data_9QI5
# 
_entry.id   9QI5 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.404 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9QI5         pdb_00009qi5 10.2210/pdb9qi5/pdb 
WWPDB D_1292145485 ?            ?                   
# 
_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                        9QI5 
_pdbx_database_status.recvd_initial_deposition_date   2025-03-17 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 3 
_pdbx_contact_author.email              m.ubbink@chem.leidenuniv.nl 
_pdbx_contact_author.name_first         Marcellus 
_pdbx_contact_author.name_last          Ubbink 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-2615-6914 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Chikunova, A.'  1 0000-0002-2818-0539 
'Radojkovic, M.' 2 0000-0003-4954-9021 
'Ubbink, M.'     3 0000-0002-2615-6914 
# 
_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                     'High-resolution activity and inhibitor profiling of residue 105 in class A beta-lactamases' 
_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 'Radojkovic, M.'  1 0000-0003-4954-9021 
primary 'Koene, S.F.'     2 ?                   
primary 'Chikunova, A.'   3 0000-0002-2818-0539 
primary 'Timmer, M.'      4 ?                   
primary 'Natarajan, S.V.' 5 ?                   
primary 'Ubbink, M.'      6 0000-0002-2615-6914 
# 
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 Beta-lactamase 28373.812 2   3.5.2.6 I105R ? ? 
2 non-polymer syn GLYCEROL       92.094    5   ?       ?     ? ? 
3 non-polymer syn 'ZINC ION'     65.409    1   ?       ?     ? ? 
4 water       nat water          18.015    261 ?       ?     ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Ambler class A beta-lactamase' 
# 
_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       
;GDLADRFAELERRYDARLGVYVPATGTTAAIEYRADERFAFCSTFKAPLVAAVLHQNPLTHLDKLITYTSDDIRSRSPVA
QQHVQTGMTIGQLCDAAIRYSDGTAANLLLADLGGPGGGTAAFTGYLRSLGDTVSRLDAEEPELNRDPPGDERDTTTPHA
IALVLQQLVLGNALPPDKRALLTDWMARNTTGAKRIRAGFPADWKVIDKTGTGDYGRANDIAVVWSPTGVPYVVAVMSDR
AGGGYDAEPREALLAEAATCVAGVLA
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GDLADRFAELERRYDARLGVYVPATGTTAAIEYRADERFAFCSTFKAPLVAAVLHQNPLTHLDKLITYTSDDIRSRSPVA
QQHVQTGMTIGQLCDAAIRYSDGTAANLLLADLGGPGGGTAAFTGYLRSLGDTVSRLDAEEPELNRDPPGDERDTTTPHA
IALVLQQLVLGNALPPDKRALLTDWMARNTTGAKRIRAGFPADWKVIDKTGTGDYGRANDIAVVWSPTGVPYVVAVMSDR
AGGGYDAEPREALLAEAATCVAGVLA
;
_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 GLYCEROL   GOL 
3 'ZINC ION' ZN  
4 water      HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   ASP n 
1 3   LEU n 
1 4   ALA n 
1 5   ASP n 
1 6   ARG n 
1 7   PHE n 
1 8   ALA n 
1 9   GLU n 
1 10  LEU n 
1 11  GLU n 
1 12  ARG n 
1 13  ARG n 
1 14  TYR n 
1 15  ASP n 
1 16  ALA n 
1 17  ARG n 
1 18  LEU n 
1 19  GLY n 
1 20  VAL n 
1 21  TYR n 
1 22  VAL n 
1 23  PRO n 
1 24  ALA n 
1 25  THR n 
1 26  GLY n 
1 27  THR n 
1 28  THR n 
1 29  ALA n 
1 30  ALA n 
1 31  ILE n 
1 32  GLU n 
1 33  TYR n 
1 34  ARG n 
1 35  ALA n 
1 36  ASP n 
1 37  GLU n 
1 38  ARG n 
1 39  PHE n 
1 40  ALA n 
1 41  PHE n 
1 42  CYS n 
1 43  SER n 
1 44  THR n 
1 45  PHE n 
1 46  LYS n 
1 47  ALA n 
1 48  PRO n 
1 49  LEU n 
1 50  VAL n 
1 51  ALA n 
1 52  ALA n 
1 53  VAL n 
1 54  LEU n 
1 55  HIS n 
1 56  GLN n 
1 57  ASN n 
1 58  PRO n 
1 59  LEU n 
1 60  THR n 
1 61  HIS n 
1 62  LEU n 
1 63  ASP n 
1 64  LYS n 
1 65  LEU n 
1 66  ILE n 
1 67  THR n 
1 68  TYR n 
1 69  THR n 
1 70  SER n 
1 71  ASP n 
1 72  ASP n 
1 73  ILE n 
1 74  ARG n 
1 75  SER n 
1 76  ARG n 
1 77  SER n 
1 78  PRO n 
1 79  VAL n 
1 80  ALA n 
1 81  GLN n 
1 82  GLN n 
1 83  HIS n 
1 84  VAL n 
1 85  GLN n 
1 86  THR n 
1 87  GLY n 
1 88  MET n 
1 89  THR n 
1 90  ILE n 
1 91  GLY n 
1 92  GLN n 
1 93  LEU n 
1 94  CYS n 
1 95  ASP n 
1 96  ALA n 
1 97  ALA n 
1 98  ILE n 
1 99  ARG n 
1 100 TYR n 
1 101 SER n 
1 102 ASP n 
1 103 GLY n 
1 104 THR n 
1 105 ALA n 
1 106 ALA n 
1 107 ASN n 
1 108 LEU n 
1 109 LEU n 
1 110 LEU n 
1 111 ALA n 
1 112 ASP n 
1 113 LEU n 
1 114 GLY n 
1 115 GLY n 
1 116 PRO n 
1 117 GLY n 
1 118 GLY n 
1 119 GLY n 
1 120 THR n 
1 121 ALA n 
1 122 ALA n 
1 123 PHE n 
1 124 THR n 
1 125 GLY n 
1 126 TYR n 
1 127 LEU n 
1 128 ARG n 
1 129 SER n 
1 130 LEU n 
1 131 GLY n 
1 132 ASP n 
1 133 THR n 
1 134 VAL n 
1 135 SER n 
1 136 ARG n 
1 137 LEU n 
1 138 ASP n 
1 139 ALA n 
1 140 GLU n 
1 141 GLU n 
1 142 PRO n 
1 143 GLU n 
1 144 LEU n 
1 145 ASN n 
1 146 ARG n 
1 147 ASP n 
1 148 PRO n 
1 149 PRO n 
1 150 GLY n 
1 151 ASP n 
1 152 GLU n 
1 153 ARG n 
1 154 ASP n 
1 155 THR n 
1 156 THR n 
1 157 THR n 
1 158 PRO n 
1 159 HIS n 
1 160 ALA n 
1 161 ILE n 
1 162 ALA n 
1 163 LEU n 
1 164 VAL n 
1 165 LEU n 
1 166 GLN n 
1 167 GLN n 
1 168 LEU n 
1 169 VAL n 
1 170 LEU n 
1 171 GLY n 
1 172 ASN n 
1 173 ALA n 
1 174 LEU n 
1 175 PRO n 
1 176 PRO n 
1 177 ASP n 
1 178 LYS n 
1 179 ARG n 
1 180 ALA n 
1 181 LEU n 
1 182 LEU n 
1 183 THR n 
1 184 ASP n 
1 185 TRP n 
1 186 MET n 
1 187 ALA n 
1 188 ARG n 
1 189 ASN n 
1 190 THR n 
1 191 THR n 
1 192 GLY n 
1 193 ALA n 
1 194 LYS n 
1 195 ARG n 
1 196 ILE n 
1 197 ARG n 
1 198 ALA n 
1 199 GLY n 
1 200 PHE n 
1 201 PRO n 
1 202 ALA n 
1 203 ASP n 
1 204 TRP n 
1 205 LYS n 
1 206 VAL n 
1 207 ILE n 
1 208 ASP n 
1 209 LYS n 
1 210 THR n 
1 211 GLY n 
1 212 THR n 
1 213 GLY n 
1 214 ASP n 
1 215 TYR n 
1 216 GLY n 
1 217 ARG n 
1 218 ALA n 
1 219 ASN n 
1 220 ASP n 
1 221 ILE n 
1 222 ALA n 
1 223 VAL n 
1 224 VAL n 
1 225 TRP n 
1 226 SER n 
1 227 PRO n 
1 228 THR n 
1 229 GLY n 
1 230 VAL n 
1 231 PRO n 
1 232 TYR n 
1 233 VAL n 
1 234 VAL n 
1 235 ALA n 
1 236 VAL n 
1 237 MET n 
1 238 SER n 
1 239 ASP n 
1 240 ARG n 
1 241 ALA n 
1 242 GLY n 
1 243 GLY n 
1 244 GLY n 
1 245 TYR n 
1 246 ASP n 
1 247 ALA n 
1 248 GLU n 
1 249 PRO n 
1 250 ARG n 
1 251 GLU n 
1 252 ALA n 
1 253 LEU n 
1 254 LEU n 
1 255 ALA n 
1 256 GLU n 
1 257 ALA n 
1 258 ALA n 
1 259 THR n 
1 260 CYS n 
1 261 VAL n 
1 262 ALA n 
1 263 GLY n 
1 264 VAL n 
1 265 LEU n 
1 266 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                   266 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'blaC, blaA, BQ2027_MB2094C' 
_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      'Mycobacterium tuberculosis' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     1773 
_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 BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ?                               'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ?                               'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ?                               'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ?                               'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE        ?                               'C3 H7 N O2 S'   121.158 
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  
GOL non-polymer         . GLYCEROL        'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'       92.094  
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   GLY 1   27  27  GLY GLY A . n 
A 1 2   ASP 2   28  28  ASP ASP A . n 
A 1 3   LEU 3   29  29  LEU LEU A . n 
A 1 4   ALA 4   30  30  ALA ALA A . n 
A 1 5   ASP 5   31  31  ASP ASP A . n 
A 1 6   ARG 6   32  32  ARG ARG A . n 
A 1 7   PHE 7   33  33  PHE PHE A . n 
A 1 8   ALA 8   34  34  ALA ALA A . n 
A 1 9   GLU 9   35  35  GLU GLU A . n 
A 1 10  LEU 10  36  36  LEU LEU A . n 
A 1 11  GLU 11  37  37  GLU GLU A . n 
A 1 12  ARG 12  38  38  ARG ARG A . n 
A 1 13  ARG 13  39  39  ARG ARG A . n 
A 1 14  TYR 14  40  40  TYR TYR A . n 
A 1 15  ASP 15  41  41  ASP ASP A . n 
A 1 16  ALA 16  42  42  ALA ALA A . n 
A 1 17  ARG 17  43  43  ARG ARG A . n 
A 1 18  LEU 18  44  44  LEU LEU A . n 
A 1 19  GLY 19  45  45  GLY GLY A . n 
A 1 20  VAL 20  46  46  VAL VAL A . n 
A 1 21  TYR 21  47  47  TYR TYR A . n 
A 1 22  VAL 22  48  48  VAL VAL A . n 
A 1 23  PRO 23  49  49  PRO PRO A . n 
A 1 24  ALA 24  50  50  ALA ALA A . n 
A 1 25  THR 25  51  51  THR THR A . n 
A 1 26  GLY 26  52  52  GLY GLY A . n 
A 1 27  THR 27  53  53  THR THR A . n 
A 1 28  THR 28  54  54  THR THR A . n 
A 1 29  ALA 29  55  55  ALA ALA A . n 
A 1 30  ALA 30  56  56  ALA ALA A . n 
A 1 31  ILE 31  57  57  ILE ILE A . n 
A 1 32  GLU 32  59  59  GLU GLU A . n 
A 1 33  TYR 33  60  60  TYR TYR A . n 
A 1 34  ARG 34  61  61  ARG ARG A . n 
A 1 35  ALA 35  62  62  ALA ALA A . n 
A 1 36  ASP 36  63  63  ASP ASP A . n 
A 1 37  GLU 37  64  64  GLU GLU A . n 
A 1 38  ARG 38  65  65  ARG ARG A . n 
A 1 39  PHE 39  66  66  PHE PHE A . n 
A 1 40  ALA 40  67  67  ALA ALA A . n 
A 1 41  PHE 41  68  68  PHE PHE A . n 
A 1 42  CYS 42  69  69  CYS CYS A . n 
A 1 43  SER 43  70  70  SER SER A . n 
A 1 44  THR 44  71  71  THR THR A . n 
A 1 45  PHE 45  72  72  PHE PHE A . n 
A 1 46  LYS 46  73  73  LYS LYS A . n 
A 1 47  ALA 47  74  74  ALA ALA A . n 
A 1 48  PRO 48  75  75  PRO PRO A . n 
A 1 49  LEU 49  76  76  LEU LEU A . n 
A 1 50  VAL 50  77  77  VAL VAL A . n 
A 1 51  ALA 51  78  78  ALA ALA A . n 
A 1 52  ALA 52  79  79  ALA ALA A . n 
A 1 53  VAL 53  80  80  VAL VAL A . n 
A 1 54  LEU 54  81  81  LEU LEU A . n 
A 1 55  HIS 55  82  82  HIS HIS A . n 
A 1 56  GLN 56  83  83  GLN GLN A . n 
A 1 57  ASN 57  86  86  ASN ASN A . n 
A 1 58  PRO 58  87  87  PRO PRO A . n 
A 1 59  LEU 59  88  88  LEU LEU A . n 
A 1 60  THR 60  89  89  THR THR A . n 
A 1 61  HIS 61  90  90  HIS HIS A . n 
A 1 62  LEU 62  91  91  LEU LEU A . n 
A 1 63  ASP 63  92  92  ASP ASP A . n 
A 1 64  LYS 64  93  93  LYS LYS A . n 
A 1 65  LEU 65  94  94  LEU LEU A . n 
A 1 66  ILE 66  95  95  ILE ILE A . n 
A 1 67  THR 67  96  96  THR THR A . n 
A 1 68  TYR 68  97  97  TYR TYR A . n 
A 1 69  THR 69  98  98  THR THR A . n 
A 1 70  SER 70  99  99  SER SER A . n 
A 1 71  ASP 71  100 100 ASP ASP A . n 
A 1 72  ASP 72  101 101 ASP ASP A . n 
A 1 73  ILE 73  102 102 ILE ILE A . n 
A 1 74  ARG 74  103 103 ARG ARG A . n 
A 1 75  SER 75  104 104 SER SER A . n 
A 1 76  ARG 76  105 105 ARG ARG A . n 
A 1 77  SER 77  106 106 SER SER A . n 
A 1 78  PRO 78  107 107 PRO PRO A . n 
A 1 79  VAL 79  108 108 VAL VAL A . n 
A 1 80  ALA 80  109 109 ALA ALA A . n 
A 1 81  GLN 81  110 110 GLN GLN A . n 
A 1 82  GLN 82  111 111 GLN GLN A . n 
A 1 83  HIS 83  112 112 HIS HIS A . n 
A 1 84  VAL 84  113 113 VAL VAL A . n 
A 1 85  GLN 85  114 114 GLN GLN A . n 
A 1 86  THR 86  115 115 THR THR A . n 
A 1 87  GLY 87  116 116 GLY GLY A . n 
A 1 88  MET 88  117 117 MET MET A . n 
A 1 89  THR 89  118 118 THR THR A . n 
A 1 90  ILE 90  119 119 ILE ILE A . n 
A 1 91  GLY 91  120 120 GLY GLY A . n 
A 1 92  GLN 92  121 121 GLN GLN A . n 
A 1 93  LEU 93  122 122 LEU LEU A . n 
A 1 94  CYS 94  123 123 CYS CYS A . n 
A 1 95  ASP 95  124 124 ASP ASP A . n 
A 1 96  ALA 96  125 125 ALA ALA A . n 
A 1 97  ALA 97  126 126 ALA ALA A . n 
A 1 98  ILE 98  127 127 ILE ILE A . n 
A 1 99  ARG 99  128 128 ARG ARG A . n 
A 1 100 TYR 100 129 129 TYR TYR A . n 
A 1 101 SER 101 130 130 SER SER A . n 
A 1 102 ASP 102 131 131 ASP ASP A . n 
A 1 103 GLY 103 132 132 GLY GLY A . n 
A 1 104 THR 104 133 133 THR THR A . n 
A 1 105 ALA 105 134 134 ALA ALA A . n 
A 1 106 ALA 106 135 135 ALA ALA A . n 
A 1 107 ASN 107 136 136 ASN ASN A . n 
A 1 108 LEU 108 137 137 LEU LEU A . n 
A 1 109 LEU 109 138 138 LEU LEU A . n 
A 1 110 LEU 110 139 139 LEU LEU A . n 
A 1 111 ALA 111 140 140 ALA ALA A . n 
A 1 112 ASP 112 141 141 ASP ASP A . n 
A 1 113 LEU 113 142 142 LEU LEU A . n 
A 1 114 GLY 114 143 143 GLY GLY A . n 
A 1 115 GLY 115 144 144 GLY GLY A . n 
A 1 116 PRO 116 145 145 PRO PRO A . n 
A 1 117 GLY 117 145 145 GLY GLY A A n 
A 1 118 GLY 118 145 145 GLY GLY A B n 
A 1 119 GLY 119 145 145 GLY GLY A C n 
A 1 120 THR 120 145 145 THR THR A D n 
A 1 121 ALA 121 146 146 ALA ALA A . n 
A 1 122 ALA 122 147 147 ALA ALA A . n 
A 1 123 PHE 123 148 148 PHE PHE A . n 
A 1 124 THR 124 149 149 THR THR A . n 
A 1 125 GLY 125 150 150 GLY GLY A . n 
A 1 126 TYR 126 151 151 TYR TYR A . n 
A 1 127 LEU 127 152 152 LEU LEU A . n 
A 1 128 ARG 128 153 153 ARG ARG A . n 
A 1 129 SER 129 154 154 SER SER A . n 
A 1 130 LEU 130 155 155 LEU LEU A . n 
A 1 131 GLY 131 156 156 GLY GLY A . n 
A 1 132 ASP 132 157 157 ASP ASP A . n 
A 1 133 THR 133 158 158 THR THR A . n 
A 1 134 VAL 134 159 159 VAL VAL A . n 
A 1 135 SER 135 160 160 SER SER A . n 
A 1 136 ARG 136 161 161 ARG ARG A . n 
A 1 137 LEU 137 162 162 LEU LEU A . n 
A 1 138 ASP 138 163 163 ASP ASP A . n 
A 1 139 ALA 139 164 164 ALA ALA A . n 
A 1 140 GLU 140 165 165 GLU GLU A . n 
A 1 141 GLU 141 166 166 GLU GLU A . n 
A 1 142 PRO 142 167 167 PRO PRO A . n 
A 1 143 GLU 143 168 168 GLU GLU A . n 
A 1 144 LEU 144 169 169 LEU LEU A . n 
A 1 145 ASN 145 170 170 ASN ASN A . n 
A 1 146 ARG 146 171 171 ARG ARG A . n 
A 1 147 ASP 147 172 172 ASP ASP A . n 
A 1 148 PRO 148 173 173 PRO PRO A . n 
A 1 149 PRO 149 174 174 PRO PRO A . n 
A 1 150 GLY 150 175 175 GLY GLY A . n 
A 1 151 ASP 151 176 176 ASP ASP A . n 
A 1 152 GLU 152 177 177 GLU GLU A . n 
A 1 153 ARG 153 178 178 ARG ARG A . n 
A 1 154 ASP 154 179 179 ASP ASP A . n 
A 1 155 THR 155 180 180 THR THR A . n 
A 1 156 THR 156 181 181 THR THR A . n 
A 1 157 THR 157 182 182 THR THR A . n 
A 1 158 PRO 158 183 183 PRO PRO A . n 
A 1 159 HIS 159 184 184 HIS HIS A . n 
A 1 160 ALA 160 185 185 ALA ALA A . n 
A 1 161 ILE 161 186 186 ILE ILE A . n 
A 1 162 ALA 162 187 187 ALA ALA A . n 
A 1 163 LEU 163 188 188 LEU LEU A . n 
A 1 164 VAL 164 189 189 VAL VAL A . n 
A 1 165 LEU 165 190 190 LEU LEU A . n 
A 1 166 GLN 166 191 191 GLN GLN A . n 
A 1 167 GLN 167 192 192 GLN GLN A . n 
A 1 168 LEU 168 193 193 LEU LEU A . n 
A 1 169 VAL 169 194 194 VAL VAL A . n 
A 1 170 LEU 170 195 195 LEU LEU A . n 
A 1 171 GLY 171 196 196 GLY GLY A . n 
A 1 172 ASN 172 197 197 ASN ASN A . n 
A 1 173 ALA 173 198 198 ALA ALA A . n 
A 1 174 LEU 174 199 199 LEU LEU A . n 
A 1 175 PRO 175 200 200 PRO PRO A . n 
A 1 176 PRO 176 201 201 PRO PRO A . n 
A 1 177 ASP 177 202 202 ASP ASP A . n 
A 1 178 LYS 178 203 203 LYS LYS A . n 
A 1 179 ARG 179 204 204 ARG ARG A . n 
A 1 180 ALA 180 205 205 ALA ALA A . n 
A 1 181 LEU 181 206 206 LEU LEU A . n 
A 1 182 LEU 182 207 207 LEU LEU A . n 
A 1 183 THR 183 208 208 THR THR A . n 
A 1 184 ASP 184 209 209 ASP ASP A . n 
A 1 185 TRP 185 210 210 TRP TRP A . n 
A 1 186 MET 186 211 211 MET MET A . n 
A 1 187 ALA 187 212 212 ALA ALA A . n 
A 1 188 ARG 188 213 213 ARG ARG A . n 
A 1 189 ASN 189 214 214 ASN ASN A . n 
A 1 190 THR 190 215 215 THR THR A . n 
A 1 191 THR 191 216 216 THR THR A . n 
A 1 192 GLY 192 217 217 GLY GLY A . n 
A 1 193 ALA 193 218 218 ALA ALA A . n 
A 1 194 LYS 194 219 219 LYS LYS A . n 
A 1 195 ARG 195 220 220 ARG ARG A . n 
A 1 196 ILE 196 221 221 ILE ILE A . n 
A 1 197 ARG 197 222 222 ARG ARG A . n 
A 1 198 ALA 198 223 223 ALA ALA A . n 
A 1 199 GLY 199 224 224 GLY GLY A . n 
A 1 200 PHE 200 225 225 PHE PHE A . n 
A 1 201 PRO 201 226 226 PRO PRO A . n 
A 1 202 ALA 202 227 227 ALA ALA A . n 
A 1 203 ASP 203 228 228 ASP ASP A . n 
A 1 204 TRP 204 229 229 TRP TRP A . n 
A 1 205 LYS 205 230 230 LYS LYS A . n 
A 1 206 VAL 206 231 231 VAL VAL A . n 
A 1 207 ILE 207 232 232 ILE ILE A . n 
A 1 208 ASP 208 233 233 ASP ASP A . n 
A 1 209 LYS 209 234 234 LYS LYS A . n 
A 1 210 THR 210 235 235 THR THR A . n 
A 1 211 GLY 211 236 236 GLY GLY A . n 
A 1 212 THR 212 237 237 THR THR A . n 
A 1 213 GLY 213 238 238 GLY GLY A . n 
A 1 214 ASP 214 240 240 ASP ASP A . n 
A 1 215 TYR 215 241 241 TYR TYR A . n 
A 1 216 GLY 216 242 242 GLY GLY A . n 
A 1 217 ARG 217 243 243 ARG ARG A . n 
A 1 218 ALA 218 244 244 ALA ALA A . n 
A 1 219 ASN 219 245 245 ASN ASN A . n 
A 1 220 ASP 220 246 246 ASP ASP A . n 
A 1 221 ILE 221 247 247 ILE ILE A . n 
A 1 222 ALA 222 248 248 ALA ALA A . n 
A 1 223 VAL 223 249 249 VAL VAL A . n 
A 1 224 VAL 224 250 250 VAL VAL A . n 
A 1 225 TRP 225 251 251 TRP TRP A . n 
A 1 226 SER 226 252 252 SER SER A . n 
A 1 227 PRO 227 254 254 PRO PRO A . n 
A 1 228 THR 228 255 255 THR THR A . n 
A 1 229 GLY 229 256 256 GLY GLY A . n 
A 1 230 VAL 230 257 257 VAL VAL A . n 
A 1 231 PRO 231 258 258 PRO PRO A . n 
A 1 232 TYR 232 259 259 TYR TYR A . n 
A 1 233 VAL 233 260 260 VAL VAL A . n 
A 1 234 VAL 234 261 261 VAL VAL A . n 
A 1 235 ALA 235 262 262 ALA ALA A . n 
A 1 236 VAL 236 263 263 VAL VAL A . n 
A 1 237 MET 237 264 264 MET MET A . n 
A 1 238 SER 238 265 265 SER SER A . n 
A 1 239 ASP 239 266 266 ASP ASP A . n 
A 1 240 ARG 240 267 267 ARG ARG A . n 
A 1 241 ALA 241 268 268 ALA ALA A . n 
A 1 242 GLY 242 269 269 GLY GLY A . n 
A 1 243 GLY 243 270 270 GLY GLY A . n 
A 1 244 GLY 244 271 271 GLY GLY A . n 
A 1 245 TYR 245 272 272 TYR TYR A . n 
A 1 246 ASP 246 273 273 ASP ASP A . n 
A 1 247 ALA 247 274 274 ALA ALA A . n 
A 1 248 GLU 248 275 275 GLU GLU A . n 
A 1 249 PRO 249 276 276 PRO PRO A . n 
A 1 250 ARG 250 277 277 ARG ARG A . n 
A 1 251 GLU 251 278 278 GLU GLU A . n 
A 1 252 ALA 252 279 279 ALA ALA A . n 
A 1 253 LEU 253 280 280 LEU LEU A . n 
A 1 254 LEU 254 281 281 LEU LEU A . n 
A 1 255 ALA 255 282 282 ALA ALA A . n 
A 1 256 GLU 256 283 283 GLU GLU A . n 
A 1 257 ALA 257 284 284 ALA ALA A . n 
A 1 258 ALA 258 285 285 ALA ALA A . n 
A 1 259 THR 259 286 286 THR THR A . n 
A 1 260 CYS 260 287 287 CYS CYS A . n 
A 1 261 VAL 261 288 288 VAL VAL A . n 
A 1 262 ALA 262 289 289 ALA ALA A . n 
A 1 263 GLY 263 290 290 GLY GLY A . n 
A 1 264 VAL 264 291 291 VAL VAL A . n 
A 1 265 LEU 265 292 292 LEU LEU A . n 
A 1 266 ALA 266 293 293 ALA ALA A . n 
B 1 1   GLY 1   27  ?   ?   ?   B . n 
B 1 2   ASP 2   28  28  ASP ASP B . n 
B 1 3   LEU 3   29  29  LEU LEU B . n 
B 1 4   ALA 4   30  30  ALA ALA B . n 
B 1 5   ASP 5   31  31  ASP ASP B . n 
B 1 6   ARG 6   32  32  ARG ARG B . n 
B 1 7   PHE 7   33  33  PHE PHE B . n 
B 1 8   ALA 8   34  34  ALA ALA B . n 
B 1 9   GLU 9   35  35  GLU GLU B . n 
B 1 10  LEU 10  36  36  LEU LEU B . n 
B 1 11  GLU 11  37  37  GLU GLU B . n 
B 1 12  ARG 12  38  38  ARG ARG B . n 
B 1 13  ARG 13  39  39  ARG ARG B . n 
B 1 14  TYR 14  40  40  TYR TYR B . n 
B 1 15  ASP 15  41  41  ASP ASP B . n 
B 1 16  ALA 16  42  42  ALA ALA B . n 
B 1 17  ARG 17  43  43  ARG ARG B . n 
B 1 18  LEU 18  44  44  LEU LEU B . n 
B 1 19  GLY 19  45  45  GLY GLY B . n 
B 1 20  VAL 20  46  46  VAL VAL B . n 
B 1 21  TYR 21  47  47  TYR TYR B . n 
B 1 22  VAL 22  48  48  VAL VAL B . n 
B 1 23  PRO 23  49  49  PRO PRO B . n 
B 1 24  ALA 24  50  50  ALA ALA B . n 
B 1 25  THR 25  51  51  THR THR B . n 
B 1 26  GLY 26  52  52  GLY GLY B . n 
B 1 27  THR 27  53  53  THR THR B . n 
B 1 28  THR 28  54  54  THR THR B . n 
B 1 29  ALA 29  55  55  ALA ALA B . n 
B 1 30  ALA 30  56  56  ALA ALA B . n 
B 1 31  ILE 31  57  57  ILE ILE B . n 
B 1 32  GLU 32  59  59  GLU GLU B . n 
B 1 33  TYR 33  60  60  TYR TYR B . n 
B 1 34  ARG 34  61  61  ARG ARG B . n 
B 1 35  ALA 35  62  62  ALA ALA B . n 
B 1 36  ASP 36  63  63  ASP ASP B . n 
B 1 37  GLU 37  64  64  GLU GLU B . n 
B 1 38  ARG 38  65  65  ARG ARG B . n 
B 1 39  PHE 39  66  66  PHE PHE B . n 
B 1 40  ALA 40  67  67  ALA ALA B . n 
B 1 41  PHE 41  68  68  PHE PHE B . n 
B 1 42  CYS 42  69  69  CYS CYS B . n 
B 1 43  SER 43  70  70  SER SER B . n 
B 1 44  THR 44  71  71  THR THR B . n 
B 1 45  PHE 45  72  72  PHE PHE B . n 
B 1 46  LYS 46  73  73  LYS LYS B . n 
B 1 47  ALA 47  74  74  ALA ALA B . n 
B 1 48  PRO 48  75  75  PRO PRO B . n 
B 1 49  LEU 49  76  76  LEU LEU B . n 
B 1 50  VAL 50  77  77  VAL VAL B . n 
B 1 51  ALA 51  78  78  ALA ALA B . n 
B 1 52  ALA 52  79  79  ALA ALA B . n 
B 1 53  VAL 53  80  80  VAL VAL B . n 
B 1 54  LEU 54  81  81  LEU LEU B . n 
B 1 55  HIS 55  82  82  HIS HIS B . n 
B 1 56  GLN 56  83  83  GLN GLN B . n 
B 1 57  ASN 57  86  86  ASN ASN B . n 
B 1 58  PRO 58  87  87  PRO PRO B . n 
B 1 59  LEU 59  88  88  LEU LEU B . n 
B 1 60  THR 60  89  89  THR THR B . n 
B 1 61  HIS 61  90  90  HIS HIS B . n 
B 1 62  LEU 62  91  91  LEU LEU B . n 
B 1 63  ASP 63  92  92  ASP ASP B . n 
B 1 64  LYS 64  93  93  LYS LYS B . n 
B 1 65  LEU 65  94  94  LEU LEU B . n 
B 1 66  ILE 66  95  95  ILE ILE B . n 
B 1 67  THR 67  96  96  THR THR B . n 
B 1 68  TYR 68  97  97  TYR TYR B . n 
B 1 69  THR 69  98  98  THR THR B . n 
B 1 70  SER 70  99  99  SER SER B . n 
B 1 71  ASP 71  100 100 ASP ASP B . n 
B 1 72  ASP 72  101 101 ASP ASP B . n 
B 1 73  ILE 73  102 102 ILE ILE B . n 
B 1 74  ARG 74  103 103 ARG ARG B . n 
B 1 75  SER 75  104 104 SER SER B . n 
B 1 76  ARG 76  105 105 ARG ARG B . n 
B 1 77  SER 77  106 106 SER SER B . n 
B 1 78  PRO 78  107 107 PRO PRO B . n 
B 1 79  VAL 79  108 108 VAL VAL B . n 
B 1 80  ALA 80  109 109 ALA ALA B . n 
B 1 81  GLN 81  110 110 GLN GLN B . n 
B 1 82  GLN 82  111 111 GLN GLN B . n 
B 1 83  HIS 83  112 112 HIS HIS B . n 
B 1 84  VAL 84  113 113 VAL VAL B . n 
B 1 85  GLN 85  114 114 GLN GLN B . n 
B 1 86  THR 86  115 115 THR THR B . n 
B 1 87  GLY 87  116 116 GLY GLY B . n 
B 1 88  MET 88  117 117 MET MET B . n 
B 1 89  THR 89  118 118 THR THR B . n 
B 1 90  ILE 90  119 119 ILE ILE B . n 
B 1 91  GLY 91  120 120 GLY GLY B . n 
B 1 92  GLN 92  121 121 GLN GLN B . n 
B 1 93  LEU 93  122 122 LEU LEU B . n 
B 1 94  CYS 94  123 123 CYS CYS B . n 
B 1 95  ASP 95  124 124 ASP ASP B . n 
B 1 96  ALA 96  125 125 ALA ALA B . n 
B 1 97  ALA 97  126 126 ALA ALA B . n 
B 1 98  ILE 98  127 127 ILE ILE B . n 
B 1 99  ARG 99  128 128 ARG ARG B . n 
B 1 100 TYR 100 129 129 TYR TYR B . n 
B 1 101 SER 101 130 130 SER SER B . n 
B 1 102 ASP 102 131 131 ASP ASP B . n 
B 1 103 GLY 103 132 132 GLY GLY B . n 
B 1 104 THR 104 133 133 THR THR B . n 
B 1 105 ALA 105 134 134 ALA ALA B . n 
B 1 106 ALA 106 135 135 ALA ALA B . n 
B 1 107 ASN 107 136 136 ASN ASN B . n 
B 1 108 LEU 108 137 137 LEU LEU B . n 
B 1 109 LEU 109 138 138 LEU LEU B . n 
B 1 110 LEU 110 139 139 LEU LEU B . n 
B 1 111 ALA 111 140 140 ALA ALA B . n 
B 1 112 ASP 112 141 141 ASP ASP B . n 
B 1 113 LEU 113 142 142 LEU LEU B . n 
B 1 114 GLY 114 143 143 GLY GLY B . n 
B 1 115 GLY 115 144 144 GLY GLY B . n 
B 1 116 PRO 116 145 145 PRO PRO B . n 
B 1 117 GLY 117 145 145 GLY GLY B A n 
B 1 118 GLY 118 145 145 GLY GLY B B n 
B 1 119 GLY 119 145 145 GLY GLY B C n 
B 1 120 THR 120 145 145 THR THR B D n 
B 1 121 ALA 121 146 146 ALA ALA B . n 
B 1 122 ALA 122 147 147 ALA ALA B . n 
B 1 123 PHE 123 148 148 PHE PHE B . n 
B 1 124 THR 124 149 149 THR THR B . n 
B 1 125 GLY 125 150 150 GLY GLY B . n 
B 1 126 TYR 126 151 151 TYR TYR B . n 
B 1 127 LEU 127 152 152 LEU LEU B . n 
B 1 128 ARG 128 153 153 ARG ARG B . n 
B 1 129 SER 129 154 154 SER SER B . n 
B 1 130 LEU 130 155 155 LEU LEU B . n 
B 1 131 GLY 131 156 156 GLY GLY B . n 
B 1 132 ASP 132 157 157 ASP ASP B . n 
B 1 133 THR 133 158 158 THR THR B . n 
B 1 134 VAL 134 159 159 VAL VAL B . n 
B 1 135 SER 135 160 160 SER SER B . n 
B 1 136 ARG 136 161 161 ARG ARG B . n 
B 1 137 LEU 137 162 162 LEU LEU B . n 
B 1 138 ASP 138 163 163 ASP ASP B . n 
B 1 139 ALA 139 164 164 ALA ALA B . n 
B 1 140 GLU 140 165 165 GLU GLU B . n 
B 1 141 GLU 141 166 166 GLU GLU B . n 
B 1 142 PRO 142 167 167 PRO PRO B . n 
B 1 143 GLU 143 168 168 GLU GLU B . n 
B 1 144 LEU 144 169 169 LEU LEU B . n 
B 1 145 ASN 145 170 170 ASN ASN B . n 
B 1 146 ARG 146 171 171 ARG ARG B . n 
B 1 147 ASP 147 172 172 ASP ASP B . n 
B 1 148 PRO 148 173 173 PRO PRO B . n 
B 1 149 PRO 149 174 174 PRO PRO B . n 
B 1 150 GLY 150 175 175 GLY GLY B . n 
B 1 151 ASP 151 176 176 ASP ASP B . n 
B 1 152 GLU 152 177 177 GLU GLU B . n 
B 1 153 ARG 153 178 178 ARG ARG B . n 
B 1 154 ASP 154 179 179 ASP ASP B . n 
B 1 155 THR 155 180 180 THR THR B . n 
B 1 156 THR 156 181 181 THR THR B . n 
B 1 157 THR 157 182 182 THR THR B . n 
B 1 158 PRO 158 183 183 PRO PRO B . n 
B 1 159 HIS 159 184 184 HIS HIS B . n 
B 1 160 ALA 160 185 185 ALA ALA B . n 
B 1 161 ILE 161 186 186 ILE ILE B . n 
B 1 162 ALA 162 187 187 ALA ALA B . n 
B 1 163 LEU 163 188 188 LEU LEU B . n 
B 1 164 VAL 164 189 189 VAL VAL B . n 
B 1 165 LEU 165 190 190 LEU LEU B . n 
B 1 166 GLN 166 191 191 GLN GLN B . n 
B 1 167 GLN 167 192 192 GLN GLN B . n 
B 1 168 LEU 168 193 193 LEU LEU B . n 
B 1 169 VAL 169 194 194 VAL VAL B . n 
B 1 170 LEU 170 195 195 LEU LEU B . n 
B 1 171 GLY 171 196 196 GLY GLY B . n 
B 1 172 ASN 172 197 197 ASN ASN B . n 
B 1 173 ALA 173 198 198 ALA ALA B . n 
B 1 174 LEU 174 199 199 LEU LEU B . n 
B 1 175 PRO 175 200 200 PRO PRO B . n 
B 1 176 PRO 176 201 201 PRO PRO B . n 
B 1 177 ASP 177 202 202 ASP ASP B . n 
B 1 178 LYS 178 203 203 LYS LYS B . n 
B 1 179 ARG 179 204 204 ARG ARG B . n 
B 1 180 ALA 180 205 205 ALA ALA B . n 
B 1 181 LEU 181 206 206 LEU LEU B . n 
B 1 182 LEU 182 207 207 LEU LEU B . n 
B 1 183 THR 183 208 208 THR THR B . n 
B 1 184 ASP 184 209 209 ASP ASP B . n 
B 1 185 TRP 185 210 210 TRP TRP B . n 
B 1 186 MET 186 211 211 MET MET B . n 
B 1 187 ALA 187 212 212 ALA ALA B . n 
B 1 188 ARG 188 213 213 ARG ARG B . n 
B 1 189 ASN 189 214 214 ASN ASN B . n 
B 1 190 THR 190 215 215 THR THR B . n 
B 1 191 THR 191 216 216 THR THR B . n 
B 1 192 GLY 192 217 217 GLY GLY B . n 
B 1 193 ALA 193 218 218 ALA ALA B . n 
B 1 194 LYS 194 219 219 LYS LYS B . n 
B 1 195 ARG 195 220 220 ARG ARG B . n 
B 1 196 ILE 196 221 221 ILE ILE B . n 
B 1 197 ARG 197 222 222 ARG ARG B . n 
B 1 198 ALA 198 223 223 ALA ALA B . n 
B 1 199 GLY 199 224 224 GLY GLY B . n 
B 1 200 PHE 200 225 225 PHE PHE B . n 
B 1 201 PRO 201 226 226 PRO PRO B . n 
B 1 202 ALA 202 227 227 ALA ALA B . n 
B 1 203 ASP 203 228 228 ASP ASP B . n 
B 1 204 TRP 204 229 229 TRP TRP B . n 
B 1 205 LYS 205 230 230 LYS LYS B . n 
B 1 206 VAL 206 231 231 VAL VAL B . n 
B 1 207 ILE 207 232 232 ILE ILE B . n 
B 1 208 ASP 208 233 233 ASP ASP B . n 
B 1 209 LYS 209 234 234 LYS LYS B . n 
B 1 210 THR 210 235 235 THR THR B . n 
B 1 211 GLY 211 236 236 GLY GLY B . n 
B 1 212 THR 212 237 237 THR THR B . n 
B 1 213 GLY 213 238 238 GLY GLY B . n 
B 1 214 ASP 214 240 240 ASP ASP B . n 
B 1 215 TYR 215 241 241 TYR TYR B . n 
B 1 216 GLY 216 242 242 GLY GLY B . n 
B 1 217 ARG 217 243 243 ARG ARG B . n 
B 1 218 ALA 218 244 244 ALA ALA B . n 
B 1 219 ASN 219 245 245 ASN ASN B . n 
B 1 220 ASP 220 246 246 ASP ASP B . n 
B 1 221 ILE 221 247 247 ILE ILE B . n 
B 1 222 ALA 222 248 248 ALA ALA B . n 
B 1 223 VAL 223 249 249 VAL VAL B . n 
B 1 224 VAL 224 250 250 VAL VAL B . n 
B 1 225 TRP 225 251 251 TRP TRP B . n 
B 1 226 SER 226 252 252 SER SER B . n 
B 1 227 PRO 227 254 254 PRO PRO B . n 
B 1 228 THR 228 255 255 THR THR B . n 
B 1 229 GLY 229 256 256 GLY GLY B . n 
B 1 230 VAL 230 257 257 VAL VAL B . n 
B 1 231 PRO 231 258 258 PRO PRO B . n 
B 1 232 TYR 232 259 259 TYR TYR B . n 
B 1 233 VAL 233 260 260 VAL VAL B . n 
B 1 234 VAL 234 261 261 VAL VAL B . n 
B 1 235 ALA 235 262 262 ALA ALA B . n 
B 1 236 VAL 236 263 263 VAL VAL B . n 
B 1 237 MET 237 264 264 MET MET B . n 
B 1 238 SER 238 265 265 SER SER B . n 
B 1 239 ASP 239 266 266 ASP ASP B . n 
B 1 240 ARG 240 267 267 ARG ARG B . n 
B 1 241 ALA 241 268 268 ALA ALA B . n 
B 1 242 GLY 242 269 269 GLY GLY B . n 
B 1 243 GLY 243 270 270 GLY GLY B . n 
B 1 244 GLY 244 271 271 GLY GLY B . n 
B 1 245 TYR 245 272 272 TYR TYR B . n 
B 1 246 ASP 246 273 273 ASP ASP B . n 
B 1 247 ALA 247 274 274 ALA ALA B . n 
B 1 248 GLU 248 275 275 GLU GLU B . n 
B 1 249 PRO 249 276 276 PRO PRO B . n 
B 1 250 ARG 250 277 277 ARG ARG B . n 
B 1 251 GLU 251 278 278 GLU GLU B . n 
B 1 252 ALA 252 279 279 ALA ALA B . n 
B 1 253 LEU 253 280 280 LEU LEU B . n 
B 1 254 LEU 254 281 281 LEU LEU B . n 
B 1 255 ALA 255 282 282 ALA ALA B . n 
B 1 256 GLU 256 283 283 GLU GLU B . n 
B 1 257 ALA 257 284 284 ALA ALA B . n 
B 1 258 ALA 258 285 285 ALA ALA B . n 
B 1 259 THR 259 286 286 THR THR B . n 
B 1 260 CYS 260 287 287 CYS CYS B . n 
B 1 261 VAL 261 288 288 VAL VAL B . n 
B 1 262 ALA 262 289 289 ALA ALA B . n 
B 1 263 GLY 263 290 290 GLY GLY B . n 
B 1 264 VAL 264 291 291 VAL VAL B . n 
B 1 265 LEU 265 292 292 LEU LEU B . n 
B 1 266 ALA 266 293 293 ALA ALA B . n 
# 
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 GOL 1   301 2   GOL GOL A . 
D 2 GOL 1   302 6   GOL GOL A . 
E 2 GOL 1   303 7   GOL GOL A . 
F 3 ZN  1   301 1   ZN  ZN  B . 
G 2 GOL 1   302 3   GOL GOL B . 
H 2 GOL 1   303 4   GOL GOL B . 
I 4 HOH 1   401 207 HOH HOH A . 
I 4 HOH 2   402 199 HOH HOH A . 
I 4 HOH 3   403 32  HOH HOH A . 
I 4 HOH 4   404 48  HOH HOH A . 
I 4 HOH 5   405 125 HOH HOH A . 
I 4 HOH 6   406 99  HOH HOH A . 
I 4 HOH 7   407 171 HOH HOH A . 
I 4 HOH 8   408 202 HOH HOH A . 
I 4 HOH 9   409 183 HOH HOH A . 
I 4 HOH 10  410 142 HOH HOH A . 
I 4 HOH 11  411 117 HOH HOH A . 
I 4 HOH 12  412 201 HOH HOH A . 
I 4 HOH 13  413 43  HOH HOH A . 
I 4 HOH 14  414 149 HOH HOH A . 
I 4 HOH 15  415 52  HOH HOH A . 
I 4 HOH 16  416 79  HOH HOH A . 
I 4 HOH 17  417 189 HOH HOH A . 
I 4 HOH 18  418 175 HOH HOH A . 
I 4 HOH 19  419 176 HOH HOH A . 
I 4 HOH 20  420 109 HOH HOH A . 
I 4 HOH 21  421 233 HOH HOH A . 
I 4 HOH 22  422 213 HOH HOH A . 
I 4 HOH 23  423 181 HOH HOH A . 
I 4 HOH 24  424 130 HOH HOH A . 
I 4 HOH 25  425 188 HOH HOH A . 
I 4 HOH 26  426 45  HOH HOH A . 
I 4 HOH 27  427 110 HOH HOH A . 
I 4 HOH 28  428 100 HOH HOH A . 
I 4 HOH 29  429 33  HOH HOH A . 
I 4 HOH 30  430 56  HOH HOH A . 
I 4 HOH 31  431 42  HOH HOH A . 
I 4 HOH 32  432 126 HOH HOH A . 
I 4 HOH 33  433 191 HOH HOH A . 
I 4 HOH 34  434 18  HOH HOH A . 
I 4 HOH 35  435 129 HOH HOH A . 
I 4 HOH 36  436 68  HOH HOH A . 
I 4 HOH 37  437 209 HOH HOH A . 
I 4 HOH 38  438 160 HOH HOH A . 
I 4 HOH 39  439 54  HOH HOH A . 
I 4 HOH 40  440 47  HOH HOH A . 
I 4 HOH 41  441 200 HOH HOH A . 
I 4 HOH 42  442 253 HOH HOH A . 
I 4 HOH 43  443 263 HOH HOH A . 
I 4 HOH 44  444 50  HOH HOH A . 
I 4 HOH 45  445 196 HOH HOH A . 
I 4 HOH 46  446 9   HOH HOH A . 
I 4 HOH 47  447 146 HOH HOH A . 
I 4 HOH 48  448 254 HOH HOH A . 
I 4 HOH 49  449 39  HOH HOH A . 
I 4 HOH 50  450 231 HOH HOH A . 
I 4 HOH 51  451 116 HOH HOH A . 
I 4 HOH 52  452 59  HOH HOH A . 
I 4 HOH 53  453 193 HOH HOH A . 
I 4 HOH 54  454 11  HOH HOH A . 
I 4 HOH 55  455 57  HOH HOH A . 
I 4 HOH 56  456 106 HOH HOH A . 
I 4 HOH 57  457 120 HOH HOH A . 
I 4 HOH 58  458 82  HOH HOH A . 
I 4 HOH 59  459 218 HOH HOH A . 
I 4 HOH 60  460 78  HOH HOH A . 
I 4 HOH 61  461 14  HOH HOH A . 
I 4 HOH 62  462 67  HOH HOH A . 
I 4 HOH 63  463 93  HOH HOH A . 
I 4 HOH 64  464 10  HOH HOH A . 
I 4 HOH 65  465 236 HOH HOH A . 
I 4 HOH 66  466 172 HOH HOH A . 
I 4 HOH 67  467 255 HOH HOH A . 
I 4 HOH 68  468 258 HOH HOH A . 
I 4 HOH 69  469 197 HOH HOH A . 
I 4 HOH 70  470 17  HOH HOH A . 
I 4 HOH 71  471 25  HOH HOH A . 
I 4 HOH 72  472 13  HOH HOH A . 
I 4 HOH 73  473 232 HOH HOH A . 
I 4 HOH 74  474 5   HOH HOH A . 
I 4 HOH 75  475 264 HOH HOH A . 
I 4 HOH 76  476 268 HOH HOH A . 
I 4 HOH 77  477 145 HOH HOH A . 
I 4 HOH 78  478 269 HOH HOH A . 
I 4 HOH 79  479 38  HOH HOH A . 
I 4 HOH 80  480 21  HOH HOH A . 
I 4 HOH 81  481 77  HOH HOH A . 
I 4 HOH 82  482 27  HOH HOH A . 
I 4 HOH 83  483 63  HOH HOH A . 
I 4 HOH 84  484 186 HOH HOH A . 
I 4 HOH 85  485 92  HOH HOH A . 
I 4 HOH 86  486 73  HOH HOH A . 
I 4 HOH 87  487 40  HOH HOH A . 
I 4 HOH 88  488 66  HOH HOH A . 
I 4 HOH 89  489 261 HOH HOH A . 
I 4 HOH 90  490 114 HOH HOH A . 
I 4 HOH 91  491 260 HOH HOH A . 
I 4 HOH 92  492 61  HOH HOH A . 
I 4 HOH 93  493 20  HOH HOH A . 
I 4 HOH 94  494 128 HOH HOH A . 
I 4 HOH 95  495 6   HOH HOH A . 
I 4 HOH 96  496 165 HOH HOH A . 
I 4 HOH 97  497 75  HOH HOH A . 
I 4 HOH 98  498 12  HOH HOH A . 
I 4 HOH 99  499 88  HOH HOH A . 
I 4 HOH 100 500 29  HOH HOH A . 
I 4 HOH 101 501 198 HOH HOH A . 
I 4 HOH 102 502 237 HOH HOH A . 
I 4 HOH 103 503 49  HOH HOH A . 
I 4 HOH 104 504 8   HOH HOH A . 
I 4 HOH 105 505 2   HOH HOH A . 
I 4 HOH 106 506 41  HOH HOH A . 
I 4 HOH 107 507 118 HOH HOH A . 
I 4 HOH 108 508 212 HOH HOH A . 
I 4 HOH 109 509 156 HOH HOH A . 
I 4 HOH 110 510 182 HOH HOH A . 
I 4 HOH 111 511 220 HOH HOH A . 
I 4 HOH 112 512 177 HOH HOH A . 
I 4 HOH 113 513 37  HOH HOH A . 
I 4 HOH 114 514 178 HOH HOH A . 
I 4 HOH 115 515 211 HOH HOH A . 
I 4 HOH 116 516 257 HOH HOH A . 
I 4 HOH 117 517 162 HOH HOH A . 
I 4 HOH 118 518 224 HOH HOH A . 
I 4 HOH 119 519 215 HOH HOH A . 
I 4 HOH 120 520 4   HOH HOH A . 
I 4 HOH 121 521 208 HOH HOH A . 
I 4 HOH 122 522 206 HOH HOH A . 
I 4 HOH 123 523 270 HOH HOH A . 
I 4 HOH 124 524 266 HOH HOH A . 
I 4 HOH 125 525 234 HOH HOH A . 
I 4 HOH 126 526 259 HOH HOH A . 
I 4 HOH 127 527 194 HOH HOH A . 
I 4 HOH 128 528 267 HOH HOH A . 
I 4 HOH 129 529 122 HOH HOH A . 
I 4 HOH 130 530 262 HOH HOH A . 
I 4 HOH 131 531 65  HOH HOH A . 
I 4 HOH 132 532 24  HOH HOH A . 
I 4 HOH 133 533 105 HOH HOH A . 
I 4 HOH 134 534 91  HOH HOH A . 
I 4 HOH 135 535 229 HOH HOH A . 
I 4 HOH 136 536 136 HOH HOH A . 
I 4 HOH 137 537 235 HOH HOH A . 
I 4 HOH 138 538 256 HOH HOH A . 
J 4 HOH 1   401 205 HOH HOH B . 
J 4 HOH 2   402 96  HOH HOH B . 
J 4 HOH 3   403 76  HOH HOH B . 
J 4 HOH 4   404 140 HOH HOH B . 
J 4 HOH 5   405 87  HOH HOH B . 
J 4 HOH 6   406 141 HOH HOH B . 
J 4 HOH 7   407 101 HOH HOH B . 
J 4 HOH 8   408 80  HOH HOH B . 
J 4 HOH 9   409 161 HOH HOH B . 
J 4 HOH 10  410 44  HOH HOH B . 
J 4 HOH 11  411 135 HOH HOH B . 
J 4 HOH 12  412 217 HOH HOH B . 
J 4 HOH 13  413 121 HOH HOH B . 
J 4 HOH 14  414 138 HOH HOH B . 
J 4 HOH 15  415 247 HOH HOH B . 
J 4 HOH 16  416 240 HOH HOH B . 
J 4 HOH 17  417 204 HOH HOH B . 
J 4 HOH 18  418 132 HOH HOH B . 
J 4 HOH 19  419 221 HOH HOH B . 
J 4 HOH 20  420 226 HOH HOH B . 
J 4 HOH 21  421 239 HOH HOH B . 
J 4 HOH 22  422 74  HOH HOH B . 
J 4 HOH 23  423 246 HOH HOH B . 
J 4 HOH 24  424 147 HOH HOH B . 
J 4 HOH 25  425 46  HOH HOH B . 
J 4 HOH 26  426 112 HOH HOH B . 
J 4 HOH 27  427 185 HOH HOH B . 
J 4 HOH 28  428 83  HOH HOH B . 
J 4 HOH 29  429 71  HOH HOH B . 
J 4 HOH 30  430 242 HOH HOH B . 
J 4 HOH 31  431 97  HOH HOH B . 
J 4 HOH 32  432 168 HOH HOH B . 
J 4 HOH 33  433 28  HOH HOH B . 
J 4 HOH 34  434 15  HOH HOH B . 
J 4 HOH 35  435 70  HOH HOH B . 
J 4 HOH 36  436 151 HOH HOH B . 
J 4 HOH 37  437 23  HOH HOH B . 
J 4 HOH 38  438 166 HOH HOH B . 
J 4 HOH 39  439 219 HOH HOH B . 
J 4 HOH 40  440 55  HOH HOH B . 
J 4 HOH 41  441 19  HOH HOH B . 
J 4 HOH 42  442 53  HOH HOH B . 
J 4 HOH 43  443 248 HOH HOH B . 
J 4 HOH 44  444 86  HOH HOH B . 
J 4 HOH 45  445 107 HOH HOH B . 
J 4 HOH 46  446 69  HOH HOH B . 
J 4 HOH 47  447 115 HOH HOH B . 
J 4 HOH 48  448 36  HOH HOH B . 
J 4 HOH 49  449 51  HOH HOH B . 
J 4 HOH 50  450 111 HOH HOH B . 
J 4 HOH 51  451 131 HOH HOH B . 
J 4 HOH 52  452 104 HOH HOH B . 
J 4 HOH 53  453 81  HOH HOH B . 
J 4 HOH 54  454 22  HOH HOH B . 
J 4 HOH 55  455 137 HOH HOH B . 
J 4 HOH 56  456 158 HOH HOH B . 
J 4 HOH 57  457 127 HOH HOH B . 
J 4 HOH 58  458 94  HOH HOH B . 
J 4 HOH 59  459 103 HOH HOH B . 
J 4 HOH 60  460 64  HOH HOH B . 
J 4 HOH 61  461 72  HOH HOH B . 
J 4 HOH 62  462 157 HOH HOH B . 
J 4 HOH 63  463 143 HOH HOH B . 
J 4 HOH 64  464 30  HOH HOH B . 
J 4 HOH 65  465 113 HOH HOH B . 
J 4 HOH 66  466 31  HOH HOH B . 
J 4 HOH 67  467 123 HOH HOH B . 
J 4 HOH 68  468 102 HOH HOH B . 
J 4 HOH 69  469 252 HOH HOH B . 
J 4 HOH 70  470 163 HOH HOH B . 
J 4 HOH 71  471 150 HOH HOH B . 
J 4 HOH 72  472 1   HOH HOH B . 
J 4 HOH 73  473 58  HOH HOH B . 
J 4 HOH 74  474 148 HOH HOH B . 
J 4 HOH 75  475 3   HOH HOH B . 
J 4 HOH 76  476 223 HOH HOH B . 
J 4 HOH 77  477 152 HOH HOH B . 
J 4 HOH 78  478 214 HOH HOH B . 
J 4 HOH 79  479 133 HOH HOH B . 
J 4 HOH 80  480 34  HOH HOH B . 
J 4 HOH 81  481 139 HOH HOH B . 
J 4 HOH 82  482 62  HOH HOH B . 
J 4 HOH 83  483 155 HOH HOH B . 
J 4 HOH 84  484 89  HOH HOH B . 
J 4 HOH 85  485 26  HOH HOH B . 
J 4 HOH 86  486 250 HOH HOH B . 
J 4 HOH 87  487 243 HOH HOH B . 
J 4 HOH 88  488 210 HOH HOH B . 
J 4 HOH 89  489 179 HOH HOH B . 
J 4 HOH 90  490 251 HOH HOH B . 
J 4 HOH 91  491 184 HOH HOH B . 
J 4 HOH 92  492 90  HOH HOH B . 
J 4 HOH 93  493 16  HOH HOH B . 
J 4 HOH 94  494 60  HOH HOH B . 
J 4 HOH 95  495 225 HOH HOH B . 
J 4 HOH 96  496 245 HOH HOH B . 
J 4 HOH 97  497 35  HOH HOH B . 
J 4 HOH 98  498 98  HOH HOH B . 
J 4 HOH 99  499 7   HOH HOH B . 
J 4 HOH 100 500 84  HOH HOH B . 
J 4 HOH 101 501 203 HOH HOH B . 
J 4 HOH 102 502 222 HOH HOH B . 
J 4 HOH 103 503 144 HOH HOH B . 
J 4 HOH 104 504 167 HOH HOH B . 
J 4 HOH 105 505 195 HOH HOH B . 
J 4 HOH 106 506 244 HOH HOH B . 
J 4 HOH 107 507 190 HOH HOH B . 
J 4 HOH 108 508 187 HOH HOH B . 
J 4 HOH 109 509 249 HOH HOH B . 
J 4 HOH 110 510 180 HOH HOH B . 
J 4 HOH 111 511 85  HOH HOH B . 
J 4 HOH 112 512 174 HOH HOH B . 
J 4 HOH 113 513 227 HOH HOH B . 
J 4 HOH 114 514 228 HOH HOH B . 
J 4 HOH 115 515 119 HOH HOH B . 
J 4 HOH 116 516 154 HOH HOH B . 
J 4 HOH 117 517 170 HOH HOH B . 
J 4 HOH 118 518 134 HOH HOH B . 
J 4 HOH 119 519 265 HOH HOH B . 
J 4 HOH 120 520 192 HOH HOH B . 
J 4 HOH 121 521 238 HOH HOH B . 
J 4 HOH 122 522 124 HOH HOH B . 
J 4 HOH 123 523 241 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       ? ? ? ? ? ? ? ? ? ? ? REFMAC  ? ? ? 5.8.0425 1 
? phasing          ? ? ? ? ? ? ? ? ? ? ? MOLREP  ? ? ? .        2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .        3 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .        4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9QI5 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     39.161 
_cell.length_a_esd                 ? 
_cell.length_b                     40.975 
_cell.length_b_esd                 ? 
_cell.length_c                     267.495 
_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                         9QI5 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9QI5 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             1.89 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          34.95 
_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              4.08 
_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    '22%v/v PEGSM, 0.2M Na Acetate, 0.024M Zn Chloride' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER2 S 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         2023-06-29 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.8731 
_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                        'ESRF BEAMLINE ID30B' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.8731 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ID30B 
_diffrn_source.pdbx_synchrotron_site       ESRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9QI5 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.8 
_reflns.d_resolution_low                               44.62 
_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                                     40588 
_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                           98.6 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                1.8 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          8.2 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.995 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.8 
_reflns_shell.d_res_low                                     1.84 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.6 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2018 
_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                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.589 
_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               ? 
# 
_refine.aniso_B[1][1]                            0.76 
_refine.aniso_B[1][2]                            -0.00 
_refine.aniso_B[1][3]                            0.00 
_refine.aniso_B[2][2]                            0.20 
_refine.aniso_B[2][3]                            -0.00 
_refine.aniso_B[3][3]                            -0.96 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               26.433 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.965 
_refine.correlation_coeff_Fo_to_Fc_free          0.950 
_refine.details                                  'HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT' 
_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                                 9QI5 
_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                            1.80 
_refine.ls_d_res_low                             44.62 
_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                     38570 
_refine.ls_number_reflns_R_free                  2018 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.31 
_refine.ls_percent_reflns_R_free                 5.0 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.17540 
_refine.ls_R_factor_R_free                       0.21118 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.17350 
_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                    MASK 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.correlation_coeff_I_to_Fcsqd_work        ? 
_refine.correlation_coeff_I_to_Fcsqd_free        ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.145 
_refine.pdbx_overall_ESU_R_Free                  0.130 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_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                 ? 
_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                             6.881 
_refine.overall_SU_ML                            0.103 
_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                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.80 
_refine_hist.d_res_low                        44.62 
_refine_hist.number_atoms_solvent             261 
_refine_hist.number_atoms_total               4279 
_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        3987 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         31 
_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' ? 0.007  0.012  4161 ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.016  3906 ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.524  1.817  5681 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 0.540  1.754  8963 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 6.677  5.000  544  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 7.586  5.000  40   ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 11.638 10.000 619  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.077  0.200  653  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.006  0.020  5101 ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  951  ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 1.117  1.509  2164 ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 1.117  1.510  2165 ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 1.675  2.706  2712 ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 1.674  2.707  2713 ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 1.820  1.730  1997 ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 1.820  1.731  1998 ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 2.836  3.077  2970 ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 4.846  17.35  4744 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 4.779  16.95  4706 ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                      'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                          1.800 
_refine_ls_shell.d_res_low                           1.847 
_refine_ls_shell.number_reflns_all                   ? 
_refine_ls_shell.number_reflns_obs                   ? 
_refine_ls_shell.number_reflns_R_free                127 
_refine_ls_shell.number_reflns_R_work                2853 
_refine_ls_shell.percent_reflns_obs                  99.90 
_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                     0.290 
_refine_ls_shell.redundancy_reflns_all               ? 
_refine_ls_shell.redundancy_reflns_obs               ? 
_refine_ls_shell.wR_factor_all                       ? 
_refine_ls_shell.wR_factor_obs                       ? 
_refine_ls_shell.wR_factor_R_free                    ? 
_refine_ls_shell.wR_factor_R_work                    ? 
_refine_ls_shell.pdbx_R_complete                     ? 
_refine_ls_shell.correlation_coeff_Fo_to_Fc          ? 
_refine_ls_shell.correlation_coeff_Fo_to_Fc_free     ? 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_work   ? 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_free   ? 
_refine_ls_shell.pdbx_total_number_of_bins_used      20 
_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                     0.326 
# 
_struct.entry_id                     9QI5 
_struct.title                        'Crystal structure of I105R mutant of BlaC from Mycobacterium tuberculosis' 
_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        9QI5 
_struct_keywords.text            'Beta-lactamase, BlaC, 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 3 ? 
G N N 2 ? 
H N N 2 ? 
I N N 4 ? 
J N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    BLAC_MYCBO 
_struct_ref.pdbx_db_accession          P0A5I7 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;DLADRFAELERRYDARLGVYVPATGTTAAIEYRADERFAFCSTFKAPLVAAVLHQNPLTHLDKLITYTSDDIRSISPVAQ
QHVQTGMTIGQLCDAAIRYSDGTAANLLLADLGGPGGGTAAFTGYLRSLGDTVSRLDAEEPELNRDPPGDERDTTTPHAI
ALVLQQLVLGNALPPDKRALLTDWMARNTTGAKRIRAGFPADWKVIDKTGTGDYGRANDIAVVWSPTGVPYVVAVMSDRA
GGGYDAEPREALLAEAATCVAGVLA
;
_struct_ref.pdbx_align_begin           43 
# 
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 9QI5 A 2 ? 266 ? P0A5I7 43 ? 307 ? 28 293 
2 1 9QI5 B 2 ? 266 ? P0A5I7 43 ? 307 ? 28 293 
# 
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 9QI5 GLY A 1  ? UNP P0A5I7 ?   ?   'expression tag'      27  1 
1 9QI5 ARG A 76 ? UNP P0A5I7 ILE 117 'engineered mutation' 105 2 
2 9QI5 GLY B 1  ? UNP P0A5I7 ?   ?   'expression tag'      27  3 
2 9QI5 ARG B 76 ? UNP P0A5I7 ILE 117 'engineered mutation' 105 4 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E,I 
2 1 B,F,G,H,J 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   homology 
_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 GLY A 1   ? ASP A 15  ? GLY A 27  ASP A 41  1 ? 15 
HELX_P HELX_P2  AA2 CYS A 42  ? THR A 44  ? CYS A 69  THR A 71  5 ? 3  
HELX_P HELX_P3  AA3 PHE A 45  ? ASN A 57  ? PHE A 72  ASN A 86  1 ? 13 
HELX_P HELX_P4  AA4 PRO A 58  ? ASP A 63  ? PRO A 87  ASP A 92  5 ? 6  
HELX_P HELX_P5  AA5 THR A 69  ? ILE A 73  ? THR A 98  ILE A 102 5 ? 5  
HELX_P HELX_P6  AA6 VAL A 79  ? VAL A 84  ? VAL A 108 VAL A 113 5 ? 6  
HELX_P HELX_P7  AA7 ILE A 90  ? TYR A 100 ? ILE A 119 TYR A 129 1 ? 11 
HELX_P HELX_P8  AA8 ASP A 102 ? GLY A 115 ? ASP A 131 GLY A 144 1 ? 14 
HELX_P HELX_P9  AA9 GLY A 118 B LEU A 130 ? GLY A 145 LEU A 155 1 ? 13 
HELX_P HELX_P10 AB1 PRO A 142 ? ARG A 146 ? PRO A 167 ARG A 171 5 ? 5  
HELX_P HELX_P11 AB2 THR A 157 ? LEU A 170 ? THR A 182 LEU A 195 1 ? 14 
HELX_P HELX_P12 AB3 PRO A 175 ? ARG A 188 ? PRO A 200 ARG A 213 1 ? 14 
HELX_P HELX_P13 AB4 ARG A 195 ? PHE A 200 ? ARG A 220 PHE A 225 1 ? 6  
HELX_P HELX_P14 AB5 ARG A 240 ? GLY A 244 ? ARG A 267 GLY A 271 5 ? 5  
HELX_P HELX_P15 AB6 ARG A 250 ? ALA A 266 ? ARG A 277 ALA A 293 1 ? 17 
HELX_P HELX_P16 AB7 LEU B 3   ? ASP B 15  ? LEU B 29  ASP B 41  1 ? 13 
HELX_P HELX_P17 AB8 CYS B 42  ? THR B 44  ? CYS B 69  THR B 71  5 ? 3  
HELX_P HELX_P18 AB9 PHE B 45  ? ASN B 57  ? PHE B 72  ASN B 86  1 ? 13 
HELX_P HELX_P19 AC1 PRO B 58  ? ASP B 63  ? PRO B 87  ASP B 92  5 ? 6  
HELX_P HELX_P20 AC2 THR B 69  ? ILE B 73  ? THR B 98  ILE B 102 5 ? 5  
HELX_P HELX_P21 AC3 VAL B 79  ? VAL B 84  ? VAL B 108 VAL B 113 5 ? 6  
HELX_P HELX_P22 AC4 ILE B 90  ? TYR B 100 ? ILE B 119 TYR B 129 1 ? 11 
HELX_P HELX_P23 AC5 ASP B 102 ? GLY B 115 ? ASP B 131 GLY B 144 1 ? 14 
HELX_P HELX_P24 AC6 GLY B 118 B LEU B 130 ? GLY B 145 LEU B 155 1 ? 13 
HELX_P HELX_P25 AC7 PRO B 142 ? ARG B 146 ? PRO B 167 ARG B 171 5 ? 5  
HELX_P HELX_P26 AC8 THR B 157 ? LEU B 170 ? THR B 182 LEU B 195 1 ? 14 
HELX_P HELX_P27 AC9 PRO B 175 ? ARG B 188 ? PRO B 200 ARG B 213 1 ? 14 
HELX_P HELX_P28 AD1 ARG B 195 ? PHE B 200 ? ARG B 220 PHE B 225 5 ? 6  
HELX_P HELX_P29 AD2 ARG B 240 ? GLY B 244 ? ARG B 267 GLY B 271 5 ? 5  
HELX_P HELX_P30 AD3 ARG B 250 ? ALA B 266 ? ARG B 277 ALA B 293 1 ? 17 
# 
_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 ? ? B ASP 5   OD2 ? ? ? 1_555 F ZN . ZN ? ? B ASP 31  B ZN 301 4_445 ? ? ? ? ? ? ? 1.979 ? ? 
metalc2 metalc ? ? B ASP 36  OD1 ? ? ? 1_555 F ZN . ZN ? ? B ASP 63  B ZN 301 1_555 ? ? ? ? ? ? ? 2.482 ? ? 
metalc3 metalc ? ? B HIS 159 ND1 ? ? ? 1_555 F ZN . ZN ? ? B HIS 184 B ZN 301 1_555 ? ? ? ? ? ? ? 2.202 ? ? 
# 
_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 OD2 ? B ASP 5  ? B ASP 31 ? 1_555 ZN ? F ZN . ? B ZN 301 ? 4_445 OD1 ? B ASP 36  ? B ASP 63  ? 1_555 75.5 ? 
2 OD2 ? B ASP 5  ? B ASP 31 ? 1_555 ZN ? F ZN . ? B ZN 301 ? 4_445 ND1 ? B HIS 159 ? B HIS 184 ? 1_555 76.1 ? 
3 OD1 ? B ASP 36 ? B ASP 63 ? 1_555 ZN ? F ZN . ? B ZN 301 ? 4_445 ND1 ? B HIS 159 ? B HIS 184 ? 1_555 7.4  ? 
# 
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 GLU 141 A . ? GLU 166 A PRO 142 A ? PRO 167 A 1 -2.45 
2 GLU 141 B . ? GLU 166 B PRO 142 B ? PRO 167 B 1 -1.97 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 2 ? 
AA3 ? 2 ? 
AA4 ? 5 ? 
AA5 ? 2 ? 
AA6 ? 2 ? 
# 
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 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA6 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 ILE A 31  ? TYR A 33  ? ILE A 57  TYR A 60  
AA1 2 ARG A 17  ? VAL A 22  ? ARG A 43  VAL A 48  
AA1 3 PRO A 231 ? ASP A 239 ? PRO A 258 ASP A 266 
AA1 4 ARG A 217 ? TRP A 225 ? ARG A 243 TRP A 251 
AA1 5 LYS A 205 ? GLY A 213 ? LYS A 230 GLY A 238 
AA2 1 PHE A 39  ? ALA A 40  ? PHE A 66  ALA A 67  
AA2 2 THR A 155 ? THR A 156 ? THR A 180 THR A 181 
AA3 1 LEU A 65  ? ILE A 66  ? LEU A 94  ILE A 95  
AA3 2 MET A 88  ? THR A 89  ? MET A 117 THR A 118 
AA4 1 ILE B 31  ? TYR B 33  ? ILE B 57  TYR B 60  
AA4 2 ARG B 17  ? VAL B 22  ? ARG B 43  VAL B 48  
AA4 3 PRO B 231 ? ASP B 239 ? PRO B 258 ASP B 266 
AA4 4 ARG B 217 ? TRP B 225 ? ARG B 243 TRP B 251 
AA4 5 LYS B 205 ? GLY B 213 ? LYS B 230 GLY B 238 
AA5 1 PHE B 39  ? ALA B 40  ? PHE B 66  ALA B 67  
AA5 2 THR B 155 ? THR B 156 ? THR B 180 THR B 181 
AA6 1 LEU B 65  ? ILE B 66  ? LEU B 94  ILE B 95  
AA6 2 MET B 88  ? THR B 89  ? MET B 117 THR B 118 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O TYR A 33  ? O TYR A 60  N VAL A 20  ? N VAL A 46  
AA1 2 3 N GLY A 19  ? N GLY A 45  O MET A 237 ? O MET A 264 
AA1 3 4 O VAL A 236 ? O VAL A 263 N ASP A 220 ? N ASP A 246 
AA1 4 5 O ASN A 219 ? O ASN A 245 N GLY A 211 ? N GLY A 236 
AA2 1 2 N PHE A 39  ? N PHE A 66  O THR A 156 ? O THR A 181 
AA3 1 2 N ILE A 66  ? N ILE A 95  O MET A 88  ? O MET A 117 
AA4 1 2 O TYR B 33  ? O TYR B 60  N VAL B 20  ? N VAL B 46  
AA4 2 3 N GLY B 19  ? N GLY B 45  O MET B 237 ? O MET B 264 
AA4 3 4 O VAL B 236 ? O VAL B 263 N ASP B 220 ? N ASP B 246 
AA4 4 5 O ASN B 219 ? O ASN B 245 N GLY B 211 ? N GLY B 236 
AA5 1 2 N PHE B 39  ? N PHE B 66  O THR B 156 ? O THR B 181 
AA6 1 2 N ILE B 66  ? N ILE B 95  O MET B 88  ? O MET B 117 
# 
_pdbx_entry_details.entry_id                   9QI5 
_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     N 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   O 
_pdbx_validate_close_contact.auth_asym_id_1   B 
_pdbx_validate_close_contact.auth_comp_id_1   GLY 
_pdbx_validate_close_contact.auth_seq_id_1    270 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   B 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    401 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.15 
# 
_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    B 
_pdbx_validate_symm_contact.auth_comp_id_1    HOH 
_pdbx_validate_symm_contact.auth_seq_id_1     515 
_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    B 
_pdbx_validate_symm_contact.auth_comp_id_2    HOH 
_pdbx_validate_symm_contact.auth_seq_id_2     516 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   4_445 
_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 CYS A 69  ? ? 46.84   -142.72 
2 1 CYS A 69  ? ? 46.84   -142.52 
3 1 THR A 181 ? ? -127.46 -168.27 
4 1 ARG A 220 ? ? -109.07 -122.54 
5 1 CYS B 69  ? ? 46.75   -143.49 
6 1 ARG B 220 ? ? -110.02 -122.98 
# 
_pdbx_validate_planes.id              1 
_pdbx_validate_planes.PDB_model_num   1 
_pdbx_validate_planes.auth_comp_id    ARG 
_pdbx_validate_planes.auth_asym_id    B 
_pdbx_validate_planes.auth_seq_id     105 
_pdbx_validate_planes.PDB_ins_code    ? 
_pdbx_validate_planes.label_alt_id    ? 
_pdbx_validate_planes.rmsd            0.084 
_pdbx_validate_planes.type            'SIDE CHAIN' 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined 1.5510   -10.4387 -51.0100 0.0534 ? 0.0167  ? 0.0130 ? 0.0239 ? 0.0045  ? 0.0051 ? 1.2714 ? 0.1470 
? -0.3588 ? 1.0902 ? -0.3107 ? 1.4947 ? -0.0144 ? -0.1080 ? 0.0015 ? 0.1318  ? 0.0503 ? 0.0523 ? 0.0391  ? -0.0301 ? -0.0359 ? 
2 'X-RAY DIFFRACTION' ? refined -10.9449 -20.9039 -17.1209 0.1548 ? -0.0136 ? 0.0057 ? 0.0807 ? -0.0072 ? 0.0047 ? 1.5270 ? 
-0.1931 ? -0.6395 ? 0.9609 ? 0.1951  ? 1.3334 ? 0.0168  ? -0.0259 ? 0.0419 ? -0.0034 ? 0.0055 ? 0.0013 ? -0.0594 ? -0.0159 ? 
-0.0223 ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 ? ? A 27 ? ? ? A 293 ? ? ? 
2 'X-RAY DIFFRACTION' 2 ? ? B 28 ? ? ? B 293 ? ? ? 
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      B 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       523 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   6.66 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
_pdbx_unobs_or_zero_occ_residues.id               1 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num    1 
_pdbx_unobs_or_zero_occ_residues.polymer_flag     Y 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag   1 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id     B 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id     GLY 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id      27 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code     ? 
