633 HOH HOH A . 
G 3 HOH 61  561 308 HOH HOH A . 
G 3 HOH 62  562 130 HOH HOH A . 
G 3 HOH 63  563 163 HOH HOH A . 
G 3 HOH 64  564 358 HOH HOH A . 
G 3 HOH 65  565 19  HOH HOH A . 
G 3 HOH 66  566 481 HOH HOH A . 
G 3 HOH 67  567 225 HOH HOH A . 
G 3 HOH 68  568 49  HOH HOH A . 
G 3 HOH 69  569 118 HOH HOH A . 
G 3 HOH 70  570 24  HOH HOH A . 
G 3 HOH 71  571 39  HOH HOH A . 
G 3 HOH 72  572 267 HOH HOH A . 
G 3 HOH 73  573 38  HOH HOH A . 
G 3 HOH 74  574 257 HOH HOH A . 
G 3 HOH 75  575 276 HOH HOH A . 
G 3 HOH 76  576 140 HOH HOH A . 
G 3 HOH 77  577 162 HOH HOH A . 
G 3 HOH 78  578 637 HOH HOH A . 
G 3 HOH 79  579 184 HOH HOH A . 
G 3 HOH 80  580 160 HOH HOH A . 
G 3 HOH 81  581 167 HOH HOH A . 
G 3 HOH 82  582 41  HOH HOH A . 
G 3 HOH 83  583 268 HOH HOH A . 
G 3 HOH 84  584 68  HOH HOH A . 
G 3 HOH 85  585 495 HOH HOH A . 
G 3 HOH 86  586 42  HOH HOH A . 
G 3 HOH 87  587 13  HOH HOH A . 
G 3 HOH 88  588 279 HOH HOH A . 
G 3 HOH 89  589 143 HOH HOH A . 
G 3 HOH 90  590 490 HOH HOH A . 
G 3 HOH 91  591 461 HOH HOH A . 
G 3 HOH 92  592 570 HOH HOH A . 
G 3 HOH 93  593 101 HOH HOH A . 
G 3 HOH 94  594 2   HOH HOH A . 
G 3 HOH 95  595 232 HOH HOH A . 
G 3 HOH 96  596 37  HOH HOH A . 
G 3 HOH 97  597 192 HOH HOH A . 
G 3 HOH 98  598 242 HOH HOH A . 
G 3 HOH 99  599 75  HOH HOH A . 
G 3 HOH 100 600 94  HOH HOH A . 
G 3 HOH 101 601 523 HOH HOH A . 
G 3 HOH 102 602 64  HOH HOH A . 
G 3 HOH 103 603 260 HOH HOH A . 
G 3 HOH 104 604 328 HOH HOH A . 
G 3 HOH 105 605 100 HOH HOH A . 
G 3 HOH 106 606 95  HOH HOH A . 
G 3 HOH 107 607 208 HOH HOH A . 
G 3 HOH 108 608 346 HOH HOH A . 
G 3 HOH 109 609 152 HOH HOH A . 
G 3 HOH 110 610 125 HOH HOH A . 
G 3 HOH 111 611 398 HOH HOH A . 
G 3 HOH 112 612 111 HOH HOH A . 
G 3 HOH 113 613 298 HOH HOH A . 
G 3 HOH 114 614 17  HOH HOH A . 
G 3 HOH 115 615 253 HOH HOH A . 
G 3 HOH 116 616 141 HOH HOH A . 
G 3 HOH 117 617 402 HOH HOH A . 
G 3 HOH 118 618 613 HOH HOH A . 
G 3 HOH 119 619 482 HOH HOH A . 
G 3 HOH 120 620 86  HOH HOH A . 
G 3 HOH 121 621 587 HOH HOH A . 
G 3 HOH 122 622 90  HOH HOH A . 
G 3 HOH 123 623 51  HOH HOH A . 
G 3 HOH 124 624 81  HOH HOH A . 
G 3 HOH 125 625 131 HOH HOH A . 
G 3 HOH 126 626 154 HOH HOH A . 
G 3 HOH 127 627 389 HOH HOH A . 
G 3 HOH 128 628 105 HOH HOH A . 
G 3 HOH 129 629 99  HOH HOH A . 
G 3 HOH 130 630 202 HOH HOH A . 
G 3 HOH 131 631 165 HOH HOH A . 
G 3 HOH 132 632 9   HOH HOH A . 
G 3 HOH 133 633 36  HOH HOH A . 
G 3 HOH 134 634 399 HOH HOH A . 
G 3 HOH 135 635 404 HOH HOH A . 
G 3 HOH 136 636 493 HOH HOH A . 
G 3 HOH 137 637 164 HOH HOH A . 
G 3 HOH 138 638 65  HOH HOH A . 
G 3 HOH 139 639 321 HOH HOH A . 
G 3 HOH 140 640 497 HOH HOH A . 
G 3 HOH 141 641 246 HOH HOH A . 
G 3 HOH 142 642 567 HOH HOH A . 
G 3 HOH 143 643 77  HOH HOH A . 
G 3 HOH 144 644 293 HOH HOH A . 
G 3 HOH 145 645 485 HOH HOH A . 
G 3 HOH 146 646 409 HOH HOH A . 
G 3 HOH 147 647 214 HOH HOH A . 
G 3 HOH 148 648 528 HOH HOH A . 
G 3 HOH 149 649 104 HOH HOH A . 
G 3 HOH 150 650 367 HOH HOH A . 
G 3 HOH 151 651 97  HOH HOH A . 
G 3 HOH 152 652 48  HOH HOH A . 
G 3 HOH 153 653 350 HOH HOH A . 
G 3 HOH 154 654 586 HOH HOH A . 
G 3 HOH 155 655 311 HOH HOH A . 
G 3 HOH 156 656 132 HOH HOH A . 
G 3 HOH 157 657 520 HOH HOH A . 
G 3 HOH 158 658 83  HOH HOH A . 
G 3 HOH 159 659 630 HOH HOH A . 
G 3 HOH 160 660 195 HOH HOH A . 
G 3 HOH 161 661 391 HOH HOH A . 
G 3 HOH 162 662 590 HOH HOH A . 
G 3 HOH 163 663 378 HOH HOH A . 
G 3 HOH 164 664 473 HOH HOH A . 
G 3 HOH 165 665 428 HOH HOH A . 
G 3 HOH 166 666 190 HOH HOH A . 
G 3 HOH 167 667 174 HOH HOH A . 
G 3 HOH 168 668 579 HOH HOH A . 
G 3 HOH 169 669 484 HOH HOH A . 
G 3 HOH 170 670 26  HOH HOH A . 
G 3 HOH 171 671 186 HOH HOH A . 
G 3 HOH 172 672 194 HOH HOH A . 
G 3 HOH 173 673 72  HOH HOH A . 
G 3 HOH 174 674 502 HOH HOH A . 
G 3 HOH 175 675 228 HOH HOH A . 
G 3 HOH 176 676 187 HOH HOH A . 
G 3 HOH 177 677 203 HOH HOH A . 
G 3 HOH 178 678 4   HOH HOH A . 
G 3 HOH 179 679 406 HOH HOH A . 
G 3 HOH 180 680 639 HOH HOH A . 
G 3 HOH 181 681 33  HOH HOH A . 
G 3 HOH 182 682 244 HOH HOH A . 
G 3 HOH 183 683 576 HOH HOH A . 
G 3 HOH 184 684 334 HOH HOH A . 
G 3 HOH 185 685 142 HOH HOH A . 
G 3 HOH 186 686 258 HOH HOH A . 
G 3 HOH 187 687 498 HOH HOH A . 
G 3 HOH 188 688 120 HOH HOH A . 
G 3 HOH 189 689 46  HOH HOH A . 
G 3 HOH 190 690 374 HOH HOH A . 
G 3 HOH 191 691 610 HOH HOH A . 
G 3 HOH 192 692 575 HOH HOH A . 
G 3 HOH 193 693 316 HOH HOH A . 
G 3 HOH 194 694 508 HOH HOH A . 
G 3 HOH 195 695 539 HOH HOH A . 
G 3 HOH 196 696 611 HOH HOH A . 
G 3 HOH 197 697 185 HOH HOH A . 
G 3 HOH 198 698 464 HOH HOH A . 
G 3 HOH 199 699 429 HOH HOH A . 
G 3 HOH 200 700 452 HOH HOH A . 
G 3 HOH 201 701 66  HOH HOH A . 
G 3 HOH 202 702 640 HOH HOH A . 
G 3 HOH 203 703 425 HOH HOH A . 
G 3 HOH 204 704 480 HOH HOH A . 
G 3 HOH 205 705 136 HOH HOH A . 
G 3 HOH 206 706 289 HOH HOH A . 
G 3 HOH 207 707 561 HOH HOH A . 
G 3 HOH 208 708 431 HOH HOH A . 
G 3 HOH 209 709 466 HOH HOH A . 
G 3 HOH 210 710 325 HOH HOH A . 
G 3 HOH 211 711 197 HOH HOH A . 
G 3 HOH 212 712 518 HOH HOH A . 
G 3 HOH 213 713 440 HOH HOH A . 
G 3 HOH 214 714 50  HOH HOH A . 
G 3 HOH 215 715 443 HOH HOH A . 
G 3 HOH 216 716 280 HOH HOH A . 
G 3 HOH 217 717 499 HOH HOH A . 
G 3 HOH 218 718 631 HOH HOH A . 
G 3 HOH 219 719 468 HOH HOH A . 
G 3 HOH 220 720 364 HOH HOH A . 
G 3 HOH 221 721 565 HOH HOH A . 
G 3 HOH 222 722 357 HOH HOH A . 
G 3 HOH 223 723 492 HOH HOH A . 
G 3 HOH 224 724 560 HOH HOH A . 
G 3 HOH 225 725 577 HOH HOH A . 
G 3 HOH 226 726 427 HOH HOH A . 
G 3 HOH 227 727 392 HOH HOH A . 
G 3 HOH 228 728 478 HOH HOH A . 
G 3 HOH 229 729 542 HOH HOH A . 
G 3 HOH 230 730 477 HOH HOH A . 
G 3 HOH 231 731 259 HOH HOH A . 
G 3 HOH 232 732 607 HOH HOH A . 
G 3 HOH 233 733 574 HOH HOH A . 
G 3 HOH 234 734 634 HOH HOH A . 
G 3 HOH 235 735 400 HOH HOH A . 
G 3 HOH 236 736 595 HOH HOH A . 
G 3 HOH 237 737 541 HOH HOH A . 
G 3 HOH 238 738 349 HOH HOH A . 
G 3 HOH 239 739 421 HOH HOH A . 
G 3 HOH 240 740 345 HOH HOH A . 
G 3 HOH 241 741 582 HOH HOH A . 
G 3 HOH 242 742 516 HOH HOH A . 
G 3 HOH 243 743 347 HOH HOH A . 
G 3 HOH 244 744 115 HOH HOH A . 
G 3 HOH 245 745 248 HOH HOH A . 
G 3 HOH 246 746 509 HOH HOH A . 
G 3 HOH 247 747 534 HOH HOH A . 
G 3 HOH 248 748 108 HOH HOH A . 
G 3 HOH 249 749 220 HOH HOH A . 
G 3 HOH 250 750 91  HOH HOH A . 
G 3 HOH 251 751 312 HOH HOH A . 
G 3 HOH 252 752 491 HOH HOH A . 
G 3 HOH 253 753 310 HOH HOH A . 
G 3 HOH 254 754 612 HOH HOH A . 
G 3 HOH 255 755 632 HOH HOH A . 
G 3 HOH 256 756 240 HOH HOH A . 
G 3 HOH 257 757 215 HOH HOH A . 
G 3 HOH 258 758 454 HOH HOH A . 
G 3 HOH 259 759 296 HOH HOH A . 
G 3 HOH 260 760 331 HOH HOH A . 
G 3 HOH 261 761 458 HOH HOH A . 
G 3 HOH 262 762 625 HOH HOH A . 
G 3 HOH 263 763 418 HOH HOH A . 
G 3 HOH 264 764 423 HOH HOH A . 
G 3 HOH 265 765 173 HOH HOH A . 
G 3 HOH 266 766 644 HOH HOH A . 
G 3 HOH 267 767 483 HOH HOH A . 
G 3 HOH 268 768 604 HOH HOH A . 
G 3 HOH 269 769 512 HOH HOH A . 
G 3 HOH 270 770 250 HOH HOH A . 
G 3 HOH 271 771 233 HOH HOH A . 
G 3 HOH 272 772 420 HOH HOH A . 
G 3 HOH 273 773 601 HOH HOH A . 
G 3 HOH 274 774 249 HOH HOH A . 
G 3 HOH 275 775 212 HOH HOH A . 
G 3 HOH 276 776 369 HOH HOH A . 
G 3 HOH 277 777 210 HOH HOH A . 
G 3 HOH 278 778 548 HOH HOH A . 
G 3 HOH 279 779 344 HOH HOH A . 
G 3 HOH 280 780 340 HOH HOH A . 
G 3 HOH 281 781 22  HOH HOH A . 
G 3 HOH 282 782 381 HOH HOH A . 
G 3 HOH 283 783 172 HOH HOH A . 
G 3 HOH 284 784 76  HOH HOH A . 
G 3 HOH 285 785 623 HOH HOH A . 
G 3 HOH 286 786 424 HOH HOH A . 
G 3 HOH 287 787 121 HOH HOH A . 
G 3 HOH 288 788 200 HOH HOH A . 
G 3 HOH 289 789 123 HOH HOH A . 
G 3 HOH 290 790 396 HOH HOH A . 
G 3 HOH 291 791 432 HOH HOH A . 
G 3 HOH 292 792 339 HOH HOH A . 
G 3 HOH 293 793 578 HOH HOH A . 
G 3 HOH 294 794 415 HOH HOH A . 
G 3 HOH 295 795 363 HOH HOH A . 
G 3 HOH 296 796 500 HOH HOH A . 
G 3 HOH 297 797 455 HOH HOH A . 
G 3 HOH 298 798 450 HOH HOH A . 
G 3 HOH 299 799 351 HOH HOH A . 
G 3 HOH 300 800 435 HOH HOH A . 
G 3 HOH 301 801 222 HOH HOH A . 
G 3 HOH 302 802 168 HOH HOH A . 
G 3 HOH 303 803 324 HOH HOH A . 
G 3 HOH 304 804 558 HOH HOH A . 
G 3 HOH 305 805 476 HOH HOH A . 
G 3 HOH 306 806 643 HOH HOH A . 
G 3 HOH 307 807 252 HOH HOH A . 
G 3 HOH 308 808 513 HOH HOH A . 
G 3 HOH 309 809 529 HOH HOH A . 
G 3 HOH 310 810 343 HOH HOH A . 
G 3 HOH 311 811 342 HOH HOH A . 
G 3 HOH 312 812 552 HOH HOH A . 
G 3 HOH 313 813 412 HOH HOH A . 
G 3 HOH 314 814 434 HOH HOH A . 
G 3 HOH 315 815 348 HOH HOH A . 
G 3 HOH 316 816 453 HOH HOH A . 
G 3 HOH 317 817 562 HOH HOH A . 
G 3 HOH 318 818 566 HOH HOH A . 
G 3 HOH 319 819 624 HOH HOH A . 
G 3 HOH 320 820 264 HOH HOH A . 
G 3 HOH 321 821 356 HOH HOH A . 
G 3 HOH 322 822 439 HOH HOH A . 
G 3 HOH 323 823 188 HOH HOH A . 
G 3 HOH 324 824 642 HOH HOH A . 
G 3 HOH 325 825 532 HOH HOH A . 
G 3 HOH 326 826 581 HOH HOH A . 
G 3 HOH 327 827 301 HOH HOH A . 
G 3 HOH 328 828 388 HOH HOH A . 
G 3 HOH 329 829 486 HOH HOH A . 
G 3 HOH 330 830 621 HOH HOH A . 
G 3 HOH 331 831 263 HOH HOH A . 
G 3 HOH 332 832 494 HOH HOH A . 
G 3 HOH 333 833 457 HOH HOH A . 
G 3 HOH 334 834 641 HOH HOH A . 
G 3 HOH 335 835 503 HOH HOH A . 
G 3 HOH 336 836 306 HOH HOH A . 
G 3 HOH 337 837 585 HOH HOH A . 
G 3 HOH 338 838 426 HOH HOH A . 
H 3 HOH 1   501 538 HOH HOH B . 
H 3 HOH 2   502 628 HOH HOH B . 
H 3 HOH 3   503 354 HOH HOH B . 
H 3 HOH 4   504 224 HOH HOH B . 
H 3 HOH 5   505 549 HOH HOH B . 
H 3 HOH 6   506 442 HOH HOH B . 
H 3 HOH 7   507 626 HOH HOH B . 
H 3 HOH 8   508 211 HOH HOH B . 
H 3 HOH 9   509 622 HOH HOH B . 
H 3 HOH 10  510 193 HOH HOH B . 
H 3 HOH 11  511 139 HOH HOH B . 
H 3 HOH 12  512 537 HOH HOH B . 
H 3 HOH 13  513 335 HOH HOH B . 
H 3 HOH 14  514 589 HOH HOH B . 
H 3 HOH 15  515 102 HOH HOH B . 
H 3 HOH 16  516 272 HOH HOH B . 
H 3 HOH 17  517 7   HOH HOH B . 
H 3 HOH 18  518 44  HOH HOH B . 
H 3 HOH 19  519 475 HOH HOH B . 
H 3 HOH 20  520 287 HOH HOH B . 
H 3 HOH 21  521 266 HOH HOH B . 
H 3 HOH 22  522 18  HOH HOH B . 
H 3 HOH 23  523 63  HOH HOH B . 
H 3 HOH 24  524 283 HOH HOH B . 
H 3 HOH 25  525 446 HOH HOH B . 
H 3 HOH 26  526 507 HOH HOH B . 
H 3 HOH 27  527 133 HOH HOH B . 
H 3 HOH 28  528 175 HOH HOH B . 
H 3 HOH 29  529 109 HOH HOH B . 
H 3 HOH 30  530 386 HOH HOH B . 
H 3 HOH 31  531 82  HOH HOH B . 
H 3 HOH 32  532 171 HOH HOH B . 
H 3 HOH 33  533 156 HOH HOH B . 
H 3 HOH 34  534 504 HOH HOH B . 
H 3 HOH 35  535 74  HOH HOH B . 
H 3 HOH 36  536 80  HOH HOH B . 
H 3 HOH 37  537 110 HOH HOH B . 
H 3 HOH 38  538 463 HOH HOH B . 
H 3 HOH 39  539 158 HOH HOH B . 
H 3 HOH 40  540 56  HOH HOH B . 
H 3 HOH 41  541 23  HOH HOH B . 
H 3 HOH 42  542 488 HOH HOH B . 
H 3 HOH 43  543 129 HOH HOH B . 
H 3 HOH 44  544 517 HOH HOH B . 
H 3 HOH 45  545 57  HOH HOH B . 
H 3 HOH 46  546 376 HOH HOH B . 
H 3 HOH 47  547 11  HOH HOH B . 
H 3 HOH 48  548 265 HOH HOH B . 
H 3 HOH 49  549 564 HOH HOH B . 
H 3 HOH 50  550 138 HOH HOH B . 
H 3 HOH 51  551 540 HOH HOH B . 
H 3 HOH 52  552 608 HOH HOH B . 
H 3 HOH 53  553 199 HOH HOH B . 
H 3 HOH 54  554 45  HOH HOH B . 
H 3 HOH 55  555 430 HOH HOH B . 
H 3 HOH 56  556 12  HOH HOH B . 
H 3 HOH 57  557 114 HOH HOH B . 
H 3 HOH 58  558 147 HOH HOH B . 
H 3 HOH 59  559 217 HOH HOH B . 
H 3 HOH 60  560 533 HOH HOH B . 
H 3 HOH 61  561 181 HOH HOH B . 
H 3 HOH 62  562 294 HOH HOH B . 
H 3 HOH 63  563 1   HOH HOH B . 
H 3 HOH 64  564 161 HOH HOH B . 
H 3 HOH 65  565 134 HOH HOH B . 
H 3 HOH 66  566 113 HOH HOH B . 
H 3 HOH 67  567 14  HOH HOH B . 
H 3 HOH 68  568 237 HOH HOH B . 
H 3 HOH 69  569 584 HOH HOH B . 
H 3 HOH 70  570 61  HOH HOH B . 
H 3 HOH 71  571 514 HOH HOH B . 
H 3 HOH 72  572 96  HOH HOH B . 
H 3 HOH 73  573 314 HOH HOH B . 
H 3 HOH 74  574 441 HOH HOH B . 
H 3 HOH 75  575 58  HOH HOH B . 
H 3 HOH 76  576 47  HOH HOH B . 
H 3 HOH 77  577 286 HOH HOH B . 
H 3 HOH 78  578 53  HOH HOH B . 
H 3 HOH 79  579 40  HOH HOH B . 
H 3 HOH 80  580 245 HOH HOH B . 
H 3 HOH 81  581 403 HOH HOH B . 
H 3 HOH 82  582 438 HOH HOH B . 
H 3 HOH 83  583 238 HOH HOH B . 
H 3 HOH 84  584 472 HOH HOH B . 
H 3 HOH 85  585 144 HOH HOH B . 
H 3 HOH 86  586 307 HOH HOH B . 
H 3 HOH 87  587 559 HOH HOH B . 
H 3 HOH 88  588 231 HOH HOH B . 
H 3 HOH 89  589 382 HOH HOH B . 
H 3 HOH 90  590 355 HOH HOH B . 
H 3 HOH 91  591 55  HOH HOH B . 
H 3 HOH 92  592 323 HOH HOH B . 
H 3 HOH 93  593 124 HOH HOH B . 
H 3 HOH 94  594 275 HOH HOH B . 
H 3 HOH 95  595 205 HOH HOH B . 
H 3 HOH 96  596 5   HOH HOH B . 
H 3 HOH 97  597 103 HOH HOH B . 
H 3 HOH 98  598 313 HOH HOH B . 
H 3 HOH 99  599 302 HOH HOH B . 
H 3 HOH 100 600 98  HOH HOH B . 
H 3 HOH 101 601 223 HOH HOH B . 
H 3 HOH 102 602 290 HOH HOH B . 
H 3 HOH 103 603 360 HOH HOH B . 
H 3 HOH 104 604 254 HOH HOH B . 
H 3 HOH 105 605 157 HOH HOH B . 
H 3 HOH 106 606 30  HOH HOH B . 
H 3 HOH 107 607 547 HOH HOH B . 
H 3 HOH 108 608 107 HOH HOH B . 
H 3 HOH 109 609 21  HOH HOH B . 
H 3 HOH 110 610 117 HOH HOH B . 
H 3 HOH 111 611 515 HOH HOH B . 
H 3 HOH 112 612 230 HOH HOH B . 
H 3 HOH 113 613 206 HOH HOH B . 
H 3 HOH 114 614 148 HOH HOH B . 
H 3 HOH 115 615 554 HOH HOH B . 
H 3 HOH 116 616 390 HOH HOH B . 
H 3 HOH 117 617 251 HOH HOH B . 
H 3 HOH 118 618 284 HOH HOH B . 
H 3 HOH 119 619 419 HOH HOH B . 
H 3 HOH 120 620 78  HOH HOH B . 
H 3 HOH 121 621 315 HOH HOH B . 
H 3 HOH 122 622 54  HOH HOH B . 
H 3 HOH 123 623 31  HOH HOH B . 
H 3 HOH 124 624 28  HOH HOH B . 
H 3 HOH 125 625 341 HOH HOH B . 
H 3 HOH 126 626 6   HOH HOH B . 
H 3 HOH 127 627 145 HOH HOH B . 
H 3 HOH 128 628 153 HOH HOH B . 
H 3 HOH 129 629 34  HOH HOH B . 
H 3 HOH 130 630 573 HOH HOH B . 
H 3 HOH 131 631 337 HOH HOH B . 
H 3 HOH 132 632 583 HOH HOH B . 
H 3 HOH 133 633 285 HOH HOH B . 
H 3 HOH 134 634 295 HOH HOH B . 
H 3 HOH 135 635 447 HOH HOH B . 
H 3 HOH 136 636 137 HOH HOH B . 
H 3 HOH 137 637 304 HOH HOH B . 
H 3 HOH 138 638 183 HOH HOH B . 
H 3 HOH 139 639 155 HOH HOH B . 
H 3 HOH 140 640 530 HOH HOH B . 
H 3 HOH 141 641 395 HOH HOH B . 
H 3 HOH 142 642 16  HOH HOH B . 
H 3 HOH 143 643 469 HOH HOH B . 
H 3 HOH 144 644 278 HOH HOH B . 
H 3 HOH 145 645 73  HOH HOH B . 
H 3 HOH 146 646 179 HOH HOH B . 
H 3 HOH 147 647 180 HOH HOH B . 
H 3 HOH 148 648 151 HOH HOH B . 
H 3 HOH 149 649 88  HOH HOH B . 
H 3 HOH 150 650 487 HOH HOH B . 
H 3 HOH 151 651 59  HOH HOH B . 
H 3 HOH 152 652 368 HOH HOH B . 
H 3 HOH 153 653 449 HOH HOH B . 
H 3 HOH 154 654 638 HOH HOH B . 
H 3 HOH 155 655 536 HOH HOH B . 
H 3 HOH 156 656 269 HOH HOH B . 
H 3 HOH 157 657 159 HOH HOH B . 
H 3 HOH 158 658 122 HOH HOH B . 
H 3 HOH 159 659 178 HOH HOH B . 
H 3 HOH 160 660 526 HOH HOH B . 
H 3 HOH 161 661 571 HOH HOH B . 
H 3 HOH 162 662 126 HOH HOH B . 
H 3 HOH 163 663 383 HOH HOH B . 
H 3 HOH 164 664 89  HOH HOH B . 
H 3 HOH 165 665 636 HOH HOH B . 
H 3 HOH 166 666 70  HOH HOH B . 
H 3 HOH 167 667 198 HOH HOH B . 
H 3 HOH 168 668 459 HOH HOH B . 
H 3 HOH 169 669 93  HOH HOH B . 
H 3 HOH 170 670 255 HOH HOH B . 
H 3 HOH 171 671 318 HOH HOH B . 
H 3 HOH 172 672 505 HOH HOH B . 
H 3 HOH 173 673 106 HOH HOH B . 
H 3 HOH 174 674 336 HOH HOH B . 
H 3 HOH 175 675 271 HOH HOH B . 
H 3 HOH 176 676 67  HOH HOH B . 
H 3 HOH 177 677 332 HOH HOH B . 
H 3 HOH 178 678 448 HOH HOH B . 
H 3 HOH 179 679 84  HOH HOH B . 
H 3 HOH 180 680 191 HOH HOH B . 
H 3 HOH 181 681 170 HOH HOH B . 
H 3 HOH 182 682 456 HOH HOH B . 
H 3 HOH 183 683 460 HOH HOH B . 
H 3 HOH 184 684 176 HOH HOH B . 
H 3 HOH 185 685 521 HOH HOH B . 
H 3 HOH 186 686 256 HOH HOH B . 
H 3 HOH 187 687 479 HOH HOH B . 
H 3 HOH 188 688 371 HOH HOH B . 
H 3 HOH 189 689 393 HOH HOH B . 
H 3 HOH 190 690 361 HOH HOH B . 
H 3 HOH 191 691 609 HOH HOH B . 
H 3 HOH 192 692 226 HOH HOH B . 
H 3 HOH 193 693 135 HOH HOH B . 
H 3 HOH 194 694 407 HOH HOH B . 
H 3 HOH 195 695 519 HOH HOH B . 
H 3 HOH 196 696 338 HOH HOH B . 
H 3 HOH 197 697 596 HOH HOH B . 
H 3 HOH 198 698 551 HOH HOH B . 
H 3 HOH 199 699 204 HOH HOH B . 
H 3 HOH 200 700 303 HOH HOH B . 
H 3 HOH 201 701 329 HOH HOH B . 
H 3 HOH 202 702 216 HOH HOH B . 
H 3 HOH 203 703 602 HOH HOH B . 
H 3 HOH 204 704 568 HOH HOH B . 
H 3 HOH 205 705 605 HOH HOH B . 
H 3 HOH 206 706 247 HOH HOH B . 
H 3 HOH 207 707 506 HOH HOH B . 
H 3 HOH 208 708 408 HOH HOH B . 
H 3 HOH 209 709 372 HOH HOH B . 
H 3 HOH 210 710 470 HOH HOH B . 
H 3 HOH 211 711 436 HOH HOH B . 
H 3 HOH 212 712 620 HOH HOH B . 
H 3 HOH 213 713 550 HOH HOH B . 
H 3 HOH 214 714 545 HOH HOH B . 
H 3 HOH 215 715 553 HOH HOH B . 
H 3 HOH 216 716 401 HOH HOH B . 
H 3 HOH 217 717 627 HOH HOH B . 
H 3 HOH 218 718 235 HOH HOH B . 
H 3 HOH 219 719 467 HOH HOH B . 
H 3 HOH 220 720 593 HOH HOH B . 
H 3 HOH 221 721 112 HOH HOH B . 
H 3 HOH 222 722 635 HOH HOH B . 
H 3 HOH 223 723 501 HOH HOH B . 
H 3 HOH 224 724 189 HOH HOH B . 
H 3 HOH 225 725 410 HOH HOH B . 
H 3 HOH 226 726 591 HOH HOH B . 
H 3 HOH 227 727 288 HOH HOH B . 
H 3 HOH 228 728 380 HOH HOH B . 
H 3 HOH 229 729 362 HOH HOH B . 
H 3 HOH 230 730 219 HOH HOH B . 
H 3 HOH 231 731 385 HOH HOH B . 
H 3 HOH 232 732 592 HOH HOH B . 
H 3 HOH 233 733 617 HOH HOH B . 
H 3 HOH 234 734 227 HOH HOH B . 
H 3 HOH 235 735 489 HOH HOH B . 
H 3 HOH 236 736 261 HOH HOH B . 
H 3 HOH 237 737 282 HOH HOH B . 
H 3 HOH 238 738 594 HOH HOH B . 
H 3 HOH 239 739 166 HOH HOH B . 
H 3 HOH 240 740 557 HOH HOH B . 
H 3 HOH 241 741 366 HOH HOH B . 
H 3 HOH 242 742 471 HOH HOH B . 
H 3 HOH 243 743 433 HOH HOH B . 
H 3 HOH 244 744 384 HOH HOH B . 
H 3 HOH 245 745 616 HOH HOH B . 
H 3 HOH 246 746 375 HOH HOH B . 
H 3 HOH 247 747 603 HOH HOH B . 
H 3 HOH 248 748 177 HOH HOH B . 
H 3 HOH 249 749 352 HOH HOH B . 
H 3 HOH 250 750 326 HOH HOH B . 
H 3 HOH 251 751 394 HOH HOH B . 
H 3 HOH 252 752 417 HOH HOH B . 
H 3 HOH 253 753 437 HOH HOH B . 
H 3 HOH 254 754 299 HOH HOH B . 
H 3 HOH 255 755 309 HOH HOH B . 
H 3 HOH 256 756 588 HOH HOH B . 
H 3 HOH 257 757 327 HOH HOH B . 
H 3 HOH 258 758 377 HOH HOH B . 
H 3 HOH 259 759 196 HOH HOH B . 
H 3 HOH 260 760 451 HOH HOH B . 
H 3 HOH 261 761 405 HOH HOH B . 
H 3 HOH 262 762 27  HOH HOH B . 
H 3 HOH 263 763 373 HOH HOH B . 
H 3 HOH 264 764 416 HOH HOH B . 
H 3 HOH 265 765 474 HOH HOH B . 
H 3 HOH 266 766 580 HOH HOH B . 
H 3 HOH 267 767 150 HOH HOH B . 
H 3 HOH 268 768 510 HOH HOH B . 
H 3 HOH 269 769 236 HOH HOH B . 
H 3 HOH 270 770 597 HOH HOH B . 
H 3 HOH 271 771 563 HOH HOH B . 
H 3 HOH 272 772 127 HOH HOH B . 
H 3 HOH 273 773 379 HOH HOH B . 
H 3 HOH 274 774 413 HOH HOH B . 
H 3 HOH 275 775 330 HOH HOH B . 
H 3 HOH 276 776 465 HOH HOH B . 
H 3 HOH 277 777 262 HOH HOH B . 
H 3 HOH 278 778 606 HOH HOH B . 
H 3 HOH 279 779 619 HOH HOH B . 
H 3 HOH 280 780 615 HOH HOH B . 
H 3 HOH 281 781 543 HOH HOH B . 
H 3 HOH 282 782 234 HOH HOH B . 
H 3 HOH 283 783 359 HOH HOH B . 
H 3 HOH 284 784 387 HOH HOH B . 
H 3 HOH 285 785 370 HOH HOH B . 
H 3 HOH 286 786 273 HOH HOH B . 
H 3 HOH 287 787 629 HOH HOH B . 
H 3 HOH 288 788 614 HOH HOH B . 
H 3 HOH 289 789 297 HOH HOH B . 
H 3 HOH 290 790 292 HOH HOH B . 
H 3 HOH 291 791 598 HOH HOH B . 
H 3 HOH 292 792 422 HOH HOH B . 
H 3 HOH 293 793 209 HOH HOH B . 
H 3 HOH 294 794 544 HOH HOH B . 
H 3 HOH 295 795 531 HOH HOH B . 
H 3 HOH 296 796 445 HOH HOH B . 
H 3 HOH 297 797 462 HOH HOH B . 
H 3 HOH 298 798 365 HOH HOH B . 
H 3 HOH 299 799 241 HOH HOH B . 
H 3 HOH 300 800 572 HOH HOH B . 
H 3 HOH 301 801 239 HOH HOH B . 
H 3 HOH 302 802 496 HOH HOH B . 
H 3 HOH 303 803 527 HOH HOH B . 
H 3 HOH 304 804 556 HOH HOH B . 
H 3 HOH 305 805 546 HOH HOH B . 
H 3 HOH 306 806 221 HOH HOH B . 
# 
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 reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .                    2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   112.81 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8ZU4 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     127.233 
_cell.length_a_esd                 ? 
_cell.length_b                     86.320 
_cell.length_b_esd                 ? 
_cell.length_c                     58.800 
_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                         8ZU4 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                5 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'C 1 2 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8ZU4 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.38 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          48.24 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.1 M Bis-Tris pH 6.5, 28% w/v Polyethylene glycol monomethyl ether 2,000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            289 
# 
_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 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2021-06-09 
_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   0.9791 
_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                        'SSRF BEAMLINE BL02U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9791 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL02U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8ZU4 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.39 
_reflns.d_resolution_low                               19.73 
_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                                     159152 
_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                           74.5 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                5.81 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          8.13 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.033 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.023 
_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                        ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_measured_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.number_unique_obs 
_reflns_shell.percent_possible_obs 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.meanI_over_sigI_gt 
_reflns_shell.meanI_over_uI_all 
_reflns_shell.meanI_over_uI_gt 
_reflns_shell.number_measured_gt 
_reflns_shell.number_unique_gt 
_reflns_shell.percent_possible_gt 
_reflns_shell.Rmerge_F_gt 
_reflns_shell.Rmerge_I_gt 
_reflns_shell.pdbx_redundancy 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_netI_over_sigmaI_all 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_rejects 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
_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 
_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 
1.39 1.47 ? ? ? ? ? ? 627  ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.953 ? ? 1 1 0.37  ? ? ? ? 0.674 ? ? ? ? ? ? ? ? ? 
1.47 1.57 ? ? ? ? ? ? 2462 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.818 ? ? 2 1 0.646 ? ? ? ? 0.578 ? ? ? ? ? ? ? ? ? 
1.57 1.7  ? ? ? ? ? ? 4847 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.285 ? ? 3 1 0.919 ? ? ? ? 0.202 ? ? ? ? ? ? ? ? ? 
1.70 1.86 ? ? ? ? ? ? 8913 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.139 ? ? 4 1 0.974 ? ? ? ? 0.098 ? ? ? ? ? ? ? ? ? 
1.86 2.08 ? ? ? ? ? ? 8793 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.092 ? ? 5 1 0.989 ? ? ? ? 0.065 ? ? ? ? ? ? ? ? ? 
2.08 2.39 ? ? ? ? ? ? 7830 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.06  ? ? 6 1 0.994 ? ? ? ? 0.042 ? ? ? ? ? ? ? ? ? 
2.39 2.92 ? ? ? ? ? ? 6172 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.039 ? ? 7 1 0.997 ? ? ? ? 0.027 ? ? ? ? ? ? ? ? ? 
2.92 4.08 ? ? ? ? ? ? 4230 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.026 ? ? 8 1 0.998 ? ? ? ? 0.019 ? ? ? ? ? ? ? ? ? 
1.44 4.08 ? ? ? ? ? ? 2242 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.026 ? ? 9 1 0.998 ? ? ? ? 0.019 ? ? ? ? ? ? ? ? ? 
# 
_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                                 8ZU4 
_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                            1.39 
_refine.ls_d_res_low                             19.73 
_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                     159152 
_refine.ls_number_reflns_R_free                  3874 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    68.25 
_refine.ls_percent_reflns_R_free                 2.43 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1675 
_refine.ls_R_factor_R_free                       0.1979 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1667 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.55 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 28.59 
_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                            0.15 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.39 
_refine_hist.d_res_low                        19.73 
_refine_hist.number_atoms_solvent             644 
_refine_hist.number_atoms_total               5066 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        4418 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         4 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.823  ? 6146 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 13.856 ? 1628 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.080  ? 694  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.007  ? 806  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.39 1.40 . . 5   114  1.00   . . . . 0.4704 . . . . . . . . . . . 0.6837 
'X-RAY DIFFRACTION' 1.40 1.42 . . 17  429  20     . . . . 0.3664 . . . . . . . . . . . 0.3664 
'X-RAY DIFFRACTION' 1.42 1.44 . . 26  847  20     . . . . 0.4313 . . . . . . . . . . . 0.4957 
'X-RAY DIFFRACTION' 1.44 1.46 . . 27  1290 20     . . . . 0.4685 . . . . . . . . . . . 0.4752 
'X-RAY DIFFRACTION' 1.46 1.48 . . 30  1699 21.00  . . . . 0.4223 . . . . . . . . . . . 0.4240 
'X-RAY DIFFRACTION' 1.48 1.50 . . 63  2274 28.00  . . . . 0.3469 . . . . . . . . . . . 0.3469 
'X-RAY DIFFRACTION' 1.50 1.53 . . 68  2623 33.00  . . . . 0.4091 . . . . . . . . . . . 0.4300 
'X-RAY DIFFRACTION' 1.53 1.55 . . 94  3259 40.00  . . . . 0.3076 . . . . . . . . . . . 0.3076 
'X-RAY DIFFRACTION' 1.55 1.58 . . 84  3771 46.00  . . . . 0.2999 . . . . . . . . . . . 0.3030 
'X-RAY DIFFRACTION' 1.58 1.61 . . 87  4277 52.00  . . . . 0.2976 . . . . . . . . . . . 0.3425 
'X-RAY DIFFRACTION' 1.64 1.67 . . 160 5225 65.00  . . . . 0.2574 . . . . . . . . . . . 0.2933 
'X-RAY DIFFRACTION' 1.71 1.75 . . 182 6854 85.00  . . . . 0.2277 . . . . . . . . . . . 0.2523 
'X-RAY DIFFRACTION' 1.75 1.79 . . 176 7815 96.00  . . . . 0.2192 . . . . . . . . . . . 0.2313 
'X-RAY DIFFRACTION' 1.79 1.84 . . 196 7972 98.00  . . . . 0.2025 . . . . . . . . . . . 0.2392 
'X-RAY DIFFRACTION' 1.84 1.89 . . 215 8040 99.00  . . . . 0.2016 . . . . . . . . . . . 0.2476 
'X-RAY DIFFRACTION' 1.89 1.96 . . 182 7788 96.00  . . . . 0.2263 . . . . . . . . . . . 0.2422 
'X-RAY DIFFRACTION' 1.96 2.03 . . 215 8047 99.00  . . . . 0.1750 . . . . . . . . . . . 0.2001 
'X-RAY DIFFRACTION' 2.03 2.11 . . 187 7985 98.00  . . . . 0.1792 . . . . . . . . . . . 0.1954 
'X-RAY DIFFRACTION' 2.11 2.20 . . 192 8062 100.00 . . . . 0.1641 . . . . . . . . . . . 0.1751 
'X-RAY DIFFRACTION' 2.20 2.32 . . 217 7992 98.00  . . . . 0.1818 . . . . . . . . . . . 0.2198 
'X-RAY DIFFRACTION' 2.32 2.46 . . 205 8054 99.00  . . . . 0.1699 . . . . . . . . . . . 0.1930 
'X-RAY DIFFRACTION' 2.46 2.65 . . 199 8043 99.00  . . . . 0.1680 . . . . . . . . . . . 0.2088 
'X-RAY DIFFRACTION' 2.65 2.92 . . 195 8036 99.00  . . . . 0.1585 . . . . . . . . . . . 0.1637 
'X-RAY DIFFRACTION' 2.92 3.34 . . 209 8109 99.00  . . . . 0.1380 . . . . . . . . . . . 0.1910 
'X-RAY DIFFRACTION' 3.34 4.20 . . 197 8028 99.00  . . . . 0.1295 . . . . . . . . . . . 0.1663 
# 
_struct.entry_id                     8ZU4 
_struct.title                        'Crystal Structure of Methyl parathion hydrolase mutant A127L/I145L/Q272D/S279A/S304P' 
_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        8ZU4 
_struct_keywords.text            Hydrolase 
_struct_keywords.pdbx_keywords   HYDROLASE 
# 
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 2 ? 
E N N 2 ? 
F N N 2 ? 
G N N 3 ? 
H N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    Q841S6_PSEWB 
_struct_ref.pdbx_db_accession          Q841S6 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;AAPQVRTSAPGYYRMLLGDFEITALSDGTVALPVDKRLNQPAPKTQSALAKSFQKAPLETSVTGYLVNTGSKLVLVDTGA
AGLFGPTLGRLAANLKAAGYQPEQVDEIYITHMHPDHVGGLMVGEQLAFPNAVVRADQKEADFWLSQTNLDKAPDDESKG
FFKGAMASLNPYVKAGKFKPFSGNTDLVPGIKALASHGHTPGHTTYVVESQGQKLALLGDLILVAAVQFDDPSVTTQLDS
DSKSVAVERKKAFADAAKGGYLIAASHLSFPGIGHIRAEGKGYRFVPVNYSVVN
;
_struct_ref.pdbx_align_begin           36 
# 
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 8ZU4 A 1 ? 294 ? Q841S6 36 ? 329 ? 36 329 
2 1 8ZU4 B 1 ? 294 ? Q841S6 36 ? 329 ? 36 329 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 8ZU4 LEU A 92  ? UNP Q841S6 ALA 127 'engineered mutation' 127 1  
1 8ZU4 LEU A 110 ? UNP Q841S6 ILE 145 'engineered mutation' 145 2  
1 8ZU4 ASP A 237 ? UNP Q841S6 GLN 272 'engineered mutation' 272 3  
1 8ZU4 ALA A 244 ? UNP Q841S6 SER 279 'engineered mutation' 279 4  
1 8ZU4 PRO A 269 ? UNP Q841S6 SER 304 'engineered mutation' 304 5  
1 8ZU4 ALA A 295 ? UNP Q841S6 ?   ?   'expression tag'      330 6  
1 8ZU4 ALA A 296 ? UNP Q841S6 ?   ?   'expression tag'      331 7  
2 8ZU4 LEU B 92  ? UNP Q841S6 ALA 127 'engineered mutation' 127 8  
2 8ZU4 LEU B 110 ? UNP Q841S6 ILE 145 'engineered mutation' 145 9  
2 8ZU4 ASP B 237 ? UNP Q841S6 GLN 272 'engineered mutation' 272 10 
2 8ZU4 ALA B 244 ? UNP Q841S6 SER 279 'engineered mutation' 279 11 
2 8ZU4 PRO B 269 ? UNP Q841S6 SER 304 'engineered mutation' 304 12 
2 8ZU4 ALA B 295 ? UNP Q841S6 ?   ?   'expression tag'      330 13 
2 8ZU4 ALA B 296 ? UNP Q841S6 ?   ?   'expression tag'      331 14 
# 
_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)' 4800  ? 
1 MORE         -168  ? 
1 'SSA (A^2)'  22840 ? 
# 
_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 
# 
_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 PRO A 33  ? LEU A 38  ? PRO A 68  LEU A 73  1 ? 6  
HELX_P HELX_P2  AA2 PRO A 41  ? SER A 52  ? PRO A 76  SER A 87  1 ? 12 
HELX_P HELX_P3  AA3 ARG A 90  ? ALA A 98  ? ARG A 125 ALA A 133 1 ? 9  
HELX_P HELX_P4  AA4 GLN A 101 ? VAL A 105 ? GLN A 136 VAL A 140 5 ? 5  
HELX_P HELX_P5  AA5 HIS A 114 ? GLY A 119 ? HIS A 149 GLY A 154 1 ? 6  
HELX_P HELX_P6  AA6 ASP A 137 ? LEU A 145 ? ASP A 172 LEU A 180 1 ? 9  
HELX_P HELX_P7  AA7 SER A 146 ? ALA A 153 ? SER A 181 ALA A 188 1 ? 8  
HELX_P HELX_P8  AA8 ASP A 155 ? ALA A 175 ? ASP A 190 ALA A 210 1 ? 21 
HELX_P HELX_P9  AA9 VAL A 224 ? PHE A 229 ? VAL A 259 PHE A 264 1 ? 6  
HELX_P HELX_P10 AB1 ASP A 241 ? GLY A 260 ? ASP A 276 GLY A 295 1 ? 20 
HELX_P HELX_P11 AB2 PRO B 33  ? LEU B 38  ? PRO B 68  LEU B 73  1 ? 6  
HELX_P HELX_P12 AB3 PRO B 41  ? SER B 52  ? PRO B 76  SER B 87  1 ? 12 
HELX_P HELX_P13 AB4 ARG B 90  ? ALA B 98  ? ARG B 125 ALA B 133 1 ? 9  
HELX_P HELX_P14 AB5 GLN B 101 ? VAL B 105 ? GLN B 136 VAL B 140 5 ? 5  
HELX_P HELX_P15 AB6 HIS B 114 ? GLY B 119 ? HIS B 149 GLY B 154 1 ? 6  
HELX_P HELX_P16 AB7 ASP B 137 ? LEU B 145 ? ASP B 172 LEU B 180 1 ? 9  
HELX_P HELX_P17 AB8 SER B 146 ? LYS B 152 ? SER B 181 LYS B 187 1 ? 7  
HELX_P HELX_P18 AB9 ASP B 155 ? ALA B 175 ? ASP B 190 ALA B 210 1 ? 21 
HELX_P HELX_P19 AC1 VAL B 224 ? PHE B 229 ? VAL B 259 PHE B 264 1 ? 6  
HELX_P HELX_P20 AC2 ASP B 241 ? GLY B 260 ? ASP B 276 GLY B 295 1 ? 20 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1  metalc ? ? A HIS 112 NE2 ? ? ? 1_555 C ZN  . ZN ? ? A HIS 147 A ZN  401 1_555 ? ? ? ? ? ? ? 2.267 ? ? 
metalc2  metalc ? ? A HIS 114 ND1 ? ? ? 1_555 C ZN  . ZN ? ? A HIS 149 A ZN  401 1_555 ? ? ? ? ? ? ? 2.257 ? ? 
metalc3  metalc ? ? A ASP 116 OD2 ? ? ? 1_555 D ZN  . ZN ? ? A ASP 151 A ZN  402 1_555 ? ? ? ? ? ? ? 2.165 ? ? 
metalc4  metalc ? ? A HIS 117 NE2 ? ? ? 1_555 D ZN  . ZN ? ? A HIS 152 A ZN  402 1_555 ? ? ? ? ? ? ? 2.253 ? ? 
metalc5  metalc ? ? A HIS 199 NE2 ? ? ? 1_555 C ZN  . ZN ? ? A HIS 234 A ZN  401 1_555 ? ? ? ? ? ? ? 2.274 ? ? 
metalc6  metalc ? ? A ASP 220 OD2 ? ? ? 1_555 C ZN  . ZN ? ? A ASP 255 A ZN  401 1_555 ? ? ? ? ? ? ? 2.288 ? ? 
metalc7  metalc ? ? A ASP 220 OD2 ? ? ? 1_555 D ZN  . ZN ? ? A ASP 255 A ZN  402 1_555 ? ? ? ? ? ? ? 2.082 ? ? 
metalc8  metalc ? ? A HIS 267 NE2 ? ? ? 1_555 D ZN  . ZN ? ? A HIS 302 A ZN  402 1_555 ? ? ? ? ? ? ? 2.193 ? ? 
metalc9  metalc ? ? C ZN  .   ZN  ? ? ? 1_555 G HOH . O  ? ? A ZN  401 A HOH 536 1_555 ? ? ? ? ? ? ? 1.984 ? ? 
metalc10 metalc ? ? C ZN  .   ZN  ? ? ? 1_555 G HOH . O  ? ? A ZN  401 A HOH 712 1_555 ? ? ? ? ? ? ? 2.393 ? ? 
metalc11 metalc ? ? D ZN  .   ZN  ? ? ? 1_555 G HOH . O  ? ? A ZN  402 A HOH 536 1_555 ? ? ? ? ? ? ? 1.997 ? ? 
metalc12 metalc ? ? D ZN  .   ZN  ? ? ? 1_555 G HOH . O  ? ? A ZN  402 A HOH 657 1_555 ? ? ? ? ? ? ? 2.416 ? ? 
metalc13 metalc ? ? B HIS 112 NE2 ? ? ? 1_555 F ZN  . ZN ? ? B HIS 147 B ZN  402 1_555 ? ? ? ? ? ? ? 2.283 ? ? 
metalc14 metalc ? ? B HIS 114 ND1 ? ? ? 1_555 F ZN  . ZN ? ? B HIS 149 B ZN  402 1_555 ? ? ? ? ? ? ? 2.268 ? ? 
metalc15 metalc ? ? B ASP 116 OD2 ? ? ? 1_555 E ZN  . ZN ? ? B ASP 151 B ZN  401 1_555 ? ? ? ? ? ? ? 2.141 ? ? 
metalc16 metalc ? ? B HIS 117 NE2 ? ? ? 1_555 E ZN  . ZN ? ? B HIS 152 B ZN  401 1_555 ? ? ? ? ? ? ? 2.252 ? ? 
metalc17 metalc ? ? B HIS 199 NE2 ? ? ? 1_555 F ZN  . ZN ? ? B HIS 234 B ZN  402 1_555 ? ? ? ? ? ? ? 2.265 ? ? 
metalc18 metalc ? ? B ASP 220 OD2 ? ? ? 1_555 E ZN  . ZN ? ? B ASP 255 B ZN  401 1_555 ? ? ? ? ? ? ? 2.079 ? ? 
metalc19 metalc ? ? B ASP 220 OD2 ? ? ? 1_555 F ZN  . ZN ? ? B ASP 255 B ZN  402 1_555 ? ? ? ? ? ? ? 2.275 ? ? 
metalc20 metalc ? ? B HIS 267 NE2 ? ? ? 1_555 E ZN  . ZN ? ? B HIS 302 B ZN  401 1_555 ? ? ? ? ? ? ? 2.207 ? ? 
metalc21 metalc ? ? E ZN  .   ZN  ? ? ? 1_555 H HOH . O  ? ? B ZN  401 B HOH 544 1_555 ? ? ? ? ? ? ? 1.972 ? ? 
metalc22 metalc ? ? E ZN  .   ZN  ? ? ? 1_555 H HOH . O  ? ? B ZN  401 B HOH 685 1_555 ? ? ? ? ? ? ? 2.540 ? ? 
metalc23 metalc ? ? F ZN  .   ZN  ? ? ? 1_555 H HOH . O  ? ? B ZN  402 B HOH 544 1_555 ? ? ? ? ? ? ? 2.050 ? ? 
metalc24 metalc ? ? F ZN  .   ZN  ? ? ? 1_555 H HOH . O  ? ? B ZN  402 B HOH 695 1_555 ? ? ? ? ? ? ? 2.371 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  NE2 ? A HIS 112 ? A HIS 147 ? 1_555 ZN ? C ZN . ? A ZN 401 ? 1_555 ND1 ? A HIS 114 ? A HIS 149 ? 1_555 92.1  ? 
2  NE2 ? A HIS 112 ? A HIS 147 ? 1_555 ZN ? C ZN . ? A ZN 401 ? 1_555 NE2 ? A HIS 199 ? A HIS 234 ? 1_555 95.8  ? 
3  ND1 ? A HIS 114 ? A HIS 149 ? 1_555 ZN ? C ZN . ? A ZN 401 ? 1_555 NE2 ? A HIS 199 ? A HIS 234 ? 1_555 89.2  ? 
4  NE2 ? A HIS 112 ? A HIS 147 ? 1_555 ZN ? C ZN . ? A ZN 401 ? 1_555 OD2 ? A ASP 220 ? A ASP 255 ? 1_555 85.5  ? 
5  ND1 ? A HIS 114 ? A HIS 149 ? 1_555 ZN ? C ZN . ? A ZN 401 ? 1_555 OD2 ? A ASP 220 ? A ASP 255 ? 1_555 171.6 ? 
6  NE2 ? A HIS 199 ? A HIS 234 ? 1_555 ZN ? C ZN . ? A ZN 401 ? 1_555 OD2 ? A ASP 220 ? A ASP 255 ? 1_555 99.1  ? 
7  NE2 ? A HIS 112 ? A HIS 147 ? 1_555 ZN ? C ZN . ? A ZN 401 ? 1_555 O   ? G HOH .   ? A HOH 536 ? 1_555 95.9  ? 
8  ND1 ? A HIS 114 ? A HIS 149 ? 1_555 ZN ? C ZN . ? A ZN 401 ? 1_555 O   ? G HOH .   ? A HOH 536 ? 1_555 94.7  ? 
9  NE2 ? A HIS 199 ? A HIS 234 ? 1_555 ZN ? C ZN . ? A ZN 401 ? 1_555 O   ? G HOH .   ? A HOH 536 ? 1_555 167.5 ? 
10 OD2 ? A ASP 220 ? A ASP 255 ? 1_555 ZN ? C ZN . ? A ZN 401 ? 1_555 O   ? G HOH .   ? A HOH 536 ? 1_555 77.6  ? 
11 NE2 ? A HIS 112 ? A HIS 147 ? 1_555 ZN ? C ZN . ? A ZN 401 ? 1_555 O   ? G HOH .   ? A HOH 712 ? 1_555 168.6 ? 
12 ND1 ? A HIS 114 ? A HIS 149 ? 1_555 ZN ? C ZN . ? A ZN 401 ? 1_555 O   ? G HOH .   ? A HOH 712 ? 1_555 98.9  ? 
13 NE2 ? A HIS 199 ? A HIS 234 ? 1_555 ZN ? C ZN . ? A ZN 401 ? 1_555 O   ? G HOH .   ? A HOH 712 ? 1_555 87.4  ? 
14 OD2 ? A ASP 220 ? A ASP 255 ? 1_555 ZN ? C ZN . ? A ZN 401 ? 1_555 O   ? G HOH .   ? A HOH 712 ? 1_555 83.2  ? 
15 O   ? G HOH .   ? A HOH 536 ? 1_555 ZN ? C ZN . ? A ZN 401 ? 1_555 O   ? G HOH .   ? A HOH 712 ? 1_555 80.3  ? 
16 OD2 ? A ASP 116 ? A ASP 151 ? 1_555 ZN ? D ZN . ? A ZN 402 ? 1_555 NE2 ? A HIS 117 ? A HIS 152 ? 1_555 89.7  ? 
17 OD2 ? A ASP 116 ? A ASP 151 ? 1_555 ZN ? D ZN . ? A ZN 402 ? 1_555 OD2 ? A ASP 220 ? A ASP 255 ? 1_555 174.3 ? 
18 NE2 ? A HIS 117 ? A HIS 152 ? 1_555 ZN ? D ZN . ? A ZN 402 ? 1_555 OD2 ? A ASP 220 ? A ASP 255 ? 1_555 91.6  ? 
19 OD2 ? A ASP 116 ? A ASP 151 ? 1_555 ZN ? D ZN . ? A ZN 402 ? 1_555 NE2 ? A HIS 267 ? A HIS 302 ? 1_555 84.8  ? 
20 NE2 ? A HIS 117 ? A HIS 152 ? 1_555 ZN ? D ZN . ? A ZN 402 ? 1_555 NE2 ? A HIS 267 ? A HIS 302 ? 1_555 104.7 ? 
21 OD2 ? A ASP 220 ? A ASP 255 ? 1_555 ZN ? D ZN . ? A ZN 402 ? 1_555 NE2 ? A HIS 267 ? A HIS 302 ? 1_555 100.2 ? 
22 OD2 ? A ASP 116 ? A ASP 151 ? 1_555 ZN ? D ZN . ? A ZN 402 ? 1_555 O   ? G HOH .   ? A HOH 536 ? 1_555 92.0  ? 
23 NE2 ? A HIS 117 ? A HIS 152 ? 1_555 ZN ? D ZN . ? A ZN 402 ? 1_555 O   ? G HOH .   ? A HOH 536 ? 1_555 96.0  ? 
24 OD2 ? A ASP 220 ? A ASP 255 ? 1_555 ZN ? D ZN . ? A ZN 402 ? 1_555 O   ? G HOH .   ? A HOH 536 ? 1_555 82.4  ? 
25 NE2 ? A HIS 267 ? A HIS 302 ? 1_555 ZN ? D ZN . ? A ZN 402 ? 1_555 O   ? G HOH .   ? A HOH 536 ? 1_555 159.1 ? 
26 OD2 ? A ASP 116 ? A ASP 151 ? 1_555 ZN ? D ZN . ? A ZN 402 ? 1_555 O   ? G HOH .   ? A HOH 657 ? 1_555 98.0  ? 
27 NE2 ? A HIS 117 ? A HIS 152 ? 1_555 ZN ? D ZN . ? A ZN 402 ? 1_555 O   ? G HOH .   ? A HOH 657 ? 1_555 171.5 ? 
28 OD2 ? A ASP 220 ? A ASP 255 ? 1_555 ZN ? D ZN . ? A ZN 402 ? 1_555 O   ? G HOH .   ? A HOH 657 ? 1_555 80.3  ? 
29 NE2 ? A HIS 267 ? A HIS 302 ? 1_555 ZN ? D ZN . ? A ZN 402 ? 1_555 O   ? G HOH .   ? A HOH 657 ? 1_555 79.8  ? 
30 O   ? G HOH .   ? A HOH 536 ? 1_555 ZN ? D ZN . ? A ZN 402 ? 1_555 O   ? G HOH .   ? A HOH 657 ? 1_555 80.2  ? 
31 NE2 ? B HIS 112 ? B HIS 147 ? 1_555 ZN ? F ZN . ? B ZN 402 ? 1_555 ND1 ? B HIS 114 ? B HIS 149 ? 1_555 91.5  ? 
32 NE2 ? B HIS 112 ? B HIS 147 ? 1_555 ZN ? F ZN . ? B ZN 402 ? 1_555 NE2 ? B HIS 199 ? B HIS 234 ? 1_555 95.4  ? 
33 ND1 ? B HIS 114 ? B HIS 149 ? 1_555 ZN ? F ZN . ? B ZN 402 ? 1_555 NE2 ? B HIS 199 ? B HIS 234 ? 1_555 90.8  ? 
34 NE2 ? B HIS 112 ? B HIS 147 ? 1_555 ZN ? F ZN . ? B ZN 402 ? 1_555 OD2 ? B ASP 220 ? B ASP 255 ? 1_555 86.4  ? 
35 ND1 ? B HIS 114 ? B HIS 149 ? 1_555 ZN ? F ZN . ? B ZN 402 ? 1_555 OD2 ? B ASP 220 ? B ASP 255 ? 1_555 171.3 ? 
36 NE2 ? B HIS 199 ? B HIS 234 ? 1_555 ZN ? F ZN . ? B ZN 402 ? 1_555 OD2 ? B ASP 220 ? B ASP 255 ? 1_555 97.8  ? 
37 NE2 ? B HIS 112 ? B HIS 147 ? 1_555 ZN ? F ZN . ? B ZN 402 ? 1_555 O   ? H HOH .   ? B HOH 544 ? 1_555 95.2  ? 
38 ND1 ? B HIS 114 ? B HIS 149 ? 1_555 ZN ? F ZN . ? B ZN 402 ? 1_555 O   ? H HOH .   ? B HOH 544 ? 1_555 95.0  ? 
39 NE2 ? B HIS 199 ? B HIS 234 ? 1_555 ZN ? F ZN . ? B ZN 402 ? 1_555 O   ? H HOH .   ? B HOH 544 ? 1_555 167.7 ? 
40 OD2 ? B ASP 220 ? B ASP 255 ? 1_555 ZN ? F ZN . ? B ZN 402 ? 1_555 O   ? H HOH .   ? B HOH 544 ? 1_555 76.8  ? 
41 NE2 ? B HIS 112 ? B HIS 147 ? 1_555 ZN ? F ZN . ? B ZN 402 ? 1_555 O   ? H HOH .   ? B HOH 695 ? 1_555 169.2 ? 
42 ND1 ? B HIS 114 ? B HIS 149 ? 1_555 ZN ? F ZN . ? B ZN 402 ? 1_555 O   ? H HOH .   ? B HOH 695 ? 1_555 99.1  ? 
43 NE2 ? B HIS 199 ? B HIS 234 ? 1_555 ZN ? F ZN . ? B ZN 402 ? 1_555 O   ? H HOH .   ? B HOH 695 ? 1_555 86.3  ? 
44 OD2 ? B ASP 220 ? B ASP 255 ? 1_555 ZN ? F ZN . ? B ZN 402 ? 1_555 O   ? H HOH .   ? B HOH 695 ? 1_555 82.7  ? 
45 O   ? H HOH .   ? B HOH 544 ? 1_555 ZN ? F ZN . ? B ZN 402 ? 1_555 O   ? H HOH .   ? B HOH 695 ? 1_555 82.1  ? 
46 OD2 ? B ASP 116 ? B ASP 151 ? 1_555 ZN ? E ZN . ? B ZN 401 ? 1_555 NE2 ? B HIS 117 ? B HIS 152 ? 1_555 89.1  ? 
47 OD2 ? B ASP 116 ? B ASP 151 ? 1_555 ZN ? E ZN . ? B ZN 401 ? 1_555 OD2 ? B ASP 220 ? B ASP 255 ? 1_555 171.4 ? 
48 NE2 ? B HIS 117 ? B HIS 152 ? 1_555 ZN ? E ZN . ? B ZN 401 ? 1_555 OD2 ? B ASP 220 ? B ASP 255 ? 1_555 91.2  ? 
49 OD2 ? B ASP 116 ? B ASP 151 ? 1_555 ZN ? E ZN . ? B ZN 401 ? 1_555 NE2 ? B HIS 267 ? B HIS 302 ? 1_555 86.0  ? 
50 NE2 ? B HIS 117 ? B HIS 152 ? 1_555 ZN ? E ZN . ? B ZN 401 ? 1_555 NE2 ? B HIS 267 ? B HIS 302 ? 1_555 104.0 ? 
51 OD2 ? B ASP 220 ? B ASP 255 ? 1_555 ZN ? E ZN . ? B ZN 401 ? 1_555 NE2 ? B HIS 267 ? B HIS 302 ? 1_555 102.3 ? 
52 OD2 ? B ASP 116 ? B ASP 151 ? 1_555 ZN ? E ZN . ? B ZN 401 ? 1_555 O   ? H HOH .   ? B HOH 544 ? 1_555 88.2  ? 
53 NE2 ? B HIS 117 ? B HIS 152 ? 1_555 ZN ? E ZN . ? B ZN 401 ? 1_555 O   ? H HOH .   ? B HOH 544 ? 1_555 94.1  ? 
54 OD2 ? B ASP 220 ? B ASP 255 ? 1_555 ZN ? E ZN . ? B ZN 401 ? 1_555 O   ? H HOH .   ? B HOH 544 ? 1_555 83.2  ? 
55 NE2 ? B HIS 267 ? B HIS 302 ? 1_555 ZN ? E ZN . ? B ZN 401 ? 1_555 O   ? H HOH .   ? B HOH 544 ? 1_555 160.8 ? 
56 OD2 ? B ASP 116 ? B ASP 151 ? 1_555 ZN ? E ZN . ? B ZN 401 ? 1_555 O   ? H HOH .   ? B HOH 685 ? 1_555 98.3  ? 
57 NE2 ? B HIS 117 ? B HIS 152 ? 1_555 ZN ? E ZN . ? B ZN 401 ? 1_555 O   ? H HOH .   ? B HOH 685 ? 1_555 170.1 ? 
58 OD2 ? B ASP 220 ? B ASP 255 ? 1_555 ZN ? E ZN . ? B ZN 401 ? 1_555 O   ? H HOH .   ? B HOH 685 ? 1_555 80.5  ? 
59 NE2 ? B HIS 267 ? B HIS 302 ? 1_555 ZN ? E ZN . ? B ZN 401 ? 1_555 O   ? H HOH .   ? B HOH 685 ? 1_555 83.2  ? 
60 O   ? H HOH .   ? B HOH 544 ? 1_555 ZN ? E ZN . ? B ZN 401 ? 1_555 O   ? H HOH .   ? B HOH 685 ? 1_555 79.6  ? 
# 
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 ALA 56  A . ? ALA 91  A PRO 57  A ? PRO 92  A 1 -4.88 
2 PHE 270 A . ? PHE 305 A PRO 271 A ? PRO 306 A 1 6.78  
3 ALA 56  B . ? ALA 91  B PRO 57  B ? PRO 92  B 1 -9.74 
4 PHE 270 B . ? PHE 305 B PRO 271 B ? PRO 306 B 1 7.53  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 6 ? 
AA2 ? 2 ? 
AA3 ? 7 ? 
AA4 ? 6 ? 
AA5 ? 2 ? 
AA6 ? 7 ? 
# 
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 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? parallel      
AA1 5 6 ? parallel      
AA2 1 2 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? parallel      
AA3 5 6 ? anti-parallel 
AA3 6 7 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? parallel      
AA4 5 6 ? parallel      
AA5 1 2 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA6 4 5 ? parallel      
AA6 5 6 ? anti-parallel 
AA6 6 7 ? 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 TYR A 12  ? LEU A 17  ? TYR A 47  LEU A 52  
AA1 2 PHE A 20  ? LEU A 32  ? PHE A 55  LEU A 67  
AA1 3 LEU A 58  ? ASN A 68  ? LEU A 93  ASN A 103 
AA1 4 LEU A 73  ? VAL A 76  ? LEU A 108 VAL A 111 
AA1 5 GLU A 107 ? TYR A 109 ? GLU A 142 TYR A 144 
AA1 6 VAL A 133 ? ARG A 135 ? VAL A 168 ARG A 170 
AA2 1 MET A 122 ? VAL A 123 ? MET A 157 VAL A 158 
AA2 2 GLN A 126 ? LEU A 127 ? GLN A 161 LEU A 162 
AA3 1 THR A 185 ? ASP A 186 ? THR A 220 ASP A 221 
AA3 2 ILE A 191 ? ALA A 195 ? ILE A 226 ALA A 230 
AA3 3 THR A 204 ? SER A 210 ? THR A 239 SER A 245 
AA3 4 GLN A 213 ? LEU A 217 ? GLN A 248 LEU A 252 
AA3 5 LEU A 262 ? ALA A 264 ? LEU A 297 ALA A 299 
AA3 6 ILE A 273 ? GLU A 279 ? ILE A 308 GLU A 314 
AA3 7 GLY A 282 ? PRO A 287 ? GLY A 317 PRO A 322 
AA4 1 TYR B 12  ? LEU B 17  ? TYR B 47  LEU B 52  
AA4 2 PHE B 20  ? LEU B 32  ? PHE B 55  LEU B 67  
AA4 3 LEU B 58  ? ASN B 68  ? LEU B 93  ASN B 103 
AA4 4 LEU B 73  ? VAL B 76  ? LEU B 108 VAL B 111 
AA4 5 GLU B 107 ? TYR B 109 ? GLU B 142 TYR B 144 
AA4 6 VAL B 133 ? ARG B 135 ? VAL B 168 ARG B 170 
AA5 1 MET B 122 ? VAL B 123 ? MET B 157 VAL B 158 
AA5 2 GLN B 126 ? LEU B 127 ? GLN B 161 LEU B 162 
AA6 1 THR B 185 ? ASP B 186 ? THR B 220 ASP B 221 
AA6 2 ILE B 191 ? ALA B 195 ? ILE B 226 ALA B 230 
AA6 3 THR B 204 ? SER B 210 ? THR B 239 SER B 245 
AA6 4 GLN B 213 ? LEU B 217 ? GLN B 248 LEU B 252 
AA6 5 LEU B 262 ? ALA B 264 ? LEU B 297 ALA B 299 
AA6 6 ILE B 273 ? GLU B 279 ? ILE B 308 GLU B 314 
AA6 7 GLY B 282 ? PRO B 287 ? GLY B 317 PRO B 322 
# 
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 N MET A 15  ? N MET A 50  O ILE A 22  ? O ILE A 57  
AA1 2 3 N ASP A 27  ? N ASP A 62  O VAL A 62  ? O VAL A 97  
AA1 3 4 N VAL A 67  ? N VAL A 102 O VAL A 74  ? O VAL A 109 
AA1 4 5 N LEU A 75  ? N LEU A 110 O TYR A 109 ? O TYR A 144 
AA1 5 6 N ILE A 108 ? N ILE A 143 O ARG A 135 ? O ARG A 170 
AA2 1 2 N VAL A 123 ? N VAL A 158 O GLN A 126 ? O GLN A 161 
AA3 1 2 N THR A 185 ? N THR A 220 O ALA A 193 ? O ALA A 228 
AA3 2 3 N LEU A 194 ? N LEU A 229 O THR A 205 ? O THR A 240 
AA3 3 4 N TYR A 206 ? N TYR A 241 O LEU A 217 ? O LEU A 252 
AA3 4 5 N ALA A 216 ? N ALA A 251 O LEU A 262 ? O LEU A 297 
AA3 5 6 N ILE A 263 ? N ILE A 298 O GLY A 274 ? O GLY A 309 
AA3 6 7 N HIS A 275 ? N HIS A 310 O VAL A 286 ? O VAL A 321 
AA4 1 2 N MET B 15  ? N MET B 50  O ILE B 22  ? O ILE B 57  
AA4 2 3 N ASP B 27  ? N ASP B 62  O VAL B 62  ? O VAL B 97  
AA4 3 4 N VAL B 67  ? N VAL B 102 O VAL B 74  ? O VAL B 109 
AA4 4 5 N LEU B 75  ? N LEU B 110 O TYR B 109 ? O TYR B 144 
AA4 5 6 N ILE B 108 ? N ILE B 143 O ARG B 135 ? O ARG B 170 
AA5 1 2 N VAL B 123 ? N VAL B 158 O GLN B 126 ? O GLN B 161 
AA6 1 2 N THR B 185 ? N THR B 220 O ALA B 193 ? O ALA B 228 
AA6 2 3 N LEU B 194 ? N LEU B 229 O THR B 205 ? O THR B 240 
AA6 3 4 N TYR B 206 ? N TYR B 241 O LEU B 217 ? O LEU B 252 
AA6 4 5 N ALA B 216 ? N ALA B 251 O LEU B 262 ? O LEU B 297 
AA6 5 6 N ILE B 263 ? N ILE B 298 O GLY B 274 ? O GLY B 309 
AA6 6 7 N HIS B 275 ? N HIS B 310 O VAL B 286 ? O VAL B 321 
# 
_pdbx_entry_details.entry_id                   8ZU4 
_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_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 O   A HOH 830 ? ? O A HOH 834 ? ? 1.90 
2  1 O   A HOH 737 ? ? O A HOH 796 ? ? 1.92 
3  1 O   A HOH 785 ? ? O A HOH 804 ? ? 1.92 
4  1 O   B HOH 715 ? ? O B HOH 745 ? ? 1.93 
5  1 OE1 B GLU 283 ? ? O B HOH 501 ? ? 1.94 
6  1 O   B HOH 778 ? ? O B HOH 787 ? ? 1.94 
7  1 O   B HOH 685 ? ? O B HOH 695 ? ? 1.96 
8  1 O   B HOH 654 ? ? O B HOH 733 ? ? 1.99 
9  1 O   B HOH 640 ? ? O B HOH 738 ? ? 2.00 
10 1 O   A HOH 835 ? ? O A HOH 837 ? ? 2.03 
11 1 O   A HOH 812 ? ? O A HOH 819 ? ? 2.04 
12 1 O   A HOH 657 ? ? O A HOH 712 ? ? 2.05 
13 1 OE1 A GLU 283 ? ? O A HOH 501 ? ? 2.08 
14 1 O   A HOH 691 ? ? O A HOH 709 ? ? 2.08 
15 1 O   B HOH 788 ? ? O B HOH 794 ? ? 2.10 
16 1 O   B HOH 635 ? ? O B HOH 694 ? ? 2.10 
17 1 O   A HOH 683 ? ? O A HOH 707 ? ? 2.13 
18 1 O   A HOH 698 ? ? O A HOH 762 ? ? 2.15 
19 1 O   A HOH 523 ? ? O B HOH 551 ? ? 2.16 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    HOH 
_pdbx_validate_symm_contact.auth_seq_id_1     740 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    O 
_pdbx_validate_symm_contact.auth_asym_id_2    A 
_pdbx_validate_symm_contact.auth_comp_id_2    HOH 
_pdbx_validate_symm_contact.auth_seq_id_2     821 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   2_556 
_pdbx_validate_symm_contact.dist              2.16 
# 
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 ASP A 112 ? ? 68.34  154.28  
2 1 ALA A 116 ? ? 52.68  -129.66 
3 1 LEU A 222 ? ? -92.05 -154.12 
4 1 ASP B 112 ? ? 70.77  154.78  
5 1 ALA B 116 ? ? 49.18  -126.52 
6 1 LEU B 222 ? ? -94.34 -157.01 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 835 ? 5.87 . 
2 1 O ? A HOH 836 ? 5.91 . 
3 1 O ? A HOH 837 ? 6.08 . 
4 1 O ? A HOH 838 ? 6.18 . 
# 
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 ALA 330 ? A ALA 295 
2 1 Y 1 A ALA 331 ? A ALA 296 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
GLN N    N  N N 74  
GLN CA   C  N S 75  
GLN C    C  N N 76  
GLN O    O  N N 77  
GLN CB   C  N N 78  
GLN CG   C  N N 79  
GLN CD   C  N N 80  
GLN OE1  O  N N 81  
GLN NE2  N  N N 82  
GLN OXT  O  N N 83  
GLN H    H  N N 84  
GLN H2   H  N N 85  
GLN HA   H  N N 86  
GLN HB2  H  N N 87  
GLN HB3  H  N N 88  
GLN HG2  H  N N 89  
GLN HG3  H  N N 90  
GLN HE21 H  N N 91  
GLN HE22 H  N N 92  
GLN HXT  H  N N 93  
GLU N    N  N N 94  
GLU CA   C  N S 95  
GLU C    C  N N 96  
GLU O    O  N N 97  
GLU CB   C  N N 98  
GLU CG   C  N N 99  
GLU CD   C  N N 100 
GLU OE1  O  N N 101 
GLU OE2  O  N N 102 
GLU OXT  O  N N 103 
GLU H    H  N N 104 
GLU H2   H  N N 105 
GLU HA   H  N N 106 
GLU HB2  H  N N 107 
GLU HB3  H  N N 108 
GLU HG2  H  N N 109 
GLU HG3  H  N N 110 
GLU HE2  H  N N 111 
GLU HXT  H  N N 112 
GLY N    N  N N 113 
GLY CA   C  N N 114 
GLY C    C  N N 115 
GLY O    O  N N 116 
GLY OXT  O  N N 117 
GLY H    H  N N 118 
GLY H2   H  N N 119 
GLY HA2  H  N N 120 
GLY HA3  H  N N 121 
GLY HXT  H  N N 122 
HIS N    N  N N 123 
HIS CA   C  N S 124 
HIS C    C  N N 125 
HIS O    O  N N 126 
HIS CB   C  N N 127 
HIS CG   C  Y N 128 
HIS ND1  N  Y N 129 
HIS CD2  C  Y N 130 
HIS CE1  C  Y N 131 
HIS NE2  N  Y N 132 
HIS OXT  O  N N 133 
HIS H    H  N N 134 
HIS H2   H  N N 135 
HIS HA   H  N N 136 
HIS HB2  H  N N 137 
HIS HB3  H  N N 138 
HIS HD1  H  N N 139 
HIS HD2  H  N N 140 
HIS HE1  H  N N 141 
HIS HE2  H  N N 142 
HIS HXT  H  N N 143 
HOH O    O  N N 144 
HOH H1   H  N N 145 
HOH H2   H  N N 146 
ILE N    N  N N 147 
ILE CA   C  N S 148 
ILE C    C  N N 149 
ILE O    O  N N 150 
ILE CB   C  N S 151 
ILE CG1  C  N N 152 
ILE CG2  C  N N 153 
ILE CD1  C  N N 154 
ILE OXT  O  N N 155 
ILE H    H  N N 156 
ILE H2   H  N N 157 
ILE HA   H  N N 158 
ILE HB   H  N N 159 
ILE HG12 H  N N 160 
ILE HG13 H  N N 161 
ILE HG21 H  N N 162 
ILE HG22 H  N N 163 
ILE HG23 H  N N 164 
ILE HD11 H  N N 165 
ILE HD12 H  N N 166 
ILE HD13 H  N N 167 
ILE HXT  H  N N 168 
LEU N    N  N N 169 
LEU CA   C  N S 170 
LEU C    C  N N 171 
LEU O    O  N N 172 
LEU CB   C  N N 173 
LEU CG   C  N N 174 
LEU CD1  C  N N 175 
LEU CD2  C  N N 176 
LEU OXT  O  N N 177 
LEU H    H  N N 178 
LEU H2   H  N N 179 
LEU HA   H  N N 180 
LEU HB2  H  N N 181 
LEU HB3  H  N N 182 
LEU HG   H  N N 183 
LEU HD11 H  N N 184 
LEU HD12 H  N N 185 
LEU HD13 H  N N 186 
LEU HD21 H  N N 187 
LEU HD22 H  N N 188 
LEU HD23 H  N N 189 
LEU HXT  H  N N 190 
LYS N    N  N N 191 
LYS CA   C  N S 192 
LYS C    C  N N 193 
LYS O    O  N N 194 
LYS CB   C  N N 195 
LYS CG   C  N N 196 
LYS CD   C  N N 197 
LYS CE   C  N N 198 
LYS NZ   N  N N 199 
LYS OXT  O  N N 200 
LYS H    H  N N 201 
LYS H2   H  N N 202 
LYS HA   H  N N 203 
LYS HB2  H  N N 204 
LYS HB3  H  N N 205 
LYS HG2  H  N N 206 
LYS HG3  H  N N 207 
LYS HD2  H  N N 208 
LYS HD3  H  N N 209 
LYS HE2  H  N N 210 
LYS HE3  H  N N 211 
LYS HZ1  H  N N 212 
LYS HZ2  H  N N 213 
LYS HZ3  H  N N 214 
LYS HXT  H  N N 215 
MET N    N  N N 216 
MET CA   C  N S 217 
MET C    C  N N 218 
MET O    O  N N 219 
MET CB   C  N N 220 
MET CG   C  N N 221 
MET SD   S  N N 222 
MET CE   C  N N 223 
MET OXT  O  N N 224 
MET H    H  N N 225 
MET H2   H  N N 226 
MET HA   H  N N 227 
MET HB2  H  N N 228 
MET HB3  H  N N 229 
MET HG2  H  N N 230 
MET HG3  H  N N 231 
MET HE1  H  N N 232 
MET HE2  H  N N 233 
MET HE3  H  N N 234 
MET HXT  H  N N 235 
PHE N    N  N N 236 
PHE CA   C  N S 237 
PHE C    C  N N 238 
PHE O    O  N N 239 
PHE CB   C  N N 240 
PHE CG   C  Y N 241 
PHE CD1  C  Y N 242 
PHE CD2  C  Y N 243 
PHE CE1  C  Y N 244 
PHE CE2  C  Y N 245 
PHE CZ   C  Y N 246 
PHE OXT  O  N N 247 
PHE H    H  N N 248 
PHE H2   H  N N 249 
PHE HA   H  N N 250 
PHE HB2  H  N N 251 
PHE HB3  H  N N 252 
PHE HD1  H  N N 253 
PHE HD2  H  N N 254 
PHE HE1  H  N N 255 
PHE HE2  H  N N 256 
PHE HZ   H  N N 257 
PHE HXT  H  N N 258 
PRO N    N  N N 259 
PRO CA   C  N S 260 
PRO C    C  N N 261 
PRO O    O  N N 262 
PRO CB   C  N N 263 
PRO CG   C  N N 264 
PRO CD   C  N N 265 
PRO OXT  O  N N 266 
PRO H    H  N N 267 
PRO HA   H  N N 268 
PRO HB2  H  N N 269 
PRO HB3  H  N N 270 
PRO HG2  H  N N 271 
PRO HG3  H  N N 272 
PRO HD2  H  N N 273 
PRO HD3  H  N N 274 
PRO HXT  H  N N 275 
SER N    N  N N 276 
SER CA   C  N S 277 
SER C    C  N N 278 
SER O    O  N N 279 
SER CB   C  N N 280 
SER OG   O  N N 281 
SER OXT  O  N N 282 
SER H    H  N N 283 
SER H2   H  N N 284 
SER HA   H  N N 285 
SER HB2  H  N N 286 
SER HB3  H  N N 287 
SER HG   H  N N 288 
SER HXT  H  N N 289 
THR N    N  N N 290 
THR CA   C  N S 291 
THR C    C  N N 292 
THR O    O  N N 293 
THR CB   C  N R 294 
THR OG1  O  N N 295 
THR CG2  C  N N 296 
THR OXT  O  N N 297 
THR H    H  N N 298 
THR H2   H  N N 299 
THR HA   H  N N 300 
THR HB   H  N N 301 
THR HG1  H  N N 302 
THR HG21 H  N N 303 
THR HG22 H  N N 304 
THR HG23 H  N N 305 
THR HXT  H  N N 306 
TRP N    N  N N 307 
TRP CA   C  N S 308 
TRP C    C  N N 309 
TRP O    O  N N 310 
TRP CB   C  N N 311 
TRP CG   C  Y N 312 
TRP CD1  C  Y N 313 
TRP CD2  C  Y N 314 
TRP NE1  N  Y N 315 
TRP CE2  C  Y N 316 
TRP CE3  C  Y N 317 
TRP CZ2  C  Y N 318 
TRP CZ3  C  Y N 319 
TRP CH2  C  Y N 320 
TRP OXT  O  N N 321 
TRP H    H  N N 322 
TRP H2   H  N N 323 
TRP HA   H  N N 324 
TRP HB2  H  N N 325 
TRP HB3  H  N N 326 
TRP HD1  H  N N 327 
TRP HE1  H  N N 328 
TRP HE3  H  N N 329 
TRP HZ2  H  N N 330 
TRP HZ3  H  N N 331 
TRP HH2  H  N N 332 
TRP HXT  H  N N 333 
TYR N    N  N N 334 
TYR CA   C  N S 335 
TYR C    C  N N 336 
TYR O    O  N N 337 
TYR CB   C  N N 338 
TYR CG   C  Y N 339 
TYR CD1  C  Y N 340 
TYR CD2  C  Y N 341 
TYR CE1  C  Y N 342 
TYR CE2  C  Y N 343 
TYR CZ   C  Y N 344 
TYR OH   O  N N 345 
TYR OXT  O  N N 346 
TYR H    H  N N 347 
TYR H2   H  N N 348 
TYR HA   H  N N 349 
TYR HB2  H  N N 350 
TYR HB3  H  N N 351 
TYR HD1  H  N N 352 
TYR HD2  H  N N 353 
TYR HE1  H  N N 354 
TYR HE2  H  N N 355 
TYR HH   H  N N 356 
TYR HXT  H  N N 357 
VAL N    N  N N 358 
VAL CA   C  N S 359 
VAL C    C  N N 360 
VAL O    O  N N 361 
VAL CB   C  N N 362 
VAL CG1  C  N N 363 
VAL CG2  C  N N 364 
VAL OXT  O  N N 365 
VAL H    H  N N 366 
VAL H2   H  N N 367 
VAL HA   H  N N 368 
VAL HB   H  N N 369 
VAL HG11 H  N N 370 
VAL HG12 H  N N 371 
VAL HG13 H  N N 372 
VAL HG21 H  N N 373 
VAL HG22 H  N N 374 
VAL HG23 H  N N 375 
VAL HXT  H  N N 376 
ZN  ZN   ZN N N 377 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
GLN N   CA   sing N N 70  
GLN N   H    sing N N 71  
GLN N   H2   sing N N 72  
GLN CA  C    sing N N 73  
GLN CA  CB   sing N N 74  
GLN CA  HA   sing N N 75  
GLN C   O    doub N N 76  
GLN C   OXT  sing N N 77  
GLN CB  CG   sing N N 78  
GLN CB  HB2  sing N N 79  
GLN CB  HB3  sing N N 80  
GLN CG  CD   sing N N 81  
GLN CG  HG2  sing N N 82  
GLN CG  HG3  sing N N 83  
GLN CD  OE1  doub N N 84  
GLN CD  NE2  sing N N 85  
GLN NE2 HE21 sing N N 86  
GLN NE2 HE22 sing N N 87  
GLN OXT HXT  sing N N 88  
GLU N   CA   sing N N 89  
GLU N   H    sing N N 90  
GLU N   H2   sing N N 91  
GLU CA  C    sing N N 92  
GLU CA  CB   sing N N 93  
GLU CA  HA   sing N N 94  
GLU C   O    doub N N 95  
GLU C   OXT  sing N N 96  
GLU CB  CG   sing N N 97  
GLU CB  HB2  sing N N 98  
GLU CB  HB3  sing N N 99  
GLU CG  CD   sing N N 100 
GLU CG  HG2  sing N N 101 
GLU CG  HG3  sing N N 102 
GLU CD  OE1  doub N N 103 
GLU CD  OE2  sing N N 104 
GLU OE2 HE2  sing N N 105 
GLU OXT HXT  sing N N 106 
GLY N   CA   sing N N 107 
GLY N   H    sing N N 108 
GLY N   H2   sing N N 109 
GLY CA  C    sing N N 110 
GLY CA  HA2  sing N N 111 
GLY CA  HA3  sing N N 112 
GLY C   O    doub N N 113 
GLY C   OXT  sing N N 114 
GLY OXT HXT  sing N N 115 
HIS N   CA   sing N N 116 
HIS N   H    sing N N 117 
HIS N   H2   sing N N 118 
HIS CA  C    sing N N 119 
HIS CA  CB   sing N N 120 
HIS CA  HA   sing N N 121 
HIS C   O    doub N N 122 
HIS C   OXT  sing N N 123 
HIS CB  CG   sing N N 124 
HIS CB  HB2  sing N N 125 
HIS CB  HB3  sing N N 126 
HIS CG  ND1  sing Y N 127 
HIS CG  CD2  doub Y N 128 
HIS ND1 CE1  doub Y N 129 
HIS ND1 HD1  sing N N 130 
HIS CD2 NE2  sing Y N 131 
HIS CD2 HD2  sing N N 132 
HIS CE1 NE2  sing Y N 133 
HIS CE1 HE1  sing N N 134 
HIS NE2 HE2  sing N N 135 
HIS OXT HXT  sing N N 136 
HOH O   H1   sing N N 137 
HOH O   H2   sing N N 138 
ILE N   CA   sing N N 139 
ILE N   H    sing N N 140 
ILE N   H2   sing N N 141 
ILE CA  C    sing N N 142 
ILE CA  CB   sing N N 143 
ILE CA  HA   sing N N 144 
ILE C   O    doub N N 145 
ILE C   OXT  sing N N 146 
ILE CB  CG1  sing N N 147 
ILE CB  CG2  sing N N 148 
ILE CB  HB   sing N N 149 
ILE CG1 CD1  sing N N 150 
ILE CG1 HG12 sing N N 151 
ILE CG1 HG13 sing N N 152 
ILE CG2 HG21 sing N N 153 
ILE CG2 HG22 sing N N 154 
ILE CG2 HG23 sing N N 155 
ILE CD1 HD11 sing N N 156 
ILE CD1 HD12 sing N N 157 
ILE CD1 HD13 sing N N 158 
ILE OXT HXT  sing N N 159 
LEU N   CA   sing N N 160 
LEU N   H    sing N N 161 
LEU N   H2   sing N N 162 
LEU CA  C    sing N N 163 
LEU CA  CB   sing N N 164 
LEU CA  HA   sing N N 165 
LEU C   O    doub N N 166 
LEU C   OXT  sing N N 167 
LEU CB  CG   sing N N 168 
LEU CB  HB2  sing N N 169 
LEU CB  HB3  sing N N 170 
LEU CG  CD1  sing N N 171 
LEU CG  CD2  sing N N 172 
LEU CG  HG   sing N N 173 
LEU CD1 HD11 sing N N 174 
LEU CD1 HD12 sing N N 175 
LEU CD1 HD13 sing N N 176 
LEU CD2 HD21 sing N N 177 
LEU CD2 HD22 sing N N 178 
LEU CD2 HD23 sing N N 179 
LEU OXT HXT  sing N N 180 
LYS N   CA   sing N N 181 
LYS N   H    sing N N 182 
LYS N   H2   sing N N 183 
LYS CA  C    sing N N 184 
LYS CA  CB   sing N N 185 
LYS CA  HA   sing N N 186 
LYS C   O    doub N N 187 
LYS C   OXT  sing N N 188 
LYS CB  CG   sing N N 189 
LYS CB  HB2  sing N N 190 
LYS CB  HB3  sing N N 191 
LYS CG  CD   sing N N 192 
LYS CG  HG2  sing N N 193 
LYS CG  HG3  sing N N 194 
LYS CD  CE   sing N N 195 
LYS CD  HD2  sing N N 196 
LYS CD  HD3  sing N N 197 
LYS CE  NZ   sing N N 198 
LYS CE  HE2  sing N N 199 
LYS CE  HE3  sing N N 200 
LYS NZ  HZ1  sing N N 201 
LYS NZ  HZ2  sing N N 202 
LYS NZ  HZ3  sing N N 203 
LYS OXT HXT  sing N N 204 
MET N   CA   sing N N 205 
MET N   H    sing N N 206 
MET N   H2   sing N N 207 
MET CA  C    sing N N 208 
MET CA  CB   sing N N 209 
MET CA  HA   sing N N 210 
MET C   O    doub N N 211 
MET C   OXT  sing N N 212 
MET CB  CG   sing N N 213 
MET CB  HB2  sing N N 214 
MET CB  HB3  sing N N 215 
MET CG  SD   sing N N 216 
MET CG  HG2  sing N N 217 
MET CG  HG3  sing N N 218 
MET SD  CE   sing N N 219 
MET CE  HE1  sing N N 220 
MET CE  HE2  sing N N 221 
MET CE  HE3  sing N N 222 
MET OXT HXT  sing N N 223 
PHE N   CA   sing N N 224 
PHE N   H    sing N N 225 
PHE N   H2   sing N N 226 
PHE CA  C    sing N N 227 
PHE CA  CB   sing N N 228 
PHE CA  HA   sing N N 229 
PHE C   O    doub N N 230 
PHE C   OXT  sing N N 231 
PHE CB  CG   sing N N 232 
PHE CB  HB2  sing N N 233 
PHE CB  HB3  sing N N 234 
PHE CG  CD1  doub Y N 235 
PHE CG  CD2  sing Y N 236 
PHE CD1 CE1  sing Y N 237 
PHE CD1 HD1  sing N N 238 
PHE CD2 CE2  doub Y N 239 
PHE CD2 HD2  sing N N 240 
PHE CE1 CZ   doub Y N 241 
PHE CE1 HE1  sing N N 242 
PHE CE2 CZ   sing Y N 243 
PHE CE2 HE2  sing N N 244 
PHE CZ  HZ   sing N N 245 
PHE OXT HXT  sing N N 246 
PRO N   CA   sing N N 247 
PRO N   CD   sing N N 248 
PRO N   H    sing N N 249 
PRO CA  C    sing N N 250 
PRO CA  CB   sing N N 251 
PRO CA  HA   sing N N 252 
PRO C   O    doub N N 253 
PRO C   OXT  sing N N 254 
PRO CB  CG   sing N N 255 
PRO CB  HB2  sing N N 256 
PRO CB  HB3  sing N N 257 
PRO CG  CD   sing N N 258 
PRO CG  HG2  sing N N 259 
PRO CG  HG3  sing N N 260 
PRO CD  HD2  sing N N 261 
PRO CD  HD3  sing N N 262 
PRO OXT HXT  sing N N 263 
SER N   CA   sing N N 264 
SER N   H    sing N N 265 
SER N   H2   sing N N 266 
SER CA  C    sing N N 267 
SER CA  CB   sing N N 268 
SER CA  HA   sing N N 269 
SER C   O    doub N N 270 
SER C   OXT  sing N N 271 
SER CB  OG   sing N N 272 
SER CB  HB2  sing N N 273 
SER CB  HB3  sing N N 274 
SER OG  HG   sing N N 275 
SER OXT HXT  sing N N 276 
THR N   CA   sing N N 277 
THR N   H    sing N N 278 
THR N   H2   sing N N 279 
THR CA  C    sing N N 280 
THR CA  CB   sing N N 281 
THR CA  HA   sing N N 282 
THR C   O    doub N N 283 
THR C   OXT  sing N N 284 
THR CB  OG1  sing N N 285 
THR CB  CG2  sing N N 286 
THR CB  HB   sing N N 287 
THR OG1 HG1  sing N N 288 
THR CG2 HG21 sing N N 289 
THR CG2 HG22 sing N N 290 
THR CG2 HG23 sing N N 291 
THR OXT HXT  sing N N 292 
TRP N   CA   sing N N 293 
TRP N   H    sing N N 294 
TRP N   H2   sing N N 295 
TRP CA  C    sing N N 296 
TRP CA  CB   sing N N 297 
TRP CA  HA   sing N N 298 
TRP C   O    doub N N 299 
TRP C   OXT  sing N N 300 
TRP CB  CG   sing N N 301 
TRP CB  HB2  sing N N 302 
TRP CB  HB3  sing N N 303 
TRP CG  CD1  doub Y N 304 
TRP CG  CD2  sing Y N 305 
TRP CD1 NE1  sing Y N 306 
TRP CD1 HD1  sing N N 307 
TRP CD2 CE2  doub Y N 308 
TRP CD2 CE3  sing Y N 309 
TRP NE1 CE2  sing Y N 310 
TRP NE1 HE1  sing N N 311 
TRP CE2 CZ2  sing Y N 312 
TRP CE3 CZ3  doub Y N 313 
TRP CE3 HE3  sing N N 314 
TRP CZ2 CH2  doub Y N 315 
TRP CZ2 HZ2  sing N N 316 
TRP CZ3 CH2  sing Y N 317 
TRP CZ3 HZ3  sing N N 318 
TRP CH2 HH2  sing N N 319 
TRP OXT HXT  sing N N 320 
TYR N   CA   sing N N 321 
TYR N   H    sing N N 322 
TYR N   H2   sing N N 323 
TYR CA  C    sing N N 324 
TYR CA  CB   sing N N 325 
TYR CA  HA   sing N N 326 
TYR C   O    doub N N 327 
TYR C   OXT  sing N N 328 
TYR CB  CG   sing N N 329 
TYR CB  HB2  sing N N 330 
TYR CB  HB3  sing N N 331 
TYR CG  CD1  doub Y N 332 
TYR CG  CD2  sing Y N 333 
TYR CD1 CE1  sing Y N 334 
TYR CD1 HD1  sing N N 335 
TYR CD2 CE2  doub Y N 336 
TYR CD2 HD2  sing N N 337 
TYR CE1 CZ   doub Y N 338 
TYR CE1 HE1  sing N N 339 
TYR CE2 CZ   sing Y N 340 
TYR CE2 HE2  sing N N 341 
TYR CZ  OH   sing N N 342 
TYR OH  HH   sing N N 343 
TYR OXT HXT  sing N N 344 
VAL N   CA   sing N N 345 
VAL N   H    sing N N 346 
VAL N   H2   sing N N 347 
VAL CA  C    sing N N 348 
VAL CA  CB   sing N N 349 
VAL CA  HA   sing N N 350 
VAL C   O    doub N N 351 
VAL C   OXT  sing N N 352 
VAL CB  CG1  sing N N 353 
VAL CB  CG2  sing N N 354 
VAL CB  HB   sing N N 355 
VAL CG1 HG11 sing N N 356 
VAL CG1 HG12 sing N N 357 
VAL CG1 HG13 sing N N 358 
VAL CG2 HG21 sing N N 359 
VAL CG2 HG22 sing N N 360 
VAL CG2 HG23 sing N N 361 
VAL OXT HXT  sing N N 362 
# 
_pdbx_audit_support.funding_organization   'National Natural Science Foundation of China (NSFC)' 
_pdbx_audit_support.country                China 
_pdbx_audit_support.grant_number           22078129 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   1P9E 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8ZU4 
_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]   0.007860 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.003305 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.011585 
_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]   0.018450 
_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  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . ALA A 1 1   ? 36.230  -60.833 -8.575  1.00 33.15 ? 36  ALA A N   1 
ATOM   2    C  CA  . ALA A 1 1   ? 35.912  -59.636 -7.798  1.00 30.99 ? 36  ALA A CA  1 
ATOM   3    C  C   . ALA A 1 1   ? 35.028  -59.943 -6.586  1.00 40.50 ? 36  ALA A C   1 
ATOM   4    O  O   . ALA A 1 1   ? 34.052  -60.689 -6.692  1.00 32.62 ? 36  ALA A O   1 
ATOM   5    C  CB  . ALA A 1 1   ? 35.245  -58.592 -8.683  1.00 38.74 ? 36  ALA A CB  1 
ATOM   6    N  N   . ALA A 1 2   ? 35.361  -59.354 -5.441  1.00 30.42 ? 37  ALA A N   1 
ATOM   7    C  CA  . ALA A 1 2   ? 34.558  -59.565 -4.240  1.00 27.71 ? 37  ALA A CA  1 
ATOM   8    C  C   . ALA A 1 2   ? 33.176  -58.950 -4.432  1.00 28.27 ? 37  ALA A C   1 
ATOM   9    O  O   . ALA A 1 2   ? 33.072  -57.768 -4.781  1.00 29.09 ? 37  ALA A O   1 
ATOM   10   C  CB  . ALA A 1 2   ? 35.235  -58.912 -3.037  1.00 31.61 ? 37  ALA A CB  1 
ATOM   11   N  N   . PRO A 1 3   ? 32.100  -59.705 -4.226  1.00 27.03 ? 38  PRO A N   1 
ATOM   12   C  CA  . PRO A 1 3   ? 30.760  -59.120 -4.360  1.00 26.60 ? 38  PRO A CA  1 
ATOM   13   C  C   . PRO A 1 3   ? 30.520  -58.043 -3.319  1.00 27.43 ? 38  PRO A C   1 
ATOM   14   O  O   . PRO A 1 3   ? 31.031  -58.101 -2.199  1.00 27.08 ? 38  PRO A O   1 
ATOM   15   C  CB  . PRO A 1 3   ? 29.814  -60.304 -4.124  1.00 30.89 ? 38  PRO A CB  1 
ATOM   16   C  CG  . PRO A 1 3   ? 30.661  -61.514 -3.960  1.00 36.16 ? 38  PRO A CG  1 
ATOM   17   C  CD  . PRO A 1 3   ? 32.088  -61.175 -4.181  1.00 31.68 ? 38  PRO A CD  1 
ATOM   18   N  N   . GLN A 1 4   ? 29.725  -57.048 -3.692  1.00 25.06 ? 39  GLN A N   1 
ATOM   19   C  CA  . GLN A 1 4   ? 29.297  -56.084 -2.695  1.00 24.18 ? 39  GLN A CA  1 
ATOM   20   C  C   . GLN A 1 4   ? 28.302  -56.744 -1.751  1.00 33.08 ? 39  GLN A C   1 
ATOM   21   O  O   . GLN A 1 4   ? 27.633  -57.719 -2.104  1.00 28.85 ? 39  GLN A O   1 
ATOM   22   C  CB  . GLN A 1 4   ? 28.686  -54.856 -3.363  1.00 23.95 ? 39  GLN A CB  1 
ATOM   23   C  CG  . GLN A 1 4   ? 29.676  -54.129 -4.270  1.00 24.48 ? 39  GLN A CG  1 
ATOM   24   C  CD  . GLN A 1 4   ? 29.101  -52.853 -4.835  1.00 29.77 ? 39  GLN A CD  1 
ATOM   25   O  OE1 . GLN A 1 4   ? 27.891  -52.635 -4.800  1.00 32.27 ? 39  GLN A OE1 1 
ATOM   26   N  NE2 . GLN A 1 4   ? 29.963  -52.004 -5.369  1.00 25.87 ? 39  GLN A NE2 1 
ATOM   27   N  N   . VAL A 1 5   ? 28.231  -56.227 -0.531  1.00 26.56 ? 40  VAL A N   1 
ATOM   28   C  CA  . VAL A 1 5   ? 27.345  -56.763 0.496   1.00 28.49 ? 40  VAL A CA  1 
ATOM   29   C  C   . VAL A 1 5   ? 26.060  -55.955 0.598   1.00 23.36 ? 40  VAL A C   1 
ATOM   30   O  O   . VAL A 1 5   ? 24.963  -56.513 0.547   1.00 28.22 ? 40  VAL A O   1 
ATOM   31   C  CB  . VAL A 1 5   ? 28.078  -56.864 1.855   1.00 27.71 ? 40  VAL A CB  1 
ATOM   32   C  CG1 . VAL A 1 5   ? 27.154  -57.423 2.923   1.00 29.14 ? 40  VAL A CG1 1 
ATOM   33   C  CG2 . VAL A 1 5   ? 29.310  -57.743 1.727   1.00 24.04 ? 40  VAL A CG2 1 
ATOM   34   N  N   . ARG A 1 6   ? 26.187  -54.631 0.725   1.00 23.59 ? 41  ARG A N   1 
ATOM   35   C  CA  . ARG A 1 6   ? 25.051  -53.708 0.653   1.00 25.30 ? 41  ARG A CA  1 
ATOM   36   C  C   . ARG A 1 6   ? 23.990  -53.984 1.718   1.00 32.24 ? 41  ARG A C   1 
ATOM   37   O  O   . ARG A 1 6   ? 22.789  -53.986 1.445   1.00 29.02 ? 41  ARG A O   1 
ATOM   38   C  CB  . ARG A 1 6   ? 24.439  -53.671 -0.747  1.00 25.86 ? 41  ARG A CB  1 
ATOM   39   C  CG  . ARG A 1 6   ? 25.356  -53.114 -1.786  1.00 27.35 ? 41  ARG A CG  1 
ATOM   40   C  CD  . ARG A 1 6   ? 24.558  -52.501 -2.919  1.00 33.25 ? 41  ARG A CD  1 
ATOM   41   N  NE  . ARG A 1 6   ? 25.439  -52.031 -3.979  1.00 49.09 ? 41  ARG A NE  1 
ATOM   42   C  CZ  . ARG A 1 6   ? 25.103  -51.124 -4.885  1.00 49.07 ? 41  ARG A CZ  1 
ATOM   43   N  NH1 . ARG A 1 6   ? 23.891  -50.588 -4.910  1.00 37.03 ? 41  ARG A NH1 1 
ATOM   44   N  NH2 . ARG A 1 6   ? 26.007  -50.741 -5.784  1.00 30.45 ? 41  ARG A NH2 1 
ATOM   45   N  N   . THR A 1 7   ? 24.438  -54.211 2.945   1.00 24.54 ? 42  THR A N   1 
ATOM   46   C  CA  . THR A 1 7   ? 23.534  -54.255 4.081   1.00 21.36 ? 42  THR A CA  1 
ATOM   47   C  C   . THR A 1 7   ? 24.082  -53.369 5.189   1.00 29.70 ? 42  THR A C   1 
ATOM   48   O  O   . THR A 1 7   ? 25.296  -53.218 5.348   1.00 24.48 ? 42  THR A O   1 
ATOM   49   C  CB  . THR A 1 7   ? 23.306  -55.681 4.591   1.00 28.24 ? 42  THR A CB  1 
ATOM   50   O  OG1 . THR A 1 7   ? 24.559  -56.275 4.941   1.00 35.11 ? 42  THR A OG1 1 
ATOM   51   C  CG2 . THR A 1 7   ? 22.600  -56.519 3.528   1.00 30.21 ? 42  THR A CG2 1 
ATOM   52   N  N   . SER A 1 8   ? 23.175  -52.762 5.939   1.00 23.69 ? 43  SER A N   1 
ATOM   53   C  CA  . SER A 1 8   ? 23.585  -51.881 7.014   1.00 19.90 ? 43  SER A CA  1 
ATOM   54   C  C   . SER A 1 8   ? 23.870  -52.682 8.279   1.00 20.84 ? 43  SER A C   1 
ATOM   55   O  O   . SER A 1 8   ? 23.400  -53.809 8.455   1.00 24.81 ? 43  SER A O   1 
ATOM   56   C  CB  . SER A 1 8   ? 22.500  -50.839 7.279   1.00 22.69 ? 43  SER A CB  1 
ATOM   57   O  OG  . SER A 1 8   ? 22.425  -49.917 6.205   1.00 22.94 ? 43  SER A OG  1 
ATOM   58   N  N   . ALA A 1 9   ? 24.645  -52.070 9.174   1.00 19.00 ? 44  ALA A N   1 
ATOM   59   C  CA  . ALA A 1 9   ? 24.938  -52.672 10.460  1.00 24.78 ? 44  ALA A CA  1 
ATOM   60   C  C   . ALA A 1 9   ? 23.656  -52.783 11.285  1.00 23.89 ? 44  ALA A C   1 
ATOM   61   O  O   . ALA A 1 9   ? 22.686  -52.063 11.032  1.00 22.78 ? 44  ALA A O   1 
ATOM   62   C  CB  . ALA A 1 9   ? 25.934  -51.791 11.210  1.00 22.03 ? 44  ALA A CB  1 
ATOM   63   N  N   . PRO A 1 10  ? 23.627  -53.681 12.275  1.00 23.33 ? 45  PRO A N   1 
ATOM   64   C  CA  . PRO A 1 10  ? 22.461  -53.759 13.164  1.00 25.34 ? 45  PRO A CA  1 
ATOM   65   C  C   . PRO A 1 10  ? 22.149  -52.396 13.763  1.00 26.75 ? 45  PRO A C   1 
ATOM   66   O  O   . PRO A 1 10  ? 23.041  -51.654 14.182  1.00 21.82 ? 45  PRO A O   1 
ATOM   67   C  CB  . PRO A 1 10  ? 22.893  -54.761 14.239  1.00 29.88 ? 45  PRO A CB  1 
ATOM   68   C  CG  . PRO A 1 10  ? 23.986  -55.560 13.613  1.00 35.24 ? 45  PRO A CG  1 
ATOM   69   C  CD  . PRO A 1 10  ? 24.674  -54.657 12.636  1.00 29.37 ? 45  PRO A CD  1 
ATOM   70   N  N   . GLY A 1 11  ? 20.865  -52.057 13.775  1.00 24.90 ? 46  GLY A N   1 
ATOM   71   C  CA  . GLY A 1 11  ? 20.461  -50.710 14.116  1.00 19.51 ? 46  GLY A CA  1 
ATOM   72   C  C   . GLY A 1 11  ? 20.241  -50.519 15.599  1.00 23.11 ? 46  GLY A C   1 
ATOM   73   O  O   . GLY A 1 11  ? 19.109  -50.310 16.041  1.00 21.03 ? 46  GLY A O   1 
ATOM   74   N  N   . TYR A 1 12  ? 21.308  -50.621 16.386  1.00 20.04 ? 47  TYR A N   1 
ATOM   75   C  CA  . TYR A 1 12  ? 21.252  -50.245 17.790  1.00 20.43 ? 47  TYR A CA  1 
ATOM   76   C  C   . TYR A 1 12  ? 22.491  -49.440 18.144  1.00 28.35 ? 47  TYR A C   1 
ATOM   77   O  O   . TYR A 1 12  ? 23.571  -49.648 17.581  1.00 23.89 ? 47  TYR A O   1 
ATOM   78   C  CB  . TYR A 1 12  ? 21.054  -51.424 18.748  1.00 19.66 ? 47  TYR A CB  1 
ATOM   79   C  CG  . TYR A 1 12  ? 22.178  -52.440 18.792  1.00 21.68 ? 47  TYR A CG  1 
ATOM   80   C  CD1 . TYR A 1 12  ? 22.263  -53.458 17.846  1.00 22.19 ? 47  TYR A CD1 1 
ATOM   81   C  CD2 . TYR A 1 12  ? 23.134  -52.403 19.804  1.00 19.88 ? 47  TYR A CD2 1 
ATOM   82   C  CE1 . TYR A 1 12  ? 23.284  -54.401 17.898  1.00 23.17 ? 47  TYR A CE1 1 
ATOM   83   C  CE2 . TYR A 1 12  ? 24.162  -53.338 19.861  1.00 18.92 ? 47  TYR A CE2 1 
ATOM   84   C  CZ  . TYR A 1 12  ? 24.228  -54.334 18.911  1.00 23.74 ? 47  TYR A CZ  1 
ATOM   85   O  OH  . TYR A 1 12  ? 25.248  -55.260 18.983  1.00 27.34 ? 47  TYR A OH  1 
ATOM   86   N  N   . TYR A 1 13  ? 22.312  -48.498 19.066  1.00 19.41 ? 48  TYR A N   1 
ATOM   87   C  CA  . TYR A 1 13  ? 23.393  -47.626 19.514  1.00 17.45 ? 48  TYR A CA  1 
ATOM   88   C  C   . TYR A 1 13  ? 23.408  -47.594 21.036  1.00 18.79 ? 48  TYR A C   1 
ATOM   89   O  O   . TYR A 1 13  ? 22.444  -47.137 21.656  1.00 20.32 ? 48  TYR A O   1 
ATOM   90   C  CB  . TYR A 1 13  ? 23.229  -46.210 18.953  1.00 18.45 ? 48  TYR A CB  1 
ATOM   91   C  CG  . TYR A 1 13  ? 24.376  -45.308 19.336  1.00 26.33 ? 48  TYR A CG  1 
ATOM   92   C  CD1 . TYR A 1 13  ? 25.558  -45.321 18.610  1.00 34.49 ? 48  TYR A CD1 1 
ATOM   93   C  CD2 . TYR A 1 13  ? 24.289  -44.462 20.432  1.00 18.03 ? 48  TYR A CD2 1 
ATOM   94   C  CE1 . TYR A 1 13  ? 26.617  -44.514 18.961  1.00 32.17 ? 48  TYR A CE1 1 
ATOM   95   C  CE2 . TYR A 1 13  ? 25.348  -43.645 20.793  1.00 17.87 ? 48  TYR A CE2 1 
ATOM   96   C  CZ  . TYR A 1 13  ? 26.512  -43.676 20.049  1.00 38.37 ? 48  TYR A CZ  1 
ATOM   97   O  OH  . TYR A 1 13  ? 27.586  -42.876 20.380  1.00 30.61 ? 48  TYR A OH  1 
ATOM   98   N  N   . ARG A 1 14  ? 24.498  -48.062 21.638  1.00 17.12 ? 49  ARG A N   1 
ATOM   99   C  CA  . ARG A 1 14  ? 24.592  -48.143 23.091  1.00 17.42 ? 49  ARG A CA  1 
ATOM   100  C  C   . ARG A 1 14  ? 25.254  -46.899 23.678  1.00 18.85 ? 49  ARG A C   1 
ATOM   101  O  O   . ARG A 1 14  ? 26.245  -46.387 23.142  1.00 21.75 ? 49  ARG A O   1 
ATOM   102  C  CB  . ARG A 1 14  ? 25.405  -49.372 23.503  1.00 23.57 ? 49  ARG A CB  1 
ATOM   103  C  CG  . ARG A 1 14  ? 25.145  -49.834 24.921  1.00 23.06 ? 49  ARG A CG  1 
ATOM   104  C  CD  . ARG A 1 14  ? 23.979  -50.809 24.944  1.00 26.77 ? 49  ARG A CD  1 
ATOM   105  N  NE  . ARG A 1 14  ? 24.341  -52.060 24.290  1.00 29.32 ? 49  ARG A NE  1 
ATOM   106  C  CZ  . ARG A 1 14  ? 23.509  -53.071 24.080  1.00 41.63 ? 49  ARG A CZ  1 
ATOM   107  N  NH1 . ARG A 1 14  ? 22.233  -53.000 24.425  1.00 23.54 ? 49  ARG A NH1 1 
ATOM   108  N  NH2 . ARG A 1 14  ? 23.970  -54.186 23.516  1.00 27.07 ? 49  ARG A NH2 1 
ATOM   109  N  N   . MET A 1 15  ? 24.725  -46.433 24.811  1.00 20.80 ? 50  MET A N   1 
ATOM   110  C  CA  . MET A 1 15  ? 25.290  -45.255 25.447  1.00 24.03 ? 50  MET A CA  1 
ATOM   111  C  C   . MET A 1 15  ? 25.029  -45.343 26.942  1.00 24.16 ? 50  MET A C   1 
ATOM   112  O  O   . MET A 1 15  ? 23.929  -45.695 27.368  1.00 23.99 ? 50  MET A O   1 
ATOM   113  C  CB  . MET A 1 15  ? 24.633  -43.983 24.904  1.00 25.24 ? 50  MET A CB  1 
ATOM   114  C  CG  . MET A 1 15  ? 25.115  -42.717 25.584  1.00 29.11 ? 50  MET A CG  1 
ATOM   115  S  SD  . MET A 1 15  ? 24.244  -41.250 24.995  1.00 26.47 ? 50  MET A SD  1 
ATOM   116  C  CE  . MET A 1 15  ? 22.736  -41.373 25.962  1.00 23.50 ? 50  MET A CE  1 
ATOM   117  N  N   . LEU A 1 16  ? 26.030  -45.018 27.744  1.00 22.97 ? 51  LEU A N   1 
ATOM   118  C  CA  . LEU A 1 16  ? 25.832  -44.999 29.184  1.00 22.54 ? 51  LEU A CA  1 
ATOM   119  C  C   . LEU A 1 16  ? 25.307  -43.634 29.604  1.00 28.60 ? 51  LEU A C   1 
ATOM   120  O  O   . LEU A 1 16  ? 25.706  -42.606 29.053  1.00 28.19 ? 51  LEU A O   1 
ATOM   121  C  CB  . LEU A 1 16  ? 27.144  -45.306 29.907  1.00 22.95 ? 51  LEU A CB  1 
ATOM   122  C  CG  . LEU A 1 16  ? 27.741  -46.690 29.623  1.00 29.58 ? 51  LEU A CG  1 
ATOM   123  C  CD1 . LEU A 1 16  ? 28.994  -46.927 30.449  1.00 36.45 ? 51  LEU A CD1 1 
ATOM   124  C  CD2 . LEU A 1 16  ? 26.718  -47.789 29.880  1.00 36.54 ? 51  LEU A CD2 1 
ATOM   125  N  N   . LEU A 1 17  ? 24.396  -43.630 30.573  1.00 24.77 ? 52  LEU A N   1 
ATOM   126  C  CA  . LEU A 1 17  ? 23.887  -42.401 31.173  1.00 23.06 ? 52  LEU A CA  1 
ATOM   127  C  C   . LEU A 1 17  ? 23.934  -42.614 32.681  1.00 27.73 ? 52  LEU A C   1 
ATOM   128  O  O   . LEU A 1 17  ? 23.020  -43.213 33.259  1.00 23.96 ? 52  LEU A O   1 
ATOM   129  C  CB  . LEU A 1 17  ? 22.467  -42.108 30.701  1.00 21.70 ? 52  LEU A CB  1 
ATOM   130  C  CG  . LEU A 1 17  ? 21.877  -40.783 31.187  1.00 22.97 ? 52  LEU A CG  1 
ATOM   131  C  CD1 . LEU A 1 17  ? 22.285  -39.644 30.265  1.00 26.98 ? 52  LEU A CD1 1 
ATOM   132  C  CD2 . LEU A 1 17  ? 20.363  -40.868 31.315  1.00 26.85 ? 52  LEU A CD2 1 
ATOM   133  N  N   . GLY A 1 18  ? 24.993  -42.122 33.317  1.00 29.28 ? 53  GLY A N   1 
ATOM   134  C  CA  . GLY A 1 18  ? 25.210  -42.454 34.714  1.00 25.97 ? 53  GLY A CA  1 
ATOM   135  C  C   . GLY A 1 18  ? 25.367  -43.957 34.848  1.00 27.13 ? 53  GLY A C   1 
ATOM   136  O  O   . GLY A 1 18  ? 26.220  -44.575 34.192  1.00 32.09 ? 53  GLY A O   1 
ATOM   137  N  N   . ASP A 1 19  ? 24.542  -44.562 35.703  1.00 26.05 ? 54  ASP A N   1 
ATOM   138  C  CA  . ASP A 1 19  ? 24.520  -46.010 35.872  1.00 32.96 ? 54  ASP A CA  1 
ATOM   139  C  C   . ASP A 1 19  ? 23.545  -46.707 34.929  1.00 28.60 ? 54  ASP A C   1 
ATOM   140  O  O   . ASP A 1 19  ? 23.495  -47.943 34.922  1.00 29.02 ? 54  ASP A O   1 
ATOM   141  C  CB  . ASP A 1 19  ? 24.192  -46.379 37.325  1.00 40.73 ? 54  ASP A CB  1 
ATOM   142  C  CG  . ASP A 1 19  ? 25.217  -45.847 38.309  1.00 53.28 ? 54  ASP A CG  1 
ATOM   143  O  OD1 . ASP A 1 19  ? 26.407  -45.758 37.938  1.00 41.99 ? 54  ASP A OD1 1 
ATOM   144  O  OD2 . ASP A 1 19  ? 24.831  -45.515 39.450  1.00 55.72 ? 54  ASP A OD2 1 
ATOM   145  N  N   . PHE A 1 20  ? 22.777  -45.954 34.143  1.00 28.40 ? 55  PHE A N   1 
ATOM   146  C  CA  . PHE A 1 20  ? 21.785  -46.527 33.246  1.00 28.52 ? 55  PHE A CA  1 
ATOM   147  C  C   . PHE A 1 20  ? 22.407  -46.842 31.892  1.00 26.32 ? 55  PHE A C   1 
ATOM   148  O  O   . PHE A 1 20  ? 23.347  -46.180 31.444  1.00 26.60 ? 55  PHE A O   1 
ATOM   149  C  CB  . PHE A 1 20  ? 20.611  -45.571 33.011  1.00 25.59 ? 55  PHE A CB  1 
ATOM   150  C  CG  . PHE A 1 20  ? 19.787  -45.269 34.237  1.00 25.05 ? 55  PHE A CG  1 
ATOM   151  C  CD1 . PHE A 1 20  ? 20.000  -45.925 35.446  1.00 26.35 ? 55  PHE A CD1 1 
ATOM   152  C  CD2 . PHE A 1 20  ? 18.753  -44.340 34.159  1.00 23.64 ? 55  PHE A CD2 1 
ATOM   153  C  CE1 . PHE A 1 20  ? 19.224  -45.630 36.553  1.00 25.49 ? 55  PHE A CE1 1 
ATOM   154  C  CE2 . PHE A 1 20  ? 17.979  -44.047 35.258  1.00 29.98 ? 55  PHE A CE2 1 
ATOM   155  C  CZ  . PHE A 1 20  ? 18.213  -44.692 36.459  1.00 24.63 ? 55  PHE A CZ  1 
ATOM   156  N  N   . GLU A 1 21  ? 21.854  -47.852 31.230  1.00 26.27 ? 56  GLU A N   1 
ATOM   157  C  CA  . GLU A 1 21  ? 22.255  -48.207 29.876  1.00 22.72 ? 56  GLU A CA  1 
ATOM   158  C  C   . GLU A 1 21  ? 21.138  -47.788 28.929  1.00 23.23 ? 56  GLU A C   1 
ATOM   159  O  O   . GLU A 1 21  ? 19.993  -48.224 29.085  1.00 20.78 ? 56  GLU A O   1 
ATOM   160  C  CB  . GLU A 1 21  ? 22.500  -49.711 29.771  1.00 22.73 ? 56  GLU A CB  1 
ATOM   161  C  CG  . GLU A 1 21  ? 22.860  -50.210 28.376  1.00 24.73 ? 56  GLU A CG  1 
ATOM   162  C  CD  . GLU A 1 21  ? 22.452  -51.661 28.181  1.00 35.89 ? 56  GLU A CD  1 
ATOM   163  O  OE1 . GLU A 1 21  ? 21.230  -51.925 28.164  1.00 29.47 ? 56  GLU A OE1 1 
ATOM   164  O  OE2 . GLU A 1 21  ? 23.341  -52.537 28.091  1.00 26.61 ? 56  GLU A OE2 1 
ATOM   165  N  N   . ILE A 1 22  ? 21.462  -46.943 27.959  1.00 21.39 ? 57  ILE A N   1 
ATOM   166  C  CA  . ILE A 1 22  ? 20.524  -46.515 26.928  1.00 18.59 ? 57  ILE A CA  1 
ATOM   167  C  C   . ILE A 1 22  ? 20.880  -47.260 25.655  1.00 26.40 ? 57  ILE A C   1 
ATOM   168  O  O   . ILE A 1 22  ? 22.058  -47.353 25.292  1.00 21.87 ? 57  ILE A O   1 
ATOM   169  C  CB  . ILE A 1 22  ? 20.610  -44.993 26.709  1.00 22.94 ? 57  ILE A CB  1 
ATOM   170  C  CG1 . ILE A 1 22  ? 20.593  -44.252 28.053  1.00 24.39 ? 57  ILE A CG1 1 
ATOM   171  C  CG2 . ILE A 1 22  ? 19.518  -44.505 25.749  1.00 20.62 ? 57  ILE A CG2 1 
ATOM   172  C  CD1 . ILE A 1 22  ? 19.342  -44.509 28.894  1.00 20.98 ? 57  ILE A CD1 1 
ATOM   173  N  N   . THR A 1 23  ? 19.878  -47.818 24.987  1.00 20.52 ? 58  THR A N   1 
ATOM   174  C  CA  . THR A 1 23  ? 20.081  -48.395 23.664  1.00 19.64 ? 58  THR A CA  1 
ATOM   175  C  C   . THR A 1 23  ? 19.079  -47.754 22.717  1.00 18.10 ? 58  THR A C   1 
ATOM   176  O  O   . THR A 1 23  ? 17.871  -47.986 22.836  1.00 21.21 ? 58  THR A O   1 
ATOM   177  C  CB  . THR A 1 23  ? 19.930  -49.915 23.690  1.00 24.97 ? 58  THR A CB  1 
ATOM   178  O  OG1 . THR A 1 23  ? 20.697  -50.454 24.775  1.00 22.35 ? 58  THR A OG1 1 
ATOM   179  C  CG2 . THR A 1 23  ? 20.428  -50.513 22.371  1.00 23.67 ? 58  THR A CG2 1 
ATOM   180  N  N   . ALA A 1 24  ? 19.572  -46.930 21.803  1.00 16.13 ? 59  ALA A N   1 
ATOM   181  C  CA  . ALA A 1 24  ? 18.721  -46.453 20.720  1.00 17.29 ? 59  ALA A CA  1 
ATOM   182  C  C   . ALA A 1 24  ? 18.472  -47.614 19.770  1.00 19.96 ? 59  ALA A C   1 
ATOM   183  O  O   . ALA A 1 24  ? 19.412  -48.316 19.379  1.00 17.48 ? 59  ALA A O   1 
ATOM   184  C  CB  . ALA A 1 24  ? 19.399  -45.297 19.987  1.00 17.90 ? 59  ALA A CB  1 
ATOM   185  N  N   . LEU A 1 25  ? 17.210  -47.833 19.412  1.00 16.02 ? 60  LEU A N   1 
ATOM   186  C  CA  . LEU A 1 25  ? 16.810  -48.952 18.572  1.00 17.67 ? 60  LEU A CA  1 
ATOM   187  C  C   . LEU A 1 25  ? 16.161  -48.413 17.309  1.00 19.04 ? 60  LEU A C   1 
ATOM   188  O  O   . LEU A 1 25  ? 15.108  -47.766 17.373  1.00 19.11 ? 60  LEU A O   1 
ATOM   189  C  CB  . LEU A 1 25  ? 15.848  -49.893 19.303  1.00 16.63 ? 60  LEU A CB  1 
ATOM   190  C  CG  . LEU A 1 25  ? 16.335  -50.495 20.620  1.00 17.09 ? 60  LEU A CG  1 
ATOM   191  C  CD1 . LEU A 1 25  ? 15.194  -51.204 21.352  1.00 20.71 ? 60  LEU A CD1 1 
ATOM   192  C  CD2 . LEU A 1 25  ? 17.499  -51.439 20.370  1.00 19.65 ? 60  LEU A CD2 1 
ATOM   193  N  N   . SER A 1 26  ? 16.784  -48.690 16.163  1.00 19.07 ? 61  SER A N   1 
ATOM   194  C  CA  . SER A 1 26  ? 16.227  -48.272 14.885  1.00 17.92 ? 61  SER A CA  1 
ATOM   195  C  C   . SER A 1 26  ? 15.058  -49.166 14.489  1.00 16.50 ? 61  SER A C   1 
ATOM   196  O  O   . SER A 1 26  ? 15.154  -50.395 14.534  1.00 20.16 ? 61  SER A O   1 
ATOM   197  C  CB  . SER A 1 26  ? 17.295  -48.335 13.796  1.00 18.58 ? 61  SER A CB  1 
ATOM   198  O  OG  . SER A 1 26  ? 16.786  -47.793 12.584  1.00 19.12 ? 61  SER A OG  1 
ATOM   199  N  N   . ASP A 1 27  ? 13.948  -48.546 14.101  1.00 16.20 ? 62  ASP A N   1 
ATOM   200  C  CA  . ASP A 1 27  ? 12.860  -49.242 13.437  1.00 21.13 ? 62  ASP A CA  1 
ATOM   201  C  C   . ASP A 1 27  ? 13.028  -49.241 11.930  1.00 17.15 ? 62  ASP A C   1 
ATOM   202  O  O   . ASP A 1 27  ? 12.210  -49.844 11.226  1.00 18.63 ? 62  ASP A O   1 
ATOM   203  C  CB  . ASP A 1 27  ? 11.531  -48.564 13.758  1.00 17.20 ? 62  ASP A CB  1 
ATOM   204  C  CG  . ASP A 1 27  ? 10.353  -49.476 13.513  1.00 19.11 ? 62  ASP A CG  1 
ATOM   205  O  OD1 . ASP A 1 27  ? 10.406  -50.660 13.929  1.00 20.99 ? 62  ASP A OD1 1 
ATOM   206  O  OD2 . ASP A 1 27  ? 9.389   -49.024 12.855  1.00 21.67 ? 62  ASP A OD2 1 
ATOM   207  N  N   . GLY A 1 28  ? 14.058  -48.577 11.432  1.00 17.67 ? 63  GLY A N   1 
ATOM   208  C  CA  . GLY A 1 28  ? 14.280  -48.390 10.016  1.00 19.52 ? 63  GLY A CA  1 
ATOM   209  C  C   . GLY A 1 28  ? 14.232  -46.921 9.661   1.00 19.72 ? 63  GLY A C   1 
ATOM   210  O  O   . GLY A 1 28  ? 14.304  -46.037 10.521  1.00 20.04 ? 63  GLY A O   1 
ATOM   211  N  N   . THR A 1 29  ? 14.140  -46.660 8.361   1.00 20.63 ? 64  THR A N   1 
ATOM   212  C  CA  . THR A 1 29  ? 13.970  -45.309 7.853   1.00 21.56 ? 64  THR A CA  1 
ATOM   213  C  C   . THR A 1 29  ? 12.872  -45.316 6.804   1.00 20.96 ? 64  THR A C   1 
ATOM   214  O  O   . THR A 1 29  ? 12.575  -46.344 6.192   1.00 22.28 ? 64  THR A O   1 
ATOM   215  C  CB  . THR A 1 29  ? 15.256  -44.739 7.211   1.00 20.32 ? 64  THR A CB  1 
ATOM   216  O  OG1 . THR A 1 29  ? 15.557  -45.469 6.010   1.00 22.92 ? 64  THR A OG1 1 
ATOM   217  C  CG2 . THR A 1 29  ? 16.453  -44.764 8.177   1.00 19.90 ? 64  THR A CG2 1 
ATOM   218  N  N   . VAL A 1 30  ? 12.292  -44.144 6.583   1.00 20.18 ? 65  VAL A N   1 
ATOM   219  C  CA  . VAL A 1 30  ? 11.240  -43.967 5.591   1.00 21.79 ? 65  VAL A CA  1 
ATOM   220  C  C   . VAL A 1 30  ? 11.421  -42.615 4.909   1.00 21.70 ? 65  VAL A C   1 
ATOM   221  O  O   . VAL A 1 30  ? 11.798  -41.627 5.547   1.00 18.39 ? 65  VAL A O   1 
ATOM   222  C  CB  . VAL A 1 30  ? 9.835   -44.142 6.215   1.00 23.83 ? 65  VAL A CB  1 
ATOM   223  C  CG1 . VAL A 1 30  ? 9.556   -43.069 7.255   1.00 19.61 ? 65  VAL A CG1 1 
ATOM   224  C  CG2 . VAL A 1 30  ? 8.768   -44.136 5.135   1.00 30.15 ? 65  VAL A CG2 1 
ATOM   225  N  N   . ALA A 1 31  ? 11.176  -42.574 3.601   1.00 22.40 ? 66  ALA A N   1 
ATOM   226  C  CA  . ALA A 1 31  ? 11.303  -41.340 2.835   1.00 23.13 ? 66  ALA A CA  1 
ATOM   227  C  C   . ALA A 1 31  ? 10.005  -40.553 2.966   1.00 25.87 ? 66  ALA A C   1 
ATOM   228  O  O   . ALA A 1 31  ? 8.935   -41.044 2.589   1.00 25.46 ? 66  ALA A O   1 
ATOM   229  C  CB  . ALA A 1 31  ? 11.609  -41.648 1.370   1.00 25.25 ? 66  ALA A CB  1 
ATOM   230  N  N   . LEU A 1 32  ? 10.099  -39.333 3.498   1.00 21.41 ? 67  LEU A N   1 
ATOM   231  C  CA  . LEU A 1 32  ? 8.926   -38.542 3.827   1.00 22.49 ? 67  LEU A CA  1 
ATOM   232  C  C   . LEU A 1 32  ? 8.883   -37.262 3.003   1.00 34.46 ? 67  LEU A C   1 
ATOM   233  O  O   . LEU A 1 32  ? 9.897   -36.565 2.885   1.00 22.32 ? 67  LEU A O   1 
ATOM   234  C  CB  . LEU A 1 32  ? 8.919   -38.157 5.311   1.00 23.79 ? 67  LEU A CB  1 
ATOM   235  C  CG  . LEU A 1 32  ? 8.816   -39.293 6.326   1.00 24.07 ? 67  LEU A CG  1 
ATOM   236  C  CD1 . LEU A 1 32  ? 8.756   -38.715 7.735   1.00 26.56 ? 67  LEU A CD1 1 
ATOM   237  C  CD2 . LEU A 1 32  ? 7.603   -40.156 6.030   1.00 27.83 ? 67  LEU A CD2 1 
ATOM   238  N  N   . PRO A 1 33  ? 7.718   -36.913 2.440   1.00 27.59 ? 68  PRO A N   1 
ATOM   239  C  CA  . PRO A 1 33  ? 7.569   -35.639 1.703   1.00 30.52 ? 68  PRO A CA  1 
ATOM   240  C  C   . PRO A 1 33  ? 7.406   -34.476 2.674   1.00 26.90 ? 68  PRO A C   1 
ATOM   241  O  O   . PRO A 1 33  ? 6.329   -33.882 2.837   1.00 30.07 ? 68  PRO A O   1 
ATOM   242  C  CB  . PRO A 1 33  ? 6.310   -35.893 0.869   1.00 29.58 ? 68  PRO A CB  1 
ATOM   243  C  CG  . PRO A 1 33  ? 5.492   -36.818 1.723   1.00 31.45 ? 68  PRO A CG  1 
ATOM   244  C  CD  . PRO A 1 33  ? 6.486   -37.719 2.415   1.00 27.72 ? 68  PRO A CD  1 
ATOM   245  N  N   . VAL A 1 34  ? 8.497   -34.144 3.369   1.00 24.77 ? 69  VAL A N   1 
ATOM   246  C  CA  . VAL A 1 34  ? 8.421   -33.136 4.421   1.00 30.92 ? 69  VAL A CA  1 
ATOM   247  C  C   . VAL A 1 34  ? 8.074   -31.762 3.862   1.00 31.86 ? 69  VAL A C   1 
ATOM   248  O  O   . VAL A 1 34  ? 7.512   -30.928 4.583   1.00 26.47 ? 69  VAL A O   1 
ATOM   249  C  CB  . VAL A 1 34  ? 9.697   -33.128 5.286   1.00 29.00 ? 69  VAL A CB  1 
ATOM   250  C  CG1 . VAL A 1 34  ? 9.899   -34.491 5.919   1.00 24.16 ? 69  VAL A CG1 1 
ATOM   251  C  CG2 . VAL A 1 34  ? 10.904  -32.727 4.460   1.00 24.64 ? 69  VAL A CG2 1 
ATOM   252  N  N   . ASP A 1 35  ? 8.382   -31.514 2.587   1.00 26.67 ? 70  ASP A N   1 
ATOM   253  C  CA  . ASP A 1 35  ? 8.013   -30.247 1.966   1.00 24.33 ? 70  ASP A CA  1 
ATOM   254  C  C   . ASP A 1 35  ? 6.501   -30.089 1.875   1.00 32.55 ? 70  ASP A C   1 
ATOM   255  O  O   . ASP A 1 35  ? 5.998   -28.961 1.853   1.00 38.77 ? 70  ASP A O   1 
ATOM   256  C  CB  . ASP A 1 35  ? 8.657   -30.124 0.584   1.00 31.02 ? 70  ASP A CB  1 
ATOM   257  C  CG  . ASP A 1 35  ? 8.352   -31.315 -0.318  1.00 47.64 ? 70  ASP A CG  1 
ATOM   258  O  OD1 . ASP A 1 35  ? 8.110   -32.424 0.199   1.00 31.45 ? 70  ASP A OD1 1 
ATOM   259  O  OD2 . ASP A 1 35  ? 8.350   -31.139 -1.554  1.00 49.73 ? 70  ASP A OD2 1 
ATOM   260  N  N   . LYS A 1 36  ? 5.767   -31.200 1.823   1.00 26.79 ? 71  LYS A N   1 
ATOM   261  C  CA  . LYS A 1 36  ? 4.311   -31.161 1.766   1.00 34.63 ? 71  LYS A CA  1 
ATOM   262  C  C   . LYS A 1 36  ? 3.666   -31.099 3.142   1.00 31.22 ? 71  LYS A C   1 
ATOM   263  O  O   . LYS A 1 36  ? 2.555   -30.569 3.273   1.00 44.18 ? 71  LYS A O   1 
ATOM   264  C  CB  . LYS A 1 36  ? 3.782   -32.384 1.011   1.00 33.70 ? 71  LYS A CB  1 
ATOM   265  C  CG  . LYS A 1 36  ? 4.332   -32.502 -0.406  1.00 42.83 ? 71  LYS A CG  1 
ATOM   266  C  CD  . LYS A 1 36  ? 4.058   -33.876 -0.999  1.00 56.14 ? 71  LYS A CD  1 
ATOM   267  C  CE  . LYS A 1 36  ? 4.435   -33.933 -2.475  1.00 70.01 ? 71  LYS A CE  1 
ATOM   268  N  NZ  . LYS A 1 36  ? 5.239   -35.154 -2.791  1.00 66.43 ? 71  LYS A NZ  1 
ATOM   269  N  N   . ARG A 1 37  ? 4.332   -31.616 4.174   1.00 26.94 ? 72  ARG A N   1 
ATOM   270  C  CA  . ARG A 1 37  ? 3.724   -31.675 5.498   1.00 32.85 ? 72  ARG A CA  1 
ATOM   271  C  C   . ARG A 1 37  ? 4.032   -30.457 6.360   1.00 29.04 ? 72  ARG A C   1 
ATOM   272  O  O   . ARG A 1 37  ? 3.218   -30.098 7.218   1.00 28.14 ? 72  ARG A O   1 
ATOM   273  C  CB  . ARG A 1 37  ? 4.134   -32.959 6.231   1.00 40.80 ? 72  ARG A CB  1 
ATOM   274  C  CG  . ARG A 1 37  ? 3.948   -34.247 5.429   1.00 47.56 ? 72  ARG A CG  1 
ATOM   275  C  CD  . ARG A 1 37  ? 2.598   -34.280 4.714   1.00 40.17 ? 72  ARG A CD  1 
ATOM   276  N  NE  . ARG A 1 37  ? 1.471   -34.377 5.635   1.00 47.14 ? 72  ARG A NE  1 
ATOM   277  C  CZ  . ARG A 1 37  ? 0.689   -35.443 5.771   1.00 44.48 ? 72  ARG A CZ  1 
ATOM   278  N  NH1 . ARG A 1 37  ? 0.884   -36.541 5.060   1.00 40.54 ? 72  ARG A NH1 1 
ATOM   279  N  NH2 . ARG A 1 37  ? -0.318  -35.404 6.639   1.00 42.67 ? 72  ARG A NH2 1 
ATOM   280  N  N   . LEU A 1 38  ? 5.183   -29.820 6.163   1.00 23.63 ? 73  LEU A N   1 
ATOM   281  C  CA  . LEU A 1 38  ? 5.532   -28.642 6.950   1.00 26.46 ? 73  LEU A CA  1 
ATOM   282  C  C   . LEU A 1 38  ? 4.636   -27.458 6.587   1.00 25.38 ? 73  LEU A C   1 
ATOM   283  O  O   . LEU A 1 38  ? 4.330   -27.222 5.416   1.00 28.89 ? 73  LEU A O   1 
ATOM   284  C  CB  . LEU A 1 38  ? 6.997   -28.284 6.713   1.00 22.43 ? 73  LEU A CB  1 
ATOM   285  C  CG  . LEU A 1 38  ? 8.013   -29.135 7.480   1.00 20.65 ? 73  LEU A CG  1 
ATOM   286  C  CD1 . LEU A 1 38  ? 9.418   -28.927 6.913   1.00 23.40 ? 73  LEU A CD1 1 
ATOM   287  C  CD2 . LEU A 1 38  ? 7.987   -28.809 8.957   1.00 24.07 ? 73  LEU A CD2 1 
ATOM   288  N  N   . ASN A 1 39  ? 4.217   -26.702 7.606   1.00 22.91 ? 74  ASN A N   1 
ATOM   289  C  CA  . ASN A 1 39  ? 3.335   -25.548 7.410   1.00 28.34 ? 74  ASN A CA  1 
ATOM   290  C  C   . ASN A 1 39  ? 4.147   -24.310 7.023   1.00 28.43 ? 74  ASN A C   1 
ATOM   291  O  O   . ASN A 1 39  ? 4.233   -23.316 7.749   1.00 31.39 ? 74  ASN A O   1 
ATOM   292  C  CB  . ASN A 1 39  ? 2.473   -25.296 8.642   1.00 31.77 ? 74  ASN A CB  1 
ATOM   293  C  CG  . ASN A 1 39  ? 1.482   -26.417 8.903   1.00 40.63 ? 74  ASN A CG  1 
ATOM   294  O  OD1 . ASN A 1 39  ? 0.829   -26.916 7.984   1.00 43.03 ? 74  ASN A OD1 1 
ATOM   295  N  ND2 . ASN A 1 39  ? 1.345   -26.797 10.165  1.00 34.17 ? 74  ASN A ND2 1 
ATOM   296  N  N   . GLN A 1 40  ? 4.741   -24.386 5.836   1.00 26.96 ? 75  GLN A N   1 
ATOM   297  C  CA  . GLN A 1 40  ? 5.439   -23.267 5.219   1.00 29.84 ? 75  GLN A CA  1 
ATOM   298  C  C   . GLN A 1 40  ? 5.616   -23.589 3.741   1.00 32.07 ? 75  GLN A C   1 
ATOM   299  O  O   . GLN A 1 40  ? 5.482   -24.754 3.344   1.00 30.41 ? 75  GLN A O   1 
ATOM   300  C  CB  . GLN A 1 40  ? 6.797   -23.010 5.903   1.00 25.43 ? 75  GLN A CB  1 
ATOM   301  C  CG  . GLN A 1 40  ? 7.920   -23.941 5.497   1.00 28.41 ? 75  GLN A CG  1 
ATOM   302  C  CD  . GLN A 1 40  ? 9.226   -23.598 6.197   1.00 23.80 ? 75  GLN A CD  1 
ATOM   303  O  OE1 . GLN A 1 40  ? 9.307   -22.599 6.915   1.00 30.54 ? 75  GLN A OE1 1 
ATOM   304  N  NE2 . GLN A 1 40  ? 10.247  -24.422 5.996   1.00 26.34 ? 75  GLN A NE2 1 
ATOM   305  N  N   . PRO A 1 41  ? 5.894   -22.584 2.902   1.00 34.32 ? 76  PRO A N   1 
ATOM   306  C  CA  . PRO A 1 41  ? 5.999   -22.838 1.458   1.00 35.93 ? 76  PRO A CA  1 
ATOM   307  C  C   . PRO A 1 41  ? 7.023   -23.917 1.138   1.00 34.00 ? 76  PRO A C   1 
ATOM   308  O  O   . PRO A 1 41  ? 8.100   -23.980 1.734   1.00 29.89 ? 76  PRO A O   1 
ATOM   309  C  CB  . PRO A 1 41  ? 6.420   -21.475 0.895   1.00 36.68 ? 76  PRO A CB  1 
ATOM   310  C  CG  . PRO A 1 41  ? 5.874   -20.504 1.899   1.00 38.30 ? 76  PRO A CG  1 
ATOM   311  C  CD  . PRO A 1 41  ? 6.157   -21.168 3.206   1.00 36.01 ? 76  PRO A CD  1 
ATOM   312  N  N   . ALA A 1 42  ? 6.658   -24.789 0.200   1.00 37.28 ? 77  ALA A N   1 
ATOM   313  C  CA  . ALA A 1 42  ? 7.533   -25.907 -0.146  1.00 33.91 ? 77  ALA A CA  1 
ATOM   314  C  C   . ALA A 1 42  ? 8.920   -25.479 -0.610  1.00 35.16 ? 77  ALA A C   1 
ATOM   315  O  O   . ALA A 1 42  ? 9.902   -26.130 -0.205  1.00 29.42 ? 77  ALA A O   1 
ATOM   316  C  CB  . ALA A 1 42  ? 6.836   -26.856 -1.131  1.00 36.58 ? 77  ALA A CB  1 
ATOM   317  N  N   . PRO A 1 43  ? 9.082   -24.454 -1.452  1.00 37.69 ? 78  PRO A N   1 
ATOM   318  C  CA  . PRO A 1 43  ? 10.442  -24.004 -1.793  1.00 36.94 ? 78  PRO A CA  1 
ATOM   319  C  C   . PRO A 1 43  ? 11.274  -23.593 -0.589  1.00 42.07 ? 78  PRO A C   1 
ATOM   320  O  O   . PRO A 1 43  ? 12.494  -23.805 -0.586  1.00 28.87 ? 78  PRO A O   1 
ATOM   321  C  CB  . PRO A 1 43  ? 10.178  -22.815 -2.728  1.00 35.65 ? 78  PRO A CB  1 
ATOM   322  C  CG  . PRO A 1 43  ? 8.958   -23.237 -3.461  1.00 42.05 ? 78  PRO A CG  1 
ATOM   323  C  CD  . PRO A 1 43  ? 8.099   -23.922 -2.412  1.00 40.03 ? 78  PRO A CD  1 
ATOM   324  N  N   . LYS A 1 44  ? 10.647  -22.994 0.430   1.00 35.24 ? 79  LYS A N   1 
ATOM   325  C  CA  . LYS A 1 44  ? 11.367  -22.617 1.645   1.00 31.50 ? 79  LYS A CA  1 
ATOM   326  C  C   . LYS A 1 44  ? 11.920  -23.848 2.356   1.00 27.50 ? 79  LYS A C   1 
ATOM   327  O  O   . LYS A 1 44  ? 13.092  -23.881 2.762   1.00 28.30 ? 79  LYS A O   1 
ATOM   328  C  CB  . LYS A 1 44  ? 10.418  -21.844 2.560   1.00 33.32 ? 79  LYS A CB  1 
ATOM   329  C  CG  . LYS A 1 44  ? 11.068  -21.175 3.752   1.00 31.71 ? 79  LYS A CG  1 
ATOM   330  C  CD  . LYS A 1 44  ? 9.999   -20.495 4.604   1.00 41.99 ? 79  LYS A CD  1 
ATOM   331  C  CE  . LYS A 1 44  ? 10.479  -19.185 5.189   1.00 41.83 ? 79  LYS A CE  1 
ATOM   332  N  NZ  . LYS A 1 44  ? 11.175  -19.407 6.489   1.00 68.31 ? 79  LYS A NZ  1 
ATOM   333  N  N   . THR A 1 45  ? 11.090  -24.879 2.503   1.00 24.96 ? 80  THR A N   1 
ATOM   334  C  CA  . THR A 1 45  ? 11.578  -26.133 3.055   1.00 26.12 ? 80  THR A CA  1 
ATOM   335  C  C   . THR A 1 45  ? 12.712  -26.690 2.210   1.00 23.09 ? 80  THR A C   1 
ATOM   336  O  O   . THR A 1 45  ? 13.741  -27.113 2.746   1.00 22.29 ? 80  THR A O   1 
ATOM   337  C  CB  . THR A 1 45  ? 10.429  -27.137 3.154   1.00 24.58 ? 80  THR A CB  1 
ATOM   338  O  OG1 . THR A 1 45  ? 9.506   -26.680 4.142   1.00 27.35 ? 80  THR A OG1 1 
ATOM   339  C  CG2 . THR A 1 45  ? 10.943  -28.524 3.553   1.00 21.82 ? 80  THR A CG2 1 
ATOM   340  N  N   . GLN A 1 46  ? 12.550  -26.682 0.885   1.00 24.49 ? 81  GLN A N   1 
ATOM   341  C  CA  . GLN A 1 46  ? 13.570  -27.273 0.024   1.00 26.61 ? 81  GLN A CA  1 
ATOM   342  C  C   . GLN A 1 46  ? 14.902  -26.539 0.153   1.00 30.64 ? 81  GLN A C   1 
ATOM   343  O  O   . GLN A 1 46  ? 15.964  -27.169 0.160   1.00 23.07 ? 81  GLN A O   1 
ATOM   344  C  CB  . GLN A 1 46  ? 13.090  -27.302 -1.426  1.00 34.43 ? 81  GLN A CB  1 
ATOM   345  C  CG  . GLN A 1 46  ? 12.093  -28.433 -1.703  1.00 41.59 ? 81  GLN A CG  1 
ATOM   346  C  CD  . GLN A 1 46  ? 12.735  -29.815 -1.796  1.00 60.19 ? 81  GLN A CD  1 
ATOM   347  O  OE1 . GLN A 1 46  ? 13.411  -30.275 -0.868  1.00 45.34 ? 81  GLN A OE1 1 
ATOM   348  N  NE2 . GLN A 1 46  ? 12.500  -30.496 -2.915  1.00 56.17 ? 81  GLN A NE2 1 
ATOM   349  N  N   . SER A 1 47  ? 14.868  -25.207 0.252   1.00 27.71 ? 82  SER A N   1 
ATOM   350  C  CA  . SER A 1 47  ? 16.107  -24.443 0.401   1.00 24.01 ? 82  SER A CA  1 
ATOM   351  C  C   . SER A 1 47  ? 16.744  -24.670 1.774   1.00 23.43 ? 82  SER A C   1 
ATOM   352  O  O   . SER A 1 47  ? 17.980  -24.776 1.892   1.00 25.87 ? 82  SER A O   1 
ATOM   353  C  CB  . SER A 1 47  ? 15.847  -22.959 0.126   1.00 29.70 ? 82  SER A CB  1 
ATOM   354  O  OG  . SER A 1 47  ? 15.189  -22.341 1.218   1.00 55.54 ? 82  SER A OG  1 
ATOM   355  N  N   . ALA A 1 48  ? 15.916  -24.775 2.823   1.00 21.89 ? 83  ALA A N   1 
ATOM   356  C  CA  . ALA A 1 48  ? 16.449  -25.130 4.136   1.00 27.20 ? 83  ALA A CA  1 
ATOM   357  C  C   . ALA A 1 48  ? 17.118  -26.499 4.104   1.00 24.96 ? 83  ALA A C   1 
ATOM   358  O  O   . ALA A 1 48  ? 18.196  -26.689 4.679   1.00 24.88 ? 83  ALA A O   1 
ATOM   359  C  CB  . ALA A 1 48  ? 15.340  -25.103 5.185   1.00 24.88 ? 83  ALA A CB  1 
ATOM   360  N  N   . LEU A 1 49  ? 16.491  -27.464 3.436   1.00 21.51 ? 84  LEU A N   1 
ATOM   361  C  CA  . LEU A 1 49  ? 17.089  -28.789 3.307   1.00 21.20 ? 84  LEU A CA  1 
ATOM   362  C  C   . LEU A 1 49  ? 18.394  -28.720 2.525   1.00 20.60 ? 84  LEU A C   1 
ATOM   363  O  O   . LEU A 1 49  ? 19.389  -29.350 2.905   1.00 22.21 ? 84  LEU A O   1 
ATOM   364  C  CB  . LEU A 1 49  ? 16.107  -29.738 2.622   1.00 21.54 ? 84  LEU A CB  1 
ATOM   365  C  CG  . LEU A 1 49  ? 14.876  -30.144 3.450   1.00 22.13 ? 84  LEU A CG  1 
ATOM   366  C  CD1 . LEU A 1 49  ? 14.114  -31.268 2.764   1.00 27.60 ? 84  LEU A CD1 1 
ATOM   367  C  CD2 . LEU A 1 49  ? 15.242  -30.527 4.869   1.00 28.07 ? 84  LEU A CD2 1 
ATOM   368  N  N   . ALA A 1 50  ? 18.416  -27.939 1.438   1.00 20.71 ? 85  ALA A N   1 
ATOM   369  C  CA  . ALA A 1 50  ? 19.624  -27.826 0.627   1.00 22.18 ? 85  ALA A CA  1 
ATOM   370  C  C   . ALA A 1 50  ? 20.793  -27.298 1.446   1.00 20.70 ? 85  ALA A C   1 
ATOM   371  O  O   . ALA A 1 50  ? 21.944  -27.708 1.231   1.00 24.47 ? 85  ALA A O   1 
ATOM   372  C  CB  . ALA A 1 50  ? 19.381  -26.933 -0.592  1.00 25.35 ? 85  ALA A CB  1 
ATOM   373  N  N   . LYS A 1 51  ? 20.526  -26.375 2.383   1.00 22.28 ? 86  LYS A N   1 
ATOM   374  C  CA  . LYS A 1 51  ? 21.610  -25.896 3.246   1.00 24.82 ? 86  LYS A CA  1 
ATOM   375  C  C   . LYS A 1 51  ? 22.288  -27.043 3.984   1.00 27.45 ? 86  LYS A C   1 
ATOM   376  O  O   . LYS A 1 51  ? 23.495  -26.984 4.245   1.00 28.02 ? 86  LYS A O   1 
ATOM   377  C  CB  . LYS A 1 51  ? 21.109  -24.873 4.266   1.00 34.55 ? 86  LYS A CB  1 
ATOM   378  C  CG  . LYS A 1 51  ? 20.775  -23.497 3.724   1.00 39.67 ? 86  LYS A CG  1 
ATOM   379  C  CD  . LYS A 1 51  ? 20.274  -22.621 4.869   1.00 41.22 ? 86  LYS A CD  1 
ATOM   380  C  CE  . LYS A 1 51  ? 19.662  -21.329 4.381   1.00 47.75 ? 86  LYS A CE  1 
ATOM   381  N  NZ  . LYS A 1 51  ? 19.233  -20.488 5.537   1.00 51.77 ? 86  LYS A NZ  1 
ATOM   382  N  N   . SER A 1 52  ? 21.537  -28.090 4.324   1.00 23.03 ? 87  SER A N   1 
ATOM   383  C  CA  . SER A 1 52  ? 22.071  -29.252 5.016   1.00 23.24 ? 87  SER A CA  1 
ATOM   384  C  C   . SER A 1 52  ? 22.351  -30.416 4.072   1.00 25.88 ? 87  SER A C   1 
ATOM   385  O  O   . SER A 1 52  ? 22.455  -31.561 4.529   1.00 21.63 ? 87  SER A O   1 
ATOM   386  C  CB  . SER A 1 52  ? 21.127  -29.679 6.141   1.00 32.36 ? 87  SER A CB  1 
ATOM   387  O  OG  . SER A 1 52  ? 21.102  -28.704 7.173   1.00 43.65 ? 87  SER A OG  1 
ATOM   388  N  N   . PHE A 1 53  ? 22.472  -30.146 2.771   1.00 20.18 ? 88  PHE A N   1 
ATOM   389  C  CA  . PHE A 1 53  ? 22.779  -31.179 1.774   1.00 22.31 ? 88  PHE A CA  1 
ATOM   390  C  C   . PHE A 1 53  ? 21.704  -32.271 1.731   1.00 23.83 ? 88  PHE A C   1 
ATOM   391  O  O   . PHE A 1 53  ? 21.995  -33.447 1.506   1.00 25.07 ? 88  PHE A O   1 
ATOM   392  C  CB  . PHE A 1 53  ? 24.183  -31.761 1.980   1.00 24.41 ? 88  PHE A CB  1 
ATOM   393  C  CG  . PHE A 1 53  ? 25.260  -30.713 2.047   1.00 24.43 ? 88  PHE A CG  1 
ATOM   394  C  CD1 . PHE A 1 53  ? 25.608  -30.124 3.260   1.00 26.11 ? 88  PHE A CD1 1 
ATOM   395  C  CD2 . PHE A 1 53  ? 25.913  -30.309 0.897   1.00 28.71 ? 88  PHE A CD2 1 
ATOM   396  C  CE1 . PHE A 1 53  ? 26.600  -29.143 3.315   1.00 24.90 ? 88  PHE A CE1 1 
ATOM   397  C  CE2 . PHE A 1 53  ? 26.907  -29.335 0.946   1.00 29.66 ? 88  PHE A CE2 1 
ATOM   398  C  CZ  . PHE A 1 53  ? 27.244  -28.754 2.158   1.00 28.31 ? 88  PHE A CZ  1 
ATOM   399  N  N   . GLN A 1 54  ? 20.469  -31.848 1.937   1.00 23.59 ? 89  GLN A N   1 
ATOM   400  C  CA  . GLN A 1 54  ? 19.346  -32.751 1.907   1.00 20.33 ? 89  GLN A CA  1 
ATOM   401  C  C   . GLN A 1 54  ? 18.307  -32.284 0.903   1.00 23.13 ? 89  GLN A C   1 
ATOM   402  O  O   . GLN A 1 54  ? 18.357  -31.169 0.455   1.00 25.40 ? 89  GLN A O   1 
ATOM   403  C  CB  . GLN A 1 54  ? 18.690  -32.834 3.306   1.00 18.80 ? 89  GLN A CB  1 
ATOM   404  C  CG  . GLN A 1 54  ? 19.543  -33.478 4.386   1.00 23.20 ? 89  GLN A CG  1 
ATOM   405  C  CD  . GLN A 1 54  ? 19.007  -33.235 5.784   1.00 28.56 ? 89  GLN A CD  1 
ATOM   406  O  OE1 . GLN A 1 54  ? 17.885  -32.788 5.958   1.00 34.69 ? 89  GLN A OE1 1 
ATOM   407  N  NE2 . GLN A 1 54  ? 19.817  -33.528 6.784   1.00 49.66 ? 89  GLN A NE2 1 
ATOM   408  N  N   . LYS A 1 55  ? 17.455  -33.191 0.478   1.00 24.84 ? 90  LYS A N   1 
ATOM   409  C  CA  . LYS A 1 55  ? 16.370  -32.851 -0.418  1.00 26.01 ? 90  LYS A CA  1 
ATOM   410  C  C   . LYS A 1 55  ? 15.153  -33.708 -0.061  1.00 47.38 ? 90  LYS A C   1 
ATOM   411  O  O   . LYS A 1 55  ? 15.314  -34.810 0.412   1.00 41.61 ? 90  LYS A O   1 
ATOM   412  C  CB  . LYS A 1 55  ? 16.810  -33.095 -1.842  1.00 33.99 ? 90  LYS A CB  1 
ATOM   413  C  CG  . LYS A 1 55  ? 15.835  -32.558 -2.872  1.00 65.00 ? 90  LYS A CG  1 
ATOM   414  C  CD  . LYS A 1 55  ? 16.490  -32.416 -4.237  1.00 68.71 ? 90  LYS A CD  1 
ATOM   415  C  CE  . LYS A 1 55  ? 17.557  -31.333 -4.225  1.00 63.23 ? 90  LYS A CE  1 
ATOM   416  N  NZ  . LYS A 1 55  ? 18.301  -31.246 -5.512  1.00 56.01 ? 90  LYS A NZ  1 
ATOM   417  N  N   . ALA A 1 56  ? 13.954  -33.177 -0.195  1.00 64.77 ? 91  ALA A N   1 
ATOM   418  C  CA  . ALA A 1 56  ? 12.753  -33.970 0.008   1.00 28.94 ? 91  ALA A CA  1 
ATOM   419  C  C   . ALA A 1 56  ? 12.513  -34.759 -1.252  1.00 32.69 ? 91  ALA A C   1 
ATOM   420  O  O   . ALA A 1 56  ? 12.823  -34.266 -2.314  1.00 39.82 ? 91  ALA A O   1 
ATOM   421  C  CB  . ALA A 1 56  ? 11.588  -33.093 0.372   1.00 56.19 ? 91  ALA A CB  1 
ATOM   422  N  N   . PRO A 1 57  ? 11.955  -35.962 -1.166  1.00 32.80 ? 92  PRO A N   1 
ATOM   423  C  CA  . PRO A 1 57  ? 11.603  -36.716 0.037   1.00 23.57 ? 92  PRO A CA  1 
ATOM   424  C  C   . PRO A 1 57  ? 12.831  -37.036 0.859   1.00 24.80 ? 92  PRO A C   1 
ATOM   425  O  O   . PRO A 1 57  ? 13.853  -37.416 0.329   1.00 27.97 ? 92  PRO A O   1 
ATOM   426  C  CB  . PRO A 1 57  ? 10.948  -37.983 -0.507  1.00 28.14 ? 92  PRO A CB  1 
ATOM   427  C  CG  . PRO A 1 57  ? 11.429  -38.093 -1.907  1.00 44.35 ? 92  PRO A CG  1 
ATOM   428  C  CD  . PRO A 1 57  ? 11.585  -36.688 -2.387  1.00 44.88 ? 92  PRO A CD  1 
ATOM   429  N  N   . LEU A 1 58  ? 12.688  -36.931 2.163   1.00 20.15 ? 93  LEU A N   1 
ATOM   430  C  CA  . LEU A 1 58  ? 13.827  -37.065 3.029   1.00 18.49 ? 93  LEU A CA  1 
ATOM   431  C  C   . LEU A 1 58  ? 13.795  -38.365 3.801   1.00 22.30 ? 93  LEU A C   1 
ATOM   432  O  O   . LEU A 1 58  ? 12.834  -38.661 4.463   1.00 21.23 ? 93  LEU A O   1 
ATOM   433  C  CB  . LEU A 1 58  ? 13.764  -35.902 3.992   1.00 21.91 ? 93  LEU A CB  1 
ATOM   434  C  CG  . LEU A 1 58  ? 14.869  -35.697 5.009   1.00 27.85 ? 93  LEU A CG  1 
ATOM   435  C  CD1 . LEU A 1 58  ? 16.176  -35.531 4.264   1.00 29.83 ? 93  LEU A CD1 1 
ATOM   436  C  CD2 . LEU A 1 58  ? 14.550  -34.452 5.814   1.00 22.48 ? 93  LEU A CD2 1 
ATOM   437  N  N   . GLU A 1 59  ? 14.886  -39.102 3.720   1.00 18.93 ? 94  GLU A N   1 
ATOM   438  C  CA  . GLU A 1 59  ? 14.931  -40.335 4.434   1.00 18.38 ? 94  GLU A CA  1 
ATOM   439  C  C   . GLU A 1 59  ? 14.959  -39.950 5.896   1.00 19.23 ? 94  GLU A C   1 
ATOM   440  O  O   . GLU A 1 59  ? 15.878  -39.307 6.337   1.00 19.38 ? 94  GLU A O   1 
ATOM   441  C  CB  . GLU A 1 59  ? 16.177  -41.114 4.042   1.00 21.62 ? 94  GLU A CB  1 
ATOM   442  C  CG  . GLU A 1 59  ? 16.338  -42.434 4.763   1.00 25.94 ? 94  GLU A CG  1 
ATOM   443  C  CD  . GLU A 1 59  ? 17.461  -43.295 4.211   1.00 31.87 ? 94  GLU A CD  1 
ATOM   444  O  OE1 . GLU A 1 59  ? 18.227  -42.813 3.363   1.00 26.96 ? 94  GLU A OE1 1 
ATOM   445  O  OE2 . GLU A 1 59  ? 17.579  -44.454 4.639   1.00 24.38 ? 94  GLU A OE2 1 
ATOM   446  N  N   . THR A 1 60  ? 14.039  -40.506 6.654   1.00 15.71 ? 95  THR A N   1 
ATOM   447  C  CA  . THR A 1 60  ? 13.863  -40.101 8.034   1.00 16.51 ? 95  THR A CA  1 
ATOM   448  C  C   . THR A 1 60  ? 13.921  -41.316 8.952   1.00 17.72 ? 95  THR A C   1 
ATOM   449  O  O   . THR A 1 60  ? 13.289  -42.306 8.691   1.00 19.13 ? 95  THR A O   1 
ATOM   450  C  CB  . THR A 1 60  ? 12.510  -39.373 8.168   1.00 20.64 ? 95  THR A CB  1 
ATOM   451  O  OG1 . THR A 1 60  ? 12.481  -38.210 7.339   1.00 17.95 ? 95  THR A OG1 1 
ATOM   452  C  CG2 . THR A 1 60  ? 12.251  -38.962 9.614   1.00 17.43 ? 95  THR A CG2 1 
ATOM   453  N  N   . SER A 1 61  ? 14.708  -41.211 10.000  1.00 15.26 ? 96  SER A N   1 
ATOM   454  C  CA  . SER A 1 61  ? 14.824  -42.282 10.980  1.00 13.83 ? 96  SER A CA  1 
ATOM   455  C  C   . SER A 1 61  ? 13.553  -42.408 11.808  1.00 14.56 ? 96  SER A C   1 
ATOM   456  O  O   . SER A 1 61  ? 12.806  -41.446 12.004  1.00 16.50 ? 96  SER A O   1 
ATOM   457  C  CB  . SER A 1 61  ? 15.997  -42.019 11.923  1.00 15.93 ? 96  SER A CB  1 
ATOM   458  O  OG  . SER A 1 61  ? 17.228  -42.057 11.219  1.00 17.31 ? 96  SER A OG  1 
ATOM   459  N  N   . VAL A 1 62  ? 13.306  -43.625 12.283  1.00 15.74 ? 97  VAL A N   1 
ATOM   460  C  CA  . VAL A 1 62  ? 12.271  -43.892 13.274  1.00 15.17 ? 97  VAL A CA  1 
ATOM   461  C  C   . VAL A 1 62  ? 12.947  -44.686 14.384  1.00 16.21 ? 97  VAL A C   1 
ATOM   462  O  O   . VAL A 1 62  ? 13.466  -45.780 14.134  1.00 18.03 ? 97  VAL A O   1 
ATOM   463  C  CB  . VAL A 1 62  ? 11.098  -44.679 12.669  1.00 14.92 ? 97  VAL A CB  1 
ATOM   464  C  CG1 . VAL A 1 62  ? 10.014  -44.945 13.724  1.00 19.28 ? 97  VAL A CG1 1 
ATOM   465  C  CG2 . VAL A 1 62  ? 10.534  -43.936 11.458  1.00 16.38 ? 97  VAL A CG2 1 
ATOM   466  N  N   . THR A 1 63  ? 12.977  -44.132 15.596  1.00 13.64 ? 98  THR A N   1 
ATOM   467  C  CA  . THR A 1 63  ? 13.793  -44.704 16.661  1.00 18.11 ? 98  THR A CA  1 
ATOM   468  C  C   . THR A 1 63  ? 12.990  -44.836 17.948  1.00 16.88 ? 98  THR A C   1 
ATOM   469  O  O   . THR A 1 63  ? 12.166  -43.969 18.263  1.00 16.29 ? 98  THR A O   1 
ATOM   470  C  CB  . THR A 1 63  ? 15.009  -43.808 16.898  1.00 18.94 ? 98  THR A CB  1 
ATOM   471  O  OG1 . THR A 1 63  ? 15.713  -43.659 15.656  1.00 17.17 ? 98  THR A OG1 1 
ATOM   472  C  CG2 . THR A 1 63  ? 15.950  -44.428 17.940  1.00 19.94 ? 98  THR A CG2 1 
ATOM   473  N  N   . GLY A 1 64  ? 13.227  -45.937 18.671  1.00 16.53 ? 99  GLY A N   1 
ATOM   474  C  CA  . GLY A 1 64  ? 12.803  -46.093 20.047  1.00 17.09 ? 99  GLY A CA  1 
ATOM   475  C  C   . GLY A 1 64  ? 14.019  -46.143 20.966  1.00 16.36 ? 99  GLY A C   1 
ATOM   476  O  O   . GLY A 1 64  ? 15.160  -46.253 20.522  1.00 17.84 ? 99  GLY A O   1 
ATOM   477  N  N   . TYR A 1 65  ? 13.766  -46.045 22.273  1.00 15.49 ? 100 TYR A N   1 
ATOM   478  C  CA  . TYR A 1 65  ? 14.859  -45.925 23.238  1.00 18.78 ? 100 TYR A CA  1 
ATOM   479  C  C   . TYR A 1 65  ? 14.657  -46.878 24.400  1.00 21.93 ? 100 TYR A C   1 
ATOM   480  O  O   . TYR A 1 65  ? 13.682  -46.762 25.146  1.00 19.45 ? 100 TYR A O   1 
ATOM   481  C  CB  . TYR A 1 65  ? 15.027  -44.479 23.721  1.00 18.44 ? 100 TYR A CB  1 
ATOM   482  C  CG  . TYR A 1 65  ? 15.407  -43.578 22.580  1.00 18.42 ? 100 TYR A CG  1 
ATOM   483  C  CD1 . TYR A 1 65  ? 16.742  -43.412 22.214  1.00 17.22 ? 100 TYR A CD1 1 
ATOM   484  C  CD2 . TYR A 1 65  ? 14.432  -42.961 21.812  1.00 15.40 ? 100 TYR A CD2 1 
ATOM   485  C  CE1 . TYR A 1 65  ? 17.091  -42.611 21.145  1.00 16.95 ? 100 TYR A CE1 1 
ATOM   486  C  CE2 . TYR A 1 65  ? 14.767  -42.157 20.729  1.00 15.66 ? 100 TYR A CE2 1 
ATOM   487  C  CZ  . TYR A 1 65  ? 16.105  -41.984 20.400  1.00 15.79 ? 100 TYR A CZ  1 
ATOM   488  O  OH  . TYR A 1 65  ? 16.423  -41.180 19.317  1.00 17.54 ? 100 TYR A OH  1 
ATOM   489  N  N   . LEU A 1 66  ? 15.594  -47.798 24.570  1.00 18.52 ? 101 LEU A N   1 
ATOM   490  C  CA  . LEU A 1 66  ? 15.566  -48.764 25.646  1.00 20.04 ? 101 LEU A CA  1 
ATOM   491  C  C   . LEU A 1 66  ? 16.397  -48.208 26.794  1.00 26.32 ? 101 LEU A C   1 
ATOM   492  O  O   . LEU A 1 66  ? 17.525  -47.758 26.584  1.00 21.63 ? 101 LEU A O   1 
ATOM   493  C  CB  . LEU A 1 66  ? 16.176  -50.066 25.136  1.00 23.99 ? 101 LEU A CB  1 
ATOM   494  C  CG  . LEU A 1 66  ? 15.975  -51.320 25.966  1.00 27.78 ? 101 LEU A CG  1 
ATOM   495  C  CD1 . LEU A 1 66  ? 14.508  -51.691 26.016  1.00 19.13 ? 101 LEU A CD1 1 
ATOM   496  C  CD2 . LEU A 1 66  ? 16.810  -52.425 25.359  1.00 20.68 ? 101 LEU A CD2 1 
ATOM   497  N  N   . VAL A 1 67  ? 15.834  -48.220 27.997  1.00 21.28 ? 102 VAL A N   1 
ATOM   498  C  CA  . VAL A 1 67  ? 16.516  -47.782 29.205  1.00 20.15 ? 102 VAL A CA  1 
ATOM   499  C  C   . VAL A 1 67  ? 16.566  -48.966 30.156  1.00 27.90 ? 102 VAL A C   1 
ATOM   500  O  O   . VAL A 1 67  ? 15.521  -49.458 30.600  1.00 24.50 ? 102 VAL A O   1 
ATOM   501  C  CB  . VAL A 1 67  ? 15.802  -46.585 29.854  1.00 20.72 ? 102 VAL A CB  1 
ATOM   502  C  CG1 . VAL A 1 67  ? 16.582  -46.083 31.067  1.00 22.34 ? 102 VAL A CG1 1 
ATOM   503  C  CG2 . VAL A 1 67  ? 15.581  -45.466 28.833  1.00 22.94 ? 102 VAL A CG2 1 
ATOM   504  N  N   . ASN A 1 68  ? 17.772  -49.436 30.455  1.00 26.49 ? 103 ASN A N   1 
ATOM   505  C  CA  . ASN A 1 68  ? 17.991  -50.409 31.516  1.00 23.43 ? 103 ASN A CA  1 
ATOM   506  C  C   . ASN A 1 68  ? 18.526  -49.655 32.726  1.00 28.28 ? 103 ASN A C   1 
ATOM   507  O  O   . ASN A 1 68  ? 19.676  -49.200 32.729  1.00 28.51 ? 103 ASN A O   1 
ATOM   508  C  CB  . ASN A 1 68  ? 18.957  -51.506 31.082  1.00 28.71 ? 103 ASN A CB  1 
ATOM   509  C  CG  . ASN A 1 68  ? 18.878  -52.726 31.980  1.00 29.27 ? 103 ASN A CG  1 
ATOM   510  O  OD1 . ASN A 1 68  ? 18.634  -52.601 33.180  1.00 29.29 ? 103 ASN A OD1 1 
ATOM   511  N  ND2 . ASN A 1 68  ? 19.115  -53.907 31.414  1.00 28.01 ? 103 ASN A ND2 1 
ATOM   512  N  N   . THR A 1 69  ? 17.681  -49.506 33.744  1.00 25.61 ? 104 THR A N   1 
ATOM   513  C  CA  . THR A 1 69  ? 18.056  -48.799 34.958  1.00 28.43 ? 104 THR A CA  1 
ATOM   514  C  C   . THR A 1 69  ? 18.893  -49.655 35.894  1.00 31.40 ? 104 THR A C   1 
ATOM   515  O  O   . THR A 1 69  ? 19.391  -49.137 36.901  1.00 37.93 ? 104 THR A O   1 
ATOM   516  C  CB  . THR A 1 69  ? 16.799  -48.351 35.704  1.00 33.60 ? 104 THR A CB  1 
ATOM   517  O  OG1 . THR A 1 69  ? 16.154  -49.502 36.269  1.00 34.09 ? 104 THR A OG1 1 
ATOM   518  C  CG2 . THR A 1 69  ? 15.839  -47.641 34.753  1.00 25.72 ? 104 THR A CG2 1 
ATOM   519  N  N   . GLY A 1 70  ? 19.062  -50.941 35.583  1.00 30.20 ? 105 GLY A N   1 
ATOM   520  C  CA  . GLY A 1 70  ? 19.628  -51.913 36.484  1.00 32.72 ? 105 GLY A CA  1 
ATOM   521  C  C   . GLY A 1 70  ? 18.581  -52.734 37.212  1.00 40.98 ? 105 GLY A C   1 
ATOM   522  O  O   . GLY A 1 70  ? 18.831  -53.900 37.532  1.00 44.66 ? 105 GLY A O   1 
ATOM   523  N  N   . SER A 1 71  ? 17.406  -52.153 37.465  1.00 35.10 ? 106 SER A N   1 
ATOM   524  C  CA  . SER A 1 71  ? 16.301  -52.863 38.088  1.00 33.06 ? 106 SER A CA  1 
ATOM   525  C  C   . SER A 1 71  ? 15.090  -53.023 37.184  1.00 34.41 ? 106 SER A C   1 
ATOM   526  O  O   . SER A 1 71  ? 14.276  -53.923 37.427  1.00 32.31 ? 106 SER A O   1 
ATOM   527  C  CB  . SER A 1 71  ? 15.847  -52.141 39.366  1.00 49.53 ? 106 SER A CB  1 
ATOM   528  O  OG  . SER A 1 71  ? 15.771  -50.746 39.142  1.00 59.91 ? 106 SER A OG  1 
ATOM   529  N  N   . LYS A 1 72  ? 14.929  -52.168 36.179  1.00 30.46 ? 107 LYS A N   1 
ATOM   530  C  CA  . LYS A 1 72  ? 13.814  -52.251 35.252  1.00 31.64 ? 107 LYS A CA  1 
ATOM   531  C  C   . LYS A 1 72  ? 14.339  -52.054 33.839  1.00 29.52 ? 107 LYS A C   1 
ATOM   532  O  O   . LYS A 1 72  ? 15.286  -51.294 33.610  1.00 29.47 ? 107 LYS A O   1 
ATOM   533  C  CB  . LYS A 1 72  ? 12.745  -51.182 35.546  1.00 28.80 ? 107 LYS A CB  1 
ATOM   534  C  CG  . LYS A 1 72  ? 11.990  -51.387 36.855  1.00 41.15 ? 107 LYS A CG  1 
ATOM   535  C  CD  . LYS A 1 72  ? 10.927  -52.475 36.724  1.00 50.91 ? 107 LYS A CD  1 
ATOM   536  C  CE  . LYS A 1 72  ? 10.329  -52.856 38.079  1.00 55.48 ? 107 LYS A CE  1 
ATOM   537  N  NZ  . LYS A 1 72  ? 9.405   -51.817 38.604  1.00 46.11 ? 107 LYS A NZ  1 
ATOM   538  N  N   . LEU A 1 73  ? 13.712  -52.745 32.891  1.00 26.01 ? 108 LEU A N   1 
ATOM   539  C  CA  . LEU A 1 73  ? 13.975  -52.557 31.470  1.00 26.12 ? 108 LEU A CA  1 
ATOM   540  C  C   . LEU A 1 73  ? 12.737  -51.890 30.878  1.00 23.05 ? 108 LEU A C   1 
ATOM   541  O  O   . LEU A 1 73  ? 11.654  -52.490 30.841  1.00 23.19 ? 108 LEU A O   1 
ATOM   542  C  CB  . LEU A 1 73  ? 14.272  -53.894 30.798  1.00 27.22 ? 108 LEU A CB  1 
ATOM   543  C  CG  . LEU A 1 73  ? 14.699  -53.844 29.334  1.00 25.14 ? 108 LEU A CG  1 
ATOM   544  C  CD1 . LEU A 1 73  ? 16.037  -53.107 29.203  1.00 25.10 ? 108 LEU A CD1 1 
ATOM   545  C  CD2 . LEU A 1 73  ? 14.791  -55.252 28.780  1.00 24.65 ? 108 LEU A CD2 1 
ATOM   546  N  N   . VAL A 1 74  ? 12.902  -50.649 30.431  1.00 20.39 ? 109 VAL A N   1 
ATOM   547  C  CA  . VAL A 1 74  ? 11.820  -49.801 29.952  1.00 23.01 ? 109 VAL A CA  1 
ATOM   548  C  C   . VAL A 1 74  ? 12.096  -49.481 28.496  1.00 24.79 ? 109 VAL A C   1 
ATOM   549  O  O   . VAL A 1 74  ? 13.230  -49.158 28.132  1.00 23.28 ? 109 VAL A O   1 
ATOM   550  C  CB  . VAL A 1 74  ? 11.733  -48.502 30.772  1.00 23.93 ? 109 VAL A CB  1 
ATOM   551  C  CG1 . VAL A 1 74  ? 10.609  -47.609 30.240  1.00 21.78 ? 109 VAL A CG1 1 
ATOM   552  C  CG2 . VAL A 1 74  ? 11.512  -48.825 32.241  1.00 26.34 ? 109 VAL A CG2 1 
ATOM   553  N  N   . LEU A 1 75  ? 11.075  -49.573 27.658  1.00 19.13 ? 110 LEU A N   1 