_pdbx_unobs_or_zero_occ_residues.label_asym_id    B 
_pdbx_unobs_or_zero_occ_residues.label_comp_id    GLY 
_pdbx_unobs_or_zero_occ_residues.label_seq_id     1 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CYS N    N  N N 74  
CYS CA   C  N R 75  
CYS C    C  N N 76  
CYS O    O  N N 77  
CYS CB   C  N N 78  
CYS SG   S  N N 79  
CYS OXT  O  N N 80  
CYS H    H  N N 81  
CYS H2   H  N N 82  
CYS HA   H  N N 83  
CYS HB2  H  N N 84  
CYS HB3  H  N N 85  
CYS HG   H  N N 86  
CYS HXT  H  N N 87  
GLN N    N  N N 88  
GLN CA   C  N S 89  
GLN C    C  N N 90  
GLN O    O  N N 91  
GLN CB   C  N N 92  
GLN CG   C  N N 93  
GLN CD   C  N N 94  
GLN OE1  O  N N 95  
GLN NE2  N  N N 96  
GLN OXT  O  N N 97  
GLN H    H  N N 98  
GLN H2   H  N N 99  
GLN HA   H  N N 100 
GLN HB2  H  N N 101 
GLN HB3  H  N N 102 
GLN HG2  H  N N 103 
GLN HG3  H  N N 104 
GLN HE21 H  N N 105 
GLN HE22 H  N N 106 
GLN HXT  H  N N 107 
GLU N    N  N N 108 
GLU CA   C  N S 109 
GLU C    C  N N 110 
GLU O    O  N N 111 
GLU CB   C  N N 112 
GLU CG   C  N N 113 
GLU CD   C  N N 114 
GLU OE1  O  N N 115 
GLU OE2  O  N N 116 
GLU OXT  O  N N 117 
GLU H    H  N N 118 
GLU H2   H  N N 119 
GLU HA   H  N N 120 
GLU HB2  H  N N 121 
GLU HB3  H  N N 122 
GLU HG2  H  N N 123 
GLU HG3  H  N N 124 
GLU HE2  H  N N 125 
GLU HXT  H  N N 126 
GLY N    N  N N 127 
GLY CA   C  N N 128 
GLY C    C  N N 129 
GLY O    O  N N 130 
GLY OXT  O  N N 131 
GLY H    H  N N 132 
GLY H2   H  N N 133 
GLY HA2  H  N N 134 
GLY HA3  H  N N 135 
GLY HXT  H  N N 136 
GOL C1   C  N N 137 
GOL O1   O  N N 138 
GOL C2   C  N N 139 
GOL O2   O  N N 140 
GOL C3   C  N N 141 
GOL O3   O  N N 142 
GOL H11  H  N N 143 
GOL H12  H  N N 144 
GOL HO1  H  N N 145 
GOL H2   H  N N 146 
GOL HO2  H  N N 147 
GOL H31  H  N N 148 
GOL H32  H  N N 149 
GOL HO3  H  N N 150 
HIS N    N  N N 151 
HIS CA   C  N S 152 
HIS C    C  N N 153 
HIS O    O  N N 154 
HIS CB   C  N N 155 
HIS CG   C  Y N 156 
HIS ND1  N  Y N 157 
HIS CD2  C  Y N 158 
HIS CE1  C  Y N 159 
HIS NE2  N  Y N 160 
HIS OXT  O  N N 161 
HIS H    H  N N 162 
HIS H2   H  N N 163 
HIS HA   H  N N 164 
HIS HB2  H  N N 165 
HIS HB3  H  N N 166 
HIS HD1  H  N N 167 
HIS HD2  H  N N 168 
HIS HE1  H  N N 169 
HIS HE2  H  N N 170 
HIS HXT  H  N N 171 
HOH O    O  N N 172 
HOH H1   H  N N 173 
HOH H2   H  N N 174 
ILE N    N  N N 175 
ILE CA   C  N S 176 
ILE C    C  N N 177 
ILE O    O  N N 178 
ILE CB   C  N S 179 
ILE CG1  C  N N 180 
ILE CG2  C  N N 181 
ILE CD1  C  N N 182 
ILE OXT  O  N N 183 
ILE H    H  N N 184 
ILE H2   H  N N 185 
ILE HA   H  N N 186 
ILE HB   H  N N 187 
ILE HG12 H  N N 188 
ILE HG13 H  N N 189 
ILE HG21 H  N N 190 
ILE HG22 H  N N 191 
ILE HG23 H  N N 192 
ILE HD11 H  N N 193 
ILE HD12 H  N N 194 
ILE HD13 H  N N 195 
ILE HXT  H  N N 196 
LEU N    N  N N 197 
LEU CA   C  N S 198 
LEU C    C  N N 199 
LEU O    O  N N 200 
LEU CB   C  N N 201 
LEU CG   C  N N 202 
LEU CD1  C  N N 203 
LEU CD2  C  N N 204 
LEU OXT  O  N N 205 
LEU H    H  N N 206 
LEU H2   H  N N 207 
LEU HA   H  N N 208 
LEU HB2  H  N N 209 
LEU HB3  H  N N 210 
LEU HG   H  N N 211 
LEU HD11 H  N N 212 
LEU HD12 H  N N 213 
LEU HD13 H  N N 214 
LEU HD21 H  N N 215 
LEU HD22 H  N N 216 
LEU HD23 H  N N 217 
LEU HXT  H  N N 218 
LYS N    N  N N 219 
LYS CA   C  N S 220 
LYS C    C  N N 221 
LYS O    O  N N 222 
LYS CB   C  N N 223 
LYS CG   C  N N 224 
LYS CD   C  N N 225 
LYS CE   C  N N 226 
LYS NZ   N  N N 227 
LYS OXT  O  N N 228 
LYS H    H  N N 229 
LYS H2   H  N N 230 
LYS HA   H  N N 231 
LYS HB2  H  N N 232 
LYS HB3  H  N N 233 
LYS HG2  H  N N 234 
LYS HG3  H  N N 235 
LYS HD2  H  N N 236 
LYS HD3  H  N N 237 
LYS HE2  H  N N 238 
LYS HE3  H  N N 239 
LYS HZ1  H  N N 240 
LYS HZ2  H  N N 241 
LYS HZ3  H  N N 242 
LYS HXT  H  N N 243 
MET N    N  N N 244 
MET CA   C  N S 245 
MET C    C  N N 246 
MET O    O  N N 247 
MET CB   C  N N 248 
MET CG   C  N N 249 
MET SD   S  N N 250 
MET CE   C  N N 251 
MET OXT  O  N N 252 
MET H    H  N N 253 
MET H2   H  N N 254 
MET HA   H  N N 255 
MET HB2  H  N N 256 
MET HB3  H  N N 257 
MET HG2  H  N N 258 
MET HG3  H  N N 259 
MET HE1  H  N N 260 
MET HE2  H  N N 261 
MET HE3  H  N N 262 
MET HXT  H  N N 263 
PHE N    N  N N 264 
PHE CA   C  N S 265 
PHE C    C  N N 266 
PHE O    O  N N 267 
PHE CB   C  N N 268 
PHE CG   C  Y N 269 
PHE CD1  C  Y N 270 
PHE CD2  C  Y N 271 
PHE CE1  C  Y N 272 
PHE CE2  C  Y N 273 
PHE CZ   C  Y N 274 
PHE OXT  O  N N 275 
PHE H    H  N N 276 
PHE H2   H  N N 277 
PHE HA   H  N N 278 
PHE HB2  H  N N 279 
PHE HB3  H  N N 280 
PHE HD1  H  N N 281 
PHE HD2  H  N N 282 
PHE HE1  H  N N 283 
PHE HE2  H  N N 284 
PHE HZ   H  N N 285 
PHE HXT  H  N N 286 
PRO N    N  N N 287 
PRO CA   C  N S 288 
PRO C    C  N N 289 
PRO O    O  N N 290 
PRO CB   C  N N 291 
PRO CG   C  N N 292 
PRO CD   C  N N 293 
PRO OXT  O  N N 294 
PRO H    H  N N 295 
PRO HA   H  N N 296 
PRO HB2  H  N N 297 
PRO HB3  H  N N 298 
PRO HG2  H  N N 299 
PRO HG3  H  N N 300 
PRO HD2  H  N N 301 
PRO HD3  H  N N 302 
PRO HXT  H  N N 303 
SER N    N  N N 304 
SER CA   C  N S 305 
SER C    C  N N 306 
SER O    O  N N 307 
SER CB   C  N N 308 
SER OG   O  N N 309 
SER OXT  O  N N 310 
SER H    H  N N 311 
SER H2   H  N N 312 
SER HA   H  N N 313 
SER HB2  H  N N 314 
SER HB3  H  N N 315 
SER HG   H  N N 316 
SER HXT  H  N N 317 
THR N    N  N N 318 
THR CA   C  N S 319 
THR C    C  N N 320 
THR O    O  N N 321 
THR CB   C  N R 322 
THR OG1  O  N N 323 
THR CG2  C  N N 324 
THR OXT  O  N N 325 
THR H    H  N N 326 
THR H2   H  N N 327 
THR HA   H  N N 328 
THR HB   H  N N 329 
THR HG1  H  N N 330 
THR HG21 H  N N 331 
THR HG22 H  N N 332 
THR HG23 H  N N 333 
THR HXT  H  N N 334 
TRP N    N  N N 335 
TRP CA   C  N S 336 
TRP C    C  N N 337 
TRP O    O  N N 338 
TRP CB   C  N N 339 
TRP CG   C  Y N 340 
TRP CD1  C  Y N 341 
TRP CD2  C  Y N 342 
TRP NE1  N  Y N 343 
TRP CE2  C  Y N 344 
TRP CE3  C  Y N 345 
TRP CZ2  C  Y N 346 
TRP CZ3  C  Y N 347 
TRP CH2  C  Y N 348 
TRP OXT  O  N N 349 
TRP H    H  N N 350 
TRP H2   H  N N 351 
TRP HA   H  N N 352 
TRP HB2  H  N N 353 
TRP HB3  H  N N 354 
TRP HD1  H  N N 355 
TRP HE1  H  N N 356 
TRP HE3  H  N N 357 
TRP HZ2  H  N N 358 
TRP HZ3  H  N N 359 
TRP HH2  H  N N 360 
TRP HXT  H  N N 361 
TYR N    N  N N 362 
TYR CA   C  N S 363 
TYR C    C  N N 364 
TYR O    O  N N 365 
TYR CB   C  N N 366 
TYR CG   C  Y N 367 
TYR CD1  C  Y N 368 
TYR CD2  C  Y N 369 
TYR CE1  C  Y N 370 
TYR CE2  C  Y N 371 
TYR CZ   C  Y N 372 
TYR OH   O  N N 373 
TYR OXT  O  N N 374 
TYR H    H  N N 375 
TYR H2   H  N N 376 
TYR HA   H  N N 377 
TYR HB2  H  N N 378 
TYR HB3  H  N N 379 
TYR HD1  H  N N 380 
TYR HD2  H  N N 381 
TYR HE1  H  N N 382 
TYR HE2  H  N N 383 
TYR HH   H  N N 384 
TYR HXT  H  N N 385 
VAL N    N  N N 386 
VAL CA   C  N S 387 
VAL C    C  N N 388 
VAL O    O  N N 389 
VAL CB   C  N N 390 
VAL CG1  C  N N 391 
VAL CG2  C  N N 392 
VAL OXT  O  N N 393 
VAL H    H  N N 394 
VAL H2   H  N N 395 
VAL HA   H  N N 396 
VAL HB   H  N N 397 
VAL HG11 H  N N 398 
VAL HG12 H  N N 399 
VAL HG13 H  N N 400 
VAL HG21 H  N N 401 
VAL HG22 H  N N 402 
VAL HG23 H  N N 403 
VAL HXT  H  N N 404 
ZN  ZN   ZN N N 405 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
GOL C1  O1   sing N N 129 
GOL C1  C2   sing N N 130 
GOL C1  H11  sing N N 131 
GOL C1  H12  sing N N 132 
GOL O1  HO1  sing N N 133 
GOL C2  O2   sing N N 134 
GOL C2  C3   sing N N 135 
GOL C2  H2   sing N N 136 
GOL O2  HO2  sing N N 137 
GOL C3  O3   sing N N 138 
GOL C3  H31  sing N N 139 
GOL C3  H32  sing N N 140 
GOL O3  HO3  sing N N 141 
HIS N   CA   sing N N 142 
HIS N   H    sing N N 143 
HIS N   H2   sing N N 144 
HIS CA  C    sing N N 145 
HIS CA  CB   sing N N 146 
HIS CA  HA   sing N N 147 
HIS C   O    doub N N 148 
HIS C   OXT  sing N N 149 
HIS CB  CG   sing N N 150 
HIS CB  HB2  sing N N 151 
HIS CB  HB3  sing N N 152 
HIS CG  ND1  sing Y N 153 
HIS CG  CD2  doub Y N 154 
HIS ND1 CE1  doub Y N 155 
HIS ND1 HD1  sing N N 156 
HIS CD2 NE2  sing Y N 157 
HIS CD2 HD2  sing N N 158 
HIS CE1 NE2  sing Y N 159 
HIS CE1 HE1  sing N N 160 
HIS NE2 HE2  sing N N 161 
HIS OXT HXT  sing N N 162 
HOH O   H1   sing N N 163 
HOH O   H2   sing N N 164 
ILE N   CA   sing N N 165 
ILE N   H    sing N N 166 
ILE N   H2   sing N N 167 
ILE CA  C    sing N N 168 
ILE CA  CB   sing N N 169 
ILE CA  HA   sing N N 170 
ILE C   O    doub N N 171 
ILE C   OXT  sing N N 172 
ILE CB  CG1  sing N N 173 
ILE CB  CG2  sing N N 174 
ILE CB  HB   sing N N 175 
ILE CG1 CD1  sing N N 176 
ILE CG1 HG12 sing N N 177 
ILE CG1 HG13 sing N N 178 
ILE CG2 HG21 sing N N 179 
ILE CG2 HG22 sing N N 180 
ILE CG2 HG23 sing N N 181 
ILE CD1 HD11 sing N N 182 
ILE CD1 HD12 sing N N 183 
ILE CD1 HD13 sing N N 184 
ILE OXT HXT  sing N N 185 
LEU N   CA   sing N N 186 
LEU N   H    sing N N 187 
LEU N   H2   sing N N 188 
LEU CA  C    sing N N 189 
LEU CA  CB   sing N N 190 
LEU CA  HA   sing N N 191 
LEU C   O    doub N N 192 
LEU C   OXT  sing N N 193 
LEU CB  CG   sing N N 194 
LEU CB  HB2  sing N N 195 
LEU CB  HB3  sing N N 196 
LEU CG  CD1  sing N N 197 
LEU CG  CD2  sing N N 198 
LEU CG  HG   sing N N 199 
LEU CD1 HD11 sing N N 200 
LEU CD1 HD12 sing N N 201 
LEU CD1 HD13 sing N N 202 
LEU CD2 HD21 sing N N 203 
LEU CD2 HD22 sing N N 204 
LEU CD2 HD23 sing N N 205 
LEU OXT HXT  sing N N 206 
LYS N   CA   sing N N 207 
LYS N   H    sing N N 208 
LYS N   H2   sing N N 209 
LYS CA  C    sing N N 210 
LYS CA  CB   sing N N 211 
LYS CA  HA   sing N N 212 
LYS C   O    doub N N 213 
LYS C   OXT  sing N N 214 
LYS CB  CG   sing N N 215 
LYS CB  HB2  sing N N 216 
LYS CB  HB3  sing N N 217 
LYS CG  CD   sing N N 218 
LYS CG  HG2  sing N N 219 
LYS CG  HG3  sing N N 220 
LYS CD  CE   sing N N 221 
LYS CD  HD2  sing N N 222 
LYS CD  HD3  sing N N 223 
LYS CE  NZ   sing N N 224 
LYS CE  HE2  sing N N 225 
LYS CE  HE3  sing N N 226 
LYS NZ  HZ1  sing N N 227 
LYS NZ  HZ2  sing N N 228 
LYS NZ  HZ3  sing N N 229 
LYS OXT HXT  sing N N 230 
MET N   CA   sing N N 231 
MET N   H    sing N N 232 
MET N   H2   sing N N 233 
MET CA  C    sing N N 234 
MET CA  CB   sing N N 235 
MET CA  HA   sing N N 236 
MET C   O    doub N N 237 
MET C   OXT  sing N N 238 
MET CB  CG   sing N N 239 
MET CB  HB2  sing N N 240 
MET CB  HB3  sing N N 241 
MET CG  SD   sing N N 242 
MET CG  HG2  sing N N 243 
MET CG  HG3  sing N N 244 
MET SD  CE   sing N N 245 
MET CE  HE1  sing N N 246 
MET CE  HE2  sing N N 247 
MET CE  HE3  sing N N 248 
MET OXT HXT  sing N N 249 
PHE N   CA   sing N N 250 
PHE N   H    sing N N 251 
PHE N   H2   sing N N 252 
PHE CA  C    sing N N 253 
PHE CA  CB   sing N N 254 
PHE CA  HA   sing N N 255 
PHE C   O    doub N N 256 
PHE C   OXT  sing N N 257 
PHE CB  CG   sing N N 258 
PHE CB  HB2  sing N N 259 
PHE CB  HB3  sing N N 260 
PHE CG  CD1  doub Y N 261 
PHE CG  CD2  sing Y N 262 
PHE CD1 CE1  sing Y N 263 
PHE CD1 HD1  sing N N 264 
PHE CD2 CE2  doub Y N 265 
PHE CD2 HD2  sing N N 266 
PHE CE1 CZ   doub Y N 267 
PHE CE1 HE1  sing N N 268 
PHE CE2 CZ   sing Y N 269 
PHE CE2 HE2  sing N N 270 
PHE CZ  HZ   sing N N 271 
PHE OXT HXT  sing N N 272 
PRO N   CA   sing N N 273 
PRO N   CD   sing N N 274 
PRO N   H    sing N N 275 
PRO CA  C    sing N N 276 
PRO CA  CB   sing N N 277 
PRO CA  HA   sing N N 278 
PRO C   O    doub N N 279 
PRO C   OXT  sing N N 280 
PRO CB  CG   sing N N 281 
PRO CB  HB2  sing N N 282 
PRO CB  HB3  sing N N 283 
PRO CG  CD   sing N N 284 
PRO CG  HG2  sing N N 285 
PRO CG  HG3  sing N N 286 
PRO CD  HD2  sing N N 287 
PRO CD  HD3  sing N N 288 
PRO OXT HXT  sing N N 289 
SER N   CA   sing N N 290 
SER N   H    sing N N 291 
SER N   H2   sing N N 292 
SER CA  C    sing N N 293 
SER CA  CB   sing N N 294 
SER CA  HA   sing N N 295 
SER C   O    doub N N 296 
SER C   OXT  sing N N 297 
SER CB  OG   sing N N 298 
SER CB  HB2  sing N N 299 
SER CB  HB3  sing N N 300 
SER OG  HG   sing N N 301 
SER OXT HXT  sing N N 302 
THR N   CA   sing N N 303 
THR N   H    sing N N 304 
THR N   H2   sing N N 305 
THR CA  C    sing N N 306 
THR CA  CB   sing N N 307 
THR CA  HA   sing N N 308 
THR C   O    doub N N 309 
THR C   OXT  sing N N 310 
THR CB  OG1  sing N N 311 
THR CB  CG2  sing N N 312 
THR CB  HB   sing N N 313 
THR OG1 HG1  sing N N 314 
THR CG2 HG21 sing N N 315 
THR CG2 HG22 sing N N 316 
THR CG2 HG23 sing N N 317 
THR OXT HXT  sing N N 318 
TRP N   CA   sing N N 319 
TRP N   H    sing N N 320 
TRP N   H2   sing N N 321 
TRP CA  C    sing N N 322 
TRP CA  CB   sing N N 323 
TRP CA  HA   sing N N 324 
TRP C   O    doub N N 325 
TRP C   OXT  sing N N 326 
TRP CB  CG   sing N N 327 
TRP CB  HB2  sing N N 328 
TRP CB  HB3  sing N N 329 
TRP CG  CD1  doub Y N 330 
TRP CG  CD2  sing Y N 331 
TRP CD1 NE1  sing Y N 332 
TRP CD1 HD1  sing N N 333 
TRP CD2 CE2  doub Y N 334 
TRP CD2 CE3  sing Y N 335 
TRP NE1 CE2  sing Y N 336 
TRP NE1 HE1  sing N N 337 
TRP CE2 CZ2  sing Y N 338 
TRP CE3 CZ3  doub Y N 339 
TRP CE3 HE3  sing N N 340 
TRP CZ2 CH2  doub Y N 341 
TRP CZ2 HZ2  sing N N 342 
TRP CZ3 CH2  sing Y N 343 
TRP CZ3 HZ3  sing N N 344 
TRP CH2 HH2  sing N N 345 
TRP OXT HXT  sing N N 346 
TYR N   CA   sing N N 347 
TYR N   H    sing N N 348 
TYR N   H2   sing N N 349 
TYR CA  C    sing N N 350 
TYR CA  CB   sing N N 351 
TYR CA  HA   sing N N 352 
TYR C   O    doub N N 353 
TYR C   OXT  sing N N 354 
TYR CB  CG   sing N N 355 
TYR CB  HB2  sing N N 356 
TYR CB  HB3  sing N N 357 
TYR CG  CD1  doub Y N 358 
TYR CG  CD2  sing Y N 359 
TYR CD1 CE1  sing Y N 360 
TYR CD1 HD1  sing N N 361 
TYR CD2 CE2  doub Y N 362 
TYR CD2 HD2  sing N N 363 
TYR CE1 CZ   doub Y N 364 
TYR CE1 HE1  sing N N 365 
TYR CE2 CZ   sing Y N 366 
TYR CE2 HE2  sing N N 367 
TYR CZ  OH   sing N N 368 
TYR OH  HH   sing N N 369 
TYR OXT HXT  sing N N 370 
VAL N   CA   sing N N 371 
VAL N   H    sing N N 372 
VAL N   H2   sing N N 373 
VAL CA  C    sing N N 374 
VAL CA  CB   sing N N 375 
VAL CA  HA   sing N N 376 
VAL C   O    doub N N 377 
VAL C   OXT  sing N N 378 
VAL CB  CG1  sing N N 379 
VAL CB  CG2  sing N N 380 
VAL CB  HB   sing N N 381 
VAL CG1 HG11 sing N N 382 
VAL CG1 HG12 sing N N 383 
VAL CG1 HG13 sing N N 384 
VAL CG2 HG21 sing N N 385 
VAL CG2 HG22 sing N N 386 
VAL CG2 HG23 sing N N 387 
VAL OXT HXT  sing N N 388 
# 
_pdbx_audit_support.funding_organization   'Netherlands Organisation for Scientific Research (NWO)' 
_pdbx_audit_support.country                Netherlands 
_pdbx_audit_support.grant_number           OCENW.KLEIN.264 
_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   2GDN 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9QI5 
_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]   0.025536 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.024405 
_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]   0.003738 
_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   . GLY A 1 1   ? 17.445  10.996  -58.986 1.00 58.34 ? 27  GLY A N   1 
ATOM   2    C  CA  . GLY A 1 1   ? 18.650  11.239  -58.168 1.00 56.27 ? 27  GLY A CA  1 
ATOM   3    C  C   . GLY A 1 1   ? 19.316  9.925   -57.755 1.00 54.19 ? 27  GLY A C   1 
ATOM   4    O  O   . GLY A 1 1   ? 19.231  8.925   -58.472 1.00 45.01 ? 27  GLY A O   1 
ATOM   5    N  N   . ASP A 1 2   ? 19.932  9.945   -56.566 1.00 52.09 ? 28  ASP A N   1 
ATOM   6    C  CA  . ASP A 1 2   ? 20.779  8.861   -56.096 1.00 51.01 ? 28  ASP A CA  1 
ATOM   7    C  C   . ASP A 1 2   ? 20.003  7.558   -56.035 1.00 41.90 ? 28  ASP A C   1 
ATOM   8    O  O   . ASP A 1 2   ? 20.468  6.562   -56.565 1.00 36.59 ? 28  ASP A O   1 
ATOM   9    C  CB  . ASP A 1 2   ? 21.460  9.167   -54.767 1.00 55.98 ? 28  ASP A CB  1 
ATOM   10   C  CG  . ASP A 1 2   ? 22.828  9.837   -54.865 1.00 64.28 ? 28  ASP A CG  1 
ATOM   11   O  OD1 . ASP A 1 2   ? 23.158  10.389  -55.945 1.00 64.09 ? 28  ASP A OD1 1 
ATOM   12   O  OD2 . ASP A 1 2   ? 23.575  9.783   -53.863 1.00 74.07 ? 28  ASP A OD2 1 
ATOM   13   N  N   . LEU A 1 3   ? 18.823  7.570   -55.421 1.00 39.38 ? 29  LEU A N   1 
ATOM   14   C  CA  . LEU A 1 3   ? 18.096  6.331   -55.212 1.00 34.75 ? 29  LEU A CA  1 
ATOM   15   C  C   . LEU A 1 3   ? 17.604  5.766   -56.545 1.00 29.96 ? 29  LEU A C   1 
ATOM   16   O  O   . LEU A 1 3   ? 17.687  4.549   -56.776 1.00 27.74 ? 29  LEU A O   1 
ATOM   17   C  CB  . LEU A 1 3   ? 16.959  6.607   -54.239 1.00 36.38 ? 29  LEU A CB  1 
ATOM   18   C  CG  . LEU A 1 3   ? 16.446  5.393   -53.464 1.00 38.53 ? 29  LEU A CG  1 
ATOM   19   C  CD1 . LEU A 1 3   ? 17.535  4.563   -52.781 1.00 39.03 ? 29  LEU A CD1 1 
ATOM   20   C  CD2 . LEU A 1 3   ? 15.426  5.906   -52.445 1.00 40.03 ? 29  LEU A CD2 1 
ATOM   21   N  N   . ALA A 1 4   ? 17.115  6.647   -57.431 1.00 26.96 ? 30  ALA A N   1 
ATOM   22   C  CA  . ALA A 1 4   ? 16.677  6.222   -58.758 1.00 24.70 ? 30  ALA A CA  1 
ATOM   23   C  C   . ALA A 1 4   ? 17.829  5.534   -59.506 1.00 24.20 ? 30  ALA A C   1 
ATOM   24   O  O   . ALA A 1 4   ? 17.636  4.469   -60.097 1.00 24.84 ? 30  ALA A O   1 
ATOM   25   C  CB  . ALA A 1 4   ? 16.116  7.387   -59.545 1.00 24.52 ? 30  ALA A CB  1 
ATOM   26   N  N   . ASP A 1 5   ? 19.031  6.112   -59.430 1.00 24.63 ? 31  ASP A N   1 
ATOM   27   C  CA  . ASP A 1 5   ? 20.210  5.551   -60.092 1.00 25.14 ? 31  ASP A CA  1 
ATOM   28   C  C   . ASP A 1 5   ? 20.572  4.178   -59.498 1.00 24.02 ? 31  ASP A C   1 
ATOM   29   O  O   . ASP A 1 5   ? 20.915  3.248   -60.235 1.00 23.77 ? 31  ASP A O   1 
ATOM   30   C  CB  . ASP A 1 5   ? 21.391  6.496   -60.075 1.00 26.57 ? 31  ASP A CB  1 
ATOM   31   C  CG  . ASP A 1 5   ? 21.234  7.811   -60.841 1.00 28.26 ? 31  ASP A CG  1 
ATOM   32   O  OD1 . ASP A 1 5   ? 20.678  7.798   -61.942 1.00 31.02 ? 31  ASP A OD1 1 
ATOM   33   O  OD2 . ASP A 1 5   ? 21.679  8.838   -60.344 1.00 31.46 ? 31  ASP A OD2 1 
ATOM   34   N  N   . ARG A 1 6   ? 20.500  4.053   -58.174 1.00 24.55 ? 32  ARG A N   1 
ATOM   35   C  CA  . ARG A 1 6   ? 20.798  2.789   -57.512 1.00 26.76 ? 32  ARG A CA  1 
ATOM   36   C  C   . ARG A 1 6   ? 19.829  1.694   -57.967 1.00 23.85 ? 32  ARG A C   1 
ATOM   37   O  O   . ARG A 1 6   ? 20.252  0.581   -58.256 1.00 22.03 ? 32  ARG A O   1 
ATOM   38   C  CB  . ARG A 1 6   ? 20.804  2.915   -55.983 1.00 29.77 ? 32  ARG A CB  1 
ATOM   39   C  CG  . ARG A 1 6   ? 21.977  3.764   -55.512 1.00 38.64 ? 32  ARG A CG  1 
ATOM   40   C  CD  . ARG A 1 6   ? 22.080  3.955   -54.001 1.00 44.69 ? 32  ARG A CD  1 
ATOM   41   N  NE  . ARG A 1 6   ? 22.203  2.672   -53.296 1.00 52.10 ? 32  ARG A NE  1 
ATOM   42   C  CZ  . ARG A 1 6   ? 21.989  2.489   -51.993 1.00 58.54 ? 32  ARG A CZ  1 
ATOM   43   N  NH1 . ARG A 1 6   ? 21.767  3.531   -51.211 1.00 59.20 ? 32  ARG A NH1 1 
ATOM   44   N  NH2 . ARG A 1 6   ? 21.986  1.266   -51.483 1.00 61.43 ? 32  ARG A NH2 1 
ATOM   45   N  N   . PHE A 1 7   ? 18.526  2.021   -58.030 1.00 22.58 ? 33  PHE A N   1 
ATOM   46   C  CA  . PHE A 1 7   ? 17.519  1.060   -58.443 1.00 20.91 ? 33  PHE A CA  1 
ATOM   47   C  C   . PHE A 1 7   ? 17.715  0.673   -59.910 1.00 19.68 ? 33  PHE A C   1 
ATOM   48   O  O   . PHE A 1 7   ? 17.503  -0.482  -60.303 1.00 19.11 ? 33  PHE A O   1 
ATOM   49   C  CB  . PHE A 1 7   ? 16.108  1.610   -58.222 1.00 20.52 ? 33  PHE A CB  1 
ATOM   50   C  CG  . PHE A 1 7   ? 15.666  1.692   -56.767 1.00 21.29 ? 33  PHE A CG  1 
ATOM   51   C  CD1 . PHE A 1 7   ? 15.963  0.681   -55.853 1.00 21.53 ? 33  PHE A CD1 1 
ATOM   52   C  CD2 . PHE A 1 7   ? 14.896  2.767   -56.331 1.00 22.24 ? 33  PHE A CD2 1 
ATOM   53   C  CE1 . PHE A 1 7   ? 15.552  0.780   -54.528 1.00 22.54 ? 33  PHE A CE1 1 
ATOM   54   C  CE2 . PHE A 1 7   ? 14.491  2.862   -55.012 1.00 23.06 ? 33  PHE A CE2 1 
ATOM   55   C  CZ  . PHE A 1 7   ? 14.798  1.868   -54.122 1.00 23.08 ? 33  PHE A CZ  1 
ATOM   56   N  N   . ALA A 1 8   ? 18.117  1.639   -60.734 1.00 19.39 ? 34  ALA A N   1 
ATOM   57   C  CA  . ALA A 1 8   ? 18.379  1.342   -62.132 1.00 19.09 ? 34  ALA A CA  1 
ATOM   58   C  C   . ALA A 1 8   ? 19.554  0.376   -62.283 1.00 18.83 ? 34  ALA A C   1 
ATOM   59   O  O   . ALA A 1 8   ? 19.543  -0.463  -63.181 1.00 19.17 ? 34  ALA A O   1 
ATOM   60   C  CB  . ALA A 1 8   ? 18.623  2.606   -62.909 1.00 19.63 ? 34  ALA A CB  1 
ATOM   61   N  N   . GLU A 1 9   ? 20.583  0.534   -61.449 1.00 19.07 ? 35  GLU A N   1 
ATOM   62   C  CA  . GLU A 1 9   ? 21.723  -0.367  -61.491 1.00 19.79 ? 35  GLU A CA  1 
ATOM   63   C  C   . GLU A 1 9   ? 21.306  -1.779  -61.080 1.00 19.43 ? 35  GLU A C   1 
ATOM   64   O  O   . GLU A 1 9   ? 21.843  -2.747  -61.612 1.00 19.74 ? 35  GLU A O   1 
ATOM   65   C  CB  . GLU A 1 9   ? 22.850  0.174   -60.614 1.00 20.72 ? 35  GLU A CB  1 
ATOM   66   C  CG  . GLU A 1 9   ? 24.155  -0.598  -60.720 1.00 21.96 ? 35  GLU A CG  1 
ATOM   67   C  CD  . GLU A 1 9   ? 24.264  -1.794  -59.810 1.00 21.84 ? 35  GLU A CD  1 
ATOM   68   O  OE1 . GLU A 1 9   ? 23.416  -1.957  -58.940 1.00 21.08 ? 35  GLU A OE1 1 
ATOM   69   O  OE2 . GLU A 1 9   ? 25.196  -2.600  -60.026 1.00 22.98 ? 35  GLU A OE2 1 
ATOM   70   N  N   . LEU A 1 10  ? 20.385  -1.903  -60.117 1.00 19.21 ? 36  LEU A N   1 
ATOM   71   C  CA  . LEU A 1 10  ? 19.858  -3.214  -59.771 1.00 20.08 ? 36  LEU A CA  1 
ATOM   72   C  C   . LEU A 1 10  ? 19.228  -3.861  -61.006 1.00 19.22 ? 36  LEU A C   1 
ATOM   73   O  O   . LEU A 1 10  ? 19.448  -5.049  -61.266 1.00 19.31 ? 36  LEU A O   1 
ATOM   74   C  CB  . LEU A 1 10  ? 18.827  -3.096  -58.648 1.00 20.87 ? 36  LEU A CB  1 
ATOM   75   C  CG  . LEU A 1 10  ? 19.335  -3.270  -57.211 1.00 23.04 ? 36  LEU A CG  1 
ATOM   76   C  CD1 . LEU A 1 10  ? 20.568  -2.507  -56.947 1.00 25.05 ? 36  LEU A CD1 1 
ATOM   77   C  CD2 . LEU A 1 10  ? 18.203  -2.889  -56.254 1.00 23.34 ? 36  LEU A CD2 1 
ATOM   78   N  N   . GLU A 1 11  ? 18.449  -3.072  -61.766 1.00 18.02 ? 37  GLU A N   1 
ATOM   79   C  CA  . GLU A 1 11  ? 17.777  -3.608  -62.942 1.00 18.27 ? 37  GLU A CA  1 
ATOM   80   C  C   . GLU A 1 11  ? 18.802  -4.115  -63.969 1.00 18.91 ? 37  GLU A C   1 
ATOM   81   O  O   . GLU A 1 11  ? 18.636  -5.192  -64.564 1.00 18.19 ? 37  GLU A O   1 
ATOM   82   C  CB  . GLU A 1 11  ? 16.829  -2.611  -63.605 1.00 18.11 ? 37  GLU A CB  1 
ATOM   83   C  CG  . GLU A 1 11  ? 15.585  -2.307  -62.780 1.00 18.50 ? 37  GLU A CG  1 
ATOM   84   C  CD  . GLU A 1 11  ? 14.592  -1.413  -63.469 1.00 17.90 ? 37  GLU A CD  1 
ATOM   85   O  OE1 . GLU A 1 11  ? 15.028  -0.383  -64.028 1.00 20.80 ? 37  GLU A OE1 1 
ATOM   86   O  OE2 . GLU A 1 11  ? 13.380  -1.701  -63.359 1.00 17.19 ? 37  GLU A OE2 1 
ATOM   87   N  N   . ARG A 1 12  ? 19.858  -3.334  -64.184 1.00 19.86 ? 38  ARG A N   1 
ATOM   88   C  CA  . ARG A 1 12  ? 20.896  -3.696  -65.144 1.00 20.43 ? 38  ARG A CA  1 
ATOM   89   C  C   . ARG A 1 12  ? 21.605  -4.969  -64.674 1.00 20.58 ? 38  ARG A C   1 
ATOM   90   O  O   . ARG A 1 12  ? 21.808  -5.901  -65.459 1.00 21.23 ? 38  ARG A O   1 
ATOM   91   C  CB  . ARG A 1 12  ? 21.939  -2.591  -65.382 1.00 21.60 ? 38  ARG A CB  1 
ATOM   92   C  CG  . ARG A 1 12  ? 21.373  -1.329  -66.015 1.00 22.04 ? 38  ARG A CG  1 
ATOM   93   C  CD  . ARG A 1 12  ? 22.455  -0.416  -66.561 1.00 23.12 ? 38  ARG A CD  1 
ATOM   94   N  NE  . ARG A 1 12  ? 23.392  0.011   -65.525 1.00 24.84 ? 38  ARG A NE  1 
ATOM   95   C  CZ  . ARG A 1 12  ? 23.202  1.044   -64.706 1.00 26.49 ? 38  ARG A CZ  1 
ATOM   96   N  NH1 . ARG A 1 12  ? 22.064  1.704   -64.733 1.00 26.75 ? 38  ARG A NH1 1 
ATOM   97   N  NH2 . ARG A 1 12  ? 24.143  1.402   -63.838 1.00 28.64 ? 38  ARG A NH2 1 
ATOM   98   N  N   . ARG A 1 13  ? 22.003  -5.012  -63.398 1.00 18.83 ? 39  ARG A N   1 
ATOM   99   C  CA  . ARG A 1 13  ? 22.792  -6.125  -62.894 1.00 19.77 ? 39  ARG A CA  1 
ATOM   100  C  C   . ARG A 1 13  ? 21.992  -7.433  -62.879 1.00 20.28 ? 39  ARG A C   1 
ATOM   101  O  O   . ARG A 1 13  ? 22.513  -8.502  -63.194 1.00 22.33 ? 39  ARG A O   1 
ATOM   102  C  CB  . ARG A 1 13  ? 23.353  -5.751  -61.526 1.00 19.77 ? 39  ARG A CB  1 
ATOM   103  C  CG  . ARG A 1 13  ? 24.196  -6.861  -60.922 1.00 20.86 ? 39  ARG A CG  1 
ATOM   104  C  CD  . ARG A 1 13  ? 25.230  -6.250  -59.983 1.00 22.16 ? 39  ARG A CD  1 
ATOM   105  N  NE  . ARG A 1 13  ? 24.681  -5.221  -59.092 1.00 21.88 ? 39  ARG A NE  1 
ATOM   106  C  CZ  . ARG A 1 13  ? 23.763  -5.431  -58.123 1.00 22.49 ? 39  ARG A CZ  1 
ATOM   107  N  NH1 . ARG A 1 13  ? 23.496  -6.646  -57.661 1.00 21.54 ? 39  ARG A NH1 1 
ATOM   108  N  NH2 . ARG A 1 13  ? 23.156  -4.391  -57.571 1.00 22.27 ? 39  ARG A NH2 1 
ATOM   109  N  N   . TYR A 1 14  ? 20.712  -7.379  -62.538 1.00 20.25 ? 40  TYR A N   1 
ATOM   110  C  CA  . TYR A 1 14  ? 19.914  -8.601  -62.461 1.00 20.51 ? 40  TYR A CA  1 
ATOM   111  C  C   . TYR A 1 14  ? 19.168  -8.903  -63.750 1.00 21.60 ? 40  TYR A C   1 
ATOM   112  O  O   . TYR A 1 14  ? 18.504  -9.944  -63.852 1.00 21.30 ? 40  TYR A O   1 
ATOM   113  C  CB  . TYR A 1 14  ? 18.890  -8.443  -61.340 1.00 18.43 ? 40  TYR A CB  1 
ATOM   114  C  CG  . TYR A 1 14  ? 19.492  -8.707  -59.975 1.00 19.31 ? 40  TYR A CG  1 
ATOM   115  C  CD1 . TYR A 1 14  ? 19.700  -10.000 -59.518 1.00 19.84 ? 40  TYR A CD1 1 
ATOM   116  C  CD2 . TYR A 1 14  ? 19.858  -7.660  -59.146 1.00 18.69 ? 40  TYR A CD2 1 
ATOM   117  C  CE1 . TYR A 1 14  ? 20.265  -10.235 -58.276 1.00 20.21 ? 40  TYR A CE1 1 
ATOM   118  C  CE2 . TYR A 1 14  ? 20.398  -7.880  -57.893 1.00 20.67 ? 40  TYR A CE2 1 
ATOM   119  C  CZ  . TYR A 1 14  ? 20.616  -9.181  -57.463 1.00 21.12 ? 40  TYR A CZ  1 
ATOM   120  O  OH  . TYR A 1 14  ? 21.098  -9.416  -56.205 1.00 23.89 ? 40  TYR A OH  1 
ATOM   121  N  N   . ASP A 1 15  ? 19.278  -7.979  -64.722 1.00 21.59 ? 41  ASP A N   1 
ATOM   122  C  CA  . ASP A 1 15  ? 18.515  -8.067  -65.951 1.00 23.32 ? 41  ASP A CA  1 
ATOM   123  C  C   . ASP A 1 15  ? 17.032  -8.275  -65.619 1.00 21.99 ? 41  ASP A C   1 
ATOM   124  O  O   . ASP A 1 15  ? 16.434  -9.288  -65.957 1.00 22.03 ? 41  ASP A O   1 
ATOM   125  C  CB  . ASP A 1 15  ? 19.073  -9.149  -66.848 1.00 25.71 ? 41  ASP A CB  1 
ATOM   126  C  CG  . ASP A 1 15  ? 18.446  -9.192  -68.223 1.00 29.65 ? 41  ASP A CG  1 
ATOM   127  O  OD1 . ASP A 1 15  ? 18.049  -8.123  -68.723 1.00 28.58 ? 41  ASP A OD1 1 
ATOM   128  O  OD2 . ASP A 1 15  ? 18.327  -10.306 -68.753 1.00 33.68 ? 41  ASP A OD2 1 
ATOM   129  N  N   . ALA A 1 16  ? 16.459  -7.285  -64.939 1.00 17.67 ? 42  ALA A N   1 
ATOM   130  C  CA  . ALA A 1 16  ? 15.157  -7.390  -64.311 1.00 17.07 ? 42  ALA A CA  1 
ATOM   131  C  C   . ALA A 1 16  ? 14.436  -6.056  -64.409 1.00 16.89 ? 42  ALA A C   1 
ATOM   132  O  O   . ALA A 1 16  ? 15.084  -5.027  -64.584 1.00 18.44 ? 42  ALA A O   1 
ATOM   133  C  CB  . ALA A 1 16  ? 15.308  -7.761  -62.853 1.00 16.63 ? 42  ALA A CB  1 
ATOM   134  N  N   . ARG A 1 17  ? 13.100  -6.089  -64.245 1.00 15.66 ? 43  ARG A N   1 
ATOM   135  C  CA  . ARG A 1 17  ? 12.324  -4.903  -63.973 1.00 16.70 ? 43  ARG A CA  1 
ATOM   136  C  C   . ARG A 1 17  ? 11.979  -4.911  -62.490 1.00 16.83 ? 43  ARG A C   1 
ATOM   137  O  O   . ARG A 1 17  ? 11.522  -5.942  -61.972 1.00 14.68 ? 43  ARG A O   1 
ATOM   138  C  CB  . ARG A 1 17  ? 11.076  -4.865  -64.864 1.00 17.13 ? 43  ARG A CB  1 
ATOM   139  C  CG  . ARG A 1 17  ? 10.224  -3.611  -64.713 1.00 17.80 ? 43  ARG A CG  1 
ATOM   140  C  CD  . ARG A 1 17  ? 9.014   -3.617  -65.603 1.00 18.44 ? 43  ARG A CD  1 
ATOM   141  N  NE  . ARG A 1 17  ? 8.078   -4.693  -65.286 1.00 18.12 ? 43  ARG A NE  1 
ATOM   142  C  CZ  . ARG A 1 17  ? 6.792   -4.546  -64.916 1.00 16.59 ? 43  ARG A CZ  1 
ATOM   143  N  NH1 . ARG A 1 17  ? 6.228   -3.354  -64.826 1.00 15.67 ? 43  ARG A NH1 1 
ATOM   144  N  NH2 . ARG A 1 17  ? 6.085   -5.635  -64.643 1.00 16.09 ? 43  ARG A NH2 1 
ATOM   145  N  N   . LEU A 1 18  ? 12.220  -3.767  -61.828 1.00 16.09 ? 44  LEU A N   1 
ATOM   146  C  CA  . LEU A 1 18  ? 12.036  -3.634  -60.390 1.00 16.09 ? 44  LEU A CA  1 
ATOM   147  C  C   . LEU A 1 18  ? 11.011  -2.552  -60.122 1.00 16.14 ? 44  LEU A C   1 
ATOM   148  O  O   . LEU A 1 18  ? 11.054  -1.482  -60.741 1.00 15.03 ? 44  LEU A O   1 
ATOM   149  C  CB  . LEU A 1 18  ? 13.360  -3.296  -59.717 1.00 16.07 ? 44  LEU A CB  1 
ATOM   150  C  CG  . LEU A 1 18  ? 13.303  -2.899  -58.242 1.00 16.34 ? 44  LEU A CG  1 
ATOM   151  C  CD1 . LEU A 1 18  ? 12.880  -4.069  -57.381 1.00 17.38 ? 44  LEU A CD1 1 
ATOM   152  C  CD2 . LEU A 1 18  ? 14.655  -2.381  -57.779 1.00 18.07 ? 44  LEU A CD2 1 
ATOM   153  N  N   . GLY A 1 19  ? 10.128  -2.839  -59.163 1.00 15.23 ? 45  GLY A N   1 
ATOM   154  C  CA  . GLY A 1 19  ? 9.182   -1.858  -58.696 1.00 15.61 ? 45  GLY A CA  1 
ATOM   155  C  C   . GLY A 1 19  ? 9.278   -1.726  -57.173 1.00 15.74 ? 45  GLY A C   1 
ATOM   156  O  O   . GLY A 1 19  ? 9.343   -2.750  -56.487 1.00 16.94 ? 45  GLY A O   1 
ATOM   157  N  N   . VAL A 1 20  ? 9.252   -0.468  -56.691 1.00 14.47 ? 46  VAL A N   1 
ATOM   158  C  CA  . VAL A 1 20  ? 9.397   -0.171  -55.273 1.00 15.19 ? 46  VAL A CA  1 
ATOM   159  C  C   . VAL A 1 20  ? 8.401   0.902   -54.869 1.00 15.95 ? 46  VAL A C   1 
ATOM   160  O  O   . VAL A 1 20  ? 8.280   1.916   -55.543 1.00 16.38 ? 46  VAL A O   1 
ATOM   161  C  CB  . VAL A 1 20  ? 10.811  0.307   -54.903 1.00 16.78 ? 46  VAL A CB  1 
ATOM   162  C  CG1 . VAL A 1 20  ? 10.925  0.520   -53.392 1.00 17.18 ? 46  VAL A CG1 1 
ATOM   163  C  CG2 . VAL A 1 20  ? 11.881  -0.646  -55.401 1.00 16.95 ? 46  VAL A CG2 1 
ATOM   164  N  N   . TYR A 1 21  ? 7.691   0.683   -53.755 1.00 16.96 ? 47  TYR A N   1 
ATOM   165  C  CA  . TYR A 1 21  ? 6.926   1.747   -53.141 1.00 15.81 ? 47  TYR A CA  1 
ATOM   166  C  C   . TYR A 1 21  ? 7.033   1.654   -51.627 1.00 16.81 ? 47  TYR A C   1 
ATOM   167  O  O   . TYR A 1 21  ? 6.800   0.600   -51.031 1.00 15.88 ? 47  TYR A O   1 
ATOM   168  C  CB  . TYR A 1 21  ? 5.443   1.720   -53.508 1.00 16.02 ? 47  TYR A CB  1 
ATOM   169  C  CG  . TYR A 1 21  ? 4.749   3.022   -53.158 1.00 17.31 ? 47  TYR A CG  1 
ATOM   170  C  CD1 . TYR A 1 21  ? 4.986   4.176   -53.891 1.00 18.32 ? 47  TYR A CD1 1 
ATOM   171  C  CD2 . TYR A 1 21  ? 3.897   3.119   -52.062 1.00 18.09 ? 47  TYR A CD2 1 
ATOM   172  C  CE1 . TYR A 1 21  ? 4.333   5.360   -53.588 1.00 20.34 ? 47  TYR A CE1 1 
ATOM   173  C  CE2 . TYR A 1 21  ? 3.247   4.296   -51.749 1.00 19.12 ? 47  TYR A CE2 1 
ATOM   174  C  CZ  . TYR A 1 21  ? 3.455   5.421   -52.520 1.00 21.10 ? 47  TYR A CZ  1 
ATOM   175  O  OH  . TYR A 1 21  ? 2.868   6.616   -52.234 1.00 24.54 ? 47  TYR A OH  1 
ATOM   176  N  N   . VAL A 1 22  ? 7.352   2.811   -51.037 1.00 18.10 ? 48  VAL A N   1 
ATOM   177  C  CA  . VAL A 1 22  ? 7.248   3.034   -49.613 1.00 19.25 ? 48  VAL A CA  1 
ATOM   178  C  C   . VAL A 1 22  ? 6.473   4.335   -49.426 1.00 20.47 ? 48  VAL A C   1 
ATOM   179  O  O   . VAL A 1 22  ? 6.944   5.385   -49.878 1.00 21.05 ? 48  VAL A O   1 
ATOM   180  C  CB  . VAL A 1 22  ? 8.639   3.146   -48.969 1.00 19.74 ? 48  VAL A CB  1 
ATOM   181  C  CG1 . VAL A 1 22  ? 8.527   3.365   -47.468 1.00 20.34 ? 48  VAL A CG1 1 
ATOM   182  C  CG2 . VAL A 1 22  ? 9.518   1.945   -49.279 1.00 19.03 ? 48  VAL A CG2 1 
ATOM   183  N  N   . PRO A 1 23  ? 5.284   4.293   -48.789 1.00 21.88 ? 49  PRO A N   1 
ATOM   184  C  CA  . PRO A 1 23  ? 4.485   5.492   -48.551 1.00 23.39 ? 49  PRO A CA  1 
ATOM   185  C  C   . PRO A 1 23  ? 5.268   6.521   -47.747 1.00 24.64 ? 49  PRO A C   1 
ATOM   186  O  O   . PRO A 1 23  ? 6.128   6.169   -46.937 1.00 24.87 ? 49  PRO A O   1 
ATOM   187  C  CB  . PRO A 1 23  ? 3.246   4.993   -47.784 1.00 23.50 ? 49  PRO A CB  1 
ATOM   188  C  CG  . PRO A 1 23  ? 3.191   3.518   -48.093 1.00 22.38 ? 49  PRO A CG  1 
ATOM   189  C  CD  . PRO A 1 23  ? 4.628   3.074   -48.298 1.00 21.33 ? 49  PRO A CD  1 
ATOM   190  N  N   . ALA A 1 24  ? 4.973   7.795   -47.998 1.00 26.05 ? 50  ALA A N   1 
ATOM   191  C  CA  . ALA A 1 24  ? 5.462   8.859   -47.145 1.00 27.47 ? 50  ALA A CA  1 
ATOM   192  C  C   . ALA A 1 24  ? 4.958   8.648   -45.714 1.00 27.73 ? 50  ALA A C   1 
ATOM   193  O  O   . ALA A 1 24  ? 3.891   8.081   -45.472 1.00 25.34 ? 50  ALA A O   1 
ATOM   194  C  CB  . ALA A 1 24  ? 5.033   10.222  -47.681 1.00 28.82 ? 50  ALA A CB  1 
ATOM   195  N  N   . THR A 1 25  ? 5.724   9.190   -44.776 1.00 30.83 ? 51  THR A N   1 
ATOM   196  C  CA  . THR A 1 25  ? 5.270   9.357   -43.407 1.00 33.21 ? 51  THR A CA  1 
ATOM   197  C  C   . THR A 1 25  ? 5.382   10.838  -43.074 1.00 35.38 ? 51  THR A C   1 
ATOM   198  O  O   . THR A 1 25  ? 5.738   11.643  -43.934 1.00 37.13 ? 51  THR A O   1 
ATOM   199  C  CB  . THR A 1 25  ? 6.087   8.488   -42.445 1.00 33.68 ? 51  THR A CB  1 
ATOM   200  O  OG1 . THR A 1 25  ? 7.397   9.043   -42.439 1.00 35.60 ? 51  THR A OG1 1 
ATOM   201  C  CG2 . THR A 1 25  ? 6.140   7.034   -42.869 1.00 33.31 ? 51  THR A CG2 1 
ATOM   202  N  N   . GLY A 1 26  ? 5.100   11.188  -41.820 1.00 35.85 ? 52  GLY A N   1 
ATOM   203  C  CA  . GLY A 1 26  ? 5.196   12.571  -41.379 1.00 39.04 ? 52  GLY A CA  1 
ATOM   204  C  C   . GLY A 1 26  ? 6.608   13.150  -41.503 1.00 38.62 ? 52  GLY A C   1 
ATOM   205  O  O   . GLY A 1 26  ? 6.773   14.376  -41.499 1.00 40.40 ? 52  GLY A O   1 
ATOM   206  N  N   . THR A 1 27  ? 7.624   12.277  -41.561 1.00 36.78 ? 53  THR A N   1 
ATOM   207  C  CA  . THR A 1 27  ? 9.007   12.724  -41.586 1.00 38.56 ? 53  THR A CA  1 
ATOM   208  C  C   . THR A 1 27  ? 9.810   12.119  -42.737 1.00 36.84 ? 53  THR A C   1 
ATOM   209  O  O   . THR A 1 27  ? 10.981  12.460  -42.871 1.00 38.61 ? 53  THR A O   1 
ATOM   210  C  CB  . THR A 1 27  ? 9.655   12.394  -40.238 1.00 41.50 ? 53  THR A CB  1 
ATOM   211  O  OG1 . THR A 1 27  ? 9.592   10.974  -40.079 1.00 42.30 ? 53  THR A OG1 1 
ATOM   212  C  CG2 . THR A 1 27  ? 8.957   13.096  -39.087 1.00 43.50 ? 53  THR A CG2 1 
ATOM   213  N  N   . THR A 1 28  ? 9.210   11.266  -43.590 1.00 35.07 ? 54  THR A N   1 
ATOM   214  C  CA  . THR A 1 28  ? 9.925   10.722  -44.738 1.00 34.58 ? 54  THR A CA  1 
ATOM   215  C  C   . THR A 1 28  ? 9.070   10.858  -46.004 1.00 32.42 ? 54  THR A C   1 
ATOM   216  O  O   . THR A 1 28  ? 7.859   10.650  -45.972 1.00 32.32 ? 54  THR A O   1 
ATOM   217  C  CB  . THR A 1 28  ? 10.332  9.261   -44.494 1.00 33.79 ? 54  THR A CB  1 
ATOM   218  O  OG1 . THR A 1 28  ? 9.139   8.514   -44.280 1.00 33.63 ? 54  THR A OG1 1 
ATOM   219  C  CG2 . THR A 1 28  ? 11.247  9.116   -43.288 1.00 35.39 ? 54  THR A CG2 1 
ATOM   220  N  N   . ALA A 1 29  ? 9.720   11.208  -47.112 1.00 31.41 ? 55  ALA A N   1 
ATOM   221  C  CA  . ALA A 1 29  ? 9.081   11.218  -48.416 1.00 30.86 ? 55  ALA A CA  1 
ATOM   222  C  C   . ALA A 1 29  ? 8.884   9.787   -48.917 1.00 28.69 ? 55  ALA A C   1 
ATOM   223  O  O   . ALA A 1 29  ? 9.607   8.855   -48.530 1.00 27.83 ? 55  ALA A O   1 
ATOM   224  C  CB  . ALA A 1 29  ? 9.902   12.016  -49.402 1.00 30.82 ? 55  ALA A CB  1 
ATOM   225  N  N   . ALA A 1 30  ? 7.875   9.627   -49.782 1.00 28.42 ? 56  ALA A N   1 
ATOM   226  C  CA  . ALA A 1 30  ? 7.639   8.370   -50.471 1.00 26.71 ? 56  ALA A CA  1 
ATOM   227  C  C   . ALA A 1 30  ? 8.911   7.947   -51.203 1.00 24.63 ? 56  ALA A C   1 
ATOM   228  O  O   . ALA A 1 30  ? 9.641   8.784   -51.711 1.00 24.68 ? 56  ALA A O   1 
ATOM   229  C  CB  . ALA A 1 30  ? 6.461   8.516   -51.414 1.00 25.99 ? 56  ALA A CB  1 
ATOM   230  N  N   . ILE A 1 31  ? 9.169   6.638   -51.234 1.00 23.74 ? 57  ILE A N   1 
ATOM   231  C  CA  . ILE A 1 31  ? 10.175  6.076   -52.119 1.00 22.93 ? 57  ILE A CA  1 
ATOM   232  C  C   . ILE A 1 31  ? 9.418   5.384   -53.254 1.00 21.84 ? 57  ILE A C   1 
ATOM   233  O  O   . ILE A 1 31  ? 8.543   4.560   -52.992 1.00 20.59 ? 57  ILE A O   1 
ATOM   234  C  CB  . ILE A 1 31  ? 11.111  5.117   -51.361 1.00 23.01 ? 57  ILE A CB  1 
ATOM   235  C  CG1 . ILE A 1 31  ? 11.810  5.811   -50.188 1.00 24.46 ? 57  ILE A CG1 1 
ATOM   236  C  CG2 . ILE A 1 31  ? 12.108  4.465   -52.324 1.00 23.01 ? 57  ILE A CG2 1 
ATOM   237  C  CD1 . ILE A 1 31  ? 12.518  4.836   -49.264 1.00 24.98 ? 57  ILE A CD1 1 
ATOM   238  N  N   . GLU A 1 32  ? 9.721   5.753   -54.504 1.00 21.32 ? 59  GLU A N   1 
ATOM   239  C  CA  . GLU A 1 32  ? 8.921   5.300   -55.648 1.00 22.94 ? 59  GLU A CA  1 
ATOM   240  C  C   . GLU A 1 32  ? 9.864   4.944   -56.796 1.00 19.86 ? 59  GLU A C   1 
ATOM   241  O  O   . GLU A 1 32  ? 10.657  5.785   -57.191 1.00 19.57 ? 59  GLU A O   1 
ATOM   242  C  CB  . GLU A 1 32  ? 8.037   6.394   -56.262 1.00 26.72 ? 59  GLU A CB  1 
ATOM   243  C  CG  . GLU A 1 32  ? 7.107   7.122   -55.305 1.00 31.90 ? 59  GLU A CG  1 
ATOM   244  C  CD  . GLU A 1 32  ? 6.471   8.364   -55.907 1.00 36.72 ? 59  GLU A CD  1 
ATOM   245  O  OE1 . GLU A 1 32  ? 7.174   9.358   -56.074 1.00 40.37 ? 59  GLU A OE1 1 
ATOM   246  O  OE2 . GLU A 1 32  ? 5.277   8.341   -56.230 1.00 44.20 ? 59  GLU A OE2 1 
ATOM   247  N  N   . TYR A 1 33  ? 9.757   3.710   -57.329 1.00 17.61 ? 60  TYR A N   1 
ATOM   248  C  CA  . TYR A 1 33  ? 10.473  3.350   -58.530 1.00 17.69 ? 60  TYR A CA  1 
ATOM   249  C  C   . TYR A 1 33  ? 9.574   2.402   -59.321 1.00 16.25 ? 60  TYR A C   1 
ATOM   250  O  O   . TYR A 1 33  ? 9.247   1.327   -58.852 1.00 17.16 ? 60  TYR A O   1 
ATOM   251  C  CB  . TYR A 1 33  ? 11.841  2.765   -58.163 1.00 17.26 ? 60  TYR A CB  1 
ATOM   252  C  CG  . TYR A 1 33  ? 12.712  2.530   -59.381 1.00 16.26 ? 60  TYR A CG  1 
ATOM   253  C  CD1 . TYR A 1 33  ? 13.485  3.562   -59.921 1.00 17.89 ? 60  TYR A CD1 1 
ATOM   254  C  CD2 . TYR A 1 33  ? 12.744  1.293   -60.020 1.00 15.89 ? 60  TYR A CD2 1 
ATOM   255  C  CE1 . TYR A 1 33  ? 14.276  3.367   -61.046 1.00 17.92 ? 60  TYR A CE1 1 
ATOM   256  C  CE2 . TYR A 1 33  ? 13.528  1.094   -61.136 1.00 16.34 ? 60  TYR A CE2 1 
ATOM   257  C  CZ  . TYR A 1 33  ? 14.276  2.130   -61.673 1.00 17.42 ? 60  TYR A CZ  1 
ATOM   258  O  OH  . TYR A 1 33  ? 15.084  1.933   -62.787 1.00 17.52 ? 60  TYR A OH  1 
ATOM   259  N  N   . ARG A 1 34  ? 9.121   2.847   -60.484 1.00 16.93 ? 61  ARG A N   1 
ATOM   260  C  CA  . ARG A 1 34  ? 8.130   2.112   -61.255 1.00 16.17 ? 61  ARG A CA  1 
ATOM   261  C  C   . ARG A 1 34  ? 6.926   1.748   -60.385 1.00 15.42 ? 61  ARG A C   1 
ATOM   262  O  O   . ARG A 1 34  ? 6.266   0.724   -60.590 1.00 14.58 ? 61  ARG A O   1 
ATOM   263  C  CB  . ARG A 1 34  ? 8.711   0.868   -61.927 1.00 16.59 ? 61  ARG A CB  1 
ATOM   264  C  CG  . ARG A 1 34  ? 9.925   1.116   -62.803 1.00 17.87 ? 61  ARG A CG  1 
ATOM   265  C  CD  . ARG A 1 34  ? 10.176  -0.131  -63.599 1.00 17.33 ? 61  ARG A CD  1 
ATOM   266  N  NE  . ARG A 1 34  ? 11.426  -0.042  -64.336 1.00 17.71 ? 61  ARG A NE  1 
ATOM   267  C  CZ  . ARG A 1 34  ? 11.653  0.674   -65.428 1.00 18.12 ? 61  ARG A CZ  1 
ATOM   268  N  NH1 . ARG A 1 34  ? 10.685  1.310   -66.045 1.00 18.50 ? 61  ARG A NH1 1 
ATOM   269  N  NH2 . ARG A 1 34  ? 12.869  0.722   -65.927 1.00 18.50 ? 61  ARG A NH2 1 
ATOM   270  N  N   . ALA A 1 35  ? 6.603   2.647   -59.452 1.00 16.44 ? 62  ALA A N   1 
ATOM   271  C  CA  . ALA A 1 35  ? 5.630   2.379   -58.412 1.00 15.56 ? 62  ALA A CA  1 
ATOM   272  C  C   . ALA A 1 35  ? 4.218   2.225   -58.987 1.00 14.71 ? 62  ALA A C   1 
ATOM   273  O  O   . ALA A 1 35  ? 3.378   1.555   -58.392 1.00 15.48 ? 62  ALA A O   1 
ATOM   274  C  CB  . ALA A 1 35  ? 5.694   3.500   -57.389 1.00 16.91 ? 62  ALA A CB  1 
ATOM   275  N  N   . ASP A 1 36  ? 3.955   2.842   -60.139 1.00 15.51 ? 63  ASP A N   1 
ATOM   276  C  CA  . ASP A 1 36  ? 2.623   2.775   -60.718 1.00 16.13 ? 63  ASP A CA  1 
ATOM   277  C  C   . ASP A 1 36  ? 2.579   1.876   -61.947 1.00 16.32 ? 63  ASP A C   1 
ATOM   278  O  O   . ASP A 1 36  ? 1.545   1.835   -62.605 1.00 17.78 ? 63  ASP A O   1 
ATOM   279  C  CB  . ASP A 1 36  ? 2.114   4.166   -61.062 1.00 18.30 ? 63  ASP A CB  1 
ATOM   280  C  CG  . ASP A 1 36  ? 1.923   5.051   -59.838 1.00 20.37 ? 63  ASP A CG  1 
ATOM   281  O  OD1 . ASP A 1 36  ? 1.244   4.586   -58.890 1.00 19.36 ? 63  ASP A OD1 1 
ATOM   282  O  OD2 . ASP A 1 36  ? 2.436   6.197   -59.861 1.00 20.82 ? 63  ASP A OD2 1 
ATOM   283  N  N   . GLU A 1 37  ? 3.656   1.138   -62.211 1.00 16.53 ? 64  GLU A N   1 
ATOM   284  C  CA  . GLU A 1 37  ? 3.615   0.111   -63.233 1.00 16.74 ? 64  GLU A CA  1 
ATOM   285  C  C   . GLU A 1 37  ? 2.993   -1.154  -62.658 1.00 16.44 ? 64  GLU A C   1 
ATOM   286  O  O   . GLU A 1 37  ? 3.206   -1.500  -61.497 1.00 16.47 ? 64  GLU A O   1 
ATOM   287  C  CB  . GLU A 1 37  ? 5.004   -0.239  -63.762 1.00 16.75 ? 64  GLU A CB  1 
ATOM   288  C  CG  . GLU A 1 37  ? 5.680   0.899   -64.506 1.00 17.37 ? 64  GLU A CG  1 
ATOM   289  C  CD  . GLU A 1 37  ? 6.962   0.493   -65.208 1.00 17.06 ? 64  GLU A CD  1 
ATOM   290  O  OE1 . GLU A 1 37  ? 7.175   -0.713  -65.450 1.00 18.17 ? 64  GLU A OE1 1 
ATOM   291  O  OE2 . GLU A 1 37  ? 7.782   1.402   -65.456 1.00 17.77 ? 64  GLU A OE2 1 
ATOM   292  N  N   . ARG A 1 38  ? 2.243   -1.875  -63.498 1.00 16.15 ? 65  ARG A N   1 
ATOM   293  C  CA  . ARG A 1 38  ? 1.637   -3.131  -63.098 1.00 15.75 ? 65  ARG A CA  1 
ATOM   294  C  C   . ARG A 1 38  ? 2.685   -4.241  -63.034 1.00 16.17 ? 65  ARG A C   1 
ATOM   295  O  O   . ARG A 1 38  ? 3.558   -4.400  -63.915 1.00 17.27 ? 65  ARG A O   1 
ATOM   296  C  CB  . ARG A 1 38  ? 0.494   -3.438  -64.078 1.00 15.42 ? 65  ARG A CB  1 
ATOM   297  C  CG  . ARG A 1 38  ? -0.763  -2.611  -63.858 1.00 14.64 ? 65  ARG A CG  1 
ATOM   298  C  CD  . ARG A 1 38  ? -1.821  -2.897  -64.919 1.00 15.97 ? 65  ARG A CD  1 
ATOM   299  N  NE  . ARG A 1 38  ? -3.038  -2.149  -64.613 1.00 16.38 ? 65  ARG A NE  1 
ATOM   300  C  CZ  . ARG A 1 38  ? -3.917  -2.362  -63.622 1.00 18.06 ? 65  ARG A CZ  1 
ATOM   301  N  NH1 . ARG A 1 38  ? -3.803  -3.426  -62.847 1.00 18.07 ? 65  ARG A NH1 1 
ATOM   302  N  NH2 . ARG A 1 38  ? -4.939  -1.534  -63.433 1.00 18.53 ? 65  ARG A NH2 1 
ATOM   303  N  N   . PHE A 1 39  ? 2.532   -5.055  -61.995 1.00 15.05 ? 66  PHE A N   1 
ATOM   304  C  CA  . PHE A 1 39  ? 3.282   -6.279  -61.822 1.00 15.60 ? 66  PHE A CA  1 
ATOM   305  C  C   . PHE A 1 39  ? 2.317   -7.346  -61.324 1.00 15.16 ? 66  PHE A C   1 
ATOM   306  O  O   . PHE A 1 39  ? 1.402   -7.024  -60.591 1.00 15.39 ? 66  PHE A O   1 
ATOM   307  C  CB  . PHE A 1 39  ? 4.373   -6.141  -60.759 1.00 15.34 ? 66  PHE A CB  1 
ATOM   308  C  CG  . PHE A 1 39  ? 5.564   -5.242  -61.049 1.00 16.20 ? 66  PHE A CG  1 
ATOM   309  C  CD1 . PHE A 1 39  ? 5.459   -3.853  -60.948 1.00 15.61 ? 66  PHE A CD1 1 
ATOM   310  C  CD2 . PHE A 1 39  ? 6.812   -5.797  -61.349 1.00 14.96 ? 66  PHE A CD2 1 
ATOM   311  C  CE1 . PHE A 1 39  ? 6.559   -3.062  -61.201 1.00 17.32 ? 66  PHE A CE1 1 
ATOM   312  C  CE2 . PHE A 1 39  ? 7.911   -4.983  -61.608 1.00 15.38 ? 66  PHE A CE2 1 
ATOM   313  C  CZ  . PHE A 1 39  ? 7.781   -3.630  -61.522 1.00 16.11 ? 66  PHE A CZ  1 
ATOM   314  N  N   . ALA A 1 40  ? 2.539   -8.599  -61.726 1.00 15.14 ? 67  ALA A N   1 
ATOM   315  C  CA  . ALA A 1 40  ? 1.749   -9.722  -61.275 1.00 15.34 ? 67  ALA A CA  1 
ATOM   316  C  C   . ALA A 1 40  ? 1.760   -9.802  -59.756 1.00 14.90 ? 67  ALA A C   1 
ATOM   317  O  O   . ALA A 1 40  ? 2.825   -9.792  -59.161 1.00 15.28 ? 67  ALA A O   1 
ATOM   318  C  CB  . ALA A 1 40  ? 2.328   -10.999 -61.873 1.00 15.73 ? 67  ALA A CB  1 
ATOM   319  N  N   . PHE A 1 41  ? 0.579   -9.943  -59.146 1.00 14.91 ? 68  PHE A N   1 
ATOM   320  C  CA  . PHE A 1 41  ? 0.500   -10.199 -57.715 1.00 16.27 ? 68  PHE A CA  1 
ATOM   321  C  C   . PHE A 1 41  ? 1.305   -11.437 -57.288 1.00 16.24 ? 68  PHE A C   1 
ATOM   322  O  O   . PHE A 1 41  ? 1.959   -11.449 -56.247 1.00 16.37 ? 68  PHE A O   1 
ATOM   323  C  CB  . PHE A 1 41  ? -0.930  -10.574 -57.310 1.00 17.34 ? 68  PHE A CB  1 
ATOM   324  C  CG  . PHE A 1 41  ? -1.939  -9.494  -57.006 1.00 17.12 ? 68  PHE A CG  1 
ATOM   325  C  CD1 . PHE A 1 41  ? -1.889  -8.830  -55.782 1.00 17.08 ? 68  PHE A CD1 1 
ATOM   326  C  CD2 . PHE A 1 41  ? -2.984  -9.209  -57.880 1.00 19.02 ? 68  PHE A CD2 1 
ATOM   327  C  CE1 . PHE A 1 41  ? -2.879  -7.929  -55.430 1.00 19.13 ? 68  PHE A CE1 1 
ATOM   328  C  CE2 . PHE A 1 41  ? -3.948  -8.270  -57.541 1.00 18.47 ? 68  PHE A CE2 1 
ATOM   329  C  CZ  . PHE A 1 41  ? -3.903  -7.649  -56.319 1.00 18.90 ? 68  PHE A CZ  1 
ATOM   330  N  N   . CYS A 1 42  ? 1.171   -12.516 -58.059 1.00 15.88 ? 69  CYS A N   1 
ATOM   331  C  CA  . CYS A 1 42  ? 1.520   -13.844 -57.574 1.00 16.40 ? 69  CYS A CA  1 
ATOM   332  C  C   . CYS A 1 42  ? 0.891   -13.991 -56.179 1.00 16.35 ? 69  CYS A C   1 
ATOM   333  O  O   . CYS A 1 42  ? -0.220  -13.512 -55.947 1.00 17.41 ? 69  CYS A O   1 
ATOM   334  C  CB  . CYS A 1 42  ? 3.024   -14.084 -57.700 1.00 16.25 ? 69  CYS A CB  1 
ATOM   335  S  SG  . CYS A 1 42  ? 3.607   -13.873 -59.403 1.00 17.84 ? 69  CYS A SG  1 
ATOM   336  N  N   A SER A 1 43  ? 1.588   -14.656 -55.252 0.50 16.11 ? 70  SER A N   1 
ATOM   337  N  N   B SER A 1 43  ? 1.591   -14.653 -55.251 0.50 17.58 ? 70  SER A N   1 
ATOM   338  C  CA  A SER A 1 43  ? 0.966   -15.052 -54.000 0.50 15.03 ? 70  SER A CA  1 
ATOM   339  C  CA  B SER A 1 43  ? 0.965   -15.055 -54.002 0.50 17.41 ? 70  SER A CA  1 
ATOM   340  C  C   A SER A 1 43  ? 0.816   -13.878 -53.034 0.50 15.36 ? 70  SER A C   1 
ATOM   341  C  C   B SER A 1 43  ? 0.817   -13.881 -53.034 0.50 16.64 ? 70  SER A C   1 
ATOM   342  O  O   A SER A 1 43  ? 0.242   -14.059 -51.963 0.50 15.46 ? 70  SER A O   1 
ATOM   343  O  O   B SER A 1 43  ? 0.243   -14.061 -51.964 0.50 16.62 ? 70  SER A O   1 
ATOM   344  C  CB  A SER A 1 43  ? 1.663   -16.217 -53.354 0.50 15.27 ? 70  SER A CB  1 
ATOM   345  C  CB  B SER A 1 43  ? 1.646   -16.242 -53.357 0.50 19.52 ? 70  SER A CB  1 
ATOM   346  O  OG  A SER A 1 43  ? 1.137   -17.436 -53.863 0.50 14.46 ? 70  SER A OG  1 
ATOM   347  O  OG  B SER A 1 43  ? 3.017   -16.018 -53.071 0.50 21.93 ? 70  SER A OG  1 
ATOM   348  N  N   . THR A 1 44  ? 1.242   -12.667 -53.410 1.00 14.93 ? 71  THR A N   1 
ATOM   349  C  CA  . THR A 1 44  ? 1.051   -11.520 -52.523 1.00 14.24 ? 71  THR A CA  1 
ATOM   350  C  C   . THR A 1 44  ? -0.441  -11.289 -52.256 1.00 14.71 ? 71  THR A C   1 
ATOM   351  O  O   . THR A 1 44  ? -0.783  -10.756 -51.207 1.00 17.10 ? 71  THR A O   1 
ATOM   352  C  CB  . THR A 1 44  ? 1.743   -10.241 -52.995 1.00 14.80 ? 71  THR A CB  1 
ATOM   353  O  OG1 . THR A 1 44  ? 1.132   -9.814  -54.214 1.00 14.40 ? 71  THR A OG1 1 
ATOM   354  C  CG2 . THR A 1 44  ? 3.256   -10.398 -53.033 1.00 14.98 ? 71  THR A CG2 1 
ATOM   355  N  N   . PHE A 1 45  ? -1.336  -11.707 -53.162 1.00 15.41 ? 72  PHE A N   1 
ATOM   356  C  CA  . PHE A 1 45  ? -2.760  -11.450 -52.993 1.00 16.28 ? 72  PHE A CA  1 
ATOM   357  C  C   . PHE A 1 45  ? -3.324  -12.213 -51.802 1.00 16.97 ? 72  PHE A C   1 
ATOM   358  O  O   . PHE A 1 45  ? -4.415  -11.899 -51.320 1.00 18.53 ? 72  PHE A O   1 
ATOM   359  C  CB  . PHE A 1 45  ? -3.525  -11.800 -54.273 1.00 17.86 ? 72  PHE A CB  1 
ATOM   360  C  CG  . PHE A 1 45  ? -3.931  -13.261 -54.414 1.00 17.95 ? 72  PHE A CG  1 
ATOM   361  C  CD1 . PHE A 1 45  ? -3.039  -14.206 -54.846 1.00 16.70 ? 72  PHE A CD1 1 