ATOM   554  C  CA  . LEU A 1 75  ? 11.197  -49.211 26.255  1.00 17.08 ? 110 LEU A CA  1 
ATOM   555  C  C   . LEU A 1 75  ? 10.324  -47.995 25.989  1.00 17.91 ? 110 LEU A C   1 
ATOM   556  O  O   . LEU A 1 75  ? 9.125   -48.011 26.295  1.00 17.87 ? 110 LEU A O   1 
ATOM   557  C  CB  . LEU A 1 75  ? 10.760  -50.372 25.360  1.00 18.64 ? 110 LEU A CB  1 
ATOM   558  C  CG  . LEU A 1 75  ? 10.637  -50.060 23.871  1.00 17.19 ? 110 LEU A CG  1 
ATOM   559  C  CD1 . LEU A 1 75  ? 11.984  -49.610 23.289  1.00 16.64 ? 110 LEU A CD1 1 
ATOM   560  C  CD2 . LEU A 1 75  ? 10.118  -51.278 23.130  1.00 22.24 ? 110 LEU A CD2 1 
ATOM   561  N  N   . VAL A 1 76  ? 10.912  -46.949 25.421  1.00 15.63 ? 111 VAL A N   1 
ATOM   562  C  CA  . VAL A 1 76  ? 10.190  -45.738 25.055  1.00 16.11 ? 111 VAL A CA  1 
ATOM   563  C  C   . VAL A 1 76  ? 9.956   -45.783 23.549  1.00 18.00 ? 111 VAL A C   1 
ATOM   564  O  O   . VAL A 1 76  ? 10.908  -45.663 22.763  1.00 16.34 ? 111 VAL A O   1 
ATOM   565  C  CB  . VAL A 1 76  ? 10.950  -44.473 25.479  1.00 18.97 ? 111 VAL A CB  1 
ATOM   566  C  CG1 . VAL A 1 76  ? 10.178  -43.228 25.042  1.00 20.17 ? 111 VAL A CG1 1 
ATOM   567  C  CG2 . VAL A 1 76  ? 11.176  -44.466 26.981  1.00 18.19 ? 111 VAL A CG2 1 
ATOM   568  N  N   . ASP A 1 77  ? 8.682   -45.958 23.164  1.00 16.38 ? 112 ASP A N   1 
ATOM   569  C  CA  . ASP A 1 77  ? 8.243   -46.125 21.775  1.00 15.97 ? 112 ASP A CA  1 
ATOM   570  C  C   . ASP A 1 77  ? 8.692   -47.438 21.147  1.00 17.95 ? 112 ASP A C   1 
ATOM   571  O  O   . ASP A 1 77  ? 9.683   -48.033 21.574  1.00 18.43 ? 112 ASP A O   1 
ATOM   572  C  CB  . ASP A 1 77  ? 8.559   -44.902 20.922  1.00 16.75 ? 112 ASP A CB  1 
ATOM   573  C  CG  . ASP A 1 77  ? 7.789   -43.669 21.370  1.00 19.27 ? 112 ASP A CG  1 
ATOM   574  O  OD1 . ASP A 1 77  ? 6.858   -43.803 22.210  1.00 17.83 ? 112 ASP A OD1 1 
ATOM   575  O  OD2 . ASP A 1 77  ? 8.156   -42.553 20.920  1.00 21.19 ? 112 ASP A OD2 1 
ATOM   576  N  N   . THR A 1 78  ? 7.944   -47.916 20.143  1.00 16.96 ? 113 THR A N   1 
ATOM   577  C  CA  . THR A 1 78  ? 8.084   -49.291 19.674  1.00 16.03 ? 113 THR A CA  1 
ATOM   578  C  C   . THR A 1 78  ? 8.225   -49.421 18.160  1.00 15.37 ? 113 THR A C   1 
ATOM   579  O  O   . THR A 1 78  ? 8.193   -50.546 17.646  1.00 17.79 ? 113 THR A O   1 
ATOM   580  C  CB  . THR A 1 78  ? 6.909   -50.167 20.157  1.00 20.06 ? 113 THR A CB  1 
ATOM   581  O  OG1 . THR A 1 78  ? 5.703   -49.799 19.470  1.00 19.80 ? 113 THR A OG1 1 
ATOM   582  C  CG2 . THR A 1 78  ? 6.699   -50.050 21.663  1.00 18.99 ? 113 THR A CG2 1 
ATOM   583  N  N   . GLY A 1 79  ? 8.344   -48.316 17.434  1.00 16.22 ? 114 GLY A N   1 
ATOM   584  C  CA  . GLY A 1 79  ? 8.348   -48.406 15.990  1.00 17.29 ? 114 GLY A CA  1 
ATOM   585  C  C   . GLY A 1 79  ? 6.958   -48.707 15.432  1.00 20.77 ? 114 GLY A C   1 
ATOM   586  O  O   . GLY A 1 79  ? 5.938   -48.655 16.128  1.00 18.54 ? 114 GLY A O   1 
ATOM   587  N  N   . ALA A 1 80  ? 6.944   -49.045 14.139  1.00 18.55 ? 115 ALA A N   1 
ATOM   588  C  CA  . ALA A 1 80  ? 5.715   -49.132 13.362  1.00 18.63 ? 115 ALA A CA  1 
ATOM   589  C  C   . ALA A 1 80  ? 5.250   -50.554 13.080  1.00 20.56 ? 115 ALA A C   1 
ATOM   590  O  O   . ALA A 1 80  ? 4.161   -50.721 12.520  1.00 21.19 ? 115 ALA A O   1 
ATOM   591  C  CB  . ALA A 1 80  ? 5.894   -48.413 12.013  1.00 18.54 ? 115 ALA A CB  1 
ATOM   592  N  N   . ALA A 1 81  ? 6.064   -51.553 13.372  1.00 18.18 ? 116 ALA A N   1 
ATOM   593  C  CA  . ALA A 1 81  ? 5.794   -52.924 12.916  1.00 22.10 ? 116 ALA A CA  1 
ATOM   594  C  C   . ALA A 1 81  ? 5.575   -52.850 11.416  1.00 21.99 ? 116 ALA A C   1 
ATOM   595  O  O   . ALA A 1 81  ? 6.370   -52.287 10.722  1.00 23.81 ? 116 ALA A O   1 
ATOM   596  C  CB  . ALA A 1 81  ? 4.634   -53.589 13.648  1.00 24.98 ? 116 ALA A CB  1 
ATOM   597  N  N   . GLY A 1 82  ? 4.496   -53.428 10.920  1.00 24.03 ? 117 GLY A N   1 
ATOM   598  C  CA  . GLY A 1 82  ? 4.153   -53.358 9.511   1.00 25.93 ? 117 GLY A CA  1 
ATOM   599  C  C   . GLY A 1 82  ? 3.182   -52.295 9.068   1.00 29.76 ? 117 GLY A C   1 
ATOM   600  O  O   . GLY A 1 82  ? 2.780   -52.292 7.934   1.00 28.54 ? 117 GLY A O   1 
ATOM   601  N  N   . LEU A 1 83  ? 2.763   -51.428 9.972   1.00 29.40 ? 118 LEU A N   1 
ATOM   602  C  CA  . LEU A 1 83  ? 1.772   -50.384 9.699   1.00 21.52 ? 118 LEU A CA  1 
ATOM   603  C  C   . LEU A 1 83  ? 2.181   -49.357 8.650   1.00 34.51 ? 118 LEU A C   1 
ATOM   604  O  O   . LEU A 1 83  ? 1.331   -48.823 7.974   1.00 33.69 ? 118 LEU A O   1 
ATOM   605  C  CB  . LEU A 1 83  ? 1.388   -49.672 10.993  1.00 21.00 ? 118 LEU A CB  1 
ATOM   606  C  CG  . LEU A 1 83  ? 0.847   -50.478 12.169  1.00 26.94 ? 118 LEU A CG  1 
ATOM   607  C  CD1 . LEU A 1 83  ? 0.302   -49.532 13.222  1.00 25.38 ? 118 LEU A CD1 1 
ATOM   608  C  CD2 . LEU A 1 83  ? -0.245  -51.415 11.699  1.00 34.13 ? 118 LEU A CD2 1 
ATOM   609  N  N   . PHE A 1 84  ? 3.440   -48.980 8.611   1.00 23.83 ? 119 PHE A N   1 
ATOM   610  C  CA  . PHE A 1 84  ? 3.926   -47.930 7.716   1.00 27.77 ? 119 PHE A CA  1 
ATOM   611  C  C   . PHE A 1 84  ? 4.714   -48.426 6.508   1.00 33.27 ? 119 PHE A C   1 
ATOM   612  O  O   . PHE A 1 84  ? 5.510   -47.696 5.962   1.00 47.42 ? 119 PHE A O   1 
ATOM   613  C  CB  . PHE A 1 84  ? 4.695   -46.868 8.497   1.00 25.95 ? 119 PHE A CB  1 
ATOM   614  C  CG  . PHE A 1 84  ? 3.841   -45.751 8.984   1.00 45.89 ? 119 PHE A CG  1 
ATOM   615  C  CD1 . PHE A 1 84  ? 2.506   -45.691 8.645   1.00 60.54 ? 119 PHE A CD1 1 
ATOM   616  C  CD2 . PHE A 1 84  ? 4.370   -44.754 9.775   1.00 53.37 ? 119 PHE A CD2 1 
ATOM   617  C  CE1 . PHE A 1 84  ? 1.711   -44.660 9.092   1.00 69.10 ? 119 PHE A CE1 1 
ATOM   618  C  CE2 . PHE A 1 84  ? 3.582   -43.720 10.227  1.00 56.19 ? 119 PHE A CE2 1 
ATOM   619  C  CZ  . PHE A 1 84  ? 2.253   -43.669 9.880   1.00 67.85 ? 119 PHE A CZ  1 
ATOM   620  N  N   . GLY A 1 85  ? 4.565   -49.678 6.157   1.00 26.61 ? 120 GLY A N   1 
ATOM   621  C  CA  . GLY A 1 85  ? 5.311   -50.255 5.079   1.00 30.05 ? 120 GLY A CA  1 
ATOM   622  C  C   . GLY A 1 85  ? 6.572   -51.042 5.313   1.00 42.70 ? 120 GLY A C   1 
ATOM   623  O  O   . GLY A 1 85  ? 7.015   -51.181 6.422   1.00 26.17 ? 120 GLY A O   1 
ATOM   624  N  N   . PRO A 1 86  ? 7.173   -51.537 4.238   1.00 33.17 ? 121 PRO A N   1 
ATOM   625  C  CA  . PRO A 1 86  ? 8.313   -52.459 4.322   1.00 31.37 ? 121 PRO A CA  1 
ATOM   626  C  C   . PRO A 1 86  ? 9.587   -51.905 4.979   1.00 28.16 ? 121 PRO A C   1 
ATOM   627  O  O   . PRO A 1 86  ? 10.348  -52.689 5.501   1.00 31.66 ? 121 PRO A O   1 
ATOM   628  C  CB  . PRO A 1 86  ? 8.494   -52.925 2.864   1.00 30.37 ? 121 PRO A CB  1 
ATOM   629  C  CG  . PRO A 1 86  ? 7.893   -51.855 2.035   1.00 35.79 ? 121 PRO A CG  1 
ATOM   630  C  CD  . PRO A 1 86  ? 6.854   -51.152 2.854   1.00 36.45 ? 121 PRO A CD  1 
ATOM   631  N  N   . THR A 1 87  ? 9.877   -50.641 4.780   1.00 23.02 ? 122 THR A N   1 
ATOM   632  C  CA  . THR A 1 87  ? 11.093  -50.051 5.317   1.00 23.78 ? 122 THR A CA  1 
ATOM   633  C  C   . THR A 1 87  ? 11.152  -49.898 6.853   1.00 24.32 ? 122 THR A C   1 
ATOM   634  O  O   . THR A 1 87  ? 12.193  -49.651 7.385   1.00 22.21 ? 122 THR A O   1 
ATOM   635  C  CB  . THR A 1 87  ? 11.339  -48.676 4.651   1.00 25.15 ? 122 THR A CB  1 
ATOM   636  O  OG1 . THR A 1 87  ? 10.413  -47.709 5.140   1.00 25.90 ? 122 THR A OG1 1 
ATOM   637  C  CG2 . THR A 1 87  ? 11.213  -48.788 3.136   1.00 25.89 ? 122 THR A CG2 1 
ATOM   638  N  N   . LEU A 1 88  ? 10.027  -50.069 7.532   1.00 20.33 ? 123 LEU A N   1 
ATOM   639  C  CA  . LEU A 1 88  ? 9.991   -49.931 8.979   1.00 18.35 ? 123 LEU A CA  1 
ATOM   640  C  C   . LEU A 1 88  ? 9.733   -51.291 9.623   1.00 20.79 ? 123 LEU A C   1 
ATOM   641  O  O   . LEU A 1 88  ? 9.727   -52.329 8.949   1.00 27.66 ? 123 LEU A O   1 
ATOM   642  C  CB  . LEU A 1 88  ? 8.983   -48.849 9.393   1.00 19.76 ? 123 LEU A CB  1 
ATOM   643  C  CG  . LEU A 1 88  ? 9.336   -47.446 8.880   1.00 24.06 ? 123 LEU A CG  1 
ATOM   644  C  CD1 . LEU A 1 88  ? 8.301   -46.420 9.311   1.00 21.86 ? 123 LEU A CD1 1 
ATOM   645  C  CD2 . LEU A 1 88  ? 10.718  -47.010 9.343   1.00 24.36 ? 123 LEU A CD2 1 
ATOM   646  N  N   . GLY A 1 89  ? 9.531   -51.289 10.938  1.00 19.17 ? 124 GLY A N   1 
ATOM   647  C  CA  . GLY A 1 89  ? 9.303   -52.531 11.650  1.00 18.79 ? 124 GLY A CA  1 
ATOM   648  C  C   . GLY A 1 89  ? 10.545  -53.300 12.031  1.00 21.37 ? 124 GLY A C   1 
ATOM   649  O  O   . GLY A 1 89  ? 10.454  -54.498 12.320  1.00 24.38 ? 124 GLY A O   1 
ATOM   650  N  N   . ARG A 1 90  ? 11.707  -52.648 12.045  1.00 19.08 ? 125 ARG A N   1 
ATOM   651  C  CA  . ARG A 1 90  ? 12.961  -53.301 12.404  1.00 20.00 ? 125 ARG A CA  1 
ATOM   652  C  C   . ARG A 1 90  ? 13.252  -53.285 13.901  1.00 19.01 ? 125 ARG A C   1 
ATOM   653  O  O   . ARG A 1 90  ? 14.217  -53.933 14.333  1.00 20.80 ? 125 ARG A O   1 
ATOM   654  C  CB  . ARG A 1 90  ? 14.126  -52.645 11.654  1.00 23.85 ? 125 ARG A CB  1 
ATOM   655  C  CG  . ARG A 1 90  ? 13.882  -52.471 10.163  1.00 23.77 ? 125 ARG A CG  1 
ATOM   656  C  CD  . ARG A 1 90  ? 14.285  -53.742 9.424   1.00 40.35 ? 125 ARG A CD  1 
ATOM   657  N  NE  . ARG A 1 90  ? 14.328  -53.596 7.971   1.00 50.52 ? 125 ARG A NE  1 
ATOM   658  C  CZ  . ARG A 1 90  ? 13.297  -53.270 7.203   1.00 32.00 ? 125 ARG A CZ  1 
ATOM   659  N  NH1 . ARG A 1 90  ? 12.081  -53.114 7.700   1.00 32.72 ? 125 ARG A NH1 1 
ATOM   660  N  NH2 . ARG A 1 90  ? 13.485  -53.127 5.892   1.00 40.98 ? 125 ARG A NH2 1 
ATOM   661  N  N   . LEU A 1 91  ? 12.435  -52.594 14.706  1.00 21.18 ? 126 LEU A N   1 
ATOM   662  C  CA  . LEU A 1 91  ? 12.811  -52.362 16.099  1.00 20.60 ? 126 LEU A CA  1 
ATOM   663  C  C   . LEU A 1 91  ? 12.952  -53.666 16.878  1.00 18.33 ? 126 LEU A C   1 
ATOM   664  O  O   . LEU A 1 91  ? 13.883  -53.811 17.673  1.00 19.85 ? 126 LEU A O   1 
ATOM   665  C  CB  . LEU A 1 91  ? 11.838  -51.406 16.790  1.00 17.47 ? 126 LEU A CB  1 
ATOM   666  C  CG  . LEU A 1 91  ? 12.219  -51.083 18.249  1.00 18.75 ? 126 LEU A CG  1 
ATOM   667  C  CD1 . LEU A 1 91  ? 11.993  -49.608 18.560  1.00 18.85 ? 126 LEU A CD1 1 
ATOM   668  C  CD2 . LEU A 1 91  ? 11.464  -51.947 19.257  1.00 20.40 ? 126 LEU A CD2 1 
ATOM   669  N  N   . LEU A 1 92  ? 12.040  -54.623 16.676  1.00 21.21 ? 127 LEU A N   1 
ATOM   670  C  CA  . LEU A 1 92  ? 12.091  -55.865 17.448  1.00 19.51 ? 127 LEU A CA  1 
ATOM   671  C  C   . LEU A 1 92  ? 13.372  -56.643 17.159  1.00 20.15 ? 127 LEU A C   1 
ATOM   672  O  O   . LEU A 1 92  ? 14.043  -57.140 18.081  1.00 26.36 ? 127 LEU A O   1 
ATOM   673  C  CB  . LEU A 1 92  ? 10.866  -56.715 17.123  1.00 28.69 ? 127 LEU A CB  1 
ATOM   674  C  CG  . LEU A 1 92  ? 9.808   -56.729 18.220  1.00 43.46 ? 127 LEU A CG  1 
ATOM   675  C  CD1 . LEU A 1 92  ? 10.391  -57.343 19.456  1.00 38.38 ? 127 LEU A CD1 1 
ATOM   676  C  CD2 . LEU A 1 92  ? 9.314   -55.318 18.504  1.00 48.15 ? 127 LEU A CD2 1 
ATOM   677  N  N   . ALA A 1 93  ? 13.748  -56.732 15.881  1.00 22.32 ? 128 ALA A N   1 
ATOM   678  C  CA  . ALA A 1 93  ? 14.973  -57.431 15.520  1.00 26.86 ? 128 ALA A CA  1 
ATOM   679  C  C   . ALA A 1 93  ? 16.194  -56.727 16.099  1.00 21.73 ? 128 ALA A C   1 
ATOM   680  O  O   . ALA A 1 93  ? 17.155  -57.379 16.525  1.00 27.50 ? 128 ALA A O   1 
ATOM   681  C  CB  . ALA A 1 93  ? 15.081  -57.542 13.999  1.00 27.97 ? 128 ALA A CB  1 
ATOM   682  N  N   . ASN A 1 94  ? 16.176  -55.392 16.122  1.00 21.91 ? 129 ASN A N   1 
ATOM   683  C  CA  . ASN A 1 94  ? 17.311  -54.656 16.666  1.00 23.33 ? 129 ASN A CA  1 
ATOM   684  C  C   . ASN A 1 94  ? 17.367  -54.760 18.186  1.00 20.69 ? 129 ASN A C   1 
ATOM   685  O  O   . ASN A 1 94  ? 18.456  -54.763 18.767  1.00 25.01 ? 129 ASN A O   1 
ATOM   686  C  CB  . ASN A 1 94  ? 17.276  -53.210 16.180  1.00 18.77 ? 129 ASN A CB  1 
ATOM   687  C  CG  . ASN A 1 94  ? 17.706  -53.088 14.736  1.00 23.53 ? 129 ASN A CG  1 
ATOM   688  O  OD1 . ASN A 1 94  ? 18.632  -53.782 14.292  1.00 24.21 ? 129 ASN A OD1 1 
ATOM   689  N  ND2 . ASN A 1 94  ? 17.037  -52.217 13.988  1.00 19.88 ? 129 ASN A ND2 1 
ATOM   690  N  N   . LEU A 1 95  ? 16.212  -54.853 18.841  1.00 23.78 ? 130 LEU A N   1 
ATOM   691  C  CA  . LEU A 1 95  ? 16.194  -55.135 20.270  1.00 21.68 ? 130 LEU A CA  1 
ATOM   692  C  C   . LEU A 1 95  ? 16.858  -56.472 20.550  1.00 22.03 ? 130 LEU A C   1 
ATOM   693  O  O   . LEU A 1 95  ? 17.673  -56.595 21.475  1.00 26.06 ? 130 LEU A O   1 
ATOM   694  C  CB  . LEU A 1 95  ? 14.745  -55.147 20.764  1.00 22.38 ? 130 LEU A CB  1 
ATOM   695  C  CG  . LEU A 1 95  ? 14.513  -55.558 22.210  1.00 25.26 ? 130 LEU A CG  1 
ATOM   696  C  CD1 . LEU A 1 95  ? 15.173  -54.563 23.123  1.00 39.24 ? 130 LEU A CD1 1 
ATOM   697  C  CD2 . LEU A 1 95  ? 13.025  -55.647 22.513  1.00 36.12 ? 130 LEU A CD2 1 
ATOM   698  N  N   . LYS A 1 96  ? 16.535  -57.489 19.744  1.00 24.33 ? 131 LYS A N   1 
ATOM   699  C  CA  . LYS A 1 96  ? 17.196  -58.783 19.893  1.00 27.44 ? 131 LYS A CA  1 
ATOM   700  C  C   . LYS A 1 96  ? 18.694  -58.687 19.606  1.00 26.96 ? 131 LYS A C   1 
ATOM   701  O  O   . LYS A 1 96  ? 19.512  -59.268 20.330  1.00 26.28 ? 131 LYS A O   1 
ATOM   702  C  CB  . LYS A 1 96  ? 16.515  -59.820 19.003  1.00 28.22 ? 131 LYS A CB  1 
ATOM   703  C  CG  . LYS A 1 96  ? 15.157  -60.251 19.557  1.00 37.30 ? 131 LYS A CG  1 
ATOM   704  C  CD  . LYS A 1 96  ? 14.299  -60.925 18.500  1.00 37.69 ? 131 LYS A CD  1 
ATOM   705  C  CE  . LYS A 1 96  ? 12.918  -61.233 19.049  1.00 38.26 ? 131 LYS A CE  1 
ATOM   706  N  NZ  . LYS A 1 96  ? 11.934  -61.455 17.955  1.00 43.75 ? 131 LYS A NZ  1 
ATOM   707  N  N   . ALA A 1 97  ? 19.076  -57.952 18.556  1.00 24.56 ? 132 ALA A N   1 
ATOM   708  C  CA  . ALA A 1 97  ? 20.490  -57.781 18.249  1.00 23.29 ? 132 ALA A CA  1 
ATOM   709  C  C   . ALA A 1 97  ? 21.218  -57.052 19.367  1.00 29.95 ? 132 ALA A C   1 
ATOM   710  O  O   . ALA A 1 97  ? 22.401  -57.317 19.616  1.00 26.62 ? 132 ALA A O   1 
ATOM   711  C  CB  . ALA A 1 97  ? 20.663  -57.038 16.921  1.00 28.56 ? 132 ALA A CB  1 
ATOM   712  N  N   . ALA A 1 98  ? 20.529  -56.147 20.061  1.00 26.03 ? 133 ALA A N   1 
ATOM   713  C  CA  . ALA A 1 98  ? 21.110  -55.436 21.192  1.00 25.64 ? 133 ALA A CA  1 
ATOM   714  C  C   . ALA A 1 98  ? 21.225  -56.305 22.433  1.00 27.55 ? 133 ALA A C   1 
ATOM   715  O  O   . ALA A 1 98  ? 21.642  -55.802 23.480  1.00 28.03 ? 133 ALA A O   1 
ATOM   716  C  CB  . ALA A 1 98  ? 20.291  -54.183 21.515  1.00 21.95 ? 133 ALA A CB  1 
ATOM   717  N  N   . GLY A 1 99  ? 20.859  -57.580 22.347  1.00 28.40 ? 134 GLY A N   1 
ATOM   718  C  CA  . GLY A 1 99  ? 21.070  -58.520 23.425  1.00 28.78 ? 134 GLY A CA  1 
ATOM   719  C  C   . GLY A 1 99  ? 19.908  -58.720 24.369  1.00 31.29 ? 134 GLY A C   1 
ATOM   720  O  O   . GLY A 1 99  ? 20.095  -59.334 25.425  1.00 31.08 ? 134 GLY A O   1 
ATOM   721  N  N   . TYR A 1 100 ? 18.721  -58.239 24.027  1.00 25.70 ? 135 TYR A N   1 
ATOM   722  C  CA  . TYR A 1 100 ? 17.552  -58.389 24.875  1.00 30.28 ? 135 TYR A CA  1 
ATOM   723  C  C   . TYR A 1 100 ? 16.466  -59.154 24.141  1.00 29.28 ? 135 TYR A C   1 
ATOM   724  O  O   . TYR A 1 100 ? 16.425  -59.196 22.909  1.00 36.66 ? 135 TYR A O   1 
ATOM   725  C  CB  . TYR A 1 100 ? 16.988  -57.031 25.303  1.00 27.66 ? 135 TYR A CB  1 
ATOM   726  C  CG  . TYR A 1 100 ? 17.888  -56.256 26.223  1.00 28.86 ? 135 TYR A CG  1 
ATOM   727  C  CD1 . TYR A 1 100 ? 17.954  -56.568 27.573  1.00 29.98 ? 135 TYR A CD1 1 
ATOM   728  C  CD2 . TYR A 1 100 ? 18.672  -55.211 25.747  1.00 26.51 ? 135 TYR A CD2 1 
ATOM   729  C  CE1 . TYR A 1 100 ? 18.775  -55.865 28.429  1.00 31.69 ? 135 TYR A CE1 1 
ATOM   730  C  CE2 . TYR A 1 100 ? 19.496  -54.492 26.597  1.00 30.60 ? 135 TYR A CE2 1 
ATOM   731  C  CZ  . TYR A 1 100 ? 19.542  -54.826 27.939  1.00 25.07 ? 135 TYR A CZ  1 
ATOM   732  O  OH  . TYR A 1 100 ? 20.353  -54.132 28.808  1.00 34.55 ? 135 TYR A OH  1 
ATOM   733  N  N   . GLN A 1 101 ? 15.581  -59.754 24.918  1.00 32.23 ? 136 GLN A N   1 
ATOM   734  C  CA  . GLN A 1 101 ? 14.408  -60.383 24.358  1.00 28.06 ? 136 GLN A CA  1 
ATOM   735  C  C   . GLN A 1 101 ? 13.155  -59.610 24.761  1.00 24.86 ? 136 GLN A C   1 
ATOM   736  O  O   . GLN A 1 101 ? 13.113  -58.990 25.829  1.00 29.92 ? 136 GLN A O   1 
ATOM   737  C  CB  . GLN A 1 101 ? 14.319  -61.825 24.866  1.00 31.45 ? 136 GLN A CB  1 
ATOM   738  C  CG  . GLN A 1 101 ? 15.452  -62.709 24.359  1.00 33.09 ? 136 GLN A CG  1 
ATOM   739  C  CD  . GLN A 1 101 ? 15.450  -62.878 22.843  1.00 44.48 ? 136 GLN A CD  1 
ATOM   740  O  OE1 . GLN A 1 101 ? 14.393  -62.902 22.205  1.00 42.27 ? 136 GLN A OE1 1 
ATOM   741  N  NE2 . GLN A 1 101 ? 16.640  -62.989 22.260  1.00 55.63 ? 136 GLN A NE2 1 
ATOM   742  N  N   . PRO A 1 102 ? 12.123  -59.619 23.915  1.00 25.03 ? 137 PRO A N   1 
ATOM   743  C  CA  . PRO A 1 102 ? 10.918  -58.827 24.213  1.00 27.91 ? 137 PRO A CA  1 
ATOM   744  C  C   . PRO A 1 102 ? 10.299  -59.172 25.553  1.00 29.27 ? 137 PRO A C   1 
ATOM   745  O  O   . PRO A 1 102 ? 9.734   -58.297 26.222  1.00 30.13 ? 137 PRO A O   1 
ATOM   746  C  CB  . PRO A 1 102 ? 9.977   -59.216 23.067  1.00 35.55 ? 137 PRO A CB  1 
ATOM   747  C  CG  . PRO A 1 102 ? 10.896  -59.572 21.959  1.00 46.26 ? 137 PRO A CG  1 
ATOM   748  C  CD  . PRO A 1 102 ? 12.008  -60.323 22.626  1.00 29.89 ? 137 PRO A CD  1 
ATOM   749  N  N   . GLU A 1 103 ? 10.385  -60.437 25.960  1.00 26.16 ? 138 GLU A N   1 
ATOM   750  C  CA  . GLU A 1 103 ? 9.793   -60.867 27.218  1.00 30.86 ? 138 GLU A CA  1 
ATOM   751  C  C   . GLU A 1 103 ? 10.479  -60.241 28.427  1.00 28.26 ? 138 GLU A C   1 
ATOM   752  O  O   . GLU A 1 103 ? 9.900   -60.245 29.519  1.00 29.37 ? 138 GLU A O   1 
ATOM   753  C  CB  . GLU A 1 103 ? 9.755   -62.403 27.311  1.00 39.25 ? 138 GLU A CB  1 
ATOM   754  C  CG  . GLU A 1 103 ? 9.407   -63.177 26.003  1.00 35.71 ? 138 GLU A CG  1 
ATOM   755  C  CD  . GLU A 1 103 ? 10.467  -63.058 24.912  1.00 56.71 ? 138 GLU A CD  1 
ATOM   756  O  OE1 . GLU A 1 103 ? 11.560  -62.570 25.227  1.00 60.55 ? 138 GLU A OE1 1 
ATOM   757  O  OE2 . GLU A 1 103 ? 10.206  -63.428 23.747  1.00 61.67 ? 138 GLU A OE2 1 
ATOM   758  N  N   . GLN A 1 104 ? 11.686  -59.690 28.253  1.00 28.44 ? 139 GLN A N   1 
ATOM   759  C  CA  . GLN A 1 104 ? 12.396  -59.031 29.344  1.00 26.47 ? 139 GLN A CA  1 
ATOM   760  C  C   . GLN A 1 104 ? 11.912  -57.612 29.597  1.00 29.63 ? 139 GLN A C   1 
ATOM   761  O  O   . GLN A 1 104 ? 12.230  -57.043 30.647  1.00 29.45 ? 139 GLN A O   1 
ATOM   762  C  CB  . GLN A 1 104 ? 13.892  -58.973 29.046  1.00 30.12 ? 139 GLN A CB  1 
ATOM   763  C  CG  . GLN A 1 104 ? 14.531  -60.334 28.885  1.00 31.64 ? 139 GLN A CG  1 
ATOM   764  C  CD  . GLN A 1 104 ? 16.010  -60.234 28.586  1.00 34.33 ? 139 GLN A CD  1 
ATOM   765  O  OE1 . GLN A 1 104 ? 16.395  -59.859 27.484  1.00 32.80 ? 139 GLN A OE1 1 
ATOM   766  N  NE2 . GLN A 1 104 ? 16.845  -60.604 29.553  1.00 35.98 ? 139 GLN A NE2 1 
ATOM   767  N  N   . VAL A 1 105 ? 11.169  -57.023 28.663  1.00 24.04 ? 140 VAL A N   1 
ATOM   768  C  CA  . VAL A 1 105 ? 10.754  -55.631 28.801  1.00 27.30 ? 140 VAL A CA  1 
ATOM   769  C  C   . VAL A 1 105 ? 9.679   -55.533 29.878  1.00 26.18 ? 140 VAL A C   1 
ATOM   770  O  O   . VAL A 1 105 ? 8.641   -56.201 29.803  1.00 26.61 ? 140 VAL A O   1 
ATOM   771  C  CB  . VAL A 1 105 ? 10.264  -55.077 27.458  1.00 22.92 ? 140 VAL A CB  1 
ATOM   772  C  CG1 . VAL A 1 105 ? 9.709   -53.662 27.637  1.00 23.38 ? 140 VAL A CG1 1 
ATOM   773  C  CG2 . VAL A 1 105 ? 11.403  -55.096 26.438  1.00 21.71 ? 140 VAL A CG2 1 
ATOM   774  N  N   . ASP A 1 106 ? 9.933   -54.702 30.894  1.00 24.55 ? 141 ASP A N   1 
ATOM   775  C  CA  . ASP A 1 106 ? 9.021   -54.559 32.024  1.00 24.58 ? 141 ASP A CA  1 
ATOM   776  C  C   . ASP A 1 106 ? 7.933   -53.526 31.776  1.00 24.61 ? 141 ASP A C   1 
ATOM   777  O  O   . ASP A 1 106 ? 6.772   -53.754 32.138  1.00 24.76 ? 141 ASP A O   1 
ATOM   778  C  CB  . ASP A 1 106 ? 9.780   -54.137 33.282  1.00 24.68 ? 141 ASP A CB  1 
ATOM   779  C  CG  . ASP A 1 106 ? 10.792  -55.159 33.724  1.00 51.06 ? 141 ASP A CG  1 
ATOM   780  O  OD1 . ASP A 1 106 ? 10.405  -56.307 34.041  1.00 41.18 ? 141 ASP A OD1 1 
ATOM   781  O  OD2 . ASP A 1 106 ? 11.978  -54.794 33.787  1.00 31.88 ? 141 ASP A OD2 1 
ATOM   782  N  N   . GLU A 1 107 ? 8.293   -52.367 31.229  1.00 21.49 ? 142 GLU A N   1 
ATOM   783  C  CA  . GLU A 1 107 ? 7.328   -51.310 30.961  1.00 21.41 ? 142 GLU A CA  1 
ATOM   784  C  C   . GLU A 1 107 ? 7.637   -50.678 29.617  1.00 24.93 ? 142 GLU A C   1 
ATOM   785  O  O   . GLU A 1 107 ? 8.794   -50.624 29.190  1.00 22.34 ? 142 GLU A O   1 
ATOM   786  C  CB  . GLU A 1 107 ? 7.321   -50.227 32.059  1.00 26.91 ? 142 GLU A CB  1 
ATOM   787  C  CG  . GLU A 1 107 ? 7.359   -50.801 33.483  1.00 37.08 ? 142 GLU A CG  1 
ATOM   788  C  CD  . GLU A 1 107 ? 6.807   -49.864 34.548  1.00 41.31 ? 142 GLU A CD  1 
ATOM   789  O  OE1 . GLU A 1 107 ? 6.707   -48.646 34.299  1.00 26.98 ? 142 GLU A OE1 1 
ATOM   790  O  OE2 . GLU A 1 107 ? 6.483   -50.355 35.652  1.00 50.64 ? 142 GLU A OE2 1 
ATOM   791  N  N   . ILE A 1 108 ? 6.587   -50.214 28.946  1.00 19.63 ? 143 ILE A N   1 
ATOM   792  C  CA  . ILE A 1 108 ? 6.701   -49.493 27.686  1.00 17.02 ? 143 ILE A CA  1 
ATOM   793  C  C   . ILE A 1 108 ? 6.035   -48.139 27.879  1.00 17.60 ? 143 ILE A C   1 
ATOM   794  O  O   . ILE A 1 108 ? 4.876   -48.072 28.310  1.00 19.24 ? 143 ILE A O   1 
ATOM   795  C  CB  . ILE A 1 108 ? 6.044   -50.270 26.535  1.00 20.06 ? 143 ILE A CB  1 
ATOM   796  C  CG1 . ILE A 1 108 ? 6.718   -51.638 26.387  1.00 24.44 ? 143 ILE A CG1 1 
ATOM   797  C  CG2 . ILE A 1 108 ? 6.069   -49.457 25.248  1.00 21.65 ? 143 ILE A CG2 1 
ATOM   798  C  CD1 . ILE A 1 108 ? 6.045   -52.534 25.409  1.00 25.21 ? 143 ILE A CD1 1 
ATOM   799  N  N   . TYR A 1 109 ? 6.778   -47.069 27.613  1.00 15.84 ? 144 TYR A N   1 
ATOM   800  C  CA  . TYR A 1 109 ? 6.266   -45.710 27.715  1.00 16.85 ? 144 TYR A CA  1 
ATOM   801  C  C   . TYR A 1 109 ? 6.137   -45.165 26.306  1.00 17.87 ? 144 TYR A C   1 
ATOM   802  O  O   . TYR A 1 109 ? 7.080   -45.258 25.516  1.00 18.45 ? 144 TYR A O   1 
ATOM   803  C  CB  . TYR A 1 109 ? 7.230   -44.827 28.505  1.00 20.58 ? 144 TYR A CB  1 
ATOM   804  C  CG  . TYR A 1 109 ? 7.476   -45.280 29.933  1.00 18.69 ? 144 TYR A CG  1 
ATOM   805  C  CD1 . TYR A 1 109 ? 6.615   -46.177 30.575  1.00 17.58 ? 144 TYR A CD1 1 
ATOM   806  C  CD2 . TYR A 1 109 ? 8.569   -44.801 30.651  1.00 23.18 ? 144 TYR A CD2 1 
ATOM   807  C  CE1 . TYR A 1 109 ? 6.849   -46.585 31.865  1.00 20.63 ? 144 TYR A CE1 1 
ATOM   808  C  CE2 . TYR A 1 109 ? 8.804   -45.198 31.945  1.00 22.98 ? 144 TYR A CE2 1 
ATOM   809  C  CZ  . TYR A 1 109 ? 7.945   -46.098 32.558  1.00 27.84 ? 144 TYR A CZ  1 
ATOM   810  O  OH  . TYR A 1 109 ? 8.181   -46.507 33.854  1.00 26.81 ? 144 TYR A OH  1 
ATOM   811  N  N   . LEU A 1 110 ? 4.972   -44.609 25.987  1.00 16.51 ? 145 LEU A N   1 
ATOM   812  C  CA  . LEU A 1 110 ? 4.673   -44.113 24.650  1.00 14.38 ? 145 LEU A CA  1 
ATOM   813  C  C   . LEU A 1 110 ? 4.667   -42.594 24.695  1.00 16.31 ? 145 LEU A C   1 
ATOM   814  O  O   . LEU A 1 110 ? 3.939   -41.997 25.502  1.00 17.53 ? 145 LEU A O   1 
ATOM   815  C  CB  . LEU A 1 110 ? 3.299   -44.608 24.196  1.00 12.40 ? 145 LEU A CB  1 
ATOM   816  C  CG  . LEU A 1 110 ? 3.102   -46.125 24.066  1.00 15.14 ? 145 LEU A CG  1 
ATOM   817  C  CD1 . LEU A 1 110 ? 1.635   -46.461 23.757  1.00 18.50 ? 145 LEU A CD1 1 
ATOM   818  C  CD2 . LEU A 1 110 ? 4.005   -46.679 22.968  1.00 16.08 ? 145 LEU A CD2 1 
ATOM   819  N  N   . THR A 1 111 ? 5.481   -41.974 23.843  1.00 14.52 ? 146 THR A N   1 
ATOM   820  C  CA  . THR A 1 111 ? 5.410   -40.525 23.730  1.00 13.24 ? 146 THR A CA  1 
ATOM   821  C  C   . THR A 1 111 ? 4.059   -40.112 23.169  1.00 15.23 ? 146 THR A C   1 
ATOM   822  O  O   . THR A 1 111 ? 3.462   -39.131 23.627  1.00 16.27 ? 146 THR A O   1 
ATOM   823  C  CB  . THR A 1 111 ? 6.560   -40.002 22.868  1.00 15.90 ? 146 THR A CB  1 
ATOM   824  O  OG1 . THR A 1 111 ? 6.487   -40.578 21.558  1.00 16.74 ? 146 THR A OG1 1 
ATOM   825  C  CG2 . THR A 1 111 ? 7.914   -40.342 23.518  1.00 13.71 ? 146 THR A CG2 1 
ATOM   826  N  N   . HIS A 1 112 ? 3.552   -40.875 22.207  1.00 15.02 ? 147 HIS A N   1 
ATOM   827  C  CA  . HIS A 1 112 ? 2.245   -40.640 21.610  1.00 15.92 ? 147 HIS A CA  1 
ATOM   828  C  C   . HIS A 1 112 ? 1.900   -41.865 20.782  1.00 18.12 ? 147 HIS A C   1 
ATOM   829  O  O   . HIS A 1 112 ? 2.716   -42.781 20.631  1.00 16.86 ? 147 HIS A O   1 
ATOM   830  C  CB  . HIS A 1 112 ? 2.221   -39.357 20.781  1.00 14.29 ? 147 HIS A CB  1 
ATOM   831  C  CG  . HIS A 1 112 ? 3.111   -39.378 19.579  1.00 14.29 ? 147 HIS A CG  1 
ATOM   832  N  ND1 . HIS A 1 112 ? 4.475   -39.573 19.658  1.00 16.59 ? 147 HIS A ND1 1 
ATOM   833  C  CD2 . HIS A 1 112 ? 2.840   -39.134 18.274  1.00 17.55 ? 147 HIS A CD2 1 
ATOM   834  C  CE1 . HIS A 1 112 ? 4.999   -39.494 18.448  1.00 16.66 ? 147 HIS A CE1 1 
ATOM   835  N  NE2 . HIS A 1 112 ? 4.030   -39.230 17.590  1.00 15.91 ? 147 HIS A NE2 1 
ATOM   836  N  N   . MET A 1 113 ? 0.683   -41.872 20.233  1.00 14.61 ? 148 MET A N   1 
ATOM   837  C  CA  . MET A 1 113 ? 0.126   -43.088 19.656  1.00 13.59 ? 148 MET A CA  1 
ATOM   838  C  C   . MET A 1 113 ? 0.032   -43.068 18.133  1.00 14.48 ? 148 MET A C   1 
ATOM   839  O  O   . MET A 1 113 ? -0.756  -43.832 17.556  1.00 16.84 ? 148 MET A O   1 
ATOM   840  C  CB  . MET A 1 113 ? -1.221  -43.396 20.296  1.00 15.16 ? 148 MET A CB  1 
ATOM   841  C  CG  . MET A 1 113 ? -1.063  -43.848 21.728  1.00 17.86 ? 148 MET A CG  1 
ATOM   842  S  SD  . MET A 1 113 ? -2.629  -44.187 22.514  1.00 19.50 ? 148 MET A SD  1 
ATOM   843  C  CE  . MET A 1 113 ? -2.081  -44.196 24.223  1.00 24.03 ? 148 MET A CE  1 
ATOM   844  N  N   . HIS A 1 114 ? 0.838   -42.246 17.470  1.00 14.93 ? 149 HIS A N   1 
ATOM   845  C  CA  . HIS A 1 114 ? 0.952   -42.351 16.027  1.00 18.93 ? 149 HIS A CA  1 
ATOM   846  C  C   . HIS A 1 114 ? 1.490   -43.738 15.658  1.00 16.95 ? 149 HIS A C   1 
ATOM   847  O  O   . HIS A 1 114 ? 2.158   -44.390 16.473  1.00 15.59 ? 149 HIS A O   1 
ATOM   848  C  CB  . HIS A 1 114 ? 1.866   -41.245 15.503  1.00 19.52 ? 149 HIS A CB  1 
ATOM   849  C  CG  . HIS A 1 114 ? 1.166   -39.936 15.310  1.00 21.67 ? 149 HIS A CG  1 
ATOM   850  N  ND1 . HIS A 1 114 ? 1.832   -38.734 15.239  1.00 17.48 ? 149 HIS A ND1 1 
ATOM   851  C  CD2 . HIS A 1 114 ? -0.147  -39.643 15.158  1.00 23.66 ? 149 HIS A CD2 1 
ATOM   852  C  CE1 . HIS A 1 114 ? 0.964   -37.755 15.055  1.00 22.66 ? 149 HIS A CE1 1 
ATOM   853  N  NE2 . HIS A 1 114 ? -0.247  -38.281 15.007  1.00 20.22 ? 149 HIS A NE2 1 
ATOM   854  N  N   . PRO A 1 115 ? 1.176   -44.226 14.447  1.00 17.21 ? 150 PRO A N   1 
ATOM   855  C  CA  . PRO A 1 115 ? 1.484   -45.630 14.104  1.00 16.16 ? 150 PRO A CA  1 
ATOM   856  C  C   . PRO A 1 115 ? 2.954   -45.989 14.206  1.00 16.38 ? 150 PRO A C   1 
ATOM   857  O  O   . PRO A 1 115 ? 3.277   -47.135 14.560  1.00 18.99 ? 150 PRO A O   1 
ATOM   858  C  CB  . PRO A 1 115 ? 1.013   -45.750 12.649  1.00 17.88 ? 150 PRO A CB  1 
ATOM   859  C  CG  . PRO A 1 115 ? 0.029   -44.653 12.460  1.00 31.12 ? 150 PRO A CG  1 
ATOM   860  C  CD  . PRO A 1 115 ? 0.478   -43.529 13.351  1.00 20.13 ? 150 PRO A CD  1 
ATOM   861  N  N   . ASP A 1 116 ? 3.849   -45.049 13.887  1.00 16.76 ? 151 ASP A N   1 
ATOM   862  C  CA  . ASP A 1 116 ? 5.289   -45.290 13.930  1.00 16.69 ? 151 ASP A CA  1 
ATOM   863  C  C   . ASP A 1 116 ? 5.849   -45.348 15.350  1.00 19.91 ? 151 ASP A C   1 
ATOM   864  O  O   . ASP A 1 116 ? 7.065   -45.518 15.515  1.00 16.91 ? 151 ASP A O   1 
ATOM   865  C  CB  . ASP A 1 116 ? 6.051   -44.269 13.072  1.00 19.37 ? 151 ASP A CB  1 
ATOM   866  C  CG  . ASP A 1 116 ? 5.671   -42.815 13.373  1.00 19.48 ? 151 ASP A CG  1 
ATOM   867  O  OD1 . ASP A 1 116 ? 4.464   -42.482 13.497  1.00 19.11 ? 151 ASP A OD1 1 
ATOM   868  O  OD2 . ASP A 1 116 ? 6.602   -41.990 13.478  1.00 17.53 ? 151 ASP A OD2 1 
ATOM   869  N  N   . HIS A 1 117 ? 4.991   -45.230 16.373  1.00 17.25 ? 152 HIS A N   1 
ATOM   870  C  CA  . HIS A 1 117 ? 5.390   -45.364 17.768  1.00 14.78 ? 152 HIS A CA  1 
ATOM   871  C  C   . HIS A 1 117 ? 4.658   -46.467 18.507  1.00 18.82 ? 152 HIS A C   1 
ATOM   872  O  O   . HIS A 1 117 ? 5.211   -47.006 19.475  1.00 17.45 ? 152 HIS A O   1 
ATOM   873  C  CB  . HIS A 1 117 ? 5.184   -44.028 18.500  1.00 14.27 ? 152 HIS A CB  1 
ATOM   874  C  CG  . HIS A 1 117 ? 5.925   -42.908 17.855  1.00 17.20 ? 152 HIS A CG  1 
ATOM   875  N  ND1 . HIS A 1 117 ? 7.137   -42.449 18.326  1.00 19.03 ? 152 HIS A ND1 1 
ATOM   876  C  CD2 . HIS A 1 117 ? 5.685   -42.233 16.707  1.00 15.65 ? 152 HIS A CD2 1 
ATOM   877  C  CE1 . HIS A 1 117 ? 7.582   -41.496 17.528  1.00 18.62 ? 152 HIS A CE1 1 
ATOM   878  N  NE2 . HIS A 1 117 ? 6.729   -41.359 16.529  1.00 15.72 ? 152 HIS A NE2 1 
ATOM   879  N  N   . VAL A 1 118 ? 3.451   -46.826 18.073  1.00 15.45 ? 153 VAL A N   1 
ATOM   880  C  CA  . VAL A 1 118 ? 2.664   -47.856 18.738  1.00 19.38 ? 153 VAL A CA  1 
ATOM   881  C  C   . VAL A 1 118 ? 2.599   -49.155 17.959  1.00 19.71 ? 153 VAL A C   1 
ATOM   882  O  O   . VAL A 1 118 ? 2.195   -50.174 18.541  1.00 19.90 ? 153 VAL A O   1 
ATOM   883  C  CB  . VAL A 1 118 ? 1.232   -47.388 19.074  1.00 19.99 ? 153 VAL A CB  1 
ATOM   884  C  CG1 . VAL A 1 118 ? 1.254   -46.316 20.127  1.00 25.55 ? 153 VAL A CG1 1 
ATOM   885  C  CG2 . VAL A 1 118 ? 0.469   -46.967 17.798  1.00 17.16 ? 153 VAL A CG2 1 
ATOM   886  N  N   . GLY A 1 119 ? 2.949   -49.156 16.668  1.00 19.74 ? 154 GLY A N   1 
ATOM   887  C  CA  . GLY A 1 119 ? 2.731   -50.343 15.857  1.00 23.00 ? 154 GLY A CA  1 
ATOM   888  C  C   . GLY A 1 119 ? 3.500   -51.548 16.359  1.00 21.23 ? 154 GLY A C   1 
ATOM   889  O  O   . GLY A 1 119 ? 2.998   -52.675 16.324  1.00 20.36 ? 154 GLY A O   1 
ATOM   890  N  N   . GLY A 1 120 ? 4.716   -51.324 16.857  1.00 21.53 ? 155 GLY A N   1 
ATOM   891  C  CA  . GLY A 1 120 ? 5.559   -52.398 17.356  1.00 20.76 ? 155 GLY A CA  1 
ATOM   892  C  C   . GLY A 1 120 ? 5.019   -53.102 18.588  1.00 21.78 ? 155 GLY A C   1 
ATOM   893  O  O   . GLY A 1 120 ? 5.591   -54.121 18.996  1.00 19.13 ? 155 GLY A O   1 
ATOM   894  N  N   . LEU A 1 121 ? 3.933   -52.598 19.182  1.00 18.67 ? 156 LEU A N   1 
ATOM   895  C  CA  . LEU A 1 121 ? 3.342   -53.279 20.329  1.00 19.72 ? 156 LEU A CA  1 
ATOM   896  C  C   . LEU A 1 121 ? 2.824   -54.665 19.976  1.00 21.87 ? 156 LEU A C   1 
ATOM   897  O  O   . LEU A 1 121 ? 2.686   -55.512 20.867  1.00 23.46 ? 156 LEU A O   1 
ATOM   898  C  CB  . LEU A 1 121 ? 2.197   -52.453 20.921  1.00 18.74 ? 156 LEU A CB  1 
ATOM   899  C  CG  . LEU A 1 121 ? 2.662   -51.238 21.724  1.00 19.68 ? 156 LEU A CG  1 
ATOM   900  C  CD1 . LEU A 1 121 ? 1.481   -50.374 22.136  1.00 20.38 ? 156 LEU A CD1 1 
ATOM   901  C  CD2 . LEU A 1 121 ? 3.471   -51.689 22.941  1.00 20.88 ? 156 LEU A CD2 1 
ATOM   902  N  N   . MET A 1 122 ? 2.537   -54.928 18.707  1.00 20.33 ? 157 MET A N   1 
ATOM   903  C  CA  . MET A 1 122 ? 1.848   -56.153 18.358  1.00 24.15 ? 157 MET A CA  1 
ATOM   904  C  C   . MET A 1 122 ? 2.610   -56.848 17.244  1.00 32.25 ? 157 MET A C   1 
ATOM   905  O  O   . MET A 1 122 ? 3.140   -56.196 16.341  1.00 26.25 ? 157 MET A O   1 
ATOM   906  C  CB  . MET A 1 122 ? 0.433   -55.836 17.884  1.00 25.07 ? 157 MET A CB  1 
ATOM   907  C  CG  . MET A 1 122 ? -0.440  -55.309 19.022  1.00 23.22 ? 157 MET A CG  1 
ATOM   908  S  SD  . MET A 1 122 ? -0.902  -56.510 20.261  1.00 26.72 ? 157 MET A SD  1 
ATOM   909  C  CE  . MET A 1 122 ? -1.568  -57.829 19.270  1.00 25.08 ? 157 MET A CE  1 
ATOM   910  N  N   . VAL A 1 123 ? 2.685   -58.167 17.322  1.00 26.81 ? 158 VAL A N   1 
ATOM   911  C  CA  . VAL A 1 123 ? 3.170   -58.974 16.213  1.00 30.52 ? 158 VAL A CA  1 
ATOM   912  C  C   . VAL A 1 123 ? 2.002   -59.861 15.795  1.00 44.50 ? 158 VAL A C   1 
ATOM   913  O  O   . VAL A 1 123 ? 1.676   -60.848 16.464  1.00 31.39 ? 158 VAL A O   1 
ATOM   914  C  CB  . VAL A 1 123 ? 4.445   -59.762 16.555  1.00 38.44 ? 158 VAL A CB  1 
ATOM   915  C  CG1 . VAL A 1 123 ? 4.326   -60.461 17.907  1.00 54.55 ? 158 VAL A CG1 1 
ATOM   916  C  CG2 . VAL A 1 123 ? 4.778   -60.752 15.450  1.00 38.71 ? 158 VAL A CG2 1 
ATOM   917  N  N   . GLY A 1 124 ? 1.336   -59.489 14.711  1.00 42.16 ? 159 GLY A N   1 
ATOM   918  C  CA  . GLY A 1 124 ? 0.111   -60.184 14.361  1.00 35.09 ? 159 GLY A CA  1 
ATOM   919  C  C   . GLY A 1 124 ? -0.930  -59.925 15.431  1.00 42.03 ? 159 GLY A C   1 
ATOM   920  O  O   . GLY A 1 124 ? -1.151  -58.781 15.846  1.00 42.08 ? 159 GLY A O   1 
ATOM   921  N  N   . GLU A 1 125 ? -1.567  -60.997 15.900  1.00 43.99 ? 160 GLU A N   1 
ATOM   922  C  CA  . GLU A 1 125 ? -2.548  -60.922 16.975  1.00 34.56 ? 160 GLU A CA  1 
ATOM   923  C  C   . GLU A 1 125 ? -1.935  -61.171 18.347  1.00 44.10 ? 160 GLU A C   1 
ATOM   924  O  O   . GLU A 1 125 ? -2.676  -61.294 19.327  1.00 39.77 ? 160 GLU A O   1 
ATOM   925  C  CB  . GLU A 1 125 ? -3.695  -61.913 16.734  1.00 39.89 ? 160 GLU A CB  1 
ATOM   926  C  CG  . GLU A 1 125 ? -4.129  -62.069 15.278  1.00 54.25 ? 160 GLU A CG  1 
ATOM   927  C  CD  . GLU A 1 125 ? -4.443  -60.740 14.607  1.00 79.78 ? 160 GLU A CD  1 
ATOM   928  O  OE1 . GLU A 1 125 ? -5.320  -60.008 15.115  1.00 73.90 ? 160 GLU A OE1 1 
ATOM   929  O  OE2 . GLU A 1 125 ? -3.805  -60.422 13.578  1.00 74.14 ? 160 GLU A OE2 1 
ATOM   930  N  N   . GLN A 1 126 ? -0.611  -61.257 18.438  1.00 35.12 ? 161 GLN A N   1 
ATOM   931  C  CA  . GLN A 1 126 ? 0.078   -61.562 19.684  1.00 28.61 ? 161 GLN A CA  1 
ATOM   932  C  C   . GLN A 1 126 ? 0.758   -60.313 20.226  1.00 31.51 ? 161 GLN A C   1 
ATOM   933  O  O   . GLN A 1 126 ? 1.309   -59.513 19.461  1.00 28.47 ? 161 GLN A O   1 
ATOM   934  C  CB  . GLN A 1 126 ? 1.115   -62.675 19.473  1.00 33.28 ? 161 GLN A CB  1 
ATOM   935  C  CG  . GLN A 1 126 ? 0.543   -63.949 18.834  1.00 48.16 ? 161 GLN A CG  1 
ATOM   936  C  CD  . GLN A 1 126 ? 0.543   -63.902 17.309  1.00 74.64 ? 161 GLN A CD  1 
ATOM   937  O  OE1 . GLN A 1 126 ? 1.564   -63.605 16.683  1.00 70.48 ? 161 GLN A OE1 1 
ATOM   938  N  NE2 . GLN A 1 126 ? -0.609  -64.188 16.707  1.00 67.96 ? 161 GLN A NE2 1 
ATOM   939  N  N   . LEU A 1 127 ? 0.699   -60.133 21.547  1.00 25.01 ? 162 LEU A N   1 
ATOM   940  C  CA  . LEU A 1 127 ? 1.457   -59.055 22.167  1.00 26.77 ? 162 LEU A CA  1 
ATOM   941  C  C   . LEU A 1 127 ? 2.935   -59.249 21.866  1.00 27.66 ? 162 LEU A C   1 
ATOM   942  O  O   . LEU A 1 127 ? 3.485   -60.336 22.072  1.00 28.92 ? 162 LEU A O   1 
ATOM   943  C  CB  . LEU A 1 127 ? 1.247   -59.036 23.682  1.00 25.00 ? 162 LEU A CB  1 
ATOM   944  C  CG  . LEU A 1 127 ? -0.182  -59.063 24.232  1.00 33.06 ? 162 LEU A CG  1 
ATOM   945  C  CD1 . LEU A 1 127 ? -0.165  -59.033 25.752  1.00 33.43 ? 162 LEU A CD1 1 
ATOM   946  C  CD2 . LEU A 1 127 ? -0.970  -57.895 23.691  1.00 25.11 ? 162 LEU A CD2 1 
ATOM   947  N  N   . ALA A 1 128 ? 3.574   -58.192 21.366  1.00 28.95 ? 163 ALA A N   1 
ATOM   948  C  CA  . ALA A 1 128 ? 5.006   -58.260 21.113  1.00 29.50 ? 163 ALA A CA  1 
ATOM   949  C  C   . ALA A 1 128 ? 5.794   -58.312 22.413  1.00 26.17 ? 163 ALA A C   1 
ATOM   950  O  O   . ALA A 1 128 ? 6.897   -58.863 22.443  1.00 27.23 ? 163 ALA A O   1 
ATOM   951  C  CB  . ALA A 1 128 ? 5.449   -57.058 20.281  1.00 22.86 ? 163 ALA A CB  1 
ATOM   952  N  N   . PHE A 1 129 ? 5.238   -57.754 23.492  1.00 23.77 ? 164 PHE A N   1 
ATOM   953  C  CA  . PHE A 1 129 ? 5.927   -57.618 24.774  1.00 26.52 ? 164 PHE A CA  1 
ATOM   954  C  C   . PHE A 1 129 ? 5.038   -58.253 25.827  1.00 24.89 ? 164 PHE A C   1 
ATOM   955  O  O   . PHE A 1 129 ? 4.275   -57.564 26.516  1.00 27.25 ? 164 PHE A O   1 
ATOM   956  C  CB  . PHE A 1 129 ? 6.246   -56.153 25.072  1.00 22.27 ? 164 PHE A CB  1 
ATOM   957  C  CG  . PHE A 1 129 ? 7.107   -55.517 24.021  1.00 24.42 ? 164 PHE A CG  1 
ATOM   958  C  CD1 . PHE A 1 129 ? 8.483   -55.661 24.066  1.00 26.46 ? 164 PHE A CD1 1 
ATOM   959  C  CD2 . PHE A 1 129 ? 6.541   -54.813 22.964  1.00 23.19 ? 164 PHE A CD2 1 
ATOM   960  C  CE1 . PHE A 1 129 ? 9.289   -55.096 23.092  1.00 25.93 ? 164 PHE A CE1 1 
ATOM   961  C  CE2 . PHE A 1 129 ? 7.340   -54.244 21.992  1.00 23.92 ? 164 PHE A CE2 1 
ATOM   962  C  CZ  . PHE A 1 129 ? 8.714   -54.385 22.054  1.00 26.33 ? 164 PHE A CZ  1 
ATOM   963  N  N   . PRO A 1 130 ? 5.115   -59.577 25.975  1.00 27.67 ? 165 PRO A N   1 
ATOM   964  C  CA  . PRO A 1 130 ? 4.079   -60.306 26.728  1.00 34.48 ? 165 PRO A CA  1 
ATOM   965  C  C   . PRO A 1 130 ? 4.071   -60.051 28.230  1.00 33.38 ? 165 PRO A C   1 
ATOM   966  O  O   . PRO A 1 130 ? 3.078   -60.402 28.884  1.00 27.58 ? 165 PRO A O   1 
ATOM   967  C  CB  . PRO A 1 130 ? 4.371   -61.779 26.404  1.00 42.53 ? 165 PRO A CB  1 
ATOM   968  C  CG  . PRO A 1 130 ? 5.807   -61.805 25.998  1.00 41.17 ? 165 PRO A CG  1 
ATOM   969  C  CD  . PRO A 1 130 ? 6.089   -60.480 25.339  1.00 26.72 ? 165 PRO A CD  1 
ATOM   970  N  N   . ASN A 1 131 ? 5.123   -59.467 28.801  1.00 26.90 ? 166 ASN A N   1 
ATOM   971  C  CA  . ASN A 1 131 ? 5.173   -59.187 30.233  1.00 28.27 ? 166 ASN A CA  1 
ATOM   972  C  C   . ASN A 1 131 ? 5.152   -57.703 30.578  1.00 32.18 ? 166 ASN A C   1 
ATOM   973  O  O   . ASN A 1 131 ? 5.183   -57.357 31.763  1.00 37.57 ? 166 ASN A O   1 
ATOM   974  C  CB  . ASN A 1 131 ? 6.387   -59.873 30.869  1.00 30.63 ? 166 ASN A CB  1 
ATOM   975  C  CG  . ASN A 1 131 ? 6.423   -61.354 30.576  1.00 35.11 ? 166 ASN A CG  1 
ATOM   976  O  OD1 . ASN A 1 131 ? 5.414   -62.047 30.729  1.00 32.94 ? 166 ASN A OD1 1 
ATOM   977  N  ND2 . ASN A 1 131 ? 7.572   -61.851 30.137  1.00 34.93 ? 166 ASN A ND2 1 
ATOM   978  N  N   . ALA A 1 132 ? 5.086   -56.823 29.588  1.00 25.17 ? 167 ALA A N   1 
ATOM   979  C  CA  . ALA A 1 132 ? 5.217   -55.395 29.823  1.00 24.77 ? 167 ALA A CA  1 
ATOM   980  C  C   . ALA A 1 132 ? 3.876   -54.771 30.185  1.00 26.97 ? 167 ALA A C   1 
ATOM   981  O  O   . ALA A 1 132 ? 2.815   -55.227 29.750  1.00 29.83 ? 167 ALA A O   1 
ATOM   982  C  CB  . ALA A 1 132 ? 5.777   -54.701 28.580  1.00 24.71 ? 167 ALA A CB  1 
ATOM   983  N  N   . VAL A 1 133 ? 3.937   -53.725 31.005  1.00 21.84 ? 168 VAL A N   1 
ATOM   984  C  CA  . VAL A 1 133 ? 2.824   -52.801 31.193  1.00 20.39 ? 168 VAL A CA  1 
ATOM   985  C  C   . VAL A 1 133 ? 3.099   -51.584 30.324  1.00 23.52 ? 168 VAL A C   1 
ATOM   986  O  O   . VAL A 1 133 ? 4.217   -51.058 30.323  1.00 23.69 ? 168 VAL A O   1 
ATOM   987  C  CB  . VAL A 1 133 ? 2.675   -52.393 32.669  1.00 27.60 ? 168 VAL A CB  1 
ATOM   988  C  CG1 . VAL A 1 133 ? 1.638   -51.299 32.815  1.00 29.36 ? 168 VAL A CG1 1 
ATOM   989  C  CG2 . VAL A 1 133 ? 2.287   -53.591 33.518  1.00 27.55 ? 168 VAL A CG2 1 
ATOM   990  N  N   . VAL A 1 134 ? 2.092   -51.146 29.576  1.00 21.82 ? 169 VAL A N   1 
ATOM   991  C  CA  . VAL A 1 134 ? 2.197   -49.989 28.696  1.00 18.72 ? 169 VAL A CA  1 
ATOM   992  C  C   . VAL A 1 134 ? 1.641   -48.774 29.426  1.00 20.13 ? 169 VAL A C   1 
ATOM   993  O  O   . VAL A 1 134 ? 0.606   -48.856 30.100  1.00 20.52 ? 169 VAL A O   1 
ATOM   994  C  CB  . VAL A 1 134 ? 1.439   -50.241 27.378  1.00 19.41 ? 169 VAL A CB  1 
ATOM   995  C  CG1 . VAL A 1 134 ? 1.532   -49.033 26.465  1.00 20.14 ? 169 VAL A CG1 1 
ATOM   996  C  CG2 . VAL A 1 134 ? 1.980   -51.494 26.695  1.00 21.46 ? 169 VAL A CG2 1 
ATOM   997  N  N   . ARG A 1 135 ? 2.346   -47.656 29.328  1.00 16.49 ? 170 ARG A N   1 
ATOM   998  C  CA  . ARG A 1 135 ? 1.911   -46.415 29.952  1.00 16.28 ? 170 ARG A CA  1 
ATOM   999  C  C   . ARG A 1 135 ? 1.959   -45.288 28.932  1.00 19.53 ? 170 ARG A C   1 
ATOM   1000 O  O   . ARG A 1 135 ? 2.861   -45.229 28.088  1.00 18.24 ? 170 ARG A O   1 
ATOM   1001 C  CB  . ARG A 1 135 ? 2.762   -46.061 31.180  1.00 17.94 ? 170 ARG A CB  1 
ATOM   1002 C  CG  . ARG A 1 135 ? 2.897   -47.202 32.187  1.00 21.08 ? 170 ARG A CG  1 
ATOM   1003 C  CD  . ARG A 1 135 ? 3.141   -46.679 33.598  1.00 26.27 ? 170 ARG A CD  1 
ATOM   1004 N  NE  . ARG A 1 135 ? 2.015   -45.899 34.101  1.00 21.87 ? 170 ARG A NE  1 
ATOM   1005 C  CZ  . ARG A 1 135 ? 1.994   -45.305 35.287  1.00 27.28 ? 170 ARG A CZ  1 
ATOM   1006 N  NH1 . ARG A 1 135 ? 3.041   -45.340 36.095  1.00 24.66 ? 170 ARG A NH1 1 
ATOM   1007 N  NH2 . ARG A 1 135 ? 0.900   -44.651 35.667  1.00 26.75 ? 170 ARG A NH2 1 
ATOM   1008 N  N   . ALA A 1 136 ? 0.961   -44.413 29.005  1.00 18.13 ? 171 ALA A N   1 
ATOM   1009 C  CA  . ALA A 1 136 ? 0.881   -43.210 28.193  1.00 16.02 ? 171 ALA A CA  1 
ATOM   1010 C  C   . ALA A 1 136 ? -0.033  -42.241 28.929  1.00 17.28 ? 171 ALA A C   1 
ATOM   1011 O  O   . ALA A 1 136 ? -0.729  -42.621 29.875  1.00 16.78 ? 171 ALA A O   1 
ATOM   1012 C  CB  . ALA A 1 136 ? 0.338   -43.515 26.792  1.00 16.45 ? 171 ALA A CB  1 
ATOM   1013 N  N   . ASP A 1 137 ? -0.008  -40.981 28.512  1.00 14.50 ? 172 ASP A N   1 
ATOM   1014 C  CA  . ASP A 1 137 ? -0.908  -40.023 29.139  1.00 17.77 ? 172 ASP A CA  1 
ATOM   1015 C  C   . ASP A 1 137 ? -2.370  -40.382 28.880  1.00 17.09 ? 172 ASP A C   1 
ATOM   1016 O  O   . ASP A 1 137 ? -2.744  -40.844 27.795  1.00 16.30 ? 172 ASP A O   1 
ATOM   1017 C  CB  . ASP A 1 137 ? -0.632  -38.594 28.674  1.00 17.84 ? 172 ASP A CB  1 
ATOM   1018 C  CG  . ASP A 1 137 ? -1.253  -37.569 29.609  1.00 21.09 ? 172 ASP A CG  1 
ATOM   1019 O  OD1 . ASP A 1 137 ? -2.484  -37.331 29.524  1.00 24.45 ? 172 ASP A OD1 1 
ATOM   1020 O  OD2 . ASP A 1 137 ? -0.520  -37.033 30.465  1.00 25.04 ? 172 ASP A OD2 1 
ATOM   1021 N  N   . GLN A 1 138 ? -3.201  -40.150 29.903  1.00 17.64 ? 173 GLN A N   1 
ATOM   1022 C  CA  . GLN A 1 138 ? -4.637  -40.370 29.778  1.00 16.45 ? 173 GLN A CA  1 
ATOM   1023 C  C   . GLN A 1 138 ? -5.217  -39.629 28.578  1.00 17.81 ? 173 GLN A C   1 
ATOM   1024 O  O   . GLN A 1 138 ? -6.080  -40.162 27.871  1.00 18.20 ? 173 GLN A O   1 
ATOM   1025 C  CB  . GLN A 1 138 ? -5.340  -39.911 31.056  1.00 18.19 ? 173 GLN A CB  1 
ATOM   1026 C  CG  . GLN A 1 138 ? -6.824  -40.291 31.086  1.00 18.85 ? 173 GLN A CG  1 
ATOM   1027 C  CD  . GLN A 1 138 ? -7.021  -41.717 31.550  1.00 24.08 ? 173 GLN A CD  1 
ATOM   1028 O  OE1 . GLN A 1 138 ? -6.597  -42.088 32.648  1.00 22.04 ? 173 GLN A OE1 1 
ATOM   1029 N  NE2 . GLN A 1 138 ? -7.642  -42.535 30.706  1.00 21.31 ? 173 GLN A NE2 1 
ATOM   1030 N  N   . LYS A 1 139 ? -4.764  -38.395 28.335  1.00 17.01 ? 174 LYS A N   1 
ATOM   1031 C  CA  . LYS A 1 139 ? -5.293  -37.625 27.211  1.00 15.48 ? 174 LYS A CA  1 
ATOM   1032 C  C   . LYS A 1 139 ? -4.979  -38.292 25.873  1.00 14.58 ? 174 LYS A C   1 
ATOM   1033 O  O   . LYS A 1 139 ? -5.806  -38.284 24.949  1.00 20.84 ? 174 LYS A O   1 
ATOM   1034 C  CB  . LYS A 1 139 ? -4.744  -36.201 27.259  1.00 17.28 ? 174 LYS A CB  1 
ATOM   1035 C  CG  . LYS A 1 139 ? -5.304  -35.383 28.412  1.00 22.78 ? 174 LYS A CG  1 
ATOM   1036 C  CD  . LYS A 1 139 ? -4.926  -33.913 28.276  1.00 30.92 ? 174 LYS A CD  1 
ATOM   1037 C  CE  . LYS A 1 139 ? -5.521  -33.089 29.411  1.00 38.98 ? 174 LYS A CE  1 
ATOM   1038 N  NZ  . LYS A 1 139 ? -4.526  -32.161 30.025  1.00 46.96 ? 174 LYS A NZ  1 
ATOM   1039 N  N   . GLU A 1 140 ? -3.789  -38.889 25.761  1.00 15.97 ? 175 GLU A N   1 
ATOM   1040 C  CA  . GLU A 1 140 ? -3.402  -39.579 24.538  1.00 17.22 ? 175 GLU A CA  1 
ATOM   1041 C  C   . GLU A 1 140 ? -4.313  -40.773 24.279  1.00 19.15 ? 175 GLU A C   1 
ATOM   1042 O  O   . GLU A 1 140 ? -4.901  -40.910 23.194  1.00 17.65 ? 175 GLU A O   1 
ATOM   1043 C  CB  . GLU A 1 140 ? -1.951  -40.045 24.667  1.00 17.81 ? 175 GLU A CB  1 
ATOM   1044 C  CG  . GLU A 1 140 ? -1.382  -40.575 23.355  1.00 17.25 ? 175 GLU A CG  1 
ATOM   1045 C  CD  . GLU A 1 140 ? -1.171  -39.471 22.336  1.00 16.43 ? 175 GLU A CD  1 
ATOM   1046 O  OE1 . GLU A 1 140 ? -1.307  -38.273 22.685  1.00 17.80 ? 175 GLU A OE1 1 
ATOM   1047 O  OE2 . GLU A 1 140 ? -0.886  -39.798 21.168  1.00 18.41 ? 175 GLU A OE2 1 
ATOM   1048 N  N   . ALA A 1 141 ? -4.459  -41.637 25.285  1.00 17.44 ? 176 ALA A N   1 
ATOM   1049 C  CA  . ALA A 1 141 ? -5.305  -42.817 25.144  1.00 15.73 ? 176 ALA A CA  1 
ATOM   1050 C  C   . ALA A 1 141 ? -6.753  -42.429 24.884  1.00 18.21 ? 176 ALA A C   1 
ATOM   1051 O  O   . ALA A 1 141 ? -7.416  -43.005 24.011  1.00 18.22 ? 176 ALA A O   1 
ATOM   1052 C  CB  . ALA A 1 141 ? -5.205  -43.675 26.406  1.00 19.67 ? 176 ALA A CB  1 
ATOM   1053 N  N   . ASP A 1 142 ? -7.267  -41.455 25.634  1.00 16.04 ? 177 ASP A N   1 
ATOM   1054 C  CA  . ASP A 1 142 ? -8.665  -41.074 25.468  1.00 18.47 ? 177 ASP A CA  1 
ATOM   1055 C  C   . ASP A 1 142 ? -8.911  -40.574 24.054  1.00 16.09 ? 177 ASP A C   1 
ATOM   1056 O  O   . ASP A 1 142 ? -9.974  -40.836 23.469  1.00 19.69 ? 177 ASP A O   1 
ATOM   1057 C  CB  . ASP A 1 142 ? -9.041  -39.983 26.476  1.00 20.84 ? 177 ASP A CB  1 
ATOM   1058 C  CG  . ASP A 1 142 ? -9.256  -40.520 27.883  1.00 23.76 ? 177 ASP A CG  1 
ATOM   1059 O  OD1 . ASP A 1 142 ? -9.012  -41.721 28.126  1.00 22.22 ? 177 ASP A OD1 1 
ATOM   1060 O  OD2 . ASP A 1 142 ? -9.657  -39.725 28.764  1.00 24.87 ? 177 ASP A OD2 1 
ATOM   1061 N  N   . PHE A 1 143 ? -7.946  -39.835 23.491  1.00 18.42 ? 178 PHE A N   1 
ATOM   1062 C  CA  . PHE A 1 143 ? -8.133  -39.311 22.149  1.00 16.40 ? 178 PHE A CA  1 
ATOM   1063 C  C   . PHE A 1 143 ? -8.089  -40.417 21.102  1.00 16.22 ? 178 PHE A C   1 
ATOM   1064 O  O   . PHE A 1 143 ? -8.985  -40.510 20.253  1.00 18.73 ? 178 PHE A O   1 
ATOM   1065 C  CB  . PHE A 1 143 ? -7.090  -38.238 21.846  1.00 17.61 ? 178 PHE A CB  1 
ATOM   1066 C  CG  . PHE A 1 143 ? -7.243  -37.643 20.486  1.00 17.96 ? 178 PHE A CG  1 
ATOM   1067 C  CD1 . PHE A 1 143 ? -8.234  -36.702 20.241  1.00 23.57 ? 178 PHE A CD1 1 
ATOM   1068 C  CD2 . PHE A 1 143 ? -6.422  -38.037 19.438  1.00 20.12 ? 178 PHE A CD2 1 
ATOM   1069 C  CE1 . PHE A 1 143 ? -8.392  -36.154 18.972  1.00 26.98 ? 178 PHE A CE1 1 
ATOM   1070 C  CE2 . PHE A 1 143 ? -6.575  -37.489 18.172  1.00 23.62 ? 178 PHE A CE2 1 
ATOM   1071 C  CZ  . PHE A 1 143 ? -7.562  -36.549 17.943  1.00 26.22 ? 178 PHE A CZ  1 
ATOM   1072 N  N   . TRP A 1 144 ? -7.045  -41.258 21.130  1.00 20.28 ? 179 TRP A N   1 
ATOM   1073 C  CA  . TRP A 1 144 ? -6.839  -42.187 20.020  1.00 13.66 ? 179 TRP A CA  1 
ATOM   1074 C  C   . TRP A 1 144 ? -7.684  -43.449 20.122  1.00 17.73 ? 179 TRP A C   1 
ATOM   1075 O  O   . TRP A 1 144 ? -7.907  -44.110 19.097  1.00 18.19 ? 179 TRP A O   1 
ATOM   1076 C  CB  . TRP A 1 144 ? -5.358  -42.557 19.875  1.00 15.86 ? 179 TRP A CB  1 
ATOM   1077 C  CG  . TRP A 1 144 ? -4.518  -41.426 19.414  1.00 17.97 ? 179 TRP A CG  1 
ATOM   1078 C  CD1 . TRP A 1 144 ? -3.608  -40.720 20.153  1.00 19.58 ? 179 TRP A CD1 1 
ATOM   1079 C  CD2 . TRP A 1 144 ? -4.503  -40.850 18.104  1.00 19.00 ? 179 TRP A CD2 1 
ATOM   1080 N  NE1 . TRP A 1 144 ? -3.031  -39.742 19.386  1.00 17.82 ? 179 TRP A NE1 1 
ATOM   1081 C  CE2 . TRP A 1 144 ? -3.562  -39.799 18.120  1.00 22.51 ? 179 TRP A CE2 1 
ATOM   1082 C  CE3 . TRP A 1 144 ? -5.207  -41.113 16.919  1.00 16.94 ? 179 TRP A CE3 1 
ATOM   1083 C  CZ2 . TRP A 1 144 ? -3.295  -39.021 16.996  1.00 22.52 ? 179 TRP A CZ2 1 
ATOM   1084 C  CZ3 . TRP A 1 144 ? -4.936  -40.345 15.798  1.00 18.91 ? 179 TRP A CZ3 1 
ATOM   1085 C  CH2 . TRP A 1 144 ? -3.991  -39.309 15.845  1.00 21.86 ? 179 TRP A CH2 1 
ATOM   1086 N  N   . LEU A 1 145 ? -8.156  -43.801 21.314  1.00 14.42 ? 180 LEU A N   1 
ATOM   1087 C  CA  . LEU A 1 145 ? -8.992  -44.975 21.481  1.00 16.74 ? 180 LEU A CA  1 
ATOM   1088 C  C   . LEU A 1 145 ? -10.472 -44.633 21.376  1.00 19.79 ? 180 LEU A C   1 
ATOM   1089 O  O   . LEU A 1 145 ? -11.318 -45.499 21.619  1.00 19.06 ? 180 LEU A O   1 
ATOM   1090 C  CB  . LEU A 1 145 ? -8.682  -45.671 22.812  1.00 16.78 ? 180 LEU A CB  1 
ATOM   1091 C  CG  . LEU A 1 145 ? -7.205  -46.070 22.934  1.00 22.93 ? 180 LEU A CG  1 
ATOM   1092 C  CD1 . LEU A 1 145 ? -6.925  -46.762 24.257  1.00 23.69 ? 180 LEU A CD1 1 
ATOM   1093 C  CD2 . LEU A 1 145 ? -6.740  -46.932 21.758  1.00 23.97 ? 180 LEU A CD2 1 
ATOM   1094 N  N   . SER A 1 146 ? -10.796 -43.393 21.008  1.00 18.54 ? 181 SER A N   1 
ATOM   1095 C  CA  . SER A 1 146 ? -12.173 -42.911 20.909  1.00 18.97 ? 181 SER A CA  1 
ATOM   1096 C  C   . SER A 1 146 ? -12.832 -43.410 19.625  1.00 17.78 ? 181 SER A C   1 
ATOM   1097 O  O   . SER A 1 146 ? -12.436 -43.016 18.523  1.00 20.82 ? 181 SER A O   1 
ATOM   1098 C  CB  . SER A 1 146 ? -12.159 -41.386 20.926  1.00 20.50 ? 181 SER A CB  1 
ATOM   1099 O  OG  . SER A 1 146 ? -13.442 -40.860 20.670  1.00 21.59 ? 181 SER A OG  1 
ATOM   1100 N  N   . GLN A 1 147 ? -13.863 -44.251 19.770  1.00 17.08 ? 182 GLN A N   1 
ATOM   1101 C  CA  . GLN A 1 147 ? -14.619 -44.724 18.608  1.00 20.37 ? 182 GLN A CA  1 
ATOM   1102 C  C   . GLN A 1 147 ? -15.269 -43.572 17.848  1.00 19.53 ? 182 GLN A C   1 
ATOM   1103 O  O   . GLN A 1 147 ? -15.341 -43.598 16.614  1.00 23.54 ? 182 GLN A O   1 
ATOM   1104 C  CB  . GLN A 1 147 ? -15.675 -45.747 19.029  1.00 26.97 ? 182 GLN A CB  1 
ATOM   1105 C  CG  . GLN A 1 147 ? -15.117 -47.020 19.671  1.00 27.57 ? 182 GLN A CG  1 
ATOM   1106 C  CD  . GLN A 1 147 ? -16.195 -47.819 20.399  1.00 45.39 ? 182 GLN A CD  1 
ATOM   1107 O  OE1 . GLN A 1 147 ? -16.152 -47.965 21.621  1.00 47.01 ? 182 GLN A OE1 1 
ATOM   1108 N  NE2 . GLN A 1 147 ? -17.174 -48.321 19.652  1.00 40.50 ? 182 GLN A NE2 1 
ATOM   1109 N  N   . THR A 1 148 ? -15.778 -42.563 18.561  1.00 19.75 ? 183 THR A N   1 
ATOM   1110 C  CA  . THR A 1 148 ? -16.434 -41.464 17.855  1.00 20.85 ? 183 THR A CA  1 
ATOM   1111 C  C   . THR A 1 148 ? -15.420 -40.562 17.155  1.00 20.04 ? 183 THR A C   1 
ATOM   1112 O  O   . THR A 1 148 ? -15.721 -40.015 16.087  1.00 23.77 ? 183 THR A O   1 
ATOM   1113 C  CB  . THR A 1 148 ? -17.348 -40.671 18.788  1.00 22.36 ? 183 THR A CB  1 
ATOM   1114 O  OG1 . THR A 1 148 ? -16.576 -40.135 19.867  1.00 22.43 ? 183 THR A OG1 1 
ATOM   1115 C  CG2 . THR A 1 148 ? -18.437 -41.583 19.335  1.00 25.73 ? 183 THR A CG2 1 
ATOM   1116 N  N   . ASN A 1 149 ? -14.232 -40.386 17.737  1.00 19.15 ? 184 ASN A N   1 
ATOM   1117 C  CA  . ASN A 1 149 ? -13.179 -39.670 17.020  1.00 21.77 ? 184 ASN A CA  1 
ATOM   1118 C  C   . ASN A 1 149 ? -12.836 -40.381 15.718  1.00 20.43 ? 184 ASN A C   1 
ATOM   1119 O  O   . ASN A 1 149 ? -12.621 -39.734 14.688  1.00 21.87 ? 184 ASN A O   1 
ATOM   1120 C  CB  . ASN A 1 149 ? -11.926 -39.525 17.888  1.00 20.24 ? 184 ASN A CB  1 
ATOM   1121 C  CG  . ASN A 1 149 ? -12.064 -38.447 18.946  1.00 23.41 ? 184 ASN A CG  1 
ATOM   1122 O  OD1 . ASN A 1 149 ? -13.012 -37.661 18.929  1.00 22.11 ? 184 ASN A OD1 1 
ATOM   1123 N  ND2 . ASN A 1 149 ? -11.112 -38.403 19.873  1.00 22.65 ? 184 ASN A ND2 1 
ATOM   1124 N  N   . LEU A 1 150 ? -12.775 -41.717 15.749  1.00 20.70 ? 185 LEU A N   1 
ATOM   1125 C  CA  . LEU A 1 150 ? -12.518 -42.473 14.527  1.00 19.85 ? 185 LEU A CA  1 
ATOM   1126 C  C   . LEU A 1 150 ? -13.639 -42.272 13.515  1.00 25.08 ? 185 LEU A C   1 
ATOM   1127 O  O   . LEU A 1 150 ? -13.387 -42.050 12.326  1.00 25.08 ? 185 LEU A O   1 
ATOM   1128 C  CB  . LEU A 1 150 ? -12.338 -43.957 14.855  1.00 22.96 ? 185 LEU A CB  1 
ATOM   1129 C  CG  . LEU A 1 150 ? -12.458 -44.978 13.716  1.00 25.30 ? 185 LEU A CG  1 
ATOM   1130 C  CD1 . LEU A 1 150 ? -11.478 -44.679 12.590  1.00 29.27 ? 185 LEU A CD1 1 
ATOM   1131 C  CD2 . LEU A 1 150 ? -12.213 -46.382 14.250  1.00 27.44 ? 185 LEU A CD2 1 
ATOM   1132 N  N   . ASP A 1 151 ? -14.894 -42.334 13.973  1.00 24.77 ? 186 ASP A N   1 
ATOM   1133 C  CA  . ASP A 1 151 ? -16.004 -42.110 13.055  1.00 29.98 ? 186 ASP A CA  1 
ATOM   1134 C  C   . ASP A 1 151 ? -16.006 -40.703 12.467  1.00 25.00 ? 186 ASP A C   1 
ATOM   1135 O  O   . ASP A 1 151 ? -16.524 -40.509 11.366  1.00 29.45 ? 186 ASP A O   1 
ATOM   1136 C  CB  . ASP A 1 151 ? -17.338 -42.428 13.737  1.00 28.02 ? 186 ASP A CB  1 
ATOM   1137 C  CG  . ASP A 1 151 ? -17.458 -43.897 14.117  1.00 53.94 ? 186 ASP A CG  1 
ATOM   1138 O  OD1 . ASP A 1 151 ? -16.734 -44.728 13.517  1.00 63.84 ? 186 ASP A OD1 1 
ATOM   1139 O  OD2 . ASP A 1 151 ? -18.278 -44.220 15.006  1.00 69.49 ? 186 ASP A OD2 1 
ATOM   1140 N  N   . LYS A 1 152 ? -15.407 -39.735 13.157  1.00 25.85 ? 187 LYS A N   1 
ATOM   1141 C  CA  . LYS A 1 152 ? -15.380 -38.347 12.716  1.00 25.31 ? 187 LYS A CA  1 
ATOM   1142 C  C   . LYS A 1 152 ? -14.149 -38.019 11.876  1.00 31.28 ? 187 LYS A C   1 
ATOM   1143 O  O   . LYS A 1 152 ? -14.092 -36.935 11.285  1.00 33.56 ? 187 LYS A O   1 
ATOM   1144 C  CB  . LYS A 1 152 ? -15.405 -37.445 13.954  1.00 33.73 ? 187 LYS A CB  1 
ATOM   1145 C  CG  . LYS A 1 152 ? -16.811 -37.063 14.402  1.00 37.99 ? 187 LYS A CG  1 
ATOM   1146 C  CD  . LYS A 1 152 ? -16.924 -37.011 15.923  1.00 51.65 ? 187 LYS A CD  1 
ATOM   1147 C  CE  . LYS A 1 152 ? -16.420 -35.714 16.519  1.00 43.96 ? 187 LYS A CE  1 
ATOM   1148 N  NZ  . LYS A 1 152 ? -16.743 -35.662 17.979  1.00 34.79 ? 187 LYS A NZ  1 
ATOM   1149 N  N   . ALA A 1 153 ? -13.186 -38.931 11.787  1.00 31.13 ? 188 ALA A N   1 
ATOM   1150 C  CA  . ALA A 1 153 ? -11.927 -38.629 11.118  1.00 30.68 ? 188 ALA A CA  1 
ATOM   1151 C  C   . ALA A 1 153 ? -12.171 -38.337 9.638   1.00 35.99 ? 188 ALA A C   1 
ATOM   1152 O  O   . ALA A 1 153 ? -12.930 -39.066 8.981   1.00 32.41 ? 188 ALA A O   1 
ATOM   1153 C  CB  . ALA A 1 153 ? -10.958 -39.797 11.276  1.00 28.22 ? 188 ALA A CB  1 
ATOM   1154 N  N   . PRO A 1 154 ? -11.549 -37.291 9.079   1.00 34.36 ? 189 PRO A N   1 
ATOM   1155 C  CA  . PRO A 1 154 ? -11.953 -36.836 7.736   1.00 36.46 ? 189 PRO A CA  1 
ATOM   1156 C  C   . PRO A 1 154 ? -11.526 -37.749 6.599   1.00 39.65 ? 189 PRO A C   1 
ATOM   1157 O  O   . PRO A 1 154 ? -12.291 -37.915 5.639   1.00 50.02 ? 189 PRO A O   1 
ATOM   1158 C  CB  . PRO A 1 154 ? -11.304 -35.447 7.627   1.00 48.99 ? 189 PRO A CB  1 
ATOM   1159 C  CG  . PRO A 1 154 ? -10.134 -35.526 8.543   1.00 37.86 ? 189 PRO A CG  1 
ATOM   1160 C  CD  . PRO A 1 154 ? -10.620 -36.344 9.714   1.00 33.68 ? 189 PRO A CD  1 
ATOM   1161 N  N   . ASP A 1 155 ? -10.326 -38.326 6.651   1.00 31.45 ? 190 ASP A N   1 
ATOM   1162 C  CA  . ASP A 1 155 ? -9.799  -39.077 5.519   1.00 38.02 ? 190 ASP A CA  1 
ATOM   1163 C  C   . ASP A 1 155 ? -9.235  -40.407 5.998   1.00 39.97 ? 190 ASP A C   1 
ATOM   1164 O  O   . ASP A 1 155 ? -9.229  -40.718 7.194   1.00 36.81 ? 190 ASP A O   1 
ATOM   1165 C  CB  . ASP A 1 155 ? -8.737  -38.271 4.764   1.00 36.74 ? 190 ASP A CB  1 
ATOM   1166 C  CG  . ASP A 1 155 ? -7.729  -37.615 5.698   1.00 69.22 ? 190 ASP A CG  1 
ATOM   1167 O  OD1 . ASP A 1 155 ? -7.231  -38.291 6.627   1.00 51.53 ? 190 ASP A OD1 1 
ATOM   1168 O  OD2 . ASP A 1 155 ? -7.420  -36.423 5.486   1.00 68.31 ? 190 ASP A OD2 1 
ATOM   1169 N  N   . ASP A 1 156 ? -8.734  -41.192 5.042   1.00 40.99 ? 191 ASP A N   1 
ATOM   1170 C  CA  . ASP A 1 156 ? -8.251  -42.528 5.373   1.00 46.52 ? 191 ASP A CA  1 
ATOM   1171 C  C   . ASP A 1 156 ? -6.927  -42.506 6.132   1.00 28.59 ? 191 ASP A C   1 
ATOM   1172 O  O   . ASP A 1 156 ? -6.671  -43.418 6.923   1.00 31.73 ? 191 ASP A O   1 
ATOM   1173 C  CB  . ASP A 1 156 ? -8.220  -43.420 4.134   1.00 39.75 ? 191 ASP A CB  1 
ATOM   1174 C  CG  . ASP A 1 156 ? -9.608  -43.862 3.711   1.00 51.93 ? 191 ASP A CG  1 
ATOM   1175 O  OD1 . ASP A 1 156 ? -10.590 -43.219 4.143   1.00 69.46 ? 191 ASP A OD1 1 
ATOM   1176 O  OD2 . ASP A 1 156 ? -9.719  -44.854 2.960   1.00 70.13 ? 191 ASP A OD2 1 
ATOM   1177 N  N   . GLU A 1 157 ? -6.082  -41.486 5.933   1.00 35.39 ? 192 GLU A N   1 
ATOM   1178 C  CA  . GLU A 1 157 ? -4.869  -41.371 6.749   1.00 35.34 ? 192 GLU A CA  1 
ATOM   1179 C  C   . GLU A 1 157 ? -5.204  -41.242 8.235   1.00 25.58 ? 192 GLU A C   1 
ATOM   1180 O  O   . GLU A 1 157 ? -4.667  -41.974 9.080   1.00 27.38 ? 192 GLU A O   1 
ATOM   1181 C  CB  . GLU A 1 157 ? -4.022  -40.178 6.290   1.00 35.63 ? 192 GLU A CB  1 
ATOM   1182 C  CG  . GLU A 1 157 ? -2.785  -39.921 7.181   1.00 42.39 ? 192 GLU A CG  1 
ATOM   1183 C  CD  . GLU A 1 157 ? -1.921  -38.750 6.711   1.00 60.75 ? 192 GLU A CD  1 
ATOM   1184 O  OE1 . GLU A 1 157 ? -2.310  -37.582 6.935   1.00 45.43 ? 192 GLU A OE1 1 
ATOM   1185 O  OE2 . GLU A 1 157 ? -0.840  -38.995 6.134   1.00 54.26 ? 192 GLU A OE2 1 
ATOM   1186 N  N   . SER A 1 158 ? -6.105  -40.317 8.577   1.00 29.48 ? 193 SER A N   1 
ATOM   1187 C  CA  . SER A 1 158 ? -6.467  -40.138 9.983   1.00 35.81 ? 193 SER A CA  1 
ATOM   1188 C  C   . SER A 1 158 ? -7.221  -41.349 10.535  1.00 23.54 ? 193 SER A C   1 
ATOM   1189 O  O   . SER A 1 158 ? -6.934  -41.809 11.652  1.00 22.83 ? 193 SER A O   1 
ATOM   1190 C  CB  . SER A 1 158 ? -7.248  -38.836 10.180  1.00 34.37 ? 193 SER A CB  1 
ATOM   1191 O  OG  . SER A 1 158 ? -8.371  -38.779 9.324   1.00 40.48 ? 193 SER A OG  1 
ATOM   1192 N  N   . LYS A 1 159 ? -8.186  -41.877 9.772   1.00 24.38 ? 194 LYS A N   1 
ATOM   1193 C  CA  . LYS A 1 159 ? -8.859  -43.100 10.204  1.00 23.44 ? 194 LYS A CA  1 
ATOM   1194 C  C   . LYS A 1 159 ? -7.848  -44.210 10.461  1.00 29.11 ? 194 LYS A C   1 
ATOM   1195 O  O   . LYS A 1 159 ? -7.970  -44.954 11.440  1.00 25.21 ? 194 LYS A O   1 
ATOM   1196 C  CB  . LYS A 1 159 ? -9.897  -43.544 9.173   1.00 25.51 ? 194 LYS A CB  1 
ATOM   1197 C  CG  . LYS A 1 159 ? -11.142 -42.683 9.160   1.00 27.51 ? 194 LYS A CG  1 
ATOM   1198 C  CD  . LYS A 1 159 ? -12.286 -43.322 8.377   1.00 46.80 ? 194 LYS A CD  1 
ATOM   1199 C  CE  . LYS A 1 159 ? -13.627 -42.689 8.747   1.00 55.52 ? 194 LYS A CE  1 
ATOM   1200 N  NZ  . LYS A 1 159 ? -14.349 -43.459 9.806   1.00 54.31 ? 194 LYS A NZ  1 
ATOM   1201 N  N   . GLY A 1 160 ? -6.834  -44.318 9.599   1.00 25.47 ? 195 GLY A N   1 
ATOM   1202 C  CA  . GLY A 1 160 ? -5.796  -45.314 9.798   1.00 23.36 ? 195 GLY A CA  1 
ATOM   1203 C  C   . GLY A 1 160 ? -5.005  -45.095 11.072  1.00 22.81 ? 195 GLY A C   1 
ATOM   1204 O  O   . GLY A 1 160 ? -4.593  -46.054 11.721  1.00 22.23 ? 195 GLY A O   1 
ATOM   1205 N  N   . PHE A 1 161 ? -4.778  -43.829 11.445  1.00 19.37 ? 196 PHE A N   1 
ATOM   1206 C  CA  . PHE A 1 161 ? -4.127  -43.538 12.725  1.00 21.47 ? 196 PHE A CA  1 
ATOM   1207 C  C   . PHE A 1 161 ? -4.955  -44.072 13.896  1.00 23.55 ? 196 PHE A C   1 
ATOM   1208 O  O   . PHE A 1 161 ? -4.428  -44.738 14.803  1.00 20.46 ? 196 PHE A O   1 
ATOM   1209 C  CB  . PHE A 1 161 ? -3.927  -42.026 12.878  1.00 23.24 ? 196 PHE A CB  1 
ATOM   1210 C  CG  . PHE A 1 161 ? -2.822  -41.459 12.021  1.00 23.57 ? 196 PHE A CG  1 
ATOM   1211 C  CD1 . PHE A 1 161 ? -2.196  -42.232 11.057  1.00 26.81 ? 196 PHE A CD1 1 
ATOM   1212 C  CD2 . PHE A 1 161 ? -2.468  -40.122 12.131  1.00 49.92 ? 196 PHE A CD2 1 
ATOM   1213 C  CE1 . PHE A 1 161 ? -1.199  -41.696 10.255  1.00 25.32 ? 196 PHE A CE1 1 
ATOM   1214 C  CE2 . PHE A 1 161 ? -1.478  -39.582 11.324  1.00 38.32 ? 196 PHE A CE2 1 
ATOM   1215 C  CZ  . PHE A 1 161 ? -0.846  -40.372 10.387  1.00 26.77 ? 196 PHE A CZ  1 
ATOM   1216 N  N   . PHE A 1 162 ? -6.261  -43.788 13.889  1.00 18.90 ? 197 PHE A N   1 
ATOM   1217 C  CA  . PHE A 1 162 ? -7.115  -44.297 14.964  1.00 17.42 ? 197 PHE A CA  1 
ATOM   1218 C  C   . PHE A 1 162 ? -7.143  -45.821 14.975  1.00 21.74 ? 197 PHE A C   1 
ATOM   1219 O  O   . PHE A 1 162 ? -6.993  -46.448 16.033  1.00 22.02 ? 197 PHE A O   1 
ATOM   1220 C  CB  . PHE A 1 162 ? -8.531  -43.731 14.868  1.00 19.91 ? 197 PHE A CB  1 
ATOM   1221 C  CG  . PHE A 1 162 ? -8.619  -42.275 15.177  1.00 19.46 ? 197 PHE A CG  1 
ATOM   1222 C  CD1 . PHE A 1 162 ? -8.674  -41.842 16.495  1.00 18.72 ? 197 PHE A CD1 1 
ATOM   1223 C  CD2 . PHE A 1 162 ? -8.661  -41.333 14.152  1.00 21.46 ? 197 PHE A CD2 1 
ATOM   1224 C  CE1 . PHE A 1 162 ? -8.760  -40.492 16.788  1.00 19.96 ? 197 PHE A CE1 1 
ATOM   1225 C  CE2 . PHE A 1 162 ? -8.738  -39.988 14.434  1.00 21.25 ? 197 PHE A CE2 1 
ATOM   1226 C  CZ  . PHE A 1 162 ? -8.796  -39.561 15.757  1.00 22.44 ? 197 PHE A CZ  1 
ATOM   1227 N  N   . LYS A 1 163 ? -7.328  -46.435 13.801  1.00 17.14 ? 198 LYS A N   1 
ATOM   1228 C  CA  . LYS A 1 163 ? -7.372  -47.891 13.724  1.00 18.29 ? 198 LYS A CA  1 
ATOM   1229 C  C   . LYS A 1 163 ? -6.064  -48.513 14.198  1.00 22.41 ? 198 LYS A C   1 
ATOM   1230 O  O   . LYS A 1 163 ? -6.074  -49.526 14.905  1.00 23.67 ? 198 LYS A O   1 
ATOM   1231 C  CB  . LYS A 1 163 ? -7.710  -48.350 12.306  1.00 27.19 ? 198 LYS A CB  1 
ATOM   1232 C  CG  . LYS A 1 163 ? -9.062  -47.881 11.797  1.00 30.94 ? 198 LYS A CG  1 
ATOM   1233 C  CD  . LYS A 1 163 ? -9.382  -48.507 10.440  1.00 32.19 ? 198 LYS A CD  1 
ATOM   1234 C  CE  . LYS A 1 163 ? -10.530 -47.774 9.746   1.00 48.37 ? 198 LYS A CE  1 
ATOM   1235 N  NZ  . LYS A 1 163 ? -10.643 -48.151 8.307   1.00 50.40 ? 198 LYS A NZ  1 
ATOM   1236 N  N   . GLY A 1 164 ? -4.929  -47.917 13.829  1.00 20.21 ? 199 GLY A N   1 
ATOM   1237 C  CA  . GLY A 1 164 ? -3.647  -48.459 14.247  1.00 22.16 ? 199 GLY A CA  1 
ATOM   1238 C  C   . GLY A 1 164 ? -3.436  -48.359 15.743  1.00 20.37 ? 199 GLY A C   1 
ATOM   1239 O  O   . GLY A 1 164 ? -2.963  -49.310 16.375  1.00 20.80 ? 199 GLY A O   1 
ATOM   1240 N  N   . ALA A 1 165 ? -3.799  -47.216 16.336  1.00 19.55 ? 200 ALA A N   1 
ATOM   1241 C  CA  . ALA A 1 165 ? -3.702  -47.088 17.788  1.00 19.83 ? 200 ALA A CA  1 
ATOM   1242 C  C   . ALA A 1 165 ? -4.585  -48.114 18.482  1.00 21.28 ? 200 ALA A C   1 
ATOM   1243 O  O   . ALA A 1 165 ? -4.171  -48.755 19.456  1.00 20.38 ? 200 ALA A O   1 
ATOM   1244 C  CB  . ALA A 1 165 ? -4.102  -45.676 18.219  1.00 17.18 ? 200 ALA A CB  1 
ATOM   1245 N  N   . MET A 1 166 ? -5.810  -48.286 17.989  1.00 17.41 ? 201 MET A N   1 
ATOM   1246 C  CA  . MET A 1 166 ? -6.736  -49.226 18.606  1.00 16.65 ? 201 MET A CA  1 
ATOM   1247 C  C   . MET A 1 166 ? -6.203  -50.652 18.510  1.00 20.86 ? 201 MET A C   1 
ATOM   1248 O  O   . MET A 1 166 ? -6.101  -51.362 19.519  1.00 22.29 ? 201 MET A O   1 
ATOM   1249 C  CB  . MET A 1 166 ? -8.062  -49.073 17.884  1.00 19.52 ? 201 MET A CB  1 
ATOM   1250 C  CG  . MET A 1 166 ? -8.751  -47.799 18.292  1.00 21.67 ? 201 MET A CG  1 
ATOM   1251 S  SD  . MET A 1 166 ? -10.252 -47.573 17.362  1.00 27.42 ? 201 MET A SD  1 
ATOM   1252 C  CE  . MET A 1 166 ? -10.823 -45.992 18.004  1.00 23.18 ? 201 MET A CE  1 
ATOM   1253 N  N   . ALA A 1 167 ? -5.787  -51.059 17.312  1.00 17.61 ? 202 ALA A N   1 
ATOM   1254 C  CA  . ALA A 1 167 ? -5.290  -52.413 17.117  1.00 22.61 ? 202 ALA A CA  1 
ATOM   1255 C  C   . ALA A 1 167 ? -4.024  -52.670 17.917  1.00 20.20 ? 202 ALA A C   1 
ATOM   1256 O  O   . ALA A 1 167 ? -3.783  -53.809 18.338  1.00 23.32 ? 202 ALA A O   1 
ATOM   1257 C  CB  . ALA A 1 167 ? -5.029  -52.671 15.632  1.00 24.85 ? 202 ALA A CB  1 
ATOM   1258 N  N   . SER A 1 168 ? -3.195  -51.638 18.124  1.00 18.54 ? 203 SER A N   1 
ATOM   1259 C  CA  . SER A 1 168 ? -1.928  -51.832 18.817  1.00 20.06 ? 203 SER A CA  1 
ATOM   1260 C  C   . SER A 1 168 ? -2.092  -51.826 20.329  1.00 19.84 ? 203 SER A C   1 
ATOM   1261 O  O   . SER A 1 168 ? -1.367  -52.546 21.026  1.00 23.33 ? 203 SER A O   1 
ATOM   1262 C  CB  . SER A 1 168 ? -0.937  -50.731 18.418  1.00 18.33 ? 203 SER A CB  1 
ATOM   1263 O  OG  . SER A 1 168 ? -0.693  -50.735 17.018  1.00 20.24 ? 203 SER A OG  1 
ATOM   1264 N  N   . LEU A 1 169 ? -3.021  -51.029 20.853  1.00 19.87 ? 204 LEU A N   1 
ATOM   1265 C  CA  . LEU A 1 169 ? -3.096  -50.810 22.288  1.00 16.63 ? 204 LEU A CA  1 
ATOM   1266 C  C   . LEU A 1 169 ? -4.218  -51.590 22.956  1.00 19.81 ? 204 LEU A C   1 
ATOM   1267 O  O   . LEU A 1 169 ? -4.046  -52.055 24.087  1.00 21.18 ? 204 LEU A O   1 
ATOM   1268 C  CB  . LEU A 1 169 ? -3.264  -49.320 22.583  1.00 26.55 ? 204 LEU A CB  1 
ATOM   1269 C  CG  . LEU A 1 169 ? -2.924  -48.906 24.012  1.00 41.07 ? 204 LEU A CG  1 
ATOM   1270 C  CD1 . LEU A 1 169 ? -1.503  -49.311 24.370  1.00 31.35 ? 204 LEU A CD1 1 
ATOM   1271 C  CD2 . LEU A 1 169 ? -3.153  -47.419 24.208  1.00 31.50 ? 204 LEU A CD2 1 
ATOM   1272 N  N   . ASN A 1 170 ? -5.360  -51.756 22.290  1.00 17.99 ? 205 ASN A N   1 
ATOM   1273 C  CA  . ASN A 1 170 ? -6.475  -52.453 22.919  1.00 22.38 ? 205 ASN A CA  1 
ATOM   1274 C  C   . ASN A 1 170 ? -6.168  -53.885 23.355  1.00 22.11 ? 205 ASN A C   1 
ATOM   1275 O  O   . ASN A 1 170 ? -6.772  -54.322 24.349  1.00 24.64 ? 205 ASN A O   1 
ATOM   1276 C  CB  . ASN A 1 170 ? -7.733  -52.351 22.040  1.00 24.60 ? 205 ASN A CB  1 
ATOM   1277 C  CG  . ASN A 1 170 ? -8.414  -51.000 22.175  1.00 29.39 ? 205 ASN A CG  1 
ATOM   1278 O  OD1 . ASN A 1 170 ? -8.231  -50.298 23.175  1.00 33.14 ? 205 ASN A OD1 1 
ATOM   1279 N  ND2 . ASN A 1 170 ? -9.193  -50.624 21.172  1.00 27.58 ? 205 ASN A ND2 1 
ATOM   1280 N  N   . PRO A 1 171 ? -5.294  -54.659 22.695  1.00 21.17 ? 206 PRO A N   1 
ATOM   1281 C  CA  . PRO A 1 171 ? -4.919  -55.957 23.286  1.00 26.39 ? 206 PRO A CA  1 
ATOM   1282 C  C   . PRO A 1 171 ? -4.244  -55.837 24.645  1.00 22.37 ? 206 PRO A C   1 
ATOM   1283 O  O   . PRO A 1 171 ? -4.433  -56.718 25.498  1.00 24.34 ? 206 PRO A O   1 
ATOM   1284 C  CB  . PRO A 1 171 ? -4.012  -56.593 22.225  1.00 24.32 ? 206 PRO A CB  1 
ATOM   1285 C  CG  . PRO A 1 171 ? -4.420  -55.931 20.943  1.00 23.84 ? 206 PRO A CG  1 
ATOM   1286 C  CD  . PRO A 1 171 ? -4.782  -54.522 21.317  1.00 20.75 ? 206 PRO A CD  1 
ATOM   1287 N  N   . TYR A 1 172 ? -3.460  -54.776 24.874  1.00 22.23 ? 207 TYR A N   1 
ATOM   1288 C  CA  . TYR A 1 172 ? -2.884  -54.566 26.199  1.00 21.21 ? 207 TYR A CA  1 
ATOM   1289 C  C   . TYR A 1 172 ? -3.942  -54.099 27.198  1.00 21.01 ? 207 TYR A C   1 
ATOM   1290 O  O   . TYR A 1 172 ? -3.940  -54.526 28.358  1.00 22.30 ? 207 TYR A O   1 
ATOM   1291 C  CB  . TYR A 1 172 ? -1.708  -53.588 26.121  1.00 19.43 ? 207 TYR A CB  1 
ATOM   1292 C  CG  . TYR A 1 172 ? -0.479  -54.166 25.435  1.00 21.13 ? 207 TYR A CG  1 
ATOM   1293 C  CD1 . TYR A 1 172 ? -0.376  -54.200 24.045  1.00 20.64 ? 207 TYR A CD1 1 
ATOM   1294 C  CD2 . TYR A 1 172 ? 0.576   -54.688 26.178  1.00 20.29 ? 207 TYR A CD2 1 
ATOM   1295 C  CE1 . TYR A 1 172 ? 0.746   -54.735 23.416  1.00 19.29 ? 207 TYR A CE1 1 
ATOM   1296 C  CE2 . TYR A 1 172 ? 1.706   -55.223 25.556  1.00 22.29 ? 207 TYR A CE2 1 
ATOM   1297 C  CZ  . TYR A 1 172 ? 1.787   -55.237 24.176  1.00 18.53 ? 207 TYR A CZ  1 
ATOM   1298 O  OH  . TYR A 1 172 ? 2.905   -55.766 23.560  1.00 24.07 ? 207 TYR A OH  1 
ATOM   1299 N  N   . VAL A 1 173 ? -4.839  -53.206 26.770  1.00 21.39 ? 208 VAL A N   1 
ATOM   1300 C  CA  . VAL A 1 173 ? -5.954  -52.796 27.622  1.00 21.55 ? 208 VAL A CA  1 
ATOM   1301 C  C   . VAL A 1 173 ? -6.758  -54.014 28.061  1.00 23.15 ? 208 VAL A C   1 
ATOM   1302 O  O   . VAL A 1 173 ? -7.085  -54.180 29.244  1.00 24.85 ? 208 VAL A O   1 
ATOM   1303 C  CB  . VAL A 1 173 ? -6.842  -51.774 26.886  1.00 23.74 ? 208 VAL A CB  1 
ATOM   1304 C  CG1 . VAL A 1 173 ? -8.097  -51.463 27.722  1.00 22.78 ? 208 VAL A CG1 1 
ATOM   1305 C  CG2 . VAL A 1 173 ? -6.063  -50.502 26.561  1.00 22.76 ? 208 VAL A CG2 1 
ATOM   1306 N  N   . LYS A 1 174 ? -7.085  -54.888 27.107  1.00 21.61 ? 209 LYS A N   1 
ATOM   1307 C  CA  . LYS A 1 174 ? -7.890  -56.065 27.407  1.00 28.52 ? 209 LYS A CA  1 
ATOM   1308 C  C   . LYS A 1 174 ? -7.192  -56.962 28.418  1.00 28.88 ? 209 LYS A C   1 
ATOM   1309 O  O   . LYS A 1 174 ? -7.840  -57.546 29.296  1.00 28.22 ? 209 LYS A O   1 
ATOM   1310 C  CB  . LYS A 1 174 ? -8.172  -56.835 26.118  1.00 29.69 ? 209 LYS A CB  1 
ATOM   1311 C  CG  . LYS A 1 174 ? -8.820  -58.199 26.325  1.00 38.27 ? 209 LYS A CG  1 
ATOM   1312 C  CD  . LYS A 1 174 ? -9.534  -58.656 25.056  1.00 53.98 ? 209 LYS A CD  1 
ATOM   1313 C  CE  . LYS A 1 174 ? -10.227 -60.000 25.238  1.00 46.60 ? 209 LYS A CE  1 
ATOM   1314 N  NZ  . LYS A 1 174 ? -10.005 -60.890 24.061  1.00 55.97 ? 209 LYS A NZ  1 
ATOM   1315 N  N   . ALA A 1 175 ? -5.867  -57.076 28.314  1.00 27.95 ? 210 ALA A N   1 
ATOM   1316 C  CA  . ALA A 1 175 ? -5.087  -57.907 29.218  1.00 28.54 ? 210 ALA A CA  1 
ATOM   1317 C  C   . ALA A 1 175 ? -4.827  -57.246 30.566  1.00 24.68 ? 210 ALA A C   1 
ATOM   1318 O  O   . ALA A 1 175 ? -4.124  -57.834 31.394  1.00 29.44 ? 210 ALA A O   1 
ATOM   1319 C  CB  . ALA A 1 175 ? -3.758  -58.298 28.558  1.00 25.15 ? 210 ALA A CB  1 
ATOM   1320 N  N   . GLY A 1 176 ? -5.370  -56.051 30.809  1.00 23.89 ? 211 GLY A N   1 
ATOM   1321 C  CA  . GLY A 1 176 ? -5.092  -55.358 32.054  1.00 25.98 ? 211 GLY A CA  1 
ATOM   1322 C  C   . GLY A 1 176 ? -3.695  -54.791 32.155  1.00 30.17 ? 211 GLY A C   1 
ATOM   1323 O  O   . GLY A 1 176 ? -3.192  -54.592 33.263  1.00 27.27 ? 211 GLY A O   1 
ATOM   1324 N  N   . LYS A 1 177 ? -3.053  -54.521 31.021  1.00 22.17 ? 212 LYS A N   1 
ATOM   1325 C  CA  . LYS A 1 177 ? -1.648  -54.138 30.991  1.00 21.71 ? 212 LYS A CA  1 
ATOM   1326 C  C   . LYS A 1 177 ? -1.430  -52.724 30.467  1.00 24.17 ? 212 LYS A C   1 
ATOM   1327 O  O   . LYS A 1 177 ? -0.301  -52.374 30.106  1.00 24.72 ? 212 LYS A O   1 
ATOM   1328 C  CB  . LYS A 1 177 ? -0.849  -55.179 30.200  1.00 25.49 ? 212 LYS A CB  1 
ATOM   1329 C  CG  . LYS A 1 177 ? -0.424  -56.366 31.063  1.00 28.58 ? 212 LYS A CG  1 
ATOM   1330 C  CD  . LYS A 1 177 ? -0.524  -57.658 30.280  1.00 44.75 ? 212 LYS A CD  1 
ATOM   1331 C  CE  . LYS A 1 177 ? 0.674   -58.546 30.501  1.00 40.21 ? 212 LYS A CE  1 
ATOM   1332 N  NZ  . LYS A 1 177 ? 0.686   -59.641 29.492  1.00 55.19 ? 212 LYS A NZ  1 
ATOM   1333 N  N   . PHE A 1 178 ? -2.473  -51.899 30.419  1.00 22.24 ? 213 PHE A N   1 
ATOM   1334 C  CA  . PHE A 1 178 ? -2.328  -50.486 30.101  1.00 21.67 ? 213 PHE A CA  1 
ATOM   1335 C  C   . PHE A 1 178 ? -2.615  -49.674 31.355  1.00 22.20 ? 213 PHE A C   1 
ATOM   1336 O  O   . PHE A 1 178 ? -3.698  -49.785 31.939  1.00 22.14 ? 213 PHE A O   1 
ATOM   1337 C  CB  . PHE A 1 178 ? -3.257  -50.052 28.971  1.00 21.16 ? 213 PHE A CB  1 
ATOM   1338 C  CG  . PHE A 1 178 ? -3.174  -48.585 28.679  1.00 21.41 ? 213 PHE A CG  1 
ATOM   1339 C  CD1 . PHE A 1 178 ? -2.004  -48.036 28.173  1.00 21.01 ? 213 PHE A CD1 1 
ATOM   1340 C  CD2 . PHE A 1 178 ? -4.239  -47.740 28.959  1.00 24.36 ? 213 PHE A CD2 1 
ATOM   1341 C  CE1 . PHE A 1 178 ? -1.908  -46.675 27.922  1.00 23.65 ? 213 PHE A CE1 1 
ATOM   1342 C  CE2 . PHE A 1 178 ? -4.151  -46.377 28.705  1.00 22.71 ? 213 PHE A CE2 1 
ATOM   1343 C  CZ  . PHE A 1 178 ? -2.988  -45.840 28.193  1.00 18.10 ? 213 PHE A CZ  1 
ATOM   1344 N  N   . LYS A 1 179 ? -1.648  -48.858 31.763  1.00 21.39 ? 214 LYS A N   1 
ATOM   1345 C  CA  . LYS A 1 179 ? -1.771  -48.057 32.979  1.00 19.64 ? 214 LYS A CA  1 
ATOM   1346 C  C   . LYS A 1 179 ? -1.466  -46.612 32.618  1.00 24.06 ? 214 LYS A C   1 
ATOM   1347 O  O   . LYS A 1 179 ? -0.289  -46.235 32.473  1.00 18.67 ? 214 LYS A O   1 
ATOM   1348 C  CB  . LYS A 1 179 ? -0.837  -48.570 34.069  1.00 24.62 ? 214 LYS A CB  1 
ATOM   1349 C  CG  . LYS A 1 179 ? -0.993  -47.838 35.395  1.00 33.51 ? 214 LYS A CG  1 
ATOM   1350 C  CD  . LYS A 1 179 ? 0.062   -48.278 36.399  1.00 39.73 ? 214 LYS A CD  1 
ATOM   1351 C  CE  . LYS A 1 179 ? -0.301  -47.845 37.817  1.00 51.61 ? 214 LYS A CE  1 
ATOM   1352 N  NZ  . LYS A 1 179 ? 0.865   -47.256 38.540  1.00 56.31 ? 214 LYS A NZ  1 
ATOM   1353 N  N   . PRO A 1 180 ? -2.485  -45.783 32.424  1.00 19.24 ? 215 PRO A N   1 
ATOM   1354 C  CA  . PRO A 1 180 ? -2.232  -44.390 32.050  1.00 17.08 ? 215 PRO A CA  1 
ATOM   1355 C  C   . PRO A 1 180 ? -1.667  -43.601 33.225  1.00 22.62 ? 215 PRO A C   1 
ATOM   1356 O  O   . PRO A 1 180 ? -1.771  -43.995 34.387  1.00 22.07 ? 215 PRO A O   1 
ATOM   1357 C  CB  . PRO A 1 180 ? -3.624  -43.877 31.660  1.00 18.30 ? 215 PRO A CB  1 
ATOM   1358 C  CG  . PRO A 1 180 ? -4.573  -44.725 32.460  1.00 23.30 ? 215 PRO A CG  1 
ATOM   1359 C  CD  . PRO A 1 180 ? -3.926  -46.094 32.490  1.00 21.34 ? 215 PRO A CD  1 
ATOM   1360 N  N   . PHE A 1 181 ? -1.035  -42.477 32.900  1.00 17.43 ? 216 PHE A N   1 
ATOM   1361 C  CA  . PHE A 1 181 ? -0.702  -41.451 33.881  1.00 20.08 ? 216 PHE A CA  1 
ATOM   1362 C  C   . PHE A 1 181 ? -1.331  -40.146 33.413  1.00 20.68 ? 216 PHE A C   1 
ATOM   1363 O  O   . PHE A 1 181 ? -1.871  -40.057 32.307  1.00 19.93 ? 216 PHE A O   1 
ATOM   1364 C  CB  . PHE A 1 181 ? 0.821   -41.304 34.050  1.00 20.02 ? 216 PHE A CB  1 
ATOM   1365 C  CG  . PHE A 1 181 ? 1.553   -41.109 32.756  1.00 18.38 ? 216 PHE A CG  1 
ATOM   1366 C  CD1 . PHE A 1 181 ? 1.589   -39.863 32.142  1.00 20.00 ? 216 PHE A CD1 1 
ATOM   1367 C  CD2 . PHE A 1 181 ? 2.181   -42.175 32.134  1.00 19.82 ? 216 PHE A CD2 1 
ATOM   1368 C  CE1 . PHE A 1 181 ? 2.237   -39.688 30.945  1.00 20.43 ? 216 PHE A CE1 1 
ATOM   1369 C  CE2 . PHE A 1 181 ? 2.839   -42.002 30.937  1.00 19.89 ? 216 PHE A CE2 1 
ATOM   1370 C  CZ  . PHE A 1 181 ? 2.876   -40.760 30.338  1.00 18.97 ? 216 PHE A CZ  1 
ATOM   1371 N  N   . SER A 1 182 ? -1.275  -39.118 34.256  1.00 19.63 ? 217 SER A N   1 
ATOM   1372 C  CA  . SER A 1 182 ? -1.861  -37.831 33.901  1.00 20.95 ? 217 SER A CA  1 
ATOM   1373 C  C   . SER A 1 182 ? -0.875  -36.716 34.207  1.00 24.86 ? 217 SER A C   1 
ATOM   1374 O  O   . SER A 1 182 ? -0.577  -36.460 35.378  1.00 27.54 ? 217 SER A O   1 
ATOM   1375 C  CB  . SER A 1 182 ? -3.168  -37.597 34.657  1.00 22.44 ? 217 SER A CB  1 
ATOM   1376 O  OG  . SER A 1 182 ? -3.659  -36.294 34.398  1.00 28.72 ? 217 SER A OG  1 
ATOM   1377 N  N   . GLY A 1 183 ? -0.402  -36.034 33.160  1.00 20.21 ? 218 GLY A N   1 
ATOM   1378 C  CA  . GLY A 1 183 ? 0.501   -34.913 33.341  1.00 26.25 ? 218 GLY A CA  1 
ATOM   1379 C  C   . GLY A 1 183 ? 1.859   -35.384 33.838  1.00 28.28 ? 218 GLY A C   1 
ATOM   1380 O  O   . GLY A 1 183 ? 2.221   -36.562 33.733  1.00 27.41 ? 218 GLY A O   1 
ATOM   1381 N  N   . ASN A 1 184 ? 2.617   -34.441 34.399  1.00 24.20 ? 219 ASN A N   1 
ATOM   1382 C  CA  . ASN A 1 184 ? 3.926   -34.780 34.941  1.00 22.05 ? 219 ASN A CA  1 
ATOM   1383 C  C   . ASN A 1 184 ? 3.772   -35.846 36.017  1.00 26.50 ? 219 ASN A C   1 
ATOM   1384 O  O   . ASN A 1 184 ? 2.965   -35.699 36.938  1.00 25.78 ? 219 ASN A O   1 
ATOM   1385 C  CB  . ASN A 1 184 ? 4.593   -33.549 35.553  1.00 22.90 ? 219 ASN A CB  1 
ATOM   1386 C  CG  . ASN A 1 184 ? 4.869   -32.459 34.536  1.00 27.22 ? 219 ASN A CG  1 
ATOM   1387 O  OD1 . ASN A 1 184 ? 4.769   -32.669 33.320  1.00 25.37 ? 219 ASN A OD1 1 
ATOM   1388 N  ND2 . ASN A 1 184 ? 5.268   -31.289 35.032  1.00 26.73 ? 219 ASN A ND2 1 
ATOM   1389 N  N   . THR A 1 185 ? 4.560   -36.914 35.903  1.00 22.46 ? 220 THR A N   1 
ATOM   1390 C  CA  . THR A 1 185 ? 4.417   -38.068 36.784  1.00 22.22 ? 220 THR A CA  1 
ATOM   1391 C  C   . THR A 1 185 ? 5.765   -38.751 36.927  1.00 23.26 ? 220 THR A C   1 
ATOM   1392 O  O   . THR A 1 185 ? 6.411   -39.058 35.921  1.00 24.63 ? 220 THR A O   1 
ATOM   1393 C  CB  . THR A 1 185 ? 3.415   -39.075 36.191  1.00 24.25 ? 220 THR A CB  1 
ATOM   1394 O  OG1 . THR A 1 185 ? 2.155   -38.433 35.967  1.00 26.86 ? 220 THR A OG1 1 
ATOM   1395 C  CG2 . THR A 1 185 ? 3.217   -40.272 37.122  1.00 27.82 ? 220 THR A CG2 1 
ATOM   1396 N  N   . ASP A 1 186 ? 6.170   -39.004 38.167  1.00 22.06 ? 221 ASP A N   1 
ATOM   1397 C  CA  . ASP A 1 186 ? 7.277   -39.915 38.410  1.00 25.98 ? 221 ASP A CA  1 
ATOM   1398 C  C   . ASP A 1 186 ? 6.829   -41.331 38.066  1.00 26.12 ? 221 ASP A C   1 
ATOM   1399 O  O   . ASP A 1 186 ? 5.876   -41.858 38.649  1.00 29.49 ? 221 ASP A O   1 
ATOM   1400 C  CB  . ASP A 1 186 ? 7.738   -39.819 39.862  1.00 25.95 ? 221 ASP A CB  1 
ATOM   1401 C  CG  . ASP A 1 186 ? 8.545   -38.558 40.132  1.00 35.16 ? 221 ASP A CG  1 
ATOM   1402 O  OD1 . ASP A 1 186 ? 8.570   -37.663 39.258  1.00 40.27 ? 221 ASP A OD1 1 
ATOM   1403 O  OD2 . ASP A 1 186 ? 9.163   -38.464 41.214  1.00 54.45 ? 221 ASP A OD2 1 
ATOM   1404 N  N   . LEU A 1 187 ? 7.475   -41.914 37.071  1.00 23.51 ? 222 LEU A N   1 
ATOM   1405 C  CA  . LEU A 1 187 ? 7.322   -43.322 36.741  1.00 22.22 ? 222 LEU A CA  1 
ATOM   1406 C  C   . LEU A 1 187 ? 8.421   -44.018 37.528  1.00 42.27 ? 222 LEU A C   1 
ATOM   1407 O  O   . LEU A 1 187 ? 8.786   -43.534 38.606  1.00 74.78 ? 222 LEU A O   1 
ATOM   1408 C  CB  . LEU A 1 187 ? 7.397   -43.526 35.228  1.00 20.62 ? 222 LEU A CB  1 
ATOM   1409 C  CG  . LEU A 1 187 ? 6.442   -42.576 34.493  1.00 22.57 ? 222 LEU A CG  1 
ATOM   1410 C  CD1 . LEU A 1 187 ? 6.693   -42.555 32.982  1.00 26.75 ? 222 LEU A CD1 1 
ATOM   1411 C  CD2 . LEU A 1 187 ? 4.989   -42.922 34.803  1.00 29.65 ? 222 LEU A CD2 1 
ATOM   1412 N  N   . VAL A 1 188 ? 8.887   -45.176 37.076  1.00 31.70 ? 223 VAL A N   1 
ATOM   1413 C  CA  . VAL A 1 188 ? 9.960   -45.903 37.762  1.00 25.87 ? 223 VAL A CA  1 
ATOM   1414 C  C   . VAL A 1 188 ? 11.070  -44.957 38.224  1.00 31.26 ? 223 VAL A C   1 
ATOM   1415 O  O   . VAL A 1 188 ? 11.292  -43.903 37.604  1.00 28.04 ? 223 VAL A O   1 
ATOM   1416 C  CB  . VAL A 1 188 ? 10.538  -47.010 36.862  1.00 36.73 ? 223 VAL A CB  1 
ATOM   1417 C  CG1 . VAL A 1 188 ? 9.475   -48.059 36.542  1.00 37.27 ? 223 VAL A CG1 1 
ATOM   1418 C  CG2 . VAL A 1 188 ? 11.141  -46.420 35.594  1.00 31.00 ? 223 VAL A CG2 1 
ATOM   1419 N  N   . PRO A 1 189 ? 11.769  -45.266 39.319  1.00 30.25 ? 224 PRO A N   1 
ATOM   1420 C  CA  . PRO A 1 189 ? 12.864  -44.388 39.755  1.00 27.40 ? 224 PRO A CA  1 
ATOM   1421 C  C   . PRO A 1 189 ? 13.861  -44.139 38.632  1.00 29.75 ? 224 PRO A C   1 
ATOM   1422 O  O   . PRO A 1 189 ? 14.392  -45.083 38.036  1.00 27.64 ? 224 PRO A O   1 
ATOM   1423 C  CB  . PRO A 1 189 ? 13.492  -45.158 40.925  1.00 31.02 ? 224 PRO A CB  1 
ATOM   1424 C  CG  . PRO A 1 189 ? 12.356  -45.981 41.471  1.00 29.05 ? 224 PRO A CG  1 
ATOM   1425 C  CD  . PRO A 1 189 ? 11.533  -46.370 40.267  1.00 26.53 ? 224 PRO A CD  1 
ATOM   1426 N  N   . GLY A 1 190 ? 14.098  -42.867 38.322  1.00 24.43 ? 225 GLY A N   1 
ATOM   1427 C  CA  . GLY A 1 190 ? 15.003  -42.494 37.260  1.00 28.11 ? 225 GLY A CA  1 
ATOM   1428 C  C   . GLY A 1 190 ? 14.338  -42.052 35.973  1.00 25.76 ? 225 GLY A C   1 
ATOM   1429 O  O   . GLY A 1 190 ? 15.027  -41.495 35.107  1.00 22.99 ? 225 GLY A O   1 
ATOM   1430 N  N   . ILE A 1 191 ? 13.029  -42.278 35.810  1.00 20.42 ? 226 ILE A N   1 
ATOM   1431 C  CA  . ILE A 1 191 ? 12.307  -41.862 34.616  1.00 21.54 ? 226 ILE A CA  1 
ATOM   1432 C  C   . ILE A 1 191 ? 11.048  -41.119 35.027  1.00 25.33 ? 226 ILE A C   1 
ATOM   1433 O  O   . ILE A 1 191 ? 10.253  -41.630 35.825  1.00 25.66 ? 226 ILE A O   1 
ATOM   1434 C  CB  . ILE A 1 191 ? 11.955  -43.039 33.689  1.00 18.56 ? 226 ILE A CB  1 
ATOM   1435 C  CG1 . ILE A 1 191 ? 13.193  -43.904 33.405  1.00 29.27 ? 226 ILE A CG1 1 
ATOM   1436 C  CG2 . ILE A 1 191 ? 11.330  -42.507 32.400  1.00 20.02 ? 226 ILE A CG2 1 
ATOM   1437 C  CD1 . ILE A 1 191 ? 12.901  -45.127 32.560  1.00 24.82 ? 226 ILE A CD1 1 
ATOM   1438 N  N   . LYS A 1 192 ? 10.863  -39.929 34.465  1.00 21.84 ? 227 LYS A N   1 
ATOM   1439 C  CA  . LYS A 1 192 ? 9.707   -39.085 34.733  1.00 22.02 ? 227 LYS A CA  1 
ATOM   1440 C  C   . LYS A 1 192 ? 8.964   -38.818 33.434  1.00 21.77 ? 227 LYS A C   1 
ATOM   1441 O  O   . LYS A 1 192 ? 9.580   -38.677 32.369  1.00 20.24 ? 227 LYS A O   1 
ATOM   1442 C  CB  . LYS A 1 192 ? 10.152  -37.734 35.299  1.00 22.37 ? 227 LYS A CB  1 
ATOM   1443 C  CG  . LYS A 1 192 ? 10.810  -37.843 36.657  1.00 39.83 ? 227 LYS A CG  1 
ATOM   1444 C  CD  . LYS A 1 192 ? 11.154  -36.480 37.239  1.00 37.77 ? 227 LYS A CD  1 
ATOM   1445 C  CE  . LYS A 1 192 ? 11.617  -36.632 38.689  1.00 49.71 ? 227 LYS A CE  1 
ATOM   1446 N  NZ  . LYS A 1 192 ? 11.202  -35.485 39.546  1.00 58.25 ? 227 LYS A NZ  1 
ATOM   1447 N  N   . ALA A 1 193 ? 7.642   -38.750 33.520  1.00 19.80 ? 228 ALA A N   1 
ATOM   1448 C  CA  . ALA A 1 193 ? 6.834   -38.232 32.423  1.00 20.34 ? 228 ALA A CA  1 
ATOM   1449 C  C   . ALA A 1 193 ? 6.742   -36.713 32.551  1.00 23.88 ? 228 ALA A C   1 
ATOM   1450 O  O   . ALA A 1 193 ? 6.478   -36.193 33.637  1.00 21.39 ? 228 ALA A O   1 
ATOM   1451 C  CB  . ALA A 1 193 ? 5.430   -38.839 32.453  1.00 20.61 ? 228 ALA A CB  1 
ATOM   1452 N  N   . LEU A 1 194 ? 6.973   -36.009 31.446  1.00 18.57 ? 229 LEU A N   1 
ATOM   1453 C  CA  . LEU A 1 194 ? 6.849   -34.560 31.356  1.00 19.43 ? 229 LEU A CA  1 
ATOM   1454 C  C   . LEU A 1 194 ? 5.848   -34.251 30.253  1.00 18.36 ? 229 LEU A C   1 
ATOM   1455 O  O   . LEU A 1 194 ? 6.109   -34.543 29.083  1.00 19.62 ? 229 LEU A O   1 
ATOM   1456 C  CB  . LEU A 1 194 ? 8.200   -33.944 30.976  1.00 23.86 ? 229 LEU A CB  1 
ATOM   1457 C  CG  . LEU A 1 194 ? 8.354   -32.428 31.106  1.00 26.19 ? 229 LEU A CG  1 
ATOM   1458 C  CD1 . LEU A 1 194 ? 8.192   -31.946 32.544  1.00 29.01 ? 229 LEU A CD1 1 
ATOM   1459 C  CD2 . LEU A 1 194 ? 9.671   -31.953 30.488  1.00 29.78 ? 229 LEU A CD2 1 
ATOM   1460 N  N   . ALA A 1 195 ? 4.721   -33.640 30.608  1.00 20.22 ? 230 ALA A N   1 
ATOM   1461 C  CA  . ALA A 1 195 ? 3.728   -33.327 29.588  1.00 21.36 ? 230 ALA A CA  1 
ATOM   1462 C  C   . ALA A 1 195 ? 4.314   -32.370 28.558  1.00 20.15 ? 230 ALA A C   1 
ATOM   1463 O  O   . ALA A 1 195 ? 4.893   -31.335 28.906  1.00 21.98 ? 230 ALA A O   1 
ATOM   1464 C  CB  . ALA A 1 195 ? 2.484   -32.715 30.229  1.00 21.00 ? 230 ALA A CB  1 
ATOM   1465 N  N   . SER A 1 196 ? 4.191   -32.742 27.288  1.00 19.86 ? 231 SER A N   1 
ATOM   1466 C  CA  . SER A 1 196 ? 4.625   -31.912 26.167  1.00 21.73 ? 231 SER A CA  1 
ATOM   1467 C  C   . SER A 1 196 ? 3.549   -31.935 25.089  1.00 18.01 ? 231 SER A C   1 
ATOM   1468 O  O   . SER A 1 196 ? 3.813   -32.216 23.919  1.00 19.46 ? 231 SER A O   1 
ATOM   1469 C  CB  . SER A 1 196 ? 6.002   -32.319 25.633  1.00 19.29 ? 231 SER A CB  1 
ATOM   1470 O  OG  . SER A 1 196 ? 6.063   -33.711 25.367  1.00 21.40 ? 231 SER A OG  1 
ATOM   1471 N  N   . HIS A 1 197 ? 2.307   -31.677 25.494  1.00 18.59 ? 232 HIS A N   1 
ATOM   1472 C  CA  . HIS A 1 197 ? 1.163   -31.854 24.610  1.00 18.07 ? 232 HIS A CA  1 
ATOM   1473 C  C   . HIS A 1 197 ? 1.205   -30.889 23.425  1.00 26.56 ? 232 HIS A C   1 
ATOM   1474 O  O   . HIS A 1 197 ? 1.670   -29.749 23.526  1.00 23.31 ? 232 HIS A O   1 
ATOM   1475 C  CB  . HIS A 1 197 ? -0.144  -31.629 25.376  1.00 16.73 ? 232 HIS A CB  1 
ATOM   1476 C  CG  . HIS A 1 197 ? -0.278  -32.442 26.629  1.00 25.55 ? 232 HIS A CG  1 
ATOM   1477 N  ND1 . HIS A 1 197 ? 0.451   -33.590 26.865  1.00 25.12 ? 232 HIS A ND1 1 
ATOM   1478 C  CD2 . HIS A 1 197 ? -1.075  -32.273 27.712  1.00 22.10 ? 232 HIS A CD2 1 
ATOM   1479 C  CE1 . HIS A 1 197 ? 0.110   -34.090 28.043  1.00 18.88 ? 232 HIS A CE1 1 
ATOM   1480 N  NE2 . HIS A 1 197 ? -0.812  -33.308 28.578  1.00 21.99 ? 232 HIS A NE2 1 
ATOM   1481 N  N   . GLY A 1 198 ? 0.660   -31.349 22.303  1.00 20.58 ? 233 GLY A N   1 
ATOM   1482 C  CA  . GLY A 1 198 ? 0.401   -30.500 21.156  1.00 21.69 ? 233 GLY A CA  1 
ATOM   1483 C  C   . GLY A 1 198 ? 0.653   -31.157 19.814  1.00 23.30 ? 233 GLY A C   1 
ATOM   1484 O  O   . GLY A 1 198 ? -0.166  -30.998 18.907  1.00 24.90 ? 233 GLY A O   1 
ATOM   1485 N  N   . HIS A 1 199 ? 1.709   -31.963 19.685  1.00 17.50 ? 234 HIS A N   1 
ATOM   1486 C  CA  . HIS A 1 199 ? 1.824   -32.809 18.504  1.00 19.16 ? 234 HIS A CA  1 
ATOM   1487 C  C   . HIS A 1 199 ? 0.651   -33.775 18.451  1.00 21.71 ? 234 HIS A C   1 
ATOM   1488 O  O   . HIS A 1 199 ? 0.062   -34.006 17.387  1.00 19.03 ? 234 HIS A O   1 
ATOM   1489 C  CB  . HIS A 1 199 ? 3.151   -33.567 18.549  1.00 19.78 ? 234 HIS A CB  1 
ATOM   1490 C  CG  . HIS A 1 199 ? 3.351   -34.522 17.414  1.00 19.78 ? 234 HIS A CG  1 
ATOM   1491 N  ND1 . HIS A 1 199 ? 3.475   -34.109 16.104  1.00 19.22 ? 234 HIS A ND1 1 
ATOM   1492 C  CD2 . HIS A 1 199 ? 3.434   -35.875 17.393  1.00 14.51 ? 234 HIS A CD2 1 
ATOM   1493 C  CE1 . HIS A 1 199 ? 3.640   -35.163 15.326  1.00 19.91 ? 234 HIS A CE1 1 
ATOM   1494 N  NE2 . HIS A 1 199 ? 3.623   -36.245 16.083  1.00 16.71 ? 234 HIS A NE2 1 
ATOM   1495 N  N   . THR A 1 200 ? 0.298   -34.329 19.597  1.00 17.29 ? 235 THR A N   1 
ATOM   1496 C  CA  . THR A 1 200 ? -0.937  -35.043 19.874  1.00 19.09 ? 235 THR A CA  1 
ATOM   1497 C  C   . THR A 1 200 ? -1.466  -34.536 21.207  1.00 19.70 ? 235 THR A C   1 
ATOM   1498 O  O   . THR A 1 200 ? -0.729  -33.913 21.983  1.00 18.83 ? 235 THR A O   1 
ATOM   1499 C  CB  . THR A 1 200 ? -0.684  -36.554 19.974  1.00 18.62 ? 235 THR A CB  1 
ATOM   1500 O  OG1 . THR A 1 200 ? 0.253   -36.797 21.030  1.00 19.45 ? 235 THR A OG1 1 
ATOM   1501 C  CG2 . THR A 1 200 ? -0.160  -37.125 18.658  1.00 15.82 ? 235 THR A CG2 1 
ATOM   1502 N  N   . PRO A 1 201 ? -2.741  -34.784 21.506  1.00 19.14 ? 236 PRO A N   1 
ATOM   1503 C  CA  . PRO A 1 201 ? -3.325  -34.231 22.743  1.00 17.07 ? 236 PRO A CA  1 
ATOM   1504 C  C   . PRO A 1 201 ? -2.627  -34.659 24.024  1.00 16.86 ? 236 PRO A C   1 
ATOM   1505 O  O   . PRO A 1 201 ? -2.690  -33.921 25.019  1.00 20.85 ? 236 PRO A O   1 
ATOM   1506 C  CB  . PRO A 1 201 ? -4.788  -34.696 22.684  1.00 23.07 ? 236 PRO A CB  1 
ATOM   1507 C  CG  . PRO A 1 201 ? -5.049  -34.843 21.210  1.00 19.41 ? 236 PRO A CG  1 
ATOM   1508 C  CD  . PRO A 1 201 ? -3.768  -35.392 20.642  1.00 17.41 ? 236 PRO A CD  1 
ATOM   1509 N  N   . GLY A 1 202 ? -1.962  -35.815 24.035  1.00 17.27 ? 237 GLY A N   1 
ATOM   1510 C  CA  . GLY A 1 202 ? -1.274  -36.281 25.225  1.00 16.29 ? 237 GLY A CA  1 
ATOM   1511 C  C   . GLY A 1 202 ? 0.198   -36.578 25.013  1.00 16.63 ? 237 GLY A C   1 
ATOM   1512 O  O   . GLY A 1 202 ? 0.776   -37.405 25.727  1.00 18.46 ? 237 GLY A O   1 
ATOM   1513 N  N   . HIS A 1 203 ? 0.815   -35.922 24.030  1.00 16.18 ? 238 HIS A N   1 
ATOM   1514 C  CA  . HIS A 1 203 ? 2.227   -36.150 23.764  1.00 16.30 ? 238 HIS A CA  1 
ATOM   1515 C  C   . HIS A 1 203 ? 3.055   -35.887 25.013  1.00 17.58 ? 238 HIS A C   1 
ATOM   1516 O  O   . HIS A 1 203 ? 2.914   -34.844 25.661  1.00 17.73 ? 238 HIS A O   1 
ATOM   1517 C  CB  . HIS A 1 203 ? 2.705   -35.245 22.636  1.00 18.79 ? 238 HIS A CB  1 
ATOM   1518 C  CG  . HIS A 1 203 ? 4.105   -35.540 22.201  1.00 19.19 ? 238 HIS A CG  1 
ATOM   1519 N  ND1 . HIS A 1 203 ? 5.207   -35.030 22.854  1.00 18.84 ? 238 HIS A ND1 1 
ATOM   1520 C  CD2 . HIS A 1 203 ? 4.585   -36.307 21.192  1.00 17.24 ? 238 HIS A CD2 1 
ATOM   1521 C  CE1 . HIS A 1 203 ? 6.308   -35.462 22.259  1.00 17.64 ? 238 HIS A CE1 1 
ATOM   1522 N  NE2 . HIS A 1 203 ? 5.958   -36.244 21.254  1.00 16.29 ? 238 HIS A NE2 1 
ATOM   1523 N  N   . THR A 1 204 ? 3.946   -36.827 25.321  1.00 16.16 ? 239 THR A N   1 
ATOM   1524 C  CA  . THR A 1 204 ? 4.686   -36.832 26.575  1.00 13.99 ? 239 THR A CA  1 
ATOM   1525 C  C   . THR A 1 204 ? 6.167   -37.044 26.296  1.00 17.36 ? 239 THR A C   1 
ATOM   1526 O  O   . THR A 1 204 ? 6.539   -37.921 25.507  1.00 16.80 ? 239 THR A O   1 
ATOM   1527 C  CB  . THR A 1 204 ? 4.167   -37.962 27.461  1.00 18.82 ? 239 THR A CB  1 
ATOM   1528 O  OG1 . THR A 1 204 ? 2.800   -37.704 27.803  1.00 19.05 ? 239 THR A OG1 1 
ATOM   1529 C  CG2 . THR A 1 204 ? 5.021   -38.080 28.748  1.00 17.85 ? 239 THR A CG2 1 
ATOM   1530 N  N   . THR A 1 205 ? 7.002   -36.231 26.940  1.00 16.17 ? 240 THR A N   1 
ATOM   1531 C  CA  . THR A 1 205 ? 8.448   -36.377 26.958  1.00 17.54 ? 240 THR A CA  1 
ATOM   1532 C  C   . THR A 1 205 ? 8.823   -37.237 28.160  1.00 16.78 ? 240 THR A C   1 
ATOM   1533 O  O   . THR A 1 205 ? 8.193   -37.152 29.212  1.00 19.04 ? 240 THR A O   1 
ATOM   1534 C  CB  . THR A 1 205 ? 9.050   -34.977 27.132  1.00 17.91 ? 240 THR A CB  1 
ATOM   1535 O  OG1 . THR A 1 205 ? 8.830   -34.213 25.938  1.00 18.62 ? 240 THR A OG1 1 
ATOM   1536 C  CG2 . THR A 1 205 ? 10.549  -35.032 27.448  1.00 16.17 ? 240 THR A CG2 1 
ATOM   1537 N  N   . TYR A 1 206 ? 9.856   -38.062 28.016  1.00 16.55 ? 241 TYR A N   1 
ATOM   1538 C  CA  . TYR A 1 206 ? 10.317  -38.880 29.133  1.00 16.06 ? 241 TYR A CA  1 
ATOM   1539 C  C   . TYR A 1 206 ? 11.723  -38.467 29.519  1.00 18.32 ? 241 TYR A C   1 
ATOM   1540 O  O   . TYR A 1 206 ? 12.638  -38.530 28.699  1.00 19.42 ? 241 TYR A O   1 
ATOM   1541 C  CB  . TYR A 1 206 ? 10.227  -40.374 28.826  1.00 19.30 ? 241 TYR A CB  1 
ATOM   1542 C  CG  . TYR A 1 206 ? 8.793   -40.794 28.615  1.00 17.62 ? 241 TYR A CG  1 
ATOM   1543 C  CD1 . TYR A 1 206 ? 7.942   -41.002 29.699  1.00 18.29 ? 241 TYR A CD1 1 
ATOM   1544 C  CD2 . TYR A 1 206 ? 8.263   -40.918 27.330  1.00 15.41 ? 241 TYR A CD2 1 
ATOM   1545 C  CE1 . TYR A 1 206 ? 6.614   -41.363 29.514  1.00 20.94 ? 241 TYR A CE1 1 
ATOM   1546 C  CE2 . TYR A 1 206 ? 6.928   -41.284 27.136  1.00 14.55 ? 241 TYR A CE2 1 
ATOM   1547 C  CZ  . TYR A 1 206 ? 6.113   -41.499 28.233  1.00 15.27 ? 241 TYR A CZ  1 
ATOM   1548 O  OH  . TYR A 1 206 ? 4.792   -41.861 28.060  1.00 18.64 ? 241 TYR A OH  1 
ATOM   1549 N  N   . VAL A 1 207 ? 11.887  -38.047 30.764  1.00 17.11 ? 242 VAL A N   1 
ATOM   1550 C  CA  . VAL A 1 207 ? 13.155  -37.530 31.252  1.00 21.79 ? 242 VAL A CA  1 
ATOM   1551 C  C   . VAL A 1 207 ? 13.805  -38.623 32.086  1.00 23.16 ? 242 VAL A C   1 
ATOM   1552 O  O   . VAL A 1 207 ? 13.235  -39.072 33.089  1.00 22.72 ? 242 VAL A O   1 
ATOM   1553 C  CB  . VAL A 1 207 ? 12.957  -36.246 32.074  1.00 21.54 ? 242 VAL A CB  1 
ATOM   1554 C  CG1 . VAL A 1 207 ? 14.298  -35.742 32.583  1.00 21.48 ? 242 VAL A CG1 1 
ATOM   1555 C  CG2 . VAL A 1 207 ? 12.253  -35.181 31.234  1.00 25.61 ? 242 VAL A CG2 1 
ATOM   1556 N  N   . VAL A 1 208 ? 15.006  -39.027 31.680  1.00 22.68 ? 243 VAL A N   1 
ATOM   1557 C  CA  . VAL A 1 208 ? 15.770  -40.101 32.301  1.00 21.81 ? 243 VAL A CA  1 
ATOM   1558 C  C   . VAL A 1 208 ? 16.947  -39.452 33.010  1.00 22.84 ? 243 VAL A C   1 
ATOM   1559 O  O   . VAL A 1 208 ? 17.604  -38.574 32.442  1.00 25.01 ? 243 VAL A O   1 
ATOM   1560 C  CB  . VAL A 1 208 ? 16.262  -41.085 31.224  1.00 19.60 ? 243 VAL A CB  1 
ATOM   1561 C  CG1 . VAL A 1 208 ? 16.990  -42.258 31.855  1.00 22.00 ? 243 VAL A CG1 1 
ATOM   1562 C  CG2 . VAL A 1 208 ? 15.087  -41.557 30.347  1.00 20.77 ? 243 VAL A CG2 1 
ATOM   1563 N  N   . GLU A 1 209 ? 17.207  -39.862 34.251  1.00 21.95 ? 244 GLU A N   1 
ATOM   1564 C  CA  . GLU A 1 209 ? 18.236  -39.206 35.048  1.00 27.43 ? 244 GLU A CA  1 
ATOM   1565 C  C   . GLU A 1 209 ? 18.930  -40.254 35.898  1.00 24.66 ? 244 GLU A C   1 
ATOM   1566 O  O   . GLU A 1 209 ? 18.264  -41.009 36.613  1.00 24.07 ? 244 GLU A O   1 
ATOM   1567 C  CB  . GLU A 1 209 ? 17.592  -38.161 35.966  1.00 35.36 ? 244 GLU A CB  1 
ATOM   1568 C  CG  . GLU A 1 209 ? 16.994  -36.967 35.231  1.00 40.78 ? 244 GLU A CG  1 
ATOM   1569 C  CD  . GLU A 1 209 ? 16.583  -35.841 36.165  1.00 74.66 ? 244 GLU A CD  1 
ATOM   1570 O  OE1 . GLU A 1 209 ? 17.476  -35.186 36.751  1.00 44.28 ? 244 GLU A OE1 1 
ATOM   1571 O  OE2 . GLU A 1 209 ? 15.355  -35.631 36.327  1.00 39.08 ? 244 GLU A OE2 1 
ATOM   1572 N  N   . SER A 1 210 ? 20.264  -40.282 35.838  1.00 25.45 ? 245 SER A N   1 
ATOM   1573 C  CA  . SER A 1 210 ? 21.051  -41.161 36.697  1.00 26.55 ? 245 SER A CA  1 
ATOM   1574 C  C   . SER A 1 210 ? 22.386  -40.506 37.028  1.00 29.23 ? 245 SER A C   1 
ATOM   1575 O  O   . SER A 1 210 ? 23.092  -40.058 36.121  1.00 28.20 ? 245 SER A O   1 
ATOM   1576 C  CB  . SER A 1 210 ? 21.295  -42.516 36.026  1.00 28.23 ? 245 SER A CB  1 
ATOM   1577 O  OG  . SER A 1 210 ? 22.173  -43.304 36.816  1.00 30.07 ? 245 SER A OG  1 
ATOM   1578 N  N   . GLN A 1 211 ? 22.728  -40.459 38.319  1.00 27.22 ? 246 GLN A N   1 
ATOM   1579 C  CA  . GLN A 1 211 ? 24.005  -39.904 38.777  1.00 34.09 ? 246 GLN A CA  1 
ATOM   1580 C  C   . GLN A 1 211 ? 24.249  -38.503 38.213  1.00 29.00 ? 246 GLN A C   1 
ATOM   1581 O  O   . GLN A 1 211 ? 25.352  -38.166 37.778  1.00 31.51 ? 246 GLN A O   1 
ATOM   1582 C  CB  . GLN A 1 211 ? 25.173  -40.848 38.466  1.00 32.16 ? 246 GLN A CB  1 
ATOM   1583 C  CG  . GLN A 1 211 ? 25.036  -42.275 39.016  1.00 31.37 ? 246 GLN A CG  1 
ATOM   1584 C  CD  . GLN A 1 211 ? 25.140  -42.373 40.539  1.00 37.32 ? 246 GLN A CD  1 
ATOM   1585 O  OE1 . GLN A 1 211 ? 25.198  -41.363 41.245  1.00 34.22 ? 246 GLN A OE1 1 
ATOM   1586 N  NE2 . GLN A 1 211 ? 25.172  -43.605 41.050  1.00 33.92 ? 246 GLN A NE2 1 
ATOM   1587 N  N   . GLY A 1 212 ? 23.196  -37.686 38.188  1.00 32.52 ? 247 GLY A N   1 
ATOM   1588 C  CA  . GLY A 1 212 ? 23.299  -36.326 37.697  1.00 30.59 ? 247 GLY A CA  1 
ATOM   1589 C  C   . GLY A 1 212 ? 23.324  -36.177 36.190  1.00 35.10 ? 247 GLY A C   1 
ATOM   1590 O  O   . GLY A 1 212 ? 23.482  -35.050 35.701  1.00 37.89 ? 247 GLY A O   1 
ATOM   1591 N  N   . GLN A 1 213 ? 23.176  -37.265 35.438  1.00 26.13 ? 248 GLN A N   1 
ATOM   1592 C  CA  . GLN A 1 213 ? 23.208  -37.241 33.983  1.00 24.38 ? 248 GLN A CA  1 
ATOM   1593 C  C   . GLN A 1 213 ? 21.775  -37.348 33.478  1.00 30.58 ? 248 GLN A C   1 
ATOM   1594 O  O   . GLN A 1 213 ? 21.059  -38.290 33.837  1.00 28.19 ? 248 GLN A O   1 
ATOM   1595 C  CB  . GLN A 1 213 ? 24.010  -38.435 33.462  1.00 27.57 ? 248 GLN A CB  1 
ATOM   1596 C  CG  . GLN A 1 213 ? 25.481  -38.452 33.881  1.00 34.89 ? 248 GLN A CG  1 
ATOM   1597 C  CD  . GLN A 1 213 ? 26.111  -37.073 33.931  1.00 43.16 ? 248 GLN A CD  1 
ATOM   1598 O  OE1 . GLN A 1 213 ? 26.267  -36.413 32.904  1.00 42.56 ? 248 GLN A OE1 1 
ATOM   1599 N  NE2 . GLN A 1 213 ? 26.478  -36.631 35.131  1.00 52.47 ? 248 GLN A NE2 1 
ATOM   1600 N  N   . LYS A 1 214 ? 21.362  -36.392 32.642  1.00 27.28 ? 249 LYS A N   1 
ATOM   1601 C  CA  . LYS A 1 214 ? 19.975  -36.255 32.211  1.00 23.90 ? 249 LYS A CA  1 
ATOM   1602 C  C   . LYS A 1 214 ? 19.848  -36.421 30.702  1.00 26.43 ? 249 LYS A C   1 
ATOM   1603 O  O   . LYS A 1 214 ? 20.675  -35.915 29.933  1.00 24.02 ? 249 LYS A O   1 
ATOM   1604 C  CB  . LYS A 1 214 ? 19.400  -34.886 32.612  1.00 24.97 ? 249 LYS A CB  1 
ATOM   1605 C  CG  . LYS A 1 214 ? 17.910  -34.745 32.321  1.00 34.86 ? 249 LYS A CG  1 
ATOM   1606 C  CD  . LYS A 1 214 ? 17.397  -33.325 32.550  1.00 40.77 ? 249 LYS A CD  1 
ATOM   1607 C  CE  . LYS A 1 214 ? 17.529  -32.896 33.993  1.00 44.21 ? 249 LYS A CE  1 
ATOM   1608 N  NZ  . LYS A 1 214 ? 16.474  -31.900 34.341  1.00 49.45 ? 249 LYS A NZ  1 
ATOM   1609 N  N   . LEU A 1 215 ? 18.785  -37.113 30.288  1.00 23.24 ? 250 LEU A N   1 
ATOM   1610 C  CA  . LEU A 1 215 ? 18.452  -37.324 28.884  1.00 18.65 ? 250 LEU A CA  1 
ATOM   1611 C  C   . LEU A 1 215 ? 16.950  -37.143 28.724  1.00 21.28 ? 250 LEU A C   1 
ATOM   1612 O  O   . LEU A 1 215 ? 16.168  -37.862 29.350  1.00 20.04 ? 250 LEU A O   1 
ATOM   1613 C  CB  . LEU A 1 215 ? 18.841  -38.743 28.459  1.00 22.88 ? 250 LEU A CB  1 
ATOM   1614 C  CG  . LEU A 1 215 ? 18.316  -39.227 27.102  1.00 20.13 ? 250 LEU A CG  1 
ATOM   1615 C  CD1 . LEU A 1 215 ? 18.817  -38.328 25.960  1.00 19.92 ? 250 LEU A CD1 1 
ATOM   1616 C  CD2 . LEU A 1 215 ? 18.699  -40.677 26.869  1.00 22.14 ? 250 LEU A CD2 1 
ATOM   1617 N  N   . ALA A 1 216 ? 16.537  -36.207 27.878  1.00 19.25 ? 251 ALA A N   1 
ATOM   1618 C  CA  . ALA A 1 216 ? 15.120  -35.954 27.647  1.00 18.33 ? 251 ALA A CA  1 
ATOM   1619 C  C   . ALA A 1 216 ? 14.736  -36.576 26.307  1.00 23.14 ? 251 ALA A C   1 
ATOM   1620 O  O   . ALA A 1 216 ? 15.239  -36.164 25.256  1.00 18.50 ? 251 ALA A O   1 
ATOM   1621 C  CB  . ALA A 1 216 ? 14.824  -34.456 27.675  1.00 20.08 ? 251 ALA A CB  1 
ATOM   1622 N  N   . LEU A 1 217 ? 13.868  -37.586 26.352  1.00 17.92 ? 252 LEU A N   1 
ATOM   1623 C  CA  . LEU A 1 217 ? 13.341  -38.260 25.172  1.00 15.91 ? 252 LEU A CA  1 
ATOM   1624 C  C   . LEU A 1 217 ? 12.115  -37.474 24.730  1.00 17.25 ? 252 LEU A C   1 
ATOM   1625 O  O   . LEU A 1 217 ? 11.052  -37.551 25.356  1.00 16.67 ? 252 LEU A O   1 
ATOM   1626 C  CB  . LEU A 1 217 ? 12.992  -39.705 25.521  1.00 16.52 ? 252 LEU A CB  1 
ATOM   1627 C  CG  . LEU A 1 217 ? 14.171  -40.480 26.129  1.00 21.78 ? 252 LEU A CG  1 
ATOM   1628 C  CD1 . LEU A 1 217 ? 13.740  -41.874 26.550  1.00 17.32 ? 252 LEU A CD1 1 
ATOM   1629 C  CD2 . LEU A 1 217 ? 15.350  -40.552 25.143  1.00 22.39 ? 252 LEU A CD2 1 
ATOM   1630 N  N   . LEU A 1 218 ? 12.283  -36.689 23.668  1.00 18.44 ? 253 LEU A N   1 
ATOM   1631 C  CA  . LEU A 1 218 ? 11.311  -35.689 23.244  1.00 18.68 ? 253 LEU A CA  1 
ATOM   1632 C  C   . LEU A 1 218 ? 10.243  -36.237 22.307  1.00 20.35 ? 253 LEU A C   1 
ATOM   1633 O  O   . LEU A 1 218 ? 9.360   -35.479 21.892  1.00 19.32 ? 253 LEU A O   1 
ATOM   1634 C  CB  . LEU A 1 218 ? 12.039  -34.523 22.558  1.00 16.77 ? 253 LEU A CB  1 
ATOM   1635 C  CG  . LEU A 1 218 ? 13.141  -33.792 23.328  1.00 15.95 ? 253 LEU A CG  1 
ATOM   1636 C  CD1 . LEU A 1 218 ? 13.728  -32.669 22.485  1.00 19.39 ? 253 LEU A CD1 1 
ATOM   1637 C  CD2 . LEU A 1 218 ? 12.615  -33.252 24.657  1.00 18.46 ? 253 LEU A CD2 1 
ATOM   1638 N  N   . GLY A 1 219 ? 10.287  -37.521 21.966  1.00 18.05 ? 254 GLY A N   1 
ATOM   1639 C  CA  . GLY A 1 219 ? 9.258   -38.048 21.081  1.00 17.80 ? 254 GLY A CA  1 
ATOM   1640 C  C   . GLY A 1 219 ? 9.297   -37.348 19.736  1.00 21.38 ? 254 GLY A C   1 
ATOM   1641 O  O   . GLY A 1 219 ? 10.347  -37.267 19.084  1.00 18.21 ? 254 GLY A O   1 
ATOM   1642 N  N   . ASP A 1 220 ? 8.140   -36.817 19.324  1.00 17.24 ? 255 ASP A N   1 
ATOM   1643 C  CA  . ASP A 1 220 ? 7.976   -36.089 18.070  1.00 15.76 ? 255 ASP A CA  1 
ATOM   1644 C  C   . ASP A 1 220 ? 7.879   -34.573 18.269  1.00 22.85 ? 255 ASP A C   1 
ATOM   1645 O  O   . ASP A 1 220 ? 7.250   -33.878 17.458  1.00 19.44 ? 255 ASP A O   1 
ATOM   1646 C  CB  . ASP A 1 220 ? 6.782   -36.635 17.278  1.00 18.51 ? 255 ASP A CB  1 
ATOM   1647 C  CG  . ASP A 1 220 ? 7.115   -37.934 16.557  1.00 18.05 ? 255 ASP A CG  1 
ATOM   1648 O  OD1 . ASP A 1 220 ? 8.194   -38.493 16.853  1.00 20.03 ? 255 ASP A OD1 1 
ATOM   1649 O  OD2 . ASP A 1 220 ? 6.328   -38.387 15.700  1.00 16.86 ? 255 ASP A OD2 1 
ATOM   1650 N  N   . LEU A 1 221 ? 8.497   -34.038 19.331  1.00 14.95 ? 256 LEU A N   1 
ATOM   1651 C  CA  . LEU A 1 221 ? 8.551   -32.587 19.485  1.00 19.32 ? 256 LEU A CA  1 
ATOM   1652 C  C   . LEU A 1 221 ? 9.298   -31.925 18.338  1.00 23.06 ? 256 LEU A C   1 
ATOM   1653 O  O   . LEU A 1 221 ? 9.024   -30.765 18.006  1.00 38.39 ? 256 LEU A O   1 
ATOM   1654 C  CB  . LEU A 1 221 ? 9.203   -32.206 20.813  1.00 29.36 ? 256 LEU A CB  1 
ATOM   1655 C  CG  . LEU A 1 221 ? 8.265   -32.120 22.005  1.00 28.29 ? 256 LEU A CG  1 
ATOM   1656 C  CD1 . LEU A 1 221 ? 9.043   -31.678 23.239  1.00 33.70 ? 256 LEU A CD1 1 
ATOM   1657 C  CD2 . LEU A 1 221 ? 7.141   -31.137 21.705  1.00 30.78 ? 256 LEU A CD2 1 
ATOM   1658 N  N   . ILE A 1 222 ? 10.241  -32.630 17.724  1.00 19.08 ? 257 ILE A N   1 
ATOM   1659 C  CA  . ILE A 1 222 ? 10.864  -32.178 16.489  1.00 22.10 ? 257 ILE A CA  1 
ATOM   1660 C  C   . ILE A 1 222 ? 10.800  -33.297 15.454  1.00 25.46 ? 257 ILE A C   1 
ATOM   1661 O  O   . ILE A 1 222 ? 10.951  -34.480 15.784  1.00 24.31 ? 257 ILE A O   1 
ATOM   1662 C  CB  . ILE A 1 222 ? 12.292  -31.621 16.703  1.00 33.85 ? 257 ILE A CB  1 
ATOM   1663 C  CG1 . ILE A 1 222 ? 12.874  -31.112 15.375  1.00 29.62 ? 257 ILE A CG1 1 
ATOM   1664 C  CG2 . ILE A 1 222 ? 13.194  -32.641 17.400  1.00 23.68 ? 257 ILE A CG2 1 
ATOM   1665 C  CD1 . ILE A 1 222 ? 14.168  -30.385 15.529  1.00 33.23 ? 257 ILE A CD1 1 
ATOM   1666 N  N   . LEU A 1 223 ? 10.507  -32.920 14.214  1.00 20.70 ? 258 LEU A N   1 
ATOM   1667 C  CA  . LEU A 1 223 ? 10.281  -33.849 13.117  1.00 19.99 ? 258 LEU A CA  1 
ATOM   1668 C  C   . LEU A 1 223 ? 11.293  -33.728 11.988  1.00 24.12 ? 258 LEU A C   1 
ATOM   1669 O  O   . LEU A 1 223 ? 11.641  -34.741 11.379  1.00 26.19 ? 258 LEU A O   1 
ATOM   1670 C  CB  . LEU A 1 223 ? 8.874   -33.631 12.543  1.00 20.38 ? 258 LEU A CB  1 
ATOM   1671 C  CG  . LEU A 1 223 ? 7.783   -33.815 13.603  1.00 24.65 ? 258 LEU A CG  1 
ATOM   1672 C  CD1 . LEU A 1 223 ? 6.401   -33.505 13.052  1.00 26.71 ? 258 LEU A CD1 1 
ATOM   1673 C  CD2 . LEU A 1 223 ? 7.846   -35.233 14.157  1.00 23.95 ? 258 LEU A CD2 1 
ATOM   1674 N  N   . VAL A 1 224 ? 11.767  -32.524 11.687  1.00 20.28 ? 259 VAL A N   1 
ATOM   1675 C  CA  . VAL A 1 224 ? 12.672  -32.273 10.568  1.00 22.49 ? 259 VAL A CA  1 
ATOM   1676 C  C   . VAL A 1 224 ? 13.812  -31.431 11.118  1.00 19.22 ? 259 VAL A C   1 
ATOM   1677 O  O   . VAL A 1 224 ? 13.682  -30.209 11.244  1.00 19.45 ? 259 VAL A O   1 
ATOM   1678 C  CB  . VAL A 1 224 ? 11.977  -31.562 9.401   1.00 22.59 ? 259 VAL A CB  1 
ATOM   1679 C  CG1 . VAL A 1 224 ? 12.899  -31.517 8.198   1.00 22.40 ? 259 VAL A CG1 1 
ATOM   1680 C  CG2 . VAL A 1 224 ? 10.667  -32.260 9.048   1.00 24.52 ? 259 VAL A CG2 1 
ATOM   1681 N  N   . ALA A 1 225 ? 14.943  -32.074 11.422  1.00 19.77 ? 260 ALA A N   1 
ATOM   1682 C  CA  . ALA A 1 225 ? 16.055  -31.370 12.064  1.00 24.58 ? 260 ALA A CA  1 
ATOM   1683 C  C   . ALA A 1 225 ? 16.535  -30.184 11.235  1.00 18.24 ? 260 ALA A C   1 
ATOM   1684 O  O   . ALA A 1 225 ? 16.807  -29.106 11.783  1.00 21.62 ? 260 ALA A O   1 
ATOM   1685 C  CB  . ALA A 1 225 ? 17.208  -32.336 12.338  1.00 24.44 ? 260 ALA A CB  1 
ATOM   1686 N  N   . ALA A 1 226 ? 16.634  -30.351 9.912   1.00 19.03 ? 261 ALA A N   1 
ATOM   1687 C  CA  . ALA A 1 226 ? 17.188  -29.302 9.059   1.00 21.34 ? 261 ALA A CA  1 
ATOM   1688 C  C   . ALA A 1 226 ? 16.285  -28.078 8.939   1.00 22.61 ? 261 ALA A C   1 
ATOM   1689 O  O   . ALA A 1 226 ? 16.721  -27.063 8.382   1.00 26.32 ? 261 ALA A O   1 
ATOM   1690 C  CB  . ALA A 1 226 ? 17.520  -29.853 7.671   1.00 29.60 ? 261 ALA A CB  1 
ATOM   1691 N  N   . VAL A 1 227 ? 15.050  -28.144 9.433   1.00 19.87 ? 262 VAL A N   1 
ATOM   1692 C  CA  . VAL A 1 227 ? 14.131  -27.014 9.423   1.00 21.14 ? 262 VAL A CA  1 
ATOM   1693 C  C   . VAL A 1 227 ? 13.874  -26.488 10.832  1.00 23.17 ? 262 VAL A C   1 
ATOM   1694 O  O   . VAL A 1 227 ? 13.976  -25.285 11.084  1.00 22.07 ? 262 VAL A O   1 
ATOM   1695 C  CB  . VAL A 1 227 ? 12.808  -27.370 8.706   1.00 25.16 ? 262 VAL A CB  1 
ATOM   1696 C  CG1 . VAL A 1 227 ? 11.749  -26.290 8.955   1.00 19.82 ? 262 VAL A CG1 1 
ATOM   1697 C  CG2 . VAL A 1 227 ? 13.047  -27.573 7.215   1.00 24.78 ? 262 VAL A CG2 1 
ATOM   1698 N  N   . GLN A 1 228 ? 13.546  -27.379 11.763  1.00 18.47 ? 263 GLN A N   1 
ATOM   1699 C  CA  . GLN A 1 228 ? 12.924  -26.965 13.014  1.00 20.27 ? 263 GLN A CA  1 
ATOM   1700 C  C   . GLN A 1 228 ? 13.905  -26.644 14.136  1.00 24.89 ? 263 GLN A C   1 
ATOM   1701 O  O   . GLN A 1 228 ? 13.474  -26.144 15.180  1.00 25.17 ? 263 GLN A O   1 
ATOM   1702 C  CB  . GLN A 1 228 ? 11.934  -28.029 13.458  1.00 19.52 ? 263 GLN A CB  1 
ATOM   1703 C  CG  . GLN A 1 228 ? 10.777  -28.145 12.487  1.00 19.58 ? 263 GLN A CG  1 
ATOM   1704 C  CD  . GLN A 1 228 ? 9.897   -29.324 12.809  1.00 20.41 ? 263 GLN A CD  1 
ATOM   1705 O  OE1 . GLN A 1 228 ? 10.387  -30.419 13.063  1.00 20.11 ? 263 GLN A OE1 1 
ATOM   1706 N  NE2 . GLN A 1 228 ? 8.590   -29.109 12.798  1.00 20.71 ? 263 GLN A NE2 1 
ATOM   1707 N  N   . PHE A 1 229 ? 15.197  -26.922 13.976  1.00 22.26 ? 264 PHE A N   1 
ATOM   1708 C  CA  . PHE A 1 229 ? 16.138  -26.388 14.956  1.00 24.36 ? 264 PHE A CA  1 
ATOM   1709 C  C   . PHE A 1 229 ? 16.419  -24.916 14.685  1.00 24.94 ? 264 PHE A C   1 
ATOM   1710 O  O   . PHE A 1 229 ? 16.445  -24.099 15.615  1.00 25.30 ? 264 PHE A O   1 
ATOM   1711 C  CB  . PHE A 1 229 ? 17.444  -27.182 14.945  1.00 23.62 ? 264 PHE A CB  1 
ATOM   1712 C  CG  . PHE A 1 229 ? 17.373  -28.491 15.681  1.00 21.48 ? 264 PHE A CG  1 
ATOM   1713 C  CD1 . PHE A 1 229 ? 17.081  -28.534 17.035  1.00 21.82 ? 264 PHE A CD1 1 
ATOM   1714 C  CD2 . PHE A 1 229 ? 17.632  -29.681 15.020  1.00 22.32 ? 264 PHE A CD2 1 
ATOM   1715 C  CE1 . PHE A 1 229 ? 17.029  -29.744 17.716  1.00 26.36 ? 264 PHE A CE1 1 
ATOM   1716 C  CE2 . PHE A 1 229 ? 17.582  -30.897 15.695  1.00 27.82 ? 264 PHE A CE2 1 
ATOM   1717 C  CZ  . PHE A 1 229 ? 17.277  -30.928 17.043  1.00 25.13 ? 264 PHE A CZ  1 
ATOM   1718 N  N   . ASP A 1 230 ? 16.618  -24.569 13.412  1.00 20.63 ? 265 ASP A N   1 
ATOM   1719 C  CA  . ASP A 1 230 ? 16.856  -23.181 13.033  1.00 22.22 ? 265 ASP A CA  1 
ATOM   1720 C  C   . ASP A 1 230 ? 15.609  -22.336 13.251  1.00 32.59 ? 265 ASP A C   1 
ATOM   1721 O  O   . ASP A 1 230 ? 15.707  -21.160 13.621  1.00 28.76 ? 265 ASP A O   1 
ATOM   1722 C  CB  . ASP A 1 230 ? 17.252  -23.120 11.557  1.00 31.16 ? 265 ASP A CB  1 
ATOM   1723 C  CG  . ASP A 1 230 ? 18.691  -23.535 11.315  1.00 43.01 ? 265 ASP A CG  1 
ATOM   1724 O  OD1 . ASP A 1 230 ? 19.491  -23.519 12.275  1.00 49.46 ? 265 ASP A OD1 1 
ATOM   1725 O  OD2 . ASP A 1 230 ? 19.019  -23.880 10.158  1.00 49.42 ? 265 ASP A OD2 1 
ATOM   1726 N  N   . ASP A 1 231 ? 14.431  -22.910 12.997  1.00 27.00 ? 266 ASP A N   1 
ATOM   1727 C  CA  . ASP A 1 231 ? 13.159  -22.206 13.137  1.00 24.94 ? 266 ASP A CA  1 
ATOM   1728 C  C   . ASP A 1 231 ? 12.195  -23.120 13.876  1.00 21.65 ? 266 ASP A C   1 
ATOM   1729 O  O   . ASP A 1 231 ? 11.411  -23.854 13.256  1.00 23.46 ? 266 ASP A O   1 
ATOM   1730 C  CB  . ASP A 1 231 ? 12.597  -21.778 11.782  1.00 29.69 ? 266 ASP A CB  1 
ATOM   1731 C  CG  . ASP A 1 231 ? 11.378  -20.870 11.917  1.00 33.89 ? 266 ASP A CG  1 
ATOM   1732 O  OD1 . ASP A 1 231 ? 10.882  -20.685 13.053  1.00 30.88 ? 266 ASP A OD1 1 
ATOM   1733 O  OD2 . ASP A 1 231 ? 10.905  -20.348 10.886  1.00 39.30 ? 266 ASP A OD2 1 
ATOM   1734 N  N   . PRO A 1 232 ? 12.221  -23.104 15.211  1.00 24.18 ? 267 PRO A N   1 
ATOM   1735 C  CA  . PRO A 1 232 ? 11.327  -23.988 15.973  1.00 22.59 ? 267 PRO A CA  1 
ATOM   1736 C  C   . PRO A 1 232 ? 9.851   -23.661 15.824  1.00 27.49 ? 267 PRO A C   1 
ATOM   1737 O  O   . PRO A 1 232 ? 9.020   -24.451 16.288  1.00 26.99 ? 267 PRO A O   1 
ATOM   1738 C  CB  . PRO A 1 232 ? 11.795  -23.807 17.426  1.00 25.98 ? 267 PRO A CB  1 
ATOM   1739 C  CG  . PRO A 1 232 ? 13.148  -23.170 17.332  1.00 29.96 ? 267 PRO A CG  1 
ATOM   1740 C  CD  . PRO A 1 232 ? 13.131  -22.346 16.086  1.00 24.95 ? 267 PRO A CD  1 
ATOM   1741 N  N   . SER A 1 233 ? 9.489   -22.535 15.205  1.00 25.58 ? 268 SER A N   1 
ATOM   1742 C  CA  . SER A 1 233 ? 8.074   -22.204 15.074  1.00 23.76 ? 268 SER A CA  1 
ATOM   1743 C  C   . SER A 1 233 ? 7.388   -22.930 13.918  1.00 28.09 ? 268 SER A C   1 
ATOM   1744 O  O   . SER A 1 233 ? 6.153   -22.914 13.847  1.00 28.40 ? 268 SER A O   1 
ATOM   1745 C  CB  . SER A 1 233 ? 7.868   -20.690 14.954  1.00 27.93 ? 268 SER A CB  1 
ATOM   1746 O  OG  . SER A 1 233 ? 8.409   -20.199 13.743  1.00 34.23 ? 268 SER A OG  1 
ATOM   1747 N  N   . VAL A 1 234 ? 8.137   -23.571 13.025  1.00 25.59 ? 269 VAL A N   1 
ATOM   1748 C  CA  . VAL A 1 234 ? 7.533   -24.252 11.884  1.00 28.75 ? 269 VAL A CA  1 
ATOM   1749 C  C   . VAL A 1 234 ? 6.920   -25.560 12.368  1.00 22.35 ? 269 VAL A C   1 
ATOM   1750 O  O   . VAL A 1 234 ? 7.605   -26.396 12.969  1.00 20.81 ? 269 VAL A O   1 
ATOM   1751 C  CB  . VAL A 1 234 ? 8.564   -24.502 10.774  1.00 30.11 ? 269 VAL A CB  1 
ATOM   1752 C  CG1 . VAL A 1 234 ? 7.887   -25.138 9.556   1.00 25.54 ? 269 VAL A CG1 1 
ATOM   1753 C  CG2 . VAL A 1 234 ? 9.283   -23.206 10.390  1.00 26.68 ? 269 VAL A CG2 1 
ATOM   1754 N  N   . THR A 1 235 ? 5.630   -25.744 12.101  1.00 22.67 ? 270 THR A N   1 
ATOM   1755 C  CA  . THR A 1 235 ? 4.896   -26.936 12.499  1.00 24.05 ? 270 THR A CA  1 
ATOM   1756 C  C   . THR A 1 235 ? 4.526   -27.753 11.264  1.00 21.04 ? 270 THR A C   1 
ATOM   1757 O  O   . THR A 1 235 ? 4.894   -27.421 10.137  1.00 25.85 ? 270 THR A O   1 
ATOM   1758 C  CB  . THR A 1 235 ? 3.652   -26.543 13.293  1.00 28.18 ? 270 THR A CB  1 
ATOM   1759 O  OG1 . THR A 1 235 ? 2.777   -25.782 12.452  1.00 26.58 ? 270 THR A OG1 1 
ATOM   1760 C  CG2 . THR A 1 235 ? 4.045   -25.709 14.510  1.00 25.10 ? 270 THR A CG2 1 
ATOM   1761 N  N   . THR A 1 236 ? 3.791   -28.842 11.486  1.00 24.31 ? 271 THR A N   1 
ATOM   1762 C  CA  . THR A 1 236 ? 3.327   -29.692 10.398  1.00 22.41 ? 271 THR A CA  1 
ATOM   1763 C  C   . THR A 1 236 ? 1.815   -29.857 10.484  1.00 24.14 ? 271 THR A C   1 
ATOM   1764 O  O   . THR A 1 236 ? 1.190   -29.588 11.516  1.00 23.94 ? 271 THR A O   1 
ATOM   1765 C  CB  . THR A 1 236 ? 3.986   -31.082 10.421  1.00 26.64 ? 271 THR A CB  1 
ATOM   1766 O  OG1 . THR A 1 236 ? 3.449   -31.850 11.507  1.00 31.69 ? 271 THR A OG1 1 
ATOM   1767 C  CG2 . THR A 1 236 ? 5.494   -30.962 10.588  1.00 28.76 ? 271 THR A CG2 1 
ATOM   1768 N  N   . ASP A 1 237 ? 1.229   -30.307 9.375   1.00 25.46 ? 272 ASP A N   1 
ATOM   1769 C  CA  . ASP A 1 237 ? -0.195  -30.620 9.366   1.00 28.94 ? 272 ASP A CA  1 
ATOM   1770 C  C   . ASP A 1 237 ? -0.531  -31.892 10.143  1.00 24.20 ? 272 ASP A C   1 
ATOM   1771 O  O   . ASP A 1 237 ? -1.714  -32.221 10.278  1.00 33.03 ? 272 ASP A O   1 
ATOM   1772 C  CB  . ASP A 1 237 ? -0.736  -30.661 7.931   1.00 33.31 ? 272 ASP A CB  1 
ATOM   1773 C  CG  . ASP A 1 237 ? -0.087  -31.744 7.079   1.00 38.12 ? 272 ASP A CG  1 
ATOM   1774 O  OD1 . ASP A 1 237 ? 0.846   -32.424 7.554   1.00 39.17 ? 272 ASP A OD1 1 
ATOM   1775 O  OD2 . ASP A 1 237 ? -0.501  -31.899 5.911   1.00 58.75 ? 272 ASP A OD2 1 
ATOM   1776 N  N   . LEU A 1 238 ? 0.470   -32.603 10.653  1.00 24.06 ? 273 LEU A N   1 
ATOM   1777 C  CA  . LEU A 1 238 ? 0.253   -33.752 11.517  1.00 28.95 ? 273 LEU A CA  1 
ATOM   1778 C  C   . LEU A 1 238 ? 0.211   -33.375 12.991  1.00 33.02 ? 273 LEU A C   1 
ATOM   1779 O  O   . LEU A 1 238 ? -0.065  -34.240 13.827  1.00 32.71 ? 273 LEU A O   1 
ATOM   1780 C  CB  . LEU A 1 238 ? 1.367   -34.782 11.305  1.00 32.25 ? 273 LEU A CB  1 
ATOM   1781 C  CG  . LEU A 1 238 ? 1.315   -35.554 9.988   1.00 46.41 ? 273 LEU A CG  1 
ATOM   1782 C  CD1 . LEU A 1 238 ? 2.638   -36.255 9.735   1.00 50.27 ? 273 LEU A CD1 1 
ATOM   1783 C  CD2 . LEU A 1 238 ? 0.167   -36.542 10.006  1.00 49.27 ? 273 LEU A CD2 1 
ATOM   1784 N  N   . ASP A 1 239 ? 0.501   -32.120 13.330  1.00 25.47 ? 274 ASP A N   1 
ATOM   1785 C  CA  . ASP A 1 239 ? 0.418   -31.669 14.711  1.00 27.17 ? 274 ASP A CA  1 
ATOM   1786 C  C   . ASP A 1 239 ? -1.037  -31.367 15.046  1.00 25.71 ? 274 ASP A C   1 
ATOM   1787 O  O   . ASP A 1 239 ? -1.733  -30.689 14.282  1.00 25.86 ? 274 ASP A O   1 
ATOM   1788 C  CB  . ASP A 1 239 ? 1.277   -30.417 14.905  1.00 21.64 ? 274 ASP A CB  1 
ATOM   1789 C  CG  . ASP A 1 239 ? 2.772   -30.691 14.724  1.00 27.77 ? 274 ASP A CG  1 
ATOM   1790 O  OD1 . ASP A 1 239 ? 3.317   -31.616 15.370  1.00 24.50 ? 274 ASP A OD1 1 
ATOM   1791 O  OD2 . ASP A 1 239 ? 3.405   -29.972 13.924  1.00 29.15 ? 274 ASP A OD2 1 
ATOM   1792 N  N   . SER A 1 240 ? -1.502  -31.887 16.187  1.00 21.06 ? 275 SER A N   1 
ATOM   1793 C  CA  . SER A 1 240 ? -2.891  -31.678 16.580  1.00 22.68 ? 275 SER A CA  1 
ATOM   1794 C  C   . SER A 1 240 ? -3.163  -30.224 16.945  1.00 26.93 ? 275 SER A C   1 
ATOM   1795 O  O   . SER A 1 240 ? -4.269  -29.720 16.715  1.00 28.72 ? 275 SER A O   1 
ATOM   1796 C  CB  . SER A 1 240 ? -3.244  -32.588 17.759  1.00 27.43 ? 275 SER A CB  1 
ATOM   1797 O  OG  . SER A 1 240 ? -3.215  -33.952 17.372  1.00 42.12 ? 275 SER A OG  1 
ATOM   1798 N  N   . ASP A 1 241 ? -2.173  -29.542 17.517  1.00 21.92 ? 276 ASP A N   1 
ATOM   1799 C  CA  . ASP A 1 241 ? -2.323  -28.165 17.980  1.00 26.47 ? 276 ASP A CA  1 
ATOM   1800 C  C   . ASP A 1 241 ? -0.992  -27.468 17.701  1.00 27.95 ? 276 ASP A C   1 
ATOM   1801 O  O   . ASP A 1 241 ? -0.025  -27.630 18.453  1.00 27.83 ? 276 ASP A O   1 
ATOM   1802 C  CB  . ASP A 1 241 ? -2.695  -28.158 19.460  1.00 25.63 ? 276 ASP A CB  1 
ATOM   1803 C  CG  . ASP A 1 241 ? -2.849  -26.762 20.028  1.00 40.04 ? 276 ASP A CG  1 
ATOM   1804 O  OD1 . ASP A 1 241 ? -2.541  -25.777 19.321  1.00 33.45 ? 276 ASP A OD1 1 
ATOM   1805 O  OD2 . ASP A 1 241 ? -3.304  -26.653 21.188  1.00 40.79 ? 276 ASP A OD2 1 
ATOM   1806 N  N   . SER A 1 242 ? -0.954  -26.695 16.613  1.00 24.74 ? 277 SER A N   1 
ATOM   1807 C  CA  . SER A 1 242 ? 0.307   -26.125 16.141  1.00 26.08 ? 277 SER A CA  1 
ATOM   1808 C  C   . SER A 1 242 ? 0.903   -25.146 17.148  1.00 32.79 ? 277 SER A C   1 
ATOM   1809 O  O   . SER A 1 242 ? 2.120   -25.151 17.386  1.00 30.43 ? 277 SER A O   1 
ATOM   1810 C  CB  . SER A 1 242 ? 0.094   -25.436 14.792  1.00 34.78 ? 277 SER A CB  1 
ATOM   1811 O  OG  . SER A 1 242 ? -0.372  -26.362 13.827  1.00 65.56 ? 277 SER A OG  1 
ATOM   1812 N  N   . LYS A 1 243 ? 0.066   -24.284 17.732  1.00 28.66 ? 278 LYS A N   1 
ATOM   1813 C  CA  . LYS A 1 243 ? 0.578   -23.292 18.672  1.00 31.10 ? 278 LYS A CA  1 
ATOM   1814 C  C   . LYS A 1 243 ? 1.203   -23.978 19.880  1.00 29.69 ? 278 LYS A C   1 
ATOM   1815 O  O   . LYS A 1 243 ? 2.301   -23.606 20.327  1.00 35.88 ? 278 LYS A O   1 
ATOM   1816 C  CB  . LYS A 1 243 ? -0.559  -22.360 19.099  1.00 29.60 ? 278 LYS A CB  1 
ATOM   1817 C  CG  . LYS A 1 243 ? -0.797  -21.201 18.139  1.00 44.69 ? 278 LYS A CG  1 
ATOM   1818 C  CD  . LYS A 1 243 ? -1.048  -19.889 18.870  1.00 59.74 ? 278 LYS A CD  1 
ATOM   1819 C  CE  . LYS A 1 243 ? -0.659  -18.696 18.003  1.00 71.24 ? 278 LYS A CE  1 
ATOM   1820 N  NZ  . LYS A 1 243 ? -0.364  -17.473 18.806  1.00 58.59 ? 278 LYS A NZ  1 
ATOM   1821 N  N   . ALA A 1 244 ? 0.531   -25.011 20.393  1.00 25.61 ? 279 ALA A N   1 
ATOM   1822 C  CA  . ALA A 1 244 ? 1.049   -25.739 21.540  1.00 23.88 ? 279 ALA A CA  1 
ATOM   1823 C  C   . ALA A 1 244 ? 2.364   -26.421 21.210  1.00 29.19 ? 279 ALA A C   1 
ATOM   1824 O  O   . ALA A 1 244 ? 3.301   -26.389 22.013  1.00 27.57 ? 279 ALA A O   1 
ATOM   1825 C  CB  . ALA A 1 244 ? 0.026   -26.764 22.027  1.00 25.15 ? 279 ALA A CB  1 
ATOM   1826 N  N   . VAL A 1 245 ? 2.452   -27.063 20.043  1.00 23.54 ? 280 VAL A N   1 
ATOM   1827 C  CA  . VAL A 1 245 ? 3.677   -27.777 19.707  1.00 27.48 ? 280 VAL A CA  1 
ATOM   1828 C  C   . VAL A 1 245 ? 4.842   -26.800 19.555  1.00 21.75 ? 280 VAL A C   1 
ATOM   1829 O  O   . VAL A 1 245 ? 5.962   -27.084 19.990  1.00 28.87 ? 280 VAL A O   1 
ATOM   1830 C  CB  . VAL A 1 245 ? 3.468   -28.717 18.498  1.00 27.36 ? 280 VAL A CB  1 
ATOM   1831 C  CG1 . VAL A 1 245 ? 3.428   -27.952 17.205  1.00 31.94 ? 280 VAL A CG1 1 
ATOM   1832 C  CG2 . VAL A 1 245 ? 4.537   -29.799 18.456  1.00 25.22 ? 280 VAL A CG2 1 
ATOM   1833 N  N   . ALA A 1 246 ? 4.591   -25.616 18.986  1.00 22.02 ? 281 ALA A N   1 
ATOM   1834 C  CA  . ALA A 1 246 ? 5.652   -24.613 18.909  1.00 25.15 ? 281 ALA A CA  1 
ATOM   1835 C  C   . ALA A 1 246 ? 6.095   -24.169 20.300  1.00 29.73 ? 281 ALA A C   1 
ATOM   1836 O  O   . ALA A 1 246 ? 7.299   -24.082 20.581  1.00 28.28 ? 281 ALA A O   1 
ATOM   1837 C  CB  . ALA A 1 246 ? 5.190   -23.416 18.076  1.00 33.07 ? 281 ALA A CB  1 
ATOM   1838 N  N   . VAL A 1 247 ? 5.136   -23.913 21.193  1.00 24.26 ? 282 VAL A N   1 
ATOM   1839 C  CA  . VAL A 1 247 ? 5.478   -23.503 22.556  1.00 26.21 ? 282 VAL A CA  1 
ATOM   1840 C  C   . VAL A 1 247 ? 6.289   -24.588 23.258  1.00 27.85 ? 282 VAL A C   1 
ATOM   1841 O  O   . VAL A 1 247 ? 7.325   -24.312 23.879  1.00 29.06 ? 282 VAL A O   1 
ATOM   1842 C  CB  . VAL A 1 247 ? 4.205   -23.152 23.346  1.00 28.93 ? 282 VAL A CB  1 
ATOM   1843 C  CG1 . VAL A 1 247 ? 4.515   -23.053 24.829  1.00 28.51 ? 282 VAL A CG1 1 
ATOM   1844 C  CG2 . VAL A 1 247 ? 3.610   -21.852 22.832  1.00 40.68 ? 282 VAL A CG2 1 
ATOM   1845 N  N   . GLU A 1 248 ? 5.829   -25.837 23.168  1.00 24.52 ? 283 GLU A N   1 
ATOM   1846 C  CA  . GLU A 1 248 ? 6.484   -26.934 23.877  1.00 25.37 ? 283 GLU A CA  1 
ATOM   1847 C  C   . GLU A 1 248 ? 7.864   -27.229 23.305  1.00 24.50 ? 283 GLU A C   1 
ATOM   1848 O  O   . GLU A 1 248 ? 8.799   -27.533 24.057  1.00 24.88 ? 283 GLU A O   1 
ATOM   1849 C  CB  . GLU A 1 248 ? 5.603   -28.184 23.861  1.00 25.58 ? 283 GLU A CB  1 
ATOM   1850 C  CG  . GLU A 1 248 ? 4.343   -28.064 24.729  1.00 24.07 ? 283 GLU A CG  1 
ATOM   1851 C  CD  . GLU A 1 248 ? 4.662   -27.697 26.173  1.00 45.65 ? 283 GLU A CD  1 
ATOM   1852 O  OE1 . GLU A 1 248 ? 5.568   -28.326 26.761  1.00 47.19 ? 283 GLU A OE1 1 
ATOM   1853 O  OE2 . GLU A 1 248 ? 4.018   -26.774 26.716  1.00 48.23 ? 283 GLU A OE2 1 
ATOM   1854 N  N   . ARG A 1 249 ? 8.016   -27.141 21.979  1.00 23.87 ? 284 ARG A N   1 
ATOM   1855 C  CA  . ARG A 1 249 ? 9.330   -27.319 21.373  1.00 20.78 ? 284 ARG A CA  1 
ATOM   1856 C  C   . ARG A 1 249 ? 10.297  -26.242 21.827  1.00 24.09 ? 284 ARG A C   1 
ATOM   1857 O  O   . ARG A 1 249 ? 11.450  -26.535 22.169  1.00 23.91 ? 284 ARG A O   1 
ATOM   1858 C  CB  . ARG A 1 249 ? 9.222   -27.305 19.850  1.00 23.64 ? 284 ARG A CB  1 
ATOM   1859 C  CG  . ARG A 1 249 ? 10.577  -27.369 19.147  1.00 25.79 ? 284 ARG A CG  1 
ATOM   1860 C  CD  . ARG A 1 249 ? 10.364  -27.262 17.665  1.00 25.84 ? 284 ARG A CD  1 
ATOM   1861 N  NE  . ARG A 1 249 ? 9.404   -28.274 17.253  1.00 35.54 ? 284 ARG A NE  1 
ATOM   1862 C  CZ  . ARG A 1 249 ? 8.573   -28.146 16.232  1.00 35.55 ? 284 ARG A CZ  1 
ATOM   1863 N  NH1 . ARG A 1 249 ? 8.497   -27.021 15.543  1.00 35.11 ? 284 ARG A NH1 1 
ATOM   1864 N  NH2 . ARG A 1 249 ? 7.784   -29.168 15.908  1.00 33.13 ? 284 ARG A NH2 1 
ATOM   1865 N  N   . LYS A 1 250 ? 9.862   -24.977 21.804  1.00 23.06 ? 285 LYS A N   1 
ATOM   1866 C  CA  . LYS A 1 250 ? 10.759  -23.921 22.259  1.00 27.39 ? 285 LYS A CA  1 
ATOM   1867 C  C   . LYS A 1 250 ? 11.122  -24.109 23.722  1.00 24.45 ? 285 LYS A C   1 
ATOM   1868 O  O   . LYS A 1 250 ? 12.281  -23.920 24.107  1.00 29.02 ? 285 LYS A O   1 
ATOM   1869 C  CB  . LYS A 1 250 ? 10.186  -22.532 21.973  1.00 29.18 ? 285 LYS A CB  1 
ATOM   1870 C  CG  . LYS A 1 250 ? 10.065  -22.246 20.483  1.00 40.83 ? 285 LYS A CG  1 
ATOM   1871 C  CD  . LYS A 1 250 ? 9.376   -20.926 20.204  1.00 54.13 ? 285 LYS A CD  1 
ATOM   1872 C  CE  . LYS A 1 250 ? 8.487   -21.029 18.973  1.00 55.96 ? 285 LYS A CE  1 
ATOM   1873 N  NZ  . LYS A 1 250 ? 7.851   -19.720 18.637  1.00 57.81 ? 285 LYS A NZ  1 
ATOM   1874 N  N   . LYS A 1 251 ? 10.153  -24.518 24.545  1.00 26.42 ? 286 LYS A N   1 
ATOM   1875 C  CA  . LYS A 1 251 ? 10.421  -24.754 25.958  1.00 29.62 ? 286 LYS A CA  1 
ATOM   1876 C  C   . LYS A 1 251 ? 11.464  -25.855 26.141  1.00 23.88 ? 286 LYS A C   1 
ATOM   1877 O  O   . LYS A 1 251 ? 12.412  -25.708 26.926  1.00 27.60 ? 286 LYS A O   1 
ATOM   1878 C  CB  . LYS A 1 251 ? 9.110   -25.121 26.653  1.00 27.28 ? 286 LYS A CB  1 
ATOM   1879 C  CG  . LYS A 1 251 ? 9.204   -25.298 28.151  1.00 34.26 ? 286 LYS A CG  1 
ATOM   1880 C  CD  . LYS A 1 251 ? 7.825   -25.575 28.744  1.00 40.29 ? 286 LYS A CD  1 
ATOM   1881 C  CE  . LYS A 1 251 ? 6.783   -24.604 28.201  1.00 37.42 ? 286 LYS A CE  1 
ATOM   1882 N  NZ  . LYS A 1 251 ? 5.397   -24.953 28.642  1.00 47.67 ? 286 LYS A NZ  1 
ATOM   1883 N  N   . ALA A 1 252 ? 11.317  -26.956 25.401  1.00 26.60 ? 287 ALA A N   1 
ATOM   1884 C  CA  . ALA A 1 252 ? 12.254  -28.068 25.526  1.00 20.91 ? 287 ALA A CA  1 
ATOM   1885 C  C   . ALA A 1 252 ? 13.647  -27.668 25.066  1.00 22.05 ? 287 ALA A C   1 
ATOM   1886 O  O   . ALA A 1 252 ? 14.644  -27.971 25.737  1.00 25.39 ? 287 ALA A O   1 
ATOM   1887 C  CB  . ALA A 1 252 ? 11.748  -29.268 24.724  1.00 26.97 ? 287 ALA A CB  1 
ATOM   1888 N  N   . PHE A 1 253 ? 13.737  -26.983 23.922  1.00 24.66 ? 288 PHE A N   1 
ATOM   1889 C  CA  . PHE A 1 253 ? 15.040  -26.559 23.420  1.00 22.58 ? 288 PHE A CA  1 
ATOM   1890 C  C   . PHE A 1 253 ? 15.704  -25.574 24.370  1.00 23.51 ? 288 PHE A C   1 
ATOM   1891 O  O   . PHE A 1 253 ? 16.906  -25.679 24.641  1.00 27.07 ? 288 PHE A O   1 
ATOM   1892 C  CB  . PHE A 1 253 ? 14.906  -25.950 22.024  1.00 23.89 ? 288 PHE A CB  1 
ATOM   1893 C  CG  . PHE A 1 253 ? 14.574  -26.946 20.949  1.00 24.22 ? 288 PHE A CG  1 
ATOM   1894 C  CD1 . PHE A 1 253 ? 14.471  -28.299 21.236  1.00 22.14 ? 288 PHE A CD1 1 
ATOM   1895 C  CD2 . PHE A 1 253 ? 14.373  -26.526 19.642  1.00 25.53 ? 288 PHE A CD2 1 
ATOM   1896 C  CE1 . PHE A 1 253 ? 14.165  -29.216 20.239  1.00 25.51 ? 288 PHE A CE1 1 
ATOM   1897 C  CE2 . PHE A 1 253 ? 14.071  -27.436 18.641  1.00 21.98 ? 288 PHE A CE2 1 
ATOM   1898 C  CZ  . PHE A 1 253 ? 13.967  -28.787 18.943  1.00 22.90 ? 288 PHE A CZ  1 
ATOM   1899 N  N   . ALA A 1 254 ? 14.946  -24.604 24.882  1.00 23.37 ? 289 ALA A N   1 
ATOM   1900 C  CA  . ALA A 1 254 ? 15.525  -23.637 25.801  1.00 27.23 ? 289 ALA A CA  1 
ATOM   1901 C  C   . ALA A 1 254 ? 16.009  -24.318 27.070  1.00 28.78 ? 289 ALA A C   1 
ATOM   1902 O  O   . ALA A 1 254 ? 17.091  -23.998 27.577  1.00 31.46 ? 289 ALA A O   1 
ATOM   1903 C  CB  . ALA A 1 254 ? 14.518  -22.530 26.119  1.00 26.75 ? 289 ALA A CB  1 
ATOM   1904 N  N   . ASP A 1 255 ? 15.233  -25.276 27.588  1.00 24.38 ? 290 ASP A N   1 
ATOM   1905 C  CA  . ASP A 1 255 ? 15.630  -25.942 28.825  1.00 30.82 ? 290 ASP A CA  1 
ATOM   1906 C  C   . ASP A 1 255 ? 16.874  -26.796 28.622  1.00 23.36 ? 290 ASP A C   1 
ATOM   1907 O  O   . ASP A 1 255 ? 17.785  -26.785 29.463  1.00 29.47 ? 290 ASP A O   1 
ATOM   1908 C  CB  . ASP A 1 255 ? 14.487  -26.788 29.379  1.00 27.69 ? 290 ASP A CB  1 
ATOM   1909 C  CG  . ASP A 1 255 ? 14.706  -27.161 30.835  1.00 40.44 ? 290 ASP A CG  1 
ATOM   1910 O  OD1 . ASP A 1 255 ? 14.482  -26.295 31.705  1.00 43.70 ? 290 ASP A OD1 1 
ATOM   1911 O  OD2 . ASP A 1 255 ? 15.125  -28.308 31.105  1.00 39.43 ? 290 ASP A OD2 1 
ATOM   1912 N  N   . ALA A 1 256 ? 16.944  -27.518 27.505  1.00 23.94 ? 291 ALA A N   1 
ATOM   1913 C  CA  . ALA A 1 256 ? 18.120  -28.337 27.234  1.00 25.22 ? 291 ALA A CA  1 
ATOM   1914 C  C   . ALA A 1 256 ? 19.351  -27.491 26.921  1.00 28.06 ? 291 ALA A C   1 
ATOM   1915 O  O   . ALA A 1 256 ? 20.472  -27.882 27.265  1.00 25.96 ? 291 ALA A O   1 
ATOM   1916 C  CB  . ALA A 1 256 ? 17.829  -29.308 26.104  1.00 23.06 ? 291 ALA A CB  1 
ATOM   1917 N  N   . ALA A 1 257 ? 19.172  -26.343 26.264  1.00 23.45 ? 292 ALA A N   1 
ATOM   1918 C  CA  . ALA A 1 257 ? 20.293  -25.431 26.076  1.00 32.09 ? 292 ALA A CA  1 
ATOM   1919 C  C   . ALA A 1 257 ? 20.778  -24.868 27.406  1.00 28.19 ? 292 ALA A C   1 
ATOM   1920 O  O   . ALA A 1 257 ? 21.988  -24.777 27.643  1.00 28.32 ? 292 ALA A O   1 
ATOM   1921 C  CB  . ALA A 1 257 ? 19.896  -24.304 25.122  1.00 30.61 ? 292 ALA A CB  1 
ATOM   1922 N  N   . LYS A 1 258 ? 19.849  -24.486 28.286  1.00 30.96 ? 293 LYS A N   1 
ATOM   1923 C  CA  . LYS A 1 258 ? 20.227  -23.906 29.569  1.00 28.09 ? 293 LYS A CA  1 
ATOM   1924 C  C   . LYS A 1 258 ? 20.917  -24.928 30.465  1.00 34.70 ? 293 LYS A C   1 
ATOM   1925 O  O   . LYS A 1 258 ? 21.918  -24.612 31.119  1.00 34.14 ? 293 LYS A O   1 
ATOM   1926 C  CB  . LYS A 1 258 ? 18.985  -23.329 30.254  1.00 30.12 ? 293 LYS A CB  1 
ATOM   1927 C  CG  . LYS A 1 258 ? 19.181  -22.909 31.702  1.00 38.89 ? 293 LYS A CG  1 
ATOM   1928 C  CD  . LYS A 1 258 ? 17.832  -22.838 32.431  1.00 42.39 ? 293 LYS A CD  1 
ATOM   1929 C  CE  . LYS A 1 258 ? 17.863  -21.858 33.597  1.00 47.49 ? 293 LYS A CE  1 
ATOM   1930 N  NZ  . LYS A 1 258 ? 16.716  -22.069 34.526  1.00 50.47 ? 293 LYS A NZ  1 
ATOM   1931 N  N   . GLY A 1 259 ? 20.397  -26.154 30.510  1.00 30.32 ? 294 GLY A N   1 
ATOM   1932 C  CA  . GLY A 1 259 ? 20.912  -27.179 31.399  1.00 31.40 ? 294 GLY A CA  1 
ATOM   1933 C  C   . GLY A 1 259 ? 22.081  -27.961 30.833  1.00 26.78 ? 294 GLY A C   1 
ATOM   1934 O  O   . GLY A 1 259 ? 22.797  -28.640 31.576  1.00 31.53 ? 294 GLY A O   1 
ATOM   1935 N  N   . GLY A 1 260 ? 22.294  -27.863 29.522  1.00 25.75 ? 295 GLY A N   1 
ATOM   1936 C  CA  . GLY A 1 260 ? 23.400  -28.561 28.893  1.00 30.73 ? 295 GLY A CA  1 
ATOM   1937 C  C   . GLY A 1 260 ? 23.295  -30.073 28.870  1.00 30.38 ? 295 GLY A C   1 
ATOM   1938 O  O   . GLY A 1 260 ? 24.321  -30.746 28.754  1.00 30.18 ? 295 GLY A O   1 
ATOM   1939 N  N   . TYR A 1 261 ? 22.092  -30.634 28.984  1.00 26.83 ? 296 TYR A N   1 
ATOM   1940 C  CA  . TYR A 1 261 ? 21.922  -32.080 29.015  1.00 28.22 ? 296 TYR A CA  1 
ATOM   1941 C  C   . TYR A 1 261 ? 21.550  -32.624 27.634  1.00 26.13 ? 296 TYR A C   1 
ATOM   1942 O  O   . TYR A 1 261 ? 21.346  -31.879 26.673  1.00 25.00 ? 296 TYR A O   1 
ATOM   1943 C  CB  . TYR A 1 261 ? 20.894  -32.489 30.071  1.00 22.03 ? 296 TYR A CB  1 
ATOM   1944 C  CG  . TYR A 1 261 ? 19.533  -31.850 29.907  1.00 21.97 ? 296 TYR A CG  1 
ATOM   1945 C  CD1 . TYR A 1 261 ? 18.606  -32.369 29.011  1.00 25.33 ? 296 TYR A CD1 1 
ATOM   1946 C  CD2 . TYR A 1 261 ? 19.160  -30.751 30.673  1.00 23.71 ? 296 TYR A CD2 1 
ATOM   1947 C  CE1 . TYR A 1 261 ? 17.352  -31.805 28.861  1.00 25.22 ? 296 TYR A CE1 1 
ATOM   1948 C  CE2 . TYR A 1 261 ? 17.898  -30.178 30.533  1.00 28.28 ? 296 TYR A CE2 1 
ATOM   1949 C  CZ  . TYR A 1 261 ? 17.001  -30.714 29.624  1.00 28.52 ? 296 TYR A CZ  1 
ATOM   1950 O  OH  . TYR A 1 261 ? 15.747  -30.168 29.466  1.00 27.50 ? 296 TYR A OH  1 
ATOM   1951 N  N   . LEU A 1 262 ? 21.444  -33.948 27.546  1.00 21.99 ? 297 LEU A N   1 
ATOM   1952 C  CA  . LEU A 1 262 ? 21.157  -34.606 26.282  1.00 21.00 ? 297 LEU A CA  1 
ATOM   1953 C  C   . LEU A 1 262 ? 19.666  -34.635 25.996  1.00 22.43 ? 297 LEU A C   1 
ATOM   1954 O  O   . LEU A 1 262 ? 18.832  -34.737 26.902  1.00 20.97 ? 297 LEU A O   1 
ATOM   1955 C  CB  . LEU A 1 262 ? 21.649  -36.048 26.303  1.00 25.66 ? 297 LEU A CB  1 
ATOM   1956 C  CG  . LEU A 1 262 ? 23.157  -36.234 26.357  1.00 24.93 ? 297 LEU A CG  1 
ATOM   1957 C  CD1 . LEU A 1 262 ? 23.491  -37.684 26.642  1.00 29.60 ? 297 LEU A CD1 1 
ATOM   1958 C  CD2 . LEU A 1 262 ? 23.745  -35.800 25.041  1.00 20.14 ? 297 LEU A CD2 1 
ATOM   1959 N  N   . ILE A 1 263 ? 19.341  -34.583 24.708  1.00 18.07 ? 298 ILE A N   1 
ATOM   1960 C  CA  . ILE A 1 263 ? 17.997  -34.832 24.226  1.00 16.58 ? 298 ILE A CA  1 
ATOM   1961 C  C   . ILE A 1 263 ? 18.076  -35.934 23.180  1.00 25.09 ? 298 ILE A C   1 
ATOM   1962 O  O   . ILE A 1 263 ? 19.138  -36.228 22.616  1.00 21.03 ? 298 ILE A O   1 
ATOM   1963 C  CB  . ILE A 1 263 ? 17.346  -33.566 23.634  1.00 22.24 ? 298 ILE A CB  1 
ATOM   1964 C  CG1 . ILE A 1 263 ? 18.151  -33.083 22.423  1.00 26.33 ? 298 ILE A CG1 1 
ATOM   1965 C  CG2 . ILE A 1 263 ? 17.251  -32.487 24.698  1.00 20.95 ? 298 ILE A CG2 1 
ATOM   1966 C  CD1 . ILE A 1 263 ? 17.402  -32.148 21.506  1.00 35.06 ? 298 ILE A CD1 1 
ATOM   1967 N  N   . ALA A 1 264 ? 16.936  -36.567 22.947  1.00 18.33 ? 299 ALA A N   1 
ATOM   1968 C  CA  . ALA A 1 264 ? 16.787  -37.492 21.837  1.00 17.96 ? 299 ALA A CA  1 
ATOM   1969 C  C   . ALA A 1 264 ? 15.379  -37.350 21.282  1.00 21.82 ? 299 ALA A C   1 
ATOM   1970 O  O   . ALA A 1 264 ? 14.458  -36.941 21.994  1.00 20.48 ? 299 ALA A O   1 
ATOM   1971 C  CB  . ALA A 1 264 ? 17.063  -38.944 22.246  1.00 19.61 ? 299 ALA A CB  1 
ATOM   1972 N  N   . ALA A 1 265 ? 15.220  -37.663 19.999  1.00 15.47 ? 300 ALA A N   1 
ATOM   1973 C  CA  . ALA A 1 265 ? 13.901  -37.607 19.390  1.00 18.32 ? 300 ALA A CA  1 
ATOM   1974 C  C   . ALA A 1 265 ? 13.807  -38.671 18.313  1.00 19.06 ? 300 ALA A C   1 
ATOM   1975 O  O   . ALA A 1 265 ? 14.796  -38.992 17.644  1.00 19.18 ? 300 ALA A O   1 
ATOM   1976 C  CB  . ALA A 1 265 ? 13.581  -36.219 18.820  1.00 19.86 ? 300 ALA A CB  1 
ATOM   1977 N  N   . SER A 1 266 ? 12.584  -39.174 18.127  1.00 14.23 ? 301 SER A N   1 
ATOM   1978 C  CA  . SER A 1 266 ? 12.364  -40.375 17.330  1.00 16.09 ? 301 SER A CA  1 
ATOM   1979 C  C   . SER A 1 266 ? 12.806  -40.202 15.890  1.00 16.01 ? 301 SER A C   1 
ATOM   1980 O  O   . SER A 1 266 ? 13.192  -41.180 15.242  1.00 18.45 ? 301 SER A O   1 
ATOM   1981 C  CB  . SER A 1 266 ? 10.877  -40.722 17.337  1.00 23.15 ? 301 SER A CB  1 
ATOM   1982 O  OG  . SER A 1 266 ? 10.392  -40.802 18.663  1.00 44.95 ? 301 SER A OG  1 
ATOM   1983 N  N   . HIS A 1 267 ? 12.721  -38.988 15.358  1.00 14.56 ? 302 HIS A N   1 
ATOM   1984 C  CA  . HIS A 1 267 ? 12.987  -38.760 13.946  1.00 15.40 ? 302 HIS A CA  1 
ATOM   1985 C  C   . HIS A 1 267 ? 14.211  -37.910 13.689  1.00 14.63 ? 302 HIS A C   1 
ATOM   1986 O  O   . HIS A 1 267 ? 14.422  -37.486 12.546  1.00 16.99 ? 302 HIS A O   1 
ATOM   1987 C  CB  . HIS A 1 267 ? 11.762  -38.169 13.267  1.00 18.39 ? 302 HIS A CB  1 
ATOM   1988 C  CG  . HIS A 1 267 ? 10.557  -39.019 13.439  1.00 15.14 ? 302 HIS A CG  1 
ATOM   1989 N  ND1 . HIS A 1 267 ? 10.549  -40.358 13.113  1.00 16.51 ? 302 HIS A ND1 1 
ATOM   1990 C  CD2 . HIS A 1 267 ? 9.350   -38.752 13.983  1.00 16.90 ? 302 HIS A CD2 1 
ATOM   1991 C  CE1 . HIS A 1 267 ? 9.373   -40.872 13.409  1.00 26.00 ? 302 HIS A CE1 1 
ATOM   1992 N  NE2 . HIS A 1 267 ? 8.635   -39.920 13.944  1.00 13.97 ? 302 HIS A NE2 1 
ATOM   1993 N  N   . LEU A 1 268 ? 15.013  -37.641 14.711  1.00 14.06 ? 303 LEU A N   1 
ATOM   1994 C  CA  . LEU A 1 268 ? 16.345  -37.143 14.435  1.00 15.80 ? 303 LEU A CA  1 
ATOM   1995 C  C   . LEU A 1 268 ? 17.152  -38.278 13.808  1.00 15.38 ? 303 LEU A C   1 
ATOM   1996 O  O   . LEU A 1 268 ? 16.831  -39.454 14.003  1.00 15.66 ? 303 LEU A O   1 
ATOM   1997 C  CB  . LEU A 1 268 ? 17.015  -36.648 15.714  1.00 16.86 ? 303 LEU A CB  1 
ATOM   1998 C  CG  . LEU A 1 268 ? 16.291  -35.432 16.307  1.00 17.94 ? 303 LEU A CG  1 
ATOM   1999 C  CD1 . LEU A 1 268 ? 16.946  -34.986 17.604  1.00 18.99 ? 303 LEU A CD1 1 
ATOM   2000 C  CD2 . LEU A 1 268 ? 16.213  -34.271 15.310  1.00 23.54 ? 303 LEU A CD2 1 
ATOM   2001 N  N   . PRO A 1 269 ? 18.163  -37.962 13.004  1.00 17.10 ? 304 PRO A N   1 
ATOM   2002 C  CA  . PRO A 1 269 ? 18.917  -39.037 12.350  1.00 17.49 ? 304 PRO A CA  1 
ATOM   2003 C  C   . PRO A 1 269 ? 19.493  -39.983 13.393  1.00 15.57 ? 304 PRO A C   1 
ATOM   2004 O  O   . PRO A 1 269 ? 20.137  -39.550 14.352  1.00 16.17 ? 304 PRO A O   1 
ATOM   2005 C  CB  . PRO A 1 269 ? 20.025  -38.283 11.608  1.00 16.78 ? 304 PRO A CB  1 
ATOM   2006 C  CG  . PRO A 1 269 ? 19.433  -36.913 11.352  1.00 22.19 ? 304 PRO A CG  1 
ATOM   2007 C  CD  . PRO A 1 269 ? 18.613  -36.621 12.583  1.00 20.11 ? 304 PRO A CD  1 
ATOM   2008 N  N   . PHE A 1 270 ? 19.287  -41.284 13.169  1.00 16.72 ? 305 PHE A N   1 
ATOM   2009 C  CA  . PHE A 1 270 ? 19.677  -42.307 14.130  1.00 15.60 ? 305 PHE A CA  1 
ATOM   2010 C  C   . PHE A 1 270 ? 21.147  -42.139 14.515  1.00 18.00 ? 305 PHE A C   1 
ATOM   2011 O  O   . PHE A 1 270 ? 21.999  -41.933 13.639  1.00 17.16 ? 305 PHE A O   1 
ATOM   2012 C  CB  . PHE A 1 270 ? 19.456  -43.695 13.515  1.00 18.43 ? 305 PHE A CB  1 
ATOM   2013 C  CG  . PHE A 1 270 ? 19.766  -44.829 14.451  1.00 19.77 ? 305 PHE A CG  1 
ATOM   2014 C  CD1 . PHE A 1 270 ? 18.871  -45.191 15.451  1.00 18.12 ? 305 PHE A CD1 1 
ATOM   2015 C  CD2 . PHE A 1 270 ? 20.964  -45.522 14.343  1.00 18.99 ? 305 PHE A CD2 1 
ATOM   2016 C  CE1 . PHE A 1 270 ? 19.165  -46.230 16.327  1.00 21.12 ? 305 PHE A CE1 1 
ATOM   2017 C  CE2 . PHE A 1 270 ? 21.264  -46.565 15.221  1.00 22.24 ? 305 PHE A CE2 1 
ATOM   2018 C  CZ  . PHE A 1 270 ? 20.366  -46.917 16.208  1.00 19.03 ? 305 PHE A CZ  1 
ATOM   2019 N  N   . PRO A 1 271 ? 21.489  -42.234 15.812  1.00 18.75 ? 306 PRO A N   1 
ATOM   2020 C  CA  . PRO A 1 271 ? 20.639  -42.622 16.955  1.00 18.19 ? 306 PRO A CA  1 
ATOM   2021 C  C   . PRO A 1 271 ? 19.792  -41.486 17.524  1.00 18.42 ? 306 PRO A C   1 
ATOM   2022 O  O   . PRO A 1 271 ? 19.028  -41.684 18.472  1.00 17.60 ? 306 PRO A O   1 
ATOM   2023 C  CB  . PRO A 1 271 ? 21.668  -43.088 17.992  1.00 19.04 ? 306 PRO A CB  1 
ATOM   2024 C  CG  . PRO A 1 271 ? 22.879  -42.233 17.707  1.00 21.17 ? 306 PRO A CG  1 
ATOM   2025 C  CD  . PRO A 1 271 ? 22.905  -42.078 16.207  1.00 19.50 ? 306 PRO A CD  1 
ATOM   2026 N  N   . GLY A 1 272 ? 19.930  -40.281 16.976  1.00 16.54 ? 307 GLY A N   1 
ATOM   2027 C  CA  . GLY A 1 272 ? 19.070  -39.172 17.349  1.00 16.37 ? 307 GLY A CA  1 
ATOM   2028 C  C   . GLY A 1 272 ? 19.322  -38.572 18.715  1.00 15.55 ? 307 GLY A C   1 
ATOM   2029 O  O   . GLY A 1 272 ? 18.406  -37.981 19.292  1.00 20.73 ? 307 GLY A O   1 
ATOM   2030 N  N   . ILE A 1 273 ? 20.529  -38.717 19.260  1.00 16.75 ? 308 ILE A N   1 
ATOM   2031 C  CA  . ILE A 1 273 ? 20.867  -38.245 20.599  1.00 18.16 ? 308 ILE A CA  1 
ATOM   2032 C  C   . ILE A 1 273 ? 21.900  -37.133 20.476  1.00 20.18 ? 308 ILE A C   1 
ATOM   2033 O  O   . ILE A 1 273 ? 22.864  -37.257 19.709  1.00 19.33 ? 308 ILE A O   1 
ATOM   2034 C  CB  . ILE A 1 273 ? 21.429  -39.398 21.453  1.00 20.34 ? 308 ILE A CB  1 
ATOM   2035 C  CG1 . ILE A 1 273 ? 20.422  -40.544 21.546  1.00 19.64 ? 308 ILE A CG1 1 
ATOM   2036 C  CG2 . ILE A 1 273 ? 21.782  -38.908 22.853  1.00 25.54 ? 308 ILE A CG2 1 
ATOM   2037 C  CD1 . ILE A 1 273 ? 21.069  -41.856 21.938  1.00 21.77 ? 308 ILE A CD1 1 
ATOM   2038 N  N   . GLY A 1 274 ? 21.713  -36.053 21.228  1.00 20.44 ? 309 GLY A N   1 
ATOM   2039 C  CA  . GLY A 1 274 ? 22.701  -34.987 21.196  1.00 20.98 ? 309 GLY A CA  1 
ATOM   2040 C  C   . GLY A 1 274 ? 22.385  -33.894 22.195  1.00 22.31 ? 309 GLY A C   1 
ATOM   2041 O  O   . GLY A 1 274 ? 21.400  -33.953 22.939  1.00 21.32 ? 309 GLY A O   1 
ATOM   2042 N  N   . HIS A 1 275 ? 23.268  -32.904 22.220  1.00 18.99 ? 310 HIS A N   1 
ATOM   2043 C  CA  . HIS A 1 275 ? 23.073  -31.686 22.986  1.00 19.82 ? 310 HIS A CA  1 
ATOM   2044 C  C   . HIS A 1 275 ? 22.463  -30.613 22.089  1.00 20.81 ? 310 HIS A C   1 
ATOM   2045 O  O   . HIS A 1 275 ? 22.323  -30.781 20.876  1.00 22.85 ? 310 HIS A O   1 
ATOM   2046 C  CB  . HIS A 1 275 ? 24.399  -31.183 23.558  1.00 21.43 ? 310 HIS A CB  1 
ATOM   2047 C  CG  . HIS A 1 275 ? 24.978  -32.053 24.627  1.00 24.31 ? 310 HIS A CG  1 
ATOM   2048 N  ND1 . HIS A 1 275 ? 25.921  -33.024 24.370  1.00 25.90 ? 310 HIS A ND1 1 
ATOM   2049 C  CD2 . HIS A 1 275 ? 24.752  -32.091 25.962  1.00 24.53 ? 310 HIS A CD2 1 
ATOM   2050 C  CE1 . HIS A 1 275 ? 26.258  -33.616 25.502  1.00 27.71 ? 310 HIS A CE1 1 
ATOM   2051 N  NE2 . HIS A 1 275 ? 25.561  -33.071 26.483  1.00 26.47 ? 310 HIS A NE2 1 
ATOM   2052 N  N   . ILE A 1 276 ? 22.127  -29.473 22.682  1.00 21.58 ? 311 ILE A N   1 
ATOM   2053 C  CA  . ILE A 1 276 ? 21.565  -28.371 21.911  1.00 22.24 ? 311 ILE A CA  1 
ATOM   2054 C  C   . ILE A 1 276 ? 22.075  -27.054 22.485  1.00 22.22 ? 311 ILE A C   1 
ATOM   2055 O  O   . ILE A 1 276 ? 22.191  -26.899 23.706  1.00 24.36 ? 311 ILE A O   1 
ATOM   2056 C  CB  . ILE A 1 276 ? 20.026  -28.465 21.890  1.00 33.96 ? 311 ILE A CB  1 
ATOM   2057 C  CG1 . ILE A 1 276 ? 19.399  -27.358 21.048  1.00 30.90 ? 311 ILE A CG1 1 
ATOM   2058 C  CG2 . ILE A 1 276 ? 19.487  -28.400 23.284  1.00 38.21 ? 311 ILE A CG2 1 
ATOM   2059 C  CD1 . ILE A 1 276 ? 17.941  -27.638 20.754  1.00 36.37 ? 311 ILE A CD1 1 
ATOM   2060 N  N   . ARG A 1 277 ? 22.421  -26.111 21.606  1.00 21.19 ? 312 ARG A N   1 
ATOM   2061 C  CA  . ARG A 1 277 ? 22.801  -24.775 22.051  1.00 26.87 ? 312 ARG A CA  1 
ATOM   2062 C  C   . ARG A 1 277 ? 21.993  -23.718 21.314  1.00 28.87 ? 312 ARG A C   1 
ATOM   2063 O  O   . ARG A 1 277 ? 21.594  -23.912 20.167  1.00 28.82 ? 312 ARG A O   1 
ATOM   2064 C  CB  . ARG A 1 277 ? 24.318  -24.496 21.973  1.00 34.60 ? 312 ARG A CB  1 
ATOM   2065 C  CG  . ARG A 1 277 ? 25.065  -25.115 20.807  1.00 39.08 ? 312 ARG A CG  1 
ATOM   2066 C  CD  . ARG A 1 277 ? 26.472  -24.511 20.747  1.00 43.24 ? 312 ARG A CD  1 
ATOM   2067 N  NE  . ARG A 1 277 ? 26.966  -24.287 19.392  1.00 54.39 ? 312 ARG A NE  1 
ATOM   2068 C  CZ  . ARG A 1 277 ? 27.647  -25.177 18.679  1.00 71.41 ? 312 ARG A CZ  1 
ATOM   2069 N  NH1 . ARG A 1 277 ? 27.962  -26.364 19.172  1.00 46.27 ? 312 ARG A NH1 1 
ATOM   2070 N  NH2 . ARG A 1 277 ? 28.044  -24.858 17.450  1.00 62.43 ? 312 ARG A NH2 1 
ATOM   2071 N  N   . ALA A 1 278 ? 21.730  -22.606 21.995  1.00 26.06 ? 313 ALA A N   1 
ATOM   2072 C  CA  . ALA A 1 278 ? 20.910  -21.545 21.421  1.00 41.17 ? 313 ALA A CA  1 
ATOM   2073 C  C   . ALA A 1 278 ? 21.765  -20.673 20.516  1.00 40.81 ? 313 ALA A C   1 
ATOM   2074 O  O   . ALA A 1 278 ? 22.846  -20.229 20.915  1.00 40.84 ? 313 ALA A O   1 
ATOM   2075 C  CB  . ALA A 1 278 ? 20.284  -20.695 22.526  1.00 37.65 ? 313 ALA A CB  1 
ATOM   2076 N  N   . GLU A 1 279 ? 21.277  -20.421 19.299  1.00 35.04 ? 314 GLU A N   1 
ATOM   2077 C  CA  . GLU A 1 279 ? 22.071  -19.752 18.270  1.00 38.65 ? 314 GLU A CA  1 
ATOM   2078 C  C   . GLU A 1 279 ? 21.132  -18.927 17.405  1.00 35.93 ? 314 GLU A C   1 
ATOM   2079 O  O   . GLU A 1 279 ? 20.191  -19.477 16.820  1.00 43.39 ? 314 GLU A O   1 
ATOM   2080 C  CB  . GLU A 1 279 ? 22.787  -20.796 17.412  1.00 35.54 ? 314 GLU A CB  1 
ATOM   2081 C  CG  . GLU A 1 279 ? 23.998  -21.427 18.077  1.00 50.17 ? 314 GLU A CG  1 
ATOM   2082 C  CD  . GLU A 1 279 ? 25.042  -21.885 17.079  1.00 58.28 ? 314 GLU A CD  1 
ATOM   2083 O  OE1 . GLU A 1 279 ? 24.811  -21.732 15.859  1.00 53.11 ? 314 GLU A OE1 1 
ATOM   2084 O  OE2 . GLU A 1 279 ? 26.096  -22.396 17.517  1.00 61.23 ? 314 GLU A OE2 1 
ATOM   2085 N  N   . GLY A 1 280 ? 21.389  -17.625 17.318  1.00 37.67 ? 315 GLY A N   1 
ATOM   2086 C  CA  . GLY A 1 280 ? 20.515  -16.754 16.552  1.00 39.46 ? 315 GLY A CA  1 
ATOM   2087 C  C   . GLY A 1 280 ? 19.080  -16.865 17.014  1.00 45.99 ? 315 GLY A C   1 
ATOM   2088 O  O   . GLY A 1 280 ? 18.789  -16.921 18.212  1.00 50.83 ? 315 GLY A O   1 
ATOM   2089 N  N   . LYS A 1 281 ? 18.163  -16.939 16.051  1.00 43.63 ? 316 LYS A N   1 
ATOM   2090 C  CA  . LYS A 1 281 ? 16.748  -17.090 16.360  1.00 34.21 ? 316 LYS A CA  1 
ATOM   2091 C  C   . LYS A 1 281 ? 16.360  -18.526 16.685  1.00 38.20 ? 316 LYS A C   1 
ATOM   2092 O  O   . LYS A 1 281 ? 15.193  -18.780 17.005  1.00 52.21 ? 316 LYS A O   1 
ATOM   2093 C  CB  . LYS A 1 281 ? 15.892  -16.568 15.202  1.00 39.63 ? 316 LYS A CB  1 
ATOM   2094 C  CG  . LYS A 1 281 ? 16.368  -15.248 14.621  1.00 52.97 ? 316 LYS A CG  1 
ATOM   2095 C  CD  . LYS A 1 281 ? 15.225  -14.250 14.526  1.00 54.54 ? 316 LYS A CD  1 
ATOM   2096 C  CE  . LYS A 1 281 ? 14.641  -14.221 13.124  1.00 58.40 ? 316 LYS A CE  1 
ATOM   2097 N  NZ  . LYS A 1 281 ? 13.417  -13.379 13.056  1.00 62.77 ? 316 LYS A NZ  1 
ATOM   2098 N  N   . GLY A 1 282 ? 17.294  -19.469 16.618  1.00 31.95 ? 317 GLY A N   1 
ATOM   2099 C  CA  . GLY A 1 282 ? 16.945  -20.846 16.887  1.00 29.60 ? 317 GLY A CA  1 
ATOM   2100 C  C   . GLY A 1 282 ? 17.982  -21.589 17.698  1.00 30.61 ? 317 GLY A C   1 
ATOM   2101 O  O   . GLY A 1 282 ? 18.530  -21.058 18.669  1.00 30.63 ? 317 GLY A O   1 
ATOM   2102 N  N   . TYR A 1 283 ? 18.267  -22.824 17.293  1.00 26.63 ? 318 TYR A N   1 
ATOM   2103 C  CA  . TYR A 1 283 ? 19.136  -23.711 18.047  1.00 25.98 ? 318 TYR A CA  1 
ATOM   2104 C  C   . TYR A 1 283 ? 19.982  -24.530 17.085  1.00 28.63 ? 318 TYR A C   1 
ATOM   2105 O  O   . TYR A 1 283 ? 19.655  -24.690 15.907  1.00 27.70 ? 318 TYR A O   1 
ATOM   2106 C  CB  . TYR A 1 283 ? 18.315  -24.639 18.957  1.00 24.87 ? 318 TYR A CB  1 
ATOM   2107 C  CG  . TYR A 1 283 ? 17.526  -23.879 20.003  1.00 22.75 ? 318 TYR A CG  1 
ATOM   2108 C  CD1 . TYR A 1 283 ? 16.269  -23.362 19.712  1.00 23.93 ? 318 TYR A CD1 1 
ATOM   2109 C  CD2 . TYR A 1 283 ? 18.049  -23.658 21.271  1.00 27.35 ? 318 TYR A CD2 1 
ATOM   2110 C  CE1 . TYR A 1 283 ? 15.556  -22.643 20.653  1.00 26.54 ? 318 TYR A CE1 1 
ATOM   2111 C  CE2 . TYR A 1 283 ? 17.339  -22.940 22.223  1.00 28.23 ? 318 TYR A CE2 1 
ATOM   2112 C  CZ  . TYR A 1 283 ? 16.089  -22.441 21.907  1.00 27.33 ? 318 TYR A CZ  1 
ATOM   2113 O  OH  . TYR A 1 283 ? 15.365  -21.725 22.841  1.00 32.02 ? 318 TYR A OH  1 
ATOM   2114 N  N   . ARG A 1 284 ? 21.090  -25.037 17.607  1.00 26.44 ? 319 ARG A N   1 
ATOM   2115 C  CA  . ARG A 1 284 ? 21.958  -25.957 16.894  1.00 28.31 ? 319 ARG A CA  1 
ATOM   2116 C  C   . ARG A 1 284 ? 21.992  -27.260 17.673  1.00 33.06 ? 319 ARG A C   1 
ATOM   2117 O  O   . ARG A 1 284 ? 22.258  -27.260 18.883  1.00 28.30 ? 319 ARG A O   1 
ATOM   2118 C  CB  . ARG A 1 284 ? 23.379  -25.405 16.761  1.00 33.16 ? 319 ARG A CB  1 
ATOM   2119 C  CG  . ARG A 1 284 ? 24.365  -26.417 16.192  1.00 35.55 ? 319 ARG A CG  1 
ATOM   2120 C  CD  . ARG A 1 284 ? 25.621  -25.763 15.646  1.00 49.47 ? 319 ARG A CD  1 
ATOM   2121 N  NE  . ARG A 1 284 ? 25.368  -24.842 14.543  1.00 75.08 ? 319 ARG A NE  1 
ATOM   2122 C  CZ  . ARG A 1 284 ? 24.977  -25.205 13.328  1.00 67.08 ? 319 ARG A CZ  1 
ATOM   2123 N  NH1 . ARG A 1 284 ? 24.765  -26.475 13.019  1.00 66.05 ? 319 ARG A NH1 1 
ATOM   2124 N  NH2 . ARG A 1 284 ? 24.803  -24.271 12.397  1.00 65.33 ? 319 ARG A NH2 1 
ATOM   2125 N  N   . PHE A 1 285 ? 21.704  -28.358 16.977  1.00 24.50 ? 320 PHE A N   1 
ATOM   2126 C  CA  . PHE A 1 285 ? 21.783  -29.698 17.534  1.00 22.95 ? 320 PHE A CA  1 
ATOM   2127 C  C   . PHE A 1 285 ? 23.204  -30.215 17.356  1.00 21.32 ? 320 PHE A C   1 
ATOM   2128 O  O   . PHE A 1 285 ? 23.795  -30.069 16.281  1.00 26.36 ? 320 PHE A O   1 
ATOM   2129 C  CB  . PHE A 1 285 ? 20.810  -30.604 16.780  1.00 28.78 ? 320 PHE A CB  1 
ATOM   2130 C  CG  . PHE A 1 285 ? 20.795  -32.030 17.261  1.00 20.45 ? 320 PHE A CG  1 
ATOM   2131 C  CD1 . PHE A 1 285 ? 20.371  -32.339 18.548  1.00 23.37 ? 320 PHE A CD1 1 
ATOM   2132 C  CD2 . PHE A 1 285 ? 21.164  -33.065 16.415  1.00 22.73 ? 320 PHE A CD2 1 
ATOM   2133 C  CE1 . PHE A 1 285 ? 20.340  -33.653 18.988  1.00 25.27 ? 320 PHE A CE1 1 
ATOM   2134 C  CE2 . PHE A 1 285 ? 21.135  -34.384 16.849  1.00 21.15 ? 320 PHE A CE2 1 
ATOM   2135 C  CZ  . PHE A 1 285 ? 20.720  -34.675 18.135  1.00 18.99 ? 320 PHE A CZ  1 
ATOM   2136 N  N   . VAL A 1 286 ? 23.753  -30.798 18.412  1.00 24.16 ? 321 VAL A N   1 
ATOM   2137 C  CA  . VAL A 1 286 ? 25.109  -31.325 18.415  1.00 24.63 ? 321 VAL A CA  1 
ATOM   2138 C  C   . VAL A 1 286 ? 25.030  -32.817 18.705  1.00 20.73 ? 321 VAL A C   1 
ATOM   2139 O  O   . VAL A 1 286 ? 24.869  -33.228 19.854  1.00 21.55 ? 321 VAL A O   1 
ATOM   2140 C  CB  . VAL A 1 286 ? 25.987  -30.602 19.452  1.00 26.05 ? 321 VAL A CB  1 
ATOM   2141 C  CG1 . VAL A 1 286 ? 27.434  -31.078 19.352  1.00 31.20 ? 321 VAL A CG1 1 
ATOM   2142 C  CG2 . VAL A 1 286 ? 25.911  -29.095 19.247  1.00 28.67 ? 321 VAL A CG2 1 
ATOM   2143 N  N   . PRO A 1 287 ? 25.117  -33.661 17.676  1.00 25.45 ? 322 PRO A N   1 
ATOM   2144 C  CA  . PRO A 1 287 ? 25.016  -35.111 17.890  1.00 18.82 ? 322 PRO A CA  1 
ATOM   2145 C  C   . PRO A 1 287 ? 26.105  -35.605 18.828  1.00 20.39 ? 322 PRO A C   1 
ATOM   2146 O  O   . PRO A 1 287 ? 27.242  -35.124 18.801  1.00 22.37 ? 322 PRO A O   1 
ATOM   2147 C  CB  . PRO A 1 287 ? 25.204  -35.693 16.483  1.00 22.43 ? 322 PRO A CB  1 
ATOM   2148 C  CG  . PRO A 1 287 ? 24.896  -34.574 15.545  1.00 32.78 ? 322 PRO A CG  1 
ATOM   2149 C  CD  . PRO A 1 287 ? 25.299  -33.311 16.258  1.00 27.25 ? 322 PRO A CD  1 
ATOM   2150 N  N   . VAL A 1 288 ? 25.742  -36.579 19.666  1.00 20.12 ? 323 VAL A N   1 
ATOM   2151 C  CA  . VAL A 1 288 ? 26.707  -37.136 20.604  1.00 18.34 ? 323 VAL A CA  1 
ATOM   2152 C  C   . VAL A 1 288 ? 27.900  -37.706 19.854  1.00 25.48 ? 323 VAL A C   1 
ATOM   2153 O  O   . VAL A 1 288 ? 27.770  -38.269 18.756  1.00 21.67 ? 323 VAL A O   1 
ATOM   2154 C  CB  . VAL A 1 288 ? 26.069  -38.181 21.537  1.00 27.47 ? 323 VAL A CB  1 
ATOM   2155 C  CG1 . VAL A 1 288 ? 24.975  -37.555 22.340  1.00 45.36 ? 323 VAL A CG1 1 
ATOM   2156 C  CG2 . VAL A 1 288 ? 25.517  -39.357 20.750  1.00 21.27 ? 323 VAL A CG2 1 
ATOM   2157 N  N   . ASN A 1 289 ? 29.076  -37.514 20.443  1.00 27.46 ? 324 ASN A N   1 
ATOM   2158 C  CA  . ASN A 1 289 ? 30.317  -38.089 19.945  1.00 27.02 ? 324 ASN A CA  1 
ATOM   2159 C  C   . ASN A 1 289 ? 30.238  -39.609 20.029  1.00 17.88 ? 324 ASN A C   1 
ATOM   2160 O  O   . ASN A 1 289 ? 29.828  -40.161 21.052  1.00 21.46 ? 324 ASN A O   1 
ATOM   2161 C  CB  . ASN A 1 289 ? 31.443  -37.601 20.862  1.00 25.65 ? 324 ASN A CB  1 
ATOM   2162 C  CG  . ASN A 1 289 ? 32.815  -38.015 20.392  1.00 40.58 ? 324 ASN A CG  1 
ATOM   2163 O  OD1 . ASN A 1 289 ? 33.101  -38.008 19.196  1.00 49.16 ? 324 ASN A OD1 1 
ATOM   2164 N  ND2 . ASN A 1 289 ? 33.685  -38.368 21.340  1.00 37.00 ? 324 ASN A ND2 1 
ATOM   2165 N  N   . TYR A 1 290 ? 30.652  -40.291 18.956  1.00 21.88 ? 325 TYR A N   1 
ATOM   2166 C  CA  . TYR A 1 290 ? 30.698  -41.750 18.997  1.00 17.79 ? 325 TYR A CA  1 
ATOM   2167 C  C   . TYR A 1 290 ? 31.551  -42.210 20.175  1.00 20.54 ? 325 TYR A C   1 
ATOM   2168 O  O   . TYR A 1 290 ? 32.692  -41.778 20.346  1.00 20.39 ? 325 TYR A O   1 
ATOM   2169 C  CB  . TYR A 1 290 ? 31.273  -42.310 17.692  1.00 24.08 ? 325 TYR A CB  1 
ATOM   2170 C  CG  . TYR A 1 290 ? 31.412  -43.822 17.719  1.00 21.72 ? 325 TYR A CG  1 
ATOM   2171 C  CD1 . TYR A 1 290 ? 30.299  -44.642 17.557  1.00 25.23 ? 325 TYR A CD1 1 
ATOM   2172 C  CD2 . TYR A 1 290 ? 32.649  -44.428 17.907  1.00 23.24 ? 325 TYR A CD2 1 
ATOM   2173 C  CE1 . TYR A 1 290 ? 30.412  -46.018 17.594  1.00 24.64 ? 325 TYR A CE1 1 
ATOM   2174 C  CE2 . TYR A 1 290 ? 32.777  -45.813 17.939  1.00 25.22 ? 325 TYR A CE2 1 
ATOM   2175 C  CZ  . TYR A 1 290 ? 31.646  -46.603 17.780  1.00 29.67 ? 325 TYR A CZ  1 
ATOM   2176 O  OH  . TYR A 1 290 ? 31.746  -47.979 17.809  1.00 27.39 ? 325 TYR A OH  1 
ATOM   2177 N  N   . SER A 1 291 ? 30.989  -43.085 20.999  1.00 20.67 ? 326 SER A N   1 
ATOM   2178 C  CA  . SER A 1 291 ? 31.683  -43.548 22.190  1.00 23.55 ? 326 SER A CA  1 
ATOM   2179 C  C   . SER A 1 291 ? 31.394  -45.029 22.359  1.00 24.05 ? 326 SER A C   1 
ATOM   2180 O  O   . SER A 1 291 ? 30.255  -45.465 22.183  1.00 27.35 ? 326 SER A O   1 
ATOM   2181 C  CB  . SER A 1 291 ? 31.201  -42.782 23.429  1.00 30.91 ? 326 SER A CB  1 
ATOM   2182 O  OG  . SER A 1 291 ? 31.864  -43.242 24.593  1.00 43.44 ? 326 SER A OG  1 
ATOM   2183 N  N   . VAL A 1 292 ? 32.422  -45.791 22.693  1.00 21.21 ? 327 VAL A N   1 
ATOM   2184 C  CA  . VAL A 1 292 ? 32.305  -47.239 22.836  1.00 33.59 ? 327 VAL A CA  1 
ATOM   2185 C  C   . VAL A 1 292 ? 31.914  -47.577 24.272  1.00 30.17 ? 327 VAL A C   1 
ATOM   2186 O  O   . VAL A 1 292 ? 32.436  -46.995 25.231  1.00 25.30 ? 327 VAL A O   1 
ATOM   2187 C  CB  . VAL A 1 292 ? 33.626  -47.921 22.430  1.00 35.44 ? 327 VAL A CB  1 
ATOM   2188 C  CG1 . VAL A 1 292 ? 33.656  -49.383 22.876  1.00 27.36 ? 327 VAL A CG1 1 
ATOM   2189 C  CG2 . VAL A 1 292 ? 33.844  -47.805 20.928  1.00 31.19 ? 327 VAL A CG2 1 
ATOM   2190 N  N   . VAL A 1 293 ? 30.988  -48.524 24.422  1.00 23.42 ? 328 VAL A N   1 
ATOM   2191 C  CA  . VAL A 1 293 ? 30.567  -49.034 25.724  1.00 25.20 ? 328 VAL A CA  1 
ATOM   2192 C  C   . VAL A 1 293 ? 31.157  -50.426 25.918  1.00 29.90 ? 328 VAL A C   1 
ATOM   2193 O  O   . VAL A 1 293 ? 31.137  -51.251 24.997  1.00 28.98 ? 328 VAL A O   1 
ATOM   2194 C  CB  . VAL A 1 293 ? 29.031  -49.078 25.811  1.00 21.38 ? 328 VAL A CB  1 
ATOM   2195 C  CG1 . VAL A 1 293 ? 28.589  -49.602 27.178  1.00 32.28 ? 328 VAL A CG1 1 
ATOM   2196 C  CG2 . VAL A 1 293 ? 28.448  -47.703 25.532  1.00 26.56 ? 328 VAL A CG2 1 
ATOM   2197 N  N   . ASN A 1 294 ? 31.679  -50.690 27.117  1.00 26.26 ? 329 ASN A N   1 
ATOM   2198 C  CA  . ASN A 1 294 ? 32.216  -52.017 27.450  1.00 32.27 ? 329 ASN A CA  1 
ATOM   2199 C  C   . ASN A 1 294 ? 31.604  -52.623 28.718  1.00 28.45 ? 329 ASN A C   1 
ATOM   2200 O  O   . ASN A 1 294 ? 31.143  -51.898 29.598  1.00 35.12 ? 329 ASN A O   1 
ATOM   2201 C  CB  . ASN A 1 294 ? 33.736  -51.973 27.603  1.00 38.47 ? 329 ASN A CB  1 
ATOM   2202 C  CG  . ASN A 1 294 ? 34.430  -51.499 26.352  1.00 35.44 ? 329 ASN A CG  1 
ATOM   2203 O  OD1 . ASN A 1 294 ? 34.979  -50.399 26.314  1.00 41.57 ? 329 ASN A OD1 1 
ATOM   2204 N  ND2 . ASN A 1 294 ? 34.396  -52.320 25.310  1.00 30.92 ? 329 ASN A ND2 1 
ATOM   2205 N  N   . ALA B 1 1   ? 13.028  -57.753 34.857  1.00 63.04 ? 36  ALA B N   1 
ATOM   2206 C  CA  . ALA B 1 1   ? 13.939  -57.015 33.983  1.00 47.33 ? 36  ALA B CA  1 
ATOM   2207 C  C   . ALA B 1 1   ? 14.993  -57.911 33.347  1.00 75.26 ? 36  ALA B C   1 
ATOM   2208 O  O   . ALA B 1 1   ? 14.682  -58.992 32.840  1.00 88.19 ? 36  ALA B O   1 
ATOM   2209 C  CB  . ALA B 1 1   ? 14.609  -55.864 34.740  1.00 46.69 ? 36  ALA B CB  1 
ATOM   2210 N  N   . ALA B 1 2   ? 16.245  -57.452 33.394  1.00 69.06 ? 37  ALA B N   1 
ATOM   2211 C  CA  . ALA B 1 2   ? 17.322  -58.084 32.652  1.00 44.49 ? 37  ALA B CA  1 
ATOM   2212 C  C   . ALA B 1 2   ? 18.658  -57.477 33.059  1.00 48.91 ? 37  ALA B C   1 
ATOM   2213 O  O   . ALA B 1 2   ? 18.720  -56.300 33.438  1.00 41.15 ? 37  ALA B O   1 
ATOM   2214 C  CB  . ALA B 1 2   ? 17.103  -57.861 31.155  1.00 45.08 ? 37  ALA B CB  1 
ATOM   2215 N  N   . PRO B 1 3   ? 19.745  -58.237 32.993  1.00 41.58 ? 38  PRO B N   1 
ATOM   2216 C  CA  . PRO B 1 3   ? 21.069  -57.632 33.164  1.00 40.15 ? 38  PRO B CA  1 
ATOM   2217 C  C   . PRO B 1 3   ? 21.397  -56.705 32.003  1.00 38.19 ? 38  PRO B C   1 
ATOM   2218 O  O   . PRO B 1 3   ? 20.932  -56.890 30.876  1.00 36.19 ? 38  PRO B O   1 
ATOM   2219 C  CB  . PRO B 1 3   ? 22.009  -58.841 33.180  1.00 40.77 ? 38  PRO B CB  1 
ATOM   2220 C  CG  . PRO B 1 3   ? 21.288  -59.876 32.369  1.00 64.41 ? 38  PRO B CG  1 
ATOM   2221 C  CD  . PRO B 1 3   ? 19.822  -59.672 32.658  1.00 43.85 ? 38  PRO B CD  1 
ATOM   2222 N  N   . GLN B 1 4   ? 22.207  -55.693 32.290  1.00 36.16 ? 39  GLN B N   1 
ATOM   2223 C  CA  . GLN B 1 4   ? 22.689  -54.829 31.225  1.00 33.56 ? 39  GLN B CA  1 
ATOM   2224 C  C   . GLN B 1 4   ? 23.656  -55.591 30.333  1.00 40.77 ? 39  GLN B C   1 
ATOM   2225 O  O   . GLN B 1 4   ? 24.351  -56.512 30.773  1.00 40.39 ? 39  GLN B O   1 
ATOM   2226 C  CB  . GLN B 1 4   ? 23.378  -53.599 31.806  1.00 33.00 ? 39  GLN B CB  1 
ATOM   2227 C  CG  . GLN B 1 4   ? 22.405  -52.639 32.462  1.00 37.86 ? 39  GLN B CG  1 
ATOM   2228 C  CD  . GLN B 1 4   ? 23.102  -51.460 33.090  1.00 38.65 ? 39  GLN B CD  1 
ATOM   2229 O  OE1 . GLN B 1 4   ? 24.330  -51.373 33.068  1.00 40.43 ? 39  GLN B OE1 1 
ATOM   2230 N  NE2 . GLN B 1 4   ? 22.325  -50.540 33.651  1.00 34.59 ? 39  GLN B NE2 1 
ATOM   2231 N  N   . VAL B 1 5   ? 23.686  -55.202 29.066  1.00 33.61 ? 40  VAL B N   1 
ATOM   2232 C  CA  . VAL B 1 5   ? 24.549  -55.821 28.072  1.00 30.11 ? 40  VAL B CA  1 
ATOM   2233 C  C   . VAL B 1 5   ? 25.867  -55.066 27.930  1.00 40.14 ? 40  VAL B C   1 
ATOM   2234 O  O   . VAL B 1 5   ? 26.942  -55.667 27.953  1.00 33.38 ? 40  VAL B O   1 
ATOM   2235 C  CB  . VAL B 1 5   ? 23.787  -55.943 26.733  1.00 28.17 ? 40  VAL B CB  1 
ATOM   2236 C  CG1 . VAL B 1 5   ? 24.657  -56.558 25.662  1.00 30.05 ? 40  VAL B CG1 1 
ATOM   2237 C  CG2 . VAL B 1 5   ? 22.516  -56.765 26.934  1.00 30.07 ? 40  VAL B CG2 1 
ATOM   2238 N  N   . ARG B 1 6   ? 25.791  -53.740 27.801  1.00 29.49 ? 41  ARG B N   1 
ATOM   2239 C  CA  . ARG B 1 6   ? 26.957  -52.848 27.850  1.00 25.31 ? 41  ARG B CA  1 
ATOM   2240 C  C   . ARG B 1 6   ? 28.002  -53.169 26.784  1.00 31.36 ? 41  ARG B C   1 
ATOM   2241 O  O   . ARG B 1 6   ? 29.207  -53.104 27.034  1.00 31.30 ? 41  ARG B O   1 
ATOM   2242 C  CB  . ARG B 1 6   ? 27.578  -52.796 29.250  1.00 34.86 ? 41  ARG B CB  1 
ATOM   2243 C  CG  . ARG B 1 6   ? 26.913  -51.786 30.173  1.00 35.09 ? 41  ARG B CG  1 
ATOM   2244 C  CD  . ARG B 1 6   ? 27.703  -51.572 31.449  1.00 46.84 ? 41  ARG B CD  1 
ATOM   2245 N  NE  . ARG B 1 6   ? 26.882  -50.931 32.469  1.00 46.87 ? 41  ARG B NE  1 
ATOM   2246 C  CZ  . ARG B 1 6   ? 27.265  -49.897 33.206  1.00 40.17 ? 41  ARG B CZ  1 
ATOM   2247 N  NH1 . ARG B 1 6   ? 28.492  -49.405 33.125  1.00 40.25 ? 41  ARG B NH1 1 
ATOM   2248 N  NH2 . ARG B 1 6   ? 26.395  -49.344 34.047  1.00 34.93 ? 41  ARG B NH2 1 
ATOM   2249 N  N   . THR B 1 7   ? 27.548  -53.500 25.579  1.00 27.30 ? 42  THR B N   1 
ATOM   2250 C  CA  . THR B 1 7   ? 28.433  -53.667 24.433  1.00 29.06 ? 42  THR B CA  1 
ATOM   2251 C  C   . THR B 1 7   ? 27.956  -52.786 23.286  1.00 26.87 ? 42  THR B C   1 
ATOM   2252 O  O   . THR B 1 7   ? 26.753  -52.570 23.113  1.00 26.37 ? 42  THR B O   1 
ATOM   2253 C  CB  . THR B 1 7   ? 28.518  -55.136 23.979  1.00 29.21 ? 42  THR B CB  1 
ATOM   2254 O  OG1 . THR B 1 7   ? 27.209  -55.623 23.652  1.00 35.76 ? 42  THR B OG1 1 
ATOM   2255 C  CG2 . THR B 1 7   ? 29.126  -55.999 25.067  1.00 30.55 ? 42  THR B CG2 1 
ATOM   2256 N  N   . SER B 1 8   ? 28.899  -52.264 22.516  1.00 25.00 ? 43  SER B N   1 
ATOM   2257 C  CA  . SER B 1 8   ? 28.518  -51.460 21.368  1.00 24.71 ? 43  SER B CA  1 
ATOM   2258 C  C   . SER B 1 8   ? 28.202  -52.356 20.171  1.00 22.71 ? 43  SER B C   1 
ATOM   2259 O  O   . SER B 1 8   ? 28.642  -53.508 20.083  1.00 24.98 ? 43  SER B O   1 
ATOM   2260 C  CB  . SER B 1 8   ? 29.624  -50.465 21.020  1.00 24.09 ? 43  SER B CB  1 
ATOM   2261 O  OG  . SER B 1 8   ? 29.744  -49.473 22.027  1.00 28.36 ? 43  SER B OG  1 
ATOM   2262 N  N   . ALA B 1 9   ? 27.422  -51.806 19.243  1.00 22.35 ? 44  ALA B N   1 
ATOM   2263 C  CA  . ALA B 1 9   ? 27.102  -52.510 18.014  1.00 22.84 ? 44  ALA B CA  1 
ATOM   2264 C  C   . ALA B 1 9   ? 28.366  -52.670 17.173  1.00 27.41 ? 44  ALA B C   1 
ATOM   2265 O  O   . ALA B 1 9   ? 29.355  -51.962 17.385  1.00 22.83 ? 44  ALA B O   1 
ATOM   2266 C  CB  . ALA B 1 9   ? 26.065  -51.717 17.223  1.00 19.75 ? 44  ALA B CB  1 
ATOM   2267 N  N   . PRO B 1 10  ? 28.371  -53.618 16.232  1.00 25.42 ? 45  PRO B N   1 
ATOM   2268 C  CA  . PRO B 1 10  ? 29.548  -53.783 15.367  1.00 26.74 ? 45  PRO B CA  1 
ATOM   2269 C  C   . PRO B 1 10  ? 29.888  -52.479 14.662  1.00 19.16 ? 45  PRO B C   1 
ATOM   2270 O  O   . PRO B 1 10  ? 29.010  -51.770 14.165  1.00 21.14 ? 45  PRO B O   1 
ATOM   2271 C  CB  . PRO B 1 10  ? 29.107  -54.858 14.370  1.00 31.50 ? 45  PRO B CB  1 
ATOM   2272 C  CG  . PRO B 1 10  ? 28.038  -55.616 15.082  1.00 31.46 ? 45  PRO B CG  1 
ATOM   2273 C  CD  . PRO B 1 10  ? 27.346  -54.649 15.985  1.00 38.03 ? 45  PRO B CD  1 
ATOM   2274 N  N   . GLY B 1 11  ? 31.178  -52.169 14.627  1.00 22.29 ? 46  GLY B N   1 
ATOM   2275 C  CA  . GLY B 1 11  ? 31.627  -50.865 14.188  1.00 19.24 ? 46  GLY B CA  1 
ATOM   2276 C  C   . GLY B 1 11  ? 31.853  -50.764 12.698  1.00 24.47 ? 46  GLY B C   1 
ATOM   2277 O  O   . GLY B 1 11  ? 32.987  -50.594 12.238  1.00 17.89 ? 46  GLY B O   1 
ATOM   2278 N  N   . TYR B 1 12  ? 30.779  -50.895 11.927  1.00 19.33 ? 47  TYR B N   1 
ATOM   2279 C  CA  . TYR B 1 12  ? 30.843  -50.641 10.499  1.00 18.13 ? 47  TYR B CA  1 
ATOM   2280 C  C   . TYR B 1 12  ? 29.638  -49.825 10.065  1.00 22.13 ? 47  TYR B C   1 
ATOM   2281 O  O   . TYR B 1 12  ? 28.538  -49.949 10.619  1.00 18.94 ? 47  TYR B O   1 
ATOM   2282 C  CB  . TYR B 1 12  ? 31.021  -51.901 9.636   1.00 17.83 ? 47  TYR B CB  1 
ATOM   2283 C  CG  . TYR B 1 12  ? 29.837  -52.845 9.598   1.00 17.58 ? 47  TYR B CG  1 
ATOM   2284 C  CD1 . TYR B 1 12  ? 29.641  -53.780 10.605  1.00 19.61 ? 47  TYR B CD1 1 
ATOM   2285 C  CD2 . TYR B 1 12  ? 28.913  -52.797 8.554   1.00 16.89 ? 47  TYR B CD2 1 
ATOM   2286 C  CE1 . TYR B 1 12  ? 28.576  -54.667 10.566  1.00 20.70 ? 47  TYR B CE1 1 
ATOM   2287 C  CE2 . TYR B 1 12  ? 27.834  -53.669 8.514   1.00 18.63 ? 47  TYR B CE2 1 
ATOM   2288 C  CZ  . TYR B 1 12  ? 27.674  -54.602 9.523   1.00 22.20 ? 47  TYR B CZ  1 
ATOM   2289 O  OH  . TYR B 1 12  ? 26.607  -55.479 9.504   1.00 25.56 ? 47  TYR B OH  1 
ATOM   2290 N  N   . TYR B 1 13  ? 29.872  -48.963 9.083   1.00 15.32 ? 48  TYR B N   1 
ATOM   2291 C  CA  . TYR B 1 13  ? 28.834  -48.082 8.556   1.00 14.66 ? 48  TYR B CA  1 
ATOM   2292 C  C   . TYR B 1 13  ? 28.848  -48.173 7.043   1.00 17.50 ? 48  TYR B C   1 
ATOM   2293 O  O   . TYR B 1 13  ? 29.836  -47.787 6.410   1.00 18.13 ? 48  TYR B O   1 
ATOM   2294 C  CB  . TYR B 1 13  ? 29.042  -46.627 8.986   1.00 17.11 ? 48  TYR B CB  1 
ATOM   2295 C  CG  . TYR B 1 13  ? 27.921  -45.727 8.507   1.00 17.34 ? 48  TYR B CG  1 
ATOM   2296 C  CD1 . TYR B 1 13  ? 26.692  -45.717 9.158   1.00 27.82 ? 48  TYR B CD1 1 
ATOM   2297 C  CD2 . TYR B 1 13  ? 28.070  -44.928 7.377   1.00 16.03 ? 48  TYR B CD2 1 
ATOM   2298 C  CE1 . TYR B 1 13  ? 25.650  -44.913 8.724   1.00 22.97 ? 48  TYR B CE1 1 
ATOM   2299 C  CE2 . TYR B 1 13  ? 27.027  -44.116 6.926   1.00 16.68 ? 48  TYR B CE2 1 
ATOM   2300 C  CZ  . TYR B 1 13  ? 25.819  -44.111 7.612   1.00 27.11 ? 48  TYR B CZ  1 
ATOM   2301 O  OH  . TYR B 1 13  ? 24.768  -43.321 7.189   1.00 27.91 ? 48  TYR B OH  1 
ATOM   2302 N  N   . ARG B 1 14  ? 27.748  -48.651 6.464   1.00 15.71 ? 49  ARG B N   1 
ATOM   2303 C  CA  . ARG B 1 14  ? 27.669  -48.848 5.024   1.00 17.01 ? 49  ARG B CA  1 
ATOM   2304 C  C   . ARG B 1 14  ? 27.038  -47.631 4.364   1.00 17.80 ? 49  ARG B C   1 
ATOM   2305 O  O   . ARG B 1 14  ? 26.069  -47.062 4.877   1.00 18.80 ? 49  ARG B O   1 
ATOM   2306 C  CB  . ARG B 1 14  ? 26.826  -50.082 4.709   1.00 20.09 ? 49  ARG B CB  1 
ATOM   2307 C  CG  . ARG B 1 14  ? 27.015  -50.601 3.299   1.00 20.80 ? 49  ARG B CG  1 
ATOM   2308 C  CD  . ARG B 1 14  ? 28.085  -51.683 3.289   1.00 18.16 ? 49  ARG B CD  1 
ATOM   2309 N  NE  . ARG B 1 14  ? 27.700  -52.818 4.121   1.00 21.05 ? 49  ARG B NE  1 
ATOM   2310 C  CZ  . ARG B 1 14  ? 28.486  -53.851 4.393   1.00 26.00 ? 49  ARG B CZ  1 
ATOM   2311 N  NH1 . ARG B 1 14  ? 29.749  -53.886 3.990   1.00 20.06 ? 49  ARG B NH1 1 
ATOM   2312 N  NH2 . ARG B 1 14  ? 27.992  -54.877 5.084   1.00 22.59 ? 49  ARG B NH2 1 
ATOM   2313 N  N   . MET B 1 15  ? 27.579  -47.243 3.210   1.00 16.75 ? 50  MET B N   1 
ATOM   2314 C  CA  . MET B 1 15  ? 27.060  -46.100 2.474   1.00 15.52 ? 50  MET B CA  1 
ATOM   2315 C  C   . MET B 1 15  ? 27.338  -46.318 0.990   1.00 23.35 ? 50  MET B C   1 
ATOM   2316 O  O   . MET B 1 15  ? 28.418  -46.781 0.616   1.00 20.38 ? 50  MET B O   1 
ATOM   2317 C  CB  . MET B 1 15  ? 27.773  -44.820 2.925   1.00 21.53 ? 50  MET B CB  1 
ATOM   2318 C  CG  . MET B 1 15  ? 27.436  -43.590 2.107   1.00 24.44 ? 50  MET B CG  1 
ATOM   2319 S  SD  . MET B 1 15  ? 28.352  -42.134 2.664   1.00 21.54 ? 50  MET B SD  1 
ATOM   2320 C  CE  . MET B 1 15  ? 29.767  -42.282 1.578   1.00 24.78 ? 50  MET B CE  1 
ATOM   2321 N  N   . LEU B 1 16  ? 26.373  -45.980 0.143   1.00 18.88 ? 51  LEU B N   1 
ATOM   2322 C  CA  . LEU B 1 16  ? 26.599  -46.055 -1.293  1.00 18.96 ? 51  LEU B CA  1 
ATOM   2323 C  C   . LEU B 1 16  ? 27.232  -44.761 -1.796  1.00 26.16 ? 51  LEU B C   1 
ATOM   2324 O  O   . LEU B 1 16  ? 26.970  -43.674 -1.277  1.00 25.73 ? 51  LEU B O   1 
ATOM   2325 C  CB  . LEU B 1 16  ? 25.289  -46.315 -2.034  1.00 21.00 ? 51  LEU B CB  1 
ATOM   2326 C  CG  . LEU B 1 16  ? 24.622  -47.665 -1.748  1.00 22.69 ? 51  LEU B CG  1 
ATOM   2327 C  CD1 . LEU B 1 16  ? 23.424  -47.855 -2.642  1.00 24.09 ? 51  LEU B CD1 1 
ATOM   2328 C  CD2 . LEU B 1 16  ? 25.598  -48.828 -1.899  1.00 28.50 ? 51  LEU B CD2 1 
ATOM   2329 N  N   . LEU B 1 17  ? 28.081  -44.891 -2.814  1.00 18.50 ? 52  LEU B N   1 
ATOM   2330 C  CA  . LEU B 1 17  ? 28.695  -43.745 -3.487  1.00 20.45 ? 52  LEU B CA  1 
ATOM   2331 C  C   . LEU B 1 17  ? 28.637  -44.056 -4.978  1.00 26.15 ? 52  LEU B C   1 
ATOM   2332 O  O   . LEU B 1 17  ? 29.515  -44.749 -5.505  1.00 23.44 ? 52  LEU B O   1 
ATOM   2333 C  CB  . LEU B 1 17  ? 30.134  -43.539 -3.036  1.00 18.31 ? 52  LEU B CB  1 
ATOM   2334 C  CG  . LEU B 1 17  ? 30.797  -42.294 -3.638  1.00 19.82 ? 52  LEU B CG  1 
ATOM   2335 C  CD1 . LEU B 1 17  ? 30.317  -41.024 -2.954  1.00 23.55 ? 52  LEU B CD1 1 
ATOM   2336 C  CD2 . LEU B 1 17  ? 32.324  -42.409 -3.576  1.00 23.04 ? 52  LEU B CD2 1 
ATOM   2337 N  N   . GLY B 1 18  ? 27.607  -43.556 -5.652  1.00 21.87 ? 53  GLY B N   1 
ATOM   2338 C  CA  . GLY B 1 18  ? 27.404  -43.967 -7.031  1.00 23.69 ? 53  GLY B CA  1 
ATOM   2339 C  C   . GLY B 1 18  ? 27.181  -45.470 -7.084  1.00 27.87 ? 53  GLY B C   1 
ATOM   2340 O  O   . GLY B 1 18  ? 26.300  -46.019 -6.407  1.00 26.41 ? 53  GLY B O   1 
ATOM   2341 N  N   . ASP B 1 19  ? 27.990  -46.161 -7.876  1.00 22.54 ? 54  ASP B N   1 
ATOM   2342 C  CA  . ASP B 1 19  ? 27.908  -47.612 -7.965  1.00 23.37 ? 54  ASP B CA  1 
ATOM   2343 C  C   . ASP B 1 19  ? 28.847  -48.317 -6.991  1.00 23.73 ? 54  ASP B C   1 
ATOM   2344 O  O   . ASP B 1 19  ? 28.880  -49.553 -6.972  1.00 28.48 ? 54  ASP B O   1 
ATOM   2345 C  CB  . ASP B 1 19  ? 28.190  -48.072 -9.394  1.00 31.24 ? 54  ASP B CB  1 
ATOM   2346 C  CG  . ASP B 1 19  ? 26.985  -47.894 -10.306 1.00 74.69 ? 54  ASP B CG  1 
ATOM   2347 O  OD1 . ASP B 1 19  ? 25.838  -47.995 -9.806  1.00 45.31 ? 54  ASP B OD1 1 
ATOM   2348 O  OD2 . ASP B 1 19  ? 27.186  -47.635 -11.514 1.00 56.59 ? 54  ASP B OD2 1 
ATOM   2349 N  N   . PHE B 1 20  ? 29.615  -47.566 -6.205  1.00 20.07 ? 55  PHE B N   1 
ATOM   2350 C  CA  . PHE B 1 20  ? 30.558  -48.128 -5.246  1.00 21.33 ? 55  PHE B CA  1 
ATOM   2351 C  C   . PHE B 1 20  ? 29.904  -48.310 -3.883  1.00 24.65 ? 55  PHE B C   1 
ATOM   2352 O  O   . PHE B 1 20  ? 28.989  -47.571 -3.500  1.00 22.57 ? 55  PHE B O   1 
ATOM   2353 C  CB  . PHE B 1 20  ? 31.768  -47.204 -5.054  1.00 18.24 ? 55  PHE B CB  1 
ATOM   2354 C  CG  . PHE B 1 20  ? 32.656  -47.051 -6.267  1.00 18.50 ? 55  PHE B CG  1 
ATOM   2355 C  CD1 . PHE B 1 20  ? 32.405  -47.721 -7.451  1.00 22.54 ? 55  PHE B CD1 1 
ATOM   2356 C  CD2 . PHE B 1 20  ? 33.739  -46.180 -6.216  1.00 24.04 ? 55  PHE B CD2 1 
ATOM   2357 C  CE1 . PHE B 1 20  ? 33.240  -47.559 -8.549  1.00 23.48 ? 55  PHE B CE1 1 
ATOM   2358 C  CE2 . PHE B 1 20  ? 34.573  -46.005 -7.317  1.00 26.09 ? 55  PHE B CE2 1 
ATOM   2359 C  CZ  . PHE B 1 20  ? 34.320  -46.692 -8.480  1.00 24.23 ? 55  PHE B CZ  1 
ATOM   2360 N  N   . GLU B 1 21  ? 30.419  -49.275 -3.130  1.00 19.60 ? 56  GLU B N   1 
ATOM   2361 C  CA  . GLU B 1 21  ? 30.022  -49.484 -1.744  1.00 20.48 ? 56  GLU B CA  1 
ATOM   2362 C  C   . GLU B 1 21  ? 31.153  -49.015 -0.839  1.00 17.09 ? 56  GLU B C   1 
ATOM   2363 O  O   . GLU B 1 21  ? 32.284  -49.498 -0.958  1.00 18.42 ? 56  GLU B O   1 
ATOM   2364 C  CB  . GLU B 1 21  ? 29.776  -50.973 -1.500  1.00 22.41 ? 56  GLU B CB  1 
ATOM   2365 C  CG  . GLU B 1 21  ? 29.278  -51.332 -0.113  1.00 19.08 ? 56  GLU B CG  1 
ATOM   2366 C  CD  . GLU B 1 21  ? 29.593  -52.776 0.221   1.00 23.91 ? 56  GLU B CD  1 
ATOM   2367 O  OE1 . GLU B 1 21  ? 30.796  -53.116 0.309   1.00 28.11 ? 56  GLU B OE1 1 
ATOM   2368 O  OE2 . GLU B 1 21  ? 28.651  -53.589 0.311   1.00 25.48 ? 56  GLU B OE2 1 
ATOM   2369 N  N   . ILE B 1 22  ? 30.846  -48.104 0.080   1.00 15.77 ? 57  ILE B N   1 
ATOM   2370 C  CA  . ILE B 1 22  ? 31.785  -47.622 1.083   1.00 16.36 ? 57  ILE B CA  1 
ATOM   2371 C  C   . ILE B 1 22  ? 31.392  -48.243 2.411   1.00 22.94 ? 57  ILE B C   1 
ATOM   2372 O  O   . ILE B 1 22  ? 30.209  -48.246 2.772   1.00 18.24 ? 57  ILE B O   1 
ATOM   2373 C  CB  . ILE B 1 22  ? 31.747  -46.086 1.188   1.00 18.05 ? 57  ILE B CB  1 
ATOM   2374 C  CG1 . ILE B 1 22  ? 31.762  -45.457 -0.212  1.00 21.66 ? 57  ILE B CG1 1 
ATOM   2375 C  CG2 . ILE B 1 22  ? 32.873  -45.575 2.094   1.00 14.93 ? 57  ILE B CG2 1 
ATOM   2376 C  CD1 . ILE B 1 22  ? 32.971  -45.870 -1.089  1.00 19.17 ? 57  ILE B CD1 1 
ATOM   2377 N  N   . THR B 1 23  ? 32.366  -48.793 3.130   1.00 16.48 ? 58  THR B N   1 
ATOM   2378 C  CA  . THR B 1 23  ? 32.128  -49.256 4.495   1.00 18.87 ? 58  THR B CA  1 
ATOM   2379 C  C   . THR B 1 23  ? 33.157  -48.606 5.403   1.00 18.32 ? 58  THR B C   1 
ATOM   2380 O  O   . THR B 1 23  ? 34.350  -48.907 5.309   1.00 16.97 ? 58  THR B O   1 
ATOM   2381 C  CB  . THR B 1 23  ? 32.218  -50.775 4.600   1.00 20.52 ? 58  THR B CB  1 
ATOM   2382 O  OG1 . THR B 1 23  ? 31.431  -51.374 3.567   1.00 20.36 ? 58  THR B OG1 1 
ATOM   2383 C  CG2 . THR B 1 23  ? 31.688  -51.229 5.967   1.00 20.79 ? 58  THR B CG2 1 
ATOM   2384 N  N   . ALA B 1 24  ? 32.703  -47.714 6.271   1.00 14.81 ? 59  ALA B N   1 
ATOM   2385 C  CA  . ALA B 1 24  ? 33.591  -47.207 7.302   1.00 13.15 ? 59  ALA B CA  1 
ATOM   2386 C  C   . ALA B 1 24  ? 33.757  -48.297 8.347   1.00 21.20 ? 59  ALA B C   1 
ATOM   2387 O  O   . ALA B 1 24  ? 32.770  -48.900 8.784   1.00 16.19 ? 59  ALA B O   1 
ATOM   2388 C  CB  . ALA B 1 24  ? 33.016  -45.937 7.927   1.00 14.60 ? 59  ALA B CB  1 
ATOM   2389 N  N   . LEU B 1 25  ? 35.006  -48.571 8.723   1.00 15.23 ? 60  LEU B N   1 
ATOM   2390 C  CA  . LEU B 1 25  ? 35.353  -49.625 9.667   1.00 16.80 ? 60  LEU B CA  1 
ATOM   2391 C  C   . LEU B 1 25  ? 35.994  -48.983 10.888  1.00 20.59 ? 60  LEU B C   1 
ATOM   2392 O  O   . LEU B 1 25  ? 37.063  -48.369 10.787  1.00 16.75 ? 60  LEU B O   1 
ATOM   2393 C  CB  . LEU B 1 25  ? 36.325  -50.619 9.030   1.00 14.48 ? 60  LEU B CB  1 
ATOM   2394 C  CG  . LEU B 1 25  ? 35.819  -51.350 7.785   1.00 15.70 ? 60  LEU B CG  1 
ATOM   2395 C  CD1 . LEU B 1 25  ? 36.931  -52.230 7.192   1.00 21.05 ? 60  LEU B CD1 1 
ATOM   2396 C  CD2 . LEU B 1 25  ? 34.556  -52.166 8.116   1.00 17.20 ? 60  LEU B CD2 1 
ATOM   2397 N  N   . SER B 1 26  ? 35.349  -49.124 12.039  1.00 17.98 ? 61  SER B N   1 
ATOM   2398 C  CA  . SER B 1 26  ? 35.915  -48.579 13.263  1.00 15.81 ? 61  SER B CA  1 
ATOM   2399 C  C   . SER B 1 26  ? 37.047  -49.469 13.758  1.00 16.47 ? 61  SER B C   1 
ATOM   2400 O  O   . SER B 1 26  ? 36.918  -50.701 13.796  1.00 18.20 ? 61  SER B O   1 
ATOM   2401 C  CB  . SER B 1 26  ? 34.850  -48.470 14.348  1.00 16.92 ? 61  SER B CB  1 
ATOM   2402 O  OG  . SER B 1 26  ? 35.429  -47.920 15.523  1.00 15.96 ? 61  SER B OG  1 
ATOM   2403 N  N   . ASP B 1 27  ? 38.168  -48.850 14.119  1.00 15.92 ? 62  ASP B N   1 
ATOM   2404 C  CA  . ASP B 1 27  ? 39.217  -49.555 14.840  1.00 17.57 ? 62  ASP B CA  1 
ATOM   2405 C  C   . ASP B 1 27  ? 39.022  -49.506 16.347  1.00 20.60 ? 62  ASP B C   1 
ATOM   2406 O  O   . ASP B 1 27  ? 39.814  -50.110 17.083  1.00 20.86 ? 62  ASP B O   1 
ATOM   2407 C  CB  . ASP B 1 27  ? 40.599  -48.986 14.503  1.00 18.65 ? 62  ASP B CB  1 
ATOM   2408 C  CG  . ASP B 1 27  ? 41.710  -49.962 14.829  1.00 20.63 ? 62  ASP B CG  1 
ATOM   2409 O  OD1 . ASP B 1 27  ? 41.564  -51.158 14.499  1.00 20.16 ? 62  ASP B OD1 1 
ATOM   2410 O  OD2 . ASP B 1 27  ? 42.732  -49.546 15.426  1.00 18.90 ? 62  ASP B OD2 1 
ATOM   2411 N  N   . GLY B 1 28  ? 37.994  -48.812 16.817  1.00 17.70 ? 63  GLY B N   1 
ATOM   2412 C  CA  . GLY B 1 28  ? 37.837  -48.479 18.213  1.00 17.28 ? 63  GLY B CA  1 
ATOM   2413 C  C   . GLY B 1 28  ? 37.984  -46.983 18.423  1.00 20.66 ? 63  GLY B C   1 
ATOM   2414 O  O   . GLY B 1 28  ? 37.935  -46.180 17.486  1.00 20.19 ? 63  GLY B O   1 
ATOM   2415 N  N   . THR B 1 29  ? 38.119  -46.607 19.689  1.00 18.72 ? 64  THR B N   1 
ATOM   2416 C  CA  . THR B 1 29  ? 38.348  -45.217 20.052  1.00 20.46 ? 64  THR B CA  1 
ATOM   2417 C  C   . THR B 1 29  ? 39.445  -45.181 21.104  1.00 22.49 ? 64  THR B C   1 
ATOM   2418 O  O   . THR B 1 29  ? 39.718  -46.178 21.777  1.00 22.10 ? 64  THR B O   1 
ATOM   2419 C  CB  . THR B 1 29  ? 37.100  -44.545 20.657  1.00 19.10 ? 64  THR B CB  1 
ATOM   2420 O  OG1 . THR B 1 29  ? 36.772  -45.191 21.893  1.00 23.98 ? 64  THR B OG1 1 
ATOM   2421 C  CG2 . THR B 1 29  ? 35.892  -44.584 19.711  1.00 20.17 ? 64  THR B CG2 1 
ATOM   2422 N  N   . VAL B 1 30  ? 40.064  -44.015 21.255  1.00 18.37 ? 65  VAL B N   1 
ATOM   2423 C  CA  . VAL B 1 30  ? 41.111  -43.839 22.260  1.00 18.69 ? 65  VAL B CA  1 
ATOM   2424 C  C   . VAL B 1 30  ? 41.011  -42.432 22.837  1.00 23.51 ? 65  VAL B C   1 
ATOM   2425 O  O   . VAL B 1 30  ? 40.722  -41.477 22.116  1.00 21.96 ? 65  VAL B O   1 
ATOM   2426 C  CB  . VAL B 1 30  ? 42.506  -44.161 21.678  1.00 24.28 ? 65  VAL B CB  1 
ATOM   2427 C  CG1 . VAL B 1 30  ? 42.811  -43.285 20.457  1.00 21.32 ? 65  VAL B CG1 1 
ATOM   2428 C  CG2 . VAL B 1 30  ? 43.579  -43.999 22.743  1.00 29.97 ? 65  VAL B CG2 1 
ATOM   2429 N  N   . ALA B 1 31  ? 41.214  -42.305 24.149  1.00 21.05 ? 66  ALA B N   1 
ATOM   2430 C  CA  . ALA B 1 31  ? 41.162  -40.992 24.787  1.00 22.19 ? 66  ALA B CA  1 
ATOM   2431 C  C   . ALA B 1 31  ? 42.482  -40.268 24.548  1.00 36.58 ? 66  ALA B C   1 
ATOM   2432 O  O   . ALA B 1 31  ? 43.546  -40.775 24.917  1.00 31.23 ? 66  ALA B O   1 
ATOM   2433 C  CB  . ALA B 1 31  ? 40.884  -41.130 26.283  1.00 23.74 ? 66  ALA B CB  1 
ATOM   2434 N  N   . LEU B 1 32  ? 42.416  -39.073 23.920  1.00 26.84 ? 67  LEU B N   1 
ATOM   2435 C  CA  . LEU B 1 32  ? 43.611  -38.319 23.569  1.00 22.80 ? 67  LEU B CA  1 
ATOM   2436 C  C   . LEU B 1 32  ? 43.664  -37.004 24.331  1.00 32.41 ? 67  LEU B C   1 
ATOM   2437 O  O   . LEU B 1 32  ? 42.640  -36.322 24.466  1.00 26.56 ? 67  LEU B O   1 
ATOM   2438 C  CB  . LEU B 1 32  ? 43.631  -38.016 22.065  1.00 24.38 ? 67  LEU B CB  1 
ATOM   2439 C  CG  . LEU B 1 32  ? 43.739  -39.230 21.140  1.00 26.45 ? 67  LEU B CG  1 
ATOM   2440 C  CD1 . LEU B 1 32  ? 43.900  -38.819 19.682  1.00 31.60 ? 67  LEU B CD1 1 
ATOM   2441 C  CD2 . LEU B 1 32  ? 44.899  -40.121 21.574  1.00 35.38 ? 67  LEU B CD2 1 
ATOM   2442 N  N   . PRO B 1 33  ? 44.834  -36.634 24.857  1.00 28.30 ? 68  PRO B N   1 
ATOM   2443 C  CA  . PRO B 1 33  ? 45.007  -35.310 25.490  1.00 28.64 ? 68  PRO B CA  1 
ATOM   2444 C  C   . PRO B 1 33  ? 45.210  -34.229 24.435  1.00 31.59 ? 68  PRO B C   1 
ATOM   2445 O  O   . PRO B 1 33  ? 46.299  -33.673 24.249  1.00 29.41 ? 68  PRO B O   1 
ATOM   2446 C  CB  . PRO B 1 33  ? 46.244  -35.529 26.370  1.00 31.94 ? 68  PRO B CB  1 
ATOM   2447 C  CG  . PRO B 1 33  ? 47.031  -36.565 25.643  1.00 32.04 ? 68  PRO B CG  1 
ATOM   2448 C  CD  . PRO B 1 33  ? 46.018  -37.495 25.030  1.00 29.06 ? 68  PRO B CD  1 
ATOM   2449 N  N   . VAL B 1 34  ? 44.131  -33.925 23.708  1.00 27.89 ? 69  VAL B N   1 
ATOM   2450 C  CA  . VAL B 1 34  ? 44.230  -33.008 22.575  1.00 28.35 ? 69  VAL B CA  1 
ATOM   2451 C  C   . VAL B 1 34  ? 44.650  -31.613 23.017  1.00 27.45 ? 69  VAL B C   1 
ATOM   2452 O  O   . VAL B 1 34  ? 45.314  -30.892 22.261  1.00 28.88 ? 69  VAL B O   1 
ATOM   2453 C  CB  . VAL B 1 34  ? 42.932  -32.999 21.743  1.00 33.89 ? 69  VAL B CB  1 
ATOM   2454 C  CG1 . VAL B 1 34  ? 42.688  -34.374 21.134  1.00 29.95 ? 69  VAL B CG1 1 
ATOM   2455 C  CG2 . VAL B 1 34  ? 41.751  -32.557 22.598  1.00 29.40 ? 69  VAL B CG2 1 
ATOM   2456 N  N   . ASP B 1 35  ? 44.282  -31.209 24.237  1.00 28.06 ? 70  ASP B N   1 
ATOM   2457 C  CA  . ASP B 1 35  ? 44.693  -29.896 24.726  1.00 31.12 ? 70  ASP B CA  1 
ATOM   2458 C  C   . ASP B 1 35  ? 46.210  -29.781 24.823  1.00 35.39 ? 70  ASP B C   1 
ATOM   2459 O  O   . ASP B 1 35  ? 46.753  -28.673 24.729  1.00 41.35 ? 70  ASP B O   1 
ATOM   2460 C  CB  . ASP B 1 35  ? 44.055  -29.596 26.083  1.00 33.08 ? 70  ASP B CB  1 
ATOM   2461 C  CG  . ASP B 1 35  ? 44.316  -30.688 27.106  1.00 38.41 ? 70  ASP B CG  1 
ATOM   2462 O  OD1 . ASP B 1 35  ? 44.509  -31.857 26.706  1.00 31.09 ? 70  ASP B OD1 1 
ATOM   2463 O  OD2 . ASP B 1 35  ? 44.353  -30.369 28.314  1.00 43.00 ? 70  ASP B OD2 1 
ATOM   2464 N  N   . LYS B 1 36  ? 46.909  -30.903 25.018  1.00 28.87 ? 71  LYS B N   1 
ATOM   2465 C  CA  . LYS B 1 36  ? 48.364  -30.889 25.097  1.00 32.27 ? 71  LYS B CA  1 
ATOM   2466 C  C   . LYS B 1 36  ? 49.053  -31.054 23.746  1.00 32.53 ? 71  LYS B C   1 
ATOM   2467 O  O   . LYS B 1 36  ? 50.217  -30.660 23.619  1.00 40.24 ? 71  LYS B O   1 
ATOM   2468 C  CB  . LYS B 1 36  ? 48.872  -31.949 26.084  1.00 33.99 ? 71  LYS B CB  1 
ATOM   2469 C  CG  . LYS B 1 36  ? 48.198  -31.887 27.444  1.00 41.21 ? 71  LYS B CG  1 
ATOM   2470 C  CD  . LYS B 1 36  ? 48.775  -32.908 28.413  1.00 62.88 ? 71  LYS B CD  1 
ATOM   2471 C  CE  . LYS B 1 36  ? 48.590  -32.448 29.857  1.00 60.26 ? 71  LYS B CE  1 
ATOM   2472 N  NZ  . LYS B 1 36  ? 49.400  -33.247 30.824  1.00 71.62 ? 71  LYS B NZ  1 
ATOM   2473 N  N   . ARG B 1 37  ? 48.377  -31.621 22.742  1.00 28.82 ? 72  ARG B N   1 
ATOM   2474 C  CA  . ARG B 1 37  ? 49.006  -31.814 21.437  1.00 32.01 ? 72  ARG B CA  1 
ATOM   2475 C  C   . ARG B 1 37  ? 48.764  -30.662 20.467  1.00 27.75 ? 72  ARG B C   1 
ATOM   2476 O  O   . ARG B 1 37  ? 49.607  -30.411 19.599  1.00 35.72 ? 72  ARG B O   1 
ATOM   2477 C  CB  . ARG B 1 37  ? 48.570  -33.137 20.791  1.00 33.44 ? 72  ARG B CB  1 
ATOM   2478 C  CG  . ARG B 1 37  ? 48.733  -34.383 21.653  1.00 47.70 ? 72  ARG B CG  1 
ATOM   2479 C  CD  . ARG B 1 37  ? 50.014  -34.362 22.491  1.00 41.27 ? 72  ARG B CD  1 
ATOM   2480 N  NE  . ARG B 1 37  ? 51.230  -34.469 21.693  1.00 58.32 ? 72  ARG B NE  1 
ATOM   2481 C  CZ  . ARG B 1 37  ? 51.921  -35.590 21.520  1.00 52.62 ? 72  ARG B CZ  1 
ATOM   2482 N  NH1 . ARG B 1 37  ? 51.521  -36.738 22.042  1.00 60.12 ? 72  ARG B NH1 1 
ATOM   2483 N  NH2 . ARG B 1 37  ? 53.041  -35.559 20.803  1.00 44.73 ? 72  ARG B NH2 1 
ATOM   2484 N  N   . LEU B 1 38  ? 47.642  -29.955 20.589  1.00 30.51 ? 73  LEU B N   1 
ATOM   2485 C  CA  . LEU B 1 38  ? 47.367  -28.828 19.703  1.00 25.07 ? 73  LEU B CA  1 
ATOM   2486 C  C   . LEU B 1 38  ? 48.316  -27.664 19.969  1.00 31.57 ? 73  LEU B C   1 
ATOM   2487 O  O   . LEU B 1 38  ? 48.649  -27.359 21.118  1.00 33.64 ? 73  LEU B O   1 
ATOM   2488 C  CB  . LEU B 1 38  ? 45.912  -28.373 19.849  1.00 24.87 ? 73  LEU B CB  1 
ATOM   2489 C  CG  . LEU B 1 38  ? 44.839  -29.354 19.374  1.00 23.08 ? 73  LEU B CG  1 
ATOM   2490 C  CD1 . LEU B 1 38  ? 43.459  -28.921 19.843  1.00 25.43 ? 73  LEU B CD1 1 
ATOM   2491 C  CD2 . LEU B 1 38  ? 44.871  -29.422 17.861  1.00 23.57 ? 73  LEU B CD2 1 
ATOM   2492 N  N   . ASN B 1 39  ? 48.739  -27.001 18.887  1.00 26.46 ? 74  ASN B N   1 
ATOM   2493 C  CA  . ASN B 1 39  ? 49.691  -25.892 18.958  1.00 29.54 ? 74  ASN B CA  1 
ATOM   2494 C  C   . ASN B 1 39  ? 48.956  -24.588 19.275  1.00 32.68 ? 74  ASN B C   1 
ATOM   2495 O  O   . ASN B 1 39  ? 48.917  -23.639 18.488  1.00 41.15 ? 74  ASN B O   1 
ATOM   2496 C  CB  . ASN B 1 39  ? 50.481  -25.786 17.661  1.00 29.93 ? 74  ASN B CB  1 
ATOM   2497 C  CG  . ASN B 1 39  ? 51.500  -26.901 17.507  1.00 42.50 ? 74  ASN B CG  1 
ATOM   2498 O  OD1 . ASN B 1 39  ? 51.986  -27.456 18.496  1.00 44.96 ? 74  ASN B OD1 1 
ATOM   2499 N  ND2 . ASN B 1 39  ? 51.825  -27.241 16.261  1.00 45.24 ? 74  ASN B ND2 1 
ATOM   2500 N  N   . GLN B 1 40  ? 48.364  -24.554 20.466  1.00 29.64 ? 75  GLN B N   1 
ATOM   2501 C  CA  . GLN B 1 40  ? 47.731  -23.352 20.990  1.00 30.90 ? 75  GLN B CA  1 
ATOM   2502 C  C   . GLN B 1 40  ? 47.534  -23.540 22.486  1.00 32.73 ? 75  GLN B C   1 
ATOM   2503 O  O   . GLN B 1 40  ? 47.592  -24.674 22.980  1.00 29.65 ? 75  GLN B O   1 
ATOM   2504 C  CB  . GLN B 1 40  ? 46.386  -23.078 20.291  1.00 31.83 ? 75  GLN B CB  1 
ATOM   2505 C  CG  . GLN B 1 40  ? 45.254  -24.016 20.680  1.00 31.61 ? 75  GLN B CG  1 
ATOM   2506 C  CD  . GLN B 1 40  ? 43.955  -23.650 19.992  1.00 34.70 ? 75  GLN B CD  1 
ATOM   2507 O  OE1 . GLN B 1 40  ? 43.906  -22.709 19.197  1.00 32.85 ? 75  GLN B OE1 1 
ATOM   2508 N  NE2 . GLN B 1 40  ? 42.894  -24.388 20.296  1.00 34.89 ? 75  GLN B NE2 1 
ATOM   2509 N  N   . PRO B 1 41  ? 47.313  -22.457 23.236  1.00 37.05 ? 76  PRO B N   1 
ATOM   2510 C  CA  . PRO B 1 41  ? 47.172  -22.594 24.691  1.00 37.28 ? 76  PRO B CA  1 
ATOM   2511 C  C   . PRO B 1 41  ? 46.046  -23.546 25.068  1.00 33.90 ? 76  PRO B C   1 
ATOM   2512 O  O   . PRO B 1 41  ? 44.982  -23.569 24.443  1.00 28.58 ? 76  PRO B O   1 
ATOM   2513 C  CB  . PRO B 1 41  ? 46.882  -21.163 25.157  1.00 34.65 ? 76  PRO B CB  1 
ATOM   2514 C  CG  . PRO B 1 41  ? 47.512  -20.304 24.107  1.00 42.38 ? 76  PRO B CG  1 
ATOM   2515 C  CD  . PRO B 1 41  ? 47.272  -21.044 22.819  1.00 39.83 ? 76  PRO B CD  1 
ATOM   2516 N  N   . ALA B 1 42  ? 46.299  -24.340 26.103  1.00 34.34 ? 77  ALA B N   1 
ATOM   2517 C  CA  . ALA B 1 42  ? 45.306  -25.303 26.572  1.00 30.26 ? 77  ALA B CA  1 
ATOM   2518 C  C   . ALA B 1 42  ? 43.945  -24.691 26.894  1.00 28.86 ? 77  ALA B C   1 
ATOM   2519 O  O   . ALA B 1 42  ? 42.927  -25.320 26.550  1.00 29.29 ? 77  ALA B O   1 
ATOM   2520 C  CB  . ALA B 1 42  ? 45.870  -26.113 27.748  1.00 35.68 ? 77  ALA B CB  1 
ATOM   2521 N  N   . PRO B 1 43  ? 43.838  -23.527 27.548  1.00 30.56 ? 78  PRO B N   1 
ATOM   2522 C  CA  . PRO B 1 43  ? 42.499  -22.956 27.790  1.00 34.08 ? 78  PRO B CA  1 
ATOM   2523 C  C   . PRO B 1 43  ? 41.714  -22.650 26.525  1.00 36.65 ? 78  PRO B C   1 
ATOM   2524 O  O   . PRO B 1 43  ? 40.483  -22.783 26.529  1.00 30.95 ? 78  PRO B O   1 
ATOM   2525 C  CB  . PRO B 1 43  ? 42.794  -21.687 28.605  1.00 43.23 ? 78  PRO B CB  1 
ATOM   2526 C  CG  . PRO B 1 43  ? 44.127  -21.937 29.220  1.00 35.10 ? 78  PRO B CG  1 
ATOM   2527 C  CD  . PRO B 1 43  ? 44.888  -22.714 28.190  1.00 33.40 ? 78  PRO B CD  1 
ATOM   2528 N  N   . LYS B 1 44  ? 42.380  -22.231 25.444  1.00 29.23 ? 79  LYS B N   1 
ATOM   2529 C  CA  . LYS B 1 44  ? 41.665  -21.979 24.195  1.00 28.52 ? 79  LYS B CA  1 
ATOM   2530 C  C   . LYS B 1 44  ? 41.074  -23.270 23.626  1.00 34.99 ? 79  LYS B C   1 
ATOM   2531 O  O   . LYS B 1 44  ? 39.915  -23.293 23.177  1.00 31.08 ? 79  LYS B O   1 
ATOM   2532 C  CB  . LYS B 1 44  ? 42.599  -21.273 23.209  1.00 31.56 ? 79  LYS B CB  1 
ATOM   2533 C  CG  . LYS B 1 44  ? 41.966  -20.810 21.908  1.00 34.67 ? 79  LYS B CG  1 
ATOM   2534 C  CD  . LYS B 1 44  ? 42.968  -20.020 21.069  1.00 42.51 ? 79  LYS B CD  1 
ATOM   2535 C  CE  . LYS B 1 44  ? 42.348  -19.546 19.765  1.00 51.64 ? 79  LYS B CE  1 
ATOM   2536 N  NZ  . LYS B 1 44  ? 42.047  -20.689 18.843  1.00 58.82 ? 79  LYS B NZ  1 
ATOM   2537 N  N   . THR B 1 45  ? 41.848  -24.364 23.659  1.00 28.94 ? 80  THR B N   1 
ATOM   2538 C  CA  . THR B 1 45  ? 41.295  -25.660 23.275  1.00 27.01 ? 80  THR B CA  1 
ATOM   2539 C  C   . THR B 1 45  ? 40.130  -26.048 24.173  1.00 23.98 ? 80  THR B C   1 
ATOM   2540 O  O   . THR B 1 45  ? 39.102  -26.538 23.689  1.00 23.96 ? 80  THR B O   1 
ATOM   2541 C  CB  . THR B 1 45  ? 42.384  -26.732 23.301  1.00 29.98 ? 80  THR B CB  1 
ATOM   2542 O  OG1 . THR B 1 45  ? 43.369  -26.406 22.320  1.00 27.30 ? 80  THR B OG1 1 
ATOM   2543 C  CG2 . THR B 1 45  ? 41.806  -28.128 23.006  1.00 24.56 ? 80  THR B CG2 1 
ATOM   2544 N  N   . GLN B 1 46  ? 40.272  -25.835 25.480  1.00 27.83 ? 81  GLN B N   1 
ATOM   2545 C  CA  . GLN B 1 46  ? 39.198  -26.188 26.399  1.00 26.40 ? 81  GLN B CA  1 
ATOM   2546 C  C   . GLN B 1 46  ? 37.919  -25.440 26.065  1.00 25.81 ? 81  GLN B C   1 
ATOM   2547 O  O   . GLN B 1 46  ? 36.836  -26.034 26.055  1.00 27.08 ? 81  GLN B O   1 
ATOM   2548 C  CB  . GLN B 1 46  ? 39.610  -25.881 27.833  1.00 31.96 ? 81  GLN B CB  1 
ATOM   2549 C  CG  . GLN B 1 46  ? 40.500  -26.899 28.559  1.00 60.75 ? 81  GLN B CG  1 
ATOM   2550 C  CD  . GLN B 1 46  ? 40.108  -28.378 28.437  1.00 58.74 ? 81  GLN B CD  1 
ATOM   2551 O  OE1 . GLN B 1 46  ? 39.396  -28.817 27.527  1.00 60.11 ? 81  GLN B OE1 1 
ATOM   2552 N  NE2 . GLN B 1 46  ? 40.553  -29.146 29.418  1.00 65.62 ? 81  GLN B NE2 1 
ATOM   2553 N  N   . SER B 1 47  ? 38.026  -24.138 25.788  1.00 25.86 ? 82  SER B N   1 
ATOM   2554 C  CA  . SER B 1 47  ? 36.843  -23.350 25.444  1.00 28.95 ? 82  SER B CA  1 
ATOM   2555 C  C   . SER B 1 47  ? 36.200  -23.840 24.151  1.00 33.79 ? 82  SER B C   1 
ATOM   2556 O  O   . SER B 1 47  ? 34.966  -23.936 24.056  1.00 29.94 ? 82  SER B O   1 
ATOM   2557 C  CB  . SER B 1 47  ? 37.206  -21.868 25.335  1.00 32.67 ? 82  SER B CB  1 
ATOM   2558 O  OG  . SER B 1 47  ? 37.613  -21.362 26.592  1.00 50.37 ? 82  SER B OG  1 
ATOM   2559 N  N   . ALA B 1 48  ? 37.017  -24.161 23.139  1.00 26.50 ? 83  ALA B N   1 
ATOM   2560 C  CA  . ALA B 1 48  ? 36.449  -24.692 21.899  1.00 24.28 ? 83  ALA B CA  1 
ATOM   2561 C  C   . ALA B 1 48  ? 35.699  -26.001 22.154  1.00 29.34 ? 83  ALA B C   1 
ATOM   2562 O  O   . ALA B 1 48  ? 34.528  -26.170 21.755  1.00 36.97 ? 83  ALA B O   1 
ATOM   2563 C  CB  . ALA B 1 48  ? 37.551  -24.875 20.855  1.00 26.31 ? 83  ALA B CB  1 
ATOM   2564 N  N   . LEU B 1 49  ? 36.354  -26.933 22.851  1.00 25.98 ? 84  LEU B N   1 
ATOM   2565 C  CA  . LEU B 1 49  ? 35.716  -28.214 23.128  1.00 28.84 ? 84  LEU B CA  1 
ATOM   2566 C  C   . LEU B 1 49  ? 34.419  -28.016 23.899  1.00 25.69 ? 84  LEU B C   1 
ATOM   2567 O  O   . LEU B 1 49  ? 33.411  -28.669 23.606  1.00 25.58 ? 84  LEU B O   1 
ATOM   2568 C  CB  . LEU B 1 49  ? 36.663  -29.122 23.906  1.00 24.73 ? 84  LEU B CB  1 
ATOM   2569 C  CG  . LEU B 1 49  ? 37.957  -29.522 23.181  1.00 26.85 ? 84  LEU B CG  1 
ATOM   2570 C  CD1 . LEU B 1 49  ? 38.802  -30.437 24.049  1.00 31.55 ? 84  LEU B CD1 1 
ATOM   2571 C  CD2 . LEU B 1 49  ? 37.667  -30.167 21.836  1.00 29.89 ? 84  LEU B CD2 1 
ATOM   2572 N  N   . ALA B 1 50  ? 34.420  -27.094 24.869  1.00 24.53 ? 85  ALA B N   1 
ATOM   2573 C  CA  . ALA B 1 50  ? 33.210  -26.817 25.636  1.00 26.22 ? 85  ALA B CA  1 
ATOM   2574 C  C   . ALA B 1 50  ? 32.088  -26.320 24.736  1.00 32.70 ? 85  ALA B C   1 
ATOM   2575 O  O   . ALA B 1 50  ? 30.915  -26.663 24.948  1.00 30.76 ? 85  ALA B O   1 
ATOM   2576 C  CB  . ALA B 1 50  ? 33.506  -25.796 26.736  1.00 25.90 ? 85  ALA B CB  1 
ATOM   2577 N  N   . LYS B 1 51  ? 32.425  -25.500 23.731  1.00 25.92 ? 86  LYS B N   1 
ATOM   2578 C  CA  . LYS B 1 51  ? 31.421  -25.119 22.737  1.00 29.04 ? 86  LYS B CA  1 
ATOM   2579 C  C   . LYS B 1 51  ? 30.803  -26.342 22.082  1.00 34.85 ? 86  LYS B C   1 
ATOM   2580 O  O   . LYS B 1 51  ? 29.608  -26.337 21.764  1.00 33.25 ? 86  LYS B O   1 
ATOM   2581 C  CB  . LYS B 1 51  ? 32.009  -24.206 21.658  1.00 40.51 ? 86  LYS B CB  1 
ATOM   2582 C  CG  . LYS B 1 51  ? 32.146  -22.753 22.066  1.00 43.74 ? 86  LYS B CG  1 
ATOM   2583 C  CD  . LYS B 1 51  ? 32.281  -21.856 20.845  1.00 55.86 ? 86  LYS B CD  1 
ATOM   2584 C  CE  . LYS B 1 51  ? 32.862  -20.503 21.227  1.00 54.99 ? 86  LYS B CE  1 
ATOM   2585 N  NZ  . LYS B 1 51  ? 33.597  -19.877 20.096  1.00 51.45 ? 86  LYS B NZ  1 
ATOM   2586 N  N   . SER B 1 52  ? 31.588  -27.397 21.872  1.00 29.51 ? 87  SER B N   1 
ATOM   2587 C  CA  . SER B 1 52  ? 31.021  -28.628 21.322  1.00 31.57 ? 87  SER B CA  1 
ATOM   2588 C  C   . SER B 1 52  ? 30.573  -29.646 22.383  1.00 25.05 ? 87  SER B C   1 
ATOM   2589 O  O   . SER B 1 52  ? 30.412  -30.828 22.052  1.00 25.15 ? 87  SER B O   1 
ATOM   2590 C  CB  . SER B 1 52  ? 31.975  -29.268 20.312  1.00 25.71 ? 87  SER B CB  1 
ATOM   2591 O  OG  . SER B 1 52  ? 31.893  -28.589 19.071  1.00 38.41 ? 87  SER B OG  1 
ATOM   2592 N  N   . PHE B 1 53  ? 30.336  -29.211 23.626  1.00 23.51 ? 88  PHE B N   1 
ATOM   2593 C  CA  . PHE B 1 53  ? 29.988  -30.104 24.743  1.00 23.53 ? 88  PHE B CA  1 
ATOM   2594 C  C   . PHE B 1 53  ? 31.014  -31.220 24.945  1.00 34.04 ? 88  PHE B C   1 
ATOM   2595 O  O   . PHE B 1 53  ? 30.662  -32.367 25.225  1.00 34.23 ? 88  PHE B O   1 
ATOM   2596 C  CB  . PHE B 1 53  ? 28.567  -30.666 24.632  1.00 24.82 ? 88  PHE B CB  1 
ATOM   2597 C  CG  . PHE B 1 53  ? 27.512  -29.612 24.472  1.00 28.02 ? 88  PHE B CG  1 
ATOM   2598 C  CD1 . PHE B 1 53  ? 27.158  -29.149 23.213  1.00 33.06 ? 88  PHE B CD1 1 
ATOM   2599 C  CD2 . PHE B 1 53  ? 26.887  -29.073 25.582  1.00 32.80 ? 88  PHE B CD2 1 
ATOM   2600 C  CE1 . PHE B 1 53  ? 26.189  -28.176 23.067  1.00 28.18 ? 88  PHE B CE1 1 
ATOM   2601 C  CE2 . PHE B 1 53  ? 25.915  -28.093 25.447  1.00 30.24 ? 88  PHE B CE2 1 
ATOM   2602 C  CZ  . PHE B 1 53  ? 25.565  -27.647 24.185  1.00 35.26 ? 88  PHE B CZ  1 
ATOM   2603 N  N   . GLN B 1 54  ? 32.276  -30.873 24.787  1.00 28.35 ? 89  GLN B N   1 
ATOM   2604 C  CA  . GLN B 1 54  ? 33.326  -31.846 24.917  1.00 23.57 ? 89  GLN B CA  1 
ATOM   2605 C  C   . GLN B 1 54  ? 34.399  -31.385 25.883  1.00 25.35 ? 89  GLN B C   1 
ATOM   2606 O  O   . GLN B 1 54  ? 34.482  -30.212 26.181  1.00 27.67 ? 89  GLN B O   1 
ATOM   2607 C  CB  . GLN B 1 54  ? 33.976  -32.081 23.559  1.00 26.51 ? 89  GLN B CB  1 
ATOM   2608 C  CG  . GLN B 1 54  ? 33.090  -32.775 22.542  1.00 29.33 ? 89  GLN B CG  1 
ATOM   2609 C  CD  . GLN B 1 54  ? 33.699  -32.800 21.157  1.00 38.91 ? 89  GLN B CD  1 
ATOM   2610 O  OE1 . GLN B 1 54  ? 34.845  -32.426 20.967  1.00 35.09 ? 89  GLN B OE1 1 
ATOM   2611 N  NE2 . GLN B 1 54  ? 32.930  -33.246 20.183  1.00 54.31 ? 89  GLN B NE2 1 
ATOM   2612 N  N   . LYS B 1 55  ? 35.156  -32.322 26.403  1.00 30.69 ? 90  LYS B N   1 
ATOM   2613 C  CA  . LYS B 1 55  ? 36.270  -31.991 27.268  1.00 34.35 ? 90  LYS B CA  1 
ATOM   2614 C  C   . LYS B 1 55  ? 37.473  -32.866 27.008  1.00 27.56 ? 90  LYS B C   1 
ATOM   2615 O  O   . LYS B 1 55  ? 37.319  -33.979 26.571  1.00 37.36 ? 90  LYS B O   1 
ATOM   2616 C  CB  . LYS B 1 55  ? 35.855  -32.201 28.712  1.00 42.84 ? 90  LYS B CB  1 
ATOM   2617 C  CG  . LYS B 1 55  ? 36.751  -31.530 29.732  1.00 52.96 ? 90  LYS B CG  1 
ATOM   2618 C  CD  . LYS B 1 55  ? 36.300  -31.870 31.140  1.00 61.90 ? 90  LYS B CD  1 
ATOM   2619 C  CE  . LYS B 1 55  ? 37.157  -31.171 32.181  1.00 63.07 ? 90  LYS B CE  1 
ATOM   2620 N  NZ  . LYS B 1 55  ? 36.493  -31.173 33.515  1.00 73.71 ? 90  LYS B NZ  1 
ATOM   2621 N  N   . ALA B 1 56  ? 38.675  -32.350 27.166  1.00 38.55 ? 91  ALA B N   1 
ATOM   2622 C  CA  . ALA B 1 56  ? 39.863  -33.200 27.120  1.00 37.50 ? 91  ALA B CA  1 
ATOM   2623 C  C   . ALA B 1 56  ? 39.954  -33.988 28.425  1.00 45.01 ? 91  ALA B C   1 
ATOM   2624 O  O   . ALA B 1 56  ? 39.576  -33.476 29.454  1.00 66.39 ? 91  ALA B O   1 
ATOM   2625 C  CB  . ALA B 1 56  ? 41.088  -32.383 26.902  1.00 42.45 ? 91  ALA B CB  1 
ATOM   2626 N  N   . PRO B 1 57  ? 40.475  -35.196 28.414  1.00 41.38 ? 92  PRO B N   1 
ATOM   2627 C  CA  . PRO B 1 57  ? 40.831  -36.014 27.262  1.00 37.14 ? 92  PRO B CA  1 
ATOM   2628 C  C   . PRO B 1 57  ? 39.638  -36.388 26.428  1.00 24.53 ? 92  PRO B C   1 
ATOM   2629 O  O   . PRO B 1 57  ? 38.595  -36.684 26.948  1.00 38.32 ? 92  PRO B O   1 
ATOM   2630 C  CB  . PRO B 1 57  ? 41.452  -37.258 27.880  1.00 52.99 ? 92  PRO B CB  1 
ATOM   2631 C  CG  . PRO B 1 57  ? 40.925  -37.303 29.271  1.00 38.14 ? 92  PRO B CG  1 
ATOM   2632 C  CD  . PRO B 1 57  ? 40.760  -35.880 29.684  1.00 45.41 ? 92  PRO B CD  1 
ATOM   2633 N  N   . LEU B 1 58  ? 39.837  -36.403 25.130  1.00 22.79 ? 93  LEU B N   1 
ATOM   2634 C  CA  . LEU B 1 58  ? 38.732  -36.606 24.248  1.00 24.53 ? 93  LEU B CA  1 
ATOM   2635 C  C   . LEU B 1 58  ? 38.767  -37.958 23.592  1.00 25.07 ? 93  LEU B C   1 
ATOM   2636 O  O   . LEU B 1 58  ? 39.751  -38.318 22.977  1.00 23.33 ? 93  LEU B O   1 
ATOM   2637 C  CB  . LEU B 1 58  ? 38.808  -35.491 23.200  1.00 28.59 ? 93  LEU B CB  1 
ATOM   2638 C  CG  . LEU B 1 58  ? 37.733  -35.314 22.146  1.00 35.33 ? 93  LEU B CG  1 
ATOM   2639 C  CD1 . LEU B 1 58  ? 36.386  -35.153 22.821  1.00 41.18 ? 93  LEU B CD1 1 
ATOM   2640 C  CD2 . LEU B 1 58  ? 38.089  -34.075 21.346  1.00 33.62 ? 93  LEU B CD2 1 
ATOM   2641 N  N   . GLU B 1 59  ? 37.667  -38.673 23.711  1.00 20.13 ? 94  GLU B N   1 
ATOM   2642 C  CA  . GLU B 1 59  ? 37.541  -39.964 23.064  1.00 18.66 ? 94  GLU B CA  1 
ATOM   2643 C  C   . GLU B 1 59  ? 37.513  -39.717 21.572  1.00 22.74 ? 94  GLU B C   1 
ATOM   2644 O  O   . GLU B 1 59  ? 36.628  -39.062 21.078  1.00 23.37 ? 94  GLU B O   1 
ATOM   2645 C  CB  . GLU B 1 59  ? 36.300  -40.682 23.518  1.00 24.17 ? 94  GLU B CB  1 
ATOM   2646 C  CG  . GLU B 1 59  ? 36.161  -42.077 22.967  1.00 25.87 ? 94  GLU B CG  1 
ATOM   2647 C  CD  . GLU B 1 59  ? 34.999  -42.836 23.567  1.00 39.39 ? 94  GLU B CD  1 
ATOM   2648 O  OE1 . GLU B 1 59  ? 34.280  -42.258 24.398  1.00 33.64 ? 94  GLU B OE1 1 
ATOM   2649 O  OE2 . GLU B 1 59  ? 34.812  -44.007 23.207  1.00 24.93 ? 94  GLU B OE2 1 
ATOM   2650 N  N   . THR B 1 60  ? 38.477  -40.273 20.876  1.00 18.52 ? 95  THR B N   1 
ATOM   2651 C  CA  . THR B 1 60  ? 38.663  -40.003 19.459  1.00 16.97 ? 95  THR B CA  1 
ATOM   2652 C  C   . THR B 1 60  ? 38.541  -41.305 18.684  1.00 15.59 ? 95  THR B C   1 
ATOM   2653 O  O   . THR B 1 60  ? 39.153  -42.312 19.057  1.00 17.12 ? 95  THR B O   1 
ATOM   2654 C  CB  . THR B 1 60  ? 40.051  -39.396 19.236  1.00 20.07 ? 95  THR B CB  1 
ATOM   2655 O  OG1 . THR B 1 60  ? 40.177  -38.207 20.028  1.00 22.64 ? 95  THR B OG1 1 
ATOM   2656 C  CG2 . THR B 1 60  ? 40.293  -39.073 17.760  1.00 18.00 ? 95  THR B CG2 1 
ATOM   2657 N  N   . SER B 1 61  ? 37.741  -41.274 17.621  1.00 14.83 ? 96  SER B N   1 
ATOM   2658 C  CA  . SER B 1 61  ? 37.592  -42.414 16.730  1.00 16.99 ? 96  SER B CA  1 
ATOM   2659 C  C   . SER B 1 61  ? 38.872  -42.665 15.937  1.00 15.16 ? 96  SER B C   1 
ATOM   2660 O  O   . SER B 1 61  ? 39.655  -41.754 15.668  1.00 16.97 ? 96  SER B O   1 
ATOM   2661 C  CB  . SER B 1 61  ? 36.431  -42.173 15.766  1.00 16.53 ? 96  SER B CB  1 
ATOM   2662 O  OG  . SER B 1 61  ? 35.191  -42.168 16.468  1.00 16.22 ? 96  SER B OG  1 
ATOM   2663 N  N   . VAL B 1 62  ? 39.085  -43.932 15.580  1.00 14.80 ? 97  VAL B N   1 
ATOM   2664 C  CA  . VAL B 1 62  ? 40.106  -44.336 14.613  1.00 14.46 ? 97  VAL B CA  1 
ATOM   2665 C  C   . VAL B 1 62  ? 39.398  -45.192 13.565  1.00 15.40 ? 97  VAL B C   1 
ATOM   2666 O  O   . VAL B 1 62  ? 38.842  -46.247 13.899  1.00 18.03 ? 97  VAL B O   1 
ATOM   2667 C  CB  . VAL B 1 62  ? 41.230  -45.136 15.288  1.00 14.61 ? 97  VAL B CB  1 
ATOM   2668 C  CG1 . VAL B 1 62  ? 42.251  -45.597 14.254  1.00 18.41 ? 97  VAL B CG1 1 
ATOM   2669 C  CG2 . VAL B 1 62  ? 41.902  -44.301 16.382  1.00 18.72 ? 97  VAL B CG2 1 
ATOM   2670 N  N   . THR B 1 63  ? 39.415  -44.752 12.310  1.00 13.33 ? 98  THR B N   1 
ATOM   2671 C  CA  . THR B 1 63  ? 38.573  -45.362 11.289  1.00 14.51 ? 98  THR B CA  1 
ATOM   2672 C  C   . THR B 1 63  ? 39.366  -45.620 10.017  1.00 15.46 ? 98  THR B C   1 
ATOM   2673 O  O   . THR B 1 63  ? 40.228  -44.816 9.637   1.00 19.83 ? 98  THR B O   1 
ATOM   2674 C  CB  . THR B 1 63  ? 37.389  -44.439 10.983  1.00 16.53 ? 98  THR B CB  1 
ATOM   2675 O  OG1 . THR B 1 63  ? 36.714  -44.142 12.212  1.00 16.65 ? 98  THR B OG1 1 
ATOM   2676 C  CG2 . THR B 1 63  ? 36.413  -45.097 10.007  1.00 17.27 ? 98  THR B CG2 1 
ATOM   2677 N  N   . GLY B 1 64  ? 39.087  -46.767 9.386   1.00 15.52 ? 99  GLY B N   1 
ATOM   2678 C  CA  . GLY B 1 64  ? 39.546  -47.058 8.045   1.00 15.98 ? 99  GLY B CA  1 
ATOM   2679 C  C   . GLY B 1 64  ? 38.338  -47.143 7.123   1.00 14.36 ? 99  GLY B C   1 
ATOM   2680 O  O   . GLY B 1 64  ? 37.198  -47.241 7.570   1.00 16.20 ? 99  GLY B O   1 
ATOM   2681 N  N   . TYR B 1 65  ? 38.595  -47.085 5.817   1.00 14.89 ? 100 TYR B N   1 
ATOM   2682 C  CA  . TYR B 1 65  ? 37.507  -46.987 4.844   1.00 16.24 ? 100 TYR B CA  1 
ATOM   2683 C  C   . TYR B 1 65  ? 37.662  -48.041 3.763   1.00 17.81 ? 100 TYR B C   1 
ATOM   2684 O  O   . TYR B 1 65  ? 38.654  -48.052 3.031   1.00 17.34 ? 100 TYR B O   1 
ATOM   2685 C  CB  . TYR B 1 65  ? 37.415  -45.573 4.254   1.00 16.37 ? 100 TYR B CB  1 
ATOM   2686 C  CG  . TYR B 1 65  ? 37.046  -44.581 5.320   1.00 15.54 ? 100 TYR B CG  1 
ATOM   2687 C  CD1 . TYR B 1 65  ? 35.714  -44.332 5.630   1.00 16.80 ? 100 TYR B CD1 1 
ATOM   2688 C  CD2 . TYR B 1 65  ? 38.027  -43.939 6.059   1.00 17.31 ? 100 TYR B CD2 1 
ATOM   2689 C  CE1 . TYR B 1 65  ? 35.374  -43.443 6.634   1.00 17.43 ? 100 TYR B CE1 1 
ATOM   2690 C  CE2 . TYR B 1 65  ? 37.702  -43.054 7.064   1.00 14.72 ? 100 TYR B CE2 1 
ATOM   2691 C  CZ  . TYR B 1 65  ? 36.372  -42.810 7.345   1.00 13.80 ? 100 TYR B CZ  1 
ATOM   2692 O  OH  . TYR B 1 65  ? 36.061  -41.932 8.363   1.00 18.88 ? 100 TYR B OH  1 
ATOM   2693 N  N   . LEU B 1 66  ? 36.678  -48.917 3.649   1.00 17.49 ? 101 LEU B N   1 
ATOM   2694 C  CA  . LEU B 1 66  ? 36.689  -49.974 2.658   1.00 16.76 ? 101 LEU B CA  1 
ATOM   2695 C  C   . LEU B 1 66  ? 35.873  -49.506 1.459   1.00 22.21 ? 101 LEU B C   1 
ATOM   2696 O  O   . LEU B 1 66  ? 34.769  -48.986 1.626   1.00 19.24 ? 101 LEU B O   1 
ATOM   2697 C  CB  . LEU B 1 66  ? 36.052  -51.214 3.280   1.00 21.58 ? 101 LEU B CB  1 
ATOM   2698 C  CG  . LEU B 1 66  ? 36.158  -52.511 2.505   1.00 21.39 ? 101 LEU B CG  1 
ATOM   2699 C  CD1 . LEU B 1 66  ? 37.580  -53.028 2.617   1.00 15.81 ? 101 LEU B CD1 1 
ATOM   2700 C  CD2 . LEU B 1 66  ? 35.199  -53.509 3.094   1.00 23.08 ? 101 LEU B CD2 1 
ATOM   2701 N  N   . VAL B 1 67  ? 36.424  -49.674 0.258   1.00 19.50 ? 102 VAL B N   1 
ATOM   2702 C  CA  . VAL B 1 67  ? 35.779  -49.275 -0.987  1.00 19.90 ? 102 VAL B CA  1 
ATOM   2703 C  C   . VAL B 1 67  ? 35.683  -50.515 -1.860  1.00 22.68 ? 102 VAL B C   1 
ATOM   2704 O  O   . VAL B 1 67  ? 36.710  -51.068 -2.278  1.00 20.65 ? 102 VAL B O   1 
ATOM   2705 C  CB  . VAL B 1 67  ? 36.580  -48.182 -1.719  1.00 20.78 ? 102 VAL B CB  1 
ATOM   2706 C  CG1 . VAL B 1 67  ? 35.825  -47.713 -2.957  1.00 18.37 ? 102 VAL B CG1 1 
ATOM   2707 C  CG2 . VAL B 1 67  ? 36.903  -47.024 -0.784  1.00 19.69 ? 102 VAL B CG2 1 
ATOM   2708 N  N   . ASN B 1 68  ? 34.460  -50.953 -2.139  1.00 17.72 ? 103 ASN B N   1 
ATOM   2709 C  CA  . ASN B 1 68  ? 34.220  -52.004 -3.117  1.00 21.73 ? 103 ASN B CA  1 
ATOM   2710 C  C   . ASN B 1 68  ? 33.720  -51.333 -4.390  1.00 22.49 ? 103 ASN B C   1 
ATOM   2711 O  O   . ASN B 1 68  ? 32.576  -50.864 -4.449  1.00 22.81 ? 103 ASN B O   1 
ATOM   2712 C  CB  . ASN B 1 68  ? 33.233  -53.046 -2.597  1.00 24.69 ? 103 ASN B CB  1 
ATOM   2713 C  CG  . ASN B 1 68  ? 33.179  -54.282 -3.473  1.00 23.27 ? 103 ASN B CG  1 
ATOM   2714 O  OD1 . ASN B 1 68  ? 33.450  -54.217 -4.676  1.00 25.60 ? 103 ASN B OD1 1 
ATOM   2715 N  ND2 . ASN B 1 68  ? 32.837  -55.419 -2.879  1.00 24.12 ? 103 ASN B ND2 1 
ATOM   2716 N  N   . THR B 1 69  ? 34.587  -51.278 -5.404  1.00 21.01 ? 104 THR B N   1 
ATOM   2717 C  CA  . THR B 1 69  ? 34.234  -50.653 -6.668  1.00 22.70 ? 104 THR B CA  1 
ATOM   2718 C  C   . THR B 1 69  ? 33.394  -51.560 -7.549  1.00 26.90 ? 104 THR B C   1 
ATOM   2719 O  O   . THR B 1 69  ? 32.922  -51.116 -8.603  1.00 28.70 ? 104 THR B O   1 
ATOM   2720 C  CB  . THR B 1 69  ? 35.492  -50.258 -7.441  1.00 27.88 ? 104 THR B CB  1 
ATOM   2721 O  OG1 . THR B 1 69  ? 36.122  -51.441 -7.951  1.00 26.70 ? 104 THR B OG1 1 
ATOM   2722 C  CG2 . THR B 1 69  ? 36.454  -49.502 -6.548  1.00 23.56 ? 104 THR B CG2 1 
ATOM   2723 N  N   . GLY B 1 70  ? 33.202  -52.817 -7.144  1.00 26.04 ? 105 GLY B N   1 
ATOM   2724 C  CA  . GLY B 1 70  ? 32.563  -53.831 -7.945  1.00 26.95 ? 105 GLY B CA  1 
ATOM   2725 C  C   . GLY B 1 70  ? 33.545  -54.728 -8.673  1.00 35.50 ? 105 GLY B C   1 
ATOM   2726 O  O   . GLY B 1 70  ? 33.230  -55.890 -8.944  1.00 33.66 ? 105 GLY B O   1 
ATOM   2727 N  N   . SER B 1 71  ? 34.739  -54.216 -8.977  1.00 28.96 ? 106 SER B N   1 
ATOM   2728 C  CA  . SER B 1 71  ? 35.804  -55.028 -9.547  1.00 28.40 ? 106 SER B CA  1 
ATOM   2729 C  C   . SER B 1 71  ? 37.032  -55.139 -8.658  1.00 26.78 ? 106 SER B C   1 
ATOM   2730 O  O   . SER B 1 71  ? 37.856  -56.035 -8.885  1.00 33.46 ? 106 SER B O   1 
ATOM   2731 C  CB  . SER B 1 71  ? 36.218  -54.503 -10.933 1.00 39.15 ? 106 SER B CB  1 
ATOM   2732 O  OG  . SER B 1 71  ? 36.783  -53.207 -10.842 1.00 44.54 ? 106 SER B OG  1 
ATOM   2733 N  N   . LYS B 1 72  ? 37.180  -54.267 -7.661  1.00 24.51 ? 107 LYS B N   1 
ATOM   2734 C  CA  . LYS B 1 72  ? 38.284  -54.332 -6.715  1.00 28.06 ? 107 LYS B CA  1 
ATOM   2735 C  C   . LYS B 1 72  ? 37.770  -53.992 -5.326  1.00 28.46 ? 107 LYS B C   1 
ATOM   2736 O  O   . LYS B 1 72  ? 36.805  -53.239 -5.170  1.00 23.14 ? 107 LYS B O   1 
ATOM   2737 C  CB  . LYS B 1 72  ? 39.422  -53.373 -7.103  1.00 27.07 ? 107 LYS B CB  1 
ATOM   2738 C  CG  . LYS B 1 72  ? 40.190  -53.812 -8.346  1.00 32.33 ? 107 LYS B CG  1 
ATOM   2739 C  CD  . LYS B 1 72  ? 41.344  -54.743 -7.983  1.00 34.40 ? 107 LYS B CD  1 
ATOM   2740 C  CE  . LYS B 1 72  ? 41.749  -55.640 -9.151  1.00 49.96 ? 107 LYS B CE  1 
ATOM   2741 N  NZ  . LYS B 1 72  ? 41.809  -54.874 -10.420 1.00 53.90 ? 107 LYS B NZ  1 
ATOM   2742 N  N   . LEU B 1 73  ? 38.416  -54.570 -4.319  1.00 23.19 ? 108 LEU B N   1 
ATOM   2743 C  CA  . LEU B 1 73  ? 38.138  -54.266 -2.922  1.00 24.50 ? 108 LEU B CA  1 
ATOM   2744 C  C   . LEU B 1 73  ? 39.384  -53.617 -2.340  1.00 20.51 ? 108 LEU B C   1 
ATOM   2745 O  O   . LEU B 1 73  ? 40.438  -54.258 -2.256  1.00 22.77 ? 108 LEU B O   1 
ATOM   2746 C  CB  . LEU B 1 73  ? 37.782  -55.538 -2.153  1.00 25.19 ? 108 LEU B CB  1 
ATOM   2747 C  CG  . LEU B 1 73  ? 37.313  -55.318 -0.717  1.00 24.92 ? 108 LEU B CG  1 
ATOM   2748 C  CD1 . LEU B 1 73  ? 36.005  -54.525 -0.686  1.00 23.76 ? 108 LEU B CD1 1 
ATOM   2749 C  CD2 . LEU B 1 73  ? 37.171  -56.654 0.008   1.00 26.53 ? 108 LEU B CD2 1 
ATOM   2750 N  N   . VAL B 1 74  ? 39.260  -52.353 -1.939  1.00 20.31 ? 109 VAL B N   1 
ATOM   2751 C  CA  . VAL B 1 74  ? 40.385  -51.532 -1.515  1.00 22.17 ? 109 VAL B CA  1 
ATOM   2752 C  C   . VAL B 1 74  ? 40.130  -51.080 -0.090  1.00 19.02 ? 109 VAL B C   1 
ATOM   2753 O  O   . VAL B 1 74  ? 39.016  -50.672 0.246   1.00 19.90 ? 109 VAL B O   1 
ATOM   2754 C  CB  . VAL B 1 74  ? 40.534  -50.307 -2.441  1.00 22.28 ? 109 VAL B CB  1 
ATOM   2755 C  CG1 . VAL B 1 74  ? 41.674  -49.426 -1.967  1.00 23.11 ? 109 VAL B CG1 1 
ATOM   2756 C  CG2 . VAL B 1 74  ? 40.748  -50.759 -3.877  1.00 24.31 ? 109 VAL B CG2 1 
ATOM   2757 N  N   . LEU B 1 75  ? 41.154  -51.151 0.754   1.00 18.25 ? 110 LEU B N   1 
ATOM   2758 C  CA  . LEU B 1 75  ? 41.043  -50.696 2.136   1.00 17.45 ? 110 LEU B CA  1 
ATOM   2759 C  C   . LEU B 1 75  ? 41.968  -49.499 2.306   1.00 20.18 ? 110 LEU B C   1 
ATOM   2760 O  O   . LEU B 1 75  ? 43.164  -49.586 2.001   1.00 18.89 ? 110 LEU B O   1 
ATOM   2761 C  CB  . LEU B 1 75  ? 41.413  -51.820 3.109   1.00 17.42 ? 110 LEU B CB  1 
ATOM   2762 C  CG  . LEU B 1 75  ? 41.443  -51.477 4.604   1.00 19.07 ? 110 LEU B CG  1 
ATOM   2763 C  CD1 . LEU B 1 75  ? 40.127  -50.890 5.090   1.00 18.45 ? 110 LEU B CD1 1 
ATOM   2764 C  CD2 . LEU B 1 75  ? 41.794  -52.714 5.416   1.00 26.75 ? 110 LEU B CD2 1 
ATOM   2765 N  N   . VAL B 1 76  ? 41.416  -48.382 2.757   1.00 18.09 ? 111 VAL B N   1 
ATOM   2766 C  CA  . VAL B 1 76  ? 42.176  -47.173 3.040   1.00 16.77 ? 111 VAL B CA  1 
ATOM   2767 C  C   . VAL B 1 76  ? 42.384  -47.113 4.549   1.00 16.33 ? 111 VAL B C   1 
ATOM   2768 O  O   . VAL B 1 76  ? 41.432  -46.896 5.311   1.00 18.88 ? 111 VAL B O   1 
ATOM   2769 C  CB  . VAL B 1 76  ? 41.470  -45.924 2.496   1.00 16.96 ? 111 VAL B CB  1 
ATOM   2770 C  CG1 . VAL B 1 76  ? 42.260  -44.661 2.852   1.00 19.01 ? 111 VAL B CG1 1 
ATOM   2771 C  CG2 . VAL B 1 76  ? 41.290  -46.055 0.982   1.00 19.25 ? 111 VAL B CG2 1 
ATOM   2772 N  N   . ASP B 1 77  ? 43.634  -47.340 4.964   1.00 14.49 ? 112 ASP B N   1 
ATOM   2773 C  CA  . ASP B 1 77  ? 44.091  -47.383 6.352   1.00 17.77 ? 112 ASP B CA  1 
ATOM   2774 C  C   . ASP B 1 77  ? 43.583  -48.623 7.081   1.00 16.07 ? 112 ASP B C   1 
ATOM   2775 O  O   . ASP B 1 77  ? 42.575  -49.213 6.682   1.00 19.10 ? 112 ASP B O   1 
ATOM   2776 C  CB  . ASP B 1 77  ? 43.770  -46.088 7.094   1.00 15.89 ? 112 ASP B CB  1 
ATOM   2777 C  CG  . ASP B 1 77  ? 44.608  -44.924 6.592   1.00 26.89 ? 112 ASP B CG  1 
ATOM   2778 O  OD1 . ASP B 1 77  ? 45.635  -45.177 5.906   1.00 20.99 ? 112 ASP B OD1 1 
ATOM   2779 O  OD2 . ASP B 1 77  ? 44.281  -43.767 6.925   1.00 22.80 ? 112 ASP B OD2 1 
ATOM   2780 N  N   . THR B 1 78  ? 44.298  -49.059 8.124   1.00 15.32 ? 113 THR B N   1 
ATOM   2781 C  CA  . THR B 1 78  ? 44.078  -50.395 8.673   1.00 19.45 ? 113 THR B CA  1 
ATOM   2782 C  C   . THR B 1 78  ? 43.914  -50.415 10.185  1.00 17.88 ? 113 THR B C   1 
ATOM   2783 O  O   . THR B 1 78  ? 43.835  -51.507 10.767  1.00 18.29 ? 113 THR B O   1 
ATOM   2784 C  CB  . THR B 1 78  ? 45.214  -51.363 8.288   1.00 16.32 ? 113 THR B CB  1 
ATOM   2785 O  OG1 . THR B 1 78  ? 46.422  -51.031 8.996   1.00 19.05 ? 113 THR B OG1 1 
ATOM   2786 C  CG2 . THR B 1 78  ? 45.471  -51.326 6.798   1.00 17.38 ? 113 THR B CG2 1 
ATOM   2787 N  N   . GLY B 1 79  ? 43.876  -49.260 10.832  1.00 16.04 ? 114 GLY B N   1 
ATOM   2788 C  CA  . GLY B 1 79  ? 43.849  -49.224 12.277  1.00 17.85 ? 114 GLY B CA  1 
ATOM   2789 C  C   . GLY B 1 79  ? 45.206  -49.539 12.881  1.00 20.70 ? 114 GLY B C   1 
ATOM   2790 O  O   . GLY B 1 79  ? 46.248  -49.566 12.210  1.00 17.22 ? 114 GLY B O   1 
ATOM   2791 N  N   . ALA B 1 80  ? 45.178  -49.801 14.187  1.00 18.70 ? 115 ALA B N   1 
ATOM   2792 C  CA  . ALA B 1 80  ? 46.390  -49.887 14.991  1.00 19.17 ? 115 ALA B CA  1 
ATOM   2793 C  C   . ALA B 1 80  ? 46.785  -51.308 15.372  1.00 19.81 ? 115 ALA B C   1 
ATOM   2794 O  O   . ALA B 1 80  ? 47.880  -51.497 15.911  1.00 20.65 ? 115 ALA B O   1 
ATOM   2795 C  CB  . ALA B 1 80  ? 46.218  -49.059 16.274  1.00 18.75 ? 115 ALA B CB  1 
ATOM   2796 N  N   . ALA B 1 81  ? 45.943  -52.307 15.113  1.00 18.58 ? 116 ALA B N   1 
ATOM   2797 C  CA  . ALA B 1 81  ? 46.126  -53.652 15.694  1.00 19.04 ? 116 ALA B CA  1 
ATOM   2798 C  C   . ALA B 1 81  ? 46.352  -53.471 17.196  1.00 22.47 ? 116 ALA B C   1 
ATOM   2799 O  O   . ALA B 1 81  ? 45.555  -52.779 17.844  1.00 21.67 ? 116 ALA B O   1 
ATOM   2800 C  CB  . ALA B 1 81  ? 47.183  -54.459 14.948  1.00 24.82 ? 116 ALA B CB  1 
ATOM   2801 N  N   . GLY B 1 82  ? 47.425  -54.014 17.772  1.00 21.89 ? 117 GLY B N   1 
ATOM   2802 C  CA  . GLY B 1 82  ? 47.742  -53.820 19.172  1.00 23.93 ? 117 GLY B CA  1 
ATOM   2803 C  C   . GLY B 1 82  ? 48.768  -52.748 19.479  1.00 27.82 ? 117 GLY B C   1 
ATOM   2804 O  O   . GLY B 1 82  ? 49.272  -52.709 20.607  1.00 33.82 ? 117 GLY B O   1 
ATOM   2805 N  N   . LEU B 1 83  ? 49.086  -51.867 18.527  1.00 22.58 ? 118 LEU B N   1 
ATOM   2806 C  CA  . LEU B 1 83  ? 50.189  -50.930 18.724  1.00 22.64 ? 118 LEU B CA  1 
ATOM   2807 C  C   . LEU B 1 83  ? 49.838  -49.805 19.697  1.00 28.99 ? 118 LEU B C   1 
ATOM   2808 O  O   . LEU B 1 83  ? 50.730  -49.275 20.369  1.00 36.80 ? 118 LEU B O   1 
ATOM   2809 C  CB  . LEU B 1 83  ? 50.646  -50.357 17.380  1.00 22.63 ? 118 LEU B CB  1 
ATOM   2810 C  CG  . LEU B 1 83  ? 51.237  -51.330 16.357  1.00 28.59 ? 118 LEU B CG  1 
ATOM   2811 C  CD1 . LEU B 1 83  ? 51.802  -50.567 15.160  1.00 27.38 ? 118 LEU B CD1 1 
ATOM   2812 C  CD2 . LEU B 1 83  ? 52.295  -52.212 16.985  1.00 30.56 ? 118 LEU B CD2 1 
ATOM   2813 N  N   . PHE B 1 84  ? 48.567  -49.413 19.782  1.00 26.01 ? 119 PHE B N   1 
ATOM   2814 C  CA  . PHE B 1 84  ? 48.131  -48.289 20.612  1.00 29.45 ? 119 PHE B CA  1 
ATOM   2815 C  C   . PHE B 1 84  ? 47.197  -48.710 21.739  1.00 33.05 ? 119 PHE B C   1 
ATOM   2816 O  O   . PHE B 1 84  ? 46.241  -48.003 22.064  1.00 44.94 ? 119 PHE B O   1 
ATOM   2817 C  CB  . PHE B 1 84  ? 47.492  -47.171 19.788  1.00 24.48 ? 119 PHE B CB  1 
ATOM   2818 C  CG  . PHE B 1 84  ? 48.468  -46.171 19.246  1.00 31.96 ? 119 PHE B CG  1 
ATOM   2819 C  CD1 . PHE B 1 84  ? 49.735  -46.051 19.790  1.00 40.64 ? 119 PHE B CD1 1 
ATOM   2820 C  CD2 . PHE B 1 84  ? 48.107  -45.331 18.201  1.00 36.84 ? 119 PHE B CD2 1 
ATOM   2821 C  CE1 . PHE B 1 84  ? 50.631  -45.116 19.298  1.00 42.15 ? 119 PHE B CE1 1 
ATOM   2822 C  CE2 . PHE B 1 84  ? 48.998  -44.398 17.701  1.00 43.15 ? 119 PHE B CE2 1 
ATOM   2823 C  CZ  . PHE B 1 84  ? 50.261  -44.290 18.248  1.00 34.23 ? 119 PHE B CZ  1 
ATOM   2824 N  N   . GLY B 1 85  ? 47.453  -49.859 22.353  1.00 29.52 ? 120 GLY B N   1 
ATOM   2825 C  CA  . GLY B 1 85  ? 46.709  -50.251 23.524  1.00 29.18 ? 120 GLY B CA  1 
ATOM   2826 C  C   . GLY B 1 85  ? 45.431  -51.013 23.227  1.00 46.86 ? 120 GLY B C   1 
ATOM   2827 O  O   . GLY B 1 85  ? 45.014  -51.173 22.073  1.00 27.55 ? 120 GLY B O   1 
ATOM   2828 N  N   . PRO B 1 86  ? 44.761  -51.471 24.290  1.00 28.16 ? 121 PRO B N   1 
ATOM   2829 C  CA  . PRO B 1 86  ? 43.666  -52.437 24.124  1.00 30.43 ? 121 PRO B CA  1 
ATOM   2830 C  C   . PRO B 1 86  ? 42.351  -51.849 23.636  1.00 27.43 ? 121 PRO B C   1 
ATOM   2831 O  O   . PRO B 1 86  ? 41.440  -52.626 23.316  1.00 29.78 ? 121 PRO B O   1 
ATOM   2832 C  CB  . PRO B 1 86  ? 43.512  -53.027 25.530  1.00 37.36 ? 121 PRO B CB  1 
ATOM   2833 C  CG  . PRO B 1 86  ? 43.929  -51.907 26.433  1.00 35.44 ? 121 PRO B CG  1 
ATOM   2834 C  CD  . PRO B 1 86  ? 45.010  -51.146 25.706  1.00 44.09 ? 121 PRO B CD  1 
ATOM   2835 N  N   . THR B 1 87  ? 42.213  -50.523 23.553  1.00 23.42 ? 122 THR B N   1 
ATOM   2836 C  CA  . THR B 1 87  ? 40.956  -49.959 23.073  1.00 20.86 ? 122 THR B CA  1 
ATOM   2837 C  C   . THR B 1 87  ? 40.884  -49.872 21.552  1.00 27.52 ? 122 THR B C   1 
ATOM   2838 O  O   . THR B 1 87  ? 39.818  -49.539 21.020  1.00 23.15 ? 122 THR B O   1 
ATOM   2839 C  CB  . THR B 1 87  ? 40.686  -48.581 23.699  1.00 24.04 ? 122 THR B CB  1 
ATOM   2840 O  OG1 . THR B 1 87  ? 41.565  -47.609 23.121  1.00 27.76 ? 122 THR B OG1 1 
ATOM   2841 C  CG2 . THR B 1 87  ? 40.898  -48.618 25.212  1.00 31.98 ? 122 THR B CG2 1 
ATOM   2842 N  N   . LEU B 1 88  ? 41.982  -50.153 20.845  1.00 22.22 ? 123 LEU B N   1 
ATOM   2843 C  CA  . LEU B 1 88  ? 42.024  -50.134 19.393  1.00 19.90 ? 123 LEU B CA  1 
ATOM   2844 C  C   . LEU B 1 88  ? 42.227  -51.548 18.859  1.00 22.37 ? 123 LEU B C   1 
ATOM   2845 O  O   . LEU B 1 88  ? 42.246  -52.529 19.614  1.00 27.02 ? 123 LEU B O   1 
ATOM   2846 C  CB  . LEU B 1 88  ? 43.095  -49.158 18.891  1.00 18.43 ? 123 LEU B CB  1 
ATOM   2847 C  CG  . LEU B 1 88  ? 42.841  -47.695 19.265  1.00 19.24 ? 123 LEU B CG  1 
ATOM   2848 C  CD1 . LEU B 1 88  ? 43.969  -46.793 18.783  1.00 23.52 ? 123 LEU B CD1 1 
ATOM   2849 C  CD2 . LEU B 1 88  ? 41.515  -47.216 18.688  1.00 19.02 ? 123 LEU B CD2 1 
ATOM   2850 N  N   . GLY B 1 89  ? 42.385  -51.652 17.542  1.00 19.09 ? 124 GLY B N   1 
ATOM   2851 C  CA  . GLY B 1 89  ? 42.568  -52.949 16.922  1.00 18.64 ? 124 GLY B CA  1 
ATOM   2852 C  C   . GLY B 1 89  ? 41.295  -53.683 16.578  1.00 20.15 ? 124 GLY B C   1 
ATOM   2853 O  O   . GLY B 1 89  ? 41.335  -54.900 16.378  1.00 23.14 ? 124 GLY B O   1 
ATOM   2854 N  N   . ARG B 1 90  ? 40.165  -52.983 16.498  1.00 17.57 ? 125 ARG B N   1 
ATOM   2855 C  CA  . ARG B 1 90  ? 38.893  -53.605 16.158  1.00 18.43 ? 125 ARG B CA  1 
ATOM   2856 C  C   . ARG B 1 90  ? 38.658  -53.743 14.662  1.00 16.91 ? 125 ARG B C   1 
ATOM   2857 O  O   . ARG B 1 90  ? 37.665  -54.372 14.270  1.00 21.15 ? 125 ARG B O   1 
ATOM   2858 C  CB  . ARG B 1 90  ? 37.724  -52.805 16.747  1.00 19.82 ? 125 ARG B CB  1 
ATOM   2859 C  CG  . ARG B 1 90  ? 37.859  -52.428 18.213  1.00 31.36 ? 125 ARG B CG  1 
ATOM   2860 C  CD  . ARG B 1 90  ? 37.521  -53.604 19.119  1.00 41.34 ? 125 ARG B CD  1 
ATOM   2861 N  NE  . ARG B 1 90  ? 37.594  -53.253 20.533  1.00 58.48 ? 125 ARG B NE  1 
ATOM   2862 C  CZ  . ARG B 1 90  ? 38.718  -53.165 21.233  1.00 40.25 ? 125 ARG B CZ  1 
ATOM   2863 N  NH1 . ARG B 1 90  ? 39.898  -53.385 20.678  1.00 32.72 ? 125 ARG B NH1 1 
ATOM   2864 N  NH2 . ARG B 1 90  ? 38.654  -52.850 22.525  1.00 50.90 ? 125 ARG B NH2 1 
ATOM   2865 N  N   . LEU B 1 91  ? 39.535  -53.192 13.817  1.00 19.28 ? 126 LEU B N   1 
ATOM   2866 C  CA  . LEU B 1 91  ? 39.174  -53.033 12.411  1.00 21.15 ? 126 LEU B CA  1 
ATOM   2867 C  C   . LEU B 1 91  ? 39.017  -54.374 11.698  1.00 19.23 ? 126 LEU B C   1 
ATOM   2868 O  O   . LEU B 1 91  ? 38.114  -54.526 10.873  1.00 19.88 ? 126 LEU B O   1 
ATOM   2869 C  CB  . LEU B 1 91  ? 40.136  -52.089 11.680  1.00 15.70 ? 126 LEU B CB  1 
ATOM   2870 C  CG  . LEU B 1 91  ? 39.821  -51.833 10.198  1.00 20.16 ? 126 LEU B CG  1 
ATOM   2871 C  CD1 . LEU B 1 91  ? 40.226  -50.427 9.826   1.00 17.19 ? 126 LEU B CD1 1 
ATOM   2872 C  CD2 . LEU B 1 91  ? 40.546  -52.828 9.278   1.00 18.78 ? 126 LEU B CD2 1 
ATOM   2873 N  N   . LEU B 1 92  ? 39.891  -55.351 11.970  1.00 18.59 ? 127 LEU B N   1 
ATOM   2874 C  CA  . LEU B 1 92  ? 39.762  -56.644 11.293  1.00 19.72 ? 127 LEU B CA  1 
ATOM   2875 C  C   . LEU B 1 92  ? 38.441  -57.324 11.640  1.00 18.93 ? 127 LEU B C   1 
ATOM   2876 O  O   . LEU B 1 92  ? 37.749  -57.862 10.759  1.00 22.83 ? 127 LEU B O   1 
ATOM   2877 C  CB  . LEU B 1 92  ? 40.937  -57.555 11.650  1.00 20.87 ? 127 LEU B CB  1 
ATOM   2878 C  CG  . LEU B 1 92  ? 42.110  -57.608 10.673  1.00 52.20 ? 127 LEU B CG  1 
ATOM   2879 C  CD1 . LEU B 1 92  ? 41.638  -58.162 9.348   1.00 32.21 ? 127 LEU B CD1 1 
ATOM   2880 C  CD2 . LEU B 1 92  ? 42.724  -56.230 10.491  1.00 44.95 ? 127 LEU B CD2 1 
ATOM   2881 N  N   . ALA B 1 93  ? 38.061  -57.286 12.920  1.00 19.40 ? 128 ALA B N   1 
ATOM   2882 C  CA  . ALA B 1 93  ? 36.800  -57.893 13.333  1.00 27.01 ? 128 ALA B CA  1 
ATOM   2883 C  C   . ALA B 1 93  ? 35.614  -57.181 12.694  1.00 19.47 ? 128 ALA B C   1 
ATOM   2884 O  O   . ALA B 1 93  ? 34.614  -57.819 12.335  1.00 22.64 ? 128 ALA B O   1 
ATOM   2885 C  CB  . ALA B 1 93  ? 36.675  -57.866 14.855  1.00 23.69 ? 128 ALA B CB  1 
ATOM   2886 N  N   . ASN B 1 94  ? 35.699  -55.859 12.564  1.00 18.43 ? 129 ASN B N   1 
ATOM   2887 C  CA  . ASN B 1 94  ? 34.606  -55.119 11.943  1.00 19.19 ? 129 ASN B CA  1 
ATOM   2888 C  C   . ASN B 1 94  ? 34.567  -55.325 10.435  1.00 25.93 ? 129 ASN B C   1 
ATOM   2889 O  O   . ASN B 1 94  ? 33.487  -55.311 9.845   1.00 20.76 ? 129 ASN B O   1 
ATOM   2890 C  CB  . ASN B 1 94  ? 34.647  -53.645 12.337  1.00 16.22 ? 129 ASN B CB  1 
ATOM   2891 C  CG  . ASN B 1 94  ? 34.225  -53.430 13.781  1.00 20.29 ? 129 ASN B CG  1 
ATOM   2892 O  OD1 . ASN B 1 94  ? 33.310  -54.101 14.274  1.00 22.51 ? 129 ASN B OD1 1 
ATOM   2893 N  ND2 . ASN B 1 94  ? 34.894  -52.515 14.470  1.00 17.08 ? 129 ASN B ND2 1 
ATOM   2894 N  N   . LEU B 1 95  ? 35.722  -55.520 9.798   1.00 22.73 ? 130 LEU B N   1 
ATOM   2895 C  CA  . LEU B 1 95  ? 35.727  -55.927 8.397   1.00 20.21 ? 130 LEU B CA  1 
ATOM   2896 C  C   . LEU B 1 95  ? 34.962  -57.232 8.222   1.00 19.12 ? 130 LEU B C   1 
ATOM   2897 O  O   . LEU B 1 95  ? 34.132  -57.368 7.310   1.00 22.05 ? 130 LEU B O   1 
ATOM   2898 C  CB  . LEU B 1 95  ? 37.169  -56.101 7.918   1.00 18.95 ? 130 LEU B CB  1 
ATOM   2899 C  CG  . LEU B 1 95  ? 37.318  -56.650 6.495   1.00 23.36 ? 130 LEU B CG  1 
ATOM   2900 C  CD1 . LEU B 1 95  ? 37.014  -55.575 5.471   1.00 35.79 ? 130 LEU B CD1 1 
ATOM   2901 C  CD2 . LEU B 1 95  ? 38.704  -57.228 6.275   1.00 36.41 ? 130 LEU B CD2 1 
ATOM   2902 N  N   . LYS B 1 96  ? 35.230  -58.207 9.100   1.00 21.29 ? 131 LYS B N   1 
ATOM   2903 C  CA  . LYS B 1 96  ? 34.522  -59.484 9.028   1.00 22.26 ? 131 LYS B CA  1 
ATOM   2904 C  C   . LYS B 1 96  ? 33.031  -59.317 9.316   1.00 23.53 ? 131 LYS B C   1 
ATOM   2905 O  O   . LYS B 1 96  ? 32.191  -59.915 8.632   1.00 24.75 ? 131 LYS B O   1 
ATOM   2906 C  CB  . LYS B 1 96  ? 35.172  -60.490 9.977   1.00 25.27 ? 131 LYS B CB  1 
ATOM   2907 C  CG  . LYS B 1 96  ? 36.622  -60.780 9.596   1.00 29.50 ? 131 LYS B CG  1 
ATOM   2908 C  CD  . LYS B 1 96  ? 37.339  -61.645 10.624  1.00 32.51 ? 131 LYS B CD  1 
ATOM   2909 C  CE  . LYS B 1 96  ? 38.821  -61.737 10.284  1.00 52.56 ? 131 LYS B CE  1 
ATOM   2910 N  NZ  . LYS B 1 96  ? 39.576  -62.575 11.251  1.00 50.23 ? 131 LYS B NZ  1 
ATOM   2911 N  N   . ALA B 1 97  ? 32.679  -58.496 10.309  1.00 21.99 ? 132 ALA B N   1 
ATOM   2912 C  CA  . ALA B 1 97  ? 31.266  -58.254 10.590  1.00 21.33 ? 132 ALA B CA  1 
ATOM   2913 C  C   . ALA B 1 97  ? 30.574  -57.577 9.414   1.00 23.37 ? 132 ALA B C   1 
ATOM   2914 O  O   . ALA B 1 97  ? 29.387  -57.825 9.162   1.00 22.38 ? 132 ALA B O   1 
ATOM   2915 C  CB  . ALA B 1 97  ? 31.115  -57.415 11.857  1.00 28.02 ? 132 ALA B CB  1 
ATOM   2916 N  N   . ALA B 1 98  ? 31.302  -56.733 8.676   1.00 20.61 ? 133 ALA B N   1 
ATOM   2917 C  CA  . ALA B 1 98  ? 30.789  -56.080 7.477   1.00 22.98 ? 133 ALA B CA  1 
ATOM   2918 C  C   . ALA B 1 98  ? 30.657  -57.034 6.291   1.00 22.62 ? 133 ALA B C   1 
ATOM   2919 O  O   . ALA B 1 98  ? 30.254  -56.602 5.204   1.00 22.66 ? 133 ALA B O   1 
ATOM   2920 C  CB  . ALA B 1 98  ? 31.669  -54.878 7.112   1.00 20.34 ? 133 ALA B CB  1 
ATOM   2921 N  N   . GLY B 1 99  ? 30.987  -58.307 6.461   1.00 21.27 ? 134 GLY B N   1 
ATOM   2922 C  CA  . GLY B 1 99  ? 30.719  -59.304 5.446   1.00 25.08 ? 134 GLY B CA  1 
ATOM   2923 C  C   . GLY B 1 99  ? 31.879  -59.648 4.543   1.00 28.34 ? 134 GLY B C   1 
ATOM   2924 O  O   . GLY B 1 99  ? 31.676  -60.353 3.549   1.00 27.49 ? 134 GLY B O   1 
ATOM   2925 N  N   . TYR B 1 100 ? 33.082  -59.177 4.849   1.00 22.74 ? 135 TYR B N   1 
ATOM   2926 C  CA  . TYR B 1 100 ? 34.247  -59.455 4.027   1.00 24.43 ? 135 TYR B CA  1 
ATOM   2927 C  C   . TYR B 1 100 ? 35.283  -60.246 4.811   1.00 25.77 ? 135 TYR B C   1 
ATOM   2928 O  O   . TYR B 1 100 ? 35.296  -60.251 6.045   1.00 34.91 ? 135 TYR B O   1 
ATOM   2929 C  CB  . TYR B 1 100 ? 34.890  -58.162 3.508   1.00 23.64 ? 135 TYR B CB  1 
ATOM   2930 C  CG  . TYR B 1 100 ? 34.027  -57.415 2.526   1.00 22.83 ? 135 TYR B CG  1 
ATOM   2931 C  CD1 . TYR B 1 100 ? 33.970  -57.811 1.194   1.00 25.71 ? 135 TYR B CD1 1 
ATOM   2932 C  CD2 . TYR B 1 100 ? 33.275  -56.317 2.922   1.00 23.04 ? 135 TYR B CD2 1 
ATOM   2933 C  CE1 . TYR B 1 100 ? 33.186  -57.135 0.282   1.00 30.66 ? 135 TYR B CE1 1 
ATOM   2934 C  CE2 . TYR B 1 100 ? 32.490  -55.628 2.016   1.00 26.26 ? 135 TYR B CE2 1 
ATOM   2935 C  CZ  . TYR B 1 100 ? 32.449  -56.043 0.696   1.00 23.76 ? 135 TYR B CZ  1 
ATOM   2936 O  OH  . TYR B 1 100 ? 31.667  -55.369 -0.213  1.00 26.82 ? 135 TYR B OH  1 
ATOM   2937 N  N   . GLN B 1 101 ? 36.160  -60.908 4.071   1.00 25.20 ? 136 GLN B N   1 
ATOM   2938 C  CA  . GLN B 1 101 ? 37.305  -61.584 4.641   1.00 25.87 ? 136 GLN B CA  1 
ATOM   2939 C  C   . GLN B 1 101 ? 38.578  -60.835 4.267   1.00 26.47 ? 136 GLN B C   1 
ATOM   2940 O  O   . GLN B 1 101 ? 38.658  -60.242 3.186   1.00 25.29 ? 136 GLN B O   1 
ATOM   2941 C  CB  . GLN B 1 101 ? 37.397  -63.017 4.107   1.00 28.47 ? 136 GLN B CB  1 
ATOM   2942 C  CG  . GLN B 1 101 ? 36.310  -63.945 4.655   1.00 30.74 ? 136 GLN B CG  1 
ATOM   2943 C  CD  . GLN B 1 101 ? 36.176  -63.858 6.171   1.00 39.52 ? 136 GLN B CD  1 
ATOM   2944 O  OE1 . GLN B 1 101 ? 37.168  -63.921 6.903   1.00 38.96 ? 136 GLN B OE1 1 
ATOM   2945 N  NE2 . GLN B 1 101 ? 34.944  -63.719 6.646   1.00 43.37 ? 136 GLN B NE2 1 
ATOM   2946 N  N   . PRO B 1 102 ? 39.589  -60.835 5.139   1.00 27.24 ? 137 PRO B N   1 
ATOM   2947 C  CA  . PRO B 1 102 ? 40.832  -60.117 4.813   1.00 20.41 ? 137 PRO B CA  1 
ATOM   2948 C  C   . PRO B 1 102 ? 41.466  -60.595 3.520   1.00 22.06 ? 137 PRO B C   1 
ATOM   2949 O  O   . PRO B 1 102 ? 42.075  -59.794 2.798   1.00 30.28 ? 137 PRO B O   1 
ATOM   2950 C  CB  . PRO B 1 102 ? 41.731  -60.417 6.021   1.00 30.30 ? 137 PRO B CB  1 
ATOM   2951 C  CG  . PRO B 1 102 ? 40.786  -60.734 7.127   1.00 39.95 ? 137 PRO B CG  1 
ATOM   2952 C  CD  . PRO B 1 102 ? 39.641  -61.451 6.477   1.00 28.95 ? 137 PRO B CD  1 
ATOM   2953 N  N   . GLU B 1 103 ? 41.329  -61.886 3.208   1.00 23.14 ? 138 GLU B N   1 
ATOM   2954 C  CA  . GLU B 1 103 ? 41.878  -62.450 1.984   1.00 25.40 ? 138 GLU B CA  1 
ATOM   2955 C  C   . GLU B 1 103 ? 41.294  -61.796 0.737   1.00 30.56 ? 138 GLU B C   1 
ATOM   2956 O  O   . GLU B 1 103 ? 41.917  -61.856 -0.330  1.00 28.05 ? 138 GLU B O   1 
ATOM   2957 C  CB  . GLU B 1 103 ? 41.575  -63.950 1.957   1.00 28.61 ? 138 GLU B CB  1 
ATOM   2958 C  CG  . GLU B 1 103 ? 42.369  -64.763 2.977   1.00 37.05 ? 138 GLU B CG  1 
ATOM   2959 C  CD  . GLU B 1 103 ? 41.879  -64.570 4.414   1.00 58.29 ? 138 GLU B CD  1 
ATOM   2960 O  OE1 . GLU B 1 103 ? 40.746  -64.069 4.612   1.00 35.19 ? 138 GLU B OE1 1 
ATOM   2961 O  OE2 . GLU B 1 103 ? 42.633  -64.916 5.348   1.00 57.77 ? 138 GLU B OE2 1 
ATOM   2962 N  N   . GLN B 1 104 ? 40.115  -61.173 0.842   1.00 28.00 ? 139 GLN B N   1 
ATOM   2963 C  CA  . GLN B 1 104 ? 39.468  -60.573 -0.320  1.00 30.86 ? 139 GLN B CA  1 
ATOM   2964 C  C   . GLN B 1 104 ? 39.988  -59.181 -0.650  1.00 26.62 ? 139 GLN B C   1 
ATOM   2965 O  O   . GLN B 1 104 ? 39.671  -58.669 -1.730  1.00 24.56 ? 139 GLN B O   1 
ATOM   2966 C  CB  . GLN B 1 104 ? 37.964  -60.460 -0.099  1.00 22.81 ? 139 GLN B CB  1 
ATOM   2967 C  CG  . GLN B 1 104 ? 37.247  -61.776 0.100   1.00 23.67 ? 139 GLN B CG  1 
ATOM   2968 C  CD  . GLN B 1 104 ? 35.765  -61.552 0.325   1.00 28.01 ? 139 GLN B CD  1 
ATOM   2969 O  OE1 . GLN B 1 104 ? 35.344  -61.188 1.428   1.00 26.23 ? 139 GLN B OE1 1 
ATOM   2970 N  NE2 . GLN B 1 104 ? 34.966  -61.774 -0.713  1.00 37.41 ? 139 GLN B NE2 1 
ATOM   2971 N  N   . VAL B 1 105 ? 40.768  -58.561 0.235   1.00 23.04 ? 140 VAL B N   1 
ATOM   2972 C  CA  . VAL B 1 105 ? 41.240  -57.201 -0.007  1.00 22.30 ? 140 VAL B CA  1 
ATOM   2973 C  C   . VAL B 1 105 ? 42.321  -57.226 -1.080  1.00 27.96 ? 140 VAL B C   1 
ATOM   2974 O  O   . VAL B 1 105 ? 43.346  -57.899 -0.932  1.00 26.35 ? 140 VAL B O   1 
ATOM   2975 C  CB  . VAL B 1 105 ? 41.751  -56.560 1.286   1.00 21.07 ? 140 VAL B CB  1 
ATOM   2976 C  CG1 . VAL B 1 105 ? 42.318  -55.172 1.006   1.00 23.81 ? 140 VAL B CG1 1 
ATOM   2977 C  CG2 . VAL B 1 105 ? 40.621  -56.490 2.324   1.00 23.98 ? 140 VAL B CG2 1 
ATOM   2978 N  N   . ASP B 1 106 ? 42.103  -56.476 -2.159  1.00 22.94 ? 141 ASP B N   1 
ATOM   2979 C  CA  . ASP B 1 106 ? 43.023  -56.472 -3.290  1.00 21.79 ? 141 ASP B CA  1 
ATOM   2980 C  C   . ASP B 1 106 ? 44.151  -55.471 -3.114  1.00 21.62 ? 141 ASP B C   1 
ATOM   2981 O  O   . ASP B 1 106 ? 45.303  -55.768 -3.460  1.00 25.50 ? 141 ASP B O   1 
ATOM   2982 C  CB  . ASP B 1 106 ? 42.270  -56.156 -4.578  1.00 28.69 ? 141 ASP B CB  1 
ATOM   2983 C  CG  . ASP B 1 106 ? 41.185  -57.174 -4.882  1.00 32.93 ? 141 ASP B CG  1 
ATOM   2984 O  OD1 . ASP B 1 106 ? 41.485  -58.391 -4.850  1.00 33.61 ? 141 ASP B OD1 1 
ATOM   2985 O  OD2 . ASP B 1 106 ? 40.042  -56.760 -5.182  1.00 30.69 ? 141 ASP B OD2 1 
ATOM   2986 N  N   . GLU B 1 107 ? 43.840  -54.275 -2.624  1.00 23.05 ? 142 GLU B N   1 
ATOM   2987 C  CA  . GLU B 1 107 ? 44.837  -53.231 -2.457  1.00 21.10 ? 142 GLU B CA  1 
ATOM   2988 C  C   . GLU B 1 107 ? 44.548  -52.500 -1.157  1.00 22.59 ? 142 GLU B C   1 
ATOM   2989 O  O   . GLU B 1 107 ? 43.395  -52.385 -0.732  1.00 19.47 ? 142 GLU B O   1 
ATOM   2990 C  CB  . GLU B 1 107 ? 44.862  -52.271 -3.672  1.00 26.45 ? 142 GLU B CB  1 
ATOM   2991 C  CG  . GLU B 1 107 ? 45.167  -52.995 -4.988  1.00 30.09 ? 142 GLU B CG  1 
ATOM   2992 C  CD  . GLU B 1 107 ? 45.498  -52.087 -6.154  1.00 43.67 ? 142 GLU B CD  1 
ATOM   2993 O  OE1 . GLU B 1 107 ? 45.657  -50.869 -5.956  1.00 30.77 ? 142 GLU B OE1 1 
ATOM   2994 O  OE2 . GLU B 1 107 ? 45.600  -52.605 -7.287  1.00 39.60 ? 142 GLU B OE2 1 
ATOM   2995 N  N   . ILE B 1 108 ? 45.610  -52.032 -0.511  1.00 20.32 ? 143 ILE B N   1 
ATOM   2996 C  CA  . ILE B 1 108 ? 45.511  -51.232 0.703   1.00 16.92 ? 143 ILE B CA  1 
ATOM   2997 C  C   . ILE B 1 108 ? 46.241  -49.931 0.432   1.00 24.91 ? 143 ILE B C   1 
ATOM   2998 O  O   . ILE B 1 108 ? 47.398  -49.949 0.001   1.00 22.12 ? 143 ILE B O   1 
ATOM   2999 C  CB  . ILE B 1 108 ? 46.125  -51.972 1.905   1.00 20.92 ? 143 ILE B CB  1 
ATOM   3000 C  CG1 . ILE B 1 108 ? 45.255  -53.178 2.260   1.00 22.88 ? 143 ILE B CG1 1 
ATOM   3001 C  CG2 . ILE B 1 108 ? 46.222  -51.037 3.098   1.00 20.09 ? 143 ILE B CG2 1 
ATOM   3002 C  CD1 . ILE B 1 108 ? 45.922  -54.167 3.172   1.00 27.89 ? 143 ILE B CD1 1 
ATOM   3003 N  N   . TYR B 1 109 ? 45.558  -48.811 0.637   1.00 19.68 ? 144 TYR B N   1 
ATOM   3004 C  CA  . TYR B 1 109 ? 46.160  -47.501 0.454   1.00 18.64 ? 144 TYR B CA  1 
ATOM   3005 C  C   . TYR B 1 109 ? 46.328  -46.874 1.827   1.00 20.32 ? 144 TYR B C   1 
ATOM   3006 O  O   . TYR B 1 109 ? 45.380  -46.844 2.617   1.00 18.26 ? 144 TYR B O   1 
ATOM   3007 C  CB  . TYR B 1 109 ? 45.283  -46.613 -0.425  1.00 17.51 ? 144 TYR B CB  1 
ATOM   3008 C  CG  . TYR B 1 109 ? 45.000  -47.185 -1.802  1.00 18.87 ? 144 TYR B CG  1 
ATOM   3009 C  CD1 . TYR B 1 109 ? 45.816  -48.171 -2.362  1.00 16.99 ? 144 TYR B CD1 1 
ATOM   3010 C  CD2 . TYR B 1 109 ? 43.916  -46.738 -2.550  1.00 24.80 ? 144 TYR B CD2 1 
ATOM   3011 C  CE1 . TYR B 1 109 ? 45.556  -48.692 -3.628  1.00 22.16 ? 144 TYR B CE1 1 
ATOM   3012 C  CE2 . TYR B 1 109 ? 43.647  -47.257 -3.815  1.00 21.84 ? 144 TYR B CE2 1 
ATOM   3013 C  CZ  . TYR B 1 109 ? 44.468  -48.235 -4.350  1.00 22.31 ? 144 TYR B CZ  1 
ATOM   3014 O  OH  . TYR B 1 109 ? 44.203  -48.756 -5.598  1.00 27.05 ? 144 TYR B OH  1 
ATOM   3015 N  N   . LEU B 1 110 ? 47.531  -46.394 2.116   1.00 18.04 ? 145 LEU B N   1 
ATOM   3016 C  CA  . LEU B 1 110 ? 47.840  -45.791 3.404   1.00 17.30 ? 145 LEU B CA  1 
ATOM   3017 C  C   . LEU B 1 110 ? 47.881  -44.277 3.225   1.00 16.02 ? 145 LEU B C   1 
ATOM   3018 O  O   . LEU B 1 110 ? 48.629  -43.771 2.379   1.00 19.53 ? 145 LEU B O   1 
ATOM   3019 C  CB  . LEU B 1 110 ? 49.200  -46.296 3.894   1.00 20.65 ? 145 LEU B CB  1 
ATOM   3020 C  CG  . LEU B 1 110 ? 49.296  -47.810 4.104   1.00 20.55 ? 145 LEU B CG  1 
ATOM   3021 C  CD1 . LEU B 1 110 ? 50.724  -48.242 4.450   1.00 22.37 ? 145 LEU B CD1 1 
ATOM   3022 C  CD2 . LEU B 1 110 ? 48.309  -48.239 5.185   1.00 18.43 ? 145 LEU B CD2 1 
ATOM   3023 N  N   . THR B 1 111 ? 47.072  -43.554 4.008   1.00 15.19 ? 146 THR B N   1 
ATOM   3024 C  CA  . THR B 1 111 ? 47.209  -42.101 4.018   1.00 17.42 ? 146 THR B CA  1 
ATOM   3025 C  C   . THR B 1 111 ? 48.576  -41.696 4.553   1.00 15.99 ? 146 THR B C   1 
ATOM   3026 O  O   . THR B 1 111 ? 49.195  -40.752 4.046   1.00 18.36 ? 146 THR B O   1 
ATOM   3027 C  CB  . THR B 1 111 ? 46.092  -41.448 4.837   1.00 15.94 ? 146 THR B CB  1 
ATOM   3028 O  OG1 . THR B 1 111 ? 46.131  -41.926 6.190   1.00 17.03 ? 146 THR B OG1 1 
ATOM   3029 C  CG2 . THR B 1 111 ? 44.717  -41.726 4.204   1.00 14.36 ? 146 THR B CG2 1 
ATOM   3030 N  N   . HIS B 1 112 ? 49.059  -42.398 5.575   1.00 14.64 ? 147 HIS B N   1 
ATOM   3031 C  CA  . HIS B 1 112 ? 50.392  -42.188 6.140   1.00 16.32 ? 147 HIS B CA  1 
ATOM   3032 C  C   . HIS B 1 112 ? 50.696  -43.375 7.046   1.00 17.53 ? 147 HIS B C   1 
ATOM   3033 O  O   . HIS B 1 112 ? 49.857  -44.264 7.226   1.00 20.23 ? 147 HIS B O   1 
ATOM   3034 C  CB  . HIS B 1 112 ? 50.501  -40.848 6.874   1.00 17.04 ? 147 HIS B CB  1 
ATOM   3035 C  CG  . HIS B 1 112 ? 49.595  -40.721 8.060   1.00 15.15 ? 147 HIS B CG  1 
ATOM   3036 N  ND1 . HIS B 1 112 ? 48.230  -40.905 7.979   1.00 18.05 ? 147 HIS B ND1 1 
ATOM   3037 C  CD2 . HIS B 1 112 ? 49.857  -40.400 9.350   1.00 19.42 ? 147 HIS B CD2 1 
ATOM   3038 C  CE1 . HIS B 1 112 ? 47.692  -40.718 9.173   1.00 14.58 ? 147 HIS B CE1 1 
ATOM   3039 N  NE2 . HIS B 1 112 ? 48.656  -40.405 10.019  1.00 17.09 ? 147 HIS B NE2 1 
ATOM   3040 N  N   . MET B 1 113 ? 51.901  -43.388 7.625   1.00 18.24 ? 148 MET B N   1 
ATOM   3041 C  CA  . MET B 1 113 ? 52.375  -44.583 8.314   1.00 15.52 ? 148 MET B CA  1 
ATOM   3042 C  C   . MET B 1 113 ? 52.439  -44.442 9.831   1.00 17.54 ? 148 MET B C   1 
ATOM   3043 O  O   . MET B 1 113 ? 53.189  -45.167 10.489  1.00 18.13 ? 148 MET B O   1 
ATOM   3044 C  CB  . MET B 1 113 ? 53.679  -45.127 7.737   1.00 17.38 ? 148 MET B CB  1 
ATOM   3045 C  CG  . MET B 1 113 ? 53.531  -45.510 6.289   1.00 20.27 ? 148 MET B CG  1 
ATOM   3046 S  SD  . MET B 1 113 ? 55.116  -45.922 5.571   1.00 22.52 ? 148 MET B SD  1 
ATOM   3047 C  CE  . MET B 1 113 ? 54.598  -46.215 3.878   1.00 21.94 ? 148 MET B CE  1 
ATOM   3048 N  N   . HIS B 1 114 ? 51.635  -43.561 10.409  1.00 16.45 ? 149 HIS B N   1 