ATOM   362  C  CD2 . PHE A 1 45  ? -5.224  -13.665 -54.103 1.00 19.10 ? 72  PHE A CD2 1 
ATOM   363  C  CE1 . PHE A 1 45  ? -3.428  -15.536 -54.967 1.00 19.05 ? 72  PHE A CE1 1 
ATOM   364  C  CE2 . PHE A 1 45  ? -5.604  -14.986 -54.228 1.00 18.72 ? 72  PHE A CE2 1 
ATOM   365  C  CZ  . PHE A 1 45  ? -4.703  -15.917 -54.630 1.00 19.15 ? 72  PHE A CZ  1 
ATOM   366  N  N   . LYS A 1 46  ? -2.607  -13.241 -51.336 1.00 18.57 ? 73  LYS A N   1 
ATOM   367  C  CA  . LYS A 1 46  ? -3.125  -14.103 -50.280 1.00 18.95 ? 73  LYS A CA  1 
ATOM   368  C  C   . LYS A 1 46  ? -3.324  -13.339 -48.976 1.00 19.45 ? 73  LYS A C   1 
ATOM   369  O  O   . LYS A 1 46  ? -4.195  -13.715 -48.177 1.00 19.30 ? 73  LYS A O   1 
ATOM   370  C  CB  . LYS A 1 46  ? -2.265  -15.348 -50.086 1.00 18.85 ? 73  LYS A CB  1 
ATOM   371  C  CG  . LYS A 1 46  ? -2.451  -16.294 -51.262 1.00 20.61 ? 73  LYS A CG  1 
ATOM   372  C  CD  . LYS A 1 46  ? -1.427  -17.411 -51.353 1.00 21.58 ? 73  LYS A CD  1 
ATOM   373  C  CE  . LYS A 1 46  ? -1.622  -18.220 -52.596 1.00 22.73 ? 73  LYS A CE  1 
ATOM   374  N  NZ  . LYS A 1 46  ? -0.604  -19.260 -52.712 1.00 23.10 ? 73  LYS A NZ  1 
ATOM   375  N  N   . ALA A 1 47  ? -2.515  -12.294 -48.765 1.00 19.33 ? 74  ALA A N   1 
ATOM   376  C  CA  . ALA A 1 47  ? -2.647  -11.505 -47.547 1.00 20.71 ? 74  ALA A CA  1 
ATOM   377  C  C   . ALA A 1 47  ? -3.983  -10.771 -47.546 1.00 19.30 ? 74  ALA A C   1 
ATOM   378  O  O   . ALA A 1 47  ? -4.780  -10.965 -46.637 1.00 19.06 ? 74  ALA A O   1 
ATOM   379  C  CB  . ALA A 1 47  ? -1.468  -10.584 -47.355 1.00 22.83 ? 74  ALA A CB  1 
ATOM   380  N  N   . PRO A 1 48  ? -4.299  -9.890  -48.519 1.00 18.20 ? 75  PRO A N   1 
ATOM   381  C  CA  . PRO A 1 48  ? -5.627  -9.292  -48.570 1.00 17.83 ? 75  PRO A CA  1 
ATOM   382  C  C   . PRO A 1 48  ? -6.776  -10.275 -48.757 1.00 17.57 ? 75  PRO A C   1 
ATOM   383  O  O   . PRO A 1 48  ? -7.887  -9.982  -48.360 1.00 18.48 ? 75  PRO A O   1 
ATOM   384  C  CB  . PRO A 1 48  ? -5.513  -8.280  -49.713 1.00 18.16 ? 75  PRO A CB  1 
ATOM   385  C  CG  . PRO A 1 48  ? -4.333  -8.743  -50.519 1.00 17.54 ? 75  PRO A CG  1 
ATOM   386  C  CD  . PRO A 1 48  ? -3.390  -9.315  -49.527 1.00 18.14 ? 75  PRO A CD  1 
ATOM   387  N  N   . LEU A 1 49  ? -6.528  -11.442 -49.364 1.00 17.46 ? 76  LEU A N   1 
ATOM   388  C  CA  . LEU A 1 49  ? -7.561  -12.459 -49.465 1.00 18.32 ? 76  LEU A CA  1 
ATOM   389  C  C   . LEU A 1 49  ? -8.036  -12.888 -48.077 1.00 18.59 ? 76  LEU A C   1 
ATOM   390  O  O   . LEU A 1 49  ? -9.239  -12.977 -47.824 1.00 19.62 ? 76  LEU A O   1 
ATOM   391  C  CB  . LEU A 1 49  ? -7.051  -13.656 -50.264 1.00 18.03 ? 76  LEU A CB  1 
ATOM   392  C  CG  . LEU A 1 49  ? -7.996  -14.849 -50.313 1.00 18.59 ? 76  LEU A CG  1 
ATOM   393  C  CD1 . LEU A 1 49  ? -9.322  -14.499 -51.002 1.00 19.46 ? 76  LEU A CD1 1 
ATOM   394  C  CD2 . LEU A 1 49  ? -7.323  -16.037 -50.966 1.00 18.94 ? 76  LEU A CD2 1 
ATOM   395  N  N   . VAL A 1 50  ? -7.073  -13.188 -47.200 1.00 17.37 ? 77  VAL A N   1 
ATOM   396  C  CA  . VAL A 1 50  ? -7.383  -13.615 -45.846 1.00 20.06 ? 77  VAL A CA  1 
ATOM   397  C  C   . VAL A 1 50  ? -8.118  -12.490 -45.123 1.00 20.00 ? 77  VAL A C   1 
ATOM   398  O  O   . VAL A 1 50  ? -9.093  -12.747 -44.413 1.00 20.05 ? 77  VAL A O   1 
ATOM   399  C  CB  . VAL A 1 50  ? -6.118  -14.089 -45.112 1.00 19.53 ? 77  VAL A CB  1 
ATOM   400  C  CG1 . VAL A 1 50  ? -6.305  -14.210 -43.602 1.00 20.38 ? 77  VAL A CG1 1 
ATOM   401  C  CG2 . VAL A 1 50  ? -5.676  -15.409 -45.680 1.00 19.50 ? 77  VAL A CG2 1 
ATOM   402  N  N   . ALA A 1 51  ? -7.669  -11.248 -45.353 1.00 20.48 ? 78  ALA A N   1 
ATOM   403  C  CA  . ALA A 1 51  ? -8.351  -10.094 -44.791 1.00 20.92 ? 78  ALA A CA  1 
ATOM   404  C  C   . ALA A 1 51  ? -9.806  -10.045 -45.251 1.00 22.33 ? 78  ALA A C   1 
ATOM   405  O  O   . ALA A 1 51  ? -10.695 -9.737  -44.455 1.00 22.22 ? 78  ALA A O   1 
ATOM   406  C  CB  . ALA A 1 51  ? -7.628  -8.814  -45.156 1.00 20.15 ? 78  ALA A CB  1 
ATOM   407  N  N   . ALA A 1 52  ? -10.051 -10.320 -46.546 1.00 20.62 ? 79  ALA A N   1 
ATOM   408  C  CA  . ALA A 1 52  ? -11.409 -10.254 -47.062 1.00 21.64 ? 79  ALA A CA  1 
ATOM   409  C  C   . ALA A 1 52  ? -12.307 -11.270 -46.358 1.00 22.40 ? 79  ALA A C   1 
ATOM   410  O  O   . ALA A 1 52  ? -13.463 -10.985 -46.002 1.00 22.71 ? 79  ALA A O   1 
ATOM   411  C  CB  . ALA A 1 52  ? -11.404 -10.447 -48.557 1.00 19.73 ? 79  ALA A CB  1 
ATOM   412  N  N   . VAL A 1 53  ? -11.787 -12.491 -46.199 1.00 22.86 ? 80  VAL A N   1 
ATOM   413  C  CA  . VAL A 1 53  ? -12.574 -13.552 -45.583 1.00 23.01 ? 80  VAL A CA  1 
ATOM   414  C  C   . VAL A 1 53  ? -12.817 -13.228 -44.113 1.00 23.56 ? 80  VAL A C   1 
ATOM   415  O  O   . VAL A 1 53  ? -13.919 -13.447 -43.578 1.00 24.87 ? 80  VAL A O   1 
ATOM   416  C  CB  . VAL A 1 53  ? -11.831 -14.891 -45.786 1.00 22.68 ? 80  VAL A CB  1 
ATOM   417  C  CG1 . VAL A 1 53  ? -12.388 -15.998 -44.900 1.00 23.33 ? 80  VAL A CG1 1 
ATOM   418  C  CG2 . VAL A 1 53  ? -11.831 -15.308 -47.247 1.00 21.47 ? 80  VAL A CG2 1 
ATOM   419  N  N   . LEU A 1 54  ? -11.789 -12.713 -43.442 1.00 23.25 ? 81  LEU A N   1 
ATOM   420  C  CA  . LEU A 1 54  ? -11.960 -12.281 -42.062 1.00 24.99 ? 81  LEU A CA  1 
ATOM   421  C  C   . LEU A 1 54  ? -13.061 -11.228 -41.983 1.00 27.48 ? 81  LEU A C   1 
ATOM   422  O  O   . LEU A 1 54  ? -13.954 -11.323 -41.148 1.00 26.44 ? 81  LEU A O   1 
ATOM   423  C  CB  . LEU A 1 54  ? -10.647 -11.739 -41.509 1.00 24.77 ? 81  LEU A CB  1 
ATOM   424  C  CG  . LEU A 1 54  ? -9.606  -12.789 -41.120 1.00 24.20 ? 81  LEU A CG  1 
ATOM   425  C  CD1 . LEU A 1 54  ? -8.250  -12.153 -40.905 1.00 22.95 ? 81  LEU A CD1 1 
ATOM   426  C  CD2 . LEU A 1 54  ? -10.033 -13.617 -39.899 1.00 25.90 ? 81  LEU A CD2 1 
ATOM   427  N  N   . HIS A 1 55  ? -12.986 -10.222 -42.863 1.00 26.46 ? 82  HIS A N   1 
ATOM   428  C  CA  . HIS A 1 55  ? -13.865 -9.063  -42.776 1.00 28.56 ? 82  HIS A CA  1 
ATOM   429  C  C   . HIS A 1 55  ? -15.328 -9.453  -42.990 1.00 29.26 ? 82  HIS A C   1 
ATOM   430  O  O   . HIS A 1 55  ? -16.196 -8.940  -42.287 1.00 30.45 ? 82  HIS A O   1 
ATOM   431  C  CB  . HIS A 1 55  ? -13.412 -7.994  -43.788 1.00 29.00 ? 82  HIS A CB  1 
ATOM   432  C  CG  . HIS A 1 55  ? -14.351 -6.841  -43.913 1.00 32.36 ? 82  HIS A CG  1 
ATOM   433  N  ND1 . HIS A 1 55  ? -14.418 -5.808  -43.003 1.00 34.51 ? 82  HIS A ND1 1 
ATOM   434  C  CD2 . HIS A 1 55  ? -15.247 -6.568  -44.859 1.00 33.37 ? 82  HIS A CD2 1 
ATOM   435  C  CE1 . HIS A 1 55  ? -15.369 -4.961  -43.375 1.00 36.27 ? 82  HIS A CE1 1 
ATOM   436  N  NE2 . HIS A 1 55  ? -15.871 -5.393  -44.515 1.00 36.19 ? 82  HIS A NE2 1 
ATOM   437  N  N   . GLN A 1 56  ? -15.578 -10.381 -43.923 1.00 30.11 ? 83  GLN A N   1 
ATOM   438  C  CA  . GLN A 1 56  ? -16.909 -10.684 -44.438 1.00 34.33 ? 83  GLN A CA  1 
ATOM   439  C  C   . GLN A 1 56  ? -17.701 -11.549 -43.445 1.00 34.79 ? 83  GLN A C   1 
ATOM   440  O  O   . GLN A 1 56  ? -18.917 -11.670 -43.584 1.00 36.63 ? 83  GLN A O   1 
ATOM   441  C  CB  . GLN A 1 56  ? -16.746 -11.391 -45.794 1.00 37.54 ? 83  GLN A CB  1 
ATOM   442  C  CG  . GLN A 1 56  ? -18.034 -11.792 -46.517 1.00 44.13 ? 83  GLN A CG  1 
ATOM   443  C  CD  . GLN A 1 56  ? -17.845 -12.713 -47.711 1.00 46.58 ? 83  GLN A CD  1 
ATOM   444  O  OE1 . GLN A 1 56  ? -17.549 -13.911 -47.588 1.00 54.48 ? 83  GLN A OE1 1 
ATOM   445  N  NE2 . GLN A 1 56  ? -18.080 -12.180 -48.901 1.00 50.87 ? 83  GLN A NE2 1 
ATOM   446  N  N   . ASN A 1 57  ? -17.024 -12.158 -42.464 1.00 32.81 ? 86  ASN A N   1 
ATOM   447  C  CA  . ASN A 1 57  ? -17.658 -13.176 -41.633 1.00 33.96 ? 86  ASN A CA  1 
ATOM   448  C  C   . ASN A 1 57  ? -17.371 -12.985 -40.151 1.00 33.92 ? 86  ASN A C   1 
ATOM   449  O  O   . ASN A 1 57  ? -16.345 -12.436 -39.759 1.00 31.73 ? 86  ASN A O   1 
ATOM   450  C  CB  . ASN A 1 57  ? -17.159 -14.572 -41.997 1.00 33.50 ? 86  ASN A CB  1 
ATOM   451  C  CG  . ASN A 1 57  ? -17.405 -14.927 -43.437 1.00 32.48 ? 86  ASN A CG  1 
ATOM   452  O  OD1 . ASN A 1 57  ? -18.498 -15.387 -43.778 1.00 34.62 ? 86  ASN A OD1 1 
ATOM   453  N  ND2 . ASN A 1 57  ? -16.390 -14.795 -44.277 1.00 31.89 ? 86  ASN A ND2 1 
ATOM   454  N  N   . PRO A 1 58  ? -18.234 -13.521 -39.253 1.00 34.25 ? 87  PRO A N   1 
ATOM   455  C  CA  . PRO A 1 58  ? -17.903 -13.558 -37.835 1.00 35.41 ? 87  PRO A CA  1 
ATOM   456  C  C   . PRO A 1 58  ? -16.730 -14.496 -37.565 1.00 33.91 ? 87  PRO A C   1 
ATOM   457  O  O   . PRO A 1 58  ? -16.380 -15.337 -38.392 1.00 31.95 ? 87  PRO A O   1 
ATOM   458  C  CB  . PRO A 1 58  ? -19.206 -13.976 -37.142 1.00 37.44 ? 87  PRO A CB  1 
ATOM   459  C  CG  . PRO A 1 58  ? -20.050 -14.585 -38.239 1.00 37.54 ? 87  PRO A CG  1 
ATOM   460  C  CD  . PRO A 1 58  ? -19.578 -14.035 -39.561 1.00 36.92 ? 87  PRO A CD  1 
ATOM   461  N  N   . LEU A 1 59  ? -16.094 -14.280 -36.424 1.00 34.89 ? 88  LEU A N   1 
ATOM   462  C  CA  . LEU A 1 59  ? -14.978 -15.088 -35.961 1.00 36.35 ? 88  LEU A CA  1 
ATOM   463  C  C   . LEU A 1 59  ? -15.284 -16.591 -35.955 1.00 36.12 ? 88  LEU A C   1 
ATOM   464  O  O   . LEU A 1 59  ? -14.375 -17.380 -36.204 1.00 37.24 ? 88  LEU A O   1 
ATOM   465  C  CB  . LEU A 1 59  ? -14.592 -14.617 -34.563 1.00 39.77 ? 88  LEU A CB  1 
ATOM   466  C  CG  . LEU A 1 59  ? -13.665 -13.408 -34.458 1.00 42.56 ? 88  LEU A CG  1 
ATOM   467  C  CD1 . LEU A 1 59  ? -13.391 -13.184 -32.984 1.00 43.74 ? 88  LEU A CD1 1 
ATOM   468  C  CD2 . LEU A 1 59  ? -12.364 -13.551 -35.241 1.00 41.87 ? 88  LEU A CD2 1 
ATOM   469  N  N   . THR A 1 60  ? -16.525 -16.997 -35.640 1.00 35.35 ? 89  THR A N   1 
ATOM   470  C  CA  . THR A 1 60  ? -16.901 -18.410 -35.591 1.00 35.40 ? 89  THR A CA  1 
ATOM   471  C  C   . THR A 1 60  ? -16.827 -19.062 -36.982 1.00 34.79 ? 89  THR A C   1 
ATOM   472  O  O   . THR A 1 60  ? -16.780 -20.289 -37.090 1.00 33.36 ? 89  THR A O   1 
ATOM   473  C  CB  . THR A 1 60  ? -18.313 -18.545 -35.016 1.00 38.05 ? 89  THR A CB  1 
ATOM   474  O  OG1 . THR A 1 60  ? -19.093 -17.674 -35.827 1.00 39.30 ? 89  THR A OG1 1 
ATOM   475  C  CG2 . THR A 1 60  ? -18.404 -18.151 -33.552 1.00 39.37 ? 89  THR A CG2 1 
ATOM   476  N  N   . HIS A 1 61  ? -16.819 -18.248 -38.046 1.00 33.08 ? 90  HIS A N   1 
ATOM   477  C  CA  . HIS A 1 61  ? -16.708 -18.748 -39.411 1.00 32.21 ? 90  HIS A CA  1 
ATOM   478  C  C   . HIS A 1 61  ? -15.340 -19.383 -39.671 1.00 29.72 ? 90  HIS A C   1 
ATOM   479  O  O   . HIS A 1 61  ? -15.189 -20.184 -40.588 1.00 30.01 ? 90  HIS A O   1 
ATOM   480  C  CB  . HIS A 1 61  ? -16.941 -17.619 -40.426 1.00 33.27 ? 90  HIS A CB  1 
ATOM   481  C  CG  . HIS A 1 61  ? -16.957 -18.033 -41.870 1.00 31.46 ? 90  HIS A CG  1 
ATOM   482  N  ND1 . HIS A 1 61  ? -17.990 -18.725 -42.461 1.00 31.86 ? 90  HIS A ND1 1 
ATOM   483  C  CD2 . HIS A 1 61  ? -16.069 -17.812 -42.839 1.00 30.75 ? 90  HIS A CD2 1 
ATOM   484  C  CE1 . HIS A 1 61  ? -17.713 -18.903 -43.746 1.00 32.82 ? 90  HIS A CE1 1 
ATOM   485  N  NE2 . HIS A 1 61  ? -16.544 -18.366 -43.995 1.00 32.20 ? 90  HIS A NE2 1 
ATOM   486  N  N   . LEU A 1 62  ? -14.328 -19.020 -38.881 1.00 28.98 ? 91  LEU A N   1 
ATOM   487  C  CA  . LEU A 1 62  ? -13.026 -19.641 -39.001 1.00 28.12 ? 91  LEU A CA  1 
ATOM   488  C  C   . LEU A 1 62  ? -13.093 -21.140 -38.684 1.00 27.90 ? 91  LEU A C   1 
ATOM   489  O  O   . LEU A 1 62  ? -12.179 -21.871 -39.065 1.00 26.73 ? 91  LEU A O   1 
ATOM   490  C  CB  . LEU A 1 62  ? -12.041 -18.924 -38.087 1.00 28.90 ? 91  LEU A CB  1 
ATOM   491  C  CG  . LEU A 1 62  ? -11.759 -17.455 -38.414 1.00 30.13 ? 91  LEU A CG  1 
ATOM   492  C  CD1 . LEU A 1 62  ? -10.847 -16.870 -37.336 1.00 31.68 ? 91  LEU A CD1 1 
ATOM   493  C  CD2 . LEU A 1 62  ? -11.134 -17.297 -39.773 1.00 29.27 ? 91  LEU A CD2 1 
ATOM   494  N  N   . ASP A 1 63  ? -14.153 -21.591 -38.004 1.00 28.57 ? 92  ASP A N   1 
ATOM   495  C  CA  . ASP A 1 63  ? -14.309 -23.000 -37.642 1.00 29.75 ? 92  ASP A CA  1 
ATOM   496  C  C   . ASP A 1 63  ? -15.178 -23.782 -38.633 1.00 29.69 ? 92  ASP A C   1 
ATOM   497  O  O   . ASP A 1 63  ? -15.419 -24.967 -38.432 1.00 29.37 ? 92  ASP A O   1 
ATOM   498  C  CB  . ASP A 1 63  ? -14.698 -23.140 -36.171 1.00 31.44 ? 92  ASP A CB  1 
ATOM   499  C  CG  . ASP A 1 63  ? -13.582 -22.619 -35.271 1.00 32.86 ? 92  ASP A CG  1 
ATOM   500  O  OD1 . ASP A 1 63  ? -12.415 -23.030 -35.496 1.00 30.46 ? 92  ASP A OD1 1 
ATOM   501  O  OD2 . ASP A 1 63  ? -13.848 -21.721 -34.430 1.00 34.37 ? 92  ASP A OD2 1 
ATOM   502  N  N   . LYS A 1 64  ? -15.625 -23.140 -39.716 1.00 29.59 ? 93  LYS A N   1 
ATOM   503  C  CA  . LYS A 1 64  ? -16.420 -23.812 -40.728 1.00 30.89 ? 93  LYS A CA  1 
ATOM   504  C  C   . LYS A 1 64  ? -15.541 -24.763 -41.534 1.00 29.39 ? 93  LYS A C   1 
ATOM   505  O  O   . LYS A 1 64  ? -14.501 -24.350 -42.044 1.00 26.70 ? 93  LYS A O   1 
ATOM   506  C  CB  . LYS A 1 64  ? -17.022 -22.766 -41.677 1.00 33.05 ? 93  LYS A CB  1 
ATOM   507  C  CG  . LYS A 1 64  ? -17.952 -23.344 -42.718 1.00 36.09 ? 93  LYS A CG  1 
ATOM   508  C  CD  . LYS A 1 64  ? -18.337 -22.289 -43.737 1.00 39.01 ? 93  LYS A CD  1 
ATOM   509  C  CE  . LYS A 1 64  ? -18.905 -22.866 -44.992 1.00 41.48 ? 93  LYS A CE  1 
ATOM   510  N  NZ  . LYS A 1 64  ? -19.974 -23.806 -44.664 1.00 45.14 ? 93  LYS A NZ  1 
ATOM   511  N  N   . LEU A 1 65  ? -15.985 -26.029 -41.651 1.00 30.85 ? 94  LEU A N   1 
ATOM   512  C  CA  . LEU A 1 65  ? -15.214 -27.032 -42.372 1.00 30.81 ? 94  LEU A CA  1 
ATOM   513  C  C   . LEU A 1 65  ? -15.465 -26.940 -43.879 1.00 31.13 ? 94  LEU A C   1 
ATOM   514  O  O   . LEU A 1 65  ? -16.626 -26.929 -44.282 1.00 31.69 ? 94  LEU A O   1 
ATOM   515  C  CB  . LEU A 1 65  ? -15.573 -28.415 -41.833 1.00 31.77 ? 94  LEU A CB  1 
ATOM   516  C  CG  . LEU A 1 65  ? -14.680 -29.544 -42.359 1.00 32.44 ? 94  LEU A CG  1 
ATOM   517  C  CD1 . LEU A 1 65  ? -13.212 -29.390 -41.894 1.00 31.33 ? 94  LEU A CD1 1 
ATOM   518  C  CD2 . LEU A 1 65  ? -15.262 -30.892 -41.970 1.00 34.58 ? 94  LEU A CD2 1 
ATOM   519  N  N   . ILE A 1 66  ? -14.380 -26.926 -44.679 1.00 29.80 ? 95  ILE A N   1 
ATOM   520  C  CA  . ILE A 1 66  ? -14.465 -26.946 -46.134 1.00 30.47 ? 95  ILE A CA  1 
ATOM   521  C  C   . ILE A 1 66  ? -13.910 -28.273 -46.647 1.00 31.62 ? 95  ILE A C   1 
ATOM   522  O  O   . ILE A 1 66  ? -12.751 -28.578 -46.400 1.00 30.99 ? 95  ILE A O   1 
ATOM   523  C  CB  . ILE A 1 66  ? -13.681 -25.764 -46.748 1.00 30.04 ? 95  ILE A CB  1 
ATOM   524  C  CG1 . ILE A 1 66  ? -14.069 -24.411 -46.163 1.00 30.54 ? 95  ILE A CG1 1 
ATOM   525  C  CG2 . ILE A 1 66  ? -13.807 -25.760 -48.279 1.00 30.36 ? 95  ILE A CG2 1 
ATOM   526  C  CD1 . ILE A 1 66  ? -15.551 -24.074 -46.291 1.00 32.49 ? 95  ILE A CD1 1 
ATOM   527  N  N   A THR A 1 67  ? -14.711 -29.056 -47.381 0.50 33.76 ? 96  THR A N   1 
ATOM   528  N  N   B THR A 1 67  ? -14.725 -29.034 -47.393 0.50 32.89 ? 96  THR A N   1 
ATOM   529  C  CA  A THR A 1 67  ? -14.198 -30.291 -47.963 0.50 35.46 ? 96  THR A CA  1 
ATOM   530  C  CA  B THR A 1 67  ? -14.280 -30.280 -48.002 0.50 33.92 ? 96  THR A CA  1 
ATOM   531  C  C   A THR A 1 67  ? -13.901 -30.052 -49.446 0.50 35.18 ? 96  THR A C   1 
ATOM   532  C  C   B THR A 1 67  ? -13.899 -30.031 -49.463 0.50 34.25 ? 96  THR A C   1 
ATOM   533  O  O   A THR A 1 67  ? -14.403 -29.118 -50.057 0.50 34.29 ? 96  THR A O   1 
ATOM   534  O  O   B THR A 1 67  ? -14.378 -29.091 -50.083 0.50 33.53 ? 96  THR A O   1 
ATOM   535  C  CB  A THR A 1 67  ? -15.155 -31.462 -47.718 0.50 38.00 ? 96  THR A CB  1 
ATOM   536  C  CB  B THR A 1 67  ? -15.374 -31.343 -47.882 0.50 35.16 ? 96  THR A CB  1 
ATOM   537  O  OG1 A THR A 1 67  ? -15.533 -31.347 -46.349 0.50 39.55 ? 96  THR A OG1 1 
ATOM   538  O  OG1 B THR A 1 67  ? -16.596 -30.731 -48.293 0.50 34.53 ? 96  THR A OG1 1 
ATOM   539  C  CG2 A THR A 1 67  ? -14.481 -32.810 -47.900 0.50 39.06 ? 96  THR A CG2 1 
ATOM   540  C  CG2 B THR A 1 67  ? -15.490 -31.874 -46.465 0.50 36.08 ? 96  THR A CG2 1 
ATOM   541  N  N   . TYR A 1 68  ? -13.028 -30.895 -49.998 1.00 36.18 ? 97  TYR A N   1 
ATOM   542  C  CA  . TYR A 1 68  ? -12.539 -30.786 -51.367 1.00 36.78 ? 97  TYR A CA  1 
ATOM   543  C  C   . TYR A 1 68  ? -11.940 -32.142 -51.728 1.00 39.85 ? 97  TYR A C   1 
ATOM   544  O  O   . TYR A 1 68  ? -11.955 -33.028 -50.874 1.00 39.75 ? 97  TYR A O   1 
ATOM   545  C  CB  . TYR A 1 68  ? -11.536 -29.636 -51.445 1.00 33.56 ? 97  TYR A CB  1 
ATOM   546  C  CG  . TYR A 1 68  ? -10.355 -29.750 -50.491 1.00 31.91 ? 97  TYR A CG  1 
ATOM   547  C  CD1 . TYR A 1 68  ? -10.437 -29.296 -49.176 1.00 31.45 ? 97  TYR A CD1 1 
ATOM   548  C  CD2 . TYR A 1 68  ? -9.150  -30.298 -50.901 1.00 32.06 ? 97  TYR A CD2 1 
ATOM   549  C  CE1 . TYR A 1 68  ? -9.362  -29.401 -48.303 1.00 29.99 ? 97  TYR A CE1 1 
ATOM   550  C  CE2 . TYR A 1 68  ? -8.072  -30.420 -50.038 1.00 31.07 ? 97  TYR A CE2 1 
ATOM   551  C  CZ  . TYR A 1 68  ? -8.181  -29.968 -48.733 1.00 29.80 ? 97  TYR A CZ  1 
ATOM   552  O  OH  . TYR A 1 68  ? -7.115  -30.089 -47.905 1.00 28.55 ? 97  TYR A OH  1 
ATOM   553  N  N   . THR A 1 69  ? -11.446 -32.321 -52.974 1.00 41.07 ? 98  THR A N   1 
ATOM   554  C  CA  . THR A 1 69  ? -10.849 -33.591 -53.384 1.00 42.73 ? 98  THR A CA  1 
ATOM   555  C  C   . THR A 1 69  ? -9.499  -33.359 -54.057 1.00 39.02 ? 98  THR A C   1 
ATOM   556  O  O   . THR A 1 69  ? -9.114  -32.219 -54.273 1.00 34.83 ? 98  THR A O   1 
ATOM   557  C  CB  . THR A 1 69  ? -11.811 -34.380 -54.277 1.00 48.37 ? 98  THR A CB  1 
ATOM   558  O  OG1 . THR A 1 69  ? -11.367 -35.736 -54.191 1.00 50.40 ? 98  THR A OG1 1 
ATOM   559  C  CG2 . THR A 1 69  ? -11.948 -33.798 -55.675 1.00 48.91 ? 98  THR A CG2 1 
ATOM   560  N  N   . SER A 1 70  ? -8.749  -34.435 -54.326 1.00 39.11 ? 99  SER A N   1 
ATOM   561  C  CA  . SER A 1 70  ? -7.409  -34.256 -54.865 1.00 39.70 ? 99  SER A CA  1 
ATOM   562  C  C   . SER A 1 70  ? -7.490  -33.626 -56.260 1.00 37.93 ? 99  SER A C   1 
ATOM   563  O  O   . SER A 1 70  ? -6.540  -32.992 -56.681 1.00 36.28 ? 99  SER A O   1 
ATOM   564  C  CB  . SER A 1 70  ? -6.582  -35.521 -54.815 1.00 39.63 ? 99  SER A CB  1 
ATOM   565  O  OG  . SER A 1 70  ? -6.967  -36.477 -55.788 1.00 42.98 ? 99  SER A OG  1 
ATOM   566  N  N   . ASP A 1 71  ? -8.649  -33.721 -56.925 1.00 38.58 ? 100 ASP A N   1 
ATOM   567  C  CA  . ASP A 1 71  ? -8.834  -33.087 -58.226 1.00 39.72 ? 100 ASP A CA  1 
ATOM   568  C  C   . ASP A 1 71  ? -8.858  -31.567 -58.093 1.00 37.04 ? 100 ASP A C   1 
ATOM   569  O  O   . ASP A 1 71  ? -8.711  -30.864 -59.098 1.00 34.26 ? 100 ASP A O   1 
ATOM   570  C  CB  . ASP A 1 71  ? -10.090 -33.559 -58.943 1.00 41.75 ? 100 ASP A CB  1 
ATOM   571  C  CG  . ASP A 1 71  ? -10.032 -35.000 -59.418 1.00 47.60 ? 100 ASP A CG  1 
ATOM   572  O  OD1 . ASP A 1 71  ? -8.933  -35.379 -59.888 1.00 51.41 ? 100 ASP A OD1 1 
ATOM   573  O  OD2 . ASP A 1 71  ? -11.071 -35.707 -59.319 1.00 51.32 ? 100 ASP A OD2 1 
ATOM   574  N  N   . ASP A 1 72  ? -9.059  -31.065 -56.863 1.00 35.20 ? 101 ASP A N   1 
ATOM   575  C  CA  . ASP A 1 72  ? -9.095  -29.632 -56.618 1.00 33.08 ? 101 ASP A CA  1 
ATOM   576  C  C   . ASP A 1 72  ? -7.687  -29.082 -56.435 1.00 30.08 ? 101 ASP A C   1 
ATOM   577  O  O   . ASP A 1 72  ? -7.519  -27.873 -56.409 1.00 29.04 ? 101 ASP A O   1 
ATOM   578  C  CB  . ASP A 1 72  ? -9.904  -29.301 -55.369 1.00 35.83 ? 101 ASP A CB  1 
ATOM   579  C  CG  . ASP A 1 72  ? -11.400 -29.531 -55.494 1.00 38.02 ? 101 ASP A CG  1 
ATOM   580  O  OD1 . ASP A 1 72  ? -11.998 -28.906 -56.381 1.00 40.29 ? 101 ASP A OD1 1 
ATOM   581  O  OD2 . ASP A 1 72  ? -11.944 -30.349 -54.725 1.00 42.29 ? 101 ASP A OD2 1 
ATOM   582  N  N   . ILE A 1 73  ? -6.692  -29.957 -56.246 1.00 29.66 ? 102 ILE A N   1 
ATOM   583  C  CA  . ILE A 1 73  ? -5.319  -29.513 -56.060 1.00 27.02 ? 102 ILE A CA  1 
ATOM   584  C  C   . ILE A 1 73  ? -4.663  -29.429 -57.437 1.00 26.71 ? 102 ILE A C   1 
ATOM   585  O  O   . ILE A 1 73  ? -4.381  -30.463 -58.042 1.00 26.33 ? 102 ILE A O   1 
ATOM   586  C  CB  . ILE A 1 73  ? -4.555  -30.448 -55.118 1.00 28.00 ? 102 ILE A CB  1 
ATOM   587  C  CG1 . ILE A 1 73  ? -5.252  -30.561 -53.754 1.00 30.09 ? 102 ILE A CG1 1 
ATOM   588  C  CG2 . ILE A 1 73  ? -3.092  -30.020 -54.957 1.00 27.15 ? 102 ILE A CG2 1 
ATOM   589  C  CD1 . ILE A 1 73  ? -4.628  -31.619 -52.860 1.00 32.68 ? 102 ILE A CD1 1 
ATOM   590  N  N   . ARG A 1 74  ? -4.484  -28.193 -57.923 1.00 25.26 ? 103 ARG A N   1 
ATOM   591  C  CA  . ARG A 1 74  ? -3.948  -27.933 -59.250 1.00 25.09 ? 103 ARG A CA  1 
ATOM   592  C  C   . ARG A 1 74  ? -2.774  -26.977 -59.158 1.00 24.63 ? 103 ARG A C   1 
ATOM   593  O  O   . ARG A 1 74  ? -2.391  -26.396 -60.167 1.00 23.36 ? 103 ARG A O   1 
ATOM   594  C  CB  . ARG A 1 74  ? -5.032  -27.337 -60.161 1.00 25.84 ? 103 ARG A CB  1 
ATOM   595  C  CG  . ARG A 1 74  ? -6.242  -28.254 -60.210 1.00 27.99 ? 103 ARG A CG  1 
ATOM   596  C  CD  . ARG A 1 74  ? -7.332  -27.796 -61.140 1.00 28.78 ? 103 ARG A CD  1 
ATOM   597  N  NE  . ARG A 1 74  ? -8.505  -28.671 -61.077 1.00 28.57 ? 103 ARG A NE  1 
ATOM   598  C  CZ  . ARG A 1 74  ? -9.603  -28.482 -61.808 1.00 30.10 ? 103 ARG A CZ  1 
ATOM   599  N  NH1 . ARG A 1 74  ? -9.623  -27.586 -62.782 1.00 30.31 ? 103 ARG A NH1 1 
ATOM   600  N  NH2 . ARG A 1 74  ? -10.694 -29.190 -61.596 1.00 32.30 ? 103 ARG A NH2 1 
ATOM   601  N  N   . SER A 1 75  ? -2.264  -26.763 -57.935 1.00 23.61 ? 104 SER A N   1 
ATOM   602  C  CA  . SER A 1 75  ? -1.188  -25.828 -57.655 1.00 23.75 ? 104 SER A CA  1 
ATOM   603  C  C   . SER A 1 75  ? -0.449  -26.348 -56.434 1.00 24.79 ? 104 SER A C   1 
ATOM   604  O  O   . SER A 1 75  ? -1.006  -27.159 -55.710 1.00 24.83 ? 104 SER A O   1 
ATOM   605  C  CB  . SER A 1 75  ? -1.702  -24.428 -57.386 1.00 22.91 ? 104 SER A CB  1 
ATOM   606  O  OG  . SER A 1 75  ? -2.588  -24.427 -56.266 1.00 22.19 ? 104 SER A OG  1 
ATOM   607  N  N   . ARG A 1 76  ? 0.774   -25.854 -56.233 1.00 27.51 ? 105 ARG A N   1 
ATOM   608  C  CA  . ARG A 1 76  ? 1.607   -26.180 -55.085 1.00 28.85 ? 105 ARG A CA  1 
ATOM   609  C  C   . ARG A 1 76  ? 0.829   -25.891 -53.802 1.00 25.68 ? 105 ARG A C   1 
ATOM   610  O  O   . ARG A 1 76  ? 0.519   -24.735 -53.515 1.00 22.90 ? 105 ARG A O   1 
ATOM   611  C  CB  . ARG A 1 76  ? 2.891   -25.338 -55.193 1.00 32.79 ? 105 ARG A CB  1 
ATOM   612  C  CG  . ARG A 1 76  ? 3.894   -25.466 -54.051 1.00 34.67 ? 105 ARG A CG  1 
ATOM   613  C  CD  . ARG A 1 76  ? 4.337   -26.882 -53.859 1.00 37.79 ? 105 ARG A CD  1 
ATOM   614  N  NE  . ARG A 1 76  ? 5.127   -27.313 -55.018 1.00 42.60 ? 105 ARG A NE  1 
ATOM   615  C  CZ  . ARG A 1 76  ? 5.586   -28.540 -55.236 1.00 41.66 ? 105 ARG A CZ  1 
ATOM   616  N  NH1 . ARG A 1 76  ? 5.480   -29.466 -54.295 1.00 42.23 ? 105 ARG A NH1 1 
ATOM   617  N  NH2 . ARG A 1 76  ? 6.154   -28.812 -56.399 1.00 39.73 ? 105 ARG A NH2 1 
ATOM   618  N  N   . SER A 1 77  ? 0.533   -26.959 -53.040 1.00 23.98 ? 106 SER A N   1 
ATOM   619  C  CA  . SER A 1 77  ? -0.401  -26.888 -51.922 1.00 23.37 ? 106 SER A CA  1 
ATOM   620  C  C   . SER A 1 77  ? 0.109   -27.762 -50.780 1.00 23.21 ? 106 SER A C   1 
ATOM   621  O  O   . SER A 1 77  ? -0.406  -28.852 -50.554 1.00 22.37 ? 106 SER A O   1 
ATOM   622  C  CB  . SER A 1 77  ? -1.784  -27.311 -52.379 1.00 23.47 ? 106 SER A CB  1 
ATOM   623  O  OG  . SER A 1 77  ? -2.206  -26.515 -53.480 1.00 21.81 ? 106 SER A OG  1 
ATOM   624  N  N   . PRO A 1 78  ? 1.163   -27.333 -50.044 1.00 24.35 ? 107 PRO A N   1 
ATOM   625  C  CA  . PRO A 1 78  ? 1.822   -28.213 -49.066 1.00 26.03 ? 107 PRO A CA  1 
ATOM   626  C  C   . PRO A 1 78  ? 0.933   -28.653 -47.902 1.00 25.90 ? 107 PRO A C   1 
ATOM   627  O  O   . PRO A 1 78  ? 1.118   -29.730 -47.347 1.00 29.32 ? 107 PRO A O   1 
ATOM   628  C  CB  . PRO A 1 78  ? 3.023   -27.380 -48.582 1.00 26.23 ? 107 PRO A CB  1 
ATOM   629  C  CG  . PRO A 1 78  ? 3.228   -26.344 -49.665 1.00 26.17 ? 107 PRO A CG  1 
ATOM   630  C  CD  . PRO A 1 78  ? 1.818   -26.031 -50.153 1.00 25.00 ? 107 PRO A CD  1 
ATOM   631  N  N   . VAL A 1 79  ? -0.062  -27.838 -47.547 1.00 24.54 ? 108 VAL A N   1 
ATOM   632  C  CA  . VAL A 1 79  ? -0.969  -28.191 -46.466 1.00 25.08 ? 108 VAL A CA  1 
ATOM   633  C  C   . VAL A 1 79  ? -2.196  -28.932 -47.014 1.00 25.17 ? 108 VAL A C   1 
ATOM   634  O  O   . VAL A 1 79  ? -2.549  -30.023 -46.533 1.00 25.71 ? 108 VAL A O   1 
ATOM   635  C  CB  . VAL A 1 79  ? -1.352  -26.949 -45.644 1.00 23.73 ? 108 VAL A CB  1 
ATOM   636  C  CG1 . VAL A 1 79  ? -2.292  -27.300 -44.501 1.00 24.50 ? 108 VAL A CG1 1 
ATOM   637  C  CG2 . VAL A 1 79  ? -0.109  -26.239 -45.116 1.00 25.10 ? 108 VAL A CG2 1 
ATOM   638  N  N   . ALA A 1 80  ? -2.832  -28.348 -48.038 1.00 25.19 ? 109 ALA A N   1 
ATOM   639  C  CA  . ALA A 1 80  ? -4.117  -28.855 -48.502 1.00 28.01 ? 109 ALA A CA  1 
ATOM   640  C  C   . ALA A 1 80  ? -3.977  -30.298 -48.987 1.00 30.46 ? 109 ALA A C   1 
ATOM   641  O  O   . ALA A 1 80  ? -4.914  -31.065 -48.846 1.00 31.36 ? 109 ALA A O   1 
ATOM   642  C  CB  . ALA A 1 80  ? -4.690  -27.954 -49.575 1.00 27.94 ? 109 ALA A CB  1 
ATOM   643  N  N   . GLN A 1 81  ? -2.789  -30.642 -49.524 1.00 32.24 ? 110 GLN A N   1 
ATOM   644  C  CA  . GLN A 1 81  ? -2.429  -32.003 -49.934 1.00 36.89 ? 110 GLN A CA  1 
ATOM   645  C  C   . GLN A 1 81  ? -2.782  -33.013 -48.844 1.00 38.61 ? 110 GLN A C   1 
ATOM   646  O  O   . GLN A 1 81  ? -3.282  -34.108 -49.118 1.00 39.61 ? 110 GLN A O   1 
ATOM   647  C  CB  . GLN A 1 81  ? -0.909  -32.078 -50.107 1.00 39.57 ? 110 GLN A CB  1 
ATOM   648  C  CG  . GLN A 1 81  ? -0.424  -33.201 -51.016 1.00 46.31 ? 110 GLN A CG  1 
ATOM   649  C  CD  . GLN A 1 81  ? -0.748  -32.936 -52.473 1.00 46.98 ? 110 GLN A CD  1 
ATOM   650  O  OE1 . GLN A 1 81  ? -0.156  -32.073 -53.142 1.00 55.36 ? 110 GLN A OE1 1 
ATOM   651  N  NE2 . GLN A 1 81  ? -1.737  -33.653 -52.975 1.00 48.62 ? 110 GLN A NE2 1 
ATOM   652  N  N   . GLN A 1 82  ? -2.485  -32.643 -47.598 1.00 35.79 ? 111 GLN A N   1 
ATOM   653  C  CA  . GLN A 1 82  ? -2.552  -33.576 -46.492 1.00 37.90 ? 111 GLN A CA  1 
ATOM   654  C  C   . GLN A 1 82  ? -3.953  -33.681 -45.893 1.00 34.74 ? 111 GLN A C   1 
ATOM   655  O  O   . GLN A 1 82  ? -4.135  -34.390 -44.914 1.00 33.74 ? 111 GLN A O   1 
ATOM   656  C  CB  . GLN A 1 82  ? -1.462  -33.209 -45.487 1.00 41.55 ? 111 GLN A CB  1 
ATOM   657  C  CG  . GLN A 1 82  ? -0.079  -33.727 -45.894 1.00 47.51 ? 111 GLN A CG  1 
ATOM   658  C  CD  . GLN A 1 82  ? 0.849   -32.636 -46.380 1.00 53.01 ? 111 GLN A CD  1 
ATOM   659  O  OE1 . GLN A 1 82  ? 1.362   -32.643 -47.511 1.00 49.18 ? 111 GLN A OE1 1 
ATOM   660  N  NE2 . GLN A 1 82  ? 1.060   -31.658 -45.506 1.00 57.78 ? 111 GLN A NE2 1 
ATOM   661  N  N   . HIS A 1 83  ? -4.947  -32.965 -46.425 1.00 32.38 ? 112 HIS A N   1 
ATOM   662  C  CA  . HIS A 1 83  ? -6.231  -32.870 -45.743 1.00 32.86 ? 112 HIS A CA  1 
ATOM   663  C  C   . HIS A 1 83  ? -7.404  -33.129 -46.678 1.00 33.64 ? 112 HIS A C   1 
ATOM   664  O  O   . HIS A 1 83  ? -8.539  -32.811 -46.336 1.00 33.12 ? 112 HIS A O   1 
ATOM   665  C  CB  . HIS A 1 83  ? -6.360  -31.517 -45.022 1.00 31.59 ? 112 HIS A CB  1 
ATOM   666  C  CG  . HIS A 1 83  ? -5.446  -31.475 -43.851 1.00 32.18 ? 112 HIS A CG  1 
ATOM   667  N  ND1 . HIS A 1 83  ? -4.314  -30.699 -43.803 1.00 33.54 ? 112 HIS A ND1 1 
ATOM   668  C  CD2 . HIS A 1 83  ? -5.491  -32.155 -42.707 1.00 34.21 ? 112 HIS A CD2 1 
ATOM   669  C  CE1 . HIS A 1 83  ? -3.706  -30.896 -42.638 1.00 32.98 ? 112 HIS A CE1 1 
ATOM   670  N  NE2 . HIS A 1 83  ? -4.404  -31.782 -41.963 1.00 35.07 ? 112 HIS A NE2 1 
ATOM   671  N  N   . VAL A 1 84  ? -7.150  -33.791 -47.808 1.00 34.80 ? 113 VAL A N   1 
ATOM   672  C  CA  . VAL A 1 84  ? -8.221  -34.071 -48.748 1.00 38.17 ? 113 VAL A CA  1 
ATOM   673  C  C   . VAL A 1 84  ? -9.378  -34.814 -48.067 1.00 39.53 ? 113 VAL A C   1 
ATOM   674  O  O   . VAL A 1 84  ? -10.554 -34.545 -48.307 1.00 39.31 ? 113 VAL A O   1 
ATOM   675  C  CB  . VAL A 1 84  ? -7.680  -34.876 -49.953 1.00 42.12 ? 113 VAL A CB  1 
ATOM   676  C  CG1 . VAL A 1 84  ? -8.814  -35.308 -50.878 1.00 43.33 ? 113 VAL A CG1 1 
ATOM   677  C  CG2 . VAL A 1 84  ? -6.622  -34.093 -50.734 1.00 39.54 ? 113 VAL A CG2 1 
ATOM   678  N  N   . GLN A 1 85  ? -9.072  -35.778 -47.205 1.00 42.09 ? 114 GLN A N   1 
ATOM   679  C  CA  . GLN A 1 85  ? -10.153 -36.611 -46.700 1.00 47.22 ? 114 GLN A CA  1 
ATOM   680  C  C   . GLN A 1 85  ? -10.953 -35.918 -45.595 1.00 45.58 ? 114 GLN A C   1 
ATOM   681  O  O   . GLN A 1 85  ? -12.130 -36.229 -45.406 1.00 46.21 ? 114 GLN A O   1 
ATOM   682  C  CB  . GLN A 1 85  ? -9.639  -37.934 -46.159 1.00 52.90 ? 114 GLN A CB  1 
ATOM   683  C  CG  . GLN A 1 85  ? -10.697 -38.725 -45.402 1.00 58.35 ? 114 GLN A CG  1 
ATOM   684  C  CD  . GLN A 1 85  ? -10.200 -40.110 -45.112 1.00 64.09 ? 114 GLN A CD  1 
ATOM   685  O  OE1 . GLN A 1 85  ? -9.036  -40.421 -45.398 1.00 69.36 ? 114 GLN A OE1 1 
ATOM   686  N  NE2 . GLN A 1 85  ? -11.091 -40.941 -44.598 1.00 66.37 ? 114 GLN A NE2 1 
ATOM   687  N  N   . THR A 1 86  ? -10.294 -35.043 -44.829 1.00 41.64 ? 115 THR A N   1 
ATOM   688  C  CA  . THR A 1 86  ? -10.896 -34.464 -43.638 1.00 41.82 ? 115 THR A CA  1 
ATOM   689  C  C   . THR A 1 86  ? -11.563 -33.134 -43.975 1.00 37.72 ? 115 THR A C   1 
ATOM   690  O  O   . THR A 1 86  ? -12.507 -32.728 -43.302 1.00 38.29 ? 115 THR A O   1 
ATOM   691  C  CB  . THR A 1 86  ? -9.818  -34.272 -42.570 1.00 42.39 ? 115 THR A CB  1 
ATOM   692  O  OG1 . THR A 1 86  ? -8.826  -33.373 -43.072 1.00 43.08 ? 115 THR A OG1 1 
ATOM   693  C  CG2 . THR A 1 86  ? -9.180  -35.590 -42.175 1.00 44.39 ? 115 THR A CG2 1 
ATOM   694  N  N   . GLY A 1 87  ? -11.043 -32.460 -44.995 1.00 32.99 ? 116 GLY A N   1 
ATOM   695  C  CA  . GLY A 1 87  ? -11.305 -31.049 -45.183 1.00 31.36 ? 116 GLY A CA  1 
ATOM   696  C  C   . GLY A 1 87  ? -10.387 -30.217 -44.292 1.00 29.10 ? 116 GLY A C   1 
ATOM   697  O  O   . GLY A 1 87  ? -9.607  -30.760 -43.518 1.00 28.68 ? 116 GLY A O   1 
ATOM   698  N  N   . MET A 1 88  ? -10.496 -28.898 -44.447 1.00 26.69 ? 117 MET A N   1 
ATOM   699  C  CA  . MET A 1 88  ? -9.804  -27.928 -43.630 1.00 25.20 ? 117 MET A CA  1 
ATOM   700  C  C   . MET A 1 88  ? -10.795 -26.847 -43.236 1.00 24.91 ? 117 MET A C   1 
ATOM   701  O  O   . MET A 1 88  ? -11.706 -26.540 -44.012 1.00 24.75 ? 117 MET A O   1 
ATOM   702  C  CB  . MET A 1 88  ? -8.658  -27.306 -44.424 1.00 24.17 ? 117 MET A CB  1 
ATOM   703  C  CG  . MET A 1 88  ? -7.540  -28.292 -44.720 1.00 24.65 ? 117 MET A CG  1 
ATOM   704  S  SD  . MET A 1 88  ? -6.208  -27.593 -45.709 1.00 25.20 ? 117 MET A SD  1 
ATOM   705  C  CE  . MET A 1 88  ? -5.775  -26.253 -44.573 1.00 23.56 ? 117 MET A CE  1 
ATOM   706  N  N   . THR A 1 89  ? -10.615 -26.265 -42.038 1.00 24.46 ? 118 THR A N   1 
ATOM   707  C  CA  . THR A 1 89  ? -11.455 -25.138 -41.643 1.00 24.31 ? 118 THR A CA  1 
ATOM   708  C  C   . THR A 1 89  ? -10.989 -23.883 -42.365 1.00 22.68 ? 118 THR A C   1 
ATOM   709  O  O   . THR A 1 89  ? -9.849  -23.771 -42.815 1.00 21.86 ? 118 THR A O   1 
ATOM   710  C  CB  . THR A 1 89  ? -11.489 -24.936 -40.121 1.00 25.20 ? 118 THR A CB  1 
ATOM   711  O  OG1 . THR A 1 89  ? -10.182 -24.534 -39.711 1.00 24.52 ? 118 THR A OG1 1 
ATOM   712  C  CG2 . THR A 1 89  ? -11.955 -26.176 -39.383 1.00 27.19 ? 118 THR A CG2 1 
ATOM   713  N  N   . ILE A 1 90  ? -11.881 -22.894 -42.427 1.00 22.76 ? 119 ILE A N   1 
ATOM   714  C  CA  . ILE A 1 90  ? -11.569 -21.594 -42.997 1.00 21.82 ? 119 ILE A CA  1 
ATOM   715  C  C   . ILE A 1 90  ? -10.314 -21.035 -42.331 1.00 20.97 ? 119 ILE A C   1 
ATOM   716  O  O   . ILE A 1 90  ? -9.429  -20.524 -43.010 1.00 19.20 ? 119 ILE A O   1 
ATOM   717  C  CB  . ILE A 1 90  ? -12.760 -20.632 -42.889 1.00 22.84 ? 119 ILE A CB  1 
ATOM   718  C  CG1 . ILE A 1 90  ? -13.915 -21.070 -43.801 1.00 24.40 ? 119 ILE A CG1 1 
ATOM   719  C  CG2 . ILE A 1 90  ? -12.320 -19.198 -43.181 1.00 21.40 ? 119 ILE A CG2 1 
ATOM   720  C  CD1 . ILE A 1 90  ? -13.606 -20.929 -45.293 1.00 24.19 ? 119 ILE A CD1 1 
ATOM   721  N  N   . GLY A 1 91  ? -10.216 -21.212 -41.005 1.00 21.90 ? 120 GLY A N   1 
ATOM   722  C  CA  . GLY A 1 91  ? -9.061  -20.732 -40.257 1.00 21.68 ? 120 GLY A CA  1 
ATOM   723  C  C   . GLY A 1 91  ? -7.783  -21.446 -40.678 1.00 21.22 ? 120 GLY A C   1 
ATOM   724  O  O   . GLY A 1 91  ? -6.745  -20.831 -40.881 1.00 20.03 ? 120 GLY A O   1 
ATOM   725  N  N   . GLN A 1 92  ? -7.862  -22.771 -40.827 1.00 21.60 ? 121 GLN A N   1 
ATOM   726  C  CA  . GLN A 1 92  ? -6.705  -23.529 -41.272 1.00 21.78 ? 121 GLN A CA  1 
ATOM   727  C  C   . GLN A 1 92  ? -6.292  -23.139 -42.684 1.00 20.49 ? 121 GLN A C   1 
ATOM   728  O  O   . GLN A 1 92  ? -5.108  -23.099 -42.985 1.00 19.81 ? 121 GLN A O   1 
ATOM   729  C  CB  . GLN A 1 92  ? -7.027  -25.016 -41.188 1.00 23.57 ? 121 GLN A CB  1 
ATOM   730  C  CG  . GLN A 1 92  ? -7.193  -25.497 -39.760 1.00 25.69 ? 121 GLN A CG  1 
ATOM   731  C  CD  . GLN A 1 92  ? -7.772  -26.886 -39.674 1.00 27.86 ? 121 GLN A CD  1 
ATOM   732  O  OE1 . GLN A 1 92  ? -8.397  -27.403 -40.607 1.00 27.47 ? 121 GLN A OE1 1 
ATOM   733  N  NE2 . GLN A 1 92  ? -7.657  -27.446 -38.489 1.00 30.22 ? 121 GLN A NE2 1 
ATOM   734  N  N   . LEU A 1 93  ? -7.277  -22.860 -43.552 1.00 20.46 ? 122 LEU A N   1 
ATOM   735  C  CA  . LEU A 1 93  ? -7.005  -22.410 -44.906 1.00 19.77 ? 122 LEU A CA  1 
ATOM   736  C  C   . LEU A 1 93  ? -6.295  -21.059 -44.912 1.00 18.78 ? 122 LEU A C   1 
ATOM   737  O  O   . LEU A 1 93  ? -5.373  -20.865 -45.693 1.00 17.65 ? 122 LEU A O   1 
ATOM   738  C  CB  . LEU A 1 93  ? -8.305  -22.385 -45.702 1.00 20.38 ? 122 LEU A CB  1 
ATOM   739  C  CG  . LEU A 1 93  ? -8.924  -23.753 -45.982 1.00 21.57 ? 122 LEU A CG  1 
ATOM   740  C  CD1 . LEU A 1 93  ? -10.352 -23.609 -46.481 1.00 23.10 ? 122 LEU A CD1 1 
ATOM   741  C  CD2 . LEU A 1 93  ? -8.107  -24.526 -47.001 1.00 21.73 ? 122 LEU A CD2 1 
ATOM   742  N  N   . CYS A 1 94  ? -6.705  -20.118 -44.041 1.00 19.88 ? 123 CYS A N   1 
ATOM   743  C  CA  . CYS A 1 94  ? -6.037  -18.826 -43.943 1.00 18.73 ? 123 CYS A CA  1 
ATOM   744  C  C   . CYS A 1 94  ? -4.568  -19.005 -43.561 1.00 18.84 ? 123 CYS A C   1 
ATOM   745  O  O   . CYS A 1 94  ? -3.672  -18.416 -44.182 1.00 18.95 ? 123 CYS A O   1 
ATOM   746  C  CB  . CYS A 1 94  ? -6.728  -17.896 -42.943 1.00 18.82 ? 123 CYS A CB  1 
ATOM   747  S  SG  . CYS A 1 94  ? -8.373  -17.350 -43.468 1.00 20.13 ? 123 CYS A SG  1 
ATOM   748  N  N   . ASP A 1 95  ? -4.324  -19.830 -42.537 1.00 21.33 ? 124 ASP A N   1 
ATOM   749  C  CA  . ASP A 1 95  ? -2.979  -20.095 -42.055 1.00 21.32 ? 124 ASP A CA  1 
ATOM   750  C  C   . ASP A 1 95  ? -2.108  -20.644 -43.184 1.00 21.34 ? 124 ASP A C   1 
ATOM   751  O  O   . ASP A 1 95  ? -0.996  -20.169 -43.436 1.00 22.08 ? 124 ASP A O   1 
ATOM   752  C  CB  . ASP A 1 95  ? -3.079  -21.027 -40.862 1.00 24.31 ? 124 ASP A CB  1 
ATOM   753  C  CG  . ASP A 1 95  ? -1.771  -21.460 -40.207 1.00 27.74 ? 124 ASP A CG  1 
ATOM   754  O  OD1 . ASP A 1 95  ? -0.873  -21.911 -40.902 1.00 32.17 ? 124 ASP A OD1 1 
ATOM   755  O  OD2 . ASP A 1 95  ? -1.714  -21.452 -38.972 1.00 32.66 ? 124 ASP A OD2 1 
ATOM   756  N  N   . ALA A 1 96  ? -2.640  -21.611 -43.920 1.00 21.22 ? 125 ALA A N   1 
ATOM   757  C  CA  . ALA A 1 96  ? -1.893  -22.264 -44.986 1.00 20.69 ? 125 ALA A CA  1 
ATOM   758  C  C   . ALA A 1 96  ? -1.592  -21.299 -46.133 1.00 19.30 ? 125 ALA A C   1 
ATOM   759  O  O   . ALA A 1 96  ? -0.490  -21.316 -46.697 1.00 20.01 ? 125 ALA A O   1 
ATOM   760  C  CB  . ALA A 1 96  ? -2.681  -23.453 -45.471 1.00 21.24 ? 125 ALA A CB  1 
ATOM   761  N  N   . ALA A 1 97  ? -2.585  -20.470 -46.463 1.00 19.10 ? 126 ALA A N   1 
ATOM   762  C  CA  . ALA A 1 97  ? -2.488  -19.530 -47.572 1.00 18.56 ? 126 ALA A CA  1 
ATOM   763  C  C   . ALA A 1 97  ? -1.395  -18.498 -47.297 1.00 19.50 ? 126 ALA A C   1 
ATOM   764  O  O   . ALA A 1 97  ? -0.604  -18.178 -48.178 1.00 18.49 ? 126 ALA A O   1 
ATOM   765  C  CB  . ALA A 1 97  ? -3.821  -18.868 -47.840 1.00 19.15 ? 126 ALA A CB  1 
ATOM   766  N  N   . ILE A 1 98  ? -1.333  -17.993 -46.064 1.00 19.08 ? 127 ILE A N   1 
ATOM   767  C  CA  . ILE A 1 98  ? -0.302  -17.027 -45.710 1.00 19.55 ? 127 ILE A CA  1 
ATOM   768  C  C   . ILE A 1 98  ? 1.053   -17.675 -45.437 1.00 19.88 ? 127 ILE A C   1 
ATOM   769  O  O   . ILE A 1 98  ? 2.074   -17.185 -45.931 1.00 19.25 ? 127 ILE A O   1 
ATOM   770  C  CB  . ILE A 1 98  ? -0.778  -16.150 -44.543 1.00 20.78 ? 127 ILE A CB  1 
ATOM   771  C  CG1 . ILE A 1 98  ? -1.870  -15.209 -45.062 1.00 22.20 ? 127 ILE A CG1 1 
ATOM   772  C  CG2 . ILE A 1 98  ? 0.395   -15.377 -43.944 1.00 20.25 ? 127 ILE A CG2 1 
ATOM   773  C  CD1 . ILE A 1 98  ? -2.549  -14.404 -43.994 1.00 25.86 ? 127 ILE A CD1 1 
ATOM   774  N  N   . ARG A 1 99  ? 1.073   -18.751 -44.640 1.00 20.72 ? 128 ARG A N   1 
ATOM   775  C  CA  . ARG A 1 99  ? 2.315   -19.233 -44.051 1.00 22.74 ? 128 ARG A CA  1 
ATOM   776  C  C   . ARG A 1 99  ? 3.032   -20.225 -44.971 1.00 25.27 ? 128 ARG A C   1 
ATOM   777  O  O   . ARG A 1 99  ? 4.242   -20.408 -44.850 1.00 26.69 ? 128 ARG A O   1 
ATOM   778  C  CB  . ARG A 1 99  ? 2.108   -19.816 -42.644 1.00 24.28 ? 128 ARG A CB  1 
ATOM   779  C  CG  . ARG A 1 99  ? 1.669   -18.862 -41.534 1.00 24.71 ? 128 ARG A CG  1 
ATOM   780  C  CD  . ARG A 1 99  ? 1.534   -19.567 -40.133 1.00 27.36 ? 128 ARG A CD  1 
ATOM   781  N  NE  . ARG A 1 99  ? 2.667   -20.437 -39.777 1.00 33.06 ? 128 ARG A NE  1 
ATOM   782  C  CZ  . ARG A 1 99  ? 2.730   -21.783 -39.895 1.00 38.08 ? 128 ARG A CZ  1 
ATOM   783  N  NH1 . ARG A 1 99  ? 1.640   -22.521 -40.094 1.00 35.34 ? 128 ARG A NH1 1 
ATOM   784  N  NH2 . ARG A 1 99  ? 3.899   -22.405 -39.804 1.00 36.71 ? 128 ARG A NH2 1 
ATOM   785  N  N   . TYR A 1 100 ? 2.297   -20.917 -45.842 1.00 25.99 ? 129 TYR A N   1 
ATOM   786  C  CA  . TYR A 1 100 ? 2.894   -21.842 -46.812 1.00 29.86 ? 129 TYR A CA  1 
ATOM   787  C  C   . TYR A 1 100 ? 2.617   -21.421 -48.254 1.00 27.96 ? 129 TYR A C   1 
ATOM   788  O  O   . TYR A 1 100 ? 2.962   -22.124 -49.204 1.00 33.52 ? 129 TYR A O   1 
ATOM   789  C  CB  . TYR A 1 100 ? 2.371   -23.260 -46.591 1.00 30.17 ? 129 TYR A CB  1 
ATOM   790  C  CG  . TYR A 1 100 ? 2.927   -23.805 -45.296 1.00 31.61 ? 129 TYR A CG  1 
ATOM   791  C  CD1 . TYR A 1 100 ? 4.249   -24.255 -45.238 1.00 34.99 ? 129 TYR A CD1 1 
ATOM   792  C  CD2 . TYR A 1 100 ? 2.186   -23.782 -44.123 1.00 32.27 ? 129 TYR A CD2 1 
ATOM   793  C  CE1 . TYR A 1 100 ? 4.799   -24.709 -44.055 1.00 34.97 ? 129 TYR A CE1 1 
ATOM   794  C  CE2 . TYR A 1 100 ? 2.726   -24.237 -42.935 1.00 35.14 ? 129 TYR A CE2 1 
ATOM   795  C  CZ  . TYR A 1 100 ? 4.027   -24.699 -42.910 1.00 34.66 ? 129 TYR A CZ  1 
ATOM   796  O  OH  . TYR A 1 100 ? 4.549   -25.148 -41.757 1.00 37.17 ? 129 TYR A OH  1 
ATOM   797  N  N   . SER A 1 101 ? 1.982   -20.266 -48.430 1.00 28.80 ? 130 SER A N   1 
ATOM   798  C  CA  . SER A 1 101 ? 1.547   -19.843 -49.746 1.00 28.76 ? 130 SER A CA  1 
ATOM   799  C  C   . SER A 1 101 ? 0.825   -20.979 -50.491 1.00 26.77 ? 130 SER A C   1 
ATOM   800  O  O   . SER A 1 101 ? 0.948   -21.125 -51.715 1.00 28.76 ? 130 SER A O   1 
ATOM   801  C  CB  . SER A 1 101 ? 2.731   -19.297 -50.514 1.00 29.87 ? 130 SER A CB  1 
ATOM   802  O  OG  . SER A 1 101 ? 2.252   -18.321 -51.410 1.00 24.48 ? 130 SER A OG  1 
ATOM   803  N  N   . ASP A 1 102 ? -0.007  -21.721 -49.767 1.00 23.87 ? 131 ASP A N   1 
ATOM   804  C  CA  . ASP A 1 102 ? -0.699  -22.881 -50.288 1.00 20.41 ? 131 ASP A CA  1 
ATOM   805  C  C   . ASP A 1 102 ? -1.701  -22.427 -51.348 1.00 19.83 ? 131 ASP A C   1 
ATOM   806  O  O   . ASP A 1 102 ? -2.557  -21.603 -51.054 1.00 20.06 ? 131 ASP A O   1 
ATOM   807  C  CB  . ASP A 1 102 ? -1.355  -23.632 -49.138 1.00 20.23 ? 131 ASP A CB  1 
ATOM   808  C  CG  . ASP A 1 102 ? -2.027  -24.941 -49.521 1.00 19.75 ? 131 ASP A CG  1 
ATOM   809  O  OD1 . ASP A 1 102 ? -2.944  -24.902 -50.380 1.00 19.90 ? 131 ASP A OD1 1 
ATOM   810  O  OD2 . ASP A 1 102 ? -1.636  -25.990 -48.953 1.00 20.15 ? 131 ASP A OD2 1 
ATOM   811  N  N   . GLY A 1 103 ? -1.590  -22.959 -52.582 1.00 18.50 ? 132 GLY A N   1 
ATOM   812  C  CA  . GLY A 1 103 ? -2.420  -22.527 -53.697 1.00 17.05 ? 132 GLY A CA  1 
ATOM   813  C  C   . GLY A 1 103 ? -3.882  -22.980 -53.587 1.00 16.83 ? 132 GLY A C   1 
ATOM   814  O  O   . GLY A 1 103 ? -4.810  -22.192 -53.827 1.00 16.08 ? 132 GLY A O   1 
ATOM   815  N  N   . THR A 1 104 ? -4.107  -24.252 -53.256 1.00 17.75 ? 133 THR A N   1 
ATOM   816  C  CA  . THR A 1 104 ? -5.467  -24.744 -53.102 1.00 19.31 ? 133 THR A CA  1 
ATOM   817  C  C   . THR A 1 104 ? -6.190  -24.020 -51.965 1.00 19.07 ? 133 THR A C   1 
ATOM   818  O  O   . THR A 1 104 ? -7.383  -23.757 -52.055 1.00 19.12 ? 133 THR A O   1 
ATOM   819  C  CB  . THR A 1 104 ? -5.476  -26.246 -52.875 1.00 21.33 ? 133 THR A CB  1 
ATOM   820  O  OG1 . THR A 1 104 ? -4.815  -26.802 -54.008 1.00 22.44 ? 133 THR A OG1 1 
ATOM   821  C  CG2 . THR A 1 104 ? -6.889  -26.782 -52.803 1.00 22.56 ? 133 THR A CG2 1 
ATOM   822  N  N   . ALA A 1 105 ? -5.480  -23.737 -50.868 1.00 18.75 ? 134 ALA A N   1 
ATOM   823  C  CA  . ALA A 1 105 ? -6.065  -22.984 -49.760 1.00 17.93 ? 134 ALA A CA  1 
ATOM   824  C  C   . ALA A 1 105 ? -6.606  -21.637 -50.259 1.00 17.75 ? 134 ALA A C   1 
ATOM   825  O  O   . ALA A 1 105 ? -7.729  -21.230 -49.930 1.00 18.54 ? 134 ALA A O   1 
ATOM   826  C  CB  . ALA A 1 105 ? -5.044  -22.819 -48.668 1.00 17.54 ? 134 ALA A CB  1 
ATOM   827  N  N   . ALA A 1 106 ? -5.817  -20.950 -51.088 1.00 17.23 ? 135 ALA A N   1 
ATOM   828  C  CA  . ALA A 1 106 ? -6.237  -19.663 -51.634 1.00 17.20 ? 135 ALA A CA  1 
ATOM   829  C  C   . ALA A 1 106 ? -7.455  -19.840 -52.541 1.00 17.73 ? 135 ALA A C   1 
ATOM   830  O  O   . ALA A 1 106 ? -8.412  -19.059 -52.445 1.00 19.37 ? 135 ALA A O   1 
ATOM   831  C  CB  . ALA A 1 106 ? -5.104  -19.007 -52.342 1.00 16.59 ? 135 ALA A CB  1 
ATOM   832  N  N   . ASN A 1 107 ? -7.491  -20.907 -53.361 1.00 18.73 ? 136 ASN A N   1 
ATOM   833  C  CA  . ASN A 1 107 ? -8.654  -21.119 -54.219 1.00 18.03 ? 136 ASN A CA  1 
ATOM   834  C  C   . ASN A 1 107 ? -9.899  -21.381 -53.385 1.00 18.19 ? 136 ASN A C   1 
ATOM   835  O  O   . ASN A 1 107 ? -10.978 -20.934 -53.745 1.00 18.15 ? 136 ASN A O   1 
ATOM   836  C  CB  . ASN A 1 107 ? -8.480  -22.249 -55.233 1.00 18.22 ? 136 ASN A CB  1 
ATOM   837  C  CG  . ASN A 1 107 ? -7.548  -21.888 -56.366 1.00 18.06 ? 136 ASN A CG  1 
ATOM   838  O  OD1 . ASN A 1 107 ? -7.135  -20.733 -56.525 1.00 16.95 ? 136 ASN A OD1 1 
ATOM   839  N  ND2 . ASN A 1 107 ? -7.180  -22.879 -57.151 1.00 19.11 ? 136 ASN A ND2 1 
ATOM   840  N  N   . LEU A 1 108 ? -9.767  -22.137 -52.285 1.00 18.61 ? 137 LEU A N   1 
ATOM   841  C  CA  . LEU A 1 108 ? -10.913 -22.462 -51.453 1.00 19.13 ? 137 LEU A CA  1 
ATOM   842  C  C   . LEU A 1 108 ? -11.413 -21.205 -50.747 1.00 19.21 ? 137 LEU A C   1 
ATOM   843  O  O   . LEU A 1 108 ? -12.613 -21.023 -50.557 1.00 19.51 ? 137 LEU A O   1 
ATOM   844  C  CB  . LEU A 1 108 ? -10.583 -23.597 -50.477 1.00 19.30 ? 137 LEU A CB  1 
ATOM   845  C  CG  . LEU A 1 108 ? -10.333 -24.965 -51.112 1.00 20.09 ? 137 LEU A CG  1 
ATOM   846  C  CD1 . LEU A 1 108 ? -9.736  -25.918 -50.130 1.00 20.76 ? 137 LEU A CD1 1 
ATOM   847  C  CD2 . LEU A 1 108 ? -11.607 -25.550 -51.702 1.00 21.45 ? 137 LEU A CD2 1 
ATOM   848  N  N   . LEU A 1 109 ? -10.494 -20.329 -50.366 1.00 18.85 ? 138 LEU A N   1 
ATOM   849  C  CA  . LEU A 1 109 ? -10.897 -19.079 -49.742 1.00 19.89 ? 138 LEU A CA  1 
ATOM   850  C  C   . LEU A 1 109 ? -11.607 -18.176 -50.750 1.00 20.63 ? 138 LEU A C   1 
ATOM   851  O  O   . LEU A 1 109 ? -12.644 -17.591 -50.435 1.00 20.58 ? 138 LEU A O   1 
ATOM   852  C  CB  . LEU A 1 109 ? -9.701  -18.392 -49.109 1.00 18.59 ? 138 LEU A CB  1 
ATOM   853  C  CG  . LEU A 1 109 ? -9.138  -19.100 -47.865 1.00 19.99 ? 138 LEU A CG  1 
ATOM   854  C  CD1 . LEU A 1 109 ? -7.764  -18.543 -47.496 1.00 18.67 ? 138 LEU A CD1 1 
ATOM   855  C  CD2 . LEU A 1 109 ? -10.074 -19.002 -46.682 1.00 20.77 ? 138 LEU A CD2 1 
ATOM   856  N  N   . LEU A 1 110 ? -11.058 -18.103 -51.970 1.00 20.43 ? 139 LEU A N   1 
ATOM   857  C  CA  . LEU A 1 110 ? -11.730 -17.414 -53.060 1.00 20.03 ? 139 LEU A CA  1 
ATOM   858  C  C   . LEU A 1 110 ? -13.173 -17.907 -53.197 1.00 21.21 ? 139 LEU A C   1 
ATOM   859  O  O   . LEU A 1 110 ? -14.080 -17.095 -53.287 1.00 21.12 ? 139 LEU A O   1 
ATOM   860  C  CB  . LEU A 1 110 ? -10.939 -17.582 -54.354 1.00 19.47 ? 139 LEU A CB  1 
ATOM   861  C  CG  . LEU A 1 110 ? -9.667  -16.742 -54.467 1.00 18.83 ? 139 LEU A CG  1 
ATOM   862  C  CD1 . LEU A 1 110 ? -8.801  -17.155 -55.668 1.00 18.74 ? 139 LEU A CD1 1 
ATOM   863  C  CD2 . LEU A 1 110 ? -9.980  -15.252 -54.556 1.00 19.12 ? 139 LEU A CD2 1 
ATOM   864  N  N   . ALA A 1 111 ? -13.385 -19.227 -53.214 1.00 22.00 ? 140 ALA A N   1 
ATOM   865  C  CA  . ALA A 1 111 ? -14.713 -19.805 -53.369 1.00 23.40 ? 140 ALA A CA  1 
ATOM   866  C  C   . ALA A 1 111 ? -15.596 -19.455 -52.172 1.00 24.65 ? 140 ALA A C   1 
ATOM   867  O  O   . ALA A 1 111 ? -16.805 -19.272 -52.311 1.00 25.06 ? 140 ALA A O   1 
ATOM   868  C  CB  . ALA A 1 111 ? -14.614 -21.293 -53.580 1.00 24.47 ? 140 ALA A CB  1 
ATOM   869  N  N   . ASP A 1 112 ? -15.019 -19.410 -50.971 1.00 24.90 ? 141 ASP A N   1 
ATOM   870  C  CA  . ASP A 1 112 ? -15.791 -19.041 -49.802 1.00 26.22 ? 141 ASP A CA  1 
ATOM   871  C  C   . ASP A 1 112 ? -16.224 -17.580 -49.925 1.00 26.66 ? 141 ASP A C   1 
ATOM   872  O  O   . ASP A 1 112 ? -17.338 -17.211 -49.553 1.00 29.64 ? 141 ASP A O   1 
ATOM   873  C  CB  . ASP A 1 112 ? -15.009 -19.231 -48.514 1.00 26.19 ? 141 ASP A CB  1 
ATOM   874  C  CG  . ASP A 1 112 ? -15.842 -19.018 -47.253 1.00 26.55 ? 141 ASP A CG  1 
ATOM   875  O  OD1 . ASP A 1 112 ? -16.779 -19.788 -47.072 1.00 30.08 ? 141 ASP A OD1 1 
ATOM   876  O  OD2 . ASP A 1 112 ? -15.570 -18.064 -46.500 1.00 25.89 ? 141 ASP A OD2 1 
ATOM   877  N  N   . LEU A 1 113 ? -15.343 -16.764 -50.491 1.00 24.81 ? 142 LEU A N   1 
ATOM   878  C  CA  . LEU A 1 113 ? -15.578 -15.336 -50.568 1.00 24.80 ? 142 LEU A CA  1 
ATOM   879  C  C   . LEU A 1 113 ? -16.616 -15.015 -51.639 1.00 25.26 ? 142 LEU A C   1 
ATOM   880  O  O   . LEU A 1 113 ? -17.500 -14.216 -51.387 1.00 26.09 ? 142 LEU A O   1 
ATOM   881  C  CB  . LEU A 1 113 ? -14.267 -14.612 -50.834 1.00 22.93 ? 142 LEU A CB  1 
ATOM   882  C  CG  . LEU A 1 113 ? -14.334 -13.095 -50.774 1.00 23.19 ? 142 LEU A CG  1 
ATOM   883  C  CD1 . LEU A 1 113 ? -14.501 -12.681 -49.327 1.00 24.06 ? 142 LEU A CD1 1 
ATOM   884  C  CD2 . LEU A 1 113 ? -13.088 -12.509 -51.426 1.00 23.14 ? 142 LEU A CD2 1 
ATOM   885  N  N   . GLY A 1 114 ? -16.494 -15.625 -52.818 1.00 24.86 ? 143 GLY A N   1 
ATOM   886  C  CA  . GLY A 1 114 ? -17.233 -15.187 -53.994 1.00 25.61 ? 143 GLY A CA  1 
ATOM   887  C  C   . GLY A 1 114 ? -18.052 -16.296 -54.644 1.00 27.91 ? 143 GLY A C   1 
ATOM   888  O  O   . GLY A 1 114 ? -18.703 -16.077 -55.674 1.00 27.79 ? 143 GLY A O   1 
ATOM   889  N  N   . GLY A 1 115 ? -18.056 -17.482 -54.033 1.00 28.67 ? 144 GLY A N   1 
ATOM   890  C  CA  . GLY A 1 115 ? -18.721 -18.629 -54.617 1.00 32.02 ? 144 GLY A CA  1 
ATOM   891  C  C   . GLY A 1 115 ? -17.873 -19.246 -55.728 1.00 34.46 ? 144 GLY A C   1 
ATOM   892  O  O   . GLY A 1 115 ? -16.781 -18.774 -56.069 1.00 30.93 ? 144 GLY A O   1 
ATOM   893  N  N   . PRO A 1 116 ? -18.362 -20.348 -56.327 1.00 39.38 ? 145 PRO A N   1 
ATOM   894  C  CA  . PRO A 1 116 ? -17.704 -20.912 -57.500 1.00 43.24 ? 145 PRO A CA  1 
ATOM   895  C  C   . PRO A 1 116 ? -17.922 -19.924 -58.644 1.00 41.84 ? 145 PRO A C   1 
ATOM   896  O  O   . PRO A 1 116 ? -19.056 -19.516 -58.908 1.00 52.19 ? 145 PRO A O   1 
ATOM   897  C  CB  . PRO A 1 116 ? -18.448 -22.243 -57.674 1.00 45.83 ? 145 PRO A CB  1 
ATOM   898  C  CG  . PRO A 1 116 ? -19.832 -21.959 -57.129 1.00 47.00 ? 145 PRO A CG  1 
ATOM   899  C  CD  . PRO A 1 116 ? -19.579 -21.063 -55.932 1.00 43.47 ? 145 PRO A CD  1 
ATOM   900  N  N   . GLY A 1 117 A -16.837 -19.496 -59.269 1.00 37.15 ? 145 GLY A N   1 
ATOM   901  C  CA  . GLY A 1 117 A -16.934 -18.572 -60.388 1.00 35.41 ? 145 GLY A CA  1 
ATOM   902  C  C   . GLY A 1 117 A -16.732 -17.110 -59.994 1.00 32.30 ? 145 GLY A C   1 
ATOM   903  O  O   . GLY A 1 117 A -16.299 -16.329 -60.831 1.00 32.47 ? 145 GLY A O   1 
ATOM   904  N  N   . GLY A 1 118 B -17.070 -16.736 -58.745 1.00 30.14 ? 145 GLY A N   1 
ATOM   905  C  CA  . GLY A 1 118 B -17.155 -15.331 -58.358 1.00 28.03 ? 145 GLY A CA  1 
ATOM   906  C  C   . GLY A 1 118 B -16.018 -14.869 -57.449 1.00 25.67 ? 145 GLY A C   1 
ATOM   907  O  O   . GLY A 1 118 B -15.958 -13.694 -57.082 1.00 25.24 ? 145 GLY A O   1 
ATOM   908  N  N   . GLY A 1 119 C -15.105 -15.787 -57.094 1.00 24.75 ? 145 GLY A N   1 
ATOM   909  C  CA  . GLY A 1 119 C -14.077 -15.491 -56.107 1.00 23.36 ? 145 GLY A CA  1 
ATOM   910  C  C   . GLY A 1 119 C -13.154 -14.334 -56.493 1.00 22.34 ? 145 GLY A C   1 
ATOM   911  O  O   . GLY A 1 119 C -12.910 -13.445 -55.672 1.00 21.94 ? 145 GLY A O   1 
ATOM   912  N  N   . THR A 1 120 D -12.591 -14.359 -57.713 1.00 22.92 ? 145 THR A N   1 
ATOM   913  C  CA  . THR A 1 120 D -11.596 -13.371 -58.098 1.00 22.31 ? 145 THR A CA  1 
ATOM   914  C  C   . THR A 1 120 D -12.267 -11.994 -58.195 1.00 21.61 ? 145 THR A C   1 
ATOM   915  O  O   . THR A 1 120 D -11.673 -11.011 -57.775 1.00 19.62 ? 145 THR A O   1 
ATOM   916  C  CB  . THR A 1 120 D -10.870 -13.776 -59.390 1.00 23.17 ? 145 THR A CB  1 
ATOM   917  O  OG1 . THR A 1 120 D -11.822 -13.922 -60.423 1.00 23.71 ? 145 THR A OG1 1 
ATOM   918  C  CG2 . THR A 1 120 D -10.147 -15.103 -59.258 1.00 24.11 ? 145 THR A CG2 1 
ATOM   919  N  N   . ALA A 1 121 ? -13.515 -11.946 -58.688 1.00 21.82 ? 146 ALA A N   1 
ATOM   920  C  CA  . ALA A 1 121 ? -14.278 -10.707 -58.699 1.00 23.04 ? 146 ALA A CA  1 
ATOM   921  C  C   . ALA A 1 121 ? -14.518 -10.201 -57.271 1.00 22.34 ? 146 ALA A C   1 
ATOM   922  O  O   . ALA A 1 121 ? -14.347 -9.011  -56.987 1.00 20.48 ? 146 ALA A O   1 
ATOM   923  C  CB  . ALA A 1 121 ? -15.582 -10.896 -59.435 1.00 24.34 ? 146 ALA A CB  1 
ATOM   924  N  N   . ALA A 1 122 ? -14.911 -11.096 -56.357 1.00 22.42 ? 147 ALA A N   1 
ATOM   925  C  CA  . ALA A 1 122 ? -15.176 -10.663 -54.987 1.00 21.88 ? 147 ALA A CA  1 
ATOM   926  C  C   . ALA A 1 122 ? -13.884 -10.183 -54.325 1.00 20.74 ? 147 ALA A C   1 
ATOM   927  O  O   . ALA A 1 122 ? -13.876 -9.226  -53.540 1.00 20.65 ? 147 ALA A O   1 
ATOM   928  C  CB  . ALA A 1 122 ? -15.831 -11.790 -54.196 1.00 22.41 ? 147 ALA A CB  1 
ATOM   929  N  N   . PHE A 1 123 ? -12.775 -10.877 -54.601 1.00 19.89 ? 148 PHE A N   1 
ATOM   930  C  CA  . PHE A 1 123 ? -11.501 -10.499 -54.010 1.00 19.02 ? 148 PHE A CA  1 
ATOM   931  C  C   . PHE A 1 123 ? -11.154 -9.085  -54.473 1.00 19.18 ? 148 PHE A C   1 
ATOM   932  O  O   . PHE A 1 123 ? -10.748 -8.229  -53.687 1.00 19.38 ? 148 PHE A O   1 
ATOM   933  C  CB  . PHE A 1 123 ? -10.394 -11.487 -54.370 1.00 19.38 ? 148 PHE A CB  1 
ATOM   934  C  CG  . PHE A 1 123 ? -8.997  -10.935 -54.107 1.00 18.41 ? 148 PHE A CG  1 
ATOM   935  C  CD1 . PHE A 1 123 ? -8.471  -10.897 -52.819 1.00 18.86 ? 148 PHE A CD1 1 
ATOM   936  C  CD2 . PHE A 1 123 ? -8.266  -10.322 -55.122 1.00 19.42 ? 148 PHE A CD2 1 
ATOM   937  C  CE1 . PHE A 1 123 ? -7.233  -10.312 -52.575 1.00 18.12 ? 148 PHE A CE1 1 
ATOM   938  C  CE2 . PHE A 1 123 ? -7.015  -9.766  -54.868 1.00 18.30 ? 148 PHE A CE2 1 
ATOM   939  C  CZ  . PHE A 1 123 ? -6.493  -9.795  -53.610 1.00 16.84 ? 148 PHE A CZ  1 
ATOM   940  N  N   . THR A 1 124 ? -11.314 -8.850  -55.774 1.00 17.61 ? 149 THR A N   1 
ATOM   941  C  CA  . THR A 1 124 ? -10.976 -7.564  -56.348 1.00 18.21 ? 149 THR A CA  1 
ATOM   942  C  C   . THR A 1 124 ? -11.865 -6.493  -55.705 1.00 19.06 ? 149 THR A C   1 
ATOM   943  O  O   . THR A 1 124 ? -11.393 -5.406  -55.405 1.00 19.87 ? 149 THR A O   1 
ATOM   944  C  CB  . THR A 1 124 ? -11.117 -7.637  -57.870 1.00 18.60 ? 149 THR A CB  1 
ATOM   945  O  OG1 . THR A 1 124 ? -10.184 -8.608  -58.351 1.00 18.37 ? 149 THR A OG1 1 
ATOM   946  C  CG2 . THR A 1 124 ? -10.799 -6.311  -58.519 1.00 18.63 ? 149 THR A CG2 1 
ATOM   947  N  N   . GLY A 1 125 ? -13.137 -6.823  -55.493 1.00 18.45 ? 150 GLY A N   1 
ATOM   948  C  CA  . GLY A 1 125 ? -14.101 -5.955  -54.843 1.00 20.46 ? 150 GLY A CA  1 
ATOM   949  C  C   . GLY A 1 125 ? -13.682 -5.566  -53.430 1.00 20.35 ? 150 GLY A C   1 
ATOM   950  O  O   . GLY A 1 125 ? -13.899 -4.444  -53.017 1.00 21.28 ? 150 GLY A O   1 
ATOM   951  N  N   . TYR A 1 126 ? -13.083 -6.497  -52.692 1.00 19.75 ? 151 TYR A N   1 
ATOM   952  C  CA  . TYR A 1 126 ? -12.596 -6.184  -51.369 1.00 20.89 ? 151 TYR A CA  1 
ATOM   953  C  C   . TYR A 1 126 ? -11.519 -5.100  -51.473 1.00 20.75 ? 151 TYR A C   1 
ATOM   954  O  O   . TYR A 1 126 ? -11.523 -4.151  -50.687 1.00 19.66 ? 151 TYR A O   1 
ATOM   955  C  CB  . TYR A 1 126 ? -12.144 -7.461  -50.647 1.00 20.34 ? 151 TYR A CB  1 
ATOM   956  C  CG  . TYR A 1 126 ? -11.650 -7.131  -49.247 1.00 20.60 ? 151 TYR A CG  1 
ATOM   957  C  CD1 . TYR A 1 126 ? -12.534 -6.673  -48.274 1.00 21.44 ? 151 TYR A CD1 1 
ATOM   958  C  CD2 . TYR A 1 126 ? -10.306 -7.205  -48.925 1.00 19.03 ? 151 TYR A CD2 1 
ATOM   959  C  CE1 . TYR A 1 126 ? -12.080 -6.317  -47.013 1.00 21.74 ? 151 TYR A CE1 1 
ATOM   960  C  CE2 . TYR A 1 126 ? -9.846  -6.854  -47.671 1.00 20.15 ? 151 TYR A CE2 1 
ATOM   961  C  CZ  . TYR A 1 126 ? -10.736 -6.427  -46.706 1.00 20.94 ? 151 TYR A CZ  1 
ATOM   962  O  OH  . TYR A 1 126 ? -10.299 -6.084  -45.462 1.00 23.30 ? 151 TYR A OH  1 
ATOM   963  N  N   . LEU A 1 127 ? -10.598 -5.239  -52.440 1.00 19.52 ? 152 LEU A N   1 
ATOM   964  C  CA  . LEU A 1 127 ? -9.585  -4.221  -52.640 1.00 20.11 ? 152 LEU A CA  1 
ATOM   965  C  C   . LEU A 1 127 ? -10.251 -2.885  -52.969 1.00 19.97 ? 152 LEU A C   1 
ATOM   966  O  O   . LEU A 1 127 ? -9.837  -1.841  -52.488 1.00 20.50 ? 152 LEU A O   1 
ATOM   967  C  CB  . LEU A 1 127 ? -8.597  -4.620  -53.726 1.00 19.27 ? 152 LEU A CB  1 
ATOM   968  C  CG  . LEU A 1 127 ? -7.800  -5.894  -53.466 1.00 20.17 ? 152 LEU A CG  1 
ATOM   969  C  CD1 . LEU A 1 127 ? -6.733  -6.058  -54.547 1.00 19.47 ? 152 LEU A CD1 1 
ATOM   970  C  CD2 . LEU A 1 127 ? -7.157  -5.845  -52.105 1.00 19.88 ? 152 LEU A CD2 1 
ATOM   971  N  N   . ARG A 1 128 ? -11.313 -2.908  -53.769 1.00 20.30 ? 153 ARG A N   1 
ATOM   972  C  CA  . ARG A 1 128 ? -12.031 -1.683  -54.090 1.00 20.48 ? 153 ARG A CA  1 
ATOM   973  C  C   . ARG A 1 128 ? -12.598 -1.035  -52.832 1.00 22.40 ? 153 ARG A C   1 
ATOM   974  O  O   . ARG A 1 128 ? -12.641 0.186   -52.747 1.00 21.64 ? 153 ARG A O   1 
ATOM   975  C  CB  . ARG A 1 128 ? -13.188 -1.917  -55.068 1.00 21.39 ? 153 ARG A CB  1 
ATOM   976  C  CG  . ARG A 1 128 ? -12.723 -2.459  -56.412 1.00 21.16 ? 153 ARG A CG  1 
ATOM   977  C  CD  . ARG A 1 128 ? -12.145 -1.381  -57.317 1.00 20.70 ? 153 ARG A CD  1 
ATOM   978  N  NE  . ARG A 1 128 ? -11.677 -1.995  -58.562 1.00 20.36 ? 153 ARG A NE  1 
ATOM   979  C  CZ  . ARG A 1 128 ? -10.496 -2.566  -58.790 1.00 18.35 ? 153 ARG A CZ  1 
ATOM   980  N  NH1 . ARG A 1 128 ? -9.532  -2.515  -57.903 1.00 17.19 ? 153 ARG A NH1 1 
ATOM   981  N  NH2 . ARG A 1 128 ? -10.282 -3.144  -59.962 1.00 18.54 ? 153 ARG A NH2 1 
ATOM   982  N  N   . SER A 1 129 ? -13.050 -1.865  -51.878 1.00 22.73 ? 154 SER A N   1 
ATOM   983  C  CA  . SER A 1 129 ? -13.621 -1.385  -50.623 1.00 23.83 ? 154 SER A CA  1 
ATOM   984  C  C   . SER A 1 129 ? -12.540 -0.712  -49.778 1.00 24.34 ? 154 SER A C   1 
ATOM   985  O  O   . SER A 1 129 ? -12.863 0.061   -48.885 1.00 24.56 ? 154 SER A O   1 
ATOM   986  C  CB  . SER A 1 129 ? -14.300 -2.502  -49.837 1.00 23.35 ? 154 SER A CB  1 
ATOM   987  O  OG  . SER A 1 129 ? -13.355 -3.308  -49.142 1.00 21.32 ? 154 SER A OG  1 
ATOM   988  N  N   . LEU A 1 130 ? -11.267 -1.030  -50.037 1.00 24.43 ? 155 LEU A N   1 
ATOM   989  C  CA  . LEU A 1 130 ? -10.149 -0.393  -49.349 1.00 25.13 ? 155 LEU A CA  1 
ATOM   990  C  C   . LEU A 1 130 ? -9.631  0.839   -50.093 1.00 26.82 ? 155 LEU A C   1 
ATOM   991  O  O   . LEU A 1 130 ? -8.643  1.404   -49.655 1.00 26.95 ? 155 LEU A O   1 
ATOM   992  C  CB  . LEU A 1 130 ? -9.007  -1.377  -49.165 1.00 24.14 ? 155 LEU A CB  1 
ATOM   993  C  CG  . LEU A 1 130 ? -9.337  -2.704  -48.473 1.00 23.48 ? 155 LEU A CG  1 
ATOM   994  C  CD1 . LEU A 1 130 ? -8.103  -3.615  -48.534 1.00 22.13 ? 155 LEU A CD1 1 
ATOM   995  C  CD2 . LEU A 1 130 ? -9.772  -2.482  -47.056 1.00 25.71 ? 155 LEU A CD2 1 
ATOM   996  N  N   . GLY A 1 131 ? -10.282 1.243   -51.190 1.00 27.41 ? 156 GLY A N   1 
ATOM   997  C  CA  . GLY A 1 131 ? -9.839  2.399   -51.958 1.00 27.72 ? 156 GLY A CA  1 
ATOM   998  C  C   . GLY A 1 131 ? -8.762  2.058   -52.995 1.00 26.37 ? 156 GLY A C   1 
ATOM   999  O  O   . GLY A 1 131 ? -8.240  2.969   -53.639 1.00 25.95 ? 156 GLY A O   1 
ATOM   1000 N  N   . ASP A 1 132 ? -8.481  0.762   -53.217 1.00 23.92 ? 157 ASP A N   1 
ATOM   1001 C  CA  . ASP A 1 132 ? -7.614  0.348   -54.317 1.00 23.52 ? 157 ASP A CA  1 
ATOM   1002 C  C   . ASP A 1 132 ? -8.459  0.171   -55.584 1.00 22.64 ? 157 ASP A C   1 
ATOM   1003 O  O   . ASP A 1 132 ? -9.174  -0.817  -55.731 1.00 20.45 ? 157 ASP A O   1 
ATOM   1004 C  CB  . ASP A 1 132 ? -6.839  -0.916  -53.985 1.00 22.16 ? 157 ASP A CB  1 
ATOM   1005 C  CG  . ASP A 1 132 ? -6.013  -1.527  -55.110 1.00 21.59 ? 157 ASP A CG  1 
ATOM   1006 O  OD1 . ASP A 1 132 ? -6.042  -0.961  -56.242 1.00 20.29 ? 157 ASP A OD1 1 
ATOM   1007 O  OD2 . ASP A 1 132 ? -5.316  -2.537  -54.838 1.00 20.03 ? 157 ASP A OD2 1 
ATOM   1008 N  N   . THR A 1 133 ? -8.347  1.126   -56.508 1.00 21.50 ? 158 THR A N   1 
ATOM   1009 C  CA  . THR A 1 133 ? -9.143  1.114   -57.721 1.00 22.24 ? 158 THR A CA  1 
ATOM   1010 C  C   . THR A 1 133 ? -8.347  0.554   -58.903 1.00 21.67 ? 158 THR A C   1 
ATOM   1011 O  O   . THR A 1 133 ? -8.858  0.605   -60.008 1.00 22.04 ? 158 THR A O   1 
ATOM   1012 C  CB  . THR A 1 133 ? -9.657  2.523   -58.032 1.00 24.71 ? 158 THR A CB  1 
ATOM   1013 O  OG1 . THR A 1 133 ? -8.505  3.326   -58.277 1.00 24.76 ? 158 THR A OG1 1 
ATOM   1014 C  CG2 . THR A 1 133 ? -10.497 3.084   -56.904 1.00 26.90 ? 158 THR A CG2 1 
ATOM   1015 N  N   . VAL A 1 134 ? -7.128  0.050   -58.669 1.00 19.53 ? 159 VAL A N   1 
ATOM   1016 C  CA  . VAL A 1 134 ? -6.203  -0.304  -59.741 1.00 20.53 ? 159 VAL A CA  1 
ATOM   1017 C  C   . VAL A 1 134 ? -5.995  -1.819  -59.845 1.00 19.11 ? 159 VAL A C   1 
ATOM   1018 O  O   . VAL A 1 134 ? -5.943  -2.375  -60.941 1.00 19.93 ? 159 VAL A O   1 
ATOM   1019 C  CB  . VAL A 1 134 ? -4.888  0.467   -59.532 1.00 21.58 ? 159 VAL A CB  1 
ATOM   1020 C  CG1 . VAL A 1 134 ? -3.677  -0.191  -60.153 1.00 23.02 ? 159 VAL A CG1 1 
ATOM   1021 C  CG2 . VAL A 1 134 ? -5.035  1.912   -60.035 1.00 22.51 ? 159 VAL A CG2 1 
ATOM   1022 N  N   . SER A 1 135 ? -5.821  -2.490  -58.710 1.00 18.71 ? 160 SER A N   1 
ATOM   1023 C  CA  . SER A 1 135 ? -5.473  -3.911  -58.711 1.00 17.93 ? 160 SER A CA  1 
ATOM   1024 C  C   . SER A 1 135 ? -6.618  -4.736  -59.272 1.00 17.88 ? 160 SER A C   1 
ATOM   1025 O  O   . SER A 1 135 ? -7.786  -4.369  -59.117 1.00 20.94 ? 160 SER A O   1 
ATOM   1026 C  CB  . SER A 1 135 ? -5.136  -4.370  -57.328 1.00 19.17 ? 160 SER A CB  1 
ATOM   1027 O  OG  . SER A 1 135 ? -4.047  -3.664  -56.766 1.00 18.99 ? 160 SER A OG  1 
ATOM   1028 N  N   . ARG A 1 136 ? -6.284  -5.887  -59.875 1.00 17.55 ? 161 ARG A N   1 
ATOM   1029 C  CA  . ARG A 1 136 ? -7.295  -6.796  -60.376 1.00 17.71 ? 161 ARG A CA  1 
ATOM   1030 C  C   . ARG A 1 136 ? -6.786  -8.239  -60.295 1.00 18.07 ? 161 ARG A C   1 
ATOM   1031 O  O   . ARG A 1 136 ? -5.638  -8.554  -60.657 1.00 17.55 ? 161 ARG A O   1 
ATOM   1032 C  CB  . ARG A 1 136 ? -7.684  -6.425  -61.816 1.00 18.27 ? 161 ARG A CB  1 
ATOM   1033 C  CG  . ARG A 1 136 ? -6.460  -6.390  -62.723 1.00 19.10 ? 161 ARG A CG  1 
ATOM   1034 C  CD  . ARG A 1 136 ? -6.803  -5.951  -64.135 1.00 20.74 ? 161 ARG A CD  1 
ATOM   1035 N  NE  . ARG A 1 136 ? -7.616  -6.960  -64.804 1.00 21.59 ? 161 ARG A NE  1 
ATOM   1036 C  CZ  . ARG A 1 136 ? -8.172  -6.819  -66.017 1.00 25.06 ? 161 ARG A CZ  1 
ATOM   1037 N  NH1 . ARG A 1 136 ? -7.978  -5.717  -66.723 1.00 24.26 ? 161 ARG A NH1 1 
ATOM   1038 N  NH2 . ARG A 1 136 ? -8.948  -7.761  -66.516 1.00 25.67 ? 161 ARG A NH2 1 
ATOM   1039 N  N   . LEU A 1 137 ? -7.673  -9.106  -59.825 1.00 18.24 ? 162 LEU A N   1 
ATOM   1040 C  CA  . LEU A 1 137 ? -7.466  -10.540 -59.886 1.00 17.54 ? 162 LEU A CA  1 
ATOM   1041 C  C   . LEU A 1 137 ? -8.521  -11.129 -60.808 1.00 19.42 ? 162 LEU A C   1 
ATOM   1042 O  O   . LEU A 1 137 ? -9.728  -10.857 -60.674 1.00 19.36 ? 162 LEU A O   1 
ATOM   1043 C  CB  . LEU A 1 137 ? -7.500  -11.167 -58.490 1.00 17.90 ? 162 LEU A CB  1 
ATOM   1044 C  CG  . LEU A 1 137 ? -7.006  -12.608 -58.396 1.00 17.59 ? 162 LEU A CG  1 
ATOM   1045 C  CD1 . LEU A 1 137 ? -5.498  -12.641 -58.647 1.00 18.00 ? 162 LEU A CD1 1 
ATOM   1046 C  CD2 . LEU A 1 137 ? -7.325  -13.251 -57.051 1.00 18.96 ? 162 LEU A CD2 1 
ATOM   1047 N  N   . ASP A 1 138 ? -8.034  -11.966 -61.729 1.00 18.86 ? 163 ASP A N   1 
ATOM   1048 C  CA  . ASP A 1 138 ? -8.832  -12.452 -62.834 1.00 21.44 ? 163 ASP A CA  1 
ATOM   1049 C  C   . ASP A 1 138 ? -8.883  -13.966 -62.859 1.00 23.26 ? 163 ASP A C   1 
ATOM   1050 O  O   . ASP A 1 138 ? -9.910  -14.504 -63.257 1.00 27.74 ? 163 ASP A O   1 
ATOM   1051 C  CB  . ASP A 1 138 ? -8.298  -11.910 -64.144 1.00 21.16 ? 163 ASP A CB  1 
ATOM   1052 C  CG  . ASP A 1 138 ? -8.419  -10.400 -64.210 1.00 21.28 ? 163 ASP A CG  1 
ATOM   1053 O  OD1 . ASP A 1 138 ? -9.497  -9.937  -64.597 1.00 23.90 ? 163 ASP A OD1 1 
ATOM   1054 O  OD2 . ASP A 1 138 ? -7.471  -9.718  -63.788 1.00 19.80 ? 163 ASP A OD2 1 
ATOM   1055 N  N   . ALA A 1 139 ? -7.777  -14.627 -62.496 1.00 20.48 ? 164 ALA A N   1 
ATOM   1056 C  CA  . ALA A 1 139 ? -7.743  -16.078 -62.516 1.00 20.27 ? 164 ALA A CA  1 
ATOM   1057 C  C   . ALA A 1 139 ? -7.456  -16.580 -61.113 1.00 20.21 ? 164 ALA A C   1 
ATOM   1058 O  O   . ALA A 1 139 ? -6.968  -15.843 -60.263 1.00 18.39 ? 164 ALA A O   1 
ATOM   1059 C  CB  . ALA A 1 139 ? -6.663  -16.557 -63.471 1.00 20.04 ? 164 ALA A CB  1 
ATOM   1060 N  N   . GLU A 1 140 ? -7.686  -17.869 -60.926 1.00 21.11 ? 165 GLU A N   1 
ATOM   1061 C  CA  . GLU A 1 140 ? -7.289  -18.501 -59.682 1.00 22.87 ? 165 GLU A CA  1 
ATOM   1062 C  C   . GLU A 1 140 ? -5.927  -19.168 -59.864 1.00 21.21 ? 165 GLU A C   1 
ATOM   1063 O  O   . GLU A 1 140 ? -5.227  -18.936 -60.858 1.00 19.43 ? 165 GLU A O   1 
ATOM   1064 C  CB  . GLU A 1 140 ? -8.464  -19.357 -59.224 1.00 26.11 ? 165 GLU A CB  1 
ATOM   1065 C  CG  . GLU A 1 140 ? -8.708  -20.607 -60.051 1.00 31.01 ? 165 GLU A CG  1 
ATOM   1066 C  CD  . GLU A 1 140 ? -9.881  -21.381 -59.477 1.00 35.91 ? 165 GLU A CD  1 
ATOM   1067 O  OE1 . GLU A 1 140 ? -10.374 -21.041 -58.366 1.00 39.45 ? 165 GLU A OE1 1 
ATOM   1068 O  OE2 . GLU A 1 140 ? -10.320 -22.285 -60.201 1.00 39.37 ? 165 GLU A OE2 1 
ATOM   1069 N  N   . GLU A 1 141 ? -5.532  -19.928 -58.840 1.00 19.89 ? 166 GLU A N   1 
ATOM   1070 C  CA  . GLU A 1 141 ? -4.257  -20.619 -58.827 1.00 19.10 ? 166 GLU A CA  1 
ATOM   1071 C  C   . GLU A 1 141 ? -4.422  -21.825 -59.739 1.00 18.79 ? 166 GLU A C   1 
ATOM   1072 O  O   . GLU A 1 141 ? -5.479  -22.464 -59.697 1.00 18.84 ? 166 GLU A O   1 
ATOM   1073 C  CB  . GLU A 1 141 ? -3.956  -21.186 -57.439 1.00 19.33 ? 166 GLU A CB  1 
ATOM   1074 C  CG  . GLU A 1 141 ? -3.598  -20.135 -56.396 1.00 19.30 ? 166 GLU A CG  1 
ATOM   1075 C  CD  . GLU A 1 141 ? -2.217  -19.544 -56.590 1.00 20.41 ? 166 GLU A CD  1 
ATOM   1076 O  OE1 . GLU A 1 141 ? -1.506  -19.894 -57.595 1.00 18.82 ? 166 GLU A OE1 1 
ATOM   1077 O  OE2 . GLU A 1 141 ? -1.875  -18.684 -55.757 1.00 21.47 ? 166 GLU A OE2 1 
ATOM   1078 N  N   . PRO A 1 142 ? -3.407  -22.219 -60.536 1.00 18.08 ? 167 PRO A N   1 
ATOM   1079 C  CA  . PRO A 1 142 ? -2.122  -21.508 -60.625 1.00 18.12 ? 167 PRO A CA  1 
ATOM   1080 C  C   . PRO A 1 142 ? -1.974  -20.446 -61.716 1.00 17.64 ? 167 PRO A C   1 
ATOM   1081 O  O   . PRO A 1 142 ? -0.908  -19.837 -61.824 1.00 17.68 ? 167 PRO A O   1 
ATOM   1082 C  CB  . PRO A 1 142 ? -1.206  -22.675 -60.887 1.00 18.91 ? 167 PRO A CB  1 
ATOM   1083 C  CG  . PRO A 1 142 ? -2.001  -23.519 -61.860 1.00 19.90 ? 167 PRO A CG  1 
ATOM   1084 C  CD  . PRO A 1 142 ? -3.410  -23.490 -61.285 1.00 19.97 ? 167 PRO A CD  1 
ATOM   1085 N  N   . GLU A 1 143 ? -3.030  -20.269 -62.528 1.00 19.02 ? 168 GLU A N   1 
ATOM   1086 C  CA  . GLU A 1 143 ? -2.978  -19.461 -63.736 1.00 20.24 ? 168 GLU A CA  1 
ATOM   1087 C  C   . GLU A 1 143 ? -2.586  -18.024 -63.414 1.00 18.08 ? 168 GLU A C   1 
ATOM   1088 O  O   . GLU A 1 143 ? -1.884  -17.396 -64.213 1.00 17.17 ? 168 GLU A O   1 
ATOM   1089 C  CB  . GLU A 1 143 ? -4.304  -19.524 -64.509 1.00 23.26 ? 168 GLU A CB  1 
ATOM   1090 C  CG  . GLU A 1 143 ? -4.491  -20.819 -65.304 1.00 27.55 ? 168 GLU A CG  1 
ATOM   1091 C  CD  . GLU A 1 143 ? -4.905  -22.032 -64.497 1.00 30.18 ? 168 GLU A CD  1 
ATOM   1092 O  OE1 . GLU A 1 143 ? -5.344  -21.875 -63.308 1.00 32.47 ? 168 GLU A OE1 1 
ATOM   1093 O  OE2 . GLU A 1 143 ? -4.756  -23.133 -65.088 1.00 36.10 ? 168 GLU A OE2 1 
ATOM   1094 N  N   . LEU A 1 144 ? -2.989  -17.524 -62.231 1.00 16.87 ? 169 LEU A N   1 
ATOM   1095 C  CA  . LEU A 1 144 ? -2.727  -16.157 -61.826 1.00 15.24 ? 169 LEU A CA  1 
ATOM   1096 C  C   . LEU A 1 144 ? -1.225  -15.856 -61.792 1.00 14.78 ? 169 LEU A C   1 
ATOM   1097 O  O   . LEU A 1 144 ? -0.857  -14.681 -61.814 1.00 14.29 ? 169 LEU A O   1 
ATOM   1098 C  CB  . LEU A 1 144 ? -3.435  -15.762 -60.524 1.00 16.10 ? 169 LEU A CB  1 
ATOM   1099 C  CG  . LEU A 1 144 ? -2.979  -16.451 -59.222 1.00 16.22 ? 169 LEU A CG  1 
ATOM   1100 C  CD1 . LEU A 1 144 ? -1.786  -15.774 -58.619 1.00 16.12 ? 169 LEU A CD1 1 
ATOM   1101 C  CD2 . LEU A 1 144 ? -4.107  -16.541 -58.190 1.00 16.73 ? 169 LEU A CD2 1 
ATOM   1102 N  N   . ASN A 1 145 ? -0.369  -16.877 -61.733 1.00 14.46 ? 170 ASN A N   1 
ATOM   1103 C  CA  . ASN A 1 145 ? 1.072   -16.652 -61.676 1.00 14.50 ? 170 ASN A CA  1 
ATOM   1104 C  C   . ASN A 1 145 ? 1.699   -16.644 -63.074 1.00 14.99 ? 170 ASN A C   1 
ATOM   1105 O  O   . ASN A 1 145 ? 2.912   -16.480 -63.186 1.00 15.33 ? 170 ASN A O   1 
ATOM   1106 C  CB  . ASN A 1 145 ? 1.783   -17.721 -60.848 1.00 15.48 ? 170 ASN A CB  1 
ATOM   1107 C  CG  . ASN A 1 145 ? 1.199   -17.848 -59.460 1.00 17.48 ? 170 ASN A CG  1 
ATOM   1108 O  OD1 . ASN A 1 145 ? 1.424   -16.974 -58.620 1.00 16.65 ? 170 ASN A OD1 1 
ATOM   1109 N  ND2 . ASN A 1 145 ? 0.445   -18.910 -59.222 1.00 17.40 ? 170 ASN A ND2 1 
ATOM   1110 N  N   . ARG A 1 146 ? 0.906   -16.916 -64.116 1.00 15.75 ? 171 ARG A N   1 
ATOM   1111 C  CA  . ARG A 1 146 ? 1.424   -17.370 -65.402 1.00 16.18 ? 171 ARG A CA  1 
ATOM   1112 C  C   . ARG A 1 146 ? 1.013   -16.466 -66.564 1.00 16.99 ? 171 ARG A C   1 
ATOM   1113 O  O   . ARG A 1 146 ? 1.105   -16.882 -67.720 1.00 17.79 ? 171 ARG A O   1 
ATOM   1114 C  CB  . ARG A 1 146 ? 0.943   -18.788 -65.717 1.00 17.58 ? 171 ARG A CB  1 
ATOM   1115 C  CG  . ARG A 1 146 ? 1.347   -19.752 -64.618 1.00 18.04 ? 171 ARG A CG  1 
ATOM   1116 C  CD  . ARG A 1 146 ? 0.800   -21.119 -64.888 1.00 19.78 ? 171 ARG A CD  1 
ATOM   1117 N  NE  . ARG A 1 146 ? 1.224   -22.037 -63.820 1.00 19.98 ? 171 ARG A NE  1 
ATOM   1118 C  CZ  . ARG A 1 146 ? 0.891   -23.326 -63.823 1.00 21.41 ? 171 ARG A CZ  1 
ATOM   1119 N  NH1 . ARG A 1 146 ? 0.070   -23.798 -64.733 1.00 21.33 ? 171 ARG A NH1 1 
ATOM   1120 N  NH2 . ARG A 1 146 ? 1.399   -24.130 -62.908 1.00 22.28 ? 171 ARG A NH2 1 
ATOM   1121 N  N   . ASP A 1 147 ? 0.480   -15.279 -66.289 1.00 16.26 ? 172 ASP A N   1 
ATOM   1122 C  CA  . ASP A 1 147 ? 0.004   -14.435 -67.377 1.00 16.53 ? 172 ASP A CA  1 
ATOM   1123 C  C   . ASP A 1 147 ? 1.213   -13.920 -68.152 1.00 16.64 ? 172 ASP A C   1 
ATOM   1124 O  O   . ASP A 1 147 ? 2.257   -13.666 -67.562 1.00 15.89 ? 172 ASP A O   1 
ATOM   1125 C  CB  . ASP A 1 147 ? -0.781  -13.215 -66.897 1.00 17.46 ? 172 ASP A CB  1 
ATOM   1126 C  CG  . ASP A 1 147 ? -2.128  -13.493 -66.251 1.00 18.96 ? 172 ASP A CG  1 
ATOM   1127 O  OD1 . ASP A 1 147 ? -3.087  -13.796 -66.976 1.00 23.91 ? 172 ASP A OD1 1 
ATOM   1128 O  OD2 . ASP A 1 147 ? -2.207  -13.432 -65.026 1.00 20.25 ? 172 ASP A OD2 1 
ATOM   1129 N  N   . PRO A 1 148 ? 1.089   -13.695 -69.471 1.00 17.10 ? 173 PRO A N   1 
ATOM   1130 C  CA  . PRO A 1 148 ? 2.197   -13.144 -70.245 1.00 18.85 ? 173 PRO A CA  1 
ATOM   1131 C  C   . PRO A 1 148 ? 2.557   -11.719 -69.790 1.00 17.44 ? 173 PRO A C   1 
ATOM   1132 O  O   . PRO A 1 148 ? 1.706   -10.968 -69.298 1.00 16.99 ? 173 PRO A O   1 
ATOM   1133 C  CB  . PRO A 1 148 ? 1.693   -13.193 -71.678 1.00 20.42 ? 173 PRO A CB  1 
ATOM   1134 C  CG  . PRO A 1 148 ? 0.430   -14.006 -71.660 1.00 20.53 ? 173 PRO A CG  1 
ATOM   1135 C  CD  . PRO A 1 148 ? -0.122  -13.947 -70.287 1.00 19.04 ? 173 PRO A CD  1 
ATOM   1136 N  N   . PRO A 1 149 ? 3.841   -11.325 -69.881 1.00 19.46 ? 174 PRO A N   1 
ATOM   1137 C  CA  . PRO A 1 149 ? 4.253   -9.940  -69.579 1.00 19.62 ? 174 PRO A CA  1 
ATOM   1138 C  C   . PRO A 1 149 ? 3.454   -8.939  -70.419 1.00 19.13 ? 174 PRO A C   1 
ATOM   1139 O  O   . PRO A 1 149 ? 3.172   -9.209  -71.587 1.00 18.99 ? 174 PRO A O   1 
ATOM   1140 C  CB  . PRO A 1 149 ? 5.718   -9.908  -69.956 1.00 22.90 ? 174 PRO A CB  1 
ATOM   1141 C  CG  . PRO A 1 149 ? 6.121   -11.363 -69.810 1.00 24.82 ? 174 PRO A CG  1 
ATOM   1142 C  CD  . PRO A 1 149 ? 4.954   -12.153 -70.360 1.00 21.37 ? 174 PRO A CD  1 
ATOM   1143 N  N   . GLY A 1 150 ? 3.057   -7.814  -69.790 1.00 18.45 ? 175 GLY A N   1 
ATOM   1144 C  CA  . GLY A 1 150 ? 2.246   -6.819  -70.459 1.00 20.39 ? 175 GLY A CA  1 
ATOM   1145 C  C   . GLY A 1 150 ? 0.752   -7.005  -70.200 1.00 20.04 ? 175 GLY A C   1 
ATOM   1146 O  O   . GLY A 1 150 ? -0.024  -6.069  -70.351 1.00 20.66 ? 175 GLY A O   1 
ATOM   1147 N  N   . ASP A 1 151 ? 0.302   -8.220  -69.877 1.00 20.74 ? 176 ASP A N   1 
ATOM   1148 C  CA  . ASP A 1 151 ? -1.120  -8.442  -69.636 1.00 21.10 ? 176 ASP A CA  1 
ATOM   1149 C  C   . ASP A 1 151 ? -1.513  -7.790  -68.300 1.00 19.15 ? 176 ASP A C   1 
ATOM   1150 O  O   . ASP A 1 151 ? -0.811  -7.976  -67.299 1.00 17.52 ? 176 ASP A O   1 
ATOM   1151 C  CB  . ASP A 1 151 ? -1.415  -9.928  -69.599 1.00 22.52 ? 176 ASP A CB  1 
ATOM   1152 C  CG  . ASP A 1 151 ? -2.870  -10.366 -69.666 1.00 26.86 ? 176 ASP A CG  1 
ATOM   1153 O  OD1 . ASP A 1 151 ? -3.782  -9.619  -69.239 1.00 23.10 ? 176 ASP A OD1 1 
ATOM   1154 O  OD2 . ASP A 1 151 ? -3.075  -11.517 -70.096 1.00 30.14 ? 176 ASP A OD2 1 
ATOM   1155 N  N   . GLU A 1 152 ? -2.648  -7.061  -68.262 1.00 19.21 ? 177 GLU A N   1 
ATOM   1156 C  CA  . GLU A 1 152 ? -3.079  -6.430  -67.009 1.00 17.80 ? 177 GLU A CA  1 
ATOM   1157 C  C   . GLU A 1 152 ? -3.740  -7.427  -66.052 1.00 17.70 ? 177 GLU A C   1 
ATOM   1158 O  O   . GLU A 1 152 ? -3.881  -7.145  -64.862 1.00 17.09 ? 177 GLU A O   1 
ATOM   1159 C  CB  . GLU A 1 152 ? -4.101  -5.331  -67.242 1.00 19.95 ? 177 GLU A CB  1 
ATOM   1160 C  CG  . GLU A 1 152 ? -3.493  -4.096  -67.887 1.00 20.43 ? 177 GLU A CG  1 
ATOM   1161 C  CD  . GLU A 1 152 ? -4.338  -2.838  -67.774 1.00 21.85 ? 177 GLU A CD  1 
ATOM   1162 O  OE1 . GLU A 1 152 ? -5.535  -2.900  -67.420 1.00 22.32 ? 177 GLU A OE1 1 
ATOM   1163 O  OE2 . GLU A 1 152 ? -3.736  -1.782  -68.034 1.00 22.24 ? 177 GLU A OE2 1 
ATOM   1164 N  N   . ARG A 1 153 ? -4.154  -8.591  -66.555 1.00 16.87 ? 178 ARG A N   1 
ATOM   1165 C  CA  . ARG A 1 153 ? -4.786  -9.569  -65.690 1.00 17.82 ? 178 ARG A CA  1 
ATOM   1166 C  C   . ARG A 1 153 ? -3.869  -9.969  -64.537 1.00 16.55 ? 178 ARG A C   1 
ATOM   1167 O  O   . ARG A 1 153 ? -2.665  -10.144 -64.706 1.00 15.89 ? 178 ARG A O   1 
ATOM   1168 C  CB  . ARG A 1 153 ? -5.225  -10.806 -66.476 1.00 20.55 ? 178 ARG A CB  1 
ATOM   1169 C  CG  . ARG A 1 153 ? -6.416  -10.566 -67.385 1.00 24.09 ? 178 ARG A CG  1 
ATOM   1170 C  CD  . ARG A 1 153 ? -6.636  -11.845 -68.202 1.00 26.84 ? 178 ARG A CD  1 
ATOM   1171 N  NE  . ARG A 1 153 ? -7.627  -11.622 -69.249 1.00 35.16 ? 178 ARG A NE  1 
ATOM   1172 C  CZ  . ARG A 1 153 ? -7.412  -10.969 -70.386 1.00 44.08 ? 178 ARG A CZ  1 
ATOM   1173 N  NH1 . ARG A 1 153 ? -6.256  -10.354 -70.614 1.00 47.84 ? 178 ARG A NH1 1 
ATOM   1174 N  NH2 . ARG A 1 153 ? -8.369  -10.911 -71.295 1.00 48.44 ? 178 ARG A NH2 1 
ATOM   1175 N  N   . ASP A 1 154 ? -4.466  -10.069 -63.338 1.00 16.44 ? 179 ASP A N   1 
ATOM   1176 C  CA  . ASP A 1 154 ? -3.795  -10.592 -62.156 1.00 16.70 ? 179 ASP A CA  1 
ATOM   1177 C  C   . ASP A 1 154 ? -2.650  -9.683  -61.724 1.00 15.95 ? 179 ASP A C   1 
ATOM   1178 O  O   . ASP A 1 154 ? -1.690  -10.170 -61.123 1.00 16.01 ? 179 ASP A O   1 
ATOM   1179 C  CB  . ASP A 1 154 ? -3.344  -12.021 -62.417 1.00 17.25 ? 179 ASP A CB  1 
ATOM   1180 C  CG  . ASP A 1 154 ? -4.476  -12.925 -62.859 1.00 17.76 ? 179 ASP A CG  1 
ATOM   1181 O  OD1 . ASP A 1 154 ? -5.542  -12.845 -62.216 1.00 19.16 ? 179 ASP A OD1 1 
ATOM   1182 O  OD2 . ASP A 1 154 ? -4.276  -13.701 -63.827 1.00 17.04 ? 179 ASP A OD2 1 
ATOM   1183 N  N   . THR A 1 155 ? -2.790  -8.361  -61.954 1.00 15.23 ? 180 THR A N   1 
ATOM   1184 C  CA  . THR A 1 155 ? -1.744  -7.432  -61.575 1.00 15.40 ? 180 THR A CA  1 
ATOM   1185 C  C   . THR A 1 155 ? -2.210  -6.453  -60.497 1.00 15.39 ? 180 THR A C   1 
ATOM   1186 O  O   . THR A 1 155 ? -3.412  -6.184  -60.312 1.00 17.18 ? 180 THR A O   1 
ATOM   1187 C  CB  . THR A 1 155 ? -1.214  -6.658  -62.787 1.00 14.85 ? 180 THR A CB  1 
ATOM   1188 O  OG1 . THR A 1 155 ? -2.274  -5.868  -63.311 1.00 16.16 ? 180 THR A OG1 1 
ATOM   1189 C  CG2 . THR A 1 155 ? -0.673  -7.598  -63.853 1.00 14.21 ? 180 THR A CG2 1 
ATOM   1190 N  N   . THR A 1 156 ? -1.200  -5.977  -59.762 1.00 14.44 ? 181 THR A N   1 
ATOM   1191 C  CA  . THR A 1 156 ? -1.320  -4.813  -58.881 1.00 15.55 ? 181 THR A CA  1 
ATOM   1192 C  C   . THR A 1 156 ? -0.184  -3.866  -59.274 1.00 15.68 ? 181 THR A C   1 
ATOM   1193 O  O   . THR A 1 156 ? 0.474   -4.072  -60.308 1.00 15.03 ? 181 THR A O   1 
ATOM   1194 C  CB  . THR A 1 156 ? -1.292  -5.282  -57.418 1.00 16.40 ? 181 THR A CB  1 
ATOM   1195 O  OG1 . THR A 1 156 ? -1.566  -4.199  -56.529 1.00 16.78 ? 181 THR A OG1 1 
ATOM   1196 C  CG2 . THR A 1 156 ? 0.053   -5.851  -56.995 1.00 16.10 ? 181 THR A CG2 1 
ATOM   1197 N  N   . THR A 1 157 ? 0.063   -2.839  -58.450 1.00 15.40 ? 182 THR A N   1 
ATOM   1198 C  CA  . THR A 1 157 ? 1.222   -1.979  -58.591 1.00 15.34 ? 182 THR A CA  1 
ATOM   1199 C  C   . THR A 1 157 ? 1.866   -1.905  -57.225 1.00 14.94 ? 182 THR A C   1 
ATOM   1200 O  O   . THR A 1 157 ? 1.187   -2.094  -56.214 1.00 15.29 ? 182 THR A O   1 
ATOM   1201 C  CB  . THR A 1 157 ? 0.880   -0.577  -59.106 1.00 15.69 ? 182 THR A CB  1 
ATOM   1202 O  OG1 . THR A 1 157 ? 0.146   0.094   -58.081 1.00 15.77 ? 182 THR A OG1 1 
ATOM   1203 C  CG2 . THR A 1 157 ? 0.096   -0.585  -60.410 1.00 16.26 ? 182 THR A CG2 1 
ATOM   1204 N  N   . PRO A 1 158 ? 3.190   -1.652  -57.148 1.00 14.90 ? 183 PRO A N   1 
ATOM   1205 C  CA  . PRO A 1 158 ? 3.806   -1.468  -55.838 1.00 14.43 ? 183 PRO A CA  1 
ATOM   1206 C  C   . PRO A 1 158 ? 3.058   -0.457  -54.964 1.00 16.11 ? 183 PRO A C   1 
ATOM   1207 O  O   . PRO A 1 158 ? 2.853   -0.675  -53.761 1.00 16.41 ? 183 PRO A O   1 
ATOM   1208 C  CB  . PRO A 1 158 ? 5.239   -1.052  -56.215 1.00 14.83 ? 183 PRO A CB  1 
ATOM   1209 C  CG  . PRO A 1 158 ? 5.490   -1.693  -57.555 1.00 14.05 ? 183 PRO A CG  1 
ATOM   1210 C  CD  . PRO A 1 158 ? 4.142   -1.576  -58.275 1.00 14.18 ? 183 PRO A CD  1 
ATOM   1211 N  N   . HIS A 1 159 ? 2.653   0.662   -55.576 1.00 16.48 ? 184 HIS A N   1 
ATOM   1212 C  CA  . HIS A 1 159 ? 1.919   1.716   -54.919 1.00 17.88 ? 184 HIS A CA  1 
ATOM   1213 C  C   . HIS A 1 159 ? 0.588   1.195   -54.361 1.00 18.86 ? 184 HIS A C   1 
ATOM   1214 O  O   . HIS A 1 159 ? 0.282   1.423   -53.190 1.00 17.38 ? 184 HIS A O   1 
ATOM   1215 C  CB  . HIS A 1 159 ? 1.705   2.858   -55.914 1.00 18.60 ? 184 HIS A CB  1 
ATOM   1216 C  CG  . HIS A 1 159 ? 1.116   4.103   -55.390 1.00 20.28 ? 184 HIS A CG  1 
ATOM   1217 N  ND1 . HIS A 1 159 ? 0.947   5.225   -56.176 1.00 21.62 ? 184 HIS A ND1 1 
ATOM   1218 C  CD2 . HIS A 1 159 ? 0.594   4.405   -54.187 1.00 21.04 ? 184 HIS A CD2 1 
ATOM   1219 C  CE1 . HIS A 1 159 ? 0.363   6.169   -55.441 1.00 22.94 ? 184 HIS A CE1 1 
ATOM   1220 N  NE2 . HIS A 1 159 ? 0.168   5.688   -54.236 1.00 21.46 ? 184 HIS A NE2 1 
ATOM   1221 N  N   . ALA A 1 160 ? -0.201  0.515   -55.207 1.00 17.91 ? 185 ALA A N   1 
ATOM   1222 C  CA  . ALA A 1 160 ? -1.525  0.070   -54.808 1.00 17.82 ? 185 ALA A CA  1 
ATOM   1223 C  C   . ALA A 1 160 ? -1.440  -0.941  -53.670 1.00 17.45 ? 185 ALA A C   1 
ATOM   1224 O  O   . ALA A 1 160 ? -2.186  -0.835  -52.703 1.00 17.75 ? 185 ALA A O   1 
ATOM   1225 C  CB  . ALA A 1 160 ? -2.282  -0.493  -55.984 1.00 17.33 ? 185 ALA A CB  1 
ATOM   1226 N  N   . ILE A 1 161 ? -0.572  -1.930  -53.796 1.00 16.99 ? 186 ILE A N   1 
ATOM   1227 C  CA  . ILE A 1 161 ? -0.571  -3.041  -52.853 1.00 18.52 ? 186 ILE A CA  1 
ATOM   1228 C  C   . ILE A 1 161 ? 0.046   -2.549  -51.539 1.00 18.06 ? 186 ILE A C   1 
ATOM   1229 O  O   . ILE A 1 161 ? -0.367  -3.002  -50.472 1.00 16.08 ? 186 ILE A O   1 
ATOM   1230 C  CB  . ILE A 1 161 ? 0.123   -4.307  -53.410 1.00 17.40 ? 186 ILE A CB  1 
ATOM   1231 C  CG1 . ILE A 1 161 ? -0.146  -5.556  -52.555 1.00 19.65 ? 186 ILE A CG1 1 
ATOM   1232 C  CG2 . ILE A 1 161 ? 1.627   -4.115  -53.577 1.00 16.75 ? 186 ILE A CG2 1 
ATOM   1233 C  CD1 . ILE A 1 161 ? -1.600  -5.914  -52.392 1.00 23.00 ? 186 ILE A CD1 1 
ATOM   1234 N  N   . ALA A 1 162 ? 0.991   -1.596  -51.615 1.00 18.42 ? 187 ALA A N   1 
ATOM   1235 C  CA  . ALA A 1 162 ? 1.503   -0.979  -50.383 1.00 19.80 ? 187 ALA A CA  1 
ATOM   1236 C  C   . ALA A 1 162 ? 0.363   -0.333  -49.595 1.00 20.46 ? 187 ALA A C   1 
ATOM   1237 O  O   . ALA A 1 162 ? 0.258   -0.529  -48.369 1.00 21.45 ? 187 ALA A O   1 
ATOM   1238 C  CB  . ALA A 1 162 ? 2.621   -0.003  -50.680 1.00 19.38 ? 187 ALA A CB  1 
ATOM   1239 N  N   . LEU A 1 163 ? -0.457  0.491   -50.252 1.00 19.85 ? 188 LEU A N   1 
ATOM   1240 C  CA  . LEU A 1 163 ? -1.558  1.152   -49.566 1.00 21.12 ? 188 LEU A CA  1 
ATOM   1241 C  C   . LEU A 1 163 ? -2.581  0.146   -49.035 1.00 21.07 ? 188 LEU A C   1 
ATOM   1242 O  O   . LEU A 1 163 ? -3.170  0.377   -47.991 1.00 21.14 ? 188 LEU A O   1 
ATOM   1243 C  CB  . LEU A 1 163 ? -2.193  2.252   -50.405 1.00 22.90 ? 188 LEU A CB  1 
ATOM   1244 C  CG  . LEU A 1 163 ? -1.241  3.392   -50.790 1.00 25.16 ? 188 LEU A CG  1 
ATOM   1245 C  CD1 . LEU A 1 163 ? -1.950  4.417   -51.628 1.00 25.40 ? 188 LEU A CD1 1 
ATOM   1246 C  CD2 . LEU A 1 163 ? -0.634  4.020   -49.524 1.00 27.98 ? 188 LEU A CD2 1 
ATOM   1247 N  N   . VAL A 1 164 ? -2.840  -0.938  -49.759 1.00 17.99 ? 189 VAL A N   1 
ATOM   1248 C  CA  . VAL A 1 164 ? -3.713  -1.994  -49.260 1.00 19.51 ? 189 VAL A CA  1 
ATOM   1249 C  C   . VAL A 1 164 ? -3.170  -2.583  -47.947 1.00 19.35 ? 189 VAL A C   1 
ATOM   1250 O  O   . VAL A 1 164 ? -3.900  -2.715  -46.960 1.00 20.25 ? 189 VAL A O   1 
ATOM   1251 C  CB  . VAL A 1 164 ? -3.863  -3.088  -50.336 1.00 19.14 ? 189 VAL A CB  1 
ATOM   1252 C  CG1 . VAL A 1 164 ? -4.341  -4.406  -49.745 1.00 18.07 ? 189 VAL A CG1 1 
ATOM   1253 C  CG2 . VAL A 1 164 ? -4.795  -2.611  -51.444 1.00 19.00 ? 189 VAL A CG2 1 
ATOM   1254 N  N   . LEU A 1 165 ? -1.884  -2.954  -47.962 1.00 19.11 ? 190 LEU A N   1 
ATOM   1255 C  CA  . LEU A 1 165 ? -1.285  -3.605  -46.812 1.00 19.76 ? 190 LEU A CA  1 
ATOM   1256 C  C   . LEU A 1 165 ? -1.271  -2.625  -45.646 1.00 20.51 ? 190 LEU A C   1 
ATOM   1257 O  O   . LEU A 1 165 ? -1.497  -2.999  -44.502 1.00 19.50 ? 190 LEU A O   1 
ATOM   1258 C  CB  . LEU A 1 165 ? 0.110   -4.133  -47.131 1.00 18.28 ? 190 LEU A CB  1 
ATOM   1259 C  CG  . LEU A 1 165 ? 0.755   -4.998  -46.043 1.00 18.82 ? 190 LEU A CG  1 
ATOM   1260 C  CD1 . LEU A 1 165 ? -0.020  -6.248  -45.726 1.00 19.96 ? 190 LEU A CD1 1 
ATOM   1261 C  CD2 . LEU A 1 165 ? 2.155   -5.374  -46.388 1.00 18.48 ? 190 LEU A CD2 1 
ATOM   1262 N  N   . GLN A 1 166 ? -1.043  -1.346  -45.961 1.00 20.65 ? 191 GLN A N   1 
ATOM   1263 C  CA  . GLN A 1 166 ? -1.027  -0.320  -44.947 1.00 22.06 ? 191 GLN A CA  1 
ATOM   1264 C  C   . GLN A 1 166 ? -2.385  -0.262  -44.246 1.00 22.59 ? 191 GLN A C   1 
ATOM   1265 O  O   . GLN A 1 166 ? -2.442  -0.156  -43.017 1.00 22.26 ? 191 GLN A O   1 
ATOM   1266 C  CB  . GLN A 1 166 ? -0.672  1.026   -45.571 1.00 23.31 ? 191 GLN A CB  1 
ATOM   1267 C  CG  . GLN A 1 166 ? -0.656  2.149   -44.540 1.00 26.98 ? 191 GLN A CG  1 
ATOM   1268 C  CD  . GLN A 1 166 ? -0.134  3.459   -45.078 1.00 33.06 ? 191 GLN A CD  1 
ATOM   1269 O  OE1 . GLN A 1 166 ? -0.901  4.329   -45.502 1.00 42.14 ? 191 GLN A OE1 1 
ATOM   1270 N  NE2 . GLN A 1 166 ? 1.179   3.611   -45.082 1.00 35.69 ? 191 GLN A NE2 1 
ATOM   1271 N  N   . GLN A 1 167 ? -3.479  -0.266  -45.020 1.00 23.07 ? 192 GLN A N   1 
ATOM   1272 C  CA  . GLN A 1 167 ? -4.805  -0.168  -44.421 1.00 25.09 ? 192 GLN A CA  1 
ATOM   1273 C  C   . GLN A 1 167 ? -5.105  -1.398  -43.558 1.00 22.87 ? 192 GLN A C   1 
ATOM   1274 O  O   . GLN A 1 167 ? -5.789  -1.283  -42.546 1.00 23.41 ? 192 GLN A O   1 
ATOM   1275 C  CB  . GLN A 1 167 ? -5.944  -0.105  -45.443 1.00 28.53 ? 192 GLN A CB  1 
ATOM   1276 C  CG  . GLN A 1 167 ? -5.909  1.078   -46.399 1.00 36.54 ? 192 GLN A CG  1 
ATOM   1277 C  CD  . GLN A 1 167 ? -5.692  2.392   -45.681 1.00 44.86 ? 192 GLN A CD  1 
ATOM   1278 O  OE1 . GLN A 1 167 ? -6.578  2.921   -45.002 1.00 53.80 ? 192 GLN A OE1 1 
ATOM   1279 N  NE2 . GLN A 1 167 ? -4.490  2.926   -45.827 1.00 53.74 ? 192 GLN A NE2 1 
ATOM   1280 N  N   . LEU A 1 168 ? -4.675  -2.573  -44.024 1.00 20.97 ? 193 LEU A N   1 
ATOM   1281 C  CA  . LEU A 1 168 ? -4.980  -3.830  -43.358 1.00 20.96 ? 193 LEU A CA  1 
ATOM   1282 C  C   . LEU A 1 168 ? -4.234  -3.955  -42.032 1.00 21.60 ? 193 LEU A C   1 
ATOM   1283 O  O   . LEU A 1 168 ? -4.798  -4.418  -41.041 1.00 22.99 ? 193 LEU A O   1 
ATOM   1284 C  CB  . LEU A 1 168 ? -4.616  -4.993  -44.287 1.00 20.10 ? 193 LEU A CB  1 
ATOM   1285 C  CG  . LEU A 1 168 ? -5.498  -5.104  -45.536 1.00 20.61 ? 193 LEU A CG  1 
ATOM   1286 C  CD1 . LEU A 1 168 ? -5.008  -6.254  -46.374 1.00 20.78 ? 193 LEU A CD1 1 
ATOM   1287 C  CD2 . LEU A 1 168 ? -6.964  -5.245  -45.166 1.00 21.09 ? 193 LEU A CD2 1 
ATOM   1288 N  N   . VAL A 1 169 ? -2.954  -3.582  -42.045 1.00 21.18 ? 194 VAL A N   1 
ATOM   1289 C  CA  . VAL A 1 169 ? -2.073  -3.831  -40.923 1.00 23.24 ? 194 VAL A CA  1 
ATOM   1290 C  C   . VAL A 1 169 ? -1.975  -2.604  -40.022 1.00 24.00 ? 194 VAL A C   1 
ATOM   1291 O  O   . VAL A 1 169 ? -1.973  -2.748  -38.808 1.00 27.08 ? 194 VAL A O   1 
ATOM   1292 C  CB  . VAL A 1 169 ? -0.692  -4.257  -41.427 1.00 21.82 ? 194 VAL A CB  1 
ATOM   1293 C  CG1 . VAL A 1 169 ? 0.290   -4.378  -40.280 1.00 23.57 ? 194 VAL A CG1 1 
ATOM   1294 C  CG2 . VAL A 1 169 ? -0.769  -5.570  -42.212 1.00 21.44 ? 194 VAL A CG2 1 
ATOM   1295 N  N   . LEU A 1 170 ? -1.912  -1.407  -40.607 1.00 23.49 ? 195 LEU A N   1 
ATOM   1296 C  CA  . LEU A 1 170 ? -1.700  -0.186  -39.842 1.00 23.91 ? 195 LEU A CA  1 
ATOM   1297 C  C   . LEU A 1 170 ? -2.980  0.620   -39.674 1.00 25.70 ? 195 LEU A C   1 
ATOM   1298 O  O   . LEU A 1 170 ? -3.056  1.404   -38.725 1.00 25.16 ? 195 LEU A O   1 
ATOM   1299 C  CB  . LEU A 1 170 ? -0.614  0.681   -40.464 1.00 24.68 ? 195 LEU A CB  1 
ATOM   1300 C  CG  . LEU A 1 170 ? 0.780   0.051   -40.534 1.00 24.14 ? 195 LEU A CG  1 
ATOM   1301 C  CD1 . LEU A 1 170 ? 1.789   0.997   -41.169 1.00 23.99 ? 195 LEU A CD1 1 
ATOM   1302 C  CD2 . LEU A 1 170 ? 1.225   -0.350  -39.154 1.00 25.17 ? 195 LEU A CD2 1 
ATOM   1303 N  N   . GLY A 1 171 ? -3.999  0.364   -40.505 1.00 24.48 ? 196 GLY A N   1 
ATOM   1304 C  CA  . GLY A 1 171 ? -5.268  1.056   -40.353 1.00 25.45 ? 196 GLY A CA  1 
ATOM   1305 C  C   . GLY A 1 171 ? -6.364  0.163   -39.783 1.00 24.95 ? 196 GLY A C   1 
ATOM   1306 O  O   . GLY A 1 171 ? -6.099  -0.894  -39.219 1.00 25.03 ? 196 GLY A O   1 
ATOM   1307 N  N   . ASN A 1 172 ? -7.611  0.587   -40.009 1.00 26.61 ? 197 ASN A N   1 
ATOM   1308 C  CA  . ASN A 1 172 ? -8.773  0.022   -39.332 1.00 26.97 ? 197 ASN A CA  1 
ATOM   1309 C  C   . ASN A 1 172 ? -9.733  -0.637  -40.318 1.00 27.06 ? 197 ASN A C   1 
ATOM   1310 O  O   . ASN A 1 172 ? -10.928 -0.688  -40.065 1.00 28.00 ? 197 ASN A O   1 
ATOM   1311 C  CB  . ASN A 1 172 ? -9.492  1.095   -38.535 1.00 29.07 ? 197 ASN A CB  1 
ATOM   1312 C  CG  . ASN A 1 172 ? -8.637  1.506   -37.366 1.00 29.05 ? 197 ASN A CG  1 
ATOM   1313 O  OD1 . ASN A 1 172 ? -8.202  0.636   -36.604 1.00 29.94 ? 197 ASN A OD1 1 
ATOM   1314 N  ND2 . ASN A 1 172 ? -8.289  2.773   -37.295 1.00 29.53 ? 197 ASN A ND2 1 
ATOM   1315 N  N   . ALA A 1 173 ? -9.206  -1.141  -41.444 1.00 26.77 ? 198 ALA A N   1 
ATOM   1316 C  CA  . ALA A 1 173 ? -9.998  -1.949  -42.354 1.00 26.04 ? 198 ALA A CA  1 
ATOM   1317 C  C   . ALA A 1 173 ? -10.614 -3.154  -41.643 1.00 25.60 ? 198 ALA A C   1 
ATOM   1318 O  O   . ALA A 1 173 ? -11.744 -3.532  -41.938 1.00 24.40 ? 198 ALA A O   1 
ATOM   1319 C  CB  . ALA A 1 173 ? -9.137  -2.394  -43.499 1.00 24.52 ? 198 ALA A CB  1 
ATOM   1320 N  N   . LEU A 1 174 ? -9.838  -3.766  -40.742 1.00 26.57 ? 199 LEU A N   1 
ATOM   1321 C  CA  . LEU A 1 174 ? -10.314 -4.852  -39.892 1.00 26.90 ? 199 LEU A CA  1 
ATOM   1322 C  C   . LEU A 1 174 ? -10.456 -4.394  -38.437 1.00 28.79 ? 199 LEU A C   1 
ATOM   1323 O  O   . LEU A 1 174 ? -9.647  -3.603  -37.951 1.00 28.06 ? 199 LEU A O   1 
ATOM   1324 C  CB  . LEU A 1 174 ? -9.302  -5.981  -39.973 1.00 24.62 ? 199 LEU A CB  1 
ATOM   1325 C  CG  . LEU A 1 174 ? -9.159  -6.643  -41.339 1.00 24.21 ? 199 LEU A CG  1 
ATOM   1326 C  CD1 . LEU A 1 174 ? -7.943  -7.532  -41.325 1.00 23.56 ? 199 LEU A CD1 1 
ATOM   1327 C  CD2 . LEU A 1 174 ? -10.432 -7.391  -41.719 1.00 25.32 ? 199 LEU A CD2 1 
ATOM   1328 N  N   . PRO A 1 175 ? -11.442 -4.930  -37.683 1.00 30.43 ? 200 PRO A N   1 
ATOM   1329 C  CA  . PRO A 1 175 ? -11.445 -4.773  -36.223 1.00 31.59 ? 200 PRO A CA  1 
ATOM   1330 C  C   . PRO A 1 175 ? -10.157 -5.364  -35.645 1.00 31.72 ? 200 PRO A C   1 
ATOM   1331 O  O   . PRO A 1 175 ? -9.561  -6.270  -36.233 1.00 30.69 ? 200 PRO A O   1 
ATOM   1332 C  CB  . PRO A 1 175 ? -12.700 -5.510  -35.715 1.00 33.75 ? 200 PRO A CB  1 
ATOM   1333 C  CG  . PRO A 1 175 ? -13.294 -6.208  -36.936 1.00 32.30 ? 200 PRO A CG  1 
ATOM   1334 C  CD  . PRO A 1 175 ? -12.541 -5.763  -38.192 1.00 30.55 ? 200 PRO A CD  1 
ATOM   1335 N  N   . PRO A 1 176 ? -9.669  -4.873  -34.484 1.00 33.90 ? 201 PRO A N   1 
ATOM   1336 C  CA  . PRO A 1 176 ? -8.354  -5.274  -33.957 1.00 33.44 ? 201 PRO A CA  1 
ATOM   1337 C  C   . PRO A 1 176 ? -8.117  -6.782  -33.813 1.00 32.58 ? 201 PRO A C   1 
ATOM   1338 O  O   . PRO A 1 176 ? -6.992  -7.259  -33.999 1.00 31.92 ? 201 PRO A O   1 
ATOM   1339 C  CB  . PRO A 1 176 ? -8.318  -4.581  -32.581 1.00 34.90 ? 201 PRO A CB  1 
ATOM   1340 C  CG  . PRO A 1 176 ? -9.263  -3.414  -32.734 1.00 35.73 ? 201 PRO A CG  1 
ATOM   1341 C  CD  . PRO A 1 176 ? -10.381 -3.927  -33.602 1.00 34.69 ? 201 PRO A CD  1 
ATOM   1342 N  N   . ASP A 1 177 ? -9.172  -7.524  -33.457 1.00 34.11 ? 202 ASP A N   1 
ATOM   1343 C  CA  . ASP A 1 177 ? -9.047  -8.961  -33.237 1.00 36.39 ? 202 ASP A CA  1 
ATOM   1344 C  C   . ASP A 1 177 ? -8.760  -9.666  -34.568 1.00 33.96 ? 202 ASP A C   1 
ATOM   1345 O  O   . ASP A 1 177 ? -7.918  -10.560 -34.623 1.00 34.26 ? 202 ASP A O   1 
ATOM   1346 C  CB  . ASP A 1 177 ? -10.212 -9.539  -32.442 1.00 40.40 ? 202 ASP A CB  1 
ATOM   1347 C  CG  . ASP A 1 177 ? -11.626 -9.280  -32.947 1.00 45.50 ? 202 ASP A CG  1 
ATOM   1348 O  OD1 . ASP A 1 177 ? -11.782 -8.548  -33.967 1.00 48.39 ? 202 ASP A OD1 1 
ATOM   1349 O  OD2 . ASP A 1 177 ? -12.571 -9.782  -32.286 1.00 45.79 ? 202 ASP A OD2 1 
ATOM   1350 N  N   . LYS A 1 178 ? -9.445  -9.238  -35.635 1.00 29.89 ? 203 LYS A N   1 
ATOM   1351 C  CA  . LYS A 1 178 ? -9.210  -9.788  -36.961 1.00 26.83 ? 203 LYS A CA  1 
ATOM   1352 C  C   . LYS A 1 178 ? -7.864  -9.307  -37.504 1.00 26.47 ? 203 LYS A C   1 
ATOM   1353 O  O   . LYS A 1 178 ? -7.121  -10.085 -38.086 1.00 24.00 ? 203 LYS A O   1 
ATOM   1354 C  CB  . LYS A 1 178 ? -10.404 -9.484  -37.866 1.00 26.48 ? 203 LYS A CB  1 
ATOM   1355 C  CG  . LYS A 1 178 ? -11.715 -10.108 -37.427 1.00 26.95 ? 203 LYS A CG  1 
ATOM   1356 C  CD  . LYS A 1 178 ? -12.866 -9.917  -38.402 1.00 27.22 ? 203 LYS A CD  1 
ATOM   1357 C  CE  . LYS A 1 178 ? -14.147 -10.476 -37.907 1.00 29.30 ? 203 LYS A CE  1 
ATOM   1358 N  NZ  . LYS A 1 178 ? -15.274 -10.229 -38.823 1.00 29.36 ? 203 LYS A NZ  1 
ATOM   1359 N  N   . ARG A 1 179 ? -7.523  -8.031  -37.274 1.00 26.39 ? 204 ARG A N   1 
ATOM   1360 C  CA  . ARG A 1 179 ? -6.252  -7.481  -37.720 1.00 26.04 ? 204 ARG A CA  1 
ATOM   1361 C  C   . ARG A 1 179 ? -5.090  -8.287  -37.154 1.00 26.26 ? 204 ARG A C   1 
ATOM   1362 O  O   . ARG A 1 179 ? -4.105  -8.533  -37.830 1.00 25.01 ? 204 ARG A O   1 
ATOM   1363 C  CB  . ARG A 1 179 ? -6.126  -6.008  -37.319 1.00 26.26 ? 204 ARG A CB  1 
ATOM   1364 C  CG  . ARG A 1 179 ? -4.812  -5.354  -37.731 1.00 25.78 ? 204 ARG A CG  1 
ATOM   1365 C  CD  . ARG A 1 179 ? -4.898  -3.857  -37.555 1.00 26.73 ? 204 ARG A CD  1 
ATOM   1366 N  NE  . ARG A 1 179 ? -5.123  -3.600  -36.133 1.00 29.78 ? 204 ARG A NE  1 
ATOM   1367 C  CZ  . ARG A 1 179 ? -5.463  -2.463  -35.582 1.00 31.93 ? 204 ARG A CZ  1 
ATOM   1368 N  NH1 . ARG A 1 179 ? -5.806  -1.433  -36.337 1.00 33.73 ? 204 ARG A NH1 1 
ATOM   1369 N  NH2 . ARG A 1 179 ? -5.457  -2.377  -34.266 1.00 32.95 ? 204 ARG A NH2 1 
ATOM   1370 N  N   . ALA A 1 180 ? -5.198  -8.675  -35.879 1.00 28.21 ? 205 ALA A N   1 
ATOM   1371 C  CA  . ALA A 1 180 ? -4.130  -9.387  -35.215 1.00 27.67 ? 205 ALA A CA  1 
ATOM   1372 C  C   . ALA A 1 180 ? -3.962  -10.789 -35.795 1.00 26.45 ? 205 ALA A C   1 
ATOM   1373 O  O   . ALA A 1 180 ? -2.841  -11.270 -35.867 1.00 25.17 ? 205 ALA A O   1 
ATOM   1374 C  CB  . ALA A 1 180 ? -4.407  -9.443  -33.733 1.00 30.06 ? 205 ALA A CB  1 
ATOM   1375 N  N   . LEU A 1 181 ? -5.051  -11.442 -36.224 1.00 26.08 ? 206 LEU A N   1 
ATOM   1376 C  CA  . LEU A 1 181 ? -4.919  -12.765 -36.832 1.00 26.09 ? 206 LEU A CA  1 
ATOM   1377 C  C   . LEU A 1 181 ? -4.087  -12.653 -38.104 1.00 24.65 ? 206 LEU A C   1 
ATOM   1378 O  O   . LEU A 1 181 ? -3.160  -13.434 -38.284 1.00 23.81 ? 206 LEU A O   1 
ATOM   1379 C  CB  . LEU A 1 181 ? -6.262  -13.422 -37.123 1.00 26.00 ? 206 LEU A CB  1 
ATOM   1380 C  CG  . LEU A 1 181 ? -7.071  -13.836 -35.891 1.00 28.25 ? 206 LEU A CG  1 
ATOM   1381 C  CD1 . LEU A 1 181 ? -8.513  -14.164 -36.200 1.00 28.16 ? 206 LEU A CD1 1 
ATOM   1382 C  CD2 . LEU A 1 181 ? -6.358  -15.017 -35.233 1.00 29.15 ? 206 LEU A CD2 1 
ATOM   1383 N  N   . LEU A 1 182 ? -4.446  -11.690 -38.965 1.00 24.01 ? 207 LEU A N   1 
ATOM   1384 C  CA  . LEU A 1 182 ? -3.735  -11.472 -40.219 1.00 23.19 ? 207 LEU A CA  1 
ATOM   1385 C  C   . LEU A 1 182 ? -2.252  -11.235 -39.926 1.00 23.15 ? 207 LEU A C   1 
ATOM   1386 O  O   . LEU A 1 182 ? -1.379  -11.842 -40.526 1.00 20.67 ? 207 LEU A O   1 
ATOM   1387 C  CB  . LEU A 1 182 ? -4.336  -10.274 -40.960 1.00 22.54 ? 207 LEU A CB  1 
ATOM   1388 C  CG  . LEU A 1 182 ? -3.586  -9.829  -42.218 1.00 22.80 ? 207 LEU A CG  1 
ATOM   1389 C  CD1 . LEU A 1 182 ? -3.600  -10.923 -43.260 1.00 23.73 ? 207 LEU A CD1 1 
ATOM   1390 C  CD2 . LEU A 1 182 ? -4.156  -8.552  -42.814 1.00 24.09 ? 207 LEU A CD2 1 
ATOM   1391 N  N   . THR A 1 183 ? -1.988  -10.293 -39.020 1.00 24.43 ? 208 THR A N   1 
ATOM   1392 C  CA  . THR A 1 183 ? -0.646  -9.872  -38.667 1.00 25.39 ? 208 THR A CA  1 
ATOM   1393 C  C   . THR A 1 183 ? 0.179   -11.050 -38.137 1.00 24.26 ? 208 THR A C   1 
ATOM   1394 O  O   . THR A 1 183 ? 1.347   -11.202 -38.501 1.00 22.30 ? 208 THR A O   1 
ATOM   1395 C  CB  . THR A 1 183 ? -0.787  -8.764  -37.614 1.00 31.36 ? 208 THR A CB  1 
ATOM   1396 O  OG1 . THR A 1 183 ? -1.221  -7.595  -38.316 1.00 32.61 ? 208 THR A OG1 1 
ATOM   1397 C  CG2 . THR A 1 183 ? 0.529   -8.403  -36.958 1.00 34.23 ? 208 THR A CG2 1 
ATOM   1398 N  N   A ASP A 1 184 ? -0.438  -11.853 -37.254 0.50 23.23 ? 209 ASP A N   1 
ATOM   1399 N  N   B ASP A 1 184 ? -0.436  -11.859 -37.261 0.50 24.45 ? 209 ASP A N   1 
ATOM   1400 C  CA  A ASP A 1 184 ? 0.207   -13.005 -36.640 0.50 23.04 ? 209 ASP A CA  1 
ATOM   1401 C  CA  B ASP A 1 184 ? 0.235   -12.995 -36.645 0.50 25.13 ? 209 ASP A CA  1 
ATOM   1402 C  C   A ASP A 1 184 ? 0.592   -14.035 -37.698 0.50 23.08 ? 209 ASP A C   1 
ATOM   1403 C  C   B ASP A 1 184 ? 0.592   -14.042 -37.696 0.50 24.24 ? 209 ASP A C   1 
ATOM   1404 O  O   A ASP A 1 184 ? 1.690   -14.592 -37.666 0.50 23.46 ? 209 ASP A O   1 
ATOM   1405 O  O   B ASP A 1 184 ? 1.689   -14.599 -37.669 0.50 24.49 ? 209 ASP A O   1 
ATOM   1406 C  CB  A ASP A 1 184 ? -0.699  -13.644 -35.602 0.50 23.19 ? 209 ASP A CB  1 
ATOM   1407 C  CB  B ASP A 1 184 ? -0.583  -13.528 -35.482 0.50 26.93 ? 209 ASP A CB  1 
ATOM   1408 C  CG  A ASP A 1 184 ? -0.154  -14.925 -34.995 0.50 22.87 ? 209 ASP A CG  1 
ATOM   1409 C  CG  B ASP A 1 184 ? -0.585  -12.609 -34.266 0.50 28.78 ? 209 ASP A CG  1 
ATOM   1410 O  OD1 A ASP A 1 184 ? 0.789   -14.813 -34.203 0.50 23.26 ? 209 ASP A OD1 1 
ATOM   1411 O  OD1 B ASP A 1 184 ? 0.192   -11.617 -34.276 0.50 28.40 ? 209 ASP A OD1 1 
ATOM   1412 O  OD2 A ASP A 1 184 ? -0.645  -16.012 -35.376 0.50 21.78 ? 209 ASP A OD2 1 
ATOM   1413 O  OD2 B ASP A 1 184 ? -1.370  -12.881 -33.328 0.50 29.43 ? 209 ASP A OD2 1 
ATOM   1414 N  N   . TRP A 1 185 ? -0.338  -14.322 -38.616 1.00 22.48 ? 210 TRP A N   1 
ATOM   1415 C  CA  . TRP A 1 185 ? -0.072  -15.303 -39.667 1.00 22.07 ? 210 TRP A CA  1 