ATOM   3049 C  CA  . HIS B 1 114 ? 51.507  -43.548 11.852  1.00 16.68 ? 149 HIS B CA  1 
ATOM   3050 C  C   . HIS B 1 114 ? 50.889  -44.864 12.327  1.00 14.90 ? 149 HIS B C   1 
ATOM   3051 O  O   . HIS B 1 114 ? 50.185  -45.537 11.562  1.00 18.27 ? 149 HIS B O   1 
ATOM   3052 C  CB  . HIS B 1 114 ? 50.651  -42.364 12.282  1.00 20.92 ? 149 HIS B CB  1 
ATOM   3053 C  CG  . HIS B 1 114 ? 51.418  -41.087 12.375  1.00 22.14 ? 149 HIS B CG  1 
ATOM   3054 N  ND1 . HIS B 1 114 ? 50.815  -39.849 12.399  1.00 20.33 ? 149 HIS B ND1 1 
ATOM   3055 C  CD2 . HIS B 1 114 ? 52.750  -40.857 12.456  1.00 24.09 ? 149 HIS B CD2 1 
ATOM   3056 C  CE1 . HIS B 1 114 ? 51.740  -38.910 12.493  1.00 29.60 ? 149 HIS B CE1 1 
ATOM   3057 N  NE2 . HIS B 1 114 ? 52.923  -39.495 12.525  1.00 26.13 ? 149 HIS B NE2 1 
ATOM   3058 N  N   . PRO B 1 115 ? 51.172  -45.269 13.569  1.00 17.74 ? 150 PRO B N   1 
ATOM   3059 C  CA  . PRO B 1 115 ? 50.806  -46.629 14.002  1.00 16.00 ? 150 PRO B CA  1 
ATOM   3060 C  C   . PRO B 1 115 ? 49.327  -46.920 13.914  1.00 17.12 ? 150 PRO B C   1 
ATOM   3061 O  O   . PRO B 1 115 ? 48.948  -48.068 13.646  1.00 19.30 ? 150 PRO B O   1 
ATOM   3062 C  CB  . PRO B 1 115 ? 51.291  -46.691 15.460  1.00 20.50 ? 150 PRO B CB  1 
ATOM   3063 C  CG  . PRO B 1 115 ? 52.269  -45.574 15.603  1.00 36.23 ? 150 PRO B CG  1 
ATOM   3064 C  CD  . PRO B 1 115 ? 51.865  -44.511 14.628  1.00 25.04 ? 150 PRO B CD  1 
ATOM   3065 N  N   . ASP B 1 116 ? 48.478  -45.918 14.137  1.00 16.30 ? 151 ASP B N   1 
ATOM   3066 C  CA  . ASP B 1 116 ? 47.034  -46.112 14.128  1.00 14.93 ? 151 ASP B CA  1 
ATOM   3067 C  C   . ASP B 1 116 ? 46.468  -46.238 12.715  1.00 18.30 ? 151 ASP B C   1 
ATOM   3068 O  O   . ASP B 1 116 ? 45.245  -46.336 12.543  1.00 17.29 ? 151 ASP B O   1 
ATOM   3069 C  CB  . ASP B 1 116 ? 46.333  -44.992 14.912  1.00 17.12 ? 151 ASP B CB  1 
ATOM   3070 C  CG  . ASP B 1 116 ? 46.798  -43.599 14.510  1.00 24.12 ? 151 ASP B CG  1 
ATOM   3071 O  OD1 . ASP B 1 116 ? 48.019  -43.350 14.483  1.00 22.19 ? 151 ASP B OD1 1 
ATOM   3072 O  OD2 . ASP B 1 116 ? 45.932  -42.727 14.263  1.00 18.84 ? 151 ASP B OD2 1 
ATOM   3073 N  N   . HIS B 1 117 ? 47.333  -46.251 11.700  1.00 16.97 ? 152 HIS B N   1 
ATOM   3074 C  CA  . HIS B 1 117 ? 46.929  -46.463 10.323  1.00 16.84 ? 152 HIS B CA  1 
ATOM   3075 C  C   . HIS B 1 117 ? 47.599  -47.657 9.677   1.00 16.15 ? 152 HIS B C   1 
ATOM   3076 O  O   . HIS B 1 117 ? 47.036  -48.213 8.727   1.00 18.94 ? 152 HIS B O   1 
ATOM   3077 C  CB  . HIS B 1 117 ? 47.232  -45.203 9.505   1.00 17.21 ? 152 HIS B CB  1 
ATOM   3078 C  CG  . HIS B 1 117 ? 46.544  -43.998 10.041  1.00 19.41 ? 152 HIS B CG  1 
ATOM   3079 N  ND1 . HIS B 1 117 ? 45.384  -43.503 9.486   1.00 19.49 ? 152 HIS B ND1 1 
ATOM   3080 C  CD2 . HIS B 1 117 ? 46.790  -43.249 11.140  1.00 18.85 ? 152 HIS B CD2 1 
ATOM   3081 C  CE1 . HIS B 1 117 ? 44.968  -42.471 10.195  1.00 20.80 ? 152 HIS B CE1 1 
ATOM   3082 N  NE2 . HIS B 1 117 ? 45.795  -42.306 11.212  1.00 17.18 ? 152 HIS B NE2 1 
ATOM   3083 N  N   . VAL B 1 118 ? 48.764  -48.066 10.169  1.00 16.96 ? 153 VAL B N   1 
ATOM   3084 C  CA  . VAL B 1 118 ? 49.496  -49.194 9.606   1.00 17.48 ? 153 VAL B CA  1 
ATOM   3085 C  C   . VAL B 1 118 ? 49.492  -50.425 10.495  1.00 18.09 ? 153 VAL B C   1 
ATOM   3086 O  O   . VAL B 1 118 ? 49.835  -51.515 10.006  1.00 20.16 ? 153 VAL B O   1 
ATOM   3087 C  CB  . VAL B 1 118 ? 50.944  -48.817 9.225   1.00 19.33 ? 153 VAL B CB  1 
ATOM   3088 C  CG1 . VAL B 1 118 ? 50.946  -47.748 8.168   1.00 29.89 ? 153 VAL B CG1 1 
ATOM   3089 C  CG2 . VAL B 1 118 ? 51.737  -48.366 10.465  1.00 16.23 ? 153 VAL B CG2 1 
ATOM   3090 N  N   . GLY B 1 119 ? 49.146  -50.294 11.777  1.00 17.18 ? 154 GLY B N   1 
ATOM   3091 C  CA  . GLY B 1 119 ? 49.278  -51.422 12.683  1.00 20.80 ? 154 GLY B CA  1 
ATOM   3092 C  C   . GLY B 1 119 ? 48.459  -52.617 12.242  1.00 23.64 ? 154 GLY B C   1 
ATOM   3093 O  O   . GLY B 1 119 ? 48.904  -53.765 12.361  1.00 21.53 ? 154 GLY B O   1 
ATOM   3094 N  N   . GLY B 1 120 ? 47.269  -52.361 11.693  1.00 19.25 ? 155 GLY B N   1 
ATOM   3095 C  CA  . GLY B 1 120 ? 46.382  -53.419 11.243  1.00 17.81 ? 155 GLY B CA  1 
ATOM   3096 C  C   . GLY B 1 120 ? 46.941  -54.266 10.115  1.00 21.62 ? 155 GLY B C   1 
ATOM   3097 O  O   . GLY B 1 120 ? 46.335  -55.289 9.776   1.00 22.96 ? 155 GLY B O   1 
ATOM   3098 N  N   . LEU B 1 121 ? 48.074  -53.874 9.527   1.00 19.86 ? 156 LEU B N   1 
ATOM   3099 C  CA  . LEU B 1 121 ? 48.632  -54.646 8.421   1.00 21.96 ? 156 LEU B CA  1 
ATOM   3100 C  C   . LEU B 1 121 ? 49.165  -56.013 8.852   1.00 22.80 ? 156 LEU B C   1 
ATOM   3101 O  O   . LEU B 1 121 ? 49.310  -56.901 8.003   1.00 23.05 ? 156 LEU B O   1 
ATOM   3102 C  CB  . LEU B 1 121 ? 49.757  -53.856 7.746   1.00 19.83 ? 156 LEU B CB  1 
ATOM   3103 C  CG  . LEU B 1 121 ? 49.360  -52.736 6.782   1.00 21.13 ? 156 LEU B CG  1 
ATOM   3104 C  CD1 . LEU B 1 121 ? 50.598  -51.961 6.329   1.00 20.15 ? 156 LEU B CD1 1 
ATOM   3105 C  CD2 . LEU B 1 121 ? 48.586  -53.288 5.583   1.00 20.46 ? 156 LEU B CD2 1 
ATOM   3106 N  N   . MET B 1 122 ? 49.470  -56.206 10.133  1.00 19.64 ? 157 MET B N   1 
ATOM   3107 C  CA  . MET B 1 122 ? 50.053  -57.453 10.612  1.00 25.55 ? 157 MET B CA  1 
ATOM   3108 C  C   . MET B 1 122 ? 49.190  -58.054 11.714  1.00 27.37 ? 157 MET B C   1 
ATOM   3109 O  O   . MET B 1 122 ? 48.661  -57.334 12.566  1.00 25.56 ? 157 MET B O   1 
ATOM   3110 C  CB  . MET B 1 122 ? 51.465  -57.214 11.160  1.00 26.19 ? 157 MET B CB  1 
ATOM   3111 C  CG  . MET B 1 122 ? 52.493  -56.796 10.114  1.00 23.12 ? 157 MET B CG  1 
ATOM   3112 S  SD  . MET B 1 122 ? 52.695  -57.941 8.734   1.00 27.86 ? 157 MET B SD  1 
ATOM   3113 C  CE  . MET B 1 122 ? 53.479  -59.329 9.567   1.00 31.88 ? 157 MET B CE  1 
ATOM   3114 N  N   . VAL B 1 123 ? 49.051  -59.377 11.691  1.00 30.54 ? 158 VAL B N   1 
ATOM   3115 C  CA  . VAL B 1 123 ? 48.514  -60.140 12.814  1.00 28.22 ? 158 VAL B CA  1 
ATOM   3116 C  C   . VAL B 1 123 ? 49.669  -60.990 13.326  1.00 31.98 ? 158 VAL B C   1 
ATOM   3117 O  O   . VAL B 1 123 ? 49.968  -62.055 12.772  1.00 34.15 ? 158 VAL B O   1 
ATOM   3118 C  CB  . VAL B 1 123 ? 47.309  -61.000 12.413  1.00 30.93 ? 158 VAL B CB  1 
ATOM   3119 C  CG1 . VAL B 1 123 ? 46.939  -61.956 13.543  1.00 33.93 ? 158 VAL B CG1 1 
ATOM   3120 C  CG2 . VAL B 1 123 ? 46.128  -60.129 12.064  1.00 33.41 ? 158 VAL B CG2 1 
ATOM   3121 N  N   . GLY B 1 124 ? 50.341  -60.521 14.373  1.00 32.05 ? 159 GLY B N   1 
ATOM   3122 C  CA  . GLY B 1 124 ? 51.573  -61.177 14.777  1.00 32.21 ? 159 GLY B CA  1 
ATOM   3123 C  C   . GLY B 1 124 ? 52.595  -61.092 13.658  1.00 38.23 ? 159 GLY B C   1 
ATOM   3124 O  O   . GLY B 1 124 ? 52.825  -60.025 13.078  1.00 36.08 ? 159 GLY B O   1 
ATOM   3125 N  N   . GLU B 1 125 ? 53.203  -62.231 13.332  1.00 37.98 ? 160 GLU B N   1 
ATOM   3126 C  CA  . GLU B 1 125 ? 54.193  -62.319 12.267  1.00 30.09 ? 160 GLU B CA  1 
ATOM   3127 C  C   . GLU B 1 125 ? 53.575  -62.622 10.905  1.00 36.82 ? 160 GLU B C   1 
ATOM   3128 O  O   . GLU B 1 125 ? 54.312  -62.820 9.934   1.00 39.22 ? 160 GLU B O   1 
ATOM   3129 C  CB  . GLU B 1 125 ? 55.260  -63.366 12.613  1.00 35.34 ? 160 GLU B CB  1 
ATOM   3130 C  CG  . GLU B 1 125 ? 56.047  -63.043 13.876  1.00 56.51 ? 160 GLU B CG  1 
ATOM   3131 C  CD  . GLU B 1 125 ? 56.930  -61.816 13.716  1.00 69.98 ? 160 GLU B CD  1 
ATOM   3132 O  OE1 . GLU B 1 125 ? 57.877  -61.860 12.898  1.00 70.38 ? 160 GLU B OE1 1 
ATOM   3133 O  OE2 . GLU B 1 125 ? 56.684  -60.809 14.417  1.00 73.52 ? 160 GLU B OE2 1 
ATOM   3134 N  N   . GLN B 1 126 ? 52.249  -62.650 10.809  1.00 31.44 ? 161 GLN B N   1 
ATOM   3135 C  CA  . GLN B 1 126 ? 51.549  -62.990 9.578   1.00 30.20 ? 161 GLN B CA  1 
ATOM   3136 C  C   . GLN B 1 126 ? 50.957  -61.736 8.948   1.00 26.76 ? 161 GLN B C   1 
ATOM   3137 O  O   . GLN B 1 126 ? 50.471  -60.844 9.652   1.00 28.62 ? 161 GLN B O   1 
ATOM   3138 C  CB  . GLN B 1 126 ? 50.424  -63.989 9.858   1.00 33.76 ? 161 GLN B CB  1 
ATOM   3139 C  CG  . GLN B 1 126 ? 50.890  -65.259 10.547  1.00 40.33 ? 161 GLN B CG  1 
ATOM   3140 C  CD  . GLN B 1 126 ? 51.956  -65.985 9.758   1.00 62.87 ? 161 GLN B CD  1 
ATOM   3141 O  OE1 . GLN B 1 126 ? 53.005  -66.344 10.293  1.00 67.34 ? 161 GLN B OE1 1 
ATOM   3142 N  NE2 . GLN B 1 126 ? 51.692  -66.208 8.473   1.00 61.24 ? 161 GLN B NE2 1 
ATOM   3143 N  N   . LEU B 1 127 ? 51.003  -61.674 7.617   1.00 24.94 ? 162 LEU B N   1 
ATOM   3144 C  CA  . LEU B 1 127 ? 50.300  -60.621 6.900   1.00 24.04 ? 162 LEU B CA  1 
ATOM   3145 C  C   . LEU B 1 127 ? 48.812  -60.696 7.220   1.00 23.05 ? 162 LEU B C   1 
ATOM   3146 O  O   . LEU B 1 127 ? 48.176  -61.740 7.047   1.00 26.60 ? 162 LEU B O   1 
ATOM   3147 C  CB  . LEU B 1 127 ? 50.504  -60.799 5.393   1.00 30.16 ? 162 LEU B CB  1 
ATOM   3148 C  CG  . LEU B 1 127 ? 51.930  -60.879 4.842   1.00 33.02 ? 162 LEU B CG  1 
ATOM   3149 C  CD1 . LEU B 1 127 ? 51.907  -60.930 3.317   1.00 33.23 ? 162 LEU B CD1 1 
ATOM   3150 C  CD2 . LEU B 1 127 ? 52.777  -59.698 5.324   1.00 31.86 ? 162 LEU B CD2 1 
ATOM   3151 N  N   . ALA B 1 128 ? 48.250  -59.585 7.687   1.00 23.48 ? 163 ALA B N   1 
ATOM   3152 C  CA  . ALA B 1 128 ? 46.822  -59.571 7.956   1.00 21.68 ? 163 ALA B CA  1 
ATOM   3153 C  C   . ALA B 1 128 ? 45.997  -59.634 6.677   1.00 30.30 ? 163 ALA B C   1 
ATOM   3154 O  O   . ALA B 1 128 ? 44.850  -60.091 6.715   1.00 26.23 ? 163 ALA B O   1 
ATOM   3155 C  CB  . ALA B 1 128 ? 46.447  -58.327 8.762   1.00 26.00 ? 163 ALA B CB  1 
ATOM   3156 N  N   . PHE B 1 129 ? 46.549  -59.187 5.549   1.00 23.59 ? 164 PHE B N   1 
ATOM   3157 C  CA  . PHE B 1 129 ? 45.827  -59.136 4.277   1.00 28.21 ? 164 PHE B CA  1 
ATOM   3158 C  C   . PHE B 1 129 ? 46.669  -59.876 3.255   1.00 24.74 ? 164 PHE B C   1 
ATOM   3159 O  O   . PHE B 1 129 ? 47.484  -59.276 2.540   1.00 27.86 ? 164 PHE B O   1 
ATOM   3160 C  CB  . PHE B 1 129 ? 45.535  -57.697 3.866   1.00 22.19 ? 164 PHE B CB  1 
ATOM   3161 C  CG  . PHE B 1 129 ? 44.714  -56.961 4.870   1.00 22.49 ? 164 PHE B CG  1 
ATOM   3162 C  CD1 . PHE B 1 129 ? 43.334  -57.050 4.848   1.00 24.85 ? 164 PHE B CD1 1 
ATOM   3163 C  CD2 . PHE B 1 129 ? 45.320  -56.198 5.855   1.00 21.77 ? 164 PHE B CD2 1 
ATOM   3164 C  CE1 . PHE B 1 129 ? 42.576  -56.385 5.777   1.00 23.45 ? 164 PHE B CE1 1 
ATOM   3165 C  CE2 . PHE B 1 129 ? 44.560  -55.524 6.792   1.00 22.78 ? 164 PHE B CE2 1 
ATOM   3166 C  CZ  . PHE B 1 129 ? 43.188  -55.620 6.752   1.00 22.35 ? 164 PHE B CZ  1 
ATOM   3167 N  N   . PRO B 1 130 ? 46.521  -61.202 3.190   1.00 25.79 ? 165 PRO B N   1 
ATOM   3168 C  CA  . PRO B 1 130 ? 47.521  -62.032 2.500   1.00 27.69 ? 165 PRO B CA  1 
ATOM   3169 C  C   . PRO B 1 130 ? 47.563  -61.859 0.989   1.00 30.79 ? 165 PRO B C   1 
ATOM   3170 O  O   . PRO B 1 130 ? 48.534  -62.313 0.368   1.00 30.11 ? 165 PRO B O   1 
ATOM   3171 C  CB  . PRO B 1 130 ? 47.127  -63.466 2.894   1.00 33.62 ? 165 PRO B CB  1 
ATOM   3172 C  CG  . PRO B 1 130 ? 45.698  -63.364 3.329   1.00 37.03 ? 165 PRO B CG  1 
ATOM   3173 C  CD  . PRO B 1 130 ? 45.546  -62.008 3.939   1.00 23.27 ? 165 PRO B CD  1 
ATOM   3174 N  N   . ASN B 1 131 ? 46.557  -61.235 0.376   1.00 29.36 ? 166 ASN B N   1 
ATOM   3175 C  CA  . ASN B 1 131 ? 46.530  -61.065 -1.070  1.00 32.20 ? 166 ASN B CA  1 
ATOM   3176 C  C   . ASN B 1 131 ? 46.663  -59.616 -1.511  1.00 32.83 ? 166 ASN B C   1 
ATOM   3177 O  O   . ASN B 1 131 ? 46.684  -59.351 -2.717  1.00 33.73 ? 166 ASN B O   1 
ATOM   3178 C  CB  . ASN B 1 131 ? 45.242  -61.662 -1.648  1.00 27.97 ? 166 ASN B CB  1 
ATOM   3179 C  CG  . ASN B 1 131 ? 45.167  -63.160 -1.450  1.00 34.09 ? 166 ASN B CG  1 
ATOM   3180 O  OD1 . ASN B 1 131 ? 44.207  -63.677 -0.875  1.00 31.93 ? 166 ASN B OD1 1 
ATOM   3181 N  ND2 . ASN B 1 131 ? 46.199  -63.866 -1.898  1.00 30.29 ? 166 ASN B ND2 1 
ATOM   3182 N  N   . ALA B 1 132 ? 46.762  -58.680 -0.577  1.00 25.63 ? 167 ALA B N   1 
ATOM   3183 C  CA  . ALA B 1 132 ? 46.711  -57.264 -0.900  1.00 26.78 ? 167 ALA B CA  1 
ATOM   3184 C  C   . ALA B 1 132 ? 48.081  -56.739 -1.312  1.00 29.85 ? 167 ALA B C   1 
ATOM   3185 O  O   . ALA B 1 132 ? 49.114  -57.173 -0.793  1.00 29.34 ? 167 ALA B O   1 
ATOM   3186 C  CB  . ALA B 1 132 ? 46.203  -56.470 0.303   1.00 23.28 ? 167 ALA B CB  1 
ATOM   3187 N  N   . VAL B 1 133 ? 48.078  -55.809 -2.263  1.00 24.38 ? 168 VAL B N   1 
ATOM   3188 C  CA  . VAL B 1 133 ? 49.232  -54.966 -2.552  1.00 29.66 ? 168 VAL B CA  1 
ATOM   3189 C  C   . VAL B 1 133 ? 49.047  -53.667 -1.782  1.00 25.76 ? 168 VAL B C   1 
ATOM   3190 O  O   . VAL B 1 133 ? 47.986  -53.036 -1.862  1.00 24.27 ? 168 VAL B O   1 
ATOM   3191 C  CB  . VAL B 1 133 ? 49.348  -54.690 -4.059  1.00 32.23 ? 168 VAL B CB  1 
ATOM   3192 C  CG1 . VAL B 1 133 ? 50.394  -53.614 -4.324  1.00 26.41 ? 168 VAL B CG1 1 
ATOM   3193 C  CG2 . VAL B 1 133 ? 49.689  -55.965 -4.793  1.00 32.06 ? 168 VAL B CG2 1 
ATOM   3194 N  N   . VAL B 1 134 ? 50.061  -53.271 -1.025  1.00 24.55 ? 169 VAL B N   1 
ATOM   3195 C  CA  . VAL B 1 134 ? 50.005  -52.052 -0.230  1.00 22.16 ? 169 VAL B CA  1 
ATOM   3196 C  C   . VAL B 1 134 ? 50.630  -50.925 -1.037  1.00 25.51 ? 169 VAL B C   1 
ATOM   3197 O  O   . VAL B 1 134 ? 51.660  -51.114 -1.695  1.00 24.95 ? 169 VAL B O   1 
ATOM   3198 C  CB  . VAL B 1 134 ? 50.717  -52.222 1.127   1.00 23.11 ? 169 VAL B CB  1 
ATOM   3199 C  CG1 . VAL B 1 134 ? 50.707  -50.897 1.893   1.00 22.53 ? 169 VAL B CG1 1 
ATOM   3200 C  CG2 . VAL B 1 134 ? 50.061  -53.329 1.940   1.00 20.99 ? 169 VAL B CG2 1 
ATOM   3201 N  N   . ARG B 1 135 ? 49.999  -49.757 -1.003  1.00 20.33 ? 170 ARG B N   1 
ATOM   3202 C  CA  . ARG B 1 135 ? 50.466  -48.603 -1.751  1.00 20.36 ? 170 ARG B CA  1 
ATOM   3203 C  C   . ARG B 1 135 ? 50.485  -47.402 -0.815  1.00 23.36 ? 170 ARG B C   1 
ATOM   3204 O  O   . ARG B 1 135 ? 49.607  -47.253 0.044   1.00 21.16 ? 170 ARG B O   1 
ATOM   3205 C  CB  . ARG B 1 135 ? 49.515  -48.340 -2.916  1.00 23.30 ? 170 ARG B CB  1 
ATOM   3206 C  CG  . ARG B 1 135 ? 49.463  -49.463 -3.940  1.00 28.66 ? 170 ARG B CG  1 
ATOM   3207 C  CD  . ARG B 1 135 ? 49.175  -48.911 -5.314  1.00 27.95 ? 170 ARG B CD  1 
ATOM   3208 N  NE  . ARG B 1 135 ? 50.362  -48.321 -5.915  1.00 25.84 ? 170 ARG B NE  1 
ATOM   3209 C  CZ  . ARG B 1 135 ? 50.426  -47.900 -7.168  1.00 30.57 ? 170 ARG B CZ  1 
ATOM   3210 N  NH1 . ARG B 1 135 ? 49.386  -47.995 -7.982  1.00 27.54 ? 170 ARG B NH1 1 
ATOM   3211 N  NH2 . ARG B 1 135 ? 51.556  -47.354 -7.610  1.00 29.30 ? 170 ARG B NH2 1 
ATOM   3212 N  N   . ALA B 1 136 ? 51.511  -46.571 -0.964  1.00 22.25 ? 171 ALA B N   1 
ATOM   3213 C  CA  . ALA B 1 136 ? 51.646  -45.319 -0.233  1.00 17.82 ? 171 ALA B CA  1 
ATOM   3214 C  C   . ALA B 1 136 ? 52.614  -44.455 -1.023  1.00 24.00 ? 171 ALA B C   1 
ATOM   3215 O  O   . ALA B 1 136 ? 53.275  -44.929 -1.950  1.00 23.01 ? 171 ALA B O   1 
ATOM   3216 C  CB  . ALA B 1 136 ? 52.162  -45.541 1.193   1.00 19.12 ? 171 ALA B CB  1 
ATOM   3217 N  N   . ASP B 1 137 ? 52.691  -43.178 -0.660  1.00 19.60 ? 172 ASP B N   1 
ATOM   3218 C  CA  . ASP B 1 137 ? 53.594  -42.294 -1.385  1.00 21.30 ? 172 ASP B CA  1 
ATOM   3219 C  C   . ASP B 1 137 ? 55.040  -42.656 -1.071  1.00 23.05 ? 172 ASP B C   1 
ATOM   3220 O  O   . ASP B 1 137 ? 55.369  -43.061 0.053   1.00 20.70 ? 172 ASP B O   1 
ATOM   3221 C  CB  . ASP B 1 137 ? 53.336  -40.831 -1.029  1.00 24.21 ? 172 ASP B CB  1 
ATOM   3222 C  CG  . ASP B 1 137 ? 54.047  -39.878 -1.975  1.00 36.12 ? 172 ASP B CG  1 
ATOM   3223 O  OD1 . ASP B 1 137 ? 55.274  -39.668 -1.832  1.00 29.94 ? 172 ASP B OD1 1 
ATOM   3224 O  OD2 . ASP B 1 137 ? 53.380  -39.371 -2.898  1.00 25.87 ? 172 ASP B OD2 1 
ATOM   3225 N  N   . GLN B 1 138 ? 55.900  -42.517 -2.084  1.00 22.99 ? 173 GLN B N   1 
ATOM   3226 C  CA  . GLN B 1 138 ? 57.312  -42.855 -1.924  1.00 23.79 ? 173 GLN B CA  1 
ATOM   3227 C  C   . GLN B 1 138 ? 57.958  -42.036 -0.810  1.00 22.07 ? 173 GLN B C   1 
ATOM   3228 O  O   . GLN B 1 138 ? 58.836  -42.534 -0.097  1.00 27.07 ? 173 GLN B O   1 
ATOM   3229 C  CB  . GLN B 1 138 ? 58.052  -42.638 -3.241  1.00 23.77 ? 173 GLN B CB  1 
ATOM   3230 C  CG  . GLN B 1 138 ? 59.499  -43.098 -3.221  1.00 38.67 ? 173 GLN B CG  1 
ATOM   3231 C  CD  . GLN B 1 138 ? 59.639  -44.614 -3.211  1.00 76.76 ? 173 GLN B CD  1 
ATOM   3232 O  OE1 . GLN B 1 138 ? 59.866  -45.234 -4.258  1.00 52.22 ? 173 GLN B OE1 1 
ATOM   3233 N  NE2 . GLN B 1 138 ? 59.520  -45.219 -2.024  1.00 45.54 ? 173 GLN B NE2 1 
ATOM   3234 N  N   . LYS B 1 139 ? 57.548  -40.775 -0.649  1.00 22.35 ? 174 LYS B N   1 
ATOM   3235 C  CA  . LYS B 1 139 ? 58.100  -39.948 0.425   1.00 25.70 ? 174 LYS B CA  1 
ATOM   3236 C  C   . LYS B 1 139 ? 57.771  -40.522 1.804   1.00 27.11 ? 174 LYS B C   1 
ATOM   3237 O  O   . LYS B 1 139 ? 58.616  -40.511 2.713   1.00 25.72 ? 174 LYS B O   1 
ATOM   3238 C  CB  . LYS B 1 139 ? 57.591  -38.513 0.287   1.00 26.06 ? 174 LYS B CB  1 
ATOM   3239 C  CG  . LYS B 1 139 ? 58.060  -37.828 -0.987  1.00 36.04 ? 174 LYS B CG  1 
ATOM   3240 C  CD  . LYS B 1 139 ? 57.934  -36.314 -0.904  1.00 32.43 ? 174 LYS B CD  1 
ATOM   3241 C  CE  . LYS B 1 139 ? 58.307  -35.667 -2.232  1.00 46.92 ? 174 LYS B CE  1 
ATOM   3242 N  NZ  . LYS B 1 139 ? 57.718  -34.309 -2.391  1.00 57.72 ? 174 LYS B NZ  1 
ATOM   3243 N  N   . GLU B 1 140 ? 56.551  -41.045 1.968   1.00 20.84 ? 175 GLU B N   1 
ATOM   3244 C  CA  . GLU B 1 140 ? 56.138  -41.639 3.237   1.00 19.30 ? 175 GLU B CA  1 
ATOM   3245 C  C   . GLU B 1 140 ? 56.995  -42.854 3.575   1.00 22.05 ? 175 GLU B C   1 
ATOM   3246 O  O   . GLU B 1 140 ? 57.566  -42.952 4.675   1.00 23.03 ? 175 GLU B O   1 
ATOM   3247 C  CB  . GLU B 1 140 ? 54.663  -42.043 3.128   1.00 19.87 ? 175 GLU B CB  1 
ATOM   3248 C  CG  . GLU B 1 140 ? 53.976  -42.375 4.448   1.00 21.03 ? 175 GLU B CG  1 
ATOM   3249 C  CD  . GLU B 1 140 ? 53.830  -41.167 5.355   1.00 20.69 ? 175 GLU B CD  1 
ATOM   3250 O  OE1 . GLU B 1 140 ? 54.015  -40.024 4.881   1.00 20.91 ? 175 GLU B OE1 1 
ATOM   3251 O  OE2 . GLU B 1 140 ? 53.535  -41.362 6.548   1.00 21.98 ? 175 GLU B OE2 1 
ATOM   3252 N  N   . ALA B 1 141 ? 57.112  -43.783 2.623   1.00 21.51 ? 176 ALA B N   1 
ATOM   3253 C  CA  . ALA B 1 141 ? 57.900  -44.985 2.847   1.00 20.18 ? 176 ALA B CA  1 
ATOM   3254 C  C   . ALA B 1 141 ? 59.367  -44.646 3.068   1.00 22.99 ? 176 ALA B C   1 
ATOM   3255 O  O   . ALA B 1 141 ? 60.015  -45.209 3.960   1.00 28.42 ? 176 ALA B O   1 
ATOM   3256 C  CB  . ALA B 1 141 ? 57.745  -45.932 1.660   1.00 26.94 ? 176 ALA B CB  1 
ATOM   3257 N  N   . ASP B 1 142 ? 59.910  -43.722 2.268   1.00 22.24 ? 177 ASP B N   1 
ATOM   3258 C  CA  . ASP B 1 142 ? 61.313  -43.364 2.413   1.00 29.20 ? 177 ASP B CA  1 
ATOM   3259 C  C   . ASP B 1 142 ? 61.595  -42.766 3.781   1.00 23.73 ? 177 ASP B C   1 
ATOM   3260 O  O   . ASP B 1 142 ? 62.674  -42.991 4.340   1.00 24.78 ? 177 ASP B O   1 
ATOM   3261 C  CB  . ASP B 1 142 ? 61.745  -42.380 1.325   1.00 25.84 ? 177 ASP B CB  1 
ATOM   3262 C  CG  . ASP B 1 142 ? 61.780  -43.004 -0.052  1.00 49.32 ? 177 ASP B CG  1 
ATOM   3263 O  OD1 . ASP B 1 142 ? 61.837  -44.249 -0.144  1.00 30.25 ? 177 ASP B OD1 1 
ATOM   3264 O  OD2 . ASP B 1 142 ? 61.800  -42.243 -1.042  1.00 34.97 ? 177 ASP B OD2 1 
ATOM   3265 N  N   . PHE B 1 143 ? 60.651  -42.007 4.336   1.00 24.12 ? 178 PHE B N   1 
ATOM   3266 C  CA  . PHE B 1 143 ? 60.880  -41.429 5.653   1.00 26.02 ? 178 PHE B CA  1 
ATOM   3267 C  C   . PHE B 1 143 ? 60.759  -42.479 6.754   1.00 20.72 ? 178 PHE B C   1 
ATOM   3268 O  O   . PHE B 1 143 ? 61.691  -42.669 7.550   1.00 24.18 ? 178 PHE B O   1 
ATOM   3269 C  CB  . PHE B 1 143 ? 59.922  -40.264 5.894   1.00 21.79 ? 178 PHE B CB  1 
ATOM   3270 C  CG  . PHE B 1 143 ? 60.093  -39.624 7.237   1.00 23.79 ? 178 PHE B CG  1 
ATOM   3271 C  CD1 . PHE B 1 143 ? 61.147  -38.754 7.463   1.00 26.13 ? 178 PHE B CD1 1 
ATOM   3272 C  CD2 . PHE B 1 143 ? 59.213  -39.892 8.274   1.00 24.78 ? 178 PHE B CD2 1 
ATOM   3273 C  CE1 . PHE B 1 143 ? 61.323  -38.159 8.707   1.00 27.14 ? 178 PHE B CE1 1 
ATOM   3274 C  CE2 . PHE B 1 143 ? 59.380  -39.299 9.517   1.00 22.76 ? 178 PHE B CE2 1 
ATOM   3275 C  CZ  . PHE B 1 143 ? 60.437  -38.432 9.732   1.00 28.44 ? 178 PHE B CZ  1 
ATOM   3276 N  N   . TRP B 1 144 ? 59.618  -43.176 6.817   1.00 23.25 ? 179 TRP B N   1 
ATOM   3277 C  CA  . TRP B 1 144 ? 59.340  -44.022 7.978   1.00 22.64 ? 179 TRP B CA  1 
ATOM   3278 C  C   . TRP B 1 144 ? 60.102  -45.342 7.988   1.00 26.76 ? 179 TRP B C   1 
ATOM   3279 O  O   . TRP B 1 144 ? 60.298  -45.915 9.067   1.00 24.36 ? 179 TRP B O   1 
ATOM   3280 C  CB  . TRP B 1 144 ? 57.840  -44.296 8.119   1.00 17.52 ? 179 TRP B CB  1 
ATOM   3281 C  CG  . TRP B 1 144 ? 57.062  -43.074 8.470   1.00 22.89 ? 179 TRP B CG  1 
ATOM   3282 C  CD1 . TRP B 1 144 ? 56.207  -42.386 7.657   1.00 18.82 ? 179 TRP B CD1 1 
ATOM   3283 C  CD2 . TRP B 1 144 ? 57.071  -42.381 9.725   1.00 20.37 ? 179 TRP B CD2 1 
ATOM   3284 N  NE1 . TRP B 1 144 ? 55.677  -41.311 8.331   1.00 22.64 ? 179 TRP B NE1 1 
ATOM   3285 C  CE2 . TRP B 1 144 ? 56.197  -41.280 9.599   1.00 21.93 ? 179 TRP B CE2 1 
ATOM   3286 C  CE3 . TRP B 1 144 ? 57.738  -42.580 10.940  1.00 22.32 ? 179 TRP B CE3 1 
ATOM   3287 C  CZ2 . TRP B 1 144 ? 55.959  -40.387 10.649  1.00 18.55 ? 179 TRP B CZ2 1 
ATOM   3288 C  CZ3 . TRP B 1 144 ? 57.511  -41.691 11.977  1.00 24.04 ? 179 TRP B CZ3 1 
ATOM   3289 C  CH2 . TRP B 1 144 ? 56.628  -40.605 11.825  1.00 21.47 ? 179 TRP B CH2 1 
ATOM   3290 N  N   . LEU B 1 145 ? 60.526  -45.851 6.835   1.00 21.97 ? 180 LEU B N   1 
ATOM   3291 C  CA  . LEU B 1 145 ? 61.230  -47.125 6.799   1.00 25.26 ? 180 LEU B CA  1 
ATOM   3292 C  C   . LEU B 1 145 ? 62.745  -46.959 6.823   1.00 27.29 ? 180 LEU B C   1 
ATOM   3293 O  O   . LEU B 1 145 ? 63.471  -47.944 6.647   1.00 33.26 ? 180 LEU B O   1 
ATOM   3294 C  CB  . LEU B 1 145 ? 60.770  -47.965 5.604   1.00 28.76 ? 180 LEU B CB  1 
ATOM   3295 C  CG  . LEU B 1 145 ? 59.241  -48.075 5.530   1.00 25.05 ? 180 LEU B CG  1 
ATOM   3296 C  CD1 . LEU B 1 145 ? 58.770  -48.780 4.258   1.00 27.90 ? 180 LEU B CD1 1 
ATOM   3297 C  CD2 . LEU B 1 145 ? 58.648  -48.727 6.780   1.00 24.30 ? 180 LEU B CD2 1 
ATOM   3298 N  N   . SER B 1 146 ? 63.226  -45.736 7.047   1.00 30.09 ? 181 SER B N   1 
ATOM   3299 C  CA  . SER B 1 146 ? 64.651  -45.432 7.117   1.00 33.76 ? 181 SER B CA  1 
ATOM   3300 C  C   . SER B 1 146 ? 65.218  -45.826 8.476   1.00 29.66 ? 181 SER B C   1 
ATOM   3301 O  O   . SER B 1 146 ? 64.835  -45.262 9.507   1.00 28.76 ? 181 SER B O   1 
ATOM   3302 C  CB  . SER B 1 146 ? 64.857  -43.935 6.894   1.00 28.07 ? 181 SER B CB  1 
ATOM   3303 O  OG  . SER B 1 146 ? 66.188  -43.550 7.175   1.00 33.96 ? 181 SER B OG  1 
ATOM   3304 N  N   . GLN B 1 147 ? 66.159  -46.769 8.471   1.00 28.08 ? 182 GLN B N   1 
ATOM   3305 C  CA  . GLN B 1 147 ? 66.875  -47.102 9.697   1.00 30.59 ? 182 GLN B CA  1 
ATOM   3306 C  C   . GLN B 1 147 ? 67.611  -45.892 10.259  1.00 30.59 ? 182 GLN B C   1 
ATOM   3307 O  O   . GLN B 1 147 ? 67.650  -45.693 11.479  1.00 32.68 ? 182 GLN B O   1 
ATOM   3308 C  CB  . GLN B 1 147 ? 67.852  -48.249 9.444   1.00 34.01 ? 182 GLN B CB  1 
ATOM   3309 C  CG  . GLN B 1 147 ? 68.646  -48.637 10.672  1.00 40.04 ? 182 GLN B CG  1 
ATOM   3310 C  CD  . GLN B 1 147 ? 67.764  -49.200 11.768  1.00 48.20 ? 182 GLN B CD  1 
ATOM   3311 O  OE1 . GLN B 1 147 ? 67.799  -48.736 12.910  1.00 49.26 ? 182 GLN B OE1 1 
ATOM   3312 N  NE2 . GLN B 1 147 ? 66.964  -50.202 11.426  1.00 40.89 ? 182 GLN B NE2 1 
ATOM   3313 N  N   . THR B 1 148 ? 68.222  -45.082 9.392   1.00 32.39 ? 183 THR B N   1 
ATOM   3314 C  CA  . THR B 1 148 ? 68.952  -43.915 9.883   1.00 34.66 ? 183 THR B CA  1 
ATOM   3315 C  C   . THR B 1 148 ? 68.017  -42.918 10.565  1.00 37.24 ? 183 THR B C   1 
ATOM   3316 O  O   . THR B 1 148 ? 68.368  -42.336 11.601  1.00 34.21 ? 183 THR B O   1 
ATOM   3317 C  CB  . THR B 1 148 ? 69.766  -43.270 8.755   1.00 39.08 ? 183 THR B CB  1 
ATOM   3318 O  OG1 . THR B 1 148 ? 68.907  -42.468 7.932   1.00 47.17 ? 183 THR B OG1 1 
ATOM   3319 C  CG2 . THR B 1 148 ? 70.469  -44.335 7.905   1.00 42.16 ? 183 THR B CG2 1 
ATOM   3320 N  N   . ASN B 1 149 ? 66.818  -42.718 10.011  1.00 31.24 ? 184 ASN B N   1 
ATOM   3321 C  CA  . ASN B 1 149 ? 65.858  -41.822 10.650  1.00 31.97 ? 184 ASN B CA  1 
ATOM   3322 C  C   . ASN B 1 149 ? 65.449  -42.337 12.022  1.00 28.92 ? 184 ASN B C   1 
ATOM   3323 O  O   . ASN B 1 149 ? 65.327  -41.557 12.976  1.00 34.58 ? 184 ASN B O   1 
ATOM   3324 C  CB  . ASN B 1 149 ? 64.624  -41.639 9.770   1.00 27.96 ? 184 ASN B CB  1 
ATOM   3325 C  CG  . ASN B 1 149 ? 64.911  -40.819 8.549   1.00 31.62 ? 184 ASN B CG  1 
ATOM   3326 O  OD1 . ASN B 1 149 ? 65.987  -40.222 8.425   1.00 36.06 ? 184 ASN B OD1 1 
ATOM   3327 N  ND2 . ASN B 1 149 ? 63.946  -40.761 7.639   1.00 33.36 ? 184 ASN B ND2 1 
ATOM   3328 N  N   . LEU B 1 150 ? 65.217  -43.645 12.138  1.00 27.04 ? 185 LEU B N   1 
ATOM   3329 C  CA  . LEU B 1 150 ? 64.884  -44.216 13.437  1.00 29.15 ? 185 LEU B CA  1 
ATOM   3330 C  C   . LEU B 1 150 ? 66.040  -44.047 14.418  1.00 49.01 ? 185 LEU B C   1 
ATOM   3331 O  O   . LEU B 1 150 ? 65.831  -43.670 15.578  1.00 32.09 ? 185 LEU B O   1 
ATOM   3332 C  CB  . LEU B 1 150 ? 64.502  -45.689 13.273  1.00 26.43 ? 185 LEU B CB  1 
ATOM   3333 C  CG  . LEU B 1 150 ? 64.606  -46.602 14.500  1.00 30.33 ? 185 LEU B CG  1 
ATOM   3334 C  CD1 . LEU B 1 150 ? 63.674  -46.145 15.617  1.00 37.06 ? 185 LEU B CD1 1 
ATOM   3335 C  CD2 . LEU B 1 150 ? 64.280  -48.029 14.110  1.00 35.66 ? 185 LEU B CD2 1 
ATOM   3336 N  N   . ASP B 1 151 ? 67.271  -44.290 13.963  1.00 32.20 ? 186 ASP B N   1 
ATOM   3337 C  CA  . ASP B 1 151 ? 68.426  -44.177 14.841  1.00 39.04 ? 186 ASP B CA  1 
ATOM   3338 C  C   . ASP B 1 151 ? 68.651  -42.746 15.309  1.00 42.59 ? 186 ASP B C   1 
ATOM   3339 O  O   . ASP B 1 151 ? 69.259  -42.538 16.366  1.00 49.91 ? 186 ASP B O   1 
ATOM   3340 C  CB  . ASP B 1 151 ? 69.673  -44.697 14.125  1.00 38.72 ? 186 ASP B CB  1 
ATOM   3341 C  CG  . ASP B 1 151 ? 69.743  -46.211 14.114  1.00 47.55 ? 186 ASP B CG  1 
ATOM   3342 O  OD1 . ASP B 1 151 ? 69.060  -46.844 14.951  1.00 59.73 ? 186 ASP B OD1 1 
ATOM   3343 O  OD2 . ASP B 1 151 ? 70.484  -46.764 13.276  1.00 61.54 ? 186 ASP B OD2 1 
ATOM   3344 N  N   . LYS B 1 152 ? 68.172  -41.763 14.548  1.00 42.20 ? 187 LYS B N   1 
ATOM   3345 C  CA  . LYS B 1 152 ? 68.301  -40.356 14.897  1.00 37.29 ? 187 LYS B CA  1 
ATOM   3346 C  C   . LYS B 1 152 ? 66.997  -39.764 15.423  1.00 40.87 ? 187 LYS B C   1 
ATOM   3347 O  O   . LYS B 1 152 ? 66.893  -38.539 15.558  1.00 47.08 ? 187 LYS B O   1 
ATOM   3348 C  CB  . LYS B 1 152 ? 68.804  -39.566 13.687  1.00 43.06 ? 187 LYS B CB  1 
ATOM   3349 C  CG  . LYS B 1 152 ? 70.131  -40.071 13.142  1.00 43.18 ? 187 LYS B CG  1 
ATOM   3350 C  CD  . LYS B 1 152 ? 70.628  -39.230 11.977  1.00 53.00 ? 187 LYS B CD  1 
ATOM   3351 C  CE  . LYS B 1 152 ? 71.311  -40.098 10.925  1.00 66.78 ? 187 LYS B CE  1 
ATOM   3352 N  NZ  . LYS B 1 152 ? 72.681  -39.608 10.593  1.00 49.21 ? 187 LYS B NZ  1 
ATOM   3353 N  N   . ALA B 1 153 ? 66.008  -40.603 15.717  1.00 35.73 ? 188 ALA B N   1 
ATOM   3354 C  CA  . ALA B 1 153 ? 64.729  -40.113 16.207  1.00 38.59 ? 188 ALA B CA  1 
ATOM   3355 C  C   . ALA B 1 153 ? 64.901  -39.455 17.575  1.00 53.36 ? 188 ALA B C   1 
ATOM   3356 O  O   . ALA B 1 153 ? 65.599  -39.992 18.442  1.00 36.05 ? 188 ALA B O   1 
ATOM   3357 C  CB  . ALA B 1 153 ? 63.723  -41.258 16.309  1.00 32.94 ? 188 ALA B CB  1 
ATOM   3358 N  N   . PRO B 1 154 ? 64.268  -38.300 17.800  1.00 36.55 ? 189 PRO B N   1 
ATOM   3359 C  CA  . PRO B 1 154 ? 64.521  -37.528 19.024  1.00 41.20 ? 189 PRO B CA  1 
ATOM   3360 C  C   . PRO B 1 154 ? 64.047  -38.190 20.313  1.00 53.81 ? 189 PRO B C   1 
ATOM   3361 O  O   . PRO B 1 154 ? 64.799  -38.213 21.293  1.00 62.20 ? 189 PRO B O   1 
ATOM   3362 C  CB  . PRO B 1 154 ? 63.774  -36.212 18.763  1.00 43.21 ? 189 PRO B CB  1 
ATOM   3363 C  CG  . PRO B 1 154 ? 62.731  -36.573 17.754  1.00 39.43 ? 189 PRO B CG  1 
ATOM   3364 C  CD  . PRO B 1 154 ? 63.394  -37.573 16.865  1.00 51.81 ? 189 PRO B CD  1 
ATOM   3365 N  N   . ASP B 1 155 ? 62.818  -38.709 20.353  1.00 37.77 ? 190 ASP B N   1 
ATOM   3366 C  CA  . ASP B 1 155 ? 62.264  -39.228 21.598  1.00 35.94 ? 190 ASP B CA  1 
ATOM   3367 C  C   . ASP B 1 155 ? 61.692  -40.629 21.390  1.00 44.01 ? 190 ASP B C   1 
ATOM   3368 O  O   . ASP B 1 155 ? 61.693  -41.178 20.282  1.00 36.50 ? 190 ASP B O   1 
ATOM   3369 C  CB  . ASP B 1 155 ? 61.209  -38.285 22.198  1.00 41.91 ? 190 ASP B CB  1 
ATOM   3370 C  CG  . ASP B 1 155 ? 60.127  -37.890 21.204  1.00 53.69 ? 190 ASP B CG  1 
ATOM   3371 O  OD1 . ASP B 1 155 ? 59.898  -38.624 20.219  1.00 43.24 ? 190 ASP B OD1 1 
ATOM   3372 O  OD2 . ASP B 1 155 ? 59.493  -36.835 21.414  1.00 61.79 ? 190 ASP B OD2 1 
ATOM   3373 N  N   . ASP B 1 156 ? 61.173  -41.197 22.481  1.00 36.03 ? 191 ASP B N   1 
ATOM   3374 C  CA  . ASP B 1 156 ? 60.652  -42.557 22.435  1.00 31.11 ? 191 ASP B CA  1 
ATOM   3375 C  C   . ASP B 1 156 ? 59.377  -42.641 21.608  1.00 30.93 ? 191 ASP B C   1 
ATOM   3376 O  O   . ASP B 1 156 ? 59.136  -43.658 20.952  1.00 32.90 ? 191 ASP B O   1 
ATOM   3377 C  CB  . ASP B 1 156 ? 60.385  -43.056 23.853  1.00 44.04 ? 191 ASP B CB  1 
ATOM   3378 C  CG  . ASP B 1 156 ? 61.643  -43.540 24.548  1.00 69.55 ? 191 ASP B CG  1 
ATOM   3379 O  OD1 . ASP B 1 156 ? 62.623  -43.878 23.847  1.00 67.49 ? 191 ASP B OD1 1 
ATOM   3380 O  OD2 . ASP B 1 156 ? 61.651  -43.581 25.797  1.00 58.65 ? 191 ASP B OD2 1 
ATOM   3381 N  N   . GLU B 1 157 ? 58.545  -41.597 21.632  1.00 37.63 ? 192 GLU B N   1 
ATOM   3382 C  CA  . GLU B 1 157 ? 57.326  -41.613 20.827  1.00 33.15 ? 192 GLU B CA  1 
ATOM   3383 C  C   . GLU B 1 157 ? 57.657  -41.742 19.345  1.00 31.25 ? 192 GLU B C   1 
ATOM   3384 O  O   . GLU B 1 157 ? 57.095  -42.586 18.632  1.00 26.46 ? 192 GLU B O   1 
ATOM   3385 C  CB  . GLU B 1 157 ? 56.525  -40.336 21.082  1.00 37.05 ? 192 GLU B CB  1 
ATOM   3386 C  CG  . GLU B 1 157 ? 55.323  -40.166 20.153  1.00 36.43 ? 192 GLU B CG  1 
ATOM   3387 C  CD  . GLU B 1 157 ? 54.377  -39.068 20.619  1.00 70.37 ? 192 GLU B CD  1 
ATOM   3388 O  OE1 . GLU B 1 157 ? 54.752  -37.878 20.527  1.00 54.03 ? 192 GLU B OE1 1 
ATOM   3389 O  OE2 . GLU B 1 157 ? 53.254  -39.391 21.063  1.00 53.11 ? 192 GLU B OE2 1 
ATOM   3390 N  N   . SER B 1 158 ? 58.590  -40.916 18.866  1.00 28.13 ? 193 SER B N   1 
ATOM   3391 C  CA  . SER B 1 158 ? 58.974  -40.978 17.459  1.00 30.45 ? 193 SER B CA  1 
ATOM   3392 C  C   . SER B 1 158 ? 59.642  -42.306 17.121  1.00 25.75 ? 193 SER B C   1 
ATOM   3393 O  O   . SER B 1 158 ? 59.339  -42.912 16.084  1.00 24.78 ? 193 SER B O   1 
ATOM   3394 C  CB  . SER B 1 158 ? 59.884  -39.800 17.111  1.00 26.98 ? 193 SER B CB  1 
ATOM   3395 O  OG  . SER B 1 158 ? 60.850  -39.585 18.122  1.00 48.05 ? 193 SER B OG  1 
ATOM   3396 N  N   . LYS B 1 159 ? 60.559  -42.773 17.980  1.00 25.72 ? 194 LYS B N   1 
ATOM   3397 C  CA  . LYS B 1 159 ? 61.168  -44.083 17.757  1.00 31.71 ? 194 LYS B CA  1 
ATOM   3398 C  C   . LYS B 1 159 ? 60.108  -45.168 17.627  1.00 23.56 ? 194 LYS B C   1 
ATOM   3399 O  O   . LYS B 1 159 ? 60.213  -46.050 16.767  1.00 27.81 ? 194 LYS B O   1 
ATOM   3400 C  CB  . LYS B 1 159 ? 62.133  -44.432 18.893  1.00 35.08 ? 194 LYS B CB  1 
ATOM   3401 C  CG  . LYS B 1 159 ? 63.541  -43.900 18.719  1.00 32.35 ? 194 LYS B CG  1 
ATOM   3402 C  CD  . LYS B 1 159 ? 64.276  -43.818 20.047  1.00 42.39 ? 194 LYS B CD  1 
ATOM   3403 C  CE  . LYS B 1 159 ? 65.472  -42.882 19.957  1.00 55.58 ? 194 LYS B CE  1 
ATOM   3404 N  NZ  . LYS B 1 159 ? 66.417  -43.303 18.879  1.00 66.72 ? 194 LYS B NZ  1 
ATOM   3405 N  N   . GLY B 1 160 ? 59.091  -45.132 18.489  1.00 22.98 ? 195 GLY B N   1 
ATOM   3406 C  CA  . GLY B 1 160 ? 58.023  -46.114 18.397  1.00 23.26 ? 195 GLY B CA  1 
ATOM   3407 C  C   . GLY B 1 160 ? 57.258  -46.011 17.094  1.00 26.76 ? 195 GLY B C   1 
ATOM   3408 O  O   . GLY B 1 160 ? 56.818  -47.021 16.539  1.00 24.52 ? 195 GLY B O   1 
ATOM   3409 N  N   . PHE B 1 161 ? 57.082  -44.786 16.590  1.00 22.00 ? 196 PHE B N   1 
ATOM   3410 C  CA  . PHE B 1 161 ? 56.444  -44.608 15.287  1.00 17.89 ? 196 PHE B CA  1 
ATOM   3411 C  C   . PHE B 1 161 ? 57.255  -45.300 14.196  1.00 23.13 ? 196 PHE B C   1 
ATOM   3412 O  O   . PHE B 1 161 ? 56.714  -46.055 13.377  1.00 21.97 ? 196 PHE B O   1 
ATOM   3413 C  CB  . PHE B 1 161 ? 56.338  -43.116 14.972  1.00 23.01 ? 196 PHE B CB  1 
ATOM   3414 C  CG  . PHE B 1 161 ? 55.262  -42.401 15.734  1.00 23.54 ? 196 PHE B CG  1 
ATOM   3415 C  CD1 . PHE B 1 161 ? 54.489  -43.066 16.670  1.00 25.73 ? 196 PHE B CD1 1 
ATOM   3416 C  CD2 . PHE B 1 161 ? 55.061  -41.044 15.549  1.00 48.96 ? 196 PHE B CD2 1 
ATOM   3417 C  CE1 . PHE B 1 161 ? 53.512  -42.400 17.383  1.00 28.37 ? 196 PHE B CE1 1 
ATOM   3418 C  CE2 . PHE B 1 161 ? 54.089  -40.368 16.261  1.00 40.07 ? 196 PHE B CE2 1 
ATOM   3419 C  CZ  . PHE B 1 161 ? 53.312  -41.047 17.180  1.00 32.31 ? 196 PHE B CZ  1 
ATOM   3420 N  N   . PHE B 1 162 ? 58.565  -45.044 14.170  1.00 21.28 ? 197 PHE B N   1 
ATOM   3421 C  CA  . PHE B 1 162 ? 59.416  -45.694 13.175  1.00 21.74 ? 197 PHE B CA  1 
ATOM   3422 C  C   . PHE B 1 162 ? 59.346  -47.211 13.299  1.00 21.35 ? 197 PHE B C   1 
ATOM   3423 O  O   . PHE B 1 162 ? 59.196  -47.924 12.296  1.00 22.73 ? 197 PHE B O   1 
ATOM   3424 C  CB  . PHE B 1 162 ? 60.864  -45.215 13.289  1.00 24.48 ? 197 PHE B CB  1 
ATOM   3425 C  CG  . PHE B 1 162 ? 61.088  -43.826 12.776  1.00 24.13 ? 197 PHE B CG  1 
ATOM   3426 C  CD1 . PHE B 1 162 ? 61.182  -43.588 11.415  1.00 22.32 ? 197 PHE B CD1 1 
ATOM   3427 C  CD2 . PHE B 1 162 ? 61.246  -42.766 13.653  1.00 24.59 ? 197 PHE B CD2 1 
ATOM   3428 C  CE1 . PHE B 1 162 ? 61.400  -42.307 10.936  1.00 25.72 ? 197 PHE B CE1 1 
ATOM   3429 C  CE2 . PHE B 1 162 ? 61.464  -41.488 13.188  1.00 24.91 ? 197 PHE B CE2 1 
ATOM   3430 C  CZ  . PHE B 1 162 ? 61.548  -41.254 11.825  1.00 26.94 ? 197 PHE B CZ  1 
ATOM   3431 N  N   . LYS B 1 163 ? 59.465  -47.723 14.526  1.00 22.57 ? 198 LYS B N   1 
ATOM   3432 C  CA  . LYS B 1 163 ? 59.474  -49.169 14.729  1.00 22.12 ? 198 LYS B CA  1 
ATOM   3433 C  C   . LYS B 1 163 ? 58.157  -49.798 14.299  1.00 24.51 ? 198 LYS B C   1 
ATOM   3434 O  O   . LYS B 1 163 ? 58.149  -50.871 13.687  1.00 24.63 ? 198 LYS B O   1 
ATOM   3435 C  CB  . LYS B 1 163 ? 59.777  -49.499 16.187  1.00 20.86 ? 198 LYS B CB  1 
ATOM   3436 C  CG  . LYS B 1 163 ? 61.223  -49.269 16.584  1.00 27.01 ? 198 LYS B CG  1 
ATOM   3437 C  CD  . LYS B 1 163 ? 61.356  -49.298 18.105  1.00 39.95 ? 198 LYS B CD  1 
ATOM   3438 C  CE  . LYS B 1 163 ? 62.758  -48.925 18.558  1.00 46.96 ? 198 LYS B CE  1 
ATOM   3439 N  NZ  . LYS B 1 163 ? 62.859  -48.947 20.048  1.00 48.99 ? 198 LYS B NZ  1 
ATOM   3440 N  N   . GLY B 1 164 ? 57.033  -49.148 14.615  1.00 23.33 ? 199 GLY B N   1 
ATOM   3441 C  CA  . GLY B 1 164 ? 55.743  -49.651 14.172  1.00 22.28 ? 199 GLY B CA  1 
ATOM   3442 C  C   . GLY B 1 164 ? 55.589  -49.639 12.663  1.00 20.23 ? 199 GLY B C   1 
ATOM   3443 O  O   . GLY B 1 164 ? 55.064  -50.593 12.077  1.00 22.76 ? 199 GLY B O   1 
ATOM   3444 N  N   . ALA B 1 165 ? 56.043  -48.562 12.008  1.00 21.77 ? 200 ALA B N   1 
ATOM   3445 C  CA  . ALA B 1 165 ? 55.971  -48.519 10.547  1.00 19.76 ? 200 ALA B CA  1 
ATOM   3446 C  C   . ALA B 1 165 ? 56.785  -49.645 9.928   1.00 22.76 ? 200 ALA B C   1 
ATOM   3447 O  O   . ALA B 1 165 ? 56.332  -50.305 8.985   1.00 22.02 ? 200 ALA B O   1 
ATOM   3448 C  CB  . ALA B 1 165 ? 56.455  -47.168 10.015  1.00 22.09 ? 200 ALA B CB  1 
ATOM   3449 N  N   . MET B 1 166 ? 57.998  -49.875 10.443  1.00 21.76 ? 201 MET B N   1 
ATOM   3450 C  CA  . MET B 1 166 ? 58.840  -50.939 9.901   1.00 20.78 ? 201 MET B CA  1 
ATOM   3451 C  C   . MET B 1 166 ? 58.229  -52.311 10.149  1.00 20.43 ? 201 MET B C   1 
ATOM   3452 O  O   . MET B 1 166 ? 58.149  -53.136 9.229   1.00 26.49 ? 201 MET B O   1 
ATOM   3453 C  CB  . MET B 1 166 ? 60.257  -50.839 10.466  1.00 24.04 ? 201 MET B CB  1 
ATOM   3454 C  CG  . MET B 1 166 ? 60.878  -49.486 10.226  1.00 27.25 ? 201 MET B CG  1 
ATOM   3455 S  SD  . MET B 1 166 ? 62.387  -49.228 11.146  1.00 31.55 ? 201 MET B SD  1 
ATOM   3456 C  CE  . MET B 1 166 ? 63.041  -47.808 10.265  1.00 32.39 ? 201 MET B CE  1 
ATOM   3457 N  N   . ALA B 1 167 ? 57.752  -52.559 11.375  1.00 20.04 ? 202 ALA B N   1 
ATOM   3458 C  CA  . ALA B 1 167 ? 57.165  -53.855 11.689  1.00 25.11 ? 202 ALA B CA  1 
ATOM   3459 C  C   . ALA B 1 167 ? 55.931  -54.126 10.841  1.00 22.87 ? 202 ALA B C   1 
ATOM   3460 O  O   . ALA B 1 167 ? 55.664  -55.283 10.486  1.00 25.28 ? 202 ALA B O   1 
ATOM   3461 C  CB  . ALA B 1 167 ? 56.825  -53.933 13.180  1.00 23.27 ? 202 ALA B CB  1 
ATOM   3462 N  N   . SER B 1 168 ? 55.178  -53.078 10.490  1.00 20.68 ? 203 SER B N   1 
ATOM   3463 C  CA  . SER B 1 168 ? 53.932  -53.247 9.753   1.00 21.72 ? 203 SER B CA  1 
ATOM   3464 C  C   . SER B 1 168 ? 54.131  -53.326 8.243   1.00 25.36 ? 203 SER B C   1 
ATOM   3465 O  O   . SER B 1 168 ? 53.420  -54.085 7.571   1.00 24.70 ? 203 SER B O   1 
ATOM   3466 C  CB  . SER B 1 168 ? 52.973  -52.093 10.072  1.00 20.63 ? 203 SER B CB  1 
ATOM   3467 O  OG  . SER B 1 168 ? 52.783  -51.938 11.472  1.00 21.97 ? 203 SER B OG  1 
ATOM   3468 N  N   . LEU B 1 169 ? 55.054  -52.538 7.680   1.00 23.51 ? 204 LEU B N   1 
ATOM   3469 C  CA  . LEU B 1 169 ? 55.206  -52.533 6.231   1.00 22.22 ? 204 LEU B CA  1 
ATOM   3470 C  C   . LEU B 1 169 ? 56.290  -53.460 5.713   1.00 18.69 ? 204 LEU B C   1 
ATOM   3471 O  O   . LEU B 1 169 ? 56.136  -54.013 4.620   1.00 23.71 ? 204 LEU B O   1 
ATOM   3472 C  CB  . LEU B 1 169 ? 55.469  -51.137 5.669   1.00 25.60 ? 204 LEU B CB  1 
ATOM   3473 C  CG  . LEU B 1 169 ? 54.245  -50.336 5.245   1.00 56.12 ? 204 LEU B CG  1 
ATOM   3474 C  CD1 . LEU B 1 169 ? 53.661  -49.503 6.383   1.00 39.92 ? 204 LEU B CD1 1 
ATOM   3475 C  CD2 . LEU B 1 169 ? 54.573  -49.544 4.004   1.00 41.09 ? 204 LEU B CD2 1 
ATOM   3476 N  N   . ASN B 1 170 ? 57.404  -53.608 6.437   1.00 20.58 ? 205 ASN B N   1 
ATOM   3477 C  CA  . ASN B 1 170 ? 58.512  -54.398 5.913   1.00 24.38 ? 205 ASN B CA  1 
ATOM   3478 C  C   . ASN B 1 170 ? 58.125  -55.811 5.489   1.00 30.66 ? 205 ASN B C   1 
ATOM   3479 O  O   . ASN B 1 170 ? 58.668  -56.278 4.474   1.00 27.96 ? 205 ASN B O   1 
ATOM   3480 C  CB  . ASN B 1 170 ? 59.708  -54.362 6.873   1.00 29.25 ? 205 ASN B CB  1 
ATOM   3481 C  CG  . ASN B 1 170 ? 60.520  -53.081 6.739   1.00 34.97 ? 205 ASN B CG  1 
ATOM   3482 O  OD1 . ASN B 1 170 ? 60.386  -52.351 5.756   1.00 36.28 ? 205 ASN B OD1 1 
ATOM   3483 N  ND2 . ASN B 1 170 ? 61.369  -52.809 7.723   1.00 30.51 ? 205 ASN B ND2 1 
ATOM   3484 N  N   . PRO B 1 171 ? 57.246  -56.542 6.191   1.00 25.39 ? 206 PRO B N   1 
ATOM   3485 C  CA  . PRO B 1 171 ? 56.850  -57.868 5.680   1.00 25.43 ? 206 PRO B CA  1 
ATOM   3486 C  C   . PRO B 1 171 ? 56.191  -57.818 4.311   1.00 30.10 ? 206 PRO B C   1 
ATOM   3487 O  O   . PRO B 1 171 ? 56.328  -58.770 3.529   1.00 31.94 ? 206 PRO B O   1 
ATOM   3488 C  CB  . PRO B 1 171 ? 55.898  -58.398 6.761   1.00 25.35 ? 206 PRO B CB  1 
ATOM   3489 C  CG  . PRO B 1 171 ? 56.288  -57.666 8.002   1.00 22.87 ? 206 PRO B CG  1 
ATOM   3490 C  CD  . PRO B 1 171 ? 56.733  -56.307 7.557   1.00 23.83 ? 206 PRO B CD  1 
ATOM   3491 N  N   . TYR B 1 172 ? 55.465  -56.742 4.001   1.00 25.47 ? 207 TYR B N   1 
ATOM   3492 C  CA  . TYR B 1 172 ? 54.880  -56.599 2.672   1.00 25.75 ? 207 TYR B CA  1 
ATOM   3493 C  C   . TYR B 1 172 ? 55.938  -56.214 1.647   1.00 29.73 ? 207 TYR B C   1 
ATOM   3494 O  O   . TYR B 1 172 ? 55.901  -56.685 0.504   1.00 30.05 ? 207 TYR B O   1 
ATOM   3495 C  CB  . TYR B 1 172 ? 53.770  -55.548 2.713   1.00 26.83 ? 207 TYR B CB  1 
ATOM   3496 C  CG  . TYR B 1 172 ? 52.518  -56.024 3.420   1.00 22.11 ? 207 TYR B CG  1 
ATOM   3497 C  CD1 . TYR B 1 172 ? 52.404  -55.930 4.802   1.00 22.63 ? 207 TYR B CD1 1 
ATOM   3498 C  CD2 . TYR B 1 172 ? 51.455  -56.568 2.712   1.00 24.77 ? 207 TYR B CD2 1 
ATOM   3499 C  CE1 . TYR B 1 172 ? 51.267  -56.368 5.463   1.00 23.57 ? 207 TYR B CE1 1 
ATOM   3500 C  CE2 . TYR B 1 172 ? 50.310  -57.006 3.365   1.00 28.01 ? 207 TYR B CE2 1 
ATOM   3501 C  CZ  . TYR B 1 172 ? 50.225  -56.899 4.745   1.00 24.79 ? 207 TYR B CZ  1 
ATOM   3502 O  OH  . TYR B 1 172 ? 49.087  -57.330 5.400   1.00 25.51 ? 207 TYR B OH  1 
ATOM   3503 N  N   . VAL B 1 173 ? 56.886  -55.360 2.040   1.00 27.57 ? 208 VAL B N   1 
ATOM   3504 C  CA  . VAL B 1 173 ? 57.990  -55.018 1.146   1.00 31.59 ? 208 VAL B CA  1 
ATOM   3505 C  C   . VAL B 1 173 ? 58.756  -56.276 0.773   1.00 29.48 ? 208 VAL B C   1 
ATOM   3506 O  O   . VAL B 1 173 ? 59.056  -56.522 -0.400  1.00 32.33 ? 208 VAL B O   1 
ATOM   3507 C  CB  . VAL B 1 173 ? 58.909  -53.969 1.798   1.00 25.44 ? 208 VAL B CB  1 
ATOM   3508 C  CG1 . VAL B 1 173 ? 60.134  -53.727 0.932   1.00 28.86 ? 208 VAL B CG1 1 
ATOM   3509 C  CG2 . VAL B 1 173 ? 58.165  -52.675 2.029   1.00 27.04 ? 208 VAL B CG2 1 
ATOM   3510 N  N   . LYS B 1 174 ? 59.052  -57.107 1.774   1.00 29.56 ? 209 LYS B N   1 
ATOM   3511 C  CA  . LYS B 1 174 ? 59.828  -58.322 1.556   1.00 34.11 ? 209 LYS B CA  1 
ATOM   3512 C  C   . LYS B 1 174 ? 59.081  -59.295 0.659   1.00 34.60 ? 209 LYS B C   1 
ATOM   3513 O  O   . LYS B 1 174 ? 59.700  -60.003 -0.144  1.00 38.12 ? 209 LYS B O   1 
ATOM   3514 C  CB  . LYS B 1 174 ? 60.113  -58.981 2.906   1.00 37.41 ? 209 LYS B CB  1 
ATOM   3515 C  CG  . LYS B 1 174 ? 61.240  -58.335 3.702   1.00 52.88 ? 209 LYS B CG  1 
ATOM   3516 C  CD  . LYS B 1 174 ? 61.496  -59.090 5.002   1.00 68.09 ? 209 LYS B CD  1 
ATOM   3517 C  CE  . LYS B 1 174 ? 62.253  -58.243 6.027   1.00 48.45 ? 209 LYS B CE  1 
ATOM   3518 N  NZ  . LYS B 1 174 ? 62.512  -56.849 5.567   1.00 47.57 ? 209 LYS B NZ  1 
ATOM   3519 N  N   . ALA B 1 175 ? 57.753  -59.337 0.774   1.00 30.20 ? 210 ALA B N   1 
ATOM   3520 C  CA  . ALA B 1 175 ? 56.927  -60.213 -0.046  1.00 36.83 ? 210 ALA B CA  1 
ATOM   3521 C  C   . ALA B 1 175 ? 56.670  -59.655 -1.440  1.00 35.74 ? 210 ALA B C   1 
ATOM   3522 O  O   . ALA B 1 175 ? 55.945  -60.288 -2.215  1.00 33.86 ? 210 ALA B O   1 
ATOM   3523 C  CB  . ALA B 1 175 ? 55.591  -60.497 0.648   1.00 31.72 ? 210 ALA B CB  1 
ATOM   3524 N  N   . GLY B 1 176 ? 57.240  -58.499 -1.777  1.00 33.00 ? 211 GLY B N   1 
ATOM   3525 C  CA  . GLY B 1 176 ? 57.001  -57.913 -3.079  1.00 32.45 ? 211 GLY B CA  1 
ATOM   3526 C  C   . GLY B 1 176 ? 55.640  -57.284 -3.227  1.00 40.00 ? 211 GLY B C   1 
ATOM   3527 O  O   . GLY B 1 176 ? 55.171  -57.091 -4.355  1.00 34.93 ? 211 GLY B O   1 
ATOM   3528 N  N   . LYS B 1 177 ? 54.982  -56.959 -2.115  1.00 33.63 ? 212 LYS B N   1 
ATOM   3529 C  CA  . LYS B 1 177 ? 53.625  -56.438 -2.138  1.00 27.26 ? 212 LYS B CA  1 
ATOM   3530 C  C   . LYS B 1 177 ? 53.534  -54.971 -1.734  1.00 28.61 ? 212 LYS B C   1 
ATOM   3531 O  O   . LYS B 1 177 ? 52.448  -54.503 -1.390  1.00 32.79 ? 212 LYS B O   1 
ATOM   3532 C  CB  . LYS B 1 177 ? 52.691  -57.291 -1.278  1.00 27.56 ? 212 LYS B CB  1 
ATOM   3533 C  CG  . LYS B 1 177 ? 52.543  -58.726 -1.728  1.00 39.35 ? 212 LYS B CG  1 
ATOM   3534 C  CD  . LYS B 1 177 ? 52.016  -59.587 -0.597  1.00 46.11 ? 212 LYS B CD  1 
ATOM   3535 C  CE  . LYS B 1 177 ? 51.202  -60.754 -1.137  1.00 31.38 ? 212 LYS B CE  1 
ATOM   3536 N  NZ  . LYS B 1 177 ? 51.008  -61.805 -0.106  1.00 60.09 ? 212 LYS B NZ  1 
ATOM   3537 N  N   . PHE B 1 178 ? 54.636  -54.228 -1.764  1.00 26.44 ? 213 PHE B N   1 
ATOM   3538 C  CA  . PHE B 1 178 ? 54.576  -52.786 -1.553  1.00 28.16 ? 213 PHE B CA  1 
ATOM   3539 C  C   . PHE B 1 178 ? 54.876  -52.083 -2.869  1.00 25.76 ? 213 PHE B C   1 
ATOM   3540 O  O   . PHE B 1 178 ? 55.923  -52.320 -3.479  1.00 29.46 ? 213 PHE B O   1 
ATOM   3541 C  CB  . PHE B 1 178 ? 55.539  -52.310 -0.469  1.00 26.41 ? 213 PHE B CB  1 
ATOM   3542 C  CG  . PHE B 1 178 ? 55.484  -50.829 -0.246  1.00 26.24 ? 213 PHE B CG  1 
ATOM   3543 C  CD1 . PHE B 1 178 ? 54.295  -50.221 0.142   1.00 23.58 ? 213 PHE B CD1 1 
ATOM   3544 C  CD2 . PHE B 1 178 ? 56.608  -50.040 -0.437  1.00 35.39 ? 213 PHE B CD2 1 
ATOM   3545 C  CE1 . PHE B 1 178 ? 54.226  -48.853 0.350   1.00 24.97 ? 213 PHE B CE1 1 
ATOM   3546 C  CE2 . PHE B 1 178 ? 56.551  -48.669 -0.233  1.00 33.45 ? 213 PHE B CE2 1 
ATOM   3547 C  CZ  . PHE B 1 178 ? 55.358  -48.076 0.160   1.00 30.76 ? 213 PHE B CZ  1 
ATOM   3548 N  N   . LYS B 1 179 ? 53.957  -51.228 -3.303  1.00 26.78 ? 214 LYS B N   1 
ATOM   3549 C  CA  . LYS B 1 179 ? 54.043  -50.553 -4.595  1.00 26.04 ? 214 LYS B CA  1 
ATOM   3550 C  C   . LYS B 1 179 ? 53.808  -49.068 -4.364  1.00 24.22 ? 214 LYS B C   1 
ATOM   3551 O  O   . LYS B 1 179 ? 52.657  -48.606 -4.327  1.00 26.19 ? 214 LYS B O   1 
ATOM   3552 C  CB  . LYS B 1 179 ? 53.019  -51.125 -5.572  1.00 29.07 ? 214 LYS B CB  1 
ATOM   3553 C  CG  . LYS B 1 179 ? 53.120  -50.556 -6.967  1.00 36.32 ? 214 LYS B CG  1 
ATOM   3554 C  CD  . LYS B 1 179 ? 52.138  -51.250 -7.895  1.00 50.92 ? 214 LYS B CD  1 
ATOM   3555 C  CE  . LYS B 1 179 ? 52.192  -50.674 -9.292  1.00 44.14 ? 214 LYS B CE  1 
ATOM   3556 N  NZ  . LYS B 1 179 ? 51.212  -51.352 -10.188 1.00 51.82 ? 214 LYS B NZ  1 
ATOM   3557 N  N   . PRO B 1 180 ? 54.872  -48.287 -4.194  1.00 25.75 ? 215 PRO B N   1 
ATOM   3558 C  CA  . PRO B 1 180 ? 54.691  -46.856 -3.940  1.00 24.35 ? 215 PRO B CA  1 
ATOM   3559 C  C   . PRO B 1 180 ? 54.200  -46.127 -5.183  1.00 27.47 ? 215 PRO B C   1 
ATOM   3560 O  O   . PRO B 1 180 ? 54.240  -46.640 -6.302  1.00 28.17 ? 215 PRO B O   1 
ATOM   3561 C  CB  . PRO B 1 180 ? 56.092  -46.388 -3.532  1.00 28.05 ? 215 PRO B CB  1 
ATOM   3562 C  CG  . PRO B 1 180 ? 57.008  -47.345 -4.203  1.00 33.84 ? 215 PRO B CG  1 
ATOM   3563 C  CD  . PRO B 1 180 ? 56.293  -48.677 -4.184  1.00 30.82 ? 215 PRO B CD  1 
ATOM   3564 N  N   . PHE B 1 181 ? 53.682  -44.925 -4.958  1.00 23.24 ? 216 PHE B N   1 
ATOM   3565 C  CA  . PHE B 1 181 ? 53.428  -43.964 -6.023  1.00 29.00 ? 216 PHE B CA  1 
ATOM   3566 C  C   . PHE B 1 181 ? 54.093  -42.654 -5.618  1.00 31.08 ? 216 PHE B C   1 
ATOM   3567 O  O   . PHE B 1 181 ? 54.631  -42.529 -4.514  1.00 27.55 ? 216 PHE B O   1 
ATOM   3568 C  CB  . PHE B 1 181 ? 51.923  -43.780 -6.243  1.00 25.90 ? 216 PHE B CB  1 
ATOM   3569 C  CG  . PHE B 1 181 ? 51.173  -43.480 -4.988  1.00 22.03 ? 216 PHE B CG  1 
ATOM   3570 C  CD1 . PHE B 1 181 ? 51.171  -42.195 -4.451  1.00 29.61 ? 216 PHE B CD1 1 
ATOM   3571 C  CD2 . PHE B 1 181 ? 50.470  -44.479 -4.328  1.00 23.72 ? 216 PHE B CD2 1 
ATOM   3572 C  CE1 . PHE B 1 181 ? 50.485  -41.911 -3.279  1.00 24.83 ? 216 PHE B CE1 1 
ATOM   3573 C  CE2 . PHE B 1 181 ? 49.774  -44.199 -3.151  1.00 22.99 ? 216 PHE B CE2 1 
ATOM   3574 C  CZ  . PHE B 1 181 ? 49.781  -42.917 -2.624  1.00 23.70 ? 216 PHE B CZ  1 
ATOM   3575 N  N   . SER B 1 182 ? 54.056  -41.661 -6.502  1.00 25.83 ? 217 SER B N   1 
ATOM   3576 C  CA  . SER B 1 182 ? 54.658  -40.362 -6.213  1.00 30.67 ? 217 SER B CA  1 
ATOM   3577 C  C   . SER B 1 182 ? 53.685  -39.263 -6.612  1.00 29.04 ? 217 SER B C   1 
ATOM   3578 O  O   . SER B 1 182 ? 53.398  -39.084 -7.799  1.00 36.78 ? 217 SER B O   1 
ATOM   3579 C  CB  . SER B 1 182 ? 55.989  -40.192 -6.941  1.00 35.29 ? 217 SER B CB  1 
ATOM   3580 O  OG  . SER B 1 182 ? 56.622  -38.992 -6.535  1.00 39.89 ? 217 SER B OG  1 
ATOM   3581 N  N   . GLY B 1 183 ? 53.188  -38.527 -5.618  1.00 30.20 ? 218 GLY B N   1 
ATOM   3582 C  CA  . GLY B 1 183 ? 52.268  -37.437 -5.869  1.00 35.54 ? 218 GLY B CA  1 
ATOM   3583 C  C   . GLY B 1 183 ? 50.940  -37.921 -6.432  1.00 28.40 ? 218 GLY B C   1 
ATOM   3584 O  O   . GLY B 1 183 ? 50.552  -39.085 -6.299  1.00 32.54 ? 218 GLY B O   1 
ATOM   3585 N  N   . ASN B 1 184 ? 50.242  -36.991 -7.081  1.00 28.94 ? 219 ASN B N   1 
ATOM   3586 C  CA  . ASN B 1 184 ? 48.935  -37.287 -7.658  1.00 26.59 ? 219 ASN B CA  1 
ATOM   3587 C  C   . ASN B 1 184 ? 49.036  -38.429 -8.660  1.00 34.05 ? 219 ASN B C   1 
ATOM   3588 O  O   . ASN B 1 184 ? 49.809  -38.357 -9.622  1.00 31.19 ? 219 ASN B O   1 
ATOM   3589 C  CB  . ASN B 1 184 ? 48.368  -36.041 -8.330  1.00 30.38 ? 219 ASN B CB  1 
ATOM   3590 C  CG  . ASN B 1 184 ? 48.137  -34.903 -7.355  1.00 33.80 ? 219 ASN B CG  1 
ATOM   3591 O  OD1 . ASN B 1 184 ? 48.181  -35.087 -6.136  1.00 30.30 ? 219 ASN B OD1 1 
ATOM   3592 N  ND2 . ASN B 1 184 ? 47.857  -33.723 -7.887  1.00 36.56 ? 219 ASN B ND2 1 
ATOM   3593 N  N   . THR B 1 185 ? 48.250  -39.483 -8.429  1.00 27.08 ? 220 THR B N   1 
ATOM   3594 C  CA  . THR B 1 185 ? 48.340  -40.706 -9.219  1.00 29.64 ? 220 THR B CA  1 
ATOM   3595 C  C   . THR B 1 185 ? 46.972  -41.368 -9.267  1.00 26.41 ? 220 THR B C   1 
ATOM   3596 O  O   . THR B 1 185 ? 46.347  -41.568 -8.221  1.00 27.25 ? 220 THR B O   1 
ATOM   3597 C  CB  . THR B 1 185 ? 49.324  -41.696 -8.571  1.00 30.53 ? 220 THR B CB  1 
ATOM   3598 O  OG1 . THR B 1 185 ? 50.613  -41.086 -8.420  1.00 36.33 ? 220 THR B OG1 1 
ATOM   3599 C  CG2 . THR B 1 185 ? 49.455  -42.958 -9.432  1.00 34.61 ? 220 THR B CG2 1 
ATOM   3600 N  N   . ASP B 1 186 ? 46.519  -41.718 -10.468 1.00 26.94 ? 221 ASP B N   1 
ATOM   3601 C  CA  . ASP B 1 186 ? 45.381  -42.617 -10.604 1.00 28.60 ? 221 ASP B CA  1 
ATOM   3602 C  C   . ASP B 1 186 ? 45.786  -43.993 -10.096 1.00 27.14 ? 221 ASP B C   1 
ATOM   3603 O  O   . ASP B 1 186 ? 46.771  -44.575 -10.561 1.00 29.07 ? 221 ASP B O   1 
ATOM   3604 C  CB  . ASP B 1 186 ? 44.964  -42.721 -12.067 1.00 33.72 ? 221 ASP B CB  1 
ATOM   3605 C  CG  . ASP B 1 186 ? 44.343  -41.445 -12.599 1.00 37.64 ? 221 ASP B CG  1 
ATOM   3606 O  OD1 . ASP B 1 186 ? 44.334  -40.425 -11.875 1.00 37.24 ? 221 ASP B OD1 1 
ATOM   3607 O  OD2 . ASP B 1 186 ? 43.908  -41.457 -13.773 1.00 36.58 ? 221 ASP B OD2 1 
ATOM   3608 N  N   . LEU B 1 187 ? 45.061  -44.483 -9.111  1.00 29.71 ? 222 LEU B N   1 
ATOM   3609 C  CA  . LEU B 1 187 ? 45.120  -45.851 -8.630  1.00 24.30 ? 222 LEU B CA  1 
ATOM   3610 C  C   . LEU B 1 187 ? 44.023  -46.625 -9.360  1.00 42.89 ? 222 LEU B C   1 
ATOM   3611 O  O   . LEU B 1 187 ? 43.645  -46.256 -10.477 1.00 62.90 ? 222 LEU B O   1 
ATOM   3612 C  CB  . LEU B 1 187 ? 45.070  -45.859 -7.095  1.00 24.88 ? 222 LEU B CB  1 
ATOM   3613 C  CG  . LEU B 1 187 ? 46.137  -44.936 -6.483  1.00 25.84 ? 222 LEU B CG  1 
ATOM   3614 C  CD1 . LEU B 1 187 ? 45.947  -44.767 -4.979  1.00 25.34 ? 222 LEU B CD1 1 
ATOM   3615 C  CD2 . LEU B 1 187 ? 47.556  -45.411 -6.824  1.00 25.00 ? 222 LEU B CD2 1 
ATOM   3616 N  N   . VAL B 1 188 ? 43.564  -47.736 -8.786  1.00 30.01 ? 223 VAL B N   1 
ATOM   3617 C  CA  . VAL B 1 188 ? 42.504  -48.536 -9.412  1.00 39.29 ? 223 VAL B CA  1 
ATOM   3618 C  C   . VAL B 1 188 ? 41.376  -47.641 -9.921  1.00 32.60 ? 223 VAL B C   1 
ATOM   3619 O  O   . VAL B 1 188 ? 41.124  -46.571 -9.341  1.00 35.22 ? 223 VAL B O   1 
ATOM   3620 C  CB  . VAL B 1 188 ? 41.976  -49.636 -8.473  1.00 31.87 ? 223 VAL B CB  1 
ATOM   3621 C  CG1 . VAL B 1 188 ? 43.115  -50.507 -7.976  1.00 41.32 ? 223 VAL B CG1 1 
ATOM   3622 C  CG2 . VAL B 1 188 ? 41.183  -49.034 -7.313  1.00 35.02 ? 223 VAL B CG2 1 
ATOM   3623 N  N   . PRO B 1 189 ? 40.695  -48.016 -11.014 1.00 35.79 ? 224 PRO B N   1 
ATOM   3624 C  CA  . PRO B 1 189 ? 39.614  -47.169 -11.543 1.00 28.33 ? 224 PRO B CA  1 
ATOM   3625 C  C   . PRO B 1 189 ? 38.622  -46.713 -10.486 1.00 28.54 ? 224 PRO B C   1 
ATOM   3626 O  O   . PRO B 1 189 ? 38.033  -47.530 -9.768  1.00 33.63 ? 224 PRO B O   1 
ATOM   3627 C  CB  . PRO B 1 189 ? 38.951  -48.069 -12.595 1.00 36.51 ? 224 PRO B CB  1 
ATOM   3628 C  CG  . PRO B 1 189 ? 40.083  -48.946 -13.065 1.00 44.98 ? 224 PRO B CG  1 
ATOM   3629 C  CD  . PRO B 1 189 ? 40.916  -49.214 -11.845 1.00 38.80 ? 224 PRO B CD  1 
ATOM   3630 N  N   . GLY B 1 190 ? 38.466  -45.395 -10.371 1.00 25.85 ? 225 GLY B N   1 
ATOM   3631 C  CA  . GLY B 1 190 ? 37.584  -44.796 -9.395  1.00 30.34 ? 225 GLY B CA  1 
ATOM   3632 C  C   . GLY B 1 190 ? 38.261  -44.282 -8.142  1.00 28.35 ? 225 GLY B C   1 
ATOM   3633 O  O   . GLY B 1 190 ? 37.581  -43.681 -7.300  1.00 23.32 ? 225 GLY B O   1 
ATOM   3634 N  N   . ILE B 1 191 ? 39.562  -44.518 -7.968  1.00 23.68 ? 226 ILE B N   1 
ATOM   3635 C  CA  . ILE B 1 191 ? 40.286  -44.038 -6.795  1.00 23.75 ? 226 ILE B CA  1 
ATOM   3636 C  C   . ILE B 1 191 ? 41.591  -43.396 -7.242  1.00 27.66 ? 226 ILE B C   1 
ATOM   3637 O  O   . ILE B 1 191 ? 42.339  -43.981 -8.033  1.00 26.17 ? 226 ILE B O   1 
ATOM   3638 C  CB  . ILE B 1 191 ? 40.561  -45.148 -5.764  1.00 23.33 ? 226 ILE B CB  1 
ATOM   3639 C  CG1 . ILE B 1 191 ? 39.284  -45.937 -5.449  1.00 23.94 ? 226 ILE B CG1 1 
ATOM   3640 C  CG2 . ILE B 1 191 ? 41.165  -44.553 -4.489  1.00 21.62 ? 226 ILE B CG2 1 
ATOM   3641 C  CD1 . ILE B 1 191 ? 39.533  -47.105 -4.514  1.00 28.14 ? 226 ILE B CD1 1 
ATOM   3642 N  N   . LYS B 1 192 ? 41.868  -42.208 -6.719  1.00 23.76 ? 227 LYS B N   1 
ATOM   3643 C  CA  . LYS B 1 192 ? 43.055  -41.444 -7.071  1.00 24.71 ? 227 LYS B CA  1 
ATOM   3644 C  C   . LYS B 1 192 ? 43.783  -41.049 -5.793  1.00 23.62 ? 227 LYS B C   1 
ATOM   3645 O  O   . LYS B 1 192 ? 43.155  -40.817 -4.752  1.00 21.16 ? 227 LYS B O   1 
ATOM   3646 C  CB  . LYS B 1 192 ? 42.626  -40.182 -7.819  1.00 33.17 ? 227 LYS B CB  1 
ATOM   3647 C  CG  . LYS B 1 192 ? 42.336  -40.441 -9.279  1.00 43.95 ? 227 LYS B CG  1 
ATOM   3648 C  CD  . LYS B 1 192 ? 41.607  -39.288 -9.939  1.00 59.32 ? 227 LYS B CD  1 
ATOM   3649 C  CE  . LYS B 1 192 ? 40.916  -39.767 -11.214 1.00 48.10 ? 227 LYS B CE  1 
ATOM   3650 N  NZ  . LYS B 1 192 ? 39.621  -40.462 -10.919 1.00 50.68 ? 227 LYS B NZ  1 
ATOM   3651 N  N   . ALA B 1 193 ? 45.108  -41.006 -5.863  1.00 25.77 ? 228 ALA B N   1 
ATOM   3652 C  CA  . ALA B 1 193 ? 45.920  -40.442 -4.796  1.00 23.21 ? 228 ALA B CA  1 
ATOM   3653 C  C   . ALA B 1 193 ? 46.117  -38.954 -5.058  1.00 23.18 ? 228 ALA B C   1 
ATOM   3654 O  O   . ALA B 1 193 ? 46.457  -38.555 -6.173  1.00 28.76 ? 228 ALA B O   1 
ATOM   3655 C  CB  . ALA B 1 193 ? 47.279  -41.141 -4.725  1.00 25.56 ? 228 ALA B CB  1 
ATOM   3656 N  N   . LEU B 1 194 ? 45.868  -38.139 -4.037  1.00 20.64 ? 229 LEU B N   1 
ATOM   3657 C  CA  . LEU B 1 194 ? 46.057  -36.694 -4.067  1.00 24.32 ? 229 LEU B CA  1 
ATOM   3658 C  C   . LEU B 1 194 ? 47.072  -36.366 -2.984  1.00 26.17 ? 229 LEU B C   1 
ATOM   3659 O  O   . LEU B 1 194 ? 46.806  -36.571 -1.798  1.00 22.24 ? 229 LEU B O   1 
ATOM   3660 C  CB  . LEU B 1 194 ? 44.735  -35.993 -3.762  1.00 21.68 ? 229 LEU B CB  1 
ATOM   3661 C  CG  . LEU B 1 194 ? 44.627  -34.496 -4.034  1.00 29.95 ? 229 LEU B CG  1 
ATOM   3662 C  CD1 . LEU B 1 194 ? 44.735  -34.182 -5.520  1.00 31.35 ? 229 LEU B CD1 1 
ATOM   3663 C  CD2 . LEU B 1 194 ? 43.339  -33.927 -3.436  1.00 30.88 ? 229 LEU B CD2 1 
ATOM   3664 N  N   . ALA B 1 195 ? 48.233  -35.862 -3.383  1.00 26.18 ? 230 ALA B N   1 
ATOM   3665 C  CA  . ALA B 1 195 ? 49.234  -35.475 -2.402  1.00 27.61 ? 230 ALA B CA  1 
ATOM   3666 C  C   . ALA B 1 195 ? 48.648  -34.434 -1.455  1.00 20.80 ? 230 ALA B C   1 
ATOM   3667 O  O   . ALA B 1 195 ? 48.037  -33.454 -1.892  1.00 24.17 ? 230 ALA B O   1 
ATOM   3668 C  CB  . ALA B 1 195 ? 50.464  -34.911 -3.112  1.00 24.93 ? 230 ALA B CB  1 
ATOM   3669 N  N   . SER B 1 196 ? 48.798  -34.677 -0.159  1.00 22.91 ? 231 SER B N   1 
ATOM   3670 C  CA  . SER B 1 196 ? 48.392  -33.739 0.889   1.00 20.60 ? 231 SER B CA  1 
ATOM   3671 C  C   . SER B 1 196 ? 49.461  -33.702 1.981   1.00 24.32 ? 231 SER B C   1 
ATOM   3672 O  O   . SER B 1 196 ? 49.177  -33.891 3.165   1.00 21.12 ? 231 SER B O   1 
ATOM   3673 C  CB  . SER B 1 196 ? 46.992  -34.034 1.438   1.00 20.17 ? 231 SER B CB  1 
ATOM   3674 O  OG  . SER B 1 196 ? 46.856  -35.375 1.876   1.00 19.23 ? 231 SER B OG  1 
ATOM   3675 N  N   . HIS B 1 197 ? 50.717  -33.529 1.573   1.00 23.98 ? 232 HIS B N   1 
ATOM   3676 C  CA  . HIS B 1 197 ? 51.851  -33.699 2.477   1.00 25.61 ? 232 HIS B CA  1 
ATOM   3677 C  C   . HIS B 1 197 ? 51.841  -32.663 3.599   1.00 26.03 ? 232 HIS B C   1 
ATOM   3678 O  O   . HIS B 1 197 ? 51.446  -31.507 3.412   1.00 26.48 ? 232 HIS B O   1 
ATOM   3679 C  CB  . HIS B 1 197 ? 53.175  -33.570 1.715   1.00 24.33 ? 232 HIS B CB  1 
ATOM   3680 C  CG  . HIS B 1 197 ? 53.310  -34.504 0.550   1.00 24.78 ? 232 HIS B CG  1 
ATOM   3681 N  ND1 . HIS B 1 197 ? 52.534  -35.636 0.406   1.00 26.38 ? 232 HIS B ND1 1 
ATOM   3682 C  CD2 . HIS B 1 197 ? 54.136  -34.473 -0.524  1.00 23.62 ? 232 HIS B CD2 1 
ATOM   3683 C  CE1 . HIS B 1 197 ? 52.871  -36.258 -0.712  1.00 23.96 ? 232 HIS B CE1 1 
ATOM   3684 N  NE2 . HIS B 1 197 ? 53.840  -35.573 -1.294  1.00 29.72 ? 232 HIS B NE2 1 
ATOM   3685 N  N   . GLY B 1 198 ? 52.335  -33.082 4.764   1.00 22.95 ? 233 GLY B N   1 
ATOM   3686 C  CA  . GLY B 1 198 ? 52.624  -32.175 5.860   1.00 27.18 ? 233 GLY B CA  1 
ATOM   3687 C  C   . GLY B 1 198 ? 52.312  -32.703 7.245   1.00 25.30 ? 233 GLY B C   1 
ATOM   3688 O  O   . GLY B 1 198 ? 53.108  -32.493 8.166   1.00 27.30 ? 233 GLY B O   1 
ATOM   3689 N  N   . HIS B 1 199 ? 51.220  -33.443 7.414   1.00 20.98 ? 234 HIS B N   1 
ATOM   3690 C  CA  . HIS B 1 199 ? 51.064  -34.198 8.650   1.00 18.89 ? 234 HIS B CA  1 
ATOM   3691 C  C   . HIS B 1 199 ? 52.208  -35.191 8.794   1.00 23.42 ? 234 HIS B C   1 
ATOM   3692 O  O   . HIS B 1 199 ? 52.761  -35.369 9.887   1.00 24.68 ? 234 HIS B O   1 
ATOM   3693 C  CB  . HIS B 1 199 ? 49.710  -34.907 8.646   1.00 20.41 ? 234 HIS B CB  1 
ATOM   3694 C  CG  . HIS B 1 199 ? 49.463  -35.754 9.857   1.00 19.78 ? 234 HIS B CG  1 
ATOM   3695 N  ND1 . HIS B 1 199 ? 49.329  -35.221 11.121  1.00 18.05 ? 234 HIS B ND1 1 
ATOM   3696 C  CD2 . HIS B 1 199 ? 49.311  -37.092 9.995   1.00 17.54 ? 234 HIS B CD2 1 
ATOM   3697 C  CE1 . HIS B 1 199 ? 49.107  -36.193 11.985  1.00 18.32 ? 234 HIS B CE1 1 
ATOM   3698 N  NE2 . HIS B 1 199 ? 49.093  -37.338 11.329  1.00 21.64 ? 234 HIS B NE2 1 
ATOM   3699 N  N   . THR B 1 200 ? 52.571  -35.835 7.694   1.00 20.62 ? 235 THR B N   1 
ATOM   3700 C  CA  . THR B 1 200 ? 53.790  -36.605 7.507   1.00 22.43 ? 235 THR B CA  1 
ATOM   3701 C  C   . THR B 1 200 ? 54.345  -36.233 6.144   1.00 24.72 ? 235 THR B C   1 
ATOM   3702 O  O   . THR B 1 200 ? 53.633  -35.646 5.316   1.00 23.33 ? 235 THR B O   1 
ATOM   3703 C  CB  . THR B 1 200 ? 53.513  -38.116 7.554   1.00 19.43 ? 235 THR B CB  1 
ATOM   3704 O  OG1 . THR B 1 200 ? 52.573  -38.460 6.527   1.00 22.41 ? 235 THR B OG1 1 
ATOM   3705 C  CG2 . THR B 1 200 ? 52.978  -38.534 8.926   1.00 18.17 ? 235 THR B CG2 1 
ATOM   3706 N  N   . PRO B 1 201 ? 55.616  -36.550 5.874   1.00 24.38 ? 236 PRO B N   1 
ATOM   3707 C  CA  . PRO B 1 201 ? 56.230  -36.127 4.601   1.00 27.39 ? 236 PRO B CA  1 
ATOM   3708 C  C   . PRO B 1 201 ? 55.511  -36.627 3.355   1.00 22.94 ? 236 PRO B C   1 
ATOM   3709 O  O   . PRO B 1 201 ? 55.604  -35.986 2.299   1.00 26.90 ? 236 PRO B O   1 
ATOM   3710 C  CB  . PRO B 1 201 ? 57.651  -36.700 4.695   1.00 26.09 ? 236 PRO B CB  1 
ATOM   3711 C  CG  . PRO B 1 201 ? 57.935  -36.724 6.160   1.00 25.59 ? 236 PRO B CG  1 
ATOM   3712 C  CD  . PRO B 1 201 ? 56.628  -37.054 6.828   1.00 21.22 ? 236 PRO B CD  1 
ATOM   3713 N  N   . GLY B 1 202 ? 54.813  -37.756 3.431   1.00 20.59 ? 237 GLY B N   1 
ATOM   3714 C  CA  . GLY B 1 202 ? 54.118  -38.269 2.268   1.00 17.93 ? 237 GLY B CA  1 
ATOM   3715 C  C   . GLY B 1 202 ? 52.634  -38.481 2.487   1.00 20.14 ? 237 GLY B C   1 
ATOM   3716 O  O   . GLY B 1 202 ? 52.040  -39.357 1.851   1.00 20.99 ? 237 GLY B O   1 
ATOM   3717 N  N   . HIS B 1 203 ? 52.022  -37.701 3.385   1.00 17.92 ? 238 HIS B N   1 
ATOM   3718 C  CA  . HIS B 1 203 ? 50.604  -37.883 3.681   1.00 15.70 ? 238 HIS B CA  1 
ATOM   3719 C  C   . HIS B 1 203 ? 49.790  -37.717 2.405   1.00 17.60 ? 238 HIS B C   1 
ATOM   3720 O  O   . HIS B 1 203 ? 49.984  -36.757 1.656   1.00 20.78 ? 238 HIS B O   1 
ATOM   3721 C  CB  . HIS B 1 203 ? 50.141  -36.855 4.712   1.00 18.74 ? 238 HIS B CB  1 
ATOM   3722 C  CG  . HIS B 1 203 ? 48.718  -37.049 5.141   1.00 18.66 ? 238 HIS B CG  1 
ATOM   3723 N  ND1 . HIS B 1 203 ? 47.649  -36.516 4.449   1.00 19.02 ? 238 HIS B ND1 1 
ATOM   3724 C  CD2 . HIS B 1 203 ? 48.191  -37.730 6.187   1.00 19.54 ? 238 HIS B CD2 1 
ATOM   3725 C  CE1 . HIS B 1 203 ? 46.523  -36.866 5.053   1.00 17.77 ? 238 HIS B CE1 1 
ATOM   3726 N  NE2 . HIS B 1 203 ? 46.826  -37.599 6.110   1.00 17.47 ? 238 HIS B NE2 1 
ATOM   3727 N  N   . THR B 1 204 ? 48.884  -38.659 2.156   1.00 17.50 ? 239 THR B N   1 
ATOM   3728 C  CA  . THR B 1 204 ? 48.123  -38.701 0.917   1.00 15.14 ? 239 THR B CA  1 
ATOM   3729 C  C   . THR B 1 204 ? 46.633  -38.810 1.217   1.00 18.09 ? 239 THR B C   1 
ATOM   3730 O  O   . THR B 1 204 ? 46.224  -39.573 2.100   1.00 18.77 ? 239 THR B O   1 
ATOM   3731 C  CB  . THR B 1 204 ? 48.575  -39.902 0.067   1.00 23.13 ? 239 THR B CB  1 
ATOM   3732 O  OG1 . THR B 1 204 ? 49.961  -39.750 -0.260  1.00 20.16 ? 239 THR B OG1 1 
ATOM   3733 C  CG2 . THR B 1 204 ? 47.758  -40.011 -1.229  1.00 20.33 ? 239 THR B CG2 1 
ATOM   3734 N  N   . THR B 1 205 ? 45.836  -38.019 0.492   1.00 17.38 ? 240 THR B N   1 
ATOM   3735 C  CA  . THR B 1 205 ? 44.381  -38.106 0.471   1.00 17.42 ? 240 THR B CA  1 
ATOM   3736 C  C   . THR B 1 205 ? 43.980  -39.042 -0.660  1.00 19.38 ? 240 THR B C   1 
ATOM   3737 O  O   . THR B 1 205 ? 44.628  -39.070 -1.706  1.00 21.11 ? 240 THR B O   1 
ATOM   3738 C  CB  . THR B 1 205 ? 43.827  -36.707 0.174   1.00 22.05 ? 240 THR B CB  1 
ATOM   3739 O  OG1 . THR B 1 205 ? 44.100  -35.845 1.285   1.00 23.50 ? 240 THR B OG1 1 
ATOM   3740 C  CG2 . THR B 1 205 ? 42.316  -36.726 -0.099  1.00 20.99 ? 240 THR B CG2 1 
ATOM   3741 N  N   . TYR B 1 206 ? 42.914  -39.812 -0.462  1.00 18.31 ? 241 TYR B N   1 
ATOM   3742 C  CA  . TYR B 1 206 ? 42.423  -40.695 -1.521  1.00 19.12 ? 241 TYR B CA  1 
ATOM   3743 C  C   . TYR B 1 206 ? 41.030  -40.263 -1.951  1.00 20.46 ? 241 TYR B C   1 
ATOM   3744 O  O   . TYR B 1 206 ? 40.114  -40.205 -1.130  1.00 19.88 ? 241 TYR B O   1 
ATOM   3745 C  CB  . TYR B 1 206 ? 42.470  -42.163 -1.085  1.00 17.81 ? 241 TYR B CB  1 
ATOM   3746 C  CG  . TYR B 1 206 ? 43.889  -42.619 -0.822  1.00 18.87 ? 241 TYR B CG  1 
ATOM   3747 C  CD1 . TYR B 1 206 ? 44.777  -42.835 -1.878  1.00 18.77 ? 241 TYR B CD1 1 
ATOM   3748 C  CD2 . TYR B 1 206 ? 44.368  -42.763 0.477   1.00 15.57 ? 241 TYR B CD2 1 
ATOM   3749 C  CE1 . TYR B 1 206 ? 46.085  -43.221 -1.648  1.00 17.98 ? 241 TYR B CE1 1 
ATOM   3750 C  CE2 . TYR B 1 206 ? 45.689  -43.143 0.720   1.00 17.11 ? 241 TYR B CE2 1 
ATOM   3751 C  CZ  . TYR B 1 206 ? 46.544  -43.370 -0.356  1.00 18.61 ? 241 TYR B CZ  1 
ATOM   3752 O  OH  . TYR B 1 206 ? 47.858  -43.756 -0.160  1.00 19.64 ? 241 TYR B OH  1 
ATOM   3753 N  N   . VAL B 1 207 ? 40.874  -39.967 -3.236  1.00 19.00 ? 242 VAL B N   1 
ATOM   3754 C  CA  . VAL B 1 207 ? 39.633  -39.441 -3.787  1.00 18.69 ? 242 VAL B CA  1 
ATOM   3755 C  C   . VAL B 1 207 ? 38.923  -40.560 -4.531  1.00 23.88 ? 242 VAL B C   1 
ATOM   3756 O  O   . VAL B 1 207 ? 39.471  -41.127 -5.486  1.00 21.59 ? 242 VAL B O   1 
ATOM   3757 C  CB  . VAL B 1 207 ? 39.903  -38.245 -4.712  1.00 22.91 ? 242 VAL B CB  1 
ATOM   3758 C  CG1 . VAL B 1 207 ? 38.591  -37.707 -5.275  1.00 23.35 ? 242 VAL B CG1 1 
ATOM   3759 C  CG2 . VAL B 1 207 ? 40.676  -37.159 -3.958  1.00 28.39 ? 242 VAL B CG2 1 
ATOM   3760 N  N   . VAL B 1 208 ? 37.693  -40.852 -4.110  1.00 20.36 ? 243 VAL B N   1 
ATOM   3761 C  CA  . VAL B 1 208 ? 36.858  -41.907 -4.671  1.00 18.23 ? 243 VAL B CA  1 
ATOM   3762 C  C   . VAL B 1 208 ? 35.719  -41.247 -5.438  1.00 22.94 ? 243 VAL B C   1 
ATOM   3763 O  O   . VAL B 1 208 ? 35.051  -40.348 -4.917  1.00 23.05 ? 243 VAL B O   1 
ATOM   3764 C  CB  . VAL B 1 208 ? 36.317  -42.809 -3.547  1.00 17.93 ? 243 VAL B CB  1 
ATOM   3765 C  CG1 . VAL B 1 208 ? 35.592  -44.018 -4.122  1.00 21.21 ? 243 VAL B CG1 1 
ATOM   3766 C  CG2 . VAL B 1 208 ? 37.463  -43.232 -2.611  1.00 21.18 ? 243 VAL B CG2 1 
ATOM   3767 N  N   . GLU B 1 209 ? 35.514  -41.662 -6.685  1.00 23.45 ? 244 GLU B N   1 
ATOM   3768 C  CA  . GLU B 1 209 ? 34.471  -41.070 -7.513  1.00 25.47 ? 244 GLU B CA  1 
ATOM   3769 C  C   . GLU B 1 209 ? 33.772  -42.152 -8.313  1.00 22.49 ? 244 GLU B C   1 
ATOM   3770 O  O   . GLU B 1 209 ? 34.426  -42.996 -8.937  1.00 24.18 ? 244 GLU B O   1 
ATOM   3771 C  CB  . GLU B 1 209 ? 35.020  -40.002 -8.471  1.00 26.73 ? 244 GLU B CB  1 
ATOM   3772 C  CG  . GLU B 1 209 ? 35.954  -38.988 -7.841  1.00 31.05 ? 244 GLU B CG  1 
ATOM   3773 C  CD  . GLU B 1 209 ? 36.478  -37.976 -8.843  1.00 38.86 ? 244 GLU B CD  1 
ATOM   3774 O  OE1 . GLU B 1 209 ? 35.661  -37.427 -9.620  1.00 41.83 ? 244 GLU B OE1 1 
ATOM   3775 O  OE2 . GLU B 1 209 ? 37.709  -37.743 -8.868  1.00 44.81 ? 244 GLU B OE2 1 
ATOM   3776 N  N   . SER B 1 210 ? 32.440  -42.109 -8.308  1.00 24.40 ? 245 SER B N   1 
ATOM   3777 C  CA  . SER B 1 210 ? 31.642  -43.015 -9.121  1.00 24.32 ? 245 SER B CA  1 
ATOM   3778 C  C   . SER B 1 210 ? 30.329  -42.329 -9.458  1.00 25.05 ? 245 SER B C   1 
ATOM   3779 O  O   . SER B 1 210 ? 29.669  -41.797 -8.561  1.00 23.87 ? 245 SER B O   1 
ATOM   3780 C  CB  . SER B 1 210 ? 31.343  -44.317 -8.373  1.00 23.71 ? 245 SER B CB  1 
ATOM   3781 O  OG  . SER B 1 210 ? 30.348  -45.063 -9.062  1.00 25.27 ? 245 SER B OG  1 
ATOM   3782 N  N   . GLN B 1 211 ? 29.961  -42.347 -10.741 1.00 27.12 ? 246 GLN B N   1 
ATOM   3783 C  CA  . GLN B 1 211 ? 28.671  -41.830 -11.202 1.00 29.24 ? 246 GLN B CA  1 
ATOM   3784 C  C   . GLN B 1 211 ? 28.441  -40.397 -10.722 1.00 28.40 ? 246 GLN B C   1 
ATOM   3785 O  O   . GLN B 1 211 ? 27.345  -40.032 -10.291 1.00 29.05 ? 246 GLN B O   1 
ATOM   3786 C  CB  . GLN B 1 211 ? 27.517  -42.744 -10.780 1.00 31.20 ? 246 GLN B CB  1 
ATOM   3787 C  CG  . GLN B 1 211 ? 27.680  -44.216 -11.162 1.00 29.21 ? 246 GLN B CG  1 
ATOM   3788 C  CD  . GLN B 1 211 ? 27.665  -44.475 -12.654 1.00 55.27 ? 246 GLN B CD  1 
ATOM   3789 O  OE1 . GLN B 1 211 ? 26.605  -44.656 -13.248 1.00 51.07 ? 246 GLN B OE1 1 
ATOM   3790 N  NE2 . GLN B 1 211 ? 28.844  -44.526 -13.263 1.00 64.05 ? 246 GLN B NE2 1 
ATOM   3791 N  N   . GLY B 1 212 ? 29.497  -39.586 -10.765 1.00 26.94 ? 247 GLY B N   1 
ATOM   3792 C  CA  . GLY B 1 212 ? 29.405  -38.192 -10.383 1.00 30.51 ? 247 GLY B CA  1 
ATOM   3793 C  C   . GLY B 1 212 ? 29.445  -37.927 -8.895  1.00 32.09 ? 247 GLY B C   1 
ATOM   3794 O  O   . GLY B 1 212 ? 29.410  -36.758 -8.490  1.00 33.55 ? 247 GLY B O   1 
ATOM   3795 N  N   . GLN B 1 213 ? 29.533  -38.965 -8.069  1.00 23.06 ? 248 GLN B N   1 
ATOM   3796 C  CA  . GLN B 1 213 ? 29.542  -38.823 -6.622  1.00 22.49 ? 248 GLN B CA  1 
ATOM   3797 C  C   . GLN B 1 213 ? 30.977  -38.969 -6.140  1.00 30.09 ? 248 GLN B C   1 
ATOM   3798 O  O   . GLN B 1 213 ? 31.644  -39.958 -6.463  1.00 29.59 ? 248 GLN B O   1 
ATOM   3799 C  CB  . GLN B 1 213 ? 28.686  -39.916 -5.979  1.00 25.53 ? 248 GLN B CB  1 
ATOM   3800 C  CG  . GLN B 1 213 ? 27.321  -40.083 -6.589  1.00 29.09 ? 248 GLN B CG  1 
ATOM   3801 C  CD  . GLN B 1 213 ? 26.526  -38.799 -6.539  1.00 33.74 ? 248 GLN B CD  1 
ATOM   3802 O  OE1 . GLN B 1 213 ? 26.312  -38.238 -5.467  1.00 47.87 ? 248 GLN B OE1 1 
ATOM   3803 N  NE2 . GLN B 1 213 ? 26.092  -38.317 -7.702  1.00 54.03 ? 248 GLN B NE2 1 
ATOM   3804 N  N   . LYS B 1 214 ? 31.444  -37.993 -5.361  1.00 22.40 ? 249 LYS B N   1 
ATOM   3805 C  CA  . LYS B 1 214 ? 32.835  -37.920 -4.931  1.00 21.76 ? 249 LYS B CA  1 
ATOM   3806 C  C   . LYS B 1 214 ? 32.950  -37.947 -3.411  1.00 20.55 ? 249 LYS B C   1 
ATOM   3807 O  O   . LYS B 1 214 ? 32.124  -37.368 -2.698  1.00 22.41 ? 249 LYS B O   1 
ATOM   3808 C  CB  . LYS B 1 214 ? 33.530  -36.662 -5.490  1.00 25.87 ? 249 LYS B CB  1 
ATOM   3809 C  CG  . LYS B 1 214 ? 35.040  -36.641 -5.220  1.00 28.66 ? 249 LYS B CG  1 
ATOM   3810 C  CD  . LYS B 1 214 ? 35.674  -35.259 -5.392  1.00 37.71 ? 249 LYS B CD  1 
ATOM   3811 C  CE  . LYS B 1 214 ? 35.995  -34.962 -6.840  1.00 42.47 ? 249 LYS B CE  1 
ATOM   3812 N  NZ  . LYS B 1 214 ? 36.014  -33.497 -7.105  1.00 59.78 ? 249 LYS B NZ  1 
ATOM   3813 N  N   . LEU B 1 215 ? 33.991  -38.624 -2.929  1.00 18.39 ? 250 LEU B N   1 
ATOM   3814 C  CA  . LEU B 1 215 ? 34.303  -38.747 -1.509  1.00 16.17 ? 250 LEU B CA  1 
ATOM   3815 C  C   . LEU B 1 215 ? 35.812  -38.615 -1.351  1.00 20.53 ? 250 LEU B C   1 
ATOM   3816 O  O   . LEU B 1 215 ? 36.567  -39.415 -1.910  1.00 20.76 ? 250 LEU B O   1 
ATOM   3817 C  CB  . LEU B 1 215 ? 33.857  -40.118 -0.992  1.00 19.43 ? 250 LEU B CB  1 
ATOM   3818 C  CG  . LEU B 1 215 ? 34.335  -40.538 0.401   1.00 21.82 ? 250 LEU B CG  1 
ATOM   3819 C  CD1 . LEU B 1 215 ? 33.777  -39.606 1.489   1.00 18.42 ? 250 LEU B CD1 1 
ATOM   3820 C  CD2 . LEU B 1 215 ? 33.961  -41.988 0.677   1.00 21.98 ? 250 LEU B CD2 1 
ATOM   3821 N  N   . ALA B 1 216 ? 36.263  -37.639 -0.572  1.00 18.00 ? 251 ALA B N   1 
ATOM   3822 C  CA  . ALA B 1 216 ? 37.689  -37.460 -0.332  1.00 16.39 ? 251 ALA B CA  1 
ATOM   3823 C  C   . ALA B 1 216 ? 38.032  -38.012 1.044   1.00 18.73 ? 251 ALA B C   1 
ATOM   3824 O  O   . ALA B 1 216 ? 37.517  -37.525 2.057   1.00 18.00 ? 251 ALA B O   1 
ATOM   3825 C  CB  . ALA B 1 216 ? 38.089  -35.990 -0.436  1.00 16.84 ? 251 ALA B CB  1 
ATOM   3826 N  N   . LEU B 1 217 ? 38.869  -39.043 1.074   1.00 16.28 ? 252 LEU B N   1 
ATOM   3827 C  CA  . LEU B 1 217 ? 39.353  -39.642 2.311   1.00 13.65 ? 252 LEU B CA  1 
ATOM   3828 C  C   . LEU B 1 217 ? 40.605  -38.886 2.708   1.00 17.15 ? 252 LEU B C   1 
ATOM   3829 O  O   . LEU B 1 217 ? 41.676  -39.095 2.132   1.00 17.02 ? 252 LEU B O   1 
ATOM   3830 C  CB  . LEU B 1 217 ? 39.625  -41.131 2.118   1.00 16.97 ? 252 LEU B CB  1 
ATOM   3831 C  CG  . LEU B 1 217 ? 38.422  -41.898 1.549   1.00 19.69 ? 252 LEU B CG  1 
ATOM   3832 C  CD1 . LEU B 1 217 ? 38.822  -43.329 1.219   1.00 20.82 ? 252 LEU B CD1 1 
ATOM   3833 C  CD2 . LEU B 1 217 ? 37.240  -41.870 2.510   1.00 19.43 ? 252 LEU B CD2 1 
ATOM   3834 N  N   . LEU B 1 218 ? 40.465  -38.016 3.704   1.00 17.76 ? 253 LEU B N   1 
ATOM   3835 C  CA  . LEU B 1 218 ? 41.483  -37.033 4.048   1.00 17.03 ? 253 LEU B CA  1 
ATOM   3836 C  C   . LEU B 1 218 ? 42.512  -37.546 5.042   1.00 17.25 ? 253 LEU B C   1 
ATOM   3837 O  O   . LEU B 1 218 ? 43.438  -36.803 5.377   1.00 20.34 ? 253 LEU B O   1 
ATOM   3838 C  CB  . LEU B 1 218 ? 40.829  -35.766 4.612   1.00 18.85 ? 253 LEU B CB  1 
ATOM   3839 C  CG  . LEU B 1 218 ? 39.733  -35.082 3.793   1.00 19.84 ? 253 LEU B CG  1 
ATOM   3840 C  CD1 . LEU B 1 218 ? 39.216  -33.859 4.535   1.00 22.13 ? 253 LEU B CD1 1 
ATOM   3841 C  CD2 . LEU B 1 218 ? 40.250  -34.672 2.429   1.00 20.52 ? 253 LEU B CD2 1 
ATOM   3842 N  N   . GLY B 1 219 ? 42.371  -38.773 5.536   1.00 18.62 ? 254 GLY B N   1 
ATOM   3843 C  CA  . GLY B 1 219 ? 43.365  -39.287 6.470   1.00 17.44 ? 254 GLY B CA  1 
ATOM   3844 C  C   . GLY B 1 219 ? 43.388  -38.468 7.748   1.00 19.17 ? 254 GLY B C   1 
ATOM   3845 O  O   . GLY B 1 219 ? 42.361  -38.284 8.418   1.00 20.23 ? 254 GLY B O   1 
ATOM   3846 N  N   . ASP B 1 220 ? 44.578  -37.961 8.091   1.00 16.07 ? 255 ASP B N   1 
ATOM   3847 C  CA  . ASP B 1 220 ? 44.788  -37.164 9.290   1.00 17.76 ? 255 ASP B CA  1 
ATOM   3848 C  C   . ASP B 1 220 ? 44.945  -35.682 8.976   1.00 24.54 ? 255 ASP B C   1 
ATOM   3849 O  O   . ASP B 1 220 ? 45.580  -34.937 9.733   1.00 19.79 ? 255 ASP B O   1 
ATOM   3850 C  CB  . ASP B 1 220 ? 45.960  -37.702 10.116  1.00 19.51 ? 255 ASP B CB  1 
ATOM   3851 C  CG  . ASP B 1 220 ? 45.581  -38.927 10.923  1.00 21.45 ? 255 ASP B CG  1 
ATOM   3852 O  OD1 . ASP B 1 220 ? 44.487  -39.485 10.666  1.00 22.90 ? 255 ASP B OD1 1 
ATOM   3853 O  OD2 . ASP B 1 220 ? 46.352  -39.323 11.825  1.00 18.43 ? 255 ASP B OD2 1 
ATOM   3854 N  N   . LEU B 1 221 ? 44.361  -35.235 7.867   1.00 17.15 ? 256 LEU B N   1 
ATOM   3855 C  CA  . LEU B 1 221 ? 44.431  -33.822 7.529   1.00 20.40 ? 256 LEU B CA  1 
ATOM   3856 C  C   . LEU B 1 221 ? 43.662  -32.969 8.538   1.00 27.08 ? 256 LEU B C   1 
ATOM   3857 O  O   . LEU B 1 221 ? 43.963  -31.781 8.701   1.00 28.54 ? 256 LEU B O   1 
ATOM   3858 C  CB  . LEU B 1 221 ? 43.919  -33.638 6.103   1.00 24.62 ? 256 LEU B CB  1 
ATOM   3859 C  CG  . LEU B 1 221 ? 44.316  -32.361 5.396   1.00 35.13 ? 256 LEU B CG  1 
ATOM   3860 C  CD1 . LEU B 1 221 ? 45.831  -32.332 5.285   1.00 30.49 ? 256 LEU B CD1 1 
ATOM   3861 C  CD2 . LEU B 1 221 ? 43.683  -32.381 4.031   1.00 25.09 ? 256 LEU B CD2 1 
ATOM   3862 N  N   . ILE B 1 222 ? 42.676  -33.548 9.224   1.00 18.18 ? 257 ILE B N   1 
ATOM   3863 C  CA  . ILE B 1 222 ? 42.057  -32.934 10.393  1.00 22.89 ? 257 ILE B CA  1 
ATOM   3864 C  C   . ILE B 1 222 ? 42.028  -33.956 11.524  1.00 23.24 ? 257 ILE B C   1 
ATOM   3865 O  O   . ILE B 1 222 ? 41.779  -35.146 11.292  1.00 27.10 ? 257 ILE B O   1 
ATOM   3866 C  CB  . ILE B 1 222 ? 40.653  -32.358 10.098  1.00 28.17 ? 257 ILE B CB  1 
ATOM   3867 C  CG1 . ILE B 1 222 ? 40.064  -31.728 11.369  1.00 31.54 ? 257 ILE B CG1 1 
ATOM   3868 C  CG2 . ILE B 1 222 ? 39.730  -33.436 9.534   1.00 24.35 ? 257 ILE B CG2 1 
ATOM   3869 C  CD1 . ILE B 1 222 ? 38.846  -30.869 11.133  1.00 31.79 ? 257 ILE B CD1 1 
ATOM   3870 N  N   . LEU B 1 223 ? 42.322  -33.495 12.741  1.00 20.27 ? 258 LEU B N   1 
ATOM   3871 C  CA  . LEU B 1 223 ? 42.462  -34.356 13.908  1.00 21.91 ? 258 LEU B CA  1 
ATOM   3872 C  C   . LEU B 1 223 ? 41.445  -34.096 15.005  1.00 25.31 ? 258 LEU B C   1 
ATOM   3873 O  O   . LEU B 1 223 ? 41.048  -35.039 15.694  1.00 25.83 ? 258 LEU B O   1 
ATOM   3874 C  CB  . LEU B 1 223 ? 43.868  -34.219 14.516  1.00 23.58 ? 258 LEU B CB  1 
ATOM   3875 C  CG  . LEU B 1 223 ? 45.023  -34.493 13.548  1.00 25.25 ? 258 LEU B CG  1 
ATOM   3876 C  CD1 . LEU B 1 223 ? 46.358  -34.106 14.169  1.00 30.65 ? 258 LEU B CD1 1 
ATOM   3877 C  CD2 . LEU B 1 223 ? 45.024  -35.961 13.114  1.00 30.67 ? 258 LEU B CD2 1 
ATOM   3878 N  N   . VAL B 1 224 ? 41.028  -32.852 15.206  1.00 21.87 ? 259 VAL B N   1 
ATOM   3879 C  CA  . VAL B 1 224 ? 40.143  -32.487 16.308  1.00 20.47 ? 259 VAL B CA  1 
ATOM   3880 C  C   . VAL B 1 224 ? 39.015  -31.665 15.701  1.00 21.52 ? 259 VAL B C   1 
ATOM   3881 O  O   . VAL B 1 224 ? 39.167  -30.457 15.496  1.00 20.89 ? 259 VAL B O   1 
ATOM   3882 C  CB  . VAL B 1 224 ? 40.873  -31.705 17.403  1.00 21.79 ? 259 VAL B CB  1 
ATOM   3883 C  CG1 . VAL B 1 224 ? 39.952  -31.462 18.595  1.00 26.62 ? 259 VAL B CG1 1 
ATOM   3884 C  CG2 . VAL B 1 224 ? 42.136  -32.443 17.836  1.00 21.16 ? 259 VAL B CG2 1 
ATOM   3885 N  N   . ALA B 1 225 ? 37.869  -32.307 15.450  1.00 20.57 ? 260 ALA B N   1 
ATOM   3886 C  CA  . ALA B 1 225 ? 36.755  -31.642 14.773  1.00 23.79 ? 260 ALA B CA  1 
ATOM   3887 C  C   . ALA B 1 225 ? 36.342  -30.348 15.469  1.00 20.08 ? 260 ALA B C   1 
ATOM   3888 O  O   . ALA B 1 225 ? 36.108  -29.325 14.813  1.00 25.20 ? 260 ALA B O   1 
ATOM   3889 C  CB  . ALA B 1 225 ? 35.557  -32.591 14.675  1.00 21.72 ? 260 ALA B CB  1 
ATOM   3890 N  N   . ALA B 1 226 ? 36.231  -30.373 16.800  1.00 21.39 ? 261 ALA B N   1 
ATOM   3891 C  CA  . ALA B 1 226 ? 35.697  -29.219 17.524  1.00 23.96 ? 261 ALA B CA  1 
ATOM   3892 C  C   . ALA B 1 226 ? 36.632  -28.017 17.516  1.00 20.18 ? 261 ALA B C   1 
ATOM   3893 O  O   . ALA B 1 226 ? 36.221  -26.934 17.948  1.00 27.37 ? 261 ALA B O   1 
ATOM   3894 C  CB  . ALA B 1 226 ? 35.345  -29.597 18.964  1.00 33.40 ? 261 ALA B CB  1 
ATOM   3895 N  N   . VAL B 1 227 ? 37.865  -28.175 17.042  1.00 20.91 ? 262 VAL B N   1 
ATOM   3896 C  CA  . VAL B 1 227 ? 38.831  -27.088 16.963  1.00 29.06 ? 262 VAL B CA  1 
ATOM   3897 C  C   . VAL B 1 227 ? 39.133  -26.703 15.516  1.00 21.68 ? 262 VAL B C   1 
ATOM   3898 O  O   . VAL B 1 227 ? 39.085  -25.522 15.159  1.00 24.09 ? 262 VAL B O   1 
ATOM   3899 C  CB  . VAL B 1 227 ? 40.125  -27.431 17.734  1.00 26.79 ? 262 VAL B CB  1 
ATOM   3900 C  CG1 . VAL B 1 227 ? 41.200  -26.375 17.470  1.00 23.08 ? 262 VAL B CG1 1 
ATOM   3901 C  CG2 . VAL B 1 227 ? 39.835  -27.547 19.228  1.00 26.83 ? 262 VAL B CG2 1 
ATOM   3902 N  N   . GLN B 1 228 ? 39.445  -27.690 14.671  1.00 19.64 ? 263 GLN B N   1 
ATOM   3903 C  CA  . GLN B 1 228 ? 40.104  -27.441 13.392  1.00 19.96 ? 263 GLN B CA  1 
ATOM   3904 C  C   . GLN B 1 228 ? 39.149  -27.174 12.232  1.00 27.82 ? 263 GLN B C   1 
ATOM   3905 O  O   . GLN B 1 228 ? 39.611  -26.802 11.146  1.00 27.27 ? 263 GLN B O   1 
ATOM   3906 C  CB  . GLN B 1 228 ? 41.082  -28.579 13.068  1.00 19.80 ? 263 GLN B CB  1 
ATOM   3907 C  CG  . GLN B 1 228 ? 42.199  -28.676 14.103  1.00 28.41 ? 263 GLN B CG  1 
ATOM   3908 C  CD  . GLN B 1 228 ? 43.083  -29.875 13.889  1.00 21.71 ? 263 GLN B CD  1 
ATOM   3909 O  OE1 . GLN B 1 228 ? 42.592  -30.991 13.730  1.00 24.75 ? 263 GLN B OE1 1 
ATOM   3910 N  NE2 . GLN B 1 228 ? 44.393  -29.661 13.906  1.00 23.62 ? 263 GLN B NE2 1 
ATOM   3911 N  N   . PHE B 1 229 ? 37.839  -27.342 12.418  1.00 21.36 ? 264 PHE B N   1 
ATOM   3912 C  CA  . PHE B 1 229 ? 36.916  -26.836 11.408  1.00 22.51 ? 264 PHE B CA  1 
ATOM   3913 C  C   . PHE B 1 229 ? 36.706  -25.339 11.571  1.00 28.42 ? 264 PHE B C   1 
ATOM   3914 O  O   . PHE B 1 229 ? 36.714  -24.587 10.588  1.00 28.28 ? 264 PHE B O   1 
ATOM   3915 C  CB  . PHE B 1 229 ? 35.579  -27.576 11.473  1.00 20.40 ? 264 PHE B CB  1 
ATOM   3916 C  CG  . PHE B 1 229 ? 35.623  -28.947 10.862  1.00 22.75 ? 264 PHE B CG  1 
ATOM   3917 C  CD1 . PHE B 1 229 ? 35.922  -29.113 9.513   1.00 23.05 ? 264 PHE B CD1 1 
ATOM   3918 C  CD2 . PHE B 1 229 ? 35.359  -30.074 11.629  1.00 27.87 ? 264 PHE B CD2 1 
ATOM   3919 C  CE1 . PHE B 1 229 ? 35.968  -30.380 8.947   1.00 25.90 ? 264 PHE B CE1 1 
ATOM   3920 C  CE2 . PHE B 1 229 ? 35.396  -31.341 11.064  1.00 30.62 ? 264 PHE B CE2 1 
ATOM   3921 C  CZ  . PHE B 1 229 ? 35.698  -31.493 9.719   1.00 26.13 ? 264 PHE B CZ  1 
ATOM   3922 N  N   . ASP B 1 230 ? 36.507  -24.891 12.812  1.00 26.50 ? 265 ASP B N   1 
ATOM   3923 C  CA  . ASP B 1 230 ? 36.358  -23.466 13.073  1.00 26.13 ? 265 ASP B CA  1 
ATOM   3924 C  C   . ASP B 1 230 ? 37.651  -22.716 12.778  1.00 28.74 ? 265 ASP B C   1 
ATOM   3925 O  O   . ASP B 1 230 ? 37.620  -21.606 12.234  1.00 35.22 ? 265 ASP B O   1 
ATOM   3926 C  CB  . ASP B 1 230 ? 35.935  -23.254 14.525  1.00 31.66 ? 265 ASP B CB  1 
ATOM   3927 C  CG  . ASP B 1 230 ? 34.464  -23.556 14.756  1.00 56.77 ? 265 ASP B CG  1 
ATOM   3928 O  OD1 . ASP B 1 230 ? 33.679  -23.508 13.782  1.00 55.51 ? 265 ASP B OD1 1 
ATOM   3929 O  OD2 . ASP B 1 230 ? 34.093  -23.848 15.913  1.00 63.11 ? 265 ASP B OD2 1 
ATOM   3930 N  N   . ASP B 1 231 ? 38.795  -23.296 13.142  1.00 27.75 ? 266 ASP B N   1 
ATOM   3931 C  CA  . ASP B 1 231 ? 40.098  -22.661 12.947  1.00 30.69 ? 266 ASP B CA  1 
ATOM   3932 C  C   . ASP B 1 231 ? 41.032  -23.665 12.285  1.00 27.03 ? 266 ASP B C   1 
ATOM   3933 O  O   . ASP B 1 231 ? 41.786  -24.376 12.965  1.00 25.46 ? 266 ASP B O   1 
ATOM   3934 C  CB  . ASP B 1 231 ? 40.659  -22.133 14.266  1.00 29.15 ? 266 ASP B CB  1 
ATOM   3935 C  CG  . ASP B 1 231 ? 41.921  -21.298 14.082  1.00 41.17 ? 266 ASP B CG  1 
ATOM   3936 O  OD1 . ASP B 1 231 ? 42.403  -21.161 12.934  1.00 37.23 ? 266 ASP B OD1 1 
ATOM   3937 O  OD2 . ASP B 1 231 ? 42.429  -20.765 15.091  1.00 43.38 ? 266 ASP B OD2 1 
ATOM   3938 N  N   . PRO B 1 232 ? 41.014  -23.747 10.951  1.00 26.08 ? 267 PRO B N   1 
ATOM   3939 C  CA  . PRO B 1 232 ? 41.875  -24.719 10.255  1.00 28.50 ? 267 PRO B CA  1 
ATOM   3940 C  C   . PRO B 1 232 ? 43.370  -24.468 10.419  1.00 26.51 ? 267 PRO B C   1 
ATOM   3941 O  O   . PRO B 1 232 ? 44.163  -25.355 10.072  1.00 24.63 ? 267 PRO B O   1 
ATOM   3942 C  CB  . PRO B 1 232 ? 41.449  -24.582 8.787   1.00 40.41 ? 267 PRO B CB  1 
ATOM   3943 C  CG  . PRO B 1 232 ? 40.085  -23.963 8.836   1.00 38.55 ? 267 PRO B CG  1 
ATOM   3944 C  CD  . PRO B 1 232 ? 40.092  -23.061 10.029  1.00 35.04 ? 267 PRO B CD  1 
ATOM   3945 N  N   . SER B 1 233 ? 43.784  -23.301 10.916  1.00 28.21 ? 268 SER B N   1 
ATOM   3946 C  CA  . SER B 1 233 ? 45.208  -23.021 11.068  1.00 31.88 ? 268 SER B CA  1 
ATOM   3947 C  C   . SER B 1 233 ? 45.825  -23.677 12.299  1.00 29.38 ? 268 SER B C   1 
ATOM   3948 O  O   . SER B 1 233 ? 47.052  -23.662 12.431  1.00 30.05 ? 268 SER B O   1 
ATOM   3949 C  CB  . SER B 1 233 ? 45.465  -21.512 11.116  1.00 35.23 ? 268 SER B CB  1 
ATOM   3950 O  OG  . SER B 1 233 ? 44.714  -20.899 12.148  1.00 39.52 ? 268 SER B OG  1 
ATOM   3951 N  N   . VAL B 1 234 ? 45.025  -24.244 13.199  1.00 27.20 ? 269 VAL B N   1 
ATOM   3952 C  CA  . VAL B 1 234 ? 45.577  -24.849 14.407  1.00 29.76 ? 269 VAL B CA  1 
ATOM   3953 C  C   . VAL B 1 234 ? 46.140  -26.219 14.058  1.00 25.13 ? 269 VAL B C   1 
ATOM   3954 O  O   . VAL B 1 234 ? 45.436  -27.069 13.498  1.00 23.19 ? 269 VAL B O   1 
ATOM   3955 C  CB  . VAL B 1 234 ? 44.511  -24.946 15.509  1.00 28.63 ? 269 VAL B CB  1 
ATOM   3956 C  CG1 . VAL B 1 234 ? 45.116  -25.538 16.777  1.00 30.14 ? 269 VAL B CG1 1 
ATOM   3957 C  CG2 . VAL B 1 234 ? 43.903  -23.583 15.789  1.00 33.90 ? 269 VAL B CG2 1 
ATOM   3958 N  N   . THR B 1 235 ? 47.410  -26.435 14.383  1.00 27.54 ? 270 THR B N   1 
ATOM   3959 C  CA  . THR B 1 235 ? 48.096  -27.685 14.092  1.00 27.10 ? 270 THR B CA  1 
ATOM   3960 C  C   . THR B 1 235 ? 48.452  -28.392 15.397  1.00 22.83 ? 270 THR B C   1 
ATOM   3961 O  O   . THR B 1 235 ? 48.106  -27.945 16.493  1.00 27.77 ? 270 THR B O   1 
ATOM   3962 C  CB  . THR B 1 235 ? 49.339  -27.414 13.240  1.00 27.57 ? 270 THR B CB  1 
ATOM   3963 O  OG1 . THR B 1 235 ? 50.244  -26.573 13.966  1.00 33.01 ? 270 THR B OG1 1 
ATOM   3964 C  CG2 . THR B 1 235 ? 48.944  -26.703 11.952  1.00 34.95 ? 270 THR B CG2 1 
ATOM   3965 N  N   . THR B 1 236 ? 49.148  -29.520 15.273  1.00 25.21 ? 271 THR B N   1 
ATOM   3966 C  CA  . THR B 1 236 ? 49.581  -30.287 16.430  1.00 28.06 ? 271 THR B CA  1 
ATOM   3967 C  C   . THR B 1 236 ? 51.081  -30.522 16.349  1.00 26.02 ? 271 THR B C   1 
ATOM   3968 O  O   . THR B 1 236 ? 51.698  -30.388 15.288  1.00 32.65 ? 271 THR B O   1 
ATOM   3969 C  CB  . THR B 1 236 ? 48.858  -31.644 16.543  1.00 28.32 ? 271 THR B CB  1 
ATOM   3970 O  OG1 . THR B 1 236 ? 49.340  -32.535 15.530  1.00 39.35 ? 271 THR B OG1 1 
ATOM   3971 C  CG2 . THR B 1 236 ? 47.364  -31.468 16.380  1.00 28.94 ? 271 THR B CG2 1 
ATOM   3972 N  N   . ASP B 1 237 ? 51.661  -30.881 17.494  1.00 28.02 ? 272 ASP B N   1 
ATOM   3973 C  CA  . ASP B 1 237 ? 53.072  -31.247 17.554  1.00 27.36 ? 272 ASP B CA  1 
ATOM   3974 C  C   . ASP B 1 237 ? 53.363  -32.591 16.897  1.00 31.55 ? 272 ASP B C   1 
ATOM   3975 O  O   . ASP B 1 237 ? 54.529  -32.994 16.839  1.00 42.84 ? 272 ASP B O   1 
ATOM   3976 C  CB  . ASP B 1 237 ? 53.566  -31.226 19.003  1.00 33.34 ? 272 ASP B CB  1 
ATOM   3977 C  CG  . ASP B 1 237 ? 52.868  -32.261 19.878  1.00 41.90 ? 272 ASP B CG  1 
ATOM   3978 O  OD1 . ASP B 1 237 ? 51.884  -32.881 19.419  1.00 47.87 ? 272 ASP B OD1 1 
ATOM   3979 O  OD2 . ASP B 1 237 ? 53.299  -32.443 21.042  1.00 56.96 ? 272 ASP B OD2 1 
ATOM   3980 N  N   . LEU B 1 238 ? 52.340  -33.291 16.418  1.00 27.49 ? 273 LEU B N   1 
ATOM   3981 C  CA  . LEU B 1 238 ? 52.518  -34.535 15.686  1.00 35.13 ? 273 LEU B CA  1 
ATOM   3982 C  C   . LEU B 1 238 ? 52.563  -34.318 14.177  1.00 36.89 ? 273 LEU B C   1 
ATOM   3983 O  O   . LEU B 1 238 ? 52.801  -35.278 13.434  1.00 36.25 ? 273 LEU B O   1 
ATOM   3984 C  CB  . LEU B 1 238 ? 51.389  -35.513 16.035  1.00 34.89 ? 273 LEU B CB  1 
ATOM   3985 C  CG  . LEU B 1 238 ? 51.509  -36.275 17.359  1.00 45.07 ? 273 LEU B CG  1 
ATOM   3986 C  CD1 . LEU B 1 238 ? 50.123  -36.584 17.910  1.00 42.40 ? 273 LEU B CD1 1 
ATOM   3987 C  CD2 . LEU B 1 238 ? 52.327  -37.546 17.214  1.00 47.05 ? 273 LEU B CD2 1 
ATOM   3988 N  N   . ASP B 1 239 ? 52.342  -33.088 13.711  1.00 28.97 ? 274 ASP B N   1 
ATOM   3989 C  CA  . ASP B 1 239 ? 52.453  -32.768 12.294  1.00 26.92 ? 274 ASP B CA  1 
ATOM   3990 C  C   . ASP B 1 239 ? 53.919  -32.525 11.963  1.00 26.72 ? 274 ASP B C   1 
ATOM   3991 O  O   . ASP B 1 239 ? 54.603  -31.767 12.658  1.00 37.34 ? 274 ASP B O   1 
ATOM   3992 C  CB  . ASP B 1 239 ? 51.643  -31.512 11.955  1.00 22.54 ? 274 ASP B CB  1 
ATOM   3993 C  CG  . ASP B 1 239 ? 50.145  -31.678 12.208  1.00 31.98 ? 274 ASP B CG  1 
ATOM   3994 O  OD1 . ASP B 1 239 ? 49.538  -32.624 11.663  1.00 26.59 ? 274 ASP B OD1 1 
ATOM   3995 O  OD2 . ASP B 1 239 ? 49.568  -30.847 12.945  1.00 33.85 ? 274 ASP B OD2 1 
ATOM   3996 N  N   . SER B 1 240 ? 54.402  -33.173 10.899  1.00 24.37 ? 275 SER B N   1 
ATOM   3997 C  CA  . SER B 1 240 ? 55.800  -33.023 10.512  1.00 26.03 ? 275 SER B CA  1 
ATOM   3998 C  C   . SER B 1 240 ? 56.092  -31.615 10.003  1.00 36.44 ? 275 SER B C   1 
ATOM   3999 O  O   . SER B 1 240 ? 57.187  -31.084 10.226  1.00 39.94 ? 275 SER B O   1 
ATOM   4000 C  CB  . SER B 1 240 ? 56.170  -34.071 9.458   1.00 29.81 ? 275 SER B CB  1 
ATOM   4001 O  OG  . SER B 1 240 ? 55.882  -35.383 9.914   1.00 54.51 ? 275 SER B OG  1 
ATOM   4002 N  N   . ASP B 1 241 ? 55.134  -31.001 9.307   1.00 30.48 ? 276 ASP B N   1 
ATOM   4003 C  CA  . ASP B 1 241 ? 55.309  -29.664 8.735   1.00 31.59 ? 276 ASP B CA  1 
ATOM   4004 C  C   . ASP B 1 241 ? 54.009  -28.904 8.992   1.00 27.92 ? 276 ASP B C   1 
ATOM   4005 O  O   . ASP B 1 241 ? 53.038  -29.053 8.244   1.00 29.09 ? 276 ASP B O   1 
ATOM   4006 C  CB  . ASP B 1 241 ? 55.637  -29.760 7.246   1.00 31.83 ? 276 ASP B CB  1 
ATOM   4007 C  CG  . ASP B 1 241 ? 55.908  -28.409 6.605   1.00 42.94 ? 276 ASP B CG  1 
ATOM   4008 O  OD1 . ASP B 1 241 ? 55.650  -27.369 7.245   1.00 40.37 ? 276 ASP B OD1 1 
ATOM   4009 O  OD2 . ASP B 1 241 ? 56.402  -28.390 5.455   1.00 45.95 ? 276 ASP B OD2 1 
ATOM   4010 N  N   . SER B 1 242 ? 54.004  -28.082 10.046  1.00 32.09 ? 277 SER B N   1 
ATOM   4011 C  CA  . SER B 1 242 ? 52.771  -27.422 10.473  1.00 33.99 ? 277 SER B CA  1 
ATOM   4012 C  C   . SER B 1 242 ? 52.230  -26.478 9.399   1.00 32.49 ? 277 SER B C   1 
ATOM   4013 O  O   . SER B 1 242 ? 51.020  -26.447 9.140   1.00 32.27 ? 277 SER B O   1 
ATOM   4014 C  CB  . SER B 1 242 ? 53.015  -26.676 11.787  1.00 32.25 ? 277 SER B CB  1 
ATOM   4015 O  OG  . SER B 1 242 ? 54.131  -25.813 11.670  1.00 59.79 ? 277 SER B OG  1 
ATOM   4016 N  N   . LYS B 1 243 ? 53.109  -25.696 8.765   1.00 35.85 ? 278 LYS B N   1 
ATOM   4017 C  CA  . LYS B 1 243 ? 52.649  -24.761 7.742   1.00 40.30 ? 278 LYS B CA  1 
ATOM   4018 C  C   . LYS B 1 243 ? 52.019  -25.503 6.568   1.00 36.83 ? 278 LYS B C   1 
ATOM   4019 O  O   . LYS B 1 243 ? 50.953  -25.113 6.067   1.00 32.66 ? 278 LYS B O   1 
ATOM   4020 C  CB  . LYS B 1 243 ? 53.822  -23.900 7.275   1.00 38.90 ? 278 LYS B CB  1 
ATOM   4021 C  CG  . LYS B 1 243 ? 54.178  -22.774 8.237   1.00 45.63 ? 278 LYS B CG  1 
ATOM   4022 C  CD  . LYS B 1 243 ? 55.015  -21.698 7.561   1.00 48.91 ? 278 LYS B CD  1 
ATOM   4023 C  CE  . LYS B 1 243 ? 54.410  -20.313 7.754   1.00 61.29 ? 278 LYS B CE  1 
ATOM   4024 N  NZ  . LYS B 1 243 ? 54.372  -19.918 9.191   1.00 66.66 ? 278 LYS B NZ  1 
ATOM   4025 N  N   . ALA B 1 244 ? 52.659  -26.590 6.129   1.00 31.59 ? 279 ALA B N   1 
ATOM   4026 C  CA  . ALA B 1 244 ? 52.122  -27.368 5.021   1.00 26.79 ? 279 ALA B CA  1 
ATOM   4027 C  C   . ALA B 1 244 ? 50.791  -28.009 5.387   1.00 35.93 ? 279 ALA B C   1 
ATOM   4028 O  O   . ALA B 1 244 ? 49.880  -28.068 4.551   1.00 27.64 ? 279 ALA B O   1 
ATOM   4029 C  CB  . ALA B 1 244 ? 53.135  -28.423 4.573   1.00 36.17 ? 279 ALA B CB  1 
ATOM   4030 N  N   . VAL B 1 245 ? 50.652  -28.510 6.620   1.00 28.57 ? 280 VAL B N   1 
ATOM   4031 C  CA  . VAL B 1 245 ? 49.374  -29.114 6.994   1.00 27.42 ? 280 VAL B CA  1 
ATOM   4032 C  C   . VAL B 1 245 ? 48.263  -28.068 7.038   1.00 25.58 ? 280 VAL B C   1 
ATOM   4033 O  O   . VAL B 1 245 ? 47.138  -28.334 6.603   1.00 27.59 ? 280 VAL B O   1 
ATOM   4034 C  CB  . VAL B 1 245 ? 49.468  -29.984 8.267   1.00 25.46 ? 280 VAL B CB  1 
ATOM   4035 C  CG1 . VAL B 1 245 ? 49.593  -29.142 9.504   1.00 41.81 ? 280 VAL B CG1 1 
ATOM   4036 C  CG2 . VAL B 1 245 ? 48.249  -30.886 8.378   1.00 37.26 ? 280 VAL B CG2 1 
ATOM   4037 N  N   . ALA B 1 246 ? 48.557  -26.859 7.530   1.00 25.35 ? 281 ALA B N   1 
ATOM   4038 C  CA  . ALA B 1 246 ? 47.549  -25.801 7.485   1.00 31.77 ? 281 ALA B CA  1 
ATOM   4039 C  C   . ALA B 1 246 ? 47.146  -25.486 6.044   1.00 28.45 ? 281 ALA B C   1 
ATOM   4040 O  O   . ALA B 1 246 ? 45.953  -25.397 5.726   1.00 36.07 ? 281 ALA B O   1 
ATOM   4041 C  CB  . ALA B 1 246 ? 48.057  -24.553 8.203   1.00 29.38 ? 281 ALA B CB  1 
ATOM   4042 N  N   . VAL B 1 247 ? 48.134  -25.355 5.151   1.00 27.74 ? 282 VAL B N   1 
ATOM   4043 C  CA  . VAL B 1 247 ? 47.845  -25.051 3.748   1.00 34.32 ? 282 VAL B CA  1 
ATOM   4044 C  C   . VAL B 1 247 ? 46.984  -26.145 3.126   1.00 26.77 ? 282 VAL B C   1 
ATOM   4045 O  O   . VAL B 1 247 ? 45.970  -25.869 2.468   1.00 30.67 ? 282 VAL B O   1 
ATOM   4046 C  CB  . VAL B 1 247 ? 49.153  -24.856 2.960   1.00 38.51 ? 282 VAL B CB  1 
ATOM   4047 C  CG1 . VAL B 1 247 ? 48.883  -24.924 1.463   1.00 30.74 ? 282 VAL B CG1 1 
ATOM   4048 C  CG2 . VAL B 1 247 ? 49.816  -23.542 3.341   1.00 37.03 ? 282 VAL B CG2 1 
ATOM   4049 N  N   . GLU B 1 248 ? 47.376  -27.405 3.332   1.00 30.23 ? 283 GLU B N   1 
ATOM   4050 C  CA  . GLU B 1 248 ? 46.681  -28.527 2.711   1.00 26.33 ? 283 GLU B CA  1 
ATOM   4051 C  C   . GLU B 1 248 ? 45.279  -28.699 3.281   1.00 24.96 ? 283 GLU B C   1 
ATOM   4052 O  O   . GLU B 1 248 ? 44.339  -29.015 2.542   1.00 25.08 ? 283 GLU B O   1 
ATOM   4053 C  CB  . GLU B 1 248 ? 47.498  -29.804 2.889   1.00 29.05 ? 283 GLU B CB  1 
ATOM   4054 C  CG  . GLU B 1 248 ? 48.747  -29.865 2.010   1.00 28.41 ? 283 GLU B CG  1 
ATOM   4055 C  CD  . GLU B 1 248 ? 48.447  -29.601 0.543   1.00 35.55 ? 283 GLU B CD  1 
ATOM   4056 O  OE1 . GLU B 1 248 ? 47.589  -30.311 -0.026  1.00 46.30 ? 283 GLU B OE1 1 
ATOM   4057 O  OE2 . GLU B 1 248 ? 49.073  -28.688 -0.040  1.00 42.07 ? 283 GLU B OE2 1 
ATOM   4058 N  N   . ARG B 1 249 ? 45.114  -28.509 4.592   1.00 21.52 ? 284 ARG B N   1 
ATOM   4059 C  CA  . ARG B 1 249 ? 43.786  -28.605 5.182   1.00 22.04 ? 284 ARG B CA  1 
ATOM   4060 C  C   . ARG B 1 249 ? 42.872  -27.524 4.633   1.00 25.97 ? 284 ARG B C   1 
ATOM   4061 O  O   . ARG B 1 249 ? 41.719  -27.793 4.270   1.00 24.63 ? 284 ARG B O   1 
ATOM   4062 C  CB  . ARG B 1 249 ? 43.878  -28.494 6.700   1.00 25.09 ? 284 ARG B CB  1 
ATOM   4063 C  CG  . ARG B 1 249 ? 42.527  -28.473 7.395   1.00 23.00 ? 284 ARG B CG  1 
ATOM   4064 C  CD  . ARG B 1 249 ? 42.735  -28.200 8.854   1.00 26.83 ? 284 ARG B CD  1 
ATOM   4065 N  NE  . ARG B 1 249 ? 43.631  -29.218 9.385   1.00 37.85 ? 284 ARG B NE  1 
ATOM   4066 C  CZ  . ARG B 1 249 ? 44.453  -29.041 10.407  1.00 32.46 ? 284 ARG B CZ  1 
ATOM   4067 N  NH1 . ARG B 1 249 ? 44.543  -27.877 11.027  1.00 36.49 ? 284 ARG B NH1 1 
ATOM   4068 N  NH2 . ARG B 1 249 ? 45.222  -30.054 10.799  1.00 27.16 ? 284 ARG B NH2 1 
ATOM   4069 N  N   . LYS B 1 250 ? 43.362  -26.285 4.582   1.00 24.91 ? 285 LYS B N   1 
ATOM   4070 C  CA  . LYS B 1 250 ? 42.532  -25.215 4.048   1.00 29.55 ? 285 LYS B CA  1 
ATOM   4071 C  C   . LYS B 1 250 ? 42.166  -25.478 2.594   1.00 25.55 ? 285 LYS B C   1 
ATOM   4072 O  O   . LYS B 1 250 ? 41.019  -25.253 2.190   1.00 25.20 ? 285 LYS B O   1 
ATOM   4073 C  CB  . LYS B 1 250 ? 43.192  -23.851 4.255   1.00 28.43 ? 285 LYS B CB  1 
ATOM   4074 C  CG  . LYS B 1 250 ? 43.277  -23.448 5.729   1.00 40.77 ? 285 LYS B CG  1 
ATOM   4075 C  CD  . LYS B 1 250 ? 44.567  -22.701 6.063   1.00 42.17 ? 285 LYS B CD  1 
ATOM   4076 C  CE  . LYS B 1 250 ? 44.333  -21.650 7.140   1.00 45.17 ? 285 LYS B CE  1 
ATOM   4077 N  NZ  . LYS B 1 250 ? 45.569  -20.869 7.448   1.00 56.66 ? 285 LYS B NZ  1 
ATOM   4078 N  N   . LYS B 1 251 ? 43.115  -25.988 1.804   1.00 26.78 ? 286 LYS B N   1 
ATOM   4079 C  CA  . LYS B 1 251 ? 42.826  -26.329 0.413   1.00 27.31 ? 286 LYS B CA  1 
ATOM   4080 C  C   . LYS B 1 251 ? 41.747  -27.407 0.319   1.00 26.06 ? 286 LYS B C   1 
ATOM   4081 O  O   . LYS B 1 251 ? 40.805  -27.292 -0.477  1.00 23.92 ? 286 LYS B O   1 
ATOM   4082 C  CB  . LYS B 1 251 ? 44.112  -26.786 -0.271  1.00 28.74 ? 286 LYS B CB  1 
ATOM   4083 C  CG  . LYS B 1 251 ? 44.003  -27.015 -1.762  1.00 41.81 ? 286 LYS B CG  1 
ATOM   4084 C  CD  . LYS B 1 251 ? 45.288  -27.640 -2.282  1.00 38.47 ? 286 LYS B CD  1 
ATOM   4085 C  CE  . LYS B 1 251 ? 46.503  -26.897 -1.748  1.00 52.22 ? 286 LYS B CE  1 
ATOM   4086 N  NZ  . LYS B 1 251 ? 47.777  -27.295 -2.418  1.00 44.38 ? 286 LYS B NZ  1 
ATOM   4087 N  N   . ALA B 1 252 ? 41.861  -28.460 1.134   1.00 24.28 ? 287 ALA B N   1 
ATOM   4088 C  CA  . ALA B 1 252 ? 40.880  -29.544 1.087   1.00 22.91 ? 287 ALA B CA  1 
ATOM   4089 C  C   . ALA B 1 252 ? 39.497  -29.052 1.500   1.00 23.88 ? 287 ALA B C   1 
ATOM   4090 O  O   . ALA B 1 252 ? 38.488  -29.382 0.864   1.00 25.46 ? 287 ALA B O   1 
ATOM   4091 C  CB  . ALA B 1 252 ? 41.330  -30.697 1.983   1.00 24.51 ? 287 ALA B CB  1 
ATOM   4092 N  N   . PHE B 1 253 ? 39.432  -28.266 2.575   1.00 20.68 ? 288 PHE B N   1 
ATOM   4093 C  CA  . PHE B 1 253 ? 38.142  -27.762 3.033   1.00 21.22 ? 288 PHE B CA  1 
ATOM   4094 C  C   . PHE B 1 253 ? 37.524  -26.827 2.002   1.00 25.33 ? 288 PHE B C   1 
ATOM   4095 O  O   . PHE B 1 253 ? 36.322  -26.907 1.721   1.00 25.75 ? 288 PHE B O   1 
ATOM   4096 C  CB  . PHE B 1 253 ? 38.304  -27.035 4.365   1.00 26.18 ? 288 PHE B CB  1 
ATOM   4097 C  CG  . PHE B 1 253 ? 38.588  -27.940 5.527   1.00 23.69 ? 288 PHE B CG  1 
ATOM   4098 C  CD1 . PHE B 1 253 ? 38.632  -29.319 5.369   1.00 20.09 ? 288 PHE B CD1 1 
ATOM   4099 C  CD2 . PHE B 1 253 ? 38.799  -27.403 6.794   1.00 24.47 ? 288 PHE B CD2 1 
ATOM   4100 C  CE1 . PHE B 1 253 ? 38.887  -30.152 6.458   1.00 25.86 ? 288 PHE B CE1 1 
ATOM   4101 C  CE2 . PHE B 1 253 ? 39.052  -28.227 7.882   1.00 34.15 ? 288 PHE B CE2 1 
ATOM   4102 C  CZ  . PHE B 1 253 ? 39.094  -29.600 7.713   1.00 24.83 ? 288 PHE B CZ  1 
ATOM   4103 N  N   . ALA B 1 254 ? 38.329  -25.936 1.420   1.00 22.59 ? 289 ALA B N   1 
ATOM   4104 C  CA  . ALA B 1 254 ? 37.804  -25.029 0.410   1.00 27.50 ? 289 ALA B CA  1 
ATOM   4105 C  C   . ALA B 1 254 ? 37.267  -25.801 -0.785  1.00 25.87 ? 289 ALA B C   1 
ATOM   4106 O  O   . ALA B 1 254 ? 36.194  -25.481 -1.310  1.00 26.91 ? 289 ALA B O   1 
ATOM   4107 C  CB  . ALA B 1 254 ? 38.894  -24.049 -0.027  1.00 31.29 ? 289 ALA B CB  1 
ATOM   4108 N  N   . ASP B 1 255 ? 37.997  -26.831 -1.225  1.00 24.78 ? 290 ASP B N   1 
ATOM   4109 C  CA  . ASP B 1 255 ? 37.555  -27.584 -2.394  1.00 31.16 ? 290 ASP B CA  1 
ATOM   4110 C  C   . ASP B 1 255 ? 36.282  -28.367 -2.097  1.00 24.32 ? 290 ASP B C   1 
ATOM   4111 O  O   . ASP B 1 255 ? 35.360  -28.393 -2.920  1.00 25.64 ? 290 ASP B O   1 
ATOM   4112 C  CB  . ASP B 1 255 ? 38.662  -28.519 -2.883  1.00 31.70 ? 290 ASP B CB  1 
ATOM   4113 C  CG  . ASP B 1 255 ? 38.426  -29.004 -4.300  1.00 39.44 ? 290 ASP B CG  1 
ATOM   4114 O  OD1 . ASP B 1 255 ? 38.522  -28.181 -5.233  1.00 46.01 ? 290 ASP B OD1 1 
ATOM   4115 O  OD2 . ASP B 1 255 ? 38.119  -30.201 -4.480  1.00 30.96 ? 290 ASP B OD2 1 
ATOM   4116 N  N   . ALA B 1 256 ? 36.210  -29.000 -0.925  1.00 23.36 ? 291 ALA B N   1 
ATOM   4117 C  CA  . ALA B 1 256 ? 35.004  -29.735 -0.561  1.00 25.63 ? 291 ALA B CA  1 
ATOM   4118 C  C   . ALA B 1 256 ? 33.805  -28.800 -0.419  1.00 26.71 ? 291 ALA B C   1 
ATOM   4119 O  O   . ALA B 1 256 ? 32.683  -29.146 -0.816  1.00 22.37 ? 291 ALA B O   1 
ATOM   4120 C  CB  . ALA B 1 256 ? 35.247  -30.517 0.730   1.00 25.98 ? 291 ALA B CB  1 
ATOM   4121 N  N   . ALA B 1 257 ? 34.016  -27.610 0.153   1.00 22.02 ? 292 ALA B N   1 
ATOM   4122 C  CA  . ALA B 1 257 ? 32.925  -26.654 0.288   1.00 22.32 ? 292 ALA B CA  1 
ATOM   4123 C  C   . ALA B 1 257 ? 32.439  -26.185 -1.080  1.00 30.72 ? 292 ALA B C   1 
ATOM   4124 O  O   . ALA B 1 257 ? 31.231  -26.157 -1.344  1.00 27.37 ? 292 ALA B O   1 
ATOM   4125 C  CB  . ALA B 1 257 ? 33.369  -25.470 1.148   1.00 26.12 ? 292 ALA B CB  1 
ATOM   4126 N  N   . LYS B 1 258 ? 33.371  -25.826 -1.969  1.00 25.82 ? 293 LYS B N   1 
ATOM   4127 C  CA  . LYS B 1 258 ? 32.982  -25.357 -3.296  1.00 28.29 ? 293 LYS B CA  1 
ATOM   4128 C  C   . LYS B 1 258 ? 32.297  -26.458 -4.098  1.00 26.12 ? 293 LYS B C   1 
ATOM   4129 O  O   . LYS B 1 258 ? 31.311  -26.204 -4.799  1.00 29.14 ? 293 LYS B O   1 
ATOM   4130 C  CB  . LYS B 1 258 ? 34.208  -24.827 -4.038  1.00 27.66 ? 293 LYS B CB  1 
ATOM   4131 C  CG  . LYS B 1 258 ? 33.881  -24.117 -5.345  1.00 46.97 ? 293 LYS B CG  1 
ATOM   4132 C  CD  . LYS B 1 258 ? 35.138  -23.525 -5.971  1.00 48.97 ? 293 LYS B CD  1 
ATOM   4133 C  CE  . LYS B 1 258 ? 34.991  -23.352 -7.476  1.00 49.59 ? 293 LYS B CE  1 
ATOM   4134 N  NZ  . LYS B 1 258 ? 36.246  -23.745 -8.187  1.00 61.87 ? 293 LYS B NZ  1 
ATOM   4135 N  N   . GLY B 1 259 ? 32.809  -27.690 -4.014  1.00 24.43 ? 294 GLY B N   1 
ATOM   4136 C  CA  . GLY B 1 259 ? 32.274  -28.789 -4.798  1.00 27.16 ? 294 GLY B CA  1 
ATOM   4137 C  C   . GLY B 1 259 ? 31.047  -29.449 -4.211  1.00 31.46 ? 294 GLY B C   1 
ATOM   4138 O  O   . GLY B 1 259 ? 30.320  -30.132 -4.939  1.00 30.35 ? 294 GLY B O   1 
ATOM   4139 N  N   . GLY B 1 260 ? 30.804  -29.266 -2.915  1.00 25.24 ? 295 GLY B N   1 
ATOM   4140 C  CA  . GLY B 1 260 ? 29.656  -29.875 -2.275  1.00 24.45 ? 295 GLY B CA  1 
ATOM   4141 C  C   . GLY B 1 260 ? 29.710  -31.381 -2.140  1.00 28.41 ? 295 GLY B C   1 
ATOM   4142 O  O   . GLY B 1 260 ? 28.656  -32.018 -2.052  1.00 27.10 ? 295 GLY B O   1 
ATOM   4143 N  N   . TYR B 1 261 ? 30.901  -31.973 -2.118  1.00 23.27 ? 296 TYR B N   1 
ATOM   4144 C  CA  . TYR B 1 261 ? 31.049  -33.422 -2.042  1.00 19.43 ? 296 TYR B CA  1 
ATOM   4145 C  C   . TYR B 1 261 ? 31.437  -33.876 -0.634  1.00 21.58 ? 296 TYR B C   1 
ATOM   4146 O  O   . TYR B 1 261 ? 31.680  -33.076 0.272   1.00 19.69 ? 296 TYR B O   1 
ATOM   4147 C  CB  . TYR B 1 261 ? 32.052  -33.935 -3.085  1.00 24.09 ? 296 TYR B CB  1 
ATOM   4148 C  CG  . TYR B 1 261 ? 33.455  -33.363 -2.986  1.00 20.26 ? 296 TYR B CG  1 
ATOM   4149 C  CD1 . TYR B 1 261 ? 34.366  -33.857 -2.055  1.00 21.59 ? 296 TYR B CD1 1 
ATOM   4150 C  CD2 . TYR B 1 261 ? 33.883  -32.360 -3.851  1.00 23.52 ? 296 TYR B CD2 1 
ATOM   4151 C  CE1 . TYR B 1 261 ? 35.654  -33.345 -1.965  1.00 25.93 ? 296 TYR B CE1 1 
ATOM   4152 C  CE2 . TYR B 1 261 ? 35.179  -31.846 -3.773  1.00 28.13 ? 296 TYR B CE2 1 
ATOM   4153 C  CZ  . TYR B 1 261 ? 36.056  -32.347 -2.821  1.00 29.07 ? 296 TYR B CZ  1 
ATOM   4154 O  OH  . TYR B 1 261 ? 37.345  -31.867 -2.718  1.00 29.26 ? 296 TYR B OH  1 
ATOM   4155 N  N   . LEU B 1 262 ? 31.483  -35.192 -0.455  1.00 19.85 ? 297 LEU B N   1 
ATOM   4156 C  CA  . LEU B 1 262 ? 31.715  -35.754 0.862   1.00 18.29 ? 297 LEU B CA  1 
ATOM   4157 C  C   . LEU B 1 262 ? 33.200  -35.821 1.171   1.00 18.72 ? 297 LEU B C   1 
ATOM   4158 O  O   . LEU B 1 262 ? 34.032  -36.052 0.290   1.00 17.48 ? 297 LEU B O   1 
ATOM   4159 C  CB  . LEU B 1 262 ? 31.158  -37.173 0.939   1.00 18.69 ? 297 LEU B CB  1 
ATOM   4160 C  CG  . LEU B 1 262 ? 29.644  -37.272 0.863   1.00 21.51 ? 297 LEU B CG  1 
ATOM   4161 C  CD1 . LEU B 1 262 ? 29.219  -38.705 0.583   1.00 24.97 ? 297 LEU B CD1 1 
ATOM   4162 C  CD2 . LEU B 1 262 ? 29.073  -36.768 2.171   1.00 22.33 ? 297 LEU B CD2 1 
ATOM   4163 N  N   . ILE B 1 263 ? 33.526  -35.657 2.450   1.00 16.22 ? 298 ILE B N   1 
ATOM   4164 C  CA  . ILE B 1 263 ? 34.864  -35.947 2.928   1.00 16.78 ? 298 ILE B CA  1 
ATOM   4165 C  C   . ILE B 1 263 ? 34.740  -36.945 4.064   1.00 17.38 ? 298 ILE B C   1 
ATOM   4166 O  O   . ILE B 1 263 ? 33.682  -37.107 4.675   1.00 16.06 ? 298 ILE B O   1 
ATOM   4167 C  CB  . ILE B 1 263 ? 35.619  -34.708 3.432   1.00 18.56 ? 298 ILE B CB  1 
ATOM   4168 C  CG1 . ILE B 1 263 ? 34.913  -34.158 4.676   1.00 20.64 ? 298 ILE B CG1 1 
ATOM   4169 C  CG2 . ILE B 1 263 ? 35.700  -33.667 2.326   1.00 21.93 ? 298 ILE B CG2 1 
ATOM   4170 C  CD1 . ILE B 1 263 ? 35.763  -33.197 5.441   1.00 35.03 ? 298 ILE B CD1 1 
ATOM   4171 N  N   . ALA B 1 264 ? 35.855  -37.595 4.366   1.00 16.02 ? 299 ALA B N   1 
ATOM   4172 C  CA  . ALA B 1 264 ? 35.932  -38.443 5.544   1.00 17.21 ? 299 ALA B CA  1 
ATOM   4173 C  C   . ALA B 1 264 ? 37.332  -38.330 6.107   1.00 18.09 ? 299 ALA B C   1 
ATOM   4174 O  O   . ALA B 1 264 ? 38.283  -38.016 5.385   1.00 19.10 ? 299 ALA B O   1 
ATOM   4175 C  CB  . ALA B 1 264 ? 35.589  -39.904 5.237   1.00 19.10 ? 299 ALA B CB  1 
ATOM   4176 N  N   . ALA B 1 265 ? 37.452  -38.554 7.410   1.00 15.95 ? 300 ALA B N   1 
ATOM   4177 C  CA  . ALA B 1 265 ? 38.772  -38.494 8.016   1.00 14.35 ? 300 ALA B CA  1 
ATOM   4178 C  C   . ALA B 1 265 ? 38.831  -39.497 9.150   1.00 14.45 ? 300 ALA B C   1 
ATOM   4179 O  O   . ALA B 1 265 ? 37.831  -39.754 9.831   1.00 16.64 ? 300 ALA B O   1 
ATOM   4180 C  CB  . ALA B 1 265 ? 39.125  -37.082 8.503   1.00 18.48 ? 300 ALA B CB  1 
ATOM   4181 N  N   . SER B 1 266 ? 40.035  -40.033 9.370   1.00 15.70 ? 301 SER B N   1 
ATOM   4182 C  CA  . SER B 1 266 ? 40.219  -41.162 10.278  1.00 15.23 ? 301 SER B CA  1 
ATOM   4183 C  C   . SER B 1 266 ? 39.741  -40.862 11.689  1.00 15.72 ? 301 SER B C   1 
ATOM   4184 O  O   . SER B 1 266 ? 39.319  -41.782 12.403  1.00 16.33 ? 301 SER B O   1 
ATOM   4185 C  CB  . SER B 1 266 ? 41.701  -41.511 10.355  1.00 18.16 ? 301 SER B CB  1 
ATOM   4186 O  OG  . SER B 1 266 ? 42.268  -41.592 9.061   1.00 37.58 ? 301 SER B OG  1 
ATOM   4187 N  N   . HIS B 1 267 ? 39.844  -39.604 12.132  1.00 14.10 ? 302 HIS B N   1 
ATOM   4188 C  CA  . HIS B 1 267 ? 39.609  -39.259 13.528  1.00 13.93 ? 302 HIS B CA  1 
ATOM   4189 C  C   . HIS B 1 267 ? 38.437  -38.316 13.721  1.00 14.40 ? 302 HIS B C   1 
ATOM   4190 O  O   . HIS B 1 267 ? 38.273  -37.761 14.819  1.00 16.81 ? 302 HIS B O   1 
ATOM   4191 C  CB  . HIS B 1 267 ? 40.870  -38.673 14.144  1.00 16.15 ? 302 HIS B CB  1 
ATOM   4192 C  CG  . HIS B 1 267 ? 42.028  -39.601 14.058  1.00 19.38 ? 302 HIS B CG  1 
ATOM   4193 N  ND1 . HIS B 1 267 ? 41.970  -40.893 14.537  1.00 17.16 ? 302 HIS B ND1 1 
ATOM   4194 C  CD2 . HIS B 1 267 ? 43.244  -39.461 13.487  1.00 17.10 ? 302 HIS B CD2 1 
ATOM   4195 C  CE1 . HIS B 1 267 ? 43.116  -41.497 14.304  1.00 23.35 ? 302 HIS B CE1 1 
ATOM   4196 N  NE2 . HIS B 1 267 ? 43.903  -40.650 13.666  1.00 14.00 ? 302 HIS B NE2 1 
ATOM   4197 N  N   . LEU B 1 268 ? 37.643  -38.101 12.682  1.00 15.09 ? 303 LEU B N   1 
ATOM   4198 C  CA  . LEU B 1 268 ? 36.325  -37.529 12.893  1.00 16.93 ? 303 LEU B CA  1 
ATOM   4199 C  C   . LEU B 1 268 ? 35.443  -38.577 13.564  1.00 14.45 ? 303 LEU B C   1 
ATOM   4200 O  O   . LEU B 1 268 ? 35.664  -39.784 13.394  1.00 17.06 ? 303 LEU B O   1 
ATOM   4201 C  CB  . LEU B 1 268 ? 35.716  -37.120 11.558  1.00 16.58 ? 303 LEU B CB  1 
ATOM   4202 C  CG  . LEU B 1 268 ? 36.484  -35.973 10.880  1.00 18.75 ? 303 LEU B CG  1 
ATOM   4203 C  CD1 . LEU B 1 268 ? 35.880  -35.651 9.521   1.00 18.45 ? 303 LEU B CD1 1 
ATOM   4204 C  CD2 . LEU B 1 268 ? 36.481  -34.747 11.770  1.00 21.92 ? 303 LEU B CD2 1 
ATOM   4205 N  N   . PRO B 1 269 ? 34.468  -38.149 14.363  1.00 16.13 ? 304 PRO B N   1 
ATOM   4206 C  CA  . PRO B 1 269 ? 33.653  -39.118 15.106  1.00 16.89 ? 304 PRO B CA  1 
ATOM   4207 C  C   . PRO B 1 269 ? 33.022  -40.121 14.151  1.00 15.12 ? 304 PRO B C   1 
ATOM   4208 O  O   . PRO B 1 269 ? 32.412  -39.744 13.148  1.00 15.73 ? 304 PRO B O   1 
ATOM   4209 C  CB  . PRO B 1 269 ? 32.597  -38.239 15.775  1.00 15.28 ? 304 PRO B CB  1 
ATOM   4210 C  CG  . PRO B 1 269 ? 33.276  -36.899 15.929  1.00 24.53 ? 304 PRO B CG  1 
ATOM   4211 C  CD  . PRO B 1 269 ? 34.112  -36.755 14.679  1.00 18.39 ? 304 PRO B CD  1 
ATOM   4212 N  N   . PHE B 1 270 ? 33.193  -41.404 14.476  1.00 16.35 ? 305 PHE B N   1 
ATOM   4213 C  CA  . PHE B 1 270 ? 32.800  -42.485 13.587  1.00 15.06 ? 305 PHE B CA  1 
ATOM   4214 C  C   . PHE B 1 270 ? 31.332  -42.319 13.191  1.00 16.16 ? 305 PHE B C   1 
ATOM   4215 O  O   . PHE B 1 270 ? 30.489  -42.026 14.050  1.00 16.33 ? 305 PHE B O   1 
ATOM   4216 C  CB  . PHE B 1 270 ? 33.007  -43.827 14.301  1.00 15.14 ? 305 PHE B CB  1 
ATOM   4217 C  CG  . PHE B 1 270 ? 32.581  -45.015 13.489  1.00 18.31 ? 305 PHE B CG  1 
ATOM   4218 C  CD1 . PHE B 1 270 ? 33.412  -45.526 12.497  1.00 17.46 ? 305 PHE B CD1 1 
ATOM   4219 C  CD2 . PHE B 1 270 ? 31.346  -45.613 13.700  1.00 19.81 ? 305 PHE B CD2 1 
ATOM   4220 C  CE1 . PHE B 1 270 ? 33.017  -46.610 11.729  1.00 20.28 ? 305 PHE B CE1 1 
ATOM   4221 C  CE2 . PHE B 1 270 ? 30.949  -46.702 12.932  1.00 20.51 ? 305 PHE B CE2 1 
ATOM   4222 C  CZ  . PHE B 1 270 ? 31.790  -47.199 11.955  1.00 20.16 ? 305 PHE B CZ  1 
ATOM   4223 N  N   . PRO B 1 271 ? 30.986  -42.493 11.904  1.00 16.36 ? 306 PRO B N   1 
ATOM   4224 C  CA  . PRO B 1 271 ? 31.826  -42.984 10.790  1.00 14.33 ? 306 PRO B CA  1 
ATOM   4225 C  C   . PRO B 1 271 ? 32.701  -41.923 10.126  1.00 15.67 ? 306 PRO B C   1 
ATOM   4226 O  O   . PRO B 1 271 ? 33.440  -42.236 9.193   1.00 17.63 ? 306 PRO B O   1 
ATOM   4227 C  CB  . PRO B 1 271 ? 30.780  -43.513 9.803   1.00 17.29 ? 306 PRO B CB  1 
ATOM   4228 C  CG  . PRO B 1 271 ? 29.626  -42.553 9.982   1.00 18.62 ? 306 PRO B CG  1 
ATOM   4229 C  CD  . PRO B 1 271 ? 29.595  -42.262 11.469  1.00 19.77 ? 306 PRO B CD  1 
ATOM   4230 N  N   . GLY B 1 272 ? 32.620  -40.664 10.553  1.00 14.86 ? 307 GLY B N   1 
ATOM   4231 C  CA  . GLY B 1 272 ? 33.556  -39.651 10.099  1.00 18.20 ? 307 GLY B CA  1 
ATOM   4232 C  C   . GLY B 1 272 ? 33.334  -39.140 8.696   1.00 18.80 ? 307 GLY B C   1 
ATOM   4233 O  O   . GLY B 1 272 ? 34.277  -38.632 8.079   1.00 16.44 ? 307 GLY B O   1 
ATOM   4234 N  N   . ILE B 1 273 ? 32.113  -39.249 8.174   1.00 15.12 ? 308 ILE B N   1 
ATOM   4235 C  CA  . ILE B 1 273 ? 31.778  -38.894 6.796   1.00 16.44 ? 308 ILE B CA  1 
ATOM   4236 C  C   . ILE B 1 273 ? 30.781  -37.743 6.828   1.00 18.13 ? 308 ILE B C   1 
ATOM   4237 O  O   . ILE B 1 273 ? 29.810  -37.777 7.600   1.00 16.80 ? 308 ILE B O   1 
ATOM   4238 C  CB  . ILE B 1 273 ? 31.171  -40.097 6.052   1.00 17.65 ? 308 ILE B CB  1 
ATOM   4239 C  CG1 . ILE B 1 273 ? 32.129  -41.291 6.074   1.00 15.91 ? 308 ILE B CG1 1 
ATOM   4240 C  CG2 . ILE B 1 273 ? 30.784  -39.723 4.617   1.00 19.07 ? 308 ILE B CG2 1 
ATOM   4241 C  CD1 . ILE B 1 273 ? 31.485  -42.577 5.657   1.00 17.04 ? 308 ILE B CD1 1 
ATOM   4242 N  N   . GLY B 1 274 ? 31.015  -36.728 6.000   1.00 17.64 ? 309 GLY B N   1 
ATOM   4243 C  CA  . GLY B 1 274 ? 30.052  -35.648 5.898   1.00 15.00 ? 309 GLY B CA  1 
ATOM   4244 C  C   . GLY B 1 274 ? 30.437  -34.654 4.826   1.00 20.22 ? 309 GLY B C   1 
ATOM   4245 O  O   . GLY B 1 274 ? 31.453  -34.800 4.138   1.00 16.65 ? 309 GLY B O   1 
ATOM   4246 N  N   . HIS B 1 275 ? 29.585  -33.646 4.680   1.00 15.85 ? 310 HIS B N   1 
ATOM   4247 C  CA  . HIS B 1 275 ? 29.858  -32.509 3.811   1.00 14.69 ? 310 HIS B CA  1 
ATOM   4248 C  C   . HIS B 1 275 ? 30.494  -31.371 4.607   1.00 20.56 ? 310 HIS B C   1 
ATOM   4249 O  O   . HIS B 1 275 ? 30.578  -31.401 5.835   1.00 18.63 ? 310 HIS B O   1 
ATOM   4250 C  CB  . HIS B 1 275 ? 28.576  -31.995 3.154   1.00 20.06 ? 310 HIS B CB  1 
ATOM   4251 C  CG  . HIS B 1 275 ? 27.930  -32.965 2.213   1.00 19.96 ? 310 HIS B CG  1 
ATOM   4252 N  ND1 . HIS B 1 275 ? 27.001  -33.897 2.623   1.00 21.26 ? 310 HIS B ND1 1 
ATOM   4253 C  CD2 . HIS B 1 275 ? 28.071  -33.137 0.877   1.00 25.31 ? 310 HIS B CD2 1 
ATOM   4254 C  CE1 . HIS B 1 275 ? 26.598  -34.602 1.581   1.00 18.34 ? 310 HIS B CE1 1 
ATOM   4255 N  NE2 . HIS B 1 275 ? 27.233  -34.161 0.508   1.00 19.73 ? 310 HIS B NE2 1 
ATOM   4256 N  N   . ILE B 1 276 ? 30.947  -30.348 3.889   1.00 18.38 ? 311 ILE B N   1 
ATOM   4257 C  CA  . ILE B 1 276 ? 31.559  -29.170 4.490   1.00 25.59 ? 311 ILE B CA  1 
ATOM   4258 C  C   . ILE B 1 276 ? 30.947  -27.924 3.885   1.00 21.08 ? 311 ILE B C   1 
ATOM   4259 O  O   . ILE B 1 276 ? 30.778  -27.833 2.663   1.00 20.19 ? 311 ILE B O   1 
ATOM   4260 C  CB  . ILE B 1 276 ? 33.092  -29.136 4.305   1.00 27.47 ? 311 ILE B CB  1 
ATOM   4261 C  CG1 . ILE B 1 276 ? 33.708  -30.442 4.764   1.00 40.57 ? 311 ILE B CG1 1 
ATOM   4262 C  CG2 . ILE B 1 276 ? 33.699  -27.926 5.015   1.00 37.95 ? 311 ILE B CG2 1 
ATOM   4263 C  CD1 . ILE B 1 276 ? 34.089  -30.376 6.210   1.00 54.96 ? 311 ILE B CD1 1 
ATOM   4264 N  N   . ARG B 1 277 ? 30.620  -26.956 4.732   1.00 20.88 ? 312 ARG B N   1 
ATOM   4265 C  CA  . ARG B 1 277 ? 30.259  -25.646 4.221   1.00 22.78 ? 312 ARG B CA  1 
ATOM   4266 C  C   . ARG B 1 277 ? 31.146  -24.566 4.820   1.00 23.46 ? 312 ARG B C   1 
ATOM   4267 O  O   . ARG B 1 277 ? 31.498  -24.617 6.000   1.00 26.59 ? 312 ARG B O   1 
ATOM   4268 C  CB  . ARG B 1 277 ? 28.750  -25.317 4.307   1.00 44.51 ? 312 ARG B CB  1 
ATOM   4269 C  CG  . ARG B 1 277 ? 28.012  -25.683 5.579   1.00 49.53 ? 312 ARG B CG  1 
ATOM   4270 C  CD  . ARG B 1 277 ? 26.780  -24.777 5.725   1.00 41.42 ? 312 ARG B CD  1 
ATOM   4271 N  NE  . ARG B 1 277 ? 25.587  -25.517 6.123   1.00 61.61 ? 312 ARG B NE  1 
ATOM   4272 C  CZ  . ARG B 1 277 ? 25.289  -25.869 7.367   1.00 73.55 ? 312 ARG B CZ  1 
ATOM   4273 N  NH1 . ARG B 1 277 ? 26.023  -25.473 8.393   1.00 61.83 ? 312 ARG B NH1 1 
ATOM   4274 N  NH2 . ARG B 1 277 ? 24.212  -26.620 7.588   1.00 60.40 ? 312 ARG B NH2 1 
ATOM   4275 N  N   . ALA B 1 278 ? 31.552  -23.624 3.985   1.00 24.50 ? 313 ALA B N   1 
ATOM   4276 C  CA  . ALA B 1 278 ? 32.365  -22.521 4.460   1.00 24.12 ? 313 ALA B CA  1 
ATOM   4277 C  C   . ALA B 1 278 ? 31.469  -21.591 5.263   1.00 29.29 ? 313 ALA B C   1 
ATOM   4278 O  O   . ALA B 1 278 ? 30.386  -21.215 4.802   1.00 30.71 ? 313 ALA B O   1 
ATOM   4279 C  CB  . ALA B 1 278 ? 32.976  -21.784 3.273   1.00 32.53 ? 313 ALA B CB  1 
ATOM   4280 N  N   . GLU B 1 279 ? 31.898  -21.253 6.480   1.00 26.47 ? 314 GLU B N   1 
ATOM   4281 C  CA  . GLU B 1 279 ? 31.153  -20.347 7.344   1.00 29.45 ? 314 GLU B CA  1 
ATOM   4282 C  C   . GLU B 1 279 ? 32.130  -19.487 8.125   1.00 30.86 ? 314 GLU B C   1 
ATOM   4283 O  O   . GLU B 1 279 ? 33.070  -20.014 8.733   1.00 30.33 ? 314 GLU B O   1 
ATOM   4284 C  CB  . GLU B 1 279 ? 30.265  -21.098 8.347   1.00 31.95 ? 314 GLU B CB  1 
ATOM   4285 C  CG  . GLU B 1 279 ? 29.324  -22.125 7.769   1.00 47.56 ? 314 GLU B CG  1 
ATOM   4286 C  CD  . GLU B 1 279 ? 28.234  -22.508 8.757   1.00 54.44 ? 314 GLU B CD  1 
ATOM   4287 O  OE1 . GLU B 1 279 ? 28.500  -22.479 9.980   1.00 57.33 ? 314 GLU B OE1 1 
ATOM   4288 O  OE2 . GLU B 1 279 ? 27.113  -22.835 8.311   1.00 51.55 ? 314 GLU B OE2 1 
ATOM   4289 N  N   . GLY B 1 280 ? 31.894  -18.175 8.117   1.00 34.27 ? 315 GLY B N   1 
ATOM   4290 C  CA  . GLY B 1 280 ? 32.735  -17.264 8.878   1.00 36.18 ? 315 GLY B CA  1 
ATOM   4291 C  C   . GLY B 1 280 ? 34.191  -17.393 8.481   1.00 35.91 ? 315 GLY B C   1 
ATOM   4292 O  O   . GLY B 1 280 ? 34.544  -17.386 7.296   1.00 33.13 ? 315 GLY B O   1 
ATOM   4293 N  N   . LYS B 1 281 ? 35.053  -17.533 9.489   1.00 42.56 ? 316 LYS B N   1 
ATOM   4294 C  CA  . LYS B 1 281 ? 36.488  -17.652 9.276   1.00 40.95 ? 316 LYS B CA  1 
ATOM   4295 C  C   . LYS B 1 281 ? 36.902  -19.073 8.926   1.00 32.69 ? 316 LYS B C   1 
ATOM   4296 O  O   . LYS B 1 281 ? 38.062  -19.295 8.556   1.00 33.76 ? 316 LYS B O   1 