ATOM   1416 C  C   . TRP A 1 185 ? 1.102   -14.826 -40.531 1.00 21.71 ? 210 TRP A C   1 
ATOM   1417 O  O   . TRP A 1 185 ? 1.979   -15.602 -40.856 1.00 22.06 ? 210 TRP A O   1 
ATOM   1418 C  CB  . TRP A 1 185 ? -1.319  -15.581 -40.514 1.00 20.39 ? 210 TRP A CB  1 
ATOM   1419 C  CG  . TRP A 1 185 ? -2.323  -16.513 -39.899 1.00 20.92 ? 210 TRP A CG  1 
ATOM   1420 C  CD1 . TRP A 1 185 ? -2.075  -17.641 -39.183 1.00 21.58 ? 210 TRP A CD1 1 
ATOM   1421 C  CD2 . TRP A 1 185 ? -3.761  -16.378 -39.957 1.00 20.77 ? 210 TRP A CD2 1 
ATOM   1422 N  NE1 . TRP A 1 185 ? -3.257  -18.225 -38.793 1.00 22.14 ? 210 TRP A NE1 1 
ATOM   1423 C  CE2 . TRP A 1 185 ? -4.305  -17.481 -39.263 1.00 21.80 ? 210 TRP A CE2 1 
ATOM   1424 C  CE3 . TRP A 1 185 ? -4.631  -15.451 -40.530 1.00 20.86 ? 210 TRP A CE3 1 
ATOM   1425 C  CZ2 . TRP A 1 185 ? -5.681  -17.659 -39.106 1.00 22.82 ? 210 TRP A CZ2 1 
ATOM   1426 C  CZ3 . TRP A 1 185 ? -5.995  -15.630 -40.369 1.00 21.77 ? 210 TRP A CZ3 1 
ATOM   1427 C  CH2 . TRP A 1 185 ? -6.510  -16.721 -39.681 1.00 22.08 ? 210 TRP A CH2 1 
ATOM   1428 N  N   . MET A 1 186 ? 1.157   -13.524 -40.834 1.00 21.88 ? 211 MET A N   1 
ATOM   1429 C  CA  . MET A 1 186 ? 2.265   -12.987 -41.605 1.00 23.25 ? 211 MET A CA  1 
ATOM   1430 C  C   . MET A 1 186 ? 3.561   -13.072 -40.794 1.00 24.58 ? 211 MET A C   1 
ATOM   1431 O  O   . MET A 1 186 ? 4.612   -13.395 -41.347 1.00 26.03 ? 211 MET A O   1 
ATOM   1432 C  CB  . MET A 1 186 ? 1.957   -11.548 -42.033 1.00 22.43 ? 211 MET A CB  1 
ATOM   1433 C  CG  . MET A 1 186 ? 0.808   -11.455 -43.027 1.00 22.57 ? 211 MET A CG  1 
ATOM   1434 S  SD  . MET A 1 186 ? 0.432   -9.771  -43.553 1.00 21.86 ? 211 MET A SD  1 
ATOM   1435 C  CE  . MET A 1 186 ? 1.953   -9.491  -44.469 1.00 22.22 ? 211 MET A CE  1 
ATOM   1436 N  N   . ALA A 1 187 ? 3.482   -12.811 -39.489 1.00 27.93 ? 212 ALA A N   1 
ATOM   1437 C  CA  . ALA A 1 187 ? 4.652   -12.882 -38.624 1.00 28.42 ? 212 ALA A CA  1 
ATOM   1438 C  C   . ALA A 1 187 ? 5.256   -14.283 -38.601 1.00 30.00 ? 212 ALA A C   1 
ATOM   1439 O  O   . ALA A 1 187 ? 6.460   -14.427 -38.451 1.00 30.67 ? 212 ALA A O   1 
ATOM   1440 C  CB  . ALA A 1 187 ? 4.285   -12.391 -37.253 1.00 30.47 ? 212 ALA A CB  1 
ATOM   1441 N  N   . ARG A 1 188 ? 4.431   -15.320 -38.763 1.00 29.15 ? 213 ARG A N   1 
ATOM   1442 C  CA  . ARG A 1 188 ? 4.863   -16.707 -38.673 1.00 30.41 ? 213 ARG A CA  1 
ATOM   1443 C  C   . ARG A 1 188 ? 5.111   -17.337 -40.043 1.00 30.01 ? 213 ARG A C   1 
ATOM   1444 O  O   . ARG A 1 188 ? 5.221   -18.559 -40.166 1.00 29.40 ? 213 ARG A O   1 
ATOM   1445 C  CB  . ARG A 1 188 ? 3.802   -17.496 -37.892 1.00 31.30 ? 213 ARG A CB  1 
ATOM   1446 C  CG  . ARG A 1 188 ? 3.800   -17.041 -36.442 1.00 34.28 ? 213 ARG A CG  1 
ATOM   1447 C  CD  . ARG A 1 188 ? 3.097   -18.005 -35.524 1.00 37.97 ? 213 ARG A CD  1 
ATOM   1448 N  NE  . ARG A 1 188 ? 1.670   -18.081 -35.791 1.00 39.93 ? 213 ARG A NE  1 
ATOM   1449 C  CZ  . ARG A 1 188 ? 0.954   -19.189 -35.857 1.00 43.62 ? 213 ARG A CZ  1 
ATOM   1450 N  NH1 . ARG A 1 188 ? 1.518   -20.367 -35.717 1.00 44.04 ? 213 ARG A NH1 1 
ATOM   1451 N  NH2 . ARG A 1 188 ? -0.350  -19.108 -36.059 1.00 45.97 ? 213 ARG A NH2 1 
ATOM   1452 N  N   A ASN A 1 189 ? 5.244   -16.507 -41.072 0.50 26.55 ? 214 ASN A N   1 
ATOM   1453 N  N   B ASN A 1 189 ? 5.153   -16.506 -41.091 0.50 29.00 ? 214 ASN A N   1 
ATOM   1454 C  CA  A ASN A 1 189 ? 5.333   -17.005 -42.433 0.50 25.04 ? 214 ASN A CA  1 
ATOM   1455 C  CA  B ASN A 1 189 ? 5.718   -16.964 -42.347 0.50 29.47 ? 214 ASN A CA  1 
ATOM   1456 C  C   A ASN A 1 189 ? 6.619   -17.820 -42.647 0.50 23.46 ? 214 ASN A C   1 
ATOM   1457 C  C   B ASN A 1 189 ? 7.206   -16.645 -42.301 0.50 28.09 ? 214 ASN A C   1 
ATOM   1458 O  O   A ASN A 1 189 ? 7.642   -17.554 -42.032 0.50 22.11 ? 214 ASN A O   1 
ATOM   1459 O  O   B ASN A 1 189 ? 7.575   -15.528 -41.936 0.50 25.82 ? 214 ASN A O   1 
ATOM   1460 C  CB  A ASN A 1 189 ? 5.149   -15.804 -43.352 0.50 23.71 ? 214 ASN A CB  1 
ATOM   1461 C  CB  B ASN A 1 189 ? 5.151   -16.286 -43.595 0.50 29.14 ? 214 ASN A CB  1 
ATOM   1462 C  CG  A ASN A 1 189 ? 5.159   -16.182 -44.800 0.50 22.60 ? 214 ASN A CG  1 
ATOM   1463 C  CG  B ASN A 1 189 ? 6.190   -15.393 -44.234 0.50 30.54 ? 214 ASN A CG  1 
ATOM   1464 O  OD1 A ASN A 1 189 ? 5.245   -17.371 -45.123 0.50 23.39 ? 214 ASN A OD1 1 
ATOM   1465 O  OD1 B ASN A 1 189 ? 6.971   -15.851 -45.076 0.50 29.89 ? 214 ASN A OD1 1 
ATOM   1466 N  ND2 A ASN A 1 189 ? 5.120   -15.180 -45.664 0.50 23.39 ? 214 ASN A ND2 1 
ATOM   1467 N  ND2 B ASN A 1 189 ? 6.298   -14.156 -43.768 0.50 31.62 ? 214 ASN A ND2 1 
ATOM   1468 N  N   A THR A 1 190 ? 6.602   -18.779 -43.590 0.50 23.65 ? 215 THR A N   1 
ATOM   1469 N  N   B THR A 1 190 ? 8.030   -17.622 -42.698 0.50 27.27 ? 215 THR A N   1 
ATOM   1470 C  CA  A THR A 1 190 ? 7.760   -19.644 -43.799 0.50 23.06 ? 215 THR A CA  1 
ATOM   1471 C  CA  B THR A 1 190 ? 9.454   -17.408 -42.886 0.50 28.55 ? 215 THR A CA  1 
ATOM   1472 C  C   A THR A 1 190 ? 8.511   -19.367 -45.112 0.50 22.43 ? 215 THR A C   1 
ATOM   1473 C  C   B THR A 1 190 ? 9.782   -17.603 -44.361 0.50 26.76 ? 215 THR A C   1 
ATOM   1474 O  O   A THR A 1 190 ? 9.402   -20.150 -45.435 0.50 23.32 ? 215 THR A O   1 
ATOM   1475 O  O   B THR A 1 190 ? 10.954  -17.569 -44.749 0.50 28.29 ? 215 THR A O   1 
ATOM   1476 C  CB  A THR A 1 190 ? 7.364   -21.127 -43.704 0.50 23.95 ? 215 THR A CB  1 
ATOM   1477 C  CB  B THR A 1 190 ? 10.213  -18.403 -42.004 0.50 31.52 ? 215 THR A CB  1 
ATOM   1478 O  OG1 A THR A 1 190 ? 6.744   -21.519 -44.931 0.50 21.59 ? 215 THR A OG1 1 
ATOM   1479 O  OG1 B THR A 1 190 ? 9.806   -19.682 -42.479 0.50 33.25 ? 215 THR A OG1 1 
ATOM   1480 C  CG2 A THR A 1 190 ? 6.514   -21.443 -42.481 0.50 24.11 ? 215 THR A CG2 1 
ATOM   1481 C  CG2 B THR A 1 190 ? 9.831   -18.324 -40.538 0.50 33.08 ? 215 THR A CG2 1 
ATOM   1482 N  N   A THR A 1 191 ? 8.240   -18.265 -45.848 0.50 21.66 ? 216 THR A N   1 
ATOM   1483 N  N   B THR A 1 191 ? 8.730   -17.879 -45.163 0.50 25.83 ? 216 THR A N   1 
ATOM   1484 C  CA  A THR A 1 191 ? 8.861   -18.096 -47.164 0.50 21.37 ? 216 THR A CA  1 
ATOM   1485 C  CA  B THR A 1 191 ? 8.857   -18.069 -46.606 0.50 23.06 ? 216 THR A CA  1 
ATOM   1486 C  C   A THR A 1 191 ? 9.591   -16.760 -47.367 0.50 20.27 ? 216 THR A C   1 
ATOM   1487 C  C   B THR A 1 191 ? 9.640   -16.886 -47.174 0.50 21.42 ? 216 THR A C   1 
ATOM   1488 O  O   A THR A 1 191 ? 10.158  -16.590 -48.449 0.50 18.03 ? 216 THR A O   1 
ATOM   1489 O  O   B THR A 1 191 ? 10.308  -16.968 -48.198 0.50 19.56 ? 216 THR A O   1 
ATOM   1490 C  CB  A THR A 1 191 ? 7.861   -18.259 -48.320 0.50 21.16 ? 216 THR A CB  1 
ATOM   1491 C  CB  B THR A 1 191 ? 7.485   -18.185 -47.286 0.50 22.26 ? 216 THR A CB  1 
ATOM   1492 O  OG1 A THR A 1 191 ? 7.000   -17.133 -48.307 0.50 22.64 ? 216 THR A OG1 1 
ATOM   1493 O  OG1 B THR A 1 191 ? 6.908   -16.895 -47.398 0.50 22.75 ? 216 THR A OG1 1 
ATOM   1494 C  CG2 A THR A 1 191 ? 6.992   -19.502 -48.244 0.50 21.94 ? 216 THR A CG2 1 
ATOM   1495 C  CG2 B THR A 1 191 ? 6.471   -19.007 -46.518 0.50 22.01 ? 216 THR A CG2 1 
ATOM   1496 N  N   . GLY A 1 192 ? 9.563   -15.784 -46.431 1.00 20.16 ? 217 GLY A N   1 
ATOM   1497 C  CA  . GLY A 1 192 ? 10.084  -14.475 -46.801 1.00 19.81 ? 217 GLY A CA  1 
ATOM   1498 C  C   . GLY A 1 192 ? 11.453  -14.107 -46.228 1.00 20.10 ? 217 GLY A C   1 
ATOM   1499 O  O   . GLY A 1 192 ? 11.848  -12.959 -46.348 1.00 20.94 ? 217 GLY A O   1 
ATOM   1500 N  N   . ALA A 1 193 ? 12.171  -15.048 -45.618 1.00 19.79 ? 218 ALA A N   1 
ATOM   1501 C  CA  . ALA A 1 193 ? 13.402  -14.736 -44.898 1.00 21.41 ? 218 ALA A CA  1 
ATOM   1502 C  C   . ALA A 1 193 ? 14.478  -14.085 -45.780 1.00 21.53 ? 218 ALA A C   1 
ATOM   1503 O  O   . ALA A 1 193 ? 15.293  -13.324 -45.260 1.00 21.10 ? 218 ALA A O   1 
ATOM   1504 C  CB  . ALA A 1 193 ? 13.913  -15.974 -44.209 1.00 23.75 ? 218 ALA A CB  1 
ATOM   1505 N  N   . LYS A 1 194 ? 14.499  -14.360 -47.098 1.00 22.68 ? 219 LYS A N   1 
ATOM   1506 C  CA  . LYS A 1 194 ? 15.577  -13.878 -47.962 1.00 23.53 ? 219 LYS A CA  1 
ATOM   1507 C  C   . LYS A 1 194 ? 15.169  -12.657 -48.792 1.00 21.59 ? 219 LYS A C   1 
ATOM   1508 O  O   . LYS A 1 194 ? 15.902  -12.281 -49.715 1.00 20.23 ? 219 LYS A O   1 
ATOM   1509 C  CB  . LYS A 1 194 ? 16.042  -14.957 -48.936 1.00 27.42 ? 219 LYS A CB  1 
ATOM   1510 C  CG  . LYS A 1 194 ? 16.532  -16.227 -48.260 1.00 33.33 ? 219 LYS A CG  1 
ATOM   1511 C  CD  . LYS A 1 194 ? 17.663  -15.941 -47.286 1.00 40.34 ? 219 LYS A CD  1 
ATOM   1512 C  CE  . LYS A 1 194 ? 18.969  -15.656 -47.996 1.00 45.70 ? 219 LYS A CE  1 
ATOM   1513 N  NZ  . LYS A 1 194 ? 20.077  -16.373 -47.352 1.00 51.53 ? 219 LYS A NZ  1 
ATOM   1514 N  N   . ARG A 1 195 ? 14.012  -12.047 -48.471 1.00 19.31 ? 220 ARG A N   1 
ATOM   1515 C  CA  . ARG A 1 195 ? 13.482  -10.934 -49.249 1.00 18.21 ? 220 ARG A CA  1 
ATOM   1516 C  C   . ARG A 1 195 ? 13.606  -9.637  -48.443 1.00 17.66 ? 220 ARG A C   1 
ATOM   1517 O  O   . ARG A 1 195 ? 14.712  -9.269  -48.050 1.00 18.03 ? 220 ARG A O   1 
ATOM   1518 C  CB  . ARG A 1 195 ? 12.116  -11.289 -49.845 1.00 17.45 ? 220 ARG A CB  1 
ATOM   1519 C  CG  . ARG A 1 195 ? 12.253  -12.414 -50.868 1.00 17.39 ? 220 ARG A CG  1 
ATOM   1520 C  CD  . ARG A 1 195 ? 10.939  -12.862 -51.473 1.00 17.23 ? 220 ARG A CD  1 
ATOM   1521 N  NE  . ARG A 1 195 ? 11.123  -14.076 -52.275 1.00 18.78 ? 220 ARG A NE  1 
ATOM   1522 C  CZ  . ARG A 1 195 ? 10.303  -14.550 -53.215 1.00 18.59 ? 220 ARG A CZ  1 
ATOM   1523 N  NH1 . ARG A 1 195 ? 9.293   -13.833 -53.654 1.00 19.97 ? 220 ARG A NH1 1 
ATOM   1524 N  NH2 . ARG A 1 195 ? 10.523  -15.748 -53.748 1.00 19.23 ? 220 ARG A NH2 1 
ATOM   1525 N  N   . ILE A 1 196 ? 12.497  -8.937  -48.199 1.00 17.31 ? 221 ILE A N   1 
ATOM   1526 C  CA  . ILE A 1 196 ? 12.577  -7.653  -47.508 1.00 18.04 ? 221 ILE A CA  1 
ATOM   1527 C  C   . ILE A 1 196 ? 13.230  -7.824  -46.136 1.00 18.56 ? 221 ILE A C   1 
ATOM   1528 O  O   . ILE A 1 196 ? 14.065  -7.016  -45.744 1.00 18.49 ? 221 ILE A O   1 
ATOM   1529 C  CB  . ILE A 1 196 ? 11.197  -6.988  -47.404 1.00 18.92 ? 221 ILE A CB  1 
ATOM   1530 C  CG1 . ILE A 1 196 ? 10.681  -6.571  -48.762 1.00 18.40 ? 221 ILE A CG1 1 
ATOM   1531 C  CG2 . ILE A 1 196 ? 11.229  -5.822  -46.403 1.00 19.57 ? 221 ILE A CG2 1 
ATOM   1532 C  CD1 . ILE A 1 196 ? 9.206   -6.203  -48.756 1.00 17.31 ? 221 ILE A CD1 1 
ATOM   1533 N  N   . ARG A 1 197 ? 12.918  -8.928  -45.429 1.00 17.71 ? 222 ARG A N   1 
ATOM   1534 C  CA  . ARG A 1 197 ? 13.535  -9.262  -44.157 1.00 18.53 ? 222 ARG A CA  1 
ATOM   1535 C  C   . ARG A 1 197 ? 15.059  -9.186  -44.240 1.00 19.69 ? 222 ARG A C   1 
ATOM   1536 O  O   . ARG A 1 197 ? 15.695  -8.735  -43.287 1.00 19.94 ? 222 ARG A O   1 
ATOM   1537 C  CB  . ARG A 1 197 ? 13.115  -10.672 -43.703 1.00 18.49 ? 222 ARG A CB  1 
ATOM   1538 C  CG  . ARG A 1 197 ? 13.804  -11.234 -42.467 1.00 20.27 ? 222 ARG A CG  1 
ATOM   1539 C  CD  . ARG A 1 197 ? 13.545  -10.508 -41.149 1.00 20.54 ? 222 ARG A CD  1 
ATOM   1540 N  NE  . ARG A 1 197 ? 14.272  -9.242  -40.983 1.00 21.37 ? 222 ARG A NE  1 
ATOM   1541 C  CZ  . ARG A 1 197 ? 14.142  -8.433  -39.926 1.00 23.28 ? 222 ARG A CZ  1 
ATOM   1542 N  NH1 . ARG A 1 197 ? 13.288  -8.750  -38.966 1.00 23.72 ? 222 ARG A NH1 1 
ATOM   1543 N  NH2 . ARG A 1 197 ? 14.847  -7.318  -39.805 1.00 23.99 ? 222 ARG A NH2 1 
ATOM   1544 N  N   . ALA A 1 198 ? 15.636  -9.645  -45.365 1.00 19.29 ? 223 ALA A N   1 
ATOM   1545 C  CA  . ALA A 1 198 ? 17.087  -9.680  -45.525 1.00 20.85 ? 223 ALA A CA  1 
ATOM   1546 C  C   . ALA A 1 198 ? 17.699  -8.292  -45.772 1.00 21.15 ? 223 ALA A C   1 
ATOM   1547 O  O   . ALA A 1 198 ? 18.930  -8.158  -45.710 1.00 22.93 ? 223 ALA A O   1 
ATOM   1548 C  CB  . ALA A 1 198 ? 17.474  -10.620 -46.656 1.00 21.11 ? 223 ALA A CB  1 
ATOM   1549 N  N   . GLY A 1 199 ? 16.879  -7.264  -46.025 1.00 20.03 ? 224 GLY A N   1 
ATOM   1550 C  CA  . GLY A 1 199 ? 17.390  -5.907  -46.185 1.00 21.22 ? 224 GLY A CA  1 
ATOM   1551 C  C   . GLY A 1 199 ? 17.303  -5.020  -44.941 1.00 22.65 ? 224 GLY A C   1 
ATOM   1552 O  O   . GLY A 1 199 ? 17.822  -3.895  -44.958 1.00 23.99 ? 224 GLY A O   1 
ATOM   1553 N  N   . PHE A 1 200 ? 16.686  -5.513  -43.847 1.00 22.82 ? 225 PHE A N   1 
ATOM   1554 C  CA  . PHE A 1 200 ? 16.495  -4.692  -42.649 1.00 22.50 ? 225 PHE A CA  1 
ATOM   1555 C  C   . PHE A 1 200 ? 17.284  -5.239  -41.473 1.00 23.32 ? 225 PHE A C   1 
ATOM   1556 O  O   . PHE A 1 200 ? 17.253  -6.445  -41.263 1.00 23.68 ? 225 PHE A O   1 
ATOM   1557 C  CB  . PHE A 1 200 ? 15.009  -4.634  -42.271 1.00 21.56 ? 225 PHE A CB  1 
ATOM   1558 C  CG  . PHE A 1 200 ? 14.292  -3.556  -43.059 1.00 20.75 ? 225 PHE A CG  1 
ATOM   1559 C  CD1 . PHE A 1 200 ? 14.218  -2.259  -42.567 1.00 21.12 ? 225 PHE A CD1 1 
ATOM   1560 C  CD2 . PHE A 1 200 ? 13.777  -3.816  -44.320 1.00 19.97 ? 225 PHE A CD2 1 
ATOM   1561 C  CE1 . PHE A 1 200 ? 13.605  -1.258  -43.292 1.00 20.97 ? 225 PHE A CE1 1 
ATOM   1562 C  CE2 . PHE A 1 200 ? 13.175  -2.808  -45.045 1.00 20.13 ? 225 PHE A CE2 1 
ATOM   1563 C  CZ  . PHE A 1 200 ? 13.093  -1.532  -44.535 1.00 20.46 ? 225 PHE A CZ  1 
ATOM   1564 N  N   . PRO A 1 201 ? 17.928  -4.399  -40.624 1.00 24.89 ? 226 PRO A N   1 
ATOM   1565 C  CA  . PRO A 1 201 ? 18.666  -4.888  -39.445 1.00 25.71 ? 226 PRO A CA  1 
ATOM   1566 C  C   . PRO A 1 201 ? 17.778  -5.685  -38.502 1.00 25.56 ? 226 PRO A C   1 
ATOM   1567 O  O   . PRO A 1 201 ? 16.553  -5.526  -38.509 1.00 24.20 ? 226 PRO A O   1 
ATOM   1568 C  CB  . PRO A 1 201 ? 19.229  -3.628  -38.766 1.00 27.49 ? 226 PRO A CB  1 
ATOM   1569 C  CG  . PRO A 1 201 ? 19.234  -2.606  -39.873 1.00 27.38 ? 226 PRO A CG  1 
ATOM   1570 C  CD  . PRO A 1 201 ? 18.045  -2.936  -40.750 1.00 25.29 ? 226 PRO A CD  1 
ATOM   1571 N  N   . ALA A 1 202 ? 18.420  -6.552  -37.715 1.00 26.54 ? 227 ALA A N   1 
ATOM   1572 C  CA  . ALA A 1 202 ? 17.723  -7.524  -36.897 1.00 28.25 ? 227 ALA A CA  1 
ATOM   1573 C  C   . ALA A 1 202 ? 16.842  -6.856  -35.830 1.00 28.57 ? 227 ALA A C   1 
ATOM   1574 O  O   . ALA A 1 202 ? 15.845  -7.433  -35.425 1.00 29.29 ? 227 ALA A O   1 
ATOM   1575 C  CB  . ALA A 1 202 ? 18.730  -8.481  -36.295 1.00 30.50 ? 227 ALA A CB  1 
ATOM   1576 N  N   . ASP A 1 203 ? 17.156  -5.636  -35.405 1.00 28.51 ? 228 ASP A N   1 
ATOM   1577 C  CA  . ASP A 1 203 ? 16.317  -4.967  -34.425 1.00 29.46 ? 228 ASP A CA  1 
ATOM   1578 C  C   . ASP A 1 203 ? 15.112  -4.254  -35.040 1.00 28.45 ? 228 ASP A C   1 
ATOM   1579 O  O   . ASP A 1 203 ? 14.410  -3.552  -34.310 1.00 29.78 ? 228 ASP A O   1 
ATOM   1580 C  CB  . ASP A 1 203 ? 17.115  -4.020  -33.553 1.00 31.03 ? 228 ASP A CB  1 
ATOM   1581 C  CG  . ASP A 1 203 ? 17.890  -2.937  -34.275 1.00 30.91 ? 228 ASP A CG  1 
ATOM   1582 O  OD1 . ASP A 1 203 ? 17.896  -2.925  -35.497 1.00 29.94 ? 228 ASP A OD1 1 
ATOM   1583 O  OD2 . ASP A 1 203 ? 18.448  -2.097  -33.585 1.00 32.46 ? 228 ASP A OD2 1 
ATOM   1584 N  N   . TRP A 1 204 ? 14.891  -4.406  -36.356 1.00 27.67 ? 229 TRP A N   1 
ATOM   1585 C  CA  . TRP A 1 204 ? 13.647  -4.010  -37.003 1.00 25.92 ? 229 TRP A CA  1 
ATOM   1586 C  C   . TRP A 1 204 ? 12.731  -5.221  -37.121 1.00 26.37 ? 229 TRP A C   1 
ATOM   1587 O  O   . TRP A 1 204 ? 13.149  -6.274  -37.596 1.00 27.54 ? 229 TRP A O   1 
ATOM   1588 C  CB  . TRP A 1 204 ? 13.910  -3.436  -38.406 1.00 25.27 ? 229 TRP A CB  1 
ATOM   1589 C  CG  . TRP A 1 204 ? 14.564  -2.086  -38.439 1.00 25.40 ? 229 TRP A CG  1 
ATOM   1590 C  CD1 . TRP A 1 204 ? 15.811  -1.777  -37.991 1.00 27.17 ? 229 TRP A CD1 1 
ATOM   1591 C  CD2 . TRP A 1 204 ? 14.049  -0.879  -39.043 1.00 25.62 ? 229 TRP A CD2 1 
ATOM   1592 N  NE1 . TRP A 1 204 ? 16.088  -0.458  -38.219 1.00 27.35 ? 229 TRP A NE1 1 
ATOM   1593 C  CE2 . TRP A 1 204 ? 15.033  0.118   -38.869 1.00 26.68 ? 229 TRP A CE2 1 
ATOM   1594 C  CE3 . TRP A 1 204 ? 12.850  -0.544  -39.695 1.00 24.52 ? 229 TRP A CE3 1 
ATOM   1595 C  CZ2 . TRP A 1 204 ? 14.849  1.430   -39.306 1.00 27.49 ? 229 TRP A CZ2 1 
ATOM   1596 C  CZ3 . TRP A 1 204 ? 12.671  0.760   -40.110 1.00 25.04 ? 229 TRP A CZ3 1 
ATOM   1597 C  CH2 . TRP A 1 204 ? 13.662  1.716   -39.952 1.00 26.04 ? 229 TRP A CH2 1 
ATOM   1598 N  N   . LYS A 1 205 ? 11.459  -5.039  -36.772 1.00 26.08 ? 230 LYS A N   1 
ATOM   1599 C  CA  . LYS A 1 205 ? 10.462  -6.077  -36.970 1.00 27.31 ? 230 LYS A CA  1 
ATOM   1600 C  C   . LYS A 1 205 ? 9.958   -6.031  -38.402 1.00 25.26 ? 230 LYS A C   1 
ATOM   1601 O  O   . LYS A 1 205 ? 9.841   -4.960  -38.984 1.00 23.37 ? 230 LYS A O   1 
ATOM   1602 C  CB  . LYS A 1 205 ? 9.310   -5.875  -35.976 1.00 31.48 ? 230 LYS A CB  1 
ATOM   1603 C  CG  . LYS A 1 205 ? 8.168   -6.870  -36.058 1.00 35.16 ? 230 LYS A CG  1 
ATOM   1604 C  CD  . LYS A 1 205 ? 7.062   -6.563  -35.045 1.00 43.23 ? 230 LYS A CD  1 
ATOM   1605 C  CE  . LYS A 1 205 ? 7.574   -6.186  -33.681 1.00 49.83 ? 230 LYS A CE  1 
ATOM   1606 N  NZ  . LYS A 1 205 ? 6.526   -5.535  -32.877 1.00 59.23 ? 230 LYS A NZ  1 
ATOM   1607 N  N   . VAL A 1 206 ? 9.746   -7.221  -38.981 1.00 23.92 ? 231 VAL A N   1 
ATOM   1608 C  CA  . VAL A 1 206 ? 9.301   -7.357  -40.359 1.00 22.09 ? 231 VAL A CA  1 
ATOM   1609 C  C   . VAL A 1 206 ? 8.232   -8.434  -40.413 1.00 21.77 ? 231 VAL A C   1 
ATOM   1610 O  O   . VAL A 1 206 ? 8.444   -9.522  -39.879 1.00 25.49 ? 231 VAL A O   1 
ATOM   1611 C  CB  . VAL A 1 206 ? 10.455  -7.702  -41.317 1.00 20.88 ? 231 VAL A CB  1 
ATOM   1612 C  CG1 . VAL A 1 206 ? 9.946   -7.918  -42.734 1.00 19.78 ? 231 VAL A CG1 1 
ATOM   1613 C  CG2 . VAL A 1 206 ? 11.561  -6.652  -41.293 1.00 20.78 ? 231 VAL A CG2 1 
ATOM   1614 N  N   . ILE A 1 207 ? 7.095   -8.129  -41.046 1.00 20.61 ? 232 ILE A N   1 
ATOM   1615 C  CA  . ILE A 1 207 ? 6.131   -9.161  -41.404 1.00 20.48 ? 232 ILE A CA  1 
ATOM   1616 C  C   . ILE A 1 207 ? 5.853   -9.011  -42.892 1.00 19.24 ? 232 ILE A C   1 
ATOM   1617 O  O   . ILE A 1 207 ? 5.813   -7.906  -43.396 1.00 18.72 ? 232 ILE A O   1 
ATOM   1618 C  CB  . ILE A 1 207 ? 4.822   -9.083  -40.588 1.00 21.38 ? 232 ILE A CB  1 
ATOM   1619 C  CG1 . ILE A 1 207 ? 3.974   -7.861  -40.988 1.00 21.96 ? 232 ILE A CG1 1 
ATOM   1620 C  CG2 . ILE A 1 207 ? 5.135   -9.132  -39.093 1.00 22.77 ? 232 ILE A CG2 1 
ATOM   1621 C  CD1 . ILE A 1 207 ? 2.720   -7.664  -40.154 1.00 21.91 ? 232 ILE A CD1 1 
ATOM   1622 N  N   . ASP A 1 208 ? 5.631   -10.123 -43.576 1.00 19.20 ? 233 ASP A N   1 
ATOM   1623 C  CA  . ASP A 1 208 ? 5.586   -10.060 -45.026 1.00 17.90 ? 233 ASP A CA  1 
ATOM   1624 C  C   . ASP A 1 208 ? 4.741   -11.186 -45.610 1.00 18.42 ? 233 ASP A C   1 
ATOM   1625 O  O   . ASP A 1 208 ? 4.438   -12.202 -44.970 1.00 17.70 ? 233 ASP A O   1 
ATOM   1626 C  CB  . ASP A 1 208 ? 7.006   -10.083 -45.597 1.00 17.00 ? 233 ASP A CB  1 
ATOM   1627 C  CG  . ASP A 1 208 ? 7.596   -11.478 -45.720 1.00 17.91 ? 233 ASP A CG  1 
ATOM   1628 O  OD1 . ASP A 1 208 ? 7.710   -12.128 -44.665 1.00 17.98 ? 233 ASP A OD1 1 
ATOM   1629 O  OD2 . ASP A 1 208 ? 7.852   -11.946 -46.876 1.00 16.76 ? 233 ASP A OD2 1 
ATOM   1630 N  N   . LYS A 1 209 ? 4.420   -10.984 -46.887 1.00 17.96 ? 234 LYS A N   1 
ATOM   1631 C  CA  . LYS A 1 209 ? 3.915   -12.045 -47.748 1.00 17.43 ? 234 LYS A CA  1 
ATOM   1632 C  C   . LYS A 1 209 ? 4.638   -11.953 -49.087 1.00 17.33 ? 234 LYS A C   1 
ATOM   1633 O  O   . LYS A 1 209 ? 4.650   -10.878 -49.712 1.00 17.27 ? 234 LYS A O   1 
ATOM   1634 C  CB  . LYS A 1 209 ? 2.395   -11.941 -47.963 1.00 17.74 ? 234 LYS A CB  1 
ATOM   1635 C  CG  . LYS A 1 209 ? 1.823   -12.980 -48.928 1.00 17.65 ? 234 LYS A CG  1 
ATOM   1636 C  CD  . LYS A 1 209 ? 1.738   -14.345 -48.273 1.00 18.51 ? 234 LYS A CD  1 
ATOM   1637 C  CE  . LYS A 1 209 ? 1.522   -15.483 -49.216 1.00 19.92 ? 234 LYS A CE  1 
ATOM   1638 N  NZ  . LYS A 1 209 ? 2.803   -15.954 -49.692 1.00 23.69 ? 234 LYS A NZ  1 
ATOM   1639 N  N   . THR A 1 210 ? 5.177   -13.106 -49.514 1.00 16.92 ? 235 THR A N   1 
ATOM   1640 C  CA  . THR A 1 210 ? 5.928   -13.195 -50.760 1.00 18.86 ? 235 THR A CA  1 
ATOM   1641 C  C   . THR A 1 210 ? 5.001   -13.577 -51.914 1.00 18.47 ? 235 THR A C   1 
ATOM   1642 O  O   . THR A 1 210 ? 3.879   -14.075 -51.739 1.00 18.72 ? 235 THR A O   1 
ATOM   1643 C  CB  . THR A 1 210 ? 7.040   -14.230 -50.628 1.00 18.93 ? 235 THR A CB  1 
ATOM   1644 O  OG1 . THR A 1 210 ? 6.458   -15.522 -50.492 1.00 19.82 ? 235 THR A OG1 1 
ATOM   1645 C  CG2 . THR A 1 210 ? 7.944   -14.010 -49.441 1.00 19.72 ? 235 THR A CG2 1 
ATOM   1646 N  N   . GLY A 1 211 ? 5.497   -13.326 -53.127 1.00 17.16 ? 236 GLY A N   1 
ATOM   1647 C  CA  . GLY A 1 211 ? 4.942   -13.937 -54.311 1.00 16.40 ? 236 GLY A CA  1 
ATOM   1648 C  C   . GLY A 1 211 ? 6.045   -14.280 -55.309 1.00 16.59 ? 236 GLY A C   1 
ATOM   1649 O  O   . GLY A 1 211 ? 7.054   -13.575 -55.395 1.00 16.43 ? 236 GLY A O   1 
ATOM   1650 N  N   . THR A 1 212 ? 5.844   -15.393 -56.029 1.00 16.97 ? 237 THR A N   1 
ATOM   1651 C  CA  . THR A 1 212 ? 6.802   -15.885 -56.996 1.00 17.32 ? 237 THR A CA  1 
ATOM   1652 C  C   . THR A 1 212 ? 5.999   -16.467 -58.153 1.00 18.17 ? 237 THR A C   1 
ATOM   1653 O  O   . THR A 1 212 ? 4.926   -17.033 -57.925 1.00 17.79 ? 237 THR A O   1 
ATOM   1654 C  CB  . THR A 1 212 ? 7.704   -16.962 -56.386 1.00 18.31 ? 237 THR A CB  1 
ATOM   1655 O  OG1 . THR A 1 212 ? 8.273   -16.479 -55.179 1.00 17.60 ? 237 THR A OG1 1 
ATOM   1656 C  CG2 . THR A 1 212 ? 8.856   -17.351 -57.287 1.00 19.45 ? 237 THR A CG2 1 
ATOM   1657 N  N   . GLY A 1 213 ? 6.505   -16.306 -59.377 1.00 17.29 ? 238 GLY A N   1 
ATOM   1658 C  CA  . GLY A 1 213 ? 5.754   -16.797 -60.526 1.00 17.13 ? 238 GLY A CA  1 
ATOM   1659 C  C   . GLY A 1 213 ? 6.641   -16.982 -61.740 1.00 16.87 ? 238 GLY A C   1 
ATOM   1660 O  O   . GLY A 1 213 ? 7.846   -16.874 -61.642 1.00 17.03 ? 238 GLY A O   1 
ATOM   1661 N  N   . ASP A 1 214 ? 5.996   -17.232 -62.887 1.00 16.54 ? 240 ASP A N   1 
ATOM   1662 C  CA  . ASP A 1 214 ? 6.696   -17.338 -64.160 1.00 16.88 ? 240 ASP A CA  1 
ATOM   1663 C  C   . ASP A 1 214 ? 7.329   -15.992 -64.545 1.00 15.44 ? 240 ASP A C   1 
ATOM   1664 O  O   . ASP A 1 214 ? 7.168   -14.979 -63.879 1.00 14.95 ? 240 ASP A O   1 
ATOM   1665 C  CB  . ASP A 1 214 ? 5.775   -17.907 -65.224 1.00 17.09 ? 240 ASP A CB  1 
ATOM   1666 C  CG  . ASP A 1 214 ? 5.474   -19.390 -65.096 1.00 20.18 ? 240 ASP A CG  1 
ATOM   1667 O  OD1 . ASP A 1 214 ? 5.817   -19.986 -64.031 1.00 20.79 ? 240 ASP A OD1 1 
ATOM   1668 O  OD2 . ASP A 1 214 ? 4.842   -19.900 -66.021 1.00 19.68 ? 240 ASP A OD2 1 
ATOM   1669 N  N   . TYR A 1 215 ? 8.114   -16.004 -65.632 1.00 15.98 ? 241 TYR A N   1 
ATOM   1670 C  CA  . TYR A 1 215 ? 8.810   -14.824 -66.102 1.00 15.82 ? 241 TYR A CA  1 
ATOM   1671 C  C   . TYR A 1 215 ? 9.727   -14.231 -65.026 1.00 16.33 ? 241 TYR A C   1 
ATOM   1672 O  O   . TYR A 1 215 ? 10.017  -13.037 -65.049 1.00 16.12 ? 241 TYR A O   1 
ATOM   1673 C  CB  . TYR A 1 215 ? 7.790   -13.828 -66.655 1.00 16.57 ? 241 TYR A CB  1 
ATOM   1674 C  CG  . TYR A 1 215 ? 7.047   -14.409 -67.843 1.00 16.70 ? 241 TYR A CG  1 
ATOM   1675 C  CD1 . TYR A 1 215 ? 7.628   -14.430 -69.109 1.00 17.69 ? 241 TYR A CD1 1 
ATOM   1676 C  CD2 . TYR A 1 215 ? 5.795   -15.002 -67.679 1.00 18.07 ? 241 TYR A CD2 1 
ATOM   1677 C  CE1 . TYR A 1 215 ? 6.985   -15.017 -70.183 1.00 18.85 ? 241 TYR A CE1 1 
ATOM   1678 C  CE2 . TYR A 1 215 ? 5.137   -15.584 -68.745 1.00 18.58 ? 241 TYR A CE2 1 
ATOM   1679 C  CZ  . TYR A 1 215 ? 5.734   -15.584 -69.999 1.00 19.72 ? 241 TYR A CZ  1 
ATOM   1680 O  OH  . TYR A 1 215 ? 5.102   -16.115 -71.064 1.00 19.39 ? 241 TYR A OH  1 
ATOM   1681 N  N   . GLY A 1 216 ? 10.291  -15.086 -64.184 1.00 16.77 ? 242 GLY A N   1 
ATOM   1682 C  CA  . GLY A 1 216 ? 11.196  -14.650 -63.119 1.00 17.55 ? 242 GLY A CA  1 
ATOM   1683 C  C   . GLY A 1 216 ? 10.552  -13.685 -62.121 1.00 17.02 ? 242 GLY A C   1 
ATOM   1684 O  O   . GLY A 1 216 ? 11.245  -12.848 -61.539 1.00 18.08 ? 242 GLY A O   1 
ATOM   1685 N  N   . ARG A 1 217 ? 9.232   -13.811 -61.914 1.00 15.82 ? 243 ARG A N   1 
ATOM   1686 C  CA  . ARG A 1 217 ? 8.509   -12.951 -61.000 1.00 15.28 ? 243 ARG A CA  1 
ATOM   1687 C  C   . ARG A 1 217 ? 8.859   -13.260 -59.546 1.00 15.95 ? 243 ARG A C   1 
ATOM   1688 O  O   . ARG A 1 217 ? 8.828   -14.411 -59.113 1.00 15.71 ? 243 ARG A O   1 
ATOM   1689 C  CB  . ARG A 1 217 ? 6.992   -13.123 -61.191 1.00 15.83 ? 243 ARG A CB  1 
ATOM   1690 C  CG  . ARG A 1 217 ? 6.506   -12.398 -62.440 1.00 15.66 ? 243 ARG A CG  1 
ATOM   1691 C  CD  . ARG A 1 217 ? 5.132   -12.784 -62.883 1.00 16.48 ? 243 ARG A CD  1 
ATOM   1692 N  NE  . ARG A 1 217 ? 4.762   -12.116 -64.132 1.00 16.08 ? 243 ARG A NE  1 
ATOM   1693 C  CZ  . ARG A 1 217 ? 4.074   -12.643 -65.124 1.00 17.61 ? 243 ARG A CZ  1 
ATOM   1694 N  NH1 . ARG A 1 217 ? 3.540   -13.855 -65.017 1.00 17.88 ? 243 ARG A NH1 1 
ATOM   1695 N  NH2 . ARG A 1 217 ? 3.970   -11.950 -66.250 1.00 19.53 ? 243 ARG A NH2 1 
ATOM   1696 N  N   . ALA A 1 218 ? 9.199   -12.208 -58.788 1.00 14.85 ? 244 ALA A N   1 
ATOM   1697 C  CA  . ALA A 1 218 ? 9.472   -12.364 -57.379 1.00 15.19 ? 244 ALA A CA  1 
ATOM   1698 C  C   . ALA A 1 218 ? 9.079   -11.057 -56.701 1.00 14.28 ? 244 ALA A C   1 
ATOM   1699 O  O   . ALA A 1 218 ? 9.554   -9.995  -57.096 1.00 15.50 ? 244 ALA A O   1 
ATOM   1700 C  CB  . ALA A 1 218 ? 10.922  -12.733 -57.123 1.00 15.58 ? 244 ALA A CB  1 
ATOM   1701 N  N   . ASN A 1 219 ? 8.149   -11.155 -55.751 1.00 14.26 ? 245 ASN A N   1 
ATOM   1702 C  CA  . ASN A 1 219 ? 7.590   -10.001 -55.060 1.00 15.12 ? 245 ASN A CA  1 
ATOM   1703 C  C   . ASN A 1 219 ? 7.700   -10.221 -53.556 1.00 15.60 ? 245 ASN A C   1 
ATOM   1704 O  O   . ASN A 1 219 ? 7.827   -11.364 -53.085 1.00 14.43 ? 245 ASN A O   1 
ATOM   1705 C  CB  . ASN A 1 219 ? 6.109   -9.784  -55.353 1.00 15.24 ? 245 ASN A CB  1 
ATOM   1706 C  CG  . ASN A 1 219 ? 5.791   -9.739  -56.836 1.00 16.54 ? 245 ASN A CG  1 
ATOM   1707 O  OD1 . ASN A 1 219 ? 6.568   -9.207  -57.650 1.00 14.84 ? 245 ASN A OD1 1 
ATOM   1708 N  ND2 . ASN A 1 219 ? 4.654   -10.313 -57.198 1.00 16.47 ? 245 ASN A ND2 1 
ATOM   1709 N  N   . ASP A 1 220 ? 7.615   -9.118  -52.812 1.00 14.90 ? 246 ASP A N   1 
ATOM   1710 C  CA  . ASP A 1 220 ? 7.452   -9.197  -51.366 1.00 16.44 ? 246 ASP A CA  1 
ATOM   1711 C  C   . ASP A 1 220 ? 6.750   -7.932  -50.894 1.00 16.45 ? 246 ASP A C   1 
ATOM   1712 O  O   . ASP A 1 220 ? 7.052   -6.851  -51.383 1.00 16.82 ? 246 ASP A O   1 
ATOM   1713 C  CB  . ASP A 1 220 ? 8.791   -9.337  -50.651 1.00 15.85 ? 246 ASP A CB  1 
ATOM   1714 C  CG  . ASP A 1 220 ? 8.703   -9.892  -49.228 1.00 16.99 ? 246 ASP A CG  1 
ATOM   1715 O  OD1 . ASP A 1 220 ? 7.688   -10.510 -48.894 1.00 17.40 ? 246 ASP A OD1 1 
ATOM   1716 O  OD2 . ASP A 1 220 ? 9.655   -9.697  -48.463 1.00 17.47 ? 246 ASP A OD2 1 
ATOM   1717 N  N   . ILE A 1 221 ? 5.761   -8.088  -49.998 1.00 16.59 ? 247 ILE A N   1 
ATOM   1718 C  CA  . ILE A 1 221 ? 5.112   -6.938  -49.376 1.00 16.20 ? 247 ILE A CA  1 
ATOM   1719 C  C   . ILE A 1 221 ? 5.246   -7.101  -47.867 1.00 16.34 ? 247 ILE A C   1 
ATOM   1720 O  O   . ILE A 1 221 ? 5.101   -8.200  -47.344 1.00 16.03 ? 247 ILE A O   1 
ATOM   1721 C  CB  . ILE A 1 221 ? 3.646   -6.759  -49.828 1.00 15.74 ? 247 ILE A CB  1 
ATOM   1722 C  CG1 . ILE A 1 221 ? 2.791   -7.963  -49.442 1.00 17.17 ? 247 ILE A CG1 1 
ATOM   1723 C  CG2 . ILE A 1 221 ? 3.589   -6.474  -51.325 1.00 15.28 ? 247 ILE A CG2 1 
ATOM   1724 C  CD1 . ILE A 1 221 ? 1.304   -7.802  -49.717 1.00 18.45 ? 247 ILE A CD1 1 
ATOM   1725 N  N   . ALA A 1 222 ? 5.576   -6.013  -47.185 1.00 16.24 ? 248 ALA A N   1 
ATOM   1726 C  CA  . ALA A 1 222 ? 5.888   -6.085  -45.772 1.00 16.93 ? 248 ALA A CA  1 
ATOM   1727 C  C   . ALA A 1 222 ? 5.417   -4.828  -45.056 1.00 17.78 ? 248 ALA A C   1 
ATOM   1728 O  O   . ALA A 1 222 ? 5.268   -3.756  -45.655 1.00 18.88 ? 248 ALA A O   1 
ATOM   1729 C  CB  . ALA A 1 222 ? 7.369   -6.271  -45.590 1.00 17.27 ? 248 ALA A CB  1 
ATOM   1730 N  N   . VAL A 1 223 ? 5.237   -4.988  -43.739 1.00 17.27 ? 249 VAL A N   1 
ATOM   1731 C  CA  . VAL A 1 223 ? 5.272   -3.881  -42.815 1.00 17.26 ? 249 VAL A CA  1 
ATOM   1732 C  C   . VAL A 1 223 ? 6.509   -4.086  -41.962 1.00 18.79 ? 249 VAL A C   1 
ATOM   1733 O  O   . VAL A 1 223 ? 6.828   -5.204  -41.583 1.00 19.24 ? 249 VAL A O   1 
ATOM   1734 C  CB  . VAL A 1 223 ? 3.982   -3.832  -41.984 1.00 18.43 ? 249 VAL A CB  1 
ATOM   1735 C  CG1 . VAL A 1 223 ? 3.962   -2.647  -41.037 1.00 19.40 ? 249 VAL A CG1 1 
ATOM   1736 C  CG2 . VAL A 1 223 ? 2.760   -3.786  -42.909 1.00 17.98 ? 249 VAL A CG2 1 
ATOM   1737 N  N   . VAL A 1 224 ? 7.209   -2.993  -41.704 1.00 20.04 ? 250 VAL A N   1 
ATOM   1738 C  CA  . VAL A 1 224 ? 8.408   -3.042  -40.892 1.00 21.28 ? 250 VAL A CA  1 
ATOM   1739 C  C   . VAL A 1 224 ? 8.232   -2.026  -39.769 1.00 21.96 ? 250 VAL A C   1 
ATOM   1740 O  O   . VAL A 1 224 ? 7.476   -1.071  -39.895 1.00 22.63 ? 250 VAL A O   1 
ATOM   1741 C  CB  . VAL A 1 224 ? 9.687   -2.789  -41.710 1.00 20.71 ? 250 VAL A CB  1 
ATOM   1742 C  CG1 . VAL A 1 224 ? 9.712   -3.631  -42.964 1.00 20.52 ? 250 VAL A CG1 1 
ATOM   1743 C  CG2 . VAL A 1 224 ? 9.821   -1.330  -42.111 1.00 21.12 ? 250 VAL A CG2 1 
ATOM   1744 N  N   . TRP A 1 225 ? 8.913   -2.289  -38.663 1.00 22.43 ? 251 TRP A N   1 
ATOM   1745 C  CA  . TRP A 1 225 ? 8.886   -1.398  -37.517 1.00 23.88 ? 251 TRP A CA  1 
ATOM   1746 C  C   . TRP A 1 225 ? 10.322  -1.158  -37.087 1.00 23.78 ? 251 TRP A C   1 
ATOM   1747 O  O   . TRP A 1 225 ? 11.068  -2.119  -36.930 1.00 23.84 ? 251 TRP A O   1 
ATOM   1748 C  CB  . TRP A 1 225 ? 8.094   -1.991  -36.347 1.00 24.90 ? 251 TRP A CB  1 
ATOM   1749 C  CG  . TRP A 1 225 ? 6.599   -2.021  -36.508 1.00 25.80 ? 251 TRP A CG  1 
ATOM   1750 C  CD1 . TRP A 1 225 ? 5.690   -1.142  -35.997 1.00 26.80 ? 251 TRP A CD1 1 
ATOM   1751 C  CD2 . TRP A 1 225 ? 5.844   -3.062  -37.158 1.00 25.10 ? 251 TRP A CD2 1 
ATOM   1752 N  NE1 . TRP A 1 225 ? 4.420   -1.552  -36.312 1.00 26.89 ? 251 TRP A NE1 1 
ATOM   1753 C  CE2 . TRP A 1 225 ? 4.482   -2.720  -37.021 1.00 25.92 ? 251 TRP A CE2 1 
ATOM   1754 C  CE3 . TRP A 1 225 ? 6.187   -4.225  -37.853 1.00 25.29 ? 251 TRP A CE3 1 
ATOM   1755 C  CZ2 . TRP A 1 225 ? 3.467   -3.504  -37.550 1.00 24.78 ? 251 TRP A CZ2 1 
ATOM   1756 C  CZ3 . TRP A 1 225 ? 5.179   -5.018  -38.355 1.00 24.52 ? 251 TRP A CZ3 1 
ATOM   1757 C  CH2 . TRP A 1 225 ? 3.841   -4.664  -38.182 1.00 25.75 ? 251 TRP A CH2 1 
ATOM   1758 N  N   . SER A 1 226 ? 10.678  0.117   -36.912 1.00 23.46 ? 252 SER A N   1 
ATOM   1759 C  CA  . SER A 1 226 ? 12.005  0.492   -36.455 1.00 25.13 ? 252 SER A CA  1 
ATOM   1760 C  C   . SER A 1 226 ? 12.189  0.016   -35.018 1.00 26.55 ? 252 SER A C   1 
ATOM   1761 O  O   . SER A 1 226 ? 11.214  -0.344  -34.330 1.00 26.06 ? 252 SER A O   1 
ATOM   1762 C  CB  . SER A 1 226 ? 12.220  1.983   -36.528 1.00 25.48 ? 252 SER A CB  1 
ATOM   1763 O  OG  . SER A 1 226 ? 11.632  2.616   -35.394 1.00 27.26 ? 252 SER A OG  1 
ATOM   1764 N  N   . PRO A 1 227 ? 13.435  0.049   -34.496 1.00 28.85 ? 254 PRO A N   1 
ATOM   1765 C  CA  . PRO A 1 227 ? 13.667  -0.283  -33.091 1.00 30.54 ? 254 PRO A CA  1 
ATOM   1766 C  C   . PRO A 1 227 ? 12.841  0.513   -32.079 1.00 31.78 ? 254 PRO A C   1 
ATOM   1767 O  O   . PRO A 1 227 ? 12.606  0.031   -30.976 1.00 32.38 ? 254 PRO A O   1 
ATOM   1768 C  CB  . PRO A 1 227 ? 15.184  -0.021  -32.940 1.00 32.16 ? 254 PRO A CB  1 
ATOM   1769 C  CG  . PRO A 1 227 ? 15.730  -0.205  -34.321 1.00 30.34 ? 254 PRO A CG  1 
ATOM   1770 C  CD  . PRO A 1 227 ? 14.667  0.349   -35.237 1.00 28.78 ? 254 PRO A CD  1 
ATOM   1771 N  N   . THR A 1 228 ? 12.420  1.735   -32.446 1.00 32.46 ? 255 THR A N   1 
ATOM   1772 C  CA  . THR A 1 228 ? 11.581  2.538   -31.569 1.00 34.05 ? 255 THR A CA  1 
ATOM   1773 C  C   . THR A 1 228 ? 10.100  2.402   -31.931 1.00 32.86 ? 255 THR A C   1 
ATOM   1774 O  O   . THR A 1 228 ? 9.263   3.099   -31.367 1.00 34.58 ? 255 THR A O   1 
ATOM   1775 C  CB  . THR A 1 228 ? 12.037  3.995   -31.584 1.00 36.00 ? 255 THR A CB  1 
ATOM   1776 O  OG1 . THR A 1 228 ? 11.854  4.461   -32.907 1.00 35.17 ? 255 THR A OG1 1 
ATOM   1777 C  CG2 . THR A 1 228 ? 13.493  4.174   -31.191 1.00 38.07 ? 255 THR A CG2 1 
ATOM   1778 N  N   . GLY A 1 229 ? 9.757   1.524   -32.871 1.00 30.46 ? 256 GLY A N   1 
ATOM   1779 C  CA  . GLY A 1 229 ? 8.362   1.187   -33.113 1.00 29.58 ? 256 GLY A CA  1 
ATOM   1780 C  C   . GLY A 1 229 ? 7.724   2.012   -34.229 1.00 28.88 ? 256 GLY A C   1 
ATOM   1781 O  O   . GLY A 1 229 ? 6.513   1.939   -34.432 1.00 27.81 ? 256 GLY A O   1 
ATOM   1782 N  N   . VAL A 1 230 ? 8.539   2.715   -35.024 1.00 27.73 ? 257 VAL A N   1 
ATOM   1783 C  CA  . VAL A 1 230 ? 7.999   3.532   -36.095 1.00 27.20 ? 257 VAL A CA  1 
ATOM   1784 C  C   . VAL A 1 230 ? 7.717   2.655   -37.310 1.00 25.38 ? 257 VAL A C   1 
ATOM   1785 O  O   . VAL A 1 230 ? 8.620   2.005   -37.832 1.00 23.75 ? 257 VAL A O   1 
ATOM   1786 C  CB  . VAL A 1 230 ? 8.922   4.689   -36.480 1.00 28.03 ? 257 VAL A CB  1 
ATOM   1787 C  CG1 . VAL A 1 230 ? 8.336   5.448   -37.660 1.00 27.70 ? 257 VAL A CG1 1 
ATOM   1788 C  CG2 . VAL A 1 230 ? 9.216   5.607   -35.303 1.00 30.23 ? 257 VAL A CG2 1 
ATOM   1789 N  N   . PRO A 1 231 ? 6.458   2.603   -37.808 1.00 25.56 ? 258 PRO A N   1 
ATOM   1790 C  CA  . PRO A 1 231 ? 6.122   1.706   -38.914 1.00 23.66 ? 258 PRO A CA  1 
ATOM   1791 C  C   . PRO A 1 231 ? 6.332   2.290   -40.303 1.00 23.19 ? 258 PRO A C   1 
ATOM   1792 O  O   . PRO A 1 231 ? 6.149   3.484   -40.503 1.00 23.28 ? 258 PRO A O   1 
ATOM   1793 C  CB  . PRO A 1 231 ? 4.635   1.394   -38.647 1.00 23.23 ? 258 PRO A CB  1 
ATOM   1794 C  CG  . PRO A 1 231 ? 4.118   2.694   -38.044 1.00 24.81 ? 258 PRO A CG  1 
ATOM   1795 C  CD  . PRO A 1 231 ? 5.282   3.304   -37.254 1.00 26.03 ? 258 PRO A CD  1 
ATOM   1796 N  N   . TYR A 1 232 ? 6.681   1.401   -41.242 1.00 21.77 ? 259 TYR A N   1 
ATOM   1797 C  CA  . TYR A 1 232 ? 6.703   1.711   -42.659 1.00 21.31 ? 259 TYR A CA  1 
ATOM   1798 C  C   . TYR A 1 232 ? 6.169   0.518   -43.434 1.00 20.31 ? 259 TYR A C   1 
ATOM   1799 O  O   . TYR A 1 232 ? 6.160   -0.621  -42.948 1.00 21.85 ? 259 TYR A O   1 
ATOM   1800 C  CB  . TYR A 1 232 ? 8.136   1.963   -43.118 1.00 21.45 ? 259 TYR A CB  1 
ATOM   1801 C  CG  . TYR A 1 232 ? 8.825   3.071   -42.355 1.00 22.21 ? 259 TYR A CG  1 
ATOM   1802 C  CD1 . TYR A 1 232 ? 8.727   4.379   -42.787 1.00 22.85 ? 259 TYR A CD1 1 
ATOM   1803 C  CD2 . TYR A 1 232 ? 9.566   2.798   -41.211 1.00 23.24 ? 259 TYR A CD2 1 
ATOM   1804 C  CE1 . TYR A 1 232 ? 9.351   5.400   -42.095 1.00 23.78 ? 259 TYR A CE1 1 
ATOM   1805 C  CE2 . TYR A 1 232 ? 10.175  3.815   -40.489 1.00 24.34 ? 259 TYR A CE2 1 
ATOM   1806 C  CZ  . TYR A 1 232 ? 10.072  5.113   -40.956 1.00 24.54 ? 259 TYR A CZ  1 
ATOM   1807 O  OH  . TYR A 1 232 ? 10.654  6.132   -40.304 1.00 26.32 ? 259 TYR A OH  1 
ATOM   1808 N  N   . VAL A 1 233 ? 5.676   0.781   -44.639 1.00 19.47 ? 260 VAL A N   1 
ATOM   1809 C  CA  . VAL A 1 233 ? 5.188   -0.276  -45.499 1.00 19.17 ? 260 VAL A CA  1 
ATOM   1810 C  C   . VAL A 1 233 ? 6.112   -0.315  -46.710 1.00 19.69 ? 260 VAL A C   1 
ATOM   1811 O  O   . VAL A 1 233 ? 6.492   0.739   -47.233 1.00 19.52 ? 260 VAL A O   1 
ATOM   1812 C  CB  . VAL A 1 233 ? 3.723   -0.062  -45.923 1.00 20.41 ? 260 VAL A CB  1 
ATOM   1813 C  CG1 . VAL A 1 233 ? 3.263   -1.119  -46.901 1.00 20.67 ? 260 VAL A CG1 1 
ATOM   1814 C  CG2 . VAL A 1 233 ? 2.802   -0.009  -44.707 1.00 22.50 ? 260 VAL A CG2 1 
ATOM   1815 N  N   . VAL A 1 234 ? 6.471   -1.535  -47.127 1.00 19.01 ? 261 VAL A N   1 
ATOM   1816 C  CA  . VAL A 1 234 ? 7.450   -1.722  -48.176 1.00 18.55 ? 261 VAL A CA  1 
ATOM   1817 C  C   . VAL A 1 234 ? 6.888   -2.737  -49.159 1.00 17.56 ? 261 VAL A C   1 
ATOM   1818 O  O   . VAL A 1 234 ? 6.634   -3.888  -48.807 1.00 17.18 ? 261 VAL A O   1 
ATOM   1819 C  CB  . VAL A 1 234 ? 8.830   -2.145  -47.625 1.00 19.12 ? 261 VAL A CB  1 
ATOM   1820 C  CG1 . VAL A 1 234 ? 9.857   -2.344  -48.737 1.00 19.06 ? 261 VAL A CG1 1 
ATOM   1821 C  CG2 . VAL A 1 234 ? 9.338   -1.162  -46.594 1.00 19.59 ? 261 VAL A CG2 1 
ATOM   1822 N  N   . ALA A 1 235 ? 6.733   -2.300  -50.409 1.00 16.22 ? 262 ALA A N   1 
ATOM   1823 C  CA  . ALA A 1 235 ? 6.397   -3.194  -51.498 1.00 16.57 ? 262 ALA A CA  1 
ATOM   1824 C  C   . ALA A 1 235 ? 7.555   -3.235  -52.498 1.00 16.53 ? 262 ALA A C   1 
ATOM   1825 O  O   . ALA A 1 235 ? 7.952   -2.195  -53.023 1.00 16.65 ? 262 ALA A O   1 
ATOM   1826 C  CB  . ALA A 1 235 ? 5.110   -2.717  -52.116 1.00 16.32 ? 262 ALA A CB  1 
ATOM   1827 N  N   . VAL A 1 236 ? 8.029   -4.451  -52.813 1.00 16.18 ? 263 VAL A N   1 
ATOM   1828 C  CA  . VAL A 1 236 ? 9.009   -4.648  -53.862 1.00 15.90 ? 263 VAL A CA  1 
ATOM   1829 C  C   . VAL A 1 236 ? 8.511   -5.752  -54.786 1.00 14.93 ? 263 VAL A C   1 
ATOM   1830 O  O   . VAL A 1 236 ? 8.114   -6.824  -54.334 1.00 16.65 ? 263 VAL A O   1 
ATOM   1831 C  CB  . VAL A 1 236 ? 10.412  -4.941  -53.295 1.00 17.14 ? 263 VAL A CB  1 
ATOM   1832 C  CG1 . VAL A 1 236 ? 10.876  -3.809  -52.395 1.00 19.18 ? 263 VAL A CG1 1 
ATOM   1833 C  CG2 . VAL A 1 236 ? 10.447  -6.223  -52.487 1.00 20.01 ? 263 VAL A CG2 1 
ATOM   1834 N  N   . MET A 1 237 ? 8.495   -5.434  -56.089 1.00 14.47 ? 264 MET A N   1 
ATOM   1835 C  CA  . MET A 1 237 ? 8.007   -6.344  -57.111 1.00 14.22 ? 264 MET A CA  1 
ATOM   1836 C  C   . MET A 1 237 ? 9.086   -6.450  -58.191 1.00 14.55 ? 264 MET A C   1 
ATOM   1837 O  O   . MET A 1 237 ? 9.833   -5.505  -58.405 1.00 14.08 ? 264 MET A O   1 
ATOM   1838 C  CB  . MET A 1 237 ? 6.668   -5.816  -57.618 1.00 15.04 ? 264 MET A CB  1 
ATOM   1839 C  CG  . MET A 1 237 ? 5.679   -5.541  -56.496 1.00 14.38 ? 264 MET A CG  1 
ATOM   1840 S  SD  . MET A 1 237 ? 3.977   -5.286  -57.029 1.00 17.24 ? 264 MET A SD  1 
ATOM   1841 C  CE  . MET A 1 237 ? 3.552   -6.997  -57.351 1.00 15.54 ? 264 MET A CE  1 
ATOM   1842 N  N   . SER A 1 238 ? 9.210   -7.617  -58.848 1.00 15.24 ? 265 SER A N   1 
ATOM   1843 C  CA  . SER A 1 238 ? 10.200  -7.749  -59.896 1.00 14.26 ? 265 SER A CA  1 
ATOM   1844 C  C   . SER A 1 238 ? 9.744   -8.808  -60.889 1.00 14.99 ? 265 SER A C   1 
ATOM   1845 O  O   . SER A 1 238 ? 9.035   -9.746  -60.543 1.00 13.76 ? 265 SER A O   1 
ATOM   1846 C  CB  . SER A 1 238 ? 11.605  -8.080  -59.368 1.00 14.16 ? 265 SER A CB  1 
ATOM   1847 O  OG  . SER A 1 238 ? 11.669  -9.397  -58.800 1.00 14.39 ? 265 SER A OG  1 
ATOM   1848 N  N   . ASP A 1 239 ? 10.254  -8.689  -62.106 1.00 15.75 ? 266 ASP A N   1 
ATOM   1849 C  CA  . ASP A 1 239 ? 10.197  -9.785  -63.061 1.00 15.88 ? 266 ASP A CA  1 
ATOM   1850 C  C   . ASP A 1 239 ? 11.446  -9.734  -63.921 1.00 16.96 ? 266 ASP A C   1 
ATOM   1851 O  O   . ASP A 1 239 ? 12.165  -8.730  -63.923 1.00 17.62 ? 266 ASP A O   1 
ATOM   1852 C  CB  . ASP A 1 239 ? 8.942   -9.709  -63.910 1.00 16.95 ? 266 ASP A CB  1 
ATOM   1853 C  CG  . ASP A 1 239 ? 8.936   -8.509  -64.845 1.00 19.04 ? 266 ASP A CG  1 
ATOM   1854 O  OD1 . ASP A 1 239 ? 9.637   -8.536  -65.897 1.00 22.12 ? 266 ASP A OD1 1 
ATOM   1855 O  OD2 . ASP A 1 239 ? 8.352   -7.523  -64.487 1.00 23.14 ? 266 ASP A OD2 1 
ATOM   1856 N  N   . ARG A 1 240 ? 11.692  -10.852 -64.624 1.00 17.19 ? 267 ARG A N   1 
ATOM   1857 C  CA  . ARG A 1 240 ? 12.795  -10.966 -65.572 1.00 17.69 ? 267 ARG A CA  1 
ATOM   1858 C  C   . ARG A 1 240 ? 12.269  -11.546 -66.890 1.00 18.49 ? 267 ARG A C   1 
ATOM   1859 O  O   . ARG A 1 240 ? 12.780  -12.529 -67.432 1.00 18.84 ? 267 ARG A O   1 
ATOM   1860 C  CB  . ARG A 1 240 ? 13.925  -11.789 -64.940 1.00 19.09 ? 267 ARG A CB  1 
ATOM   1861 C  CG  . ARG A 1 240 ? 14.298  -11.327 -63.541 1.00 20.29 ? 267 ARG A CG  1 
ATOM   1862 C  CD  . ARG A 1 240 ? 15.330  -12.172 -62.832 1.00 21.67 ? 267 ARG A CD  1 
ATOM   1863 N  NE  . ARG A 1 240 ? 16.590  -12.101 -63.562 1.00 22.85 ? 267 ARG A NE  1 
ATOM   1864 C  CZ  . ARG A 1 240 ? 17.193  -13.084 -64.215 1.00 24.91 ? 267 ARG A CZ  1 
ATOM   1865 N  NH1 . ARG A 1 240 ? 16.800  -14.349 -64.132 1.00 24.36 ? 267 ARG A NH1 1 
ATOM   1866 N  NH2 . ARG A 1 240 ? 18.262  -12.795 -64.919 1.00 26.38 ? 267 ARG A NH2 1 
ATOM   1867 N  N   . ALA A 1 241 ? 11.254  -10.864 -67.417 1.00 19.17 ? 268 ALA A N   1 
ATOM   1868 C  CA  . ALA A 1 241 ? 10.449  -11.380 -68.510 1.00 18.53 ? 268 ALA A CA  1 
ATOM   1869 C  C   . ALA A 1 241 ? 11.261  -11.584 -69.782 1.00 18.84 ? 268 ALA A C   1 
ATOM   1870 O  O   . ALA A 1 241 ? 10.875  -12.405 -70.619 1.00 18.09 ? 268 ALA A O   1 
ATOM   1871 C  CB  . ALA A 1 241 ? 9.298   -10.449 -68.742 1.00 19.23 ? 268 ALA A CB  1 
ATOM   1872 N  N   . GLY A 1 242 ? 12.360  -10.826 -69.929 1.00 19.40 ? 269 GLY A N   1 
ATOM   1873 C  CA  . GLY A 1 242 ? 13.321  -11.009 -71.004 1.00 20.04 ? 269 GLY A CA  1 
ATOM   1874 C  C   . GLY A 1 242 ? 13.844  -12.442 -71.116 1.00 21.12 ? 269 GLY A C   1 
ATOM   1875 O  O   . GLY A 1 242 ? 14.243  -12.874 -72.198 1.00 22.28 ? 269 GLY A O   1 
ATOM   1876 N  N   . GLY A 1 243 ? 13.842  -13.184 -69.997 1.00 20.81 ? 270 GLY A N   1 
ATOM   1877 C  CA  . GLY A 1 243 ? 14.335  -14.548 -69.996 1.00 22.51 ? 270 GLY A CA  1 
ATOM   1878 C  C   . GLY A 1 243 ? 13.257  -15.574 -70.352 1.00 23.27 ? 270 GLY A C   1 
ATOM   1879 O  O   . GLY A 1 243 ? 13.553  -16.761 -70.417 1.00 24.85 ? 270 GLY A O   1 
ATOM   1880 N  N   . GLY A 1 244 ? 12.022  -15.118 -70.603 1.00 21.29 ? 271 GLY A N   1 
ATOM   1881 C  CA  . GLY A 1 244 ? 10.939  -16.039 -70.890 1.00 20.54 ? 271 GLY A CA  1 
ATOM   1882 C  C   . GLY A 1 244 ? 10.288  -16.596 -69.617 1.00 19.05 ? 271 GLY A C   1 
ATOM   1883 O  O   . GLY A 1 244 ? 10.635  -16.211 -68.492 1.00 16.65 ? 271 GLY A O   1 
ATOM   1884 N  N   . TYR A 1 245 ? 9.338   -17.519 -69.828 1.00 18.20 ? 272 TYR A N   1 
ATOM   1885 C  CA  . TYR A 1 245 ? 8.416   -17.937 -68.781 1.00 18.61 ? 272 TYR A CA  1 
ATOM   1886 C  C   . TYR A 1 245 ? 9.211   -18.641 -67.680 1.00 18.90 ? 272 TYR A C   1 
ATOM   1887 O  O   . TYR A 1 245 ? 8.799   -18.594 -66.515 1.00 19.48 ? 272 TYR A O   1 
ATOM   1888 C  CB  . TYR A 1 245 ? 7.300   -18.828 -69.327 1.00 18.36 ? 272 TYR A CB  1 
ATOM   1889 C  CG  . TYR A 1 245 ? 7.717   -20.282 -69.438 1.00 19.19 ? 272 TYR A CG  1 
ATOM   1890 C  CD1 . TYR A 1 245 ? 8.425   -20.742 -70.547 1.00 19.88 ? 272 TYR A CD1 1 
ATOM   1891 C  CD2 . TYR A 1 245 ? 7.494   -21.168 -68.389 1.00 19.38 ? 272 TYR A CD2 1 
ATOM   1892 C  CE1 . TYR A 1 245 ? 8.882   -22.046 -70.607 1.00 21.95 ? 272 TYR A CE1 1 
ATOM   1893 C  CE2 . TYR A 1 245 ? 7.913   -22.486 -68.465 1.00 21.19 ? 272 TYR A CE2 1 
ATOM   1894 C  CZ  . TYR A 1 245 ? 8.620   -22.918 -69.571 1.00 21.57 ? 272 TYR A CZ  1 
ATOM   1895 O  OH  . TYR A 1 245 ? 9.064   -24.193 -69.642 1.00 27.50 ? 272 TYR A OH  1 
ATOM   1896 N  N   . ASP A 1 246 ? 10.328  -19.283 -68.054 1.00 18.76 ? 273 ASP A N   1 
ATOM   1897 C  CA  . ASP A 1 246 ? 11.125  -20.049 -67.106 1.00 19.72 ? 273 ASP A CA  1 
ATOM   1898 C  C   . ASP A 1 246 ? 12.337  -19.256 -66.609 1.00 19.94 ? 273 ASP A C   1 
ATOM   1899 O  O   . ASP A 1 246 ? 13.270  -19.836 -66.060 1.00 19.79 ? 273 ASP A O   1 
ATOM   1900 C  CB  . ASP A 1 246 ? 11.564  -21.377 -67.711 1.00 21.29 ? 273 ASP A CB  1 
ATOM   1901 C  CG  . ASP A 1 246 ? 12.457  -21.237 -68.931 1.00 23.66 ? 273 ASP A CG  1 
ATOM   1902 O  OD1 . ASP A 1 246 ? 12.255  -20.229 -69.703 1.00 24.79 ? 273 ASP A OD1 1 
ATOM   1903 O  OD2 . ASP A 1 246 ? 13.302  -22.152 -69.137 1.00 25.58 ? 273 ASP A OD2 1 
ATOM   1904 N  N   . ALA A 1 247 ? 12.344  -17.931 -66.782 1.00 19.71 ? 274 ALA A N   1 
ATOM   1905 C  CA  . ALA A 1 247 ? 13.421  -17.119 -66.235 1.00 19.46 ? 274 ALA A CA  1 
ATOM   1906 C  C   . ALA A 1 247 ? 13.501  -17.351 -64.729 1.00 18.34 ? 274 ALA A C   1 
ATOM   1907 O  O   . ALA A 1 247 ? 12.489  -17.472 -64.058 1.00 17.69 ? 274 ALA A O   1 
ATOM   1908 C  CB  . ALA A 1 247 ? 13.198  -15.655 -66.523 1.00 18.10 ? 274 ALA A CB  1 
ATOM   1909 N  N   . GLU A 1 248 ? 14.715  -17.350 -64.197 1.00 19.51 ? 275 GLU A N   1 
ATOM   1910 C  CA  . GLU A 1 248 ? 14.912  -17.582 -62.777 1.00 20.74 ? 275 GLU A CA  1 
ATOM   1911 C  C   . GLU A 1 248 ? 14.535  -16.331 -61.981 1.00 19.66 ? 275 GLU A C   1 
ATOM   1912 O  O   . GLU A 1 248 ? 15.019  -15.245 -62.294 1.00 20.22 ? 275 GLU A O   1 
ATOM   1913 C  CB  . GLU A 1 248 ? 16.356  -17.966 -62.457 1.00 23.32 ? 275 GLU A CB  1 
ATOM   1914 C  CG  . GLU A 1 248 ? 16.833  -19.213 -63.188 1.00 29.17 ? 275 GLU A CG  1 
ATOM   1915 C  CD  . GLU A 1 248 ? 18.292  -19.602 -63.016 1.00 35.82 ? 275 GLU A CD  1 
ATOM   1916 O  OE1 . GLU A 1 248 ? 19.049  -18.897 -62.318 1.00 37.45 ? 275 GLU A OE1 1 
ATOM   1917 O  OE2 . GLU A 1 248 ? 18.661  -20.654 -63.596 1.00 43.90 ? 275 GLU A OE2 1 
ATOM   1918 N  N   . PRO A 1 249 ? 13.670  -16.426 -60.951 1.00 19.54 ? 276 PRO A N   1 
ATOM   1919 C  CA  . PRO A 1 249 ? 13.441  -15.291 -60.056 1.00 18.33 ? 276 PRO A CA  1 
ATOM   1920 C  C   . PRO A 1 249 ? 14.709  -15.014 -59.253 1.00 18.80 ? 276 PRO A C   1 
ATOM   1921 O  O   . PRO A 1 249 ? 15.511  -15.921 -59.054 1.00 17.26 ? 276 PRO A O   1 
ATOM   1922 C  CB  . PRO A 1 249 ? 12.257  -15.717 -59.168 1.00 19.84 ? 276 PRO A CB  1 
ATOM   1923 C  CG  . PRO A 1 249 ? 12.201  -17.224 -59.298 1.00 22.74 ? 276 PRO A CG  1 
ATOM   1924 C  CD  . PRO A 1 249 ? 12.918  -17.629 -60.557 1.00 20.79 ? 276 PRO A CD  1 
ATOM   1925 N  N   . ARG A 1 250 ? 14.860  -13.770 -58.766 1.00 18.43 ? 277 ARG A N   1 
ATOM   1926 C  CA  . ARG A 1 250 ? 16.028  -13.399 -57.975 1.00 19.65 ? 277 ARG A CA  1 
ATOM   1927 C  C   . ARG A 1 250 ? 15.584  -12.753 -56.669 1.00 18.12 ? 277 ARG A C   1 
ATOM   1928 O  O   . ARG A 1 250 ? 15.330  -11.561 -56.604 1.00 16.47 ? 277 ARG A O   1 
ATOM   1929 C  CB  . ARG A 1 250 ? 16.900  -12.392 -58.743 1.00 20.82 ? 277 ARG A CB  1 
ATOM   1930 C  CG  . ARG A 1 250 ? 17.536  -12.982 -59.996 1.00 22.98 ? 277 ARG A CG  1 
ATOM   1931 C  CD  . ARG A 1 250 ? 18.679  -13.930 -59.646 1.00 23.51 ? 277 ARG A CD  1 
ATOM   1932 N  NE  . ARG A 1 250 ? 19.261  -14.435 -60.889 1.00 25.95 ? 277 ARG A NE  1 
ATOM   1933 C  CZ  . ARG A 1 250 ? 19.336  -15.692 -61.293 1.00 24.48 ? 277 ARG A CZ  1 
ATOM   1934 N  NH1 . ARG A 1 250 ? 18.940  -16.680 -60.526 1.00 25.15 ? 277 ARG A NH1 1 
ATOM   1935 N  NH2 . ARG A 1 250 ? 19.820  -15.965 -62.488 1.00 25.26 ? 277 ARG A NH2 1 
ATOM   1936 N  N   . GLU A 1 251 ? 15.493  -13.553 -55.618 1.00 19.22 ? 278 GLU A N   1 
ATOM   1937 C  CA  . GLU A 1 251 ? 15.138  -13.024 -54.318 1.00 19.13 ? 278 GLU A CA  1 
ATOM   1938 C  C   . GLU A 1 251 ? 16.095  -11.923 -53.874 1.00 17.64 ? 278 GLU A C   1 
ATOM   1939 O  O   . GLU A 1 251 ? 15.664  -10.973 -53.217 1.00 16.77 ? 278 GLU A O   1 
ATOM   1940 C  CB  . GLU A 1 251 ? 15.233  -14.117 -53.255 1.00 20.73 ? 278 GLU A CB  1 
ATOM   1941 C  CG  . GLU A 1 251 ? 14.174  -15.186 -53.437 1.00 20.80 ? 278 GLU A CG  1 
ATOM   1942 C  CD  . GLU A 1 251 ? 14.035  -16.034 -52.206 1.00 20.74 ? 278 GLU A CD  1 
ATOM   1943 O  OE1 . GLU A 1 251 ? 14.966  -16.787 -51.948 1.00 21.25 ? 278 GLU A OE1 1 
ATOM   1944 O  OE2 . GLU A 1 251 ? 13.026  -15.874 -51.501 1.00 20.06 ? 278 GLU A OE2 1 
ATOM   1945 N  N   . ALA A 1 252 ? 17.374  -12.079 -54.217 1.00 16.74 ? 279 ALA A N   1 
ATOM   1946 C  CA  . ALA A 1 252 ? 18.403  -11.167 -53.777 1.00 18.33 ? 279 ALA A CA  1 
ATOM   1947 C  C   . ALA A 1 252 ? 18.139  -9.757  -54.305 1.00 17.15 ? 279 ALA A C   1 
ATOM   1948 O  O   . ALA A 1 252 ? 18.512  -8.785  -53.664 1.00 15.92 ? 279 ALA A O   1 
ATOM   1949 C  CB  . ALA A 1 252 ? 19.782  -11.669 -54.170 1.00 19.38 ? 279 ALA A CB  1 
ATOM   1950 N  N   . LEU A 1 253 ? 17.498  -9.653  -55.483 1.00 17.25 ? 280 LEU A N   1 
ATOM   1951 C  CA  . LEU A 1 253 ? 17.135  -8.359  -56.046 1.00 16.57 ? 280 LEU A CA  1 
ATOM   1952 C  C   . LEU A 1 253 ? 16.215  -7.620  -55.069 1.00 16.96 ? 280 LEU A C   1 
ATOM   1953 O  O   . LEU A 1 253 ? 16.386  -6.415  -54.806 1.00 16.30 ? 280 LEU A O   1 
ATOM   1954 C  CB  . LEU A 1 253 ? 16.493  -8.554  -57.412 1.00 16.92 ? 280 LEU A CB  1 
ATOM   1955 C  CG  . LEU A 1 253 ? 15.730  -7.362  -57.997 1.00 17.45 ? 280 LEU A CG  1 
ATOM   1956 C  CD1 . LEU A 1 253 ? 16.559  -6.098  -58.169 1.00 17.83 ? 280 LEU A CD1 1 
ATOM   1957 C  CD2 . LEU A 1 253 ? 15.071  -7.762  -59.313 1.00 17.87 ? 280 LEU A CD2 1 
ATOM   1958 N  N   . LEU A 1 254 ? 15.276  -8.362  -54.471 1.00 16.47 ? 281 LEU A N   1 
ATOM   1959 C  CA  . LEU A 1 254 ? 14.339  -7.766  -53.527 1.00 17.43 ? 281 LEU A CA  1 
ATOM   1960 C  C   . LEU A 1 254 ? 15.054  -7.383  -52.223 1.00 17.63 ? 281 LEU A C   1 
ATOM   1961 O  O   . LEU A 1 254 ? 14.789  -6.320  -51.645 1.00 18.11 ? 281 LEU A O   1 
ATOM   1962 C  CB  . LEU A 1 254 ? 13.178  -8.733  -53.277 1.00 17.17 ? 281 LEU A CB  1 
ATOM   1963 C  CG  . LEU A 1 254 ? 12.412  -9.231  -54.502 1.00 17.44 ? 281 LEU A CG  1 
ATOM   1964 C  CD1 . LEU A 1 254 ? 11.353  -10.190 -54.038 1.00 17.89 ? 281 LEU A CD1 1 
ATOM   1965 C  CD2 . LEU A 1 254 ? 11.818  -8.100  -55.322 1.00 17.72 ? 281 LEU A CD2 1 
ATOM   1966 N  N   . ALA A 1 255 ? 15.946  -8.254  -51.757 1.00 18.07 ? 282 ALA A N   1 
ATOM   1967 C  CA  . ALA A 1 255 ? 16.739  -7.996  -50.556 1.00 18.87 ? 282 ALA A CA  1 
ATOM   1968 C  C   . ALA A 1 255 ? 17.566  -6.729  -50.721 1.00 20.21 ? 282 ALA A C   1 
ATOM   1969 O  O   . ALA A 1 255 ? 17.638  -5.898  -49.821 1.00 19.02 ? 282 ALA A O   1 
ATOM   1970 C  CB  . ALA A 1 255 ? 17.632  -9.174  -50.225 1.00 19.25 ? 282 ALA A CB  1 
ATOM   1971 N  N   . GLU A 1 256 ? 18.173  -6.568  -51.904 1.00 20.47 ? 283 GLU A N   1 
ATOM   1972 C  CA  . GLU A 1 256 ? 18.954  -5.382  -52.167 1.00 21.44 ? 283 GLU A CA  1 
ATOM   1973 C  C   . GLU A 1 256 ? 18.088  -4.140  -52.226 1.00 19.90 ? 283 GLU A C   1 
ATOM   1974 O  O   . GLU A 1 256 ? 18.490  -3.099  -51.720 1.00 22.48 ? 283 GLU A O   1 
ATOM   1975 C  CB  . GLU A 1 256 ? 19.704  -5.475  -53.484 1.00 23.11 ? 283 GLU A CB  1 
ATOM   1976 C  CG  . GLU A 1 256 ? 20.880  -6.423  -53.387 1.00 25.10 ? 283 GLU A CG  1 
ATOM   1977 C  CD  . GLU A 1 256 ? 21.636  -6.359  -54.684 1.00 27.94 ? 283 GLU A CD  1 
ATOM   1978 O  OE1 . GLU A 1 256 ? 21.953  -5.232  -55.126 1.00 30.36 ? 283 GLU A OE1 1 
ATOM   1979 O  OE2 . GLU A 1 256 ? 21.886  -7.450  -55.222 1.00 29.85 ? 283 GLU A OE2 1 
ATOM   1980 N  N   . ALA A 1 257 ? 16.931  -4.237  -52.868 1.00 18.88 ? 284 ALA A N   1 
ATOM   1981 C  CA  . ALA A 1 257 ? 16.060  -3.079  -52.948 1.00 19.22 ? 284 ALA A CA  1 
ATOM   1982 C  C   . ALA A 1 257 ? 15.672  -2.670  -51.530 1.00 19.04 ? 284 ALA A C   1 
ATOM   1983 O  O   . ALA A 1 257 ? 15.635  -1.484  -51.211 1.00 19.38 ? 284 ALA A O   1 
ATOM   1984 C  CB  . ALA A 1 257 ? 14.833  -3.362  -53.801 1.00 18.18 ? 284 ALA A CB  1 
ATOM   1985 N  N   . ALA A 1 258 ? 15.386  -3.678  -50.684 1.00 17.89 ? 285 ALA A N   1 
ATOM   1986 C  CA  . ALA A 1 258 ? 15.022  -3.459  -49.289 1.00 17.75 ? 285 ALA A CA  1 
ATOM   1987 C  C   . ALA A 1 258 ? 16.161  -2.803  -48.516 1.00 19.53 ? 285 ALA A C   1 
ATOM   1988 O  O   . ALA A 1 258 ? 15.931  -1.880  -47.724 1.00 19.82 ? 285 ALA A O   1 
ATOM   1989 C  CB  . ALA A 1 258 ? 14.554  -4.758  -48.695 1.00 17.12 ? 285 ALA A CB  1 
ATOM   1990 N  N   . THR A 1 259 ? 17.408  -3.233  -48.776 1.00 19.34 ? 286 THR A N   1 
ATOM   1991 C  CA  . THR A 1 259 ? 18.578  -2.639  -48.150 1.00 21.37 ? 286 THR A CA  1 
ATOM   1992 C  C   . THR A 1 259 ? 18.660  -1.154  -48.511 1.00 22.67 ? 286 THR A C   1 
ATOM   1993 O  O   . THR A 1 259 ? 18.988  -0.332  -47.656 1.00 22.99 ? 286 THR A O   1 
ATOM   1994 C  CB  . THR A 1 259 ? 19.847  -3.392  -48.551 1.00 21.40 ? 286 THR A CB  1 
ATOM   1995 O  OG1 . THR A 1 259 ? 19.625  -4.767  -48.230 1.00 20.66 ? 286 THR A OG1 1 
ATOM   1996 C  CG2 . THR A 1 259 ? 21.108  -2.858  -47.884 1.00 23.02 ? 286 THR A CG2 1 
ATOM   1997 N  N   . CYS A 1 260 ? 18.414  -0.809  -49.781 1.00 23.05 ? 287 CYS A N   1 
ATOM   1998 C  CA  . CYS A 1 260 ? 18.388  0.600   -50.190 1.00 24.25 ? 287 CYS A CA  1 
ATOM   1999 C  C   . CYS A 1 260 ? 17.365  1.395   -49.359 1.00 23.94 ? 287 CYS A C   1 
ATOM   2000 O  O   . CYS A 1 260 ? 17.665  2.487   -48.870 1.00 22.53 ? 287 CYS A O   1 
ATOM   2001 C  CB  . CYS A 1 260 ? 18.086  0.785   -51.681 1.00 25.48 ? 287 CYS A CB  1 
ATOM   2002 S  SG  . CYS A 1 260 ? 19.289  -0.005  -52.800 1.00 29.32 ? 287 CYS A SG  1 
ATOM   2003 N  N   . VAL A 1 261 ? 16.142  0.866   -49.256 1.00 22.61 ? 288 VAL A N   1 
ATOM   2004 C  CA  . VAL A 1 261 ? 15.100  1.484   -48.445 1.00 23.38 ? 288 VAL A CA  1 
ATOM   2005 C  C   . VAL A 1 261 ? 15.543  1.626   -46.981 1.00 23.60 ? 288 VAL A C   1 
ATOM   2006 O  O   . VAL A 1 261 ? 15.453  2.710   -46.400 1.00 22.90 ? 288 VAL A O   1 
ATOM   2007 C  CB  . VAL A 1 261 ? 13.804  0.666   -48.565 1.00 21.67 ? 288 VAL A CB  1 
ATOM   2008 C  CG1 . VAL A 1 261 ? 12.769  1.032   -47.501 1.00 22.10 ? 288 VAL A CG1 1 
ATOM   2009 C  CG2 . VAL A 1 261 ? 13.235  0.752   -49.984 1.00 20.79 ? 288 VAL A CG2 1 
ATOM   2010 N  N   . ALA A 1 262 ? 16.014  0.535   -46.372 1.00 22.48 ? 289 ALA A N   1 
ATOM   2011 C  CA  . ALA A 1 262 ? 16.439  0.567   -44.980 1.00 24.14 ? 289 ALA A CA  1 
ATOM   2012 C  C   . ALA A 1 262 ? 17.499  1.647   -44.746 1.00 26.31 ? 289 ALA A C   1 
ATOM   2013 O  O   . ALA A 1 262 ? 17.501  2.324   -43.713 1.00 25.72 ? 289 ALA A O   1 
ATOM   2014 C  CB  . ALA A 1 262 ? 16.932  -0.817  -44.569 1.00 23.64 ? 289 ALA A CB  1 
ATOM   2015 N  N   . GLY A 1 263 ? 18.428  1.806   -45.702 1.00 27.30 ? 290 GLY A N   1 
ATOM   2016 C  CA  . GLY A 1 263 ? 19.449  2.835   -45.622 1.00 29.47 ? 290 GLY A CA  1 
ATOM   2017 C  C   . GLY A 1 263 ? 18.853  4.239   -45.547 1.00 30.16 ? 290 GLY A C   1 
ATOM   2018 O  O   . GLY A 1 263 ? 19.391  5.104   -44.862 1.00 30.46 ? 290 GLY A O   1 
ATOM   2019 N  N   . VAL A 1 264 ? 17.734  4.453   -46.237 1.00 29.01 ? 291 VAL A N   1 
ATOM   2020 C  CA  . VAL A 1 264 ? 17.050  5.736   -46.263 1.00 31.20 ? 291 VAL A CA  1 
ATOM   2021 C  C   . VAL A 1 264 ? 16.279  5.942   -44.960 1.00 31.64 ? 291 VAL A C   1 
ATOM   2022 O  O   . VAL A 1 264 ? 16.223  7.050   -44.444 1.00 31.03 ? 291 VAL A O   1 
ATOM   2023 C  CB  . VAL A 1 264 ? 16.123  5.760   -47.494 1.00 32.82 ? 291 VAL A CB  1 
ATOM   2024 C  CG1 . VAL A 1 264 ? 15.074  6.861   -47.437 1.00 35.80 ? 291 VAL A CG1 1 
ATOM   2025 C  CG2 . VAL A 1 264 ? 16.941  5.873   -48.765 1.00 34.25 ? 291 VAL A CG2 1 
ATOM   2026 N  N   . LEU A 1 265 ? 15.674  4.869   -44.443 1.00 30.34 ? 292 LEU A N   1 
ATOM   2027 C  CA  . LEU A 1 265 ? 14.842  4.992   -43.265 1.00 32.99 ? 292 LEU A CA  1 
ATOM   2028 C  C   . LEU A 1 265 ? 15.667  4.953   -41.968 1.00 35.32 ? 292 LEU A C   1 
ATOM   2029 O  O   . LEU A 1 265 ? 15.142  5.310   -40.918 1.00 38.46 ? 292 LEU A O   1 
ATOM   2030 C  CB  . LEU A 1 265 ? 13.751  3.927   -43.294 1.00 31.60 ? 292 LEU A CB  1 
ATOM   2031 C  CG  . LEU A 1 265 ? 12.842  3.895   -44.527 1.00 32.02 ? 292 LEU A CG  1 
ATOM   2032 C  CD1 . LEU A 1 265 ? 11.882  2.754   -44.342 1.00 31.05 ? 292 LEU A CD1 1 
ATOM   2033 C  CD2 . LEU A 1 265 ? 12.123  5.199   -44.817 1.00 33.20 ? 292 LEU A CD2 1 
ATOM   2034 N  N   A ALA A 1 266 ? 16.949  4.562   -42.031 0.50 36.12 ? 293 ALA A N   1 
ATOM   2035 N  N   B ALA A 1 266 ? 16.938  4.526   -42.028 0.50 36.19 ? 293 ALA A N   1 
ATOM   2036 C  CA  A ALA A 1 266 ? 17.777  4.444   -40.835 0.50 38.04 ? 293 ALA A CA  1 
ATOM   2037 C  CA  B ALA A 1 266 ? 17.769  4.439   -40.834 0.50 38.25 ? 293 ALA A CA  1 
ATOM   2038 C  C   A ALA A 1 266 ? 17.976  5.803   -40.163 0.50 39.54 ? 293 ALA A C   1 
ATOM   2039 C  C   B ALA A 1 266 ? 17.803  5.787   -40.113 0.50 39.92 ? 293 ALA A C   1 
ATOM   2040 O  O   A ALA A 1 266 ? 17.781  6.834   -40.834 0.50 39.26 ? 293 ALA A O   1 
ATOM   2041 O  O   B ALA A 1 266 ? 17.415  5.765   -38.930 0.50 40.21 ? 293 ALA A O   1 
ATOM   2042 C  CB  A ALA A 1 266 ? 19.122  3.834   -41.169 0.50 39.18 ? 293 ALA A CB  1 
ATOM   2043 C  CB  B ALA A 1 266 ? 19.174  3.989   -41.176 0.50 39.44 ? 293 ALA A CB  1 
ATOM   2044 O  OXT A ALA A 1 266 ? 18.344  5.773   -38.974 0.50 40.66 ? 293 ALA A OXT 1 
ATOM   2045 N  N   . ASP B 1 2   ? -31.297 -7.750  -2.660  1.00 44.57 ? 28  ASP B N   1 
ATOM   2046 C  CA  . ASP B 1 2   ? -29.955 -7.316  -3.120  1.00 45.09 ? 28  ASP B CA  1 
ATOM   2047 C  C   . ASP B 1 2   ? -29.220 -8.536  -3.658  1.00 41.82 ? 28  ASP B C   1 
ATOM   2048 O  O   . ASP B 1 2   ? -29.693 -9.674  -3.595  1.00 39.32 ? 28  ASP B O   1 
ATOM   2049 C  CB  . ASP B 1 2   ? -29.159 -6.524  -2.090  1.00 49.46 ? 28  ASP B CB  1 
ATOM   2050 C  CG  . ASP B 1 2   ? -28.398 -7.293  -1.009  1.00 55.35 ? 28  ASP B CG  1 
ATOM   2051 O  OD1 . ASP B 1 2   ? -28.677 -8.498  -0.769  1.00 57.71 ? 28  ASP B OD1 1 
ATOM   2052 O  OD2 . ASP B 1 2   ? -27.500 -6.678  -0.403  1.00 63.36 ? 28  ASP B OD2 1 
ATOM   2053 N  N   . LEU B 1 3   ? -28.044 -8.249  -4.199  1.00 40.68 ? 29  LEU B N   1 
ATOM   2054 C  CA  . LEU B 1 3   ? -27.346 -9.187  -5.043  1.00 39.88 ? 29  LEU B CA  1 
ATOM   2055 C  C   . LEU B 1 3   ? -26.914 -10.401 -4.232  1.00 36.30 ? 29  LEU B C   1 
ATOM   2056 O  O   . LEU B 1 3   ? -27.084 -11.525 -4.693  1.00 33.41 ? 29  LEU B O   1 
ATOM   2057 C  CB  . LEU B 1 3   ? -26.173 -8.431  -5.655  1.00 42.59 ? 29  LEU B CB  1 
ATOM   2058 C  CG  . LEU B 1 3   ? -25.607 -9.022  -6.942  1.00 44.80 ? 29  LEU B CG  1 
ATOM   2059 C  CD1 . LEU B 1 3   ? -26.674 -9.219  -8.000  1.00 45.15 ? 29  LEU B CD1 1 
ATOM   2060 C  CD2 . LEU B 1 3   ? -24.511 -8.093  -7.433  1.00 46.52 ? 29  LEU B CD2 1 
ATOM   2061 N  N   . ALA B 1 4   ? -26.320 -10.153 -3.059  1.00 35.93 ? 30  ALA B N   1 
ATOM   2062 C  CA  . ALA B 1 4   ? -25.854 -11.206 -2.165  1.00 35.95 ? 30  ALA B CA  1 
ATOM   2063 C  C   . ALA B 1 4   ? -27.004 -12.152 -1.815  1.00 34.64 ? 30  ALA B C   1 
ATOM   2064 O  O   . ALA B 1 4   ? -26.849 -13.362 -1.845  1.00 34.52 ? 30  ALA B O   1 
ATOM   2065 C  CB  . ALA B 1 4   ? -25.240 -10.594 -0.913  1.00 36.96 ? 30  ALA B CB  1 
ATOM   2066 N  N   . ASP B 1 5   ? -28.177 -11.607 -1.519  1.00 35.15 ? 31  ASP B N   1 
ATOM   2067 C  CA  . ASP B 1 5   ? -29.334 -12.420 -1.171  1.00 36.96 ? 31  ASP B CA  1 
ATOM   2068 C  C   . ASP B 1 5   ? -29.821 -13.262 -2.351  1.00 35.88 ? 31  ASP B C   1 
ATOM   2069 O  O   . ASP B 1 5   ? -30.194 -14.433 -2.184  1.00 33.64 ? 31  ASP B O   1 
ATOM   2070 C  CB  . ASP B 1 5   ? -30.463 -11.561 -0.640  1.00 39.90 ? 31  ASP B CB  1 
ATOM   2071 C  CG  . ASP B 1 5   ? -30.531 -11.485 0.869   1.00 43.51 ? 31  ASP B CG  1 
ATOM   2072 O  OD1 . ASP B 1 5   ? -29.451 -11.479 1.501   1.00 44.86 ? 31  ASP B OD1 1 
ATOM   2073 O  OD2 . ASP B 1 5   ? -31.671 -11.414 1.362   1.00 45.70 ? 31  ASP B OD2 1 
ATOM   2074 N  N   . ARG B 1 6   ? -29.815 -12.674 -3.547  1.00 35.85 ? 32  ARG B N   1 
ATOM   2075 C  CA  . ARG B 1 6   ? -30.207 -13.416 -4.737  1.00 35.74 ? 32  ARG B CA  1 
ATOM   2076 C  C   . ARG B 1 6   ? -29.240 -14.575 -4.985  1.00 33.86 ? 32  ARG B C   1 
ATOM   2077 O  O   . ARG B 1 6   ? -29.680 -15.670 -5.342  1.00 33.26 ? 32  ARG B O   1 
ATOM   2078 C  CB  . ARG B 1 6   ? -30.322 -12.485 -5.952  1.00 38.38 ? 32  ARG B CB  1 
ATOM   2079 C  CG  . ARG B 1 6   ? -31.474 -11.500 -5.789  1.00 42.49 ? 32  ARG B CG  1 
ATOM   2080 C  CD  . ARG B 1 6   ? -31.370 -10.241 -6.635  1.00 47.52 ? 32  ARG B CD  1 
ATOM   2081 N  NE  . ARG B 1 6   ? -31.265 -10.509 -8.074  1.00 53.67 ? 32  ARG B NE  1 
ATOM   2082 C  CZ  . ARG B 1 6   ? -30.995 -9.567  -8.985  1.00 57.35 ? 32  ARG B CZ  1 
ATOM   2083 N  NH1 . ARG B 1 6   ? -30.735 -8.320  -8.616  1.00 58.99 ? 32  ARG B NH1 1 
ATOM   2084 N  NH2 . ARG B 1 6   ? -30.977 -9.868  -10.269 1.00 60.22 ? 32  ARG B NH2 1 
ATOM   2085 N  N   . PHE B 1 7   ? -27.930 -14.332 -4.833  1.00 30.46 ? 33  PHE B N   1 
ATOM   2086 C  CA  . PHE B 1 7   ? -26.913 -15.360 -5.001  1.00 28.85 ? 33  PHE B CA  1 
ATOM   2087 C  C   . PHE B 1 7   ? -27.101 -16.468 -3.964  1.00 28.45 ? 33  PHE B C   1 
ATOM   2088 O  O   . PHE B 1 7   ? -26.922 -17.649 -4.254  1.00 26.43 ? 33  PHE B O   1 
ATOM   2089 C  CB  . PHE B 1 7   ? -25.499 -14.786 -4.890  1.00 28.10 ? 33  PHE B CB  1 
ATOM   2090 C  CG  . PHE B 1 7   ? -25.042 -13.918 -6.054  1.00 28.17 ? 33  PHE B CG  1 
ATOM   2091 C  CD1 . PHE B 1 7   ? -25.395 -14.214 -7.369  1.00 28.32 ? 33  PHE B CD1 1 
ATOM   2092 C  CD2 . PHE B 1 7   ? -24.212 -12.824 -5.833  1.00 29.23 ? 33  PHE B CD2 1 
ATOM   2093 C  CE1 . PHE B 1 7   ? -24.928 -13.438 -8.419  1.00 28.35 ? 33  PHE B CE1 1 
ATOM   2094 C  CE2 . PHE B 1 7   ? -23.757 -12.049 -6.890  1.00 29.11 ? 33  PHE B CE2 1 
ATOM   2095 C  CZ  . PHE B 1 7   ? -24.123 -12.351 -8.181  1.00 28.28 ? 33  PHE B CZ  1 
ATOM   2096 N  N   . ALA B 1 8   ? -27.457 -16.087 -2.737  1.00 29.85 ? 34  ALA B N   1 
ATOM   2097 C  CA  . ALA B 1 8   ? -27.683 -17.068 -1.692  1.00 30.23 ? 34  ALA B CA  1 
ATOM   2098 C  C   . ALA B 1 8   ? -28.883 -17.944 -2.041  1.00 29.71 ? 34  ALA B C   1 
ATOM   2099 O  O   . ALA B 1 8   ? -28.906 -19.103 -1.673  1.00 29.38 ? 34  ALA B O   1 
ATOM   2100 C  CB  . ALA B 1 8   ? -27.882 -16.387 -0.343  1.00 31.51 ? 34  ALA B CB  1 
ATOM   2101 N  N   . GLU B 1 9   ? -29.908 -17.374 -2.671  1.00 30.03 ? 35  GLU B N   1 
ATOM   2102 C  CA  . GLU B 1 9   ? -31.075 -18.137 -3.056  1.00 30.99 ? 35  GLU B CA  1 
ATOM   2103 C  C   . GLU B 1 9   ? -30.701 -19.145 -4.143  1.00 30.34 ? 35  GLU B C   1 
ATOM   2104 O  O   . GLU B 1 9   ? -31.219 -20.257 -4.129  1.00 29.17 ? 35  GLU B O   1 
ATOM   2105 C  CB  . GLU B 1 9   ? -32.224 -17.227 -3.479  1.00 32.90 ? 35  GLU B CB  1 
ATOM   2106 C  CG  . GLU B 1 9   ? -33.532 -17.991 -3.694  1.00 34.20 ? 35  GLU B CG  1 
ATOM   2107 C  CD  . GLU B 1 9   ? -33.635 -18.649 -5.068  1.00 34.21 ? 35  GLU B CD  1 
ATOM   2108 O  OE1 . GLU B 1 9   ? -32.865 -18.224 -5.976  1.00 33.00 ? 35  GLU B OE1 1 
ATOM   2109 O  OE2 . GLU B 1 9   ? -34.422 -19.614 -5.188  1.00 34.13 ? 35  GLU B OE2 1 
ATOM   2110 N  N   . LEU B 1 10  ? -29.814 -18.753 -5.065  1.00 31.08 ? 36  LEU B N   1 
ATOM   2111 C  CA  . LEU B 1 10  ? -29.297 -19.680 -6.068  1.00 30.95 ? 36  LEU B CA  1 
ATOM   2112 C  C   . LEU B 1 10  ? -28.662 -20.872 -5.360  1.00 29.70 ? 36  LEU B C   1 
ATOM   2113 O  O   . LEU B 1 10  ? -28.909 -22.020 -5.720  1.00 29.97 ? 36  LEU B O   1 
ATOM   2114 C  CB  . LEU B 1 10  ? -28.261 -19.035 -6.990  1.00 32.17 ? 36  LEU B CB  1 
ATOM   2115 C  CG  . LEU B 1 10  ? -28.666 -17.829 -7.845  1.00 32.79 ? 36  LEU B CG  1 
ATOM   2116 C  CD1 . LEU B 1 10  ? -27.560 -17.539 -8.863  1.00 32.69 ? 36  LEU B CD1 1 
ATOM   2117 C  CD2 . LEU B 1 10  ? -29.974 -17.979 -8.525  1.00 34.13 ? 36  LEU B CD2 1 
ATOM   2118 N  N   . GLU B 1 11  ? -27.853 -20.589 -4.335  1.00 29.81 ? 37  GLU B N   1 
ATOM   2119 C  CA  . GLU B 1 11  ? -27.144 -21.631 -3.605  1.00 28.90 ? 37  GLU B CA  1 
ATOM   2120 C  C   . GLU B 1 11  ? -28.141 -22.586 -2.959  1.00 29.26 ? 37  GLU B C   1 
ATOM   2121 O  O   . GLU B 1 11  ? -27.978 -23.803 -3.052  1.00 29.89 ? 37  GLU B O   1 
ATOM   2122 C  CB  . GLU B 1 11  ? -26.213 -21.080 -2.522  1.00 28.76 ? 37  GLU B CB  1 
ATOM   2123 C  CG  . GLU B 1 11  ? -25.021 -20.328 -3.080  1.00 26.94 ? 37  GLU B CG  1 
ATOM   2124 C  CD  . GLU B 1 11  ? -24.071 -19.840 -2.028  1.00 27.27 ? 37  GLU B CD  1 
ATOM   2125 O  OE1 . GLU B 1 11  ? -24.534 -19.237 -1.019  1.00 27.67 ? 37  GLU B OE1 1 
ATOM   2126 O  OE2 . GLU B 1 11  ? -22.855 -20.047 -2.236  1.00 26.15 ? 37  GLU B OE2 1 
ATOM   2127 N  N   . ARG B 1 12  ? -29.160 -22.036 -2.294  1.00 29.60 ? 38  ARG B N   1 
ATOM   2128 C  CA  . ARG B 1 12  ? -30.155 -22.864 -1.635  1.00 31.68 ? 38  ARG B CA  1 
ATOM   2129 C  C   . ARG B 1 12  ? -30.907 -23.705 -2.665  1.00 29.52 ? 38  ARG B C   1 
ATOM   2130 O  O   . ARG B 1 12  ? -31.083 -24.899 -2.458  1.00 28.55 ? 38  ARG B O   1 
ATOM   2131 C  CB  . ARG B 1 12  ? -31.169 -22.080 -0.789  1.00 33.92 ? 38  ARG B CB  1 
ATOM   2132 C  CG  . ARG B 1 12  ? -30.576 -21.366 0.419   1.00 36.50 ? 38  ARG B CG  1 
ATOM   2133 C  CD  . ARG B 1 12  ? -31.715 -20.867 1.325   1.00 39.68 ? 38  ARG B CD  1 
ATOM   2134 N  NE  . ARG B 1 12  ? -32.626 -19.919 0.661   1.00 40.05 ? 38  ARG B NE  1 
ATOM   2135 C  CZ  . ARG B 1 12  ? -32.394 -18.623 0.492   1.00 40.99 ? 38  ARG B CZ  1 
ATOM   2136 N  NH1 . ARG B 1 12  ? -31.239 -18.101 0.830   1.00 41.24 ? 38  ARG B NH1 1 
ATOM   2137 N  NH2 . ARG B 1 12  ? -33.318 -17.832 -0.016  1.00 42.52 ? 38  ARG B NH2 1 
ATOM   2138 N  N   . ARG B 1 13  ? -31.336 -23.101 -3.777  1.00 28.10 ? 39  ARG B N   1 
ATOM   2139 C  CA  . ARG B 1 13  ? -32.167 -23.828 -4.730  1.00 28.31 ? 39  ARG B CA  1 
ATOM   2140 C  C   . ARG B 1 13  ? -31.400 -24.947 -5.431  1.00 27.57 ? 39  ARG B C   1 
ATOM   2141 O  O   . ARG B 1 13  ? -31.942 -26.041 -5.627  1.00 28.20 ? 39  ARG B O   1 
ATOM   2142 C  CB  . ARG B 1 13  ? -32.750 -22.851 -5.746  1.00 28.54 ? 39  ARG B CB  1 
ATOM   2143 C  CG  . ARG B 1 13  ? -33.506 -23.495 -6.897  1.00 28.55 ? 39  ARG B CG  1 
ATOM   2144 C  CD  . ARG B 1 13  ? -34.546 -22.533 -7.393  1.00 29.79 ? 39  ARG B CD  1 
ATOM   2145 N  NE  . ARG B 1 13  ? -33.996 -21.185 -7.539  1.00 29.85 ? 39  ARG B NE  1 
ATOM   2146 C  CZ  . ARG B 1 13  ? -33.126 -20.788 -8.470  1.00 30.96 ? 39  ARG B CZ  1 
ATOM   2147 N  NH1 . ARG B 1 13  ? -32.916 -21.512 -9.551  1.00 30.76 ? 39  ARG B NH1 1 
ATOM   2148 N  NH2 . ARG B 1 13  ? -32.509 -19.626 -8.364  1.00 30.87 ? 39  ARG B NH2 1 
ATOM   2149 N  N   . TYR B 1 14  ? -30.141 -24.684 -5.786  1.00 25.78 ? 40  TYR B N   1 
ATOM   2150 C  CA  . TYR B 1 14  ? -29.346 -25.668 -6.495  1.00 26.27 ? 40  TYR B CA  1 
ATOM   2151 C  C   . TYR B 1 14  ? -28.556 -26.551 -5.539  1.00 26.02 ? 40  TYR B C   1 
ATOM   2152 O  O   . TYR B 1 14  ? -27.855 -27.456 -5.982  1.00 26.08 ? 40  TYR B O   1 
ATOM   2153 C  CB  . TYR B 1 14  ? -28.367 -24.961 -7.420  1.00 26.10 ? 40  TYR B CB  1 
ATOM   2154 C  CG  . TYR B 1 14  ? -28.983 -24.437 -8.712  1.00 26.00 ? 40  TYR B CG  1 
ATOM   2155 C  CD1 . TYR B 1 14  ? -29.203 -25.278 -9.798  1.00 25.92 ? 40  TYR B CD1 1 
ATOM   2156 C  CD2 . TYR B 1 14  ? -29.284 -23.091 -8.865  1.00 25.32 ? 40  TYR B CD2 1 
ATOM   2157 C  CE1 . TYR B 1 14  ? -29.718 -24.796 -10.993 1.00 25.84 ? 40  TYR B CE1 1 
ATOM   2158 C  CE2 . TYR B 1 14  ? -29.810 -22.602 -10.048 1.00 25.39 ? 40  TYR B CE2 1 
ATOM   2159 C  CZ  . TYR B 1 14  ? -30.040 -23.457 -11.114 1.00 26.40 ? 40  TYR B CZ  1 
ATOM   2160 O  OH  . TYR B 1 14  ? -30.550 -22.978 -12.291 1.00 27.83 ? 40  TYR B OH  1 
ATOM   2161 N  N   . ASP B 1 15  ? -28.676 -26.282 -4.238  1.00 26.19 ? 41  ASP B N   1 
ATOM   2162 C  CA  . ASP B 1 15  ? -27.854 -26.927 -3.234  1.00 27.00 ? 41  ASP B CA  1 
ATOM   2163 C  C   . ASP B 1 15  ? -26.384 -26.838 -3.645  1.00 26.27 ? 41  ASP B C   1 
ATOM   2164 O  O   . ASP B 1 15  ? -25.723 -27.848 -3.829  1.00 27.84 ? 41  ASP B O   1 
ATOM   2165 C  CB  . ASP B 1 15  ? -28.325 -28.350 -3.009  1.00 27.00 ? 41  ASP B CB  1 
ATOM   2166 C  CG  . ASP B 1 15  ? -27.614 -29.006 -1.843  1.00 28.20 ? 41  ASP B CG  1 
ATOM   2167 O  OD1 . ASP B 1 15  ? -27.302 -28.265 -0.869  1.00 28.08 ? 41  ASP B OD1 1 
ATOM   2168 O  OD2 . ASP B 1 15  ? -27.394 -30.232 -1.927  1.00 28.52 ? 41  ASP B OD2 1 
ATOM   2169 N  N   . ALA B 1 16  ? -25.878 -25.608 -3.755  1.00 26.14 ? 42  ALA B N   1 
ATOM   2170 C  CA  . ALA B 1 16  ? -24.583 -25.343 -4.349  1.00 25.26 ? 42  ALA B CA  1 
ATOM   2171 C  C   . ALA B 1 16  ? -23.840 -24.287 -3.542  1.00 25.76 ? 42  ALA B C   1 
ATOM   2172 O  O   . ALA B 1 16  ? -24.453 -23.592 -2.740  1.00 25.85 ? 42  ALA B O   1 
ATOM   2173 C  CB  . ALA B 1 16  ? -24.816 -24.846 -5.755  1.00 24.84 ? 42  ALA B CB  1 
ATOM   2174 N  N   . ARG B 1 17  ? -22.529 -24.202 -3.768  1.00 24.27 ? 43  ARG B N   1 
ATOM   2175 C  CA  . ARG B 1 17  ? -21.740 -23.064 -3.345  1.00 24.98 ? 43  ARG B CA  1 
ATOM   2176 C  C   . ARG B 1 17  ? -21.402 -22.278 -4.606  1.00 24.58 ? 43  ARG B C   1 
ATOM   2177 O  O   . ARG B 1 17  ? -20.935 -22.871 -5.590  1.00 24.57 ? 43  ARG B O   1 
ATOM   2178 C  CB  . ARG B 1 17  ? -20.482 -23.531 -2.608  1.00 24.73 ? 43  ARG B CB  1 
ATOM   2179 C  CG  . ARG B 1 17  ? -19.684 -22.386 -2.003  1.00 24.98 ? 43  ARG B CG  1 
ATOM   2180 C  CD  . ARG B 1 17  ? -18.504 -22.911 -1.204  1.00 25.87 ? 43  ARG B CD  1 
ATOM   2181 N  NE  . ARG B 1 17  ? -17.561 -23.673 -2.020  1.00 25.56 ? 43  ARG B NE  1 
ATOM   2182 C  CZ  . ARG B 1 17  ? -16.301 -23.405 -2.249  1.00 24.57 ? 43  ARG B CZ  1 
ATOM   2183 N  NH1 . ARG B 1 17  ? -15.704 -22.372 -1.717  1.00 25.43 ? 43  ARG B NH1 1 
ATOM   2184 N  NH2 . ARG B 1 17  ? -15.631 -24.179 -3.044  1.00 25.73 ? 43  ARG B NH2 1 
ATOM   2185 N  N   . LEU B 1 18  ? -21.623 -20.963 -4.559  1.00 25.63 ? 44  LEU B N   1 
ATOM   2186 C  CA  . LEU B 1 18  ? -21.420 -20.092 -5.710  1.00 24.90 ? 44  LEU B CA  1 
ATOM   2187 C  C   . LEU B 1 18  ? -20.416 -19.009 -5.351  1.00 25.03 ? 44  LEU B C   1 
ATOM   2188 O  O   . LEU B 1 18  ? -20.476 -18.433 -4.258  1.00 26.03 ? 44  LEU B O   1 
ATOM   2189 C  CB  . LEU B 1 18  ? -22.748 -19.461 -6.133  1.00 26.23 ? 44  LEU B CB  1 
ATOM   2190 C  CG  . LEU B 1 18  ? -22.650 -18.354 -7.188  1.00 25.54 ? 44  LEU B CG  1 
ATOM   2191 C  CD1 . LEU B 1 18  ? -22.210 -18.941 -8.518  1.00 25.27 ? 44  LEU B CD1 1 
ATOM   2192 C  CD2 . LEU B 1 18  ? -23.973 -17.638 -7.309  1.00 26.25 ? 44  LEU B CD2 1 
ATOM   2193 N  N   . GLY B 1 19  ? -19.498 -18.760 -6.283  1.00 23.74 ? 45  GLY B N   1 
ATOM   2194 C  CA  . GLY B 1 19  ? -18.519 -17.706 -6.136  1.00 24.24 ? 45  GLY B CA  1 
ATOM   2195 C  C   . GLY B 1 19  ? -18.548 -16.791 -7.356  1.00 23.51 ? 45  GLY B C   1 
ATOM   2196 O  O   . GLY B 1 19  ? -18.537 -17.275 -8.491  1.00 21.95 ? 45  GLY B O   1 
ATOM   2197 N  N   . VAL B 1 20  ? -18.548 -15.478 -7.103  1.00 23.72 ? 46  VAL B N   1 
ATOM   2198 C  CA  . VAL B 1 20  ? -18.644 -14.469 -8.146  1.00 23.64 ? 46  VAL B CA  1 
ATOM   2199 C  C   . VAL B 1 20  ? -17.653 -13.352 -7.871  1.00 23.73 ? 46  VAL B C   1 
ATOM   2200 O  O   . VAL B 1 20  ? -17.572 -12.854 -6.753  1.00 24.13 ? 46  VAL B O   1 
ATOM   2201 C  CB  . VAL B 1 20  ? -20.062 -13.882 -8.245  1.00 25.50 ? 46  VAL B CB  1 
ATOM   2202 C  CG1 . VAL B 1 20  ? -20.135 -12.852 -9.372  1.00 26.07 ? 46  VAL B CG1 1 
ATOM   2203 C  CG2 . VAL B 1 20  ? -21.109 -14.988 -8.421  1.00 25.04 ? 46  VAL B CG2 1 
ATOM   2204 N  N   . TYR B 1 21  ? -16.901 -12.958 -8.911  1.00 23.41 ? 47  TYR B N   1 
ATOM   2205 C  CA  . TYR B 1 21  ? -16.127 -11.736 -8.837  1.00 23.43 ? 47  TYR B CA  1 
ATOM   2206 C  C   . TYR B 1 21  ? -16.221 -10.998 -10.166 1.00 23.42 ? 47  TYR B C   1 
ATOM   2207 O  O   . TYR B 1 21  ? -16.010 -11.586 -11.238 1.00 22.58 ? 47  TYR B O   1 
ATOM   2208 C  CB  . TYR B 1 21  ? -14.649 -11.969 -8.515  1.00 23.61 ? 47  TYR B CB  1 
ATOM   2209 C  CG  . TYR B 1 21  ? -13.973 -10.685 -8.066  1.00 25.16 ? 47  TYR B CG  1 
ATOM   2210 C  CD1 . TYR B 1 21  ? -14.237 -10.116 -6.824  1.00 27.05 ? 47  TYR B CD1 1 
ATOM   2211 C  CD2 . TYR B 1 21  ? -13.082 -10.022 -8.898  1.00 25.24 ? 47  TYR B CD2 1 
ATOM   2212 C  CE1 . TYR B 1 21  ? -13.590 -8.960  -6.405  1.00 27.38 ? 47  TYR B CE1 1 
ATOM   2213 C  CE2 . TYR B 1 21  ? -12.470 -8.839  -8.511  1.00 26.35 ? 47  TYR B CE2 1 
ATOM   2214 C  CZ  . TYR B 1 21  ? -12.716 -8.309  -7.265  1.00 28.00 ? 47  TYR B CZ  1 
ATOM   2215 O  OH  . TYR B 1 21  ? -12.091 -7.141  -6.923  1.00 30.78 ? 47  TYR B OH  1 
ATOM   2216 N  N   . VAL B 1 22  ? -16.483 -9.706  -10.054 1.00 23.89 ? 48  VAL B N   1 
ATOM   2217 C  CA  . VAL B 1 22  ? -16.358 -8.766  -11.148 1.00 25.26 ? 48  VAL B CA  1 
ATOM   2218 C  C   . VAL B 1 22  ? -15.530 -7.594  -10.634 1.00 26.18 ? 48  VAL B C   1 
ATOM   2219 O  O   . VAL B 1 22  ? -15.952 -6.922  -9.706  1.00 25.62 ? 48  VAL B O   1 
ATOM   2220 C  CB  . VAL B 1 22  ? -17.723 -8.263  -11.654 1.00 26.31 ? 48  VAL B CB  1 
ATOM   2221 C  CG1 . VAL B 1 22  ? -17.563 -7.323  -12.842 1.00 26.81 ? 48  VAL B CG1 1 
ATOM   2222 C  CG2 . VAL B 1 22  ? -18.670 -9.404  -11.991 1.00 25.81 ? 48  VAL B CG2 1 
ATOM   2223 N  N   . PRO B 1 23  ? -14.324 -7.338  -11.189 1.00 25.64 ? 49  PRO B N   1 
ATOM   2224 C  CA  . PRO B 1 23  ? -13.496 -6.214  -10.767 1.00 26.34 ? 49  PRO B CA  1 
ATOM   2225 C  C   . PRO B 1 23  ? -14.235 -4.894  -10.963 1.00 27.47 ? 49  PRO B C   1 
ATOM   2226 O  O   . PRO B 1 23  ? -15.092 -4.762  -11.830 1.00 27.18 ? 49  PRO B O   1 
ATOM   2227 C  CB  . PRO B 1 23  ? -12.234 -6.309  -11.643 1.00 26.60 ? 49  PRO B CB  1 
ATOM   2228 C  CG  . PRO B 1 23  ? -12.201 -7.751  -12.085 1.00 25.67 ? 49  PRO B CG  1 
ATOM   2229 C  CD  . PRO B 1 23  ? -13.661 -8.176  -12.195 1.00 24.99 ? 49  PRO B CD  1 
ATOM   2230 N  N   . ALA B 1 24  ? -13.910 -3.931  -10.112 1.00 28.42 ? 50  ALA B N   1 
ATOM   2231 C  CA  . ALA B 1 24  ? -14.397 -2.572  -10.266 1.00 29.64 ? 50  ALA B CA  1 
ATOM   2232 C  C   . ALA B 1 24  ? -13.946 -2.017  -11.620 1.00 30.57 ? 50  ALA B C   1 
ATOM   2233 O  O   . ALA B 1 24  ? -12.879 -2.368  -12.127 1.00 28.77 ? 50  ALA B O   1 
ATOM   2234 C  CB  . ALA B 1 24  ? -13.911 -1.718  -9.131  1.00 30.24 ? 50  ALA B CB  1 
ATOM   2235 N  N   . THR B 1 25  ? -14.806 -1.179  -12.201 1.00 32.42 ? 51  THR B N   1 
ATOM   2236 C  CA  . THR B 1 25  ? -14.522 -0.505  -13.460 1.00 33.94 ? 51  THR B CA  1 
ATOM   2237 C  C   . THR B 1 25  ? -14.773 0.978   -13.211 1.00 35.51 ? 51  THR B C   1 
ATOM   2238 O  O   . THR B 1 25  ? -15.072 1.368   -12.082 1.00 35.26 ? 51  THR B O   1 
ATOM   2239 C  CB  . THR B 1 25  ? -15.409 -1.049  -14.582 1.00 32.81 ? 51  THR B CB  1 
ATOM   2240 O  OG1 . THR B 1 25  ? -16.727 -0.594  -14.287 1.00 34.37 ? 51  THR B OG1 1 
ATOM   2241 C  CG2 . THR B 1 25  ? -15.408 -2.558  -14.676 1.00 32.35 ? 51  THR B CG2 1 
ATOM   2242 N  N   . GLY B 1 26  ? -14.677 1.779   -14.279 1.00 36.21 ? 52  GLY B N   1 
ATOM   2243 C  CA  . GLY B 1 26  ? -14.950 3.200   -14.197 1.00 38.77 ? 52  GLY B CA  1 
ATOM   2244 C  C   . GLY B 1 26  ? -16.423 3.523   -13.935 1.00 41.19 ? 52  GLY B C   1 
ATOM   2245 O  O   . GLY B 1 26  ? -16.744 4.690   -13.721 1.00 45.65 ? 52  GLY B O   1 
ATOM   2246 N  N   . THR B 1 27  ? -17.324 2.536   -13.991 1.00 43.54 ? 53  THR B N   1 
ATOM   2247 C  CA  . THR B 1 27  ? -18.742 2.804   -13.765 1.00 46.17 ? 53  THR B CA  1 
ATOM   2248 C  C   . THR B 1 27  ? -19.334 1.890   -12.692 1.00 45.51 ? 53  THR B C   1 
ATOM   2249 O  O   . THR B 1 27  ? -20.434 2.172   -12.228 1.00 47.36 ? 53  THR B O   1 
ATOM   2250 C  CB  . THR B 1 27  ? -19.507 2.649   -15.081 1.00 50.40 ? 53  THR B CB  1 
ATOM   2251 O  OG1 . THR B 1 27  ? -19.361 1.300   -15.518 1.00 51.90 ? 53  THR B OG1 1 
ATOM   2252 C  CG2 . THR B 1 27  ? -18.978 3.566   -16.174 1.00 52.49 ? 53  THR B CG2 1 
ATOM   2253 N  N   . THR B 1 28  ? -18.639 0.805   -12.313 1.00 41.84 ? 54  THR B N   1 
ATOM   2254 C  CA  . THR B 1 28  ? -19.206 -0.174  -11.395 1.00 39.15 ? 54  THR B CA  1 
ATOM   2255 C  C   . THR B 1 28  ? -18.201 -0.520  -10.293 1.00 36.38 ? 54  THR B C   1 
ATOM   2256 O  O   . THR B 1 28  ? -16.991 -0.642  -10.537 1.00 34.48 ? 54  THR B O   1 
ATOM   2257 C  CB  . THR B 1 28  ? -19.657 -1.428  -12.158 1.00 39.81 ? 54  THR B CB  1 
ATOM   2258 O  OG1 . THR B 1 28  ? -18.510 -1.987  -12.792 1.00 38.79 ? 54  THR B OG1 1 
ATOM   2259 C  CG2 . THR B 1 28  ? -20.787 -1.123  -13.130 1.00 41.32 ? 54  THR B CG2 1 
ATOM   2260 N  N   . ALA B 1 29  ? -18.740 -0.714  -9.075  1.00 33.40 ? 55  ALA B N   1 
ATOM   2261 C  CA  . ALA B 1 29  ? -17.966 -1.269  -7.976  1.00 32.29 ? 55  ALA B CA  1 
ATOM   2262 C  C   . ALA B 1 29  ? -17.749 -2.760  -8.207  1.00 30.30 ? 55  ALA B C   1 
ATOM   2263 O  O   . ALA B 1 29  ? -18.506 -3.411  -8.936  1.00 29.69 ? 55  ALA B O   1 
ATOM   2264 C  CB  . ALA B 1 29  ? -18.651 -1.027  -6.643  1.00 32.79 ? 55  ALA B CB  1 
ATOM   2265 N  N   . ALA B 1 30  ? -16.714 -3.302  -7.565  1.00 29.33 ? 56  ALA B N   1 
ATOM   2266 C  CA  . ALA B 1 30  ? -16.494 -4.742  -7.587  1.00 28.77 ? 56  ALA B CA  1 
ATOM   2267 C  C   . ALA B 1 30  ? -17.757 -5.471  -7.124  1.00 28.80 ? 56  ALA B C   1 
ATOM   2268 O  O   . ALA B 1 30  ? -18.458 -5.011  -6.229  1.00 28.57 ? 56  ALA B O   1 
ATOM   2269 C  CB  . ALA B 1 30  ? -15.282 -5.108  -6.758  1.00 28.66 ? 56  ALA B CB  1 
ATOM   2270 N  N   . ILE B 1 31  ? -18.068 -6.601  -7.787  1.00 28.14 ? 57  ILE B N   1 
ATOM   2271 C  CA  . ILE B 1 31  ? -19.109 -7.494  -7.312  1.00 28.89 ? 57  ILE B CA  1 
ATOM   2272 C  C   . ILE B 1 31  ? -18.383 -8.696  -6.706  1.00 29.03 ? 57  ILE B C   1 
ATOM   2273 O  O   . ILE B 1 31  ? -17.487 -9.240  -7.345  1.00 27.42 ? 57  ILE B O   1 
ATOM   2274 C  CB  . ILE B 1 31  ? -20.084 -7.866  -8.449  1.00 29.33 ? 57  ILE B CB  1 
ATOM   2275 C  CG1 . ILE B 1 31  ? -20.831 -6.641  -8.967  1.00 29.75 ? 57  ILE B CG1 1 
ATOM   2276 C  CG2 . ILE B 1 31  ? -21.052 -8.970  -8.024  1.00 29.59 ? 57  ILE B CG2 1 
ATOM   2277 C  CD1 . ILE B 1 31  ? -21.484 -6.851  -10.319 1.00 30.40 ? 57  ILE B CD1 1 
ATOM   2278 N  N   . GLU B 1 32  ? -18.696 -9.017  -5.440  1.00 29.71 ? 59  GLU B N   1 
ATOM   2279 C  CA  . GLU B 1 32  ? -18.022 -10.108 -4.756  1.00 31.55 ? 59  GLU B CA  1 
ATOM   2280 C  C   . GLU B 1 32  ? -19.045 -10.954 -4.004  1.00 29.44 ? 59  GLU B C   1 
ATOM   2281 O  O   . GLU B 1 32  ? -19.878 -10.424 -3.268  1.00 27.40 ? 59  GLU B O   1 
ATOM   2282 C  CB  . GLU B 1 32  ? -16.854 -9.704  -3.851  1.00 35.74 ? 59  GLU B CB  1 
ATOM   2283 C  CG  . GLU B 1 32  ? -16.902 -8.269  -3.346  1.00 43.18 ? 59  GLU B CG  1 
ATOM   2284 C  CD  . GLU B 1 32  ? -15.652 -7.880  -2.567  1.00 49.01 ? 59  GLU B CD  1 
ATOM   2285 O  OE1 . GLU B 1 32  ? -14.524 -7.779  -3.132  1.00 49.99 ? 59  GLU B OE1 1 
ATOM   2286 O  OE2 . GLU B 1 32  ? -15.838 -7.702  -1.350  1.00 58.15 ? 59  GLU B OE2 1 
ATOM   2287 N  N   . TYR B 1 33  ? -18.986 -12.275 -4.245  1.00 26.95 ? 60  TYR B N   1 
ATOM   2288 C  CA  . TYR B 1 33  ? -19.760 -13.215 -3.468  1.00 26.55 ? 60  TYR B CA  1 
ATOM   2289 C  C   . TYR B 1 33  ? -18.901 -14.460 -3.299  1.00 25.84 ? 60  TYR B C   1 
ATOM   2290 O  O   . TYR B 1 33  ? -18.561 -15.100 -4.288  1.00 25.15 ? 60  TYR B O   1 
ATOM   2291 C  CB  . TYR B 1 33  ? -21.126 -13.455 -4.116  1.00 27.29 ? 60  TYR B CB  1 
ATOM   2292 C  CG  . TYR B 1 33  ? -22.033 -14.321 -3.250  1.00 26.99 ? 60  TYR B CG  1 
ATOM   2293 C  CD1 . TYR B 1 33  ? -22.775 -13.768 -2.220  1.00 28.12 ? 60  TYR B CD1 1 
ATOM   2294 C  CD2 . TYR B 1 33  ? -22.080 -15.701 -3.409  1.00 25.86 ? 60  TYR B CD2 1 
ATOM   2295 C  CE1 . TYR B 1 33  ? -23.558 -14.546 -1.388  1.00 28.20 ? 60  TYR B CE1 1 
ATOM   2296 C  CE2 . TYR B 1 33  ? -22.873 -16.489 -2.597  1.00 26.62 ? 60  TYR B CE2 1 
ATOM   2297 C  CZ  . TYR B 1 33  ? -23.617 -15.914 -1.584  1.00 27.52 ? 60  TYR B CZ  1 
ATOM   2298 O  OH  . TYR B 1 33  ? -24.428 -16.673 -0.781  1.00 27.97 ? 60  TYR B OH  1 
ATOM   2299 N  N   . ARG B 1 34  ? -18.473 -14.722 -2.048  1.00 26.17 ? 61  ARG B N   1 
ATOM   2300 C  CA  . ARG B 1 34  ? -17.519 -15.790 -1.755  1.00 25.83 ? 61  ARG B CA  1 
ATOM   2301 C  C   . ARG B 1 34  ? -16.304 -15.668 -2.676  1.00 26.17 ? 61  ARG B C   1 
ATOM   2302 O  O   . ARG B 1 34  ? -15.680 -16.665 -3.086  1.00 25.41 ? 61  ARG B O   1 
ATOM   2303 C  CB  . ARG B 1 34  ? -18.163 -17.174 -1.917  1.00 24.95 ? 61  ARG B CB  1 
ATOM   2304 C  CG  . ARG B 1 34  ? -19.387 -17.380 -1.026  1.00 25.72 ? 61  ARG B CG  1 
ATOM   2305 C  CD  . ARG B 1 34  ? -19.713 -18.863 -1.041  1.00 26.16 ? 61  ARG B CD  1 
ATOM   2306 N  NE  . ARG B 1 34  ? -20.995 -19.185 -0.410  1.00 26.69 ? 61  ARG B NE  1 
ATOM   2307 C  CZ  . ARG B 1 34  ? -21.231 -19.301 0.872   1.00 28.18 ? 61  ARG B CZ  1 
ATOM   2308 N  NH1 . ARG B 1 34  ? -20.270 -19.131 1.760   1.00 28.91 ? 61  ARG B NH1 1 
ATOM   2309 N  NH2 . ARG B 1 34  ? -22.461 -19.576 1.277   1.00 29.80 ? 61  ARG B NH2 1 
ATOM   2310 N  N   . ALA B 1 35  ? -15.939 -14.419 -2.973  1.00 26.10 ? 62  ALA B N   1 
ATOM   2311 C  CA  . ALA B 1 35  ? -14.953 -14.161 -4.003  1.00 25.92 ? 62  ALA B CA  1 
ATOM   2312 C  C   . ALA B 1 35  ? -13.568 -14.614 -3.561  1.00 25.13 ? 62  ALA B C   1 
ATOM   2313 O  O   . ALA B 1 35  ? -12.703 -14.802 -4.415  1.00 25.08 ? 62  ALA B O   1 
ATOM   2314 C  CB  . ALA B 1 35  ? -14.959 -12.689 -4.382  1.00 26.17 ? 62  ALA B CB  1 
ATOM   2315 N  N   . ASP B 1 36  ? -13.349 -14.736 -2.252  1.00 25.25 ? 63  ASP B N   1 
ATOM   2316 C  CA  . ASP B 1 36  ? -12.038 -15.114 -1.772  1.00 27.07 ? 63  ASP B CA  1 
ATOM   2317 C  C   . ASP B 1 36  ? -12.029 -16.541 -1.230  1.00 27.76 ? 63  ASP B C   1 
ATOM   2318 O  O   . ASP B 1 36  ? -11.037 -16.960 -0.638  1.00 28.04 ? 63  ASP B O   1 
ATOM   2319 C  CB  . ASP B 1 36  ? -11.513 -14.149 -0.729  1.00 30.13 ? 63  ASP B CB  1 
ATOM   2320 C  CG  . ASP B 1 36  ? -11.403 -12.711 -1.207  1.00 30.50 ? 63  ASP B CG  1 
ATOM   2321 O  OD1 . ASP B 1 36  ? -10.770 -12.482 -2.278  1.00 27.36 ? 63  ASP B OD1 1 
ATOM   2322 O  OD2 . ASP B 1 36  ? -11.903 -11.837 -0.444  1.00 32.68 ? 63  ASP B OD2 1 
ATOM   2323 N  N   . GLU B 1 37  ? -13.121 -17.278 -1.435  1.00 27.16 ? 64  GLU B N   1 
ATOM   2324 C  CA  . GLU B 1 37  ? -13.138 -18.703 -1.139  1.00 26.61 ? 64  GLU B CA  1 
ATOM   2325 C  C   . GLU B 1 37  ? -12.515 -19.476 -2.295  1.00 26.99 ? 64  GLU B C   1 
ATOM   2326 O  O   . GLU B 1 37  ? -12.664 -19.114 -3.465  1.00 25.95 ? 64  GLU B O   1 
ATOM   2327 C  CB  . GLU B 1 37  ? -14.553 -19.214 -0.890  1.00 25.89 ? 64  GLU B CB  1 
ATOM   2328 C  CG  . GLU B 1 37  ? -15.215 -18.647 0.363   1.00 26.07 ? 64  GLU B CG  1 
ATOM   2329 C  CD  . GLU B 1 37  ? -16.525 -19.333 0.682   1.00 26.08 ? 64  GLU B CD  1 
ATOM   2330 O  OE1 . GLU B 1 37  ? -16.780 -20.484 0.226   1.00 25.98 ? 64  GLU B OE1 1 
ATOM   2331 O  OE2 . GLU B 1 37  ? -17.342 -18.693 1.345   1.00 26.74 ? 64  GLU B OE2 1 
ATOM   2332 N  N   . ARG B 1 38  ? -11.834 -20.571 -1.960  1.00 26.35 ? 65  ARG B N   1 
ATOM   2333 C  CA  . ARG B 1 38  ? -11.175 -21.378 -2.976  1.00 26.09 ? 65  ARG B CA  1 
ATOM   2334 C  C   . ARG B 1 38  ? -12.195 -22.265 -3.682  1.00 24.05 ? 65  ARG B C   1 
ATOM   2335 O  O   . ARG B 1 38  ? -13.068 -22.869 -3.059  1.00 23.79 ? 65  ARG B O   1 
ATOM   2336 C  CB  . ARG B 1 38  ? -10.051 -22.230 -2.369  1.00 27.02 ? 65  ARG B CB  1 
ATOM   2337 C  CG  . ARG B 1 38  ? -8.824  -21.418 -1.997  1.00 27.28 ? 65  ARG B CG  1 
ATOM   2338 C  CD  . ARG B 1 38  ? -7.825  -22.277 -1.257  1.00 27.95 ? 65  ARG B CD  1 
ATOM   2339 N  NE  . ARG B 1 38  ? -6.591  -21.528 -0.983  1.00 28.45 ? 65  ARG B NE  1 
ATOM   2340 C  CZ  . ARG B 1 38  ? -5.663  -21.150 -1.837  1.00 30.18 ? 65  ARG B CZ  1 
ATOM   2341 N  NH1 . ARG B 1 38  ? -5.683  -21.569 -3.099  1.00 28.61 ? 65  ARG B NH1 1 
ATOM   2342 N  NH2 . ARG B 1 38  ? -4.714  -20.323 -1.414  1.00 30.86 ? 65  ARG B NH2 1 
ATOM   2343 N  N   . PHE B 1 39  ? -12.045 -22.343 -5.003  1.00 22.30 ? 66  PHE B N   1 
ATOM   2344 C  CA  . PHE B 1 39  ? -12.783 -23.282 -5.820  1.00 20.78 ? 66  PHE B CA  1 
ATOM   2345 C  C   . PHE B 1 39  ? -11.797 -23.972 -6.743  1.00 20.80 ? 66  PHE B C   1 
ATOM   2346 O  O   . PHE B 1 39  ? -10.859 -23.333 -7.196  1.00 21.83 ? 66  PHE B O   1 
ATOM   2347 C  CB  . PHE B 1 39  ? -13.836 -22.542 -6.645  1.00 20.88 ? 66  PHE B CB  1 
ATOM   2348 C  CG  . PHE B 1 39  ? -15.028 -21.937 -5.910  1.00 21.51 ? 66  PHE B CG  1 
ATOM   2349 C  CD1 . PHE B 1 39  ? -14.912 -20.722 -5.250  1.00 22.29 ? 66  PHE B CD1 1 
ATOM   2350 C  CD2 . PHE B 1 39  ? -16.278 -22.540 -5.956  1.00 22.62 ? 66  PHE B CD2 1 
ATOM   2351 C  CE1 . PHE B 1 39  ? -16.000 -20.159 -4.610  1.00 23.28 ? 66  PHE B CE1 1 
ATOM   2352 C  CE2 . PHE B 1 39  ? -17.363 -21.975 -5.319  1.00 23.37 ? 66  PHE B CE2 1 
ATOM   2353 C  CZ  . PHE B 1 39  ? -17.228 -20.782 -4.658  1.00 23.87 ? 66  PHE B CZ  1 
ATOM   2354 N  N   . ALA B 1 40  ? -12.058 -25.241 -7.065  1.00 20.67 ? 67  ALA B N   1 
ATOM   2355 C  CA  . ALA B 1 40  ? -11.287 -25.952 -8.066  1.00 21.19 ? 67  ALA B CA  1 
ATOM   2356 C  C   . ALA B 1 40  ? -11.296 -25.194 -9.392  1.00 20.93 ? 67  ALA B C   1 
ATOM   2357 O  O   . ALA B 1 40  ? -12.360 -24.857 -9.887  1.00 20.83 ? 67  ALA B O   1 
ATOM   2358 C  CB  . ALA B 1 40  ? -11.855 -27.342 -8.256  1.00 22.10 ? 67  ALA B CB  1 
ATOM   2359 N  N   . PHE B 1 41  ? -10.107 -24.973 -9.971  1.00 20.04 ? 68  PHE B N   1 
ATOM   2360 C  CA  . PHE B 1 41  ? -9.990  -24.435 -11.319 1.00 20.81 ? 68  PHE B CA  1 
ATOM   2361 C  C   . PHE B 1 41  ? -10.798 -25.236 -12.348 1.00 20.84 ? 68  PHE B C   1 
ATOM   2362 O  O   . PHE B 1 41  ? -11.452 -24.684 -13.227 1.00 22.05 ? 68  PHE B O   1 
ATOM   2363 C  CB  . PHE B 1 41  ? -8.552  -24.573 -11.817 1.00 20.85 ? 68  PHE B CB  1 
ATOM   2364 C  CG  . PHE B 1 41  ? -7.550  -23.484 -11.491 1.00 20.88 ? 68  PHE B CG  1 
ATOM   2365 C  CD1 . PHE B 1 41  ? -7.598  -22.264 -12.161 1.00 21.51 ? 68  PHE B CD1 1 
ATOM   2366 C  CD2 . PHE B 1 41  ? -6.478  -23.734 -10.655 1.00 22.34 ? 68  PHE B CD2 1 
ATOM   2367 C  CE1 . PHE B 1 41  ? -6.626  -21.301 -11.954 1.00 22.25 ? 68  PHE B CE1 1 
ATOM   2368 C  CE2 . PHE B 1 41  ? -5.525  -22.748 -10.413 1.00 22.99 ? 68  PHE B CE2 1 
ATOM   2369 C  CZ  . PHE B 1 41  ? -5.591  -21.540 -11.086 1.00 22.99 ? 68  PHE B CZ  1 
ATOM   2370 N  N   . CYS B 1 42  ? -10.688 -26.556 -12.286 1.00 20.91 ? 69  CYS B N   1 
ATOM   2371 C  CA  . CYS B 1 42  ? -11.031 -27.398 -13.420 1.00 21.63 ? 69  CYS B CA  1 
ATOM   2372 C  C   . CYS B 1 42  ? -10.375 -26.777 -14.659 1.00 21.85 ? 69  CYS B C   1 
ATOM   2373 O  O   . CYS B 1 42  ? -9.263  -26.240 -14.573 1.00 21.35 ? 69  CYS B O   1 
ATOM   2374 C  CB  . CYS B 1 42  ? -12.543 -27.646 -13.470 1.00 23.00 ? 69  CYS B CB  1 
ATOM   2375 S  SG  . CYS B 1 42  ? -13.220 -28.281 -11.902 1.00 22.76 ? 69  CYS B SG  1 
ATOM   2376 N  N   . SER B 1 43  ? -11.054 -26.839 -15.807 1.00 19.70 ? 70  SER B N   1 
ATOM   2377 C  CA  . SER B 1 43  ? -10.432 -26.446 -17.067 1.00 20.57 ? 70  SER B CA  1 
ATOM   2378 C  C   . SER B 1 43  ? -10.238 -24.933 -17.208 1.00 19.63 ? 70  SER B C   1 
ATOM   2379 O  O   . SER B 1 43  ? -9.641  -24.500 -18.179 1.00 19.33 ? 70  SER B O   1 
ATOM   2380 C  CB  . SER B 1 43  ? -11.214 -27.013 -18.226 1.00 20.13 ? 70  SER B CB  1 
ATOM   2381 O  OG  . SER B 1 43  ? -10.852 -28.384 -18.423 1.00 22.20 ? 70  SER B OG  1 
ATOM   2382 N  N   . THR B 1 44  ? -10.664 -24.118 -16.227 1.00 20.08 ? 71  THR B N   1 
ATOM   2383 C  CA  . THR B 1 44  ? -10.427 -22.682 -16.345 1.00 20.24 ? 71  THR B CA  1 
ATOM   2384 C  C   . THR B 1 44  ? -8.932  -22.363 -16.401 1.00 20.61 ? 71  THR B C   1 
ATOM   2385 O  O   . THR B 1 44  ? -8.556  -21.348 -16.983 1.00 21.46 ? 71  THR B O   1 
ATOM   2386 C  CB  . THR B 1 44  ? -11.138 -21.869 -15.267 1.00 20.15 ? 71  THR B CB  1 
ATOM   2387 O  OG1 . THR B 1 44  ? -10.597 -22.199 -13.987 1.00 20.23 ? 71  THR B OG1 1 
ATOM   2388 C  CG2 . THR B 1 44  ? -12.651 -21.999 -15.376 1.00 19.97 ? 71  THR B CG2 1 
ATOM   2389 N  N   . PHE B 1 45  ? -8.065  -23.238 -15.870 1.00 20.35 ? 72  PHE B N   1 
ATOM   2390 C  CA  . PHE B 1 45  ? -6.629  -22.965 -15.837 1.00 19.73 ? 72  PHE B CA  1 
ATOM   2391 C  C   . PHE B 1 45  ? -6.033  -22.965 -17.251 1.00 20.07 ? 72  PHE B C   1 
ATOM   2392 O  O   . PHE B 1 45  ? -4.952  -22.412 -17.458 1.00 20.65 ? 72  PHE B O   1 
ATOM   2393 C  CB  . PHE B 1 45  ? -5.885  -23.990 -14.970 1.00 20.59 ? 72  PHE B CB  1 
ATOM   2394 C  CG  . PHE B 1 45  ? -5.510  -25.292 -15.646 1.00 20.97 ? 72  PHE B CG  1 
ATOM   2395 C  CD1 . PHE B 1 45  ? -6.437  -26.302 -15.816 1.00 20.66 ? 72  PHE B CD1 1 
ATOM   2396 C  CD2 . PHE B 1 45  ? -4.234  -25.488 -16.166 1.00 21.69 ? 72  PHE B CD2 1 
ATOM   2397 C  CE1 . PHE B 1 45  ? -6.101  -27.489 -16.447 1.00 21.83 ? 72  PHE B CE1 1 
ATOM   2398 C  CE2 . PHE B 1 45  ? -3.900  -26.679 -16.796 1.00 22.12 ? 72  PHE B CE2 1 
ATOM   2399 C  CZ  . PHE B 1 45  ? -4.837  -27.667 -16.963 1.00 21.84 ? 72  PHE B CZ  1 
ATOM   2400 N  N   . LYS B 1 46  ? -6.746  -23.559 -18.209 1.00 19.68 ? 73  LYS B N   1 
ATOM   2401 C  CA  . LYS B 1 46  ? -6.231  -23.686 -19.568 1.00 20.99 ? 73  LYS B CA  1 
ATOM   2402 C  C   . LYS B 1 46  ? -6.022  -22.314 -20.211 1.00 22.20 ? 73  LYS B C   1 
ATOM   2403 O  O   . LYS B 1 46  ? -5.168  -22.169 -21.093 1.00 22.69 ? 73  LYS B O   1 
ATOM   2404 C  CB  . LYS B 1 46  ? -7.122  -24.591 -20.427 1.00 19.31 ? 73  LYS B CB  1 
ATOM   2405 C  CG  . LYS B 1 46  ? -7.078  -26.032 -19.945 1.00 21.12 ? 73  LYS B CG  1 
ATOM   2406 C  CD  . LYS B 1 46  ? -8.100  -27.007 -20.516 1.00 21.93 ? 73  LYS B CD  1 
ATOM   2407 C  CE  . LYS B 1 46  ? -7.977  -28.357 -19.877 1.00 23.40 ? 73  LYS B CE  1 
ATOM   2408 N  NZ  . LYS B 1 46  ? -9.033  -29.250 -20.347 1.00 25.20 ? 73  LYS B NZ  1 
ATOM   2409 N  N   . ALA B 1 47  ? -6.805  -21.320 -19.806 1.00 22.71 ? 74  ALA B N   1 
ATOM   2410 C  CA  . ALA B 1 47  ? -6.657  -19.985 -20.380 1.00 23.92 ? 74  ALA B CA  1 
ATOM   2411 C  C   . ALA B 1 47  ? -5.324  -19.372 -19.951 1.00 23.50 ? 74  ALA B C   1 
ATOM   2412 O  O   . ALA B 1 47  ? -4.511  -19.030 -20.803 1.00 24.25 ? 74  ALA B O   1 
ATOM   2413 C  CB  . ALA B 1 47  ? -7.838  -19.120 -20.031 1.00 25.04 ? 74  ALA B CB  1 
ATOM   2414 N  N   . PRO B 1 48  ? -5.021  -19.186 -18.644 1.00 21.45 ? 75  PRO B N   1 
ATOM   2415 C  CA  . PRO B 1 48  ? -3.688  -18.729 -18.250 1.00 21.26 ? 75  PRO B CA  1 
ATOM   2416 C  C   . PRO B 1 48  ? -2.531  -19.655 -18.637 1.00 21.52 ? 75  PRO B C   1 
ATOM   2417 O  O   . PRO B 1 48  ? -1.406  -19.187 -18.807 1.00 22.48 ? 75  PRO B O   1 
ATOM   2418 C  CB  . PRO B 1 48  ? -3.804  -18.527 -16.748 1.00 21.14 ? 75  PRO B CB  1 
ATOM   2419 C  CG  . PRO B 1 48  ? -5.019  -19.333 -16.349 1.00 20.99 ? 75  PRO B CG  1 
ATOM   2420 C  CD  . PRO B 1 48  ? -5.950  -19.240 -17.512 1.00 21.00 ? 75  PRO B CD  1 
ATOM   2421 N  N   . LEU B 1 49  ? -2.798  -20.959 -18.799 1.00 21.25 ? 76  LEU B N   1 
ATOM   2422 C  CA  . LEU B 1 49  ? -1.780  -21.882 -19.285 1.00 21.01 ? 76  LEU B CA  1 
ATOM   2423 C  C   . LEU B 1 49  ? -1.309  -21.481 -20.686 1.00 20.64 ? 76  LEU B C   1 
ATOM   2424 O  O   . LEU B 1 49  ? -0.103  -21.414 -20.950 1.00 20.91 ? 76  LEU B O   1 
ATOM   2425 C  CB  . LEU B 1 49  ? -2.312  -23.318 -19.300 1.00 20.73 ? 76  LEU B CB  1 
ATOM   2426 C  CG  . LEU B 1 49  ? -1.385  -24.351 -19.946 1.00 21.49 ? 76  LEU B CG  1 
ATOM   2427 C  CD1 . LEU B 1 49  ? -0.067  -24.456 -19.199 1.00 23.28 ? 76  LEU B CD1 1 
ATOM   2428 C  CD2 . LEU B 1 49  ? -2.056  -25.734 -20.023 1.00 21.86 ? 76  LEU B CD2 1 
ATOM   2429 N  N   . VAL B 1 50  ? -2.267  -21.211 -21.576 1.00 20.16 ? 77  VAL B N   1 
ATOM   2430 C  CA  . VAL B 1 50  ? -1.957  -20.815 -22.934 1.00 21.47 ? 77  VAL B CA  1 
ATOM   2431 C  C   . VAL B 1 50  ? -1.199  -19.494 -22.898 1.00 22.51 ? 77  VAL B C   1 
ATOM   2432 O  O   . VAL B 1 50  ? -0.207  -19.324 -23.609 1.00 21.64 ? 77  VAL B O   1 
ATOM   2433 C  CB  . VAL B 1 50  ? -3.231  -20.765 -23.802 1.00 21.35 ? 77  VAL B CB  1 
ATOM   2434 C  CG1 . VAL B 1 50  ? -3.043  -19.982 -25.101 1.00 22.20 ? 77  VAL B CG1 1 
ATOM   2435 C  CG2 . VAL B 1 50  ? -3.711  -22.170 -24.071 1.00 21.41 ? 77  VAL B CG2 1 
ATOM   2436 N  N   . ALA B 1 51  ? -1.612  -18.588 -21.997 1.00 21.66 ? 78  ALA B N   1 
ATOM   2437 C  CA  . ALA B 1 51  ? -0.903  -17.326 -21.832 1.00 21.29 ? 78  ALA B CA  1 
ATOM   2438 C  C   . ALA B 1 51  ? 0.552   -17.572 -21.419 1.00 21.45 ? 78  ALA B C   1 
ATOM   2439 O  O   . ALA B 1 51  ? 1.466   -16.906 -21.901 1.00 22.04 ? 78  ALA B O   1 
ATOM   2440 C  CB  . ALA B 1 51  ? -1.615  -16.459 -20.828 1.00 20.88 ? 78  ALA B CB  1 
ATOM   2441 N  N   . ALA B 1 52  ? 0.784   -18.533 -20.528 1.00 21.13 ? 79  ALA B N   1 
ATOM   2442 C  CA  . ALA B 1 52  ? 2.130   -18.782 -20.037 1.00 21.65 ? 79  ALA B CA  1 
ATOM   2443 C  C   . ALA B 1 52  ? 3.011   -19.287 -21.187 1.00 22.54 ? 79  ALA B C   1 
ATOM   2444 O  O   . ALA B 1 52  ? 4.167   -18.884 -21.340 1.00 23.12 ? 79  ALA B O   1 
ATOM   2445 C  CB  . ALA B 1 52  ? 2.072   -19.751 -18.881 1.00 21.46 ? 79  ALA B CB  1 
ATOM   2446 N  N   . VAL B 1 53  ? 2.472   -20.212 -21.994 1.00 21.63 ? 80  VAL B N   1 
ATOM   2447 C  CA  . VAL B 1 53  ? 3.246   -20.756 -23.107 1.00 22.84 ? 80  VAL B CA  1 
ATOM   2448 C  C   . VAL B 1 53  ? 3.509   -19.659 -24.146 1.00 23.02 ? 80  VAL B C   1 
ATOM   2449 O  O   . VAL B 1 53  ? 4.597   -19.551 -24.704 1.00 23.77 ? 80  VAL B O   1 
ATOM   2450 C  CB  . VAL B 1 53  ? 2.483   -21.947 -23.704 1.00 22.14 ? 80  VAL B CB  1 
ATOM   2451 C  CG1 . VAL B 1 53  ? 3.039   -22.370 -25.057 1.00 22.52 ? 80  VAL B CG1 1 
ATOM   2452 C  CG2 . VAL B 1 53  ? 2.451   -23.106 -22.709 1.00 21.72 ? 80  VAL B CG2 1 
ATOM   2453 N  N   . LEU B 1 54  ? 2.503   -18.834 -24.408 1.00 23.94 ? 81  LEU B N   1 
ATOM   2454 C  CA  . LEU B 1 54  ? 2.684   -17.709 -25.312 1.00 25.91 ? 81  LEU B CA  1 
ATOM   2455 C  C   . LEU B 1 54  ? 3.810   -16.824 -24.791 1.00 27.46 ? 81  LEU B C   1 
ATOM   2456 O  O   . LEU B 1 54  ? 4.729   -16.464 -25.523 1.00 28.88 ? 81  LEU B O   1 
ATOM   2457 C  CB  . LEU B 1 54  ? 1.386   -16.926 -25.479 1.00 25.63 ? 81  LEU B CB  1 
ATOM   2458 C  CG  . LEU B 1 54  ? 0.303   -17.581 -26.339 1.00 24.26 ? 81  LEU B CG  1 
ATOM   2459 C  CD1 . LEU B 1 54  ? -0.992  -16.827 -26.178 1.00 23.33 ? 81  LEU B CD1 1 
ATOM   2460 C  CD2 . LEU B 1 54  ? 0.683   -17.637 -27.825 1.00 25.37 ? 81  LEU B CD2 1 
ATOM   2461 N  N   . HIS B 1 55  ? 3.728   -16.479 -23.507 1.00 28.38 ? 82  HIS B N   1 
ATOM   2462 C  CA  . HIS B 1 55  ? 4.625   -15.486 -22.940 1.00 29.82 ? 82  HIS B CA  1 
ATOM   2463 C  C   . HIS B 1 55  ? 6.080   -15.968 -22.969 1.00 29.83 ? 82  HIS B C   1 
ATOM   2464 O  O   . HIS B 1 55  ? 6.987   -15.184 -23.219 1.00 29.01 ? 82  HIS B O   1 
ATOM   2465 C  CB  . HIS B 1 55  ? 4.160   -15.124 -21.526 1.00 29.52 ? 82  HIS B CB  1 
ATOM   2466 C  CG  . HIS B 1 55  ? 5.068   -14.142 -20.882 1.00 31.35 ? 82  HIS B CG  1 
ATOM   2467 N  ND1 . HIS B 1 55  ? 6.056   -14.537 -20.008 1.00 31.31 ? 82  HIS B ND1 1 
ATOM   2468 C  CD2 . HIS B 1 55  ? 5.147   -12.805 -20.989 1.00 32.39 ? 82  HIS B CD2 1 
ATOM   2469 C  CE1 . HIS B 1 55  ? 6.725   -13.459 -19.613 1.00 35.03 ? 82  HIS B CE1 1 
ATOM   2470 N  NE2 . HIS B 1 55  ? 6.176   -12.399 -20.187 1.00 34.54 ? 82  HIS B NE2 1 