ATOM   4297 C  CB  . LYS B 1 281 ? 37.223  -17.251 10.557  1.00 37.84 ? 316 LYS B CB  1 
ATOM   4298 C  CG  . LYS B 1 281 ? 37.443  -15.767 10.723  1.00 52.30 ? 316 LYS B CG  1 
ATOM   4299 C  CD  . LYS B 1 281 ? 36.224  -15.135 11.393  1.00 65.72 ? 316 LYS B CD  1 
ATOM   4300 C  CE  . LYS B 1 281 ? 36.618  -13.998 12.319  1.00 48.47 ? 316 LYS B CE  1 
ATOM   4301 N  NZ  . LYS B 1 281 ? 37.468  -12.989 11.634  1.00 55.20 ? 316 LYS B NZ  1 
ATOM   4302 N  N   . GLY B 1 282 ? 35.995  -20.036 9.045   1.00 27.08 ? 317 GLY B N   1 
ATOM   4303 C  CA  . GLY B 1 282 ? 36.356  -21.418 8.820   1.00 30.63 ? 317 GLY B CA  1 
ATOM   4304 C  C   . GLY B 1 282 ? 35.265  -22.221 8.152   1.00 33.40 ? 317 GLY B C   1 
ATOM   4305 O  O   . GLY B 1 282 ? 34.677  -21.794 7.151   1.00 28.55 ? 317 GLY B O   1 
ATOM   4306 N  N   . TYR B 1 283 ? 34.983  -23.392 8.712   1.00 26.45 ? 318 TYR B N   1 
ATOM   4307 C  CA  . TYR B 1 283 ? 34.129  -24.371 8.064   1.00 25.83 ? 318 TYR B CA  1 
ATOM   4308 C  C   . TYR B 1 283 ? 33.244  -25.047 9.099   1.00 28.52 ? 318 TYR B C   1 
ATOM   4309 O  O   . TYR B 1 283 ? 33.544  -25.065 10.295  1.00 26.05 ? 318 TYR B O   1 
ATOM   4310 C  CB  . TYR B 1 283 ? 34.970  -25.395 7.282   1.00 22.82 ? 318 TYR B CB  1 
ATOM   4311 C  CG  . TYR B 1 283 ? 35.779  -24.737 6.191   1.00 20.86 ? 318 TYR B CG  1 
ATOM   4312 C  CD1 . TYR B 1 283 ? 37.036  -24.205 6.449   1.00 27.41 ? 318 TYR B CD1 1 
ATOM   4313 C  CD2 . TYR B 1 283 ? 35.259  -24.603 4.910   1.00 22.59 ? 318 TYR B CD2 1 
ATOM   4314 C  CE1 . TYR B 1 283 ? 37.759  -23.575 5.451   1.00 28.26 ? 318 TYR B CE1 1 
ATOM   4315 C  CE2 . TYR B 1 283 ? 35.969  -23.980 3.914   1.00 25.31 ? 318 TYR B CE2 1 
ATOM   4316 C  CZ  . TYR B 1 283 ? 37.214  -23.471 4.183   1.00 26.08 ? 318 TYR B CZ  1 
ATOM   4317 O  OH  . TYR B 1 283 ? 37.907  -22.857 3.175   1.00 31.63 ? 318 TYR B OH  1 
ATOM   4318 N  N   . ARG B 1 284 ? 32.125  -25.574 8.610   1.00 23.68 ? 319 ARG B N   1 
ATOM   4319 C  CA  . ARG B 1 284 ? 31.171  -26.351 9.383   1.00 23.57 ? 319 ARG B CA  1 
ATOM   4320 C  C   . ARG B 1 284 ? 31.099  -27.734 8.747   1.00 24.38 ? 319 ARG B C   1 
ATOM   4321 O  O   . ARG B 1 284 ? 30.850  -27.856 7.539   1.00 26.34 ? 319 ARG B O   1 
ATOM   4322 C  CB  . ARG B 1 284 ? 29.794  -25.695 9.278   1.00 26.40 ? 319 ARG B CB  1 
ATOM   4323 C  CG  . ARG B 1 284 ? 28.634  -26.564 9.735   1.00 41.23 ? 319 ARG B CG  1 
ATOM   4324 C  CD  . ARG B 1 284 ? 28.435  -26.523 11.233  1.00 55.65 ? 319 ARG B CD  1 
ATOM   4325 N  NE  . ARG B 1 284 ? 28.672  -25.182 11.751  1.00 66.19 ? 319 ARG B NE  1 
ATOM   4326 C  CZ  . ARG B 1 284 ? 28.942  -24.897 13.017  1.00 56.67 ? 319 ARG B CZ  1 
ATOM   4327 N  NH1 . ARG B 1 284 ? 28.958  -25.836 13.949  1.00 69.13 ? 319 ARG B NH1 1 
ATOM   4328 N  NH2 . ARG B 1 284 ? 29.194  -23.636 13.358  1.00 50.14 ? 319 ARG B NH2 1 
ATOM   4329 N  N   . PHE B 1 285 ? 31.327  -28.769 9.552   1.00 23.77 ? 320 PHE B N   1 
ATOM   4330 C  CA  . PHE B 1 285 ? 31.201  -30.152 9.109   1.00 20.51 ? 320 PHE B CA  1 
ATOM   4331 C  C   . PHE B 1 285 ? 29.754  -30.583 9.312   1.00 21.22 ? 320 PHE B C   1 
ATOM   4332 O  O   . PHE B 1 285 ? 29.165  -30.322 10.366  1.00 23.88 ? 320 PHE B O   1 
ATOM   4333 C  CB  . PHE B 1 285 ? 32.136  -31.035 9.940   1.00 19.98 ? 320 PHE B CB  1 
ATOM   4334 C  CG  . PHE B 1 285 ? 32.084  -32.493 9.592   1.00 18.60 ? 320 PHE B CG  1 
ATOM   4335 C  CD1 . PHE B 1 285 ? 32.460  -32.938 8.334   1.00 18.27 ? 320 PHE B CD1 1 
ATOM   4336 C  CD2 . PHE B 1 285 ? 31.701  -33.431 10.543  1.00 24.27 ? 320 PHE B CD2 1 
ATOM   4337 C  CE1 . PHE B 1 285 ? 32.429  -34.292 8.021   1.00 18.69 ? 320 PHE B CE1 1 
ATOM   4338 C  CE2 . PHE B 1 285 ? 31.667  -34.782 10.239  1.00 19.88 ? 320 PHE B CE2 1 
ATOM   4339 C  CZ  . PHE B 1 285 ? 32.023  -35.213 8.970   1.00 17.29 ? 320 PHE B CZ  1 
ATOM   4340 N  N   . VAL B 1 286 ? 29.181  -31.221 8.303   1.00 18.55 ? 321 VAL B N   1 
ATOM   4341 C  CA  . VAL B 1 286 ? 27.802  -31.681 8.328   1.00 19.86 ? 321 VAL B CA  1 
ATOM   4342 C  C   . VAL B 1 286 ? 27.813  -33.195 8.162   1.00 18.02 ? 321 VAL B C   1 
ATOM   4343 O  O   . VAL B 1 286 ? 27.925  -33.708 7.047   1.00 17.68 ? 321 VAL B O   1 
ATOM   4344 C  CB  . VAL B 1 286 ? 26.964  -31.000 7.230   1.00 22.96 ? 321 VAL B CB  1 
ATOM   4345 C  CG1 . VAL B 1 286 ? 25.506  -31.427 7.321   1.00 28.01 ? 321 VAL B CG1 1 
ATOM   4346 C  CG2 . VAL B 1 286 ? 27.076  -29.478 7.350   1.00 23.08 ? 321 VAL B CG2 1 
ATOM   4347 N  N   . PRO B 1 287 ? 27.745  -33.946 9.263   1.00 18.51 ? 322 PRO B N   1 
ATOM   4348 C  CA  . PRO B 1 287 ? 27.798  -35.408 9.162   1.00 19.61 ? 322 PRO B CA  1 
ATOM   4349 C  C   . PRO B 1 287 ? 26.659  -35.923 8.298   1.00 18.58 ? 322 PRO B C   1 
ATOM   4350 O  O   . PRO B 1 287 ? 25.558  -35.365 8.285   1.00 20.17 ? 322 PRO B O   1 
ATOM   4351 C  CB  . PRO B 1 287 ? 27.635  -35.879 10.615  1.00 20.54 ? 322 PRO B CB  1 
ATOM   4352 C  CG  . PRO B 1 287 ? 27.871  -34.677 11.465  1.00 30.86 ? 322 PRO B CG  1 
ATOM   4353 C  CD  . PRO B 1 287 ? 27.528  -33.476 10.640  1.00 21.74 ? 322 PRO B CD  1 
ATOM   4354 N  N   . VAL B 1 288 ? 26.939  -36.998 7.559   1.00 16.64 ? 323 VAL B N   1 
ATOM   4355 C  CA  . VAL B 1 288 ? 25.911  -37.577 6.709   1.00 19.22 ? 323 VAL B CA  1 
ATOM   4356 C  C   . VAL B 1 288 ? 24.726  -38.022 7.546   1.00 23.07 ? 323 VAL B C   1 
ATOM   4357 O  O   . VAL B 1 288 ? 24.872  -38.501 8.678   1.00 18.87 ? 323 VAL B O   1 
ATOM   4358 C  CB  . VAL B 1 288 ? 26.442  -38.755 5.877   1.00 19.74 ? 323 VAL B CB  1 
ATOM   4359 C  CG1 . VAL B 1 288 ? 27.430  -38.260 4.855   1.00 25.62 ? 323 VAL B CG1 1 
ATOM   4360 C  CG2 . VAL B 1 288 ? 27.020  -39.864 6.765   1.00 19.64 ? 323 VAL B CG2 1 
ATOM   4361 N  N   . ASN B 1 289 ? 23.538  -37.839 6.978   1.00 22.87 ? 324 ASN B N   1 
ATOM   4362 C  CA  . ASN B 1 289 ? 22.304  -38.354 7.550   1.00 22.14 ? 324 ASN B CA  1 
ATOM   4363 C  C   . ASN B 1 289 ? 22.335  -39.880 7.520   1.00 16.93 ? 324 ASN B C   1 
ATOM   4364 O  O   . ASN B 1 289 ? 22.700  -40.476 6.502   1.00 19.35 ? 324 ASN B O   1 
ATOM   4365 C  CB  . ASN B 1 289 ? 21.155  -37.841 6.680   1.00 26.77 ? 324 ASN B CB  1 
ATOM   4366 C  CG  . ASN B 1 289 ? 19.796  -38.300 7.152   1.00 54.69 ? 324 ASN B CG  1 
ATOM   4367 O  OD1 . ASN B 1 289 ? 19.508  -38.310 8.349   1.00 57.62 ? 324 ASN B OD1 1 
ATOM   4368 N  ND2 . ASN B 1 289 ? 18.941  -38.681 6.201   1.00 31.97 ? 324 ASN B ND2 1 
ATOM   4369 N  N   . TYR B 1 290 ? 21.942  -40.512 8.628   1.00 18.71 ? 325 TYR B N   1 
ATOM   4370 C  CA  . TYR B 1 290 ? 21.839  -41.966 8.667   1.00 15.11 ? 325 TYR B CA  1 
ATOM   4371 C  C   . TYR B 1 290 ? 20.986  -42.477 7.512   1.00 20.94 ? 325 TYR B C   1 
ATOM   4372 O  O   . TYR B 1 290 ? 19.857  -42.023 7.295   1.00 19.43 ? 325 TYR B O   1 
ATOM   4373 C  CB  . TYR B 1 290 ? 21.213  -42.404 9.988   1.00 21.92 ? 325 TYR B CB  1 
ATOM   4374 C  CG  . TYR B 1 290 ? 21.016  -43.903 10.091  1.00 19.59 ? 325 TYR B CG  1 
ATOM   4375 C  CD1 . TYR B 1 290 ? 22.090  -44.757 10.310  1.00 21.36 ? 325 TYR B CD1 1 
ATOM   4376 C  CD2 . TYR B 1 290 ? 19.753  -44.464 9.965   1.00 18.88 ? 325 TYR B CD2 1 
ATOM   4377 C  CE1 . TYR B 1 290 ? 21.903  -46.127 10.406  1.00 27.01 ? 325 TYR B CE1 1 
ATOM   4378 C  CE2 . TYR B 1 290 ? 19.554  -45.823 10.059  1.00 20.24 ? 325 TYR B CE2 1 
ATOM   4379 C  CZ  . TYR B 1 290 ? 20.630  -46.654 10.282  1.00 24.77 ? 325 TYR B CZ  1 
ATOM   4380 O  OH  . TYR B 1 290 ? 20.431  -48.013 10.370  1.00 23.35 ? 325 TYR B OH  1 
ATOM   4381 N  N   . SER B 1 291 ? 21.529  -43.430 6.768   1.00 16.98 ? 326 SER B N   1 
ATOM   4382 C  CA  . SER B 1 291 ? 20.829  -43.970 5.617   1.00 19.82 ? 326 SER B CA  1 
ATOM   4383 C  C   . SER B 1 291 ? 21.016  -45.475 5.600   1.00 25.15 ? 326 SER B C   1 
ATOM   4384 O  O   . SER B 1 291 ? 22.120  -45.975 5.836   1.00 23.46 ? 326 SER B O   1 
ATOM   4385 C  CB  . SER B 1 291 ? 21.357  -43.370 4.306   1.00 20.46 ? 326 SER B CB  1 
ATOM   4386 O  OG  . SER B 1 291 ? 20.642  -43.886 3.196   1.00 28.72 ? 326 SER B OG  1 
ATOM   4387 N  N   . VAL B 1 292 ? 19.938  -46.186 5.324   1.00 17.54 ? 327 VAL B N   1 
ATOM   4388 C  CA  . VAL B 1 292 ? 19.966  -47.637 5.224   1.00 20.31 ? 327 VAL B CA  1 
ATOM   4389 C  C   . VAL B 1 292 ? 20.376  -48.034 3.809   1.00 22.96 ? 327 VAL B C   1 
ATOM   4390 O  O   . VAL B 1 292 ? 19.914  -47.450 2.819   1.00 22.96 ? 327 VAL B O   1 
ATOM   4391 C  CB  . VAL B 1 292 ? 18.590  -48.222 5.593   1.00 22.28 ? 327 VAL B CB  1 
ATOM   4392 C  CG1 . VAL B 1 292 ? 18.574  -49.730 5.353   1.00 24.34 ? 327 VAL B CG1 1 
ATOM   4393 C  CG2 . VAL B 1 292 ? 18.235  -47.879 7.037   1.00 26.29 ? 327 VAL B CG2 1 
ATOM   4394 N  N   . VAL B 1 293 ? 21.252  -49.032 3.713   1.00 20.79 ? 328 VAL B N   1 
ATOM   4395 C  CA  . VAL B 1 293 ? 21.656  -49.628 2.444   1.00 22.25 ? 328 VAL B CA  1 
ATOM   4396 C  C   . VAL B 1 293 ? 21.018  -51.006 2.333   1.00 31.66 ? 328 VAL B C   1 
ATOM   4397 O  O   . VAL B 1 293 ? 21.005  -51.777 3.300   1.00 29.16 ? 328 VAL B O   1 
ATOM   4398 C  CB  . VAL B 1 293 ? 23.190  -49.723 2.328   1.00 23.39 ? 328 VAL B CB  1 
ATOM   4399 C  CG1 . VAL B 1 293 ? 23.602  -50.333 0.976   1.00 24.78 ? 328 VAL B CG1 1 
ATOM   4400 C  CG2 . VAL B 1 293 ? 23.813  -48.349 2.530   1.00 21.62 ? 328 VAL B CG2 1 
ATOM   4401 N  N   . ASN B 1 294 ? 20.480  -51.310 1.154   1.00 28.56 ? 329 ASN B N   1 
ATOM   4402 C  CA  . ASN B 1 294 ? 19.874  -52.601 0.868   1.00 33.51 ? 329 ASN B CA  1 
ATOM   4403 C  C   . ASN B 1 294 ? 20.500  -53.195 -0.386  1.00 24.02 ? 329 ASN B C   1 
ATOM   4404 O  O   . ASN B 1 294 ? 21.088  -52.489 -1.209  1.00 32.55 ? 329 ASN B O   1 
ATOM   4405 C  CB  . ASN B 1 294 ? 18.359  -52.478 0.699   1.00 33.11 ? 329 ASN B CB  1 
ATOM   4406 C  CG  . ASN B 1 294 ? 17.664  -52.146 1.995   1.00 32.60 ? 329 ASN B CG  1 
ATOM   4407 O  OD1 . ASN B 1 294 ? 17.016  -51.105 2.118   1.00 36.92 ? 329 ASN B OD1 1 
ATOM   4408 N  ND2 . ASN B 1 294 ? 17.796  -53.032 2.978   1.00 32.11 ? 329 ASN B ND2 1 
ATOM   4409 N  N   . ALA B 1 295 ? 20.383  -54.516 -0.512  1.00 31.44 ? 330 ALA B N   1 
ATOM   4410 C  CA  . ALA B 1 295 ? 20.942  -55.200 -1.671  1.00 37.21 ? 330 ALA B CA  1 
ATOM   4411 C  C   . ALA B 1 295 ? 20.270  -54.717 -2.954  1.00 41.28 ? 330 ALA B C   1 
ATOM   4412 O  O   . ALA B 1 295 ? 19.078  -54.394 -2.968  1.00 41.62 ? 330 ALA B O   1 
ATOM   4413 C  CB  . ALA B 1 295 ? 20.772  -56.712 -1.519  1.00 38.14 ? 330 ALA B CB  1 
ATOM   4414 N  N   . ALA B 1 296 ? 21.049  -54.650 -4.031  1.00 44.40 ? 331 ALA B N   1 
ATOM   4415 C  CA  . ALA B 1 296 ? 20.548  -54.184 -5.325  1.00 46.87 ? 331 ALA B CA  1 
ATOM   4416 C  C   . ALA B 1 296 ? 19.814  -55.292 -6.082  1.00 48.18 ? 331 ALA B C   1 
ATOM   4417 O  O   . ALA B 1 296 ? 18.860  -55.888 -5.571  1.00 49.07 ? 331 ALA B O   1 
ATOM   4418 C  CB  . ALA B 1 296 ? 21.691  -53.621 -6.170  1.00 46.96 ? 331 ALA B CB  1 
HETATM 4419 ZN ZN  . ZN  C 2 .   ? 4.050   -38.396 15.482  1.00 20.44 ? 401 ZN  A ZN  1 
HETATM 4420 ZN ZN  . ZN  D 2 .   ? 6.566   -40.157 14.630  1.00 21.21 ? 402 ZN  A ZN  1 
HETATM 4421 ZN ZN  . ZN  E 2 .   ? 45.988  -40.982 13.024  1.00 21.29 ? 401 ZN  B ZN  1 
HETATM 4422 ZN ZN  . ZN  F 2 .   ? 48.611  -39.420 12.078  1.00 21.16 ? 402 ZN  B ZN  1 
HETATM 4423 O  O   . HOH G 3 .   ? 6.562   -29.188 28.369  1.00 42.59 ? 501 HOH A O   1 
HETATM 4424 O  O   . HOH G 3 .   ? 9.525   -40.015 42.798  1.00 29.01 ? 502 HOH A O   1 
HETATM 4425 O  O   . HOH G 3 .   ? 0.826   -37.185 37.380  1.00 43.27 ? 503 HOH A O   1 
HETATM 4426 O  O   . HOH G 3 .   ? 37.301  -61.979 -6.844  1.00 48.30 ? 504 HOH A O   1 
HETATM 4427 O  O   . HOH G 3 .   ? 2.036   -25.572 25.979  1.00 42.78 ? 505 HOH A O   1 
HETATM 4428 O  O   . HOH G 3 .   ? 11.326  -21.041 8.297   1.00 28.31 ? 506 HOH A O   1 
HETATM 4429 O  O   . HOH G 3 .   ? 10.975  -42.237 20.593  1.00 21.24 ? 507 HOH A O   1 
HETATM 4430 O  O   . HOH G 3 .   ? 2.564   -27.391 3.678   1.00 42.00 ? 508 HOH A O   1 
HETATM 4431 O  O   . HOH G 3 .   ? 28.551  -44.095 33.430  1.00 45.17 ? 509 HOH A O   1 
HETATM 4432 O  O   . HOH G 3 .   ? 6.986   -26.761 3.325   1.00 23.96 ? 510 HOH A O   1 
HETATM 4433 O  O   . HOH G 3 .   ? 8.064   -48.345 4.461   1.00 23.00 ? 511 HOH A O   1 
HETATM 4434 O  O   . HOH G 3 .   ? -6.515  -30.326 15.710  1.00 40.10 ? 512 HOH A O   1 
HETATM 4435 O  O   . HOH G 3 .   ? 11.067  -36.956 16.323  1.00 20.07 ? 513 HOH A O   1 
HETATM 4436 O  O   . HOH G 3 .   ? 31.778  -52.697 23.009  1.00 33.26 ? 514 HOH A O   1 
HETATM 4437 O  O   . HOH G 3 .   ? 1.759   -36.128 29.750  1.00 21.34 ? 515 HOH A O   1 
HETATM 4438 O  O   . HOH G 3 .   ? -10.883 -37.533 28.272  1.00 28.33 ? 516 HOH A O   1 
HETATM 4439 O  O   . HOH G 3 .   ? -15.774 -46.104 15.451  1.00 35.88 ? 517 HOH A O   1 
HETATM 4440 O  O   . HOH G 3 .   ? 23.613  -25.477 25.774  1.00 35.22 ? 518 HOH A O   1 
HETATM 4441 O  O   . HOH G 3 .   ? 26.812  -30.253 29.187  1.00 36.81 ? 519 HOH A O   1 
HETATM 4442 O  O   . HOH G 3 .   ? 20.954  -25.301 13.436  1.00 38.72 ? 520 HOH A O   1 
HETATM 4443 O  O   . HOH G 3 .   ? 5.743   -20.226 20.052  1.00 42.53 ? 521 HOH A O   1 
HETATM 4444 O  O   . HOH G 3 .   ? 22.659  -49.471 10.929  1.00 23.30 ? 522 HOH A O   1 
HETATM 4445 O  O   . HOH G 3 .   ? 29.382  -38.171 16.721  1.00 34.23 ? 523 HOH A O   1 
HETATM 4446 O  O   . HOH G 3 .   ? 19.321  -26.718 7.021   1.00 28.98 ? 524 HOH A O   1 
HETATM 4447 O  O   . HOH G 3 .   ? 3.961   -32.050 21.328  1.00 23.16 ? 525 HOH A O   1 
HETATM 4448 O  O   . HOH G 3 .   ? 9.858   -49.537 39.777  1.00 35.11 ? 526 HOH A O   1 
HETATM 4449 O  O   . HOH G 3 .   ? 3.515   -43.989 38.272  1.00 51.72 ? 527 HOH A O   1 
HETATM 4450 O  O   . HOH G 3 .   ? 19.278  -61.318 21.929  1.00 40.66 ? 528 HOH A O   1 
HETATM 4451 O  O   . HOH G 3 .   ? 8.495   -51.866 15.238  1.00 16.12 ? 529 HOH A O   1 
HETATM 4452 O  O   . HOH G 3 .   ? 19.429  -50.318 27.163  1.00 20.27 ? 530 HOH A O   1 
HETATM 4453 O  O   . HOH G 3 .   ? -15.654 -37.689 19.878  1.00 21.39 ? 531 HOH A O   1 
HETATM 4454 O  O   . HOH G 3 .   ? 29.556  -49.310 17.277  1.00 25.65 ? 532 HOH A O   1 
HETATM 4455 O  O   . HOH G 3 .   ? 3.248   -62.860 22.757  1.00 42.69 ? 533 HOH A O   1 
HETATM 4456 O  O   . HOH G 3 .   ? -4.798  -60.034 20.226  1.00 47.89 ? 534 HOH A O   1 
HETATM 4457 O  O   . HOH G 3 .   ? 13.490  -19.793 18.731  1.00 43.94 ? 535 HOH A O   1 
HETATM 4458 O  O   . HOH G 3 .   ? 4.570   -40.093 14.595  1.00 17.71 ? 536 HOH A O   1 
HETATM 4459 O  O   . HOH G 3 .   ? 17.777  -19.024 20.159  1.00 39.43 ? 537 HOH A O   1 
HETATM 4460 O  O   . HOH G 3 .   ? 9.001   -43.714 41.223  1.00 21.43 ? 538 HOH A O   1 
HETATM 4461 O  O   . HOH G 3 .   ? -3.050  -24.225 17.257  1.00 38.51 ? 539 HOH A O   1 
HETATM 4462 O  O   . HOH G 3 .   ? -1.811  -35.514 15.784  1.00 29.32 ? 540 HOH A O   1 
HETATM 4463 O  O   . HOH G 3 .   ? 16.560  -41.099 16.052  1.00 15.81 ? 541 HOH A O   1 
HETATM 4464 O  O   . HOH G 3 .   ? 2.262   -57.415 28.366  1.00 30.70 ? 542 HOH A O   1 
HETATM 4465 O  O   . HOH G 3 .   ? 1.037   -28.466 5.843   1.00 37.73 ? 543 HOH A O   1 
HETATM 4466 O  O   . HOH G 3 .   ? 6.099   -30.018 14.045  1.00 23.21 ? 544 HOH A O   1 
HETATM 4467 O  O   . HOH G 3 .   ? -9.854  -52.308 19.228  1.00 44.05 ? 545 HOH A O   1 
HETATM 4468 O  O   . HOH G 3 .   ? 10.341  -60.683 32.102  1.00 46.72 ? 546 HOH A O   1 
HETATM 4469 O  O   . HOH G 3 .   ? 28.057  -44.505 23.644  1.00 21.63 ? 547 HOH A O   1 
HETATM 4470 O  O   . HOH G 3 .   ? 16.915  -20.566 24.668  1.00 29.75 ? 548 HOH A O   1 
HETATM 4471 O  O   . HOH G 3 .   ? 17.890  -49.033 10.501  1.00 18.44 ? 549 HOH A O   1 
HETATM 4472 O  O   . HOH G 3 .   ? 7.689   -63.186 22.903  1.00 48.55 ? 550 HOH A O   1 
HETATM 4473 O  O   . HOH G 3 .   ? -11.124 -48.157 21.521  1.00 29.92 ? 551 HOH A O   1 
HETATM 4474 O  O   . HOH G 3 .   ? 0.381   -52.987 15.891  1.00 28.27 ? 552 HOH A O   1 
HETATM 4475 O  O   . HOH G 3 .   ? 21.851  -37.612 15.035  1.00 25.43 ? 553 HOH A O   1 
HETATM 4476 O  O   . HOH G 3 .   ? 16.684  -29.425 -1.104  1.00 26.03 ? 554 HOH A O   1 
HETATM 4477 O  O   . HOH G 3 .   ? 1.067   -28.204 25.639  1.00 29.46 ? 555 HOH A O   1 
HETATM 4478 O  O   . HOH G 3 .   ? 14.732  -49.399 6.537   1.00 25.47 ? 556 HOH A O   1 
HETATM 4479 O  O   . HOH G 3 .   ? 32.019  -48.583 28.756  1.00 34.15 ? 557 HOH A O   1 
HETATM 4480 O  O   . HOH G 3 .   ? 21.201  -44.097 39.199  1.00 30.63 ? 558 HOH A O   1 
HETATM 4481 O  O   . HOH G 3 .   ? 0.642   -34.375 37.266  1.00 38.75 ? 559 HOH A O   1 
HETATM 4482 O  O   . HOH G 3 .   ? 9.590   -29.464 -3.266  1.00 47.94 ? 560 HOH A O   1 
HETATM 4483 O  O   . HOH G 3 .   ? 26.793  -33.771 21.929  1.00 28.11 ? 561 HOH A O   1 
HETATM 4484 O  O   . HOH G 3 .   ? 17.290  -26.475 11.429  1.00 23.26 ? 562 HOH A O   1 
HETATM 4485 O  O   . HOH G 3 .   ? -5.283  -59.245 25.079  1.00 26.70 ? 563 HOH A O   1 
HETATM 4486 O  O   . HOH G 3 .   ? 18.707  -56.005 12.753  1.00 44.63 ? 564 HOH A O   1 
HETATM 4487 O  O   . HOH G 3 .   ? 9.706   -31.727 26.561  1.00 18.44 ? 565 HOH A O   1 
HETATM 4488 O  O   . HOH G 3 .   ? 8.405   -19.519 10.248  1.00 43.27 ? 566 HOH A O   1 
HETATM 4489 O  O   . HOH G 3 .   ? -4.784  -56.076 17.239  1.00 30.56 ? 567 HOH A O   1 
HETATM 4490 O  O   . HOH G 3 .   ? 22.143  -29.489 25.663  1.00 21.02 ? 568 HOH A O   1 
HETATM 4491 O  O   . HOH G 3 .   ? -4.056  -31.580 25.166  1.00 26.68 ? 569 HOH A O   1 
HETATM 4492 O  O   . HOH G 3 .   ? 28.190  -47.269 21.461  1.00 20.15 ? 570 HOH A O   1 
HETATM 4493 O  O   . HOH G 3 .   ? 6.213   -31.684 16.234  1.00 21.21 ? 571 HOH A O   1 
HETATM 4494 O  O   . HOH G 3 .   ? 26.200  -29.335 15.239  1.00 37.33 ? 572 HOH A O   1 
HETATM 4495 O  O   . HOH G 3 .   ? -3.600  -35.971 31.604  1.00 23.23 ? 573 HOH A O   1 
HETATM 4496 O  O   . HOH G 3 .   ? 14.401  -47.813 38.031  1.00 36.76 ? 574 HOH A O   1 
HETATM 4497 O  O   . HOH G 3 .   ? 23.205  -30.358 13.630  1.00 47.60 ? 575 HOH A O   1 
HETATM 4498 O  O   . HOH G 3 .   ? -2.604  -33.205 31.665  1.00 36.60 ? 576 HOH A O   1 
HETATM 4499 O  O   . HOH G 3 .   ? 23.169  -16.267 18.887  1.00 29.49 ? 577 HOH A O   1 
HETATM 4500 O  O   . HOH G 3 .   ? -10.635 -44.696 0.388   1.00 47.58 ? 578 HOH A O   1 
HETATM 4501 O  O   . HOH G 3 .   ? 24.090  -57.150 21.761  1.00 33.92 ? 579 HOH A O   1 
HETATM 4502 O  O   . HOH G 3 .   ? 7.969   -20.402 7.848   1.00 36.78 ? 580 HOH A O   1 
HETATM 4503 O  O   . HOH G 3 .   ? 17.011  -24.165 8.319   1.00 32.77 ? 581 HOH A O   1 
HETATM 4504 O  O   . HOH G 3 .   ? 14.456  -30.435 27.066  1.00 20.07 ? 582 HOH A O   1 
HETATM 4505 O  O   . HOH G 3 .   ? 2.145   -56.598 13.819  1.00 36.19 ? 583 HOH A O   1 
HETATM 4506 O  O   . HOH G 3 .   ? 11.897  -56.407 13.659  1.00 20.59 ? 584 HOH A O   1 
HETATM 4507 O  O   . HOH G 3 .   ? 24.298  -42.995 12.586  1.00 37.04 ? 585 HOH A O   1 
HETATM 4508 O  O   . HOH G 3 .   ? 5.832   -50.345 8.858   1.00 21.09 ? 586 HOH A O   1 
HETATM 4509 O  O   . HOH G 3 .   ? 23.106  -38.758 17.423  1.00 18.68 ? 587 HOH A O   1 
HETATM 4510 O  O   . HOH G 3 .   ? -2.837  -43.815 8.177   1.00 30.61 ? 588 HOH A O   1 
HETATM 4511 O  O   . HOH G 3 .   ? 17.754  -59.857 15.496  1.00 27.90 ? 589 HOH A O   1 
HETATM 4512 O  O   . HOH G 3 .   ? 24.743  -49.571 14.764  1.00 38.87 ? 590 HOH A O   1 
HETATM 4513 O  O   . HOH G 3 .   ? 5.936   -55.024 34.433  1.00 34.83 ? 591 HOH A O   1 
HETATM 4514 O  O   . HOH G 3 .   ? -5.012  -35.054 15.601  1.00 48.29 ? 592 HOH A O   1 
HETATM 4515 O  O   . HOH G 3 .   ? 5.427   -47.004 36.101  1.00 25.35 ? 593 HOH A O   1 
HETATM 4516 O  O   . HOH G 3 .   ? 16.001  -38.734 10.648  1.00 15.29 ? 594 HOH A O   1 
HETATM 4517 O  O   . HOH G 3 .   ? 23.419  -35.561 29.928  1.00 29.68 ? 595 HOH A O   1 
HETATM 4518 O  O   . HOH G 3 .   ? -7.693  -36.271 25.155  1.00 19.52 ? 596 HOH A O   1 
HETATM 4519 O  O   . HOH G 3 .   ? -2.750  -56.546 15.516  1.00 38.72 ? 597 HOH A O   1 
HETATM 4520 O  O   . HOH G 3 .   ? -15.697 -49.705 23.726  1.00 37.63 ? 598 HOH A O   1 
HETATM 4521 O  O   . HOH G 3 .   ? 16.492  -32.761 8.536   1.00 24.73 ? 599 HOH A O   1 
HETATM 4522 O  O   . HOH G 3 .   ? -1.675  -44.969 15.153  1.00 23.54 ? 600 HOH A O   1 
HETATM 4523 O  O   . HOH G 3 .   ? -11.378 -36.683 22.051  1.00 23.63 ? 601 HOH A O   1 
HETATM 4524 O  O   . HOH G 3 .   ? 7.544   -57.993 27.970  1.00 21.94 ? 602 HOH A O   1 
HETATM 4525 O  O   . HOH G 3 .   ? 27.646  -41.587 22.854  1.00 35.74 ? 603 HOH A O   1 
HETATM 4526 O  O   . HOH G 3 .   ? -3.602  -44.955 36.261  1.00 32.07 ? 604 HOH A O   1 
HETATM 4527 O  O   . HOH G 3 .   ? 7.799   -34.597 35.508  1.00 25.27 ? 605 HOH A O   1 
HETATM 4528 O  O   . HOH G 3 .   ? 14.665  -23.463 9.082   1.00 25.24 ? 606 HOH A O   1 
HETATM 4529 O  O   . HOH G 3 .   ? 4.059   -40.751 40.460  1.00 30.59 ? 607 HOH A O   1 
HETATM 4530 O  O   . HOH G 3 .   ? 7.742   -21.677 24.713  1.00 32.02 ? 608 HOH A O   1 
HETATM 4531 O  O   . HOH G 3 .   ? 16.126  -45.104 12.991  1.00 23.41 ? 609 HOH A O   1 
HETATM 4532 O  O   . HOH G 3 .   ? 12.344  -23.861 29.030  1.00 35.28 ? 610 HOH A O   1 
HETATM 4533 O  O   . HOH G 3 .   ? -10.507 -57.605 30.149  1.00 38.44 ? 611 HOH A O   1 
HETATM 4534 O  O   . HOH G 3 .   ? 23.033  -22.389 24.467  1.00 28.29 ? 612 HOH A O   1 
HETATM 4535 O  O   . HOH G 3 .   ? 17.831  -41.279 39.372  1.00 37.73 ? 613 HOH A O   1 
HETATM 4536 O  O   . HOH G 3 .   ? -11.768 -42.820 24.346  1.00 17.36 ? 614 HOH A O   1 
HETATM 4537 O  O   . HOH G 3 .   ? 13.486  -55.050 39.887  1.00 38.27 ? 615 HOH A O   1 
HETATM 4538 O  O   . HOH G 3 .   ? 16.909  -38.527 1.842   1.00 28.10 ? 616 HOH A O   1 
HETATM 4539 O  O   . HOH G 3 .   ? 32.259  -60.178 -0.731  1.00 32.00 ? 617 HOH A O   1 
HETATM 4540 O  O   . HOH G 3 .   ? -19.753 -41.880 15.584  1.00 47.35 ? 618 HOH A O   1 
HETATM 4541 O  O   . HOH G 3 .   ? 3.815   -27.166 1.795   1.00 43.11 ? 619 HOH A O   1 
HETATM 4542 O  O   . HOH G 3 .   ? 5.917   -55.812 16.753  1.00 27.04 ? 620 HOH A O   1 
HETATM 4543 O  O   . HOH G 3 .   ? -4.197  -35.942 5.613   1.00 47.45 ? 621 HOH A O   1 
HETATM 4544 O  O   . HOH G 3 .   ? 15.109  -34.943 11.509  1.00 23.30 ? 622 HOH A O   1 
HETATM 4545 O  O   . HOH G 3 .   ? 19.441  -23.230 0.022   1.00 23.43 ? 623 HOH A O   1 
HETATM 4546 O  O   . HOH G 3 .   ? -0.487  -39.696 36.915  1.00 28.44 ? 624 HOH A O   1 
HETATM 4547 O  O   . HOH G 3 .   ? 7.522   -61.044 20.743  1.00 30.93 ? 625 HOH A O   1 
HETATM 4548 O  O   . HOH G 3 .   ? -8.398  -44.312 27.151  1.00 24.85 ? 626 HOH A O   1 
HETATM 4549 O  O   . HOH G 3 .   ? 28.163  -41.551 28.109  1.00 44.47 ? 627 HOH A O   1 
HETATM 4550 O  O   . HOH G 3 .   ? 5.043   -30.405 31.633  1.00 38.23 ? 628 HOH A O   1 
HETATM 4551 O  O   . HOH G 3 .   ? -13.111 -38.835 22.634  1.00 27.32 ? 629 HOH A O   1 
HETATM 4552 O  O   . HOH G 3 .   ? 2.889   -20.948 19.515  1.00 35.93 ? 630 HOH A O   1 
HETATM 4553 O  O   . HOH G 3 .   ? 12.685  -60.297 15.470  1.00 31.85 ? 631 HOH A O   1 
HETATM 4554 O  O   . HOH G 3 .   ? 9.067   -45.456 17.534  1.00 17.00 ? 632 HOH A O   1 
HETATM 4555 O  O   . HOH G 3 .   ? 28.470  -44.185 26.534  1.00 20.98 ? 633 HOH A O   1 
HETATM 4556 O  O   . HOH G 3 .   ? 4.377   -23.347 10.600  1.00 33.63 ? 634 HOH A O   1 
HETATM 4557 O  O   . HOH G 3 .   ? 16.923  -37.096 -0.173  1.00 42.64 ? 635 HOH A O   1 
HETATM 4558 O  O   . HOH G 3 .   ? 22.361  -48.665 -6.366  1.00 46.57 ? 636 HOH A O   1 
HETATM 4559 O  O   . HOH G 3 .   ? 1.367   -31.872 34.317  1.00 34.12 ? 637 HOH A O   1 
HETATM 4560 O  O   . HOH G 3 .   ? 16.778  -37.415 8.282   1.00 24.85 ? 638 HOH A O   1 
HETATM 4561 O  O   . HOH G 3 .   ? 18.228  -21.503 26.763  1.00 33.13 ? 639 HOH A O   1 
HETATM 4562 O  O   . HOH G 3 .   ? 7.089   -35.486 38.140  1.00 33.33 ? 640 HOH A O   1 
HETATM 4563 O  O   . HOH G 3 .   ? 25.230  -57.270 16.946  1.00 36.56 ? 641 HOH A O   1 
HETATM 4564 O  O   . HOH G 3 .   ? 26.053  -39.780 28.731  1.00 45.88 ? 642 HOH A O   1 
HETATM 4565 O  O   . HOH G 3 .   ? 20.171  -53.117 10.151  1.00 25.77 ? 643 HOH A O   1 
HETATM 4566 O  O   . HOH G 3 .   ? 27.288  -60.436 -1.260  1.00 35.80 ? 644 HOH A O   1 
HETATM 4567 O  O   . HOH G 3 .   ? -3.764  -36.684 9.240   1.00 50.18 ? 645 HOH A O   1 
HETATM 4568 O  O   . HOH G 3 .   ? 24.445  -59.140 4.658   1.00 43.29 ? 646 HOH A O   1 
HETATM 4569 O  O   . HOH G 3 .   ? 21.037  -48.473 39.173  1.00 38.01 ? 647 HOH A O   1 
HETATM 4570 O  O   . HOH G 3 .   ? 23.397  -34.173 5.331   1.00 32.62 ? 648 HOH A O   1 
HETATM 4571 O  O   . HOH G 3 .   ? 12.734  -23.239 6.875   1.00 24.02 ? 649 HOH A O   1 
HETATM 4572 O  O   . HOH G 3 .   ? 9.274   -58.279 32.253  1.00 42.14 ? 650 HOH A O   1 
HETATM 4573 O  O   . HOH G 3 .   ? 18.265  -51.860 11.393  1.00 25.64 ? 651 HOH A O   1 
HETATM 4574 O  O   . HOH G 3 .   ? 25.729  -39.297 16.982  1.00 21.45 ? 652 HOH A O   1 
HETATM 4575 O  O   . HOH G 3 .   ? 37.076  -49.603 24.469  1.00 39.19 ? 653 HOH A O   1 
HETATM 4576 O  O   . HOH G 3 .   ? -2.225  -36.570 13.743  1.00 41.21 ? 654 HOH A O   1 
HETATM 4577 O  O   . HOH G 3 .   ? 31.572  -35.627 18.510  1.00 34.47 ? 655 HOH A O   1 
HETATM 4578 O  O   . HOH G 3 .   ? 12.526  -35.609 8.649   1.00 24.12 ? 656 HOH A O   1 
HETATM 4579 O  O   . HOH G 3 .   ? 6.234   -38.617 12.798  1.00 22.34 ? 657 HOH A O   1 
HETATM 4580 O  O   . HOH G 3 .   ? 14.067  -38.379 35.800  1.00 23.90 ? 658 HOH A O   1 
HETATM 4581 O  O   . HOH G 3 .   ? -4.143  -60.759 31.478  1.00 50.22 ? 659 HOH A O   1 
HETATM 4582 O  O   . HOH G 3 .   ? -8.449  -51.235 14.751  1.00 29.57 ? 660 HOH A O   1 
HETATM 4583 O  O   . HOH G 3 .   ? 7.829   -54.266 7.836   1.00 47.61 ? 661 HOH A O   1 
HETATM 4584 O  O   . HOH G 3 .   ? 13.823  -33.262 35.516  1.00 43.87 ? 662 HOH A O   1 
HETATM 4585 O  O   . HOH G 3 .   ? 8.558   -34.608 -1.713  1.00 40.65 ? 663 HOH A O   1 
HETATM 4586 O  O   . HOH G 3 .   ? -2.414  -34.327 36.220  1.00 47.24 ? 664 HOH A O   1 
HETATM 4587 O  O   . HOH G 3 .   ? 27.287  -40.985 31.871  1.00 34.83 ? 665 HOH A O   1 
HETATM 4588 O  O   . HOH G 3 .   ? 10.677  -45.074 2.128   1.00 30.91 ? 666 HOH A O   1 
HETATM 4589 O  O   . HOH G 3 .   ? 4.548   -38.038 40.435  1.00 24.70 ? 667 HOH A O   1 
HETATM 4590 O  O   . HOH G 3 .   ? 4.138   -24.469 -1.313  1.00 42.98 ? 668 HOH A O   1 
HETATM 4591 O  O   . HOH G 3 .   ? 16.799  -22.052 6.171   1.00 43.96 ? 669 HOH A O   1 
HETATM 4592 O  O   . HOH G 3 .   ? 9.517   -54.417 15.137  1.00 22.45 ? 670 HOH A O   1 
HETATM 4593 O  O   . HOH G 3 .   ? 25.303  -33.946 29.305  1.00 37.67 ? 671 HOH A O   1 
HETATM 4594 O  O   . HOH G 3 .   ? 23.982  -59.234 1.212   1.00 30.84 ? 672 HOH A O   1 
HETATM 4595 O  O   . HOH G 3 .   ? 8.502   -29.194 26.500  1.00 24.08 ? 673 HOH A O   1 
HETATM 4596 O  O   . HOH G 3 .   ? 20.129  -26.596 10.623  1.00 40.79 ? 674 HOH A O   1 
HETATM 4597 O  O   . HOH G 3 .   ? 18.258  -35.936 1.288   1.00 33.80 ? 675 HOH A O   1 
HETATM 4598 O  O   . HOH G 3 .   ? 2.024   -54.786 11.877  1.00 33.71 ? 676 HOH A O   1 
HETATM 4599 O  O   . HOH G 3 .   ? 13.117  -49.779 40.090  1.00 36.13 ? 677 HOH A O   1 
HETATM 4600 O  O   . HOH G 3 .   ? 1.447   -40.318 25.990  1.00 14.52 ? 678 HOH A O   1 
HETATM 4601 O  O   . HOH G 3 .   ? -5.733  -40.002 3.361   1.00 42.71 ? 679 HOH A O   1 
HETATM 4602 O  O   . HOH G 3 .   ? -8.003  -33.496 5.684   1.00 47.17 ? 680 HOH A O   1 
HETATM 4603 O  O   . HOH G 3 .   ? 21.097  -28.237 14.050  1.00 24.16 ? 681 HOH A O   1 
HETATM 4604 O  O   . HOH G 3 .   ? 10.980  -41.157 38.763  1.00 32.10 ? 682 HOH A O   1 
HETATM 4605 O  O   . HOH G 3 .   ? -3.780  -51.034 34.662  1.00 44.88 ? 683 HOH A O   1 
HETATM 4606 O  O   . HOH G 3 .   ? -11.428 -36.983 14.554  1.00 35.91 ? 684 HOH A O   1 
HETATM 4607 O  O   . HOH G 3 .   ? 1.879   -29.957 27.920  1.00 23.98 ? 685 HOH A O   1 
HETATM 4608 O  O   . HOH G 3 .   ? 13.435  -19.684 21.773  1.00 38.95 ? 686 HOH A O   1 
HETATM 4609 O  O   . HOH G 3 .   ? 25.326  -25.399 2.462   1.00 44.89 ? 687 HOH A O   1 
HETATM 4610 O  O   . HOH G 3 .   ? 13.499  -32.020 30.223  1.00 24.12 ? 688 HOH A O   1 
HETATM 4611 O  O   . HOH G 3 .   ? -14.307 -45.306 22.554  1.00 21.36 ? 689 HOH A O   1 
HETATM 4612 O  O   . HOH G 3 .   ? 6.799   -28.898 34.032  1.00 44.71 ? 690 HOH A O   1 
HETATM 4613 O  O   . HOH G 3 .   ? 19.299  -61.098 27.862  1.00 53.71 ? 691 HOH A O   1 
HETATM 4614 O  O   . HOH G 3 .   ? -6.170  -33.554 16.840  1.00 47.58 ? 692 HOH A O   1 
HETATM 4615 O  O   . HOH G 3 .   ? -3.558  -26.581 15.069  1.00 38.96 ? 693 HOH A O   1 
HETATM 4616 O  O   . HOH G 3 .   ? 21.123  -24.983 8.278   1.00 45.54 ? 694 HOH A O   1 
HETATM 4617 O  O   . HOH G 3 .   ? -0.672  -62.477 22.891  1.00 32.44 ? 695 HOH A O   1 
HETATM 4618 O  O   . HOH G 3 .   ? 29.442  -35.718 22.858  1.00 46.05 ? 696 HOH A O   1 
HETATM 4619 O  O   . HOH G 3 .   ? 19.466  -33.709 9.793   1.00 27.91 ? 697 HOH A O   1 
HETATM 4620 O  O   . HOH G 3 .   ? 22.589  -29.036 -1.423  1.00 42.49 ? 698 HOH A O   1 
HETATM 4621 O  O   . HOH G 3 .   ? -3.378  -30.593 27.684  1.00 39.11 ? 699 HOH A O   1 
HETATM 4622 O  O   . HOH G 3 .   ? -4.505  -27.541 23.840  1.00 49.10 ? 700 HOH A O   1 
HETATM 4623 O  O   . HOH G 3 .   ? 12.163  -39.924 21.930  1.00 20.51 ? 701 HOH A O   1 
HETATM 4624 O  O   . HOH G 3 .   ? 5.534   -25.665 31.608  1.00 48.97 ? 702 HOH A O   1 
HETATM 4625 O  O   . HOH G 3 .   ? 14.291  -18.527 12.963  1.00 42.02 ? 703 HOH A O   1 
HETATM 4626 O  O   . HOH G 3 .   ? -9.624  -41.101 2.097   1.00 33.02 ? 704 HOH A O   1 
HETATM 4627 O  O   . HOH G 3 .   ? -5.529  -52.267 31.089  1.00 24.85 ? 705 HOH A O   1 
HETATM 4628 O  O   . HOH G 3 .   ? 19.907  -21.125 14.170  1.00 42.92 ? 706 HOH A O   1 
HETATM 4629 O  O   . HOH G 3 .   ? -1.966  -52.145 34.689  1.00 50.12 ? 707 HOH A O   1 
HETATM 4630 O  O   . HOH G 3 .   ? 5.854   -31.367 38.069  1.00 44.24 ? 708 HOH A O   1 
HETATM 4631 O  O   . HOH G 3 .   ? 18.443  -61.859 26.122  1.00 45.90 ? 709 HOH A O   1 
HETATM 4632 O  O   . HOH G 3 .   ? -1.295  -61.492 27.983  1.00 36.39 ? 710 HOH A O   1 
HETATM 4633 O  O   . HOH G 3 .   ? 13.725  -24.274 -3.401  1.00 33.65 ? 711 HOH A O   1 
HETATM 4634 O  O   . HOH G 3 .   ? 4.542   -37.573 13.290  1.00 19.71 ? 712 HOH A O   1 
HETATM 4635 O  O   . HOH G 3 .   ? 23.314  -33.988 32.333  1.00 32.90 ? 713 HOH A O   1 
HETATM 4636 O  O   . HOH G 3 .   ? 25.327  -49.112 8.452   1.00 23.23 ? 714 HOH A O   1 
HETATM 4637 O  O   . HOH G 3 .   ? 9.085   -61.937 19.200  1.00 46.46 ? 715 HOH A O   1 
HETATM 4638 O  O   . HOH G 3 .   ? -9.790  -48.893 25.540  1.00 36.09 ? 716 HOH A O   1 
HETATM 4639 O  O   . HOH G 3 .   ? 13.002  -52.288 2.828   1.00 48.97 ? 717 HOH A O   1 
HETATM 4640 O  O   . HOH G 3 .   ? 8.517   -55.863 10.135  1.00 46.71 ? 718 HOH A O   1 
HETATM 4641 O  O   . HOH G 3 .   ? 6.682   -53.590 35.922  1.00 45.82 ? 719 HOH A O   1 
HETATM 4642 O  O   . HOH G 3 .   ? 30.823  -45.217 27.442  1.00 38.29 ? 720 HOH A O   1 
HETATM 4643 O  O   . HOH G 3 .   ? 8.183   -40.462 -0.536  1.00 48.74 ? 721 HOH A O   1 
HETATM 4644 O  O   . HOH G 3 .   ? 14.579  -23.285 30.435  1.00 38.66 ? 722 HOH A O   1 
HETATM 4645 O  O   . HOH G 3 .   ? -16.327 -37.391 8.862   1.00 46.35 ? 723 HOH A O   1 
HETATM 4646 O  O   . HOH G 3 .   ? 7.395   -55.856 12.157  1.00 41.54 ? 724 HOH A O   1 
HETATM 4647 O  O   . HOH G 3 .   ? 25.387  -37.383 29.816  1.00 43.41 ? 725 HOH A O   1 
HETATM 4648 O  O   . HOH G 3 .   ? 0.115   -42.310 37.941  1.00 33.66 ? 726 HOH A O   1 
HETATM 4649 O  O   . HOH G 3 .   ? -12.045 -49.430 19.857  1.00 46.56 ? 727 HOH A O   1 
HETATM 4650 O  O   . HOH G 3 .   ? 22.234  -21.819 13.689  1.00 46.64 ? 728 HOH A O   1 
HETATM 4651 O  O   . HOH G 3 .   ? 13.454  -45.778 2.982   1.00 37.50 ? 729 HOH A O   1 
HETATM 4652 O  O   . HOH G 3 .   ? 3.286   -28.492 29.799  1.00 49.11 ? 730 HOH A O   1 
HETATM 4653 O  O   . HOH G 3 .   ? 27.496  -41.590 17.228  1.00 45.58 ? 731 HOH A O   1 
HETATM 4654 O  O   . HOH G 3 .   ? 14.303  -21.809 5.180   1.00 40.19 ? 732 HOH A O   1 
HETATM 4655 O  O   . HOH G 3 .   ? 3.268   -28.289 -0.085  1.00 49.23 ? 733 HOH A O   1 
HETATM 4656 O  O   . HOH G 3 .   ? 15.426  -63.746 29.619  1.00 47.62 ? 734 HOH A O   1 
HETATM 4657 O  O   . HOH G 3 .   ? 13.575  -39.449 38.291  1.00 33.12 ? 735 HOH A O   1 
HETATM 4658 O  O   . HOH G 3 .   ? 32.836  -36.011 23.769  1.00 44.87 ? 736 HOH A O   1 
HETATM 4659 O  O   . HOH G 3 .   ? -2.984  -31.278 21.062  1.00 47.32 ? 737 HOH A O   1 
HETATM 4660 O  O   . HOH G 3 .   ? 10.412  -21.165 25.688  1.00 38.51 ? 738 HOH A O   1 
HETATM 4661 O  O   . HOH G 3 .   ? -4.624  -51.111 12.022  1.00 44.39 ? 739 HOH A O   1 
HETATM 4662 O  O   . HOH G 3 .   ? -7.693  -45.756 29.097  1.00 51.04 ? 740 HOH A O   1 
HETATM 4663 O  O   . HOH G 3 .   ? 6.280   -20.756 10.888  1.00 48.57 ? 741 HOH A O   1 
HETATM 4664 O  O   . HOH G 3 .   ? -0.822  -34.822 2.368   1.00 45.22 ? 742 HOH A O   1 
HETATM 4665 O  O   . HOH G 3 .   ? -5.468  -58.451 18.382  1.00 35.68 ? 743 HOH A O   1 
HETATM 4666 O  O   . HOH G 3 .   ? 10.510  -28.784 28.423  1.00 25.66 ? 744 HOH A O   1 
HETATM 4667 O  O   . HOH G 3 .   ? -11.750 -47.252 24.780  1.00 40.70 ? 745 HOH A O   1 
HETATM 4668 O  O   . HOH G 3 .   ? 2.608   -36.984 -1.060  1.00 50.54 ? 746 HOH A O   1 
HETATM 4669 O  O   . HOH G 3 .   ? -10.345 -37.130 24.075  1.00 34.77 ? 747 HOH A O   1 
HETATM 4670 O  O   . HOH G 3 .   ? 16.671  -50.775 8.514   1.00 25.14 ? 748 HOH A O   1 
HETATM 4671 O  O   . HOH G 3 .   ? 10.913  -41.717 41.628  1.00 39.18 ? 749 HOH A O   1 
HETATM 4672 O  O   . HOH G 3 .   ? -6.450  -36.309 31.915  1.00 25.38 ? 750 HOH A O   1 
HETATM 4673 O  O   . HOH G 3 .   ? -2.788  -29.882 22.996  1.00 35.60 ? 751 HOH A O   1 
HETATM 4674 O  O   . HOH G 3 .   ? -8.753  -53.223 16.545  1.00 45.48 ? 752 HOH A O   1 
HETATM 4675 O  O   . HOH G 3 .   ? 22.282  -23.972 0.094   1.00 29.47 ? 753 HOH A O   1 
HETATM 4676 O  O   . HOH G 3 .   ? 16.004  -25.181 -3.350  1.00 46.49 ? 754 HOH A O   1 
HETATM 4677 O  O   . HOH G 3 .   ? 20.543  -29.695 11.542  1.00 48.61 ? 755 HOH A O   1 
HETATM 4678 O  O   . HOH G 3 .   ? 13.010  -31.454 32.751  1.00 39.50 ? 756 HOH A O   1 
HETATM 4679 O  O   . HOH G 3 .   ? 13.236  -56.822 11.020  1.00 32.47 ? 757 HOH A O   1 
HETATM 4680 O  O   . HOH G 3 .   ? 10.847  -25.119 31.184  1.00 49.33 ? 758 HOH A O   1 
HETATM 4681 O  O   . HOH G 3 .   ? -6.227  -60.785 27.304  1.00 30.43 ? 759 HOH A O   1 
HETATM 4682 O  O   . HOH G 3 .   ? -19.527 -39.413 15.777  1.00 38.55 ? 760 HOH A O   1 
HETATM 4683 O  O   . HOH G 3 .   ? -11.040 -51.626 25.480  1.00 37.73 ? 761 HOH A O   1 
HETATM 4684 O  O   . HOH G 3 .   ? 21.081  -30.359 -2.185  1.00 53.59 ? 762 HOH A O   1 
HETATM 4685 O  O   . HOH G 3 .   ? -0.594  -31.479 31.993  1.00 42.09 ? 763 HOH A O   1 
HETATM 4686 O  O   . HOH G 3 .   ? 21.206  -21.101 26.650  1.00 38.43 ? 764 HOH A O   1 
HETATM 4687 O  O   . HOH G 3 .   ? 10.994  -58.907 14.157  1.00 30.66 ? 765 HOH A O   1 
HETATM 4688 O  O   . HOH G 3 .   ? -4.323  -33.376 13.053  1.00 49.74 ? 766 HOH A O   1 
HETATM 4689 O  O   . HOH G 3 .   ? 27.084  -47.872 17.270  1.00 46.77 ? 767 HOH A O   1 
HETATM 4690 O  O   . HOH G 3 .   ? 8.519   -20.560 -2.120  1.00 45.75 ? 768 HOH A O   1 
HETATM 4691 O  O   . HOH G 3 .   ? 5.967   -55.025 6.721   1.00 49.78 ? 769 HOH A O   1 
HETATM 4692 O  O   . HOH G 3 .   ? 8.061   -46.571 2.097   1.00 41.37 ? 770 HOH A O   1 
HETATM 4693 O  O   . HOH G 3 .   ? 15.185  -35.236 8.928   1.00 35.43 ? 771 HOH A O   1 
HETATM 4694 O  O   . HOH G 3 .   ? -14.344 -48.105 16.761  1.00 45.25 ? 772 HOH A O   1 
HETATM 4695 O  O   . HOH G 3 .   ? -5.670  -60.908 33.546  1.00 44.25 ? 773 HOH A O   1 
HETATM 4696 O  O   . HOH G 3 .   ? -8.777  -35.916 27.650  1.00 31.14 ? 774 HOH A O   1 
HETATM 4697 O  O   . HOH G 3 .   ? 20.373  -55.559 10.691  1.00 44.76 ? 775 HOH A O   1 
HETATM 4698 O  O   . HOH G 3 .   ? 0.203   -29.522 29.818  1.00 42.90 ? 776 HOH A O   1 
HETATM 4699 O  O   . HOH G 3 .   ? 18.880  -58.846 13.079  1.00 46.05 ? 777 HOH A O   1 
HETATM 4700 O  O   . HOH G 3 .   ? 14.565  -18.994 25.829  1.00 40.06 ? 778 HOH A O   1 
HETATM 4701 O  O   . HOH G 3 .   ? 9.144   -29.829 35.077  1.00 38.45 ? 779 HOH A O   1 
HETATM 4702 O  O   . HOH G 3 .   ? -6.680  -59.004 22.452  1.00 42.66 ? 780 HOH A O   1 
HETATM 4703 O  O   . HOH G 3 .   ? 11.974  -31.123 27.887  1.00 21.90 ? 781 HOH A O   1 
HETATM 4704 O  O   . HOH G 3 .   ? -1.588  -27.691 25.275  1.00 43.34 ? 782 HOH A O   1 
HETATM 4705 O  O   . HOH G 3 .   ? 24.935  -32.222 12.814  1.00 31.22 ? 783 HOH A O   1 
HETATM 4706 O  O   . HOH G 3 .   ? -10.826 -44.925 25.800  1.00 22.83 ? 784 HOH A O   1 
HETATM 4707 O  O   . HOH G 3 .   ? 27.018  -39.514 26.442  1.00 59.71 ? 785 HOH A O   1 
HETATM 4708 O  O   . HOH G 3 .   ? 15.458  -20.578 29.574  1.00 42.48 ? 786 HOH A O   1 
HETATM 4709 O  O   . HOH G 3 .   ? 7.669   -56.537 14.880  1.00 26.09 ? 787 HOH A O   1 
HETATM 4710 O  O   . HOH G 3 .   ? 13.297  -21.662 -4.238  1.00 27.86 ? 788 HOH A O   1 
HETATM 4711 O  O   . HOH G 3 .   ? 18.255  -23.479 -2.228  1.00 36.24 ? 789 HOH A O   1 
HETATM 4712 O  O   . HOH G 3 .   ? 5.574   -64.100 22.599  1.00 47.08 ? 790 HOH A O   1 
HETATM 4713 O  O   . HOH G 3 .   ? 5.431   -35.637 41.473  1.00 43.69 ? 791 HOH A O   1 
HETATM 4714 O  O   . HOH G 3 .   ? 24.667  -59.448 23.327  1.00 39.11 ? 792 HOH A O   1 
HETATM 4715 O  O   . HOH G 3 .   ? 15.137  -20.755 9.276   1.00 44.06 ? 793 HOH A O   1 
HETATM 4716 O  O   . HOH G 3 .   ? 6.951   -28.114 31.251  1.00 41.73 ? 794 HOH A O   1 
HETATM 4717 O  O   . HOH G 3 .   ? 23.107  -25.330 -2.265  1.00 43.40 ? 795 HOH A O   1 
HETATM 4718 O  O   . HOH G 3 .   ? -4.840  -30.791 20.979  1.00 40.74 ? 796 HOH A O   1 
HETATM 4719 O  O   . HOH G 3 .   ? -7.461  -52.650 12.066  1.00 48.01 ? 797 HOH A O   1 
HETATM 4720 O  O   . HOH G 3 .   ? 10.963  -24.573 33.898  1.00 45.69 ? 798 HOH A O   1 
HETATM 4721 O  O   . HOH G 3 .   ? 9.463   -32.671 35.863  1.00 36.11 ? 799 HOH A O   1 
HETATM 4722 O  O   . HOH G 3 .   ? 7.124   -19.786 23.077  1.00 42.92 ? 800 HOH A O   1 
HETATM 4723 O  O   . HOH G 3 .   ? -1.100  -54.614 14.125  1.00 40.48 ? 801 HOH A O   1 
HETATM 4724 O  O   . HOH G 3 .   ? 11.234  -21.529 28.173  1.00 35.66 ? 802 HOH A O   1 
HETATM 4725 O  O   . HOH G 3 .   ? 23.766  -37.200 12.960  1.00 31.44 ? 803 HOH A O   1 
HETATM 4726 O  O   . HOH G 3 .   ? 28.265  -40.591 25.447  1.00 45.57 ? 804 HOH A O   1 
HETATM 4727 O  O   . HOH G 3 .   ? -10.623 -49.894 14.820  1.00 50.43 ? 805 HOH A O   1 
HETATM 4728 O  O   . HOH G 3 .   ? 29.843  -42.770 30.999  1.00 47.24 ? 806 HOH A O   1 
HETATM 4729 O  O   . HOH G 3 .   ? 11.020  -29.181 32.969  1.00 42.11 ? 807 HOH A O   1 
HETATM 4730 O  O   . HOH G 3 .   ? 12.054  -25.883 -4.659  1.00 48.83 ? 808 HOH A O   1 
HETATM 4731 O  O   . HOH G 3 .   ? 5.506   -36.882 11.438  1.00 38.06 ? 809 HOH A O   1 
HETATM 4732 O  O   . HOH G 3 .   ? 18.803  -52.487 7.845   1.00 40.67 ? 810 HOH A O   1 
HETATM 4733 O  O   . HOH G 3 .   ? -6.908  -55.331 15.299  1.00 45.25 ? 811 HOH A O   1 
HETATM 4734 O  O   . HOH G 3 .   ? 24.959  -45.482 13.288  1.00 41.36 ? 812 HOH A O   1 
HETATM 4735 O  O   . HOH G 3 .   ? 0.517   -23.512 24.780  1.00 40.61 ? 813 HOH A O   1 
HETATM 4736 O  O   . HOH G 3 .   ? 26.269  -24.606 25.828  1.00 41.04 ? 814 HOH A O   1 
HETATM 4737 O  O   . HOH G 3 .   ? 15.361  -61.241 14.602  1.00 42.55 ? 815 HOH A O   1 
HETATM 4738 O  O   . HOH G 3 .   ? -0.152  -52.564 36.187  1.00 49.08 ? 816 HOH A O   1 
HETATM 4739 O  O   . HOH G 3 .   ? 11.711  -33.236 34.610  1.00 42.76 ? 817 HOH A O   1 
HETATM 4740 O  O   . HOH G 3 .   ? -6.742  -31.541 24.873  1.00 40.98 ? 818 HOH A O   1 
HETATM 4741 O  O   . HOH G 3 .   ? 24.958  -45.434 15.330  1.00 49.17 ? 819 HOH A O   1 
HETATM 4742 O  O   . HOH G 3 .   ? 26.331  -61.049 1.032   1.00 40.52 ? 820 HOH A O   1 
HETATM 4743 O  O   . HOH G 3 .   ? -14.203 -47.528 25.945  1.00 42.75 ? 821 HOH A O   1 
HETATM 4744 O  O   . HOH G 3 .   ? 22.094  -35.277 13.554  1.00 37.67 ? 822 HOH A O   1 
HETATM 4745 O  O   . HOH G 3 .   ? 9.959   -27.906 30.844  1.00 34.86 ? 823 HOH A O   1 
HETATM 4746 O  O   . HOH G 3 .   ? 5.601   -22.192 -4.205  1.00 49.54 ? 824 HOH A O   1 
HETATM 4747 O  O   . HOH G 3 .   ? 6.480   -35.363 9.591   1.00 35.71 ? 825 HOH A O   1 
HETATM 4748 O  O   . HOH G 3 .   ? -4.327  -37.012 11.970  1.00 47.80 ? 826 HOH A O   1 
HETATM 4749 O  O   . HOH G 3 .   ? 20.462  -33.417 12.473  1.00 32.85 ? 827 HOH A O   1 
HETATM 4750 O  O   . HOH G 3 .   ? 8.463   -59.243 14.694  1.00 36.71 ? 828 HOH A O   1 
HETATM 4751 O  O   . HOH G 3 .   ? -12.337 -50.212 12.852  1.00 53.20 ? 829 HOH A O   1 
HETATM 4752 O  O   . HOH G 3 .   ? -6.176  -36.801 13.891  1.00 46.90 ? 830 HOH A O   1 
HETATM 4753 O  O   . HOH G 3 .   ? -3.152  -53.449 12.448  1.00 42.63 ? 831 HOH A O   1 
HETATM 4754 O  O   . HOH G 3 .   ? 1.916   -21.391 26.281  1.00 44.85 ? 832 HOH A O   1 
HETATM 4755 O  O   . HOH G 3 .   ? -5.210  -54.952 12.484  1.00 47.11 ? 833 HOH A O   1 
HETATM 4756 O  O   . HOH G 3 .   ? -7.669  -35.638 14.073  1.00 51.07 ? 834 HOH A O   1 
HETATM 4757 O  O   . HOH G 3 .   ? 32.527  -55.279 34.192  1.00 46.21 ? 835 HOH A O   1 
HETATM 4758 O  O   . HOH G 3 .   ? 13.217  -19.643 28.541  1.00 41.73 ? 836 HOH A O   1 
HETATM 4759 O  O   . HOH G 3 .   ? 34.077  -54.003 34.492  1.00 50.03 ? 837 HOH A O   1 
HETATM 4760 O  O   . HOH G 3 .   ? -2.812  -54.103 10.052  1.00 44.70 ? 838 HOH A O   1 
HETATM 4761 O  O   . HOH H 3 .   ? 46.933  -30.757 -1.793  1.00 45.15 ? 501 HOH B O   1 
HETATM 4762 O  O   . HOH H 3 .   ? 47.381  -27.714 -4.716  1.00 50.42 ? 502 HOH B O   1 
HETATM 4763 O  O   . HOH H 3 .   ? 26.528  -55.710 21.375  1.00 43.49 ? 503 HOH B O   1 
HETATM 4764 O  O   . HOH H 3 .   ? 38.966  -52.511 -11.575 1.00 47.59 ? 504 HOH B O   1 
HETATM 4765 O  O   . HOH H 3 .   ? 38.315  -31.285 -6.657  1.00 47.34 ? 505 HOH B O   1 
HETATM 4766 O  O   . HOH H 3 .   ? 16.319  -53.417 4.926   1.00 41.96 ? 506 HOH B O   1 
HETATM 4767 O  O   . HOH H 3 .   ? 15.690  -61.246 33.033  1.00 48.76 ? 507 HOH B O   1 
HETATM 4768 O  O   . HOH H 3 .   ? 34.678  -31.417 -7.480  1.00 44.48 ? 508 HOH B O   1 
HETATM 4769 O  O   . HOH H 3 .   ? 50.040  -27.758 23.162  1.00 48.84 ? 509 HOH B O   1 
HETATM 4770 O  O   . HOH H 3 .   ? 52.948  -63.168 0.706   1.00 29.21 ? 510 HOH B O   1 
HETATM 4771 O  O   . HOH H 3 .   ? 37.724  -57.636 -5.633  1.00 28.47 ? 511 HOH B O   1 
HETATM 4772 O  O   . HOH H 3 .   ? 31.801  -57.115 -7.257  1.00 36.28 ? 512 HOH B O   1 
HETATM 4773 O  O   . HOH H 3 .   ? 33.118  -56.095 15.854  1.00 36.48 ? 513 HOH B O   1 
HETATM 4774 O  O   . HOH H 3 .   ? 29.744  -61.143 2.079   1.00 50.64 ? 514 HOH B O   1 
HETATM 4775 O  O   . HOH H 3 .   ? 44.187  -48.077 23.609  1.00 28.04 ? 515 HOH B O   1 
HETATM 4776 O  O   . HOH H 3 .   ? 48.847  -24.982 -2.788  1.00 48.26 ? 516 HOH B O   1 
HETATM 4777 O  O   . HOH H 3 .   ? 41.559  -37.703 11.022  1.00 17.67 ? 517 HOH B O   1 
HETATM 4778 O  O   . HOH H 3 .   ? 45.851  -26.750 23.253  1.00 25.36 ? 518 HOH B O   1 
HETATM 4779 O  O   . HOH H 3 .   ? 49.402  -64.405 13.713  1.00 52.59 ? 519 HOH B O   1 
HETATM 4780 O  O   . HOH H 3 .   ? 44.104  -33.759 28.434  1.00 40.11 ? 520 HOH B O   1 
HETATM 4781 O  O   . HOH H 3 .   ? 63.390  -50.473 7.255   1.00 37.30 ? 521 HOH B O   1 
HETATM 4782 O  O   . HOH H 3 .   ? 35.988  -41.550 11.507  1.00 15.88 ? 522 HOH B O   1 
HETATM 4783 O  O   . HOH H 3 .   ? 37.315  -49.236 21.687  1.00 25.06 ? 523 HOH B O   1 
HETATM 4784 O  O   . HOH H 3 .   ? 32.513  -25.614 12.762  1.00 33.98 ? 524 HOH B O   1 
HETATM 4785 O  O   . HOH H 3 .   ? 61.810  -51.346 3.807   1.00 51.24 ? 525 HOH B O   1 
HETATM 4786 O  O   . HOH H 3 .   ? 44.863  -19.819 15.273  1.00 48.99 ? 526 HOH B O   1 
HETATM 4787 O  O   . HOH H 3 .   ? 51.050  -38.328 -2.318  1.00 26.75 ? 527 HOH B O   1 
HETATM 4788 O  O   . HOH H 3 .   ? 56.998  -33.765 2.217   1.00 27.63 ? 528 HOH B O   1 
HETATM 4789 O  O   . HOH H 3 .   ? 36.665  -21.674 1.187   1.00 28.26 ? 529 HOH B O   1 
HETATM 4790 O  O   . HOH H 3 .   ? 31.004  -50.411 -10.258 1.00 45.57 ? 530 HOH B O   1 
HETATM 4791 O  O   . HOH H 3 .   ? 20.318  -53.239 5.376   1.00 24.71 ? 531 HOH B O   1 
HETATM 4792 O  O   . HOH H 3 .   ? 57.204  -61.158 4.205   1.00 31.72 ? 532 HOH B O   1 
HETATM 4793 O  O   . HOH H 3 .   ? 36.165  -45.431 15.084  1.00 23.37 ? 533 HOH B O   1 
HETATM 4794 O  O   . HOH H 3 .   ? 42.964  -28.125 29.789  1.00 45.95 ? 534 HOH B O   1 
HETATM 4795 O  O   . HOH H 3 .   ? 51.627  -54.015 12.642  1.00 23.96 ? 535 HOH B O   1 
HETATM 4796 O  O   . HOH H 3 .   ? 46.850  -30.798 12.758  1.00 26.27 ? 536 HOH B O   1 
HETATM 4797 O  O   . HOH H 3 .   ? 41.529  -43.246 7.119   1.00 25.07 ? 537 HOH B O   1 
HETATM 4798 O  O   . HOH H 3 .   ? 36.064  -53.061 23.074  1.00 52.22 ? 538 HOH B O   1 
HETATM 4799 O  O   . HOH H 3 .   ? 24.948  -42.248 4.766   1.00 25.88 ? 539 HOH B O   1 
HETATM 4800 O  O   . HOH H 3 .   ? 38.586  -31.826 -0.185  1.00 21.35 ? 540 HOH B O   1 
HETATM 4801 O  O   . HOH H 3 .   ? 43.371  -33.394 0.545   1.00 19.86 ? 541 HOH B O   1 
HETATM 4802 O  O   . HOH H 3 .   ? 21.439  -51.000 -3.390  1.00 35.84 ? 542 HOH B O   1 
HETATM 4803 O  O   . HOH H 3 .   ? 37.898  -50.540 -9.721  1.00 37.25 ? 543 HOH B O   1 
HETATM 4804 O  O   . HOH H 3 .   ? 47.957  -41.090 13.070  1.00 16.28 ? 544 HOH B O   1 
HETATM 4805 O  O   . HOH H 3 .   ? 32.765  -51.465 1.260   1.00 19.76 ? 545 HOH B O   1 
HETATM 4806 O  O   . HOH H 3 .   ? 48.699  -64.176 6.081   1.00 45.04 ? 546 HOH B O   1 
HETATM 4807 O  O   . HOH H 3 .   ? 43.557  -52.509 13.334  1.00 17.56 ? 547 HOH B O   1 
HETATM 4808 O  O   . HOH H 3 .   ? 60.071  -52.658 14.210  1.00 33.60 ? 548 HOH B O   1 
HETATM 4809 O  O   . HOH H 3 .   ? 38.209  -57.789 -10.878 1.00 49.58 ? 549 HOH B O   1 
HETATM 4810 O  O   . HOH H 3 .   ? 28.155  -42.984 14.962  1.00 30.08 ? 550 HOH B O   1 
HETATM 4811 O  O   . HOH H 3 .   ? 29.724  -40.034 15.680  1.00 48.05 ? 551 HOH B O   1 
HETATM 4812 O  O   . HOH H 3 .   ? 40.089  -60.179 -6.297  1.00 46.78 ? 552 HOH B O   1 
HETATM 4813 O  O   . HOH H 3 .   ? 49.098  -33.212 5.774   1.00 26.37 ? 553 HOH B O   1 
HETATM 4814 O  O   . HOH H 3 .   ? 29.499  -26.527 0.684   1.00 26.46 ? 554 HOH B O   1 
HETATM 4815 O  O   . HOH H 3 .   ? 27.959  -59.862 10.195  1.00 43.58 ? 555 HOH B O   1 
HETATM 4816 O  O   . HOH H 3 .   ? 24.086  -47.721 6.579   1.00 19.46 ? 556 HOH B O   1 
HETATM 4817 O  O   . HOH H 3 .   ? 33.854  -60.131 13.495  1.00 30.28 ? 557 HOH B O   1 
HETATM 4818 O  O   . HOH H 3 .   ? 56.579  -57.447 11.815  1.00 35.04 ? 558 HOH B O   1 
HETATM 4819 O  O   . HOH H 3 .   ? 56.346  -38.313 -3.937  1.00 27.72 ? 559 HOH B O   1 
HETATM 4820 O  O   . HOH H 3 .   ? 45.619  -38.383 -10.661 1.00 35.54 ? 560 HOH B O   1 
HETATM 4821 O  O   . HOH H 3 .   ? 33.642  -26.528 19.168  1.00 26.27 ? 561 HOH B O   1 
HETATM 4822 O  O   . HOH H 3 .   ? 26.442  -41.032 -1.543  1.00 44.92 ? 562 HOH B O   1 
HETATM 4823 O  O   . HOH H 3 .   ? 29.582  -39.008 10.005  1.00 15.81 ? 563 HOH B O   1 
HETATM 4824 O  O   . HOH H 3 .   ? 35.822  -26.593 14.809  1.00 25.76 ? 564 HOH B O   1 
HETATM 4825 O  O   . HOH H 3 .   ? 64.645  -44.464 3.196   1.00 27.15 ? 565 HOH B O   1 
HETATM 4826 O  O   . HOH H 3 .   ? 45.948  -56.765 12.020  1.00 27.15 ? 566 HOH B O   1 
HETATM 4827 O  O   . HOH H 3 .   ? 30.826  -30.614 1.033   1.00 19.28 ? 567 HOH B O   1 
HETATM 4828 O  O   . HOH H 3 .   ? 45.854  -57.427 -5.541  1.00 35.62 ? 568 HOH B O   1 
HETATM 4829 O  O   . HOH H 3 .   ? 41.925  -60.935 -2.887  1.00 45.46 ? 569 HOH B O   1 
HETATM 4830 O  O   . HOH H 3 .   ? 31.241  -46.066 -11.427 1.00 23.16 ? 570 HOH B O   1 
HETATM 4831 O  O   . HOH H 3 .   ? 39.818  -65.008 6.993   1.00 54.00 ? 571 HOH B O   1 
HETATM 4832 O  O   . HOH H 3 .   ? 46.908  -49.361 -7.849  1.00 24.67 ? 572 HOH B O   1 
HETATM 4833 O  O   . HOH H 3 .   ? 26.755  -29.508 11.349  1.00 32.71 ? 573 HOH B O   1 
HETATM 4834 O  O   . HOH H 3 .   ? 30.811  -49.632 31.704  1.00 43.06 ? 574 HOH B O   1 
HETATM 4835 O  O   . HOH H 3 .   ? 46.183  -50.764 19.578  1.00 24.08 ? 575 HOH B O   1 
HETATM 4836 O  O   . HOH H 3 .   ? 34.573  -40.653 18.660  1.00 15.90 ? 576 HOH B O   1 
HETATM 4837 O  O   . HOH H 3 .   ? 27.180  -48.092 12.101  1.00 42.59 ? 577 HOH B O   1 
HETATM 4838 O  O   . HOH H 3 .   ? 34.295  -49.156 17.688  1.00 20.60 ? 578 HOH B O   1 
HETATM 4839 O  O   . HOH H 3 .   ? 39.869  -56.984 15.368  1.00 22.38 ? 579 HOH B O   1 
HETATM 4840 O  O   . HOH H 3 .   ? 52.042  -30.150 1.104   1.00 29.04 ? 580 HOH B O   1 
HETATM 4841 O  O   . HOH H 3 .   ? 41.777  -44.272 -10.846 1.00 34.40 ? 581 HOH B O   1 
HETATM 4842 O  O   . HOH H 3 .   ? 54.479  -57.881 13.557  1.00 38.58 ? 582 HOH B O   1 
HETATM 4843 O  O   . HOH H 3 .   ? 54.398  -29.373 14.003  1.00 46.02 ? 583 HOH B O   1 
HETATM 4844 O  O   . HOH H 3 .   ? 17.495  -46.259 2.255   1.00 39.05 ? 584 HOH B O   1 
HETATM 4845 O  O   . HOH H 3 .   ? 46.605  -32.636 10.852  1.00 25.37 ? 585 HOH B O   1 
HETATM 4846 O  O   . HOH H 3 .   ? 25.961  -34.452 5.116   1.00 25.43 ? 586 HOH B O   1 
HETATM 4847 O  O   . HOH H 3 .   ? 20.126  -55.848 35.770  1.00 48.42 ? 587 HOH B O   1 
HETATM 4848 O  O   . HOH H 3 .   ? 26.018  -31.521 -2.715  1.00 39.98 ? 588 HOH B O   1 
HETATM 4849 O  O   . HOH H 3 .   ? 35.703  -42.607 -11.361 1.00 39.80 ? 589 HOH B O   1 
HETATM 4850 O  O   . HOH H 3 .   ? 23.129  -55.670 34.901  1.00 45.99 ? 590 HOH B O   1 
HETATM 4851 O  O   . HOH H 3 .   ? 44.303  -59.685 1.157   1.00 19.08 ? 591 HOH B O   1 
HETATM 4852 O  O   . HOH H 3 .   ? 45.665  -23.361 1.326   1.00 32.54 ? 592 HOH B O   1 
HETATM 4853 O  O   . HOH H 3 .   ? 50.423  -64.045 1.428   1.00 28.28 ? 593 HOH B O   1 
HETATM 4854 O  O   . HOH H 3 .   ? 29.410  -30.297 13.129  1.00 41.18 ? 594 HOH B O   1 
HETATM 4855 O  O   . HOH H 3 .   ? 47.969  -32.658 -4.550  1.00 32.47 ? 595 HOH B O   1 
HETATM 4856 O  O   . HOH H 3 .   ? 36.617  -38.826 16.777  1.00 15.81 ? 596 HOH B O   1 
HETATM 4857 O  O   . HOH H 3 .   ? 31.835  -52.887 18.230  1.00 26.41 ? 597 HOH B O   1 
HETATM 4858 O  O   . HOH H 3 .   ? 56.021  -48.113 -7.850  1.00 34.24 ? 598 HOH B O   1 
HETATM 4859 O  O   . HOH H 3 .   ? 48.813  -24.182 27.288  1.00 38.72 ? 599 HOH B O   1 
HETATM 4860 O  O   . HOH H 3 .   ? 27.643  -57.631 6.999   1.00 26.90 ? 600 HOH B O   1 
HETATM 4861 O  O   . HOH H 3 .   ? 48.872  -46.406 -10.575 1.00 39.53 ? 601 HOH B O   1 
HETATM 4862 O  O   . HOH H 3 .   ? 64.485  -38.916 12.669  1.00 36.98 ? 602 HOH B O   1 
HETATM 4863 O  O   . HOH H 3 .   ? 30.188  -27.557 27.488  1.00 42.56 ? 603 HOH B O   1 
HETATM 4864 O  O   . HOH H 3 .   ? 43.962  -54.408 20.766  1.00 43.13 ? 604 HOH B O   1 
HETATM 4865 O  O   . HOH H 3 .   ? 52.261  -46.290 -10.096 1.00 38.83 ? 605 HOH B O   1 
HETATM 4866 O  O   . HOH H 3 .   ? 18.057  -40.642 8.927   1.00 18.93 ? 606 HOH B O   1 
HETATM 4867 O  O   . HOH H 3 .   ? 28.375  -20.690 2.933   1.00 53.14 ? 607 HOH B O   1 
HETATM 4868 O  O   . HOH H 3 .   ? 53.951  -46.296 13.015  1.00 23.68 ? 608 HOH B O   1 
HETATM 4869 O  O   . HOH H 3 .   ? 30.802  -37.688 12.144  1.00 22.97 ? 609 HOH B O   1 
HETATM 4870 O  O   . HOH H 3 .   ? 38.764  -40.674 -8.263  1.00 23.01 ? 610 HOH B O   1 
HETATM 4871 O  O   . HOH H 3 .   ? 47.712  -21.505 5.762   1.00 48.96 ? 611 HOH B O   1 
HETATM 4872 O  O   . HOH H 3 .   ? 23.539  -55.933 -3.982  1.00 36.39 ? 612 HOH B O   1 
HETATM 4873 O  O   . HOH H 3 .   ? 45.123  -37.222 -8.248  1.00 31.68 ? 613 HOH B O   1 
HETATM 4874 O  O   . HOH H 3 .   ? 57.300  -59.854 11.023  1.00 40.70 ? 614 HOH B O   1 
HETATM 4875 O  O   . HOH H 3 .   ? 35.722  -36.234 27.070  1.00 42.69 ? 615 HOH B O   1 
HETATM 4876 O  O   . HOH H 3 .   ? 52.408  -37.301 -9.774  1.00 37.02 ? 616 HOH B O   1 
HETATM 4877 O  O   . HOH H 3 .   ? 35.886  -19.892 5.460   1.00 37.62 ? 617 HOH B O   1 
HETATM 4878 O  O   . HOH H 3 .   ? 34.967  -45.701 25.454  1.00 37.68 ? 618 HOH B O   1 
HETATM 4879 O  O   . HOH H 3 .   ? 40.451  -55.893 19.516  1.00 46.97 ? 619 HOH B O   1 
HETATM 4880 O  O   . HOH H 3 .   ? 36.080  -32.676 18.420  1.00 24.22 ? 620 HOH B O   1 
HETATM 4881 O  O   . HOH H 3 .   ? 32.303  -62.267 7.078   1.00 36.58 ? 621 HOH B O   1 
HETATM 4882 O  O   . HOH H 3 .   ? 38.565  -23.540 17.099  1.00 24.74 ? 622 HOH B O   1 
HETATM 4883 O  O   . HOH H 3 .   ? 24.000  -44.938 1.264   1.00 18.04 ? 623 HOH B O   1 
HETATM 4884 O  O   . HOH H 3 .   ? 26.865  -39.481 10.427  1.00 19.54 ? 624 HOH B O   1 
HETATM 4885 O  O   . HOH H 3 .   ? 24.011  -44.785 -5.296  1.00 34.85 ? 625 HOH B O   1 
HETATM 4886 O  O   . HOH H 3 .   ? 43.250  -46.300 10.539  1.00 15.76 ? 626 HOH B O   1 
HETATM 4887 O  O   . HOH H 3 .   ? 25.465  -42.194 -4.403  1.00 29.19 ? 627 HOH B O   1 
HETATM 4888 O  O   . HOH H 3 .   ? 40.940  -25.674 -2.794  1.00 29.98 ? 628 HOH B O   1 
HETATM 4889 O  O   . HOH H 3 .   ? 37.549  -35.117 15.560  1.00 20.51 ? 629 HOH B O   1 
HETATM 4890 O  O   . HOH H 3 .   ? 67.036  -47.874 6.016   1.00 44.13 ? 630 HOH B O   1 
HETATM 4891 O  O   . HOH H 3 .   ? 49.440  -57.856 15.239  1.00 40.30 ? 631 HOH B O   1 
HETATM 4892 O  O   . HOH H 3 .   ? 32.713  -57.448 -11.253 1.00 48.82 ? 632 HOH B O   1 
HETATM 4893 O  O   . HOH H 3 .   ? 44.762  -55.305 -7.487  1.00 39.84 ? 633 HOH B O   1 
HETATM 4894 O  O   . HOH H 3 .   ? 38.666  -60.118 -3.953  1.00 45.27 ? 634 HOH B O   1 
HETATM 4895 O  O   . HOH H 3 .   ? 39.338  -20.558 4.023   1.00 48.49 ? 635 HOH B O   1 
HETATM 4896 O  O   . HOH H 3 .   ? 29.655  -33.416 21.156  1.00 39.61 ? 636 HOH B O   1 
HETATM 4897 O  O   . HOH H 3 .   ? 48.739  -23.967 15.668  1.00 36.59 ? 637 HOH B O   1 
HETATM 4898 O  O   . HOH H 3 .   ? 36.173  -28.338 27.589  1.00 26.87 ? 638 HOH B O   1 
HETATM 4899 O  O   . HOH H 3 .   ? 39.353  -33.796 -3.310  1.00 25.29 ? 639 HOH B O   1 
HETATM 4900 O  O   . HOH H 3 .   ? 54.443  -48.301 17.448  1.00 35.24 ? 640 HOH B O   1 
HETATM 4901 O  O   . HOH H 3 .   ? 61.381  -40.303 25.176  1.00 43.51 ? 641 HOH B O   1 
HETATM 4902 O  O   . HOH H 3 .   ? 35.868  -37.264 19.004  1.00 21.22 ? 642 HOH B O   1 
HETATM 4903 O  O   . HOH H 3 .   ? 33.382  -21.924 25.306  1.00 26.42 ? 643 HOH B O   1 
HETATM 4904 O  O   . HOH H 3 .   ? 41.427  -44.651 25.754  1.00 41.25 ? 644 HOH B O   1 
HETATM 4905 O  O   . HOH H 3 .   ? 44.548  -30.834 0.356   1.00 22.55 ? 645 HOH B O   1 
HETATM 4906 O  O   . HOH H 3 .   ? 29.318  -36.832 -2.679  1.00 31.50 ? 646 HOH B O   1 
HETATM 4907 O  O   . HOH H 3 .   ? 35.244  -56.164 -5.757  1.00 25.84 ? 647 HOH B O   1 
HETATM 4908 O  O   . HOH H 3 .   ? 44.069  -62.078 8.624   1.00 27.03 ? 648 HOH B O   1 
HETATM 4909 O  O   . HOH H 3 .   ? 24.280  -44.969 4.076   1.00 18.80 ? 649 HOH B O   1 
HETATM 4910 O  O   . HOH H 3 .   ? 39.666  -19.358 26.689  1.00 30.97 ? 650 HOH B O   1 
HETATM 4911 O  O   . HOH H 3 .   ? 53.195  -42.284 -9.180  1.00 26.91 ? 651 HOH B O   1 
HETATM 4912 O  O   . HOH H 3 .   ? 40.074  -20.688 7.032   1.00 42.53 ? 652 HOH B O   1 
HETATM 4913 O  O   . HOH H 3 .   ? 45.290  -20.532 17.907  1.00 50.74 ? 653 HOH B O   1 
HETATM 4914 O  O   . HOH H 3 .   ? 64.494  -38.830 5.563   1.00 46.67 ? 654 HOH B O   1 
HETATM 4915 O  O   . HOH H 3 .   ? 34.141  -34.998 26.009  1.00 35.05 ? 655 HOH B O   1 
HETATM 4916 O  O   . HOH H 3 .   ? 14.956  -50.088 3.872   1.00 37.73 ? 656 HOH B O   1 
HETATM 4917 O  O   . HOH H 3 .   ? 40.365  -23.296 19.414  1.00 29.00 ? 657 HOH B O   1 
HETATM 4918 O  O   . HOH H 3 .   ? 33.848  -51.851 17.085  1.00 24.70 ? 658 HOH B O   1 
HETATM 4919 O  O   . HOH H 3 .   ? 60.740  -38.563 2.439   1.00 28.09 ? 659 HOH B O   1 
HETATM 4920 O  O   . HOH H 3 .   ? 35.428  -37.721 25.291  1.00 32.20 ? 660 HOH B O   1 
HETATM 4921 O  O   . HOH H 3 .   ? 24.846  -41.248 -9.442  1.00 43.86 ? 661 HOH B O   1 
HETATM 4922 O  O   . HOH H 3 .   ? 55.172  -44.348 19.918  1.00 29.64 ? 662 HOH B O   1 
HETATM 4923 O  O   . HOH H 3 .   ? 27.071  -58.490 24.134  1.00 43.26 ? 663 HOH B O   1 
HETATM 4924 O  O   . HOH H 3 .   ? 51.247  -32.073 -0.893  1.00 24.85 ? 664 HOH B O   1 
HETATM 4925 O  O   . HOH H 3 .   ? 46.446  -31.338 -6.984  1.00 47.17 ? 665 HOH B O   1 
HETATM 4926 O  O   . HOH H 3 .   ? 40.459  -40.976 5.685   1.00 20.68 ? 666 HOH B O   1 
HETATM 4927 O  O   . HOH H 3 .   ? 21.424  -46.032 0.756   1.00 30.38 ? 667 HOH B O   1 
HETATM 4928 O  O   . HOH H 3 .   ? 49.823  -55.545 17.093  1.00 30.30 ? 668 HOH B O   1 
HETATM 4929 O  O   . HOH H 3 .   ? 31.860  -28.303 12.400  1.00 25.73 ? 669 HOH B O   1 
HETATM 4930 O  O   . HOH H 3 .   ? 26.627  -57.442 11.697  1.00 35.31 ? 670 HOH B O   1 
HETATM 4931 O  O   . HOH H 3 .   ? 36.260  -23.978 17.934  1.00 38.48 ? 671 HOH B O   1 
HETATM 4932 O  O   . HOH H 3 .   ? 36.033  -21.456 19.533  1.00 45.42 ? 672 HOH B O   1 
HETATM 4933 O  O   . HOH H 3 .   ? 42.391  -55.052 13.529  1.00 20.30 ? 673 HOH B O   1 
HETATM 4934 O  O   . HOH H 3 .   ? 52.314  -64.610 14.862  1.00 45.61 ? 674 HOH B O   1 
HETATM 4935 O  O   . HOH H 3 .   ? 27.540  -58.553 27.563  1.00 37.28 ? 675 HOH B O   1 
HETATM 4936 O  O   . HOH H 3 .   ? 40.155  -35.630 18.536  1.00 25.86 ? 676 HOH B O   1 
HETATM 4937 O  O   . HOH H 3 .   ? 39.026  -60.970 13.705  1.00 37.91 ? 677 HOH B O   1 
HETATM 4938 O  O   . HOH H 3 .   ? 27.764  -47.803 36.206  1.00 41.36 ? 678 HOH B O   1 
HETATM 4939 O  O   . HOH H 3 .   ? 51.194  -42.222 1.749   1.00 20.52 ? 679 HOH B O   1 
HETATM 4940 O  O   . HOH H 3 .   ? 20.212  -49.083 -0.822  1.00 27.88 ? 680 HOH B O   1 
HETATM 4941 O  O   . HOH H 3 .   ? 30.153  -23.500 1.338   1.00 26.75 ? 681 HOH B O   1 
HETATM 4942 O  O   . HOH H 3 .   ? 29.695  -35.561 -5.571  1.00 47.08 ? 682 HOH B O   1 
HETATM 4943 O  O   . HOH H 3 .   ? 23.282  -39.156 11.141  1.00 36.14 ? 683 HOH B O   1 
HETATM 4944 O  O   . HOH H 3 .   ? 57.499  -54.858 -2.427  1.00 25.84 ? 684 HOH B O   1 
HETATM 4945 O  O   . HOH H 3 .   ? 46.499  -39.267 14.827  1.00 21.94 ? 685 HOH B O   1 
HETATM 4946 O  O   . HOH H 3 .   ? 27.113  -35.683 -2.099  1.00 42.40 ? 686 HOH B O   1 
HETATM 4947 O  O   . HOH H 3 .   ? 66.447  -35.756 21.937  1.00 47.02 ? 687 HOH B O   1 
HETATM 4948 O  O   . HOH H 3 .   ? 32.858  -26.585 15.491  1.00 46.63 ? 688 HOH B O   1 
HETATM 4949 O  O   . HOH H 3 .   ? 49.672  -22.681 11.242  1.00 50.28 ? 689 HOH B O   1 
HETATM 4950 O  O   . HOH H 3 .   ? 35.245  -22.660 -0.629  1.00 34.71 ? 690 HOH B O   1 
HETATM 4951 O  O   . HOH H 3 .   ? 51.569  -40.154 -11.377 1.00 42.40 ? 691 HOH B O   1 
HETATM 4952 O  O   . HOH H 3 .   ? 27.224  -38.534 -2.553  1.00 39.31 ? 692 HOH B O   1 
HETATM 4953 O  O   . HOH H 3 .   ? 26.850  -48.815 19.622  1.00 24.31 ? 693 HOH B O   1 
HETATM 4954 O  O   . HOH H 3 .   ? 40.768  -22.101 3.997   1.00 40.66 ? 694 HOH B O   1 
HETATM 4955 O  O   . HOH H 3 .   ? 48.120  -38.393 14.158  1.00 22.11 ? 695 HOH B O   1 
HETATM 4956 O  O   . HOH H 3 .   ? 51.665  -34.259 -7.094  1.00 38.58 ? 696 HOH B O   1 
HETATM 4957 O  O   . HOH H 3 .   ? 64.295  -55.394 7.628   1.00 50.05 ? 697 HOH B O   1 
HETATM 4958 O  O   . HOH H 3 .   ? 39.552  -58.497 -8.090  1.00 41.02 ? 698 HOH B O   1 
HETATM 4959 O  O   . HOH H 3 .   ? 52.274  -64.106 6.155   1.00 35.27 ? 699 HOH B O   1 
HETATM 4960 O  O   . HOH H 3 .   ? 56.581  -27.819 11.779  1.00 44.82 ? 700 HOH B O   1 
HETATM 4961 O  O   . HOH H 3 .   ? 33.311  -33.609 17.096  1.00 34.30 ? 701 HOH B O   1 
HETATM 4962 O  O   . HOH H 3 .   ? 58.568  -39.599 24.060  1.00 38.87 ? 702 HOH B O   1 
HETATM 4963 O  O   . HOH H 3 .   ? 19.868  -59.060 28.855  1.00 46.41 ? 703 HOH B O   1 
HETATM 4964 O  O   . HOH H 3 .   ? 56.051  -53.217 -6.499  1.00 45.90 ? 704 HOH B O   1 
HETATM 4965 O  O   . HOH H 3 .   ? 51.805  -28.735 21.390  1.00 48.20 ? 705 HOH B O   1 
HETATM 4966 O  O   . HOH H 3 .   ? 48.603  -51.905 -8.466  1.00 40.70 ? 706 HOH B O   1 
HETATM 4967 O  O   . HOH H 3 .   ? 58.471  -35.995 11.653  1.00 46.52 ? 707 HOH B O   1 
HETATM 4968 O  O   . HOH H 3 .   ? 56.954  -61.361 8.932   1.00 41.27 ? 708 HOH B O   1 
HETATM 4969 O  O   . HOH H 3 .   ? 38.623  -21.292 21.046  1.00 38.94 ? 709 HOH B O   1 
HETATM 4970 O  O   . HOH H 3 .   ? 27.696  -24.758 23.810  1.00 33.71 ? 710 HOH B O   1 
HETATM 4971 O  O   . HOH H 3 .   ? 24.996  -50.589 36.697  1.00 43.04 ? 711 HOH B O   1 
HETATM 4972 O  O   . HOH H 3 .   ? 43.115  -25.675 29.893  1.00 50.43 ? 712 HOH B O   1 
HETATM 4973 O  O   . HOH H 3 .   ? 67.611  -40.833 5.421   1.00 43.09 ? 713 HOH B O   1 
HETATM 4974 O  O   . HOH H 3 .   ? 46.188  -63.417 9.021   1.00 45.95 ? 714 HOH B O   1 
HETATM 4975 O  O   . HOH H 3 .   ? 55.235  -35.276 -4.281  1.00 41.02 ? 715 HOH B O   1 
HETATM 4976 O  O   . HOH H 3 .   ? 16.487  -57.518 36.675  1.00 35.78 ? 716 HOH B O   1 
HETATM 4977 O  O   . HOH H 3 .   ? 38.777  -51.741 25.642  1.00 48.61 ? 717 HOH B O   1 
HETATM 4978 O  O   . HOH H 3 .   ? 35.507  -50.660 19.851  1.00 32.96 ? 718 HOH B O   1 
HETATM 4979 O  O   . HOH H 3 .   ? 60.536  -63.145 0.897   1.00 44.85 ? 719 HOH B O   1 
HETATM 4980 O  O   . HOH H 3 .   ? 26.479  -53.843 34.208  1.00 51.78 ? 720 HOH B O   1 
HETATM 4981 O  O   . HOH H 3 .   ? 59.207  -38.239 -4.429  1.00 37.28 ? 721 HOH B O   1 
HETATM 4982 O  O   . HOH H 3 .   ? 28.042  -34.220 -4.603  1.00 49.79 ? 722 HOH B O   1 
HETATM 4983 O  O   . HOH H 3 .   ? 62.245  -38.942 -0.064  1.00 40.26 ? 723 HOH B O   1 
HETATM 4984 O  O   . HOH H 3 .   ? 42.427  -30.441 -1.673  1.00 28.31 ? 724 HOH B O   1 
HETATM 4985 O  O   . HOH H 3 .   ? 37.093  -62.265 -3.446  1.00 39.51 ? 725 HOH B O   1 
HETATM 4986 O  O   . HOH H 3 .   ? 44.562  -36.966 -12.345 1.00 53.34 ? 726 HOH B O   1 
HETATM 4987 O  O   . HOH H 3 .   ? 72.222  -47.101 10.214  1.00 43.42 ? 727 HOH B O   1 
HETATM 4988 O  O   . HOH H 3 .   ? 46.065  -54.555 22.306  1.00 49.10 ? 728 HOH B O   1 
HETATM 4989 O  O   . HOH H 3 .   ? 42.984  -22.651 0.465   1.00 39.44 ? 729 HOH B O   1 
HETATM 4990 O  O   . HOH H 3 .   ? 25.104  -41.669 10.373  1.00 41.66 ? 730 HOH B O   1 
HETATM 4991 O  O   . HOH H 3 .   ? 30.559  -22.778 25.187  1.00 35.96 ? 731 HOH B O   1 
HETATM 4992 O  O   . HOH H 3 .   ? 50.191  -31.913 -5.811  1.00 50.79 ? 732 HOH B O   1 
HETATM 4993 O  O   . HOH H 3 .   ? 63.403  -39.443 4.021   1.00 44.35 ? 733 HOH B O   1 
HETATM 4994 O  O   . HOH H 3 .   ? 38.840  -24.720 -4.142  1.00 41.68 ? 734 HOH B O   1 
HETATM 4995 O  O   . HOH H 3 .   ? 39.502  -19.876 29.335  1.00 45.02 ? 735 HOH B O   1 
HETATM 4996 O  O   . HOH H 3 .   ? 55.705  -31.806 4.080   1.00 38.39 ? 736 HOH B O   1 
HETATM 4997 O  O   . HOH H 3 .   ? 31.942  -61.547 12.210  1.00 34.90 ? 737 HOH B O   1 
HETATM 4998 O  O   . HOH H 3 .   ? 53.878  -46.875 18.738  1.00 49.57 ? 738 HOH B O   1 
HETATM 4999 O  O   . HOH H 3 .   ? 38.572  -57.023 17.772  1.00 29.79 ? 739 HOH B O   1 
HETATM 5000 O  O   . HOH H 3 .   ? 39.730  -63.425 -2.970  1.00 43.50 ? 740 HOH B O   1 
HETATM 5001 O  O   . HOH H 3 .   ? 23.294  -52.894 36.442  1.00 44.18 ? 741 HOH B O   1 
HETATM 5002 O  O   . HOH H 3 .   ? 34.131  -22.174 27.843  1.00 38.17 ? 742 HOH B O   1 
HETATM 5003 O  O   . HOH H 3 .   ? 35.942  -65.458 -0.964  1.00 49.51 ? 743 HOH B O   1 
HETATM 5004 O  O   . HOH H 3 .   ? 55.566  -50.217 18.370  1.00 41.17 ? 744 HOH B O   1 
HETATM 5005 O  O   . HOH H 3 .   ? 53.785  -34.175 -4.932  1.00 53.77 ? 745 HOH B O   1 
HETATM 5006 O  O   . HOH H 3 .   ? 63.401  -46.967 2.857   1.00 42.08 ? 746 HOH B O   1 
HETATM 5007 O  O   . HOH H 3 .   ? 32.431  -22.310 -0.498  1.00 43.66 ? 747 HOH B O   1 
HETATM 5008 O  O   . HOH H 3 .   ? 40.660  -59.334 15.050  1.00 27.41 ? 748 HOH B O   1 
HETATM 5009 O  O   . HOH H 3 .   ? 56.156  -52.409 16.712  1.00 36.92 ? 749 HOH B O   1 
HETATM 5010 O  O   . HOH H 3 .   ? 35.719  -19.651 2.443   1.00 41.61 ? 750 HOH B O   1 
HETATM 5011 O  O   . HOH H 3 .   ? 35.319  -65.152 1.524   1.00 44.57 ? 751 HOH B O   1 
HETATM 5012 O  O   . HOH H 3 .   ? 42.296  -27.081 -4.629  1.00 47.56 ? 752 HOH B O   1 
HETATM 5013 O  O   . HOH H 3 .   ? 37.541  -35.202 18.209  1.00 25.99 ? 753 HOH B O   1 
HETATM 5014 O  O   . HOH H 3 .   ? 24.951  -48.234 11.184  1.00 46.50 ? 754 HOH B O   1 
HETATM 5015 O  O   . HOH H 3 .   ? 57.997  -63.114 2.248   1.00 27.73 ? 755 HOH B O   1 
HETATM 5016 O  O   . HOH H 3 .   ? 53.081  -32.079 -3.224  1.00 48.97 ? 756 HOH B O   1 
HETATM 5017 O  O   . HOH H 3 .   ? 45.817  -30.377 -4.212  1.00 37.48 ? 757 HOH B O   1 
HETATM 5018 O  O   . HOH H 3 .   ? 39.588  -65.120 -1.118  1.00 41.48 ? 758 HOH B O   1 
HETATM 5019 O  O   . HOH H 3 .   ? 39.992  -33.479 -6.061  1.00 36.34 ? 759 HOH B O   1 
HETATM 5020 O  O   . HOH H 3 .   ? 60.066  -46.480 28.227  1.00 47.35 ? 760 HOH B O   1 
HETATM 5021 O  O   . HOH H 3 .   ? 44.378  -18.625 25.132  1.00 34.72 ? 761 HOH B O   1 
HETATM 5022 O  O   . HOH H 3 .   ? 41.009  -32.849 -1.007  1.00 22.51 ? 762 HOH B O   1 
HETATM 5023 O  O   . HOH H 3 .   ? 32.243  -58.675 15.669  1.00 43.71 ? 763 HOH B O   1 
HETATM 5024 O  O   . HOH H 3 .   ? 30.213  -23.826 27.937  1.00 43.02 ? 764 HOH B O   1 
HETATM 5025 O  O   . HOH H 3 .   ? 41.565  -21.099 1.892   1.00 45.59 ? 765 HOH B O   1 
HETATM 5026 O  O   . HOH H 3 .   ? 28.447  -54.848 32.567  1.00 45.01 ? 766 HOH B O   1 
HETATM 5027 O  O   . HOH H 3 .   ? 27.479  -31.982 13.893  1.00 26.44 ? 767 HOH B O   1 
HETATM 5028 O  O   . HOH H 3 .   ? 24.072  -58.358 11.346  1.00 46.31 ? 768 HOH B O   1 
HETATM 5029 O  O   . HOH H 3 .   ? 54.788  -29.794 1.393   1.00 35.07 ? 769 HOH B O   1 
HETATM 5030 O  O   . HOH H 3 .   ? 59.915  -53.563 16.504  1.00 48.86 ? 770 HOH B O   1 
HETATM 5031 O  O   . HOH H 3 .   ? 41.224  -35.815 -7.360  1.00 43.50 ? 771 HOH B O   1 
HETATM 5032 O  O   . HOH H 3 .   ? 44.104  -57.150 13.964  1.00 26.07 ? 772 HOH B O   1 
HETATM 5033 O  O   . HOH H 3 .   ? 38.889  -20.334 -0.200  1.00 39.57 ? 773 HOH B O   1 
HETATM 5034 O  O   . HOH H 3 .   ? 41.834  -31.356 -6.382  1.00 39.51 ? 774 HOH B O   1 
HETATM 5035 O  O   . HOH H 3 .   ? 32.504  -48.502 -12.037 1.00 37.18 ? 775 HOH B O   1 
HETATM 5036 O  O   . HOH H 3 .   ? 44.178  -31.416 -8.053  1.00 48.70 ? 776 HOH B O   1 
HETATM 5037 O  O   . HOH H 3 .   ? 53.132  -55.275 14.234  1.00 33.94 ? 777 HOH B O   1 
HETATM 5038 O  O   . HOH H 3 .   ? 25.603  -40.299 1.138   1.00 40.60 ? 778 HOH B O   1 
HETATM 5039 O  O   . HOH H 3 .   ? 67.718  -50.005 5.916   1.00 48.13 ? 779 HOH B O   1 
HETATM 5040 O  O   . HOH H 3 .   ? 30.608  -62.523 -0.610  1.00 41.20 ? 780 HOH B O   1 
HETATM 5041 O  O   . HOH H 3 .   ? 32.081  -30.911 13.857  1.00 36.50 ? 781 HOH B O   1 
HETATM 5042 O  O   . HOH H 3 .   ? 33.280  -52.185 20.716  1.00 38.36 ? 782 HOH B O   1 
HETATM 5043 O  O   . HOH H 3 .   ? 58.380  -61.128 6.706   1.00 40.77 ? 783 HOH B O   1 
HETATM 5044 O  O   . HOH H 3 .   ? 46.407  -21.109 3.070   1.00 42.37 ? 784 HOH B O   1 
HETATM 5045 O  O   . HOH H 3 .   ? 56.965  -50.377 -7.600  1.00 40.58 ? 785 HOH B O   1 
HETATM 5046 O  O   . HOH H 3 .   ? 26.975  -60.072 5.377   1.00 36.71 ? 786 HOH B O   1 
HETATM 5047 O  O   . HOH H 3 .   ? 24.154  -41.510 1.586   1.00 47.08 ? 787 HOH B O   1 
HETATM 5048 O  O   . HOH H 3 .   ? 27.498  -45.246 12.925  1.00 46.96 ? 788 HOH B O   1 
HETATM 5049 O  O   . HOH H 3 .   ? 28.897  -36.998 14.115  1.00 33.21 ? 789 HOH B O   1 
HETATM 5050 O  O   . HOH H 3 .   ? 42.281  -23.178 -1.881  1.00 39.78 ? 790 HOH B O   1 
HETATM 5051 O  O   . HOH H 3 .   ? 59.168  -56.622 13.140  1.00 50.23 ? 791 HOH B O   1 
HETATM 5052 O  O   . HOH H 3 .   ? 36.224  -61.705 14.341  1.00 45.62 ? 792 HOH B O   1 
HETATM 5053 O  O   . HOH H 3 .   ? 43.502  -35.176 -8.669  1.00 37.08 ? 793 HOH B O   1 
HETATM 5054 O  O   . HOH H 3 .   ? 27.564  -45.536 15.000  1.00 37.66 ? 794 HOH B O   1 
HETATM 5055 O  O   . HOH H 3 .   ? 47.121  -37.422 16.065  1.00 33.34 ? 795 HOH B O   1 
HETATM 5056 O  O   . HOH H 3 .   ? 36.183  -64.005 14.346  1.00 47.55 ? 796 HOH B O   1 
HETATM 5057 O  O   . HOH H 3 .   ? 54.949  -63.156 5.164   1.00 45.59 ? 797 HOH B O   1 
HETATM 5058 O  O   . HOH H 3 .   ? 26.808  -25.413 0.531   1.00 36.86 ? 798 HOH B O   1 
HETATM 5059 O  O   . HOH H 3 .   ? 26.395  -37.863 13.445  1.00 39.88 ? 799 HOH B O   1 
HETATM 5060 O  O   . HOH H 3 .   ? 57.080  -37.687 15.227  1.00 48.10 ? 800 HOH B O   1 
HETATM 5061 O  O   . HOH H 3 .   ? 43.329  -29.912 -4.122  1.00 38.54 ? 801 HOH B O   1 
HETATM 5062 O  O   . HOH H 3 .   ? 58.986  -38.498 13.405  1.00 47.00 ? 802 HOH B O   1 
HETATM 5063 O  O   . HOH H 3 .   ? 45.872  -35.954 17.450  1.00 30.02 ? 803 HOH B O   1 
HETATM 5064 O  O   . HOH H 3 .   ? 43.232  -59.926 14.328  1.00 43.08 ? 804 HOH B O   1 
HETATM 5065 O  O   . HOH H 3 .   ? 32.073  -33.210 14.214  1.00 38.17 ? 805 HOH B O   1 
HETATM 5066 O  O   . HOH H 3 .   ? 54.943  -54.777 16.342  1.00 36.42 ? 806 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   . ALA A 1   ? 0.3501 0.3922 0.5172 0.0538  0.0324  -0.2323 36  ALA A N   
2    C CA  . ALA A 1   ? 0.3316 0.3679 0.4780 0.0544  0.0316  -0.2175 36  ALA A CA  
3    C C   . ALA A 1   ? 0.4507 0.4738 0.6144 0.0510  0.0276  -0.2100 36  ALA A C   
4    O O   . ALA A 1   ? 0.3456 0.3694 0.5245 0.0480  0.0236  -0.2180 36  ALA A O   
5    C CB  . ALA A 1   ? 0.4365 0.4861 0.5493 0.0564  0.0300  -0.2193 36  ALA A CB  
6    N N   . ALA A 2   ? 0.3271 0.3394 0.4893 0.0516  0.0289  -0.1947 37  ALA A N   
7    C CA  . ALA A 2   ? 0.2918 0.2918 0.4691 0.0489  0.0255  -0.1854 37  ALA A CA  
8    C C   . ALA A 2   ? 0.3036 0.3075 0.4629 0.0471  0.0206  -0.1876 37  ALA A C   
9    O O   . ALA A 2   ? 0.3216 0.3326 0.4511 0.0489  0.0210  -0.1851 37  ALA A O   
10   C CB  . ALA A 2   ? 0.3444 0.3358 0.5209 0.0506  0.0278  -0.1687 37  ALA A CB  
11   N N   . PRO A 3   ? 0.2831 0.2837 0.4604 0.0435  0.0166  -0.1917 38  PRO A N   
12   C CA  . PRO A 3   ? 0.2812 0.2864 0.4429 0.0418  0.0116  -0.1936 38  PRO A CA  
13   C C   . PRO A 3   ? 0.2997 0.2961 0.4466 0.0421  0.0111  -0.1783 38  PRO A C   
14   O O   . PRO A 3   ? 0.2954 0.2805 0.4529 0.0410  0.0127  -0.1627 38  PRO A O   
15   C CB  . PRO A 3   ? 0.3269 0.3282 0.5187 0.0373  0.0088  -0.1993 38  PRO A CB  
16   C CG  . PRO A 3   ? 0.3854 0.3806 0.6078 0.0368  0.0128  -0.2007 38  PRO A CG  
17   C CD  . PRO A 3   ? 0.3317 0.3281 0.5439 0.0409  0.0172  -0.1979 38  PRO A CD  
18   N N   . GLN A 4   ? 0.2760 0.2803 0.3960 0.0425  0.0084  -0.1782 39  GLN A N   
19   C CA  . GLN A 4   ? 0.2720 0.2700 0.3766 0.0395  0.0068  -0.1573 39  GLN A CA  
20   C C   . GLN A 4   ? 0.3808 0.3687 0.5074 0.0350  0.0029  -0.1525 39  GLN A C   
21   O O   . GLN A 4   ? 0.3199 0.3082 0.4679 0.0340  0.0008  -0.1673 39  GLN A O   
22   C CB  . GLN A 4   ? 0.2764 0.2856 0.3481 0.0415  0.0057  -0.1563 39  GLN A CB  
23   C CG  . GLN A 4   ? 0.2872 0.3061 0.3368 0.0464  0.0111  -0.1582 39  GLN A CG  
24   C CD  . GLN A 4   ? 0.3614 0.3902 0.3795 0.0492  0.0115  -0.1530 39  GLN A CD  
25   O OE1 . GLN A 4   ? 0.3939 0.4255 0.4067 0.0484  0.0067  -0.1527 39  GLN A OE1 
26   N NE2 . GLN A 4   ? 0.3167 0.3511 0.3150 0.0530  0.0180  -0.1484 39  GLN A NE2 
27   N N   . VAL A 5   ? 0.3025 0.2818 0.4250 0.0321  0.0027  -0.1322 40  VAL A N   
28   C CA  . VAL A 5   ? 0.3237 0.2936 0.4653 0.0280  0.0001  -0.1240 40  VAL A CA  
29   C C   . VAL A 5   ? 0.2636 0.2364 0.3877 0.0255  -0.0038 -0.1202 40  VAL A C   
30   O O   . VAL A 5   ? 0.3207 0.2928 0.4588 0.0233  -0.0070 -0.1276 40  VAL A O   
31   C CB  . VAL A 5   ? 0.3136 0.2744 0.4649 0.0271  0.0024  -0.1042 40  VAL A CB  
32   C CG1 . VAL A 5   ? 0.3283 0.2804 0.4986 0.0237  0.0007  -0.0940 40  VAL A CG1 
33   C CG2 . VAL A 5   ? 0.2611 0.2198 0.4326 0.0304  0.0062  -0.1080 40  VAL A CG2 
34   N N   . ARG A 6   ? 0.2749 0.2513 0.3702 0.0259  -0.0031 -0.1094 41  ARG A N   
35   C CA  . ARG A 6   ? 0.3016 0.2823 0.3775 0.0248  -0.0059 -0.1062 41  ARG A CA  
36   C C   . ARG A 6   ? 0.3877 0.3606 0.4768 0.0201  -0.0088 -0.0974 41  ARG A C   
37   O O   . ARG A 6   ? 0.3456 0.3222 0.4350 0.0190  -0.0125 -0.1034 41  ARG A O   
38   C CB  . ARG A 6   ? 0.3075 0.3013 0.3739 0.0283  -0.0085 -0.1238 41  ARG A CB  
39   C CG  . ARG A 6   ? 0.3297 0.3331 0.3763 0.0336  -0.0049 -0.1291 41  ARG A CG  
40   C CD  . ARG A 6   ? 0.4062 0.4252 0.4320 0.0379  -0.0072 -0.1378 41  ARG A CD  
41   N NE  . ARG A 6   ? 0.6094 0.6390 0.6167 0.0438  -0.0028 -0.1426 41  ARG A NE  
42   C CZ  . ARG A 6   ? 0.6131 0.6564 0.5949 0.0494  -0.0020 -0.1427 41  ARG A CZ  
43   N NH1 . ARG A 6   ? 0.4620 0.5110 0.4340 0.0501  -0.0060 -0.1394 41  ARG A NH1 
44   N NH2 . ARG A 6   ? 0.3794 0.4317 0.3459 0.0549  0.0035  -0.1453 41  ARG A NH2 
45   N N   . THR A 7   ? 0.2894 0.2534 0.3896 0.0177  -0.0070 -0.0829 42  THR A N   
46   C CA  . THR A 7   ? 0.2485 0.2065 0.3565 0.0137  -0.0085 -0.0708 42  THR A CA  
47   C C   . THR A 7   ? 0.3594 0.3159 0.4533 0.0122  -0.0062 -0.0526 42  THR A C   
48   O O   . THR A 7   ? 0.2939 0.2517 0.3846 0.0139  -0.0035 -0.0486 42  THR A O   
49   C CB  . THR A 7   ? 0.3270 0.2769 0.4691 0.0123  -0.0082 -0.0713 42  THR A CB  
50   O OG1 . THR A 7   ? 0.4109 0.3572 0.5658 0.0146  -0.0049 -0.0663 42  THR A OG1 
51   C CG2 . THR A 7   ? 0.3456 0.2980 0.5041 0.0124  -0.0103 -0.0920 42  THR A CG2 
52   N N   . SER A 8   ? 0.2861 0.2417 0.3724 0.0090  -0.0074 -0.0431 43  SER A N   
53   C CA  . SER A 8   ? 0.2421 0.1984 0.3155 0.0071  -0.0053 -0.0281 43  SER A CA  
54   C C   . SER A 8   ? 0.2488 0.2020 0.3411 0.0061  -0.0047 -0.0156 43  SER A C   
55   O O   . SER A 8   ? 0.2931 0.2410 0.4085 0.0062  -0.0055 -0.0160 43  SER A O   
56   C CB  . SER A 8   ? 0.2824 0.2401 0.3395 0.0044  -0.0060 -0.0236 43  SER A CB  
57   O OG  . SER A 8   ? 0.2908 0.2529 0.3280 0.0065  -0.0053 -0.0311 43  SER A OG  
58   N N   . ALA A 9   ? 0.2271 0.1848 0.3102 0.0055  -0.0029 -0.0045 44  ALA A N   
59   C CA  . ALA A 9   ? 0.2952 0.2541 0.3922 0.0057  -0.0025 0.0095  44  ALA A CA  
60   C C   . ALA A 9   ? 0.2832 0.2395 0.3849 0.0027  -0.0034 0.0179  44  ALA A C   
61   O O   . ALA A 9   ? 0.2736 0.2290 0.3629 -0.0001 -0.0044 0.0142  44  ALA A O   
62   C CB  . ALA A 9   ? 0.2619 0.2306 0.3447 0.0052  -0.0010 0.0173  44  ALA A CB  
63   N N   . PRO A 10  ? 0.2702 0.2258 0.3903 0.0038  -0.0026 0.0303  45  PRO A N   
64   C CA  . PRO A 10  ? 0.2947 0.2489 0.4191 0.0011  -0.0024 0.0402  45  PRO A CA  
65   C C   . PRO A 10  ? 0.3183 0.2802 0.4180 -0.0025 -0.0026 0.0444  45  PRO A C   
66   O O   . PRO A 10  ? 0.2575 0.2285 0.3432 -0.0023 -0.0021 0.0475  45  PRO A O   
67   C CB  . PRO A 10  ? 0.3451 0.3011 0.4892 0.0044  -0.0002 0.0562  45  PRO A CB  
68   C CG  . PRO A 10  ? 0.4090 0.3625 0.5676 0.0089  0.0005  0.0510  45  PRO A CG  
69   C CD  . PRO A 10  ? 0.3402 0.2969 0.4787 0.0083  -0.0011 0.0371  45  PRO A CD  
70   N N   . GLY A 11  ? 0.2972 0.2557 0.3933 -0.0058 -0.0032 0.0431  46  GLY A N   
71   C CA  . GLY A 11  ? 0.2345 0.1984 0.3084 -0.0092 -0.0028 0.0440  46  GLY A CA  
72   C C   . GLY A 11  ? 0.2781 0.2499 0.3501 -0.0109 -0.0013 0.0584  46  GLY A C   
73   O O   . GLY A 11  ? 0.2523 0.2231 0.3236 -0.0137 -0.0007 0.0620  46  GLY A O   
74   N N   . TYR A 12  ? 0.2361 0.2177 0.3077 -0.0088 -0.0006 0.0667  47  TYR A N   
75   C CA  . TYR A 12  ? 0.2389 0.2332 0.3040 -0.0100 0.0007  0.0789  47  TYR A CA  
76   C C   . TYR A 12  ? 0.3392 0.3473 0.3907 -0.0100 0.0008  0.0774  47  TYR A C   
77   O O   . TYR A 12  ? 0.2817 0.2903 0.3359 -0.0073 0.0001  0.0727  47  TYR A O   
78   C CB  . TYR A 12  ? 0.2223 0.2192 0.3055 -0.0068 0.0017  0.0948  47  TYR A CB  
79   C CG  . TYR A 12  ? 0.2420 0.2414 0.3403 -0.0008 0.0016  0.1009  47  TYR A CG  
80   C CD1 . TYR A 12  ? 0.2466 0.2321 0.3644 0.0017  0.0018  0.0956  47  TYR A CD1 
81   C CD2 . TYR A 12  ? 0.2145 0.2317 0.3090 0.0026  0.0015  0.1118  47  TYR A CD2 
82   C CE1 . TYR A 12  ? 0.2531 0.2403 0.3870 0.0075  0.0024  0.1015  47  TYR A CE1 
83   C CE2 . TYR A 12  ? 0.1963 0.2168 0.3058 0.0089  0.0015  0.1187  47  TYR A CE2 
84   C CZ  . TYR A 12  ? 0.2561 0.2604 0.3856 0.0114  0.0023  0.1140  47  TYR A CZ  
85   O OH  . TYR A 12  ? 0.2952 0.3024 0.4413 0.0181  0.0030  0.1211  47  TYR A OH  
86   N N   . TYR A 13  ? 0.2264 0.2466 0.2644 -0.0133 0.0020  0.0801  48  TYR A N   
87   C CA  . TYR A 13  ? 0.2003 0.2362 0.2267 -0.0144 0.0026  0.0767  48  TYR A CA  
88   C C   . TYR A 13  ? 0.2114 0.2674 0.2353 -0.0143 0.0026  0.0878  48  TYR A C   
89   O O   . TYR A 13  ? 0.2320 0.2905 0.2497 -0.0175 0.0042  0.0904  48  TYR A O   
90   C CB  . TYR A 13  ? 0.2191 0.2513 0.2305 -0.0196 0.0053  0.0640  48  TYR A CB  
91   C CG  . TYR A 13  ? 0.3166 0.3641 0.3198 -0.0216 0.0070  0.0582  48  TYR A CG  
92   C CD1 . TYR A 13  ? 0.4193 0.4666 0.4244 -0.0198 0.0071  0.0517  48  TYR A CD1 
93   C CD2 . TYR A 13  ? 0.2089 0.2724 0.2039 -0.0256 0.0088  0.0582  48  TYR A CD2 
94   C CE1 . TYR A 13  ? 0.3867 0.4487 0.3870 -0.0221 0.0091  0.0454  48  TYR A CE1 
95   C CE2 . TYR A 13  ? 0.2031 0.2824 0.1934 -0.0281 0.0106  0.0507  48  TYR A CE2 
96   C CZ  . TYR A 13  ? 0.4620 0.5402 0.4556 -0.0264 0.0107  0.0444  48  TYR A CZ  
97   O OH  . TYR A 13  ? 0.3590 0.4534 0.3505 -0.0294 0.0129  0.0358  48  TYR A OH  
98   N N   . ARG A 14  ? 0.1834 0.2554 0.2116 -0.0100 0.0010  0.0943  49  ARG A N   
99   C CA  . ARG A 14  ? 0.1803 0.2756 0.2060 -0.0082 0.0005  0.1061  49  ARG A CA  
100  C C   . ARG A 14  ? 0.1962 0.3127 0.2075 -0.0123 0.0008  0.0965  49  ARG A C   
101  O O   . ARG A 14  ? 0.2328 0.3517 0.2420 -0.0137 0.0007  0.0854  49  ARG A O   
102  C CB  . ARG A 14  ? 0.2504 0.3552 0.2899 0.0001  -0.0015 0.1200  49  ARG A CB  
103  C CG  . ARG A 14  ? 0.2369 0.3620 0.2773 0.0043  -0.0014 0.1378  49  ARG A CG  
104  C CD  . ARG A 14  ? 0.2850 0.3934 0.3386 0.0064  0.0013  0.1506  49  ARG A CD  
105  N NE  . ARG A 14  ? 0.3152 0.4089 0.3898 0.0122  0.0015  0.1568  49  ARG A NE  
106  C CZ  . ARG A 14  ? 0.4710 0.5471 0.5637 0.0141  0.0045  0.1656  49  ARG A CZ  
107  N NH1 . ARG A 14  ? 0.2441 0.3145 0.3359 0.0105  0.0071  0.1663  49  ARG A NH1 
108  N NH2 . ARG A 14  ? 0.2835 0.3479 0.3973 0.0195  0.0053  0.1697  49  ARG A NH2 
109  N N   . MET A 15  ? 0.2180 0.3513 0.2209 -0.0145 0.0018  0.1004  50  MET A N   
110  C CA  . MET A 15  ? 0.2554 0.4109 0.2468 -0.0191 0.0026  0.0894  50  MET A CA  
111  C C   . MET A 15  ? 0.2496 0.4325 0.2359 -0.0173 0.0019  0.0995  50  MET A C   
112  O O   . MET A 15  ? 0.2491 0.4272 0.2353 -0.0167 0.0034  0.1098  50  MET A O   
113  C CB  . MET A 15  ? 0.2780 0.4198 0.2611 -0.0272 0.0070  0.0744  50  MET A CB  
114  C CG  . MET A 15  ? 0.3227 0.4861 0.2973 -0.0330 0.0094  0.0612  50  MET A CG  
115  S SD  . MET A 15  ? 0.2973 0.4427 0.2656 -0.0417 0.0164  0.0461  50  MET A SD  
116  C CE  . MET A 15  ? 0.2602 0.4089 0.2239 -0.0424 0.0173  0.0557  50  MET A CE  
117  N N   . LEU A 16  ? 0.2258 0.4392 0.2078 -0.0163 -0.0002 0.0963  51  LEU A N   
118  C CA  . LEU A 16  ? 0.2124 0.4568 0.1872 -0.0143 -0.0010 0.1043  51  LEU A CA  
119  C C   . LEU A 16  ? 0.2902 0.5426 0.2539 -0.0233 0.0027  0.0883  51  LEU A C   
120  O O   . LEU A 16  ? 0.2872 0.5345 0.2493 -0.0301 0.0050  0.0697  51  LEU A O   
121  C CB  . LEU A 16  ? 0.2059 0.4844 0.1816 -0.0083 -0.0056 0.1078  51  LEU A CB  
122  C CG  . LEU A 16  ? 0.2872 0.5608 0.2758 0.0018  -0.0087 0.1251  51  LEU A CG  
123  C CD1 . LEU A 16  ? 0.3616 0.6704 0.3529 0.0083  -0.0127 0.1272  51  LEU A CD1 
124  C CD2 . LEU A 16  ? 0.3775 0.6346 0.3761 0.0073  -0.0063 0.1429  51  LEU A CD2 
125  N N   . LEU A 17  ? 0.2399 0.4980 0.2031 -0.0224 0.0034  0.0921  52  LEU A N   
126  C CA  . LEU A 17  ? 0.2176 0.4843 0.1742 -0.0294 0.0063  0.0767  52  LEU A CA  
127  C C   . LEU A 17  ? 0.2662 0.5646 0.2230 -0.0247 0.0039  0.0817  52  LEU A C   
128  O O   . LEU A 17  ? 0.2189 0.5138 0.1777 -0.0207 0.0046  0.0940  52  LEU A O   
129  C CB  . LEU A 17  ? 0.2105 0.4478 0.1662 -0.0335 0.0105  0.0759  52  LEU A CB  
130  C CG  . LEU A 17  ? 0.2270 0.4683 0.1775 -0.0407 0.0142  0.0597  52  LEU A CG  
131  C CD1 . LEU A 17  ? 0.2820 0.5116 0.2315 -0.0483 0.0183  0.0418  52  LEU A CD1 
132  C CD2 . LEU A 17  ? 0.2822 0.5052 0.2329 -0.0408 0.0167  0.0655  52  LEU A CD2 
133  N N   . GLY A 18  ? 0.2755 0.6057 0.2312 -0.0253 0.0017  0.0715  53  GLY A N   
134  C CA  . GLY A 18  ? 0.2219 0.5860 0.1789 -0.0193 -0.0005 0.0776  53  GLY A CA  
135  C C   . GLY A 18  ? 0.2346 0.5981 0.1983 -0.0083 -0.0023 0.1011  53  GLY A C   
136  O O   . GLY A 18  ? 0.2972 0.6564 0.2656 -0.0044 -0.0044 0.1069  53  GLY A O   
137  N N   . ASP A 19  ? 0.2189 0.5863 0.1845 -0.0032 -0.0009 0.1145  54  ASP A N   
138  C CA  . ASP A 19  ? 0.3047 0.6682 0.2795 0.0069  -0.0006 0.1371  54  ASP A CA  
139  C C   . ASP A 19  ? 0.2607 0.5841 0.2420 0.0067  0.0019  0.1468  54  ASP A C   
140  O O   . ASP A 19  ? 0.2649 0.5805 0.2574 0.0143  0.0032  0.1642  54  ASP A O   
141  C CB  . ASP A 19  ? 0.3939 0.7846 0.3692 0.0133  0.0008  0.1472  54  ASP A CB  
142  C CG  . ASP A 19  ? 0.5397 0.9739 0.5109 0.0149  -0.0016 0.1387  54  ASP A CG  
143  O OD1 . ASP A 19  ? 0.3929 0.8374 0.3652 0.0154  -0.0043 0.1328  54  ASP A OD1 
144  O OD2 . ASP A 19  ? 0.5637 1.0224 0.5309 0.0157  -0.0007 0.1371  54  ASP A OD2 
145  N N   . PHE A 20  ? 0.2680 0.5667 0.2443 -0.0016 0.0034  0.1355  55  PHE A N   
146  C CA  . PHE A 20  ? 0.2793 0.5419 0.2623 -0.0024 0.0059  0.1422  55  PHE A CA  
147  C C   . PHE A 20  ? 0.2568 0.4986 0.2446 -0.0029 0.0044  0.1415  55  PHE A C   
148  O O   . PHE A 20  ? 0.2599 0.5091 0.2416 -0.0062 0.0024  0.1307  55  PHE A O   
149  C CB  . PHE A 20  ? 0.2502 0.4961 0.2261 -0.0106 0.0086  0.1305  55  PHE A CB  
150  C CG  . PHE A 20  ? 0.2396 0.5008 0.2113 -0.0106 0.0105  0.1311  55  PHE A CG  
151  C CD1 . PHE A 20  ? 0.2465 0.5337 0.2211 -0.0032 0.0101  0.1432  55  PHE A CD1 
152  C CD2 . PHE A 20  ? 0.2279 0.4769 0.1933 -0.0176 0.0133  0.1202  55  PHE A CD2 
153  C CE1 . PHE A 20  ? 0.2321 0.5340 0.2024 -0.0031 0.0121  0.1437  55  PHE A CE1 
154  C CE2 . PHE A 20  ? 0.3049 0.5675 0.2666 -0.0176 0.0153  0.1204  55  PHE A CE2 
155  C CZ  . PHE A 20  ? 0.2277 0.5170 0.1912 -0.0106 0.0145  0.1321  55  PHE A CZ  
156  N N   . GLU A 21  ? 0.2607 0.4768 0.2606 0.0000  0.0060  0.1521  56  GLU A N   
157  C CA  . GLU A 21  ? 0.2212 0.4146 0.2275 -0.0006 0.0050  0.1513  56  GLU A CA  
158  C C   . GLU A 21  ? 0.2376 0.4020 0.2430 -0.0073 0.0072  0.1432  56  GLU A C   
159  O O   . GLU A 21  ? 0.2085 0.3603 0.2206 -0.0070 0.0097  0.1478  56  GLU A O   
160  C CB  . GLU A 21  ? 0.2177 0.4037 0.2423 0.0078  0.0054  0.1673  56  GLU A CB  
161  C CG  . GLU A 21  ? 0.2479 0.4093 0.2823 0.0079  0.0045  0.1666  56  GLU A CG  
162  C CD  . GLU A 21  ? 0.3876 0.5322 0.4439 0.0135  0.0073  0.1787  56  GLU A CD  
163  O OE1 . GLU A 21  ? 0.3093 0.4389 0.3716 0.0114  0.0103  0.1793  56  GLU A OE1 
164  O OE2 . GLU A 21  ? 0.2651 0.4125 0.3336 0.0201  0.0069  0.1871  56  GLU A OE2 
165  N N   . ILE A 22  ? 0.2200 0.3752 0.2177 -0.0133 0.0070  0.1309  57  ILE A N   
166  C CA  . ILE A 22  ? 0.1934 0.3223 0.1907 -0.0191 0.0092  0.1228  57  ILE A CA  
167  C C   . ILE A 22  ? 0.2955 0.4033 0.3041 -0.0169 0.0077  0.1239  57  ILE A C   
168  O O   . ILE A 22  ? 0.2363 0.3483 0.2463 -0.0145 0.0053  0.1198  57  ILE A O   
169  C CB  . ILE A 22  ? 0.2520 0.3846 0.2350 -0.0269 0.0113  0.1063  57  ILE A CB  
170  C CG1 . ILE A 22  ? 0.2649 0.4225 0.2393 -0.0283 0.0119  0.1015  57  ILE A CG1 
171  C CG2 . ILE A 22  ? 0.2311 0.3381 0.2143 -0.0316 0.0138  0.0984  57  ILE A CG2 
172  C CD1 . ILE A 22  ? 0.2215 0.3777 0.1981 -0.0268 0.0132  0.1075  57  ILE A CD1 
173  N N   . THR A 23  ? 0.2252 0.3106 0.2439 -0.0173 0.0088  0.1261  58  THR A N   
174  C CA  . THR A 23  ? 0.2174 0.2814 0.2473 -0.0158 0.0071  0.1204  58  THR A CA  
175  C C   . THR A 23  ? 0.2052 0.2509 0.2315 -0.0209 0.0080  0.1083  58  THR A C   
176  O O   . THR A 23  ? 0.2453 0.2834 0.2770 -0.0224 0.0096  0.1124  58  THR A O   
177  C CB  . THR A 23  ? 0.2806 0.3369 0.3312 -0.0101 0.0074  0.1344  58  THR A CB  
178  O OG1 . THR A 23  ? 0.2399 0.3164 0.2930 -0.0043 0.0073  0.1481  58  THR A OG1 
179  C CG2 . THR A 23  ? 0.2660 0.3049 0.3285 -0.0082 0.0056  0.1261  58  THR A CG2 
180  N N   . ALA A 24  ? 0.1850 0.2250 0.2027 -0.0231 0.0074  0.0942  59  ALA A N   
181  C CA  . ALA A 24  ? 0.2061 0.2290 0.2217 -0.0259 0.0079  0.0841  59  ALA A CA  
182  C C   . ALA A 24  ? 0.2398 0.2474 0.2712 -0.0227 0.0057  0.0841  59  ALA A C   
183  O O   . ALA A 24  ? 0.2062 0.2126 0.2453 -0.0190 0.0040  0.0842  59  ALA A O   
184  C CB  . ALA A 24  ? 0.2183 0.2402 0.2215 -0.0280 0.0091  0.0710  59  ALA A CB  
185  N N   . LEU A 25  ? 0.1913 0.1883 0.2291 -0.0241 0.0057  0.0831  60  LEU A N   
186  C CA  . LEU A 25  ? 0.2105 0.1947 0.2662 -0.0219 0.0039  0.0811  60  LEU A CA  
187  C C   . LEU A 25  ? 0.2327 0.2074 0.2833 -0.0233 0.0023  0.0675  60  LEU A C   
188  O O   . LEU A 25  ? 0.2358 0.2095 0.2808 -0.0260 0.0032  0.0660  60  LEU A O   
189  C CB  . LEU A 25  ? 0.1923 0.1745 0.2650 -0.0220 0.0056  0.0923  60  LEU A CB  
190  C CG  . LEU A 25  ? 0.1925 0.1859 0.2709 -0.0193 0.0080  0.1091  60  LEU A CG  
191  C CD1 . LEU A 25  ? 0.2343 0.2269 0.3257 -0.0191 0.0109  0.1172  60  LEU A CD1 
192  C CD2 . LEU A 25  ? 0.2212 0.2137 0.3116 -0.0143 0.0070  0.1122  60  LEU A CD2 
193  N N   . SER A 26  ? 0.2343 0.2034 0.2870 -0.0207 0.0002  0.0581  61  SER A N   
194  C CA  . SER A 26  ? 0.2234 0.1864 0.2710 -0.0205 -0.0016 0.0457  61  SER A CA  
195  C C   . SER A 26  ? 0.2016 0.1584 0.2670 -0.0208 -0.0036 0.0425  61  SER A C   
196  O O   . SER A 26  ? 0.2425 0.1954 0.3282 -0.0197 -0.0040 0.0442  61  SER A O   
197  C CB  . SER A 26  ? 0.2335 0.1948 0.2776 -0.0172 -0.0028 0.0366  61  SER A CB  
198  O OG  . SER A 26  ? 0.2440 0.2028 0.2796 -0.0160 -0.0041 0.0258  61  SER A OG  
199  N N   . ASP A 27  ? 0.1997 0.1561 0.2596 -0.0222 -0.0045 0.0375  62  ASP A N   
200  C CA  . ASP A 27  ? 0.2581 0.2111 0.3337 -0.0224 -0.0073 0.0300  62  ASP A CA  
201  C C   . ASP A 27  ? 0.2087 0.1621 0.2809 -0.0191 -0.0109 0.0152  62  ASP A C   
202  O O   . ASP A 27  ? 0.2230 0.1764 0.3086 -0.0189 -0.0140 0.0056  62  ASP A O   
203  C CB  . ASP A 27  ? 0.2089 0.1640 0.2806 -0.0249 -0.0068 0.0318  62  ASP A CB  
204  C CG  . ASP A 27  ? 0.2264 0.1795 0.3202 -0.0264 -0.0088 0.0269  62  ASP A CG  
205  O OD1 . ASP A 27  ? 0.2444 0.1932 0.3600 -0.0275 -0.0074 0.0306  62  ASP A OD1 
206  O OD2 . ASP A 27  ? 0.2586 0.2149 0.3497 -0.0262 -0.0114 0.0191  62  ASP A OD2 
207  N N   . GLY A 28  ? 0.2203 0.1754 0.2756 -0.0165 -0.0103 0.0128  63  GLY A N   
208  C CA  . GLY A 28  ? 0.2455 0.2031 0.2930 -0.0125 -0.0128 0.0004  63  GLY A CA  
209  C C   . GLY A 28  ? 0.2546 0.2159 0.2787 -0.0107 -0.0108 0.0013  63  GLY A C   
210  O O   . GLY A 28  ? 0.2622 0.2230 0.2764 -0.0131 -0.0069 0.0103  63  GLY A O   
211  N N   . THR A 29  ? 0.2674 0.2331 0.2832 -0.0062 -0.0128 -0.0082 64  THR A N   
212  C CA  . THR A 29  ? 0.2848 0.2541 0.2804 -0.0031 -0.0102 -0.0066 64  THR A CA  
213  C C   . THR A 29  ? 0.2746 0.2520 0.2697 0.0011  -0.0148 -0.0150 64  THR A C   
214  O O   . THR A 29  ? 0.2857 0.2673 0.2937 0.0020  -0.0200 -0.0257 64  THR A O   
215  C CB  . THR A 29  ? 0.2736 0.2434 0.2549 0.0004  -0.0064 -0.0075 64  THR A CB  
216  O OG1 . THR A 29  ? 0.3041 0.2788 0.2878 0.0048  -0.0100 -0.0187 64  THR A OG1 
217  C CG2 . THR A 29  ? 0.2695 0.2343 0.2522 -0.0033 -0.0024 -0.0011 64  THR A CG2 
218  N N   . VAL A 30  ? 0.2683 0.2491 0.2494 0.0039  -0.0126 -0.0106 65  VAL A N   
219  C CA  . VAL A 30  ? 0.2861 0.2777 0.2642 0.0092  -0.0168 -0.0167 65  VAL A CA  
220  C C   . VAL A 30  ? 0.2907 0.2861 0.2478 0.0157  -0.0119 -0.0111 65  VAL A C   
221  O O   . VAL A 30  ? 0.2539 0.2418 0.2029 0.0140  -0.0047 -0.0011 65  VAL A O   
222  C CB  . VAL A 30  ? 0.3073 0.3002 0.2979 0.0058  -0.0198 -0.0157 65  VAL A CB  
223  C CG1 . VAL A 30  ? 0.2582 0.2446 0.2422 0.0029  -0.0137 -0.0031 65  VAL A CG1 
224  C CG2 . VAL A 30  ? 0.3826 0.3900 0.3728 0.0115  -0.0257 -0.0243 65  VAL A CG2 
225  N N   . ALA A 31  ? 0.2979 0.3059 0.2472 0.0235  -0.0152 -0.0178 66  ALA A N   
226  C CA  . ALA A 31  ? 0.3119 0.3251 0.2420 0.0314  -0.0100 -0.0109 66  ALA A CA  
227  C C   . ALA A 31  ? 0.3455 0.3633 0.2740 0.0340  -0.0099 -0.0046 66  ALA A C   
228  O O   . ALA A 31  ? 0.3341 0.3637 0.2696 0.0361  -0.0175 -0.0117 66  ALA A O   
229  C CB  . ALA A 31  ? 0.3368 0.3647 0.2579 0.0398  -0.0133 -0.0198 66  ALA A CB  
230  N N   . LEU A 32  ? 0.2944 0.3035 0.2155 0.0339  -0.0011 0.0079  67  LEU A N   
231  C CA  . LEU A 32  ? 0.3073 0.3180 0.2293 0.0354  0.0004  0.0149  67  LEU A CA  
232  C C   . LEU A 32  ? 0.4623 0.4778 0.3694 0.0454  0.0074  0.0246  67  LEU A C   
233  O O   . LEU A 32  ? 0.3139 0.3218 0.2124 0.0467  0.0164  0.0309  67  LEU A O   
234  C CB  . LEU A 32  ? 0.3261 0.3224 0.2556 0.0263  0.0060  0.0214  67  LEU A CB  
235  C CG  . LEU A 32  ? 0.3261 0.3177 0.2709 0.0170  0.0008  0.0160  67  LEU A CG  
236  C CD1 . LEU A 32  ? 0.3597 0.3411 0.3084 0.0097  0.0072  0.0234  67  LEU A CD1 
237  C CD2 . LEU A 32  ? 0.3664 0.3681 0.3228 0.0177  -0.0084 0.0083  67  LEU A CD2 
238  N N   . PRO A 33  ? 0.3530 0.4208 0.2744 -0.1345 0.0162  0.0046  68  PRO A N   
239  C CA  . PRO A 33  ? 0.3749 0.4857 0.2990 -0.1307 -0.0022 0.0236  68  PRO A CA  
240  C C   . PRO A 33  ? 0.3251 0.4284 0.2685 -0.1088 -0.0013 0.0474  68  PRO A C   
241  O O   . PRO A 33  ? 0.3480 0.4768 0.3176 -0.1069 -0.0060 0.0641  68  PRO A O   
242  C CB  . PRO A 33  ? 0.3406 0.5022 0.2812 -0.1522 -0.0152 0.0193  68  PRO A CB  
243  C CG  . PRO A 33  ? 0.3630 0.5031 0.3287 -0.1610 -0.0028 0.0097  68  PRO A CG  
244  C CD  . PRO A 33  ? 0.3413 0.4224 0.2896 -0.1541 0.0183  -0.0052 68  PRO A CD  
245  N N   . VAL A 34  ? 0.3135 0.3821 0.2455 -0.0913 0.0053  0.0474  69  VAL A N   
246  C CA  . VAL A 34  ? 0.3903 0.4461 0.3386 -0.0704 0.0070  0.0599  69  VAL A CA  
247  C C   . VAL A 34  ? 0.3843 0.4698 0.3566 -0.0664 -0.0033 0.0816  69  VAL A C   
248  O O   . VAL A 34  ? 0.3097 0.3921 0.3039 -0.0525 -0.0012 0.0928  69  VAL A O   
249  C CB  . VAL A 34  ? 0.3833 0.4029 0.3157 -0.0541 0.0132  0.0496  69  VAL A CB  
250  C CG1 . VAL A 34  ? 0.3364 0.3314 0.2503 -0.0530 0.0283  0.0363  69  VAL A CG1 
251  C CG2 . VAL A 34  ? 0.3296 0.3520 0.2547 -0.0567 0.0067  0.0500  69  VAL A CG2 
252  N N   . ASP A 35  ? 0.3094 0.4249 0.2789 -0.0754 -0.0116 0.0899  70  ASP A N   
253  C CA  . ASP A 35  ? 0.2590 0.4089 0.2566 -0.0689 -0.0171 0.1180  70  ASP A CA  
254  C C   . ASP A 35  ? 0.3435 0.5305 0.3627 -0.0722 -0.0204 0.1337  70  ASP A C   
255  O O   . ASP A 35  ? 0.4057 0.6108 0.4564 -0.0602 -0.0191 0.1600  70  ASP A O   
256  C CB  . ASP A 35  ? 0.3362 0.5190 0.3234 -0.0738 -0.0226 0.1281  70  ASP A CB  
257  C CG  . ASP A 35  ? 0.5474 0.7592 0.5035 -0.0926 -0.0293 0.1110  70  ASP A CG  
258  O OD1 . ASP A 35  ? 0.3551 0.5429 0.2968 -0.1039 -0.0262 0.0852  70  ASP A OD1 
259  O OD2 . ASP A 35  ? 0.5602 0.8211 0.5084 -0.0949 -0.0365 0.1231  70  ASP A OD2 
260  N N   . LYS A 36  ? 0.2699 0.4689 0.2790 -0.0883 -0.0229 0.1189  71  LYS A N   
261  C CA  . LYS A 36  ? 0.3473 0.5862 0.3822 -0.0939 -0.0268 0.1330  71  LYS A CA  
262  C C   . LYS A 36  ? 0.3082 0.5165 0.3615 -0.0814 -0.0146 0.1361  71  LYS A C   
263  O O   . LYS A 36  ? 0.4529 0.6897 0.5360 -0.0760 -0.0141 0.1585  71  LYS A O   
264  C CB  . LYS A 36  ? 0.3281 0.5992 0.3533 -0.1202 -0.0362 0.1129  71  LYS A CB  
265  C CG  . LYS A 36  ? 0.4391 0.7491 0.4392 -0.1302 -0.0488 0.1065  71  LYS A CG  
266  C CD  . LYS A 36  ? 0.6077 0.9330 0.5923 -0.1572 -0.0562 0.0716  71  LYS A CD  
267  C CE  . LYS A 36  ? 0.7757 1.1528 0.7315 -0.1642 -0.0704 0.0642  71  LYS A CE  
268  N NZ  . LYS A 36  ? 0.7529 1.0975 0.6738 -0.1788 -0.0663 0.0231  71  LYS A NZ  
269  N N   . ARG A 37  ? 0.2775 0.4332 0.3130 -0.0734 -0.0035 0.1171  72  ARG A N   
270  C CA  . ARG A 37  ? 0.3564 0.4886 0.4031 -0.0576 0.0099  0.1202  72  ARG A CA  
271  C C   . ARG A 37  ? 0.3145 0.4225 0.3664 -0.0308 0.0155  0.1273  72  ARG A C   
272  O O   . ARG A 37  ? 0.2990 0.4038 0.3663 -0.0143 0.0251  0.1381  72  ARG A O   
273  C CB  . ARG A 37  ? 0.4753 0.5725 0.5025 -0.0590 0.0222  0.0997  72  ARG A CB  
274  C CG  . ARG A 37  ? 0.5570 0.6668 0.5834 -0.0871 0.0202  0.0850  72  ARG A CG  
275  C CD  . ARG A 37  ? 0.4354 0.5963 0.4944 -0.1058 0.0104  0.0960  72  ARG A CD  
276  N NE  . ARG A 37  ? 0.5120 0.6759 0.6032 -0.0971 0.0227  0.1125  72  ARG A NE  
277  C CZ  . ARG A 37  ? 0.4672 0.6372 0.5856 -0.1130 0.0308  0.1082  72  ARG A CZ  
278  N NH1 . ARG A 37  ? 0.4173 0.5877 0.5354 -0.1405 0.0276  0.0827  72  ARG A NH1 
279  N NH2 . ARG A 37  ? 0.4316 0.6069 0.5826 -0.1006 0.0442  0.1297  72  ARG A NH2 
280  N N   . LEU A 38  ? 0.2549 0.3457 0.2973 -0.0260 0.0107  0.1199  73  LEU A N   
281  C CA  . LEU A 38  ? 0.2950 0.3611 0.3491 -0.0040 0.0149  0.1191  73  LEU A CA  
282  C C   . LEU A 38  ? 0.2607 0.3504 0.3533 0.0031  0.0168  0.1468  73  LEU A C   
283  O O   . LEU A 38  ? 0.2868 0.4150 0.3957 -0.0084 0.0107  0.1685  73  LEU A O   
284  C CB  . LEU A 38  ? 0.2532 0.2996 0.2994 -0.0050 0.0088  0.1049  73  LEU A CB  
285  C CG  . LEU A 38  ? 0.2515 0.2691 0.2640 -0.0013 0.0100  0.0781  73  LEU A CG  
286  C CD1 . LEU A 38  ? 0.2897 0.2999 0.2994 -0.0079 0.0026  0.0700  73  LEU A CD1 
287  C CD2 . LEU A 38  ? 0.3044 0.2987 0.3114 0.0228  0.0161  0.0632  73  LEU A CD2 
288  N N   . ASN A 39  ? 0.2315 0.3008 0.3381 0.0250  0.0270  0.1469  74  ASN A N   
289  C CA  . ASN A 39  ? 0.2815 0.3670 0.4284 0.0363  0.0344  0.1747  74  ASN A CA  
290  C C   . ASN A 39  ? 0.2781 0.3486 0.4534 0.0411  0.0353  0.1774  74  ASN A C   
291  O O   . ASN A 39  ? 0.3187 0.3583 0.5158 0.0589  0.0449  0.1693  74  ASN A O   
292  C CB  . ASN A 39  ? 0.3291 0.3982 0.4797 0.0597  0.0486  0.1739  74  ASN A CB  
293  C CG  . ASN A 39  ? 0.4376 0.5291 0.5772 0.0556  0.0521  0.1830  74  ASN A CG  
294  O OD1 . ASN A 39  ? 0.4496 0.5832 0.6022 0.0364  0.0455  0.2028  74  ASN A OD1 
295  N ND2 . ASN A 39  ? 0.3704 0.4380 0.4898 0.0746  0.0630  0.1689  74  ASN A ND2 
296  N N   . GLN A 40  ? 0.2506 0.3445 0.4292 0.0254  0.0267  0.1889  75  GLN A N   
297  C CA  . GLN A 40  ? 0.2758 0.3660 0.4920 0.0287  0.0305  0.2030  75  GLN A CA  
298  C C   . GLN A 40  ? 0.2889 0.4278 0.5019 0.0144  0.0227  0.2281  75  GLN A C   
299  O O   . GLN A 40  ? 0.2727 0.4353 0.4476 -0.0008 0.0116  0.2197  75  GLN A O   
300  C CB  . GLN A 40  ? 0.2370 0.2786 0.4508 0.0305  0.0283  0.1679  75  GLN A CB  
301  C CG  . GLN A 40  ? 0.2860 0.3283 0.4652 0.0148  0.0161  0.1512  75  GLN A CG  
302  C CD  . GLN A 40  ? 0.2388 0.2417 0.4239 0.0174  0.0129  0.1194  75  GLN A CD  
303  O OE1 . GLN A 40  ? 0.3222 0.2975 0.5405 0.0288  0.0185  0.1065  75  GLN A OE1 
304  N NE2 . GLN A 40  ? 0.2812 0.2829 0.4366 0.0068  0.0041  0.1049  75  GLN A NE2 
305  N N   . PRO A 41  ? 0.2977 0.4562 0.5501 0.0206  0.0292  0.2491  76  PRO A N   
306  C CA  . PRO A 41  ? 0.3014 0.5161 0.5476 0.0142  0.0213  0.2645  76  PRO A CA  
307  C C   . PRO A 41  ? 0.2950 0.5019 0.4950 -0.0016 0.0093  0.2450  76  PRO A C   
308  O O   . PRO A 41  ? 0.2603 0.4213 0.4540 -0.0043 0.0106  0.2282  76  PRO A O   
309  C CB  . PRO A 41  ? 0.2895 0.5126 0.5915 0.0283  0.0357  0.2862  76  PRO A CB  
310  C CG  . PRO A 41  ? 0.3082 0.4979 0.6492 0.0402  0.0523  0.2870  76  PRO A CG  
311  C CD  . PRO A 41  ? 0.3097 0.4419 0.6168 0.0347  0.0457  0.2551  76  PRO A CD  
312  N N   . ALA A 42  ? 0.3307 0.5850 0.5006 -0.0125 -0.0019 0.2460  77  ALA A N   
313  C CA  . ALA A 42  ? 0.3058 0.5538 0.4290 -0.0276 -0.0105 0.2247  77  ALA A CA  
314  C C   . ALA A 42  ? 0.3234 0.5575 0.4550 -0.0220 -0.0058 0.2269  77  ALA A C   
315  O O   . ALA A 42  ? 0.2718 0.4704 0.3758 -0.0299 -0.0072 0.2064  77  ALA A O   
316  C CB  . ALA A 42  ? 0.3305 0.6344 0.4250 -0.0413 -0.0221 0.2219  77  ALA A CB  
317  N N   . PRO A 43  ? 0.3323 0.5958 0.5038 -0.0082 0.0015  0.2527  78  PRO A N   
318  C CA  . PRO A 43  ? 0.3223 0.5702 0.5110 -0.0023 0.0082  0.2569  78  PRO A CA  
319  C C   . PRO A 43  ? 0.4012 0.5863 0.6111 -0.0031 0.0132  0.2426  78  PRO A C   
320  O O   . PRO A 43  ? 0.2425 0.4069 0.4476 -0.0068 0.0132  0.2333  78  PRO A O   
321  C CB  . PRO A 43  ? 0.2732 0.5664 0.5151 0.0156  0.0196  0.2919  78  PRO A CB  
322  C CG  . PRO A 43  ? 0.3403 0.6936 0.5639 0.0136  0.0131  0.3011  78  PRO A CG  
323  C CD  . PRO A 43  ? 0.3321 0.6597 0.5290 0.0008  0.0038  0.2801  78  PRO A CD  
324  N N   . LYS A 44  ? 0.3150 0.4721 0.5517 0.0007  0.0178  0.2396  79  LYS A N   
325  C CA  . LYS A 44  ? 0.2796 0.3783 0.5390 -0.0007 0.0206  0.2193  79  LYS A CA  
326  C C   . LYS A 44  ? 0.2557 0.3291 0.4600 -0.0115 0.0085  0.1814  79  LYS A C   
327  O O   . LYS A 44  ? 0.2731 0.3204 0.4817 -0.0142 0.0054  0.1606  79  LYS A O   
328  C CB  . LYS A 44  ? 0.2998 0.3762 0.5900 0.0088  0.0280  0.2176  79  LYS A CB  
329  C CG  . LYS A 44  ? 0.2871 0.3087 0.6090 0.0121  0.0297  0.1851  79  LYS A CG  
330  C CD  . LYS A 44  ? 0.4169 0.4194 0.7593 0.0250  0.0386  0.1802  79  LYS A CD  
331  C CE  . LYS A 44  ? 0.4065 0.3724 0.8105 0.0307  0.0489  0.1625  79  LYS A CE  
332  N NZ  . LYS A 44  ? 0.7617 0.6847 1.1491 0.0301  0.0363  0.1085  79  LYS A NZ  
333  N N   . THR A 45  ? 0.2357 0.3209 0.3918 -0.0168 0.0022  0.1706  80  THR A N   
334  C CA  . THR A 45  ? 0.2735 0.3394 0.3794 -0.0243 -0.0047 0.1378  80  THR A CA  
335  C C   . THR A 45  ? 0.2386 0.3134 0.3255 -0.0315 -0.0063 0.1393  80  THR A C   
336  O O   . THR A 45  ? 0.2414 0.2908 0.3148 -0.0322 -0.0081 0.1177  80  THR A O   
337  C CB  . THR A 45  ? 0.2611 0.3415 0.3315 -0.0303 -0.0071 0.1323  80  THR A CB  
338  O OG1 . THR A 45  ? 0.2953 0.3624 0.3814 -0.0201 -0.0034 0.1295  80  THR A OG1 
339  C CG2 . THR A 45  ? 0.2476 0.3093 0.2720 -0.0375 -0.0088 0.1046  80  THR A CG2 
340  N N   . GLN A 46  ? 0.2433 0.3590 0.3283 -0.0342 -0.0049 0.1662  81  GLN A N   
341  C CA  . GLN A 46  ? 0.2744 0.4014 0.3352 -0.0381 -0.0042 0.1680  81  GLN A CA  
342  C C   . GLN A 46  ? 0.3194 0.4267 0.4180 -0.0321 0.0009  0.1742  81  GLN A C   
343  O O   . GLN A 46  ? 0.2346 0.3290 0.3129 -0.0346 0.0011  0.1613  81  GLN A O   
344  C CB  . GLN A 46  ? 0.3586 0.5382 0.4114 -0.0354 -0.0050 0.1852  81  GLN A CB  
345  C CG  . GLN A 46  ? 0.4569 0.6578 0.4657 -0.0476 -0.0129 0.1683  81  GLN A CG  
346  C CD  . GLN A 46  ? 0.7150 0.8977 0.6742 -0.0581 -0.0131 0.1394  81  GLN A CD  
347  O OE1 . GLN A 46  ? 0.5452 0.6862 0.4913 -0.0611 -0.0093 0.1240  81  GLN A OE1 
348  N NE2 . GLN A 46  ? 0.6618 0.8773 0.5952 -0.0627 -0.0164 0.1309  81  GLN A NE2 
349  N N   . SER A 47  ? 0.2628 0.3675 0.4226 -0.0244 0.0067  0.1940  82  SER A N   
350  C CA  . SER A 47  ? 0.2056 0.2918 0.4147 -0.0211 0.0112  0.1957  82  SER A CA  
351  C C   . SER A 47  ? 0.2129 0.2573 0.4199 -0.0259 0.0025  0.1559  82  SER A C   
352  O O   . SER A 47  ? 0.2433 0.2786 0.4612 -0.0282 0.0008  0.1475  82  SER A O   
353  C CB  . SER A 47  ? 0.2520 0.3471 0.5294 -0.0090 0.0204  0.2156  82  SER A CB  
354  O OG  . SER A 47  ? 0.5801 0.6443 0.8858 -0.0093 0.0205  0.2023  82  SER A OG  
355  N N   . ALA A 48  ? 0.2052 0.2305 0.3959 -0.0245 -0.0034 0.1305  83  ALA A N   
356  C CA  . ALA A 48  ? 0.2871 0.2842 0.4621 -0.0238 -0.0125 0.0907  83  ALA A CA  
357  C C   . ALA A 48  ? 0.2760 0.2762 0.3961 -0.0271 -0.0153 0.0793  83  ALA A C   
358  O O   . ALA A 48  ? 0.2776 0.2684 0.3992 -0.0262 -0.0204 0.0612  83  ALA A O   
359  C CB  . ALA A 48  ? 0.2677 0.2505 0.4270 -0.0169 -0.0148 0.0711  83  ALA A CB  
360  N N   . LEU A 49  ? 0.2426 0.2574 0.3173 -0.0309 -0.0113 0.0889  84  LEU A N   
361  C CA  . LEU A 49  ? 0.2553 0.2682 0.2821 -0.0338 -0.0090 0.0789  84  LEU A CA  
362  C C   . LEU A 49  ? 0.2403 0.2623 0.2802 -0.0346 -0.0054 0.0929  84  LEU A C   
363  O O   . LEU A 49  ? 0.2689 0.2814 0.2937 -0.0324 -0.0047 0.0810  84  LEU A O   
364  C CB  . LEU A 49  ? 0.2685 0.2953 0.2546 -0.0408 -0.0050 0.0827  84  LEU A CB  
365  C CG  . LEU A 49  ? 0.2841 0.3021 0.2547 -0.0406 -0.0058 0.0693  84  LEU A CG  
366  C CD1 . LEU A 49  ? 0.3604 0.3915 0.2969 -0.0517 -0.0021 0.0674  84  LEU A CD1 
367  C CD2 . LEU A 49  ? 0.3717 0.3637 0.3311 -0.0306 -0.0051 0.0468  84  LEU A CD2 
368  N N   . ALA A 50  ? 0.2238 0.2681 0.2949 -0.0348 -0.0011 0.1225  85  ALA A N   
369  C CA  . ALA A 50  ? 0.2327 0.2896 0.3205 -0.0325 0.0057  0.1423  85  ALA A CA  
370  C C   . ALA A 50  ? 0.2046 0.2448 0.3370 -0.0318 0.0013  0.1315  85  ALA A C   
371  O O   . ALA A 50  ? 0.2518 0.2956 0.3824 -0.0303 0.0050  0.1355  85  ALA A O   
372  C CB  . ALA A 50  ? 0.2512 0.3397 0.3724 -0.0272 0.0134  0.1796  85  ALA A CB  
373  N N   . LYS A 51  ? 0.2157 0.2402 0.3906 -0.0325 -0.0067 0.1163  86  LYS A N   
374  C CA  . LYS A 51  ? 0.2372 0.2508 0.4552 -0.0340 -0.0152 0.0966  86  LYS A CA  
375  C C   . LYS A 51  ? 0.2872 0.2982 0.4575 -0.0312 -0.0213 0.0726  86  LYS A C   
376  O O   . LYS A 51  ? 0.2836 0.3010 0.4802 -0.0318 -0.0258 0.0677  86  LYS A O   
377  C CB  . LYS A 51  ? 0.3527 0.3482 0.6120 -0.0345 -0.0241 0.0722  86  LYS A CB  
378  C CG  . LYS A 51  ? 0.3938 0.3871 0.7262 -0.0362 -0.0152 0.0952  86  LYS A CG  
379  C CD  . LYS A 51  ? 0.4106 0.3794 0.7761 -0.0355 -0.0228 0.0621  86  LYS A CD  
380  C CE  . LYS A 51  ? 0.4733 0.4356 0.9052 -0.0335 -0.0088 0.0859  86  LYS A CE  
381  N NZ  . LYS A 51  ? 0.5235 0.4597 0.9838 -0.0310 -0.0143 0.0477  86  LYS A NZ  
382  N N   . SER A 52  ? 0.2548 0.2592 0.3612 -0.0274 -0.0197 0.0606  87  SER A N   
383  C CA  . SER A 52  ? 0.2729 0.2750 0.3350 -0.0209 -0.0196 0.0442  87  SER A CA  
384  C C   . SER A 52  ? 0.3197 0.3248 0.3388 -0.0209 -0.0047 0.0608  87  SER A C   
385  O O   . SER A 52  ? 0.2825 0.2804 0.2590 -0.0147 0.0020  0.0509  87  SER A O   
386  C CB  . SER A 52  ? 0.4036 0.3947 0.4311 -0.0135 -0.0231 0.0212  87  SER A CB  
387  O OG  . SER A 52  ? 0.5362 0.5258 0.5964 -0.0095 -0.0370 -0.0013 87  SER A OG  
388  N N   . PHE A 53  ? 0.2198 0.2949 0.2521 0.0097  0.0265  0.1077  88  PHE A N   
389  C CA  . PHE A 53  ? 0.2520 0.3327 0.2628 0.0106  0.0339  0.1044  88  PHE A CA  
390  C C   . PHE A 53  ? 0.2803 0.3584 0.2668 0.0084  0.0301  0.0919  88  PHE A C   
391  O O   . PHE A 53  ? 0.3013 0.3767 0.2745 0.0084  0.0352  0.0816  88  PHE A O   
392  C CB  . PHE A 53  ? 0.2770 0.3537 0.2969 0.0127  0.0412  0.1011  88  PHE A CB  
393  C CG  . PHE A 53  ? 0.2675 0.3471 0.3138 0.0142  0.0444  0.1131  88  PHE A CG  
394  C CD1 . PHE A 53  ? 0.2832 0.3557 0.3531 0.0129  0.0378  0.1123  88  PHE A CD1 
395  C CD2 . PHE A 53  ? 0.3175 0.4079 0.3653 0.0163  0.0540  0.1249  88  PHE A CD2 
396  C CE1 . PHE A 53  ? 0.2580 0.3332 0.3547 0.0134  0.0403  0.1225  88  PHE A CE1 
397  C CE2 . PHE A 53  ? 0.3194 0.4127 0.3949 0.0176  0.0574  0.1369  88  PHE A CE2 
398  C CZ  . PHE A 53  ? 0.2964 0.3816 0.3975 0.0159  0.0502  0.1353  88  PHE A CZ  
399  N N   . GLN A 54  ? 0.2779 0.3568 0.2617 0.0065  0.0219  0.0929  89  GLN A N   
400  C CA  . GLN A 54  ? 0.2434 0.3210 0.2080 0.0038  0.0171  0.0827  89  GLN A CA  
401  C C   . GLN A 54  ? 0.2778 0.3699 0.2310 0.0018  0.0138  0.0920  89  GLN A C   
402  O O   . GLN A 54  ? 0.2999 0.4016 0.2637 0.0030  0.0146  0.1075  89  GLN A O   
403  C CB  . GLN A 54  ? 0.2248 0.2906 0.1988 0.0031  0.0096  0.0755  89  GLN A CB  
404  C CG  . GLN A 54  ? 0.2820 0.3363 0.2631 0.0042  0.0111  0.0664  89  GLN A CG  
405  C CD  . GLN A 54  ? 0.3492 0.3948 0.3413 0.0033  0.0043  0.0624  89  GLN A CD  
406  O OE1 . GLN A 54  ? 0.4271 0.4724 0.4187 0.0020  -0.0007 0.0628  89  GLN A OE1 
407  N NE2 . GLN A 54  ? 0.6151 0.6546 0.6172 0.0038  0.0043  0.0590  89  GLN A NE2 
408  N N   . LYS A 55  ? 0.3051 0.4002 0.2386 -0.0016 0.0099  0.0835  90  LYS A N   
409  C CA  . LYS A 55  ? 0.3188 0.4295 0.2398 -0.0045 0.0061  0.0904  90  LYS A CA  
410  C C   . LYS A 55  ? 0.5940 0.7045 0.5019 -0.0088 -0.0014 0.0799  90  LYS A C   
411  O O   . LYS A 55  ? 0.5258 0.6251 0.4302 -0.0096 -0.0018 0.0671  90  LYS A O   
412  C CB  . LYS A 55  ? 0.4223 0.5422 0.3271 -0.0053 0.0139  0.0896  90  LYS A CB  
413  C CG  . LYS A 55  ? 0.8138 0.9483 0.7077 -0.0087 0.0097  0.0940  90  LYS A CG  
414  C CD  . LYS A 55  ? 0.8616 1.0054 0.7435 -0.0087 0.0180  0.0969  90  LYS A CD  
415  C CE  . LYS A 55  ? 0.7824 0.9356 0.6845 -0.0054 0.0184  0.1161  90  LYS A CE  
416  N NZ  . LYS A 55  ? 0.6916 0.8499 0.5867 -0.0038 0.0290  0.1192  90  LYS A NZ  
417  N N   . ALA A 56  ? 0.8111 0.9331 0.7167 -0.0116 -0.0075 0.0851  91  ALA A N   
418  C CA  . ALA A 56  ? 0.3608 0.4884 0.2504 -0.0170 -0.0135 0.0763  91  ALA A CA  
419  C C   . ALA A 56  ? 0.4115 0.5278 0.3029 -0.0182 -0.0179 0.0658  91  ALA A C   
420  O O   . ALA A 56  ? 0.4986 0.6068 0.4077 -0.0148 -0.0194 0.0709  91  ALA A O   
421  C CB  . ALA A 56  ? 0.7126 0.8450 0.5775 -0.0201 -0.0074 0.0661  91  ALA A CB  
422  N N   . PRO A 57  ? 0.4184 0.5338 0.2940 -0.0230 -0.0201 0.0513  92  PRO A N   
423  C CA  . PRO A 57  ? 0.3048 0.4078 0.1828 -0.0235 -0.0216 0.0405  92  PRO A CA  
424  C C   . PRO A 57  ? 0.3231 0.4111 0.2079 -0.0188 -0.0127 0.0352  92  PRO A C   
425  O O   . PRO A 57  ? 0.3661 0.4543 0.2424 -0.0181 -0.0042 0.0313  92  PRO A O   
426  C CB  . PRO A 57  ? 0.3678 0.4722 0.2292 -0.0299 -0.0230 0.0244  92  PRO A CB  
427  C CG  . PRO A 57  ? 0.5741 0.6904 0.4207 -0.0324 -0.0205 0.0251  92  PRO A CG  
428  C CD  . PRO A 57  ? 0.5733 0.6994 0.4325 -0.0289 -0.0234 0.0451  92  PRO A CD  
429  N N   . LEU A 58  ? 0.2627 0.3377 0.1653 -0.0155 -0.0142 0.0351  93  LEU A N   
430  C CA  . LEU A 58  ? 0.2420 0.3042 0.1563 -0.0109 -0.0081 0.0335  93  LEU A CA  
431  C C   . LEU A 58  ? 0.2943 0.3439 0.2090 -0.0114 -0.0060 0.0199  93  LEU A C   
432  O O   . LEU A 58  ? 0.2809 0.3261 0.1997 -0.0127 -0.0110 0.0166  93  LEU A O   
433  C CB  . LEU A 58  ? 0.2803 0.3387 0.2136 -0.0079 -0.0116 0.0431  93  LEU A CB  
434  C CG  . LEU A 58  ? 0.3544 0.4028 0.3009 -0.0043 -0.0076 0.0430  93  LEU A CG  
435  C CD1 . LEU A 58  ? 0.3785 0.4311 0.3237 -0.0026 -0.0008 0.0468  93  LEU A CD1 
436  C CD2 . LEU A 58  ? 0.2815 0.3276 0.2449 -0.0030 -0.0112 0.0502  93  LEU A CD2 
437  N N   . GLU A 59  ? 0.2540 0.2981 0.1673 -0.0099 0.0023  0.0132  94  GLU A N   
438  C CA  . GLU A 59  ? 0.2490 0.2812 0.1680 -0.0096 0.0054  0.0029  94  GLU A CA  
439  C C   . GLU A 59  ? 0.2571 0.2817 0.1920 -0.0064 0.0019  0.0083  94  GLU A C   
440  O O   . GLU A 59  ? 0.2562 0.2800 0.2003 -0.0033 0.0033  0.0150  94  GLU A O   
441  C CB  . GLU A 59  ? 0.2912 0.3196 0.2107 -0.0078 0.0163  -0.0029 94  GLU A CB  
442  C CG  . GLU A 59  ? 0.3460 0.3624 0.2773 -0.0065 0.0206  -0.0107 94  GLU A CG  
443  C CD  . GLU A 59  ? 0.4216 0.4339 0.3555 -0.0053 0.0332  -0.0183 94  GLU A CD  
444  O OE1 . GLU A 59  ? 0.3594 0.3777 0.2874 -0.0043 0.0391  -0.0159 94  GLU A OE1 
445  O OE2 . GLU A 59  ? 0.3263 0.3292 0.2709 -0.0049 0.0382  -0.0258 94  GLU A OE2 
446  N N   . THR A 60  ? 0.2130 0.2331 0.1508 -0.0078 -0.0027 0.0051  95  THR A N   
447  C CA  . THR A 60  ? 0.2211 0.2364 0.1698 -0.0059 -0.0066 0.0098  95  THR A CA  
448  C C   . THR A 60  ? 0.2368 0.2440 0.1925 -0.0051 -0.0041 0.0051  95  THR A C   
449  O O   . THR A 60  ? 0.2562 0.2606 0.2101 -0.0072 -0.0027 -0.0021 95  THR A O   
450  C CB  . THR A 60  ? 0.2725 0.2911 0.2206 -0.0078 -0.0131 0.0125  95  THR A CB  
451  O OG1 . THR A 60  ? 0.2364 0.2638 0.1820 -0.0081 -0.0151 0.0196  95  THR A OG1 
452  C CG2 . THR A 60  ? 0.2303 0.2440 0.1878 -0.0063 -0.0154 0.0153  95  THR A CG2 
453  N N   . SER A 61  ? 0.2034 0.2079 0.1684 -0.0025 -0.0037 0.0099  96  SER A N   
454  C CA  . SER A 61  ? 0.1841 0.1834 0.1579 -0.0013 -0.0021 0.0096  96  SER A CA  
455  C C   . SER A 61  ? 0.1940 0.1916 0.1675 -0.0028 -0.0062 0.0094  96  SER A C   
456  O O   . SER A 61  ? 0.2191 0.2193 0.1884 -0.0039 -0.0106 0.0109  96  SER A O   
457  C CB  . SER A 61  ? 0.2073 0.2081 0.1900 0.0010  -0.0026 0.0169  96  SER A CB  
458  O OG  . SER A 61  ? 0.2228 0.2249 0.2100 0.0028  0.0024  0.0181  96  SER A OG  
459  N N   . VAL A 62  ? 0.2080 0.2012 0.1887 -0.0025 -0.0036 0.0079  97  VAL A N   
460  C CA  . VAL A 62  ? 0.2003 0.1923 0.1837 -0.0032 -0.0060 0.0098  97  VAL A CA  
461  C C   . VAL A 62  ? 0.2102 0.2015 0.2043 -0.0009 -0.0038 0.0164  97  VAL A C   
462  O O   . VAL A 62  ? 0.2308 0.2186 0.2356 0.0004  0.0014  0.0160  97  VAL A O   
463  C CB  . VAL A 62  ? 0.1979 0.1868 0.1823 -0.0059 -0.0052 0.0029  97  VAL A CB  
464  C CG1 . VAL A 62  ? 0.2516 0.2398 0.2413 -0.0063 -0.0067 0.0062  97  VAL A CG1 
465  C CG2 . VAL A 62  ? 0.2185 0.2117 0.1923 -0.0088 -0.0084 -0.0019 97  VAL A CG2 
466  N N   . THR A 63  ? 0.1769 0.1724 0.1689 -0.0007 -0.0074 0.0229  98  THR A N   
467  C CA  . THR A 63  ? 0.2295 0.2288 0.2297 0.0010  -0.0071 0.0318  98  THR A CA  
468  C C   . THR A 63  ? 0.2136 0.2161 0.2117 0.0002  -0.0087 0.0368  98  THR A C   
469  O O   . THR A 63  ? 0.2093 0.2126 0.1972 -0.0016 -0.0110 0.0335  98  THR A O   
470  C CB  . THR A 63  ? 0.2389 0.2441 0.2367 0.0011  -0.0105 0.0354  98  THR A CB  
471  O OG1 . THR A 63  ? 0.2166 0.2192 0.2165 0.0021  -0.0077 0.0315  98  THR A OG1 
472  C CG2 . THR A 63  ? 0.2460 0.2582 0.2536 0.0023  -0.0117 0.0464  98  THR A CG2 
473  N N   . GLY A 64  ? 0.2046 0.2093 0.2141 0.0018  -0.0065 0.0456  99  GLY A N   
474  C CA  . GLY A 64  ? 0.2103 0.2218 0.2174 0.0013  -0.0079 0.0540  99  GLY A CA  
475  C C   . GLY A 64  ? 0.1966 0.2191 0.2060 0.0016  -0.0114 0.0654  99  GLY A C   
476  O O   . GLY A 64  ? 0.2121 0.2357 0.2302 0.0030  -0.0119 0.0679  99  GLY A O   
477  N N   . TYR A 65  ? 0.1850 0.2173 0.1864 -0.0001 -0.0140 0.0727  100 TYR A N   
478  C CA  . TYR A 65  ? 0.2225 0.2690 0.2221 -0.0014 -0.0197 0.0834  100 TYR A CA  
479  C C   . TYR A 65  ? 0.2572 0.3143 0.2619 -0.0008 -0.0190 0.0989  100 TYR A C   
480  O O   . TYR A 65  ? 0.2287 0.2886 0.2217 -0.0025 -0.0176 0.0988  100 TYR A O   
481  C CB  . TYR A 65  ? 0.2230 0.2752 0.2024 -0.0062 -0.0255 0.0755  100 TYR A CB  
482  C CG  . TYR A 65  ? 0.2258 0.2693 0.2049 -0.0062 -0.0261 0.0641  100 TYR A CG  
483  C CD1 . TYR A 65  ? 0.2064 0.2538 0.1939 -0.0060 -0.0294 0.0672  100 TYR A CD1 
484  C CD2 . TYR A 65  ? 0.1931 0.2257 0.1665 -0.0062 -0.0228 0.0523  100 TYR A CD2 
485  C CE1 . TYR A 65  ? 0.2052 0.2455 0.1935 -0.0058 -0.0289 0.0585  100 TYR A CE1 
486  C CE2 . TYR A 65  ? 0.1981 0.2246 0.1723 -0.0061 -0.0231 0.0444  100 TYR A CE2 
487  C CZ  . TYR A 65  ? 0.1962 0.2264 0.1772 -0.0058 -0.0257 0.0475  100 TYR A CZ  
488  O OH  . TYR A 65  ? 0.2198 0.2447 0.2020 -0.0055 -0.0251 0.0411  100 TYR A OH  
489  N N   . LEU A 66  ? 0.2052 0.2693 0.2290 0.0017  -0.0194 0.1136  101 LEU A N   
490  C CA  . LEU A 66  ? 0.2175 0.2929 0.2512 0.0023  -0.0180 0.1270  101 LEU A CA  
491  C C   . LEU A 66  ? 0.2948 0.3883 0.3168 -0.0023 -0.0256 0.1301  101 LEU A C   
492  O O   . LEU A 66  ? 0.2333 0.3310 0.2577 -0.0036 -0.0305 0.1294  101 LEU A O   
493  C CB  . LEU A 66  ? 0.2577 0.3301 0.3239 0.0070  -0.0125 0.1363  101 LEU A CB  
494  C CG  . LEU A 66  ? 0.2963 0.3775 0.3817 0.0088  -0.0082 0.1495  101 LEU A CG  
495  C CD1 . LEU A 66  ? 0.1903 0.2630 0.2736 0.0096  -0.0025 0.1473  101 LEU A CD1 
496  C CD2 . LEU A 66  ? 0.1959 0.2744 0.3154 0.0129  -0.0024 0.1562  101 LEU A CD2 
497  N N   . VAL A 67  ? 0.2318 0.3356 0.2411 -0.0050 -0.0262 0.1334  102 VAL A N   
498  C CA  . VAL A 67  ? 0.2156 0.3373 0.2128 -0.0101 -0.0329 0.1365  102 VAL A CA  
499  C C   . VAL A 67  ? 0.3040 0.4400 0.3159 -0.0089 -0.0311 0.1533  102 VAL A C   