ATOM   2471 N  N   . GLN B 1 56  ? 6.301   -17.261 -22.693 1.00 31.24 ? 83  GLN B N   1 
ATOM   2472 C  CA  . GLN B 1 56  ? 7.637   -17.760 -22.396 1.00 34.76 ? 83  GLN B CA  1 
ATOM   2473 C  C   . GLN B 1 56  ? 8.426   -18.086 -23.666 1.00 34.11 ? 83  GLN B C   1 
ATOM   2474 O  O   . GLN B 1 56  ? 9.623   -18.336 -23.585 1.00 35.29 ? 83  GLN B O   1 
ATOM   2475 C  CB  . GLN B 1 56  ? 7.514   -18.941 -21.436 1.00 40.27 ? 83  GLN B CB  1 
ATOM   2476 C  CG  . GLN B 1 56  ? 7.076   -18.513 -20.033 1.00 47.00 ? 83  GLN B CG  1 
ATOM   2477 C  CD  . GLN B 1 56  ? 7.961   -17.467 -19.373 1.00 55.83 ? 83  GLN B CD  1 
ATOM   2478 O  OE1 . GLN B 1 56  ? 7.938   -16.275 -19.717 1.00 55.71 ? 83  GLN B OE1 1 
ATOM   2479 N  NE2 . GLN B 1 56  ? 8.706   -17.890 -18.356 1.00 58.05 ? 83  GLN B NE2 1 
ATOM   2480 N  N   . ASN B 1 57  ? 7.778   -18.021 -24.827 1.00 30.98 ? 86  ASN B N   1 
ATOM   2481 C  CA  . ASN B 1 57  ? 8.388   -18.458 -26.070 1.00 32.47 ? 86  ASN B CA  1 
ATOM   2482 C  C   . ASN B 1 57  ? 8.194   -17.434 -27.185 1.00 32.22 ? 86  ASN B C   1 
ATOM   2483 O  O   . ASN B 1 57  ? 7.213   -16.679 -27.237 1.00 31.22 ? 86  ASN B O   1 
ATOM   2484 C  CB  . ASN B 1 57  ? 7.811   -19.784 -26.556 1.00 30.63 ? 86  ASN B CB  1 
ATOM   2485 C  CG  . ASN B 1 57  ? 8.025   -20.901 -25.568 1.00 29.41 ? 86  ASN B CG  1 
ATOM   2486 O  OD1 . ASN B 1 57  ? 9.098   -21.517 -25.541 1.00 30.39 ? 86  ASN B OD1 1 
ATOM   2487 N  ND2 . ASN B 1 57  ? 7.020   -21.212 -24.757 1.00 27.96 ? 86  ASN B ND2 1 
ATOM   2488 N  N   . PRO B 1 58  ? 9.110   -17.434 -28.182 1.00 34.54 ? 87  PRO B N   1 
ATOM   2489 C  CA  . PRO B 1 58  ? 8.875   -16.676 -29.399 1.00 34.65 ? 87  PRO B CA  1 
ATOM   2490 C  C   . PRO B 1 58  ? 7.645   -17.189 -30.154 1.00 32.90 ? 87  PRO B C   1 
ATOM   2491 O  O   . PRO B 1 58  ? 7.191   -18.313 -29.967 1.00 29.66 ? 87  PRO B O   1 
ATOM   2492 C  CB  . PRO B 1 58  ? 10.193  -16.822 -30.180 1.00 35.83 ? 87  PRO B CB  1 
ATOM   2493 C  CG  . PRO B 1 58  ? 10.812  -18.081 -29.640 1.00 36.67 ? 87  PRO B CG  1 
ATOM   2494 C  CD  . PRO B 1 58  ? 10.407  -18.137 -28.192 1.00 35.31 ? 87  PRO B CD  1 
ATOM   2495 N  N   . LEU B 1 59  ? 7.111   -16.318 -31.004 1.00 32.87 ? 88  LEU B N   1 
ATOM   2496 C  CA  . LEU B 1 59  ? 5.923   -16.608 -31.786 1.00 33.94 ? 88  LEU B CA  1 
ATOM   2497 C  C   . LEU B 1 59  ? 6.124   -17.838 -32.672 1.00 33.66 ? 88  LEU B C   1 
ATOM   2498 O  O   . LEU B 1 59  ? 5.169   -18.571 -32.906 1.00 35.05 ? 88  LEU B O   1 
ATOM   2499 C  CB  . LEU B 1 59  ? 5.647   -15.353 -32.607 1.00 35.27 ? 88  LEU B CB  1 
ATOM   2500 C  CG  . LEU B 1 59  ? 4.189   -14.965 -32.842 1.00 36.44 ? 88  LEU B CG  1 
ATOM   2501 C  CD1 . LEU B 1 59  ? 3.394   -14.938 -31.542 1.00 36.18 ? 88  LEU B CD1 1 
ATOM   2502 C  CD2 . LEU B 1 59  ? 4.203   -13.597 -33.534 1.00 36.53 ? 88  LEU B CD2 1 
ATOM   2503 N  N   . THR B 1 60  ? 7.352   -18.069 -33.158 1.00 33.73 ? 89  THR B N   1 
ATOM   2504 C  CA  . THR B 1 60  ? 7.631   -19.200 -34.036 1.00 33.59 ? 89  THR B CA  1 
ATOM   2505 C  C   . THR B 1 60  ? 7.471   -20.526 -33.288 1.00 30.48 ? 89  THR B C   1 
ATOM   2506 O  O   . THR B 1 60  ? 7.348   -21.572 -33.932 1.00 29.71 ? 89  THR B O   1 
ATOM   2507 C  CB  . THR B 1 60  ? 9.036   -19.073 -34.614 1.00 36.37 ? 89  THR B CB  1 
ATOM   2508 O  OG1 . THR B 1 60  ? 9.866   -18.949 -33.466 1.00 38.47 ? 89  THR B OG1 1 
ATOM   2509 C  CG2 . THR B 1 60  ? 9.186   -17.874 -35.533 1.00 40.44 ? 89  THR B CG2 1 
ATOM   2510 N  N   . HIS B 1 61  ? 7.492   -20.487 -31.939 1.00 29.24 ? 90  HIS B N   1 
ATOM   2511 C  CA  . HIS B 1 61  ? 7.327   -21.681 -31.115 1.00 27.67 ? 90  HIS B CA  1 
ATOM   2512 C  C   . HIS B 1 61  ? 5.932   -22.284 -31.272 1.00 25.17 ? 90  HIS B C   1 
ATOM   2513 O  O   . HIS B 1 61  ? 5.730   -23.456 -30.989 1.00 24.40 ? 90  HIS B O   1 
ATOM   2514 C  CB  . HIS B 1 61  ? 7.585   -21.357 -29.631 1.00 28.48 ? 90  HIS B CB  1 
ATOM   2515 C  CG  . HIS B 1 61  ? 7.551   -22.507 -28.685 1.00 27.62 ? 90  HIS B CG  1 
ATOM   2516 N  ND1 . HIS B 1 61  ? 8.552   -23.452 -28.600 1.00 28.38 ? 90  HIS B ND1 1 
ATOM   2517 C  CD2 . HIS B 1 61  ? 6.646   -22.843 -27.754 1.00 27.21 ? 90  HIS B CD2 1 
ATOM   2518 C  CE1 . HIS B 1 61  ? 8.241   -24.330 -27.648 1.00 29.40 ? 90  HIS B CE1 1 
ATOM   2519 N  NE2 . HIS B 1 61  ? 7.089   -23.979 -27.119 1.00 26.98 ? 90  HIS B NE2 1 
ATOM   2520 N  N   . LEU B 1 62  ? 4.961   -21.500 -31.731 1.00 25.26 ? 91  LEU B N   1 
ATOM   2521 C  CA  . LEU B 1 62  ? 3.634   -22.007 -32.012 1.00 25.01 ? 91  LEU B CA  1 
ATOM   2522 C  C   . LEU B 1 62  ? 3.655   -23.082 -33.100 1.00 25.48 ? 91  LEU B C   1 
ATOM   2523 O  O   . LEU B 1 62  ? 2.693   -23.847 -33.205 1.00 23.98 ? 91  LEU B O   1 
ATOM   2524 C  CB  . LEU B 1 62  ? 2.750   -20.829 -32.397 1.00 26.64 ? 91  LEU B CB  1 
ATOM   2525 C  CG  . LEU B 1 62  ? 2.462   -19.810 -31.289 1.00 27.69 ? 91  LEU B CG  1 
ATOM   2526 C  CD1 . LEU B 1 62  ? 1.683   -18.643 -31.893 1.00 29.52 ? 91  LEU B CD1 1 
ATOM   2527 C  CD2 . LEU B 1 62  ? 1.713   -20.430 -30.144 1.00 28.99 ? 91  LEU B CD2 1 
ATOM   2528 N  N   . ASP B 1 63  ? 4.728   -23.118 -33.910 1.00 25.74 ? 92  ASP B N   1 
ATOM   2529 C  CA  . ASP B 1 63  ? 4.831   -24.068 -35.007 1.00 27.69 ? 92  ASP B CA  1 
ATOM   2530 C  C   . ASP B 1 63  ? 5.682   -25.278 -34.633 1.00 27.81 ? 92  ASP B C   1 
ATOM   2531 O  O   . ASP B 1 63  ? 5.908   -26.148 -35.462 1.00 26.89 ? 92  ASP B O   1 
ATOM   2532 C  CB  . ASP B 1 63  ? 5.234   -23.361 -36.297 1.00 30.22 ? 92  ASP B CB  1 
ATOM   2533 C  CG  . ASP B 1 63  ? 4.196   -22.333 -36.722 1.00 32.29 ? 92  ASP B CG  1 
ATOM   2534 O  OD1 . ASP B 1 63  ? 3.018   -22.724 -36.792 1.00 32.87 ? 92  ASP B OD1 1 
ATOM   2535 O  OD2 . ASP B 1 63  ? 4.534   -21.121 -36.847 1.00 36.10 ? 92  ASP B OD2 1 
ATOM   2536 N  N   . LYS B 1 64  ? 6.133   -25.383 -33.386 1.00 27.22 ? 93  LYS B N   1 
ATOM   2537 C  CA  . LYS B 1 64  ? 6.886   -26.555 -32.961 1.00 29.53 ? 93  LYS B CA  1 
ATOM   2538 C  C   . LYS B 1 64  ? 5.951   -27.753 -32.838 1.00 28.15 ? 93  LYS B C   1 
ATOM   2539 O  O   . LYS B 1 64  ? 4.936   -27.658 -32.146 1.00 26.62 ? 93  LYS B O   1 
ATOM   2540 C  CB  . LYS B 1 64  ? 7.543   -26.202 -31.624 1.00 31.86 ? 93  LYS B CB  1 
ATOM   2541 C  CG  . LYS B 1 64  ? 7.691   -27.285 -30.576 1.00 35.44 ? 93  LYS B CG  1 
ATOM   2542 C  CD  . LYS B 1 64  ? 8.942   -28.132 -30.617 1.00 40.50 ? 93  LYS B CD  1 
ATOM   2543 C  CE  . LYS B 1 64  ? 9.282   -28.514 -29.205 1.00 43.75 ? 93  LYS B CE  1 
ATOM   2544 N  NZ  . LYS B 1 64  ? 10.394  -29.455 -29.251 1.00 48.93 ? 93  LYS B NZ  1 
ATOM   2545 N  N   . LEU B 1 65  ? 6.326   -28.880 -33.460 1.00 27.97 ? 94  LEU B N   1 
ATOM   2546 C  CA  . LEU B 1 65  ? 5.505   -30.091 -33.429 1.00 26.86 ? 94  LEU B CA  1 
ATOM   2547 C  C   . LEU B 1 65  ? 5.751   -30.857 -32.128 1.00 25.53 ? 94  LEU B C   1 
ATOM   2548 O  O   . LEU B 1 65  ? 6.897   -31.114 -31.776 1.00 25.20 ? 94  LEU B O   1 
ATOM   2549 C  CB  . LEU B 1 65  ? 5.796   -30.990 -34.633 1.00 27.19 ? 94  LEU B CB  1 
ATOM   2550 C  CG  . LEU B 1 65  ? 4.886   -32.215 -34.781 1.00 27.36 ? 94  LEU B CG  1 
ATOM   2551 C  CD1 . LEU B 1 65  ? 3.446   -31.844 -35.135 1.00 26.63 ? 94  LEU B CD1 1 
ATOM   2552 C  CD2 . LEU B 1 65  ? 5.443   -33.176 -35.795 1.00 28.55 ? 94  LEU B CD2 1 
ATOM   2553 N  N   . ILE B 1 66  ? 4.660   -31.240 -31.442 1.00 24.14 ? 95  ILE B N   1 
ATOM   2554 C  CA  . ILE B 1 66  ? 4.716   -32.084 -30.260 1.00 24.13 ? 95  ILE B CA  1 
ATOM   2555 C  C   . ILE B 1 66  ? 4.171   -33.464 -30.625 1.00 24.51 ? 95  ILE B C   1 
ATOM   2556 O  O   . ILE B 1 66  ? 3.008   -33.578 -31.043 1.00 25.39 ? 95  ILE B O   1 
ATOM   2557 C  CB  . ILE B 1 66  ? 3.900   -31.458 -29.106 1.00 23.20 ? 95  ILE B CB  1 
ATOM   2558 C  CG1 . ILE B 1 66  ? 4.313   -30.009 -28.811 1.00 23.05 ? 95  ILE B CG1 1 
ATOM   2559 C  CG2 . ILE B 1 66  ? 3.973   -32.327 -27.851 1.00 23.64 ? 95  ILE B CG2 1 
ATOM   2560 C  CD1 . ILE B 1 66  ? 5.795   -29.821 -28.498 1.00 24.57 ? 95  ILE B CD1 1 
ATOM   2561 N  N   . THR B 1 67  ? 4.988   -34.507 -30.422 1.00 24.53 ? 96  THR B N   1 
ATOM   2562 C  CA  . THR B 1 67  ? 4.540   -35.869 -30.665 1.00 25.16 ? 96  THR B CA  1 
ATOM   2563 C  C   . THR B 1 67  ? 4.065   -36.494 -29.347 1.00 25.23 ? 96  THR B C   1 
ATOM   2564 O  O   . THR B 1 67  ? 4.505   -36.093 -28.264 1.00 25.31 ? 96  THR B O   1 
ATOM   2565 C  CB  . THR B 1 67  ? 5.634   -36.687 -31.338 1.00 26.13 ? 96  THR B CB  1 
ATOM   2566 O  OG1 . THR B 1 67  ? 6.810   -36.572 -30.546 1.00 26.73 ? 96  THR B OG1 1 
ATOM   2567 C  CG2 . THR B 1 67  ? 6.015   -36.146 -32.701 1.00 26.22 ? 96  THR B CG2 1 
ATOM   2568 N  N   . TYR B 1 68  ? 3.110   -37.420 -29.457 1.00 24.75 ? 97  TYR B N   1 
ATOM   2569 C  CA  . TYR B 1 68  ? 2.544   -38.069 -28.278 1.00 25.69 ? 97  TYR B CA  1 
ATOM   2570 C  C   . TYR B 1 68  ? 1.887   -39.352 -28.752 1.00 26.83 ? 97  TYR B C   1 
ATOM   2571 O  O   . TYR B 1 68  ? 1.932   -39.618 -29.952 1.00 27.00 ? 97  TYR B O   1 
ATOM   2572 C  CB  . TYR B 1 68  ? 1.605   -37.107 -27.547 1.00 24.43 ? 97  TYR B CB  1 
ATOM   2573 C  CG  . TYR B 1 68  ? 0.444   -36.622 -28.395 1.00 24.12 ? 97  TYR B CG  1 
ATOM   2574 C  CD1 . TYR B 1 68  ? 0.563   -35.519 -29.237 1.00 24.66 ? 97  TYR B CD1 1 
ATOM   2575 C  CD2 . TYR B 1 68  ? -0.800  -37.205 -28.271 1.00 24.10 ? 97  TYR B CD2 1 
ATOM   2576 C  CE1 . TYR B 1 68  ? -0.507  -35.096 -30.016 1.00 24.08 ? 97  TYR B CE1 1 
ATOM   2577 C  CE2 . TYR B 1 68  ? -1.884  -36.774 -29.016 1.00 24.85 ? 97  TYR B CE2 1 
ATOM   2578 C  CZ  . TYR B 1 68  ? -1.734  -35.730 -29.921 1.00 24.31 ? 97  TYR B CZ  1 
ATOM   2579 O  OH  . TYR B 1 68  ? -2.834  -35.316 -30.634 1.00 23.63 ? 97  TYR B OH  1 
ATOM   2580 N  N   . THR B 1 69  ? 1.347   -40.161 -27.826 1.00 27.53 ? 98  THR B N   1 
ATOM   2581 C  CA  . THR B 1 69  ? 0.729   -41.418 -28.217 1.00 29.49 ? 98  THR B CA  1 
ATOM   2582 C  C   . THR B 1 69  ? -0.647  -41.553 -27.565 1.00 29.44 ? 98  THR B C   1 
ATOM   2583 O  O   . THR B 1 69  ? -1.026  -40.752 -26.727 1.00 28.16 ? 98  THR B O   1 
ATOM   2584 C  CB  . THR B 1 69  ? 1.622   -42.614 -27.877 1.00 30.26 ? 98  THR B CB  1 
ATOM   2585 O  OG1 . THR B 1 69  ? 1.354   -42.840 -26.498 1.00 30.88 ? 98  THR B OG1 1 
ATOM   2586 C  CG2 . THR B 1 69  ? 3.088   -42.410 -28.231 1.00 31.15 ? 98  THR B CG2 1 
ATOM   2587 N  N   . SER B 1 70  ? -1.368  -42.623 -27.938 1.00 31.03 ? 99  SER B N   1 
ATOM   2588 C  CA  . SER B 1 70  ? -2.676  -42.887 -27.350 1.00 33.38 ? 99  SER B CA  1 
ATOM   2589 C  C   . SER B 1 70  ? -2.553  -43.053 -25.831 1.00 31.76 ? 99  SER B C   1 
ATOM   2590 O  O   . SER B 1 70  ? -3.489  -42.774 -25.082 1.00 30.05 ? 99  SER B O   1 
ATOM   2591 C  CB  . SER B 1 70  ? -3.315  -44.115 -27.971 1.00 36.63 ? 99  SER B CB  1 
ATOM   2592 O  OG  . SER B 1 70  ? -3.831  -43.825 -29.261 1.00 41.89 ? 99  SER B OG  1 
ATOM   2593 N  N   . ASP B 1 71  ? -1.384  -43.535 -25.392 1.00 31.01 ? 100 ASP B N   1 
ATOM   2594 C  CA  . ASP B 1 71  ? -1.103  -43.744 -23.982 1.00 31.56 ? 100 ASP B CA  1 
ATOM   2595 C  C   . ASP B 1 71  ? -1.072  -42.424 -23.217 1.00 31.04 ? 100 ASP B C   1 
ATOM   2596 O  O   . ASP B 1 71  ? -1.135  -42.423 -21.992 1.00 30.73 ? 100 ASP B O   1 
ATOM   2597 C  CB  . ASP B 1 71  ? 0.176   -44.550 -23.805 1.00 31.68 ? 100 ASP B CB  1 
ATOM   2598 C  CG  . ASP B 1 71  ? 0.014   -46.039 -24.062 1.00 32.67 ? 100 ASP B CG  1 
ATOM   2599 O  OD1 . ASP B 1 71  ? -1.036  -46.424 -24.614 1.00 32.82 ? 100 ASP B OD1 1 
ATOM   2600 O  OD2 . ASP B 1 71  ? 0.926   -46.802 -23.689 1.00 32.46 ? 100 ASP B OD2 1 
ATOM   2601 N  N   . ASP B 1 72  ? -0.938  -41.303 -23.934 1.00 30.94 ? 101 ASP B N   1 
ATOM   2602 C  CA  . ASP B 1 72  ? -0.901  -39.991 -23.307 1.00 31.07 ? 101 ASP B CA  1 
ATOM   2603 C  C   . ASP B 1 72  ? -2.304  -39.447 -23.077 1.00 30.33 ? 101 ASP B C   1 
ATOM   2604 O  O   . ASP B 1 72  ? -2.452  -38.415 -22.422 1.00 29.76 ? 101 ASP B O   1 
ATOM   2605 C  CB  . ASP B 1 72  ? -0.119  -38.992 -24.144 1.00 30.90 ? 101 ASP B CB  1 
ATOM   2606 C  CG  . ASP B 1 72  ? 1.373   -39.258 -24.176 1.00 32.10 ? 101 ASP B CG  1 
ATOM   2607 O  OD1 . ASP B 1 72  ? 1.983   -39.257 -23.077 1.00 35.23 ? 101 ASP B OD1 1 
ATOM   2608 O  OD2 . ASP B 1 72  ? 1.893   -39.503 -25.272 1.00 31.52 ? 101 ASP B OD2 1 
ATOM   2609 N  N   . ILE B 1 73  ? -3.312  -40.096 -23.666 1.00 29.51 ? 102 ILE B N   1 
ATOM   2610 C  CA  . ILE B 1 73  ? -4.672  -39.600 -23.572 1.00 31.35 ? 102 ILE B CA  1 
ATOM   2611 C  C   . ILE B 1 73  ? -5.331  -40.275 -22.378 1.00 32.06 ? 102 ILE B C   1 
ATOM   2612 O  O   . ILE B 1 73  ? -5.694  -41.440 -22.484 1.00 30.02 ? 102 ILE B O   1 
ATOM   2613 C  CB  . ILE B 1 73  ? -5.429  -39.797 -24.899 1.00 32.67 ? 102 ILE B CB  1 
ATOM   2614 C  CG1 . ILE B 1 73  ? -4.690  -39.046 -26.033 1.00 34.65 ? 102 ILE B CG1 1 
ATOM   2615 C  CG2 . ILE B 1 73  ? -6.880  -39.333 -24.776 1.00 33.37 ? 102 ILE B CG2 1 
ATOM   2616 C  CD1 . ILE B 1 73  ? -5.172  -39.335 -27.429 1.00 34.19 ? 102 ILE B CD1 1 
ATOM   2617 N  N   . ARG B 1 74  ? -5.431  -39.540 -21.259 1.00 33.48 ? 103 ARG B N   1 
ATOM   2618 C  CA  . ARG B 1 74  ? -5.963  -40.071 -20.010 1.00 38.08 ? 103 ARG B CA  1 
ATOM   2619 C  C   . ARG B 1 74  ? -7.108  -39.194 -19.498 1.00 36.29 ? 103 ARG B C   1 
ATOM   2620 O  O   . ARG B 1 74  ? -7.564  -39.362 -18.356 1.00 33.05 ? 103 ARG B O   1 
ATOM   2621 C  CB  . ARG B 1 74  ? -4.897  -40.079 -18.917 1.00 43.64 ? 103 ARG B CB  1 
ATOM   2622 C  CG  . ARG B 1 74  ? -3.517  -40.605 -19.289 1.00 50.39 ? 103 ARG B CG  1 
ATOM   2623 C  CD  . ARG B 1 74  ? -2.497  -39.977 -18.297 1.00 55.68 ? 103 ARG B CD  1 
ATOM   2624 N  NE  . ARG B 1 74  ? -2.746  -40.396 -16.909 1.00 58.92 ? 103 ARG B NE  1 
ATOM   2625 C  CZ  . ARG B 1 74  ? -3.000  -39.620 -15.847 1.00 57.42 ? 103 ARG B CZ  1 
ATOM   2626 N  NH1 . ARG B 1 74  ? -2.915  -38.301 -15.904 1.00 54.06 ? 103 ARG B NH1 1 
ATOM   2627 N  NH2 . ARG B 1 74  ? -3.312  -40.192 -14.703 1.00 58.35 ? 103 ARG B NH2 1 
ATOM   2628 N  N   . SER B 1 75  ? -7.557  -38.275 -20.362 1.00 32.38 ? 104 SER B N   1 
ATOM   2629 C  CA  . SER B 1 75  ? -8.630  -37.345 -20.065 1.00 32.92 ? 104 SER B CA  1 
ATOM   2630 C  C   . SER B 1 75  ? -9.372  -37.065 -21.365 1.00 31.49 ? 104 SER B C   1 
ATOM   2631 O  O   . SER B 1 75  ? -8.825  -37.309 -22.426 1.00 32.70 ? 104 SER B O   1 
ATOM   2632 C  CB  . SER B 1 75  ? -8.102  -36.056 -19.478 1.00 31.15 ? 104 SER B CB  1 
ATOM   2633 O  OG  . SER B 1 75  ? -7.221  -35.423 -20.403 1.00 30.46 ? 104 SER B OG  1 
ATOM   2634 N  N   . ARG B 1 76  ? -10.589 -36.539 -21.240 1.00 31.76 ? 105 ARG B N   1 
ATOM   2635 C  CA  . ARG B 1 76  ? -11.421 -36.133 -22.360 1.00 33.55 ? 105 ARG B CA  1 
ATOM   2636 C  C   . ARG B 1 76  ? -10.638 -35.189 -23.275 1.00 30.56 ? 105 ARG B C   1 
ATOM   2637 O  O   . ARG B 1 76  ? -10.289 -34.079 -22.884 1.00 30.09 ? 105 ARG B O   1 
ATOM   2638 C  CB  . ARG B 1 76  ? -12.678 -35.469 -21.781 1.00 37.49 ? 105 ARG B CB  1 
ATOM   2639 C  CG  . ARG B 1 76  ? -13.695 -35.063 -22.833 1.00 43.27 ? 105 ARG B CG  1 
ATOM   2640 C  CD  . ARG B 1 76  ? -15.019 -34.616 -22.213 1.00 49.12 ? 105 ARG B CD  1 
ATOM   2641 N  NE  . ARG B 1 76  ? -16.027 -34.635 -23.279 1.00 54.82 ? 105 ARG B NE  1 
ATOM   2642 C  CZ  . ARG B 1 76  ? -16.062 -33.802 -24.316 1.00 56.41 ? 105 ARG B CZ  1 
ATOM   2643 N  NH1 . ARG B 1 76  ? -15.423 -32.648 -24.260 1.00 55.18 ? 105 ARG B NH1 1 
ATOM   2644 N  NH2 . ARG B 1 76  ? -16.803 -34.097 -25.370 1.00 59.94 ? 105 ARG B NH2 1 
ATOM   2645 N  N   . SER B 1 77  ? -10.357 -35.651 -24.496 1.00 29.86 ? 106 SER B N   1 
ATOM   2646 C  CA  . SER B 1 77  ? -9.425  -34.986 -25.401 1.00 28.07 ? 106 SER B CA  1 
ATOM   2647 C  C   . SER B 1 77  ? -9.976  -35.058 -26.830 1.00 28.54 ? 106 SER B C   1 
ATOM   2648 O  O   . SER B 1 77  ? -9.484  -35.824 -27.645 1.00 28.54 ? 106 SER B O   1 
ATOM   2649 C  CB  . SER B 1 77  ? -8.064  -35.615 -25.287 1.00 26.83 ? 106 SER B CB  1 
ATOM   2650 O  OG  . SER B 1 77  ? -7.620  -35.592 -23.941 1.00 27.62 ? 106 SER B OG  1 
ATOM   2651 N  N   . PRO B 1 78  ? -11.023 -34.269 -27.171 1.00 31.42 ? 107 PRO B N   1 
ATOM   2652 C  CA  . PRO B 1 78  ? -11.690 -34.382 -28.478 1.00 32.18 ? 107 PRO B CA  1 
ATOM   2653 C  C   . PRO B 1 78  ? -10.785 -34.122 -29.687 1.00 31.56 ? 107 PRO B C   1 
ATOM   2654 O  O   . PRO B 1 78  ? -10.963 -34.733 -30.750 1.00 34.95 ? 107 PRO B O   1 
ATOM   2655 C  CB  . PRO B 1 78  ? -12.840 -33.345 -28.398 1.00 32.73 ? 107 PRO B CB  1 
ATOM   2656 C  CG  . PRO B 1 78  ? -12.992 -33.033 -26.925 1.00 32.92 ? 107 PRO B CG  1 
ATOM   2657 C  CD  . PRO B 1 78  ? -11.603 -33.206 -26.323 1.00 30.85 ? 107 PRO B CD  1 
ATOM   2658 N  N   . VAL B 1 79  ? -9.788  -33.248 -29.513 1.00 27.82 ? 108 VAL B N   1 
ATOM   2659 C  CA  . VAL B 1 79  ? -8.903  -32.881 -30.600 1.00 28.24 ? 108 VAL B CA  1 
ATOM   2660 C  C   . VAL B 1 79  ? -7.671  -33.783 -30.574 1.00 26.96 ? 108 VAL B C   1 
ATOM   2661 O  O   . VAL B 1 79  ? -7.304  -34.346 -31.588 1.00 28.18 ? 108 VAL B O   1 
ATOM   2662 C  CB  . VAL B 1 79  ? -8.528  -31.388 -30.539 1.00 28.21 ? 108 VAL B CB  1 
ATOM   2663 C  CG1 . VAL B 1 79  ? -7.578  -30.984 -31.663 1.00 27.43 ? 108 VAL B CG1 1 
ATOM   2664 C  CG2 . VAL B 1 79  ? -9.763  -30.516 -30.579 1.00 30.31 ? 108 VAL B CG2 1 
ATOM   2665 N  N   . ALA B 1 80  ? -7.036  -33.959 -29.412 1.00 24.87 ? 109 ALA B N   1 
ATOM   2666 C  CA  . ALA B 1 80  ? -5.759  -34.655 -29.355 1.00 24.78 ? 109 ALA B CA  1 
ATOM   2667 C  C   . ALA B 1 80  ? -5.948  -36.099 -29.824 1.00 25.88 ? 109 ALA B C   1 
ATOM   2668 O  O   . ALA B 1 80  ? -5.049  -36.660 -30.445 1.00 25.33 ? 109 ALA B O   1 
ATOM   2669 C  CB  . ALA B 1 80  ? -5.152  -34.600 -27.963 1.00 25.63 ? 109 ALA B CB  1 
ATOM   2670 N  N   . GLN B 1 81  ? -7.139  -36.659 -29.583 1.00 26.38 ? 110 GLN B N   1 
ATOM   2671 C  CA  . GLN B 1 81  ? -7.425  -38.014 -30.008 1.00 31.38 ? 110 GLN B CA  1 
ATOM   2672 C  C   . GLN B 1 81  ? -7.352  -38.084 -31.534 1.00 31.64 ? 110 GLN B C   1 
ATOM   2673 O  O   . GLN B 1 81  ? -6.924  -39.094 -32.079 1.00 31.97 ? 110 GLN B O   1 
ATOM   2674 C  CB  . GLN B 1 81  ? -8.742  -38.495 -29.391 1.00 36.77 ? 110 GLN B CB  1 
ATOM   2675 C  CG  . GLN B 1 81  ? -9.207  -39.866 -29.878 1.00 44.91 ? 110 GLN B CG  1 
ATOM   2676 C  CD  . GLN B 1 81  ? -8.261  -40.991 -29.509 1.00 52.69 ? 110 GLN B CD  1 
ATOM   2677 O  OE1 . GLN B 1 81  ? -8.180  -41.415 -28.344 1.00 57.45 ? 110 GLN B OE1 1 
ATOM   2678 N  NE2 . GLN B 1 81  ? -7.551  -41.497 -30.511 1.00 55.12 ? 110 GLN B NE2 1 
ATOM   2679 N  N   . GLN B 1 82  ? -7.727  -37.009 -32.223 1.00 31.10 ? 111 GLN B N   1 
ATOM   2680 C  CA  . GLN B 1 82  ? -7.799  -37.031 -33.680 1.00 34.00 ? 111 GLN B CA  1 
ATOM   2681 C  C   . GLN B 1 82  ? -6.425  -36.862 -34.330 1.00 31.86 ? 111 GLN B C   1 
ATOM   2682 O  O   . GLN B 1 82  ? -6.303  -37.122 -35.527 1.00 31.59 ? 111 GLN B O   1 
ATOM   2683 C  CB  . GLN B 1 82  ? -8.663  -35.882 -34.198 1.00 38.12 ? 111 GLN B CB  1 
ATOM   2684 C  CG  . GLN B 1 82  ? -10.126 -35.918 -33.777 1.00 42.53 ? 111 GLN B CG  1 
ATOM   2685 C  CD  . GLN B 1 82  ? -10.804 -34.569 -33.944 1.00 51.54 ? 111 GLN B CD  1 
ATOM   2686 O  OE1 . GLN B 1 82  ? -10.178 -33.544 -34.259 1.00 55.81 ? 111 GLN B OE1 1 
ATOM   2687 N  NE2 . GLN B 1 82  ? -12.110 -34.552 -33.721 1.00 55.99 ? 111 GLN B NE2 1 
ATOM   2688 N  N   . HIS B 1 83  ? -5.403  -36.447 -33.559 1.00 29.73 ? 112 HIS B N   1 
ATOM   2689 C  CA  . HIS B 1 83  ? -4.091  -36.128 -34.114 1.00 30.53 ? 112 HIS B CA  1 
ATOM   2690 C  C   . HIS B 1 83  ? -2.979  -36.956 -33.469 1.00 29.17 ? 112 HIS B C   1 
ATOM   2691 O  O   . HIS B 1 83  ? -1.804  -36.620 -33.562 1.00 28.34 ? 112 HIS B O   1 
ATOM   2692 C  CB  . HIS B 1 83  ? -3.789  -34.628 -33.976 1.00 31.60 ? 112 HIS B CB  1 
ATOM   2693 C  CG  . HIS B 1 83  ? -4.840  -33.784 -34.609 1.00 34.95 ? 112 HIS B CG  1 
ATOM   2694 N  ND1 . HIS B 1 83  ? -4.984  -33.761 -35.979 1.00 38.28 ? 112 HIS B ND1 1 
ATOM   2695 C  CD2 . HIS B 1 83  ? -5.845  -33.047 -34.121 1.00 34.31 ? 112 HIS B CD2 1 
ATOM   2696 C  CE1 . HIS B 1 83  ? -6.022  -32.991 -36.299 1.00 39.05 ? 112 HIS B CE1 1 
ATOM   2697 N  NE2 . HIS B 1 83  ? -6.557  -32.542 -35.184 1.00 37.35 ? 112 HIS B NE2 1 
ATOM   2698 N  N   . VAL B 1 84  ? -3.334  -38.062 -32.821 1.00 28.76 ? 113 VAL B N   1 
ATOM   2699 C  CA  . VAL B 1 84  ? -2.322  -38.803 -32.094 1.00 29.19 ? 113 VAL B CA  1 
ATOM   2700 C  C   . VAL B 1 84  ? -1.205  -39.270 -33.039 1.00 29.26 ? 113 VAL B C   1 
ATOM   2701 O  O   . VAL B 1 84  ? -0.044  -39.347 -32.639 1.00 27.90 ? 113 VAL B O   1 
ATOM   2702 C  CB  . VAL B 1 84  ? -2.952  -39.949 -31.287 1.00 31.33 ? 113 VAL B CB  1 
ATOM   2703 C  CG1 . VAL B 1 84  ? -3.667  -40.982 -32.154 1.00 32.77 ? 113 VAL B CG1 1 
ATOM   2704 C  CG2 . VAL B 1 84  ? -1.900  -40.605 -30.400 1.00 33.36 ? 113 VAL B CG2 1 
ATOM   2705 N  N   . GLN B 1 85  ? -1.530  -39.630 -34.278 1.00 28.48 ? 114 GLN B N   1 
ATOM   2706 C  CA  . GLN B 1 85  ? -0.494  -40.186 -35.141 1.00 31.23 ? 114 GLN B CA  1 
ATOM   2707 C  C   . GLN B 1 85  ? 0.411   -39.113 -35.748 1.00 29.52 ? 114 GLN B C   1 
ATOM   2708 O  O   . GLN B 1 85  ? 1.537   -39.424 -36.121 1.00 29.71 ? 114 GLN B O   1 
ATOM   2709 C  CB  . GLN B 1 85  ? -1.101  -41.012 -36.272 1.00 34.45 ? 114 GLN B CB  1 
ATOM   2710 C  CG  . GLN B 1 85  ? -1.903  -42.208 -35.772 1.00 38.68 ? 114 GLN B CG  1 
ATOM   2711 C  CD  . GLN B 1 85  ? -1.047  -43.324 -35.199 1.00 43.70 ? 114 GLN B CD  1 
ATOM   2712 O  OE1 . GLN B 1 85  ? -1.111  -43.641 -34.006 1.00 46.88 ? 114 GLN B OE1 1 
ATOM   2713 N  NE2 . GLN B 1 85  ? -0.261  -43.962 -36.060 1.00 49.67 ? 114 GLN B NE2 1 
ATOM   2714 N  N   . THR B 1 86  ? -0.082  -37.880 -35.904 1.00 28.08 ? 115 THR B N   1 
ATOM   2715 C  CA  . THR B 1 86  ? 0.677   -36.815 -36.553 1.00 27.87 ? 115 THR B CA  1 
ATOM   2716 C  C   . THR B 1 86  ? 1.422   -35.963 -35.533 1.00 26.49 ? 115 THR B C   1 
ATOM   2717 O  O   . THR B 1 86  ? 2.455   -35.365 -35.847 1.00 27.18 ? 115 THR B O   1 
ATOM   2718 C  CB  . THR B 1 86  ? -0.250  -35.926 -37.380 1.00 28.00 ? 115 THR B CB  1 
ATOM   2719 O  OG1 . THR B 1 86  ? -1.227  -35.376 -36.497 1.00 26.43 ? 115 THR B OG1 1 
ATOM   2720 C  CG2 . THR B 1 86  ? -0.890  -36.694 -38.523 1.00 28.75 ? 115 THR B CG2 1 
ATOM   2721 N  N   . GLY B 1 87  ? 0.894   -35.934 -34.313 1.00 24.95 ? 116 GLY B N   1 
ATOM   2722 C  CA  . GLY B 1 87  ? 1.277   -34.925 -33.341 1.00 24.05 ? 116 GLY B CA  1 
ATOM   2723 C  C   . GLY B 1 87  ? 0.491   -33.641 -33.615 1.00 23.82 ? 116 GLY B C   1 
ATOM   2724 O  O   . GLY B 1 87  ? -0.300  -33.591 -34.560 1.00 23.15 ? 116 GLY B O   1 
ATOM   2725 N  N   . MET B 1 88  ? 0.680   -32.659 -32.733 1.00 22.61 ? 117 MET B N   1 
ATOM   2726 C  CA  . MET B 1 88  ? 0.062   -31.347 -32.866 1.00 22.57 ? 117 MET B CA  1 
ATOM   2727 C  C   . MET B 1 88  ? 1.116   -30.282 -32.597 1.00 21.83 ? 117 MET B C   1 
ATOM   2728 O  O   . MET B 1 88  ? 2.010   -30.508 -31.803 1.00 21.60 ? 117 MET B O   1 
ATOM   2729 C  CB  . MET B 1 88  ? -1.106  -31.195 -31.887 1.00 21.91 ? 117 MET B CB  1 
ATOM   2730 C  CG  . MET B 1 88  ? -2.212  -32.201 -32.093 1.00 22.50 ? 117 MET B CG  1 
ATOM   2731 S  SD  . MET B 1 88  ? -3.608  -32.069 -30.957 1.00 23.39 ? 117 MET B SD  1 
ATOM   2732 C  CE  . MET B 1 88  ? -4.011  -30.325 -31.110 1.00 23.50 ? 117 MET B CE  1 
ATOM   2733 N  N   . THR B 1 89  ? 1.014   -29.117 -33.253 1.00 21.97 ? 118 THR B N   1 
ATOM   2734 C  CA  . THR B 1 89  ? 1.892   -28.002 -32.917 1.00 22.03 ? 118 THR B CA  1 
ATOM   2735 C  C   . THR B 1 89  ? 1.452   -27.354 -31.611 1.00 22.01 ? 118 THR B C   1 
ATOM   2736 O  O   . THR B 1 89  ? 0.301   -27.479 -31.184 1.00 21.47 ? 118 THR B O   1 
ATOM   2737 C  CB  . THR B 1 89  ? 1.956   -26.956 -34.037 1.00 22.55 ? 118 THR B CB  1 
ATOM   2738 O  OG1 . THR B 1 89  ? 0.652   -26.401 -34.148 1.00 22.89 ? 118 THR B OG1 1 
ATOM   2739 C  CG2 . THR B 1 89  ? 2.393   -27.520 -35.365 1.00 23.79 ? 118 THR B CG2 1 
ATOM   2740 N  N   . ILE B 1 90  ? 2.374   -26.594 -31.006 1.00 23.18 ? 119 ILE B N   1 
ATOM   2741 C  CA  . ILE B 1 90  ? 2.049   -25.828 -29.807 1.00 23.31 ? 119 ILE B CA  1 
ATOM   2742 C  C   . ILE B 1 90  ? 0.812   -24.962 -30.043 1.00 22.58 ? 119 ILE B C   1 
ATOM   2743 O  O   . ILE B 1 90  ? -0.071  -24.917 -29.215 1.00 22.02 ? 119 ILE B O   1 
ATOM   2744 C  CB  . ILE B 1 90  ? 3.251   -25.008 -29.334 1.00 25.03 ? 119 ILE B CB  1 
ATOM   2745 C  CG1 . ILE B 1 90  ? 4.349   -25.911 -28.783 1.00 25.15 ? 119 ILE B CG1 1 
ATOM   2746 C  CG2 . ILE B 1 90  ? 2.814   -23.957 -28.301 1.00 24.59 ? 119 ILE B CG2 1 
ATOM   2747 C  CD1 . ILE B 1 90  ? 3.999   -26.619 -27.480 1.00 25.28 ? 119 ILE B CD1 1 
ATOM   2748 N  N   . GLY B 1 91  ? 0.716   -24.337 -31.212 1.00 22.85 ? 120 GLY B N   1 
ATOM   2749 C  CA  . GLY B 1 91  ? -0.426  -23.501 -31.536 1.00 22.86 ? 120 GLY B CA  1 
ATOM   2750 C  C   . GLY B 1 91  ? -1.718  -24.306 -31.631 1.00 22.16 ? 120 GLY B C   1 
ATOM   2751 O  O   . GLY B 1 91  ? -2.757  -23.890 -31.122 1.00 21.61 ? 120 GLY B O   1 
ATOM   2752 N  N   . GLN B 1 92  ? -1.657  -25.481 -32.269 1.00 22.17 ? 121 GLN B N   1 
ATOM   2753 C  CA  . GLN B 1 92  ? -2.839  -26.329 -32.334 1.00 22.67 ? 121 GLN B CA  1 
ATOM   2754 C  C   . GLN B 1 92  ? -3.244  -26.806 -30.933 1.00 21.90 ? 121 GLN B C   1 
ATOM   2755 O  O   . GLN B 1 92  ? -4.438  -26.927 -30.628 1.00 22.22 ? 121 GLN B O   1 
ATOM   2756 C  CB  . GLN B 1 92  ? -2.552  -27.505 -33.261 1.00 23.42 ? 121 GLN B CB  1 
ATOM   2757 C  CG  . GLN B 1 92  ? -2.353  -27.099 -34.715 1.00 24.25 ? 121 GLN B CG  1 
ATOM   2758 C  CD  . GLN B 1 92  ? -1.863  -28.242 -35.569 1.00 25.79 ? 121 GLN B CD  1 
ATOM   2759 O  OE1 . GLN B 1 92  ? -1.154  -29.146 -35.129 1.00 24.29 ? 121 GLN B OE1 1 
ATOM   2760 N  NE2 . GLN B 1 92  ? -2.271  -28.236 -36.829 1.00 27.99 ? 121 GLN B NE2 1 
ATOM   2761 N  N   . LEU B 1 93  ? -2.255  -27.082 -30.069 1.00 21.05 ? 122 LEU B N   1 
ATOM   2762 C  CA  . LEU B 1 93  ? -2.542  -27.469 -28.686 1.00 20.92 ? 122 LEU B CA  1 
ATOM   2763 C  C   . LEU B 1 93  ? -3.219  -26.350 -27.885 1.00 19.81 ? 122 LEU B C   1 
ATOM   2764 O  O   . LEU B 1 93  ? -4.166  -26.620 -27.158 1.00 20.17 ? 122 LEU B O   1 
ATOM   2765 C  CB  . LEU B 1 93  ? -1.250  -27.938 -28.019 1.00 21.02 ? 122 LEU B CB  1 
ATOM   2766 C  CG  . LEU B 1 93  ? -0.681  -29.245 -28.569 1.00 21.51 ? 122 LEU B CG  1 
ATOM   2767 C  CD1 . LEU B 1 93  ? 0.716   -29.430 -28.016 1.00 21.91 ? 122 LEU B CD1 1 
ATOM   2768 C  CD2 . LEU B 1 93  ? -1.543  -30.428 -28.176 1.00 22.14 ? 122 LEU B CD2 1 
ATOM   2769 N  N   . CYS B 1 94  ? -2.784  -25.100 -28.063 1.00 21.03 ? 123 CYS B N   1 
ATOM   2770 C  CA  . CYS B 1 94  ? -3.416  -23.954 -27.424 1.00 20.92 ? 123 CYS B CA  1 
ATOM   2771 C  C   . CYS B 1 94  ? -4.891  -23.840 -27.844 1.00 22.11 ? 123 CYS B C   1 
ATOM   2772 O  O   . CYS B 1 94  ? -5.781  -23.693 -27.001 1.00 22.39 ? 123 CYS B O   1 
ATOM   2773 C  CB  . CYS B 1 94  ? -2.680  -22.659 -27.744 1.00 21.07 ? 123 CYS B CB  1 
ATOM   2774 S  SG  . CYS B 1 94  ? -1.016  -22.552 -27.031 1.00 23.32 ? 123 CYS B SG  1 
ATOM   2775 N  N   . ASP B 1 95  ? -5.140  -23.943 -29.148 1.00 22.92 ? 124 ASP B N   1 
ATOM   2776 C  CA  . ASP B 1 95  ? -6.477  -23.856 -29.713 1.00 23.69 ? 124 ASP B CA  1 
ATOM   2777 C  C   . ASP B 1 95  ? -7.380  -24.913 -29.077 1.00 22.16 ? 124 ASP B C   1 
ATOM   2778 O  O   . ASP B 1 95  ? -8.462  -24.594 -28.592 1.00 22.55 ? 124 ASP B O   1 
ATOM   2779 C  CB  . ASP B 1 95  ? -6.387  -23.948 -31.227 1.00 25.10 ? 124 ASP B CB  1 
ATOM   2780 C  CG  . ASP B 1 95  ? -7.704  -23.888 -31.988 1.00 27.50 ? 124 ASP B CG  1 
ATOM   2781 O  OD1 . ASP B 1 95  ? -8.630  -24.650 -31.666 1.00 29.42 ? 124 ASP B OD1 1 
ATOM   2782 O  OD2 . ASP B 1 95  ? -7.762  -23.136 -32.954 1.00 30.79 ? 124 ASP B OD2 1 
ATOM   2783 N  N   . ALA B 1 96  ? -6.905  -26.161 -29.030 1.00 21.10 ? 125 ALA B N   1 
ATOM   2784 C  CA  . ALA B 1 96  ? -7.707  -27.264 -28.522 1.00 19.81 ? 125 ALA B CA  1 
ATOM   2785 C  C   . ALA B 1 96  ? -7.980  -27.130 -27.025 1.00 19.93 ? 125 ALA B C   1 
ATOM   2786 O  O   . ALA B 1 96  ? -9.077  -27.456 -26.554 1.00 18.85 ? 125 ALA B O   1 
ATOM   2787 C  CB  . ALA B 1 96  ? -6.975  -28.542 -28.792 1.00 20.44 ? 125 ALA B CB  1 
ATOM   2788 N  N   . ALA B 1 97  ? -6.959  -26.664 -26.299 1.00 19.24 ? 126 ALA B N   1 
ATOM   2789 C  CA  . ALA B 1 97  ? -7.020  -26.516 -24.857 1.00 19.74 ? 126 ALA B CA  1 
ATOM   2790 C  C   . ALA B 1 97  ? -8.089  -25.491 -24.484 1.00 21.07 ? 126 ALA B C   1 
ATOM   2791 O  O   . ALA B 1 97  ? -8.876  -25.722 -23.563 1.00 19.90 ? 126 ALA B O   1 
ATOM   2792 C  CB  . ALA B 1 97  ? -5.651  -26.152 -24.324 1.00 19.08 ? 126 ALA B CB  1 
ATOM   2793 N  N   . ILE B 1 98  ? -8.135  -24.361 -25.212 1.00 21.88 ? 127 ILE B N   1 
ATOM   2794 C  CA  . ILE B 1 98  ? -9.132  -23.340 -24.926 1.00 23.12 ? 127 ILE B CA  1 
ATOM   2795 C  C   . ILE B 1 98  ? -10.504 -23.705 -25.507 1.00 24.52 ? 127 ILE B C   1 
ATOM   2796 O  O   . ILE B 1 98  ? -11.510 -23.612 -24.797 1.00 23.48 ? 127 ILE B O   1 
ATOM   2797 C  CB  . ILE B 1 98  ? -8.638  -21.960 -25.391 1.00 24.24 ? 127 ILE B CB  1 
ATOM   2798 C  CG1 . ILE B 1 98  ? -7.530  -21.513 -24.474 1.00 26.35 ? 127 ILE B CG1 1 
ATOM   2799 C  CG2 . ILE B 1 98  ? -9.787  -20.956 -25.484 1.00 24.78 ? 127 ILE B CG2 1 
ATOM   2800 C  CD1 . ILE B 1 98  ? -6.821  -20.258 -24.909 1.00 29.85 ? 127 ILE B CD1 1 
ATOM   2801 N  N   . ARG B 1 99  ? -10.544 -24.094 -26.788 1.00 23.68 ? 128 ARG B N   1 
ATOM   2802 C  CA  . ARG B 1 99  ? -11.796 -24.118 -27.536 1.00 25.73 ? 128 ARG B CA  1 
ATOM   2803 C  C   . ARG B 1 99  ? -12.575 -25.419 -27.315 1.00 25.39 ? 128 ARG B C   1 
ATOM   2804 O  O   . ARG B 1 99  ? -13.802 -25.432 -27.456 1.00 25.87 ? 128 ARG B O   1 
ATOM   2805 C  CB  . ARG B 1 99  ? -11.544 -23.862 -29.032 1.00 27.18 ? 128 ARG B CB  1 
ATOM   2806 C  CG  . ARG B 1 99  ? -11.103 -22.456 -29.430 1.00 29.31 ? 128 ARG B CG  1 
ATOM   2807 C  CD  . ARG B 1 99  ? -11.002 -22.281 -30.970 1.00 31.10 ? 128 ARG B CD  1 
ATOM   2808 N  NE  . ARG B 1 99  ? -12.174 -22.798 -31.695 1.00 34.25 ? 128 ARG B NE  1 
ATOM   2809 C  CZ  . ARG B 1 99  ? -12.260 -23.929 -32.387 1.00 36.97 ? 128 ARG B CZ  1 
ATOM   2810 N  NH1 . ARG B 1 99  ? -11.173 -24.617 -32.723 1.00 36.94 ? 128 ARG B NH1 1 
ATOM   2811 N  NH2 . ARG B 1 99  ? -13.456 -24.385 -32.745 1.00 38.62 ? 128 ARG B NH2 1 
ATOM   2812 N  N   . TYR B 1 100 ? -11.868 -26.518 -27.009 1.00 24.75 ? 129 TYR B N   1 
ATOM   2813 C  CA  . TYR B 1 100 ? -12.512 -27.795 -26.720 1.00 26.50 ? 129 TYR B CA  1 
ATOM   2814 C  C   . TYR B 1 100 ? -12.195 -28.310 -25.322 1.00 26.63 ? 129 TYR B C   1 
ATOM   2815 O  O   . TYR B 1 100 ? -12.540 -29.441 -24.988 1.00 27.58 ? 129 TYR B O   1 
ATOM   2816 C  CB  . TYR B 1 100 ? -12.047 -28.826 -27.744 1.00 28.66 ? 129 TYR B CB  1 
ATOM   2817 C  CG  . TYR B 1 100 ? -12.693 -28.541 -29.084 1.00 31.26 ? 129 TYR B CG  1 
ATOM   2818 C  CD1 . TYR B 1 100 ? -14.003 -28.931 -29.312 1.00 34.11 ? 129 TYR B CD1 1 
ATOM   2819 C  CD2 . TYR B 1 100 ? -12.019 -27.862 -30.092 1.00 33.30 ? 129 TYR B CD2 1 
ATOM   2820 C  CE1 . TYR B 1 100 ? -14.614 -28.697 -30.529 1.00 35.82 ? 129 TYR B CE1 1 
ATOM   2821 C  CE2 . TYR B 1 100 ? -12.614 -27.622 -31.317 1.00 34.29 ? 129 TYR B CE2 1 
ATOM   2822 C  CZ  . TYR B 1 100 ? -13.920 -28.028 -31.523 1.00 35.66 ? 129 TYR B CZ  1 
ATOM   2823 O  OH  . TYR B 1 100 ? -14.568 -27.804 -32.683 1.00 39.66 ? 129 TYR B OH  1 
ATOM   2824 N  N   . SER B 1 101 ? -11.528 -27.488 -24.507 1.00 25.23 ? 130 SER B N   1 
ATOM   2825 C  CA  . SER B 1 101 ? -11.122 -27.922 -23.182 1.00 27.42 ? 130 SER B CA  1 
ATOM   2826 C  C   . SER B 1 101 ? -10.412 -29.281 -23.232 1.00 26.71 ? 130 SER B C   1 
ATOM   2827 O  O   . SER B 1 101 ? -10.548 -30.115 -22.344 1.00 26.69 ? 130 SER B O   1 
ATOM   2828 C  CB  . SER B 1 101 ? -12.329 -27.953 -22.269 1.00 27.27 ? 130 SER B CB  1 
ATOM   2829 O  OG  . SER B 1 101 ? -11.922 -27.690 -20.951 1.00 25.38 ? 130 SER B OG  1 
ATOM   2830 N  N   . ASP B 1 102 ? -9.570  -29.463 -24.238 1.00 25.51 ? 131 ASP B N   1 
ATOM   2831 C  CA  . ASP B 1 102 ? -8.930  -30.745 -24.478 1.00 25.13 ? 131 ASP B CA  1 
ATOM   2832 C  C   . ASP B 1 102 ? -7.937  -31.026 -23.349 1.00 23.69 ? 131 ASP B C   1 
ATOM   2833 O  O   . ASP B 1 102 ? -7.049  -30.217 -23.116 1.00 22.81 ? 131 ASP B O   1 
ATOM   2834 C  CB  . ASP B 1 102 ? -8.291  -30.727 -25.856 1.00 23.94 ? 131 ASP B CB  1 
ATOM   2835 C  CG  . ASP B 1 102 ? -7.701  -32.051 -26.279 1.00 23.99 ? 131 ASP B CG  1 
ATOM   2836 O  OD1 . ASP B 1 102 ? -6.774  -32.539 -25.574 1.00 22.46 ? 131 ASP B OD1 1 
ATOM   2837 O  OD2 . ASP B 1 102 ? -8.188  -32.576 -27.306 1.00 25.26 ? 131 ASP B OD2 1 
ATOM   2838 N  N   . GLY B 1 103 ? -8.094  -32.169 -22.658 1.00 22.68 ? 132 GLY B N   1 
ATOM   2839 C  CA  . GLY B 1 103 ? -7.273  -32.487 -21.497 1.00 21.70 ? 132 GLY B CA  1 
ATOM   2840 C  C   . GLY B 1 103 ? -5.817  -32.801 -21.856 1.00 20.97 ? 132 GLY B C   1 
ATOM   2841 O  O   . GLY B 1 103 ? -4.893  -32.300 -21.213 1.00 19.76 ? 132 GLY B O   1 
ATOM   2842 N  N   . THR B 1 104 ? -5.613  -33.674 -22.852 1.00 20.91 ? 133 THR B N   1 
ATOM   2843 C  CA  . THR B 1 104 ? -4.261  -34.035 -23.258 1.00 21.24 ? 133 THR B CA  1 
ATOM   2844 C  C   . THR B 1 104 ? -3.497  -32.814 -23.778 1.00 21.03 ? 133 THR B C   1 
ATOM   2845 O  O   . THR B 1 104 ? -2.297  -32.674 -23.529 1.00 20.75 ? 133 THR B O   1 
ATOM   2846 C  CB  . THR B 1 104 ? -4.305  -35.128 -24.320 1.00 21.92 ? 133 THR B CB  1 
ATOM   2847 O  OG1 . THR B 1 104 ? -5.042  -36.182 -23.718 1.00 22.77 ? 133 THR B OG1 1 
ATOM   2848 C  CG2 . THR B 1 104 ? -2.911  -35.565 -24.726 1.00 22.71 ? 133 THR B CG2 1 
ATOM   2849 N  N   . ALA B 1 105 ? -4.187  -31.939 -24.521 1.00 20.34 ? 134 ALA B N   1 
ATOM   2850 C  CA  . ALA B 1 105 ? -3.571  -30.717 -25.020 1.00 20.54 ? 134 ALA B CA  1 
ATOM   2851 C  C   . ALA B 1 105 ? -2.988  -29.913 -23.851 1.00 21.04 ? 134 ALA B C   1 
ATOM   2852 O  O   . ALA B 1 105 ? -1.836  -29.434 -23.893 1.00 20.43 ? 134 ALA B O   1 
ATOM   2853 C  CB  . ALA B 1 105 ? -4.590  -29.924 -25.832 1.00 20.60 ? 134 ALA B CB  1 
ATOM   2854 N  N   . ALA B 1 106 ? -3.771  -29.796 -22.771 1.00 19.75 ? 135 ALA B N   1 
ATOM   2855 C  CA  . ALA B 1 106 ? -3.325  -29.030 -21.623 1.00 19.55 ? 135 ALA B CA  1 
ATOM   2856 C  C   . ALA B 1 106 ? -2.127  -29.717 -20.966 1.00 20.28 ? 135 ALA B C   1 
ATOM   2857 O  O   . ALA B 1 106 ? -1.167  -29.061 -20.586 1.00 21.50 ? 135 ALA B O   1 
ATOM   2858 C  CB  . ALA B 1 106 ? -4.466  -28.871 -20.654 1.00 19.96 ? 135 ALA B CB  1 
ATOM   2859 N  N   . ASN B 1 107 ? -2.146  -31.056 -20.851 1.00 19.38 ? 136 ASN B N   1 
ATOM   2860 C  CA  . ASN B 1 107 ? -1.025  -31.758 -20.247 1.00 20.07 ? 136 ASN B CA  1 
ATOM   2861 C  C   . ASN B 1 107 ? 0.249   -31.565 -21.067 1.00 20.08 ? 136 ASN B C   1 
ATOM   2862 O  O   . ASN B 1 107 ? 1.322   -31.426 -20.489 1.00 20.08 ? 136 ASN B O   1 
ATOM   2863 C  CB  . ASN B 1 107 ? -1.312  -33.240 -20.043 1.00 19.97 ? 136 ASN B CB  1 
ATOM   2864 C  CG  . ASN B 1 107 ? -2.272  -33.508 -18.901 1.00 21.50 ? 136 ASN B CG  1 
ATOM   2865 O  OD1 . ASN B 1 107 ? -2.659  -32.616 -18.128 1.00 21.55 ? 136 ASN B OD1 1 
ATOM   2866 N  ND2 . ASN B 1 107 ? -2.692  -34.763 -18.800 1.00 22.16 ? 136 ASN B ND2 1 
ATOM   2867 N  N   . LEU B 1 108 ? 0.131   -31.536 -22.406 1.00 20.13 ? 137 LEU B N   1 
ATOM   2868 C  CA  . LEU B 1 108 ? 1.290   -31.391 -23.270 1.00 19.99 ? 137 LEU B CA  1 
ATOM   2869 C  C   . LEU B 1 108 ? 1.833   -29.966 -23.139 1.00 20.86 ? 137 LEU B C   1 
ATOM   2870 O  O   . LEU B 1 108 ? 3.046   -29.742 -23.156 1.00 20.50 ? 137 LEU B O   1 
ATOM   2871 C  CB  . LEU B 1 108 ? 0.953   -31.754 -24.709 1.00 20.35 ? 137 LEU B CB  1 
ATOM   2872 C  CG  . LEU B 1 108 ? 0.634   -33.233 -24.975 1.00 20.87 ? 137 LEU B CG  1 
ATOM   2873 C  CD1 . LEU B 1 108 ? 0.041   -33.414 -26.361 1.00 20.44 ? 137 LEU B CD1 1 
ATOM   2874 C  CD2 . LEU B 1 108 ? 1.877   -34.076 -24.800 1.00 21.62 ? 137 LEU B CD2 1 
ATOM   2875 N  N   . LEU B 1 109 ? 0.938   -28.992 -23.000 1.00 19.95 ? 138 LEU B N   1 
ATOM   2876 C  CA  . LEU B 1 109 ? 1.377   -27.623 -22.804 1.00 20.11 ? 138 LEU B CA  1 
ATOM   2877 C  C   . LEU B 1 109 ? 2.075   -27.475 -21.449 1.00 20.69 ? 138 LEU B C   1 
ATOM   2878 O  O   . LEU B 1 109 ? 3.111   -26.819 -21.346 1.00 20.66 ? 138 LEU B O   1 
ATOM   2879 C  CB  . LEU B 1 109 ? 0.181   -26.701 -22.954 1.00 20.52 ? 138 LEU B CB  1 
ATOM   2880 C  CG  . LEU B 1 109 ? -0.367  -26.538 -24.377 1.00 20.56 ? 138 LEU B CG  1 
ATOM   2881 C  CD1 . LEU B 1 109 ? -1.736  -25.851 -24.343 1.00 20.94 ? 138 LEU B CD1 1 
ATOM   2882 C  CD2 . LEU B 1 109 ? 0.582   -25.783 -25.276 1.00 21.16 ? 138 LEU B CD2 1 
ATOM   2883 N  N   . LEU B 1 110 ? 1.524   -28.107 -20.412 1.00 21.17 ? 139 LEU B N   1 
ATOM   2884 C  CA  . LEU B 1 110 ? 2.172   -28.125 -19.107 1.00 21.46 ? 139 LEU B CA  1 
ATOM   2885 C  C   . LEU B 1 110 ? 3.605   -28.651 -19.238 1.00 22.51 ? 139 LEU B C   1 
ATOM   2886 O  O   . LEU B 1 110 ? 4.532   -28.033 -18.722 1.00 23.36 ? 139 LEU B O   1 
ATOM   2887 C  CB  . LEU B 1 110 ? 1.342   -28.962 -18.136 1.00 21.10 ? 139 LEU B CB  1 
ATOM   2888 C  CG  . LEU B 1 110 ? 0.069   -28.302 -17.599 1.00 21.27 ? 139 LEU B CG  1 
ATOM   2889 C  CD1 . LEU B 1 110 ? -0.812  -29.368 -16.891 1.00 20.91 ? 139 LEU B CD1 1 
ATOM   2890 C  CD2 . LEU B 1 110 ? 0.405   -27.120 -16.691 1.00 21.10 ? 139 LEU B CD2 1 
ATOM   2891 N  N   . ALA B 1 111 ? 3.787   -29.785 -19.936 1.00 23.91 ? 140 ALA B N   1 
ATOM   2892 C  CA  . ALA B 1 111 ? 5.113   -30.359 -20.156 1.00 24.95 ? 140 ALA B CA  1 
ATOM   2893 C  C   . ALA B 1 111 ? 6.019   -29.414 -20.948 1.00 25.44 ? 140 ALA B C   1 
ATOM   2894 O  O   . ALA B 1 111 ? 7.227   -29.367 -20.718 1.00 26.57 ? 140 ALA B O   1 
ATOM   2895 C  CB  . ALA B 1 111 ? 4.999   -31.718 -20.833 1.00 26.11 ? 140 ALA B CB  1 
ATOM   2896 N  N   . ASP B 1 112 ? 5.455   -28.703 -21.928 1.00 24.50 ? 141 ASP B N   1 
ATOM   2897 C  CA  . ASP B 1 112 ? 6.245   -27.763 -22.701 1.00 25.66 ? 141 ASP B CA  1 
ATOM   2898 C  C   . ASP B 1 112 ? 6.701   -26.630 -21.784 1.00 26.53 ? 141 ASP B C   1 
ATOM   2899 O  O   . ASP B 1 112 ? 7.826   -26.148 -21.889 1.00 26.08 ? 141 ASP B O   1 
ATOM   2900 C  CB  . ASP B 1 112 ? 5.477   -27.198 -23.881 1.00 25.30 ? 141 ASP B CB  1 
ATOM   2901 C  CG  . ASP B 1 112 ? 6.327   -26.345 -24.812 1.00 26.39 ? 141 ASP B CG  1 
ATOM   2902 O  OD1 . ASP B 1 112 ? 7.230   -26.927 -25.435 1.00 28.88 ? 141 ASP B OD1 1 
ATOM   2903 O  OD2 . ASP B 1 112 ? 6.103   -25.107 -24.882 1.00 26.11 ? 141 ASP B OD2 1 
ATOM   2904 N  N   . LEU B 1 113 ? 5.814   -26.238 -20.858 1.00 25.31 ? 142 LEU B N   1 
ATOM   2905 C  CA  . LEU B 1 113 ? 6.073   -25.095 -20.001 1.00 26.22 ? 142 LEU B CA  1 
ATOM   2906 C  C   . LEU B 1 113 ? 7.140   -25.440 -18.968 1.00 26.92 ? 142 LEU B C   1 
ATOM   2907 O  O   . LEU B 1 113 ? 8.068   -24.665 -18.764 1.00 27.70 ? 142 LEU B O   1 
ATOM   2908 C  CB  . LEU B 1 113 ? 4.794   -24.618 -19.313 1.00 24.28 ? 142 LEU B CB  1 
ATOM   2909 C  CG  . LEU B 1 113 ? 4.930   -23.290 -18.559 1.00 24.58 ? 142 LEU B CG  1 
ATOM   2910 C  CD1 . LEU B 1 113 ? 5.179   -22.124 -19.491 1.00 24.94 ? 142 LEU B CD1 1 
ATOM   2911 C  CD2 . LEU B 1 113 ? 3.686   -23.026 -17.733 1.00 24.35 ? 142 LEU B CD2 1 
ATOM   2912 N  N   . GLY B 1 114 ? 6.987   -26.591 -18.301 1.00 27.71 ? 143 GLY B N   1 
ATOM   2913 C  CA  . GLY B 1 114 ? 7.761   -26.860 -17.103 1.00 29.89 ? 143 GLY B CA  1 
ATOM   2914 C  C   . GLY B 1 114 ? 8.525   -28.176 -17.163 1.00 31.31 ? 143 GLY B C   1 
ATOM   2915 O  O   . GLY B 1 114 ? 9.139   -28.555 -16.176 1.00 30.89 ? 143 GLY B O   1 
ATOM   2916 N  N   . GLY B 1 115 ? 8.492   -28.859 -18.304 1.00 32.29 ? 144 GLY B N   1 
ATOM   2917 C  CA  . GLY B 1 115 ? 9.087   -30.183 -18.404 1.00 35.20 ? 144 GLY B CA  1 
ATOM   2918 C  C   . GLY B 1 115 ? 8.167   -31.245 -17.820 1.00 37.02 ? 144 GLY B C   1 
ATOM   2919 O  O   . GLY B 1 115 ? 7.104   -30.961 -17.274 1.00 38.57 ? 144 GLY B O   1 
ATOM   2920 N  N   . PRO B 1 116 ? 8.537   -32.530 -17.942 1.00 45.84 ? 145 PRO B N   1 
ATOM   2921 C  CA  . PRO B 1 116 ? 7.809   -33.591 -17.249 1.00 46.44 ? 145 PRO B CA  1 
ATOM   2922 C  C   . PRO B 1 116 ? 8.125   -33.420 -15.765 1.00 46.67 ? 145 PRO B C   1 
ATOM   2923 O  O   . PRO B 1 116 ? 9.291   -33.323 -15.377 1.00 52.45 ? 145 PRO B O   1 
ATOM   2924 C  CB  . PRO B 1 116 ? 8.394   -34.867 -17.872 1.00 50.18 ? 145 PRO B CB  1 
ATOM   2925 C  CG  . PRO B 1 116 ? 9.806   -34.469 -18.252 1.00 51.68 ? 145 PRO B CG  1 
ATOM   2926 C  CD  . PRO B 1 116 ? 9.688   -33.019 -18.721 1.00 49.51 ? 145 PRO B CD  1 
ATOM   2927 N  N   . GLY B 1 117 A 7.080   -33.307 -14.950 1.00 41.51 ? 145 GLY B N   1 
ATOM   2928 C  CA  . GLY B 1 117 A 7.269   -33.167 -13.518 1.00 40.02 ? 145 GLY B CA  1 
ATOM   2929 C  C   . GLY B 1 117 A 7.133   -31.716 -13.060 1.00 36.38 ? 145 GLY B C   1 
ATOM   2930 O  O   . GLY B 1 117 A 6.692   -31.487 -11.939 1.00 37.19 ? 145 GLY B O   1 
ATOM   2931 N  N   . GLY B 1 118 B 7.481   -30.751 -13.925 1.00 32.67 ? 145 GLY B N   1 
ATOM   2932 C  CA  . GLY B 1 118 B 7.601   -29.354 -13.523 1.00 31.65 ? 145 GLY B CA  1 
ATOM   2933 C  C   . GLY B 1 118 B 6.481   -28.452 -14.051 1.00 29.19 ? 145 GLY B C   1 
ATOM   2934 O  O   . GLY B 1 118 B 6.445   -27.263 -13.748 1.00 27.48 ? 145 GLY B O   1 
ATOM   2935 N  N   . GLY B 1 119 C 5.547   -29.002 -14.823 1.00 27.91 ? 145 GLY B N   1 
ATOM   2936 C  CA  . GLY B 1 119 C 4.548   -28.194 -15.505 1.00 25.17 ? 145 GLY B CA  1 
ATOM   2937 C  C   . GLY B 1 119 C 3.617   -27.439 -14.557 1.00 24.67 ? 145 GLY B C   1 
ATOM   2938 O  O   . GLY B 1 119 C 3.379   -26.242 -14.744 1.00 23.67 ? 145 GLY B O   1 
ATOM   2939 N  N   . THR B 1 120 D 3.058   -28.143 -13.555 1.00 24.51 ? 145 THR B N   1 
ATOM   2940 C  CA  . THR B 1 120 D 2.091   -27.516 -12.656 1.00 23.79 ? 145 THR B CA  1 
ATOM   2941 C  C   . THR B 1 120 D 2.795   -26.452 -11.815 1.00 23.82 ? 145 THR B C   1 
ATOM   2942 O  O   . THR B 1 120 D 2.222   -25.381 -11.625 1.00 24.19 ? 145 THR B O   1 
ATOM   2943 C  CB  . THR B 1 120 D 1.336   -28.553 -11.826 1.00 24.46 ? 145 THR B CB  1 
ATOM   2944 O  OG1 . THR B 1 120 D 2.279   -29.290 -11.060 1.00 26.17 ? 145 THR B OG1 1 
ATOM   2945 C  CG2 . THR B 1 120 D 0.563   -29.537 -12.694 1.00 25.33 ? 145 THR B CG2 1 
ATOM   2946 N  N   . ALA B 1 121 ? 4.048   -26.708 -11.415 1.00 23.98 ? 146 ALA B N   1 
ATOM   2947 C  CA  . ALA B 1 121 ? 4.878   -25.715 -10.743 1.00 25.24 ? 146 ALA B CA  1 
ATOM   2948 C  C   . ALA B 1 121 ? 5.107   -24.496 -11.635 1.00 24.68 ? 146 ALA B C   1 
ATOM   2949 O  O   . ALA B 1 121 ? 4.952   -23.362 -11.197 1.00 23.78 ? 146 ALA B O   1 
ATOM   2950 C  CB  . ALA B 1 121 ? 6.199   -26.311 -10.318 1.00 26.17 ? 146 ALA B CB  1 
ATOM   2951 N  N   . ALA B 1 122 ? 5.474   -24.721 -12.906 1.00 25.02 ? 147 ALA B N   1 
ATOM   2952 C  CA  . ALA B 1 122 ? 5.739   -23.598 -13.803 1.00 24.72 ? 147 ALA B CA  1 
ATOM   2953 C  C   . ALA B 1 122 ? 4.463   -22.803 -14.062 1.00 23.32 ? 147 ALA B C   1 
ATOM   2954 O  O   . ALA B 1 122 ? 4.473   -21.567 -14.142 1.00 23.70 ? 147 ALA B O   1 
ATOM   2955 C  CB  . ALA B 1 122 ? 6.363   -24.094 -15.080 1.00 25.51 ? 147 ALA B CB  1 
ATOM   2956 N  N   . PHE B 1 123 ? 3.349   -23.512 -14.200 1.00 22.43 ? 148 PHE B N   1 
ATOM   2957 C  CA  . PHE B 1 123 ? 2.082   -22.844 -14.426 1.00 22.25 ? 148 PHE B CA  1 
ATOM   2958 C  C   . PHE B 1 123 ? 1.785   -21.925 -13.244 1.00 22.73 ? 148 PHE B C   1 
ATOM   2959 O  O   . PHE B 1 123 ? 1.416   -20.760 -13.424 1.00 23.76 ? 148 PHE B O   1 
ATOM   2960 C  CB  . PHE B 1 123 ? 0.950   -23.850 -14.639 1.00 21.12 ? 148 PHE B CB  1 
ATOM   2961 C  CG  . PHE B 1 123 ? -0.416  -23.197 -14.553 1.00 22.16 ? 148 PHE B CG  1 
ATOM   2962 C  CD1 . PHE B 1 123 ? -0.940  -22.497 -15.623 1.00 22.93 ? 148 PHE B CD1 1 
ATOM   2963 C  CD2 . PHE B 1 123 ? -1.147  -23.222 -13.375 1.00 23.84 ? 148 PHE B CD2 1 
ATOM   2964 C  CE1 . PHE B 1 123 ? -2.173  -21.856 -15.519 1.00 22.82 ? 148 PHE B CE1 1 
ATOM   2965 C  CE2 . PHE B 1 123 ? -2.388  -22.604 -13.286 1.00 23.57 ? 148 PHE B CE2 1 
ATOM   2966 C  CZ  . PHE B 1 123 ? -2.896  -21.918 -14.359 1.00 22.67 ? 148 PHE B CZ  1 
ATOM   2967 N  N   . THR B 1 124 ? 1.941   -22.471 -12.040 1.00 24.45 ? 149 THR B N   1 
ATOM   2968 C  CA  . THR B 1 124 ? 1.625   -21.723 -10.827 1.00 24.45 ? 149 THR B CA  1 
ATOM   2969 C  C   . THR B 1 124 ? 2.547   -20.505 -10.761 1.00 25.17 ? 149 THR B C   1 
ATOM   2970 O  O   . THR B 1 124 ? 2.107   -19.419 -10.407 1.00 24.23 ? 149 THR B O   1 
ATOM   2971 C  CB  . THR B 1 124 ? 1.749   -22.634 -9.605  1.00 24.73 ? 149 THR B CB  1 
ATOM   2972 O  OG1 . THR B 1 124 ? 0.849   -23.745 -9.706  1.00 23.74 ? 149 THR B OG1 1 
ATOM   2973 C  CG2 . THR B 1 124 ? 1.482   -21.882 -8.310  1.00 25.28 ? 149 THR B CG2 1 
ATOM   2974 N  N   . GLY B 1 125 ? 3.819   -20.695 -11.160 1.00 25.98 ? 150 GLY B N   1 
ATOM   2975 C  CA  . GLY B 1 125 ? 4.800   -19.623 -11.204 1.00 26.94 ? 150 GLY B CA  1 
ATOM   2976 C  C   . GLY B 1 125 ? 4.378   -18.483 -12.127 1.00 26.86 ? 150 GLY B C   1 
ATOM   2977 O  O   . GLY B 1 125 ? 4.586   -17.320 -11.813 1.00 27.61 ? 150 GLY B O   1 
ATOM   2978 N  N   . TYR B 1 126 ? 3.770   -18.812 -13.258 1.00 27.22 ? 151 TYR B N   1 
ATOM   2979 C  CA  . TYR B 1 126 ? 3.323   -17.782 -14.168 1.00 27.38 ? 151 TYR B CA  1 
ATOM   2980 C  C   . TYR B 1 126 ? 2.274   -16.915 -13.469 1.00 28.27 ? 151 TYR B C   1 
ATOM   2981 O  O   . TYR B 1 126 ? 2.328   -15.683 -13.574 1.00 29.30 ? 151 TYR B O   1 
ATOM   2982 C  CB  . TYR B 1 126 ? 2.858   -18.409 -15.486 1.00 26.31 ? 151 TYR B CB  1 
ATOM   2983 C  CG  . TYR B 1 126 ? 2.383   -17.351 -16.462 1.00 25.25 ? 151 TYR B CG  1 
ATOM   2984 C  CD1 . TYR B 1 126 ? 3.283   -16.448 -17.020 1.00 26.49 ? 151 TYR B CD1 1 
ATOM   2985 C  CD2 . TYR B 1 126 ? 1.040   -17.221 -16.775 1.00 24.23 ? 151 TYR B CD2 1 
ATOM   2986 C  CE1 . TYR B 1 126 ? 2.858   -15.450 -17.886 1.00 26.69 ? 151 TYR B CE1 1 
ATOM   2987 C  CE2 . TYR B 1 126 ? 0.608   -16.246 -17.657 1.00 25.36 ? 151 TYR B CE2 1 
ATOM   2988 C  CZ  . TYR B 1 126 ? 1.516   -15.358 -18.210 1.00 25.86 ? 151 TYR B CZ  1 
ATOM   2989 O  OH  . TYR B 1 126 ? 1.056   -14.384 -19.051 1.00 28.83 ? 151 TYR B OH  1 
ATOM   2990 N  N   . LEU B 1 127 ? 1.330   -17.554 -12.756 1.00 27.65 ? 152 LEU B N   1 
ATOM   2991 C  CA  . LEU B 1 127 ? 0.359   -16.804 -11.979 1.00 27.93 ? 152 LEU B CA  1 
ATOM   2992 C  C   . LEU B 1 127 ? 1.055   -15.916 -10.945 1.00 28.56 ? 152 LEU B C   1 
ATOM   2993 O  O   . LEU B 1 127 ? 0.670   -14.770 -10.753 1.00 30.13 ? 152 LEU B O   1 
ATOM   2994 C  CB  . LEU B 1 127 ? -0.637  -17.742 -11.313 1.00 27.80 ? 152 LEU B CB  1 
ATOM   2995 C  CG  . LEU B 1 127 ? -1.455  -18.626 -12.262 1.00 26.29 ? 152 LEU B CG  1 
ATOM   2996 C  CD1 . LEU B 1 127 ? -2.468  -19.413 -11.473 1.00 25.43 ? 152 LEU B CD1 1 
ATOM   2997 C  CD2 . LEU B 1 127 ? -2.122  -17.785 -13.339 1.00 26.93 ? 152 LEU B CD2 1 