500  O O   . VAL A 67  ? 0.2617 0.3974 0.2718 -0.0074 -0.0260 0.1567  102 VAL A O   
501  C CB  . VAL A 67  ? 0.2328 0.3554 0.1990 -0.0153 -0.0347 0.1236  102 VAL A CB  
502  C CG1 . VAL A 67  ? 0.2517 0.3923 0.2048 -0.0215 -0.0419 0.1249  102 VAL A CG1 
503  C CG2 . VAL A 67  ? 0.2691 0.3774 0.2250 -0.0160 -0.0351 0.1076  102 VAL A CG2 
504  N N   . ASN A 68  ? 0.2762 0.4255 0.3047 -0.0095 -0.0349 0.1650  103 ASN A N   
505  C CA  . ASN A 68  ? 0.2268 0.3949 0.2686 -0.0097 -0.0349 0.1825  103 ASN A CA  
506  C C   . ASN A 68  ? 0.2893 0.4761 0.3092 -0.0170 -0.0435 0.1831  103 ASN A C   
507  O O   . ASN A 68  ? 0.2893 0.4835 0.3105 -0.0204 -0.0502 0.1835  103 ASN A O   
508  C CB  . ASN A 68  ? 0.2800 0.4523 0.3585 -0.0058 -0.0325 0.1967  103 ASN A CB  
509  C CG  . ASN A 68  ? 0.2747 0.4637 0.3739 -0.0043 -0.0295 0.2159  103 ASN A CG  
510  O OD1 . ASN A 68  ? 0.2747 0.4800 0.3583 -0.0081 -0.0332 0.2218  103 ASN A OD1 
511  N ND2 . ASN A 68  ? 0.2476 0.4336 0.3831 0.0011  -0.0223 0.2257  103 ASN A ND2 
512  N N   . THR A 69  ? 0.2596 0.4540 0.2593 -0.0195 -0.0429 0.1826  104 THR A N   
513  C CA  . THR A 69  ? 0.2973 0.5095 0.2735 -0.0270 -0.0502 0.1816  104 THR A CA  
514  C C   . THR A 69  ? 0.3214 0.5586 0.3131 -0.0289 -0.0543 0.2025  104 THR A C   
515  O O   . THR A 69  ? 0.4041 0.6588 0.3783 -0.0358 -0.0616 0.2034  104 THR A O   
516  C CB  . THR A 69  ? 0.3724 0.5833 0.3211 -0.0290 -0.0464 0.1731  104 THR A CB  
517  O OG1 . THR A 69  ? 0.3717 0.5910 0.3326 -0.0254 -0.0409 0.1888  104 THR A OG1 
518  C CG2 . THR A 69  ? 0.2840 0.4712 0.2221 -0.0267 -0.0408 0.1551  104 THR A CG2 
519  N N   . GLY A 70  ? 0.2941 0.5338 0.3194 -0.0231 -0.0496 0.2191  105 GLY A N   
520  C CA  . GLY A 70  ? 0.3114 0.5757 0.3560 -0.0239 -0.0515 0.2416  105 GLY A CA  
521  C C   . GLY A 70  ? 0.4127 0.6845 0.4599 -0.0211 -0.0454 0.2521  105 GLY A C   
522  O O   . GLY A 70  ? 0.4446 0.7308 0.5215 -0.0182 -0.0428 0.2725  105 GLY A O   
523  N N   . SER A 71  ? 0.3508 0.6132 0.3698 -0.0217 -0.0424 0.2392  106 SER A N   
524  C CA  . SER A 71  ? 0.3229 0.5898 0.3434 -0.0187 -0.0356 0.2480  106 SER A CA  
525  C C   . SER A 71  ? 0.3469 0.5889 0.3718 -0.0127 -0.0262 0.2380  106 SER A C   
526  O O   . SER A 71  ? 0.3148 0.5584 0.3545 -0.0083 -0.0192 0.2483  106 SER A O   
527  C CB  . SER A 71  ? 0.5393 0.8196 0.5229 -0.0250 -0.0385 0.2439  106 SER A CB  
528  O OG  . SER A 71  ? 0.6855 0.9532 0.6376 -0.0298 -0.0415 0.2211  106 SER A OG  
529  N N   . LYS A 72  ? 0.3079 0.5282 0.3211 -0.0127 -0.0259 0.2189  107 LYS A N   
530  C CA  . LYS A 72  ? 0.3292 0.5266 0.3464 -0.0079 -0.0178 0.2093  107 LYS A CA  
531  C C   . LYS A 72  ? 0.3041 0.4837 0.3338 -0.0056 -0.0183 0.1999  107 LYS A C   
532  O O   . LYS A 72  ? 0.3060 0.4867 0.3269 -0.0090 -0.0250 0.1932  107 LYS A O   
533  C CB  . LYS A 72  ? 0.3075 0.4966 0.2902 -0.0110 -0.0156 0.1935  107 LYS A CB  
534  C CG  . LYS A 72  ? 0.4638 0.6670 0.4326 -0.0126 -0.0124 0.2011  107 LYS A CG  
535  C CD  . LYS A 72  ? 0.5819 0.7798 0.5728 -0.0065 -0.0030 0.2112  107 LYS A CD  
536  C CE  . LYS A 72  ? 0.6369 0.8523 0.6189 -0.0075 0.0002  0.2230  107 LYS A CE  
537  N NZ  . LYS A 72  ? 0.5317 0.7422 0.4781 -0.0114 0.0039  0.2089  107 LYS A NZ  
538  N N   . LEU A 73  ? 0.2580 0.4214 0.3089 -0.0001 -0.0108 0.1991  108 LEU A N   
539  C CA  . LEU A 73  ? 0.2627 0.4069 0.3229 0.0021  -0.0097 0.1886  108 LEU A CA  
540  C C   . LEU A 73  ? 0.2357 0.3617 0.2784 0.0022  -0.0057 0.1738  108 LEU A C   
541  O O   . LEU A 73  ? 0.2366 0.3563 0.2883 0.0048  0.0013  0.1760  108 LEU A O   
542  C CB  . LEU A 73  ? 0.2649 0.4047 0.3648 0.0076  -0.0036 0.1983  108 LEU A CB  
543  C CG  . LEU A 73  ? 0.2406 0.3619 0.3528 0.0100  -0.0015 0.1884  108 LEU A CG  
544  C CD1 . LEU A 73  ? 0.2405 0.3679 0.3453 0.0072  -0.0091 0.1862  108 LEU A CD1 
545  C CD2 . LEU A 73  ? 0.2228 0.3390 0.3749 0.0150  0.0070  0.1960  108 LEU A CD2 
546  N N   . VAL A 74  ? 0.2119 0.3308 0.2319 -0.0010 -0.0100 0.1593  109 VAL A N   
547  C CA  . VAL A 74  ? 0.2558 0.3609 0.2574 -0.0020 -0.0071 0.1455  109 VAL A CA  
548  C C   . VAL A 74  ? 0.2816 0.3706 0.2897 -0.0005 -0.0075 0.1363  109 VAL A C   
549  O O   . VAL A 74  ? 0.2612 0.3522 0.2711 -0.0011 -0.0129 0.1347  109 VAL A O   
550  C CB  . VAL A 74  ? 0.2759 0.3883 0.2449 -0.0077 -0.0110 0.1356  109 VAL A CB  
551  C CG1 . VAL A 74  ? 0.2582 0.3574 0.2119 -0.0086 -0.0066 0.1217  109 VAL A CG1 
552  C CG2 . VAL A 74  ? 0.3037 0.4328 0.2643 -0.0096 -0.0104 0.1447  109 VAL A CG2 
553  N N   . LEU A 75  ? 0.2133 0.2874 0.2261 0.0014  -0.0018 0.1309  110 LEU A N   
554  C CA  . LEU A 75  ? 0.1911 0.2499 0.2080 0.0023  -0.0020 0.1202  110 LEU A CA  
555  C C   . LEU A 75  ? 0.2108 0.2624 0.2072 -0.0006 -0.0020 0.1024  110 LEU A C   
556  O O   . LEU A 75  ? 0.2121 0.2614 0.2056 -0.0009 0.0028  0.1006  110 LEU A O   
557  C CB  . LEU A 75  ? 0.2061 0.2515 0.2505 0.0058  0.0048  0.1203  110 LEU A CB  
558  C CG  . LEU A 75  ? 0.1923 0.2216 0.2393 0.0056  0.0055  0.1021  110 LEU A CG  
559  C CD1 . LEU A 75  ? 0.1857 0.2155 0.2309 0.0059  0.0011  0.0987  110 LEU A CD1 
560  C CD2 . LEU A 75  ? 0.2515 0.2692 0.3243 0.0075  0.0124  0.1009  110 LEU A CD2 
561  N N   . VAL A 76  ? 0.1866 0.2350 0.1722 -0.0024 -0.0068 0.0906  111 VAL A N   
562  C CA  . VAL A 76  ? 0.1998 0.2412 0.1711 -0.0046 -0.0065 0.0749  111 VAL A CA  
563  C C   . VAL A 76  ? 0.2248 0.2521 0.2072 -0.0029 -0.0053 0.0653  111 VAL A C   
564  O O   . VAL A 76  ? 0.2033 0.2280 0.1897 -0.0022 -0.0081 0.0626  111 VAL A O   
565  C CB  . VAL A 76  ? 0.2398 0.2878 0.1930 -0.0084 -0.0121 0.0686  111 VAL A CB  
566  C CG1 . VAL A 76  ? 0.2609 0.3002 0.2052 -0.0101 -0.0102 0.0532  111 VAL A CG1 
567  C CG2 . VAL A 76  ? 0.2293 0.2936 0.1683 -0.0116 -0.0139 0.0771  111 VAL A CG2 
568  N N   . ASP A 77  ? 0.2050 0.2249 0.1924 -0.0025 -0.0011 0.0605  112 ASP A N   
569  C CA  . ASP A 77  ? 0.2001 0.2093 0.1972 -0.0020 -0.0004 0.0519  112 ASP A CA  
570  C C   . ASP A 77  ? 0.2206 0.2253 0.2360 -0.0001 0.0018  0.0553  112 ASP A C   
571  O O   . ASP A 77  ? 0.2229 0.2322 0.2451 0.0015  0.0019  0.0645  112 ASP A O   
572  C CB  . ASP A 77  ? 0.2142 0.2205 0.2017 -0.0032 -0.0042 0.0416  112 ASP A CB  
573  C CG  . ASP A 77  ? 0.2495 0.2570 0.2258 -0.0049 -0.0040 0.0364  112 ASP A CG  
574  O OD1 . ASP A 77  ? 0.2308 0.2404 0.2064 -0.0052 -0.0001 0.0391  112 ASP A OD1 
575  O OD2 . ASP A 77  ? 0.2763 0.2827 0.2462 -0.0059 -0.0066 0.0302  112 ASP A OD2 
576  N N   . THR A 78  ? 0.2076 0.2040 0.2329 -0.0008 0.0038  0.0479  113 THR A N   
577  C CA  . THR A 78  ? 0.1908 0.1815 0.2366 0.0001  0.0080  0.0492  113 THR A CA  
578  C C   . THR A 78  ? 0.1843 0.1672 0.2326 -0.0016 0.0080  0.0362  113 THR A C   
579  O O   . THR A 78  ? 0.2113 0.1877 0.2769 -0.0020 0.0126  0.0332  113 THR A O   
580  C CB  . THR A 78  ? 0.2375 0.2267 0.2980 -0.0003 0.0124  0.0539  113 THR A CB  
581  O OG1 . THR A 78  ? 0.2363 0.2216 0.2945 -0.0033 0.0109  0.0437  113 THR A OG1 
582  C CG2 . THR A 78  ? 0.2224 0.2211 0.2780 0.0011  0.0135  0.0673  113 THR A CG2 
583  N N   . GLY A 79  ? 0.2002 0.1838 0.2324 -0.0030 0.0036  0.0282  114 GLY A N   
584  C CA  . GLY A 79  ? 0.2156 0.1944 0.2469 -0.0054 0.0034  0.0164  114 GLY A CA  
585  C C   . GLY A 79  ? 0.2590 0.2355 0.2947 -0.0092 0.0025  0.0092  114 GLY A C   
586  O O   . GLY A 79  ? 0.2290 0.2073 0.2683 -0.0096 0.0019  0.0136  114 GLY A O   
587  N N   . ALA A 80  ? 0.2320 0.2054 0.2674 -0.0125 0.0025  -0.0022 115 ALA A N   
588  C CA  . ALA A 80  ? 0.2325 0.2068 0.2685 -0.0178 -0.0011 -0.0105 115 ALA A CA  
589  C C   . ALA A 80  ? 0.2529 0.2206 0.3076 -0.0211 0.0033  -0.0175 115 ALA A C   
590  O O   . ALA A 80  ? 0.2594 0.2287 0.3171 -0.0264 -0.0004 -0.0244 115 ALA A O   
591  C CB  . ALA A 80  ? 0.2354 0.2140 0.2550 -0.0210 -0.0055 -0.0192 115 ALA A CB  
592  N N   . ALA A 81  ? 0.2200 0.1809 0.2899 -0.0185 0.0109  -0.0159 116 ALA A N   
593  C CA  . ALA A 81  ? 0.2655 0.2181 0.3561 -0.0221 0.0169  -0.0254 116 ALA A CA  
594  C C   . ALA A 81  ? 0.2679 0.2212 0.3464 -0.0290 0.0140  -0.0436 116 ALA A C   
595  O O   . ALA A 81  ? 0.2961 0.2521 0.3566 -0.0286 0.0132  -0.0478 116 ALA A O   
596  C CB  . ALA A 81  ? 0.2956 0.2467 0.4069 -0.0229 0.0182  -0.0190 116 ALA A CB  
597  N N   . GLY A 82  ? 0.2913 0.2438 0.3779 -0.0360 0.0118  -0.0539 117 GLY A N   
598  C CA  . GLY A 82  ? 0.3188 0.2754 0.3910 -0.0439 0.0073  -0.0708 117 GLY A CA  
599  C C   . GLY A 82  ? 0.3685 0.3379 0.4242 -0.0477 -0.0048 -0.0687 117 GLY A C   
600  O O   . GLY A 82  ? 0.3544 0.3301 0.3999 -0.0558 -0.0102 -0.0814 117 GLY A O   
601  N N   . LEU A 83  ? 0.3630 0.3374 0.4167 -0.0426 -0.0088 -0.0530 118 LEU A N   
602  C CA  . LEU A 83  ? 0.2621 0.2482 0.3075 -0.0455 -0.0189 -0.0489 118 LEU A CA  
603  C C   . LEU A 83  ? 0.4313 0.4272 0.4527 -0.0469 -0.0248 -0.0508 118 LEU A C   
604  O O   . LEU A 83  ? 0.4189 0.4265 0.4348 -0.0514 -0.0339 -0.0498 118 LEU A O   
605  C CB  . LEU A 83  ? 0.2533 0.2407 0.3039 -0.0391 -0.0189 -0.0328 118 LEU A CB  
606  C CG  . LEU A 83  ? 0.3231 0.3045 0.3960 -0.0369 -0.0135 -0.0261 118 LEU A CG  
607  C CD1 . LEU A 83  ? 0.3021 0.2881 0.3742 -0.0322 -0.0143 -0.0125 118 LEU A CD1 
608  C CD2 . LEU A 83  ? 0.4083 0.3894 0.4989 -0.0442 -0.0155 -0.0344 118 LEU A CD2 
609  N N   . PHE A 84  ? 0.3012 0.2940 0.3104 -0.0431 -0.0200 -0.0516 119 PHE A N   
610  C CA  . PHE A 84  ? 0.3548 0.3573 0.3432 -0.0429 -0.0246 -0.0492 119 PHE A CA  
611  C C   . PHE A 84  ? 0.4289 0.4316 0.4037 -0.0465 -0.0208 -0.0622 119 PHE A C   
612  O O   . PHE A 84  ? 0.6116 0.6185 0.5716 -0.0439 -0.0199 -0.0590 119 PHE A O   
613  C CB  . PHE A 84  ? 0.3330 0.3341 0.3188 -0.0348 -0.0226 -0.0358 119 PHE A CB  
614  C CG  . PHE A 84  ? 0.5855 0.5978 0.5604 -0.0342 -0.0294 -0.0276 119 PHE A CG  
615  C CD1 . PHE A 84  ? 0.7666 0.7845 0.7492 -0.0344 -0.0349 -0.0194 119 PHE A CD1 
616  C CD2 . PHE A 84  ? 0.6836 0.7007 0.6437 -0.0332 -0.0291 -0.0267 119 PHE A CD2 
617  C CE1 . PHE A 84  ? 0.8733 0.9012 0.8511 -0.0334 -0.0401 -0.0105 119 PHE A CE1 
618  C CE2 . PHE A 84  ? 0.7177 0.7453 0.6719 -0.0324 -0.0347 -0.0172 119 PHE A CE2 
619  C CZ  . PHE A 84  ? 0.8604 0.8932 0.8244 -0.0325 -0.0402 -0.0090 119 PHE A CZ  
620  N N   . GLY A 85  ? 0.3442 0.3421 0.3249 -0.0526 -0.0175 -0.0774 120 GLY A N   
621  C CA  . GLY A 85  ? 0.3921 0.3901 0.3594 -0.0571 -0.0124 -0.0927 120 GLY A CA  
622  C C   . GLY A 85  ? 0.5537 0.5369 0.5319 -0.0524 0.0013  -0.0978 120 GLY A C   
623  O O   . GLY A 85  ? 0.3415 0.3161 0.3367 -0.0450 0.0059  -0.0870 120 GLY A O   
624  N N   . PRO A 86  ? 0.4366 0.4182 0.4054 -0.0566 0.0084  -0.1138 121 PRO A N   
625  C CA  . PRO A 86  ? 0.4133 0.3800 0.3986 -0.0529 0.0232  -0.1209 121 PRO A CA  
626  C C   . PRO A 86  ? 0.3733 0.3374 0.3593 -0.0433 0.0293  -0.1079 121 PRO A C   
627  O O   . PRO A 86  ? 0.4148 0.3674 0.4207 -0.0388 0.0407  -0.1086 121 PRO A O   
628  C CB  . PRO A 86  ? 0.4046 0.3719 0.3775 -0.0618 0.0291  -0.1445 121 PRO A CB  
629  C CG  . PRO A 86  ? 0.4776 0.4636 0.4186 -0.0669 0.0181  -0.1436 121 PRO A CG  
630  C CD  . PRO A 86  ? 0.4826 0.4775 0.4250 -0.0649 0.0040  -0.1255 121 PRO A CD  
631  N N   . THR A 87  ? 0.3106 0.2851 0.2790 -0.0400 0.0222  -0.0953 122 THR A N   
632  C CA  . THR A 87  ? 0.3201 0.2928 0.2908 -0.0318 0.0275  -0.0838 122 THR A CA  
633  C C   . THR A 87  ? 0.3225 0.2912 0.3105 -0.0250 0.0249  -0.0670 122 THR A C   
634  O O   . THR A 87  ? 0.2942 0.2615 0.2880 -0.0187 0.0288  -0.0573 122 THR A O   
635  C CB  . THR A 87  ? 0.3411 0.3263 0.2882 -0.0315 0.0226  -0.0780 122 THR A CB  
636  O OG1 . THR A 87  ? 0.3495 0.3430 0.2916 -0.0311 0.0105  -0.0656 122 THR A OG1 
637  C CG2 . THR A 87  ? 0.3550 0.3480 0.2808 -0.0392 0.0241  -0.0933 122 THR A CG2 
638  N N   . LEU A 88  ? 0.2694 0.2377 0.2655 -0.0264 0.0187  -0.0631 123 LEU A N   
639  C CA  . LEU A 88  ? 0.2405 0.2068 0.2501 -0.0208 0.0167  -0.0480 123 LEU A CA  
640  C C   . LEU A 88  ? 0.2662 0.2229 0.3008 -0.0205 0.0229  -0.0493 123 LEU A C   
641  O O   . LEU A 88  ? 0.3524 0.3022 0.3964 -0.0242 0.0299  -0.0627 123 LEU A O   
642  C CB  . LEU A 88  ? 0.2589 0.2333 0.2585 -0.0215 0.0061  -0.0398 123 LEU A CB  
643  C CG  . LEU A 88  ? 0.3167 0.3001 0.2973 -0.0207 0.0010  -0.0355 123 LEU A CG  
644  C CD1 . LEU A 88  ? 0.2879 0.2782 0.2643 -0.0211 -0.0077 -0.0275 123 LEU A CD1 
645  C CD2 . LEU A 88  ? 0.3205 0.3028 0.3021 -0.0149 0.0049  -0.0275 123 LEU A CD2 
646  N N   . GLY A 89  ? 0.2419 0.1985 0.2879 -0.0164 0.0211  -0.0353 124 GLY A N   
647  C CA  . GLY A 89  ? 0.2309 0.1801 0.3029 -0.0154 0.0272  -0.0323 124 GLY A CA  
648  C C   . GLY A 89  ? 0.2588 0.2025 0.3505 -0.0103 0.0367  -0.0264 124 GLY A C   
649  O O   . GLY A 89  ? 0.2907 0.2270 0.4085 -0.0099 0.0441  -0.0261 124 GLY A O   
650  N N   . ARG A 90  ? 0.2313 0.1790 0.3147 -0.0063 0.0369  -0.0204 125 ARG A N   
651  C CA  . ARG A 90  ? 0.2370 0.1816 0.3412 -0.0011 0.0453  -0.0126 125 ARG A CA  
652  C C   . ARG A 90  ? 0.2186 0.1694 0.3342 0.0038  0.0421  0.0085  125 ARG A C   
653  O O   . ARG A 90  ? 0.2341 0.1845 0.3718 0.0082  0.0483  0.0186  125 ARG A O   
654  C CB  . ARG A 90  ? 0.2890 0.2360 0.3813 0.0005  0.0473  -0.0159 125 ARG A CB  
655  C CG  . ARG A 90  ? 0.2946 0.2394 0.3692 -0.0047 0.0495  -0.0352 125 ARG A CG  
656  C CD  . ARG A 90  ? 0.5019 0.4358 0.5956 -0.0058 0.0634  -0.0487 125 ARG A CD  
657  N NE  . ARG A 90  ? 0.6372 0.5707 0.7118 -0.0109 0.0673  -0.0676 125 ARG A NE  
658  C CZ  . ARG A 90  ? 0.4086 0.3459 0.4612 -0.0181 0.0607  -0.0799 125 ARG A CZ  
659  N NH1 . ARG A 90  ? 0.4175 0.3579 0.4677 -0.0209 0.0507  -0.0765 125 ARG A NH1 
660  N NH2 . ARG A 90  ? 0.5279 0.4675 0.5616 -0.0228 0.0645  -0.0955 125 ARG A NH2 
661  N N   . LEU A 91  ? 0.2483 0.2060 0.3505 0.0030  0.0333  0.0156  126 LEU A N   
662  C CA  . LEU A 91  ? 0.2369 0.2036 0.3421 0.0066  0.0294  0.0344  126 LEU A CA  
663  C C   . LEU A 91  ? 0.1985 0.1638 0.3342 0.0096  0.0360  0.0471  126 LEU A C   
664  O O   . LEU A 91  ? 0.2117 0.1844 0.3582 0.0134  0.0360  0.0630  126 LEU A O   
665  C CB  . LEU A 91  ? 0.2018 0.1751 0.2867 0.0046  0.0210  0.0373  126 LEU A CB  
666  C CG  . LEU A 91  ? 0.2150 0.1995 0.2978 0.0070  0.0168  0.0545  126 LEU A CG  
667  C CD1 . LEU A 91  ? 0.2229 0.2141 0.2793 0.0051  0.0089  0.0524  126 LEU A CD1 
668  C CD2 . LEU A 91  ? 0.2305 0.2170 0.3276 0.0078  0.0194  0.0658  126 LEU A CD2 
669  N N   . LEU A 92  ? 0.2322 0.1893 0.3842 0.0077  0.0414  0.0417  127 LEU A N   
670  C CA  . LEU A 92  ? 0.2002 0.1561 0.3851 0.0108  0.0483  0.0557  127 LEU A CA  
671  C C   . LEU A 92  ? 0.2008 0.1527 0.4120 0.0147  0.0573  0.0596  127 LEU A C   
672  O O   . LEU A 92  ? 0.2700 0.2289 0.5025 0.0193  0.0592  0.0800  127 LEU A O   
673  C CB  . LEU A 92  ? 0.3146 0.2608 0.5145 0.0072  0.0530  0.0463  127 LEU A CB  
674  C CG  . LEU A 92  ? 0.4993 0.4521 0.6997 0.0070  0.0494  0.0590  127 LEU A CG  
675  C CD1 . LEU A 92  ? 0.4252 0.3862 0.6468 0.0123  0.0525  0.0836  127 LEU A CD1 
676  C CD2 . LEU A 92  ? 0.5678 0.5294 0.7323 0.0053  0.0390  0.0577  127 LEU A CD2 
677  N N   . ALA A 93  ? 0.2319 0.1740 0.4422 0.0129  0.0631  0.0410  128 ALA A N   
678  C CA  . ALA A 93  ? 0.2823 0.2195 0.5186 0.0168  0.0737  0.0428  128 ALA A CA  
679  C C   . ALA A 93  ? 0.2149 0.1647 0.4460 0.0213  0.0685  0.0592  128 ALA A C   
680  O O   . ALA A 93  ? 0.2771 0.2329 0.5348 0.0254  0.0736  0.0728  128 ALA A O   
681  C CB  . ALA A 93  ? 0.3024 0.2278 0.5326 0.0132  0.0814  0.0173  128 ALA A CB  
682  N N   . ASN A 94  ? 0.2260 0.1841 0.4223 0.0193  0.0574  0.0570  129 ASN A N   
683  C CA  . ASN A 94  ? 0.2416 0.2122 0.4327 0.0223  0.0514  0.0708  129 ASN A CA  
684  C C   . ASN A 94  ? 0.2010 0.1855 0.3997 0.0243  0.0447  0.0943  129 ASN A C   
685  O O   . ASN A 94  ? 0.2479 0.2433 0.4592 0.0273  0.0426  0.1106  129 ASN A O   
686  C CB  . ASN A 94  ? 0.1946 0.1687 0.3498 0.0191  0.0428  0.0603  129 ASN A CB  
687  C CG  . ASN A 94  ? 0.2593 0.2248 0.4098 0.0183  0.0499  0.0430  129 ASN A CG  
688  O OD1 . ASN A 94  ? 0.2619 0.2228 0.4350 0.0214  0.0601  0.0432  129 ASN A OD1 
689  N ND2 . ASN A 94  ? 0.2231 0.1870 0.3452 0.0142  0.0453  0.0288  129 ASN A ND2 
690  N N   . LEU A 95  ? 0.2421 0.2280 0.4335 0.0223  0.0412  0.0970  130 LEU A N   
691  C CA  . LEU A 95  ? 0.2080 0.2093 0.4063 0.0236  0.0366  0.1182  130 LEU A CA  
692  C C   . LEU A 95  ? 0.1980 0.2068 0.4322 0.0263  0.0445  0.1273  130 LEU A C   
693  O O   . LEU A 95  ? 0.2401 0.2678 0.4821 0.0272  0.0406  0.1429  130 LEU A O   
694  C CB  . LEU A 95  ? 0.2211 0.2206 0.4088 0.0211  0.0349  0.1175  130 LEU A CB  
695  C CG  . LEU A 95  ? 0.2501 0.2684 0.4413 0.0214  0.0317  0.1337  130 LEU A CG  
696  C CD1 . LEU A 95  ? 0.4290 0.4649 0.5971 0.0200  0.0213  0.1424  130 LEU A CD1 
697  C CD2 . LEU A 95  ? 0.3914 0.4053 0.5756 0.0195  0.0326  0.1313  130 LEU A CD2 
698  N N   . LYS A 96  ? 0.2240 0.2191 0.4815 0.0268  0.0559  0.1169  131 LYS A N   
699  C CA  . LYS A 96  ? 0.2485 0.2502 0.5439 0.0291  0.0654  0.1247  131 LYS A CA  
700  C C   . LYS A 96  ? 0.2368 0.2441 0.5433 0.0310  0.0677  0.1290  131 LYS A C   
701  O O   . LYS A 96  ? 0.2149 0.2388 0.5449 0.0325  0.0688  0.1455  131 LYS A O   
702  C CB  . LYS A 96  ? 0.2569 0.2423 0.5732 0.0278  0.0775  0.1092  131 LYS A CB  
703  C CG  . LYS A 96  ? 0.3712 0.3569 0.6890 0.0264  0.0764  0.1108  131 LYS A CG  
704  C CD  . LYS A 96  ? 0.3788 0.3465 0.7069 0.0230  0.0851  0.0898  131 LYS A CD  
705  C CE  . LYS A 96  ? 0.3854 0.3540 0.7144 0.0213  0.0828  0.0918  131 LYS A CE  
706  N NZ  . LYS A 96  ? 0.4614 0.4128 0.7881 0.0161  0.0866  0.0684  131 LYS A NZ  
707  N N   . ALA A 97  ? 0.2157 0.2104 0.5069 0.0308  0.0687  0.1150  132 ALA A N   
708  C CA  . ALA A 97  ? 0.1946 0.1946 0.4959 0.0326  0.0712  0.1190  132 ALA A CA  
709  C C   . ALA A 97  ? 0.2748 0.2965 0.5666 0.0325  0.0584  0.1374  132 ALA A C   
710  O O   . ALA A 97  ? 0.2218 0.2558 0.5338 0.0333  0.0601  0.1487  132 ALA A O   
711  C CB  . ALA A 97  ? 0.2727 0.2559 0.5567 0.0326  0.0746  0.1001  132 ALA A CB  
712  N N   . ALA A 98  ? 0.2334 0.2607 0.4950 0.0304  0.0461  0.1399  133 ALA A N   
713  C CA  . ALA A 98  ? 0.2257 0.2741 0.4743 0.0283  0.0336  0.1541  133 ALA A CA  
714  C C   . ALA A 98  ? 0.2370 0.3047 0.5050 0.0278  0.0326  0.1720  133 ALA A C   
715  O O   . ALA A 98  ? 0.2406 0.3272 0.4973 0.0248  0.0224  0.1833  133 ALA A O   
716  C CB  . ALA A 98  ? 0.1923 0.2402 0.4016 0.0252  0.0224  0.1484  133 ALA A CB  
717  N N   . GLY A 99  ? 0.2392 0.3033 0.5364 0.0300  0.0432  0.1744  134 GLY A N   
718  C CA  . GLY A 99  ? 0.2291 0.3125 0.5518 0.0302  0.0443  0.1933  134 GLY A CA  
719  C C   . GLY A 99  ? 0.2620 0.3519 0.5748 0.0294  0.0406  0.1989  134 GLY A C   
720  O O   . GLY A 99  ? 0.2473 0.3570 0.5767 0.0292  0.0395  0.2166  134 GLY A O   
721  N N   . TYR A 100 ? 0.2045 0.2795 0.4926 0.0287  0.0392  0.1855  135 TYR A N   
722  C CA  . TYR A 100 ? 0.2639 0.3440 0.5425 0.0279  0.0369  0.1900  135 TYR A CA  
723  C C   . TYR A 100 ? 0.2526 0.3142 0.5456 0.0294  0.0467  0.1791  135 TYR A C   
724  O O   . TYR A 100 ? 0.3513 0.3934 0.6481 0.0296  0.0529  0.1631  135 TYR A O   
725  C CB  . TYR A 100 ? 0.2450 0.3261 0.4797 0.0243  0.0260  0.1845  135 TYR A CB  
726  C CG  . TYR A 100 ? 0.2592 0.3602 0.4770 0.0212  0.0155  0.1938  135 TYR A CG  
727  C CD1 . TYR A 100 ? 0.2654 0.3885 0.4853 0.0196  0.0116  0.2098  135 TYR A CD1 
728  C CD2 . TYR A 100 ? 0.2362 0.3345 0.4366 0.0193  0.0095  0.1862  135 TYR A CD2 
729  C CE1 . TYR A 100 ? 0.2863 0.4277 0.4901 0.0154  0.0018  0.2168  135 TYR A CE1 
730  C CE2 . TYR A 100 ? 0.2868 0.4031 0.4727 0.0153  -0.0003 0.1931  135 TYR A CE2 
731  C CZ  . TYR A 100 ? 0.2092 0.3468 0.3964 0.0129  -0.0042 0.2077  135 TYR A CZ  
732  O OH  . TYR A 100 ? 0.3283 0.4839 0.5007 0.0078  -0.0140 0.2136  135 TYR A OH  
733  N N   . GLN A 101 ? 0.2850 0.3536 0.5859 0.0299  0.0483  0.1872  136 GLN A N   
734  C CA  . GLN A 101 ? 0.2337 0.2865 0.5458 0.0302  0.0560  0.1768  136 GLN A CA  
735  C C   . GLN A 101 ? 0.2046 0.2545 0.4854 0.0278  0.0500  0.1728  136 GLN A C   
736  O O   . GLN A 101 ? 0.2709 0.3361 0.5300 0.0267  0.0422  0.1830  136 GLN A O   
737  C CB  . GLN A 101 ? 0.2595 0.3224 0.6131 0.0331  0.0646  0.1897  136 GLN A CB  
738  C CG  . GLN A 101 ? 0.2675 0.3317 0.6582 0.0352  0.0736  0.1924  136 GLN A CG  
739  C CD  . GLN A 101 ? 0.4176 0.4577 0.8148 0.0340  0.0821  0.1699  136 GLN A CD  
740  O OE1 . GLN A 101 ? 0.3975 0.4211 0.7874 0.0319  0.0846  0.1540  136 GLN A OE1 
741  N NE2 . GLN A 101 ? 0.5547 0.5935 0.9653 0.0346  0.0868  0.1682  136 GLN A NE2 
742  N N   . PRO A 102 ? 0.2141 0.2450 0.4921 0.0261  0.0537  0.1571  137 PRO A N   
743  C CA  . PRO A 102 ? 0.2608 0.2885 0.5110 0.0234  0.0489  0.1531  137 PRO A CA  
744  C C   . PRO A 102 ? 0.2718 0.3161 0.5242 0.0246  0.0483  0.1687  137 PRO A C   
745  O O   . PRO A 102 ? 0.2904 0.3404 0.5141 0.0227  0.0428  0.1706  137 PRO A O   
746  C CB  . PRO A 102 ? 0.3610 0.3680 0.6218 0.0211  0.0549  0.1354  137 PRO A CB  
747  C CG  . PRO A 102 ? 0.4953 0.4916 0.7709 0.0214  0.0598  0.1247  137 PRO A CG  
748  C CD  . PRO A 102 ? 0.2746 0.2867 0.5744 0.0256  0.0628  0.1410  137 PRO A CD  
749  N N   . GLU A 103 ? 0.2179 0.2708 0.5052 0.0279  0.0548  0.1799  138 GLU A N   
750  C CA  . GLU A 103 ? 0.2701 0.3396 0.5630 0.0296  0.0553  0.1960  138 GLU A CA  
751  C C   . GLU A 103 ? 0.2372 0.3285 0.5082 0.0291  0.0472  0.2104  138 GLU A C   
752  O O   . GLU A 103 ? 0.2493 0.3543 0.5123 0.0293  0.0460  0.2213  138 GLU A O   
753  C CB  . GLU A 103 ? 0.3592 0.4334 0.6989 0.0334  0.0648  0.2052  138 GLU A CB  
754  C CG  . GLU A 103 ? 0.3122 0.3658 0.6790 0.0330  0.0737  0.1885  138 GLU A CG  
755  C CD  . GLU A 103 ? 0.5809 0.6234 0.9506 0.0319  0.0752  0.1765  138 GLU A CD  
756  O OE1 . GLU A 103 ? 0.6316 0.6559 1.0132 0.0299  0.0813  0.1585  138 GLU A OE1 
757  O OE2 . GLU A 103 ? 0.6439 0.6965 1.0029 0.0326  0.0702  0.1844  138 GLU A OE2 
758  N N   . GLN A 104 ? 0.2415 0.3367 0.5023 0.0279  0.0417  0.2098  139 GLN A N   
759  C CA  . GLN A 104 ? 0.2168 0.3329 0.4559 0.0259  0.0330  0.2208  139 GLN A CA  
760  C C   . GLN A 104 ? 0.2728 0.3862 0.4668 0.0217  0.0257  0.2108  139 GLN A C   
761  O O   . GLN A 104 ? 0.2719 0.4026 0.4445 0.0189  0.0192  0.2177  139 GLN A O   
762  C CB  . GLN A 104 ? 0.2582 0.3800 0.5063 0.0257  0.0299  0.2237  139 GLN A CB  
763  C CG  . GLN A 104 ? 0.2600 0.3875 0.5548 0.0295  0.0379  0.2349  139 GLN A CG  
764  C CD  . GLN A 104 ? 0.2888 0.4222 0.5935 0.0290  0.0357  0.2382  139 GLN A CD  
765  O OE1 . GLN A 104 ? 0.2760 0.3928 0.5773 0.0289  0.0371  0.2241  139 GLN A OE1 
766  N NE2 . GLN A 104 ? 0.2967 0.4546 0.6157 0.0285  0.0328  0.2575  139 GLN A NE2 
767  N N   . VAL A 105 ? 0.2134 0.3065 0.3937 0.0205  0.0271  0.1943  140 VAL A N   
768  C CA  . VAL A 105 ? 0.2687 0.3591 0.4096 0.0166  0.0213  0.1843  140 VAL A CA  
769  C C   . VAL A 105 ? 0.2561 0.3553 0.3834 0.0157  0.0228  0.1895  140 VAL A C   
770  O O   . VAL A 105 ? 0.2584 0.3514 0.4013 0.0176  0.0296  0.1908  140 VAL A O   
771  C CB  . VAL A 105 ? 0.2229 0.2908 0.3572 0.0156  0.0229  0.1672  140 VAL A CB  
772  C CG1 . VAL A 105 ? 0.2414 0.3081 0.3390 0.0118  0.0184  0.1579  140 VAL A CG1 
773  C CG2 . VAL A 105 ? 0.2066 0.2668 0.3514 0.0166  0.0218  0.1619  140 VAL A CG2 
774  N N   . ASP A 106 ? 0.2401 0.3538 0.3389 0.0123  0.0170  0.1917  141 ASP A N   
775  C CA  . ASP A 106 ? 0.2423 0.3660 0.3255 0.0111  0.0190  0.1965  141 ASP A CA  
776  C C   . ASP A 106 ? 0.2551 0.3667 0.3131 0.0086  0.0213  0.1822  141 ASP A C   
777  O O   . ASP A 106 ? 0.2571 0.3673 0.3165 0.0095  0.0277  0.1842  141 ASP A O   
778  C CB  . ASP A 106 ? 0.2430 0.3885 0.3062 0.0076  0.0124  0.2038  141 ASP A CB  
779  C CG  . ASP A 106 ? 0.5628 0.7251 0.6522 0.0096  0.0104  0.2212  141 ASP A CG  
780  O OD1 . ASP A 106 ? 0.4267 0.5951 0.5429 0.0135  0.0161  0.2348  141 ASP A OD1 
781  O OD2 . ASP A 106 ? 0.3187 0.4894 0.4033 0.0070  0.0033  0.2219  141 ASP A OD2 
782  N N   . GLU A 107 ? 0.2253 0.3298 0.2616 0.0055  0.0166  0.1687  142 GLU A N   
783  C CA  . GLU A 107 ? 0.2347 0.3294 0.2495 0.0031  0.0192  0.1554  142 GLU A CA  
784  C C   . GLU A 107 ? 0.2845 0.3644 0.2983 0.0026  0.0165  0.1433  142 GLU A C   
785  O O   . GLU A 107 ? 0.2505 0.3310 0.2675 0.0026  0.0106  0.1427  142 GLU A O   
786  C CB  . GLU A 107 ? 0.3117 0.4178 0.2928 -0.0014 0.0171  0.1504  142 GLU A CB  
787  C CG  . GLU A 107 ? 0.4353 0.5597 0.4137 -0.0018 0.0177  0.1634  142 GLU A CG  
788  C CD  . GLU A 107 ? 0.4971 0.6287 0.4437 -0.0062 0.0202  0.1567  142 GLU A CD  
789  O OE1 . GLU A 107 ? 0.3249 0.4499 0.2502 -0.0096 0.0197  0.1409  142 GLU A OE1 
790  O OE2 . GLU A 107 ? 0.6120 0.7564 0.5558 -0.0063 0.0232  0.1670  142 GLU A OE2 
791  N N   . ILE A 108 ? 0.2224 0.2899 0.2337 0.0021  0.0210  0.1347  143 ILE A N   
792  C CA  . ILE A 108 ? 0.1946 0.2485 0.2037 0.0013  0.0180  0.1190  143 ILE A CA  
793  C C   . ILE A 108 ? 0.2100 0.2628 0.1959 -0.0016 0.0185  0.1048  143 ILE A C   
794  O O   . ILE A 108 ? 0.2312 0.2838 0.2159 -0.0017 0.0250  0.1045  143 ILE A O   
795  C CB  . ILE A 108 ? 0.2296 0.2682 0.2644 0.0031  0.0215  0.1138  143 ILE A CB  
796  C CG1 . ILE A 108 ? 0.2762 0.3146 0.3377 0.0060  0.0231  0.1269  143 ILE A CG1 
797  C CG2 . ILE A 108 ? 0.2554 0.2821 0.2850 0.0018  0.0175  0.0950  143 ILE A CG2 
798  C CD1 . ILE A 108 ? 0.2819 0.3062 0.3699 0.0067  0.0278  0.1213  143 ILE A CD1 
799  N N   . TYR A 109 ? 0.1931 0.2455 0.1631 -0.0039 0.0126  0.0938  144 TYR A N   
800  C CA  . TYR A 109 ? 0.2127 0.2625 0.1649 -0.0066 0.0136  0.0794  144 TYR A CA  
801  C C   . TYR A 109 ? 0.2276 0.2635 0.1879 -0.0059 0.0112  0.0663  144 TYR A C   
802  O O   . TYR A 109 ? 0.2343 0.2670 0.1996 -0.0054 0.0058  0.0649  144 TYR A O   
803  C CB  . TYR A 109 ? 0.2639 0.3247 0.1935 -0.0106 0.0088  0.0764  144 TYR A CB  
804  C CG  . TYR A 109 ? 0.2382 0.3170 0.1551 -0.0126 0.0094  0.0898  144 TYR A CG  
805  C CD1 . TYR A 109 ? 0.2204 0.3042 0.1435 -0.0106 0.0166  0.1023  144 TYR A CD1 
806  C CD2 . TYR A 109 ? 0.2963 0.3869 0.1977 -0.0166 0.0024  0.0887  144 TYR A CD2 
807  C CE1 . TYR A 109 ? 0.2570 0.3539 0.1729 -0.0117 0.0162  0.1097  144 TYR A CE1 
808  C CE2 . TYR A 109 ? 0.2916 0.3955 0.1859 -0.0182 0.0016  0.0960  144 TYR A CE2 
809  C CZ  . TYR A 109 ? 0.3499 0.4575 0.2505 -0.0156 0.0085  0.1069  144 TYR A CZ  
810  O OH  . TYR A 109 ? 0.3342 0.4569 0.2274 -0.0173 0.0075  0.1155  144 TYR A OH  
811  N N   . LEU A 110 ? 0.2120 0.2409 0.1745 -0.0060 0.0156  0.0580  145 LEU A N   
812  C CA  . LEU A 110 ? 0.1856 0.2040 0.1566 -0.0056 0.0131  0.0482  145 LEU A CA  
813  C C   . LEU A 110 ? 0.2144 0.2317 0.1736 -0.0075 0.0130  0.0374  145 LEU A C   
814  O O   . LEU A 110 ? 0.2314 0.2506 0.1841 -0.0085 0.0192  0.0344  145 LEU A O   
815  C CB  . LEU A 110 ? 0.1569 0.1699 0.1443 -0.0045 0.0172  0.0486  145 LEU A CB  
816  C CG  . LEU A 110 ? 0.1862 0.1983 0.1909 -0.0032 0.0186  0.0576  145 LEU A CG  
817  C CD1 . LEU A 110 ? 0.2246 0.2328 0.2457 -0.0033 0.0226  0.0571  145 LEU A CD1 
818  C CD2 . LEU A 110 ? 0.1973 0.2043 0.2095 -0.0029 0.0132  0.0552  145 LEU A CD2 
819  N N   . THR A 111 ? 0.1933 0.2071 0.1512 -0.0080 0.0073  0.0316  146 THR A N   
820  C CA  . THR A 111 ? 0.1797 0.1908 0.1326 -0.0096 0.0079  0.0219  146 THR A CA  
821  C C   . THR A 111 ? 0.2027 0.2082 0.1677 -0.0084 0.0120  0.0189  146 THR A C   
822  O O   . THR A 111 ? 0.2165 0.2209 0.1807 -0.0091 0.0176  0.0133  146 THR A O   
823  C CB  . THR A 111 ? 0.2142 0.2235 0.1666 -0.0100 0.0014  0.0187  146 THR A CB  
824  O OG1 . THR A 111 ? 0.2226 0.2275 0.1860 -0.0080 -0.0016 0.0206  146 THR A OG1 
825  C CG2 . THR A 111 ? 0.1871 0.2037 0.1300 -0.0114 -0.0029 0.0227  146 THR A CG2 
826  N N   . HIS A 112 ? 0.1967 0.1994 0.1745 -0.0070 0.0097  0.0224  147 HIS A N   
827  C CA  . HIS A 112 ? 0.2043 0.2044 0.1960 -0.0064 0.0117  0.0217  147 HIS A CA  
828  C C   . HIS A 112 ? 0.2289 0.2281 0.2316 -0.0063 0.0082  0.0255  147 HIS A C   
829  O O   . HIS A 112 ? 0.2138 0.2127 0.2141 -0.0063 0.0055  0.0275  147 HIS A O   
830  C CB  . HIS A 112 ? 0.1830 0.1810 0.1788 -0.0066 0.0095  0.0170  147 HIS A CB  
831  C CG  . HIS A 112 ? 0.1837 0.1813 0.1780 -0.0069 0.0019  0.0166  147 HIS A CG  
832  N ND1 . HIS A 112 ? 0.2162 0.2142 0.1998 -0.0071 -0.0011 0.0159  147 HIS A ND1 
833  C CD2 . HIS A 112 ? 0.2222 0.2205 0.2242 -0.0071 -0.0028 0.0172  147 HIS A CD2 
834  C CE1 . HIS A 112 ? 0.2167 0.2145 0.2017 -0.0072 -0.0061 0.0155  147 HIS A CE1 
835  N NE2 . HIS A 112 ? 0.2039 0.2022 0.1983 -0.0074 -0.0074 0.0162  147 HIS A NE2 
836  N N   . MET A 113 ? 0.1798 0.1787 0.1966 -0.0067 0.0084  0.0260  148 MET A N   
837  C CA  . MET A 113 ? 0.1629 0.1614 0.1920 -0.0079 0.0061  0.0283  148 MET A CA  
838  C C   . MET A 113 ? 0.1724 0.1715 0.2064 -0.0102 -0.0017 0.0246  148 MET A C   
839  O O   . MET A 113 ? 0.1978 0.1978 0.2442 -0.0126 -0.0041 0.0245  148 MET A O   
840  C CB  . MET A 113 ? 0.1777 0.1776 0.2206 -0.0076 0.0121  0.0327  148 MET A CB  
841  C CG  . MET A 113 ? 0.2135 0.2146 0.2505 -0.0059 0.0198  0.0378  148 MET A CG  
842  S SD  . MET A 113 ? 0.2280 0.2314 0.2816 -0.0052 0.0288  0.0440  148 MET A SD  
843  C CE  . MET A 113 ? 0.2901 0.2978 0.3253 -0.0035 0.0377  0.0486  148 MET A CE  
844  N N   . HIS A 114 ? 0.1811 0.1807 0.2055 -0.0102 -0.0057 0.0216  149 HIS A N   
845  C CA  . HIS A 114 ? 0.2309 0.2329 0.2555 -0.0128 -0.0128 0.0186  149 HIS A CA  
846  C C   . HIS A 114 ? 0.2071 0.2059 0.2309 -0.0144 -0.0136 0.0150  149 HIS A C   
847  O O   . HIS A 114 ? 0.1919 0.1868 0.2137 -0.0125 -0.0094 0.0166  149 HIS A O   
848  C CB  . HIS A 114 ? 0.2413 0.2446 0.2557 -0.0118 -0.0153 0.0178  149 HIS A CB  
849  C CG  . HIS A 114 ? 0.2647 0.2720 0.2865 -0.0112 -0.0159 0.0212  149 HIS A CG  
850  N ND1 . HIS A 114 ? 0.2129 0.2203 0.2309 -0.0097 -0.0154 0.0219  149 HIS A ND1 
851  C CD2 . HIS A 114 ? 0.2836 0.2952 0.3201 -0.0119 -0.0164 0.0251  149 HIS A CD2 
852  C CE1 . HIS A 114 ? 0.2730 0.2839 0.3039 -0.0091 -0.0149 0.0262  149 HIS A CE1 
853  N NE2 . HIS A 114 ? 0.2374 0.2513 0.2797 -0.0103 -0.0156 0.0287  149 HIS A NE2 
854  N N   . PRO A 115 ? 0.2086 0.2099 0.2354 -0.0183 -0.0188 0.0103  150 PRO A N   
855  C CA  . PRO A 115 ? 0.1955 0.1923 0.2262 -0.0207 -0.0178 0.0047  150 PRO A CA  
856  C C   . PRO A 115 ? 0.2026 0.1945 0.2251 -0.0182 -0.0144 0.0030  150 PRO A C   
857  O O   . PRO A 115 ? 0.2347 0.2211 0.2656 -0.0178 -0.0099 0.0024  150 PRO A O   
858  C CB  . PRO A 115 ? 0.2157 0.2181 0.2456 -0.0264 -0.0247 -0.0024 150 PRO A CB  
859  C CG  . PRO A 115 ? 0.3795 0.3905 0.4124 -0.0270 -0.0296 0.0034  150 PRO A CG  
860  C CD  . PRO A 115 ? 0.2426 0.2519 0.2705 -0.0214 -0.0256 0.0101  150 PRO A CD  
861  N N   . ASP A 116 ? 0.2112 0.2050 0.2205 -0.0165 -0.0160 0.0032  151 ASP A N   
862  C CA  . ASP A 116 ? 0.2135 0.2039 0.2168 -0.0142 -0.0131 0.0025  151 ASP A CA  
863  C C   . ASP A 116 ? 0.2542 0.2430 0.2591 -0.0104 -0.0092 0.0100  151 ASP A C   
864  O O   . ASP A 116 ? 0.2175 0.2052 0.2199 -0.0083 -0.0075 0.0116  151 ASP A O   
865  C CB  . ASP A 116 ? 0.2502 0.2444 0.2412 -0.0140 -0.0160 0.0011  151 ASP A CB  
866  C CG  . ASP A 116 ? 0.2513 0.2500 0.2389 -0.0128 -0.0187 0.0063  151 ASP A CG  
867  O OD1 . ASP A 116 ? 0.2437 0.2451 0.2374 -0.0140 -0.0204 0.0082  151 ASP A OD1 
868  O OD2 . ASP A 116 ? 0.2284 0.2278 0.2100 -0.0108 -0.0184 0.0084  151 ASP A OD2 
869  N N   . HIS A 117 ? 0.2188 0.2088 0.2279 -0.0097 -0.0077 0.0150  152 HIS A N   
870  C CA  . HIS A 117 ? 0.1874 0.1784 0.1957 -0.0071 -0.0042 0.0223  152 HIS A CA  
871  C C   . HIS A 117 ? 0.2347 0.2247 0.2557 -0.0069 0.0001  0.0276  152 HIS A C   
872  O O   . HIS A 117 ? 0.2161 0.2081 0.2390 -0.0049 0.0031  0.0355  152 HIS A O   
873  C CB  . HIS A 117 ? 0.1831 0.1777 0.1815 -0.0066 -0.0044 0.0236  152 HIS A CB  
874  C CG  . HIS A 117 ? 0.2229 0.2183 0.2124 -0.0068 -0.0079 0.0198  152 HIS A CG  
875  N ND1 . HIS A 117 ? 0.2480 0.2453 0.2296 -0.0060 -0.0087 0.0211  152 HIS A ND1 
876  C CD2 . HIS A 117 ? 0.2033 0.1990 0.1925 -0.0079 -0.0112 0.0160  152 HIS A CD2 
877  C CE1 . HIS A 117 ? 0.2440 0.2414 0.2220 -0.0063 -0.0114 0.0178  152 HIS A CE1 
878  N NE2 . HIS A 117 ? 0.2061 0.2029 0.1882 -0.0072 -0.0127 0.0154  152 HIS A NE2 
879  N N   . VAL A 118 ? 0.1889 0.1775 0.2205 -0.0091 0.0001  0.0249  153 VAL A N   
880  C CA  . VAL A 118 ? 0.2338 0.2214 0.2810 -0.0090 0.0048  0.0305  153 VAL A CA  
881  C C   . VAL A 118 ? 0.2343 0.2165 0.2982 -0.0113 0.0056  0.0261  153 VAL A C   
882  O O   . VAL A 118 ? 0.2316 0.2121 0.3124 -0.0108 0.0105  0.0320  153 VAL A O   
883  C CB  . VAL A 118 ? 0.2389 0.2293 0.2912 -0.0099 0.0058  0.0321  153 VAL A CB  
884  C CG1 . VAL A 118 ? 0.3123 0.3069 0.3515 -0.0076 0.0085  0.0362  153 VAL A CG1 
885  C CG2 . VAL A 118 ? 0.2019 0.1928 0.2574 -0.0135 -0.0002 0.0241  153 VAL A CG2 
886  N N   . GLY A 119 ? 0.2367 0.2163 0.2969 -0.0140 0.0018  0.0156  154 GLY A N   
887  C CA  . GLY A 119 ? 0.2747 0.2490 0.3503 -0.0177 0.0032  0.0076  154 GLY A CA  
888  C C   . GLY A 119 ? 0.2489 0.2175 0.3403 -0.0152 0.0104  0.0122  154 GLY A C   
889  O O   . GLY A 119 ? 0.2324 0.1960 0.3453 -0.0172 0.0144  0.0108  154 GLY A O   
890  N N   . GLY A 120 ? 0.2548 0.2246 0.3387 -0.0109 0.0121  0.0189  155 GLY A N   
891  C CA  . GLY A 120 ? 0.2404 0.2069 0.3415 -0.0078 0.0186  0.0264  155 GLY A CA  
892  C C   . GLY A 120 ? 0.2469 0.2156 0.3650 -0.0056 0.0231  0.0407  155 GLY A C   
893  O O   . GLY A 120 ? 0.2074 0.1740 0.3455 -0.0031 0.0291  0.0493  155 GLY A O   
894  N N   . LEU A 121 ? 0.2078 0.1813 0.3204 -0.0063 0.0214  0.0446  156 LEU A N   
895  C CA  . LEU A 121 ? 0.2147 0.1914 0.3431 -0.0044 0.0269  0.0588  156 LEU A CA  
896  C C   . LEU A 121 ? 0.2340 0.2030 0.3940 -0.0063 0.0324  0.0574  156 LEU A C   
897  O O   . LEU A 121 ? 0.2469 0.2177 0.4267 -0.0039 0.0386  0.0718  156 LEU A O   
898  C CB  . LEU A 121 ? 0.2040 0.1865 0.3217 -0.0051 0.0256  0.0612  156 LEU A CB  
899  C CG  . LEU A 121 ? 0.2219 0.2128 0.3132 -0.0029 0.0233  0.0657  156 LEU A CG  
900  C CD1 . LEU A 121 ? 0.2322 0.2268 0.3154 -0.0038 0.0238  0.0648  156 LEU A CD1 
901  C CD2 . LEU A 121 ? 0.2345 0.2329 0.3259 0.0004  0.0267  0.0817  156 LEU A CD2 
902  N N   . MET A 122 ? 0.2462 0.1586 0.3675 -0.0101 0.0738  -0.0047 157 MET A N   
903  C CA  . MET A 122 ? 0.3008 0.1874 0.4294 -0.0146 0.0725  -0.0195 157 MET A CA  
904  C C   . MET A 122 ? 0.4108 0.2782 0.5362 -0.0019 0.0832  -0.0381 157 MET A C   
905  O O   . MET A 122 ? 0.3381 0.2165 0.4427 0.0071  0.0899  -0.0461 157 MET A O   
906  C CB  . MET A 122 ? 0.3168 0.2082 0.4275 -0.0268 0.0624  -0.0334 157 MET A CB  
907  C CG  . MET A 122 ? 0.2853 0.1948 0.4023 -0.0379 0.0539  -0.0160 157 MET A CG  
908  S SD  . MET A 122 ? 0.3228 0.2190 0.4733 -0.0475 0.0522  0.0000  157 MET A SD  
909  C CE  . MET A 122 ? 0.3093 0.1739 0.4699 -0.0554 0.0501  -0.0254 157 MET A CE  
910  N N   . VAL A 123 ? 0.3449 0.1827 0.4911 0.0000  0.0862  -0.0440 158 VAL A N   
911  C CA  . VAL A 123 ? 0.4020 0.2150 0.5428 0.0119  0.0957  -0.0683 158 VAL A CA  
912  C C   . VAL A 123 ? 0.5884 0.3746 0.7278 -0.0010 0.0864  -0.0910 158 VAL A C   
913  O O   . VAL A 123 ? 0.4197 0.1919 0.5811 -0.0080 0.0804  -0.0818 158 VAL A O   
914  C CB  . VAL A 123 ? 0.4974 0.2988 0.6644 0.0283  0.1076  -0.0572 158 VAL A CB  
915  C CG1 . VAL A 123 ? 0.6926 0.4912 0.8889 0.0215  0.1003  -0.0321 158 VAL A CG1 
916  C CG2 . VAL A 123 ? 0.5119 0.2908 0.6680 0.0393  0.1133  -0.0823 158 VAL A CG2 
917  N N   . GLY A 124 ? 0.5676 0.3583 0.6759 -0.0049 0.0809  -0.1158 159 GLY A N   
918  C CA  . GLY A 124 ? 0.4834 0.2598 0.5901 -0.0205 0.0665  -0.1348 159 GLY A CA  
919  C C   . GLY A 124 ? 0.5599 0.3500 0.6871 -0.0396 0.0555  -0.1154 159 GLY A C   
920  O O   . GLY A 124 ? 0.5532 0.3741 0.6715 -0.0421 0.0531  -0.0995 159 GLY A O   
921  N N   . GLU A 125 ? 0.5823 0.3581 0.7309 -0.0506 0.0476  -0.1106 160 GLU A N   
922  C CA  . GLU A 125 ? 0.4509 0.2431 0.6190 -0.0665 0.0395  -0.0886 160 GLU A CA  
923  C C   . GLU A 125 ? 0.5636 0.3588 0.7533 -0.0612 0.0466  -0.0555 160 GLU A C   
924  O O   . GLU A 125 ? 0.5000 0.3083 0.7027 -0.0713 0.0419  -0.0357 160 GLU A O   
925  C CB  . GLU A 125 ? 0.5195 0.2989 0.6973 -0.0826 0.0275  -0.1000 160 GLU A CB  
926  C CG  . GLU A 125 ? 0.7121 0.4823 0.8668 -0.0854 0.0184  -0.1361 160 GLU A CG  
927  C CD  . GLU A 125 ? 1.0346 0.8346 1.1621 -0.0846 0.0138  -0.1480 160 GLU A CD  
928  O OE1 . GLU A 125 ? 0.9712 0.7679 1.0686 -0.0712 0.0181  -0.1685 160 GLU A OE1 
929  O OE2 . GLU A 125 ? 0.9511 0.7801 1.0858 -0.0957 0.0068  -0.1354 160 GLU A OE2 
930  N N   . GLN A 126 ? 0.4516 0.2391 0.6437 -0.0443 0.0575  -0.0489 161 GLN A N   
931  C CA  . GLN A 126 ? 0.3609 0.1544 0.5719 -0.0373 0.0623  -0.0190 161 GLN A CA  
932  C C   . GLN A 126 ? 0.3904 0.2123 0.5944 -0.0300 0.0659  -0.0021 161 GLN A C   
933  O O   . GLN A 126 ? 0.3556 0.1806 0.5456 -0.0228 0.0715  -0.0137 161 GLN A O   
934  C CB  . GLN A 126 ? 0.4243 0.1915 0.6485 -0.0233 0.0705  -0.0216 161 GLN A CB  
935  C CG  . GLN A 126 ? 0.6226 0.3557 0.8516 -0.0297 0.0668  -0.0416 161 GLN A CG  
936  C CD  . GLN A 126 ? 0.9710 0.6883 1.1765 -0.0263 0.0667  -0.0777 161 GLN A CD  
937  O OE1 . GLN A 126 ? 0.9225 0.6397 1.1159 -0.0094 0.0764  -0.0868 161 GLN A OE1 
938  N NE2 . GLN A 126 ? 0.8923 0.6003 1.0897 -0.0417 0.0556  -0.0978 161 GLN A NE2 
939  N N   . LEU A 127 ? 0.2989 0.1416 0.5098 -0.0316 0.0627  0.0246  162 LEU A N   
940  C CA  . LEU A 127 ? 0.3145 0.1836 0.5189 -0.0243 0.0638  0.0405  162 LEU A CA  
941  C C   . LEU A 127 ? 0.3244 0.1871 0.5396 -0.0081 0.0730  0.0422  162 LEU A C   
942  O O   . LEU A 127 ? 0.3389 0.1877 0.5722 -0.0004 0.0767  0.0477  162 LEU A O   
943  C CB  . LEU A 127 ? 0.2839 0.1747 0.4911 -0.0259 0.0581  0.0655  162 LEU A CB  
944  C CG  . LEU A 127 ? 0.3854 0.2846 0.5863 -0.0390 0.0517  0.0690  162 LEU A CG  
945  C CD1 . LEU A 127 ? 0.3830 0.3031 0.5839 -0.0363 0.0492  0.0930  162 LEU A CD1 
946  C CD2 . LEU A 127 ? 0.2866 0.1996 0.4680 -0.0469 0.0479  0.0566  162 LEU A CD2 
947  N N   . ALA A 128 ? 0.3402 0.2138 0.5459 -0.0026 0.0776  0.0386  163 ALA A N   
948  C CA  . ALA A 128 ? 0.3425 0.2173 0.5610 0.0139  0.0873  0.0427  163 ALA A CA  
949  C C   . ALA A 128 ? 0.2868 0.1847 0.5228 0.0191  0.0828  0.0700  163 ALA A C   
950  O O   . ALA A 128 ? 0.2934 0.1923 0.5488 0.0324  0.0890  0.0771  163 ALA A O   
951  C CB  . ALA A 128 ? 0.2586 0.1541 0.4557 0.0172  0.0905  0.0323  163 ALA A CB  
952  N N   . PHE A 129 ? 0.2524 0.1713 0.4795 0.0097  0.0719  0.0838  164 PHE A N   
953  C CA  . PHE A 129 ? 0.2753 0.2199 0.5123 0.0141  0.0653  0.1070  164 PHE A CA  
954  C C   . PHE A 129 ? 0.2554 0.2009 0.4894 0.0079  0.0585  0.1173  164 PHE A C   
955  O O   . PHE A 129 ? 0.2863 0.2473 0.5017 -0.0001 0.0508  0.1206  164 PHE A O   
956  C CB  . PHE A 129 ? 0.2168 0.1883 0.4412 0.0106  0.0589  0.1113  164 PHE A CB  
957  C CG  . PHE A 129 ? 0.2420 0.2157 0.4703 0.0157  0.0670  0.1026  164 PHE A CG  
958  C CD1 . PHE A 129 ? 0.2550 0.2430 0.5075 0.0279  0.0705  0.1128  164 PHE A CD1 
959  C CD2 . PHE A 129 ? 0.2358 0.2045 0.4408 0.0100  0.0703  0.0820  164 PHE A CD2 
960  C CE1 . PHE A 129 ? 0.2441 0.2423 0.4989 0.0331  0.0789  0.1032  164 PHE A CE1 
961  C CE2 . PHE A 129 ? 0.2428 0.2196 0.4463 0.0159  0.0782  0.0733  164 PHE A CE2 
962  C CZ  . PHE A 129 ? 0.2600 0.2517 0.4889 0.0269  0.0835  0.0840  164 PHE A CZ  
963  N N   . PRO A 130 ? 0.2903 0.2184 0.5425 0.0124  0.0625  0.1228  165 PRO A N   
964  C CA  . PRO A 130 ? 0.3789 0.3013 0.6300 0.0048  0.0592  0.1307  165 PRO A CA  
965  C C   . PRO A 130 ? 0.3572 0.3072 0.6037 0.0054  0.0521  0.1536  165 PRO A C   
966  O O   . PRO A 130 ? 0.2855 0.2357 0.5268 -0.0016 0.0504  0.1604  165 PRO A O   
967  C CB  . PRO A 130 ? 0.4827 0.3765 0.7569 0.0105  0.0662  0.1308  165 PRO A CB  
968  C CG  . PRO A 130 ? 0.4601 0.3558 0.7485 0.0250  0.0720  0.1318  165 PRO A CG  
969  C CD  . PRO A 130 ? 0.2771 0.1873 0.5510 0.0244  0.0718  0.1201  165 PRO A CD  
970  N N   . ASN A 131 ? 0.2664 0.2407 0.5151 0.0131  0.0480  0.1658  166 ASN A N   
971  C CA  . ASN A 131 ? 0.2771 0.2791 0.5181 0.0139  0.0402  0.1861  166 ASN A CA  
972  C C   . ASN A 131 ? 0.3260 0.3528 0.5438 0.0095  0.0317  0.1828  166 ASN A C   
973  O O   . ASN A 131 ? 0.3901 0.4407 0.5967 0.0099  0.0244  0.1970  166 ASN A O   
974  C CB  . ASN A 131 ? 0.2961 0.3088 0.5589 0.0256  0.0398  0.2064  166 ASN A CB  
975  C CG  . ASN A 131 ? 0.3544 0.3397 0.6401 0.0307  0.0487  0.2102  166 ASN A CG  
976  O OD1 . ASN A 131 ? 0.3329 0.3014 0.6174 0.0245  0.0516  0.2109  166 ASN A OD1 
977  N ND2 . ASN A 131 ? 0.3466 0.3265 0.6542 0.0419  0.0534  0.2125  166 ASN A ND2 
978  N N   . ALA A 132 ? 0.2422 0.2632 0.4509 0.0053  0.0325  0.1643  167 ALA A N   
979  C CA  . ALA A 132 ? 0.2369 0.2778 0.4266 0.0011  0.0247  0.1609  167 ALA A CA  
980  C C   . ALA A 132 ? 0.2731 0.3165 0.4352 -0.0076 0.0226  0.1534  167 ALA A C   
981  O O   . ALA A 132 ? 0.3158 0.3431 0.4744 -0.0123 0.0279  0.1444  167 ALA A O   
982  C CB  . ALA A 132 ? 0.2372 0.2711 0.4307 0.0006  0.0284  0.1460  167 ALA A CB  
983  N N   . VAL A 133 ? 0.2069 0.2722 0.3506 -0.0098 0.0145  0.1577  168 VAL A N   
984  C CA  . VAL A 133 ? 0.1960 0.2654 0.3132 -0.0165 0.0137  0.1477  168 VAL A CA  
985  C C   . VAL A 133 ? 0.2390 0.3057 0.3488 -0.0210 0.0123  0.1322  168 VAL A C   
986  O O   . VAL A 133 ? 0.2356 0.3118 0.3527 -0.0208 0.0068  0.1360  168 VAL A O   
987  C CB  . VAL A 133 ? 0.2856 0.3801 0.3830 -0.0151 0.0069  0.1607  168 VAL A CB  
988  C CG1 . VAL A 133 ? 0.3153 0.4151 0.3853 -0.0197 0.0074  0.1491  168 VAL A CG1 
989  C CG2 . VAL A 133 ? 0.2815 0.3792 0.3859 -0.0109 0.0106  0.1763  168 VAL A CG2 
990  N N   . VAL A 134 ? 0.2251 0.2805 0.3233 -0.0254 0.0169  0.1158  169 VAL A N   
991  C CA  . VAL A 134 ? 0.1898 0.2414 0.2801 -0.0290 0.0170  0.1010  169 VAL A CA  
992  C C   . VAL A 134 ? 0.2115 0.2755 0.2779 -0.0315 0.0118  0.0973  169 VAL A C   
993  O O   . VAL A 134 ? 0.2180 0.2895 0.2720 -0.0314 0.0137  0.1012  169 VAL A O   
994  C CB  . VAL A 134 ? 0.2046 0.2382 0.2948 -0.0304 0.0240  0.0860  169 VAL A CB  
995  C CG1 . VAL A 134 ? 0.2179 0.2488 0.2987 -0.0324 0.0248  0.0737  169 VAL A CG1 
996  C CG2 . VAL A 134 ? 0.2287 0.2480 0.3388 -0.0271 0.0292  0.0869  169 VAL A CG2 
997  N N   . ARG A 135 ? 0.1669 0.2326 0.2269 -0.0323 0.0054  0.0876  170 ARG A N   
998  C CA  . ARG A 135 ? 0.1707 0.2412 0.2066 -0.0327 -0.0006 0.0774  170 ARG A CA  
999  C C   . ARG A 135 ? 0.2175 0.2738 0.2508 -0.0351 0.0006  0.0627  170 ARG A C   
1000 O O   . ARG A 135 ? 0.1977 0.2481 0.2474 -0.0374 0.0020  0.0622  170 ARG A O   
1001 C CB  . ARG A 135 ? 0.1889 0.2753 0.2173 -0.0324 -0.0133 0.0805  170 ARG A CB  
1002 C CG  . ARG A 135 ? 0.2223 0.3253 0.2533 -0.0282 -0.0152 0.0998  170 ARG A CG  
1003 C CD  . ARG A 135 ? 0.2895 0.4120 0.2968 -0.0259 -0.0278 0.0998  170 ARG A CD  
1004 N NE  . ARG A 135 ? 0.2439 0.3666 0.2204 -0.0233 -0.0253 0.0881  170 ARG A NE  
1005 C CZ  . ARG A 135 ? 0.3174 0.4544 0.2649 -0.0197 -0.0344 0.0823  170 ARG A CZ  
1006 N NH1 . ARG A 135 ? 0.2796 0.4335 0.2240 -0.0198 -0.0493 0.0864  170 ARG A NH1 
1007 N NH2 . ARG A 135 ? 0.3198 0.4561 0.2403 -0.0147 -0.0287 0.0713  170 ARG A NH2 
1008 N N   . ALA A 136 ? 0.2077 0.2596 0.2217 -0.0332 0.0016  0.0528  171 ALA A N   
1009 C CA  . ALA A 136 ? 0.1875 0.2246 0.1964 -0.0337 0.0025  0.0412  171 ALA A CA  
1010 C C   . ALA A 136 ? 0.2116 0.2476 0.1973 -0.0289 0.0003  0.0315  171 ALA A C   
1011 O O   . ALA A 136 ? 0.2048 0.2542 0.1785 -0.0247 0.0009  0.0342  171 ALA A O   
1012 C CB  . ALA A 136 ? 0.1937 0.2222 0.2090 -0.0326 0.0117  0.0410  171 ALA A CB  
1013 N N   . ASP A 137 ? 0.1837 0.2034 0.1637 -0.0284 -0.0010 0.0211  172 ASP A N   
1014 C CA  . ASP A 137 ? 0.2340 0.2487 0.1926 -0.0211 -0.0016 0.0100  172 ASP A CA  
1015 C C   . ASP A 137 ? 0.2240 0.2479 0.1776 -0.0128 0.0077  0.0130  172 ASP A C   
1016 O O   . ASP A 137 ? 0.2100 0.2341 0.1752 -0.0135 0.0131  0.0187  172 ASP A O   
1017 C CB  . ASP A 137 ? 0.2437 0.2337 0.2006 -0.0215 -0.0040 -0.0005 172 ASP A CB  
1018 C CG  . ASP A 137 ? 0.2952 0.2763 0.2297 -0.0135 -0.0069 -0.0156 172 ASP A CG  
1019 O OD1 . ASP A 137 ? 0.3408 0.3230 0.2651 -0.0020 0.0007  -0.0177 172 ASP A OD1 
1020 O OD2 . ASP A 137 ? 0.3496 0.3249 0.2770 -0.0181 -0.0172 -0.0264 172 ASP A OD2 
1021 N N   . GLN A 138 ? 0.2334 0.2675 0.1694 -0.0047 0.0092  0.0085  173 GLN A N   
1022 C CA  . GLN A 138 ? 0.2140 0.2621 0.1489 0.0035  0.0183  0.0117  173 GLN A CA  
1023 C C   . GLN A 138 ? 0.2337 0.2692 0.1739 0.0085  0.0214  0.0080  173 GLN A C   
1024 O O   . GLN A 138 ? 0.2307 0.2788 0.1819 0.0097  0.0260  0.0144  173 GLN A O   
1025 C CB  . GLN A 138 ? 0.2395 0.2992 0.1525 0.0143  0.0211  0.0051  173 GLN A CB  
1026 C CG  . GLN A 138 ? 0.2386 0.3219 0.1559 0.0224  0.0322  0.0120  173 GLN A CG  
1027 C CD  . GLN A 138 ? 0.2930 0.4010 0.2209 0.0157  0.0364  0.0289  173 GLN A CD  
1028 O OE1 . GLN A 138 ? 0.2682 0.3861 0.1833 0.0154  0.0353  0.0335  173 GLN A OE1 
1029 N NE2 . GLN A 138 ? 0.2468 0.3642 0.1986 0.0099  0.0403  0.0386  173 GLN A NE2 
1030 N N   . LYS A 139 ? 0.2338 0.2449 0.1675 0.0111  0.0180  -0.0014 174 LYS A N   
1031 C CA  . LYS A 139 ? 0.2174 0.2157 0.1549 0.0179  0.0211  -0.0014 174 LYS A CA  
1032 C C   . LYS A 139 ? 0.2007 0.2007 0.1526 0.0105  0.0218  0.0085  174 LYS A C   
1033 O O   . LYS A 139 ? 0.2767 0.2831 0.2320 0.0163  0.0246  0.0125  174 LYS A O   
1034 C CB  . LYS A 139 ? 0.2530 0.2201 0.1833 0.0205  0.0178  -0.0113 174 LYS A CB  
1035 C CG  . LYS A 139 ? 0.3306 0.2919 0.2429 0.0321  0.0181  -0.0255 174 LYS A CG  
1036 C CD  . LYS A 139 ? 0.4475 0.3712 0.3561 0.0355  0.0153  -0.0363 174 LYS A CD  
1037 C CE  . LYS A 139 ? 0.5595 0.4740 0.4477 0.0494  0.0163  -0.0545 174 LYS A CE  
1038 N NZ  . LYS A 139 ? 0.6738 0.5560 0.5546 0.0422  0.0067  -0.0720 174 LYS A NZ  
1039 N N   . GLU A 140 ? 0.2166 0.2133 0.1768 -0.0010 0.0190  0.0119  175 GLU A N   
1040 C CA  . GLU A 140 ? 0.2284 0.2264 0.1995 -0.0063 0.0212  0.0191  175 GLU A CA  
1041 C C   . GLU A 140 ? 0.2442 0.2625 0.2209 -0.0065 0.0234  0.0224  175 GLU A C   
1042 O O   . GLU A 140 ? 0.2235 0.2459 0.2013 -0.0040 0.0247  0.0235  175 GLU A O   
1043 C CB  . GLU A 140 ? 0.2337 0.2278 0.2153 -0.0165 0.0190  0.0220  175 GLU A CB  
1044 C CG  . GLU A 140 ? 0.2240 0.2166 0.2148 -0.0196 0.0236  0.0276  175 GLU A CG  
1045 C CD  . GLU A 140 ? 0.2198 0.1975 0.2070 -0.0167 0.0269  0.0300  175 GLU A CD  
1046 O OE1 . GLU A 140 ? 0.2435 0.2073 0.2254 -0.0138 0.0249  0.0274  175 GLU A OE1 
1047 O OE2 . GLU A 140 ? 0.2440 0.2227 0.2328 -0.0163 0.0323  0.0347  175 GLU A OE2 
1048 N N   . ALA A 141 ? 0.2167 0.2486 0.1972 -0.0100 0.0231  0.0246  176 ALA A N   
1049 C CA  . ALA A 141 ? 0.1857 0.2350 0.1770 -0.0130 0.0253  0.0289  176 ALA A CA  
1050 C C   . ALA A 141 ? 0.2126 0.2763 0.2030 -0.0057 0.0267  0.0273  176 ALA A C   
1051 O O   . ALA A 141 ? 0.2064 0.2798 0.2062 -0.0083 0.0258  0.0276  176 ALA A O   
1052 C CB  . ALA A 141 ? 0.2304 0.2910 0.2260 -0.0171 0.0261  0.0355  176 ALA A CB  
1053 N N   . ASP A 142 ? 0.1878 0.2543 0.1675 0.0040  0.0284  0.0245  177 ASP A N   
1054 C CA  . ASP A 142 ? 0.2116 0.2961 0.1941 0.0136  0.0309  0.0245  177 ASP A CA  
1055 C C   . ASP A 142 ? 0.1831 0.2620 0.1661 0.0178  0.0275  0.0235  177 ASP A C   
1056 O O   . ASP A 142 ? 0.2183 0.3184 0.2114 0.0202  0.0261  0.0256  177 ASP A O   
1057 C CB  . ASP A 142 ? 0.2466 0.3300 0.2151 0.0268  0.0347  0.0196  177 ASP A CB  
1058 C CG  . ASP A 142 ? 0.2789 0.3799 0.2441 0.0263  0.0396  0.0222  177 ASP A CG  
1059 O OD1 . ASP A 142 ? 0.2525 0.3637 0.2279 0.0149  0.0397  0.0305  177 ASP A OD1 
1060 O OD2 . ASP A 142 ? 0.2969 0.4005 0.2477 0.0386  0.0440  0.0164  177 ASP A OD2 
1061 N N   . PHE A 143 ? 0.2245 0.2778 0.1975 0.0187  0.0260  0.0217  178 PHE A N   
1062 C CA  . PHE A 143 ? 0.2016 0.2502 0.1713 0.0244  0.0241  0.0241  178 PHE A CA  
1063 C C   . PHE A 143 ? 0.1940 0.2530 0.1694 0.0157  0.0209  0.0247  178 PHE A C   
1064 O O   . PHE A 143 ? 0.2197 0.2953 0.1967 0.0197  0.0169  0.0254  178 PHE A O   
1065 C CB  . PHE A 143 ? 0.2301 0.2488 0.1902 0.0265  0.0254  0.0251  178 PHE A CB  
1066 C CG  . PHE A 143 ? 0.2380 0.2519 0.1924 0.0337  0.0250  0.0317  178 PHE A CG  
1067 C CD1 . PHE A 143 ? 0.3092 0.3258 0.2604 0.0490  0.0247  0.0354  178 PHE A CD1 
1068 C CD2 . PHE A 143 ? 0.2681 0.2771 0.2193 0.0274  0.0258  0.0356  178 PHE A CD2 
1069 C CE1 . PHE A 143 ? 0.3555 0.3698 0.2998 0.0573  0.0239  0.0448  178 PHE A CE1 
1070 C CE2 . PHE A 143 ? 0.3162 0.3237 0.2576 0.0355  0.0262  0.0438  178 PHE A CE2 
1071 C CZ  . PHE A 143 ? 0.3495 0.3598 0.2871 0.0501  0.0246  0.0493  178 PHE A CZ  
1072 N N   . TRP A 144 ? 0.2475 0.2971 0.2259 0.0046  0.0219  0.0235  179 TRP A N   
1073 C CA  . TRP A 144 ? 0.1623 0.2146 0.1421 -0.0014 0.0201  0.0209  179 TRP A CA  
1074 C C   . TRP A 144 ? 0.2028 0.2737 0.1973 -0.0093 0.0165  0.0171  179 TRP A C   
1075 O O   . TRP A 144 ? 0.2069 0.2828 0.2013 -0.0129 0.0123  0.0113  179 TRP A O   
1076 C CB  . TRP A 144 ? 0.1962 0.2307 0.1757 -0.0074 0.0242  0.0212  179 TRP A CB  
1077 C CG  . TRP A 144 ? 0.2316 0.2501 0.2010 -0.0025 0.0278  0.0260  179 TRP A CG  
1078 C CD1 . TRP A 144 ? 0.2558 0.2601 0.2280 -0.0042 0.0299  0.0291  179 TRP A CD1 
1079 C CD2 . TRP A 144 ? 0.2499 0.2657 0.2063 0.0042  0.0295  0.0295  179 TRP A CD2 
1080 N NE1 . TRP A 144 ? 0.2400 0.2311 0.2060 -0.0007 0.0336  0.0350  179 TRP A NE1 
1081 C CE2 . TRP A 144 ? 0.3007 0.2988 0.2556 0.0055  0.0345  0.0370  179 TRP A CE2 
1082 C CE3 . TRP A 144 ? 0.2234 0.2517 0.1687 0.0090  0.0265  0.0275  179 TRP A CE3 
1083 C CZ2 . TRP A 144 ? 0.3068 0.2983 0.2504 0.0118  0.0391  0.0459  179 TRP A CZ2 
1084 C CZ3 . TRP A 144 ? 0.2551 0.2789 0.1844 0.0169  0.0299  0.0352  179 TRP A CZ3 
1085 C CH2 . TRP A 144 ? 0.2989 0.3040 0.2278 0.0186  0.0374  0.0460  179 TRP A CH2 
1086 N N   . LEU A 145 ? 0.1533 0.2346 0.1600 -0.0126 0.0180  0.0203  180 LEU A N   
1087 C CA  . LEU A 145 ? 0.1703 0.2693 0.1965 -0.0221 0.0158  0.0198  180 LEU A CA  
1088 C C   . LEU A 145 ? 0.1967 0.3239 0.2315 -0.0176 0.0123  0.0208  180 LEU A C   
1089 O O   . LEU A 145 ? 0.1736 0.3206 0.2300 -0.0265 0.0107  0.0223  180 LEU A O   
1090 C CB  . LEU A 145 ? 0.1675 0.2656 0.2045 -0.0285 0.0211  0.0270  180 LEU A CB  
1091 C CG  . LEU A 145 ? 0.2546 0.3293 0.2874 -0.0319 0.0233  0.0277  180 LEU A CG  
1092 C CD1 . LEU A 145 ? 0.2603 0.3372 0.3026 -0.0365 0.0271  0.0376  180 LEU A CD1 
1093 C CD2 . LEU A 145 ? 0.2706 0.3329 0.3073 -0.0376 0.0212  0.0200  180 LEU A CD2 
1094 N N   . SER A 146 ? 0.1842 0.3142 0.2062 -0.0039 0.0113  0.0215  181 SER A N   
1095 C CA  . SER A 146 ? 0.1767 0.3359 0.2082 0.0045  0.0083  0.0241  181 SER A CA  
1096 C C   . SER A 146 ? 0.1533 0.3305 0.1916 0.0000  -0.0030 0.0190  181 SER A C   
1097 O O   . SER A 146 ? 0.2014 0.3683 0.2213 0.0052  -0.0078 0.0159  181 SER A O   
1098 C CB  . SER A 146 ? 0.2047 0.3544 0.2198 0.0228  0.0113  0.0271  181 SER A CB  
1099 O OG  . SER A 146 ? 0.2059 0.3837 0.2306 0.0344  0.0082  0.0307  181 SER A OG  
1100 N N   . GLN A 147 ? 0.1259 0.3322 0.1907 -0.0097 -0.0075 0.0186  182 GLN A N   
1101 C CA  . GLN A 147 ? 0.1573 0.3856 0.2310 -0.0155 -0.0215 0.0114  182 GLN A CA  
1102 C C   . GLN A 147 ? 0.1441 0.3908 0.2073 0.0023  -0.0280 0.0150  182 GLN A C   
1103 O O   . GLN A 147 ? 0.1972 0.4492 0.2481 0.0033  -0.0396 0.0088  182 GLN A O   
1104 C CB  . GLN A 147 ? 0.2182 0.4771 0.3295 -0.0309 -0.0252 0.0119  182 GLN A CB  
1105 C CG  . GLN A 147 ? 0.2276 0.4673 0.3528 -0.0492 -0.0197 0.0107  182 GLN A CG  
1106 C CD  . GLN A 147 ? 0.4293 0.6998 0.5955 -0.0630 -0.0185 0.0183  182 GLN A CD  
1107 O OE1 . GLN A 147 ? 0.4462 0.7177 0.6221 -0.0638 -0.0054 0.0310  182 GLN A OE1 
1108 N NE2 . GLN A 147 ? 0.3500 0.6481 0.5406 -0.0739 -0.0322 0.0115  182 GLN A NE2 
1109 N N   . THR A 148 ? 0.1419 0.3994 0.2091 0.0179  -0.0208 0.0251  183 THR A N   
1110 C CA  . THR A 148 ? 0.1526 0.4266 0.2131 0.0371  -0.0266 0.0310  183 THR A CA  
1111 C C   . THR A 148 ? 0.1653 0.4044 0.1917 0.0485  -0.0246 0.0330  183 THR A C   
1112 O O   . THR A 148 ? 0.2131 0.4620 0.2279 0.0596  -0.0332 0.0371  183 THR A O   
1113 C CB  . THR A 148 ? 0.1588 0.4546 0.2362 0.0528  -0.0184 0.0403  183 THR A CB  
1114 O OG1 . THR A 148 ? 0.1751 0.4388 0.2385 0.0584  -0.0037 0.0413  183 THR A OG1 
1115 C CG2 . THR A 148 ? 0.1746 0.5130 0.2899 0.0411  -0.0198 0.0416  183 THR A CG2 
1116 N N   . ASN A 149 ? 0.1716 0.3727 0.1833 0.0458  -0.0137 0.0321  184 ASN A N   
1117 C CA  . ASN A 149 ? 0.2243 0.3937 0.2090 0.0523  -0.0112 0.0350  184 ASN A CA  
1118 C C   . ASN A 149 ? 0.2111 0.3831 0.1822 0.0445  -0.0197 0.0292  184 ASN A C   
1119 O O   . ASN A 149 ? 0.2377 0.4051 0.1881 0.0549  -0.0221 0.0353  184 ASN A O   
1120 C CB  . ASN A 149 ? 0.2194 0.3529 0.1968 0.0468  0.0000  0.0336  184 ASN A CB  
1121 C CG  . ASN A 149 ? 0.2628 0.3849 0.2417 0.0589  0.0078  0.0376  184 ASN A CG  
1122 O OD1 . ASN A 149 ? 0.2403 0.3762 0.2237 0.0746  0.0071  0.0428  184 ASN A OD1 
1123 N ND2 . ASN A 149 ? 0.2628 0.3602 0.2377 0.0526  0.0147  0.0341  184 ASN A ND2 
1124 N N   . LEU A 150 ? 0.2090 0.3870 0.1904 0.0272  -0.0236 0.0175  185 LEU A N   
1125 C CA  . LEU A 150 ? 0.2024 0.3822 0.1695 0.0205  -0.0321 0.0073  185 LEU A CA  
1126 C C   . LEU A 150 ? 0.2581 0.4725 0.2222 0.0278  -0.0474 0.0071  185 LEU A C   
1127 O O   . LEU A 150 ? 0.2670 0.4818 0.2042 0.0349  -0.0527 0.0065  185 LEU A O   
1128 C CB  . LEU A 150 ? 0.2376 0.4137 0.2211 0.0007  -0.0335 -0.0064 185 LEU A CB  
1129 C CG  . LEU A 150 ? 0.2673 0.4504 0.2434 -0.0086 -0.0455 -0.0233 185 LEU A CG  
1130 C CD1 . LEU A 150 ? 0.3357 0.5013 0.2752 0.0002  -0.0425 -0.0260 185 LEU A CD1 
1131 C CD2 . LEU A 150 ? 0.2917 0.4620 0.2890 -0.0274 -0.0442 -0.0350 185 LEU A CD2 
1132 N N   . ASP A 151 ? 0.2339 0.4814 0.2259 0.0272  -0.0546 0.0090  186 ASP A N   
1133 C CA  . ASP A 151 ? 0.2863 0.5729 0.2800 0.0349  -0.0712 0.0103  186 ASP A CA  
1134 C C   . ASP A 151 ? 0.2311 0.5166 0.2022 0.0590  -0.0699 0.0267  186 ASP A C   
1135 O O   . ASP A 151 ? 0.2860 0.5875 0.2454 0.0654  -0.0807 0.0277  186 ASP A O   
1136 C CB  . ASP A 151 ? 0.2344 0.5611 0.2693 0.0296  -0.0775 0.0115  186 ASP A CB  
1137 C CG  . ASP A 151 ? 0.5530 0.8834 0.6132 0.0038  -0.0812 -0.0029 186 ASP A CG  
1138 O OD1 . ASP A 151 ? 0.6909 0.9996 0.7350 -0.0084 -0.0849 -0.0177 186 ASP A OD1 
1139 O OD2 . ASP A 151 ? 0.7295 1.0841 0.8267 -0.0034 -0.0791 0.0013  186 ASP A OD2 
1140 N N   . LYS A 152 ? 0.2536 0.5093 0.2193 0.0700  -0.0541 0.0386  187 LYS A N   
1141 C CA  . LYS A 152 ? 0.2552 0.5023 0.2040 0.0926  -0.0508 0.0562  187 LYS A CA  
1142 C C   . LYS A 152 ? 0.3529 0.5682 0.2675 0.0948  -0.0445 0.0610  187 LYS A C   
1143 O O   . LYS A 152 ? 0.3900 0.5924 0.2927 0.1091  -0.0401 0.0753  187 LYS A O   
1144 C CB  . LYS A 152 ? 0.3632 0.5916 0.3267 0.1024  -0.0371 0.0641  187 LYS A CB  
1145 C CG  . LYS A 152 ? 0.3961 0.6609 0.3865 0.1156  -0.0413 0.0699  187 LYS A CG  
1146 C CD  . LYS A 152 ? 0.5650 0.8219 0.5754 0.1139  -0.0284 0.0660  187 LYS A CD  
1147 C CE  . LYS A 152 ? 0.4841 0.7022 0.4838 0.1304  -0.0149 0.0729  187 LYS A CE  
1148 N NZ  . LYS A 152 ? 0.3622 0.5811 0.3784 0.1320  -0.0040 0.0671  187 LYS A NZ  
1149 N N   . ALA A 153 ? 0.3601 0.5576 0.2651 0.0785  -0.0405 0.0482  188 ALA A N   
1150 C CA  . ALA A 153 ? 0.3733 0.5422 0.2503 0.0805  -0.0307 0.0539  188 ALA A CA  
1151 C C   . ALA A 153 ? 0.4438 0.6242 0.2993 0.0892  -0.0369 0.0588  188 ALA A C   
1152 O O   . ALA A 153 ? 0.3899 0.5974 0.2442 0.0849  -0.0510 0.0469  188 ALA A O   
1153 C CB  . ALA A 153 ? 0.3479 0.5007 0.2237 0.0624  -0.0254 0.0374  188 ALA A CB  
1154 N N   . PRO A 154 ? 0.4351 0.5940 0.2765 0.0994  -0.0265 0.0755  189 PRO A N   
1155 C CA  . PRO A 154 ? 0.4630 0.6350 0.2875 0.1094  -0.0319 0.0836  189 PRO A CA  
1156 C C   . PRO A 154 ? 0.5092 0.6886 0.3087 0.1028  -0.0356 0.0710  189 PRO A C   
1157 O O   . PRO A 154 ? 0.6362 0.8400 0.4245 0.1070  -0.0482 0.0678  189 PRO A O   
1158 C CB  . PRO A 154 ? 0.6321 0.7760 0.4533 0.1202  -0.0177 0.1061  189 PRO A CB  
1159 C CG  . PRO A 154 ? 0.4991 0.6125 0.3269 0.1105  -0.0044 0.1044  189 PRO A CG  
1160 C CD  . PRO A 154 ? 0.4370 0.5608 0.2819 0.1025  -0.0107 0.0894  189 PRO A CD  
1161 N N   . ASP A 155 ? 0.4152 0.5745 0.2051 0.0937  -0.0249 0.0637  190 ASP A N   
1162 C CA  . ASP A 155 ? 0.5063 0.6685 0.2698 0.0905  -0.0249 0.0525  190 ASP A CA  
1163 C C   . ASP A 155 ? 0.5328 0.6876 0.2984 0.0763  -0.0234 0.0300  190 ASP A C   
1164 O O   . ASP A 155 ? 0.4875 0.6366 0.2746 0.0684  -0.0224 0.0251  190 ASP A O   
1165 C CB  . ASP A 155 ? 0.5014 0.6464 0.2481 0.0979  -0.0089 0.0703  190 ASP A CB  
1166 C CG  . ASP A 155 ? 0.9165 1.0327 0.6809 0.0949  0.0077  0.0833  190 ASP A CG  
1167 O OD1 . ASP A 155 ? 0.6919 0.7972 0.4688 0.0843  0.0118  0.0721  190 ASP A OD1 
1168 O OD2 . ASP A 155 ? 0.9082 1.0125 0.6747 0.1026  0.0164  0.1047  190 ASP A OD2 
1169 N N   . ASP A 156 ? 0.5537 0.7080 0.2959 0.0740  -0.0223 0.0162  191 ASP A N   
1170 C CA  . ASP A 156 ? 0.6261 0.7719 0.3697 0.0620  -0.0213 -0.0077 191 ASP A CA  
1171 C C   . ASP A 156 ? 0.4042 0.5249 0.1570 0.0588  -0.0016 -0.0018 191 ASP A C   
1172 O O   . ASP A 156 ? 0.4420 0.5557 0.2079 0.0491  -0.0004 -0.0170 191 ASP A O   
1173 C CB  . ASP A 156 ? 0.5478 0.6989 0.2638 0.0615  -0.0270 -0.0275 191 ASP A CB  
1174 C CG  . ASP A 156 ? 0.6936 0.8695 0.4099 0.0579  -0.0506 -0.0417 191 ASP A CG  
1175 O OD1 . ASP A 156 ? 0.9035 1.0969 0.6386 0.0600  -0.0605 -0.0301 191 ASP A OD1 
1176 O OD2 . ASP A 156 ? 0.9291 1.1066 0.6289 0.0529  -0.0590 -0.0648 191 ASP A OD2 
1177 N N   . GLU A 157 ? 0.4954 0.6037 0.2456 0.0657  0.0136  0.0203  192 GLU A N   
1178 C CA  . GLU A 157 ? 0.4964 0.5835 0.2629 0.0610  0.0306  0.0277  192 GLU A CA  
1179 C C   . GLU A 157 ? 0.3658 0.4475 0.1586 0.0548  0.0278  0.0297  192 GLU A C   
1180 O O   . GLU A 157 ? 0.3865 0.4578 0.1962 0.0455  0.0326  0.0201  192 GLU A O   
1181 C CB  . GLU A 157 ? 0.5036 0.5808 0.2695 0.0671  0.0444  0.0518  192 GLU A CB  
1182 C CG  . GLU A 157 ? 0.5877 0.6454 0.3777 0.0601  0.0596  0.0608  192 GLU A CG  
1183 C CD  . GLU A 157 ? 0.8214 0.8706 0.6162 0.0635  0.0718  0.0833  192 GLU A CD  
1184 O OE1 . GLU A 157 ? 0.6269 0.6692 0.4301 0.0668  0.0695  0.0993  192 GLU A OE1 
1185 O OE2 . GLU A 157 ? 0.7401 0.7895 0.5321 0.0630  0.0843  0.0850  192 GLU A OE2 
1186 N N   . SER A 158 ? 0.3506 0.4909 0.2787 0.0226  -0.0433 0.0204  193 SER A N   
1187 C CA  . SER A 158 ? 0.4259 0.5572 0.3776 0.0287  -0.0403 0.0221  193 SER A CA  
1188 C C   . SER A 158 ? 0.2603 0.4026 0.2317 0.0241  -0.0412 0.0094  193 SER A C   
1189 O O   . SER A 158 ? 0.2501 0.3816 0.2356 0.0230  -0.0337 0.0049  193 SER A O   
1190 C CB  . SER A 158 ? 0.4059 0.5371 0.3629 0.0403  -0.0467 0.0375  193 SER A CB  
1191 O OG  . SER A 158 ? 0.4757 0.6302 0.4321 0.0427  -0.0596 0.0414  193 SER A OG  
1192 N N   . LYS A 159 ? 0.2632 0.4277 0.2356 0.0201  -0.0508 0.0040  194 LYS A N   
1193 C CA  . LYS A 159 ? 0.2419 0.4159 0.2329 0.0126  -0.0512 -0.0089 194 LYS A CA  
1194 C C   . LYS A 159 ? 0.3194 0.4767 0.3099 0.0045  -0.0411 -0.0215 194 LYS A C   
1195 O O   . LYS A 159 ? 0.2662 0.4169 0.2748 0.0014  -0.0363 -0.0262 194 LYS A O   
1196 C CB  . LYS A 159 ? 0.2595 0.4608 0.2490 0.0067  -0.0635 -0.0150 194 LYS A CB  
1197 C CG  . LYS A 159 ? 0.2739 0.4967 0.2747 0.0155  -0.0746 -0.0033 194 LYS A CG  
1198 C CD  . LYS A 159 ? 0.5056 0.7603 0.5123 0.0078  -0.0874 -0.0112 194 LYS A CD  
1199 C CE  . LYS A 159 ? 0.6039 0.8724 0.6332 0.0163  -0.0932 -0.0015 194 LYS A CE  
1200 N NZ  . LYS A 159 ? 0.5760 0.8536 0.6341 0.0112  -0.0892 -0.0096 194 LYS A NZ  
1201 N N   . GLY A 160 ? 0.2821 0.4330 0.2528 0.0014  -0.0374 -0.0262 195 GLY A N   
1202 C CA  . GLY A 160 ? 0.2598 0.3952 0.2326 -0.0038 -0.0274 -0.0382 195 GLY A CA  
1203 C C   . GLY A 160 ? 0.2555 0.3718 0.2392 0.0015  -0.0188 -0.0312 195 GLY A C   
1204 O O   . GLY A 160 ? 0.2476 0.3530 0.2442 -0.0014 -0.0130 -0.0381 195 GLY A O   
1205 N N   . PHE A 161 ? 0.2152 0.3270 0.1938 0.0089  -0.0183 -0.0172 196 PHE A N   
1206 C CA  . PHE A 161 ? 0.2436 0.3402 0.2319 0.0129  -0.0114 -0.0113 196 PHE A CA  
1207 C C   . PHE A 161 ? 0.2629 0.3606 0.2713 0.0124  -0.0119 -0.0116 196 PHE A C   
1208 O O   . PHE A 161 ? 0.2239 0.3114 0.2422 0.0106  -0.0063 -0.0134 196 PHE A O   
1209 C CB  . PHE A 161 ? 0.2708 0.3619 0.2504 0.0197  -0.0115 0.0019  196 PHE A CB  
1210 C CG  . PHE A 161 ? 0.2829 0.3688 0.2440 0.0185  -0.0079 0.0049  196 PHE A CG  
1211 C CD1 . PHE A 161 ? 0.3255 0.4162 0.2769 0.0126  -0.0049 -0.0048 196 PHE A CD1 
1212 C CD2 . PHE A 161 ? 0.6223 0.6988 0.5755 0.0226  -0.0068 0.0169  196 PHE A CD2 
1213 C CE1 . PHE A 161 ? 0.3129 0.4023 0.2469 0.0105  -0.0001 -0.0020 196 PHE A CE1 
1214 C CE2 . PHE A 161 ? 0.4824 0.5550 0.4186 0.0196  -0.0028 0.0211  196 PHE A CE2 
1215 C CZ  . PHE A 161 ? 0.3367 0.4175 0.2630 0.0134  0.0008  0.0120  196 PHE A CZ  
1216 N N   . PHE A 162 ? 0.1969 0.3090 0.2121 0.0140  -0.0186 -0.0090 197 PHE A N   
1217 C CA  . PHE A 162 ? 0.1700 0.2871 0.2046 0.0121  -0.0179 -0.0094 197 PHE A CA  
1218 C C   . PHE A 162 ? 0.2224 0.3374 0.2663 0.0022  -0.0164 -0.0196 197 PHE A C   
1219 O O   . PHE A 162 ? 0.2251 0.3314 0.2803 -0.0006 -0.0113 -0.0184 197 PHE A O   
1220 C CB  . PHE A 162 ? 0.1918 0.3293 0.2353 0.0160  -0.0250 -0.0057 197 PHE A CB  
1221 C CG  . PHE A 162 ? 0.1878 0.3232 0.2283 0.0272  -0.0251 0.0046  197 PHE A CG  
1222 C CD1 . PHE A 162 ? 0.1773 0.3069 0.2270 0.0313  -0.0187 0.0081  197 PHE A CD1 
1223 C CD2 . PHE A 162 ? 0.2163 0.3547 0.2443 0.0335  -0.0315 0.0108  197 PHE A CD2 
1224 C CE1 . PHE A 162 ? 0.1952 0.3200 0.2432 0.0418  -0.0180 0.0151  197 PHE A CE1 
1225 C CE2 . PHE A 162 ? 0.2162 0.3480 0.2432 0.0442  -0.0315 0.0207  197 PHE A CE2 
1226 C CZ  . PHE A 162 ? 0.2301 0.3543 0.2682 0.0486  -0.0244 0.0216  197 PHE A CZ  
1227 N N   . LYS A 163 ? 0.1634 0.2856 0.2021 -0.0037 -0.0209 -0.0296 198 LYS A N   
1228 C CA  . LYS A 163 ? 0.1766 0.2933 0.2249 -0.0137 -0.0193 -0.0415 198 LYS A CA  
1229 C C   . LYS A 163 ? 0.2361 0.3300 0.2855 -0.0130 -0.0107 -0.0432 198 LYS A C   
1230 O O   . LYS A 163 ? 0.2507 0.3338 0.3148 -0.0179 -0.0075 -0.0450 198 LYS A O   
1231 C CB  . LYS A 163 ? 0.2884 0.4168 0.3278 -0.0205 -0.0254 -0.0547 198 LYS A CB  
1232 C CG  . LYS A 163 ? 0.3264 0.4816 0.3675 -0.0218 -0.0361 -0.0530 198 LYS A CG  
1233 C CD  . LYS A 163 ? 0.3411 0.5093 0.3725 -0.0312 -0.0429 -0.0680 198 LYS A CD  
1234 C CE  . LYS A 163 ? 0.5370 0.7357 0.5653 -0.0300 -0.0557 -0.0632 198 LYS A CE  
1235 N NZ  . LYS A 163 ? 0.5636 0.7770 0.5743 -0.0383 -0.0632 -0.0763 198 LYS A NZ  
1236 N N   . GLY A 164 ? 0.2151 0.3023 0.2506 -0.0070 -0.0072 -0.0415 199 GLY A N   
1237 C CA  . GLY A 164 ? 0.2442 0.3141 0.2836 -0.0051 0.0003  -0.0429 199 GLY A CA  
1238 C C   . GLY A 164 ? 0.2206 0.2823 0.2710 -0.0021 0.0031  -0.0310 199 GLY A C   
1239 O O   . GLY A 164 ? 0.2263 0.2753 0.2887 -0.0034 0.0064  -0.0312 199 GLY A O   
1240 N N   . ALA A 165 ? 0.2094 0.2778 0.2555 0.0021  0.0016  -0.0205 200 ALA A N   
1241 C CA  . ALA A 165 ? 0.2121 0.2757 0.2657 0.0036  0.0042  -0.0107 200 ALA A CA  
1242 C C   . ALA A 165 ? 0.2253 0.2895 0.2938 -0.0030 0.0039  -0.0102 200 ALA A C   
1243 O O   . ALA A 165 ? 0.2146 0.2691 0.2907 -0.0046 0.0069  -0.0046 200 ALA A O   
1244 C CB  . ALA A 165 ? 0.1784 0.2494 0.2251 0.0088  0.0033  -0.0032 200 ALA A CB  
1245 N N   . MET A 166 ? 0.1706 0.2472 0.2437 -0.0077 0.0000  -0.0150 201 MET A N   
1246 C CA  . MET A 166 ? 0.1550 0.2343 0.2435 -0.0163 0.0003  -0.0144 201 MET A CA  
1247 C C   . MET A 166 ? 0.2115 0.2724 0.3085 -0.0224 0.0023  -0.0196 201 MET A C   
1248 O O   . MET A 166 ? 0.2300 0.2804 0.3365 -0.0260 0.0054  -0.0119 201 MET A O   
1249 C CB  . MET A 166 ? 0.1830 0.2827 0.2758 -0.0203 -0.0054 -0.0203 201 MET A CB  
1250 C CG  . MET A 166 ? 0.2051 0.3219 0.2965 -0.0132 -0.0065 -0.0131 201 MET A CG  
1251 S SD  . MET A 166 ? 0.2658 0.4109 0.3652 -0.0156 -0.0150 -0.0187 201 MET A SD  
1252 C CE  . MET A 166 ? 0.2069 0.3665 0.3075 -0.0028 -0.0144 -0.0092 201 MET A CE  
1253 N N   . ALA A 167 ? 0.1735 0.2293 0.2664 -0.0230 0.0010  -0.0321 202 ALA A N   
1254 C CA  . ALA A 167 ? 0.2399 0.2762 0.3428 -0.0276 0.0036  -0.0400 202 ALA A CA  
1255 C C   . ALA A 167 ? 0.2141 0.2328 0.3206 -0.0207 0.0082  -0.0314 202 ALA A C   
1256 O O   . ALA A 167 ? 0.2550 0.2556 0.3755 -0.0236 0.0103  -0.0304 202 ALA A O   
1257 C CB  . ALA A 167 ? 0.2708 0.3075 0.3659 -0.0288 0.0026  -0.0578 202 ALA A CB  
1258 N N   . SER A 168 ? 0.1951 0.2187 0.2907 -0.0117 0.0093  -0.0249 203 SER A N   
1259 C CA  . SER A 168 ? 0.2168 0.2286 0.3167 -0.0051 0.0123  -0.0173 203 SER A CA  
1260 C C   . SER A 168 ? 0.2129 0.2237 0.3174 -0.0061 0.0119  -0.0008 203 SER A C   
1261 O O   . SER A 168 ? 0.2580 0.2563 0.3720 -0.0039 0.0127  0.0070  203 SER A O   
1262 C CB  . SER A 168 ? 0.1967 0.2161 0.2838 0.0026  0.0137  -0.0177 203 SER A CB  
1263 O OG  . SER A 168 ? 0.2222 0.2443 0.3024 0.0030  0.0150  -0.0319 203 SER A OG  
1264 N N   . LEU A 169 ? 0.2107 0.2355 0.3086 -0.0089 0.0108  0.0049  204 LEU A N   
1265 C CA  . LEU A 169 ? 0.1689 0.1968 0.2661 -0.0098 0.0117  0.0192  204 LEU A CA  
1266 C C   . LEU A 169 ? 0.2057 0.2344 0.3124 -0.0196 0.0125  0.0249  204 LEU A C   
1267 O O   . LEU A 169 ? 0.2239 0.2476 0.3333 -0.0222 0.0136  0.0379  204 LEU A O   
1268 C CB  . LEU A 169 ? 0.2940 0.3368 0.3778 -0.0058 0.0119  0.0211  204 LEU A CB  
1269 C CG  . LEU A 169 ? 0.4786 0.5248 0.5570 -0.0054 0.0133  0.0328  204 LEU A CG  
1270 C CD1 . LEU A 169 ? 0.3584 0.3946 0.4383 -0.0015 0.0121  0.0387  204 LEU A CD1 
1271 C CD2 . LEU A 169 ? 0.3576 0.4155 0.4239 -0.0016 0.0144  0.0309  204 LEU A CD2 
1272 N N   . ASN A 170 ? 0.1784 0.2150 0.2901 -0.0260 0.0117  0.0165  205 ASN A N   
1273 C CA  . ASN A 170 ? 0.2291 0.2698 0.3516 -0.0371 0.0133  0.0217  205 ASN A CA  
1274 C C   . ASN A 170 ? 0.2291 0.2475 0.3636 -0.0437 0.0144  0.0286  205 ASN A C   
1275 O O   . ASN A 170 ? 0.2589 0.2791 0.3983 -0.0523 0.0170  0.0404  205 ASN A O   
1276 C CB  . ASN A 170 ? 0.2498 0.3068 0.3779 -0.0431 0.0111  0.0103  205 ASN A CB  
1277 C CG  . ASN A 170 ? 0.3045 0.3861 0.4259 -0.0379 0.0109  0.0106  205 ASN A CG  
1278 O OD1 . ASN A 170 ? 0.3527 0.4393 0.4672 -0.0335 0.0143  0.0194  205 ASN A OD1 
1279 N ND2 . ASN A 170 ? 0.2757 0.3728 0.3993 -0.0379 0.0066  0.0008  205 ASN A ND2 
1280 N N   . PRO A 171 ? 0.2222 0.2194 0.3626 -0.0403 0.0133  0.0224  206 PRO A N   
1281 C CA  . PRO A 171 ? 0.2922 0.2650 0.4456 -0.0442 0.0143  0.0323  206 PRO A CA  
1282 C C   . PRO A 171 ? 0.2434 0.2146 0.3920 -0.0399 0.0144  0.0529  206 PRO A C   
1283 O O   . PRO A 171 ? 0.2699 0.2290 0.4260 -0.0469 0.0151  0.0676  206 PRO A O   
1284 C CB  . PRO A 171 ? 0.2701 0.2231 0.4309 -0.0377 0.0138  0.0186  206 PRO A CB  
1285 C CG  . PRO A 171 ? 0.2616 0.2301 0.4141 -0.0376 0.0128  -0.0006 206 PRO A CG  
1286 C CD  . PRO A 171 ? 0.2189 0.2132 0.3564 -0.0344 0.0118  0.0052  206 PRO A CD  
1287 N N   . TYR A 172 ? 0.2420 0.2253 0.3774 -0.0298 0.0133  0.0548  207 TYR A N   
1288 C CA  . TYR A 172 ? 0.2303 0.2171 0.3584 -0.0274 0.0123  0.0731  207 TYR A CA  
1289 C C   . TYR A 172 ? 0.2248 0.2299 0.3434 -0.0365 0.0153  0.0818  207 TYR A C   
1290 O O   . TYR A 172 ? 0.2423 0.2465 0.3586 -0.0415 0.0157  0.0992  207 TYR A O   
1291 C CB  . TYR A 172 ? 0.2084 0.2032 0.3266 -0.0159 0.0102  0.0705  207 TYR A CB  
1292 C CG  . TYR A 172 ? 0.2312 0.2107 0.3610 -0.0065 0.0083  0.0659  207 TYR A CG  
1293 C CD1 . TYR A 172 ? 0.2249 0.1999 0.3593 -0.0033 0.0100  0.0474  207 TYR A CD1 
1294 C CD2 . TYR A 172 ? 0.2208 0.1927 0.3576 -0.0005 0.0048  0.0800  207 TYR A CD2 
1295 C CE1 . TYR A 172 ? 0.2080 0.1712 0.3539 0.0056  0.0102  0.0413  207 TYR A CE1 
1296 C CE2 . TYR A 172 ? 0.2450 0.2054 0.3965 0.0098  0.0038  0.0750  207 TYR A CE2 
1297 C CZ  . TYR A 172 ? 0.1972 0.1534 0.3534 0.0128  0.0074  0.0547  207 TYR A CZ  
1298 O OH  . TYR A 172 ? 0.2654 0.2124 0.4369 0.0232  0.0083  0.0479  207 TYR A OH  
1299 N N   . VAL A 173 ? 0.2253 0.2489 0.3387 -0.0381 0.0176  0.0703  208 VAL A N   
1300 C CA  . VAL A 173 ? 0.2223 0.2657 0.3307 -0.0461 0.0221  0.0755  208 VAL A CA  
1301 C C   . VAL A 173 ? 0.2407 0.2777 0.3611 -0.0597 0.0247  0.0851  208 VAL A C   
1302 O O   . VAL A 173 ? 0.2615 0.3060 0.3766 -0.0672 0.0284  0.0998  208 VAL A O   
1303 C CB  . VAL A 173 ? 0.2440 0.3067 0.3513 -0.0439 0.0234  0.0607  208 VAL A CB  
1304 C CG1 . VAL A 173 ? 0.2241 0.3096 0.3318 -0.0518 0.0293  0.0643  208 VAL A CG1 
1305 C CG2 . VAL A 173 ? 0.2346 0.3012 0.3290 -0.0317 0.0215  0.0538  208 VAL A CG2 
1306 N N   . LYS A 174 ? 0.2207 0.2438 0.3564 -0.0645 0.0233  0.0767  209 LYS A N   
1307 C CA  . LYS A 174 ? 0.3066 0.3209 0.4560 -0.0795 0.0260  0.0843  209 LYS A CA  
1308 C C   . LYS A 174 ? 0.3182 0.3117 0.4675 -0.0818 0.0257  0.1056  209 LYS A C   
1309 O O   . LYS A 174 ? 0.3108 0.3052 0.4562 -0.0915 0.0288  0.1159  209 LYS A O   
1310 C CB  . LYS A 174 ? 0.3211 0.3206 0.4862 -0.0838 0.0236  0.0684  209 LYS A CB  
1311 C CG  . LYS A 174 ? 0.4299 0.4122 0.6118 -0.1002 0.0258  0.0750  209 LYS A CG  
1312 C CD  . LYS A 174 ? 0.6249 0.6053 0.8207 -0.1083 0.0241  0.0544  209 LYS A CD  
1313 C CE  . LYS A 174 ? 0.5338 0.4965 0.7403 -0.1243 0.0261  0.0573  209 LYS A CE  
1314 N NZ  . LYS A 174 ? 0.6573 0.5946 0.8748 -0.1263 0.0230  0.0395  209 LYS A NZ  
1315 N N   . ALA A 175 ? 0.3128 0.2890 0.4603 -0.0694 0.0209  0.1084  210 ALA A N   
1316 C CA  . ALA A 175 ? 0.3270 0.2851 0.4722 -0.0666 0.0180  0.1266  210 ALA A CA  
1317 C C   . ALA A 175 ? 0.2788 0.2564 0.4025 -0.0645 0.0175  0.1404  210 ALA A C   
1318 O O   . ALA A 175 ? 0.3439 0.3122 0.4626 -0.0609 0.0133  0.1545  210 ALA A O   
1319 C CB  . ALA A 175 ? 0.2878 0.2237 0.4441 -0.0533 0.0130  0.1235  210 ALA A CB  
1320 N N   . GLY A 176 ? 0.2638 0.2689 0.3751 -0.0664 0.0214  0.1352  211 GLY A N   
1321 C CA  . GLY A 176 ? 0.2914 0.3146 0.3810 -0.0645 0.0212  0.1437  211 GLY A CA  
1322 C C   . GLY A 176 ? 0.3468 0.3702 0.4295 -0.0525 0.0149  0.1463  211 GLY A C   
1323 O O   . GLY A 176 ? 0.3121 0.3447 0.3793 -0.0512 0.0119  0.1554  211 GLY A O   
1324 N N   . LYS A 177 ? 0.2445 0.2595 0.3385 -0.0441 0.0127  0.1369  212 LYS A N   
1325 C CA  . LYS A 177 ? 0.2400 0.2539 0.3311 -0.0320 0.0065  0.1373  212 LYS A CA  
1326 C C   . LYS A 177 ? 0.2693 0.2987 0.3502 -0.0257 0.0076  0.1196  212 LYS A C   
1327 O O   . LYS A 177 ? 0.2764 0.3044 0.3585 -0.0164 0.0034  0.1154  212 LYS A O   
1328 C CB  . LYS A 177 ? 0.2893 0.2779 0.4012 -0.0244 0.0025  0.1370  212 LYS A CB  
1329 C CG  . LYS A 177 ? 0.3312 0.3070 0.4477 -0.0242 -0.0022 0.1541  212 LYS A CG  
1330 C CD  . LYS A 177 ? 0.5382 0.4857 0.6763 -0.0236 -0.0015 0.1505  212 LYS A CD  
1331 C CE  . LYS A 177 ? 0.4817 0.4152 0.6308 -0.0128 -0.0076 0.1582  212 LYS A CE  
1332 N NZ  . LYS A 177 ? 0.6735 0.5791 0.8443 -0.0100 -0.0057 0.1484  212 LYS A NZ  
1333 N N   . PHE A 178 ? 0.2427 0.2870 0.3152 -0.0303 0.0132  0.1096  213 PHE A N   
1334 C CA  . PHE A 178 ? 0.2348 0.2919 0.2966 -0.0246 0.0144  0.0957  213 PHE A CA  
1335 C C   . PHE A 178 ? 0.2413 0.3172 0.2849 -0.0291 0.0175  0.0999  213 PHE A C   
1336 O O   . PHE A 178 ? 0.2381 0.3243 0.2789 -0.0371 0.0232  0.1030  213 PHE A O   
1337 C CB  . PHE A 178 ? 0.2257 0.2850 0.2934 -0.0238 0.0177  0.0797  213 PHE A CB  
1338 C CG  . PHE A 178 ? 0.2289 0.2983 0.2861 -0.0177 0.0189  0.0680  213 PHE A CG  
1339 C CD1 . PHE A 178 ? 0.2268 0.2907 0.2807 -0.0103 0.0155  0.0634  213 PHE A CD1 
1340 C CD2 . PHE A 178 ? 0.2631 0.3475 0.3151 -0.0194 0.0240  0.0622  213 PHE A CD2 
1341 C CE1 . PHE A 178 ? 0.2615 0.3313 0.3059 -0.0061 0.0168  0.0541  213 PHE A CE1 
1342 C CE2 . PHE A 178 ? 0.2432 0.3327 0.2871 -0.0130 0.0251  0.0522  213 PHE A CE2 
1343 C CZ  . PHE A 178 ? 0.1893 0.2699 0.2285 -0.0070 0.0213  0.0487  213 PHE A CZ  
1344 N N   . LYS A 179 ? 0.2331 0.3149 0.2649 -0.0249 0.0143  0.0987  214 LYS A N   
1345 C CA  . LYS A 179 ? 0.2115 0.3108 0.2239 -0.0296 0.0170  0.1001  214 LYS A CA  
1346 C C   . LYS A 179 ? 0.2686 0.3720 0.2735 -0.0241 0.0182  0.0837  214 LYS A C   
1347 O O   . LYS A 179 ? 0.2020 0.3025 0.2049 -0.0201 0.0127  0.0822  214 LYS A O   
1348 C CB  . LYS A 179 ? 0.2763 0.3796 0.2797 -0.0326 0.0105  0.1170  214 LYS A CB  
1349 C CG  . LYS A 179 ? 0.3904 0.5104 0.3726 -0.0379 0.0121  0.1131  214 LYS A CG  
1350 C CD  . LYS A 179 ? 0.4701 0.5942 0.4452 -0.0391 0.0030  0.1250  214 LYS A CD  
1351 C CE  . LYS A 179 ? 0.6221 0.7624 0.5764 -0.0468 0.0053  0.1231  214 LYS A CE  
1352 N NZ  . LYS A 179 ? 0.6817 0.8335 0.6242 -0.0475 -0.0021 0.1223  214 LYS A NZ  
1353 N N   . PRO A 180 ? 0.2062 0.3158 0.2091 -0.0236 0.0252  0.0716  215 PRO A N   
1354 C CA  . PRO A 180 ? 0.1809 0.2899 0.1781 -0.0180 0.0265  0.0571  215 PRO A CA  
1355 C C   . PRO A 180 ? 0.2541 0.3729 0.2326 -0.0219 0.0269  0.0550  215 PRO A C   
1356 O O   . PRO A 180 ? 0.2467 0.3776 0.2141 -0.0291 0.0279  0.0632  215 PRO A O   
1357 C CB  . PRO A 180 ? 0.1928 0.3070 0.1957 -0.0157 0.0337  0.0473  215 PRO A CB  
1358 C CG  . PRO A 180 ? 0.2515 0.3783 0.2556 -0.0236 0.0385  0.0555  215 PRO A CG  
1359 C CD  . PRO A 180 ? 0.2281 0.3458 0.2370 -0.0278 0.0322  0.0709  215 PRO A CD  
1360 N N   . PHE A 181 ? 0.1915 0.3049 0.1657 -0.0183 0.0260  0.0440  216 PHE A N   
1361 C CA  . PHE A 181 ? 0.2282 0.3495 0.1852 -0.0224 0.0279  0.0357  216 PHE A CA  
1362 C C   . PHE A 181 ? 0.2380 0.3521 0.1958 -0.0170 0.0346  0.0193  216 PHE A C   
1363 O O   . PHE A 181 ? 0.2272 0.3319 0.1983 -0.0099 0.0358  0.0169  216 PHE A O   
1364 C CB  . PHE A 181 ? 0.2292 0.3499 0.1814 -0.0249 0.0195  0.0384  216 PHE A CB  
1365 C CG  . PHE A 181 ? 0.2088 0.3154 0.1743 -0.0190 0.0158  0.0359  216 PHE A CG  
1366 C CD1 . PHE A 181 ? 0.2330 0.3291 0.1977 -0.0163 0.0191  0.0229  216 PHE A CD1 
1367 C CD2 . PHE A 181 ? 0.2236 0.3268 0.2026 -0.0159 0.0100  0.0467  216 PHE A CD2 
1368 C CE1 . PHE A 181 ? 0.2389 0.3237 0.2136 -0.0123 0.0167  0.0221  216 PHE A CE1 
1369 C CE2 . PHE A 181 ? 0.2243 0.3174 0.2141 -0.0111 0.0084  0.0433  216 PHE A CE2 
1370 C CZ  . PHE A 181 ? 0.2164 0.3015 0.2030 -0.0099 0.0117  0.0317  216 PHE A CZ  
1371 N N   . SER A 182 ? 0.2279 0.3462 0.1716 -0.0202 0.0388  0.0076  217 SER A N   
1372 C CA  . SER A 182 ? 0.2472 0.3556 0.1931 -0.0140 0.0456  -0.0081 217 SER A CA  
1373 C C   . SER A 182 ? 0.3033 0.4030 0.2382 -0.0178 0.0441  -0.0190 217 SER A C   
1374 O O   . SER A 182 ? 0.3390 0.4497 0.2576 -0.0260 0.0454  -0.0249 217 SER A O   
1375 C CB  . SER A 182 ? 0.2625 0.3841 0.2059 -0.0131 0.0562  -0.0161 217 SER A CB  
1376 O OG  . SER A 182 ? 0.3444 0.4552 0.2916 -0.0055 0.0625  -0.0320 217 SER A OG  
1377 N N   . GLY A 183 ? 0.2480 0.3288 0.1909 -0.0132 0.0417  -0.0220 218 GLY A N   
1378 C CA  . GLY A 183 ? 0.3309 0.4006 0.2659 -0.0182 0.0410  -0.0327 218 GLY A CA  
1379 C C   . GLY A 183 ? 0.3554 0.4360 0.2832 -0.0284 0.0325  -0.0265 218 GLY A C   
1380 O O   . GLY A 183 ? 0.3392 0.4306 0.2718 -0.0287 0.0263  -0.0120 218 GLY A O   
1381 N N   . ASN A 184 ? 0.3080 0.3859 0.2255 -0.0367 0.0318  -0.0380 219 ASN A N   
1382 C CA  . ASN A 184 ? 0.2778 0.3705 0.1895 -0.0470 0.0227  -0.0332 219 ASN A CA  
1383 C C   . ASN A 184 ? 0.3294 0.4465 0.2309 -0.0507 0.0193  -0.0234 219 ASN A C   
1384 O O   . ASN A 184 ? 0.3221 0.4475 0.2099 -0.0531 0.0254  -0.0304 219 ASN A O   
1385 C CB  . ASN A 184 ? 0.2938 0.3823 0.1941 -0.0577 0.0231  -0.0501 219 ASN A CB  
1386 C CG  . ASN A 184 ? 0.3541 0.4160 0.2640 -0.0562 0.0262  -0.0577 219 ASN A CG  
1387 O OD1 . ASN A 184 ? 0.3300 0.3800 0.2541 -0.0479 0.0264  -0.0484 219 ASN A OD1 
1388 N ND2 . ASN A 184 ? 0.3540 0.4065 0.2553 -0.0656 0.0284  -0.0746 219 ASN A ND2 
1389 N N   . THR A 185 ? 0.2719 0.4008 0.1807 -0.0511 0.0098  -0.0069 220 THR A N   
1390 C CA  . THR A 185 ? 0.2647 0.4133 0.1663 -0.0534 0.0055  0.0076  220 THR A CA  
1391 C C   . THR A 185 ? 0.2712 0.4339 0.1787 -0.0564 -0.0073 0.0209  220 THR A C   
1392 O O   . THR A 185 ? 0.2846 0.4400 0.2112 -0.0507 -0.0109 0.0265  220 THR A O   
1393 C CB  . THR A 185 ? 0.2885 0.4309 0.2021 -0.0444 0.0095  0.0191  220 THR A CB  
1394 O OG1 . THR A 185 ? 0.3252 0.4577 0.2378 -0.0403 0.0206  0.0071  220 THR A OG1 
1395 C CG2 . THR A 185 ? 0.3305 0.4900 0.2367 -0.0480 0.0058  0.0358  220 THR A CG2 
1396 N N   . ASP A 186 ? 0.2539 0.4386 0.1458 -0.0649 -0.0140 0.0261  221 ASP A N   
1397 C CA  . ASP A 186 ? 0.2951 0.4941 0.1980 -0.0645 -0.0267 0.0430  221 ASP A CA  
1398 C C   . ASP A 186 ? 0.2942 0.4878 0.2105 -0.0553 -0.0275 0.0625  221 ASP A C   
1399 O O   . ASP A 186 ? 0.3395 0.5314 0.2497 -0.0553 -0.0228 0.0675  221 ASP A O   
1400 C CB  . ASP A 186 ? 0.2929 0.5098 0.1833 -0.0734 -0.0320 0.0428  221 ASP A CB  
1401 C CG  . ASP A 186 ? 0.4101 0.6331 0.2928 -0.0833 -0.0341 0.0252  221 ASP A CG  
1402 O OD1 . ASP A 186 ? 0.4783 0.6886 0.3632 -0.0841 -0.0296 0.0112  221 ASP A OD1 
1403 O OD2 . ASP A 186 ? 0.6514 0.8913 0.5260 -0.0910 -0.0402 0.0253  221 ASP A OD2 
1404 N N   . LEU A 187 ? 0.2557 0.4452 0.1925 -0.0476 -0.0325 0.0716  222 LEU A N   
1405 C CA  . LEU A 187 ? 0.2360 0.4190 0.1892 -0.0389 -0.0349 0.0896  222 LEU A CA  
1406 C C   . LEU A 187 ? 0.4827 0.6797 0.4437 -0.0390 -0.0458 0.1021  222 LEU A C   
1407 O O   . LEU A 187 ? 0.8942 1.1062 0.8408 -0.0474 -0.0493 0.0987  222 LEU A O   
1408 C CB  . LEU A 187 ? 0.2142 0.3789 0.1904 -0.0291 -0.0309 0.0859  222 LEU A CB  
1409 C CG  . LEU A 187 ? 0.2461 0.3942 0.2172 -0.0290 -0.0193 0.0685  222 LEU A CG  
1410 C CD1 . LEU A 187 ? 0.2977 0.4307 0.2878 -0.0213 -0.0160 0.0630  222 LEU A CD1 
1411 C CD2 . LEU A 187 ? 0.3407 0.4830 0.3029 -0.0294 -0.0120 0.0704  222 LEU A CD2 
1412 N N   . VAL A 188 ? 0.3433 0.5348 0.3262 -0.0297 -0.0503 0.1160  223 VAL A N   
1413 C CA  . VAL A 188 ? 0.2624 0.4656 0.2548 -0.0277 -0.0602 0.1286  223 VAL A CA  
1414 C C   . VAL A 188 ? 0.3254 0.5495 0.3130 -0.0343 -0.0666 0.1205  223 VAL A C   
1415 O O   . VAL A 188 ? 0.2841 0.5104 0.2709 -0.0376 -0.0641 0.1059  223 VAL A O   
1416 C CB  . VAL A 188 ? 0.3940 0.5862 0.4154 -0.0148 -0.0628 0.1381  223 VAL A CB  
1417 C CG1 . VAL A 188 ? 0.4064 0.5770 0.4327 -0.0102 -0.0573 0.1462  223 VAL A CG1 
1418 C CG2 . VAL A 188 ? 0.3162 0.5081 0.3537 -0.0099 -0.0609 0.1265  223 VAL A CG2 
1419 N N   . PRO A 189 ? 0.3085 0.5487 0.2922 -0.0374 -0.0751 0.1293  224 PRO A N   
1420 C CA  . PRO A 189 ? 0.2664 0.5277 0.2470 -0.0446 -0.0816 0.1211  224 PRO A CA  
1421 C C   . PRO A 189 ? 0.2874 0.5510 0.2921 -0.0388 -0.0833 0.1154  224 PRO A C   
1422 O O   . PRO A 189 ? 0.2540 0.5134 0.2829 -0.0270 -0.0860 0.1252  224 PRO A O   
1423 C CB  . PRO A 189 ? 0.3075 0.5842 0.2868 -0.0447 -0.0919 0.1368  224 PRO A CB  
1424 C CG  . PRO A 189 ? 0.2904 0.5553 0.2582 -0.0442 -0.0880 0.1482  224 PRO A CG  
1425 C CD  . PRO A 189 ? 0.2625 0.5030 0.2425 -0.0362 -0.0791 0.1469  224 PRO A CD  
1426 N N   . GLY A 190 ? 0.2201 0.4892 0.2191 -0.0475 -0.0808 0.0982  225 GLY A N   
1427 C CA  . GLY A 190 ? 0.2580 0.5309 0.2790 -0.0447 -0.0808 0.0911  225 GLY A CA  
1428 C C   . GLY A 190 ? 0.2323 0.4885 0.2581 -0.0425 -0.0714 0.0815  225 GLY A C   
1429 O O   . GLY A 190 ? 0.1907 0.4510 0.2317 -0.0437 -0.0695 0.0727  225 GLY A O   
1430 N N   . ILE A 191 ? 0.1745 0.4130 0.1883 -0.0398 -0.0651 0.0829  226 ILE A N   
1431 C CA  . ILE A 191 ? 0.1948 0.4122 0.2113 -0.0368 -0.0542 0.0727  226 ILE A CA  
1432 C C   . ILE A 191 ? 0.2567 0.4590 0.2466 -0.0433 -0.0459 0.0623  226 ILE A C   
1433 O O   . ILE A 191 ? 0.2654 0.4684 0.2412 -0.0436 -0.0465 0.0701  226 ILE A O   
1434 C CB  . ILE A 191 ? 0.1561 0.3576 0.1915 -0.0228 -0.0503 0.0819  226 ILE A CB  
1435 C CG1 . ILE A 191 ? 0.2770 0.4941 0.3410 -0.0140 -0.0581 0.0922  226 ILE A CG1 
1436 C CG2 . ILE A 191 ? 0.1821 0.3599 0.2188 -0.0204 -0.0377 0.0686  226 ILE A CG2 
1437 C CD1 . ILE A 191 ? 0.2200 0.4198 0.3031 -0.0003 -0.0541 0.0992  226 ILE A CD1 
1438 N N   . LYS A 192 ? 0.2189 0.4075 0.2036 -0.0482 -0.0377 0.0454  227 LYS A N   
1439 C CA  . LYS A 192 ? 0.2332 0.4062 0.1972 -0.0524 -0.0288 0.0332  227 LYS A CA  
1440 C C   . LYS A 192 ? 0.2361 0.3834 0.2075 -0.0448 -0.0183 0.0273  227 LYS A C   
1441 O O   . LYS A 192 ? 0.2137 0.3554 0.2000 -0.0422 -0.0170 0.0261  227 LYS A O   
1442 C CB  . LYS A 192 ? 0.2407 0.4181 0.1913 -0.0654 -0.0289 0.0171  227 LYS A CB  
1443 C CG  . LYS A 192 ? 0.4565 0.6620 0.3949 -0.0753 -0.0398 0.0200  227 LYS A CG  
1444 C CD  . LYS A 192 ? 0.4345 0.6426 0.3579 -0.0900 -0.0392 0.0006  227 LYS A CD  
1445 C CE  . LYS A 192 ? 0.5820 0.8145 0.4921 -0.0982 -0.0475 0.0031  227 LYS A CE  
1446 N NZ  . LYS A 192 ? 0.6995 0.9257 0.5882 -0.1089 -0.0411 -0.0170 227 LYS A NZ  
1447 N N   . ALA A 193 ? 0.2189 0.3535 0.1800 -0.0417 -0.0110 0.0242  228 ALA A N   
1448 C CA  . ALA A 193 ? 0.2319 0.3441 0.1967 -0.0358 -0.0021 0.0169  228 ALA A CA  
1449 C C   . ALA A 193 ? 0.2840 0.3852 0.2381 -0.0421 0.0030  0.0010  228 ALA A C   
1450 O O   . ALA A 193 ? 0.2558 0.3623 0.1946 -0.0486 0.0040  -0.0071 228 ALA A O   
1451 C CB  . ALA A 193 ? 0.2380 0.3446 0.2004 -0.0295 0.0029  0.0206  228 ALA A CB  
1452 N N   . LEU A 194 ? 0.2197 0.3047 0.1812 -0.0406 0.0066  -0.0034 229 LEU A N   
1453 C CA  . LEU A 194 ? 0.2389 0.3062 0.1933 -0.0453 0.0120  -0.0168 229 LEU A CA  
1454 C C   . LEU A 194 ? 0.2310 0.2770 0.1897 -0.0353 0.0186  -0.0166 229 LEU A C   
1455 O O   . LEU A 194 ? 0.2453 0.2865 0.2137 -0.0311 0.0184  -0.0095 229 LEU A O   
1456 C CB  . LEU A 194 ? 0.2927 0.3606 0.2531 -0.0546 0.0093  -0.0192 229 LEU A CB  
1457 C CG  . LEU A 194 ? 0.3308 0.3805 0.2839 -0.0637 0.0135  -0.0332 229 LEU A CG  
1458 C CD1 . LEU A 194 ? 0.3694 0.4255 0.3072 -0.0719 0.0129  -0.0461 229 LEU A CD1 
1459 C CD2 . LEU A 194 ? 0.3728 0.4234 0.3354 -0.0735 0.0117  -0.0327 229 LEU A CD2 
1460 N N   . ALA A 195 ? 0.2605 0.2956 0.2122 -0.0314 0.0244  -0.0247 230 ALA A N   
1461 C CA  . ALA A 195 ? 0.2788 0.2965 0.2362 -0.0208 0.0291  -0.0233 230 ALA A CA  
1462 C C   . ALA A 195 ? 0.2691 0.2669 0.2296 -0.0227 0.0301  -0.0234 230 ALA A C   
1463 O O   . ALA A 195 ? 0.2975 0.2843 0.2534 -0.0310 0.0316  -0.0321 230 ALA A O   
1464 C CB  . ALA A 195 ? 0.2780 0.2894 0.2305 -0.0156 0.0355  -0.0334 230 ALA A CB  
1465 N N   . SER A 196 ? 0.2645 0.2582 0.2320 -0.0163 0.0295  -0.0138 231 SER A N   
1466 C CA  . SER A 196 ? 0.2937 0.2695 0.2625 -0.0177 0.0310  -0.0106 231 SER A CA  
1467 C C   . SER A 196 ? 0.2488 0.2153 0.2202 -0.0060 0.0319  -0.0040 231 SER A C   
1468 O O   . SER A 196 ? 0.2666 0.2331 0.2397 -0.0047 0.0308  0.0044  231 SER A O   
1469 C CB  . SER A 196 ? 0.2578 0.2442 0.2308 -0.0259 0.0286  -0.0051 231 SER A CB  
1470 O OG  . SER A 196 ? 0.2761 0.2815 0.2554 -0.0213 0.0256  0.0015  231 SER A OG  
1471 N N   . HIS A 197 ? 0.2574 0.2195 0.2295 0.0027  0.0339  -0.0082 232 HIS A N   
1472 C CA  . HIS A 197 ? 0.2497 0.2102 0.2268 0.0145  0.0331  -0.0020 232 HIS A CA  
1473 C C   . HIS A 197 ? 0.3646 0.3042 0.3402 0.0173  0.0329  0.0050  232 HIS A C   
1474 O O   . HIS A 197 ? 0.3315 0.2503 0.3039 0.0130  0.0355  0.0024  232 HIS A O   
1475 C CB  . HIS A 197 ? 0.2308 0.1931 0.2119 0.0231  0.0361  -0.0091 232 HIS A CB  
1476 C CG  . HIS A 197 ? 0.3362 0.3184 0.3160 0.0192  0.0374  -0.0151 232 HIS A CG  
1477 N ND1 . HIS A 197 ? 0.3259 0.3245 0.3039 0.0121  0.0340  -0.0105 232 HIS A ND1 
1478 C CD2 . HIS A 197 ? 0.2905 0.2791 0.2702 0.0217  0.0422  -0.0244 232 HIS A CD2 
1479 C CE1 . HIS A 197 ? 0.2429 0.2562 0.2184 0.0097  0.0357  -0.0147 232 HIS A CE1 
1480 N NE2 . HIS A 197 ? 0.2837 0.2926 0.2591 0.0147  0.0413  -0.0237 232 HIS A NE2 
1481 N N   . GLY A 198 ? 0.2866 0.2314 0.2640 0.0241  0.0295  0.0142  233 GLY A N   
1482 C CA  . GLY A 198 ? 0.3072 0.2350 0.2820 0.0291  0.0281  0.0236  233 GLY A CA  
1483 C C   . GLY A 198 ? 0.3259 0.2635 0.2958 0.0279  0.0245  0.0337  233 GLY A C   
1484 O O   . GLY A 198 ? 0.3468 0.2834 0.3159 0.0360  0.0206  0.0417  233 GLY A O   
1485 N N   . HIS A 199 ? 0.2492 0.1993 0.2164 0.0186  0.0255  0.0328  234 HIS A N   
1486 C CA  . HIS A 199 ? 0.2671 0.2305 0.2304 0.0184  0.0233  0.0383  234 HIS A CA  
1487 C C   . HIS A 199 ? 0.2923 0.2711 0.2616 0.0264  0.0190  0.0363  234 HIS A C   
1488 O O   . HIS A 199 ? 0.2576 0.2421 0.2232 0.0304  0.0151  0.0415  234 HIS A O   
1489 C CB  . HIS A 199 ? 0.2707 0.2462 0.2348 0.0088  0.0262  0.0350  234 HIS A CB  
1490 C CG  . HIS A 199 ? 0.2670 0.2567 0.2280 0.0084  0.0258  0.0369  234 HIS A CG  
1491 N ND1 . HIS A 199 ? 0.2647 0.2515 0.2142 0.0067  0.0264  0.0445  234 HIS A ND1 
1492 C CD2 . HIS A 199 ? 0.1926 0.1987 0.1600 0.0091  0.0252  0.0315  234 HIS A CD2 
1493 C CE1 . HIS A 199 ? 0.2685 0.2714 0.2164 0.0061  0.0267  0.0417  234 HIS A CE1 
1494 N NE2 . HIS A 199 ? 0.2206 0.2337 0.1805 0.0079  0.0261  0.0333  234 HIS A NE2 
1495 N N   . THR A 200 ? 0.2308 0.2175 0.2087 0.0275  0.0196  0.0290  235 THR A N   
1496 C CA  . THR A 200 ? 0.2465 0.2460 0.2328 0.0340  0.0170  0.0264  235 THR A CA  
1497 C C   . THR A 200 ? 0.2534 0.2500 0.2453 0.0368  0.0200  0.0206  235 THR A C   
1498 O O   . THR A 200 ? 0.2468 0.2335 0.2351 0.0320  0.0236  0.0168  235 THR A O   
1499 C CB  . THR A 200 ? 0.2338 0.2490 0.2245 0.0296  0.0163  0.0233  235 THR A CB  
1500 O OG1 . THR A 200 ? 0.2438 0.2594 0.2358 0.0236  0.0193  0.0200  235 THR A OG1 
1501 C CG2 . THR A 200 ? 0.1987 0.2181 0.1842 0.0269  0.0148  0.0255  235 THR A CG2 
1502 N N   . PRO A 201 ? 0.2398 0.2468 0.2406 0.0436  0.0191  0.0186  236 PRO A N   
1503 C CA  . PRO A 201 ? 0.2121 0.2183 0.2180 0.0469  0.0238  0.0115  236 PRO A CA  
1504 C C   . PRO A 201 ? 0.2093 0.2200 0.2112 0.0383  0.0277  0.0056  236 PRO A C   
1505 O O   . PRO A 201 ? 0.2622 0.2676 0.2623 0.0383  0.0324  -0.0017 236 PRO A O   
1506 C CB  . PRO A 201 ? 0.2781 0.3019 0.2966 0.0544  0.0222  0.0112  236 PRO A CB  
1507 C CG  . PRO A 201 ? 0.2310 0.2568 0.2496 0.0580  0.0152  0.0192  236 PRO A CG  
1508 C CD  . PRO A 201 ? 0.2112 0.2320 0.2184 0.0488  0.0140  0.0220  236 PRO A CD  
1509 N N   . GLY A 202 ? 0.2118 0.2321 0.2123 0.0312  0.0257  0.0084  237 GLY A N   
1510 C CA  . GLY A 202 ? 0.1985 0.2251 0.1954 0.0236  0.0274  0.0058  237 GLY A CA  
1511 C C   . GLY A 202 ? 0.2049 0.2291 0.1977 0.0166  0.0251  0.0087  237 GLY A C   
1512 O O   . GLY A 202 ? 0.2248 0.2587 0.2180 0.0114  0.0239  0.0102  237 GLY A O   
1513 N N   . HIS A 203 ? 0.2040 0.2168 0.1939 0.0164  0.0246  0.0105  238 HIS A N   
1514 C CA  . HIS A 203 ? 0.2055 0.2195 0.1942 0.0096  0.0237  0.0126  238 HIS A CA  
1515 C C   . HIS A 203 ? 0.2215 0.2389 0.2074 0.0022  0.0239  0.0087  238 HIS A C   
1516 O O   . HIS A 203 ? 0.2283 0.2368 0.2086 0.0003  0.0263  0.0027  238 HIS A O   
1517 C CB  . HIS A 203 ? 0.2429 0.2441 0.2271 0.0087  0.0248  0.0152  238 HIS A CB  
1518 C CG  . HIS A 203 ? 0.2457 0.2523 0.2310 0.0018  0.0252  0.0171  238 HIS A CG  
1519 N ND1 . HIS A 203 ? 0.2413 0.2482 0.2264 -0.0067 0.0260  0.0145  238 HIS A ND1 
1520 C CD2 . HIS A 203 ? 0.2175 0.2319 0.2055 0.0019  0.0253  0.0199  238 HIS A CD2 
1521 C CE1 . HIS A 203 ? 0.2214 0.2378 0.2112 -0.0109 0.0267  0.0167  238 HIS A CE1 
1522 N NE2 . HIS A 203 ? 0.2024 0.2229 0.1937 -0.0054 0.0269  0.0195  238 HIS A NE2 
1523 N N   . THR A 204 ? 0.1934 0.2200 0.2007 -0.0127 0.0402  0.0198  239 THR A N   
1524 C CA  . THR A 204 ? 0.1705 0.1991 0.1620 -0.0154 0.0442  0.0147  239 THR A CA  
1525 C C   . THR A 204 ? 0.2179 0.2432 0.1984 -0.0207 0.0369  0.0114  239 THR A C   
1526 O O   . THR A 204 ? 0.2089 0.2350 0.1943 -0.0222 0.0296  0.0164  239 THR A O   
1527 C CB  . THR A 204 ? 0.2261 0.2682 0.2208 -0.0155 0.0463  0.0220  239 THR A CB  
1528 O OG1 . THR A 204 ? 0.2235 0.2710 0.2293 -0.0104 0.0543  0.0255  239 THR A OG1 
1529 C CG2 . THR A 204 ? 0.2178 0.2659 0.1945 -0.0185 0.0489  0.0187  239 THR A CG2 
1530 N N   . THR A 205 ? 0.2089 0.2306 0.1748 -0.0238 0.0394  0.0028  240 THR A N   
1531 C CA  . THR A 205 ? 0.2292 0.2525 0.1848 -0.0295 0.0334  0.0002  240 THR A CA  
1532 C C   . THR A 205 ? 0.2174 0.2558 0.1645 -0.0317 0.0333  0.0037  240 THR A C   
1533 O O   . THR A 205 ? 0.2457 0.2901 0.1875 -0.0305 0.0398  0.0027  240 THR A O   
1534 C CB  . THR A 205 ? 0.2407 0.2539 0.1859 -0.0333 0.0365  -0.0112 240 THR A CB  
1535 O OG1 . THR A 205 ? 0.2514 0.2508 0.2053 -0.0308 0.0365  -0.0120 240 THR A OG1 
1536 C CG2 . THR A 205 ? 0.2202 0.2399 0.1542 -0.0409 0.0308  -0.0144 240 THR A CG2 
1537 N N   . TYR A 206 ? 0.2124 0.2581 0.1585 -0.0341 0.0266  0.0089  241 TYR A N   
1538 C CA  . TYR A 206 ? 0.2030 0.2651 0.1420 -0.0354 0.0260  0.0148  241 TYR A CA  
1539 C C   . TYR A 206 ? 0.2330 0.3030 0.1599 -0.0415 0.0216  0.0105  241 TYR A C   
1540 O O   . TYR A 206 ? 0.2464 0.3142 0.1774 -0.0429 0.0161  0.0115  241 TYR A O   
1541 C CB  . TYR A 206 ? 0.2387 0.3054 0.1893 -0.0319 0.0234  0.0277  241 TYR A CB  
1542 C CG  . TYR A 206 ? 0.2148 0.2770 0.1777 -0.0282 0.0274  0.0319  241 TYR A CG  
1543 C CD1 . TYR A 206 ? 0.2207 0.2921 0.1823 -0.0267 0.0339  0.0357  241 TYR A CD1 
1544 C CD2 . TYR A 206 ? 0.1865 0.2372 0.1618 -0.0268 0.0249  0.0319  241 TYR A CD2 
1545 C CE1 . TYR A 206 ? 0.2503 0.3200 0.2255 -0.0239 0.0378  0.0405  241 TYR A CE1 
1546 C CE2 . TYR A 206 ? 0.1716 0.2215 0.1596 -0.0249 0.0275  0.0361  241 TYR A CE2 
1547 C CZ  . TYR A 206 ? 0.1772 0.2367 0.1663 -0.0235 0.0341  0.0406  241 TYR A CZ  
1548 O OH  . TYR A 206 ? 0.2143 0.2756 0.2185 -0.0221 0.0369  0.0458  241 TYR A OH  
1549 N N   . VAL A 207 ? 0.2192 0.2998 0.1311 -0.0455 0.0240  0.0056  242 VAL A N   
1550 C CA  . VAL A 207 ? 0.2792 0.3700 0.1786 -0.0536 0.0192  0.0000  242 VAL A CA  
1551 C C   . VAL A 207 ? 0.2896 0.4045 0.1857 -0.0534 0.0150  0.0122  242 VAL A C   
1552 O O   . VAL A 207 ? 0.2826 0.4084 0.1722 -0.0514 0.0189  0.0169  242 VAL A O   
1553 C CB  . VAL A 207 ? 0.2833 0.3694 0.1657 -0.0598 0.0243  -0.0156 242 VAL A CB  
1554 C CG1 . VAL A 207 ? 0.2827 0.3812 0.1521 -0.0707 0.0180  -0.0222 242 VAL A CG1 
1555 C CG2 . VAL A 207 ? 0.3413 0.4021 0.2296 -0.0580 0.0301  -0.0253 242 VAL A CG2 
1556 N N   . VAL A 208 ? 0.2787 0.4031 0.1800 -0.0550 0.0079  0.0184  243 VAL A N   
1557 C CA  . VAL A 208 ? 0.2594 0.4074 0.1617 -0.0532 0.0036  0.0329  243 VAL A CA  
1558 C C   . VAL A 208 ? 0.2699 0.4359 0.1619 -0.0622 -0.0027 0.0275  243 VAL A C   
1559 O O   . VAL A 208 ? 0.2997 0.4611 0.1896 -0.0693 -0.0058 0.0184  243 VAL A O   
1560 C CB  . VAL A 208 ? 0.2267 0.3707 0.1472 -0.0466 0.0012  0.0445  243 VAL A CB  
1561 C CG1 . VAL A 208 ? 0.2482 0.4143 0.1734 -0.0423 -0.0014 0.0614  243 VAL A CG1 
1562 C CG2 . VAL A 208 ? 0.2451 0.3668 0.1773 -0.0399 0.0062  0.0455  243 VAL A CG2 
1563 N N   . GLU A 209 ? 0.2533 0.4383 0.1424 -0.0619 -0.0045 0.0328  244 GLU A N   
1564 C CA  . GLU A 209 ? 0.3195 0.5213 0.2013 -0.0712 -0.0103 0.0266  244 GLU A CA  
1565 C C   . GLU A 209 ? 0.2731 0.5013 0.1624 -0.0672 -0.0144 0.0422  244 GLU A C   
1566 O O   . GLU A 209 ? 0.2644 0.4972 0.1531 -0.0608 -0.0109 0.0504  244 GLU A O   
1567 C CB  . GLU A 209 ? 0.4284 0.6238 0.2912 -0.0778 -0.0062 0.0105  244 GLU A CB  
1568 C CG  . GLU A 209 ? 0.5082 0.6773 0.3640 -0.0822 -0.0011 -0.0064 244 GLU A CG  
1569 C CD  . GLU A 209 ? 0.9458 1.1074 0.7836 -0.0891 0.0035  -0.0236 244 GLU A CD  
1570 O OE1 . GLU A 209 ? 0.5680 0.7152 0.3991 -0.0843 0.0127  -0.0288 244 GLU A OE1 
1571 O OE2 . GLU A 209 ? 0.4945 0.6650 0.3255 -0.0991 -0.0012 -0.0314 244 GLU A OE2 
1572 N N   . SER A 210 ? 0.2744 0.5209 0.1715 -0.0712 -0.0210 0.0469  245 SER A N   
1573 C CA  . SER A 210 ? 0.2763 0.5513 0.1811 -0.0683 -0.0247 0.0618  245 SER A CA  
1574 C C   . SER A 210 ? 0.3034 0.5997 0.2075 -0.0792 -0.0315 0.0585  245 SER A C   
1575 O O   . SER A 210 ? 0.2893 0.5821 0.2002 -0.0832 -0.0340 0.0555  245 SER A O   
1576 C CB  . SER A 210 ? 0.2901 0.5671 0.2154 -0.0559 -0.0234 0.0804  245 SER A CB  
1577 O OG  . SER A 210 ? 0.3007 0.6065 0.2355 -0.0531 -0.0263 0.0953  245 SER A OG  
1578 N N   . GLN A 211 ? 0.2730 0.5922 0.1690 -0.0842 -0.0344 0.0596  246 GLN A N   
1579 C CA  . GLN A 211 ? 0.3523 0.6955 0.2475 -0.0954 -0.0411 0.0577  246 GLN A CA  
1580 C C   . GLN A 211 ? 0.2960 0.6229 0.1829 -0.1079 -0.0424 0.0389  246 GLN A C   
1581 O O   . GLN A 211 ? 0.3217 0.6590 0.2167 -0.1144 -0.0467 0.0400  246 GLN A O   
1582 C CB  . GLN A 211 ? 0.3126 0.6800 0.2292 -0.0897 -0.0442 0.0774  246 GLN A CB  
1583 C CG  . GLN A 211 ? 0.2936 0.6769 0.2214 -0.0768 -0.0420 0.0975  246 GLN A CG  
1584 C CD  . GLN A 211 ? 0.3637 0.7733 0.2810 -0.0809 -0.0447 0.1008  246 GLN A CD  
1585 O OE1 . GLN A 211 ? 0.3291 0.7430 0.2281 -0.0934 -0.0480 0.0864  246 GLN A OE1 
1586 N NE2 . GLN A 211 ? 0.3110 0.7378 0.2399 -0.0701 -0.0429 0.1201  246 GLN A NE2 
1587 N N   . GLY A 212 ? 0.3546 0.6547 0.2262 -0.1108 -0.0376 0.0221  247 GLY A N   
1588 C CA  . GLY A 212 ? 0.3392 0.6199 0.2031 -0.1220 -0.0371 0.0037  247 GLY A CA  
1589 C C   . GLY A 212 ? 0.3988 0.6601 0.2747 -0.1191 -0.0357 0.0035  247 GLY A C   
1590 O O   . GLY A 212 ? 0.4409 0.6858 0.3128 -0.1283 -0.0350 -0.0105 247 GLY A O   
1591 N N   . GLN A 213 ? 0.2803 0.5419 0.1705 -0.1068 -0.0347 0.0184  248 GLN A N   
1592 C CA  . GLN A 213 ? 0.2601 0.5052 0.1609 -0.1032 -0.0336 0.0197  248 GLN A CA  
1593 C C   . GLN A 213 ? 0.3494 0.5675 0.2450 -0.0955 -0.0269 0.0153  248 GLN A C   
1594 O O   . GLN A 213 ? 0.3183 0.5380 0.2149 -0.0858 -0.0240 0.0244  248 GLN A O   
1595 C CB  . GLN A 213 ? 0.2883 0.5510 0.2082 -0.0938 -0.0360 0.0395  248 GLN A CB  
1596 C CG  . GLN A 213 ? 0.3682 0.6610 0.2964 -0.0999 -0.0418 0.0471  248 GLN A CG  
1597 C CD  . GLN A 213 ? 0.4760 0.7675 0.3964 -0.1156 -0.0449 0.0325  248 GLN A CD  
1598 O OE1 . GLN A 213 ? 0.4725 0.7483 0.3962 -0.1192 -0.0443 0.0260  248 GLN A OE1 
1599 N NE2 . GLN A 213 ? 0.5919 0.8995 0.5021 -0.1252 -0.0480 0.0273  248 GLN A NE2 
1600 N N   . LYS A 214 ? 0.3172 0.5111 0.2084 -0.0998 -0.0240 0.0023  249 LYS A N   
1601 C CA  . LYS A 214 ? 0.2850 0.4535 0.1696 -0.0944 -0.0169 -0.0039 249 LYS A CA  
1602 C C   . LYS A 214 ? 0.3186 0.4695 0.2161 -0.0883 -0.0152 -0.0001 249 LYS A C   
1603 O O   . LYS A 214 ? 0.2863 0.4350 0.1913 -0.0929 -0.0180 -0.0020 249 LYS A O   
1604 C CB  . LYS A 214 ? 0.3097 0.4594 0.1798 -0.1029 -0.0119 -0.0237 249 LYS A CB  
1605 C CG  . LYS A 214 ? 0.4446 0.5708 0.3090 -0.0963 -0.0028 -0.0292 249 LYS A CG  
1606 C CD  . LYS A 214 ? 0.5309 0.6347 0.3835 -0.1033 0.0040  -0.0488 249 LYS A CD  
1607 C CE  . LYS A 214 ? 0.5756 0.6886 0.4156 -0.1092 0.0045  -0.0567 249 LYS A CE  
1608 N NZ  . LYS A 214 ? 0.6539 0.7427 0.4823 -0.1093 0.0153  -0.0724 249 LYS A NZ  
1609 N N   . LEU A 215 ? 0.2809 0.4175 0.1847 -0.0770 -0.0098 0.0054  250 LEU A N   
1610 C CA  . LEU A 215 ? 0.2248 0.3413 0.1425 -0.0694 -0.0072 0.0083  250 LEU A CA  
1611 C C   . LEU A 215 ? 0.2653 0.3609 0.1822 -0.0641 -0.0004 0.0032  250 LEU A C   
1612 O O   . LEU A 215 ? 0.2488 0.3486 0.1642 -0.0592 0.0024  0.0084  250 LEU A O   
1613 C CB  . LEU A 215 ? 0.2710 0.3970 0.2012 -0.0603 -0.0089 0.0243  250 LEU A CB  
1614 C CG  . LEU A 215 ? 0.2391 0.3448 0.1810 -0.0519 -0.0058 0.0271  250 LEU A CG  
1615 C CD1 . LEU A 215 ? 0.2392 0.3333 0.1844 -0.0552 -0.0064 0.0207  250 LEU A CD1 
1616 C CD2 . LEU A 215 ? 0.2586 0.3719 0.2108 -0.0435 -0.0060 0.0413  250 LEU A CD2 
1617 N N   . ALA A 216 ? 0.2458 0.3206 0.1652 -0.0648 0.0027  -0.0052 251 ALA A N   
1618 C CA  . ALA A 216 ? 0.2394 0.2966 0.1606 -0.0593 0.0091  -0.0087 251 ALA A CA  
1619 C C   . ALA A 216 ? 0.2991 0.3462 0.2338 -0.0517 0.0084  -0.0014 251 ALA A C   
1620 O O   . ALA A 216 ? 0.2413 0.2806 0.1809 -0.0524 0.0067  -0.0022 251 ALA A O   
1621 C CB  . ALA A 216 ? 0.2690 0.3099 0.1841 -0.0642 0.0140  -0.0221 251 ALA A CB  
1622 N N   . LEU A 217 ? 0.2308 0.2791 0.1711 -0.0453 0.0098  0.0058  252 LEU A N   
1623 C CA  . LEU A 217 ? 0.2046 0.2437 0.1561 -0.0395 0.0090  0.0112  252 LEU A CA  
1624 C C   . LEU A 217 ? 0.2250 0.2507 0.1798 -0.0373 0.0128  0.0064  252 LEU A C   
1625 O O   . LEU A 217 ? 0.2169 0.2435 0.1728 -0.0351 0.0169  0.0068  252 LEU A O   
1626 C CB  . LEU A 217 ? 0.2081 0.2545 0.1649 -0.0354 0.0089  0.0208  252 LEU A CB  
1627 C CG  . LEU A 217 ? 0.2704 0.3322 0.2251 -0.0359 0.0062  0.0280  252 LEU A CG  
1628 C CD1 . LEU A 217 ? 0.2102 0.2767 0.1712 -0.0312 0.0079  0.0387  252 LEU A CD1 
1629 C CD2 . LEU A 217 ? 0.2773 0.3381 0.2355 -0.0357 0.0028  0.0293  252 LEU A CD2 
1630 N N   . LEU A 218 ? 0.2428 0.2578 0.2000 -0.0376 0.0120  0.0033  253 LEU A N   
1631 C CA  . LEU A 218 ? 0.2486 0.2518 0.2093 -0.0352 0.0160  -0.0002 253 LEU A CA  
1632 C C   . LEU A 218 ? 0.2671 0.2678 0.2383 -0.0299 0.0146  0.0057  253 LEU A C   
1633 O O   . LEU A 218 ? 0.2544 0.2486 0.2311 -0.0268 0.0174  0.0054  253 LEU A O   
1634 C CB  . LEU A 218 ? 0.2283 0.2217 0.1872 -0.0382 0.0163  -0.0046 253 LEU A CB  
1635 C CG  . LEU A 218 ? 0.2204 0.2154 0.1702 -0.0460 0.0170  -0.0118 253 LEU A CG  
1636 C CD1 . LEU A 218 ? 0.2673 0.2506 0.2187 -0.0490 0.0180  -0.0146 253 LEU A CD1 
1637 C CD2 . LEU A 218 ? 0.2551 0.2492 0.1970 -0.0482 0.0228  -0.0196 253 LEU A CD2 
1638 N N   . GLY A 219 ? 0.2351 0.2409 0.2097 -0.0291 0.0104  0.0111  254 GLY A N   
1639 C CA  . GLY A 219 ? 0.2295 0.2336 0.2132 -0.0263 0.0081  0.0152  254 GLY A CA  
1640 C C   . GLY A 219 ? 0.2767 0.2741 0.2615 -0.0252 0.0056  0.0148  254 GLY A C   
1641 O O   . GLY A 219 ? 0.2394 0.2338 0.2188 -0.0265 0.0034  0.0139  254 GLY A O   
1642 N N   . ASP A 220 ? 0.2220 0.2187 0.2145 -0.0223 0.0063  0.0169  255 ASP A N   
1643 C CA  . ASP A 220 ? 0.2039 0.1966 0.1984 -0.0202 0.0042  0.0191  255 ASP A CA  
1644 C C   . ASP A 220 ? 0.2956 0.2811 0.2914 -0.0176 0.0103  0.0179  255 ASP A C   
1645 O O   . ASP A 220 ? 0.2508 0.2349 0.2530 -0.0136 0.0104  0.0226  255 ASP A O   
1646 C CB  . ASP A 220 ? 0.2334 0.2329 0.2369 -0.0189 -0.0006 0.0242  255 ASP A CB  
1647 C CG  . ASP A 220 ? 0.2285 0.2294 0.2280 -0.0226 -0.0071 0.0236  255 ASP A CG  
1648 O OD1 . ASP A 220 ? 0.2573 0.2544 0.2492 -0.0244 -0.0064 0.0206  255 ASP A OD1 
1649 O OD2 . ASP A 220 ? 0.2103 0.2162 0.2141 -0.0237 -0.0125 0.0261  255 ASP A OD2 
1650 N N   . LEU A 221 ? 0.1993 0.1799 0.1889 -0.0199 0.0157  0.0118  256 LEU A N   
1651 C CA  . LEU A 221 ? 0.2584 0.2278 0.2480 -0.0187 0.0225  0.0087  256 LEU A CA  
1652 C C   . LEU A 221 ? 0.3084 0.2708 0.2971 -0.0194 0.0207  0.0111  256 LEU A C   
1653 O O   . LEU A 221 ? 0.5043 0.4568 0.4976 -0.0163 0.0258  0.0128  256 LEU A O   
1654 C CB  . LEU A 221 ? 0.3898 0.3556 0.3702 -0.0236 0.0275  -0.0004 256 LEU A CB  
1655 C CG  . LEU A 221 ? 0.3756 0.3428 0.3565 -0.0211 0.0343  -0.0037 256 LEU A CG  
1656 C CD1 . LEU A 221 ? 0.4495 0.4135 0.4173 -0.0275 0.0385  -0.0141 256 LEU A CD1 
1657 C CD2 . LEU A 221 ? 0.4064 0.3652 0.3978 -0.0137 0.0416  -0.0010 256 LEU A CD2 
1658 N N   . ILE A 222 ? 0.2582 0.2252 0.2415 -0.0227 0.0147  0.0121  257 ILE A N   
1659 C CA  . ILE A 222 ? 0.2980 0.2614 0.2804 -0.0225 0.0129  0.0163  257 ILE A CA  
1660 C C   . ILE A 222 ? 0.3383 0.3102 0.3188 -0.0212 0.0058  0.0207  257 ILE A C   
1661 O O   . ILE A 222 ? 0.3227 0.3006 0.3004 -0.0229 0.0026  0.0186  257 ILE A O   
1662 C CB  . ILE A 222 ? 0.4503 0.4089 0.4271 -0.0287 0.0149  0.0121  257 ILE A CB  
1663 C CG1 . ILE A 222 ? 0.3976 0.3532 0.3747 -0.0280 0.0143  0.0182  257 ILE A CG1 
1664 C CG2 . ILE A 222 ? 0.3202 0.2884 0.2912 -0.0333 0.0116  0.0084  257 ILE A CG2 
1665 C CD1 . ILE A 222 ? 0.4455 0.3964 0.4205 -0.0345 0.0172  0.0154  257 ILE A CD1 
1666 N N   . LEU A 223 ? 0.2775 0.2495 0.2595 -0.0180 0.0039  0.0270  258 LEU A N   
1667 C CA  . LEU A 223 ? 0.2673 0.2467 0.2455 -0.0172 -0.0028 0.0301  258 LEU A CA  
1668 C C   . LEU A 223 ? 0.3226 0.3013 0.2926 -0.0177 -0.0036 0.0325  258 LEU A C   
1669 O O   . LEU A 223 ? 0.3500 0.3326 0.3125 -0.0187 -0.0074 0.0308  258 LEU A O   
1670 C CB  . LEU A 223 ? 0.2676 0.2532 0.2534 -0.0131 -0.0057 0.0366  258 LEU A CB  
1671 C CG  . LEU A 223 ? 0.3174 0.3062 0.3131 -0.0120 -0.0041 0.0355  258 LEU A CG  
1672 C CD1 . LEU A 223 ? 0.3366 0.3349 0.3433 -0.0075 -0.0066 0.0438  258 LEU A CD1 
1673 C CD2 . LEU A 223 ? 0.3082 0.3009 0.3009 -0.0162 -0.0073 0.0300  258 LEU A CD2 
1674 N N   . VAL A 224 ? 0.2754 0.2483 0.2468 -0.0169 0.0007  0.0365  259 VAL A N   
1675 C CA  . VAL A 224 ? 0.3054 0.2788 0.2702 -0.0169 0.0011  0.0409  259 VAL A CA  
1676 C C   . VAL A 224 ? 0.2657 0.2317 0.2327 -0.0208 0.0071  0.0392  259 VAL A C   
1677 O O   . VAL A 224 ? 0.2694 0.2269 0.2429 -0.0205 0.0120  0.0423  259 VAL A O   
1678 C CB  . VAL A 224 ? 0.3054 0.2814 0.2714 -0.0121 0.0000  0.0510  259 VAL A CB  
1679 C CG1 . VAL A 224 ? 0.3052 0.2841 0.2617 -0.0120 0.0002  0.0556  259 VAL A CG1 
1680 C CG2 . VAL A 224 ? 0.3264 0.3122 0.2931 -0.0098 -0.0069 0.0525  259 VAL A CG2 
1681 N N   . ALA A 225 ? 0.2730 0.2426 0.2357 -0.0246 0.0070  0.0348  260 ALA A N   
1682 C CA  . ALA A 225 ? 0.3338 0.3003 0.2998 -0.0304 0.0113  0.0325  260 ALA A CA  
1683 C C   . ALA A 225 ? 0.2546 0.2154 0.2232 -0.0311 0.0157  0.0395  260 ALA A C   
1684 O O   . ALA A 225 ? 0.2983 0.2501 0.2731 -0.0357 0.0203  0.0382  260 ALA A O   
1685 C CB  . ALA A 225 ? 0.3300 0.3059 0.2927 -0.0331 0.0099  0.0297  260 ALA A CB  
1686 N N   . ALA A 226 ? 0.2647 0.2302 0.2283 -0.0269 0.0149  0.0469  261 ALA A N   
1687 C CA  . ALA A 226 ? 0.2943 0.2563 0.2602 -0.0273 0.0198  0.0557  261 ALA A CA  
1688 C C   . ALA A 226 ? 0.3116 0.2625 0.2851 -0.0245 0.0232  0.0619  261 ALA A C   
1689 O O   . ALA A 226 ? 0.3590 0.3040 0.3370 -0.0252 0.0286  0.0700  261 ALA A O   
1690 C CB  . ALA A 226 ? 0.3990 0.3706 0.3552 -0.0230 0.0186  0.0623  261 ALA A CB  
1691 N N   . VAL A 227 ? 0.2769 0.2249 0.2533 -0.0207 0.0212  0.0596  262 VAL A N   
1692 C CA  . VAL A 227 ? 0.2933 0.2308 0.2791 -0.0163 0.0257  0.0659  262 VAL A CA  
1693 C C   . VAL A 227 ? 0.3210 0.2456 0.3137 -0.0196 0.0305  0.0564  262 VAL A C   
1694 O O   . VAL A 227 ? 0.3098 0.2186 0.3100 -0.0211 0.0383  0.0576  262 VAL A O   
1695 C CB  . VAL A 227 ? 0.3410 0.2883 0.3266 -0.0079 0.0206  0.0735  262 VAL A CB  
1696 C CG1 . VAL A 227 ? 0.2723 0.2101 0.2708 -0.0019 0.0260  0.0800  262 VAL A CG1 
1697 C CG2 . VAL A 227 ? 0.3353 0.2938 0.3124 -0.0050 0.0171  0.0838  262 VAL A CG2 
1698 N N   . GLN A 228 ? 0.2608 0.1907 0.2503 -0.0211 0.0267  0.0468  263 GLN A N   
1699 C CA  . GLN A 228 ? 0.2852 0.2054 0.2794 -0.0217 0.0312  0.0389  263 GLN A CA  
1700 C C   . GLN A 228 ? 0.3472 0.2598 0.3387 -0.0316 0.0345  0.0274  263 GLN A C   
1701 O O   . GLN A 228 ? 0.3536 0.2560 0.3467 -0.0330 0.0397  0.0196  263 GLN A O   
1702 C CB  . GLN A 228 ? 0.2726 0.2036 0.2655 -0.0179 0.0260  0.0361  263 GLN A CB  
1703 C CG  . GLN A 228 ? 0.2691 0.2078 0.2670 -0.0093 0.0228  0.0469  263 GLN A CG  
1704 C CD  . GLN A 228 ? 0.2756 0.2270 0.2730 -0.0078 0.0166  0.0444  263 GLN A CD  
1705 O OE1 . GLN A 228 ? 0.2720 0.2301 0.2619 -0.0122 0.0118  0.0384  263 GLN A OE1 
1706 N NE2 . GLN A 228 ? 0.2749 0.2301 0.2820 -0.0013 0.0173  0.0501  263 GLN A NE2 
1707 N N   . PHE A 229 ? 0.3132 0.2322 0.3005 -0.0387 0.0319  0.0261  264 PHE A N   
1708 C CA  . PHE A 229 ? 0.3420 0.2551 0.3285 -0.0496 0.0348  0.0165  264 PHE A CA  
1709 C C   . PHE A 229 ? 0.3532 0.2476 0.3468 -0.0533 0.0430  0.0184  264 PHE A C   
1710 O O   . PHE A 229 ? 0.3623 0.2421 0.3567 -0.0597 0.0486  0.0088  264 PHE A O   
1711 C CB  . PHE A 229 ? 0.3285 0.2579 0.3111 -0.0560 0.0293  0.0157  264 PHE A CB  
1712 C CG  . PHE A 229 ? 0.2985 0.2425 0.2751 -0.0551 0.0233  0.0110  264 PHE A CG  
1713 C CD1 . PHE A 229 ? 0.3042 0.2476 0.2774 -0.0589 0.0235  0.0014  264 PHE A CD1 
1714 C CD2 . PHE A 229 ? 0.3055 0.2633 0.2793 -0.0504 0.0183  0.0164  264 PHE A CD2 
1715 C CE1 . PHE A 229 ? 0.3585 0.3160 0.3270 -0.0577 0.0185  -0.0007 264 PHE A CE1 
1716 C CE2 . PHE A 229 ? 0.3726 0.3418 0.3426 -0.0493 0.0139  0.0133  264 PHE A CE2 
1717 C CZ  . PHE A 229 ? 0.3390 0.3087 0.3070 -0.0528 0.0138  0.0058  264 PHE A CZ  
1718 N N   . ASP A 230 ? 0.2973 0.1912 0.2953 -0.0495 0.0443  0.0308  265 ASP A N   
1719 C CA  . ASP A 230 ? 0.3208 0.1961 0.3273 -0.0521 0.0529  0.0356  265 ASP A CA  
1720 C C   . ASP A 230 ? 0.4563 0.3128 0.4692 -0.0445 0.0605  0.0367  265 ASP A C   
1721 O O   . ASP A 230 ? 0.4131 0.2475 0.4323 -0.0488 0.0698  0.0332  265 ASP A O   
1722 C CB  . ASP A 230 ? 0.4310 0.3133 0.4398 -0.0478 0.0526  0.0512  265 ASP A CB  
1723 C CG  . ASP A 230 ? 0.5772 0.4731 0.5837 -0.0564 0.0495  0.0512  265 ASP A CG  
1724 O OD1 . ASP A 230 ? 0.6586 0.5553 0.6652 -0.0675 0.0487  0.0405  265 ASP A OD1 
1725 O OD2 . ASP A 230 ? 0.6553 0.5626 0.6597 -0.0518 0.0480  0.0623  265 ASP A OD2 
1726 N N   . ASP A 231 ? 0.3828 0.2476 0.3954 -0.0330 0.0574  0.0419  266 ASP A N   
1727 C CA  . ASP A 231 ? 0.3583 0.2100 0.3794 -0.0234 0.0645  0.0456  266 ASP A CA  
1728 C C   . ASP A 231 ? 0.3141 0.1769 0.3315 -0.0188 0.0601  0.0393  266 ASP A C   
1729 O O   . ASP A 231 ? 0.3315 0.2103 0.3497 -0.0107 0.0538  0.0478  266 ASP A O   
1730 C CB  . ASP A 231 ? 0.4150 0.2689 0.4443 -0.0127 0.0658  0.0648  266 ASP A CB  
1731 C CG  . ASP A 231 ? 0.4687 0.3082 0.5106 -0.0020 0.0752  0.0711  266 ASP A CG  
1732 O OD1 . ASP A 231 ? 0.4340 0.2623 0.4771 -0.0021 0.0807  0.0595  266 ASP A OD1 
1733 O OD2 . ASP A 231 ? 0.5340 0.3745 0.5847 0.0073  0.0774  0.0885  266 ASP A OD2 
1734 N N   . PRO A 232 ? 0.3501 0.2056 0.3631 -0.0245 0.0633  0.0244  267 PRO A N   
1735 C CA  . PRO A 232 ? 0.3273 0.1941 0.3371 -0.0204 0.0600  0.0192  267 PRO A CA  
1736 C C   . PRO A 232 ? 0.3864 0.2509 0.4071 -0.0075 0.0653  0.0273  267 PRO A C   
1737 O O   . PRO A 232 ? 0.3760 0.2530 0.3966 -0.0035 0.0621  0.0259  267 PRO A O   
1738 C CB  . PRO A 232 ? 0.3760 0.2339 0.3773 -0.0300 0.0640  0.0020  267 PRO A CB  
1739 C CG  . PRO A 232 ? 0.4304 0.2791 0.4290 -0.0417 0.0651  -0.0024 267 PRO A CG  
1740 C CD  . PRO A 232 ? 0.3667 0.2054 0.3760 -0.0365 0.0692  0.0112  267 PRO A CD  
1741 N N   . SER A 233 ? 0.3634 0.2134 0.3953 -0.0007 0.0735  0.0370  268 SER A N   
1742 C CA  . SER A 233 ? 0.3357 0.1862 0.3808 0.0128  0.0789  0.0466  268 SER A CA  
1743 C C   . SER A 233 ? 0.3806 0.2557 0.4309 0.0205  0.0687  0.0627  268 SER A C   
1744 O O   . SER A 233 ? 0.3779 0.2614 0.4398 0.0309  0.0703  0.0713  268 SER A O   
1745 C CB  . SER A 233 ? 0.3933 0.2177 0.4503 0.0187  0.0934  0.0518  268 SER A CB  
1746 O OG  . SER A 233 ? 0.4722 0.2947 0.5335 0.0193  0.0922  0.0653  268 SER A OG  
1747 N N   . VAL A 234 ? 0.3474 0.2355 0.3895 0.0154  0.0585  0.0666  269 VAL A N   
1748 C CA  . VAL A 234 ? 0.3792 0.2901 0.4231 0.0211  0.0484  0.0799  269 VAL A CA  
1749 C C   . VAL A 234 ? 0.2934 0.2221 0.3336 0.0196  0.0400  0.0736  269 VAL A C   
1750 O O   . VAL A 234 ? 0.2771 0.2075 0.3062 0.0112  0.0360  0.0615  269 VAL A O   
1751 C CB  . VAL A 234 ? 0.3977 0.3148 0.4317 0.0162  0.0419  0.0848  269 VAL A CB  
1752 C CG1 . VAL A 234 ? 0.3323 0.2727 0.3655 0.0215  0.0318  0.0975  269 VAL A CG1 
1753 C CG2 . VAL A 234 ? 0.3590 0.2574 0.3974 0.0160  0.0512  0.0910  269 VAL A CG2 
1754 N N   . THR A 235 ? 0.2889 0.2322 0.3401 0.0276  0.0375  0.0831  270 THR A N   
1755 C CA  . THR A 235 ? 0.3006 0.2614 0.3518 0.0261  0.0301  0.0792  270 THR A CA  
1756 C C   . THR A 235 ? 0.2557 0.2390 0.3049 0.0258  0.0172  0.0883  270 THR A C   
1757 O O   . THR A 235 ? 0.3168 0.3030 0.3622 0.0270  0.0141  0.0971  270 THR A O   
1758 C CB  . THR A 235 ? 0.3474 0.3091 0.4142 0.0342  0.0378  0.0819  270 THR A CB  
1759 O OG1 . THR A 235 ? 0.3195 0.2886 0.4019 0.0449  0.0395  0.0991  270 THR A OG1 
1760 C CG2 . THR A 235 ? 0.3170 0.2544 0.3824 0.0338  0.0514  0.0706  270 THR A CG2 
1761 N N   . THR A 236 ? 0.2911 0.2906 0.3420 0.0234  0.0099  0.0858  271 THR A N   
1762 C CA  . THR A 236 ? 0.2606 0.2815 0.3092 0.0212  -0.0027 0.0919  271 THR A CA  
1763 C C   . THR A 236 ? 0.2703 0.3106 0.3364 0.0258  -0.0056 0.1005  271 THR A C   
1764 O O   . THR A 236 ? 0.2647 0.3019 0.3431 0.0300  0.0022  0.0995  271 THR A O   
1765 C CB  . THR A 236 ? 0.3188 0.3416 0.3519 0.0110  -0.0104 0.0797  271 THR A CB  
1766 O OG1 . THR A 236 ? 0.3800 0.4053 0.4187 0.0082  -0.0099 0.0727  271 THR A OG1 
1767 C CG2 . THR A 236 ? 0.3561 0.3615 0.3750 0.0068  -0.0062 0.0711  271 THR A CG2 
1768 N N   . ASP A 237 ? 0.2794 0.3416 0.3463 0.0246  -0.0170 0.1091  272 ASP A N   
1769 C CA  . ASP A 237 ? 0.3098 0.3957 0.3942 0.0267  -0.0223 0.1177  272 ASP A CA  
1770 C C   . ASP A 237 ? 0.2479 0.3386 0.3328 0.0181  -0.0262 0.1067  272 ASP A C   
1771 O O   . ASP A 237 ? 0.3477 0.4583 0.4490 0.0185  -0.0300 0.1130  272 ASP A O   
1772 C CB  . ASP A 237 ? 0.3566 0.4673 0.4416 0.0268  -0.0344 0.1307  272 ASP A CB  
1773 C CG  . ASP A 237 ? 0.4238 0.5381 0.4864 0.0152  -0.0460 0.1213  272 ASP A CG  
1774 O OD1 . ASP A 237 ? 0.4478 0.5444 0.4961 0.0085  -0.0440 0.1061  272 ASP A OD1 
1775 O OD2 . ASP A 237 ? 0.6793 0.8147 0.7383 0.0133  -0.0569 0.1294  272 ASP A OD2 
1776 N N   . LEU A 238 ? 0.2570 0.3312 0.3259 0.0107  -0.0251 0.0920  273 LEU A N   
1777 C CA  . LEU A 238 ? 0.3183 0.3935 0.3881 0.0036  -0.0265 0.0827  273 LEU A CA  
1778 C C   . LEU A 238 ? 0.3715 0.4350 0.4482 0.0079  -0.0142 0.0787  273 LEU A C   
1779 O O   . LEU A 238 ? 0.3659 0.4317 0.4453 0.0034  -0.0137 0.0733  273 LEU A O   
1780 C CB  . LEU A 238 ? 0.3704 0.4348 0.4200 -0.0056 -0.0311 0.0704  273 LEU A CB  
1781 C CG  . LEU A 238 ? 0.5492 0.6249 0.5892 -0.0125 -0.0433 0.0701  273 LEU A CG  
1782 C CD1 . LEU A 238 ? 0.6103 0.6704 0.6294 -0.0180 -0.0438 0.0587  273 LEU A CD1 
1783 C CD2 . LEU A 238 ? 0.5760 0.6690 0.6269 -0.0194 -0.0513 0.0705  273 LEU A CD2 
1784 N N   . ASP A 239 ? 0.2796 0.3299 0.3582 0.0159  -0.0037 0.0808  274 ASP A N   
1785 C CA  . ASP A 239 ? 0.3035 0.3423 0.3864 0.0199  0.0087  0.0757  274 ASP A CA  
1786 C C   . ASP A 239 ? 0.2726 0.3266 0.3776 0.0277  0.0131  0.0857  274 ASP A C   
1787 O O   . ASP A 239 ? 0.2665 0.3312 0.3848 0.0350  0.0122  0.0986  274 ASP A O   
1788 C CB  . ASP A 239 ? 0.2431 0.2597 0.3193 0.0242  0.0187  0.0726  274 ASP A CB  
1789 C CG  . ASP A 239 ? 0.3317 0.3352 0.3881 0.0163  0.0155  0.0629  274 ASP A CG  
1790 O OD1 . ASP A 239 ? 0.2940 0.2960 0.3407 0.0092  0.0133  0.0534  274 ASP A OD1 
1791 O OD2 . ASP A 239 ? 0.3533 0.3490 0.4052 0.0176  0.0157  0.0664  274 ASP A OD2 
1792 N N   . SER A 240 ? 0.2111 0.2681 0.3209 0.0266  0.0181  0.0813  275 SER A N   
1793 C CA  . SER A 240 ? 0.2187 0.2922 0.3509 0.0341  0.0235  0.0911  275 SER A CA  
1794 C C   . SER A 240 ? 0.2735 0.3353 0.4143 0.0470  0.0382  0.0953  275 SER A C   
1795 O O   . SER A 240 ? 0.2840 0.3608 0.4464 0.0566  0.0417  0.1086  275 SER A O   
1796 C CB  . SER A 240 ? 0.2767 0.3552 0.4105 0.0297  0.0268  0.0855  275 SER A CB  
1797 O OG  . SER A 240 ? 0.4599 0.5497 0.5908 0.0184  0.0141  0.0839  275 SER A OG  
1798 N N   . ASP A 241 ? 0.2239 0.2595 0.3494 0.0473  0.0473  0.0842  276 ASP A N   
1799 C CA  . ASP A 241 ? 0.2855 0.3037 0.4166 0.0582  0.0633  0.0847  276 ASP A CA  
1800 C C   . ASP A 241 ? 0.3184 0.3113 0.4323 0.0545  0.0647  0.0765  276 ASP A C   
1801 O O   . ASP A 241 ? 0.3280 0.3058 0.4237 0.0466  0.0668  0.0619  276 ASP A O   
1802 C CB  . ASP A 241 ? 0.2769 0.2896 0.4074 0.0607  0.0764  0.0761  276 ASP A CB  
1803 C CG  . ASP A 241 ? 0.4654 0.4565 0.5995 0.0715  0.0948  0.0736  276 ASP A CG  
1804 O OD1 . ASP A 241 ? 0.3856 0.3627 0.5225 0.0764  0.0978  0.0780  276 ASP A OD1 
1805 O OD2 . ASP A 241 ? 0.4759 0.4637 0.6103 0.0754  0.1073  0.0674  276 ASP A OD2 
1806 N N   . SER A 242 ? 0.2763 0.2669 0.3968 0.0599  0.0635  0.0874  277 SER A N   
1807 C CA  . SER A 242 ? 0.3048 0.2751 0.4111 0.0553  0.0631  0.0824  277 SER A CA  
1808 C C   . SER A 242 ? 0.4022 0.3429 0.5009 0.0556  0.0783  0.0696  277 SER A C   
1809 O O   . SER A 242 ? 0.3830 0.3089 0.4643 0.0458  0.0770  0.0575  277 SER A O   
1810 C CB  . SER A 242 ? 0.4097 0.3851 0.5266 0.0624  0.0603  0.0993  277 SER A CB  
1811 O OG  . SER A 242 ? 0.7891 0.7925 0.9092 0.0599  0.0449  0.1090  277 SER A OG  
1812 N N   . LYS A 243 ? 0.3485 0.2804 0.4602 0.0665  0.0930  0.0720  278 LYS A N   
1813 C CA  . LYS A 243 ? 0.3924 0.2934 0.4958 0.0663  0.1085  0.0582  278 LYS A CA  
1814 C C   . LYS A 243 ? 0.3823 0.2802 0.4655 0.0549  0.1077  0.0393  278 LYS A C   
1815 O O   . LYS A 243 ? 0.4727 0.3510 0.5394 0.0457  0.1102  0.0252  278 LYS A O   
1816 C CB  . LYS A 243 ? 0.3700 0.2631 0.4915 0.0816  0.1258  0.0642  278 LYS A CB  
1817 C CG  . LYS A 243 ? 0.5592 0.4413 0.6975 0.0929  0.1327  0.0796  278 LYS A CG  
1818 C CD  . LYS A 243 ? 0.7582 0.6106 0.9009 0.1010  0.1541  0.0734  278 LYS A CD  
1819 C CE  . LYS A 243 ? 0.9074 0.7455 1.0539 0.1014  0.1570  0.0809  278 LYS A CE  
1820 N NZ  . LYS A 243 ? 0.7602 0.5663 0.8996 0.0993  0.1735  0.0665  278 LYS A NZ  
1821 N N   . ALA A 244 ? 0.3229 0.2423 0.4080 0.0548  0.1034  0.0399  279 ALA A N   
1822 C CA  . ALA A 244 ? 0.3068 0.2269 0.3738 0.0451  0.1023  0.0250  279 ALA A CA  
1823 C C   . ALA A 244 ? 0.3790 0.3006 0.4296 0.0319  0.0889  0.0191  279 ALA A C   
1824 O O   . ALA A 244 ? 0.3678 0.2788 0.4009 0.0231  0.0904  0.0052  279 ALA A O   
1825 C CB  . ALA A 244 ? 0.3120 0.2564 0.3871 0.0479  0.1002  0.0302  279 ALA A CB  
1826 N N   . VAL A 245 ? 0.3010 0.2369 0.3567 0.0304  0.0758  0.0296  280 VAL A N   
1827 C CA  . VAL A 245 ? 0.3549 0.2930 0.3962 0.0194  0.0643  0.0247  280 VAL A CA  
1828 C C   . VAL A 245 ? 0.2925 0.2094 0.3245 0.0146  0.0680  0.0180  280 VAL A C   
1829 O O   . VAL A 245 ? 0.3886 0.3022 0.4062 0.0047  0.0646  0.0080  280 VAL A O   
1830 C CB  . VAL A 245 ? 0.3452 0.3022 0.3921 0.0189  0.0507  0.0358  280 VAL A CB  
1831 C CG1 . VAL A 245 ? 0.4016 0.3558 0.4562 0.0239  0.0492  0.0466  280 VAL A CG1 
1832 C CG2 . VAL A 245 ? 0.3213 0.2831 0.3539 0.0086  0.0407  0.0297  280 VAL A CG2 
1833 N N   . ALA A 246 ? 0.2973 0.2004 0.3391 0.0215  0.0756  0.0240  281 ALA A N   
1834 C CA  . ALA A 246 ? 0.3467 0.2273 0.3816 0.0160  0.0808  0.0175  281 ALA A CA  
1835 C C   . ALA A 246 ? 0.4143 0.2786 0.4368 0.0094  0.0900  -0.0002 281 ALA A C   
1836 O O   . ALA A 246 ? 0.4026 0.2598 0.4123 -0.0021 0.0874  -0.0104 281 ALA A O   
1837 C CB  . ALA A 246 ? 0.4464 0.3139 0.4963 0.0258  0.0889  0.0291  281 ALA A CB  
1838 N N   . VAL A 247 ? 0.3452 0.2056 0.3710 0.0162  0.1006  -0.0042 282 VAL A N   
1839 C CA  . VAL A 247 ? 0.3798 0.2254 0.3908 0.0099  0.1100  -0.0224 282 VAL A CA  
1840 C C   . VAL A 247 ? 0.4009 0.2625 0.3947 -0.0020 0.0994  -0.0311 282 VAL A C   
1841 O O   . VAL A 247 ? 0.4243 0.2771 0.4029 -0.0136 0.0994  -0.0445 282 VAL A O   
1842 C CB  . VAL A 247 ? 0.4134 0.2549 0.4308 0.0210  0.1241  -0.0239 282 VAL A CB  
1843 C CG1 . VAL A 247 ? 0.4176 0.2507 0.4151 0.0135  0.1315  -0.0433 282 VAL A CG1 
1844 C CG2 . VAL A 247 ? 0.5642 0.3839 0.5974 0.0323  0.1377  -0.0175 282 VAL A CG2 
1845 N N   . GLU A 248 ? 0.3496 0.2354 0.3465 0.0005  0.0904  -0.0230 283 GLU A N   
1846 C CA  . GLU A 248 ? 0.3598 0.2614 0.3428 -0.0085 0.0818  -0.0286 283 GLU A CA  
1847 C C   . GLU A 248 ? 0.3501 0.2544 0.3263 -0.0185 0.0709  -0.0292 283 GLU A C   
1848 O O   . GLU A 248 ? 0.3581 0.2668 0.3204 -0.0282 0.0674  -0.0380 283 GLU A O   
1849 C CB  . GLU A 248 ? 0.3524 0.2763 0.3431 -0.0033 0.0762  -0.0187 283 GLU A CB  
1850 C CG  . GLU A 248 ? 0.3309 0.2572 0.3266 0.0049  0.0874  -0.0191 283 GLU A CG  
1851 C CD  . GLU A 248 ? 0.6128 0.5313 0.5903 0.0000  0.0963  -0.0344 283 GLU A CD  
1852 O OE1 . GLU A 248 ? 0.6347 0.5615 0.5969 -0.0097 0.0895  -0.0403 283 GLU A OE1 
1853 O OE2 . GLU A 248 ? 0.6499 0.5546 0.6279 0.0060  0.1105  -0.0403 283 GLU A OE2 
1854 N N   . ARG A 249 ? 0.3391 0.2428 0.3251 -0.0159 0.0657  -0.0190 284 ARG A N   
1855 C CA  . ARG A 249 ? 0.3011 0.2068 0.2818 -0.0242 0.0574  -0.0189 284 ARG A CA  
1856 C C   . ARG A 249 ? 0.3513 0.2398 0.3241 -0.0334 0.0628  -0.0301 284 ARG A C   
1857 O O   . ARG A 249 ? 0.3500 0.2450 0.3134 -0.0438 0.0571  -0.0359 284 ARG A O   
1858 C CB  . ARG A 249 ? 0.3332 0.2407 0.3245 -0.0189 0.0527  -0.0059 284 ARG A CB  
1859 C CG  . ARG A 249 ? 0.3616 0.2702 0.3482 -0.0264 0.0464  -0.0049 284 ARG A CG  
1860 C CD  . ARG A 249 ? 0.3589 0.2691 0.3539 -0.0204 0.0433  0.0079  284 ARG A CD  
1861 N NE  . ARG A 249 ? 0.4750 0.4008 0.4744 -0.0139 0.0372  0.0153  284 ARG A NE  
1862 C CZ  . ARG A 249 ? 0.4708 0.4007 0.4792 -0.0063 0.0357  0.0264  284 ARG A CZ  
1863 N NH1 . ARG A 249 ? 0.4666 0.3857 0.4817 -0.0021 0.0409  0.0333  284 ARG A NH1 
1864 N NH2 . ARG A 249 ? 0.4339 0.3796 0.4453 -0.0032 0.0288  0.0314  284 ARG A NH2 
1865 N N   . LYS A 250 ? 0.3437 0.2105 0.3218 -0.0299 0.0740  -0.0328 285 LYS A N   
1866 C CA  . LYS A 250 ? 0.4074 0.2550 0.3782 -0.0404 0.0798  -0.0451 285 LYS A CA  
1867 C C   . LYS A 250 ? 0.3746 0.2256 0.3286 -0.0499 0.0806  -0.0611 285 LYS A C   
1868 O O   . LYS A 250 ? 0.4358 0.2868 0.3801 -0.0633 0.0769  -0.0702 285 LYS A O   
1869 C CB  . LYS A 250 ? 0.4361 0.2561 0.4165 -0.0343 0.0935  -0.0450 285 LYS A CB  
1870 C CG  . LYS A 250 ? 0.5791 0.3974 0.5749 -0.0268 0.0918  -0.0279 285 LYS A CG  
1871 C CD  . LYS A 250 ? 0.7521 0.5445 0.7601 -0.0181 0.1062  -0.0243 285 LYS A CD  
1872 C CE  . LYS A 250 ? 0.7665 0.5685 0.7911 -0.0037 0.1044  -0.0036 285 LYS A CE  
1873 N NZ  . LYS A 250 ? 0.7932 0.5711 0.8323 0.0063  0.1189  0.0033  285 LYS A NZ  
1874 N N   . LYS A 251 ? 0.3990 0.2558 0.3492 -0.0434 0.0849  -0.0636 286 LYS A N   
1875 C CA  . LYS A 251 ? 0.4435 0.3064 0.3757 -0.0516 0.0858  -0.0776 286 LYS A CA  
1876 C C   . LYS A 251 ? 0.3650 0.2529 0.2893 -0.0605 0.0717  -0.0755 286 LYS A C   
1877 O O   . LYS A 251 ? 0.4156 0.3072 0.3260 -0.0732 0.0689  -0.0866 286 LYS A O   
1878 C CB  . LYS A 251 ? 0.4121 0.2802 0.3444 -0.0410 0.0931  -0.0767 286 LYS A CB  
1879 C CG  . LYS A 251 ? 0.5051 0.3793 0.4173 -0.0475 0.0963  -0.0905 286 LYS A CG  
1880 C CD  . LYS A 251 ? 0.5792 0.4577 0.4938 -0.0356 0.1058  -0.0879 286 LYS A CD  
1881 C CE  . LYS A 251 ? 0.5447 0.4019 0.4750 -0.0232 0.1191  -0.0847 286 LYS A CE  
1882 N NZ  . LYS A 251 ? 0.6692 0.5351 0.6068 -0.0103 0.1278  -0.0787 286 LYS A NZ  
1883 N N   . ALA A 252 ? 0.3905 0.2961 0.3241 -0.0542 0.0630  -0.0612 287 ALA A N   
1884 C CA  . ALA A 252 ? 0.3127 0.2408 0.2411 -0.0603 0.0513  -0.0573 287 ALA A CA  
1885 C C   . ALA A 252 ? 0.3275 0.2549 0.2553 -0.0708 0.0458  -0.0593 287 ALA A C   
1886 O O   . ALA A 252 ? 0.3683 0.3096 0.2867 -0.0808 0.0399  -0.0638 287 ALA A O   
1887 C CB  . ALA A 252 ? 0.3812 0.3231 0.3205 -0.0511 0.0449  -0.0428 287 ALA A CB  
1888 N N   . PHE A 253 ? 0.3617 0.2750 0.3001 -0.0686 0.0477  -0.0544 288 PHE A N   
1889 C CA  . PHE A 253 ? 0.3351 0.2478 0.2750 -0.0785 0.0436  -0.0548 288 PHE A CA  
1890 C C   . PHE A 253 ? 0.3536 0.2564 0.2834 -0.0924 0.0474  -0.0704 288 PHE A C   
1891 O O   . PHE A 253 ? 0.3956 0.3114 0.3214 -0.1043 0.0406  -0.0734 288 PHE A O   
1892 C CB  . PHE A 253 ? 0.3520 0.2510 0.3048 -0.0729 0.0465  -0.0455 288 PHE A CB  
1893 C CG  . PHE A 253 ? 0.3494 0.2612 0.3097 -0.0628 0.0405  -0.0312 288 PHE A CG  
1894 C CD1 . PHE A 253 ? 0.3176 0.2491 0.2747 -0.0598 0.0336  -0.0278 288 PHE A CD1 
1895 C CD2 . PHE A 253 ? 0.3654 0.2691 0.3355 -0.0567 0.0420  -0.0212 288 PHE A CD2 
1896 C CE1 . PHE A 253 ? 0.3554 0.2958 0.3181 -0.0519 0.0286  -0.0168 288 PHE A CE1 
1897 C CE2 . PHE A 253 ? 0.3151 0.2308 0.2893 -0.0488 0.0361  -0.0098 288 PHE A CE2 
1898 C CZ  . PHE A 253 ? 0.3223 0.2553 0.2926 -0.0469 0.0295  -0.0087 288 PHE A CZ  
1899 N N   . ALA A 254 ? 0.3605 0.2409 0.2867 -0.0914 0.0584  -0.0807 289 ALA A N   
1900 C CA  . ALA A 254 ? 0.4174 0.2851 0.3320 -0.1059 0.0628  -0.0982 289 ALA A CA  
1901 C C   . ALA A 254 ? 0.4352 0.3256 0.3328 -0.1150 0.0559  -0.1066 289 ALA A C   
1902 O O   . ALA A 254 ? 0.4692 0.3666 0.3595 -0.1300 0.0509  -0.1150 289 ALA A O   
1903 C CB  . ALA A 254 ? 0.4220 0.2588 0.3354 -0.1010 0.0781  -0.1080 289 ALA A CB  
1904 N N   . ASP A 255 ? 0.3761 0.2813 0.2689 -0.1056 0.0549  -0.1023 290 ASP A N   
1905 C CA  . ASP A 255 ? 0.4555 0.3838 0.3318 -0.1130 0.0490  -0.1081 290 ASP A CA  
1906 C C   . ASP A 255 ? 0.3507 0.3069 0.2300 -0.1196 0.0353  -0.0989 290 ASP A C   
1907 O O   . ASP A 255 ? 0.4266 0.3988 0.2944 -0.1328 0.0291  -0.1062 290 ASP A O   
1908 C CB  . ASP A 255 ? 0.4140 0.3515 0.2865 -0.1008 0.0522  -0.1032 290 ASP A CB  
1909 C CG  . ASP A 255 ? 0.5763 0.5321 0.4282 -0.1083 0.0500  -0.1118 290 ASP A CG  
1910 O OD1 . ASP A 255 ? 0.6259 0.5693 0.4651 -0.1131 0.0576  -0.1264 290 ASP A OD1 
1911 O OD2 . ASP A 255 ? 0.5547 0.5382 0.4054 -0.1079 0.0405  -0.1016 290 ASP A OD2 
1912 N N   . ALA A 256 ? 0.3506 0.3137 0.2455 -0.1106 0.0306  -0.0830 291 ALA A N   
1913 C CA  . ALA A 256 ? 0.3568 0.3450 0.2565 -0.1147 0.0196  -0.0733 291 ALA A CA  
1914 C C   . ALA A 256 ? 0.3921 0.3788 0.2954 -0.1286 0.0166  -0.0779 291 ALA A C   
1915 O O   . ALA A 256 ? 0.3578 0.3687 0.2600 -0.1375 0.0080  -0.0756 291 ALA A O   
1916 C CB  . ALA A 256 ? 0.3232 0.3159 0.2369 -0.1014 0.0171  -0.0571 291 ALA A CB  
1917 N N   . ALA A 257 ? 0.3407 0.3005 0.2497 -0.1304 0.0239  -0.0830 292 ALA A N   
1918 C CA  . ALA A 257 ? 0.4503 0.4063 0.3628 -0.1456 0.0225  -0.0886 292 ALA A CA  
1919 C C   . ALA A 257 ? 0.4027 0.3653 0.3032 -0.1557 0.0213  -0.1007 292 ALA A C   
1920 O O   . ALA A 257 ? 0.3975 0.3784 0.3003 -0.1655 0.0141  -0.0995 292 ALA A O   
1921 C CB  . ALA A 257 ? 0.4389 0.3628 0.3614 -0.1431 0.0322  -0.0892 292 ALA A CB  
1922 N N   . LYS A 258 ? 0.4466 0.3954 0.3345 -0.1532 0.0286  -0.1118 293 LYS A N   
1923 C CA  . LYS A 258 ? 0.4130 0.3663 0.2881 -0.1627 0.0284  -0.1239 293 LYS A CA  
1924 C C   . LYS A 258 ? 0.4869 0.4771 0.3544 -0.1667 0.0174  -0.1191 293 LYS A C   
1925 O O   . LYS A 258 ? 0.4762 0.4809 0.3402 -0.1780 0.0117  -0.1230 293 LYS A O   
1926 C CB  . LYS A 258 ? 0.4501 0.3803 0.3141 -0.1571 0.0401  -0.1356 293 LYS A CB  
1927 C CG  . LYS A 258 ? 0.5647 0.5010 0.4121 -0.1657 0.0402  -0.1485 293 LYS A CG  
1928 C CD  . LYS A 258 ? 0.6174 0.5401 0.4532 -0.1565 0.0508  -0.1561 293 LYS A CD  
1929 C CE  . LYS A 258 ? 0.6903 0.6028 0.5112 -0.1648 0.0560  -0.1726 293 LYS A CE  
1930 N NZ  . LYS A 258 ? 0.7336 0.6433 0.5408 -0.1563 0.0639  -0.1783 293 LYS A NZ  
1931 N N   . GLY A 259 ? 0.4268 0.4327 0.2926 -0.1572 0.0144  -0.1099 294 GLY A N   
1932 C CA  . GLY A 259 ? 0.4310 0.4710 0.2909 -0.1582 0.0055  -0.1029 294 GLY A CA  
1933 C C   . GLY A 259 ? 0.3595 0.4260 0.2322 -0.1598 -0.0048 -0.0884 294 GLY A C   
1934 O O   . GLY A 259 ? 0.4103 0.5065 0.2811 -0.1621 -0.0123 -0.0815 294 GLY A O   
1935 N N   . GLY A 260 ? 0.3451 0.4016 0.2316 -0.1579 -0.0045 -0.0827 295 GLY A N   
1936 C CA  . GLY A 260 ? 0.3957 0.4761 0.2957 -0.1583 -0.0127 -0.0686 295 GLY A CA  
1937 C C   . GLY A 260 ? 0.3825 0.4862 0.2855 -0.1480 -0.0178 -0.0541 295 GLY A C   
1938 O O   . GLY A 260 ? 0.3682 0.4979 0.2807 -0.1480 -0.0245 -0.0420 295 GLY A O   
1939 N N   . TYR A 261 ? 0.3429 0.4380 0.2387 -0.1386 -0.0141 -0.0542 296 TYR A N   
1940 C CA  . TYR A 261 ? 0.3529 0.4663 0.2530 -0.1263 -0.0172 -0.0389 296 TYR A CA  
1941 C C   . TYR A 261 ? 0.3260 0.4254 0.2414 -0.1125 -0.0137 -0.0282 296 TYR A C   
1942 O O   . TYR A 261 ? 0.3170 0.3944 0.2384 -0.1120 -0.0093 -0.0318 296 TYR A O   
1943 C CB  . TYR A 261 ? 0.2789 0.3932 0.1648 -0.1216 -0.0140 -0.0418 296 TYR A CB  
1944 C CG  . TYR A 261 ? 0.2900 0.3734 0.1714 -0.1162 -0.0039 -0.0517 296 TYR A CG  
1945 C CD1 . TYR A 261 ? 0.3337 0.4024 0.2262 -0.1023 0.0007  -0.0435 296 TYR A CD1 
1946 C CD2 . TYR A 261 ? 0.3217 0.3915 0.1878 -0.1251 0.0013  -0.0690 296 TYR A CD2 
1947 C CE1 . TYR A 261 ? 0.3409 0.3854 0.2318 -0.0967 0.0096  -0.0503 296 TYR A CE1 
1948 C CE2 . TYR A 261 ? 0.3893 0.4317 0.2534 -0.1183 0.0119  -0.0764 296 TYR A CE2 
1949 C CZ  . TYR A 261 ? 0.3914 0.4231 0.2692 -0.1038 0.0156  -0.0659 296 TYR A CZ  
1950 O OH  . TYR A 261 ? 0.3859 0.3944 0.2645 -0.0964 0.0257  -0.0709 296 TYR A OH  
1951 N N   . LEU A 262 ? 0.2675 0.3794 0.1886 -0.1013 -0.0153 -0.0147 297 LEU A N   
1952 C CA  . LEU A 262 ? 0.2545 0.3553 0.1881 -0.0893 -0.0126 -0.0055 297 LEU A CA  
1953 C C   . LEU A 262 ? 0.2810 0.3589 0.2125 -0.0809 -0.0065 -0.0086 297 LEU A C   
1954 O O   . LEU A 262 ? 0.2655 0.3429 0.1885 -0.0799 -0.0042 -0.0122 297 LEU A O   
1955 C CB  . LEU A 262 ? 0.3044 0.4250 0.2456 -0.0809 -0.0157 0.0095  297 LEU A CB  
1956 C CG  . LEU A 262 ? 0.2841 0.4305 0.2328 -0.0856 -0.0214 0.0173  297 LEU A CG  
1957 C CD1 . LEU A 262 ? 0.3345 0.5002 0.2900 -0.0758 -0.0229 0.0328  297 LEU A CD1 
1958 C CD2 . LEU A 262 ? 0.2229 0.3603 0.1820 -0.0854 -0.0197 0.0182  297 LEU A CD2 
1959 N N   . ILE A 263 ? 0.2283 0.2900 0.1681 -0.0747 -0.0038 -0.0061 298 ILE A N   
1960 C CA  . ILE A 263 ? 0.2144 0.2595 0.1560 -0.0658 0.0004  -0.0057 298 ILE A CA  
1961 C C   . ILE A 263 ? 0.3191 0.3648 0.2694 -0.0572 -0.0008 0.0043  298 ILE A C   
1962 O O   . ILE A 263 ? 0.2634 0.3172 0.2186 -0.0572 -0.0031 0.0096  298 ILE A O   
1963 C CB  . ILE A 263 ? 0.2934 0.3167 0.2351 -0.0670 0.0053  -0.0133 298 ILE A CB  
1964 C CG1 . ILE A 263 ? 0.3446 0.3629 0.2930 -0.0685 0.0045  -0.0106 298 ILE A CG1 
1965 C CG2 . ILE A 263 ? 0.2817 0.3005 0.2139 -0.0755 0.0084  -0.0251 298 ILE A CG2 
1966 C CD1 . ILE A 263 ? 0.4609 0.4585 0.4127 -0.0656 0.0093  -0.0126 298 ILE A CD1 
1967 N N   . ALA A 264 ? 0.2355 0.2731 0.1877 -0.0501 0.0011  0.0066  299 ALA A N   
1968 C CA  . ALA A 264 ? 0.2304 0.2632 0.1889 -0.0431 0.0006  0.0129  299 ALA A CA  
1969 C C   . ALA A 264 ? 0.2833 0.3020 0.2436 -0.0393 0.0025  0.0108  299 ALA A C   
1970 O O   . ALA A 264 ? 0.2678 0.2839 0.2265 -0.0398 0.0049  0.0073  299 ALA A O   
1971 C CB  . ALA A 264 ? 0.2467 0.2902 0.2083 -0.0388 -0.0005 0.0209  299 ALA A CB  
1972 N N   . ALA A 265 ? 0.2043 0.2157 0.1679 -0.0355 0.0016  0.0132  300 ALA A N   
1973 C CA  . ALA A 265 ? 0.2424 0.2447 0.2088 -0.0324 0.0019  0.0127  300 ALA A CA  
1974 C C   . ALA A 265 ? 0.2522 0.2517 0.2202 -0.0290 -0.0003 0.0158  300 ALA A C   
1975 O O   . ALA A 265 ? 0.2542 0.2544 0.2202 -0.0281 -0.0007 0.0172  300 ALA A O   
1976 C CB  . ALA A 265 ? 0.2648 0.2585 0.2313 -0.0331 0.0036  0.0099  300 ALA A CB  
1977 N N   . SER A 266 ? 0.1908 0.1873 0.1625 -0.0275 -0.0014 0.0164  301 SER A N   
1978 C CA  . SER A 266 ? 0.2152 0.2083 0.1878 -0.0261 -0.0035 0.0175  301 SER A CA  
1979 C C   . SER A 266 ? 0.2176 0.2059 0.1849 -0.0252 -0.0051 0.0163  301 SER A C   
1980 O O   . SER A 266 ? 0.2507 0.2353 0.2150 -0.0241 -0.0053 0.0156  301 SER A O   
1981 C CB  . SER A 266 ? 0.3028 0.2952 0.2815 -0.0268 -0.0052 0.0179  301 SER A CB  
1982 O OG  . SER A 266 ? 0.5756 0.5734 0.5590 -0.0271 -0.0026 0.0197  301 SER A OG  
1983 N N   . HIS A 267 ? 0.2000 0.1875 0.1657 -0.0253 -0.0055 0.0162  302 HIS A N   
1984 C CA  . HIS A 267 ? 0.2134 0.1982 0.1734 -0.0242 -0.0069 0.0165  302 HIS A CA  
1985 C C   . HIS A 267 ? 0.2045 0.1899 0.1614 -0.0242 -0.0041 0.0179  302 HIS A C   
1986 O O   . HIS A 267 ? 0.2365 0.2204 0.1886 -0.0230 -0.0043 0.0196  302 HIS A O   
1987 C CB  . HIS A 267 ? 0.2506 0.2355 0.2125 -0.0237 -0.0101 0.0181  302 HIS A CB  
1988 C CG  . HIS A 267 ? 0.2071 0.1941 0.1740 -0.0251 -0.0135 0.0174  302 HIS A CG  
1989 N ND1 . HIS A 267 ? 0.2264 0.2107 0.1902 -0.0269 -0.0155 0.0143  302 HIS A ND1 
1990 C CD2 . HIS A 267 ? 0.2249 0.2161 0.2010 -0.0251 -0.0144 0.0194  302 HIS A CD2 
1991 C CE1 . HIS A 267 ? 0.3432 0.3303 0.3145 -0.0293 -0.0183 0.0145  302 HIS A CE1 
1992 N NE2 . HIS A 267 ? 0.1863 0.1791 0.1655 -0.0279 -0.0177 0.0181  302 HIS A NE2 
1993 N N   . LEU A 268 ? 0.1953 0.1842 0.1547 -0.0261 -0.0016 0.0176  303 LEU A N   
1994 C CA  . LEU A 268 ? 0.2167 0.2088 0.1747 -0.0273 0.0007  0.0193  303 LEU A CA  
1995 C C   . LEU A 268 ? 0.2118 0.2061 0.1666 -0.0239 0.0017  0.0207  303 LEU A C   
1996 O O   . LEU A 268 ? 0.2158 0.2086 0.1706 -0.0218 0.0012  0.0197  303 LEU A O   
1997 C CB  . LEU A 268 ? 0.2270 0.2252 0.1884 -0.0317 0.0019  0.0182  303 LEU A CB  
1998 C CG  . LEU A 268 ? 0.2420 0.2345 0.2050 -0.0350 0.0029  0.0150  303 LEU A CG  
1999 C CD1 . LEU A 268 ? 0.2532 0.2517 0.2165 -0.0411 0.0038  0.0116  303 LEU A CD1 
2000 C CD2 . LEU A 268 ? 0.3155 0.3000 0.2789 -0.0349 0.0048  0.0168  303 LEU A CD2 
2001 N N   . PRO A 269 ? 0.2335 0.2303 0.1861 -0.0231 0.0043  0.0232  304 PRO A N   
2002 C CA  . PRO A 269 ? 0.2391 0.2371 0.1885 -0.0185 0.0072  0.0242  304 PRO A CA  
2003 C C   . PRO A 269 ? 0.2106 0.2149 0.1662 -0.0170 0.0085  0.0259  304 PRO A C   
2004 O O   . PRO A 269 ? 0.2126 0.2273 0.1745 -0.0201 0.0081  0.0286  304 PRO A O   
2005 C CB  . PRO A 269 ? 0.2284 0.2317 0.1773 -0.0186 0.0107  0.0282  304 PRO A CB  
2006 C CG  . PRO A 269 ? 0.2983 0.2978 0.2469 -0.0224 0.0089  0.0288  304 PRO A CG  
2007 C CD  . PRO A 269 ? 0.2710 0.2684 0.2245 -0.0259 0.0058  0.0257  304 PRO A CD  
2008 N N   . PHE A 270 ? 0.2278 0.2259 0.1814 -0.0125 0.0101  0.0245  305 PHE A N   
2009 C CA  . PHE A 270 ? 0.2099 0.2123 0.1705 -0.0097 0.0121  0.0280  305 PHE A CA  
2010 C C   . PHE A 270 ? 0.2328 0.2506 0.2005 -0.0080 0.0149  0.0349  305 PHE A C   
2011 O O   . PHE A 270 ? 0.2217 0.2421 0.1881 -0.0056 0.0187  0.0366  305 PHE A O   
2012 C CB  . PHE A 270 ? 0.2510 0.2407 0.2084 -0.0045 0.0158  0.0255  305 PHE A CB  
2013 C CG  . PHE A 270 ? 0.2646 0.2559 0.2306 -0.0003 0.0191  0.0307  305 PHE A CG  
2014 C CD1 . PHE A 270 ? 0.2426 0.2328 0.2130 -0.0029 0.0162  0.0316  305 PHE A CD1 
2015 C CD2 . PHE A 270 ? 0.2517 0.2471 0.2227 0.0069  0.0258  0.0365  305 PHE A CD2 
2016 C CE1 . PHE A 270 ? 0.2771 0.2696 0.2559 0.0014  0.0196  0.0387  305 PHE A CE1 
2017 C CE2 . PHE A 270 ? 0.2889 0.2867 0.2695 0.0120  0.0293  0.0438  305 PHE A CE2 
2018 C CZ  . PHE A 270 ? 0.2476 0.2437 0.2317 0.0091  0.0261  0.0452  305 PHE A CZ  
2019 N N   . PRO A 271 ? 0.2355 0.2661 0.2108 -0.0095 0.0132  0.0398  306 PRO A N   
2020 C CA  . PRO A 271 ? 0.2280 0.2583 0.2049 -0.0112 0.0103  0.0399  306 PRO A CA  
2021 C C   . PRO A 271 ? 0.2321 0.2622 0.2055 -0.0187 0.0057  0.0347  306 PRO A C   
2022 O O   . PRO A 271 ? 0.2214 0.2521 0.1952 -0.0203 0.0040  0.0344  306 PRO A O   
2023 C CB  . PRO A 271 ? 0.2296 0.2787 0.2151 -0.0091 0.0110  0.0492  306 PRO A CB  
2024 C CG  . PRO A 271 ? 0.2508 0.3140 0.2394 -0.0117 0.0109  0.0516  306 PRO A CG  
2025 C CD  . PRO A 271 ? 0.2358 0.2858 0.2194 -0.0089 0.0146  0.0475  306 PRO A CD  
2026 N N   . GLY A 272 ? 0.2098 0.2386 0.1802 -0.0229 0.0047  0.0312  307 GLY A N   
2027 C CA  . GLY A 272 ? 0.2101 0.2342 0.1776 -0.0286 0.0023  0.0260  307 GLY A CA  
2028 C C   . GLY A 272 ? 0.1959 0.2308 0.1642 -0.0346 0.0005  0.0251  307 GLY A C   
2029 O O   . GLY A 272 ? 0.2641 0.2938 0.2296 -0.0376 0.0000  0.0203  307 GLY A O   
2030 N N   . ILE A 273 ? 0.2044 0.2556 0.1764 -0.0365 -0.0002 0.0295  308 ILE A N   
2031 C CA  . ILE A 273 ? 0.2181 0.2830 0.1889 -0.0435 -0.0030 0.0284  308 ILE A CA  
2032 C C   . ILE A 273 ? 0.2406 0.3130 0.2133 -0.0516 -0.0041 0.0266  308 ILE A C   
2033 O O   . ILE A 273 ? 0.2256 0.3043 0.2044 -0.0499 -0.0030 0.0319  308 ILE A O   
2034 C CB  . ILE A 273 ? 0.2385 0.3212 0.2133 -0.0399 -0.0041 0.0371  308 ILE A CB  
2035 C CG1 . ILE A 273 ? 0.2327 0.3060 0.2075 -0.0325 -0.0020 0.0397  308 ILE A CG1 
2036 C CG2 . ILE A 273 ? 0.2996 0.4001 0.2708 -0.0480 -0.0081 0.0360  308 ILE A CG2 
2037 C CD1 . ILE A 273 ? 0.2533 0.3389 0.2351 -0.0258 -0.0008 0.0510  308 ILE A CD1 
2038 N N   . GLY A 274 ? 0.2599 0.3135 0.2033 -0.0518 -0.0137 0.0387  309 GLY A N   
2039 C CA  . GLY A 274 ? 0.2679 0.3208 0.2084 -0.0583 -0.0060 0.0352  309 GLY A CA  
2040 C C   . GLY A 274 ? 0.2787 0.3413 0.2277 -0.0620 -0.0089 0.0273  309 GLY A C   
2041 O O   . GLY A 274 ? 0.2633 0.3345 0.2122 -0.0579 -0.0150 0.0266  309 GLY A O   
2042 N N   . HIS A 275 ? 0.2317 0.2945 0.1953 -0.0685 -0.0035 0.0200  310 HIS A N   
2043 C CA  . HIS A 275 ? 0.2345 0.3038 0.2148 -0.0710 -0.0085 0.0062  310 HIS A CA  
2044 C C   . HIS A 275 ? 0.2596 0.2963 0.2348 -0.0737 -0.0027 0.0106  310 HIS A C   
2045 O O   . HIS A 275 ? 0.3010 0.3121 0.2552 -0.0702 0.0060  0.0245  310 HIS A O   
2046 C CB  . HIS A 275 ? 0.2358 0.3253 0.2531 -0.0755 -0.0085 -0.0098 310 HIS A CB  
2047 C CG  . HIS A 275 ? 0.2597 0.3851 0.2787 -0.0666 -0.0181 -0.0184 310 HIS A CG  
2048 N ND1 . HIS A 275 ? 0.2767 0.4098 0.2974 -0.0667 -0.0132 -0.0123 310 HIS A ND1 
2049 C CD2 . HIS A 275 ? 0.2534 0.4100 0.2685 -0.0523 -0.0316 -0.0315 310 HIS A CD2 
2050 C CE1 . HIS A 275 ? 0.2894 0.4552 0.3081 -0.0538 -0.0239 -0.0208 310 HIS A CE1 
2051 N NE2 . HIS A 275 ? 0.2708 0.4520 0.2831 -0.0427 -0.0344 -0.0316 310 HIS A NE2 
2052 N N   . ILE A 276 ? 0.2627 0.3010 0.2562 -0.0759 -0.0083 -0.0024 311 ILE A N   
2053 C CA  . ILE A 276 ? 0.2821 0.2884 0.2744 -0.0770 -0.0022 0.0030  311 ILE A CA  
2054 C C   . ILE A 276 ? 0.2641 0.2747 0.3053 -0.0841 -0.0027 -0.0141 311 ILE A C   
2055 O O   . ILE A 276 ? 0.2737 0.3154 0.3363 -0.0824 -0.0181 -0.0374 311 ILE A O   
2056 C CB  . ILE A 276 ? 0.4435 0.4411 0.4056 -0.0691 -0.0130 0.0043  311 ILE A CB  
2057 C CG1 . ILE A 276 ? 0.4187 0.3820 0.3733 -0.0660 -0.0085 0.0101  311 ILE A CG1 
2058 C CG2 . ILE A 276 ? 0.4843 0.5117 0.4558 -0.0668 -0.0269 -0.0119 311 ILE A CG2 
2059 C CD1 . ILE A 276 ? 0.5015 0.4546 0.4259 -0.0557 -0.0201 0.0105  311 ILE A CD1 
2060 N N   . ARG A 277 ? 0.2538 0.2344 0.3169 -0.0885 0.0148  -0.0029 312 ARG A N   
2061 C CA  . ARG A 277 ? 0.3054 0.2848 0.4308 -0.0959 0.0152  -0.0196 312 ARG A CA  
2062 C C   . ARG A 277 ? 0.3451 0.2862 0.4658 -0.0931 0.0247  -0.0053 312 ARG A C   
2063 O O   . ARG A 277 ? 0.3692 0.2806 0.4452 -0.0842 0.0395  0.0224  312 ARG A O   
2064 C CB  . ARG A 277 ? 0.3792 0.3647 0.5708 -0.1059 0.0303  -0.0237 312 ARG A CB  
2065 C CG  . ARG A 277 ? 0.4469 0.4152 0.6229 -0.1058 0.0579  0.0067  312 ARG A CG  
2066 C CD  . ARG A 277 ? 0.4715 0.4433 0.7281 -0.1150 0.0756  0.0025  312 ARG A CD  
2067 N NE  . ARG A 277 ? 0.6262 0.5683 0.8721 -0.1068 0.1086  0.0381  312 ARG A NE  
2068 C CZ  . ARG A 277 ? 0.8501 0.7942 1.0688 -0.1011 0.1233  0.0556  312 ARG A CZ  
2069 N NH1 . ARG A 277 ? 0.5273 0.4987 0.7320 -0.1059 0.1103  0.0434  312 ARG A NH1 
2070 N NH2 . ARG A 277 ? 0.7480 0.6691 0.9550 -0.0877 0.1512  0.0846  312 ARG A NH2 
2071 N N   . ALA A 278 ? 0.2937 0.2374 0.4592 -0.0966 0.0138  -0.0268 313 ALA A N   
2072 C CA  . ALA A 278 ? 0.4972 0.4052 0.6620 -0.0929 0.0206  -0.0152 313 ALA A CA  
2073 C C   . ALA A 278 ? 0.4865 0.3612 0.7029 -0.0976 0.0531  0.0080  313 ALA A C   
2074 O O   . ALA A 278 ? 0.4581 0.3487 0.7449 -0.1055 0.0575  -0.0060 313 ALA A O   
2075 C CB  . ALA A 278 ? 0.4362 0.3609 0.6333 -0.0934 -0.0043 -0.0490 313 ALA A CB  
2076 N N   . GLU A 279 ? 0.4408 0.2750 0.6154 -0.0851 0.0747  0.0437  314 GLU A N   
2077 C CA  . GLU A 279 ? 0.4865 0.2958 0.6861 -0.0786 0.1098  0.0751  314 GLU A CA  
2078 C C   . GLU A 279 ? 0.4766 0.2475 0.6410 -0.0606 0.1203  0.0997  314 GLU A C   
2079 O O   . GLU A 279 ? 0.6037 0.3551 0.6900 -0.0441 0.1161  0.1142  314 GLU A O   
2080 C CB  . GLU A 279 ? 0.4604 0.2730 0.6169 -0.0696 0.1282  0.0985  314 GLU A CB  
2081 C CG  . GLU A 279 ? 0.6189 0.4671 0.8202 -0.0844 0.1245  0.0791  314 GLU A CG  
2082 C CD  . GLU A 279 ? 0.7254 0.5735 0.9153 -0.0739 0.1507  0.1034  314 GLU A CD  
2083 O OE1 . GLU A 279 ? 0.6831 0.5076 0.8273 -0.0528 0.1708  0.1336  314 GLU A OE1 
2084 O OE2 . GLU A 279 ? 0.7423 0.6162 0.9681 -0.0837 0.1493  0.0896  314 GLU A OE2 
2085 N N   . GLY A 280 ? 0.4822 0.2445 0.7047 -0.0605 0.1325  0.1028  315 GLY A N   
2086 C CA  . GLY A 280 ? 0.5257 0.2538 0.7199 -0.0427 0.1420  0.1252  315 GLY A CA  
2087 C C   . GLY A 280 ? 0.6272 0.3421 0.7781 -0.0404 0.1129  0.1095  315 GLY A C   
2088 O O   . GLY A 280 ? 0.6705 0.4058 0.8549 -0.0575 0.0856  0.0730  315 GLY A O   
2089 N N   . LYS A 281 ? 0.6324 0.3188 0.7067 -0.0147 0.1162  0.1333  316 LYS A N   
2090 C CA  . LYS A 281 ? 0.5322 0.2078 0.5599 -0.0065 0.0875  0.1171  316 LYS A CA  
2091 C C   . LYS A 281 ? 0.5887 0.3005 0.5624 -0.0072 0.0597  0.0948  316 LYS A C   
2092 O O   . LYS A 281 ? 0.7736 0.4958 0.7145 -0.0017 0.0308  0.0736  316 LYS A O   
2093 C CB  . LYS A 281 ? 0.6325 0.2734 0.5999 0.0265  0.0947  0.1436  316 LYS A CB  
2094 C CG  . LYS A 281 ? 0.7911 0.4194 0.8020 0.0308  0.1211  0.1661  316 LYS A CG  
2095 C CD  . LYS A 281 ? 0.8228 0.4247 0.8246 0.0441  0.1097  0.1656  316 LYS A CD  
2096 C CE  . LYS A 281 ? 0.9034 0.4894 0.8261 0.0830  0.1186  0.1928  316 LYS A CE  
2097 N NZ  . LYS A 281 ? 0.9718 0.5346 0.8787 0.0982  0.1021  0.1888  316 LYS A NZ  
2098 N N   . GLY A 282 ? 0.5040 0.2348 0.4750 -0.0136 0.0691  0.0994  317 GLY A N   
2099 C CA  . GLY A 282 ? 0.4782 0.2400 0.4064 -0.0134 0.0457  0.0813  317 GLY A CA  
2100 C C   . GLY A 282 ? 0.4670 0.2644 0.4318 -0.0349 0.0449  0.0676  317 GLY A C   
2101 O O   . GLY A 282 ? 0.4403 0.2549 0.4685 -0.0540 0.0423  0.0497  317 GLY A O   
2102 N N   . TYR A 283 ? 0.4252 0.2348 0.3520 -0.0286 0.0449  0.0730  318 TYR A N   
2103 C CA  . TYR A 283 ? 0.3970 0.2415 0.3485 -0.0452 0.0409  0.0600  318 TYR A CA  
2104 C C   . TYR A 283 ? 0.4409 0.2807 0.3661 -0.0356 0.0599  0.0812  318 TYR A C   
2105 O O   . TYR A 283 ? 0.4542 0.2705 0.3277 -0.0116 0.0684  0.1004  318 TYR A O   
2106 C CB  . TYR A 283 ? 0.3778 0.2536 0.3137 -0.0486 0.0121  0.0361  318 TYR A CB  
2107 C CG  . TYR A 283 ? 0.3391 0.2260 0.2994 -0.0550 -0.0051 0.0145  318 TYR A CG  
2108 C CD1 . TYR A 283 ? 0.3677 0.2360 0.3056 -0.0442 -0.0151 0.0130  318 TYR A CD1 
2109 C CD2 . TYR A 283 ? 0.3722 0.2902 0.3767 -0.0675 -0.0131 -0.0071 318 TYR A CD2 
2110 C CE1 . TYR A 283 ? 0.3894 0.2690 0.3499 -0.0485 -0.0300 -0.0073 318 TYR A CE1 
2111 C CE2 . TYR A 283 ? 0.3727 0.3040 0.3959 -0.0680 -0.0297 -0.0293 318 TYR A CE2 
2112 C CZ  . TYR A 283 ? 0.3750 0.2867 0.3766 -0.0598 -0.0368 -0.0282 318 TYR A CZ  
2113 O OH  . TYR A 283 ? 0.4236 0.3497 0.4434 -0.0587 -0.0528 -0.0508 318 TYR A OH  
2114 N N   . ARG A 284 ? 0.3935 0.2578 0.3533 -0.0508 0.0649  0.0751  319 ARG A N   
2115 C CA  . ARG A 284 ? 0.4225 0.2903 0.3629 -0.0441 0.0798  0.0898  319 ARG A CA  
2116 C C   . ARG A 284 ? 0.4728 0.3756 0.4079 -0.0519 0.0575  0.0697  319 ARG A C   
2117 O O   . ARG A 284 ? 0.3908 0.3204 0.3642 -0.0677 0.0453  0.0498  319 ARG A O   
2118 C CB  . ARG A 284 ? 0.4660 0.3313 0.4627 -0.0546 0.1102  0.1030  319 ARG A CB  
2119 C CG  . ARG A 284 ? 0.4969 0.3743 0.4797 -0.0492 0.1230  0.1132  319 ARG A CG  
2120 C CD  . ARG A 284 ? 0.6580 0.5352 0.6866 -0.0481 0.1479  0.1247  319 ARG A CD  
2121 N NE  . ARG A 284 ? 0.9968 0.8472 1.0088 -0.0269 0.1671  0.1475  319 ARG A NE  
2122 C CZ  . ARG A 284 ? 0.9206 0.7598 0.8683 0.0020  0.1719  0.1631  319 ARG A CZ  
2123 N NH1 . ARG A 284 ? 0.9204 0.7718 0.8175 0.0128  0.1563  0.1560  319 ARG A NH1 
2124 N NH2 . ARG A 284 ? 0.9087 0.7262 0.8473 0.0231  0.1920  0.1836  319 ARG A NH2 
2125 N N   . PHE A 285 ? 0.3798 0.2823 0.2687 -0.0369 0.0516  0.0743  320 PHE A N   
2126 C CA  . PHE A 285 ? 0.3511 0.2818 0.2390 -0.0417 0.0353  0.0612  320 PHE A CA  
2127 C C   . PHE A 285 ? 0.3212 0.2637 0.2252 -0.0464 0.0513  0.0682  320 PHE A C   
2128 O O   . PHE A 285 ? 0.3957 0.3214 0.2843 -0.0346 0.0727  0.0864  320 PHE A O   
2129 C CB  . PHE A 285 ? 0.4415 0.3651 0.2869 -0.0220 0.0199  0.0586  320 PHE A CB  
2130 C CG  . PHE A 285 ? 0.3248 0.2731 0.1791 -0.0257 0.0053  0.0476  320 PHE A CG  
2131 C CD1 . PHE A 285 ? 0.3452 0.3159 0.2267 -0.0391 -0.0063 0.0374  320 PHE A CD1 
2132 C CD2 . PHE A 285 ? 0.3595 0.3085 0.1956 -0.0119 0.0043  0.0488  320 PHE A CD2 
2133 C CE1 . PHE A 285 ? 0.3585 0.3490 0.2527 -0.0401 -0.0147 0.0336  320 PHE A CE1 
2134 C CE2 . PHE A 285 ? 0.3268 0.2961 0.1806 -0.0153 -0.0085 0.0396  320 PHE A CE2 
2135 C CZ  . PHE A 285 ? 0.2828 0.2712 0.1675 -0.0300 -0.0161 0.0344  320 PHE A CZ  
2136 N N   . VAL A 286 ? 0.3374 0.3097 0.2707 -0.0602 0.0423  0.0548  321 VAL A N   
2137 C CA  . VAL A 286 ? 0.3308 0.3191 0.2859 -0.0657 0.0534  0.0564  321 VAL A CA  
2138 C C   . VAL A 286 ? 0.2800 0.2882 0.2195 -0.0622 0.0380  0.0504  321 VAL A C   
2139 O O   . VAL A 286 ? 0.2779 0.3093 0.2316 -0.0679 0.0236  0.0389  321 VAL A O   
2140 C CB  . VAL A 286 ? 0.3229 0.3307 0.3360 -0.0816 0.0550  0.0421  321 VAL A CB  
2141 C CG1 . VAL A 286 ? 0.3731 0.3967 0.4158 -0.0863 0.0672  0.0421  321 VAL A CG1 
2142 C CG2 . VAL A 286 ? 0.3533 0.3397 0.3964 -0.0862 0.0683  0.0458  321 VAL A CG2 
2143 N N   . PRO A 287 ? 0.3520 0.3519 0.2631 -0.0489 0.0412  0.0583  322 PRO A N   
2144 C CA  . PRO A 287 ? 0.2639 0.2802 0.1711 -0.0453 0.0263  0.0518  322 PRO A CA  
2145 C C   . PRO A 287 ? 0.2644 0.3081 0.2023 -0.0566 0.0271  0.0470  322 PRO A C   
2146 O O   . PRO A 287 ? 0.2804 0.3297 0.2397 -0.0632 0.0411  0.0478  322 PRO A O   
2147 C CB  . PRO A 287 ? 0.3242 0.3275 0.2007 -0.0260 0.0312  0.0573  322 PRO A CB  
2148 C CG  . PRO A 287 ? 0.4733 0.4503 0.3220 -0.0132 0.0449  0.0686  322 PRO A CG  
2149 C CD  . PRO A 287 ? 0.3928 0.3685 0.2741 -0.0320 0.0591  0.0738  322 PRO A CD  
2150 N N   . VAL A 288 ? 0.2529 0.3140 0.1975 -0.0566 0.0129  0.0425  323 VAL A N   
2151 C CA  . VAL A 288 ? 0.2142 0.3023 0.1803 -0.0607 0.0114  0.0385  323 VAL A CA  
2152 C C   . VAL A 288 ? 0.3025 0.3931 0.2725 -0.0593 0.0203  0.0402  323 VAL A C   
2153 O O   . VAL A 288 ? 0.2650 0.3418 0.2166 -0.0503 0.0223  0.0447  323 VAL A O   
2154 C CB  . VAL A 288 ? 0.3238 0.4268 0.2932 -0.0553 0.0004  0.0415  323 VAL A CB  
2155 C CG1 . VAL A 288 ? 0.5507 0.6552 0.5177 -0.0546 -0.0042 0.0411  323 VAL A CG1 
2156 C CG2 . VAL A 288 ? 0.2500 0.3411 0.2171 -0.0483 -0.0040 0.0465  323 VAL A CG2 
2157 N N   . ASN A 289 ? 0.3121 0.4229 0.3085 -0.0653 0.0241  0.0330  324 ASN A N   
2158 C CA  . ASN A 289 ? 0.2996 0.4190 0.3080 -0.0647 0.0326  0.0327  324 ASN A CA  
2159 C C   . ASN A 289 ? 0.1844 0.3121 0.1830 -0.0563 0.0216  0.0350  324 ASN A C   
2160 O O   . ASN A 289 ? 0.2244 0.3652 0.2258 -0.0532 0.0098  0.0351  324 ASN A O   
2161 C CB  . ASN A 289 ? 0.2602 0.4050 0.3094 -0.0716 0.0320  0.0177  324 ASN A CB  
2162 C CG  . ASN A 289 ? 0.4377 0.5935 0.5108 -0.0727 0.0427  0.0150  324 ASN A CG  
2163 O OD1 . ASN A 289 ? 0.5541 0.6942 0.6196 -0.0712 0.0612  0.0267  324 ASN A OD1 
2164 N ND2 . ASN A 289 ? 0.3735 0.5585 0.4739 -0.0714 0.0314  -0.0011 324 ASN A ND2 
2165 N N   . TYR A 290 ? 0.2404 0.3612 0.2299 -0.0496 0.0271  0.0382  325 TYR A N   
2166 C CA  . TYR A 290 ? 0.1851 0.3139 0.1771 -0.0418 0.0160  0.0375  325 TYR A CA  
2167 C C   . TYR A 290 ? 0.2035 0.3586 0.2183 -0.0442 0.0111  0.0339  325 TYR A C   
2168 O O   . TYR A 290 ? 0.1908 0.3607 0.2231 -0.0488 0.0175  0.0261  325 TYR A O   
2169 C CB  . TYR A 290 ? 0.2700 0.3933 0.2515 -0.0314 0.0220  0.0359  325 TYR A CB  
2170 C CG  . TYR A 290 ? 0.2332 0.3653 0.2268 -0.0234 0.0088  0.0315  325 TYR A CG  
2171 C CD1 . TYR A 290 ? 0.2798 0.4015 0.2774 -0.0154 -0.0066 0.0291  325 TYR A CD1 
2172 C CD2 . TYR A 290 ? 0.2406 0.3912 0.2512 -0.0237 0.0113  0.0282  325 TYR A CD2 
2173 C CE1 . TYR A 290 ? 0.2620 0.3898 0.2845 -0.0086 -0.0179 0.0250  325 TYR A CE1 
2174 C CE2 . TYR A 290 ? 0.2585 0.4154 0.2842 -0.0158 -0.0008 0.0249  325 TYR A CE2 
2175 C CZ  . TYR A 290 ? 0.3164 0.4608 0.3500 -0.0085 -0.0147 0.0241  325 TYR A CZ  
2176 O OH  . TYR A 290 ? 0.2767 0.4253 0.3386 -0.0009 -0.0260 0.0206  325 TYR A OH  
2177 N N   . SER A 291 ? 0.2018 0.3633 0.2203 -0.0383 0.0006  0.0399  326 SER A N   
2178 C CA  . SER A 291 ? 0.2260 0.4125 0.2562 -0.0325 -0.0044 0.0396  326 SER A CA  
2179 C C   . SER A 291 ? 0.2296 0.4154 0.2689 -0.0225 -0.0089 0.0519  326 SER A C   
2180 O O   . SER A 291 ? 0.2750 0.4450 0.3193 -0.0209 -0.0098 0.0617  326 SER A O   
2181 C CB  . SER A 291 ? 0.3174 0.5160 0.3411 -0.0289 -0.0079 0.0396  326 SER A CB  
2182 O OG  . SER A 291 ? 0.4662 0.6918 0.4924 -0.0143 -0.0145 0.0382  326 SER A OG  
2183 N N   . VAL A 292 ? 0.1845 0.3870 0.2343 -0.0154 -0.0116 0.0503  327 VAL A N   
2184 C CA  . VAL A 292 ? 0.3362 0.5370 0.4029 -0.0053 -0.0143 0.0631  327 VAL A CA  
2185 C C   . VAL A 292 ? 0.2897 0.5025 0.3542 0.0098  -0.0120 0.0827  327 VAL A C   
2186 O O   . VAL A 292 ? 0.2265 0.4612 0.2736 0.0191  -0.0145 0.0782  327 VAL A O   
2187 C CB  . VAL A 292 ? 0.3522 0.5644 0.4300 -0.0024 -0.0176 0.0527  327 VAL A CB  
2188 C CG1 . VAL A 292 ? 0.2421 0.4559 0.3414 0.0108  -0.0206 0.0673  327 VAL A CG1 
2189 C CG2 . VAL A 292 ? 0.3028 0.5023 0.3799 -0.0100 -0.0159 0.0391  327 VAL A CG2 
2190 N N   . VAL A 293 ? 0.2012 0.4010 0.2875 0.0159  -0.0067 0.1039  328 VAL A N   
2191 C CA  . VAL A 293 ? 0.2205 0.4293 0.3078 0.0354  0.0034  0.1322  328 VAL A CA  
2192 C C   . VAL A 293 ? 0.2710 0.4820 0.3832 0.0487  0.0055  0.1469  328 VAL A C   
2193 O O   . VAL A 293 ? 0.2523 0.4476 0.4011 0.0403  0.0016  0.1419  328 VAL A O   
2194 C CB  . VAL A 293 ? 0.1708 0.3624 0.2790 0.0330  0.0146  0.1511  328 VAL A CB  
2195 C CG1 . VAL A 293 ? 0.3053 0.5068 0.4145 0.0575  0.0328  0.1876  328 VAL A CG1 
2196 C CG2 . VAL A 293 ? 0.2459 0.4337 0.3296 0.0200  0.0106  0.1348  328 VAL A CG2 
2197 N N   . ASN A 294 ? 0.2249 0.4562 0.3166 0.0736  0.0101  0.1633  329 ASN A N   
2198 C CA  . ASN A 294 ? 0.2935 0.5263 0.4064 0.0913  0.0145  0.1830  329 ASN A CA  
2199 C C   . ASN A 294 ? 0.2486 0.4762 0.3560 0.1127  0.0391  0.2150  329 ASN A C   
2200 O O   . ASN A 294 ? 0.3405 0.5785 0.4154 0.1233  0.0480  0.2167  329 ASN A O   
2201 C CB  . ASN A 294 ? 0.3719 0.6282 0.4615 0.1004  -0.0009 0.1609  329 ASN A CB  
2202 C CG  . ASN A 294 ? 0.3316 0.5856 0.4292 0.0742  -0.0149 0.1239  329 ASN A CG  
2203 O OD1 . ASN A 294 ? 0.4114 0.6803 0.4877 0.0672  -0.0231 0.0986  329 ASN A OD1 
2204 N ND2 . ASN A 294 ? 0.2688 0.5045 0.4017 0.0622  -0.0165 0.1205  329 ASN A ND2 
2205 N N   . ALA B 1   ? 0.6132 0.9569 0.8250 0.0651  0.1688  0.3817  36  ALA B N   
2206 C CA  . ALA B 1   ? 0.4293 0.7483 0.6208 0.0633  0.1606  0.3557  36  ALA B CA  
2207 C C   . ALA B 1   ? 0.7886 1.0795 0.9915 0.0538  0.1512  0.3544  36  ALA B C   
2208 O O   . ALA B 1   ? 0.9446 1.2239 1.1825 0.0421  0.1477  0.3653  36  ALA B O   
2209 C CB  . ALA B 1   ? 0.4325 0.7622 0.5794 0.0783  0.1634  0.3413  36  ALA B CB  
2210 N N   . ALA B 2   ? 0.7233 1.0035 0.8970 0.0592  0.1469  0.3402  37  ALA B N   
2211 C CA  . ALA B 2   ? 0.4194 0.6712 0.5997 0.0512  0.1375  0.3343  37  ALA B CA  
2212 C C   . ALA B 2   ? 0.4886 0.7379 0.6319 0.0606  0.1348  0.3219  37  ALA B C   
2213 O O   . ALA B 2   ? 0.3968 0.6576 0.5093 0.0701  0.1377  0.3087  37  ALA B O   
2214 C CB  . ALA B 2   ? 0.4299 0.6576 0.6253 0.0393  0.1302  0.3176  37  ALA B CB  
2215 N N   . PRO B 3   ? 0.4001 0.6342 0.5456 0.0583  0.1289  0.3249  38  PRO B N   
2216 C CA  . PRO B 3   ? 0.3949 0.6237 0.5069 0.0654  0.1244  0.3106  38  PRO B CA  
2217 C C   . PRO B 3   ? 0.3807 0.5889 0.4815 0.0608  0.1185  0.2861  38  PRO B C   
2218 O O   . PRO B 3   ? 0.3536 0.5442 0.4773 0.0500  0.1151  0.2812  38  PRO B O   
2219 C CB  . PRO B 3   ? 0.4026 0.6179 0.5284 0.0621  0.1192  0.3217  38  PRO B CB  
2220 C CG  . PRO B 3   ? 0.6937 0.8926 0.8611 0.0491  0.1174  0.3306  38  PRO B CG  
2221 C CD  . PRO B 3   ? 0.4224 0.6413 0.6025 0.0486  0.1253  0.3396  38  PRO B CD  
2222 N N   . GLN B 4   ? 0.3657 0.5770 0.4312 0.0693  0.1169  0.2703  39  GLN B N   
2223 C CA  . GLN B 4   ? 0.3433 0.5349 0.3969 0.0657  0.1113  0.2481  39  GLN B CA  
2224 C C   . GLN B 4   ? 0.4392 0.6041 0.5058 0.0573  0.1024  0.2466  39  GLN B C   
2225 O O   . GLN B 4   ? 0.4332 0.5964 0.5050 0.0584  0.0997  0.2580  39  GLN B O   
2226 C CB  . GLN B 4   ? 0.3464 0.5474 0.3600 0.0766  0.1110  0.2309  39  GLN B CB  
2227 C CG  . GLN B 4   ? 0.4055 0.6275 0.4054 0.0847  0.1187  0.2259  39  GLN B CG  
2228 C CD  . GLN B 4   ? 0.4258 0.6553 0.3876 0.0952  0.1171  0.2063  39  GLN B CD  
2229 O OE1 . GLN B 4   ? 0.4565 0.6777 0.4021 0.0961  0.1099  0.1974  39  GLN B OE1 
2230 N NE2 . GLN B 4   ? 0.3736 0.6186 0.3221 0.1031  0.1230  0.1985  39  GLN B NE2 
2231 N N   . VAL B 5   ? 0.3534 0.4977 0.4261 0.0497  0.0978  0.2322  40  VAL B N   
2232 C CA  . VAL B 5   ? 0.3139 0.4310 0.3990 0.0420  0.0887  0.2276  40  VAL B CA  
2233 C C   . VAL B 5   ? 0.4535 0.5630 0.5085 0.0474  0.0834  0.2127  40  VAL B C   
2234 O O   . VAL B 5   ? 0.3716 0.4711 0.4254 0.0484  0.0772  0.2149  40  VAL B O   
2235 C CB  . VAL B 5   ? 0.2860 0.3860 0.3983 0.0300  0.0857  0.2209  40  VAL B CB  
2236 C CG1 . VAL B 5   ? 0.3152 0.3863 0.4402 0.0228  0.0756  0.2129  40  VAL B CG1 
2237 C CG2 . VAL B 5   ? 0.2967 0.4060 0.4399 0.0245  0.0897  0.2359  40  VAL B CG2 
2238 N N   . ARG B 6   ? 0.3248 0.4397 0.3560 0.0515  0.0857  0.1972  41  ARG B N   
2239 C CA  . ARG B 6   ? 0.2832 0.3957 0.2827 0.0578  0.0808  0.1805  41  ARG B CA  
2240 C C   . ARG B 6   ? 0.3658 0.4516 0.3740 0.0515  0.0684  0.1666  41  ARG B C   
2241 O O   . ARG B 6   ? 0.3708 0.4553 0.3631 0.0558  0.0619  0.1601  41  ARG B O   
2242 C CB  . ARG B 6   ? 0.4053 0.5389 0.3805 0.0685  0.0815  0.1849  41  ARG B CB  
2243 C CG  . ARG B 6   ? 0.4077 0.5638 0.3619 0.0769  0.0883  0.1774  41  ARG B CG  
2244 C CD  . ARG B 6   ? 0.5589 0.7338 0.4870 0.0870  0.0859  0.1749  41  ARG B CD  
2245 N NE  . ARG B 6   ? 0.5562 0.7533 0.4715 0.0950  0.0929  0.1727  41  ARG B NE  
2246 C CZ  . ARG B 6   ? 0.4771 0.6854 0.3636 0.1031  0.0909  0.1550  41  ARG B CZ  
2247 N NH1 . ARG B 6   ? 0.4867 0.6885 0.3543 0.1040  0.0819  0.1385  41  ARG B NH1 
2248 N NH2 . ARG B 6   ? 0.4077 0.6340 0.2856 0.1103  0.0976  0.1532  41  ARG B NH2 
2249 N N   . THR B 7   ? 0.3124 0.3792 0.3458 0.0416  0.0648  0.1612  42  THR B N   
2250 C CA  . THR B 7   ? 0.3403 0.3835 0.3804 0.0364  0.0539  0.1449  42  THR B CA  
2251 C C   . THR B 7   ? 0.3151 0.3486 0.3572 0.0311  0.0512  0.1246  42  THR B C   
2252 O O   . THR B 7   ? 0.3032 0.3427 0.3560 0.0281  0.0566  0.1278  42  THR B O   
2253 C CB  . THR B 7   ? 0.3375 0.3649 0.4076 0.0303  0.0503  0.1577  42  THR B CB  
2254 O OG1 . THR B 7   ? 0.4117 0.4384 0.5086 0.0225  0.0548  0.1679  42  THR B OG1 
2255 C CG2 . THR B 7   ? 0.3523 0.3877 0.4208 0.0367  0.0523  0.1790  42  THR B CG2 
2256 N N   . SER B 8   ? 0.2989 0.3197 0.3313 0.0304  0.0433  0.1050  43  SER B N   
2257 C CA  . SER B 8   ? 0.2975 0.3094 0.3320 0.0259  0.0405  0.0877  43  SER B CA  
2258 C C   . SER B 8   ? 0.2683 0.2651 0.3294 0.0174  0.0352  0.0866  43  SER B C   
2259 O O   . SER B 8   ? 0.2954 0.2829 0.3709 0.0152  0.0316  0.0937  43  SER B O   
2260 C CB  . SER B 8   ? 0.2983 0.3045 0.3124 0.0282  0.0351  0.0684  43  SER B CB  
2261 O OG  . SER B 8   ? 0.3559 0.3751 0.3465 0.0351  0.0393  0.0652  43  SER B OG  
2262 N N   . ALA B 9   ? 0.2624 0.2570 0.3299 0.0132  0.0344  0.0771  44  ALA B N   
2263 C CA  . ALA B 9   ? 0.2651 0.2476 0.3550 0.0054  0.0280  0.0720  44  ALA B CA  
2264 C C   . ALA B 9   ? 0.3297 0.2975 0.4143 0.0054  0.0197  0.0577  44  ALA B C   
2265 O O   . ALA B 9   ? 0.2784 0.2468 0.3424 0.0103  0.0190  0.0502  44  ALA B O   
2266 C CB  . ALA B 9   ? 0.2231 0.2105 0.3169 0.0026  0.0284  0.0643  44  ALA B CB  
2267 N N   . PRO B 10  ? 0.3022 0.2576 0.4061 -0.0001 0.0133  0.0534  45  PRO B N   
2268 C CA  . PRO B 10  ? 0.3245 0.2680 0.4234 0.0012  0.0063  0.0391  45  PRO B CA  
2269 C C   . PRO B 10  ? 0.2337 0.1807 0.3136 0.0031  0.0051  0.0242  45  PRO B C   
2270 O O   . PRO B 10  ? 0.2570 0.2095 0.3368 0.0009  0.0061  0.0204  45  PRO B O   
2271 C CB  . PRO B 10  ? 0.3805 0.3124 0.5039 -0.0052 0.0001  0.0343  45  PRO B CB  
2272 C CG  . PRO B 10  ? 0.3721 0.3066 0.5167 -0.0099 0.0039  0.0514  45  PRO B CG  
2273 C CD  . PRO B 10  ? 0.4535 0.4056 0.5859 -0.0074 0.0123  0.0614  45  PRO B CD  
2274 N N   . GLY B 11  ? 0.2789 0.2236 0.3446 0.0072  0.0031  0.0171  46  GLY B N   
2275 C CA  . GLY B 11  ? 0.2448 0.1933 0.2928 0.0089  0.0032  0.0062  46  GLY B CA  
2276 C C   . GLY B 11  ? 0.3118 0.2557 0.3621 0.0069  -0.0018 -0.0070 46  GLY B C   
2277 O O   . GLY B 11  ? 0.2316 0.1739 0.2744 0.0091  -0.0042 -0.0150 46  GLY B O   
2278 N N   . TYR B 12  ? 0.2431 0.1873 0.3040 0.0031  -0.0034 -0.0091 47  TYR B N   
2279 C CA  . TYR B 12  ? 0.2282 0.1724 0.2881 0.0022  -0.0079 -0.0213 47  TYR B CA  
2280 C C   . TYR B 12  ? 0.2761 0.2282 0.3364 0.0004  -0.0067 -0.0207 47  TYR B C   
2281 O O   . TYR B 12  ? 0.2311 0.1875 0.3012 -0.0018 -0.0042 -0.0122 47  TYR B O   
2282 C CB  . TYR B 12  ? 0.2224 0.1591 0.2960 0.0004  -0.0146 -0.0291 47  TYR B CB  
2283 C CG  . TYR B 12  ? 0.2130 0.1470 0.3079 -0.0051 -0.0174 -0.0256 47  TYR B CG  
2284 C CD1 . TYR B 12  ? 0.2361 0.1639 0.3452 -0.0069 -0.0156 -0.0140 47  TYR B CD1 
2285 C CD2 . TYR B 12  ? 0.2001 0.1394 0.3023 -0.0089 -0.0221 -0.0330 47  TYR B CD2 
2286 C CE1 . TYR B 12  ? 0.2430 0.1680 0.3754 -0.0134 -0.0181 -0.0098 47  TYR B CE1 
2287 C CE2 . TYR B 12  ? 0.2150 0.1530 0.3397 -0.0154 -0.0256 -0.0306 47  TYR B CE2 
2288 C CZ  . TYR B 12  ? 0.2576 0.1876 0.3984 -0.0181 -0.0234 -0.0189 47  TYR B CZ  
2289 O OH  . TYR B 12  ? 0.2920 0.2205 0.4588 -0.0259 -0.0266 -0.0151 47  TYR B OH  
2290 N N   . TYR B 13  ? 0.1919 0.1478 0.2423 0.0019  -0.0079 -0.0283 48  TYR B N   
2291 C CA  . TYR B 13  ? 0.1810 0.1452 0.2309 0.0018  -0.0070 -0.0273 48  TYR B CA  
2292 C C   . TYR B 13  ? 0.2154 0.1842 0.2655 0.0015  -0.0131 -0.0369 48  TYR B C   
2293 O O   . TYR B 13  ? 0.2272 0.1959 0.2659 0.0042  -0.0135 -0.0427 48  TYR B O   
2294 C CB  . TYR B 13  ? 0.2163 0.1819 0.2518 0.0055  -0.0009 -0.0243 48  TYR B CB  
2295 C CG  . TYR B 13  ? 0.2161 0.1896 0.2531 0.0069  0.0006  -0.0215 48  TYR B CG  
2296 C CD1 . TYR B 13  ? 0.3439 0.3232 0.3901 0.0069  0.0038  -0.0140 48  TYR B CD1 
2297 C CD2 . TYR B 13  ? 0.2005 0.1777 0.2309 0.0089  -0.0009 -0.0251 48  TYR B CD2 
2298 C CE1 . TYR B 13  ? 0.2785 0.2666 0.3277 0.0094  0.0051  -0.0109 48  TYR B CE1 
2299 C CE2 . TYR B 13  ? 0.2053 0.1905 0.2380 0.0114  0.0002  -0.0209 48  TYR B CE2 
2300 C CZ  . TYR B 13  ? 0.3324 0.3229 0.3749 0.0118  0.0031  -0.0143 48  TYR B CZ  
2301 O OH  . TYR B 13  ? 0.3379 0.3380 0.3845 0.0153  0.0042  -0.0095 48  TYR B OH  
2302 N N   . ARG B 14  ? 0.1863 0.1615 0.2491 -0.0016 -0.0179 -0.0383 49  ARG B N   
2303 C CA  . ARG B 14  ? 0.2005 0.1829 0.2630 -0.0015 -0.0251 -0.0488 49  ARG B CA  
2304 C C   . ARG B 14  ? 0.2087 0.2038 0.2639 0.0015  -0.0240 -0.0455 49  ARG B C   
2305 O O   . ARG B 14  ? 0.2180 0.2181 0.2784 0.0015  -0.0205 -0.0367 49  ARG B O   
2306 C CB  . ARG B 14  ? 0.2326 0.2159 0.3148 -0.0072 -0.0327 -0.0539 49  ARG B CB  
2307 C CG  . ARG B 14  ? 0.2404 0.2287 0.3212 -0.0068 -0.0415 -0.0692 49  ARG B CG  
2308 C CD  . ARG B 14  ? 0.2110 0.1856 0.2935 -0.0062 -0.0438 -0.0786 49  ARG B CD  
2309 N NE  . ARG B 14  ? 0.2447 0.2069 0.3482 -0.0119 -0.0452 -0.0754 49  ARG B NE  
2310 C CZ  . ARG B 14  ? 0.3101 0.2574 0.4203 -0.0115 -0.0465 -0.0798 49  ARG B CZ  
2311 N NH1 . ARG B 14  ? 0.2404 0.1859 0.3357 -0.0049 -0.0449 -0.0860 49  ARG B NH1 
2312 N NH2 . ARG B 14  ? 0.2633 0.2007 0.3943 -0.0169 -0.0474 -0.0739 49  ARG B NH2 
2313 N N   . MET B 15  ? 0.1970 0.1988 0.2405 0.0049  -0.0264 -0.0518 50  MET B N   
2314 C CA  . MET B 15  ? 0.1795 0.1940 0.2160 0.0088  -0.0256 -0.0470 50  MET B CA  
2315 C C   . MET B 15  ? 0.2771 0.3040 0.3061 0.0112  -0.0321 -0.0564 50  MET B C   
2316 O O   . MET B 15  ? 0.2431 0.2666 0.2647 0.0125  -0.0328 -0.0645 50  MET B O   
2317 C CB  . MET B 15  ? 0.2618 0.2701 0.2860 0.0125  -0.0169 -0.0391 50  MET B CB  
2318 C CG  . MET B 15  ? 0.2976 0.3162 0.3148 0.0173  -0.0152 -0.0326 50  MET B CG  
2319 S SD  . MET B 15  ? 0.2681 0.2751 0.2752 0.0200  -0.0055 -0.0244 50  MET B SD  
2320 C CE  . MET B 15  ? 0.3112 0.3233 0.3072 0.0209  -0.0067 -0.0297 50  MET B CE  
2321 N N   . LEU B 16  ? 0.2145 0.2579 0.2449 0.0129  -0.0366 -0.0553 51  LEU B N   
2322 C CA  . LEU B 16  ? 0.2137 0.2730 0.2337 0.0167  -0.0426 -0.0633 51  LEU B CA  
2323 C C   . LEU B 16  ? 0.3082 0.3734 0.3122 0.0232  -0.0359 -0.0536 51  LEU B C   
2324 O O   . LEU B 16  ? 0.3040 0.3652 0.3083 0.0248  -0.0292 -0.0405 51  LEU B O   
2325 C CB  . LEU B 16  ? 0.2304 0.3085 0.2590 0.0158  -0.0520 -0.0666 51  LEU B CB  
2326 C CG  . LEU B 16  ? 0.2466 0.3209 0.2945 0.0081  -0.0602 -0.0773 51  LEU B CG  
2327 C CD1 . LEU B 16  ? 0.2543 0.3508 0.3102 0.0069  -0.0709 -0.0821 51  LEU B CD1 
2328 C CD2 . LEU B 16  ? 0.3247 0.3870 0.3712 0.0063  -0.0636 -0.0927 51  LEU B CD2 
2329 N N   . LEU B 17  ? 0.2125 0.2871 0.2034 0.0270  -0.0373 -0.0601 52  LEU B N   
2330 C CA  . LEU B 17  ? 0.2388 0.3226 0.2157 0.0329  -0.0312 -0.0498 52  LEU B CA  
2331 C C   . LEU B 17  ? 0.3065 0.4147 0.2722 0.0382  -0.0378 -0.0573 52  LEU B C   
2332 O O   . LEU B 17  ? 0.2737 0.3857 0.2314 0.0401  -0.0392 -0.0690 52  LEU B O   
2333 C CB  . LEU B 17  ? 0.2177 0.2889 0.1891 0.0324  -0.0232 -0.0484 52  LEU B CB  
2334 C CG  . LEU B 17  ? 0.2375 0.3168 0.1987 0.0368  -0.0158 -0.0354 52  LEU B CG  
2335 C CD1 . LEU B 17  ? 0.2864 0.3551 0.2532 0.0362  -0.0098 -0.0199 52  LEU B CD1 
2336 C CD2 . LEU B 17  ? 0.2814 0.3566 0.2375 0.0364  -0.0104 -0.0380 52  LEU B CD2 
2337 N N   . GLY B 18  ? 0.2466 0.3730 0.2114 0.0416  -0.0421 -0.0510 53  GLY B N   
2338 C CA  . GLY B 18  ? 0.2646 0.4172 0.2184 0.0467  -0.0505 -0.0601 53  GLY B CA  
2339 C C   . GLY B 18  ? 0.3158 0.4663 0.2767 0.0421  -0.0609 -0.0826 53  GLY B C   
2340 O O   . GLY B 18  ? 0.2946 0.4361 0.2729 0.0354  -0.0661 -0.0865 53  GLY B O   
2341 N N   . ASP B 19  ? 0.2497 0.4082 0.1985 0.0458  -0.0637 -0.0974 54  ASP B N   
2342 C CA  . ASP B 19  ? 0.2600 0.4090 0.2190 0.0414  -0.0705 -0.1167 54  ASP B CA  
2343 C C   . ASP B 19  ? 0.2708 0.3933 0.2377 0.0376  -0.0657 -0.1221 54  ASP B C   
2344 O O   . ASP B 19  ? 0.3314 0.4416 0.3093 0.0342  -0.0691 -0.1340 54  ASP B O   
2345 C CB  . ASP B 19  ? 0.3578 0.5233 0.3058 0.0474  -0.0722 -0.1255 54  ASP B CB  
2346 C CG  . ASP B 19  ? 0.9011 1.0891 0.8476 0.0488  -0.0803 -0.1255 54  ASP B CG  
2347 O OD1 . ASP B 19  ? 0.5249 0.7108 0.4860 0.0425  -0.0871 -0.1250 54  ASP B OD1 
2348 O OD2 . ASP B 19  ? 0.6697 0.8791 0.6015 0.0563  -0.0796 -0.1251 54  ASP B OD2 
2349 N N   . PHE B 20  ? 0.2291 0.3417 0.1919 0.0381  -0.0568 -0.1113 55  PHE B N   
2350 C CA  . PHE B 20  ? 0.2504 0.3401 0.2201 0.0352  -0.0518 -0.1144 55  PHE B CA  
2351 C C   . PHE B 20  ? 0.2931 0.3622 0.2814 0.0271  -0.0513 -0.1078 55  PHE B C   
2352 O O   . PHE B 20  ? 0.2643 0.3352 0.2579 0.0247  -0.0501 -0.0955 55  PHE B O   
2353 C CB  . PHE B 20  ? 0.2149 0.3035 0.1745 0.0387  -0.0403 -0.1019 55  PHE B CB  
2354 C CG  . PHE B 20  ? 0.2172 0.3264 0.1594 0.0469  -0.0380 -0.1058 55  PHE B CG  
2355 C CD1 . PHE B 20  ? 0.2645 0.3878 0.2040 0.0505  -0.0433 -0.1150 55  PHE B CD1 
2356 C CD2 . PHE B 20  ? 0.2888 0.4005 0.2241 0.0493  -0.0275 -0.0932 55  PHE B CD2 
2357 C CE1 . PHE B 20  ? 0.2745 0.4161 0.2015 0.0579  -0.0391 -0.1142 55  PHE B CE1 
2358 C CE2 . PHE B 20  ? 0.3123 0.4452 0.2337 0.0568  -0.0237 -0.0936 55  PHE B CE2 
2359 C CZ  . PHE B 20  ? 0.2851 0.4321 0.2035 0.0609  -0.0291 -0.1027 55  PHE B CZ  
2360 N N   . GLU B 21  ? 0.2320 0.2824 0.2303 0.0241  -0.0514 -0.1149 56  GLU B N   
2361 C CA  . GLU B 21  ? 0.2441 0.2757 0.2582 0.0174  -0.0491 -0.1069 56  GLU B CA  
2362 C C   . GLU B 21  ? 0.2067 0.2266 0.2161 0.0186  -0.0397 -0.0977 56  GLU B C   
2363 O O   . GLU B 21  ? 0.2261 0.2424 0.2315 0.0219  -0.0382 -0.1046 56  GLU B O   
2364 C CB  . GLU B 21  ? 0.2673 0.2862 0.2981 0.0131  -0.0556 -0.1180 56  GLU B CB  
2365 C CG  . GLU B 21  ? 0.2247 0.2268 0.2734 0.0063  -0.0542 -0.1102 56  GLU B CG  
2366 C CD  . GLU B 21  ? 0.2866 0.2737 0.3483 0.0042  -0.0554 -0.1137 56  GLU B CD  
2367 O OE1 . GLU B 21  ? 0.3439 0.3248 0.3994 0.0087  -0.0511 -0.1141 56  GLU B OE1 
2368 O OE2 . GLU B 21  ? 0.3020 0.2853 0.3807 -0.0016 -0.0607 -0.1157 56  GLU B OE2 
2369 N N   . ILE B 22  ? 0.1912 0.2060 0.2021 0.0162  -0.0337 -0.0833 57  ILE B N   
2370 C CA  . ILE B 22  ? 0.2032 0.2072 0.2112 0.0161  -0.0260 -0.0753 57  ILE B CA  
2371 C C   . ILE B 22  ? 0.2871 0.2766 0.3079 0.0116  -0.0257 -0.0718 57  ILE B C   
2372 O O   . ILE B 22  ? 0.2245 0.2141 0.2543 0.0083  -0.0272 -0.0672 57  ILE B O   
2373 C CB  . ILE B 22  ? 0.2260 0.2340 0.2258 0.0172  -0.0194 -0.0629 57  ILE B CB  
2374 C CG1 . ILE B 22  ? 0.2695 0.2947 0.2587 0.0216  -0.0200 -0.0627 57  ILE B CG1 
2375 C CG2 . ILE B 22  ? 0.1908 0.1893 0.1873 0.0166  -0.0128 -0.0578 57  ILE B CG2 
2376 C CD1 . ILE B 22  ? 0.2381 0.2718 0.2185 0.0257  -0.0199 -0.0710 57  ILE B CD1 
2377 N N   . THR B 23  ? 0.2081 0.1874 0.2306 0.0119  -0.0238 -0.0728 58  THR B N   
2378 C CA  . THR B 23  ? 0.2390 0.2065 0.2713 0.0087  -0.0222 -0.0660 58  THR B CA  
2379 C C   . THR B 23  ? 0.2359 0.1999 0.2602 0.0102  -0.0162 -0.0597 58  THR B C   
2380 O O   . THR B 23  ? 0.2201 0.1834 0.2413 0.0128  -0.0160 -0.0639 58  THR B O   
2381 C CB  . THR B 23  ? 0.2585 0.2168 0.3042 0.0077  -0.0272 -0.0726 58  THR B CB  
2382 O OG1 . THR B 23  ? 0.2527 0.2151 0.3056 0.0061  -0.0342 -0.0825 58  THR B OG1 
2383 C CG2 . THR B 23  ? 0.2611 0.2101 0.3186 0.0041  -0.0251 -0.0620 58  THR B CG2 
2384 N N   . ALA B 24  ? 0.1928 0.1557 0.2141 0.0088  -0.0117 -0.0508 59  ALA B N   
2385 C CA  . ALA B 24  ? 0.1752 0.1344 0.1902 0.0094  -0.0075 -0.0465 59  ALA B CA  
2386 C C   . ALA B 24  ? 0.2768 0.2295 0.2993 0.0092  -0.0084 -0.0436 59  ALA B C   
2387 O O   . ALA B 24  ? 0.2111 0.1611 0.2431 0.0073  -0.0091 -0.0392 59  ALA B O   
2388 C CB  . ALA B 24  ? 0.1954 0.1547 0.2048 0.0089  -0.0026 -0.0400 59  ALA B CB  
2389 N N   . LEU B 25  ? 0.2023 0.1539 0.2223 0.0113  -0.0085 -0.0449 60  LEU B N   
2390 C CA  . LEU B 25  ? 0.2216 0.1682 0.2485 0.0126  -0.0096 -0.0407 60  LEU B CA  
2391 C C   . LEU B 25  ? 0.2715 0.2211 0.2896 0.0135  -0.0067 -0.0352 60  LEU B C   
2392 O O   . LEU B 25  ? 0.2236 0.1779 0.2349 0.0143  -0.0065 -0.0388 60  LEU B O   
2393 C CB  . LEU B 25  ? 0.1910 0.1356 0.2237 0.0159  -0.0132 -0.0477 60  LEU B CB  
2394 C CG  . LEU B 25  ? 0.2048 0.1466 0.2452 0.0158  -0.0172 -0.0569 60  LEU B CG  
2395 C CD1 . LEU B 25  ? 0.2718 0.2122 0.3159 0.0212  -0.0198 -0.0656 60  LEU B CD1 
2396 C CD2 . LEU B 25  ? 0.2218 0.1557 0.2761 0.0121  -0.0193 -0.0528 60  LEU B CD2 
2397 N N   . SER B 26  ? 0.2386 0.1873 0.2574 0.0133  -0.0046 -0.0266 61  SER B N   
2398 C CA  . SER B 26  ? 0.2128 0.1664 0.2216 0.0149  -0.0026 -0.0226 61  SER B CA  
2399 C C   . SER B 26  ? 0.2196 0.1749 0.2314 0.0183  -0.0055 -0.0202 61  SER B C   
2400 O O   . SER B 26  ? 0.2393 0.1896 0.2626 0.0200  -0.0071 -0.0153 61  SER B O   
2401 C CB  . SER B 26  ? 0.2269 0.1824 0.2337 0.0152  0.0013  -0.0138 61  SER B CB  
2402 O OG  . SER B 26  ? 0.2166 0.1786 0.2112 0.0176  0.0025  -0.0122 61  SER B OG  
2403 N N   . ASP B 27  ? 0.2130 0.1754 0.2165 0.0193  -0.0066 -0.0234 62  ASP B N   
2404 C CA  . ASP B 27  ? 0.2314 0.1994 0.2366 0.0235  -0.0094 -0.0194 62  ASP B CA  
2405 C C   . ASP B 27  ? 0.2702 0.2450 0.2674 0.0257  -0.0084 -0.0106 62  ASP B C   
2406 O O   . ASP B 27  ? 0.2711 0.2528 0.2688 0.0300  -0.0110 -0.0049 62  ASP B O   
2407 C CB  . ASP B 27  ? 0.2433 0.2197 0.2457 0.0233  -0.0119 -0.0268 62  ASP B CB  
2408 C CG  . ASP B 27  ? 0.2640 0.2465 0.2732 0.0289  -0.0154 -0.0233 62  ASP B CG  
2409 O OD1 . ASP B 27  ? 0.2569 0.2320 0.2772 0.0327  -0.0160 -0.0200 62  ASP B OD1 
2410 O OD2 . ASP B 27  ? 0.2395 0.2342 0.2445 0.0296  -0.0180 -0.0241 62  ASP B OD2 
2411 N N   . GLY B 28  ? 0.2362 0.2108 0.2257 0.0239  -0.0046 -0.0091 63  GLY B N   
2412 C CA  . GLY B 28  ? 0.2316 0.2157 0.2091 0.0266  -0.0030 -0.0038 63  GLY B CA  
2413 C C   . GLY B 28  ? 0.2778 0.2651 0.2420 0.0243  -0.0026 -0.0145 63  GLY B C   
2414 O O   . GLY B 28  ? 0.2737 0.2541 0.2394 0.0202  -0.0021 -0.0232 63  GLY B O   
2415 N N   . THR B 29  ? 0.2541 0.2520 0.2052 0.0274  -0.0027 -0.0138 64  THR B N   
2416 C CA  . THR B 29  ? 0.2795 0.2797 0.2182 0.0255  -0.0033 -0.0260 64  THR B CA  
2417 C C   . THR B 29  ? 0.3034 0.3185 0.2325 0.0279  -0.0090 -0.0283 64  THR B C   
2418 O O   . THR B 29  ? 0.2952 0.3206 0.2239 0.0329  -0.0106 -0.0176 64  THR B O   
2419 C CB  . THR B 29  ? 0.2658 0.2651 0.1947 0.0279  0.0028  -0.0264 64  THR B CB  
2420 O OG1 . THR B 29  ? 0.3261 0.3384 0.2466 0.0342  0.0048  -0.0162 64  THR B OG1 
2421 C CG2 . THR B 29  ? 0.2797 0.2677 0.2188 0.0262  0.0081  -0.0228 64  THR B CG2 
2422 N N   . VAL B 30  ? 0.2529 0.2697 0.1754 0.0243  -0.0124 -0.0420 65  VAL B N   
2423 C CA  . VAL B 30  ? 0.2544 0.2877 0.1679 0.0256  -0.0193 -0.0470 65  VAL B CA  
2424 C C   . VAL B 30  ? 0.3199 0.3524 0.2211 0.0233  -0.0203 -0.0627 65  VAL B C   
2425 O O   . VAL B 30  ? 0.3036 0.3211 0.2095 0.0180  -0.0179 -0.0713 65  VAL B O   
2426 C CB  . VAL B 30  ? 0.3193 0.3582 0.2451 0.0222  -0.0259 -0.0482 65  VAL B CB  
2427 C CG1 . VAL B 30  ? 0.2822 0.3089 0.2188 0.0139  -0.0253 -0.0577 65  VAL B CG1 
2428 C CG2 . VAL B 30  ? 0.3872 0.4464 0.3051 0.0234  -0.0342 -0.0531 65  VAL B CG2 
2429 N N   . ALA B 31  ? 0.2887 0.3372 0.1738 0.0279  -0.0239 -0.0663 66  ALA B N   
2430 C CA  . ALA B 31  ? 0.3075 0.3555 0.1802 0.0264  -0.0258 -0.0842 66  ALA B CA  
2431 C C   . ALA B 31  ? 0.4865 0.5362 0.3671 0.0177  -0.0349 -0.0979 66  ALA B C   
2432 O O   . ALA B 31  ? 0.4124 0.4798 0.2943 0.0177  -0.0427 -0.0960 66  ALA B O   
2433 C CB  . ALA B 31  ? 0.3279 0.3952 0.1788 0.0354  -0.0265 -0.0844 66  ALA B CB  
2434 N N   . LEU B 32  ? 0.3667 0.3980 0.2552 0.0101  -0.0336 -0.1094 67  LEU B N   
2435 C CA  . LEU B 32  ? 0.3117 0.3407 0.2140 -0.0002 -0.0399 -0.1172 67  LEU B CA  
2436 C C   . LEU B 32  ? 0.4375 0.4586 0.3352 -0.0038 -0.0417 -0.1294 67  LEU B C   
2437 O O   . LEU B 32  ? 0.3707 0.3766 0.2619 -0.0012 -0.0354 -0.1326 67  LEU B O   
2438 C CB  . LEU B 32  ? 0.3312 0.3438 0.2515 -0.0071 -0.0361 -0.1153 67  LEU B CB  
2439 C CG  . LEU B 32  ? 0.3528 0.3696 0.2826 -0.0050 -0.0337 -0.1010 67  LEU B CG  
2440 C CD1 . LEU B 32  ? 0.4167 0.4204 0.3637 -0.0119 -0.0300 -0.0987 67  LEU B CD1 
2441 C CD2 . LEU B 32  ? 0.4577 0.4968 0.3899 -0.0035 -0.0412 -0.0968 67  LEU B CD2 
2442 N N   . PRO B 33  ? 0.3823 0.3932 0.2998 0.0575  -0.0124 -0.0494 68  PRO B N   
2443 C CA  . PRO B 33  ? 0.3706 0.4051 0.3124 0.0506  -0.0306 -0.0710 68  PRO B CA  
2444 C C   . PRO B 33  ? 0.3911 0.4275 0.3816 0.0385  -0.0220 -0.0777 68  PRO B C   
2445 O O   . PRO B 33  ? 0.3408 0.3970 0.3796 0.0370  -0.0287 -0.0842 68  PRO B O   
2446 C CB  . PRO B 33  ? 0.3977 0.4607 0.3551 0.0630  -0.0552 -0.0726 68  PRO B CB  
2447 C CG  . PRO B 33  ? 0.3947 0.4525 0.3701 0.0744  -0.0462 -0.0531 68  PRO B CG  
2448 C CD  . PRO B 33  ? 0.3834 0.4044 0.3163 0.0731  -0.0206 -0.0372 68  PRO B CD  
2449 N N   . VAL B 34  ? 0.3558 0.3702 0.3337 0.0293  -0.0066 -0.0757 69  VAL B N   
2450 C CA  . VAL B 34  ? 0.3523 0.3594 0.3656 0.0185  0.0029  -0.0749 69  VAL B CA  
2451 C C   . VAL B 34  ? 0.3217 0.3447 0.3764 0.0118  -0.0094 -0.0945 69  VAL B C   
2452 O O   . VAL B 34  ? 0.3271 0.3489 0.4214 0.0039  -0.0035 -0.0942 69  VAL B O   
2453 C CB  . VAL B 34  ? 0.4389 0.4210 0.4276 0.0123  0.0167  -0.0671 69  VAL B CB  
2454 C CG1 . VAL B 34  ? 0.4051 0.3728 0.3601 0.0154  0.0323  -0.0505 69  VAL B CG1 
2455 C CG2 . VAL B 34  ? 0.3879 0.3699 0.3592 0.0116  0.0096  -0.0821 69  VAL B CG2 
2456 N N   . ASP B 35  ? 0.3282 0.3643 0.3737 0.0126  -0.0239 -0.1133 70  ASP B N   
2457 C CA  . ASP B 35  ? 0.3479 0.4000 0.4347 0.0046  -0.0341 -0.1364 70  ASP B CA  
2458 C C   . ASP B 35  ? 0.3790 0.4579 0.5078 0.0048  -0.0433 -0.1422 70  ASP B C   
2459 O O   . ASP B 35  ? 0.4357 0.5232 0.6121 -0.0053 -0.0441 -0.1579 70  ASP B O   
2460 C CB  . ASP B 35  ? 0.3762 0.4398 0.4407 0.0036  -0.0461 -0.1591 70  ASP B CB  
2461 C CG  . ASP B 35  ? 0.4534 0.5319 0.4741 0.0134  -0.0590 -0.1564 70  ASP B CG  
2462 O OD1 . ASP B 35  ? 0.3713 0.4409 0.3690 0.0233  -0.0542 -0.1332 70  ASP B OD1 
2463 O OD2 . ASP B 35  ? 0.5094 0.6069 0.5175 0.0108  -0.0738 -0.1773 70  ASP B OD2 
2464 N N   . LYS B 36  ? 0.2958 0.3882 0.4128 0.0165  -0.0499 -0.1309 71  LYS B N   
2465 C CA  . LYS B 36  ? 0.3128 0.4358 0.4774 0.0190  -0.0602 -0.1374 71  LYS B CA  
2466 C C   . LYS B 36  ? 0.3076 0.4209 0.5075 0.0152  -0.0394 -0.1238 71  LYS B C   
2467 O O   . LYS B 36  ? 0.3788 0.5162 0.6340 0.0111  -0.0417 -0.1351 71  LYS B O   
2468 C CB  . LYS B 36  ? 0.3344 0.4805 0.4765 0.0360  -0.0820 -0.1331 71  LYS B CB  
2469 C CG  . LYS B 36  ? 0.4396 0.5923 0.5339 0.0378  -0.1005 -0.1450 71  LYS B CG  
2470 C CD  . LYS B 36  ? 0.7168 0.8891 0.7834 0.0551  -0.1248 -0.1366 71  LYS B CD  
2471 C CE  . LYS B 36  ? 0.6869 0.8804 0.7222 0.0515  -0.1492 -0.1579 71  LYS B CE  
2472 N NZ  . LYS B 36  ? 0.8289 1.0482 0.8441 0.0683  -0.1803 -0.1506 71  LYS B NZ  
2473 N N   . ARG B 37  ? 0.2815 0.3620 0.4516 0.0144  -0.0182 -0.1026 72  ARG B N   
2474 C CA  . ARG B 37  ? 0.3172 0.3865 0.5125 0.0078  0.0045  -0.0910 72  ARG B CA  
2475 C C   . ARG B 37  ? 0.2657 0.3118 0.4767 -0.0103 0.0211  -0.0907 72  ARG B C   
2476 O O   . ARG B 37  ? 0.3560 0.3998 0.6015 -0.0207 0.0380  -0.0893 72  ARG B O   
2477 C CB  . ARG B 37  ? 0.3559 0.4038 0.5110 0.0148  0.0202  -0.0694 72  ARG B CB  
2478 C CG  . ARG B 37  ? 0.5394 0.5992 0.6738 0.0338  0.0075  -0.0639 72  ARG B CG  
2479 C CD  . ARG B 37  ? 0.4295 0.5286 0.6099 0.0441  -0.0144 -0.0760 72  ARG B CD  
2480 N NE  . ARG B 37  ? 0.6217 0.7343 0.8600 0.0416  -0.0012 -0.0779 72  ARG B NE  
2481 C CZ  . ARG B 37  ? 0.5419 0.6610 0.7966 0.0552  0.0035  -0.0690 72  ARG B CZ  
2482 N NH1 . ARG B 37  ? 0.6539 0.7624 0.8681 0.0727  -0.0035 -0.0539 72  ARG B NH1 
2483 N NH2 . ARG B 37  ? 0.4164 0.5510 0.7322 0.0505  0.0179  -0.0759 72  ARG B NH2 
2484 N N   . LEU B 38  ? 0.3148 0.3420 0.5025 -0.0142 0.0177  -0.0917 73  LEU B N   
2485 C CA  . LEU B 38  ? 0.2501 0.2508 0.4516 -0.0285 0.0305  -0.0877 73  LEU B CA  
2486 C C   . LEU B 38  ? 0.3085 0.3228 0.5681 -0.0392 0.0290  -0.1075 73  LEU B C   
2487 O O   . LEU B 38  ? 0.3173 0.3612 0.5996 -0.0360 0.0111  -0.1304 73  LEU B O   
2488 C CB  . LEU B 38  ? 0.2646 0.2447 0.4357 -0.0266 0.0245  -0.0853 73  LEU B CB  
2489 C CG  . LEU B 38  ? 0.2651 0.2286 0.3832 -0.0203 0.0294  -0.0673 73  LEU B CG  
2490 C CD1 . LEU B 38  ? 0.3034 0.2587 0.4040 -0.0165 0.0198  -0.0732 73  LEU B CD1 
2491 C CD2 . LEU B 38  ? 0.2841 0.2211 0.3903 -0.0297 0.0480  -0.0455 73  LEU B CD2 
2492 N N   . ASN B 39  ? 0.2444 0.2357 0.5253 -0.0540 0.0492  -0.0993 74  ASN B N   
2493 C CA  . ASN B 39  ? 0.2614 0.2601 0.6009 -0.0681 0.0549  -0.1177 74  ASN B CA  
2494 C C   . ASN B 39  ? 0.3048 0.2831 0.6538 -0.0734 0.0499  -0.1262 74  ASN B C   
2495 O O   . ASN B 39  ? 0.4220 0.3706 0.7711 -0.0803 0.0643  -0.1130 74  ASN B O   
2496 C CB  . ASN B 39  ? 0.2679 0.2462 0.6230 -0.0839 0.0835  -0.1050 74  ASN B CB  
2497 C CG  . ASN B 39  ? 0.4124 0.4193 0.7830 -0.0805 0.0905  -0.1072 74  ASN B CG  
2498 O OD1 . ASN B 39  ? 0.4228 0.4711 0.8145 -0.0677 0.0711  -0.1234 74  ASN B OD1 
2499 N ND2 . ASN B 39  ? 0.4593 0.4436 0.8161 -0.0903 0.1174  -0.0904 74  ASN B ND2 
2500 N N   . GLN B 40  ? 0.2620 0.2602 0.6039 -0.0635 0.0286  -0.1436 75  GLN B N   
2501 C CA  . GLN B 40  ? 0.2780 0.2673 0.6288 -0.0636 0.0239  -0.1547 75  GLN B CA  
2502 C C   . GLN B 40  ? 0.2905 0.3158 0.6372 -0.0559 0.0027  -0.1809 75  GLN B C   
2503 O O   . GLN B 40  ? 0.2515 0.2989 0.5762 -0.0489 -0.0104 -0.1845 75  GLN B O   
2504 C CB  . GLN B 40  ? 0.3142 0.2629 0.6323 -0.0596 0.0282  -0.1320 75  GLN B CB  
2505 C CG  . GLN B 40  ? 0.3246 0.2743 0.6021 -0.0485 0.0164  -0.1305 75  GLN B CG  
2506 C CD  . GLN B 40  ? 0.3824 0.2978 0.6383 -0.0437 0.0184  -0.1110 75  GLN B CD  
2507 O OE1 . GLN B 40  ? 0.3642 0.2533 0.6308 -0.0478 0.0264  -0.0954 75  GLN B OE1 
2508 N NE2 . GLN B 40  ? 0.3952 0.3151 0.6155 -0.0333 0.0103  -0.1095 75  GLN B NE2 
2509 N N   . PRO B 41  ? 0.3382 0.3695 0.7000 -0.0563 0.0002  -0.1973 76  PRO B N   
2510 C CA  . PRO B 41  ? 0.3342 0.3987 0.6834 -0.0509 -0.0167 -0.2206 76  PRO B CA  
2511 C C   . PRO B 41  ? 0.3096 0.3710 0.6075 -0.0414 -0.0256 -0.2140 76  PRO B C   
2512 O O   . PRO B 41  ? 0.2580 0.2904 0.5374 -0.0383 -0.0183 -0.1980 76  PRO B O   
2513 C CB  . PRO B 41  ? 0.2941 0.3541 0.6682 -0.0551 -0.0099 -0.2350 76  PRO B CB  
2514 C CG  . PRO B 41  ? 0.3869 0.4245 0.7990 -0.0638 0.0072  -0.2259 76  PRO B CG  
2515 C CD  . PRO B 41  ? 0.3714 0.3800 0.7621 -0.0629 0.0143  -0.1956 76  PRO B CD  
2516 N N   . ALA B 42  ? 0.3135 0.4051 0.5860 -0.0361 -0.0417 -0.2253 77  ALA B N   
2517 C CA  . ALA B 42  ? 0.2813 0.3697 0.4986 -0.0276 -0.0475 -0.2188 77  ALA B CA  
2518 C C   . ALA B 42  ? 0.2740 0.3458 0.4766 -0.0273 -0.0387 -0.2192 77  ALA B C   
2519 O O   . ALA B 42  ? 0.2961 0.3502 0.4664 -0.0221 -0.0340 -0.2053 77  ALA B O   
2520 C CB  . ALA B 42  ? 0.3486 0.4699 0.5371 -0.0221 -0.0665 -0.2280 77  ALA B CB  
2521 N N   . PRO B 43  ? 0.2850 0.3637 0.5123 -0.0327 -0.0353 -0.2356 78  PRO B N   
2522 C CA  . PRO B 43  ? 0.3355 0.4010 0.5582 -0.0320 -0.0264 -0.2367 78  PRO B CA  
2523 C C   . PRO B 43  ? 0.3734 0.4081 0.6109 -0.0287 -0.0173 -0.2184 78  PRO B C   
2524 O O   . PRO B 43  ? 0.3096 0.3352 0.5310 -0.0244 -0.0139 -0.2130 78  PRO B O   
2525 C CB  . PRO B 43  ? 0.4351 0.5149 0.6925 -0.0393 -0.0235 -0.2605 78  PRO B CB  
2526 C CG  . PRO B 43  ? 0.3229 0.4299 0.5807 -0.0430 -0.0351 -0.2734 78  PRO B CG  
2527 C CD  . PRO B 43  ? 0.3021 0.4039 0.5630 -0.0396 -0.0393 -0.2566 78  PRO B CD  
2528 N N   . LYS B 44  ? 0.2751 0.2931 0.5424 -0.0315 -0.0133 -0.2077 79  LYS B N   
2529 C CA  . LYS B 44  ? 0.2754 0.2598 0.5483 -0.0286 -0.0070 -0.1858 79  LYS B CA  
2530 C C   . LYS B 44  ? 0.3748 0.3492 0.6053 -0.0224 -0.0092 -0.1687 79  LYS B C   
2531 O O   . LYS B 44  ? 0.3338 0.2927 0.5543 -0.0167 -0.0082 -0.1585 79  LYS B O   
2532 C CB  . LYS B 44  ? 0.3096 0.2747 0.6150 -0.0354 0.0006  -0.1748 79  LYS B CB  
2533 C CG  . LYS B 44  ? 0.3612 0.2869 0.6692 -0.0332 0.0064  -0.1486 79  LYS B CG  
2534 C CD  . LYS B 44  ? 0.4586 0.3643 0.7924 -0.0424 0.0175  -0.1372 79  LYS B CD  
2535 C CE  . LYS B 44  ? 0.5914 0.4540 0.9166 -0.0401 0.0216  -0.1067 79  LYS B CE  
2536 N NZ  . LYS B 44  ? 0.7014 0.5492 0.9843 -0.0375 0.0201  -0.0826 79  LYS B NZ  
2537 N N   . THR B 45  ? 0.3021 0.2872 0.5101 -0.0229 -0.0125 -0.1674 80  THR B N   
2538 C CA  . THR B 45  ? 0.2946 0.2722 0.4595 -0.0169 -0.0121 -0.1550 80  THR B CA  
2539 C C   . THR B 45  ? 0.2631 0.2519 0.3962 -0.0117 -0.0136 -0.1610 80  THR B C   
2540 O O   . THR B 45  ? 0.2741 0.2508 0.3856 -0.0074 -0.0096 -0.1502 80  THR B O   
2541 C CB  . THR B 45  ? 0.3332 0.3262 0.4798 -0.0156 -0.0140 -0.1484 80  THR B CB  
2542 O OG1 . THR B 45  ? 0.2929 0.2768 0.4674 -0.0214 -0.0066 -0.1347 80  THR B OG1 
2543 C CG2 . THR B 45  ? 0.2833 0.2714 0.3786 -0.0077 -0.0096 -0.1293 80  THR B CG2 
2544 N N   . GLN B 46  ? 0.3052 0.3169 0.4354 -0.0136 -0.0178 -0.1778 81  GLN B N   
2545 C CA  . GLN B 46  ? 0.2951 0.3133 0.3947 -0.0122 -0.0151 -0.1812 81  GLN B CA  
2546 C C   . GLN B 46  ? 0.2836 0.2918 0.4051 -0.0110 -0.0089 -0.1810 81  GLN B C   
2547 O O   . GLN B 46  ? 0.3084 0.3133 0.4074 -0.0085 -0.0043 -0.1747 81  GLN B O   
2548 C CB  . GLN B 46  ? 0.3598 0.3993 0.4552 -0.0170 -0.0196 -0.1996 81  GLN B CB  
2549 C CG  . GLN B 46  ? 0.7325 0.7854 0.7902 -0.0158 -0.0293 -0.1996 81  GLN B CG  
2550 C CD  . GLN B 46  ? 0.7282 0.7694 0.7343 -0.0100 -0.0267 -0.1812 81  GLN B CD  
2551 O OE1 . GLN B 46  ? 0.7535 0.7775 0.7529 -0.0069 -0.0178 -0.1668 81  GLN B OE1 
2552 N NE2 . GLN B 46  ? 0.8256 0.8749 0.7928 -0.0089 -0.0343 -0.1813 81  GLN B NE2 
2553 N N   . SER B 47  ? 0.2700 0.2739 0.4386 -0.0126 -0.0086 -0.1879 82  SER B N   
2554 C CA  . SER B 47  ? 0.3026 0.2977 0.4995 -0.0093 -0.0054 -0.1884 82  SER B CA  
2555 C C   . SER B 47  ? 0.3736 0.3483 0.5621 -0.0028 -0.0072 -0.1687 82  SER B C   
2556 O O   . SER B 47  ? 0.3239 0.2998 0.5140 0.0015  -0.0064 -0.1690 82  SER B O   
2557 C CB  . SER B 47  ? 0.3343 0.3237 0.5835 -0.0115 -0.0044 -0.1965 82  SER B CB  
2558 O OG  . SER B 47  ? 0.5481 0.5590 0.8068 -0.0180 -0.0016 -0.2191 82  SER B OG  
2559 N N   . ALA B 48  ? 0.2895 0.2461 0.4711 -0.0030 -0.0093 -0.1527 83  ALA B N   
2560 C CA  . ALA B 48  ? 0.2731 0.2084 0.4412 0.0021  -0.0110 -0.1339 83  ALA B CA  
2561 C C   . ALA B 48  ? 0.3470 0.2949 0.4730 0.0042  -0.0079 -0.1349 83  ALA B C   
2562 O O   . ALA B 48  ? 0.4441 0.3904 0.5702 0.0088  -0.0092 -0.1331 83  ALA B O   
2563 C CB  . ALA B 48  ? 0.3076 0.2200 0.4719 -0.0017 -0.0096 -0.1157 83  ALA B CB  
2564 N N   . LEU B 49  ? 0.3113 0.2725 0.4032 0.0008  -0.0040 -0.1374 84  LEU B N   
2565 C CA  . LEU B 49  ? 0.3597 0.3278 0.4081 0.0015  0.0019  -0.1326 84  LEU B CA  
2566 C C   . LEU B 49  ? 0.3142 0.2942 0.3678 0.0010  0.0049  -0.1415 84  LEU B C   
2567 O O   . LEU B 49  ? 0.3174 0.2976 0.3570 0.0020  0.0091  -0.1368 84  LEU B O   
2568 C CB  . LEU B 49  ? 0.3164 0.2922 0.3311 -0.0001 0.0036  -0.1309 84  LEU B CB  
2569 C CG  . LEU B 49  ? 0.3461 0.3156 0.3583 0.0007  0.0029  -0.1250 84  LEU B CG  
2570 C CD1 . LEU B 49  ? 0.4114 0.3929 0.3943 0.0025  0.0014  -0.1255 84  LEU B CD1 
2571 C CD2 . LEU B 49  ? 0.3948 0.3489 0.3919 0.0016  0.0101  -0.1057 84  LEU B CD2 
2572 N N   . ALA B 50  ? 0.2877 0.2788 0.3654 -0.0016 0.0040  -0.1566 85  ALA B N   
2573 C CA  . ALA B 50  ? 0.3014 0.3045 0.3905 -0.0034 0.0093  -0.1684 85  ALA B CA  
2574 C C   . ALA B 50  ? 0.3719 0.3736 0.4969 0.0021  0.0068  -0.1699 85  ALA B C   
2575 O O   . ALA B 50  ? 0.3436 0.3555 0.4698 0.0013  0.0119  -0.1750 85  ALA B O   
2576 C CB  . ALA B 50  ? 0.2854 0.3003 0.3983 -0.0079 0.0101  -0.1869 85  ALA B CB  
2577 N N   . LYS B 51  ? 0.2800 0.2674 0.4373 0.0078  -0.0021 -0.1653 86  LYS B N   
2578 C CA  . LYS B 51  ? 0.3114 0.2915 0.5006 0.0161  -0.0099 -0.1629 86  LYS B CA  
2579 C C   . LYS B 51  ? 0.3952 0.3761 0.5527 0.0174  -0.0090 -0.1554 86  LYS B C   
2580 O O   . LYS B 51  ? 0.3645 0.3544 0.5443 0.0221  -0.0129 -0.1621 86  LYS B O   
2581 C CB  . LYS B 51  ? 0.4566 0.4087 0.6740 0.0222  -0.0210 -0.1490 86  LYS B CB  
2582 C CG  . LYS B 51  ? 0.4822 0.4322 0.7476 0.0226  -0.0221 -0.1568 86  LYS B CG  
2583 C CD  . LYS B 51  ? 0.6371 0.5544 0.9308 0.0303  -0.0332 -0.1355 86  LYS B CD  
2584 C CE  . LYS B 51  ? 0.6160 0.5263 0.9471 0.0269  -0.0293 -0.1403 86  LYS B CE  
2585 N NZ  . LYS B 51  ? 0.5820 0.4556 0.9171 0.0284  -0.0335 -0.1128 86  LYS B NZ  
2586 N N   . SER B 52  ? 0.3458 0.3197 0.4557 0.0131  -0.0039 -0.1435 87  SER B N   
2587 C CA  . SER B 52  ? 0.3821 0.3584 0.4590 0.0118  0.0007  -0.1372 87  SER B CA  
2588 C C   . SER B 52  ? 0.3058 0.2958 0.3500 0.0045  0.0138  -0.1367 87  SER B C   
2589 O O   . SER B 52  ? 0.3194 0.3062 0.3298 0.0018  0.0200  -0.1257 87  SER B O   
2590 C CB  . SER B 52  ? 0.3243 0.2817 0.3707 0.0111  0.0003  -0.1229 87  SER B CB  
2591 O OG  . SER B 52  ? 0.4835 0.4267 0.5493 0.0164  -0.0136 -0.1050 87  SER B OG  
2592 N N   . PHE B 53  ? 0.2720 0.2751 0.3462 -0.0478 0.0526  -0.1445 88  PHE B N   
2593 C CA  . PHE B 53  ? 0.2886 0.2875 0.3178 -0.0403 0.0586  -0.1494 88  PHE B CA  
2594 C C   . PHE B 53  ? 0.4319 0.4361 0.4255 -0.0330 0.0493  -0.1474 88  PHE B C   
2595 O O   . PHE B 53  ? 0.4465 0.4448 0.4091 -0.0265 0.0547  -0.1323 88  PHE B O   
2596 C CB  . PHE B 53  ? 0.3125 0.2941 0.3366 -0.0418 0.0760  -0.1375 88  PHE B CB  
2597 C CG  . PHE B 53  ? 0.3423 0.3206 0.4016 -0.0485 0.0848  -0.1377 88  PHE B CG  
2598 C CD1 . PHE B 53  ? 0.3937 0.3707 0.4919 -0.0558 0.0842  -0.1238 88  PHE B CD1 
2599 C CD2 . PHE B 53  ? 0.4045 0.3855 0.4563 -0.0453 0.0933  -0.1490 88  PHE B CD2 
2600 C CE1 . PHE B 53  ? 0.3208 0.3007 0.4494 -0.0586 0.0926  -0.1212 88  PHE B CE1 
2601 C CE2 . PHE B 53  ? 0.3613 0.3403 0.4473 -0.0519 0.1019  -0.1493 88  PHE B CE2 
2602 C CZ  . PHE B 53  ? 0.4114 0.3907 0.5375 -0.0591 0.1020  -0.1352 88  PHE B CZ  
2603 N N   . GLN B 54  ? 0.3526 0.3695 0.3551 -0.0323 0.0337  -0.1536 89  GLN B N   
2604 C CA  . GLN B 54  ? 0.2986 0.3226 0.2745 -0.0260 0.0227  -0.1501 89  GLN B CA  
2605 C C   . GLN B 54  ? 0.3190 0.3602 0.2841 -0.0189 0.0099  -0.1640 89  GLN B C   
2606 O O   . GLN B 54  ? 0.3385 0.3864 0.3265 -0.0212 0.0080  -0.1775 89  GLN B O   
2607 C CB  . GLN B 54  ? 0.3284 0.3493 0.3294 -0.0321 0.0157  -0.1389 89  GLN B CB  
2608 C CG  . GLN B 54  ? 0.3686 0.3733 0.3724 -0.0351 0.0244  -0.1153 89  GLN B CG  
2609 C CD  . GLN B 54  ? 0.4817 0.4853 0.5113 -0.0403 0.0182  -0.1049 89  GLN B CD  
2610 O OE1 . GLN B 54  ? 0.4258 0.4400 0.4674 -0.0404 0.0078  -0.1116 89  GLN B OE1 
2611 N NE2 . GLN B 54  ? 0.6778 0.6697 0.7159 -0.0437 0.0246  -0.0887 89  GLN B NE2 
2612 N N   . LYS B 55  ? 0.3951 0.4440 0.3270 -0.0101 0.0015  -0.1596 90  LYS B N   
2613 C CA  . LYS B 55  ? 0.4410 0.5059 0.3581 -0.0024 -0.0108 -0.1701 90  LYS B CA  
2614 C C   . LYS B 55  ? 0.3530 0.4255 0.2687 0.0002  -0.0247 -0.1635 90  LYS B C   
2615 O O   . LYS B 55  ? 0.4807 0.5465 0.3924 -0.0008 -0.0237 -0.1489 90  LYS B O   
2616 C CB  . LYS B 55  ? 0.5626 0.6313 0.4337 0.0090  -0.0055 -0.1688 90  LYS B CB  
2617 C CG  . LYS B 55  ? 0.6881 0.7719 0.5522 0.0143  -0.0137 -0.1865 90  LYS B CG  
2618 C CD  . LYS B 55  ? 0.8115 0.8937 0.6468 0.0208  -0.0014 -0.1897 90  LYS B CD  
2619 C CE  . LYS B 55  ? 0.8328 0.9313 0.6323 0.0326  -0.0093 -0.1939 90  LYS B CE  
2620 N NZ  . LYS B 55  ? 0.9741 1.0743 0.7524 0.0383  0.0008  -0.2033 90  LYS B NZ  
2621 N N   . ALA B 56  ? 0.4860 0.5736 0.4053 0.0039  -0.0373 -0.1751 91  ALA B N   
2622 C CA  . ALA B 56  ? 0.4650 0.5620 0.3978 0.0048  -0.0512 -0.1742 91  ALA B CA  
2623 C C   . ALA B 56  ? 0.5683 0.6634 0.4784 0.0096  -0.0546 -0.1558 91  ALA B C   
2624 O O   . ALA B 56  ? 0.8336 0.9237 0.7653 0.0044  -0.0566 -0.1480 91  ALA B O   
2625 C CB  . ALA B 56  ? 0.5224 0.6372 0.4532 0.0107  -0.0628 -0.1903 91  ALA B CB  
2626 N N   . PRO B 57  ? 0.5345 0.6343 0.4036 0.0200  -0.0548 -0.1468 92  PRO B N   
2627 C CA  . PRO B 57  ? 0.4870 0.5833 0.3407 0.0242  -0.0557 -0.1266 92  PRO B CA  
2628 C C   . PRO B 57  ? 0.3322 0.4123 0.1876 0.0191  -0.0423 -0.1170 92  PRO B C   
2629 O O   . PRO B 57  ? 0.5160 0.5900 0.3498 0.0224  -0.0297 -0.1119 92  PRO B O   
2630 C CB  . PRO B 57  ? 0.6983 0.8030 0.5119 0.0367  -0.0555 -0.1173 92  PRO B CB  
2631 C CG  . PRO B 57  ? 0.5090 0.6236 0.3164 0.0389  -0.0571 -0.1357 92  PRO B CG  
2632 C CD  . PRO B 57  ? 0.5947 0.7004 0.4304 0.0285  -0.0506 -0.1501 92  PRO B CD  
2633 N N   . LEU B 58  ? 0.3031 0.3769 0.1861 0.0112  -0.0440 -0.1145 93  LEU B N   
2634 C CA  . LEU B 58  ? 0.3259 0.3804 0.2258 0.0030  -0.0304 -0.1032 93  LEU B CA  
2635 C C   . LEU B 58  ? 0.3388 0.3827 0.2311 0.0057  -0.0269 -0.0794 93  LEU B C   
2636 O O   . LEU B 58  ? 0.3124 0.3598 0.2141 0.0062  -0.0354 -0.0745 93  LEU B O   
2637 C CB  . LEU B 58  ? 0.3634 0.4164 0.3063 -0.0080 -0.0326 -0.1125 93  LEU B CB  
2638 C CG  . LEU B 58  ? 0.4472 0.4838 0.4115 -0.0166 -0.0203 -0.1031 93  LEU B CG  
2639 C CD1 . LEU B 58  ? 0.5278 0.5570 0.4798 -0.0167 -0.0080 -0.1055 93  LEU B CD1 
2640 C CD2 . LEU B 58  ? 0.4102 0.4501 0.4171 -0.0253 -0.0230 -0.1119 93  LEU B CD2 
2641 N N   . GLU B 59  ? 0.2852 0.3164 0.1633 0.0078  -0.0139 -0.0654 94  GLU B N   
2642 C CA  . GLU B 59  ? 0.2709 0.2910 0.1472 0.0100  -0.0096 -0.0447 94  GLU B CA  
2643 C C   . GLU B 59  ? 0.3154 0.3260 0.2225 0.0004  -0.0096 -0.0429 94  GLU B C   
2644 O O   . GLU B 59  ? 0.3205 0.3232 0.2443 -0.0071 -0.0027 -0.0461 94  GLU B O   
2645 C CB  . GLU B 59  ? 0.3495 0.3584 0.2106 0.0140  0.0051  -0.0314 94  GLU B CB  
2646 C CG  . GLU B 59  ? 0.3736 0.3705 0.2388 0.0162  0.0102  -0.0116 94  GLU B CG  
2647 C CD  . GLU B 59  ? 0.5516 0.5381 0.4068 0.0210  0.0256  0.0028  94  GLU B CD  
2648 O OE1 . GLU B 59  ? 0.4821 0.4701 0.3260 0.0223  0.0334  -0.0022 94  GLU B OE1 
2649 O OE2 . GLU B 59  ? 0.3696 0.3469 0.2306 0.0240  0.0305  0.0190  94  GLU B OE2 
2650 N N   . THR B 60  ? 0.2586 0.2717 0.1734 0.0014  -0.0171 -0.0375 95  THR B N   
2651 C CA  . THR B 60  ? 0.2316 0.2406 0.1727 -0.0057 -0.0185 -0.0368 95  THR B CA  
2652 C C   . THR B 60  ? 0.2177 0.2166 0.1582 -0.0035 -0.0152 -0.0223 95  THR B C   
2653 O O   . THR B 60  ? 0.2406 0.2413 0.1685 0.0037  -0.0179 -0.0145 95  THR B O   
2654 C CB  . THR B 60  ? 0.2618 0.2845 0.2161 -0.0059 -0.0300 -0.0453 95  THR B CB  
2655 O OG1 . THR B 60  ? 0.2895 0.3224 0.2482 -0.0078 -0.0340 -0.0616 95  THR B OG1 
2656 C CG2 . THR B 60  ? 0.2274 0.2482 0.2083 -0.0116 -0.0298 -0.0425 95  THR B CG2 
2657 N N   . SER B 61  ? 0.2060 0.1954 0.1620 -0.0092 -0.0098 -0.0193 96  SER B N   
2658 C CA  . SER B 61  ? 0.2349 0.2157 0.1950 -0.0078 -0.0078 -0.0099 96  SER B CA  
2659 C C   . SER B 61  ? 0.2071 0.1952 0.1739 -0.0057 -0.0154 -0.0095 96  SER B C   
2660 O O   . SER B 61  ? 0.2233 0.2216 0.1999 -0.0078 -0.0208 -0.0158 96  SER B O   
2661 C CB  . SER B 61  ? 0.2269 0.1991 0.2021 -0.0141 -0.0023 -0.0096 96  SER B CB  
2662 O OG  . SER B 61  ? 0.2270 0.1906 0.1985 -0.0154 0.0061  -0.0079 96  SER B OG  
2663 N N   . VAL B 62  ? 0.2049 0.1877 0.1698 -0.0012 -0.0147 -0.0020 97  VAL B N   
2664 C CA  . VAL B 62  ? 0.1962 0.1836 0.1695 0.0009  -0.0194 -0.0013 97  VAL B CA  
2665 C C   . VAL B 62  ? 0.2088 0.1864 0.1899 0.0003  -0.0151 0.0011  97  VAL B C   
2666 O O   . VAL B 62  ? 0.2461 0.2139 0.2252 0.0030  -0.0108 0.0063  97  VAL B O   
2667 C CB  . VAL B 62  ? 0.1992 0.1914 0.1644 0.0082  -0.0239 0.0037  97  VAL B CB  
2668 C CG1 . VAL B 62  ? 0.2425 0.2385 0.2185 0.0106  -0.0271 0.0045  97  VAL B CG1 
2669 C CG2 . VAL B 62  ? 0.2501 0.2542 0.2071 0.0095  -0.0302 -0.0010 97  VAL B CG2 
2670 N N   . THR B 63  ? 0.1779 0.1593 0.1693 -0.0024 -0.0163 -0.0027 98  THR B N   
2671 C CA  . THR B 63  ? 0.1928 0.1676 0.1909 -0.0033 -0.0138 -0.0040 98  THR B CA  
2672 C C   . THR B 63  ? 0.2008 0.1830 0.2037 -0.0001 -0.0166 -0.0063 98  THR B C   
2673 O O   . THR B 63  ? 0.2517 0.2449 0.2569 0.0003  -0.0188 -0.0063 98  THR B O   
2674 C CB  . THR B 63  ? 0.2169 0.1905 0.2208 -0.0095 -0.0115 -0.0064 98  THR B CB  
2675 O OG1 . THR B 63  ? 0.2220 0.1895 0.2211 -0.0119 -0.0076 -0.0048 98  THR B OG1 
2676 C CG2 . THR B 63  ? 0.2256 0.1935 0.2371 -0.0101 -0.0107 -0.0090 98  THR B CG2 
2677 N N   . GLY B 64  ? 0.2024 0.1786 0.2088 0.0028  -0.0159 -0.0088 99  GLY B N   
2678 C CA  . GLY B 64  ? 0.2048 0.1881 0.2141 0.0064  -0.0177 -0.0136 99  GLY B CA  
2679 C C   . GLY B 64  ? 0.1833 0.1651 0.1971 0.0044  -0.0182 -0.0200 99  GLY B C   
2680 O O   . GLY B 64  ? 0.2083 0.1809 0.2265 0.0004  -0.0168 -0.0203 99  GLY B O   
2681 N N   . TYR B 65  ? 0.1869 0.1794 0.1996 0.0080  -0.0203 -0.0249 100 TYR B N   
2682 C CA  . TYR B 65  ? 0.2020 0.1980 0.2170 0.0071  -0.0228 -0.0314 100 TYR B CA  
2683 C C   . TYR B 65  ? 0.2206 0.2203 0.2358 0.0134  -0.0255 -0.0426 100 TYR B C   
2684 O O   . TYR B 65  ? 0.2133 0.2239 0.2217 0.0194  -0.0251 -0.0435 100 TYR B O   
2685 C CB  . TYR B 65  ? 0.2000 0.2097 0.2121 0.0058  -0.0228 -0.0259 100 TYR B CB  
2686 C CG  . TYR B 65  ? 0.1898 0.1945 0.2062 -0.0011 -0.0202 -0.0186 100 TYR B CG  
2687 C CD1 . TYR B 65  ? 0.2060 0.2037 0.2287 -0.0067 -0.0200 -0.0192 100 TYR B CD1 
2688 C CD2 . TYR B 65  ? 0.2114 0.2186 0.2276 -0.0018 -0.0181 -0.0126 100 TYR B CD2 
2689 C CE1 . TYR B 65  ? 0.2142 0.2073 0.2408 -0.0124 -0.0166 -0.0141 100 TYR B CE1 
2690 C CE2 . TYR B 65  ? 0.1786 0.1820 0.1988 -0.0076 -0.0162 -0.0092 100 TYR B CE2 
2691 C CZ  . TYR B 65  ? 0.1679 0.1642 0.1924 -0.0127 -0.0149 -0.0101 100 TYR B CZ  
2692 O OH  . TYR B 65  ? 0.2320 0.2249 0.2604 -0.0179 -0.0120 -0.0082 100 TYR B OH  
2693 N N   . LEU B 66  ? 0.2161 0.2072 0.2413 0.0123  -0.0279 -0.0520 101 LEU B N   
2694 C CA  . LEU B 66  ? 0.2044 0.1987 0.2338 0.0180  -0.0316 -0.0667 101 LEU B CA  
2695 C C   . LEU B 66  ? 0.2704 0.2784 0.2950 0.0195  -0.0378 -0.0749 101 LEU B C   
2696 O O   . LEU B 66  ? 0.2316 0.2376 0.2619 0.0142  -0.0400 -0.0730 101 LEU B O   
2697 C CB  . LEU B 66  ? 0.2643 0.2415 0.3142 0.0160  -0.0308 -0.0728 101 LEU B CB  
2698 C CG  . LEU B 66  ? 0.2579 0.2347 0.3201 0.0214  -0.0336 -0.0899 101 LEU B CG  
2699 C CD1 . LEU B 66  ? 0.1883 0.1656 0.2469 0.0268  -0.0292 -0.0871 101 LEU B CD1 
2700 C CD2 . LEU B 66  ? 0.2756 0.2359 0.3656 0.0179  -0.0326 -0.0946 101 LEU B CD2 
2701 N N   . VAL B 67  ? 0.2345 0.2580 0.2483 0.0275  -0.0404 -0.0835 102 VAL B N   
2702 C CA  . VAL B 67  ? 0.2366 0.2779 0.2415 0.0316  -0.0471 -0.0911 102 VAL B CA  
2703 C C   . VAL B 67  ? 0.2695 0.3145 0.2779 0.0381  -0.0529 -0.1135 102 VAL B C   
2704 O O   . VAL B 67  ? 0.2444 0.2940 0.2461 0.0451  -0.0500 -0.1192 102 VAL B O   
2705 C CB  . VAL B 67  ? 0.2475 0.3089 0.2331 0.0376  -0.0438 -0.0795 102 VAL B CB  
2706 C CG1 . VAL B 67  ? 0.2136 0.2957 0.1888 0.0430  -0.0505 -0.0841 102 VAL B CG1 
2707 C CG2 . VAL B 67  ? 0.2345 0.2913 0.2225 0.0313  -0.0373 -0.0595 102 VAL B CG2 
2708 N N   . ASN B 68  ? 0.2027 0.2460 0.2245 0.0359  -0.0606 -0.1262 103 ASN B N   
2709 C CA  . ASN B 68  ? 0.2486 0.2993 0.2776 0.0414  -0.0646 -0.1417 103 ASN B CA  
2710 C C   . ASN B 68  ? 0.2561 0.3299 0.2684 0.0475  -0.0710 -0.1442 103 ASN B C   
2711 O O   . ASN B 68  ? 0.2577 0.3331 0.2759 0.0437  -0.0762 -0.1424 103 ASN B O   
2712 C CB  . ASN B 68  ? 0.2807 0.3161 0.3413 0.0355  -0.0660 -0.1480 103 ASN B CB  
2713 C CG  . ASN B 68  ? 0.2561 0.2987 0.3294 0.0409  -0.0698 -0.1655 103 ASN B CG  
2714 O OD1 . ASN B 68  ? 0.2848 0.3463 0.3416 0.0491  -0.0740 -0.1748 103 ASN B OD1 
2715 N ND2 . ASN B 68  ? 0.2613 0.2904 0.3647 0.0369  -0.0677 -0.1693 103 ASN B ND2 
2716 N N   . THR B 69  ? 0.2582 0.3385 0.2014 0.0427  -0.0702 -0.1250 104 THR B N   
2717 C CA  . THR B 69  ? 0.2842 0.3788 0.1994 0.0477  -0.0787 -0.1227 104 THR B CA  
2718 C C   . THR B 69  ? 0.3311 0.4414 0.2495 0.0386  -0.0881 -0.1334 104 THR B C   
2719 O O   . THR B 69  ? 0.3558 0.4803 0.2544 0.0418  -0.0961 -0.1298 104 THR B O   
2720 C CB  . THR B 69  ? 0.3634 0.4472 0.2488 0.0480  -0.0679 -0.1195 104 THR B CB  
2721 O OG1 . THR B 69  ? 0.3482 0.4296 0.2365 0.0418  -0.0606 -0.1340 104 THR B OG1 
2722 C CG2 . THR B 69  ? 0.3146 0.3803 0.2004 0.0486  -0.0560 -0.1059 104 THR B CG2 
2723 N N   . GLY B 70  ? 0.3163 0.4189 0.2542 0.0257  -0.0883 -0.1452 105 GLY B N   
2724 C CA  . GLY B 70  ? 0.3287 0.4335 0.2617 0.0121  -0.0974 -0.1566 105 GLY B CA  
2725 C C   . GLY B 70  ? 0.4542 0.5296 0.3649 0.0108  -0.0902 -0.1693 105 GLY B C   
2726 O O   . GLY B 70  ? 0.4390 0.4962 0.3438 -0.0019 -0.0964 -0.1814 105 GLY B O   
2727 N N   . SER B 71  ? 0.3779 0.4488 0.2738 0.0234  -0.0776 -0.1665 106 SER B N   
2728 C CA  . SER B 71  ? 0.3825 0.4348 0.2616 0.0277  -0.0683 -0.1781 106 SER B CA  
2729 C C   . SER B 71  ? 0.3616 0.4025 0.2535 0.0369  -0.0540 -0.1752 106 SER B C   
2730 O O   . SER B 71  ? 0.4539 0.4795 0.3381 0.0437  -0.0476 -0.1856 106 SER B O   
2731 C CB  . SER B 71  ? 0.5235 0.5924 0.3717 0.0331  -0.0654 -0.1787 106 SER B CB  
2732 O OG  . SER B 71  ? 0.5879 0.6736 0.4310 0.0386  -0.0575 -0.1630 106 SER B OG  
2733 N N   . LYS B 72  ? 0.3245 0.3730 0.2339 0.0387  -0.0499 -0.1619 107 LYS B N   
2734 C CA  . LYS B 72  ? 0.3670 0.4086 0.2906 0.0451  -0.0383 -0.1577 107 LYS B CA  
2735 C C   . LYS B 72  ? 0.3666 0.4010 0.3139 0.0410  -0.0410 -0.1480 107 LYS B C   
2736 O O   . LYS B 72  ? 0.2949 0.3394 0.2448 0.0376  -0.0488 -0.1421 107 LYS B O   
2737 C CB  . LYS B 72  ? 0.3512 0.4156 0.2618 0.0504  -0.0267 -0.1509 107 LYS B CB  
2738 C CG  . LYS B 72  ? 0.4200 0.4982 0.3102 0.0564  -0.0201 -0.1608 107 LYS B CG  
2739 C CD  . LYS B 72  ? 0.4429 0.5199 0.3444 0.0684  -0.0112 -0.1686 107 LYS B CD  
2740 C CE  . LYS B 72  ? 0.6460 0.7247 0.5277 0.0784  -0.0089 -0.1844 107 LYS B CE  
2741 N NZ  . LYS B 72  ? 0.6947 0.8019 0.5512 0.0744  -0.0052 -0.1827 107 LYS B NZ  
2742 N N   . LEU B 73  ? 0.2998 0.3187 0.2628 0.0437  -0.0353 -0.1463 108 LEU B N   
2743 C CA  . LEU B 73  ? 0.3118 0.3238 0.2954 0.0405  -0.0353 -0.1362 108 LEU B CA  
2744 C C   . LEU B 73  ? 0.2579 0.2767 0.2447 0.0469  -0.0248 -0.1278 108 LEU B C   
2745 O O   . LEU B 73  ? 0.2861 0.3041 0.2750 0.0538  -0.0188 -0.1305 108 LEU B O   
2746 C CB  . LEU B 73  ? 0.3256 0.3113 0.3201 0.0346  -0.0393 -0.1388 108 LEU B CB  
2747 C CG  . LEU B 73  ? 0.3171 0.2982 0.3315 0.0289  -0.0398 -0.1287 108 LEU B CG  
2748 C CD1 . LEU B 73  ? 0.2924 0.2956 0.3147 0.0224  -0.0476 -0.1287 108 LEU B CD1 
2749 C CD2 . LEU B 73  ? 0.3470 0.2969 0.3640 0.0213  -0.0428 -0.1295 108 LEU B CD2 
2750 N N   . VAL B 74  ? 0.2539 0.2793 0.2383 0.0453  -0.0239 -0.1188 109 VAL B N   
2751 C CA  . VAL B 74  ? 0.2760 0.3089 0.2576 0.0447  -0.0151 -0.1086 109 VAL B CA  
2752 C C   . VAL B 74  ? 0.2367 0.2543 0.2316 0.0417  -0.0159 -0.0960 109 VAL B C   
2753 O O   . VAL B 74  ? 0.2505 0.2593 0.2464 0.0412  -0.0217 -0.0904 109 VAL B O   
2754 C CB  . VAL B 74  ? 0.2828 0.3256 0.2380 0.0386  -0.0139 -0.0985 109 VAL B CB  
2755 C CG1 . VAL B 74  ? 0.2932 0.3415 0.2432 0.0290  -0.0063 -0.0849 109 VAL B CG1 
2756 C CG2 . VAL B 74  ? 0.3077 0.3699 0.2459 0.0415  -0.0124 -0.1112 109 VAL B CG2 
2757 N N   . LEU B 75  ? 0.2230 0.2427 0.2276 0.0414  -0.0103 -0.0922 110 LEU B N   
2758 C CA  . LEU B 75  ? 0.2152 0.2206 0.2274 0.0382  -0.0110 -0.0811 110 LEU B CA  
2759 C C   . LEU B 75  ? 0.2531 0.2623 0.2512 0.0284  -0.0076 -0.0695 110 LEU B C   
2760 O O   . LEU B 75  ? 0.2281 0.2618 0.2279 0.0245  -0.0023 -0.0705 110 LEU B O   
2761 C CB  . LEU B 75  ? 0.2099 0.2104 0.2414 0.0436  -0.0106 -0.0850 110 LEU B CB  
2762 C CG  . LEU B 75  ? 0.2327 0.2219 0.2701 0.0405  -0.0108 -0.0741 110 LEU B CG  
2763 C CD1 . LEU B 75  ? 0.2305 0.2069 0.2637 0.0383  -0.0135 -0.0681 110 LEU B CD1 
2764 C CD2 . LEU B 75  ? 0.3281 0.3108 0.3773 0.0448  -0.0118 -0.0733 110 LEU B CD2 
2765 N N   . VAL B 76  ? 0.2399 0.2258 0.2215 0.0241  -0.0113 -0.0592 111 VAL B N   
2766 C CA  . VAL B 76  ? 0.2346 0.2083 0.1943 0.0101  -0.0113 -0.0476 111 VAL B CA  
2767 C C   . VAL B 76  ? 0.2305 0.1921 0.1979 0.0089  -0.0124 -0.0444 111 VAL B C   
2768 O O   . VAL B 76  ? 0.2714 0.2105 0.2355 0.0178  -0.0155 -0.0436 111 VAL B O   
2769 C CB  . VAL B 76  ? 0.2594 0.2011 0.1840 0.0089  -0.0172 -0.0393 111 VAL B CB  
2770 C CG1 . VAL B 76  ? 0.3052 0.2189 0.1981 -0.0103 -0.0196 -0.0268 111 VAL B CG1 
2771 C CG2 . VAL B 76  ? 0.2864 0.2437 0.2015 0.0099  -0.0169 -0.0417 111 VAL B CG2 
2772 N N   . ASP B 77  ? 0.1962 0.1802 0.1743 -0.0007 -0.0097 -0.0430 112 ASP B N   
2773 C CA  . ASP B 77  ? 0.2363 0.2172 0.2216 -0.0035 -0.0118 -0.0400 112 ASP B CA  
2774 C C   . ASP B 77  ? 0.2059 0.1892 0.2156 0.0131  -0.0113 -0.0457 112 ASP B C   
2775 O O   . ASP B 77  ? 0.2443 0.2210 0.2605 0.0235  -0.0108 -0.0511 112 ASP B O   
2776 C CB  . ASP B 77  ? 0.2367 0.1764 0.1908 -0.0127 -0.0174 -0.0326 112 ASP B CB  
2777 C CG  . ASP B 77  ? 0.3886 0.3194 0.3137 -0.0374 -0.0201 -0.0242 112 ASP B CG  
2778 O OD1 . ASP B 77  ? 0.2960 0.2687 0.2329 -0.0502 -0.0159 -0.0228 112 ASP B OD1 
2779 O OD2 . ASP B 77  ? 0.3655 0.2474 0.2535 -0.0447 -0.0267 -0.0189 112 ASP B OD2 
2780 N N   . THR B 78  ? 0.1892 0.1825 0.2103 0.0134  -0.0128 -0.0436 113 THR B N   
2781 C CA  . THR B 78  ? 0.2349 0.2290 0.2753 0.0277  -0.0132 -0.0470 113 THR B CA  
2782 C C   . THR B 78  ? 0.2209 0.2001 0.2582 0.0273  -0.0164 -0.0402 113 THR B C   
2783 O O   . THR B 78  ? 0.2238 0.1992 0.2718 0.0364  -0.0179 -0.0395 113 THR B O   
2784 C CB  . THR B 78  ? 0.1790 0.2039 0.2372 0.0378  -0.0127 -0.0524 113 THR B CB  
2785 O OG1 . THR B 78  ? 0.2032 0.2551 0.2657 0.0322  -0.0153 -0.0465 113 THR B OG1 
2786 C CG2 . THR B 78  ? 0.1854 0.2315 0.2435 0.0388  -0.0079 -0.0602 113 THR B CG2 
2787 N N   . GLY B 79  ? 0.2088 0.1745 0.2263 0.0172  -0.0183 -0.0353 114 GLY B N   
2788 C CA  . GLY B 79  ? 0.2379 0.1928 0.2477 0.0168  -0.0213 -0.0302 114 GLY B CA  
2789 C C   . GLY B 79  ? 0.2630 0.2422 0.2812 0.0133  -0.0268 -0.0266 114 GLY B C   
2790 O O   . GLY B 79  ? 0.2046 0.2150 0.2345 0.0094  -0.0277 -0.0280 114 GLY B O   
2791 N N   . ALA B 80  ? 0.2421 0.2137 0.2546 0.0157  -0.0304 -0.0214 115 ALA B N   
2792 C CA  . ALA B 80  ? 0.2395 0.2343 0.2545 0.0119  -0.0386 -0.0168 115 ALA B CA  
2793 C C   . ALA B 80  ? 0.2371 0.2451 0.2705 0.0298  -0.0420 -0.0129 115 ALA B C   
2794 O O   . ALA B 80  ? 0.2360 0.2726 0.2759 0.0320  -0.0501 -0.0091 115 ALA B O   
2795 C CB  . ALA B 80  ? 0.2506 0.2246 0.2371 0.0019  -0.0432 -0.0136 115 ALA B CB  
2796 N N   . ALA B 81  ? 0.2268 0.2130 0.2660 0.0421  -0.0378 -0.0134 116 ALA B N   
2797 C CA  . ALA B 81  ? 0.2346 0.2111 0.2779 0.0578  -0.0433 -0.0072 116 ALA B CA  
2798 C C   . ALA B 81  ? 0.2839 0.2584 0.3113 0.0539  -0.0498 0.0035  116 ALA B C   
2799 O O   . ALA B 81  ? 0.2850 0.2440 0.2942 0.0419  -0.0457 0.0058  116 ALA B O   
2800 C CB  . ALA B 81  ? 0.2938 0.2938 0.3554 0.0770  -0.0475 -0.0126 116 ALA B CB  
2801 N N   . GLY B 82  ? 0.2690 0.2622 0.3005 0.0658  -0.0603 0.0092  117 GLY B N   
2802 C CA  . GLY B 82  ? 0.2997 0.2955 0.3140 0.0618  -0.0686 0.0193  117 GLY B CA  
2803 C C   . GLY B 82  ? 0.3359 0.3713 0.3499 0.0489  -0.0758 0.0168  117 GLY B C   
2804 O O   . GLY B 82  ? 0.4129 0.4582 0.4140 0.0477  -0.0862 0.0244  117 GLY B O   
2805 N N   . LEU B 83  ? 0.2590 0.3159 0.2830 0.0356  -0.0717 0.0076  118 LEU B N   
2806 C CA  . LEU B 83  ? 0.2461 0.3438 0.2702 0.0172  -0.0804 0.0066  118 LEU B CA  
2807 C C   . LEU B 83  ? 0.3477 0.4176 0.3363 -0.0052 -0.0842 0.0066  118 LEU B C   
2808 O O   . LEU B 83  ? 0.4407 0.5366 0.4209 -0.0204 -0.0964 0.0084  118 LEU B O   
2809 C CB  . LEU B 83  ? 0.2307 0.3578 0.2714 0.0055  -0.0746 -0.0008 118 LEU B CB  
2810 C CG  . LEU B 83  ? 0.2818 0.4489 0.3554 0.0282  -0.0711 -0.0043 118 LEU B CG  
2811 C CD1 . LEU B 83  ? 0.2497 0.4561 0.3347 0.0100  -0.0651 -0.0097 118 LEU B CD1 
2812 C CD2 . LEU B 83  ? 0.2860 0.4981 0.3772 0.0503  -0.0826 0.0007  118 LEU B CD2 
2813 N N   . PHE B 84  ? 0.3339 0.3545 0.2999 -0.0066 -0.0748 0.0035  119 PHE B N   
2814 C CA  . PHE B 84  ? 0.4017 0.3892 0.3281 -0.0217 -0.0771 -0.0003 119 PHE B CA  
2815 C C   . PHE B 84  ? 0.4628 0.4246 0.3685 -0.0095 -0.0732 0.0040  119 PHE B C   
2816 O O   . PHE B 84  ? 0.6339 0.5624 0.5111 -0.0102 -0.0666 -0.0019 119 PHE B O   
2817 C CB  . PHE B 84  ? 0.3554 0.3099 0.2648 -0.0322 -0.0702 -0.0093 119 PHE B CB  
2818 C CG  . PHE B 84  ? 0.4491 0.4137 0.3514 -0.0586 -0.0784 -0.0122 119 PHE B CG  
2819 C CD1 . PHE B 84  ? 0.5457 0.5478 0.4505 -0.0764 -0.0920 -0.0088 119 PHE B CD1 
2820 C CD2 . PHE B 84  ? 0.5236 0.4616 0.4144 -0.0682 -0.0735 -0.0168 119 PHE B CD2 
2821 C CE1 . PHE B 84  ? 0.5625 0.5789 0.4601 -0.1083 -0.0997 -0.0097 119 PHE B CE1 
2822 C CE2 . PHE B 84  ? 0.6059 0.5489 0.4847 -0.0985 -0.0812 -0.0165 119 PHE B CE2 
2823 C CZ  . PHE B 84  ? 0.4780 0.4618 0.3609 -0.1212 -0.0938 -0.0129 119 PHE B CZ  
2824 N N   . GLY B 85  ? 0.4093 0.3866 0.3259 0.0033  -0.0773 0.0147  120 GLY B N   
2825 C CA  . GLY B 85  ? 0.4196 0.3773 0.3119 0.0096  -0.0746 0.0221  120 GLY B CA  
2826 C C   . GLY B 85  ? 0.6472 0.5862 0.5471 0.0194  -0.0602 0.0264  120 GLY B C   
2827 O O   . GLY B 85  ? 0.3959 0.3326 0.3182 0.0221  -0.0526 0.0215  120 GLY B O   
2828 N N   . PRO B 86  ? 0.4210 0.3494 0.2996 0.0216  -0.0565 0.0361  121 PRO B N   
2829 C CA  . PRO B 86  ? 0.4507 0.3681 0.3374 0.0248  -0.0452 0.0449  121 PRO B CA  
2830 C C   . PRO B 86  ? 0.4130 0.3285 0.3007 0.0227  -0.0295 0.0357  121 PRO B C   
2831 O O   . PRO B 86  ? 0.4390 0.3536 0.3390 0.0208  -0.0208 0.0420  121 PRO B O   
2832 C CB  . PRO B 86  ? 0.5494 0.4619 0.4081 0.0236  -0.0472 0.0609  121 PRO B CB  
2833 C CG  . PRO B 86  ? 0.5329 0.4521 0.3617 0.0205  -0.0523 0.0532  121 PRO B CG  
2834 C CD  . PRO B 86  ? 0.6344 0.5629 0.4778 0.0181  -0.0631 0.0404  121 PRO B CD  
2835 N N   . THR B 87  ? 0.3678 0.2813 0.2408 0.0231  -0.0271 0.0213  122 THR B N   
2836 C CA  . THR B 87  ? 0.3351 0.2492 0.2083 0.0281  -0.0137 0.0125  122 THR B CA  
2837 C C   . THR B 87  ? 0.4101 0.3238 0.3116 0.0293  -0.0129 0.0053  122 THR B C   
2838 O O   . THR B 87  ? 0.3514 0.2704 0.2578 0.0352  -0.0035 -0.0006 122 THR B O   
2839 C CB  . THR B 87  ? 0.3921 0.2938 0.2276 0.0343  -0.0119 -0.0004 122 THR B CB  
2840 O OG1 . THR B 87  ? 0.4488 0.3296 0.2762 0.0297  -0.0227 -0.0111 122 THR B OG1 
2841 C CG2 . THR B 87  ? 0.5036 0.4058 0.3057 0.0328  -0.0142 0.0047  122 THR B CG2 
2842 N N   . LEU B 88  ? 0.3371 0.2506 0.2566 0.0254  -0.0224 0.0055  123 LEU B N   
2843 C CA  . LEU B 88  ? 0.2990 0.2148 0.2423 0.0260  -0.0215 -0.0009 123 LEU B CA  
2844 C C   . LEU B 88  ? 0.3195 0.2411 0.2894 0.0278  -0.0231 0.0057  123 LEU B C   
2845 O O   . LEU B 88  ? 0.3806 0.2979 0.3483 0.0283  -0.0253 0.0167  123 LEU B O   
2846 C CB  . LEU B 88  ? 0.2831 0.1966 0.2206 0.0194  -0.0296 -0.0081 123 LEU B CB  
2847 C CG  . LEU B 88  ? 0.3132 0.2028 0.2150 0.0165  -0.0304 -0.0163 123 LEU B CG  
2848 C CD1 . LEU B 88  ? 0.3729 0.2558 0.2649 0.0011  -0.0404 -0.0204 123 LEU B CD1 
2849 C CD2 . LEU B 88  ? 0.3157 0.1940 0.2129 0.0281  -0.0209 -0.0227 123 LEU B CD2 
2850 N N   . GLY B 89  ? 0.2701 0.1956 0.2595 0.0295  -0.0229 -0.0012 124 GLY B N   
2851 C CA  . GLY B 89  ? 0.2589 0.1820 0.2674 0.0343  -0.0252 0.0009  124 GLY B CA  
2852 C C   . GLY B 89  ? 0.2794 0.1925 0.2937 0.0303  -0.0192 0.0023  124 GLY B C   
2853 O O   . GLY B 89  ? 0.3208 0.2178 0.3405 0.0313  -0.0230 0.0060  124 GLY B O   
2854 N N   . ARG B 90  ? 0.2446 0.1668 0.2562 0.0260  -0.0112 -0.0008 125 ARG B N   
2855 C CA  . ARG B 90  ? 0.2508 0.1778 0.2717 0.0184  -0.0059 0.0008  125 ARG B CA  
2856 C C   . ARG B 90  ? 0.2254 0.1549 0.2621 0.0189  -0.0072 -0.0096 125 ARG B C   
2857 O O   . ARG B 90  ? 0.2745 0.2091 0.3200 0.0092  -0.0055 -0.0092 125 ARG B O   
2858 C CB  . ARG B 90  ? 0.2632 0.2130 0.2770 0.0180  0.0035  0.0015  125 ARG B CB  
2859 C CG  . ARG B 90  ? 0.4164 0.3669 0.4082 0.0198  0.0064  0.0086  125 ARG B CG  
2860 C CD  . ARG B 90  ? 0.5446 0.4936 0.5324 0.0064  0.0081  0.0242  125 ARG B CD  
2861 N NE  . ARG B 90  ? 0.7684 0.7218 0.7316 0.0080  0.0115  0.0314  125 ARG B NE  
2862 C CZ  . ARG B 90  ? 0.5491 0.4846 0.4957 0.0123  0.0033  0.0346  125 ARG B CZ  
2863 N NH1 . ARG B 90  ? 0.4566 0.3750 0.4116 0.0169  -0.0081 0.0318  125 ARG B NH1 
2864 N NH2 . ARG B 90  ? 0.6907 0.6319 0.6112 0.0127  0.0064  0.0404  125 ARG B NH2 
2865 N N   . LEU B 91  ? 0.2586 0.1952 0.2786 0.0107  -0.0128 -0.0121 126 LEU B N   
2866 C CA  . LEU B 91  ? 0.2770 0.2192 0.3074 0.0161  -0.0153 -0.0227 126 LEU B CA  
2867 C C   . LEU B 91  ? 0.2501 0.1850 0.2957 0.0199  -0.0223 -0.0273 126 LEU B C   
2868 O O   . LEU B 91  ? 0.2543 0.1903 0.3109 0.0199  -0.0235 -0.0343 126 LEU B O   
2869 C CB  . LEU B 91  ? 0.2069 0.1606 0.2289 0.0214  -0.0166 -0.0276 126 LEU B CB  
2870 C CG  . LEU B 91  ? 0.2587 0.2201 0.2870 0.0259  -0.0194 -0.0371 126 LEU B CG  
2871 C CD1 . LEU B 91  ? 0.2209 0.1929 0.2393 0.0263  -0.0167 -0.0377 126 LEU B CD1 
2872 C CD2 . LEU B 91  ? 0.2392 0.2013 0.2731 0.0329  -0.0262 -0.0443 126 LEU B CD2 
2873 N N   . LEU B 92  ? 0.2437 0.1711 0.2916 0.0234  -0.0278 -0.0241 127 LEU B N   
2874 C CA  . LEU B 92  ? 0.2554 0.1738 0.3202 0.0274  -0.0344 -0.0302 127 LEU B CA  
2875 C C   . LEU B 92  ? 0.2450 0.1525 0.3218 0.0199  -0.0331 -0.0269 127 LEU B C   
2876 O O   . LEU B 92  ? 0.2906 0.1957 0.3813 0.0206  -0.0364 -0.0362 127 LEU B O   
2877 C CB  . LEU B 92  ? 0.2712 0.1821 0.3398 0.0330  -0.0406 -0.0262 127 LEU B CB  
2878 C CG  . LEU B 92  ? 0.6641 0.5838 0.7355 0.0434  -0.0446 -0.0369 127 LEU B CG  
2879 C CD1 . LEU B 92  ? 0.4070 0.3265 0.4904 0.0473  -0.0472 -0.0525 127 LEU B CD1 
2880 C CD2 . LEU B 92  ? 0.5718 0.5089 0.6271 0.0440  -0.0402 -0.0379 127 LEU B CD2 
2881 N N   . ALA B 93  ? 0.2547 0.1568 0.3257 0.0118  -0.0280 -0.0140 128 ALA B N   
2882 C CA  . ALA B 93  ? 0.3499 0.2436 0.4327 0.0031  -0.0250 -0.0095 128 ALA B CA  
2883 C C   . ALA B 93  ? 0.2486 0.1526 0.3385 0.0004  -0.0204 -0.0179 128 ALA B C   
2884 O O   . ALA B 93  ? 0.2842 0.1842 0.3917 -0.0033 -0.0217 -0.0212 128 ALA B O   
2885 C CB  . ALA B 93  ? 0.3132 0.2024 0.3844 -0.0060 -0.0187 0.0062  128 ALA B CB  
2886 N N   . ASN B 94  ? 0.2349 0.1520 0.3134 0.0021  -0.0155 -0.0208 129 ASN B N   
2887 C CA  . ASN B 94  ? 0.2381 0.1653 0.3256 0.0006  -0.0125 -0.0276 129 ASN B CA  
2888 C C   . ASN B 94  ? 0.3191 0.2506 0.4154 0.0070  -0.0214 -0.0395 129 ASN B C   
2889 O O   . ASN B 94  ? 0.2474 0.1834 0.3580 0.0047  -0.0228 -0.0447 129 ASN B O   
2890 C CB  . ASN B 94  ? 0.2012 0.1387 0.2762 0.0001  -0.0047 -0.0262 129 ASN B CB  
2891 C CG  . ASN B 94  ? 0.2554 0.1909 0.3246 -0.0084 0.0059  -0.0175 129 ASN B CG  
2892 O OD1 . ASN B 94  ? 0.2812 0.2125 0.3615 -0.0154 0.0097  -0.0137 129 ASN B OD1 
2893 N ND2 . ASN B 94  ? 0.2197 0.1586 0.2707 -0.0089 0.0110  -0.0148 129 ASN B ND2 
2894 N N   . LEU B 95  ? 0.2812 0.2128 0.3695 0.0144  -0.0273 -0.0444 130 LEU B N   
2895 C CA  . LEU B 95  ? 0.2460 0.1811 0.3407 0.0195  -0.0353 -0.0570 130 LEU B CA  
2896 C C   . LEU B 95  ? 0.2295 0.1536 0.3433 0.0162  -0.0401 -0.0611 130 LEU B C   
2897 O O   . LEU B 95  ? 0.2617 0.1903 0.3859 0.0151  -0.0449 -0.0701 130 LEU B O   
2898 C CB  . LEU B 95  ? 0.2329 0.1697 0.3176 0.0276  -0.0387 -0.0618 130 LEU B CB  
2899 C CG  . LEU B 95  ? 0.2859 0.2266 0.3749 0.0329  -0.0458 -0.0768 130 LEU B CG  
2900 C CD1 . LEU B 95  ? 0.4410 0.3977 0.5210 0.0334  -0.0466 -0.0817 130 LEU B CD1 
2901 C CD2 . LEU B 95  ? 0.4528 0.3919 0.5388 0.0406  -0.0479 -0.0819 130 LEU B CD2 
2902 N N   . LYS B 96  ? 0.2601 0.1694 0.3793 0.0141  -0.0399 -0.0540 131 LYS B N   
2903 C CA  . LYS B 96  ? 0.2702 0.1662 0.4094 0.0098  -0.0444 -0.0565 131 LYS B CA  
2904 C C   . LYS B 96  ? 0.2810 0.1802 0.4330 0.0001  -0.0404 -0.0531 131 LYS B C   
2905 O O   . LYS B 96  ? 0.2911 0.1888 0.4605 -0.0029 -0.0457 -0.0614 131 LYS B O   
2906 C CB  . LYS B 96  ? 0.3131 0.1916 0.4553 0.0093  -0.0454 -0.0465 131 LYS B CB  
2907 C CG  . LYS B 96  ? 0.3694 0.2458 0.5057 0.0200  -0.0505 -0.0516 131 LYS B CG  
2908 C CD  . LYS B 96  ? 0.4118 0.2720 0.5513 0.0204  -0.0527 -0.0389 131 LYS B CD  
2909 C CE  . LYS B 96  ? 0.6663 0.5290 0.8018 0.0319  -0.0570 -0.0439 131 LYS B CE  
2910 N NZ  . LYS B 96  ? 0.6399 0.4875 0.7810 0.0335  -0.0613 -0.0307 131 LYS B NZ  
2911 N N   . ALA B 97  ? 0.2620 0.1668 0.4067 -0.0050 -0.0308 -0.0422 132 ALA B N   
2912 C CA  . ALA B 97  ? 0.2467 0.1576 0.4060 -0.0135 -0.0253 -0.0399 132 ALA B CA  
2913 C C   . ALA B 97  ? 0.2649 0.1906 0.4323 -0.0108 -0.0297 -0.0510 132 ALA B C   
2914 O O   . ALA B 97  ? 0.2442 0.1740 0.4323 -0.0165 -0.0310 -0.0539 132 ALA B O   
2915 C CB  . ALA B 97  ? 0.3335 0.2493 0.4820 -0.0186 -0.0128 -0.0286 132 ALA B CB  
2916 N N   . ALA B 98  ? 0.2320 0.1666 0.3843 -0.0027 -0.0328 -0.0564 133 ALA B N   
2917 C CA  . ALA B 98  ? 0.2562 0.2045 0.4125 0.0003  -0.0390 -0.0651 133 ALA B CA  
2918 C C   . ALA B 98  ? 0.2494 0.1957 0.4144 0.0015  -0.0507 -0.0776 133 ALA B C   
2919 O O   . ALA B 98  ? 0.2456 0.2038 0.4117 0.0033  -0.0578 -0.0851 133 ALA B O   
2920 C CB  . ALA B 98  ? 0.2266 0.1840 0.3623 0.0072  -0.0381 -0.0648 133 ALA B CB  
2921 N N   . GLY B 99  ? 0.2354 0.1666 0.4063 0.0004  -0.0534 -0.0802 134 GLY B N   
2922 C CA  . GLY B 99  ? 0.2811 0.2083 0.4637 0.0001  -0.0638 -0.0938 134 GLY B CA  
2923 C C   . GLY B 99  ? 0.3274 0.2532 0.4961 0.0086  -0.0694 -0.1055 134 GLY B C   
2924 O O   . GLY B 99  ? 0.3144 0.2435 0.4866 0.0091  -0.0762 -0.1163 134 GLY B O   
2925 N N   . TYR B 100 ? 0.2624 0.1887 0.4131 0.0151  -0.0647 -0.1011 135 TYR B N   
2926 C CA  . TYR B 100 ? 0.2870 0.2156 0.4257 0.0233  -0.0679 -0.1117 135 TYR B CA  
2927 C C   . TYR B 100 ? 0.3081 0.2237 0.4473 0.0270  -0.0647 -0.1058 135 TYR B C   
2928 O O   . TYR B 100 ? 0.4263 0.3309 0.5691 0.0242  -0.0605 -0.0931 135 TYR B O   
2929 C CB  . TYR B 100 ? 0.2786 0.2238 0.3960 0.0282  -0.0657 -0.1116 135 TYR B CB  
2930 C CG  . TYR B 100 ? 0.2642 0.2246 0.3785 0.0256  -0.0705 -0.1159 135 TYR B CG  
2931 C CD1 . TYR B 100 ? 0.2995 0.2669 0.4105 0.0268  -0.0788 -0.1315 135 TYR B CD1 
2932 C CD2 . TYR B 100 ? 0.2641 0.2324 0.3791 0.0220  -0.0674 -0.1047 135 TYR B CD2 
2933 C CE1 . TYR B 100 ? 0.3587 0.3408 0.4655 0.0240  -0.0852 -0.1339 135 TYR B CE1 
2934 C CE2 . TYR B 100 ? 0.3002 0.2825 0.4150 0.0204  -0.0736 -0.1070 135 TYR B CE2 
2935 C CZ  . TYR B 100 ? 0.2679 0.2572 0.3777 0.0211  -0.0831 -0.1206 135 TYR B CZ  
2936 O OH  . TYR B 100 ? 0.3023 0.3062 0.4105 0.0190  -0.0911 -0.1213 135 TYR B OH  
2937 N N   . GLN B 101 ? 0.3011 0.2189 0.4374 0.0332  -0.0671 -0.1153 136 GLN B N   
2938 C CA  . GLN B 101 ? 0.3121 0.2208 0.4502 0.0385  -0.0655 -0.1113 136 GLN B CA  
2939 C C   . GLN B 101 ? 0.3208 0.2422 0.4429 0.0465  -0.0627 -0.1148 136 GLN B C   
2940 O O   . GLN B 101 ? 0.3044 0.2413 0.4152 0.0483  -0.0630 -0.1247 136 GLN B O   
2941 C CB  . GLN B 101 ? 0.3428 0.2443 0.4945 0.0399  -0.0696 -0.1204 136 GLN B CB  
2942 C CG  . GLN B 101 ? 0.3706 0.2570 0.5405 0.0320  -0.0721 -0.1148 136 GLN B CG  
2943 C CD  . GLN B 101 ? 0.4850 0.3584 0.6582 0.0275  -0.0688 -0.0961 136 GLN B CD  
2944 O OE1 . GLN B 101 ? 0.4812 0.3483 0.6508 0.0319  -0.0674 -0.0878 136 GLN B OE1 
2945 N NE2 . GLN B 101 ? 0.5324 0.4026 0.7129 0.0182  -0.0674 -0.0892 136 GLN B NE2 
2946 N N   . PRO B 102 ? 0.3326 0.2488 0.4535 0.0508  -0.0603 -0.1063 137 PRO B N   
2947 C CA  . PRO B 102 ? 0.2456 0.1759 0.3538 0.0579  -0.0573 -0.1093 137 PRO B CA  
2948 C C   . PRO B 102 ? 0.2629 0.2048 0.3705 0.0628  -0.0578 -0.1246 137 PRO B C   
2949 O O   . PRO B 102 ? 0.3659 0.3249 0.4598 0.0658  -0.0548 -0.1302 137 PRO B O   
2950 C CB  . PRO B 102 ? 0.3724 0.2926 0.4861 0.0615  -0.0572 -0.0976 137 PRO B CB  
2951 C CG  . PRO B 102 ? 0.4981 0.4005 0.6193 0.0544  -0.0585 -0.0849 137 PRO B CG  
2952 C CD  . PRO B 102 ? 0.3568 0.2552 0.4879 0.0488  -0.0608 -0.0922 137 PRO B CD  
2953 N N   . GLU B 103 ? 0.2746 0.2077 0.3969 0.0631  -0.0611 -0.1315 138 GLU B N   
2954 C CA  . GLU B 103 ? 0.2997 0.2425 0.4228 0.0674  -0.0610 -0.1475 138 GLU B CA  
2955 C C   . GLU B 103 ? 0.3647 0.3232 0.4731 0.0645  -0.0610 -0.1578 138 GLU B C   
2956 O O   . GLU B 103 ? 0.3306 0.3027 0.4323 0.0678  -0.0588 -0.1700 138 GLU B O   
2957 C CB  . GLU B 103 ? 0.3388 0.2663 0.4818 0.0671  -0.0652 -0.1528 138 GLU B CB  
2958 C CG  . GLU B 103 ? 0.4454 0.3585 0.6039 0.0714  -0.0662 -0.1441 138 GLU B CG  
2959 C CD  . GLU B 103 ? 0.7185 0.6170 0.8793 0.0666  -0.0675 -0.1248 138 GLU B CD  
2960 O OE1 . GLU B 103 ? 0.4283 0.3250 0.5839 0.0592  -0.0675 -0.1199 138 GLU B OE1 
2961 O OE2 . GLU B 103 ? 0.7123 0.6020 0.8806 0.0702  -0.0685 -0.1143 138 GLU B OE2 
2962 N N   . GLN B 104 ? 0.3341 0.2918 0.4379 0.0581  -0.0634 -0.1529 139 GLN B N   
2963 C CA  . GLN B 104 ? 0.3700 0.3420 0.4606 0.0549  -0.0654 -0.1611 139 GLN B CA  
2964 C C   . GLN B 104 ? 0.3176 0.3066 0.3874 0.0563  -0.0617 -0.1580 139 GLN B C   
2965 O O   . GLN B 104 ? 0.2914 0.2943 0.3474 0.0541  -0.0633 -0.1640 139 GLN B O   
2966 C CB  . GLN B 104 ? 0.2680 0.2334 0.3652 0.0475  -0.0706 -0.1570 139 GLN B CB  
2967 C CG  . GLN B 104 ? 0.2771 0.2274 0.3947 0.0441  -0.0747 -0.1599 139 GLN B CG  
2968 C CD  . GLN B 104 ? 0.3305 0.2776 0.4561 0.0362  -0.0791 -0.1553 139 GLN B CD  
2969 O OE1 . GLN B 104 ? 0.3085 0.2476 0.4406 0.0328  -0.0770 -0.1425 139 GLN B OE1 
2970 N NE2 . GLN B 104 ? 0.4471 0.4011 0.5731 0.0327  -0.0848 -0.1656 139 GLN B NE2 
2971 N N   . VAL B 105 ? 0.2734 0.2618 0.3401 0.0593  -0.0571 -0.1481 140 VAL B N   
2972 C CA  . VAL B 105 ? 0.2652 0.2690 0.3130 0.0598  -0.0534 -0.1441 140 VAL B CA  
2973 C C   . VAL B 105 ? 0.3344 0.3555 0.3723 0.0633  -0.0492 -0.1532 140 VAL B C   
2974 O O   . VAL B 105 ? 0.3113 0.3320 0.3578 0.0685  -0.0460 -0.1568 140 VAL B O   
2975 C CB  . VAL B 105 ? 0.2515 0.2495 0.2997 0.0616  -0.0496 -0.1316 140 VAL B CB  
2976 C CG1 . VAL B 105 ? 0.2866 0.3017 0.3164 0.0608  -0.0451 -0.1254 140 VAL B CG1 
2977 C CG2 . VAL B 105 ? 0.2903 0.2735 0.3473 0.0559  -0.0516 -0.1200 140 VAL B CG2 
2978 N N   . ASP B 106 ? 0.2716 0.3085 0.2917 0.0602  -0.0493 -0.1560 141 ASP B N   
2979 C CA  . ASP B 106 ? 0.2549 0.3093 0.2636 0.0616  -0.0444 -0.1642 141 ASP B CA  
2980 C C   . ASP B 106 ? 0.2518 0.3194 0.2501 0.0632  -0.0373 -0.1567 141 ASP B C   
2981 O O   . ASP B 106 ? 0.2971 0.3747 0.2970 0.0668  -0.0313 -0.1625 141 ASP B O   
2982 C CB  . ASP B 106 ? 0.3441 0.4094 0.3364 0.0560  -0.0479 -0.1687 141 ASP B CB  
2983 C CG  . ASP B 106 ? 0.3980 0.4525 0.4006 0.0539  -0.0552 -0.1777 141 ASP B CG  
2984 O OD1 . ASP B 106 ? 0.4044 0.4508 0.4218 0.0573  -0.0545 -0.1876 141 ASP B OD1 
2985 O OD2 . ASP B 106 ? 0.3714 0.4262 0.3685 0.0485  -0.0621 -0.1747 141 ASP B OD2 
2986 N N   . GLU B 107 ? 0.2727 0.3415 0.2616 0.0601  -0.0378 -0.1446 142 GLU B N   
2987 C CA  . GLU B 107 ? 0.2472 0.3286 0.2260 0.0602  -0.0314 -0.1364 142 GLU B CA  
2988 C C   . GLU B 107 ? 0.2686 0.3390 0.2507 0.0592  -0.0324 -0.1233 142 GLU B C   
2989 O O   . GLU B 107 ? 0.2317 0.2898 0.2181 0.0557  -0.0373 -0.1168 142 GLU B O   
2990 C CB  . GLU B 107 ? 0.3161 0.4156 0.2732 0.0544  -0.0297 -0.1332 142 GLU B CB  
2991 C CG  . GLU B 107 ? 0.3603 0.4707 0.3124 0.0541  -0.0276 -0.1456 142 GLU B CG  
2992 C CD  . GLU B 107 ? 0.5334 0.6625 0.4634 0.0481  -0.0239 -0.1412 142 GLU B CD  
2993 O OE1 . GLU B 107 ? 0.3715 0.5061 0.2917 0.0444  -0.0225 -0.1275 142 GLU B OE1 
2994 O OE2 . GLU B 107 ? 0.4815 0.6193 0.4039 0.0466  -0.0226 -0.1512 142 GLU B OE2 
2995 N N   . ILE B 108 ? 0.2378 0.3127 0.2215 0.0606  -0.0268 -0.1159 143 ILE B N   
2996 C CA  . ILE B 108 ? 0.1968 0.2628 0.1832 0.0572  -0.0261 -0.0998 143 ILE B CA  
2997 C C   . ILE B 108 ? 0.2973 0.3781 0.2711 0.0532  -0.0212 -0.0912 143 ILE B C   
2998 O O   . ILE B 108 ? 0.2576 0.3536 0.2294 0.0554  -0.0163 -0.0960 143 ILE B O   
2999 C CB  . ILE B 108 ? 0.2458 0.3015 0.2475 0.0616  -0.0257 -0.0983 143 ILE B CB  
3000 C CG1 . ILE B 108 ? 0.2722 0.3101 0.2870 0.0638  -0.0309 -0.1034 143 ILE B CG1 
3001 C CG2 . ILE B 108 ? 0.2377 0.2882 0.2376 0.0571  -0.0241 -0.0830 143 ILE B CG2 
3002 C CD1 . ILE B 108 ? 0.3336 0.3618 0.3642 0.0692  -0.0321 -0.1034 143 ILE B CD1 
3003 N N   . TYR B 109 ? 0.2345 0.3113 0.2018 0.0472  -0.0224 -0.0792 144 TYR B N   
3004 C CA  . TYR B 109 ? 0.2212 0.3084 0.1785 0.0423  -0.0185 -0.0693 144 TYR B CA  
3005 C C   . TYR B 109 ? 0.2439 0.3207 0.2075 0.0399  -0.0168 -0.0591 144 TYR B C   
3006 O O   . TYR B 109 ? 0.2209 0.2828 0.1902 0.0388  -0.0192 -0.0551 144 TYR B O   
3007 C CB  . TYR B 109 ? 0.2097 0.2998 0.1557 0.0372  -0.0219 -0.0629 144 TYR B CB  
3008 C CG  . TYR B 109 ? 0.2267 0.3277 0.1626 0.0381  -0.0250 -0.0728 144 TYR B CG  
3009 C CD1 . TYR B 109 ? 0.1997 0.3117 0.1342 0.0425  -0.0215 -0.0873 144 TYR B CD1 
3010 C CD2 . TYR B 109 ? 0.3043 0.4054 0.2325 0.0345  -0.0317 -0.0685 144 TYR B CD2 
3011 C CE1 . TYR B 109 ? 0.2654 0.3878 0.1888 0.0425  -0.0237 -0.0984 144 TYR B CE1 
3012 C CE2 . TYR B 109 ? 0.2671 0.3793 0.1833 0.0341  -0.0357 -0.0780 144 TYR B CE2 
3013 C CZ  . TYR B 109 ? 0.2708 0.3932 0.1836 0.0377  -0.0311 -0.0935 144 TYR B CZ  
3014 O OH  . TYR B 109 ? 0.3313 0.4607 0.2356 0.0356  -0.0330 -0.1009 144 TYR B OH  
3015 N N   . LEU B 110 ? 0.2121 0.2981 0.1751 0.0386  -0.0124 -0.0557 145 LEU B N   
3016 C CA  . LEU B 110 ? 0.2039 0.2821 0.1712 0.0355  -0.0112 -0.0476 145 LEU B CA  
3017 C C   . LEU B 110 ? 0.1893 0.2701 0.1492 0.0282  -0.0091 -0.0377 145 LEU B C   
3018 O O   . LEU B 110 ? 0.2309 0.3265 0.1847 0.0257  -0.0062 -0.0361 145 LEU B O   
3019 C CB  . LEU B 110 ? 0.2410 0.3281 0.2154 0.0386  -0.0093 -0.0505 145 LEU B CB  
3020 C CG  . LEU B 110 ? 0.2374 0.3207 0.2227 0.0466  -0.0121 -0.0594 145 LEU B CG  
3021 C CD1 . LEU B 110 ? 0.2531 0.3481 0.2487 0.0506  -0.0110 -0.0618 145 LEU B CD1 
3022 C CD2 . LEU B 110 ? 0.2161 0.2789 0.2052 0.0462  -0.0160 -0.0558 145 LEU B CD2 
3023 N N   . THR B 111 ? 0.1831 0.2494 0.1446 0.0246  -0.0100 -0.0313 146 THR B N   
3024 C CA  . THR B 111 ? 0.2126 0.2784 0.1707 0.0180  -0.0081 -0.0223 146 THR B CA  
3025 C C   . THR B 111 ? 0.1917 0.2655 0.1505 0.0145  -0.0048 -0.0206 146 THR B C   
3026 O O   . THR B 111 ? 0.2200 0.3021 0.1756 0.0091  -0.0026 -0.0148 146 THR B O   
3027 C CB  . THR B 111 ? 0.1982 0.2466 0.1609 0.0157  -0.0088 -0.0185 146 THR B CB  
3028 O OG1 . THR B 111 ? 0.2136 0.2534 0.1802 0.0162  -0.0075 -0.0216 146 THR B OG1 
3029 C CG2 . THR B 111 ? 0.1790 0.2223 0.1443 0.0187  -0.0128 -0.0192 146 THR B CG2 
3030 N N   . HIS B 112 ? 0.1735 0.2453 0.1373 0.0168  -0.0052 -0.0244 147 HIS B N   
3031 C CA  . HIS B 112 ? 0.1907 0.2721 0.1574 0.0140  -0.0039 -0.0234 147 HIS B CA  
3032 C C   . HIS B 112 ? 0.2047 0.2840 0.1773 0.0193  -0.0069 -0.0278 147 HIS B C   
3033 O O   . HIS B 112 ? 0.2419 0.3109 0.2157 0.0240  -0.0091 -0.0308 147 HIS B O   
3034 C CB  . HIS B 112 ? 0.2027 0.2771 0.1678 0.0055  -0.0027 -0.0174 147 HIS B CB  
3035 C CG  . HIS B 112 ? 0.1851 0.2412 0.1492 0.0041  -0.0036 -0.0176 147 HIS B CG  
3036 N ND1 . HIS B 112 ? 0.2260 0.2697 0.1900 0.0068  -0.0038 -0.0185 147 HIS B ND1 
3037 C CD2 . HIS B 112 ? 0.2417 0.2914 0.2046 -0.0005 -0.0039 -0.0177 147 HIS B CD2 
3038 C CE1 . HIS B 112 ? 0.1865 0.2175 0.1499 0.0042  -0.0028 -0.0193 147 HIS B CE1 
3039 N NE2 . HIS B 112 ? 0.2181 0.2521 0.1791 -0.0004 -0.0028 -0.0190 147 HIS B NE2 
3040 N N   . MET B 113 ? 0.2088 0.2980 0.1864 0.0181  -0.0078 -0.0271 148 MET B N   
3041 C CA  . MET B 113 ? 0.1714 0.2614 0.1568 0.0240  -0.0121 -0.0298 148 MET B CA  
3042 C C   . MET B 113 ? 0.2011 0.2816 0.1837 0.0196  -0.0160 -0.0252 148 MET B C   
3043 O O   . MET B 113 ? 0.2048 0.2899 0.1942 0.0226  -0.0209 -0.0244 148 MET B O   
3044 C CB  . MET B 113 ? 0.1842 0.2950 0.1812 0.0291  -0.0117 -0.0339 148 MET B CB  
3045 C CG  . MET B 113 ? 0.2176 0.3376 0.2150 0.0339  -0.0074 -0.0407 148 MET B CG  
3046 S SD  . MET B 113 ? 0.2319 0.3800 0.2437 0.0386  -0.0038 -0.0471 148 MET B SD  
3047 C CE  . MET B 113 ? 0.2247 0.3804 0.2286 0.0418  0.0023  -0.0559 148 MET B CE  
3048 N N   . HIS B 114 ? 0.1949 0.2622 0.1680 0.0128  -0.0141 -0.0224 149 HIS B N   
3049 C CA  . HIS B 114 ? 0.2031 0.2607 0.1701 0.0084  -0.0169 -0.0198 149 HIS B CA  
3050 C C   . HIS B 114 ? 0.1835 0.2314 0.1513 0.0138  -0.0200 -0.0193 149 HIS B C   
3051 O O   . HIS B 114 ? 0.2260 0.2699 0.1983 0.0196  -0.0189 -0.0221 149 HIS B O   
3052 C CB  . HIS B 114 ? 0.2638 0.3091 0.2219 0.0008  -0.0124 -0.0195 149 HIS B CB  
3053 C CG  . HIS B 114 ? 0.2777 0.3289 0.2347 -0.0070 -0.0112 -0.0189 149 HIS B CG  
3054 N ND1 . HIS B 114 ? 0.2591 0.3005 0.2128 -0.0131 -0.0068 -0.0195 149 HIS B ND1 
3055 C CD2 . HIS B 114 ? 0.2962 0.3618 0.2574 -0.0100 -0.0142 -0.0178 149 HIS B CD2 
3056 C CE1 . HIS B 114 ? 0.3739 0.4219 0.3290 -0.0200 -0.0072 -0.0188 149 HIS B CE1 
3057 N NE2 . HIS B 114 ? 0.3233 0.3870 0.2827 -0.0187 -0.0116 -0.0177 149 HIS B NE2 
3058 N N   . PRO B 115 ? 0.2221 0.2664 0.1856 0.0114  -0.0247 -0.0152 150 PRO B N   
3059 C CA  . PRO B 115 ? 0.2019 0.2379 0.1683 0.0164  -0.0291 -0.0123 150 PRO B CA  
3060 C C   . PRO B 115 ? 0.2220 0.2432 0.1853 0.0165  -0.0246 -0.0135 150 PRO B C   
3061 O O   . PRO B 115 ? 0.2488 0.2645 0.2200 0.0223  -0.0269 -0.0135 150 PRO B O   
3062 C CB  . PRO B 115 ? 0.2623 0.2969 0.2196 0.0106  -0.0347 -0.0056 150 PRO B CB  
3063 C CG  . PRO B 115 ? 0.4584 0.5052 0.4130 0.0048  -0.0353 -0.0068 150 PRO B CG  
3064 C CD  . PRO B 115 ? 0.3161 0.3638 0.2714 0.0031  -0.0272 -0.0125 150 PRO B CD  
3065 N N   . ASP B 116 ? 0.2167 0.2315 0.1713 0.0101  -0.0183 -0.0149 151 ASP B N   
3066 C CA  . ASP B 116 ? 0.2033 0.2061 0.1577 0.0096  -0.0136 -0.0161 151 ASP B CA  
3067 C C   . ASP B 116 ? 0.2422 0.2466 0.2066 0.0155  -0.0123 -0.0209 151 ASP B C   
3068 O O   . ASP B 116 ? 0.2310 0.2276 0.1983 0.0153  -0.0092 -0.0224 151 ASP B O   
3069 C CB  . ASP B 116 ? 0.2364 0.2330 0.1811 0.0015  -0.0068 -0.0173 151 ASP B CB  
3070 C CG  . ASP B 116 ? 0.3236 0.3256 0.2673 -0.0015 -0.0045 -0.0203 151 ASP B CG  
3071 O OD1 . ASP B 116 ? 0.2963 0.3078 0.2390 -0.0024 -0.0084 -0.0193 151 ASP B OD1 
3072 O OD2 . ASP B 116 ? 0.2579 0.2544 0.2036 -0.0033 0.0012  -0.0234 151 ASP B OD2 
3073 N N   . HIS B 117 ? 0.2198 0.2356 0.1895 0.0202  -0.0147 -0.0234 152 HIS B N   
3074 C CA  . HIS B 117 ? 0.2148 0.2344 0.1907 0.0252  -0.0144 -0.0283 152 HIS B CA  
3075 C C   . HIS B 117 ? 0.2010 0.2271 0.1855 0.0329  -0.0184 -0.0325 152 HIS B C   
3076 O O   . HIS B 117 ? 0.2349 0.2605 0.2241 0.0371  -0.0189 -0.0380 152 HIS B O   
3077 C CB  . HIS B 117 ? 0.2175 0.2461 0.1902 0.0227  -0.0115 -0.0285 152 HIS B CB  
3078 C CG  . HIS B 117 ? 0.2496 0.2702 0.2176 0.0162  -0.0077 -0.0258 152 HIS B CG  
3079 N ND1 . HIS B 117 ? 0.2516 0.2666 0.2222 0.0160  -0.0058 -0.0261 152 HIS B ND1 
3080 C CD2 . HIS B 117 ? 0.2458 0.2623 0.2082 0.0100  -0.0056 -0.0237 152 HIS B CD2 
3081 C CE1 . HIS B 117 ? 0.2712 0.2790 0.2402 0.0108  -0.0020 -0.0246 152 HIS B CE1 
3082 N NE2 . HIS B 117 ? 0.2273 0.2353 0.1901 0.0067  -0.0014 -0.0240 152 HIS B NE2 
3083 N N   . VAL B 118 ? 0.2080 0.2404 0.1960 0.0350  -0.0217 -0.0307 153 VAL B N   
3084 C CA  . VAL B 118 ? 0.2083 0.2473 0.2085 0.0435  -0.0252 -0.0358 153 VAL B CA  
3085 C C   . VAL B 118 ? 0.2172 0.2451 0.2250 0.0468  -0.0310 -0.0321 153 VAL B C   
3086 O O   . VAL B 118 ? 0.2387 0.2674 0.2600 0.0548  -0.0342 -0.0374 153 VAL B O   
3087 C CB  . VAL B 118 ? 0.2238 0.2821 0.2286 0.0453  -0.0247 -0.0374 153 VAL B CB  
3088 C CG1 . VAL B 118 ? 0.3562 0.4254 0.3542 0.0420  -0.0190 -0.0402 153 VAL B CG1 
3089 C CG2 . VAL B 118 ? 0.1845 0.2452 0.1869 0.0405  -0.0280 -0.0295 153 VAL B CG2 
3090 N N   . GLY B 119 ? 0.2117 0.2295 0.2116 0.0407  -0.0324 -0.0233 154 GLY B N   
3091 C CA  . GLY B 119 ? 0.2589 0.2670 0.2645 0.0427  -0.0390 -0.0167 154 GLY B CA  
3092 C C   . GLY B 119 ? 0.2954 0.2909 0.3118 0.0474  -0.0404 -0.0201 154 GLY B C   
3093 O O   . GLY B 119 ? 0.2658 0.2565 0.2958 0.0537  -0.0467 -0.0188 154 GLY B O   
3094 N N   . GLY B 120 ? 0.2428 0.2329 0.2558 0.0447  -0.0353 -0.0248 155 GLY B N   
3095 C CA  . GLY B 120 ? 0.2249 0.2034 0.2485 0.0476  -0.0368 -0.0290 155 GLY B CA  
3096 C C   . GLY B 120 ? 0.2667 0.2497 0.3050 0.0572  -0.0399 -0.0401 155 GLY B C   
3097 O O   . GLY B 120 ? 0.2836 0.2556 0.3330 0.0599  -0.0424 -0.0448 155 GLY B O   
3098 N N   . LEU B 121 ? 0.2385 0.2379 0.2781 0.0619  -0.0391 -0.0453 156 LEU B N   
3099 C CA  . LEU B 121 ? 0.2583 0.2645 0.3116 0.0711  -0.0400 -0.0582 156 LEU B CA  
3100 C C   . LEU B 121 ? 0.2656 0.2622 0.3384 0.0786  -0.0468 -0.0577 156 LEU B C   
3101 O O   . LEU B 121 ? 0.2641 0.2602 0.3514 0.0864  -0.0477 -0.0702 156 LEU B O   
3102 C CB  . LEU B 121 ? 0.2248 0.2533 0.2754 0.0733  -0.0360 -0.0631 156 LEU B CB  
3103 C CG  . LEU B 121 ? 0.2426 0.2821 0.2782 0.0684  -0.0297 -0.0673 156 LEU B CG  
3104 C CD1 . LEU B 121 ? 0.2235 0.2848 0.2573 0.0690  -0.0256 -0.0689 156 LEU B CD1 
3105 C CD2 . LEU B 121 ? 0.2343 0.2720 0.2709 0.0711  -0.0290 -0.0797 156 LEU B CD2 
3106 N N   . MET B 122 ? 0.2278 0.2169 0.3017 0.0766  -0.0520 -0.0438 157 MET B N   
3107 C CA  . MET B 122 ? 0.2992 0.2788 0.3929 0.0839  -0.0602 -0.0402 157 MET B CA  
3108 C C   . MET B 122 ? 0.3303 0.2882 0.4216 0.0778  -0.0648 -0.0263 157 MET B C   
3109 O O   . MET B 122 ? 0.3143 0.2699 0.3869 0.0678  -0.0626 -0.0156 157 MET B O   
3110 C CB  . MET B 122 ? 0.3006 0.2943 0.4001 0.0876  -0.0644 -0.0338 157 MET B CB  
3111 C CG  . MET B 122 ? 0.2513 0.2684 0.3586 0.0942  -0.0597 -0.0470 157 MET B CG  
3112 S SD  . MET B 122 ? 0.3031 0.3214 0.4342 0.1070  -0.0577 -0.0676 157 MET B SD  
3113 C CE  . MET B 122 ? 0.3483 0.3548 0.5082 0.1163  -0.0690 -0.0600 157 MET B CE  
3114 N N   . VAL B 123 ? 0.3692 0.3111 0.4801 0.0833  -0.0708 -0.0270 158 VAL B N   
3115 C CA  . VAL B 123 ? 0.3462 0.2674 0.4588 0.0783  -0.0769 -0.0109 158 VAL B CA  
3116 C C   . VAL B 123 ? 0.3883 0.3065 0.5203 0.0870  -0.0874 -0.0031 158 VAL B C   
3117 O O   . VAL B 123 ? 0.4101 0.3205 0.5669 0.0965  -0.0915 -0.0111 158 VAL B O   
3118 C CB  . VAL B 123 ? 0.3836 0.2861 0.5054 0.0762  -0.0762 -0.0160 158 VAL B CB  
3119 C CG1 . VAL B 123 ? 0.4268 0.3075 0.5547 0.0716  -0.0833 0.0020  158 VAL B CG1 
3120 C CG2 . VAL B 123 ? 0.4196 0.3261 0.5238 0.0671  -0.0673 -0.0208 158 VAL B CG2 
3121 N N   . GLY B 124 ? 0.3904 0.3156 0.5118 0.0834  -0.0920 0.0120  159 GLY B N   
3122 C CA  . GLY B 124 ? 0.3850 0.3123 0.5265 0.0926  -0.1032 0.0191  159 GLY B CA  
3123 C C   . GLY B 124 ? 0.4486 0.3948 0.6093 0.1049  -0.1007 0.0011  159 GLY B C   
3124 O O   . GLY B 124 ? 0.4188 0.3848 0.5671 0.1030  -0.0923 -0.0087 159 GLY B O   
3125 N N   . GLU B 125 ? 0.4390 0.3819 0.6222 0.1120  -0.1023 -0.0034 160 GLU B N   
3126 C CA  . GLU B 125 ? 0.3277 0.2890 0.5267 0.1209  -0.0966 -0.0207 160 GLU B CA  
3127 C C   . GLU B 125 ? 0.4130 0.3724 0.6137 0.1222  -0.0868 -0.0416 160 GLU B C   
3128 O O   . GLU B 125 ? 0.4349 0.4080 0.6471 0.1285  -0.0812 -0.0568 160 GLU B O   
3129 C CB  . GLU B 125 ? 0.3866 0.3468 0.6095 0.1282  -0.1035 -0.0154 160 GLU B CB  
3130 C CG  . GLU B 125 ? 0.6531 0.6200 0.8741 0.1268  -0.1140 0.0045  160 GLU B CG  
3131 C CD  . GLU B 125 ? 0.8159 0.8111 1.0321 0.1276  -0.1114 0.0008  160 GLU B CD  
3132 O OE1 . GLU B 125 ? 0.8262 0.8262 1.0218 0.1198  -0.1145 0.0110  160 GLU B OE1 
3133 O OE2 . GLU B 125 ? 0.8491 0.8621 1.0823 0.1351  -0.1060 -0.0124 160 GLU B OE2 
3134 N N   . GLN B 126 ? 0.3540 0.2980 0.5427 0.1155  -0.0848 -0.0424 161 GLN B N   
3135 C CA  . GLN B 126 ? 0.3390 0.2807 0.5276 0.1148  -0.0775 -0.0607 161 GLN B CA  
3136 C C   . GLN B 126 ? 0.2983 0.2526 0.4658 0.1103  -0.0700 -0.0688 161 GLN B C   
3137 O O   . GLN B 126 ? 0.3273 0.2802 0.4799 0.1054  -0.0713 -0.0583 161 GLN B O   
3138 C CB  . GLN B 126 ? 0.3911 0.3077 0.5838 0.1097  -0.0811 -0.0563 161 GLN B CB  
3139 C CG  . GLN B 126 ? 0.4725 0.3742 0.6855 0.1131  -0.0891 -0.0462 161 GLN B CG  
3140 C CD  . GLN B 126 ? 0.7483 0.6586 0.9818 0.1228  -0.0879 -0.0600 161 GLN B CD  
3141 O OE1 . GLN B 126 ? 0.7993 0.7124 1.0471 0.1290  -0.0933 -0.0523 161 GLN B OE1 
3142 N NE2 . GLN B 126 ? 0.7256 0.6408 0.9605 0.1240  -0.0812 -0.0805 161 GLN B NE2 
3143 N N   . LEU B 127 ? 0.2718 0.2383 0.4374 0.1119  -0.0627 -0.0870 162 LEU B N   
3144 C CA  . LEU B 127 ? 0.2639 0.2405 0.4092 0.1068  -0.0562 -0.0944 162 LEU B CA  
3145 C C   . LEU B 127 ? 0.2602 0.2182 0.3974 0.0992  -0.0583 -0.0894 162 LEU B C   
3146 O O   . LEU B 127 ? 0.3070 0.2501 0.4536 0.0975  -0.0607 -0.0925 162 LEU B O   
3147 C CB  . LEU B 127 ? 0.3370 0.3273 0.4815 0.1084  -0.0497 -0.1135 162 LEU B CB  
3148 C CG  . LEU B 127 ? 0.3635 0.3729 0.5182 0.1154  -0.0456 -0.1218 162 LEU B CG  
3149 C CD1 . LEU B 127 ? 0.3639 0.3866 0.5121 0.1148  -0.0385 -0.1401 162 LEU B CD1 
3150 C CD2 . LEU B 127 ? 0.3447 0.3723 0.4934 0.1162  -0.0436 -0.1138 162 LEU B CD2 
3151 N N   . ALA B 128 ? 0.2704 0.2299 0.3917 0.0946  -0.0571 -0.0821 163 ALA B N   
3152 C CA  . ALA B 128 ? 0.2552 0.2003 0.3683 0.0855  -0.0570 -0.0768 163 ALA B CA  
3153 C C   . ALA B 128 ? 0.3643 0.3126 0.4744 0.0836  -0.0540 -0.0924 163 ALA B C   
3154 O O   . ALA B 128 ? 0.3163 0.2514 0.4290 0.0779  -0.0557 -0.0917 163 ALA B O   
3155 C CB  . ALA B 128 ? 0.3153 0.2656 0.4071 0.0757  -0.0532 -0.0625 163 ALA B CB  
3156 N N   . PHE B 129 ? 0.2752 0.2429 0.3783 0.0864  -0.0495 -0.1046 164 PHE B N   
3157 C CA  . PHE B 129 ? 0.3339 0.3086 0.4294 0.0829  -0.0474 -0.1171 164 PHE B CA  
3158 C C   . PHE B 129 ? 0.2842 0.2689 0.3870 0.0880  -0.0457 -0.1308 164 PHE B C   
3159 O O   . PHE B 129 ? 0.3199 0.3242 0.4145 0.0904  -0.0407 -0.1370 164 PHE B O   
3160 C CB  . PHE B 129 ? 0.2595 0.2485 0.3350 0.0795  -0.0434 -0.1168 164 PHE B CB  
3161 C CG  . PHE B 129 ? 0.2686 0.2493 0.3366 0.0723  -0.0435 -0.1015 164 PHE B CG  
3162 C CD1 . PHE B 129 ? 0.3016 0.2725 0.3700 0.0660  -0.0455 -0.1006 164 PHE B CD1 
3163 C CD2 . PHE B 129 ? 0.2606 0.2448 0.3219 0.0702  -0.0411 -0.0877 164 PHE B CD2 
3164 C CE1 . PHE B 129 ? 0.2875 0.2531 0.3504 0.0586  -0.0437 -0.0866 164 PHE B CE1 
3165 C CE2 . PHE B 129 ? 0.2783 0.2559 0.3315 0.0623  -0.0398 -0.0744 164 PHE B CE2 
3166 C CZ  . PHE B 129 ? 0.2754 0.2440 0.3299 0.0568  -0.0404 -0.0741 164 PHE B CZ  
3167 N N   . PRO B 130 ? 0.2964 0.2680 0.4155 0.0894  -0.0493 -0.1356 165 PRO B N   
3168 C CA  . PRO B 130 ? 0.3142 0.2925 0.4453 0.0958  -0.0477 -0.1476 165 PRO B CA  
3169 C C   . PRO B 130 ? 0.3511 0.3469 0.4717 0.0953  -0.0431 -0.1640 165 PRO B C   
3170 O O   . PRO B 130 ? 0.3368 0.3426 0.4647 0.1007  -0.0395 -0.1745 165 PRO B O   
3171 C CB  . PRO B 130 ? 0.3899 0.3466 0.5410 0.0964  -0.0535 -0.1474 165 PRO B CB  
3172 C CG  . PRO B 130 ? 0.4392 0.3822 0.5854 0.0883  -0.0570 -0.1398 165 PRO B CG  
3173 C CD  . PRO B 130 ? 0.2683 0.2175 0.3982 0.0854  -0.0548 -0.1283 165 PRO B CD  
3174 N N   . ASN B 131 ? 0.3369 0.3373 0.4412 0.0890  -0.0431 -0.1661 166 ASN B N   
3175 C CA  . ASN B 131 ? 0.3714 0.3885 0.4634 0.0876  -0.0396 -0.1801 166 ASN B CA  
3176 C C   . ASN B 131 ? 0.3806 0.4169 0.4500 0.0844  -0.0351 -0.1761 166 ASN B C   
3177 O O   . ASN B 131 ? 0.3914 0.4430 0.4473 0.0823  -0.0319 -0.1851 166 ASN B O   
3178 C CB  . ASN B 131 ? 0.3208 0.3289 0.4129 0.0826  -0.0447 -0.1873 166 ASN B CB  
3179 C CG  . ASN B 131 ? 0.3966 0.3875 0.5111 0.0853  -0.0485 -0.1936 166 ASN B CG  
3180 O OD1 . ASN B 131 ? 0.3719 0.3454 0.4958 0.0816  -0.0541 -0.1884 166 ASN B OD1 
3181 N ND2 . ASN B 131 ? 0.3435 0.3393 0.4679 0.0915  -0.0452 -0.2045 166 ASN B ND2 
3182 N N   . ALA B 132 ? 0.2912 0.3268 0.3557 0.0837  -0.0346 -0.1624 167 ALA B N   
3183 C CA  . ALA B 132 ? 0.3077 0.3585 0.3515 0.0797  -0.0312 -0.1568 167 ALA B CA  
3184 C C   . ALA B 132 ? 0.3412 0.4127 0.3801 0.0823  -0.0237 -0.1586 167 ALA B C   
3185 O O   . ALA B 132 ? 0.3298 0.4020 0.3831 0.0880  -0.0218 -0.1588 167 ALA B O   
3186 C CB  . ALA B 132 ? 0.2676 0.3082 0.3089 0.0775  -0.0334 -0.1425 167 ALA B CB  
3187 N N   . VAL B 133 ? 0.2728 0.3616 0.2920 0.0776  -0.0197 -0.1589 168 VAL B N   
3188 C CA  . VAL B 133 ? 0.3353 0.4447 0.3468 0.0773  -0.0121 -0.1561 168 VAL B CA  
3189 C C   . VAL B 133 ? 0.2892 0.3988 0.2907 0.0736  -0.0122 -0.1413 168 VAL B C   
3190 O O   . VAL B 133 ? 0.2764 0.3806 0.2652 0.0684  -0.0159 -0.1354 168 VAL B O   
3191 C CB  . VAL B 133 ? 0.3674 0.4950 0.3622 0.0727  -0.0074 -0.1629 168 VAL B CB  
3192 C CG1 . VAL B 133 ? 0.2900 0.4385 0.2749 0.0698  0.0006  -0.1564 168 VAL B CG1 
3193 C CG2 . VAL B 133 ? 0.3614 0.4902 0.3665 0.0768  -0.0058 -0.1794 168 VAL B CG2 
3194 N N   . VAL B 134 ? 0.2695 0.3854 0.2778 0.0763  -0.0087 -0.1357 169 VAL B N   
3195 C CA  . VAL B 134 ? 0.2419 0.3585 0.2416 0.0728  -0.0081 -0.1227 169 VAL B CA  
3196 C C   . VAL B 134 ? 0.2822 0.4204 0.2665 0.0667  -0.0014 -0.1182 169 VAL B C   
3197 O O   . VAL B 134 ? 0.2684 0.4234 0.2563 0.0676  0.0045  -0.1239 169 VAL B O   
3198 C CB  . VAL B 134 ? 0.2507 0.3604 0.2670 0.0761  -0.0097 -0.1145 169 VAL B CB  
3199 C CG1 . VAL B 134 ? 0.2467 0.3554 0.2538 0.0680  -0.0094 -0.0972 169 VAL B CG1 
3200 C CG2 . VAL B 134 ? 0.2268 0.3136 0.2572 0.0804  -0.0167 -0.1153 169 VAL B CG2 
3201 N N   . ARG B 135 ? 0.2224 0.3582 0.1919 0.0588  -0.0027 -0.1055 170 ARG B N   
3202 C CA  . ARG B 135 ? 0.2219 0.3756 0.1759 0.0518  0.0027  -0.0987 170 ARG B CA  
3203 C C   . ARG B 135 ? 0.2625 0.4088 0.2164 0.0454  0.0018  -0.0812 170 ARG B C   
3204 O O   . ARG B 135 ? 0.2399 0.3668 0.1971 0.0443  -0.0037 -0.0742 170 ARG B O   
3205 C CB  . ARG B 135 ? 0.2646 0.4193 0.2014 0.0466  -0.0001 -0.0982 170 ARG B CB  
3206 C CG  . ARG B 135 ? 0.3307 0.4890 0.2691 0.0494  0.0001  -0.1123 170 ARG B CG  
3207 C CD  . ARG B 135 ? 0.3247 0.4941 0.2432 0.0420  0.0009  -0.1094 170 ARG B CD  
3208 N NE  . ARG B 135 ? 0.2934 0.4826 0.2059 0.0379  0.0097  -0.1061 170 ARG B NE  
3209 C CZ  . ARG B 135 ? 0.3549 0.5565 0.2501 0.0313  0.0124  -0.1040 170 ARG B CZ  
3210 N NH1 . ARG B 135 ? 0.3226 0.5197 0.2040 0.0282  0.0063  -0.1047 170 ARG B NH1 
3211 N NH2 . ARG B 135 ? 0.3340 0.5535 0.2257 0.0271  0.0211  -0.1004 170 ARG B NH2 
3212 N N   . ALA B 136 ? 0.2439 0.4062 0.1953 0.0408  0.0078  -0.0752 171 ALA B N   
3213 C CA  . ALA B 136 ? 0.1898 0.3470 0.1404 0.0334  0.0076  -0.0600 171 ALA B CA  
3214 C C   . ALA B 136 ? 0.2632 0.4422 0.2064 0.0268  0.0149  -0.0553 171 ALA B C   
3215 O O   . ALA B 136 ? 0.2448 0.4439 0.1854 0.0288  0.0210  -0.0646 171 ALA B O   
3216 C CB  . ALA B 136 ? 0.2038 0.3526 0.1701 0.0360  0.0058  -0.0581 171 ALA B CB  
3217 N N   . ASP B 137 ? 0.2097 0.3848 0.1501 0.0183  0.0149  -0.0413 172 ASP B N   
3218 C CA  . ASP B 137 ? 0.2267 0.4215 0.1610 0.0103  0.0218  -0.0347 172 ASP B CA  
3219 C C   . ASP B 137 ? 0.2375 0.4514 0.1868 0.0123  0.0280  -0.0408 172 ASP B C   
3220 O O   . ASP B 137 ? 0.2049 0.4119 0.1696 0.0167  0.0248  -0.0434 172 ASP B O   
3221 C CB  . ASP B 137 ? 0.2685 0.4520 0.1995 0.0005  0.0196  -0.0183 172 ASP B CB  
3222 C CG  . ASP B 137 ? 0.4163 0.6178 0.3383 -0.0095 0.0259  -0.0088 172 ASP B CG  
3223 O OD1 . ASP B 137 ? 0.3296 0.5477 0.2604 -0.0132 0.0323  -0.0087 172 ASP B OD1 
3224 O OD2 . ASP B 137 ? 0.2920 0.4924 0.1985 -0.0140 0.0242  -0.0008 172 ASP B OD2 
3225 N N   . GLN B 138 ? 0.2297 0.4692 0.1746 0.0087  0.0368  -0.0429 173 GLN B N   
3226 C CA  . GLN B 138 ? 0.2266 0.4887 0.1888 0.0107  0.0438  -0.0495 173 GLN B CA  
3227 C C   . GLN B 138 ? 0.2013 0.4601 0.1771 0.0048  0.0415  -0.0393 173 GLN B C   
3228 O O   . GLN B 138 ? 0.2552 0.5225 0.2508 0.0095  0.0412  -0.0448 173 GLN B O   
3229 C CB  . GLN B 138 ? 0.2213 0.5045 0.1774 0.0049  0.0523  -0.0500 173 GLN B CB  
3230 C CG  . GLN B 138 ? 0.3956 0.7012 0.3723 0.0078  0.0592  -0.0583 173 GLN B CG  
3231 C CD  . GLN B 138 ? 0.8736 1.1793 0.8638 0.0214  0.0583  -0.0761 173 GLN B CD  
3232 O OE1 . GLN B 138 ? 0.5611 0.8749 0.5481 0.0236  0.0630  -0.0859 173 GLN B OE1 
3233 N NE2 . GLN B 138 ? 0.4759 0.7723 0.4820 0.0303  0.0522  -0.0801 173 GLN B NE2 
3234 N N   . LYS B 139 ? 0.2121 0.4585 0.1786 -0.0056 0.0390  -0.0248 174 LYS B N   
3235 C CA  . LYS B 139 ? 0.2522 0.4935 0.2306 -0.0123 0.0363  -0.0168 174 LYS B CA  
3236 C C   . LYS B 139 ? 0.2732 0.4957 0.2612 -0.0054 0.0277  -0.0210 174 LYS B C   
3237 O O   . LYS B 139 ? 0.2489 0.4768 0.2517 -0.0062 0.0256  -0.0214 174 LYS B O   
3238 C CB  . LYS B 139 ? 0.2650 0.4929 0.2323 -0.0241 0.0351  -0.0018 174 LYS B CB  
3239 C CG  . LYS B 139 ? 0.3881 0.6354 0.3460 -0.0335 0.0432  0.0061  174 LYS B CG  
3240 C CD  . LYS B 139 ? 0.3473 0.5826 0.3023 -0.0466 0.0417  0.0226  174 LYS B CD  
3241 C CE  . LYS B 139 ? 0.5288 0.7821 0.4718 -0.0567 0.0493  0.0332  174 LYS B CE  
3242 N NZ  . LYS B 139 ? 0.6742 0.9087 0.6103 -0.0673 0.0453  0.0510  174 LYS B NZ  
3243 N N   . GLU B 140 ? 0.2035 0.4051 0.1832 0.0009  0.0224  -0.0238 175 GLU B N   
3244 C CA  . GLU B 140 ? 0.1878 0.3714 0.1740 0.0066  0.0151  -0.0267 175 GLU B CA  
3245 C C   . GLU B 140 ? 0.2131 0.4094 0.2154 0.0158  0.0142  -0.0360 175 GLU B C   
3246 O O   . GLU B 140 ? 0.2221 0.4174 0.2355 0.0160  0.0095  -0.0347 175 GLU B O   
3247 C CB  . GLU B 140 ? 0.2055 0.3683 0.1813 0.0112  0.0112  -0.0283 175 GLU B CB  
3248 C CG  . GLU B 140 ? 0.2264 0.3676 0.2049 0.0139  0.0047  -0.0281 175 GLU B CG  
3249 C CD  . GLU B 140 ? 0.2271 0.3560 0.2032 0.0050  0.0032  -0.0200 175 GLU B CD  
3250 O OE1 . GLU B 140 ? 0.2299 0.3623 0.2024 -0.0030 0.0062  -0.0134 175 GLU B OE1 
3251 O OE2 . GLU B 140 ? 0.2473 0.3629 0.2249 0.0056  -0.0008 -0.0203 175 GLU B OE2 
3252 N N   . ALA B 141 ? 0.2014 0.4100 0.2057 0.0234  0.0183  -0.0459 176 ALA B N   
3253 C CA  . ALA B 141 ? 0.1746 0.3944 0.1978 0.0337  0.0176  -0.0558 176 ALA B CA  
3254 C C   . ALA B 141 ? 0.1965 0.4403 0.2368 0.0308  0.0206  -0.0545 176 ALA B C   
3255 O O   . ALA B 141 ? 0.2584 0.5048 0.3167 0.0361  0.0150  -0.0557 176 ALA B O   
3256 C CB  . ALA B 141 ? 0.2576 0.4866 0.2795 0.0416  0.0228  -0.0688 176 ALA B CB  
3257 N N   . ASP B 142 ? 0.1824 0.4446 0.2182 0.0220  0.0289  -0.0508 177 ASP B N   
3258 C CA  . ASP B 142 ? 0.2559 0.5435 0.3101 0.0180  0.0326  -0.0496 177 ASP B CA  
3259 C C   . ASP B 142 ? 0.1875 0.4656 0.2487 0.0122  0.0237  -0.0408 177 ASP B C   
3260 O O   . ASP B 142 ? 0.1881 0.4827 0.2707 0.0138  0.0212  -0.0421 177 ASP B O   
3261 C CB  . ASP B 142 ? 0.2095 0.5168 0.2556 0.0071  0.0434  -0.0450 177 ASP B CB  
3262 C CG  . ASP B 142 ? 0.5029 0.8280 0.5431 0.0120  0.0537  -0.0555 177 ASP B CG  
3263 O OD1 . ASP B 142 ? 0.2569 0.5850 0.3076 0.0247  0.0535  -0.0690 177 ASP B OD1 
3264 O OD2 . ASP B 142 ? 0.3233 0.6569 0.3484 0.0025  0.0610  -0.0498 177 ASP B OD2 
3265 N N   . PHE B 143 ? 0.2064 0.4592 0.2509 0.0054  0.0187  -0.0326 178 PHE B N   
3266 C CA  . PHE B 143 ? 0.2323 0.4757 0.2807 -0.0009 0.0107  -0.0264 178 PHE B CA  
3267 C C   . PHE B 143 ? 0.1664 0.3992 0.2218 0.0082  0.0010  -0.0295 178 PHE B C   
3268 O O   . PHE B 143 ? 0.2013 0.4452 0.2723 0.0085  -0.0049 -0.0288 178 PHE B O   
3269 C CB  . PHE B 143 ? 0.1926 0.4128 0.2227 -0.0108 0.0097  -0.0185 178 PHE B CB  
3270 C CG  . PHE B 143 ? 0.2210 0.4305 0.2525 -0.0182 0.0024  -0.0145 178 PHE B CG  
3271 C CD1 . PHE B 143 ? 0.2424 0.4664 0.2842 -0.0285 0.0027  -0.0110 178 PHE B CD1 
3272 C CD2 . PHE B 143 ? 0.2444 0.4305 0.2666 -0.0157 -0.0043 -0.0149 178 PHE B CD2 
3273 C CE1 . PHE B 143 ? 0.2582 0.4729 0.3002 -0.0362 -0.0047 -0.0091 178 PHE B CE1 
3274 C CE2 . PHE B 143 ? 0.2222 0.3997 0.2428 -0.0233 -0.0105 -0.0128 178 PHE B CE2 
3275 C CZ  . PHE B 143 ? 0.2864 0.4779 0.3164 -0.0335 -0.0112 -0.0104 178 PHE B CZ  
3276 N N   . TRP B 144 ? 0.2090 0.4209 0.2535 0.0151  -0.0014 -0.0319 179 TRP B N   
3277 C CA  . TRP B 144 ? 0.2052 0.4026 0.2524 0.0211  -0.0110 -0.0316 179 TRP B CA  
3278 C C   . TRP B 144 ? 0.2460 0.4564 0.3144 0.0331  -0.0144 -0.0374 179 TRP B C   
3279 O O   . TRP B 144 ? 0.2153 0.4196 0.2906 0.0362  -0.0240 -0.0341 179 TRP B O   
3280 C CB  . TRP B 144 ? 0.1549 0.3254 0.1854 0.0231  -0.0122 -0.0313 179 TRP B CB  
3281 C CG  . TRP B 144 ? 0.2336 0.3884 0.2476 0.0127  -0.0111 -0.0255 179 TRP B CG  
3282 C CD1 . TRP B 144 ? 0.1886 0.3357 0.1909 0.0091  -0.0056 -0.0244 179 TRP B CD1 
3283 C CD2 . TRP B 144 ? 0.2068 0.3518 0.2152 0.0046  -0.0159 -0.0206 179 TRP B CD2 
3284 N NE1 . TRP B 144 ? 0.2451 0.3772 0.2381 0.0003  -0.0064 -0.0193 179 TRP B NE1 
3285 C CE2 . TRP B 144 ? 0.2356 0.3663 0.2312 -0.0029 -0.0119 -0.0181 179 TRP B CE2 
3286 C CE3 . TRP B 144 ? 0.2292 0.3766 0.2421 0.0027  -0.0237 -0.0185 179 TRP B CE3 
3287 C CZ2 . TRP B 144 ? 0.1996 0.3177 0.1875 -0.0118 -0.0141 -0.0157 179 TRP B CZ2 
3288 C CZ3 . TRP B 144 ? 0.2585 0.3945 0.2603 -0.0072 -0.0264 -0.0156 179 TRP B CZ3 
3289 C CH2 . TRP B 144 ? 0.2350 0.3562 0.2247 -0.0142 -0.0209 -0.0153 179 TRP B CH2 
3290 N N   . LEU B 145 ? 0.2014 0.4063 0.2272 0.0044  0.0276  -0.0046 180 LEU B N   
3291 C CA  . LEU B 145 ? 0.2228 0.4616 0.2753 0.0192  0.0262  -0.0214 180 LEU B CA  
3292 C C   . LEU B 145 ? 0.2209 0.5069 0.3092 0.0100  0.0348  -0.0289 180 LEU B C   
3293 O O   . LEU B 145 ? 0.2748 0.5957 0.3934 0.0245  0.0363  -0.0443 180 LEU B O   
3294 C CB  . LEU B 145 ? 0.2709 0.5142 0.3075 0.0315  0.0326  -0.0302 180 LEU B CB  
3295 C CG  . LEU B 145 ? 0.2461 0.4508 0.2549 0.0377  0.0218  -0.0236 180 LEU B CG  
3296 C CD1 . LEU B 145 ? 0.2870 0.4978 0.2752 0.0452  0.0251  -0.0341 180 LEU B CD1 
3297 C CD2 . LEU B 145 ? 0.2401 0.4213 0.2620 0.0477  0.0065  -0.0252 180 LEU B CD2 
3298 N N   . SER B 146 ? 0.2549 0.5428 0.3455 -0.0138 0.0405  -0.0199 181 SER B N   
3299 C CA  . SER B 146 ? 0.2711 0.6089 0.4027 -0.0286 0.0486  -0.0272 181 SER B CA  
3300 C C   . SER B 146 ? 0.2021 0.5562 0.3685 -0.0218 0.0254  -0.0355 181 SER B C   
3301 O O   . SER B 146 ? 0.2064 0.5287 0.3576 -0.0302 0.0104  -0.0298 181 SER B O   
3302 C CB  . SER B 146 ? 0.2076 0.5322 0.3266 -0.0611 0.0619  -0.0137 181 SER B CB  
3303 O OG  . SER B 146 ? 0.2511 0.6236 0.4157 -0.0810 0.0671  -0.0217 181 SER B OG  
3304 N N   . GLN B 147 ? 0.1502 0.5546 0.3623 -0.0060 0.0221  -0.0496 182 GLN B N   
3305 C CA  . GLN B 147 ? 0.1688 0.5837 0.4099 0.0006  -0.0038 -0.0531 182 GLN B CA  
3306 C C   . GLN B 147 ? 0.1563 0.5911 0.4147 -0.0301 -0.0071 -0.0525 182 GLN B C   
3307 O O   . GLN B 147 ? 0.1865 0.6127 0.4426 -0.0345 -0.0317 -0.0519 182 GLN B O   
3308 C CB  . GLN B 147 ? 0.1920 0.6299 0.4702 0.0232  -0.0054 -0.0626 182 GLN B CB  
3309 C CG  . GLN B 147 ? 0.2546 0.7040 0.5627 0.0315  -0.0340 -0.0612 182 GLN B CG  
3310 C CD  . GLN B 147 ? 0.3834 0.7888 0.6590 0.0455  -0.0595 -0.0510 182 GLN B CD  
3311 O OE1 . GLN B 147 ? 0.4024 0.8016 0.6675 0.0352  -0.0810 -0.0451 182 GLN B OE1 
3312 N NE2 . GLN B 147 ? 0.3085 0.6806 0.5644 0.0663  -0.0564 -0.0495 182 GLN B NE2 
3313 N N   . THR B 148 ? 0.1679 0.6241 0.4388 -0.0536 0.0175  -0.0530 183 THR B N   
3314 C CA  . THR B 148 ? 0.1867 0.6546 0.4756 -0.0863 0.0156  -0.0534 183 THR B CA  
3315 C C   . THR B 148 ? 0.2471 0.6699 0.4979 -0.1080 0.0083  -0.0466 183 THR B C   
3316 O O   . THR B 148 ? 0.2072 0.6276 0.4650 -0.1252 -0.0101 -0.0527 183 THR B O   
3317 C CB  . THR B 148 ? 0.2294 0.7203 0.5353 -0.1082 0.0463  -0.0521 183 THR B CB  
3318 O OG1 . THR B 148 ? 0.3598 0.8127 0.6198 -0.1262 0.0690  -0.0376 183 THR B OG1 
3319 C CG2 . THR B 148 ? 0.2467 0.7746 0.5805 -0.0845 0.0589  -0.0608 183 THR B CG2 
3320 N N   . ASN B 149 ? 0.2079 0.5723 0.4067 -0.1018 0.0206  -0.0333 184 ASN B N   
3321 C CA  . ASN B 149 ? 0.2539 0.5513 0.4095 -0.1117 0.0146  -0.0260 184 ASN B CA  
3322 C C   . ASN B 149 ? 0.2251 0.5059 0.3677 -0.0965 -0.0125 -0.0331 184 ASN B C   
3323 O O   . ASN B 149 ? 0.3114 0.5641 0.4382 -0.1128 -0.0223 -0.0383 184 ASN B O   
3324 C CB  . ASN B 149 ? 0.2345 0.4816 0.3461 -0.1019 0.0292  -0.0102 184 ASN B CB  
3325 C CG  . ASN B 149 ? 0.2830 0.5292 0.3892 -0.1230 0.0542  0.0026  184 ASN B CG  
3326 O OD1 . ASN B 149 ? 0.3194 0.5961 0.4546 -0.1507 0.0647  -0.0003 184 ASN B OD1 
3327 N ND2 . ASN B 149 ? 0.3292 0.5411 0.3973 -0.1124 0.0633  0.0181  184 ASN B ND2 
3328 N N   . LEU B 150 ? 0.1964 0.4898 0.3411 -0.0667 -0.0233 -0.0336 185 LEU B N   
3329 C CA  . LEU B 150 ? 0.2344 0.5116 0.3615 -0.0539 -0.0480 -0.0359 185 LEU B CA  
3330 C C   . LEU B 150 ? 0.4638 0.7802 0.6180 -0.0668 -0.0710 -0.0462 185 LEU B C   
3331 O O   . LEU B 150 ? 0.2672 0.5596 0.3926 -0.0763 -0.0875 -0.0501 185 LEU B O   
3332 C CB  . LEU B 150 ? 0.1990 0.4786 0.3267 -0.0215 -0.0541 -0.0318 185 LEU B CB  
3333 C CG  . LEU B 150 ? 0.2507 0.5293 0.3724 -0.0058 -0.0819 -0.0303 185 LEU B CG  
3334 C CD1 . LEU B 150 ? 0.3700 0.5987 0.4393 -0.0149 -0.0879 -0.0269 185 LEU B CD1 
3335 C CD2 . LEU B 150 ? 0.3173 0.5920 0.4456 0.0241  -0.0836 -0.0257 185 LEU B CD2 
3336 N N   . ASP B 151 ? 0.2106 0.5915 0.4213 -0.0685 -0.0723 -0.0527 186 ASP B N   
3337 C CA  . ASP B 151 ? 0.2786 0.6880 0.5169 -0.0763 -0.0952 -0.0599 186 ASP B CA  
3338 C C   . ASP B 151 ? 0.3297 0.7283 0.5601 -0.1146 -0.0951 -0.0688 186 ASP B C   
3339 O O   . ASP B 151 ? 0.4205 0.8238 0.6522 -0.1224 -0.1196 -0.0757 186 ASP B O   
3340 C CB  . ASP B 151 ? 0.2376 0.6981 0.5353 -0.0664 -0.0885 -0.0622 186 ASP B CB  
3341 C CG  . ASP B 151 ? 0.3445 0.8086 0.6535 -0.0281 -0.0992 -0.0564 186 ASP B CG  
3342 O OD1 . ASP B 151 ? 0.5220 0.9515 0.7959 -0.0121 -0.1192 -0.0484 186 ASP B OD1 
3343 O OD2 . ASP B 151 ? 0.4966 0.9942 0.8476 -0.0159 -0.0859 -0.0598 186 ASP B OD2 
3344 N N   . LYS B 152 ? 0.3352 0.7130 0.5551 -0.1390 -0.0687 -0.0681 187 LYS B N   
3345 C CA  . LYS B 152 ? 0.2859 0.6354 0.4956 -0.1761 -0.0643 -0.0760 187 LYS B CA  
3346 C C   . LYS B 152 ? 0.3785 0.6486 0.5256 -0.1771 -0.0607 -0.0748 187 LYS B C   
3347 O O   . LYS B 152 ? 0.4747 0.7053 0.6090 -0.2051 -0.0517 -0.0813 187 LYS B O   
3348 C CB  . LYS B 152 ? 0.3472 0.7051 0.5839 -0.1992 -0.0337 -0.0701 187 LYS B CB  
3349 C CG  . LYS B 152 ? 0.3081 0.7309 0.6017 -0.1925 -0.0302 -0.0711 187 LYS B CG  
3350 C CD  . LYS B 152 ? 0.4254 0.8521 0.7364 -0.2182 0.0026  -0.0638 187 LYS B CD  
3351 C CE  . LYS B 152 ? 0.5707 1.0502 0.9166 -0.1994 0.0197  -0.0607 187 LYS B CE  
3352 N NZ  . LYS B 152 ? 0.3167 0.8393 0.7137 -0.2211 0.0305  -0.0649 187 LYS B NZ  
3353 N N   . ALA B 153 ? 0.3346 0.5776 0.4455 -0.1464 -0.0655 -0.0672 188 ALA B N   
3354 C CA  . ALA B 153 ? 0.4115 0.5849 0.4697 -0.1432 -0.0583 -0.0673 188 ALA B CA  
3355 C C   . ALA B 153 ? 0.6127 0.7686 0.6460 -0.1637 -0.0752 -0.0872 188 ALA B C   
3356 O O   . ALA B 153 ? 0.3800 0.5732 0.4165 -0.1643 -0.1023 -0.0949 188 ALA B O   
3357 C CB  . ALA B 153 ? 0.3535 0.5124 0.3855 -0.1097 -0.0598 -0.0566 188 ALA B CB  
3358 N N   . PRO B 154 ? 0.4282 0.5259 0.4347 -0.1795 -0.0613 -0.0967 189 PRO B N   
3359 C CA  . PRO B 154 ? 0.5016 0.5803 0.4837 -0.2042 -0.0746 -0.1221 189 PRO B CA  
3360 C C   . PRO B 154 ? 0.6798 0.7521 0.6125 -0.1910 -0.0916 -0.1304 189 PRO B C   
3361 O O   . PRO B 154 ? 0.7817 0.8746 0.7070 -0.1982 -0.1149 -0.1410 189 PRO B O   
3362 C CB  . PRO B 154 ? 0.5555 0.5634 0.5230 -0.2166 -0.0496 -0.1287 189 PRO B CB  
3363 C CG  . PRO B 154 ? 0.5149 0.5015 0.4818 -0.1873 -0.0291 -0.1045 189 PRO B CG  
3364 C CD  . PRO B 154 ? 0.6399 0.6871 0.6414 -0.1763 -0.0339 -0.0855 189 PRO B CD  
3365 N N   . ASP B 155 ? 0.4979 0.5382 0.3990 -0.1651 -0.0775 -0.1201 190 ASP B N   
3366 C CA  . ASP B 155 ? 0.4974 0.5241 0.3439 -0.1573 -0.0866 -0.1270 190 ASP B CA  
3367 C C   . ASP B 155 ? 0.5969 0.6366 0.4386 -0.1268 -0.0867 -0.1027 190 ASP B C   
3368 O O   . ASP B 155 ? 0.4829 0.5411 0.3630 -0.1107 -0.0803 -0.0847 190 ASP B O   
3369 C CB  . ASP B 155 ? 0.6072 0.5729 0.4123 -0.1636 -0.0642 -0.1475 190 ASP B CB  
3370 C CG  . ASP B 155 ? 0.7617 0.6912 0.5871 -0.1472 -0.0337 -0.1376 190 ASP B CG  
3371 O OD1 . ASP B 155 ? 0.6136 0.5625 0.4670 -0.1273 -0.0297 -0.1132 190 ASP B OD1 
3372 O OD2 . ASP B 155 ? 0.8846 0.7652 0.6980 -0.1532 -0.0152 -0.1556 190 ASP B OD2 
3373 N N   . ASP B 156 ? 0.5178 0.5439 0.3072 -0.1211 -0.0923 -0.1034 191 ASP B N   
3374 C CA  . ASP B 156 ? 0.4565 0.4883 0.2373 -0.0967 -0.0934 -0.0800 191 ASP B CA  
3375 C C   . ASP B 156 ? 0.4585 0.4641 0.2526 -0.0807 -0.0625 -0.0718 191 ASP B C   
3376 O O   . ASP B 156 ? 0.4725 0.4902 0.2875 -0.0618 -0.0620 -0.0529 191 ASP B O   
3377 C CB  . ASP B 156 ? 0.6450 0.6627 0.3658 -0.0960 -0.1022 -0.0789 191 ASP B CB  
3378 C CG  . ASP B 156 ? 0.9558 1.0060 0.6807 -0.0929 -0.1372 -0.0727 191 ASP B CG  
3379 O OD1 . ASP B 156 ? 0.9000 0.9888 0.6755 -0.0872 -0.1559 -0.0654 191 ASP B OD1 
3380 O OD2 . ASP B 156 ? 0.8365 0.8761 0.5159 -0.0950 -0.1452 -0.0763 191 ASP B OD2 
3381 N N   . GLU B 157 ? 0.5582 0.5284 0.3433 -0.0869 -0.0383 -0.0874 192 GLU B N   
3382 C CA  . GLU B 157 ? 0.5009 0.4525 0.3061 -0.0702 -0.0133 -0.0799 192 GLU B CA  
3383 C C   . GLU B 157 ? 0.4535 0.4251 0.3086 -0.0609 -0.0151 -0.0645 192 GLU B C   
3384 O O   . GLU B 157 ? 0.3843 0.3648 0.2561 -0.0435 -0.0108 -0.0495 192 GLU B O   
3385 C CB  . GLU B 157 ? 0.5665 0.4782 0.3630 -0.0758 0.0098  -0.1008 192 GLU B CB  
3386 C CG  . GLU B 157 ? 0.5528 0.4501 0.3812 -0.0567 0.0310  -0.0930 192 GLU B CG  
3387 C CD  . GLU B 157 ? 0.9980 0.8560 0.8197 -0.0557 0.0547  -0.1150 192 GLU B CD  
3388 O OE1 . GLU B 157 ? 0.7950 0.6488 0.6092 -0.0448 0.0733  -0.1197 192 GLU B OE1 
3389 O OE2 . GLU B 157 ? 0.7865 0.6173 0.6142 -0.0661 0.0563  -0.1285 192 GLU B OE2 
3390 N N   . SER B 158 ? 0.4042 0.3834 0.2811 -0.0751 -0.0207 -0.0692 193 SER B N   
3391 C CA  . SER B 158 ? 0.4137 0.4131 0.3302 -0.0700 -0.0189 -0.0547 193 SER B CA  
3392 C C   . SER B 158 ? 0.3337 0.3771 0.2676 -0.0582 -0.0338 -0.0428 193 SER B C   
3393 O O   . SER B 158 ? 0.3117 0.3656 0.2644 -0.0431 -0.0278 -0.0308 193 SER B O   
3394 C CB  . SER B 158 ? 0.3645 0.3620 0.2986 -0.0931 -0.0184 -0.0616 193 SER B CB  
3395 O OG  . SER B 158 ? 0.6293 0.6419 0.5546 -0.1133 -0.0353 -0.0776 193 SER B OG  
3396 N N   . LYS B 159 ? 0.3267 0.3955 0.2550 -0.0638 -0.0549 -0.0470 194 LYS B N   
3397 C CA  . LYS B 159 ? 0.3834 0.4892 0.3321 -0.0475 -0.0706 -0.0360 194 LYS B CA  
3398 C C   . LYS B 159 ? 0.2909 0.3781 0.2263 -0.0262 -0.0638 -0.0240 194 LYS B C   
3399 O O   . LYS B 159 ? 0.3303 0.4348 0.2916 -0.0103 -0.0639 -0.0160 194 LYS B O   
3400 C CB  . LYS B 159 ? 0.4213 0.5510 0.3605 -0.0529 -0.0992 -0.0396 194 LYS B CB  
3401 C CG  . LYS B 159 ? 0.3582 0.5336 0.3374 -0.0687 -0.1132 -0.0491 194 LYS B CG  
3402 C CD  . LYS B 159 ? 0.4868 0.6780 0.4460 -0.0812 -0.1436 -0.0578 194 LYS B CD  
3403 C CE  . LYS B 159 ? 0.6288 0.8558 0.6270 -0.1060 -0.1520 -0.0732 194 LYS B CE  
3404 N NZ  . LYS B 159 ? 0.7296 1.0094 0.7961 -0.0972 -0.1501 -0.0675 194 LYS B NZ  
3405 N N   . GLY B 160 ? 0.3080 0.3609 0.2042 -0.0275 -0.0562 -0.0251 195 GLY B N   
3406 C CA  . GLY B 160 ? 0.3200 0.3561 0.2078 -0.0126 -0.0471 -0.0145 195 GLY B CA  
3407 C C   . GLY B 160 ? 0.3558 0.3895 0.2715 -0.0038 -0.0303 -0.0126 195 GLY B C   
3408 O O   . GLY B 160 ? 0.3225 0.3586 0.2504 0.0092  -0.0293 -0.0048 195 GLY B O   
3409 N N   . PHE B 161 ? 0.2953 0.3211 0.2194 -0.0113 -0.0190 -0.0193 196 PHE B N   
3410 C CA  . PHE B 161 ? 0.2361 0.2612 0.1823 -0.0027 -0.0083 -0.0142 196 PHE B CA  
3411 C C   . PHE B 161 ? 0.2844 0.3405 0.2540 0.0040  -0.0154 -0.0084 196 PHE B C   
3412 O O   . PHE B 161 ? 0.2648 0.3259 0.2441 0.0162  -0.0133 -0.0043 196 PHE B O   
3413 C CB  . PHE B 161 ? 0.3066 0.3126 0.2551 -0.0121 0.0014  -0.0181 196 PHE B CB  
3414 C CG  . PHE B 161 ? 0.3289 0.3020 0.2634 -0.0120 0.0140  -0.0269 196 PHE B CG  
3415 C CD1 . PHE B 161 ? 0.3640 0.3317 0.2820 -0.0076 0.0191  -0.0312 196 PHE B CD1 
3416 C CD2 . PHE B 161 ? 0.6589 0.6043 0.5972 -0.0172 0.0229  -0.0316 196 PHE B CD2 
3417 C CE1 . PHE B 161 ? 0.4089 0.3520 0.3172 -0.0075 0.0356  -0.0432 196 PHE B CE1 
3418 C CE2 . PHE B 161 ? 0.5586 0.4740 0.4898 -0.0139 0.0366  -0.0440 196 PHE B CE2 
3419 C CZ  . PHE B 161 ? 0.4641 0.3821 0.3814 -0.0088 0.0443  -0.0516 196 PHE B CZ  
3420 N N   . PHE B 162 ? 0.2490 0.3293 0.2304 -0.0051 -0.0229 -0.0112 197 PHE B N   
3421 C CA  . PHE B 162 ? 0.2341 0.3499 0.2419 0.0017  -0.0253 -0.0098 197 PHE B CA  
3422 C C   . PHE B 162 ? 0.2249 0.3479 0.2385 0.0203  -0.0347 -0.0086 197 PHE B C   
3423 O O   . PHE B 162 ? 0.2350 0.3675 0.2611 0.0319  -0.0301 -0.0094 197 PHE B O   
3424 C CB  . PHE B 162 ? 0.2506 0.3997 0.2797 -0.0121 -0.0312 -0.0151 197 PHE B CB  
3425 C CG  . PHE B 162 ? 0.2480 0.3905 0.2785 -0.0327 -0.0185 -0.0148 197 PHE B CG  
3426 C CD1 . PHE B 162 ? 0.2189 0.3715 0.2577 -0.0344 -0.0039 -0.0083 197 PHE B CD1 
3427 C CD2 . PHE B 162 ? 0.2639 0.3868 0.2837 -0.0521 -0.0211 -0.0210 197 PHE B CD2 
3428 C CE1 . PHE B 162 ? 0.2673 0.4066 0.3035 -0.0552 0.0082  -0.0029 197 PHE B CE1 
3429 C CE2 . PHE B 162 ? 0.2721 0.3799 0.2945 -0.0726 -0.0092 -0.0198 197 PHE B CE2 
3430 C CZ  . PHE B 162 ? 0.2927 0.4073 0.3237 -0.0743 0.0055  -0.0082 197 PHE B CZ  
3431 N N   . LYS B 163 ? 0.2474 0.3621 0.2481 0.0223  -0.0483 -0.0066 198 LYS B N   
3432 C CA  . LYS B 163 ? 0.2409 0.3535 0.2461 0.0396  -0.0590 -0.0016 198 LYS B CA  
3433 C C   . LYS B 163 ? 0.2831 0.3685 0.2797 0.0464  -0.0479 0.0012  198 LYS B C   
3434 O O   . LYS B 163 ? 0.2788 0.3657 0.2914 0.0598  -0.0498 -0.0001 198 LYS B O   
3435 C CB  . LYS B 163 ? 0.2361 0.3383 0.2182 0.0383  -0.0771 0.0055  198 LYS B CB  
3436 C CG  . LYS B 163 ? 0.2952 0.4343 0.2966 0.0362  -0.0970 0.0023  198 LYS B CG  
3437 C CD  . LYS B 163 ? 0.4765 0.6017 0.4397 0.0299  -0.1168 0.0093  198 LYS B CD  
3438 C CE  . LYS B 163 ? 0.5442 0.7117 0.5282 0.0244  -0.1412 0.0038  198 LYS B CE  
3439 N NZ  . LYS B 163 ? 0.5904 0.7441 0.5269 0.0171  -0.1643 0.0105  198 LYS B NZ  
3440 N N   . GLY B 164 ? 0.2828 0.3449 0.2587 0.0371  -0.0363 0.0022  199 GLY B N   
3441 C CA  . GLY B 164 ? 0.2745 0.3202 0.2517 0.0411  -0.0265 0.0029  199 GLY B CA  
3442 C C   . GLY B 164 ? 0.2366 0.2981 0.2339 0.0470  -0.0223 -0.0027 199 GLY B C   
3443 O O   . GLY B 164 ? 0.2666 0.3250 0.2733 0.0539  -0.0227 -0.0057 199 GLY B O   
3444 N N   . ALA B 165 ? 0.2503 0.3264 0.2506 0.0419  -0.0183 -0.0041 200 ALA B N   
3445 C CA  . ALA B 165 ? 0.2172 0.3083 0.2253 0.0458  -0.0145 -0.0067 200 ALA B CA  
3446 C C   . ALA B 165 ? 0.2439 0.3551 0.2659 0.0556  -0.0181 -0.0151 200 ALA B C   
3447 O O   . ALA B 165 ? 0.2330 0.3468 0.2567 0.0620  -0.0171 -0.0222 200 ALA B O   
3448 C CB  . ALA B 165 ? 0.2459 0.3441 0.2494 0.0359  -0.0082 -0.0022 200 ALA B CB  
3449 N N   . MET B 166 ? 0.2216 0.3489 0.2562 0.0577  -0.0232 -0.0168 201 MET B N   
3450 C CA  . MET B 166 ? 0.1949 0.3431 0.2516 0.0715  -0.0255 -0.0274 201 MET B CA  
3451 C C   . MET B 166 ? 0.1984 0.3205 0.2572 0.0841  -0.0326 -0.0300 201 MET B C   
3452 O O   . MET B 166 ? 0.2716 0.3957 0.3391 0.0934  -0.0293 -0.0430 201 MET B O   
3453 C CB  . MET B 166 ? 0.2188 0.3961 0.2987 0.0731  -0.0325 -0.0282 201 MET B CB  
3454 C CG  . MET B 166 ? 0.2508 0.4522 0.3324 0.0552  -0.0239 -0.0266 201 MET B CG  
3455 S SD  . MET B 166 ? 0.2825 0.5210 0.3952 0.0508  -0.0369 -0.0284 201 MET B SD  
3456 C CE  . MET B 166 ? 0.2807 0.5485 0.4014 0.0261  -0.0173 -0.0303 201 MET B CE  
3457 N N   . ALA B 167 ? 0.2070 0.3008 0.2538 0.0819  -0.0406 -0.0184 202 ALA B N   
3458 C CA  . ALA B 167 ? 0.2817 0.3437 0.3286 0.0896  -0.0457 -0.0168 202 ALA B CA  
3459 C C   . ALA B 167 ? 0.2580 0.3082 0.3027 0.0847  -0.0374 -0.0252 202 ALA B C   
3460 O O   . ALA B 167 ? 0.2912 0.3235 0.3458 0.0912  -0.0395 -0.0335 202 ALA B O   
3461 C CB  . ALA B 167 ? 0.2752 0.3091 0.2999 0.0830  -0.0522 0.0006  202 ALA B CB  
3462 N N   . SER B 168 ? 0.2306 0.2900 0.2653 0.0737  -0.0300 -0.0240 203 SER B N   
3463 C CA  . SER B 168 ? 0.2447 0.2997 0.2810 0.0691  -0.0271 -0.0307 203 SER B CA  
3464 C C   . SER B 168 ? 0.2831 0.3594 0.3209 0.0736  -0.0271 -0.0458 203 SER B C   
3465 O O   . SER B 168 ? 0.2751 0.3462 0.3172 0.0732  -0.0301 -0.0583 203 SER B O   
3466 C CB  . SER B 168 ? 0.2327 0.2888 0.2625 0.0595  -0.0218 -0.0221 203 SER B CB  
3467 O OG  . SER B 168 ? 0.2583 0.2966 0.2798 0.0536  -0.0177 -0.0118 203 SER B OG  
3468 N N   . LEU B 169 ? 0.2538 0.3545 0.2851 0.0750  -0.0228 -0.0456 204 LEU B N   
3469 C CA  . LEU B 169 ? 0.2338 0.3552 0.2554 0.0764  -0.0195 -0.0582 204 LEU B CA  
3470 C C   . LEU B 169 ? 0.1810 0.3155 0.2135 0.0874  -0.0146 -0.0768 204 LEU B C   
3471 O O   . LEU B 169 ? 0.2454 0.3865 0.2690 0.0899  -0.0124 -0.0955 204 LEU B O   
3472 C CB  . LEU B 169 ? 0.2766 0.4158 0.2801 0.0687  -0.0134 -0.0466 204 LEU B CB  
3473 C CG  . LEU B 169 ? 0.6705 0.8029 0.6588 0.0632  -0.0194 -0.0360 204 LEU B CG  
3474 C CD1 . LEU B 169 ? 0.4685 0.5829 0.4655 0.0597  -0.0204 -0.0208 204 LEU B CD1 
3475 C CD2 . LEU B 169 ? 0.4840 0.6327 0.4446 0.0588  -0.0153 -0.0305 204 LEU B CD2 
3476 N N   . ASN B 170 ? 0.1958 0.3377 0.2483 0.0948  -0.0135 -0.0744 205 ASN B N   
3477 C CA  . ASN B 170 ? 0.2306 0.3923 0.3036 0.1091  -0.0073 -0.0938 205 ASN B CA  
3478 C C   . ASN B 170 ? 0.3162 0.4533 0.3953 0.1195  -0.0102 -0.1142 205 ASN B C   
3479 O O   . ASN B 170 ? 0.2777 0.4279 0.3568 0.1226  -0.0008 -0.1333 205 ASN B O   
3480 C CB  . ASN B 170 ? 0.2796 0.4527 0.3792 0.1146  -0.0114 -0.0847 205 ASN B CB  
3481 C CG  . ASN B 170 ? 0.3382 0.5506 0.4399 0.1035  -0.0021 -0.0780 205 ASN B CG  
3482 O OD1 . ASN B 170 ? 0.3553 0.5856 0.4375 0.0930  0.0113  -0.0802 205 ASN B OD1 
3483 N ND2 . ASN B 170 ? 0.2714 0.4944 0.3936 0.1027  -0.0101 -0.0683 205 ASN B ND2 
3484 N N   . PRO B 171 ? 0.2616 0.3590 0.3440 0.1202  -0.0213 -0.1097 206 PRO B N   
3485 C CA  . PRO B 171 ? 0.2693 0.3388 0.3582 0.1260  -0.0232 -0.1316 206 PRO B CA  
3486 C C   . PRO B 171 ? 0.3316 0.4140 0.3981 0.1178  -0.0187 -0.1544 206 PRO B C   
3487 O O   . PRO B 171 ? 0.3576 0.4305 0.4253 0.1203  -0.0158 -0.1769 206 PRO B O   
3488 C CB  . PRO B 171 ? 0.2820 0.3069 0.3744 0.1197  -0.0337 -0.1160 206 PRO B CB  
3489 C CG  . PRO B 171 ? 0.2498 0.2785 0.3408 0.1187  -0.0375 -0.0876 206 PRO B CG  
3490 C CD  . PRO B 171 ? 0.2508 0.3234 0.3311 0.1131  -0.0304 -0.0844 206 PRO B CD  
3491 N N   . TYR B 172 ? 0.2754 0.3751 0.3174 0.1026  -0.0204 -0.1414 207 TYR B N   
3492 C CA  . TYR B 172 ? 0.2831 0.3986 0.2966 0.0944  -0.0211 -0.1580 207 TYR B CA  
3493 C C   . TYR B 172 ? 0.3286 0.4788 0.3222 0.0987  -0.0057 -0.1702 207 TYR B C   
3494 O O   . TYR B 172 ? 0.3376 0.4923 0.3119 0.0944  -0.0028 -0.1888 207 TYR B O   
3495 C CB  . TYR B 172 ? 0.2997 0.4218 0.2978 0.0806  -0.0310 -0.1363 207 TYR B CB  
3496 C CG  . TYR B 172 ? 0.2414 0.3389 0.2597 0.0729  -0.0427 -0.1323 207 TYR B CG  
3497 C CD1 . TYR B 172 ? 0.2477 0.3259 0.2862 0.0721  -0.0410 -0.1118 207 TYR B CD1 
3498 C CD2 . TYR B 172 ? 0.2760 0.3727 0.2926 0.0638  -0.0546 -0.1500 207 TYR B CD2 
3499 C CE1 . TYR B 172 ? 0.2601 0.3188 0.3167 0.0620  -0.0461 -0.1079 207 TYR B CE1 
3500 C CE2 . TYR B 172 ? 0.3137 0.3939 0.3567 0.0531  -0.0623 -0.1471 207 TYR B CE2 
3501 C CZ  . TYR B 172 ? 0.2725 0.3337 0.3356 0.0520  -0.0556 -0.1252 207 TYR B CZ  
3502 O OH  . TYR B 172 ? 0.2777 0.3254 0.3662 0.0383  -0.0578 -0.1220 207 TYR B OH  
3503 N N   . VAL B 173 ? 0.2917 0.4636 0.2921 0.1003  0.0045  -0.1525 208 VAL B N   
3504 C CA  . VAL B 173 ? 0.3361 0.5379 0.3264 0.0970  0.0218  -0.1561 208 VAL B CA  
3505 C C   . VAL B 173 ? 0.3039 0.5003 0.3159 0.1072  0.0293  -0.1798 208 VAL B C   
3506 O O   . VAL B 173 ? 0.3427 0.5510 0.3346 0.1038  0.0412  -0.1966 208 VAL B O   
3507 C CB  . VAL B 173 ? 0.2457 0.4703 0.2506 0.0940  0.0303  -0.1350 208 VAL B CB  
3508 C CG1 . VAL B 173 ? 0.2792 0.5346 0.2829 0.0886  0.0507  -0.1408 208 VAL B CG1 
3509 C CG2 . VAL B 173 ? 0.2751 0.4971 0.2551 0.0815  0.0246  -0.1094 208 VAL B CG2 
3510 N N   . LYS B 174 ? 0.2997 0.4738 0.3497 0.1202  0.0221  -0.1797 209 LYS B N   
3511 C CA  . LYS B 174 ? 0.3522 0.5163 0.4274 0.1336  0.0282  -0.1991 209 LYS B CA  
3512 C C   . LYS B 174 ? 0.3725 0.5126 0.4297 0.1318  0.0272  -0.2250 209 LYS B C   
3513 O O   . LYS B 174 ? 0.4151 0.5583 0.4749 0.1382  0.0399  -0.2475 209 LYS B O   
3514 C CB  . LYS B 174 ? 0.3909 0.5275 0.5031 0.1471  0.0158  -0.1863 209 LYS B CB  
3515 C CG  . LYS B 174 ? 0.5694 0.7330 0.7068 0.1517  0.0166  -0.1676 209 LYS B CG  
3516 C CD  . LYS B 174 ? 0.7623 0.8963 0.9284 0.1656  0.0009  -0.1532 209 LYS B CD  
3517 C CE  . LYS B 174 ? 0.5003 0.6585 0.6819 0.1644  -0.0062 -0.1301 209 LYS B CE  
3518 N NZ  . LYS B 174 ? 0.4792 0.6800 0.6483 0.1486  0.0051  -0.1275 209 LYS B NZ  
3519 N N   . ALA B 175 ? 0.3081 0.4112 0.4283 0.1441  -0.0155 -0.1853 210 ALA B N   
3520 C CA  . ALA B 175 ? 0.3971 0.4888 0.5136 0.1431  -0.0152 -0.1979 210 ALA B CA  
3521 C C   . ALA B 175 ? 0.3773 0.4963 0.4845 0.1407  -0.0139 -0.2081 210 ALA B C   
3522 O O   . ALA B 175 ? 0.3563 0.4701 0.4600 0.1393  -0.0143 -0.2196 210 ALA B O   
3523 C CB  . ALA B 175 ? 0.3439 0.4036 0.4578 0.1339  -0.0191 -0.1923 210 ALA B CB  
3524 N N   . GLY B 176 ? 0.3339 0.4830 0.4370 0.1400  -0.0120 -0.2037 211 GLY B N   
3525 C CA  . GLY B 176 ? 0.3211 0.4982 0.4137 0.1377  -0.0099 -0.2107 211 GLY B CA  
3526 C C   . GLY B 176 ? 0.4218 0.5931 0.5048 0.1273  -0.0137 -0.2079 211 GLY B C   
3527 O O   . GLY B 176 ? 0.3545 0.5440 0.4287 0.1256  -0.0131 -0.2154 211 GLY B O   
3528 N N   . LYS B 177 ? 0.3486 0.4961 0.4331 0.1205  -0.0176 -0.1970 212 LYS B N   
3529 C CA  . LYS B 177 ? 0.2733 0.4120 0.3503 0.1109  -0.0210 -0.1936 212 LYS B CA  
3530 C C   . LYS B 177 ? 0.2889 0.4379 0.3604 0.1051  -0.0205 -0.1807 212 LYS B C   
3531 O O   . LYS B 177 ? 0.3478 0.4832 0.4149 0.0975  -0.0234 -0.1749 212 LYS B O   
3532 C CB  . LYS B 177 ? 0.2879 0.3894 0.3698 0.1066  -0.0250 -0.1915 212 LYS B CB  
3533 C CG  . LYS B 177 ? 0.4397 0.5290 0.5265 0.1106  -0.0248 -0.2043 212 LYS B CG  
3534 C CD  . LYS B 177 ? 0.5352 0.5881 0.6286 0.1078  -0.0265 -0.1980 212 LYS B CD  
3535 C CE  . LYS B 177 ? 0.3526 0.3915 0.4482 0.1066  -0.0268 -0.2097 212 LYS B CE  
3536 N NZ  . LYS B 177 ? 0.7249 0.7307 0.8276 0.1066  -0.0261 -0.2042 212 LYS B NZ  
3537 N N   . PHE B 178 ? 0.2531 0.4260 0.3256 0.1084  -0.0163 -0.1757 213 PHE B N   
3538 C CA  . PHE B 178 ? 0.2719 0.4587 0.3393 0.1025  -0.0140 -0.1639 213 PHE B CA  
3539 C C   . PHE B 178 ? 0.2320 0.4565 0.2904 0.1028  -0.0081 -0.1647 213 PHE B C   
3540 O O   . PHE B 178 ? 0.2706 0.5173 0.3314 0.1088  -0.0040 -0.1686 213 PHE B O   
3541 C CB  . PHE B 178 ? 0.2464 0.4334 0.3236 0.1035  -0.0129 -0.1538 213 PHE B CB  
3542 C CG  . PHE B 178 ? 0.2401 0.4421 0.3149 0.0967  -0.0096 -0.1414 213 PHE B CG  
3543 C CD1 . PHE B 178 ? 0.2141 0.3995 0.2825 0.0895  -0.0119 -0.1363 213 PHE B CD1 
3544 C CD2 . PHE B 178 ? 0.3440 0.5768 0.4240 0.0964  -0.0036 -0.1337 213 PHE B CD2 
3545 C CE1 . PHE B 178 ? 0.2284 0.4252 0.2951 0.0817  -0.0084 -0.1225 213 PHE B CE1 
3546 C CE2 . PHE B 178 ? 0.3144 0.5614 0.3951 0.0880  0.0002  -0.1200 213 PHE B CE2 
3547 C CZ  . PHE B 178 ? 0.2901 0.5158 0.3627 0.0794  -0.0027 -0.1130 213 PHE B CZ  
3548 N N   . LYS B 179 ? 0.2462 0.4778 0.2936 0.0964  -0.0075 -0.1597 214 LYS B N   
3549 C CA  . LYS B 179 ? 0.2290 0.4951 0.2654 0.0957  -0.0023 -0.1576 214 LYS B CA  
3550 C C   . LYS B 179 ? 0.2043 0.4809 0.2351 0.0881  0.0022  -0.1407 214 LYS B C   
3551 O O   . LYS B 179 ? 0.2351 0.5023 0.2577 0.0827  0.0001  -0.1367 214 LYS B O   
3552 C CB  . LYS B 179 ? 0.2700 0.5365 0.2979 0.0960  -0.0061 -0.1683 214 LYS B CB  
3553 C CG  . LYS B 179 ? 0.3536 0.6566 0.3698 0.0966  -0.0016 -0.1663 214 LYS B CG  
3554 C CD  . LYS B 179 ? 0.5399 0.8443 0.5504 0.0976  -0.0062 -0.1787 214 LYS B CD  
3555 C CE  . LYS B 179 ? 0.4457 0.7873 0.4440 0.0989  -0.0023 -0.1758 214 LYS B CE  
3556 N NZ  . LYS B 179 ? 0.5433 0.8884 0.5371 0.0999  -0.0071 -0.1888 214 LYS B NZ  
3557 N N   . PRO B 180 ? 0.2154 0.5111 0.2517 0.0866  0.0086  -0.1292 215 PRO B N   
3558 C CA  . PRO B 180 ? 0.1954 0.5002 0.2297 0.0776  0.0139  -0.1107 215 PRO B CA  
3559 C C   . PRO B 180 ? 0.2325 0.5599 0.2513 0.0744  0.0181  -0.1027 215 PRO B C   
3560 O O   . PRO B 180 ? 0.2387 0.5818 0.2497 0.0795  0.0176  -0.1111 215 PRO B O   
3561 C CB  . PRO B 180 ? 0.2325 0.5528 0.2806 0.0760  0.0190  -0.1013 215 PRO B CB  
3562 C CG  . PRO B 180 ? 0.3008 0.6342 0.3507 0.0850  0.0193  -0.1133 215 PRO B CG  
3563 C CD  . PRO B 180 ? 0.2715 0.5809 0.3185 0.0921  0.0116  -0.1314 215 PRO B CD  
3564 N N   . PHE B 181 ? 0.1801 0.5079 0.1951 0.0658  0.0219  -0.0854 216 PHE B N   
3565 C CA  . PHE B 181 ? 0.2500 0.5994 0.2525 0.0616  0.0271  -0.0706 216 PHE B CA  
3566 C C   . PHE B 181 ? 0.2714 0.6273 0.2821 0.0518  0.0349  -0.0483 216 PHE B C   
3567 O O   . PHE B 181 ? 0.2267 0.5682 0.2520 0.0473  0.0340  -0.0456 216 PHE B O   
3568 C CB  . PHE B 181 ? 0.2188 0.5574 0.2079 0.0597  0.0231  -0.0693 216 PHE B CB  
3569 C CG  . PHE B 181 ? 0.1807 0.4816 0.1746 0.0522  0.0178  -0.0627 216 PHE B CG  
3570 C CD1 . PHE B 181 ? 0.2793 0.5692 0.2764 0.0416  0.0212  -0.0402 216 PHE B CD1 
3571 C CD2 . PHE B 181 ? 0.2111 0.4831 0.2072 0.0548  0.0088  -0.0780 216 PHE B CD2 
3572 C CE1 . PHE B 181 ? 0.2300 0.4824 0.2311 0.0345  0.0157  -0.0343 216 PHE B CE1 
3573 C CE2 . PHE B 181 ? 0.2126 0.4478 0.2130 0.0475  0.0035  -0.0703 216 PHE B CE2 
3574 C CZ  . PHE B 181 ? 0.2241 0.4501 0.2263 0.0377  0.0069  -0.0491 216 PHE B CZ  
3575 N N   . SER B 182 ? 0.2025 0.5743 0.2048 0.0472  0.0403  -0.0311 217 SER B N   
3576 C CA  . SER B 182 ? 0.2604 0.6338 0.2712 0.0364  0.0475  -0.0090 217 SER B CA  
3577 C C   . SER B 182 ? 0.2453 0.6124 0.2456 0.0303  0.0495  0.0101  217 SER B C   
3578 O O   . SER B 182 ? 0.3419 0.7250 0.3304 0.0342  0.0503  0.0144  217 SER B O   
3579 C CB  . SER B 182 ? 0.3088 0.7073 0.3247 0.0372  0.0533  -0.0050 217 SER B CB  
3580 O OG  . SER B 182 ? 0.3641 0.7600 0.3914 0.0256  0.0595  0.0142  217 SER B OG  
3581 N N   . GLY B 183 ? 0.2661 0.6094 0.2718 0.0213  0.0500  0.0216  218 GLY B N   
3582 C CA  . GLY B 183 ? 0.3406 0.6716 0.3383 0.0158  0.0516  0.0406  218 GLY B CA  
3583 C C   . GLY B 183 ? 0.2555 0.5865 0.2372 0.0232  0.0458  0.0340  218 GLY B C   
3584 O O   . GLY B 183 ? 0.3093 0.6404 0.2866 0.0303  0.0399  0.0136  218 GLY B O   
3585 N N   . ASN B 184 ? 0.2652 0.5946 0.2398 0.0216  0.0470  0.0509  219 ASN B N   
3586 C CA  . ASN B 184 ? 0.2390 0.5705 0.2008 0.0277  0.0410  0.0472  219 ASN B CA  
3587 C C   . ASN B 184 ? 0.3270 0.6854 0.2812 0.0377  0.0367  0.0276  219 ASN B C   
3588 O O   . ASN B 184 ? 0.2829 0.6658 0.2365 0.0409  0.0401  0.0294  219 ASN B O   
3589 C CB  . ASN B 184 ? 0.2882 0.6186 0.2476 0.0258  0.0436  0.0692  219 ASN B CB  
3590 C CG  . ASN B 184 ? 0.3396 0.6372 0.3074 0.0164  0.0468  0.0863  219 ASN B CG  
3591 O OD1 . ASN B 184 ? 0.3007 0.5761 0.2745 0.0109  0.0460  0.0821  219 ASN B OD1 
3592 N ND2 . ASN B 184 ? 0.3756 0.6690 0.3447 0.0149  0.0503  0.1046  219 ASN B ND2 
3593 N N   . THR B 185 ? 0.2426 0.5946 0.1919 0.0424  0.0289  0.0082  220 THR B N   
3594 C CA  . THR B 185 ? 0.2700 0.6403 0.2157 0.0510  0.0238  -0.0143 220 THR B CA  
3595 C C   . THR B 185 ? 0.2341 0.5953 0.1741 0.0536  0.0149  -0.0270 220 THR B C   
3596 O O   . THR B 185 ? 0.2532 0.5879 0.1944 0.0505  0.0109  -0.0311 220 THR B O   
3597 C CB  . THR B 185 ? 0.2803 0.6450 0.2347 0.0535  0.0234  -0.0329 220 THR B CB  
3598 O OG1 . THR B 185 ? 0.3482 0.7212 0.3108 0.0500  0.0314  -0.0213 220 THR B OG1 
3599 C CG2 . THR B 185 ? 0.3274 0.7074 0.2802 0.0622  0.0182  -0.0557 220 THR B CG2 
3600 N N   . ASP B 186 ? 0.2350 0.6187 0.1698 0.0590  0.0116  -0.0335 221 ASP B N   
3601 C CA  . ASP B 186 ? 0.2586 0.6362 0.1920 0.0614  0.0030  -0.0508 221 ASP B CA  
3602 C C   . ASP B 186 ? 0.2424 0.6056 0.1833 0.0640  -0.0014 -0.0761 221 ASP B C   
3603 O O   . ASP B 186 ? 0.2611 0.6385 0.2050 0.0687  0.0005  -0.0864 221 ASP B O   
3604 C CB  . ASP B 186 ? 0.3150 0.7237 0.2425 0.0667  0.0016  -0.0533 221 ASP B CB  
3605 C CG  . ASP B 186 ? 0.3626 0.7831 0.2843 0.0653  0.0046  -0.0290 221 ASP B CG  
3606 O OD1 . ASP B 186 ? 0.3626 0.7664 0.2858 0.0600  0.0086  -0.0090 221 ASP B OD1 
3607 O OD2 . ASP B 186 ? 0.3422 0.7890 0.2588 0.0699  0.0033  -0.0297 221 ASP B OD2 
3608 N N   . LEU B 187 ? 0.2834 0.6168 0.2286 0.0611  -0.0071 -0.0845 222 LEU B N   
3609 C CA  . LEU B 187 ? 0.2183 0.5318 0.1733 0.0631  -0.0126 -0.1073 222 LEU B CA  
3610 C C   . LEU B 187 ? 0.4523 0.7695 0.4077 0.0644  -0.0190 -0.1206 222 LEU B C   
3611 O O   . LEU B 187 ? 0.6992 1.0437 0.6470 0.0663  -0.0182 -0.1162 222 LEU B O   
3612 C CB  . LEU B 187 ? 0.2355 0.5134 0.1964 0.0587  -0.0145 -0.1063 222 LEU B CB  
3613 C CG  . LEU B 187 ? 0.2474 0.5274 0.2069 0.0568  -0.0069 -0.0916 222 LEU B CG  
3614 C CD1 . LEU B 187 ? 0.2509 0.4916 0.2202 0.0504  -0.0095 -0.0850 222 LEU B CD1 
3615 C CD2 . LEU B 187 ? 0.2292 0.5253 0.1952 0.0622  -0.0024 -0.0992 222 LEU B CD2 
3616 N N   . VAL B 188 ? 0.2946 0.5858 0.2600 0.0634  -0.0248 -0.1367 223 VAL B N   
3617 C CA  . VAL B 188 ? 0.4106 0.7038 0.3784 0.0633  -0.0304 -0.1498 223 VAL B CA  
3618 C C   . VAL B 188 ? 0.3241 0.6320 0.2824 0.0606  -0.0315 -0.1375 223 VAL B C   
3619 O O   . VAL B 188 ? 0.3612 0.6624 0.3145 0.0570  -0.0297 -0.1193 223 VAL B O   
3620 C CB  . VAL B 188 ? 0.3243 0.5813 0.3054 0.0600  -0.0357 -0.1621 223 VAL B CB  
3621 C CG1 . VAL B 188 ? 0.4454 0.6880 0.4364 0.0635  -0.0344 -0.1716 223 VAL B CG1 
3622 C CG2 . VAL B 188 ? 0.3727 0.6031 0.3548 0.0534  -0.0376 -0.1500 223 VAL B CG2 
3623 N N   . PRO B 189 ? 0.3584 0.6875 0.3139 0.0625  -0.0344 -0.1461 224 PRO B N   
3624 C CA  . PRO B 189 ? 0.2613 0.6067 0.2085 0.0608  -0.0357 -0.1335 224 PRO B CA  
3625 C C   . PRO B 189 ? 0.2719 0.5909 0.2216 0.0545  -0.0388 -0.1233 224 PRO B C   
3626 O O   . PRO B 189 ? 0.3419 0.6346 0.3014 0.0505  -0.0437 -0.1345 224 PRO B O   
3627 C CB  . PRO B 189 ? 0.3587 0.7218 0.3067 0.0628  -0.0405 -0.1514 224 PRO B CB  
3628 C CG  . PRO B 189 ? 0.4622 0.8336 0.4133 0.0680  -0.0386 -0.1672 224 PRO B CG  
3629 C CD  . PRO B 189 ? 0.3913 0.7318 0.3510 0.0666  -0.0367 -0.1674 224 PRO B CD  
3630 N N   . GLY B 190 ? 0.2382 0.5635 0.1803 0.0535  -0.0355 -0.1006 225 GLY B N   
3631 C CA  . GLY B 190 ? 0.3020 0.6049 0.2457 0.0482  -0.0380 -0.0881 225 GLY B CA  
3632 C C   . GLY B 190 ? 0.2847 0.5625 0.2299 0.0452  -0.0352 -0.0777 225 GLY B C   
3633 O O   . GLY B 190 ? 0.2265 0.4865 0.1729 0.0411  -0.0372 -0.0655 225 GLY B O   
3634 N N   . ILE B 191 ? 0.2258 0.5022 0.1717 0.0472  -0.0310 -0.0824 226 ILE B N   
3635 C CA  . ILE B 191 ? 0.2334 0.4887 0.1804 0.0443  -0.0284 -0.0735 226 ILE B CA  
3636 C C   . ILE B 191 ? 0.2780 0.5537 0.2193 0.0471  -0.0199 -0.0634 226 ILE B C   
3637 O O   . ILE B 191 ? 0.2525 0.5470 0.1948 0.0519  -0.0177 -0.0747 226 ILE B O   
3638 C CB  . ILE B 191 ? 0.2344 0.4591 0.1928 0.0429  -0.0323 -0.0912 226 ILE B CB  
3639 C CG1 . ILE B 191 ? 0.2457 0.4511 0.2127 0.0397  -0.0394 -0.1015 226 ILE B CG1 
3640 C CG2 . ILE B 191 ? 0.2199 0.4183 0.1832 0.0389  -0.0291 -0.0783 226 ILE B CG2 
3641 C CD1 . ILE B 191 ? 0.3049 0.4787 0.2857 0.0385  -0.0417 -0.1159 226 ILE B CD1 
3642 N N   . LYS B 192 ? 0.2316 0.5020 0.1691 0.0436  -0.0147 -0.0415 227 LYS B N   
3643 C CA  . LYS B 192 ? 0.2389 0.5263 0.1738 0.0442  -0.0050 -0.0278 227 LYS B CA  
3644 C C   . LYS B 192 ? 0.2313 0.4869 0.1793 0.0377  -0.0013 -0.0193 227 LYS B C   
3645 O O   . LYS B 192 ? 0.2087 0.4318 0.1636 0.0325  -0.0042 -0.0138 227 LYS B O   
3646 C CB  . LYS B 192 ? 0.3423 0.6453 0.2727 0.0436  0.0001  -0.0034 227 LYS B CB  
3647 C CG  . LYS B 192 ? 0.4695 0.8037 0.3968 0.0495  -0.0012 -0.0087 227 LYS B CG  
3648 C CD  . LYS B 192 ? 0.6613 1.0066 0.5861 0.0498  0.0015  0.0135  227 LYS B CD  
3649 C CE  . LYS B 192 ? 0.5112 0.8846 0.4319 0.0556  -0.0027 0.0040  227 LYS B CE  
3650 N NZ  . LYS B 192 ? 0.5473 0.9093 0.4689 0.0548  -0.0113 -0.0092 227 LYS B NZ  
3651 N N   . ALA B 193 ? 0.2537 0.5203 0.2052 0.0383  0.0048  -0.0192 228 ALA B N   
3652 C CA  . ALA B 193 ? 0.2249 0.4689 0.1881 0.0316  0.0089  -0.0089 228 ALA B CA  
3653 C C   . ALA B 193 ? 0.2224 0.4743 0.1840 0.0264  0.0178  0.0171  228 ALA B C   
3654 O O   . ALA B 193 ? 0.2847 0.5694 0.2385 0.0296  0.0240  0.0250  228 ALA B O   
3655 C CB  . ALA B 193 ? 0.2489 0.5030 0.2194 0.0346  0.0110  -0.0217 228 ALA B CB  
3656 N N   . LEU B 194 ? 0.1982 0.4193 0.1669 0.0186  0.0187  0.0303  229 LEU B N   
3657 C CA  . LEU B 194 ? 0.2446 0.4643 0.2152 0.0123  0.0273  0.0546  229 LEU B CA  
3658 C C   . LEU B 194 ? 0.2702 0.4700 0.2543 0.0042  0.0299  0.0563  229 LEU B C   
3659 O O   . LEU B 194 ? 0.2289 0.3973 0.2188 0.0006  0.0246  0.0505  229 LEU B O   
3660 C CB  . LEU B 194 ? 0.2193 0.4177 0.1869 0.0105  0.0258  0.0672  229 LEU B CB  
3661 C CG  . LEU B 194 ? 0.3244 0.5207 0.2930 0.0065  0.0343  0.0926  229 LEU B CG  
3662 C CD1 . LEU B 194 ? 0.3336 0.5594 0.2981 0.0125  0.0362  0.0977  229 LEU B CD1 
3663 C CD2 . LEU B 194 ? 0.3456 0.5121 0.3157 0.0054  0.0313  0.1000  229 LEU B CD2 
3664 N N   . ALA B 195 ? 0.2619 0.4818 0.2512 0.0011  0.0379  0.0643  230 ALA B N   
3665 C CA  . ALA B 195 ? 0.2802 0.4851 0.2836 -0.0077 0.0401  0.0662  230 ALA B CA  
3666 C C   . ALA B 195 ? 0.2043 0.3743 0.2118 -0.0165 0.0409  0.0791  230 ALA B C   
3667 O O   . ALA B 195 ? 0.2490 0.4169 0.2526 -0.0182 0.0464  0.0966  230 ALA B O   
3668 C CB  . ALA B 195 ? 0.2342 0.4692 0.2438 -0.0108 0.0500  0.0762  230 ALA B CB  
3669 N N   . SER B 196 ? 0.2376 0.3803 0.2524 -0.0211 0.0353  0.0703  231 SER B N   
3670 C CA  . SER B 196 ? 0.2183 0.3270 0.2374 -0.0298 0.0361  0.0792  231 SER B CA  
3671 C C   . SER B 196 ? 0.2650 0.3628 0.2961 -0.0377 0.0343  0.0729  231 SER B C   
3672 O O   . SER B 196 ? 0.2332 0.3039 0.2654 -0.0401 0.0284  0.0657  231 SER B O   
3673 C CB  . SER B 196 ? 0.2241 0.3066 0.2356 -0.0260 0.0298  0.0753  231 SER B CB  
3674 O OG  . SER B 196 ? 0.2141 0.2928 0.2237 -0.0201 0.0209  0.0567  231 SER B OG  
3675 N N   . HIS B 197 ? 0.2495 0.3719 0.2899 -0.0413 0.0392  0.0749  232 HIS B N   
3676 C CA  . HIS B 197 ? 0.2664 0.3876 0.3192 -0.0473 0.0362  0.0666  232 HIS B CA  
3677 C C   . HIS B 197 ? 0.2793 0.3709 0.3389 -0.0596 0.0368  0.0725  232 HIS B C   
3678 O O   . HIS B 197 ? 0.2903 0.3675 0.3483 -0.0642 0.0428  0.0842  232 HIS B O   
3679 C CB  . HIS B 197 ? 0.2347 0.3916 0.2982 -0.0495 0.0428  0.0699  232 HIS B CB  
3680 C CG  . HIS B 197 ? 0.2319 0.4210 0.2887 -0.0376 0.0437  0.0636  232 HIS B CG  
3681 N ND1 . HIS B 197 ? 0.2570 0.4429 0.3025 -0.0261 0.0366  0.0503  232 HIS B ND1 
3682 C CD2 . HIS B 197 ? 0.2037 0.4296 0.2640 -0.0355 0.0513  0.0678  232 HIS B CD2 
3683 C CE1 . HIS B 197 ? 0.2168 0.4351 0.2583 -0.0174 0.0394  0.0454  232 HIS B CE1 
3684 N NE2 . HIS B 197 ? 0.2787 0.5225 0.3282 -0.0223 0.0485  0.0561  232 HIS B NE2 
3685 N N   . GLY B 198 ? 0.2422 0.3225 0.3073 -0.0623 0.0295  0.0609  233 GLY B N   
3686 C CA  . GLY B 198 ? 0.3006 0.3589 0.3733 -0.0747 0.0293  0.0629  233 GLY B CA  
3687 C C   . GLY B 198 ? 0.2866 0.3199 0.3549 -0.0737 0.0196  0.0509  233 GLY B C   
3688 O O   . GLY B 198 ? 0.3100 0.3404 0.3868 -0.0815 0.0160  0.0456  233 GLY B O   
3689 N N   . HIS B 199 ? 0.2410 0.2592 0.2969 -0.0643 0.0149  0.0460  234 HIS B N   
3690 C CA  . HIS B 199 ? 0.2218 0.2224 0.2737 -0.0614 0.0058  0.0345  234 HIS B CA  
3691 C C   . HIS B 199 ? 0.2691 0.2921 0.3287 -0.0570 0.0001  0.0242  234 HIS B C   
3692 O O   . HIS B 199 ? 0.2858 0.3030 0.3489 -0.0597 -0.0061 0.0177  234 HIS B O   
3693 C CB  . HIS B 199 ? 0.2506 0.2348 0.2900 -0.0518 0.0029  0.0320  234 HIS B CB  
3694 C CG  . HIS B 199 ? 0.2502 0.2164 0.2851 -0.0479 -0.0054 0.0221  234 HIS B CG  
3695 N ND1 . HIS B 199 ? 0.2368 0.1808 0.2684 -0.0530 -0.0068 0.0208  234 HIS B ND1 
3696 C CD2 . HIS B 199 ? 0.2221 0.1900 0.2543 -0.0380 -0.0115 0.0129  234 HIS B CD2 
3697 C CE1 . HIS B 199 ? 0.2449 0.1803 0.2710 -0.0460 -0.0130 0.0127  234 HIS B CE1 
3698 N NE2 . HIS B 199 ? 0.2826 0.2288 0.3108 -0.0385 -0.0169 0.0089  234 HIS B NE2 
3699 N N   . THR B 200 ? 0.2239 0.2737 0.2858 -0.0495 0.0021  0.0226  235 THR B N   
3700 C CA  . THR B 200 ? 0.2343 0.3119 0.3062 -0.0449 -0.0004 0.0149  235 THR B CA  
3701 C C   . THR B 200 ? 0.2511 0.3595 0.3287 -0.0455 0.0083  0.0216  235 THR B C   
3702 O O   . THR B 200 ? 0.2362 0.3435 0.3069 -0.0465 0.0147  0.0310  235 THR B O   
3703 C CB  . THR B 200 ? 0.1981 0.2752 0.2651 -0.0310 -0.0070 0.0031  235 THR B CB  
3704 O OG1 . THR B 200 ? 0.2384 0.3169 0.2960 -0.0241 -0.0039 0.0034  235 THR B OG1 
3705 C CG2 . THR B 200 ? 0.1938 0.2413 0.2552 -0.0299 -0.0148 -0.0017 235 THR B CG2 
3706 N N   . PRO B 201 ? 0.2327 0.3709 0.3227 -0.0444 0.0090  0.0178  236 PRO B N   
3707 C CA  . PRO B 201 ? 0.2582 0.4284 0.3542 -0.0457 0.0185  0.0253  236 PRO B CA  
3708 C C   . PRO B 201 ? 0.2023 0.3835 0.2860 -0.0351 0.0223  0.0252  236 PRO B C   
3709 O O   . PRO B 201 ? 0.2461 0.4466 0.3294 -0.0374 0.0314  0.0358  236 PRO B O   
3710 C CB  . PRO B 201 ? 0.2267 0.4264 0.3382 -0.0432 0.0167  0.0177  236 PRO B CB  
3711 C CG  . PRO B 201 ? 0.2246 0.4061 0.3417 -0.0482 0.0078  0.0123  236 PRO B CG  
3712 C CD  . PRO B 201 ? 0.1868 0.3315 0.2879 -0.0442 0.0019  0.0092  236 PRO B CD  
3713 N N   . GLY B 202 ? 0.1791 0.3498 0.2533 -0.0239 0.0158  0.0136  237 GLY B N   
3714 C CA  . GLY B 202 ? 0.1454 0.3276 0.2081 -0.0144 0.0183  0.0110  237 GLY B CA  
3715 C C   . GLY B 202 ? 0.1874 0.3411 0.2368 -0.0118 0.0137  0.0096  237 GLY B C   
3716 O O   . GLY B 202 ? 0.1991 0.3579 0.2404 -0.0023 0.0116  0.0006  237 GLY B O   
3717 N N   . HIS B 203 ? 0.1695 0.2940 0.2173 -0.0202 0.0124  0.0175  238 HIS B N   
3718 C CA  . HIS B 203 ? 0.1539 0.2518 0.1908 -0.0177 0.0084  0.0167  238 HIS B CA  
3719 C C   . HIS B 203 ? 0.1765 0.2883 0.2038 -0.0136 0.0127  0.0221  238 HIS B C   
3720 O O   . HIS B 203 ? 0.2119 0.3388 0.2390 -0.0177 0.0204  0.0353  238 HIS B O   
3721 C CB  . HIS B 203 ? 0.2022 0.2705 0.2392 -0.0276 0.0087  0.0261  238 HIS B CB  
3722 C CG  . HIS B 203 ? 0.2133 0.2549 0.2409 -0.0250 0.0050  0.0254  238 HIS B CG  
3723 N ND1 . HIS B 203 ? 0.2210 0.2605 0.2411 -0.0242 0.0087  0.0345  238 HIS B ND1 
3724 C CD2 . HIS B 203 ? 0.2332 0.2509 0.2584 -0.0226 -0.0017 0.0174  238 HIS B CD2 
3725 C CE1 . HIS B 203 ? 0.2148 0.2310 0.2294 -0.0218 0.0043  0.0313  238 HIS B CE1 
3726 N NE2 . HIS B 203 ? 0.2148 0.2169 0.2321 -0.0211 -0.0016 0.0212  238 HIS B NE2 
3727 N N   . THR B 204 ? 0.1793 0.2868 0.1989 -0.0055 0.0076  0.0121  239 THR B N   
3728 C CA  . THR B 204 ? 0.1468 0.2718 0.1567 -0.0003 0.0097  0.0138  239 THR B CA  
3729 C C   . THR B 204 ? 0.1940 0.2963 0.1972 0.0006  0.0051  0.0139  239 THR B C   
3730 O O   . THR B 204 ? 0.2094 0.2893 0.2143 0.0019  -0.0013 0.0040  239 THR B O   
3731 C CB  . THR B 204 ? 0.2398 0.3906 0.2483 0.0094  0.0078  -0.0023 239 THR B CB  
3732 O OG1 . THR B 204 ? 0.1917 0.3669 0.2075 0.0091  0.0131  -0.0012 239 THR B OG1 
3733 C CG2 . THR B 204 ? 0.2013 0.3729 0.1981 0.0150  0.0088  -0.0029 239 THR B CG2 
3734 N N   . THR B 205 ? 0.1850 0.2941 0.1812 0.0001  0.0088  0.0264  240 THR B N   
3735 C CA  . THR B 205 ? 0.1916 0.2885 0.1816 0.0023  0.0051  0.0271  240 THR B CA  
3736 C C   . THR B 205 ? 0.2102 0.3326 0.1935 0.0104  0.0014  0.0151  240 THR B C   
3737 O O   . THR B 205 ? 0.2231 0.3762 0.2026 0.0139  0.0049  0.0144  240 THR B O   
3738 C CB  . THR B 205 ? 0.2518 0.3472 0.2388 -0.0013 0.0114  0.0481  240 THR B CB  
3739 O OG1 . THR B 205 ? 0.2770 0.3453 0.2705 -0.0094 0.0145  0.0570  240 THR B OG1 
3740 C CG2 . THR B 205 ? 0.2416 0.3332 0.2226 0.0024  0.0081  0.0508  240 THR B CG2 
3741 N N   . TYR B 206 ? 0.2009 0.3119 0.1829 0.0130  -0.0054 0.0050  241 TYR B N   
3742 C CA  . TYR B 206 ? 0.2053 0.3396 0.1814 0.0196  -0.0097 -0.0084 241 TYR B CA  
3743 C C   . TYR B 206 ? 0.2230 0.3607 0.1936 0.0201  -0.0117 -0.0004 241 TYR B C   
3744 O O   . TYR B 206 ? 0.2227 0.3355 0.1973 0.0172  -0.0146 0.0022  241 TYR B O   
3745 C CB  . TYR B 206 ? 0.1908 0.3134 0.1724 0.0225  -0.0165 -0.0305 241 TYR B CB  
3746 C CG  . TYR B 206 ? 0.2015 0.3267 0.1888 0.0243  -0.0145 -0.0381 241 TYR B CG  
3747 C CD1 . TYR B 206 ? 0.1907 0.3480 0.1745 0.0295  -0.0112 -0.0442 241 TYR B CD1 
3748 C CD2 . TYR B 206 ? 0.1658 0.2639 0.1617 0.0212  -0.0155 -0.0379 241 TYR B CD2 
3749 C CE1 . TYR B 206 ? 0.1768 0.3389 0.1674 0.0318  -0.0090 -0.0504 241 TYR B CE1 
3750 C CE2 . TYR B 206 ? 0.1815 0.2849 0.1837 0.0234  -0.0142 -0.0437 241 TYR B CE2 
3751 C CZ  . TYR B 206 ? 0.1904 0.3260 0.1908 0.0288  -0.0107 -0.0499 241 TYR B CZ  
3752 O OH  . TYR B 206 ? 0.1980 0.3420 0.2062 0.0318  -0.0090 -0.0556 241 TYR B OH  
3753 N N   . VAL B 207 ? 0.1967 0.3672 0.1579 0.0243  -0.0101 0.0040  242 VAL B N   
3754 C CA  . VAL B 207 ? 0.1913 0.3719 0.1469 0.0259  -0.0117 0.0142  242 VAL B CA  
3755 C C   . VAL B 207 ? 0.2519 0.4518 0.2035 0.0305  -0.0201 -0.0054 242 VAL B C   
3756 O O   . VAL B 207 ? 0.2158 0.4439 0.1606 0.0352  -0.0207 -0.0174 242 VAL B O   
3757 C CB  . VAL B 207 ? 0.2392 0.4447 0.1867 0.0278  -0.0040 0.0353  242 VAL B CB  
3758 C CG1 . VAL B 207 ? 0.2426 0.4599 0.1846 0.0310  -0.0062 0.0472  242 VAL B CG1 
3759 C CG2 . VAL B 207 ? 0.3134 0.4980 0.2672 0.0217  0.0046  0.0528  242 VAL B CG2 
3760 N N   . VAL B 208 ? 0.2105 0.3964 0.1668 0.0290  -0.0262 -0.0088 243 VAL B N   
3761 C CA  . VAL B 208 ? 0.1788 0.3791 0.1347 0.0312  -0.0351 -0.0281 243 VAL B CA  
3762 C C   . VAL B 208 ? 0.2327 0.4562 0.1826 0.0336  -0.0374 -0.0161 243 VAL B C   
3763 O O   . VAL B 208 ? 0.2377 0.4470 0.1912 0.0319  -0.0350 0.0024  243 VAL B O   
3764 C CB  . VAL B 208 ? 0.1818 0.3488 0.1505 0.0267  -0.0402 -0.0410 243 VAL B CB  
3765 C CG1 . VAL B 208 ? 0.2183 0.3984 0.1893 0.0276  -0.0491 -0.0638 243 VAL B CG1 
3766 C CG2 . VAL B 208 ? 0.2295 0.3708 0.2043 0.0249  -0.0371 -0.0466 243 VAL B CG2 
3767 N N   . GLU B 209 ? 0.2313 0.4835 0.1762 0.0373  -0.0389 -0.0256 244 GLU B N   
3768 C CA  . GLU B 209 ? 0.2511 0.5230 0.1935 0.0397  -0.0391 -0.0145 244 GLU B CA  
3769 C C   . GLU B 209 ? 0.2077 0.4949 0.1521 0.0403  -0.0454 -0.0355 244 GLU B C   
3770 O O   . GLU B 209 ? 0.2259 0.5240 0.1688 0.0422  -0.0453 -0.0528 244 GLU B O   
3771 C CB  . GLU B 209 ? 0.2619 0.5573 0.1964 0.0441  -0.0305 0.0043  244 GLU B CB  
3772 C CG  . GLU B 209 ? 0.3218 0.6024 0.2555 0.0426  -0.0223 0.0238  244 GLU B CG  
3773 C CD  . GLU B 209 ? 0.4146 0.7171 0.3449 0.0461  -0.0136 0.0415  244 GLU B CD  
3774 O OE1 . GLU B 209 ? 0.4467 0.7657 0.3768 0.0496  -0.0133 0.0515  244 GLU B OE1 
3775 O OE2 . GLU B 209 ? 0.4897 0.7938 0.4189 0.0455  -0.0075 0.0451  244 GLU B OE2 
3776 N N   . SER B 210 ? 0.2298 0.5182 0.1789 0.0389  -0.0505 -0.0334 245 SER B N   
3777 C CA  . SER B 210 ? 0.2225 0.5276 0.1739 0.0388  -0.0565 -0.0510 245 SER B CA  
3778 C C   . SER B 210 ? 0.2269 0.5459 0.1790 0.0398  -0.0591 -0.0376 245 SER B C   
3779 O O   . SER B 210 ? 0.2154 0.5173 0.1742 0.0376  -0.0601 -0.0251 245 SER B O   
3780 C CB  . SER B 210 ? 0.2188 0.4998 0.1821 0.0329  -0.0627 -0.0728 245 SER B CB  
3781 O OG  . SER B 210 ? 0.2325 0.5275 0.2001 0.0315  -0.0687 -0.0866 245 SER B OG  
3782 N N   . GLN B 211 ? 0.2443 0.5954 0.1906 0.0438  -0.0599 -0.0402 246 GLN B N   
3783 C CA  . GLN B 211 ? 0.2650 0.6336 0.2125 0.0454  -0.0631 -0.0301 246 GLN B CA  
3784 C C   . GLN B 211 ? 0.2568 0.6178 0.2045 0.0481  -0.0574 -0.0014 246 GLN B C   
3785 O O   . GLN B 211 ? 0.2643 0.6200 0.2194 0.0473  -0.0603 0.0075  246 GLN B O   
3786 C CB  . GLN B 211 ? 0.2889 0.6486 0.2481 0.0395  -0.0723 -0.0456 246 GLN B CB  
3787 C CG  . GLN B 211 ? 0.2621 0.6234 0.2244 0.0360  -0.0771 -0.0744 246 GLN B CG  
3788 C CD  . GLN B 211 ? 0.5829 0.9806 0.5364 0.0406  -0.0781 -0.0834 246 GLN B CD  
3789 O OE1 . GLN B 211 ? 0.5226 0.9398 0.4781 0.0400  -0.0839 -0.0877 246 GLN B OE1 
3790 N NE2 . GLN B 211 ? 0.6935 1.1021 0.6380 0.0451  -0.0727 -0.0868 246 GLN B NE2 
3791 N N   . GLY B 212 ? 0.2410 0.6001 0.1825 0.0511  -0.0487 0.0133  247 GLY B N   
3792 C CA  . GLY B 212 ? 0.2889 0.6382 0.2321 0.0535  -0.0415 0.0406  247 GLY B CA  
3793 C C   . GLY B 212 ? 0.3187 0.6308 0.2696 0.0492  -0.0403 0.0476  247 GLY B C   
3794 O O   . GLY B 212 ? 0.3407 0.6394 0.2948 0.0508  -0.0332 0.0693  247 GLY B O   
3795 N N   . GLN B 213 ? 0.2089 0.5028 0.1645 0.0439  -0.0465 0.0295  248 GLN B N   
3796 C CA  . GLN B 213 ? 0.2102 0.4707 0.1738 0.0401  -0.0464 0.0347  248 GLN B CA  
3797 C C   . GLN B 213 ? 0.3127 0.5585 0.2719 0.0382  -0.0425 0.0314  248 GLN B C   
3798 O O   . GLN B 213 ? 0.3052 0.5577 0.2612 0.0371  -0.0455 0.0114  248 GLN B O   
3799 C CB  . GLN B 213 ? 0.2479 0.4992 0.2229 0.0352  -0.0560 0.0167  248 GLN B CB  
3800 C CG  . GLN B 213 ? 0.2849 0.5556 0.2649 0.0359  -0.0615 0.0140  248 GLN B CG  
3801 C CD  . GLN B 213 ? 0.3424 0.6148 0.3248 0.0404  -0.0567 0.0389  248 GLN B CD  
3802 O OE1 . GLN B 213 ? 0.5269 0.7751 0.5169 0.0399  -0.0534 0.0517  248 GLN B OE1 
3803 N NE2 . GLN B 213 ? 0.5921 0.8923 0.5685 0.0454  -0.0553 0.0459  248 GLN B NE2 
3804 N N   . LYS B 214 ? 0.2224 0.4463 0.1824 0.0378  -0.0352 0.0503  249 LYS B N   
3805 C CA  . LYS B 214 ? 0.2200 0.4312 0.1756 0.0358  -0.0303 0.0510  249 LYS B CA  
3806 C C   . LYS B 214 ? 0.2157 0.3830 0.1820 0.0297  -0.0277 0.0503  249 LYS B C   
3807 O O   . LYS B 214 ? 0.2433 0.3914 0.2166 0.0289  -0.0259 0.0618  249 LYS B O   
3808 C CB  . LYS B 214 ? 0.2718 0.4876 0.2236 0.0377  -0.0189 0.0710  249 LYS B CB  
3809 C CG  . LYS B 214 ? 0.3109 0.5194 0.2588 0.0350  -0.0136 0.0704  249 LYS B CG  
3810 C CD  . LYS B 214 ? 0.4266 0.6282 0.3780 0.0340  -0.0022 0.0908  249 LYS B CD  
3811 C CE  . LYS B 214 ? 0.4769 0.7122 0.4244 0.0387  0.0008  0.0945  249 LYS B CE  
3812 N NZ  . LYS B 214 ? 0.6959 0.9248 0.6506 0.0392  0.0090  0.1150  249 LYS B NZ  
3813 N N   . LEU B 215 ? 0.1929 0.3454 0.1605 0.0261  -0.0270 0.0365  250 LEU B N   
3814 C CA  . LEU B 215 ? 0.1750 0.2882 0.1510 0.0205  -0.0246 0.0341  250 LEU B CA  
3815 C C   . LEU B 215 ? 0.2330 0.3409 0.2062 0.0187  -0.0193 0.0337  250 LEU B C   
3816 O O   . LEU B 215 ? 0.2314 0.3557 0.2015 0.0203  -0.0216 0.0193  250 LEU B O   
3817 C CB  . LEU B 215 ? 0.2177 0.3192 0.2015 0.0181  -0.0321 0.0129  250 LEU B CB  
3818 C CG  . LEU B 215 ? 0.2578 0.3227 0.2487 0.0134  -0.0306 0.0074  250 LEU B CG  
3819 C CD1 . LEU B 215 ? 0.2225 0.2600 0.2173 0.0108  -0.0257 0.0234  250 LEU B CD1 
3820 C CD2 . LEU B 215 ? 0.2597 0.3173 0.2583 0.0118  -0.0376 -0.0133 250 LEU B CD2 
3821 N N   . ALA B 216 ? 0.2077 0.2932 0.1830 0.0152  -0.0122 0.0481  251 ALA B N   
3822 C CA  . ALA B 216 ? 0.1890 0.2697 0.1641 0.0122  -0.0074 0.0481  251 ALA B CA  
3823 C C   . ALA B 216 ? 0.2269 0.2758 0.2090 0.0077  -0.0092 0.0382  251 ALA B C   
3824 O O   . ALA B 216 ? 0.2253 0.2474 0.2111 0.0046  -0.0075 0.0452  251 ALA B O   
3825 C CB  . ALA B 216 ? 0.1956 0.2747 0.1694 0.0103  0.0017  0.0699  251 ALA B CB  
3826 N N   . LEU B 217 ? 0.1941 0.2469 0.1776 0.0084  -0.0125 0.0221  252 LEU B N   
3827 C CA  . LEU B 217 ? 0.1675 0.1940 0.1570 0.0054  -0.0144 0.0133  252 LEU B CA  
3828 C C   . LEU B 217 ? 0.2130 0.2352 0.2035 0.0016  -0.0089 0.0210  252 LEU B C   
3829 O O   . LEU B 217 ? 0.2049 0.2466 0.1952 0.0030  -0.0076 0.0167  252 LEU B O   
3830 C CB  . LEU B 217 ? 0.2067 0.2394 0.1988 0.0090  -0.0205 -0.0071 252 LEU B CB  
3831 C CG  . LEU B 217 ? 0.2382 0.2792 0.2306 0.0116  -0.0262 -0.0168 252 LEU B CG  
3832 C CD1 . LEU B 217 ? 0.2492 0.2970 0.2447 0.0152  -0.0313 -0.0381 252 LEU B CD1 
3833 C CD2 . LEU B 217 ? 0.2418 0.2572 0.2392 0.0085  -0.0279 -0.0126 252 LEU B CD2 
3834 N N   . LEU B 218 ? 0.2649 0.2597 0.1503 -0.0177 0.0097  0.0007  253 LEU B N   
3835 C CA  . LEU B 218 ? 0.2515 0.2473 0.1483 -0.0147 0.0114  0.0097  253 LEU B CA  
3836 C C   . LEU B 218 ? 0.2544 0.2400 0.1612 -0.0054 0.0156  -0.0007 253 LEU B C   
3837 O O   . LEU B 218 ? 0.2874 0.2784 0.2070 -0.0040 0.0167  0.0027  253 LEU B O   
3838 C CB  . LEU B 218 ? 0.2723 0.2611 0.1830 -0.0134 0.0035  0.0245  253 LEU B CB  
3839 C CG  . LEU B 218 ? 0.2828 0.2803 0.1907 -0.0176 -0.0055 0.0389  253 LEU B CG  
3840 C CD1 . LEU B 218 ? 0.3083 0.2938 0.2387 -0.0118 -0.0124 0.0492  253 LEU B CD1 
3841 C CD2 . LEU B 218 ? 0.2915 0.3054 0.1827 -0.0267 -0.0045 0.0512  253 LEU B CD2 
3842 N N   . GLY B 219 ? 0.2782 0.2487 0.1807 0.0007  0.0168  -0.0122 254 GLY B N   
3843 C CA  . GLY B 219 ? 0.2637 0.2243 0.1745 0.0124  0.0172  -0.0186 254 GLY B CA  
3844 C C   . GLY B 219 ? 0.2848 0.2394 0.2042 0.0161  0.0111  -0.0107 254 GLY B C   
3845 O O   . GLY B 219 ? 0.3035 0.2465 0.2186 0.0139  0.0082  -0.0059 254 GLY B O   
3846 N N   . ASP B 220 ? 0.2366 0.2039 0.1701 0.0207  0.0100  -0.0125 255 ASP B N   
3847 C CA  . ASP B 220 ? 0.2553 0.2217 0.1977 0.0231  0.0039  -0.0101 255 ASP B CA  
3848 C C   . ASP B 220 ? 0.3323 0.3106 0.2896 0.0133  0.0048  -0.0051 255 ASP B C   
3849 O O   . ASP B 220 ? 0.2652 0.2497 0.2369 0.0132  0.0014  -0.0086 255 ASP B O   
3850 C CB  . ASP B 220 ? 0.2734 0.2452 0.2228 0.0355  -0.0015 -0.0171 255 ASP B CB  
3851 C CG  . ASP B 220 ? 0.3118 0.2597 0.2436 0.0457  -0.0060 -0.0154 255 ASP B CG  
3852 O OD1 . ASP B 220 ? 0.3417 0.2703 0.2582 0.0406  -0.0018 -0.0119 255 ASP B OD1 
3853 O OD2 . ASP B 220 ? 0.2729 0.2215 0.2059 0.0577  -0.0145 -0.0163 255 ASP B OD2 
3854 N N   . LEU B 221 ? 0.2394 0.2194 0.1930 0.0043  0.0083  0.0036  256 LEU B N   
3855 C CA  . LEU B 221 ? 0.2754 0.2578 0.2419 -0.0051 0.0084  0.0134  256 LEU B CA  
3856 C C   . LEU B 221 ? 0.3616 0.3286 0.3386 -0.0029 0.0026  0.0138  256 LEU B C   
3857 O O   . LEU B 221 ? 0.3754 0.3387 0.3702 -0.0083 0.0018  0.0164  256 LEU B O   
3858 C CB  . LEU B 221 ? 0.3314 0.3184 0.2858 -0.0135 0.0109  0.0265  256 LEU B CB  
3859 C CG  . LEU B 221 ? 0.4611 0.4504 0.4233 -0.0255 0.0131  0.0418  256 LEU B CG  
3860 C CD1 . LEU B 221 ? 0.3924 0.4009 0.3652 -0.0323 0.0223  0.0344  256 LEU B CD1 
3861 C CD2 . LEU B 221 ? 0.3389 0.3344 0.2799 -0.0322 0.0127  0.0570  256 LEU B CD2 
3862 N N   . ILE B 222 ? 0.2549 0.2130 0.2229 0.0036  0.0000  0.0095  257 ILE B N   
3863 C CA  . ILE B 222 ? 0.3143 0.2643 0.2913 0.0065  -0.0027 0.0031  257 ILE B CA  
3864 C C   . ILE B 222 ? 0.3246 0.2731 0.2855 0.0121  -0.0028 -0.0059 257 ILE B C   
3865 O O   . ILE B 222 ? 0.3803 0.3250 0.3243 0.0139  -0.0011 -0.0037 257 ILE B O   
3866 C CB  . ILE B 222 ? 0.3802 0.3246 0.3656 0.0068  -0.0045 0.0088  257 ILE B CB  
3867 C CG1 . ILE B 222 ? 0.4198 0.3602 0.4182 0.0106  -0.0044 -0.0038 257 ILE B CG1 
3868 C CG2 . ILE B 222 ? 0.3357 0.2843 0.3053 0.0068  -0.0038 0.0119  257 ILE B CG2 
3869 C CD1 . ILE B 222 ? 0.4169 0.3543 0.4366 0.0142  -0.0068 -0.0015 257 ILE B CD1 
3870 N N   . LEU B 223 ? 0.2851 0.2353 0.2496 0.0138  -0.0050 -0.0158 258 LEU B N   
3871 C CA  . LEU B 223 ? 0.3128 0.2628 0.2567 0.0184  -0.0069 -0.0208 258 LEU B CA  
3872 C C   . LEU B 223 ? 0.3586 0.3075 0.2954 0.0166  -0.0038 -0.0284 258 LEU B C   
3873 O O   . LEU B 223 ? 0.3750 0.3193 0.2872 0.0169  -0.0018 -0.0260 258 LEU B O   
3874 C CB  . LEU B 223 ? 0.3285 0.2911 0.2763 0.0218  -0.0141 -0.0276 258 LEU B CB  
3875 C CG  . LEU B 223 ? 0.3425 0.3148 0.3022 0.0237  -0.0153 -0.0244 258 LEU B CG  
3876 C CD1 . LEU B 223 ? 0.3991 0.3924 0.3730 0.0255  -0.0228 -0.0346 258 LEU B CD1 
3877 C CD2 . LEU B 223 ? 0.4196 0.3832 0.3624 0.0315  -0.0145 -0.0174 258 LEU B CD2 
3878 N N   . VAL B 224 ? 0.3070 0.2591 0.2649 0.0141  -0.0022 -0.0381 259 VAL B N   
3879 C CA  . VAL B 224 ? 0.2882 0.2455 0.2439 0.0128  0.0030  -0.0518 259 VAL B CA  
3880 C C   . VAL B 224 ? 0.2929 0.2480 0.2767 0.0136  0.0069  -0.0538 259 VAL B C   
3881 O O   . VAL B 224 ? 0.2772 0.2277 0.2890 0.0149  0.0046  -0.0598 259 VAL B O   
3882 C CB  . VAL B 224 ? 0.3009 0.2678 0.2592 0.0116  -0.0003 -0.0698 259 VAL B CB  
3883 C CG1 . VAL B 224 ? 0.3615 0.3385 0.3113 0.0091  0.0075  -0.0873 259 VAL B CG1 
3884 C CG2 . VAL B 224 ? 0.2979 0.2718 0.2344 0.0135  -0.0092 -0.0657 259 VAL B CG2 
3885 N N   . ALA B 225 ? 0.2814 0.2397 0.2606 0.0128  0.0122  -0.0490 260 ALA B N   
3886 C CA  . ALA B 225 ? 0.3111 0.2730 0.3200 0.0162  0.0126  -0.0492 260 ALA B CA  
3887 C C   . ALA B 225 ? 0.2530 0.2185 0.2915 0.0212  0.0151  -0.0685 260 ALA B C   
3888 O O   . ALA B 225 ? 0.3097 0.2670 0.3806 0.0279  0.0097  -0.0661 260 ALA B O   
3889 C CB  . ALA B 225 ? 0.2834 0.2568 0.2850 0.0123  0.0188  -0.0473 260 ALA B CB  
3890 N N   . ALA B 226 ? 0.2696 0.2462 0.2969 0.0181  0.0233  -0.0879 261 ALA B N   
3891 C CA  . ALA B 226 ? 0.2899 0.2736 0.3468 0.0228  0.0286  -0.1131 261 ALA B CA  
3892 C C   . ALA B 226 ? 0.2405 0.2071 0.3191 0.0253  0.0218  -0.1212 261 ALA B C   
3893 O O   . ALA B 226 ? 0.3213 0.2864 0.4321 0.0306  0.0251  -0.1432 261 ALA B O   
3894 C CB  . ALA B 226 ? 0.4102 0.4155 0.4434 0.0160  0.0412  -0.1339 261 ALA B CB  
3895 N N   . VAL B 227 ? 0.2582 0.2126 0.3236 0.0208  0.0137  -0.1065 262 VAL B N   
3896 C CA  . VAL B 227 ? 0.3593 0.2983 0.4464 0.0184  0.0084  -0.1129 262 VAL B CA  
3897 C C   . VAL B 227 ? 0.2672 0.1854 0.3713 0.0190  0.0015  -0.0873 262 VAL B C   
3898 O O   . VAL B 227 ? 0.2936 0.1908 0.4310 0.0210  -0.0009 -0.0882 262 VAL B O   
3899 C CB  . VAL B 227 ? 0.3352 0.2852 0.3976 0.0102  0.0053  -0.1213 262 VAL B CB  
3900 C CG1 . VAL B 227 ? 0.2838 0.2206 0.3724 0.0037  0.0001  -0.1265 262 VAL B CG1 
3901 C CG2 . VAL B 227 ? 0.3350 0.3056 0.3788 0.0083  0.0110  -0.1476 262 VAL B CG2 
3902 N N   . GLN B 228 ? 0.2477 0.1702 0.3282 0.0167  -0.0012 -0.0644 263 GLN B N   
3903 C CA  . GLN B 228 ? 0.2543 0.1641 0.3398 0.0126  -0.0060 -0.0418 263 GLN B CA  
3904 C C   . GLN B 228 ? 0.3532 0.2535 0.4504 0.0185  -0.0102 -0.0216 263 GLN B C   
3905 O O   . GLN B 228 ? 0.3494 0.2382 0.4487 0.0138  -0.0140 -0.0007 263 GLN B O   
3906 C CB  . GLN B 228 ? 0.2577 0.1805 0.3141 0.0072  -0.0061 -0.0324 263 GLN B CB  
3907 C CG  . GLN B 228 ? 0.3650 0.2992 0.4154 0.0030  -0.0066 -0.0493 263 GLN B CG  
3908 C CD  . GLN B 228 ? 0.2831 0.2315 0.3101 0.0029  -0.0083 -0.0419 263 GLN B CD  
3909 O OE1 . GLN B 228 ? 0.3284 0.2788 0.3332 0.0079  -0.0072 -0.0342 263 GLN B OE1 
3910 N NE2 . GLN B 228 ? 0.3010 0.2599 0.3367 -0.0026 -0.0107 -0.0463 263 GLN B NE2 
3911 N N   . PHE B 229 ? 0.2661 0.1747 0.3709 0.0278  -0.0100 -0.0267 264 PHE B N   
3912 C CA  . PHE B 229 ? 0.2761 0.1783 0.4008 0.0361  -0.0180 -0.0095 264 PHE B CA  
3913 C C   . PHE B 229 ? 0.3457 0.2234 0.5109 0.0440  -0.0217 -0.0142 264 PHE B C   
3914 O O   . PHE B 229 ? 0.3465 0.2030 0.5250 0.0466  -0.0305 0.0090  264 PHE B O   
3915 C CB  . PHE B 229 ? 0.2413 0.1676 0.3662 0.0429  -0.0175 -0.0146 264 PHE B CB  
3916 C CG  . PHE B 229 ? 0.2773 0.2192 0.3679 0.0352  -0.0169 -0.0036 264 PHE B CG  
3917 C CD1 . PHE B 229 ? 0.2864 0.2260 0.3635 0.0318  -0.0246 0.0197  264 PHE B CD1 
3918 C CD2 . PHE B 229 ? 0.3436 0.3010 0.4142 0.0301  -0.0080 -0.0168 264 PHE B CD2 
3919 C CE1 . PHE B 229 ? 0.3276 0.2811 0.3754 0.0245  -0.0231 0.0243  264 PHE B CE1 
3920 C CE2 . PHE B 229 ? 0.3852 0.3502 0.4280 0.0228  -0.0072 -0.0085 264 PHE B CE2 
3921 C CZ  . PHE B 229 ? 0.3319 0.2956 0.3652 0.0206  -0.0147 0.0095  264 PHE B CZ  
3922 N N   . ASP B 230 ? 0.3147 0.1935 0.4987 0.0477  -0.0147 -0.0442 265 ASP B N   
3923 C CA  . ASP B 230 ? 0.3053 0.1627 0.5248 0.0533  -0.0163 -0.0533 265 ASP B CA  
3924 C C   . ASP B 230 ? 0.3476 0.1791 0.5652 0.0402  -0.0173 -0.0435 265 ASP B C   
3925 O O   . ASP B 230 ? 0.4317 0.2396 0.6670 0.0417  -0.0221 -0.0302 265 ASP B O   
3926 C CB  . ASP B 230 ? 0.3664 0.2420 0.5947 0.0552  -0.0062 -0.0898 265 ASP B CB  
3927 C CG  . ASP B 230 ? 0.6710 0.5720 0.9141 0.0678  -0.0035 -0.1001 265 ASP B CG  
3928 O OD1 . ASP B 230 ? 0.6501 0.5505 0.9087 0.0785  -0.0128 -0.0805 265 ASP B OD1 
3929 O OD2 . ASP B 230 ? 0.7449 0.6705 0.9826 0.0656  0.0077  -0.1274 265 ASP B OD2 
3930 N N   . ASP B 231 ? 0.3399 0.1764 0.5379 0.0269  -0.0128 -0.0510 266 ASP B N   
3931 C CA  . ASP B 231 ? 0.3819 0.2019 0.5824 0.0115  -0.0121 -0.0463 266 ASP B CA  
3932 C C   . ASP B 231 ? 0.3407 0.1748 0.5115 0.0004  -0.0117 -0.0287 266 ASP B C   
3933 O O   . ASP B 231 ? 0.3192 0.1772 0.4711 -0.0057 -0.0084 -0.0438 266 ASP B O   
3934 C CB  . ASP B 231 ? 0.3571 0.1845 0.5660 0.0050  -0.0068 -0.0800 266 ASP B CB  
3935 C CG  . ASP B 231 ? 0.5108 0.3226 0.7308 -0.0118 -0.0061 -0.0781 266 ASP B CG  
3936 O OD1 . ASP B 231 ? 0.4669 0.2624 0.6854 -0.0201 -0.0076 -0.0497 266 ASP B OD1 
3937 O OD2 . ASP B 231 ? 0.5336 0.3523 0.7625 -0.0183 -0.0033 -0.1052 266 ASP B OD2 
3938 N N   . PRO B 232 ? 0.3345 0.1608 0.4955 -0.0018 -0.0152 0.0038  267 PRO B N   
3939 C CA  . PRO B 232 ? 0.3683 0.2166 0.4979 -0.0120 -0.0123 0.0178  267 PRO B CA  
3940 C C   . PRO B 232 ? 0.3401 0.1928 0.4742 -0.0292 -0.0066 0.0108  267 PRO B C   
3941 O O   . PRO B 232 ? 0.3149 0.1927 0.4283 -0.0352 -0.0032 0.0141  267 PRO B O   
3942 C CB  . PRO B 232 ? 0.5257 0.3637 0.6461 -0.0122 -0.0171 0.0521  267 PRO B CB  
3943 C CG  . PRO B 232 ? 0.5006 0.3211 0.6429 0.0043  -0.0257 0.0554  267 PRO B CG  
3944 C CD  . PRO B 232 ? 0.4510 0.2539 0.6266 0.0073  -0.0230 0.0283  267 PRO B CD  
3945 N N   . SER B 233 ? 0.3589 0.1900 0.5231 -0.0375 -0.0054 -0.0011 268 SER B N   
3946 C CA  . SER B 233 ? 0.3989 0.2394 0.5729 -0.0567 -0.0001 -0.0102 268 SER B CA  
3947 C C   . SER B 233 ? 0.3578 0.2321 0.5264 -0.0553 -0.0010 -0.0417 268 SER B C   
3948 O O   . SER B 233 ? 0.3570 0.2513 0.5336 -0.0692 0.0012  -0.0510 268 SER B O   
3949 C CB  . SER B 233 ? 0.4421 0.2463 0.6500 -0.0692 0.0018  -0.0123 268 SER B CB  
3950 O OG  . SER B 233 ? 0.4956 0.2902 0.7157 -0.0560 -0.0015 -0.0361 268 SER B OG  
3951 N N   . VAL B 234 ? 0.3314 0.2154 0.4866 -0.0399 -0.0047 -0.0573 269 VAL B N   
3952 C CA  . VAL B 234 ? 0.3574 0.2720 0.5013 -0.0385 -0.0076 -0.0830 269 VAL B CA  
3953 C C   . VAL B 234 ? 0.2986 0.2415 0.4148 -0.0344 -0.0091 -0.0713 269 VAL B C   
3954 O O   . VAL B 234 ? 0.2818 0.2230 0.3762 -0.0247 -0.0082 -0.0545 269 VAL B O   
3955 C CB  . VAL B 234 ? 0.3458 0.2608 0.4813 -0.0263 -0.0086 -0.1024 269 VAL B CB  
3956 C CG1 . VAL B 234 ? 0.3606 0.3075 0.4772 -0.0263 -0.0131 -0.1253 269 VAL B CG1 
3957 C CG2 . VAL B 234 ? 0.4109 0.2970 0.5800 -0.0272 -0.0062 -0.1174 269 VAL B CG2 
3958 N N   . THR B 235 ? 0.3185 0.2885 0.4395 -0.0413 -0.0119 -0.0823 270 THR B N   
3959 C CA  . THR B 235 ? 0.3096 0.3070 0.4129 -0.0350 -0.0141 -0.0748 270 THR B CA  
3960 C C   . THR B 235 ? 0.2523 0.2747 0.3405 -0.0255 -0.0244 -0.0923 270 THR B C   
3961 O O   . THR B 235 ? 0.3160 0.3375 0.4018 -0.0256 -0.0285 -0.1103 270 THR B O   
3962 C CB  . THR B 235 ? 0.3025 0.3171 0.4278 -0.0492 -0.0090 -0.0706 270 THR B CB  
3963 O OG1 . THR B 235 ? 0.3570 0.3867 0.5105 -0.0624 -0.0122 -0.0928 270 THR B OG1 
3964 C CG2 . THR B 235 ? 0.4028 0.3905 0.5345 -0.0603 0.0010  -0.0482 270 THR B CG2 
3965 N N   . THR B 236 ? 0.2786 0.3239 0.3555 -0.0165 -0.0291 -0.0871 271 THR B N   
3966 C CA  . THR B 236 ? 0.3125 0.3807 0.3728 -0.0052 -0.0421 -0.0973 271 THR B CA  
3967 C C   . THR B 236 ? 0.2664 0.3728 0.3494 -0.0051 -0.0495 -0.1051 271 THR B C   
3968 O O   . THR B 236 ? 0.3397 0.4549 0.4458 -0.0123 -0.0411 -0.1003 271 THR B O   
3969 C CB  . THR B 236 ? 0.3322 0.3877 0.3561 0.0112  -0.0440 -0.0818 271 THR B CB  
3970 O OG1 . THR B 236 ? 0.4696 0.5291 0.4965 0.0182  -0.0414 -0.0693 271 THR B OG1 
3971 C CG2 . THR B 236 ? 0.3554 0.3799 0.3641 0.0095  -0.0345 -0.0740 271 THR B CG2 
3972 N N   . ASP B 237 ? 0.2853 0.4185 0.3610 0.0031  -0.0654 -0.1173 272 ASP B N   
3973 C CA  . ASP B 237 ? 0.2543 0.4312 0.3540 0.0083  -0.0766 -0.1259 272 ASP B CA  
3974 C C   . ASP B 237 ? 0.3084 0.4881 0.4024 0.0276  -0.0776 -0.1100 272 ASP B C   
3975 O O   . ASP B 237 ? 0.4300 0.6481 0.5496 0.0358  -0.0862 -0.1174 272 ASP B O   
3976 C CB  . ASP B 237 ? 0.3226 0.5301 0.4141 0.0130  -0.0973 -0.1427 272 ASP B CB  
3977 C CG  . ASP B 237 ? 0.4526 0.6447 0.4946 0.0314  -0.1080 -0.1288 272 ASP B CG  
3978 O OD1 . ASP B 237 ? 0.5491 0.7036 0.5663 0.0375  -0.0974 -0.1093 272 ASP B OD1 
3979 O OD2 . ASP B 237 ? 0.6396 0.8586 0.6661 0.0379  -0.1272 -0.1372 272 ASP B OD2 
3980 N N   . LEU B 238 ? 0.2789 0.4212 0.3444 0.0351  -0.0691 -0.0915 273 LEU B N   
3981 C CA  . LEU B 238 ? 0.3783 0.5164 0.4402 0.0513  -0.0672 -0.0799 273 LEU B CA  
3982 C C   . LEU B 238 ? 0.3951 0.5312 0.4753 0.0406  -0.0484 -0.0768 273 LEU B C   
3983 O O   . LEU B 238 ? 0.3860 0.5236 0.4679 0.0519  -0.0441 -0.0729 273 LEU B O   
3984 C CB  . LEU B 238 ? 0.4024 0.5014 0.4220 0.0629  -0.0686 -0.0633 273 LEU B CB  
3985 C CG  . LEU B 238 ? 0.5396 0.6396 0.5332 0.0789  -0.0877 -0.0585 273 LEU B CG  
3986 C CD1 . LEU B 238 ? 0.5328 0.5949 0.4832 0.0760  -0.0832 -0.0454 273 LEU B CD1 
3987 C CD2 . LEU B 238 ? 0.5601 0.6666 0.5611 0.1024  -0.0987 -0.0521 273 LEU B CD2 
3988 N N   . ASP B 239 ? 0.2922 0.4237 0.3848 0.0190  -0.0372 -0.0784 274 ASP B N   
3989 C CA  . ASP B 239 ? 0.2617 0.3942 0.3671 0.0058  -0.0200 -0.0723 274 ASP B CA  
3990 C C   . ASP B 239 ? 0.2305 0.4096 0.3750 -0.0014 -0.0169 -0.0862 274 ASP B C   
3991 O O   . ASP B 239 ? 0.3493 0.5514 0.5182 -0.0106 -0.0236 -0.1001 274 ASP B O   
3992 C CB  . ASP B 239 ? 0.2161 0.3210 0.3192 -0.0137 -0.0111 -0.0641 274 ASP B CB  
3993 C CG  . ASP B 239 ? 0.3590 0.4251 0.4309 -0.0070 -0.0129 -0.0530 274 ASP B CG  
3994 O OD1 . ASP B 239 ? 0.3021 0.3558 0.3525 0.0022  -0.0099 -0.0427 274 ASP B OD1 
3995 O OD2 . ASP B 239 ? 0.3879 0.4382 0.4600 -0.0120 -0.0162 -0.0573 274 ASP B OD2 
3996 N N   . SER B 240 ? 0.1921 0.3892 0.3447 0.0015  -0.0057 -0.0857 275 SER B N   
3997 C CA  . SER B 240 ? 0.1821 0.4312 0.3759 -0.0055 0.0005  -0.1012 275 SER B CA  
3998 C C   . SER B 240 ? 0.3053 0.5611 0.5182 -0.0379 0.0146  -0.1001 275 SER B C   
3999 O O   . SER B 240 ? 0.3230 0.6199 0.5747 -0.0501 0.0152  -0.1160 275 SER B O   
4000 C CB  . SER B 240 ? 0.2228 0.4901 0.4198 0.0054  0.0122  -0.1042 275 SER B CB  
4001 O OG  . SER B 240 ? 0.5459 0.7979 0.7273 0.0350  -0.0008 -0.1043 275 SER B OG  
4002 N N   . ASP B 241 ? 0.2513 0.4674 0.4395 -0.0527 0.0255  -0.0806 276 ASP B N   
4003 C CA  . ASP B 241 ? 0.2627 0.4731 0.4646 -0.0836 0.0390  -0.0727 276 ASP B CA  
4004 C C   . ASP B 241 ? 0.2427 0.3971 0.4209 -0.0868 0.0341  -0.0563 276 ASP B C   
4005 O O   . ASP B 241 ? 0.2774 0.4023 0.4257 -0.0844 0.0385  -0.0364 276 ASP B O   
4006 C CB  . ASP B 241 ? 0.2615 0.4888 0.4592 -0.0983 0.0606  -0.0622 276 ASP B CB  
4007 C CG  . ASP B 241 ? 0.4007 0.6209 0.6100 -0.1330 0.0759  -0.0493 276 ASP B CG  
4008 O OD1 . ASP B 241 ? 0.3745 0.5653 0.5942 -0.1440 0.0694  -0.0468 276 ASP B OD1 
4009 O OD2 . ASP B 241 ? 0.4314 0.6750 0.6394 -0.1503 0.0955  -0.0421 276 ASP B OD2 
4010 N N   . SER B 242 ? 0.2825 0.4421 0.4947 -0.1466 -0.0251 0.0033  277 SER B N   
4011 C CA  . SER B 242 ? 0.3317 0.4424 0.5175 -0.1479 -0.0260 -0.0114 277 SER B CA  
4012 C C   . SER B 242 ? 0.3201 0.4035 0.5109 -0.1498 -0.0129 -0.0007 277 SER B C   
4013 O O   . SER B 242 ? 0.3352 0.3878 0.5033 -0.1373 -0.0065 -0.0039 277 SER B O   
4014 C CB  . SER B 242 ? 0.3132 0.4124 0.4997 -0.1687 -0.0422 -0.0302 277 SER B CB  
4015 O OG  . SER B 242 ? 0.6451 0.7594 0.8671 -0.1918 -0.0470 -0.0238 277 SER B OG  
4016 N N   . LYS B 243 ? 0.3477 0.4442 0.5702 -0.1659 -0.0093 0.0147  278 LYS B N   
4017 C CA  . LYS B 243 ? 0.4100 0.4819 0.6394 -0.1691 0.0020  0.0298  278 LYS B CA  
4018 C C   . LYS B 243 ? 0.3695 0.4496 0.5801 -0.1468 0.0164  0.0437  278 LYS B C   
4019 O O   . LYS B 243 ? 0.3321 0.3812 0.5278 -0.1392 0.0222  0.0476  278 LYS B O   
4020 C CB  . LYS B 243 ? 0.3738 0.4643 0.6401 -0.1905 0.0038  0.0464  278 LYS B CB  
4021 C CG  . LYS B 243 ? 0.4655 0.5297 0.7386 -0.2099 -0.0073 0.0291  278 LYS B CG  
4022 C CD  . LYS B 243 ? 0.4986 0.5647 0.7949 -0.2249 -0.0012 0.0447  278 LYS B CD  
4023 C CE  . LYS B 243 ? 0.6751 0.6869 0.9666 -0.2350 -0.0031 0.0380  278 LYS B CE  
4024 N NZ  . LYS B 243 ? 0.7542 0.7434 1.0353 -0.2464 -0.0173 0.0077  278 LYS B NZ  
4025 N N   . ALA B 244 ? 0.2886 0.4111 0.5005 -0.1357 0.0218  0.0500  279 ALA B N   
4026 C CA  . ALA B 244 ? 0.2313 0.3633 0.4232 -0.1154 0.0349  0.0589  279 ALA B CA  
4027 C C   . ALA B 244 ? 0.3681 0.4711 0.5258 -0.0980 0.0316  0.0437  279 ALA B C   
4028 O O   . ALA B 244 ? 0.2737 0.3637 0.4129 -0.0871 0.0392  0.0500  279 ALA B O   
4029 C CB  . ALA B 244 ? 0.3298 0.5117 0.5329 -0.1062 0.0417  0.0640  279 ALA B CB  
4030 N N   . VAL B 245 ? 0.2803 0.3761 0.4293 -0.0959 0.0199  0.0254  280 VAL B N   
4031 C CA  . VAL B 245 ? 0.2840 0.3550 0.4028 -0.0811 0.0177  0.0129  280 VAL B CA  
4032 C C   . VAL B 245 ? 0.2771 0.3075 0.3875 -0.0845 0.0184  0.0102  280 VAL B C   
4033 O O   . VAL B 245 ? 0.3140 0.3288 0.4054 -0.0713 0.0228  0.0107  280 VAL B O   
4034 C CB  . VAL B 245 ? 0.2601 0.3372 0.3699 -0.0776 0.0061  -0.0023 280 VAL B CB  
4035 C CG1 . VAL B 245 ? 0.4711 0.5333 0.5842 -0.0944 -0.0053 -0.0152 280 VAL B CG1 
4036 C CG2 . VAL B 245 ? 0.4244 0.4854 0.5061 -0.0605 0.0069  -0.0096 280 VAL B CG2 
4037 N N   . ALA B 246 ? 0.2744 0.2872 0.4017 -0.1021 0.0138  0.0073  281 ALA B N   
4038 C CA  . ALA B 246 ? 0.3697 0.3420 0.4954 -0.1035 0.0158  0.0056  281 ALA B CA  
4039 C C   . ALA B 246 ? 0.3272 0.2977 0.4559 -0.0973 0.0262  0.0290  281 ALA B C   
4040 O O   . ALA B 246 ? 0.4352 0.3846 0.5507 -0.0855 0.0291  0.0305  281 ALA B O   
4041 C CB  . ALA B 246 ? 0.3391 0.2908 0.4864 -0.1245 0.0091  -0.0028 281 ALA B CB  
4042 N N   . VAL B 247 ? 0.3037 0.3010 0.4493 -0.1052 0.0319  0.0487  282 VAL B N   
4043 C CA  . VAL B 247 ? 0.3856 0.3874 0.5309 -0.1011 0.0419  0.0737  282 VAL B CA  
4044 C C   . VAL B 247 ? 0.2965 0.3087 0.4118 -0.0803 0.0461  0.0728  282 VAL B C   
4045 O O   . VAL B 247 ? 0.3547 0.3515 0.4593 -0.0725 0.0484  0.0827  282 VAL B O   
4046 C CB  . VAL B 247 ? 0.4196 0.4572 0.5865 -0.1136 0.0490  0.0942  282 VAL B CB  
4047 C CG1 . VAL B 247 ? 0.3191 0.3740 0.4750 -0.1062 0.0606  0.1188  282 VAL B CG1 
4048 C CG2 . VAL B 247 ? 0.3952 0.4163 0.5954 -0.1371 0.0447  0.1007  282 VAL B CG2 
4049 N N   . GLU B 248 ? 0.3355 0.3737 0.4393 -0.0714 0.0460  0.0613  283 GLU B N   
4050 C CA  . GLU B 248 ? 0.2916 0.3399 0.3691 -0.0535 0.0496  0.0584  283 GLU B CA  
4051 C C   . GLU B 248 ? 0.2901 0.3082 0.3501 -0.0440 0.0433  0.0458  283 GLU B C   
4052 O O   . GLU B 248 ? 0.2982 0.3137 0.3409 -0.0335 0.0454  0.0504  283 GLU B O   
4053 C CB  . GLU B 248 ? 0.3165 0.3950 0.3922 -0.0463 0.0506  0.0482  283 GLU B CB  
4054 C CG  . GLU B 248 ? 0.2904 0.4078 0.3811 -0.0501 0.0609  0.0615  283 GLU B CG  
4055 C CD  . GLU B 248 ? 0.3813 0.5099 0.4597 -0.0475 0.0720  0.0792  283 GLU B CD  
4056 O OE1 . GLU B 248 ? 0.5271 0.6531 0.5791 -0.0340 0.0735  0.0742  283 GLU B OE1 
4057 O OE2 . GLU B 248 ? 0.4539 0.5955 0.5489 -0.0603 0.0786  0.0991  283 GLU B OE2 
4058 N N   . ARG B 249 ? 0.2518 0.2503 0.3154 -0.0481 0.0356  0.0296  284 ARG B N   
4059 C CA  . ARG B 249 ? 0.2715 0.2450 0.3209 -0.0396 0.0319  0.0180  284 ARG B CA  
4060 C C   . ARG B 249 ? 0.3273 0.2771 0.3825 -0.0387 0.0344  0.0293  284 ARG B C   
4061 O O   . ARG B 249 ? 0.3165 0.2598 0.3595 -0.0273 0.0346  0.0311  284 ARG B O   
4062 C CB  . ARG B 249 ? 0.3139 0.2748 0.3647 -0.0457 0.0248  -0.0014 284 ARG B CB  
4063 C CG  . ARG B 249 ? 0.2993 0.2372 0.3374 -0.0379 0.0233  -0.0139 284 ARG B CG  
4064 C CD  . ARG B 249 ? 0.3511 0.2798 0.3884 -0.0463 0.0177  -0.0332 284 ARG B CD  
4065 N NE  . ARG B 249 ? 0.4843 0.4384 0.5155 -0.0487 0.0119  -0.0371 284 ARG B NE  
4066 C CZ  . ARG B 249 ? 0.4128 0.3731 0.4474 -0.0605 0.0045  -0.0475 284 ARG B CZ  
4067 N NH1 . ARG B 249 ? 0.4677 0.4088 0.5101 -0.0728 0.0024  -0.0587 284 ARG B NH1 
4068 N NH2 . ARG B 249 ? 0.3380 0.3244 0.3697 -0.0602 -0.0017 -0.0469 284 ARG B NH2 
4069 N N   . LYS B 250 ? 0.3111 0.2473 0.3880 -0.0511 0.0352  0.0380  285 LYS B N   
4070 C CA  . LYS B 250 ? 0.3746 0.2859 0.4622 -0.0495 0.0369  0.0519  285 LYS B CA  
4071 C C   . LYS B 250 ? 0.3212 0.2509 0.3988 -0.0417 0.0411  0.0753  285 LYS B C   
4072 O O   . LYS B 250 ? 0.3219 0.2396 0.3961 -0.0320 0.0401  0.0830  285 LYS B O   
4073 C CB  . LYS B 250 ? 0.3580 0.2481 0.4742 -0.0656 0.0365  0.0578  285 LYS B CB  
4074 C CG  . LYS B 250 ? 0.5200 0.3862 0.6428 -0.0728 0.0312  0.0304  285 LYS B CG  
4075 C CD  . LYS B 250 ? 0.5306 0.3951 0.6767 -0.0941 0.0281  0.0301  285 LYS B CD  
4076 C CE  . LYS B 250 ? 0.5772 0.4016 0.7373 -0.1025 0.0237  0.0087  285 LYS B CE  
4077 N NZ  . LYS B 250 ? 0.7172 0.5426 0.8929 -0.1229 0.0178  0.0074  285 LYS B NZ  
4078 N N   . LYS B 251 ? 0.3278 0.2898 0.4000 -0.0455 0.0457  0.0861  286 LYS B N   
4079 C CA  . LYS B 251 ? 0.3323 0.3168 0.3885 -0.0388 0.0501  0.1052  286 LYS B CA  
4080 C C   . LYS B 251 ? 0.3236 0.3121 0.3545 -0.0236 0.0467  0.0931  286 LYS B C   
4081 O O   . LYS B 251 ? 0.2996 0.2883 0.3210 -0.0168 0.0450  0.1060  286 LYS B O   
4082 C CB  . LYS B 251 ? 0.3387 0.3604 0.3929 -0.0447 0.0580  0.1128  286 LYS B CB  
4083 C CG  . LYS B 251 ? 0.5011 0.5507 0.5368 -0.0405 0.0645  0.1326  286 LYS B CG  
4084 C CD  . LYS B 251 ? 0.4463 0.5359 0.4795 -0.0436 0.0747  0.1332  286 LYS B CD  
4085 C CE  . LYS B 251 ? 0.6089 0.7011 0.6743 -0.0595 0.0773  0.1391  286 LYS B CE  
4086 N NZ  . LYS B 251 ? 0.4931 0.6303 0.5627 -0.0634 0.0895  0.1463  286 LYS B NZ  
4087 N N   . ALA B 252 ? 0.3029 0.2952 0.3243 -0.0189 0.0444  0.0701  287 ALA B N   
4088 C CA  . ALA B 252 ? 0.2917 0.2867 0.2922 -0.0067 0.0407  0.0587  287 ALA B CA  
4089 C C   . ALA B 252 ? 0.3109 0.2814 0.3150 -0.0014 0.0355  0.0578  287 ALA B C   
4090 O O   . ALA B 252 ? 0.3331 0.3083 0.3259 0.0064  0.0326  0.0628  287 ALA B O   
4091 C CB  . ALA B 252 ? 0.3119 0.3125 0.3067 -0.0041 0.0388  0.0376  287 ALA B CB  
4092 N N   . PHE B 253 ? 0.2728 0.2193 0.2938 -0.0055 0.0345  0.0501  288 PHE B N   
4093 C CA  . PHE B 253 ? 0.2844 0.2092 0.3126 0.0014  0.0321  0.0470  288 PHE B CA  
4094 C C   . PHE B 253 ? 0.3346 0.2540 0.3737 0.0044  0.0318  0.0710  288 PHE B C   
4095 O O   . PHE B 253 ? 0.3404 0.2595 0.3785 0.0142  0.0286  0.0756  288 PHE B O   
4096 C CB  . PHE B 253 ? 0.3505 0.2509 0.3935 -0.0038 0.0327  0.0309  288 PHE B CB  
4097 C CG  . PHE B 253 ? 0.3212 0.2273 0.3515 -0.0053 0.0309  0.0088  288 PHE B CG  
4098 C CD1 . PHE B 253 ? 0.2748 0.2021 0.2866 -0.0008 0.0290  0.0053  288 PHE B CD1 
4099 C CD2 . PHE B 253 ? 0.3345 0.2239 0.3713 -0.0114 0.0307  -0.0087 288 PHE B CD2 
4100 C CE1 . PHE B 253 ? 0.3493 0.2814 0.3518 -0.0021 0.0263  -0.0108 288 PHE B CE1 
4101 C CE2 . PHE B 253 ? 0.4588 0.3570 0.4817 -0.0135 0.0279  -0.0259 288 PHE B CE2 
4102 C CZ  . PHE B 253 ? 0.3389 0.2585 0.3459 -0.0086 0.0256  -0.0248 288 PHE B CZ  
4103 N N   . ALA B 254 ? 0.2964 0.2137 0.3484 -0.0045 0.0345  0.0890  289 ALA B N   
4104 C CA  . ALA B 254 ? 0.3561 0.2692 0.4195 -0.0023 0.0334  0.1170  289 ALA B CA  
4105 C C   . ALA B 254 ? 0.3335 0.2762 0.3733 0.0044  0.0305  0.1302  289 ALA B C   
4106 O O   . ALA B 254 ? 0.3458 0.2874 0.3894 0.0124  0.0254  0.1449  289 ALA B O   
4107 C CB  . ALA B 254 ? 0.3998 0.3089 0.4803 -0.0158 0.0373  0.1365  289 ALA B CB  
4108 N N   . ASP B 255 ? 0.3184 0.2889 0.3344 0.0017  0.0333  0.1239  290 ASP B N   
4109 C CA  . ASP B 255 ? 0.3983 0.3971 0.3884 0.0067  0.0306  0.1323  290 ASP B CA  
4110 C C   . ASP B 255 ? 0.3153 0.3124 0.2965 0.0167  0.0229  0.1179  290 ASP B C   
4111 O O   . ASP B 255 ? 0.3306 0.3397 0.3039 0.0215  0.0163  0.1311  290 ASP B O   
4112 C CB  . ASP B 255 ? 0.4029 0.4297 0.3718 0.0028  0.0371  0.1243  290 ASP B CB  
4113 C CG  . ASP B 255 ? 0.4999 0.5577 0.4409 0.0051  0.0365  0.1359  290 ASP B CG  
4114 O OD1 . ASP B 255 ? 0.5794 0.6487 0.5202 0.0005  0.0379  0.1638  290 ASP B OD1 
4115 O OD2 . ASP B 255 ? 0.3958 0.4660 0.3145 0.0107  0.0339  0.1173  290 ASP B OD2 
4116 N N   . ALA B 256 ? 0.3065 0.2914 0.2898 0.0188  0.0230  0.0929  291 ALA B N   
4117 C CA  . ALA B 256 ? 0.3371 0.3213 0.3156 0.0265  0.0167  0.0808  291 ALA B CA  
4118 C C   . ALA B 256 ? 0.3480 0.3188 0.3482 0.0329  0.0128  0.0925  291 ALA B C   
4119 O O   . ALA B 256 ? 0.2900 0.2720 0.2878 0.0389  0.0057  0.0966  291 ALA B O   
4120 C CB  . ALA B 256 ? 0.3449 0.3196 0.3227 0.0261  0.0185  0.0557  291 ALA B CB  
4121 N N   . ALA B 257 ? 0.2883 0.2354 0.3128 0.0319  0.0171  0.0971  292 ALA B N   
4122 C CA  . ALA B 257 ? 0.2886 0.2206 0.3390 0.0404  0.0149  0.1076  292 ALA B CA  
4123 C C   . ALA B 257 ? 0.3894 0.3361 0.4418 0.0434  0.0082  0.1386  292 ALA B C   
4124 O O   . ALA B 257 ? 0.3413 0.2957 0.4029 0.0526  0.0015  0.1471  292 ALA B O   
4125 C CB  . ALA B 257 ? 0.3389 0.2384 0.4150 0.0380  0.0212  0.1032  292 ALA B CB  
4126 N N   . LYS B 258 ? 0.3274 0.2821 0.3715 0.0352  0.0098  0.1574  293 LYS B N   
4127 C CA  . LYS B 258 ? 0.3536 0.3265 0.3949 0.0356  0.0031  0.1858  293 LYS B CA  
4128 C C   . LYS B 258 ? 0.3244 0.3303 0.3376 0.0384  -0.0054 0.1851  293 LYS B C   
4129 O O   . LYS B 258 ? 0.3570 0.3756 0.3744 0.0422  -0.0144 0.1962  293 LYS B O   
4130 C CB  . LYS B 258 ? 0.3454 0.3251 0.3804 0.0238  0.0083  0.2003  293 LYS B CB  
4131 C CG  . LYS B 258 ? 0.5844 0.5810 0.6192 0.0223  0.0024  0.2246  293 LYS B CG  
4132 C CD  . LYS B 258 ? 0.6084 0.6111 0.6411 0.0105  0.0090  0.2390  293 LYS B CD  
4133 C CE  . LYS B 258 ? 0.6116 0.6445 0.6280 0.0078  0.0043  0.2604  293 LYS B CE  
4134 N NZ  . LYS B 258 ? 0.7666 0.8248 0.7593 -0.0023 0.0126  0.2623  293 LYS B NZ  
4135 N N   . GLY B 259 ? 0.3077 0.3275 0.2930 0.0350  -0.0029 0.1654  294 GLY B N   
4136 C CA  . GLY B 259 ? 0.3423 0.3909 0.2989 0.0356  -0.0111 0.1600  294 GLY B CA  
4137 C C   . GLY B 259 ? 0.3946 0.4420 0.3586 0.0419  -0.0189 0.1446  294 GLY B C   
4138 O O   . GLY B 259 ? 0.3783 0.4491 0.3259 0.0420  -0.0293 0.1453  294 GLY B O   
4139 N N   . GLY B 260 ? 0.3161 0.3392 0.3038 0.0461  -0.0140 0.1303  295 GLY B N   
4140 C CA  . GLY B 260 ? 0.3023 0.3272 0.2995 0.0512  -0.0191 0.1170  295 GLY B CA  
4141 C C   . GLY B 260 ? 0.3570 0.3920 0.3306 0.0464  -0.0215 0.0939  295 GLY B C   
4142 O O   . GLY B 260 ? 0.3356 0.3812 0.3129 0.0478  -0.0293 0.0886  295 GLY B O   
4143 N N   . TYR B 261 ? 0.2996 0.3318 0.2529 0.0408  -0.0153 0.0807  296 TYR B N   
4144 C CA  . TYR B 261 ? 0.2555 0.2935 0.1891 0.0373  -0.0175 0.0592  296 TYR B CA  
4145 C C   . TYR B 261 ? 0.2863 0.3052 0.2286 0.0369  -0.0107 0.0407  296 TYR B C   
4146 O O   . TYR B 261 ? 0.2620 0.2650 0.2213 0.0384  -0.0039 0.0416  296 TYR B O   
4147 C CB  . TYR B 261 ? 0.3193 0.3716 0.2244 0.0333  -0.0155 0.0563  296 TYR B CB  
4148 C CG  . TYR B 261 ? 0.2724 0.3192 0.1781 0.0315  -0.0037 0.0598  296 TYR B CG  
4149 C CD1 . TYR B 261 ? 0.2924 0.3265 0.2016 0.0306  0.0035  0.0429  296 TYR B CD1 
4150 C CD2 . TYR B 261 ? 0.3110 0.3680 0.2147 0.0295  -0.0007 0.0822  296 TYR B CD2 
4151 C CE1 . TYR B 261 ? 0.3462 0.3795 0.2594 0.0277  0.0130  0.0465  296 TYR B CE1 
4152 C CE2 . TYR B 261 ? 0.3690 0.4235 0.2765 0.0257  0.0101  0.0866  296 TYR B CE2 
4153 C CZ  . TYR B 261 ? 0.3827 0.4261 0.2958 0.0247  0.0167  0.0677  296 TYR B CZ  
4154 O OH  . TYR B 261 ? 0.3822 0.4269 0.3025 0.0199  0.0261  0.0719  296 TYR B OH  
4155 N N   . LEU B 262 ? 0.2679 0.2882 0.1980 0.0344  -0.0134 0.0237  297 LEU B N   
4156 C CA  . LEU B 262 ? 0.2506 0.2563 0.1880 0.0336  -0.0094 0.0097  297 LEU B CA  
4157 C C   . LEU B 262 ? 0.2603 0.2592 0.1919 0.0324  -0.0017 0.0032  297 LEU B C   
4158 O O   . LEU B 262 ? 0.2460 0.2540 0.1640 0.0320  0.0002  0.0027  297 LEU B O   
4159 C CB  . LEU B 262 ? 0.2571 0.2649 0.1882 0.0308  -0.0165 -0.0028 297 LEU B CB  
4160 C CG  . LEU B 262 ? 0.2860 0.3032 0.2280 0.0300  -0.0249 0.0022  297 LEU B CG  
4161 C CD1 . LEU B 262 ? 0.3317 0.3517 0.2654 0.0243  -0.0339 -0.0097 297 LEU B CD1 
4162 C CD2 . LEU B 262 ? 0.2916 0.3018 0.2549 0.0321  -0.0192 0.0043  297 LEU B CD2 
4163 N N   . ILE B 263 ? 0.2293 0.2156 0.1714 0.0315  0.0028  -0.0023 298 ILE B N   
4164 C CA  . ILE B 263 ? 0.2384 0.2214 0.1779 0.0297  0.0073  -0.0094 298 ILE B CA  
4165 C C   . ILE B 263 ? 0.2477 0.2240 0.1885 0.0287  0.0050  -0.0198 298 ILE B C   
4166 O O   . ILE B 263 ? 0.2304 0.2037 0.1761 0.0282  0.0026  -0.0204 298 ILE B O   
4167 C CB  . ILE B 263 ? 0.2596 0.2359 0.2098 0.0270  0.0134  -0.0044 298 ILE B CB  
4168 C CG1 . ILE B 263 ? 0.2864 0.2502 0.2477 0.0266  0.0144  -0.0081 298 ILE B CG1 
4169 C CG2 . ILE B 263 ? 0.2999 0.2812 0.2521 0.0269  0.0155  0.0105  298 ILE B CG2 
4170 C CD1 . ILE B 263 ? 0.4689 0.4232 0.4388 0.0220  0.0188  -0.0105 298 ILE B CD1 
4171 N N   . ALA B 264 ? 0.2312 0.2076 0.1698 0.0285  0.0060  -0.0258 299 ALA B N   
4172 C CA  . ALA B 264 ? 0.2474 0.2179 0.1887 0.0271  0.0032  -0.0313 299 ALA B CA  
4173 C C   . ALA B 264 ? 0.2562 0.2294 0.2016 0.0261  0.0054  -0.0325 299 ALA B C   
4174 O O   . ALA B 264 ? 0.2660 0.2471 0.2127 0.0274  0.0091  -0.0312 299 ALA B O   
4175 C CB  . ALA B 264 ? 0.2734 0.2412 0.2110 0.0289  -0.0025 -0.0367 299 ALA B CB  
4176 N N   . ALA B 265 ? 0.2292 0.1996 0.1771 0.0229  0.0031  -0.0336 300 ALA B N   
4177 C CA  . ALA B 265 ? 0.2052 0.1818 0.1583 0.0210  0.0025  -0.0338 300 ALA B CA  
4178 C C   . ALA B 265 ? 0.2067 0.1828 0.1597 0.0201  -0.0037 -0.0330 300 ALA B C   
4179 O O   . ALA B 265 ? 0.2378 0.2089 0.1855 0.0175  -0.0052 -0.0319 300 ALA B O   
4180 C CB  . ALA B 265 ? 0.2563 0.2332 0.2125 0.0145  0.0056  -0.0339 300 ALA B CB  
4181 N N   . SER B 266 ? 0.2172 0.2013 0.1781 0.0221  -0.0070 -0.0313 301 SER B N   
4182 C CA  . SER B 266 ? 0.2102 0.1943 0.1742 0.0231  -0.0145 -0.0264 301 SER B CA  
4183 C C   . SER B 266 ? 0.2189 0.2051 0.1734 0.0146  -0.0176 -0.0230 301 SER B C   
4184 O O   . SER B 266 ? 0.2281 0.2120 0.1804 0.0136  -0.0227 -0.0161 301 SER B O   
4185 C CB  . SER B 266 ? 0.2382 0.2352 0.2166 0.0271  -0.0178 -0.0236 301 SER B CB  
4186 O OG  . SER B 266 ? 0.4802 0.4809 0.4666 0.0349  -0.0118 -0.0285 301 SER B OG  
4187 N N   . HIS B 267 ? 0.1989 0.1895 0.1475 0.0078  -0.0146 -0.0279 302 HIS B N   
4188 C CA  . HIS B 267 ? 0.1988 0.1950 0.1355 -0.0004 -0.0169 -0.0285 302 HIS B CA  
4189 C C   . HIS B 267 ? 0.2103 0.1993 0.1375 -0.0034 -0.0088 -0.0365 302 HIS B C   
4190 O O   . HIS B 267 ? 0.2430 0.2371 0.1585 -0.0101 -0.0079 -0.0421 302 HIS B O   
4191 C CB  . HIS B 267 ? 0.2219 0.2312 0.1607 -0.0069 -0.0222 -0.0304 302 HIS B CB  
4192 C CG  . HIS B 267 ? 0.2541 0.2751 0.2070 -0.0025 -0.0303 -0.0211 302 HIS B CG  
4193 N ND1 . HIS B 267 ? 0.2249 0.2479 0.1793 0.0014  -0.0373 -0.0097 302 HIS B ND1 
4194 C CD2 . HIS B 267 ? 0.2160 0.2475 0.1861 -0.0002 -0.0317 -0.0202 302 HIS B CD2 
4195 C CE1 . HIS B 267 ? 0.2937 0.3268 0.2666 0.0074  -0.0433 -0.0031 302 HIS B CE1 
4196 N NE2 . HIS B 267 ? 0.1696 0.2101 0.1521 0.0067  -0.0394 -0.0099 302 HIS B NE2 
4197 N N   . LEU B 268 ? 0.2206 0.1998 0.1530 0.0020  -0.0030 -0.0378 303 LEU B N   
4198 C CA  . LEU B 268 ? 0.2467 0.2216 0.1751 0.0020  0.0041  -0.0420 303 LEU B CA  
4199 C C   . LEU B 268 ? 0.2152 0.1956 0.1381 0.0007  0.0028  -0.0356 303 LEU B C   
4200 O O   . LEU B 268 ? 0.2473 0.2276 0.1732 0.0017  -0.0037 -0.0269 303 LEU B O   
4201 C CB  . LEU B 268 ? 0.2418 0.2088 0.1795 0.0081  0.0080  -0.0412 303 LEU B CB  
4202 C CG  . LEU B 268 ? 0.2688 0.2307 0.2131 0.0080  0.0104  -0.0438 303 LEU B CG  
4203 C CD1 . LEU B 268 ? 0.2640 0.2217 0.2152 0.0138  0.0129  -0.0387 303 LEU B CD1 
4204 C CD2 . LEU B 268 ? 0.3109 0.2675 0.2544 0.0033  0.0148  -0.0533 303 LEU B CD2 
4205 N N   . PRO B 269 ? 0.2369 0.2223 0.1536 -0.0017 0.0096  -0.0394 304 PRO B N   
4206 C CA  . PRO B 269 ? 0.2450 0.2401 0.1568 -0.0051 0.0096  -0.0306 304 PRO B CA  
4207 C C   . PRO B 269 ? 0.2202 0.2096 0.1447 -0.0022 0.0058  -0.0216 304 PRO B C   
4208 O O   . PRO B 269 ? 0.2264 0.2108 0.1606 0.0025  0.0082  -0.0247 304 PRO B O   
4209 C CB  . PRO B 269 ? 0.2233 0.2262 0.1310 -0.0054 0.0213  -0.0392 304 PRO B CB  
4210 C CG  . PRO B 269 ? 0.3441 0.3402 0.2476 -0.0049 0.0247  -0.0544 304 PRO B CG  
4211 C CD  . PRO B 269 ? 0.2669 0.2497 0.1820 -0.0013 0.0185  -0.0522 304 PRO B CD  
4212 N N   . PHE B 270 ? 0.2354 0.2253 0.1604 -0.0056 -0.0015 -0.0101 305 PHE B N   
4213 C CA  . PHE B 270 ? 0.2182 0.1982 0.1557 -0.0043 -0.0073 -0.0042 305 PHE B CA  
4214 C C   . PHE B 270 ? 0.2279 0.2125 0.1735 -0.0054 -0.0024 -0.0045 305 PHE B C   
4215 O O   . PHE B 270 ? 0.2261 0.2248 0.1696 -0.0094 0.0049  -0.0018 305 PHE B O   
4216 C CB  . PHE B 270 ? 0.2191 0.1977 0.1585 -0.0093 -0.0149 0.0102  305 PHE B CB  
4217 C CG  . PHE B 270 ? 0.2592 0.2232 0.2134 -0.0095 -0.0216 0.0146  305 PHE B CG  
4218 C CD1 . PHE B 270 ? 0.2512 0.1995 0.2128 -0.0024 -0.0277 0.0083  305 PHE B CD1 
4219 C CD2 . PHE B 270 ? 0.2746 0.2416 0.2366 -0.0173 -0.0214 0.0233  305 PHE B CD2 
4220 C CE1 . PHE B 270 ? 0.2882 0.2203 0.2621 -0.0029 -0.0339 0.0077  305 PHE B CE1 
4221 C CE2 . PHE B 270 ? 0.2837 0.2348 0.2607 -0.0196 -0.0291 0.0250  305 PHE B CE2 
4222 C CZ  . PHE B 270 ? 0.2841 0.2161 0.2658 -0.0122 -0.0356 0.0158  305 PHE B CZ  
4223 N N   . PRO B 271 ? 0.2300 0.2067 0.1850 -0.0021 -0.0060 -0.0080 306 PRO B N   
4224 C CA  . PRO B 271 ? 0.2084 0.1713 0.1647 0.0026  -0.0131 -0.0128 306 PRO B CA  
4225 C C   . PRO B 271 ? 0.2274 0.1895 0.1783 0.0093  -0.0097 -0.0210 306 PRO B C   
4226 O O   . PRO B 271 ? 0.2545 0.2101 0.2053 0.0136  -0.0129 -0.0255 306 PRO B O   
4227 C CB  . PRO B 271 ? 0.2437 0.2044 0.2090 0.0006  -0.0176 -0.0138 306 PRO B CB  
4228 C CG  . PRO B 271 ? 0.2538 0.2299 0.2237 -0.0002 -0.0109 -0.0121 306 PRO B CG  
4229 C CD  . PRO B 271 ? 0.2668 0.2522 0.2323 -0.0032 -0.0034 -0.0073 306 PRO B CD  
4230 N N   . GLY B 272 ? 0.2161 0.1847 0.1638 0.0100  -0.0024 -0.0236 307 GLY B N   
4231 C CA  . GLY B 272 ? 0.2600 0.2263 0.2051 0.0137  0.0004  -0.0288 307 GLY B CA  
4232 C C   . GLY B 272 ? 0.2670 0.2319 0.2153 0.0182  0.0008  -0.0297 307 GLY B C   
4233 O O   . GLY B 272 ? 0.2380 0.2017 0.1848 0.0205  0.0020  -0.0311 307 GLY B O   
4234 N N   . ILE B 273 ? 0.2176 0.1859 0.1710 0.0187  -0.0005 -0.0272 308 ILE B N   
4235 C CA  . ILE B 273 ? 0.2330 0.2040 0.1875 0.0221  -0.0028 -0.0256 308 ILE B CA  
4236 C C   . ILE B 273 ? 0.2492 0.2257 0.2141 0.0249  0.0015  -0.0210 308 ILE B C   
4237 O O   . ILE B 273 ? 0.2276 0.2097 0.2010 0.0239  0.0040  -0.0201 308 ILE B O   
4238 C CB  . ILE B 273 ? 0.2482 0.2207 0.2018 0.0198  -0.0112 -0.0268 308 ILE B CB  
4239 C CG1 . ILE B 273 ? 0.2311 0.1942 0.1791 0.0192  -0.0148 -0.0327 308 ILE B CG1 
4240 C CG2 . ILE B 273 ? 0.2647 0.2447 0.2151 0.0221  -0.0151 -0.0251 308 ILE B CG2 
4241 C CD1 . ILE B 273 ? 0.2463 0.2047 0.1965 0.0152  -0.0232 -0.0363 308 ILE B CD1 
4242 N N   . GLY B 274 ? 0.2392 0.2045 0.2264 0.0104  -0.0053 0.0100  309 GLY B N   
4243 C CA  . GLY B 274 ? 0.2074 0.1680 0.1947 0.0117  0.0037  0.0128  309 GLY B CA  
4244 C C   . GLY B 274 ? 0.2636 0.2422 0.2625 0.0133  0.0019  0.0215  309 GLY B C   
4245 O O   . GLY B 274 ? 0.2115 0.2093 0.2119 0.0118  -0.0047 0.0226  309 GLY B O   
4246 N N   . HIS B 275 ? 0.2049 0.1796 0.2177 0.0151  0.0076  0.0289  310 HIS B N   
4247 C CA  . HIS B 275 ? 0.1798 0.1685 0.2097 0.0137  0.0033  0.0442  310 HIS B CA  
4248 C C   . HIS B 275 ? 0.2635 0.2253 0.2922 0.0099  0.0067  0.0439  310 HIS B C   
4249 O O   . HIS B 275 ? 0.2532 0.1884 0.2662 0.0059  0.0145  0.0304  310 HIS B O   
4250 C CB  . HIS B 275 ? 0.2336 0.2346 0.2938 0.0170  0.0046  0.0585  310 HIS B CB  
4251 C CG  . HIS B 275 ? 0.2213 0.2553 0.2817 0.0157  0.0004  0.0613  310 HIS B CG  
4252 N ND1 . HIS B 275 ? 0.2413 0.2693 0.2970 0.0197  0.0066  0.0503  310 HIS B ND1 
4253 C CD2 . HIS B 275 ? 0.2742 0.3506 0.3369 0.0065  -0.0086 0.0725  310 HIS B CD2 
4254 C CE1 . HIS B 275 ? 0.1927 0.2550 0.2492 0.0147  0.0018  0.0538  310 HIS B CE1 
4255 N NE2 . HIS B 275 ? 0.1987 0.2927 0.2581 0.0051  -0.0067 0.0661  310 HIS B NE2 
4256 N N   . ILE B 276 ? 0.2272 0.1992 0.2720 0.0072  0.0005  0.0595  311 ILE B N   
4257 C CA  . ILE B 276 ? 0.3253 0.2726 0.3743 0.0022  0.0036  0.0598  311 ILE B CA  
4258 C C   . ILE B 276 ? 0.2531 0.2008 0.3470 0.0040  0.0024  0.0791  311 ILE B C   
4259 O O   . ILE B 276 ? 0.2250 0.2057 0.3365 0.0026  -0.0100 0.1021  311 ILE B O   
4260 C CB  . ILE B 276 ? 0.3531 0.3107 0.3798 -0.0055 -0.0062 0.0625  311 ILE B CB  
4261 C CG1 . ILE B 276 ? 0.5271 0.4891 0.5254 -0.0060 -0.0082 0.0492  311 ILE B CG1 
4262 C CG2 . ILE B 276 ? 0.4946 0.4247 0.5225 -0.0132 -0.0024 0.0612  311 ILE B CG2 
4263 C CD1 . ILE B 276 ? 0.7264 0.6586 0.7034 -0.0140 -0.0028 0.0375  311 ILE B CD1 
4264 N N   . ARG B 277 ? 0.2543 0.1680 0.3712 0.0041  0.0153  0.0702  312 ARG B N   
4265 C CA  . ARG B 277 ? 0.2613 0.1737 0.4304 0.0055  0.0126  0.0881  312 ARG B CA  
4266 C C   . ARG B 277 ? 0.2783 0.1658 0.4471 -0.0025 0.0170  0.0791  312 ARG B C   
4267 O O   . ARG B 277 ? 0.3361 0.1939 0.4802 -0.0092 0.0316  0.0533  312 ARG B O   
4268 C CB  . ARG B 277 ? 0.5208 0.4351 0.7354 0.0141  0.0223  0.0845  312 ARG B CB  
4269 C CG  . ARG B 277 ? 0.5951 0.4842 0.8026 0.0165  0.0447  0.0528  312 ARG B CG  
4270 C CD  . ARG B 277 ? 0.4716 0.3636 0.7386 0.0216  0.0558  0.0493  312 ARG B CD  
4271 N NE  . ARG B 277 ? 0.7247 0.6208 0.9954 0.0259  0.0674  0.0372  312 ARG B NE  
4272 C CZ  . ARG B 277 ? 0.8890 0.7679 1.1375 0.0209  0.0874  0.0056  312 ARG B CZ  
4273 N NH1 . ARG B 277 ? 0.7559 0.6138 0.9796 0.0096  0.0997  -0.0185 312 ARG B NH1 
4274 N NH2 . ARG B 277 ? 0.7192 0.6064 0.9693 0.0237  0.0949  -0.0011 312 ARG B NH2 
4275 N N   . ALA B 278 ? 0.2780 0.1820 0.4710 -0.0055 0.0035  0.1005  313 ALA B N   
4276 C CA  . ALA B 278 ? 0.2794 0.1607 0.4762 -0.0130 0.0066  0.0941  313 ALA B CA  
4277 C C   . ALA B 278 ? 0.3389 0.1959 0.5782 -0.0085 0.0254  0.0742  313 ALA B C   
4278 O O   . ALA B 278 ? 0.3343 0.2068 0.6257 0.0002  0.0250  0.0847  313 ALA B O   
4279 C CB  . ALA B 278 ? 0.3702 0.2808 0.5849 -0.0182 -0.0142 0.1242  313 ALA B CB  
4280 N N   . GLU B 279 ? 0.3204 0.1456 0.5396 -0.0173 0.0424  0.0447  314 GLU B N   
4281 C CA  . GLU B 279 ? 0.3510 0.1590 0.6089 -0.0167 0.0639  0.0197  314 GLU B CA  
4282 C C   . GLU B 279 ? 0.3824 0.1658 0.6243 -0.0315 0.0719  0.0016  314 GLU B C   
4283 O O   . GLU B 279 ? 0.3982 0.1721 0.5822 -0.0461 0.0720  -0.0101 314 GLU B O   
4284 C CB  . GLU B 279 ? 0.3888 0.1929 0.6322 -0.0170 0.0847  -0.0097 314 GLU B CB  
4285 C CG  . GLU B 279 ? 0.5780 0.4029 0.8261 -0.0052 0.0788  0.0033  314 GLU B CG  
4286 C CD  . GLU B 279 ? 0.6645 0.4878 0.9163 -0.0061 0.1017  -0.0251 314 GLU B CD  
4287 O OE1 . GLU B 279 ? 0.6848 0.5248 0.9686 0.0045  0.1014  -0.0157 314 GLU B OE1 
4288 O OE2 . GLU B 279 ? 0.6423 0.4524 0.8640 -0.0208 0.1195  -0.0557 314 GLU B OE2 
4289 N N   . GLY B 280 ? 0.4096 0.1856 0.7069 -0.0294 0.0784  -0.0001 315 GLY B N   
4290 C CA  . GLY B 280 ? 0.4449 0.1975 0.7323 -0.0443 0.0881  -0.0198 315 GLY B CA  
4291 C C   . GLY B 280 ? 0.4590 0.2084 0.6970 -0.0562 0.0679  -0.0017 315 GLY B C   
4292 O O   . GLY B 280 ? 0.4151 0.1818 0.6619 -0.0503 0.0457  0.0331  315 GLY B O   
4293 N N   . LYS B 281 ? 0.5651 0.3005 0.7514 -0.0759 0.0757  -0.0248 316 LYS B N   
4294 C CA  . LYS B 281 ? 0.5597 0.2949 0.7013 -0.0910 0.0584  -0.0099 316 LYS B CA  
4295 C C   . LYS B 281 ? 0.4635 0.2179 0.5607 -0.0917 0.0451  0.0052  316 LYS B C   
4296 O O   . LYS B 281 ? 0.4837 0.2469 0.5520 -0.1021 0.0301  0.0229  316 LYS B O   
4297 C CB  . LYS B 281 ? 0.5355 0.2576 0.6448 -0.1141 0.0716  -0.0396 316 LYS B CB  
4298 C CG  . LYS B 281 ? 0.7136 0.4159 0.8575 -0.1199 0.0787  -0.0480 316 LYS B CG  
4299 C CD  . LYS B 281 ? 0.8701 0.5643 1.0626 -0.1128 0.1073  -0.0784 316 LYS B CD  
4300 C CE  . LYS B 281 ? 0.6543 0.3318 0.8555 -0.1305 0.1267  -0.1079 316 LYS B CE  
4301 N NZ  . LYS B 281 ? 0.7382 0.4005 0.9586 -0.1330 0.1095  -0.0862 316 LYS B NZ  
4302 N N   . GLY B 282 ? 0.3904 0.1537 0.4849 -0.0814 0.0517  -0.0016 317 GLY B N   
4303 C CA  . GLY B 282 ? 0.4430 0.2225 0.4983 -0.0824 0.0425  0.0091  317 GLY B CA  
4304 C C   . GLY B 282 ? 0.4662 0.2605 0.5422 -0.0628 0.0406  0.0196  317 GLY B C   
4305 O O   . GLY B 282 ? 0.3864 0.1941 0.5044 -0.0478 0.0319  0.0398  317 GLY B O   
4306 N N   . TYR B 283 ? 0.3876 0.1882 0.4290 -0.0639 0.0455  0.0069  318 TYR B N   
4307 C CA  . TYR B 283 ? 0.3701 0.1920 0.4194 -0.0465 0.0395  0.0174  318 TYR B CA  
4308 C C   . TYR B 283 ? 0.4125 0.2244 0.4466 -0.0500 0.0567  -0.0081 318 TYR B C   
4309 O O   . TYR B 283 ? 0.3964 0.1954 0.3980 -0.0698 0.0682  -0.0306 318 TYR B O   
4310 C CB  . TYR B 283 ? 0.3305 0.1870 0.3495 -0.0423 0.0180  0.0366  318 TYR B CB  
4311 C CG  . TYR B 283 ? 0.2951 0.1693 0.3282 -0.0423 0.0022  0.0609  318 TYR B CG  
4312 C CD1 . TYR B 283 ? 0.3859 0.2562 0.3993 -0.0556 -0.0032 0.0624  318 TYR B CD1 
4313 C CD2 . TYR B 283 ? 0.2980 0.1964 0.3639 -0.0330 -0.0081 0.0844  318 TYR B CD2 
4314 C CE1 . TYR B 283 ? 0.3862 0.2754 0.4123 -0.0582 -0.0177 0.0854  318 TYR B CE1 
4315 C CE2 . TYR B 283 ? 0.3214 0.2418 0.3984 -0.0387 -0.0236 0.1088  318 TYR B CE2 
4316 C CZ  . TYR B 283 ? 0.3394 0.2546 0.3968 -0.0504 -0.0279 0.1087  318 TYR B CZ  
4317 O OH  . TYR B 283 ? 0.3973 0.3413 0.4632 -0.0561 -0.0426 0.1287  318 TYR B OH  
4318 N N   . ARG B 284 ? 0.3400 0.1623 0.3976 -0.0344 0.0578  -0.0029 319 ARG B N   
4319 C CA  . ARG B 284 ? 0.3433 0.1631 0.3890 -0.0358 0.0712  -0.0223 319 ARG B CA  
4320 C C   . ARG B 284 ? 0.3515 0.1985 0.3765 -0.0253 0.0545  -0.0065 319 ARG B C   
4321 O O   . ARG B 284 ? 0.3619 0.2286 0.4104 -0.0111 0.0428  0.0142  319 ARG B O   
4322 C CB  . ARG B 284 ? 0.3611 0.1814 0.4606 -0.0236 0.0843  -0.0282 319 ARG B CB  
4323 C CG  . ARG B 284 ? 0.5477 0.3755 0.6432 -0.0209 0.0949  -0.0409 319 ARG B CG  
4324 C CD  . ARG B 284 ? 0.7403 0.5635 0.8107 -0.0405 0.1149  -0.0722 319 ARG B CD  
4325 N NE  . ARG B 284 ? 0.8691 0.6846 0.9614 -0.0487 0.1282  -0.0868 319 ARG B NE  
4326 C CZ  . ARG B 284 ? 0.7577 0.5719 0.8235 -0.0717 0.1447  -0.1120 319 ARG B CZ  
4327 N NH1 . ARG B 284 ? 0.9289 0.7525 0.9453 -0.0911 0.1484  -0.1224 319 ARG B NH1 
4328 N NH2 . ARG B 284 ? 0.6692 0.4759 0.7601 -0.0780 0.1574  -0.1252 319 ARG B NH2 
4329 N N   . PHE B 285 ? 0.3563 0.2067 0.3401 -0.0356 0.0530  -0.0156 320 PHE B N   
4330 C CA  . PHE B 285 ? 0.3123 0.1834 0.2834 -0.0270 0.0400  -0.0054 320 PHE B CA  
4331 C C   . PHE B 285 ? 0.3173 0.1874 0.3014 -0.0215 0.0516  -0.0146 320 PHE B C   
4332 O O   . PHE B 285 ? 0.3577 0.2133 0.3365 -0.0336 0.0687  -0.0342 320 PHE B O   
4333 C CB  . PHE B 285 ? 0.3176 0.1918 0.2499 -0.0419 0.0302  -0.0056 320 PHE B CB  
4334 C CG  . PHE B 285 ? 0.2954 0.1866 0.2246 -0.0339 0.0174  0.0031  320 PHE B CG  
4335 C CD1 . PHE B 285 ? 0.2789 0.1903 0.2251 -0.0188 0.0064  0.0139  320 PHE B CD1 
4336 C CD2 . PHE B 285 ? 0.3740 0.2632 0.2849 -0.0451 0.0167  -0.0006 320 PHE B CD2 
4337 C CE1 . PHE B 285 ? 0.2781 0.2034 0.2286 -0.0126 -0.0021 0.0163  320 PHE B CE1 
4338 C CE2 . PHE B 285 ? 0.3124 0.2139 0.2289 -0.0379 0.0044  0.0079  320 PHE B CE2 
4339 C CZ  . PHE B 285 ? 0.2668 0.1843 0.2057 -0.0204 -0.0036 0.0140  320 PHE B CZ  
4340 N N   . VAL B 286 ? 0.2719 0.1606 0.2723 -0.0064 0.0437  -0.0024 321 VAL B N   
4341 C CA  . VAL B 286 ? 0.2825 0.1747 0.2974 -0.0002 0.0522  -0.0072 321 VAL B CA  
4342 C C   . VAL B 286 ? 0.2614 0.1684 0.2547 0.0012  0.0407  -0.0035 321 VAL B C   
4343 O O   . VAL B 286 ? 0.2474 0.1751 0.2492 0.0102  0.0298  0.0077  321 VAL B O   
4344 C CB  . VAL B 286 ? 0.3023 0.2058 0.3642 0.0136  0.0527  0.0069  321 VAL B CB  
4345 C CG1 . VAL B 286 ? 0.3584 0.2669 0.4389 0.0192  0.0621  0.0025  321 VAL B CG1 
4346 C CG2 . VAL B 286 ? 0.2984 0.1843 0.3944 0.0130  0.0618  0.0064  321 VAL B CG2 
4347 N N   . PRO B 287 ? 0.2791 0.1782 0.2461 -0.0111 0.0427  -0.0130 322 PRO B N   
4348 C CA  . PRO B 287 ? 0.2932 0.2028 0.2490 -0.0103 0.0302  -0.0075 322 PRO B CA  
4349 C C   . PRO B 287 ? 0.2690 0.1925 0.2443 0.0023  0.0319  -0.0055 322 PRO B C   
4350 O O   . PRO B 287 ? 0.2839 0.2067 0.2758 0.0059  0.0440  -0.0092 322 PRO B O   
4351 C CB  . PRO B 287 ? 0.3173 0.2172 0.2461 -0.0304 0.0329  -0.0142 322 PRO B CB  
4352 C CG  . PRO B 287 ? 0.4560 0.3431 0.3734 -0.0454 0.0464  -0.0263 322 PRO B CG  
4353 C CD  . PRO B 287 ? 0.3310 0.2141 0.2808 -0.0298 0.0573  -0.0297 322 PRO B CD  
4354 N N   . VAL B 288 ? 0.2389 0.1766 0.2169 0.0077  0.0204  -0.0006 323 VAL B N   
4355 C CA  . VAL B 288 ? 0.2613 0.2157 0.2534 0.0150  0.0214  0.0002  323 VAL B CA  
4356 C C   . VAL B 288 ? 0.3147 0.2609 0.3010 0.0103  0.0288  -0.0052 323 VAL B C   
4357 O O   . VAL B 288 ? 0.2722 0.2052 0.2396 -0.0011 0.0276  -0.0086 323 VAL B O   
4358 C CB  . VAL B 288 ? 0.2609 0.2313 0.2580 0.0174  0.0116  -0.0013 323 VAL B CB  
4359 C CG1 . VAL B 288 ? 0.3268 0.3150 0.3317 0.0197  0.0077  0.0012  323 VAL B CG1 
4360 C CG2 . VAL B 288 ? 0.2664 0.2225 0.2573 0.0118  0.0035  -0.0034 323 VAL B CG2 
4361 N N   . ASN B 289 ? 0.3023 0.2608 0.3060 0.0164  0.0354  -0.0032 324 ASN B N   
4362 C CA  . ASN B 289 ? 0.2937 0.2514 0.2961 0.0128  0.0426  -0.0082 324 ASN B CA  
4363 C C   . ASN B 289 ? 0.2308 0.1914 0.2210 0.0088  0.0321  -0.0086 324 ASN B C   
4364 O O   . ASN B 289 ? 0.2544 0.2284 0.2523 0.0134  0.0241  -0.0069 324 ASN B O   
4365 C CB  . ASN B 289 ? 0.3361 0.3124 0.3685 0.0214  0.0482  -0.0008 324 ASN B CB  
4366 C CG  . ASN B 289 ? 0.6870 0.6671 0.7238 0.0188  0.0567  -0.0053 324 ASN B CG  
4367 O OD1 . ASN B 289 ? 0.7328 0.6992 0.7573 0.0101  0.0667  -0.0173 324 ASN B OD1 
4368 N ND2 . ASN B 289 ? 0.3863 0.3895 0.4391 0.0227  0.0529  0.0043  324 ASN B ND2 
4369 N N   . TYR B 290 ? 0.2621 0.2123 0.2364 -0.0025 0.0329  -0.0119 325 TYR B N   
4370 C CA  . TYR B 290 ? 0.2174 0.1680 0.1886 -0.0072 0.0218  -0.0094 325 TYR B CA  
4371 C C   . TYR B 290 ? 0.2800 0.2486 0.2669 0.0008  0.0228  -0.0105 325 TYR B C   
4372 O O   . TYR B 290 ? 0.2548 0.2349 0.2484 0.0032  0.0322  -0.0101 325 TYR B O   
4373 C CB  . TYR B 290 ? 0.3121 0.2559 0.2648 -0.0243 0.0232  -0.0090 325 TYR B CB  
4374 C CG  . TYR B 290 ? 0.2822 0.2248 0.2373 -0.0308 0.0098  -0.0022 325 TYR B CG  
4375 C CD1 . TYR B 290 ? 0.3053 0.2381 0.2683 -0.0353 -0.0076 0.0074  325 TYR B CD1 
4376 C CD2 . TYR B 290 ? 0.2698 0.2211 0.2266 -0.0326 0.0138  -0.0041 325 TYR B CD2 
4377 C CE1 . TYR B 290 ? 0.3734 0.3024 0.3505 -0.0409 -0.0206 0.0150  325 TYR B CE1 
4378 C CE2 . TYR B 290 ? 0.2862 0.2343 0.2485 -0.0396 0.0014  0.0022  325 TYR B CE2 
4379 C CZ  . TYR B 290 ? 0.3436 0.2792 0.3185 -0.0436 -0.0159 0.0117  325 TYR B CZ  
4380 O OH  . TYR B 290 ? 0.3219 0.2516 0.3137 -0.0502 -0.0290 0.0192  325 TYR B OH  
4381 N N   . SER B 291 ? 0.2251 0.1983 0.2219 0.0029  0.0139  -0.0130 326 SER B N   
4382 C CA  . SER B 291 ? 0.2503 0.2445 0.2581 0.0046  0.0156  -0.0176 326 SER B CA  
4383 C C   . SER B 291 ? 0.3169 0.3039 0.3347 -0.0001 0.0082  -0.0248 326 SER B C   
4384 O O   . SER B 291 ? 0.2958 0.2697 0.3259 0.0005  0.0006  -0.0269 326 SER B O   
4385 C CB  . SER B 291 ? 0.2477 0.2652 0.2645 0.0086  0.0172  -0.0196 326 SER B CB  
4386 O OG  . SER B 291 ? 0.3413 0.3861 0.3638 0.0032  0.0189  -0.0240 326 SER B OG  
4387 N N   . VAL B 292 ? 0.2171 0.2130 0.2362 -0.0049 0.0099  -0.0275 327 VAL B N   
4388 C CA  . VAL B 292 ? 0.2494 0.2376 0.2847 -0.0103 0.0041  -0.0359 327 VAL B CA  
4389 C C   . VAL B 292 ? 0.2703 0.2791 0.3231 -0.0108 0.0094  -0.0551 327 VAL B C   
4390 O O   . VAL B 292 ? 0.2634 0.3018 0.3070 -0.0137 0.0165  -0.0576 327 VAL B O   
4391 C CB  . VAL B 292 ? 0.2768 0.2663 0.3036 -0.0183 0.0043  -0.0313 327 VAL B CB  
4392 C CG1 . VAL B 292 ? 0.2982 0.2793 0.3473 -0.0248 -0.0013 -0.0410 327 VAL B CG1 
4393 C CG2 . VAL B 292 ? 0.3386 0.3135 0.3469 -0.0235 0.0015  -0.0167 327 VAL B CG2 
4394 N N   . VAL B 293 ? 0.2370 0.2334 0.3195 -0.0109 0.0062  -0.0684 328 VAL B N   
4395 C CA  . VAL B 293 ? 0.2413 0.2576 0.3466 -0.0156 0.0154  -0.0957 328 VAL B CA  
4396 C C   . VAL B 293 ? 0.3558 0.3645 0.4825 -0.0240 0.0163  -0.1093 328 VAL B C   
4397 O O   . VAL B 293 ? 0.3278 0.3066 0.4736 -0.0224 0.0054  -0.0987 328 VAL B O   
4398 C CB  . VAL B 293 ? 0.2474 0.2572 0.3843 -0.0090 0.0155  -0.1074 328 VAL B CB  
4399 C CG1 . VAL B 293 ? 0.2475 0.2836 0.4105 -0.0177 0.0304  -0.1437 328 VAL B CG1 
4400 C CG2 . VAL B 293 ? 0.2310 0.2458 0.3446 -0.0021 0.0132  -0.0918 328 VAL B CG2 
4401 N N   . ASN B 294 ? 0.3078 0.3461 0.4312 -0.0366 0.0281  -0.1310 329 ASN B N   
4402 C CA  . ASN B 294 ? 0.3649 0.3994 0.5090 -0.0478 0.0321  -0.1499 329 ASN B CA  
4403 C C   . ASN B 294 ? 0.2278 0.2889 0.3958 -0.0555 0.0484  -0.1798 329 ASN B C   
4404 O O   . ASN B 294 ? 0.3287 0.4207 0.4874 -0.0597 0.0569  -0.1884 329 ASN B O   
4405 C CB  . ASN B 294 ? 0.3651 0.4188 0.4741 -0.0588 0.0321  -0.1383 329 ASN B CB  
4406 C CG  . ASN B 294 ? 0.3724 0.4037 0.4627 -0.0504 0.0196  -0.1057 329 ASN B CG  
4407 O OD1 . ASN B 294 ? 0.4316 0.4788 0.4925 -0.0481 0.0193  -0.0866 329 ASN B OD1 
4408 N ND2 . ASN B 294 ? 0.3704 0.3672 0.4826 -0.0483 0.0094  -0.0991 329 ASN B ND2 
4409 N N   . ALA B 295 ? 0.3093 0.3907 0.4947 -0.0635 0.0341  -0.1926 330 ALA B N   
4410 C CA  . ALA B 295 ? 0.3628 0.4493 0.6016 -0.0563 0.0642  -0.1625 330 ALA B CA  
4411 C C   . ALA B 295 ? 0.4116 0.5037 0.6532 -0.0555 0.1015  -0.1469 330 ALA B C   
4412 O O   . ALA B 295 ? 0.4180 0.5156 0.6476 -0.0348 0.0822  -0.1530 330 ALA B O   
4413 C CB  . ALA B 295 ? 0.3669 0.4433 0.6390 -0.0531 0.0629  -0.1489 330 ALA B CB  
4414 N N   . ALA B 296 ? 0.4542 0.5379 0.6950 -0.0645 0.1503  -0.1257 331 ALA B N   
4415 C CA  . ALA B 296 ? 0.4858 0.5542 0.7407 -0.0755 0.1954  -0.1053 331 ALA B CA  
4416 C C   . ALA B 296 ? 0.5017 0.5687 0.7603 -0.0840 0.2224  -0.0910 331 ALA B C   
4417 O O   . ALA B 296 ? 0.5117 0.5786 0.7743 -0.0928 0.2464  -0.0761 331 ALA B O   
4418 C CB  . ALA B 296 ? 0.4918 0.5532 0.7394 -0.0719 0.2163  -0.1119 331 ALA B CB  
# 