ATOM   2998 N  N   . ARG B 1 128 ? 2.096   -16.423 -10.301 1.00 27.22 ? 153 ARG B N   1 
ATOM   2999 C  CA  . ARG B 1 128 ? 2.833   -15.617 -9.334  1.00 28.64 ? 153 ARG B CA  1 
ATOM   3000 C  C   . ARG B 1 128 ? 3.433   -14.376 -10.003 1.00 29.31 ? 153 ARG B C   1 
ATOM   3001 O  O   . ARG B 1 128 ? 3.504   -13.314 -9.374  1.00 28.31 ? 153 ARG B O   1 
ATOM   3002 C  CB  . ARG B 1 128 ? 3.950   -16.418 -8.658  1.00 28.69 ? 153 ARG B CB  1 
ATOM   3003 C  CG  . ARG B 1 128 ? 3.433   -17.613 -7.868  1.00 28.56 ? 153 ARG B CG  1 
ATOM   3004 C  CD  . ARG B 1 128 ? 2.824   -17.244 -6.504  1.00 27.98 ? 153 ARG B CD  1 
ATOM   3005 N  NE  . ARG B 1 128 ? 2.367   -18.460 -5.818  1.00 26.41 ? 153 ARG B NE  1 
ATOM   3006 C  CZ  . ARG B 1 128 ? 1.156   -18.997 -5.897  1.00 26.18 ? 153 ARG B CZ  1 
ATOM   3007 N  NH1 . ARG B 1 128 ? 0.182   -18.432 -6.599  1.00 26.15 ? 153 ARG B NH1 1 
ATOM   3008 N  NH2 . ARG B 1 128 ? 0.913   -20.170 -5.327  1.00 26.51 ? 153 ARG B NH2 1 
ATOM   3009 N  N   . SER B 1 129 ? 3.893   -14.532 -11.256 1.00 28.87 ? 154 SER B N   1 
ATOM   3010 C  CA  . SER B 1 129 ? 4.471   -13.436 -12.028 1.00 29.26 ? 154 SER B CA  1 
ATOM   3011 C  C   . SER B 1 129 ? 3.425   -12.360 -12.310 1.00 29.28 ? 154 SER B C   1 
ATOM   3012 O  O   . SER B 1 129 ? 3.785   -11.210 -12.564 1.00 30.22 ? 154 SER B O   1 
ATOM   3013 C  CB  . SER B 1 129 ? 5.140   -13.924 -13.314 1.00 28.24 ? 154 SER B CB  1 
ATOM   3014 O  OG  . SER B 1 129 ? 4.186   -14.163 -14.348 1.00 26.24 ? 154 SER B OG  1 
ATOM   3015 N  N   . LEU B 1 130 ? 2.141   -12.726 -12.277 1.00 28.37 ? 155 LEU B N   1 
ATOM   3016 C  CA  . LEU B 1 130 ? 1.053   -11.780 -12.460 1.00 30.08 ? 155 LEU B CA  1 
ATOM   3017 C  C   . LEU B 1 130 ? 0.473   -11.285 -11.133 1.00 32.22 ? 155 LEU B C   1 
ATOM   3018 O  O   . LEU B 1 130 ? -0.609  -10.698 -11.136 1.00 34.68 ? 155 LEU B O   1 
ATOM   3019 C  CB  . LEU B 1 130 ? -0.057  -12.415 -13.288 1.00 29.71 ? 155 LEU B CB  1 
ATOM   3020 C  CG  . LEU B 1 130 ? 0.349   -12.900 -14.692 1.00 30.76 ? 155 LEU B CG  1 
ATOM   3021 C  CD1 . LEU B 1 130 ? -0.809  -13.656 -15.313 1.00 29.92 ? 155 LEU B CD1 1 
ATOM   3022 C  CD2 . LEU B 1 130 ? 0.830   -11.743 -15.536 1.00 31.60 ? 155 LEU B CD2 1 
ATOM   3023 N  N   . GLY B 1 131 ? 1.158   -11.530 -10.013 1.00 32.16 ? 156 GLY B N   1 
ATOM   3024 C  CA  . GLY B 1 131 ? 0.735   -10.992 -8.728  1.00 31.76 ? 156 GLY B CA  1 
ATOM   3025 C  C   . GLY B 1 131 ? -0.300  -11.867 -8.015  1.00 31.42 ? 156 GLY B C   1 
ATOM   3026 O  O   . GLY B 1 131 ? -0.830  -11.476 -6.965  1.00 30.87 ? 156 GLY B O   1 
ATOM   3027 N  N   . ASP B 1 132 ? -0.596  -13.055 -8.574  1.00 29.18 ? 157 ASP B N   1 
ATOM   3028 C  CA  . ASP B 1 132 ? -1.534  -13.980 -7.959  1.00 28.08 ? 157 ASP B CA  1 
ATOM   3029 C  C   . ASP B 1 132 ? -0.765  -14.891 -7.007  1.00 27.95 ? 157 ASP B C   1 
ATOM   3030 O  O   . ASP B 1 132 ? -0.079  -15.810 -7.453  1.00 27.09 ? 157 ASP B O   1 
ATOM   3031 C  CB  . ASP B 1 132 ? -2.318  -14.776 -8.989  1.00 26.95 ? 157 ASP B CB  1 
ATOM   3032 C  CG  . ASP B 1 132 ? -3.227  -15.867 -8.429  1.00 27.04 ? 157 ASP B CG  1 
ATOM   3033 O  OD1 . ASP B 1 132 ? -3.268  -16.039 -7.172  1.00 26.75 ? 157 ASP B OD1 1 
ATOM   3034 O  OD2 . ASP B 1 132 ? -3.917  -16.511 -9.248  1.00 26.63 ? 157 ASP B OD2 1 
ATOM   3035 N  N   . THR B 1 133 ? -0.909  -14.637 -5.697  1.00 29.31 ? 158 THR B N   1 
ATOM   3036 C  CA  . THR B 1 133 ? -0.169  -15.389 -4.695  1.00 30.23 ? 158 THR B CA  1 
ATOM   3037 C  C   . THR B 1 133 ? -1.052  -16.476 -4.070  1.00 29.51 ? 158 THR B C   1 
ATOM   3038 O  O   . THR B 1 133 ? -0.640  -17.121 -3.117  1.00 29.97 ? 158 THR B O   1 
ATOM   3039 C  CB  . THR B 1 133 ? 0.366   -14.444 -3.621  1.00 32.68 ? 158 THR B CB  1 
ATOM   3040 O  OG1 . THR B 1 133 ? -0.761  -13.883 -2.963  1.00 32.28 ? 158 THR B OG1 1 
ATOM   3041 C  CG2 . THR B 1 133 ? 1.250   -13.351 -4.186  1.00 33.49 ? 158 THR B CG2 1 
ATOM   3042 N  N   . VAL B 1 134 ? -2.260  -16.673 -4.602  1.00 28.10 ? 159 VAL B N   1 
ATOM   3043 C  CA  . VAL B 1 134 ? -3.293  -17.481 -3.971  1.00 29.44 ? 159 VAL B CA  1 
ATOM   3044 C  C   . VAL B 1 134 ? -3.475  -18.799 -4.728  1.00 28.10 ? 159 VAL B C   1 
ATOM   3045 O  O   . VAL B 1 134 ? -3.477  -19.867 -4.117  1.00 27.34 ? 159 VAL B O   1 
ATOM   3046 C  CB  . VAL B 1 134 ? -4.593  -16.655 -3.952  1.00 31.94 ? 159 VAL B CB  1 
ATOM   3047 C  CG1 . VAL B 1 134 ? -5.795  -17.497 -3.579  1.00 32.67 ? 159 VAL B CG1 1 
ATOM   3048 C  CG2 . VAL B 1 134 ? -4.507  -15.437 -3.035  1.00 33.63 ? 159 VAL B CG2 1 
ATOM   3049 N  N   . SER B 1 135 ? -3.635  -18.707 -6.055  1.00 25.39 ? 160 SER B N   1 
ATOM   3050 C  CA  . SER B 1 135 ? -3.945  -19.854 -6.899  1.00 25.37 ? 160 SER B CA  1 
ATOM   3051 C  C   . SER B 1 135 ? -2.802  -20.855 -6.904  1.00 25.25 ? 160 SER B C   1 
ATOM   3052 O  O   . SER B 1 135 ? -1.628  -20.484 -6.771  1.00 25.81 ? 160 SER B O   1 
ATOM   3053 C  CB  . SER B 1 135 ? -4.254  -19.420 -8.318  1.00 25.59 ? 160 SER B CB  1 
ATOM   3054 O  OG  . SER B 1 135 ? -5.289  -18.439 -8.340  1.00 25.16 ? 160 SER B OG  1 
ATOM   3055 N  N   . ARG B 1 136 ? -3.159  -22.140 -7.073  1.00 24.87 ? 161 ARG B N   1 
ATOM   3056 C  CA  . ARG B 1 136 ? -2.150  -23.173 -7.199  1.00 25.59 ? 161 ARG B CA  1 
ATOM   3057 C  C   . ARG B 1 136 ? -2.687  -24.308 -8.067  1.00 24.97 ? 161 ARG B C   1 
ATOM   3058 O  O   . ARG B 1 136 ? -3.846  -24.712 -7.954  1.00 25.74 ? 161 ARG B O   1 
ATOM   3059 C  CB  . ARG B 1 136 ? -1.698  -23.669 -5.820  1.00 27.92 ? 161 ARG B CB  1 
ATOM   3060 C  CG  . ARG B 1 136 ? -2.867  -24.171 -4.982  1.00 28.77 ? 161 ARG B CG  1 
ATOM   3061 C  CD  . ARG B 1 136 ? -2.450  -24.614 -3.591  1.00 30.69 ? 161 ARG B CD  1 
ATOM   3062 N  NE  . ARG B 1 136 ? -1.553  -25.771 -3.681  1.00 30.15 ? 161 ARG B NE  1 
ATOM   3063 C  CZ  . ARG B 1 136 ? -0.900  -26.316 -2.648  1.00 33.03 ? 161 ARG B CZ  1 
ATOM   3064 N  NH1 . ARG B 1 136 ? -0.987  -25.807 -1.415  1.00 33.37 ? 161 ARG B NH1 1 
ATOM   3065 N  NH2 . ARG B 1 136 ? -0.137  -27.379 -2.865  1.00 33.45 ? 161 ARG B NH2 1 
ATOM   3066 N  N   . LEU B 1 137 ? -1.827  -24.796 -8.954  1.00 23.58 ? 162 LEU B N   1 
ATOM   3067 C  CA  . LEU B 1 137 ? -2.083  -26.037 -9.674  1.00 23.91 ? 162 LEU B CA  1 
ATOM   3068 C  C   . LEU B 1 137 ? -1.058  -27.076 -9.240  1.00 24.37 ? 162 LEU B C   1 
ATOM   3069 O  O   . LEU B 1 137 ? 0.134   -26.786 -9.192  1.00 24.88 ? 162 LEU B O   1 
ATOM   3070 C  CB  . LEU B 1 137 ? -2.038  -25.818 -11.177 1.00 23.96 ? 162 LEU B CB  1 
ATOM   3071 C  CG  . LEU B 1 137 ? -2.548  -26.967 -12.054 1.00 23.52 ? 162 LEU B CG  1 
ATOM   3072 C  CD1 . LEU B 1 137 ? -4.024  -27.107 -11.926 1.00 24.11 ? 162 LEU B CD1 1 
ATOM   3073 C  CD2 . LEU B 1 137 ? -2.196  -26.750 -13.505 1.00 24.49 ? 162 LEU B CD2 1 
ATOM   3074 N  N   . ASP B 1 138 ? -1.546  -28.301 -8.995  1.00 24.98 ? 163 ASP B N   1 
ATOM   3075 C  CA  . ASP B 1 138 ? -0.778  -29.346 -8.344  1.00 26.81 ? 163 ASP B CA  1 
ATOM   3076 C  C   . ASP B 1 138 ? -0.764  -30.634 -9.152  1.00 27.60 ? 163 ASP B C   1 
ATOM   3077 O  O   . ASP B 1 138 ? 0.240   -31.338 -9.137  1.00 30.39 ? 163 ASP B O   1 
ATOM   3078 C  CB  . ASP B 1 138 ? -1.318  -29.611 -6.952  1.00 28.11 ? 163 ASP B CB  1 
ATOM   3079 C  CG  . ASP B 1 138 ? -1.091  -28.406 -6.062  1.00 27.91 ? 163 ASP B CG  1 
ATOM   3080 O  OD1 . ASP B 1 138 ? 0.013   -28.353 -5.495  1.00 28.54 ? 163 ASP B OD1 1 
ATOM   3081 O  OD2 . ASP B 1 138 ? -1.980  -27.505 -6.042  1.00 25.66 ? 163 ASP B OD2 1 
ATOM   3082 N  N   . ALA B 1 139 ? -1.887  -30.961 -9.794  1.00 26.56 ? 164 ALA B N   1 
ATOM   3083 C  CA  . ALA B 1 139 ? -1.998  -32.170 -10.587 1.00 26.65 ? 164 ALA B CA  1 
ATOM   3084 C  C   . ALA B 1 139 ? -2.261  -31.812 -12.043 1.00 25.51 ? 164 ALA B C   1 
ATOM   3085 O  O   . ALA B 1 139 ? -2.656  -30.703 -12.360 1.00 24.12 ? 164 ALA B O   1 
ATOM   3086 C  CB  . ALA B 1 139 ? -3.113  -33.033 -10.038 1.00 27.27 ? 164 ALA B CB  1 
ATOM   3087 N  N   . GLU B 1 140 ? -2.090  -32.806 -12.909 1.00 27.33 ? 165 GLU B N   1 
ATOM   3088 C  CA  . GLU B 1 140 ? -2.470  -32.663 -14.294 1.00 27.34 ? 165 GLU B CA  1 
ATOM   3089 C  C   . GLU B 1 140 ? -3.849  -33.289 -14.476 1.00 26.51 ? 165 GLU B C   1 
ATOM   3090 O  O   . GLU B 1 140 ? -4.525  -33.659 -13.519 1.00 24.73 ? 165 GLU B O   1 
ATOM   3091 C  CB  . GLU B 1 140 ? -1.320  -33.168 -15.165 1.00 29.56 ? 165 GLU B CB  1 
ATOM   3092 C  CG  . GLU B 1 140 ? -1.123  -34.676 -15.150 1.00 34.89 ? 165 GLU B CG  1 
ATOM   3093 C  CD  . GLU B 1 140 ? -0.088  -35.115 -16.175 1.00 40.33 ? 165 GLU B CD  1 
ATOM   3094 O  OE1 . GLU B 1 140 ? 0.546   -34.229 -16.803 1.00 39.22 ? 165 GLU B OE1 1 
ATOM   3095 O  OE2 . GLU B 1 140 ? 0.013   -36.347 -16.384 1.00 43.41 ? 165 GLU B OE2 1 
ATOM   3096 N  N   . GLU B 1 141 ? -4.276  -33.311 -15.740 1.00 26.80 ? 166 GLU B N   1 
ATOM   3097 C  CA  . GLU B 1 141 ? -5.564  -33.839 -16.134 1.00 26.06 ? 166 GLU B CA  1 
ATOM   3098 C  C   . GLU B 1 141 ? -5.447  -35.350 -16.106 1.00 26.58 ? 166 GLU B C   1 
ATOM   3099 O  O   . GLU B 1 141 ? -4.420  -35.845 -16.551 1.00 27.32 ? 166 GLU B O   1 
ATOM   3100 C  CB  . GLU B 1 141 ? -5.868  -33.459 -17.585 1.00 26.95 ? 166 GLU B CB  1 
ATOM   3101 C  CG  . GLU B 1 141 ? -6.208  -31.987 -17.797 1.00 26.97 ? 166 GLU B CG  1 
ATOM   3102 C  CD  . GLU B 1 141 ? -7.576  -31.596 -17.250 1.00 28.63 ? 166 GLU B CD  1 
ATOM   3103 O  OE1 . GLU B 1 141 ? -8.262  -32.444 -16.645 1.00 26.76 ? 166 GLU B OE1 1 
ATOM   3104 O  OE2 . GLU B 1 141 ? -7.933  -30.404 -17.410 1.00 29.34 ? 166 GLU B OE2 1 
ATOM   3105 N  N   . PRO B 1 142 ? -6.475  -36.111 -15.656 1.00 25.57 ? 167 PRO B N   1 
ATOM   3106 C  CA  . PRO B 1 142 ? -7.726  -35.534 -15.137 1.00 25.71 ? 167 PRO B CA  1 
ATOM   3107 C  C   . PRO B 1 142 ? -7.849  -35.304 -13.629 1.00 26.36 ? 167 PRO B C   1 
ATOM   3108 O  O   . PRO B 1 142 ? -8.881  -34.815 -13.173 1.00 27.69 ? 167 PRO B O   1 
ATOM   3109 C  CB  . PRO B 1 142 ? -8.720  -36.601 -15.610 1.00 26.47 ? 167 PRO B CB  1 
ATOM   3110 C  CG  . PRO B 1 142 ? -7.966  -37.898 -15.333 1.00 27.28 ? 167 PRO B CG  1 
ATOM   3111 C  CD  . PRO B 1 142 ? -6.525  -37.580 -15.757 1.00 26.68 ? 167 PRO B CD  1 
ATOM   3112 N  N   . GLU B 1 143 ? -6.801  -35.650 -12.880 1.00 26.49 ? 168 GLU B N   1 
ATOM   3113 C  CA  . GLU B 1 143 ? -6.821  -35.665 -11.421 1.00 27.81 ? 168 GLU B CA  1 
ATOM   3114 C  C   . GLU B 1 143 ? -7.145  -34.287 -10.844 1.00 26.27 ? 168 GLU B C   1 
ATOM   3115 O  O   . GLU B 1 143 ? -7.837  -34.189 -9.825  1.00 26.65 ? 168 GLU B O   1 
ATOM   3116 C  CB  . GLU B 1 143 ? -5.513  -36.191 -10.825 1.00 30.36 ? 168 GLU B CB  1 
ATOM   3117 C  CG  . GLU B 1 143 ? -5.300  -37.685 -11.059 1.00 32.70 ? 168 GLU B CG  1 
ATOM   3118 C  CD  . GLU B 1 143 ? -4.716  -38.048 -12.418 1.00 35.00 ? 168 GLU B CD  1 
ATOM   3119 O  OE1 . GLU B 1 143 ? -4.335  -37.159 -13.235 1.00 32.92 ? 168 GLU B OE1 1 
ATOM   3120 O  OE2 . GLU B 1 143 ? -4.639  -39.277 -12.655 1.00 39.19 ? 168 GLU B OE2 1 
ATOM   3121 N  N   . LEU B 1 144 ? -6.740  -33.216 -11.550 1.00 25.81 ? 169 LEU B N   1 
ATOM   3122 C  CA  . LEU B 1 144 ? -6.918  -31.860 -11.050 1.00 25.09 ? 169 LEU B CA  1 
ATOM   3123 C  C   . LEU B 1 144 ? -8.407  -31.540 -10.883 1.00 25.53 ? 169 LEU B C   1 
ATOM   3124 O  O   . LEU B 1 144 ? -8.734  -30.537 -10.248 1.00 24.42 ? 169 LEU B O   1 
ATOM   3125 C  CB  . LEU B 1 144 ? -6.203  -30.822 -11.924 1.00 25.27 ? 169 LEU B CB  1 
ATOM   3126 C  CG  . LEU B 1 144 ? -6.684  -30.615 -13.365 1.00 25.84 ? 169 LEU B CG  1 
ATOM   3127 C  CD1 . LEU B 1 144 ? -7.836  -29.654 -13.462 1.00 26.41 ? 169 LEU B CD1 1 
ATOM   3128 C  CD2 . LEU B 1 144 ? -5.573  -30.121 -14.275 1.00 27.08 ? 169 LEU B CD2 1 
ATOM   3129 N  N   . ASN B 1 145 ? -9.308  -32.345 -11.476 1.00 25.24 ? 170 ASN B N   1 
ATOM   3130 C  CA  . ASN B 1 145 ? -10.735 -32.040 -11.389 1.00 28.08 ? 170 ASN B CA  1 
ATOM   3131 C  C   . ASN B 1 145 ? -11.397 -32.708 -10.174 1.00 28.10 ? 170 ASN B C   1 
ATOM   3132 O  O   . ASN B 1 145 ? -12.598 -32.531 -9.971  1.00 29.25 ? 170 ASN B O   1 
ATOM   3133 C  CB  . ASN B 1 145 ? -11.488 -32.434 -12.653 1.00 26.51 ? 170 ASN B CB  1 
ATOM   3134 C  CG  . ASN B 1 145 ? -10.872 -31.803 -13.871 1.00 26.49 ? 170 ASN B CG  1 
ATOM   3135 O  OD1 . ASN B 1 145 ? -10.986 -30.591 -14.070 1.00 28.15 ? 170 ASN B OD1 1 
ATOM   3136 N  ND2 . ASN B 1 145 ? -10.222 -32.601 -14.706 1.00 25.79 ? 170 ASN B ND2 1 
ATOM   3137 N  N   . ARG B 1 146 ? -10.629 -33.502 -9.417  1.00 28.53 ? 171 ARG B N   1 
ATOM   3138 C  CA  . ARG B 1 146 ? -11.178 -34.546 -8.567  1.00 29.72 ? 171 ARG B CA  1 
ATOM   3139 C  C   . ARG B 1 146 ? -10.760 -34.369 -7.111  1.00 29.93 ? 171 ARG B C   1 
ATOM   3140 O  O   . ARG B 1 146 ? -11.020 -35.257 -6.312  1.00 31.68 ? 171 ARG B O   1 
ATOM   3141 C  CB  . ARG B 1 146 ? -10.704 -35.928 -9.040  1.00 30.82 ? 171 ARG B CB  1 
ATOM   3142 C  CG  . ARG B 1 146 ? -10.908 -36.134 -10.532 1.00 32.80 ? 171 ARG B CG  1 
ATOM   3143 C  CD  . ARG B 1 146 ? -10.671 -37.547 -10.992 1.00 35.17 ? 171 ARG B CD  1 
ATOM   3144 N  NE  . ARG B 1 146 ? -11.058 -37.675 -12.407 1.00 37.33 ? 171 ARG B NE  1 
ATOM   3145 C  CZ  . ARG B 1 146 ? -10.938 -38.800 -13.097 1.00 38.90 ? 171 ARG B CZ  1 
ATOM   3146 N  NH1 . ARG B 1 146 ? -10.422 -39.856 -12.498 1.00 39.92 ? 171 ARG B NH1 1 
ATOM   3147 N  NH2 . ARG B 1 146 ? -11.289 -38.860 -14.374 1.00 40.18 ? 171 ARG B NH2 1 
ATOM   3148 N  N   . ASP B 1 147 ? -10.167 -33.228 -6.727  1.00 29.23 ? 172 ASP B N   1 
ATOM   3149 C  CA  . ASP B 1 147 ? -9.682  -33.088 -5.360  1.00 29.29 ? 172 ASP B CA  1 
ATOM   3150 C  C   . ASP B 1 147 ? -10.873 -33.064 -4.417  1.00 27.96 ? 172 ASP B C   1 
ATOM   3151 O  O   . ASP B 1 147 ? -11.936 -32.579 -4.781  1.00 26.87 ? 172 ASP B O   1 
ATOM   3152 C  CB  . ASP B 1 147 ? -8.885  -31.806 -5.155  1.00 30.33 ? 172 ASP B CB  1 
ATOM   3153 C  CG  . ASP B 1 147 ? -7.524  -31.735 -5.840  1.00 30.63 ? 172 ASP B CG  1 
ATOM   3154 O  OD1 . ASP B 1 147 ? -6.592  -32.378 -5.340  1.00 34.15 ? 172 ASP B OD1 1 
ATOM   3155 O  OD2 . ASP B 1 147 ? -7.411  -31.046 -6.868  1.00 31.49 ? 172 ASP B OD2 1 
ATOM   3156 N  N   . PRO B 1 148 ? -10.750 -33.574 -3.170  1.00 30.15 ? 173 PRO B N   1 
ATOM   3157 C  CA  . PRO B 1 148 ? -11.837 -33.472 -2.199  1.00 29.77 ? 173 PRO B CA  1 
ATOM   3158 C  C   . PRO B 1 148 ? -12.219 -32.025 -1.893  1.00 28.67 ? 173 PRO B C   1 
ATOM   3159 O  O   . PRO B 1 148 ? -11.382 -31.118 -1.936  1.00 26.91 ? 173 PRO B O   1 
ATOM   3160 C  CB  . PRO B 1 148 ? -11.293 -34.197 -0.966  1.00 32.06 ? 173 PRO B CB  1 
ATOM   3161 C  CG  . PRO B 1 148 ? -10.123 -34.991 -1.468  1.00 32.21 ? 173 PRO B CG  1 
ATOM   3162 C  CD  . PRO B 1 148 ? -9.544  -34.197 -2.611  1.00 31.72 ? 173 PRO B CD  1 
ATOM   3163 N  N   . PRO B 1 149 ? -13.511 -31.739 -1.609  1.00 29.03 ? 174 PRO B N   1 
ATOM   3164 C  CA  . PRO B 1 149 ? -13.921 -30.417 -1.120  1.00 28.12 ? 174 PRO B CA  1 
ATOM   3165 C  C   . PRO B 1 149 ? -13.095 -30.007 0.092   1.00 28.05 ? 174 PRO B C   1 
ATOM   3166 O  O   . PRO B 1 149 ? -12.794 -30.844 0.908   1.00 29.01 ? 174 PRO B O   1 
ATOM   3167 C  CB  . PRO B 1 149 ? -15.405 -30.615 -0.769  1.00 29.61 ? 174 PRO B CB  1 
ATOM   3168 C  CG  . PRO B 1 149 ? -15.825 -31.730 -1.708  1.00 29.81 ? 174 PRO B CG  1 
ATOM   3169 C  CD  . PRO B 1 149 ? -14.638 -32.681 -1.717  1.00 29.10 ? 174 PRO B CD  1 
ATOM   3170 N  N   . GLY B 1 150 ? -12.704 -28.726 0.165   1.00 28.43 ? 175 GLY B N   1 
ATOM   3171 C  CA  . GLY B 1 150 ? -11.842 -28.224 1.220   1.00 29.97 ? 175 GLY B CA  1 
ATOM   3172 C  C   . GLY B 1 150 ? -10.359 -28.234 0.831   1.00 29.54 ? 175 GLY B C   1 
ATOM   3173 O  O   . GLY B 1 150 ? -9.571  -27.502 1.405   1.00 29.48 ? 175 GLY B O   1 
ATOM   3174 N  N   . ASP B 1 151 ? -9.959  -29.069 -0.131  1.00 29.19 ? 176 ASP B N   1 
ATOM   3175 C  CA  . ASP B 1 151 ? -8.548  -29.223 -0.463  1.00 28.22 ? 176 ASP B CA  1 
ATOM   3176 C  C   . ASP B 1 151 ? -8.082  -28.003 -1.256  1.00 27.60 ? 176 ASP B C   1 
ATOM   3177 O  O   . ASP B 1 151 ? -8.733  -27.612 -2.220  1.00 26.69 ? 176 ASP B O   1 
ATOM   3178 C  CB  . ASP B 1 151 ? -8.336  -30.507 -1.262  1.00 27.97 ? 176 ASP B CB  1 
ATOM   3179 C  CG  . ASP B 1 151 ? -6.898  -30.993 -1.388  1.00 27.19 ? 176 ASP B CG  1 
ATOM   3180 O  OD1 . ASP B 1 151 ? -6.069  -30.209 -1.863  1.00 26.02 ? 176 ASP B OD1 1 
ATOM   3181 O  OD2 . ASP B 1 151 ? -6.638  -32.151 -1.011  1.00 27.85 ? 176 ASP B OD2 1 
ATOM   3182 N  N   . GLU B 1 152 ? -6.899  -27.477 -0.934  1.00 27.13 ? 177 GLU B N   1 
ATOM   3183 C  CA  . GLU B 1 152 ? -6.425  -26.246 -1.560  1.00 28.07 ? 177 GLU B CA  1 
ATOM   3184 C  C   . GLU B 1 152 ? -5.737  -26.531 -2.894  1.00 26.78 ? 177 GLU B C   1 
ATOM   3185 O  O   . GLU B 1 152 ? -5.560  -25.643 -3.719  1.00 26.33 ? 177 GLU B O   1 
ATOM   3186 C  CB  . GLU B 1 152 ? -5.479  -25.428 -0.679  1.00 31.04 ? 177 GLU B CB  1 
ATOM   3187 C  CG  . GLU B 1 152 ? -6.174  -24.924 0.580   1.00 33.74 ? 177 GLU B CG  1 
ATOM   3188 C  CD  . GLU B 1 152 ? -5.339  -24.048 1.500   1.00 37.61 ? 177 GLU B CD  1 
ATOM   3189 O  OE1 . GLU B 1 152 ? -4.185  -23.668 1.181   1.00 35.87 ? 177 GLU B OE1 1 
ATOM   3190 O  OE2 . GLU B 1 152 ? -5.890  -23.781 2.589   1.00 39.23 ? 177 GLU B OE2 1 
ATOM   3191 N  N   . ARG B 1 153 ? -5.328  -27.766 -3.109  1.00 26.82 ? 178 ARG B N   1 
ATOM   3192 C  CA  . ARG B 1 153 ? -4.694  -28.151 -4.362  1.00 27.33 ? 178 ARG B CA  1 
ATOM   3193 C  C   . ARG B 1 153 ? -5.622  -27.875 -5.537  1.00 25.20 ? 178 ARG B C   1 
ATOM   3194 O  O   . ARG B 1 153 ? -6.832  -28.113 -5.475  1.00 25.83 ? 178 ARG B O   1 
ATOM   3195 C  CB  . ARG B 1 153 ? -4.305  -29.635 -4.314  1.00 29.32 ? 178 ARG B CB  1 
ATOM   3196 C  CG  . ARG B 1 153 ? -3.148  -29.875 -3.345  1.00 33.46 ? 178 ARG B CG  1 
ATOM   3197 C  CD  . ARG B 1 153 ? -2.726  -31.330 -3.276  1.00 36.34 ? 178 ARG B CD  1 
ATOM   3198 N  NE  . ARG B 1 153 ? -3.761  -32.213 -2.734  1.00 39.02 ? 178 ARG B NE  1 
ATOM   3199 C  CZ  . ARG B 1 153 ? -4.018  -33.456 -3.154  1.00 42.76 ? 178 ARG B CZ  1 
ATOM   3200 N  NH1 . ARG B 1 153 ? -3.193  -34.071 -3.988  1.00 45.95 ? 178 ARG B NH1 1 
ATOM   3201 N  NH2 . ARG B 1 153 ? -5.080  -34.106 -2.717  1.00 41.89 ? 178 ARG B NH2 1 
ATOM   3202 N  N   . ASP B 1 154 ? -5.033  -27.345 -6.608  1.00 23.96 ? 179 ASP B N   1 
ATOM   3203 C  CA  . ASP B 1 154 ? -5.725  -27.174 -7.878  1.00 23.17 ? 179 ASP B CA  1 
ATOM   3204 C  C   . ASP B 1 154 ? -6.867  -26.165 -7.741  1.00 22.04 ? 179 ASP B C   1 
ATOM   3205 O  O   . ASP B 1 154 ? -7.865  -26.263 -8.445  1.00 21.17 ? 179 ASP B O   1 
ATOM   3206 C  CB  . ASP B 1 154 ? -6.203  -28.518 -8.414  1.00 23.51 ? 179 ASP B CB  1 
ATOM   3207 C  CG  . ASP B 1 154 ? -5.105  -29.564 -8.510  1.00 23.65 ? 179 ASP B CG  1 
ATOM   3208 O  OD1 . ASP B 1 154 ? -4.068  -29.192 -9.084  1.00 21.67 ? 179 ASP B OD1 1 
ATOM   3209 O  OD2 . ASP B 1 154 ? -5.302  -30.728 -8.033  1.00 23.56 ? 179 ASP B OD2 1 
ATOM   3210 N  N   . THR B 1 155 ? -6.694  -25.151 -6.885  1.00 21.56 ? 180 THR B N   1 
ATOM   3211 C  CA  . THR B 1 155 ? -7.741  -24.176 -6.653  1.00 22.93 ? 180 THR B CA  1 
ATOM   3212 C  C   . THR B 1 155 ? -7.255  -22.789 -7.025  1.00 22.51 ? 180 THR B C   1 
ATOM   3213 O  O   . THR B 1 155 ? -6.055  -22.509 -7.005  1.00 22.78 ? 180 THR B O   1 
ATOM   3214 C  CB  . THR B 1 155 ? -8.246  -24.170 -5.205  1.00 23.90 ? 180 THR B CB  1 
ATOM   3215 O  OG1 . THR B 1 155 ? -7.216  -23.750 -4.312  1.00 27.04 ? 180 THR B OG1 1 
ATOM   3216 C  CG2 . THR B 1 155 ? -8.802  -25.517 -4.797  1.00 24.36 ? 180 THR B CG2 1 
ATOM   3217 N  N   . THR B 1 156 ? -8.243  -21.955 -7.329  1.00 22.46 ? 181 THR B N   1 
ATOM   3218 C  CA  . THR B 1 156 ? -8.099  -20.509 -7.396  1.00 22.87 ? 181 THR B CA  1 
ATOM   3219 C  C   . THR B 1 156 ? -9.229  -19.911 -6.558  1.00 23.67 ? 181 THR B C   1 
ATOM   3220 O  O   . THR B 1 156 ? -9.933  -20.645 -5.848  1.00 22.45 ? 181 THR B O   1 
ATOM   3221 C  CB  . THR B 1 156 ? -8.092  -20.062 -8.867  1.00 22.32 ? 181 THR B CB  1 
ATOM   3222 O  OG1 . THR B 1 156 ? -7.747  -18.678 -8.974  1.00 24.50 ? 181 THR B OG1 1 
ATOM   3223 C  CG2 . THR B 1 156 ? -9.421  -20.317 -9.558  1.00 22.62 ? 181 THR B CG2 1 
ATOM   3224 N  N   . THR B 1 157 ? -9.387  -18.576 -6.627  1.00 23.04 ? 182 THR B N   1 
ATOM   3225 C  CA  . THR B 1 157 ? -10.583 -17.932 -6.098  1.00 23.10 ? 182 THR B CA  1 
ATOM   3226 C  C   . THR B 1 157 ? -11.195 -17.104 -7.222  1.00 22.79 ? 182 THR B C   1 
ATOM   3227 O  O   . THR B 1 157 ? -10.493 -16.702 -8.143  1.00 22.04 ? 182 THR B O   1 
ATOM   3228 C  CB  . THR B 1 157 ? -10.281 -17.055 -4.887  1.00 23.54 ? 182 THR B CB  1 
ATOM   3229 O  OG1 . THR B 1 157 ? -9.569  -15.920 -5.387  1.00 24.47 ? 182 THR B OG1 1 
ATOM   3230 C  CG2 . THR B 1 157 ? -9.536  -17.815 -3.789  1.00 23.52 ? 182 THR B CG2 1 
ATOM   3231 N  N   . PRO B 1 158 ? -12.509 -16.818 -7.185  1.00 22.92 ? 183 PRO B N   1 
ATOM   3232 C  CA  . PRO B 1 158 ? -13.085 -15.926 -8.186  1.00 23.28 ? 183 PRO B CA  1 
ATOM   3233 C  C   . PRO B 1 158 ? -12.320 -14.606 -8.346  1.00 24.83 ? 183 PRO B C   1 
ATOM   3234 O  O   . PRO B 1 158 ? -12.048 -14.162 -9.472  1.00 25.45 ? 183 PRO B O   1 
ATOM   3235 C  CB  . PRO B 1 158 ? -14.534 -15.780 -7.674  1.00 23.64 ? 183 PRO B CB  1 
ATOM   3236 C  CG  . PRO B 1 158 ? -14.813 -17.089 -6.946  1.00 22.84 ? 183 PRO B CG  1 
ATOM   3237 C  CD  . PRO B 1 158 ? -13.498 -17.381 -6.246  1.00 23.50 ? 183 PRO B CD  1 
ATOM   3238 N  N   . HIS B 1 159 ? -11.922 -14.015 -7.218  1.00 25.24 ? 184 HIS B N   1 
ATOM   3239 C  CA  . HIS B 1 159 ? -11.177 -12.767 -7.177  1.00 26.36 ? 184 HIS B CA  1 
ATOM   3240 C  C   . HIS B 1 159 ? -9.828  -12.928 -7.876  1.00 25.82 ? 184 HIS B C   1 
ATOM   3241 O  O   . HIS B 1 159 ? -9.464  -12.104 -8.711  1.00 24.66 ? 184 HIS B O   1 
ATOM   3242 C  CB  . HIS B 1 159 ? -11.007 -12.325 -5.721  1.00 27.49 ? 184 HIS B CB  1 
ATOM   3243 C  CG  . HIS B 1 159 ? -10.456 -10.958 -5.499  1.00 29.51 ? 184 HIS B CG  1 
ATOM   3244 N  ND1 . HIS B 1 159 ? -10.461 -10.350 -4.252  1.00 32.68 ? 184 HIS B ND1 1 
ATOM   3245 C  CD2 . HIS B 1 159 ? -9.860  -10.094 -6.323  1.00 31.29 ? 184 HIS B CD2 1 
ATOM   3246 C  CE1 . HIS B 1 159 ? -9.903  -9.140  -4.343  1.00 33.11 ? 184 HIS B CE1 1 
ATOM   3247 N  NE2 . HIS B 1 159 ? -9.495  -8.981  -5.588  1.00 32.51 ? 184 HIS B NE2 1 
ATOM   3248 N  N   . ALA B 1 160 ? -9.079  -13.984 -7.533  1.00 24.69 ? 185 ALA B N   1 
ATOM   3249 C  CA  . ALA B 1 160 ? -7.727  -14.148 -8.055  1.00 24.39 ? 185 ALA B CA  1 
ATOM   3250 C  C   . ALA B 1 160 ? -7.758  -14.378 -9.569  1.00 24.25 ? 185 ALA B C   1 
ATOM   3251 O  O   . ALA B 1 160 ? -6.999  -13.761 -10.329 1.00 22.21 ? 185 ALA B O   1 
ATOM   3252 C  CB  . ALA B 1 160 ? -7.008  -15.282 -7.339  1.00 24.69 ? 185 ALA B CB  1 
ATOM   3253 N  N   . ILE B 1 161 ? -8.640  -15.283 -10.012 1.00 24.30 ? 186 ILE B N   1 
ATOM   3254 C  CA  . ILE B 1 161 ? -8.643  -15.662 -11.404 1.00 23.61 ? 186 ILE B CA  1 
ATOM   3255 C  C   . ILE B 1 161 ? -9.197  -14.503 -12.226 1.00 23.76 ? 186 ILE B C   1 
ATOM   3256 O  O   . ILE B 1 161 ? -8.769  -14.301 -13.359 1.00 23.91 ? 186 ILE B O   1 
ATOM   3257 C  CB  . ILE B 1 161 ? -9.336  -17.013 -11.666 1.00 23.28 ? 186 ILE B CB  1 
ATOM   3258 C  CG1 . ILE B 1 161 ? -9.009  -17.555 -13.074 1.00 25.47 ? 186 ILE B CG1 1 
ATOM   3259 C  CG2 . ILE B 1 161 ? -10.843 -16.938 -11.468 1.00 23.67 ? 186 ILE B CG2 1 
ATOM   3260 C  CD1 . ILE B 1 161 ? -7.529  -17.745 -13.360 1.00 27.08 ? 186 ILE B CD1 1 
ATOM   3261 N  N   . ALA B 1 162 ? -10.122 -13.727 -11.670 1.00 22.56 ? 187 ALA B N   1 
ATOM   3262 C  CA  . ALA B 1 162 ? -10.631 -12.555 -12.383 1.00 22.72 ? 187 ALA B CA  1 
ATOM   3263 C  C   . ALA B 1 162 ? -9.513  -11.548 -12.649 1.00 24.34 ? 187 ALA B C   1 
ATOM   3264 O  O   . ALA B 1 162 ? -9.393  -11.045 -13.765 1.00 25.77 ? 187 ALA B O   1 
ATOM   3265 C  CB  . ALA B 1 162 ? -11.775 -11.929 -11.649 1.00 23.25 ? 187 ALA B CB  1 
ATOM   3266 N  N   . LEU B 1 163 ? -8.677  -11.251 -11.645 1.00 25.21 ? 188 LEU B N   1 
ATOM   3267 C  CA  . LEU B 1 163 ? -7.578  -10.312 -11.833 1.00 26.53 ? 188 LEU B CA  1 
ATOM   3268 C  C   . LEU B 1 163 ? -6.555  -10.854 -12.837 1.00 26.76 ? 188 LEU B C   1 
ATOM   3269 O  O   . LEU B 1 163 ? -5.975  -10.074 -13.600 1.00 25.86 ? 188 LEU B O   1 
ATOM   3270 C  CB  . LEU B 1 163 ? -6.924  -9.903  -10.516 1.00 27.94 ? 188 LEU B CB  1 
ATOM   3271 C  CG  . LEU B 1 163 ? -7.852  -9.183  -9.530  1.00 28.65 ? 188 LEU B CG  1 
ATOM   3272 C  CD1 . LEU B 1 163 ? -7.102  -8.799  -8.276  1.00 31.37 ? 188 LEU B CD1 1 
ATOM   3273 C  CD2 . LEU B 1 163 ? -8.553  -7.956  -10.125 1.00 29.28 ? 188 LEU B CD2 1 
ATOM   3274 N  N   . VAL B 1 164 ? -6.305  -12.170 -12.813 1.00 25.04 ? 189 VAL B N   1 
ATOM   3275 C  CA  . VAL B 1 164 ? -5.396  -12.757 -13.790 1.00 24.69 ? 189 VAL B CA  1 
ATOM   3276 C  C   . VAL B 1 164 ? -5.957  -12.586 -15.205 1.00 25.06 ? 189 VAL B C   1 
ATOM   3277 O  O   . VAL B 1 164 ? -5.236  -12.152 -16.110 1.00 23.83 ? 189 VAL B O   1 
ATOM   3278 C  CB  . VAL B 1 164 ? -5.112  -14.231 -13.454 1.00 23.92 ? 189 VAL B CB  1 
ATOM   3279 C  CG1 . VAL B 1 164 ? -4.574  -15.005 -14.655 1.00 23.23 ? 189 VAL B CG1 1 
ATOM   3280 C  CG2 . VAL B 1 164 ? -4.160  -14.344 -12.264 1.00 24.92 ? 189 VAL B CG2 1 
ATOM   3281 N  N   . LEU B 1 165 ? -7.237  -12.938 -15.403 1.00 23.65 ? 190 LEU B N   1 
ATOM   3282 C  CA  . LEU B 1 165 ? -7.837  -12.849 -16.725 1.00 24.41 ? 190 LEU B CA  1 
ATOM   3283 C  C   . LEU B 1 165 ? -7.853  -11.390 -17.186 1.00 26.76 ? 190 LEU B C   1 
ATOM   3284 O  O   . LEU B 1 165 ? -7.631  -11.089 -18.372 1.00 25.53 ? 190 LEU B O   1 
ATOM   3285 C  CB  . LEU B 1 165 ? -9.240  -13.457 -16.721 1.00 23.97 ? 190 LEU B CB  1 
ATOM   3286 C  CG  . LEU B 1 165 ? -9.972  -13.505 -18.064 1.00 23.60 ? 190 LEU B CG  1 
ATOM   3287 C  CD1 . LEU B 1 165 ? -9.200  -14.357 -19.081 1.00 24.67 ? 190 LEU B CD1 1 
ATOM   3288 C  CD2 . LEU B 1 165 ? -11.385 -14.024 -17.929 1.00 24.27 ? 190 LEU B CD2 1 
ATOM   3289 N  N   . GLN B 1 166 ? -8.099  -10.484 -16.243 1.00 25.72 ? 191 GLN B N   1 
ATOM   3290 C  CA  . GLN B 1 166 ? -8.112  -9.079  -16.580 1.00 26.13 ? 191 GLN B CA  1 
ATOM   3291 C  C   . GLN B 1 166 ? -6.757  -8.638  -17.127 1.00 25.72 ? 191 GLN B C   1 
ATOM   3292 O  O   . GLN B 1 166 ? -6.696  -7.918  -18.118 1.00 24.92 ? 191 GLN B O   1 
ATOM   3293 C  CB  . GLN B 1 166 ? -8.476  -8.255  -15.348 1.00 27.66 ? 191 GLN B CB  1 
ATOM   3294 C  CG  . GLN B 1 166 ? -8.561  -6.765  -15.653 1.00 28.94 ? 191 GLN B CG  1 
ATOM   3295 C  CD  . GLN B 1 166 ? -8.971  -5.987  -14.435 1.00 32.40 ? 191 GLN B CD  1 
ATOM   3296 O  OE1 . GLN B 1 166 ? -8.182  -5.819  -13.510 1.00 35.42 ? 191 GLN B OE1 1 
ATOM   3297 N  NE2 . GLN B 1 166 ? -10.221 -5.573  -14.395 1.00 33.48 ? 191 GLN B NE2 1 
ATOM   3298 N  N   . GLN B 1 167 ? -5.670  -9.055  -16.473 1.00 25.31 ? 192 GLN B N   1 
ATOM   3299 C  CA  . GLN B 1 167 ? -4.352  -8.663  -16.935 1.00 27.09 ? 192 GLN B CA  1 
ATOM   3300 C  C   . GLN B 1 167 ? -4.028  -9.306  -18.283 1.00 26.27 ? 192 GLN B C   1 
ATOM   3301 O  O   . GLN B 1 167 ? -3.350  -8.695  -19.115 1.00 27.18 ? 192 GLN B O   1 
ATOM   3302 C  CB  . GLN B 1 167 ? -3.227  -9.064  -15.996 1.00 29.21 ? 192 GLN B CB  1 
ATOM   3303 C  CG  . GLN B 1 167 ? -3.263  -8.365  -14.642 1.00 32.47 ? 192 GLN B CG  1 
ATOM   3304 C  CD  . GLN B 1 167 ? -2.156  -8.864  -13.741 1.00 35.08 ? 192 GLN B CD  1 
ATOM   3305 O  OE1 . GLN B 1 167 ? -0.980  -8.518  -13.922 1.00 37.43 ? 192 GLN B OE1 1 
ATOM   3306 N  NE2 . GLN B 1 167 ? -2.521  -9.700  -12.778 1.00 35.27 ? 192 GLN B NE2 1 
ATOM   3307 N  N   . LEU B 1 168 ? -4.445  -10.556 -18.475 1.00 25.16 ? 193 LEU B N   1 
ATOM   3308 C  CA  . LEU B 1 168 ? -4.157  -11.276 -19.714 1.00 25.40 ? 193 LEU B CA  1 
ATOM   3309 C  C   . LEU B 1 168 ? -4.874  -10.648 -20.914 1.00 25.92 ? 193 LEU B C   1 
ATOM   3310 O  O   . LEU B 1 168 ? -4.275  -10.495 -21.983 1.00 25.71 ? 193 LEU B O   1 
ATOM   3311 C  CB  . LEU B 1 168 ? -4.569  -12.740 -19.577 1.00 24.19 ? 193 LEU B CB  1 
ATOM   3312 C  CG  . LEU B 1 168 ? -3.785  -13.572 -18.566 1.00 23.65 ? 193 LEU B CG  1 
ATOM   3313 C  CD1 . LEU B 1 168 ? -4.372  -14.969 -18.531 1.00 23.12 ? 193 LEU B CD1 1 
ATOM   3314 C  CD2 . LEU B 1 168 ? -2.292  -13.562 -18.884 1.00 23.21 ? 193 LEU B CD2 1 
ATOM   3315 N  N   . VAL B 1 169 ? -6.159  -10.324 -20.739 1.00 24.47 ? 194 VAL B N   1 
ATOM   3316 C  CA  . VAL B 1 169 ? -6.984  -9.899  -21.857 1.00 26.76 ? 194 VAL B CA  1 
ATOM   3317 C  C   . VAL B 1 169 ? -7.003  -8.376  -21.979 1.00 26.85 ? 194 VAL B C   1 
ATOM   3318 O  O   . VAL B 1 169 ? -6.953  -7.862  -23.083 1.00 28.58 ? 194 VAL B O   1 
ATOM   3319 C  CB  . VAL B 1 169 ? -8.400  -10.470 -21.696 1.00 27.50 ? 194 VAL B CB  1 
ATOM   3320 C  CG1 . VAL B 1 169 ? -9.343  -9.918  -22.748 1.00 27.72 ? 194 VAL B CG1 1 
ATOM   3321 C  CG2 . VAL B 1 169 ? -8.378  -11.991 -21.756 1.00 27.13 ? 194 VAL B CG2 1 
ATOM   3322 N  N   . LEU B 1 170 ? -7.076  -7.671  -20.849 1.00 27.62 ? 195 LEU B N   1 
ATOM   3323 C  CA  . LEU B 1 170 ? -7.254  -6.232  -20.835 1.00 28.79 ? 195 LEU B CA  1 
ATOM   3324 C  C   . LEU B 1 170 ? -5.969  -5.494  -20.464 1.00 29.54 ? 195 LEU B C   1 
ATOM   3325 O  O   . LEU B 1 170 ? -5.899  -4.279  -20.642 1.00 32.10 ? 195 LEU B O   1 
ATOM   3326 C  CB  . LEU B 1 170 ? -8.388  -5.911  -19.861 1.00 29.40 ? 195 LEU B CB  1 
ATOM   3327 C  CG  . LEU B 1 170 ? -9.777  -6.410  -20.279 1.00 30.03 ? 195 LEU B CG  1 
ATOM   3328 C  CD1 . LEU B 1 170 ? -10.849 -6.059  -19.257 1.00 30.17 ? 195 LEU B CD1 1 
ATOM   3329 C  CD2 . LEU B 1 170 ? -10.125 -5.876  -21.676 1.00 31.06 ? 195 LEU B CD2 1 
ATOM   3330 N  N   . GLY B 1 171 ? -4.965  -6.188  -19.935 1.00 27.86 ? 196 GLY B N   1 
ATOM   3331 C  CA  . GLY B 1 171 ? -3.755  -5.525  -19.463 1.00 29.32 ? 196 GLY B CA  1 
ATOM   3332 C  C   . GLY B 1 171 ? -2.536  -5.858  -20.316 1.00 29.92 ? 196 GLY B C   1 
ATOM   3333 O  O   . GLY B 1 171 ? -2.672  -6.283  -21.464 1.00 30.24 ? 196 GLY B O   1 
ATOM   3334 N  N   . ASN B 1 172 ? -1.341  -5.734  -19.711 1.00 31.21 ? 197 ASN B N   1 
ATOM   3335 C  CA  . ASN B 1 172 ? -0.084  -5.835  -20.427 1.00 31.34 ? 197 ASN B CA  1 
ATOM   3336 C  C   . ASN B 1 172 ? 0.745   -7.056  -20.030 1.00 30.94 ? 197 ASN B C   1 
ATOM   3337 O  O   . ASN B 1 172 ? 1.961   -7.040  -20.197 1.00 31.85 ? 197 ASN B O   1 
ATOM   3338 C  CB  . ASN B 1 172 ? 0.747   -4.585  -20.208 1.00 34.58 ? 197 ASN B CB  1 
ATOM   3339 C  CG  . ASN B 1 172 ? 1.208   -4.451  -18.774 1.00 35.52 ? 197 ASN B CG  1 
ATOM   3340 O  OD1 . ASN B 1 172 ? 0.721   -5.133  -17.863 1.00 34.17 ? 197 ASN B OD1 1 
ATOM   3341 N  ND2 . ASN B 1 172 ? 2.162   -3.567  -18.562 1.00 37.84 ? 197 ASN B ND2 1 
ATOM   3342 N  N   . ALA B 1 173 ? 0.115   -8.126  -19.547 1.00 29.77 ? 198 ALA B N   1 
ATOM   3343 C  CA  . ALA B 1 173 ? 0.836   -9.360  -19.263 1.00 29.03 ? 198 ALA B CA  1 
ATOM   3344 C  C   . ALA B 1 173 ? 1.498   -9.898  -20.537 1.00 29.82 ? 198 ALA B C   1 
ATOM   3345 O  O   . ALA B 1 173 ? 2.610   -10.433 -20.492 1.00 29.24 ? 198 ALA B O   1 
ATOM   3346 C  CB  . ALA B 1 173 ? -0.105  -10.383 -18.697 1.00 27.44 ? 198 ALA B CB  1 
ATOM   3347 N  N   . LEU B 1 174 ? 0.767   -9.803  -21.654 1.00 29.05 ? 199 LEU B N   1 
ATOM   3348 C  CA  . LEU B 1 174 ? 1.232   -10.319 -22.936 1.00 28.86 ? 199 LEU B CA  1 
ATOM   3349 C  C   . LEU B 1 174 ? 1.467   -9.158  -23.892 1.00 29.60 ? 199 LEU B C   1 
ATOM   3350 O  O   . LEU B 1 174 ? 0.697   -8.188  -23.899 1.00 29.12 ? 199 LEU B O   1 
ATOM   3351 C  CB  . LEU B 1 174 ? 0.193   -11.264 -23.514 1.00 27.75 ? 199 LEU B CB  1 
ATOM   3352 C  CG  . LEU B 1 174 ? -0.033  -12.562 -22.738 1.00 27.99 ? 199 LEU B CG  1 
ATOM   3353 C  CD1 . LEU B 1 174 ? -1.275  -13.268 -23.292 1.00 26.87 ? 199 LEU B CD1 1 
ATOM   3354 C  CD2 . LEU B 1 174 ? 1.227   -13.431 -22.868 1.00 27.96 ? 199 LEU B CD2 1 
ATOM   3355 N  N   . PRO B 1 175 ? 2.497   -9.263  -24.763 1.00 30.15 ? 200 PRO B N   1 
ATOM   3356 C  CA  . PRO B 1 175 ? 2.625   -8.358  -25.911 1.00 31.19 ? 200 PRO B CA  1 
ATOM   3357 C  C   . PRO B 1 175 ? 1.355   -8.452  -26.752 1.00 31.29 ? 200 PRO B C   1 
ATOM   3358 O  O   . PRO B 1 175 ? 0.704   -9.502  -26.784 1.00 31.32 ? 200 PRO B O   1 
ATOM   3359 C  CB  . PRO B 1 175 ? 3.861   -8.801  -26.686 1.00 31.64 ? 200 PRO B CB  1 
ATOM   3360 C  CG  . PRO B 1 175 ? 4.539   -9.825  -25.802 1.00 31.61 ? 200 PRO B CG  1 
ATOM   3361 C  CD  . PRO B 1 175 ? 3.575   -10.262 -24.706 1.00 29.87 ? 200 PRO B CD  1 
ATOM   3362 N  N   . PRO B 1 176 ? 0.946   -7.366  -27.439 1.00 31.59 ? 201 PRO B N   1 
ATOM   3363 C  CA  . PRO B 1 176 ? -0.366  -7.312  -28.096 1.00 32.50 ? 201 PRO B CA  1 
ATOM   3364 C  C   . PRO B 1 176 ? -0.673  -8.457  -29.065 1.00 33.17 ? 201 PRO B C   1 
ATOM   3365 O  O   . PRO B 1 176 ? -1.827  -8.865  -29.201 1.00 32.78 ? 201 PRO B O   1 
ATOM   3366 C  CB  . PRO B 1 176 ? -0.331  -5.961  -28.849 1.00 33.71 ? 201 PRO B CB  1 
ATOM   3367 C  CG  . PRO B 1 176 ? 0.756   -5.158  -28.179 1.00 34.77 ? 201 PRO B CG  1 
ATOM   3368 C  CD  . PRO B 1 176 ? 1.748   -6.143  -27.607 1.00 33.62 ? 201 PRO B CD  1 
ATOM   3369 N  N   . ASP B 1 177 ? 0.360   -8.933  -29.776 1.00 35.12 ? 202 ASP B N   1 
ATOM   3370 C  CA  . ASP B 1 177 ? 0.185   -9.975  -30.778 1.00 36.09 ? 202 ASP B CA  1 
ATOM   3371 C  C   . ASP B 1 177 ? -0.212  -11.279 -30.077 1.00 32.02 ? 202 ASP B C   1 
ATOM   3372 O  O   . ASP B 1 177 ? -1.098  -11.995 -30.537 1.00 33.30 ? 202 ASP B O   1 
ATOM   3373 C  CB  . ASP B 1 177 ? 1.383   -10.079 -31.716 1.00 39.57 ? 202 ASP B CB  1 
ATOM   3374 C  CG  . ASP B 1 177 ? 2.778   -10.211 -31.106 1.00 43.68 ? 202 ASP B CG  1 
ATOM   3375 O  OD1 . ASP B 1 177 ? 2.908   -10.252 -29.868 1.00 41.41 ? 202 ASP B OD1 1 
ATOM   3376 O  OD2 . ASP B 1 177 ? 3.755   -10.265 -31.888 1.00 50.52 ? 202 ASP B OD2 1 
ATOM   3377 N  N   . LYS B 1 178 ? 0.448   -11.584 -28.963 1.00 30.91 ? 203 LYS B N   1 
ATOM   3378 C  CA  . LYS B 1 178 ? 0.121   -12.773 -28.181 1.00 29.07 ? 203 LYS B CA  1 
ATOM   3379 C  C   . LYS B 1 178 ? -1.217  -12.587 -27.464 1.00 27.40 ? 203 LYS B C   1 
ATOM   3380 O  O   . LYS B 1 178 ? -2.022  -13.509 -27.406 1.00 26.12 ? 203 LYS B O   1 
ATOM   3381 C  CB  . LYS B 1 178 ? 1.275   -13.124 -27.239 1.00 29.03 ? 203 LYS B CB  1 
ATOM   3382 C  CG  . LYS B 1 178 ? 2.573   -13.487 -27.948 1.00 29.34 ? 203 LYS B CG  1 
ATOM   3383 C  CD  . LYS B 1 178 ? 3.743   -13.736 -27.011 1.00 29.48 ? 203 LYS B CD  1 
ATOM   3384 C  CE  . LYS B 1 178 ? 5.029   -13.957 -27.727 1.00 30.43 ? 203 LYS B CE  1 
ATOM   3385 N  NZ  . LYS B 1 178 ? 6.136   -14.274 -26.821 1.00 31.06 ? 203 LYS B NZ  1 
ATOM   3386 N  N   . ARG B 1 179 ? -1.482  -11.380 -26.952 1.00 26.59 ? 204 ARG B N   1 
ATOM   3387 C  CA  . ARG B 1 179 ? -2.748  -11.100 -26.291 1.00 27.17 ? 204 ARG B CA  1 
ATOM   3388 C  C   . ARG B 1 179 ? -3.943  -11.373 -27.205 1.00 27.14 ? 204 ARG B C   1 
ATOM   3389 O  O   . ARG B 1 179 ? -4.977  -11.901 -26.781 1.00 26.89 ? 204 ARG B O   1 
ATOM   3390 C  CB  . ARG B 1 179 ? -2.785  -9.637  -25.821 1.00 28.28 ? 204 ARG B CB  1 
ATOM   3391 C  CG  . ARG B 1 179 ? -3.984  -9.356  -24.930 1.00 28.01 ? 204 ARG B CG  1 
ATOM   3392 C  CD  . ARG B 1 179 ? -3.841  -7.951  -24.372 1.00 29.19 ? 204 ARG B CD  1 
ATOM   3393 N  NE  . ARG B 1 179 ? -4.328  -6.918  -25.282 1.00 29.71 ? 204 ARG B NE  1 
ATOM   3394 C  CZ  . ARG B 1 179 ? -4.607  -5.667  -24.906 1.00 30.94 ? 204 ARG B CZ  1 
ATOM   3395 N  NH1 . ARG B 1 179 ? -4.344  -5.242  -23.679 1.00 31.92 ? 204 ARG B NH1 1 
ATOM   3396 N  NH2 . ARG B 1 179 ? -5.163  -4.829  -25.756 1.00 30.98 ? 204 ARG B NH2 1 
ATOM   3397 N  N   . ALA B 1 180 ? -3.800  -11.011 -28.479 1.00 28.13 ? 205 ALA B N   1 
ATOM   3398 C  CA  . ALA B 1 180 ? -4.869  -11.179 -29.442 1.00 27.41 ? 205 ALA B CA  1 
ATOM   3399 C  C   . ALA B 1 180 ? -5.126  -12.659 -29.727 1.00 26.80 ? 205 ALA B C   1 
ATOM   3400 O  O   . ALA B 1 180 ? -6.273  -13.057 -29.926 1.00 28.20 ? 205 ALA B O   1 
ATOM   3401 C  CB  . ALA B 1 180 ? -4.505  -10.416 -30.701 1.00 29.99 ? 205 ALA B CB  1 
ATOM   3402 N  N   . LEU B 1 181 ? -4.075  -13.487 -29.749 1.00 26.02 ? 206 LEU B N   1 
ATOM   3403 C  CA  . LEU B 1 181 ? -4.269  -14.914 -29.970 1.00 25.97 ? 206 LEU B CA  1 
ATOM   3404 C  C   . LEU B 1 181 ? -5.110  -15.512 -28.848 1.00 25.81 ? 206 LEU B C   1 
ATOM   3405 O  O   . LEU B 1 181 ? -6.051  -16.264 -29.098 1.00 25.01 ? 206 LEU B O   1 
ATOM   3406 C  CB  . LEU B 1 181 ? -2.945  -15.656 -30.072 1.00 26.46 ? 206 LEU B CB  1 
ATOM   3407 C  CG  . LEU B 1 181 ? -2.113  -15.369 -31.323 1.00 27.90 ? 206 LEU B CG  1 
ATOM   3408 C  CD1 . LEU B 1 181 ? -0.727  -15.946 -31.193 1.00 27.26 ? 206 LEU B CD1 1 
ATOM   3409 C  CD2 . LEU B 1 181 ? -2.829  -15.955 -32.524 1.00 28.91 ? 206 LEU B CD2 1 
ATOM   3410 N  N   . LEU B 1 182 ? -4.743  -15.196 -27.602 1.00 26.67 ? 207 LEU B N   1 
ATOM   3411 C  CA  . LEU B 1 182 ? -5.468  -15.713 -26.450 1.00 25.93 ? 207 LEU B CA  1 
ATOM   3412 C  C   . LEU B 1 182 ? -6.937  -15.301 -26.552 1.00 25.56 ? 207 LEU B C   1 
ATOM   3413 O  O   . LEU B 1 182 ? -7.846  -16.122 -26.380 1.00 23.77 ? 207 LEU B O   1 
ATOM   3414 C  CB  . LEU B 1 182 ? -4.854  -15.197 -25.149 1.00 26.76 ? 207 LEU B CB  1 
ATOM   3415 C  CG  . LEU B 1 182 ? -5.631  -15.566 -23.882 1.00 27.61 ? 207 LEU B CG  1 
ATOM   3416 C  CD1 . LEU B 1 182 ? -5.526  -17.091 -23.676 1.00 28.48 ? 207 LEU B CD1 1 
ATOM   3417 C  CD2 . LEU B 1 182 ? -5.155  -14.792 -22.668 1.00 28.55 ? 207 LEU B CD2 1 
ATOM   3418 N  N   . THR B 1 183 ? -7.146  -13.996 -26.783 1.00 25.20 ? 208 THR B N   1 
ATOM   3419 C  CA  . THR B 1 183 ? -8.477  -13.417 -26.871 1.00 25.66 ? 208 THR B CA  1 
ATOM   3420 C  C   . THR B 1 183 ? -9.315  -14.106 -27.954 1.00 25.72 ? 208 THR B C   1 
ATOM   3421 O  O   . THR B 1 183 ? -10.480 -14.416 -27.738 1.00 26.25 ? 208 THR B O   1 
ATOM   3422 C  CB  . THR B 1 183 ? -8.343  -11.924 -27.176 1.00 27.40 ? 208 THR B CB  1 
ATOM   3423 O  OG1 . THR B 1 183 ? -7.636  -11.284 -26.119 1.00 27.29 ? 208 THR B OG1 1 
ATOM   3424 C  CG2 . THR B 1 183 ? -9.704  -11.282 -27.352 1.00 27.95 ? 208 THR B CG2 1 
ATOM   3425 N  N   A ASP B 1 184 ? -8.706  -14.300 -29.132 0.50 25.40 ? 209 ASP B N   1 
ATOM   3426 N  N   B ASP B 1 184 ? -8.722  -14.331 -29.130 0.50 25.97 ? 209 ASP B N   1 
ATOM   3427 C  CA  A ASP B 1 184 ? -9.360  -14.922 -30.275 0.50 25.39 ? 209 ASP B CA  1 
ATOM   3428 C  CA  B ASP B 1 184 ? -9.460  -14.910 -30.241 0.50 26.36 ? 209 ASP B CA  1 
ATOM   3429 C  C   A ASP B 1 184 ? -9.791  -16.361 -29.967 0.50 25.66 ? 209 ASP B C   1 
ATOM   3430 C  C   B ASP B 1 184 ? -9.808  -16.376 -29.972 0.50 26.20 ? 209 ASP B C   1 
ATOM   3431 O  O   A ASP B 1 184 ? -10.904 -16.775 -30.300 0.50 25.87 ? 209 ASP B O   1 
ATOM   3432 O  O   B ASP B 1 184 ? -10.902 -16.815 -30.320 0.50 26.31 ? 209 ASP B O   1 
ATOM   3433 C  CB  A ASP B 1 184 ? -8.452  -14.886 -31.495 0.50 25.71 ? 209 ASP B CB  1 
ATOM   3434 C  CB  B ASP B 1 184 ? -8.729  -14.648 -31.546 0.50 27.57 ? 209 ASP B CB  1 
ATOM   3435 C  CG  A ASP B 1 184 ? -8.982  -15.673 -32.688 0.50 24.98 ? 209 ASP B CG  1 
ATOM   3436 C  CG  B ASP B 1 184 ? -8.811  -13.205 -32.012 0.50 28.29 ? 209 ASP B CG  1 
ATOM   3437 O  OD1 A ASP B 1 184 ? -9.951  -15.185 -33.294 0.50 24.57 ? 209 ASP B OD1 1 
ATOM   3438 O  OD1 B ASP B 1 184 ? -9.752  -12.508 -31.562 0.50 27.30 ? 209 ASP B OD1 1 
ATOM   3439 O  OD2 A ASP B 1 184 ? -8.469  -16.798 -32.943 0.50 23.57 ? 209 ASP B OD2 1 
ATOM   3440 O  OD2 B ASP B 1 184 ? -7.925  -12.794 -32.795 0.50 28.98 ? 209 ASP B OD2 1 
ATOM   3441 N  N   . TRP B 1 185 ? -8.893  -17.133 -29.347 1.00 25.19 ? 210 TRP B N   1 
ATOM   3442 C  CA  . TRP B 1 185 ? -9.202  -18.512 -28.991 1.00 25.50 ? 210 TRP B CA  1 
ATOM   3443 C  C   . TRP B 1 185 ? -10.401 -18.547 -28.027 1.00 24.03 ? 210 TRP B C   1 
ATOM   3444 O  O   . TRP B 1 185 ? -11.313 -19.357 -28.188 1.00 23.47 ? 210 TRP B O   1 
ATOM   3445 C  CB  . TRP B 1 185 ? -7.974  -19.248 -28.421 1.00 23.87 ? 210 TRP B CB  1 
ATOM   3446 C  CG  . TRP B 1 185 ? -6.966  -19.667 -29.470 1.00 23.86 ? 210 TRP B CG  1 
ATOM   3447 C  CD1 . TRP B 1 185 ? -7.214  -20.158 -30.722 1.00 24.56 ? 210 TRP B CD1 1 
ATOM   3448 C  CD2 . TRP B 1 185 ? -5.534  -19.626 -29.342 1.00 22.95 ? 210 TRP B CD2 1 
ATOM   3449 N  NE1 . TRP B 1 185 ? -6.044  -20.438 -31.377 1.00 23.90 ? 210 TRP B NE1 1 
ATOM   3450 C  CE2 . TRP B 1 185 ? -4.996  -20.117 -30.556 1.00 23.55 ? 210 TRP B CE2 1 
ATOM   3451 C  CE3 . TRP B 1 185 ? -4.659  -19.227 -28.326 1.00 22.25 ? 210 TRP B CE3 1 
ATOM   3452 C  CZ2 . TRP B 1 185 ? -3.625  -20.210 -30.768 1.00 24.10 ? 210 TRP B CZ2 1 
ATOM   3453 C  CZ3 . TRP B 1 185 ? -3.301  -19.316 -28.542 1.00 22.54 ? 210 TRP B CZ3 1 
ATOM   3454 C  CH2 . TRP B 1 185 ? -2.795  -19.814 -29.744 1.00 23.49 ? 210 TRP B CH2 1 
ATOM   3455 N  N   . MET B 1 186 ? -10.428 -17.623 -27.067 1.00 24.32 ? 211 MET B N   1 
ATOM   3456 C  CA  . MET B 1 186 ? -11.524 -17.560 -26.120 1.00 25.54 ? 211 MET B CA  1 
ATOM   3457 C  C   . MET B 1 186 ? -12.807 -17.118 -26.831 1.00 26.55 ? 211 MET B C   1 
ATOM   3458 O  O   . MET B 1 186 ? -13.887 -17.637 -26.524 1.00 26.46 ? 211 MET B O   1 
ATOM   3459 C  CB  . MET B 1 186 ? -11.170 -16.654 -24.939 1.00 26.14 ? 211 MET B CB  1 
ATOM   3460 C  CG  . MET B 1 186 ? -10.064 -17.212 -24.049 1.00 24.63 ? 211 MET B CG  1 
ATOM   3461 S  SD  . MET B 1 186 ? -9.692  -16.201 -22.593 1.00 24.22 ? 211 MET B SD  1 
ATOM   3462 C  CE  . MET B 1 186 ? -11.276 -16.437 -21.752 1.00 23.39 ? 211 MET B CE  1 
ATOM   3463 N  N   . ALA B 1 187 ? -12.680 -16.223 -27.820 1.00 26.92 ? 212 ALA B N   1 
ATOM   3464 C  CA  . ALA B 1 187 ? -13.828 -15.741 -28.572 1.00 27.93 ? 212 ALA B CA  1 
ATOM   3465 C  C   . ALA B 1 187 ? -14.486 -16.876 -29.337 1.00 28.57 ? 212 ALA B C   1 
ATOM   3466 O  O   . ALA B 1 187 ? -15.700 -16.868 -29.546 1.00 31.36 ? 212 ALA B O   1 
ATOM   3467 C  CB  . ALA B 1 187 ? -13.413 -14.613 -29.509 1.00 29.02 ? 212 ALA B CB  1 
ATOM   3468 N  N   . ARG B 1 188 ? -13.697 -17.872 -29.751 1.00 29.20 ? 213 ARG B N   1 
ATOM   3469 C  CA  . ARG B 1 188 ? -14.193 -18.960 -30.585 1.00 28.54 ? 213 ARG B CA  1 
ATOM   3470 C  C   . ARG B 1 188 ? -14.469 -20.210 -29.770 1.00 28.55 ? 213 ARG B C   1 
ATOM   3471 O  O   . ARG B 1 188 ? -14.622 -21.289 -30.325 1.00 28.44 ? 213 ARG B O   1 
ATOM   3472 C  CB  . ARG B 1 188 ? -13.158 -19.253 -31.677 1.00 30.17 ? 213 ARG B CB  1 
ATOM   3473 C  CG  . ARG B 1 188 ? -13.046 -18.099 -32.657 1.00 31.75 ? 213 ARG B CG  1 
ATOM   3474 C  CD  . ARG B 1 188 ? -11.787 -18.141 -33.500 1.00 33.41 ? 213 ARG B CD  1 
ATOM   3475 N  NE  . ARG B 1 188 ? -11.550 -19.454 -34.120 1.00 36.25 ? 213 ARG B NE  1 
ATOM   3476 C  CZ  . ARG B 1 188 ? -10.372 -20.059 -34.133 1.00 41.27 ? 213 ARG B CZ  1 
ATOM   3477 N  NH1 . ARG B 1 188 ? -9.283  -19.409 -33.766 1.00 42.82 ? 213 ARG B NH1 1 
ATOM   3478 N  NH2 . ARG B 1 188 ? -10.279 -21.316 -34.508 1.00 46.16 ? 213 ARG B NH2 1 
ATOM   3479 N  N   . ASN B 1 189 ? -14.587 -20.068 -28.442 1.00 28.31 ? 214 ASN B N   1 
ATOM   3480 C  CA  . ASN B 1 189 ? -14.780 -21.213 -27.579 1.00 28.05 ? 214 ASN B CA  1 
ATOM   3481 C  C   . ASN B 1 189 ? -16.068 -21.958 -27.957 1.00 28.35 ? 214 ASN B C   1 
ATOM   3482 O  O   . ASN B 1 189 ? -17.076 -21.315 -28.229 1.00 27.34 ? 214 ASN B O   1 
ATOM   3483 C  CB  . ASN B 1 189 ? -14.761 -20.734 -26.130 1.00 28.31 ? 214 ASN B CB  1 
ATOM   3484 C  CG  . ASN B 1 189 ? -15.012 -21.883 -25.187 1.00 29.20 ? 214 ASN B CG  1 
ATOM   3485 O  OD1 . ASN B 1 189 ? -14.615 -23.017 -25.486 1.00 28.16 ? 214 ASN B OD1 1 
ATOM   3486 N  ND2 . ASN B 1 189 ? -15.728 -21.636 -24.096 1.00 28.95 ? 214 ASN B ND2 1 
ATOM   3487 N  N   . THR B 1 190 ? -16.056 -23.306 -27.913 1.00 27.20 ? 215 THR B N   1 
ATOM   3488 C  CA  . THR B 1 190 ? -17.240 -24.099 -28.229 1.00 28.99 ? 215 THR B CA  1 
ATOM   3489 C  C   . THR B 1 190 ? -18.034 -24.556 -26.997 1.00 28.28 ? 215 THR B C   1 
ATOM   3490 O  O   . THR B 1 190 ? -19.115 -25.128 -27.176 1.00 30.26 ? 215 THR B O   1 
ATOM   3491 C  CB  . THR B 1 190 ? -16.866 -25.315 -29.081 1.00 29.37 ? 215 THR B CB  1 
ATOM   3492 O  OG1 . THR B 1 190 ? -16.311 -26.324 -28.246 1.00 28.12 ? 215 THR B OG1 1 
ATOM   3493 C  CG2 . THR B 1 190 ? -15.910 -24.967 -30.209 1.00 29.40 ? 215 THR B CG2 1 
ATOM   3494 N  N   . THR B 1 191 ? -17.542 -24.345 -25.764 1.00 27.13 ? 216 THR B N   1 
ATOM   3495 C  CA  . THR B 1 191 ? -18.124 -25.047 -24.630 1.00 25.97 ? 216 THR B CA  1 
ATOM   3496 C  C   . THR B 1 191 ? -18.966 -24.143 -23.715 1.00 24.33 ? 216 THR B C   1 
ATOM   3497 O  O   . THR B 1 191 ? -19.515 -24.648 -22.741 1.00 23.39 ? 216 THR B O   1 
ATOM   3498 C  CB  . THR B 1 191 ? -17.030 -25.747 -23.804 1.00 26.28 ? 216 THR B CB  1 
ATOM   3499 O  OG1 . THR B 1 191 ? -16.316 -24.737 -23.103 1.00 26.06 ? 216 THR B OG1 1 
ATOM   3500 C  CG2 . THR B 1 191 ? -16.067 -26.601 -24.616 1.00 26.99 ? 216 THR B CG2 1 
ATOM   3501 N  N   . GLY B 1 192 ? -19.050 -22.832 -23.983 1.00 22.71 ? 217 GLY B N   1 
ATOM   3502 C  CA  . GLY B 1 192 ? -19.438 -21.873 -22.968 1.00 21.87 ? 217 GLY B CA  1 
ATOM   3503 C  C   . GLY B 1 192 ? -20.833 -21.289 -23.196 1.00 23.58 ? 217 GLY B C   1 
ATOM   3504 O  O   . GLY B 1 192 ? -21.221 -20.386 -22.465 1.00 25.92 ? 217 GLY B O   1 
ATOM   3505 N  N   . ALA B 1 193 ? -21.584 -21.805 -24.181 1.00 23.22 ? 218 ALA B N   1 
ATOM   3506 C  CA  . ALA B 1 193 ? -22.791 -21.129 -24.642 1.00 24.46 ? 218 ALA B CA  1 
ATOM   3507 C  C   . ALA B 1 193 ? -23.858 -21.041 -23.546 1.00 25.43 ? 218 ALA B C   1 
ATOM   3508 O  O   . ALA B 1 193 ? -24.680 -20.128 -23.567 1.00 25.58 ? 218 ALA B O   1 
ATOM   3509 C  CB  . ALA B 1 193 ? -23.345 -21.824 -25.870 1.00 24.99 ? 218 ALA B CB  1 
ATOM   3510 N  N   . LYS B 1 194 ? -23.869 -21.985 -22.585 1.00 25.64 ? 219 LYS B N   1 
ATOM   3511 C  CA  . LYS B 1 194 ? -24.955 -22.080 -21.610 1.00 25.89 ? 219 LYS B CA  1 
ATOM   3512 C  C   . LYS B 1 194 ? -24.538 -21.523 -20.249 1.00 24.60 ? 219 LYS B C   1 
ATOM   3513 O  O   . LYS B 1 194 ? -25.261 -21.727 -19.271 1.00 23.08 ? 219 LYS B O   1 
ATOM   3514 C  CB  . LYS B 1 194 ? -25.391 -23.535 -21.404 1.00 28.70 ? 219 LYS B CB  1 
ATOM   3515 C  CG  . LYS B 1 194 ? -25.851 -24.277 -22.650 1.00 33.61 ? 219 LYS B CG  1 
ATOM   3516 C  CD  . LYS B 1 194 ? -26.877 -23.535 -23.501 1.00 39.04 ? 219 LYS B CD  1 
ATOM   3517 C  CE  . LYS B 1 194 ? -28.237 -23.395 -22.866 1.00 45.51 ? 219 LYS B CE  1 
ATOM   3518 N  NZ  . LYS B 1 194 ? -29.154 -24.455 -23.310 1.00 47.50 ? 219 LYS B NZ  1 
ATOM   3519 N  N   . ARG B 1 195 ? -23.384 -20.836 -20.190 1.00 22.25 ? 220 ARG B N   1 
ATOM   3520 C  CA  . ARG B 1 195 ? -22.858 -20.300 -18.939 1.00 21.91 ? 220 ARG B CA  1 
ATOM   3521 C  C   . ARG B 1 195 ? -22.969 -18.775 -18.970 1.00 20.76 ? 220 ARG B C   1 
ATOM   3522 O  O   . ARG B 1 195 ? -24.064 -18.253 -19.095 1.00 21.45 ? 220 ARG B O   1 
ATOM   3523 C  CB  . ARG B 1 195 ? -21.482 -20.914 -18.636 1.00 21.40 ? 220 ARG B CB  1 
ATOM   3524 C  CG  . ARG B 1 195 ? -21.601 -22.426 -18.462 1.00 22.64 ? 220 ARG B CG  1 
ATOM   3525 C  CD  . ARG B 1 195 ? -20.295 -23.143 -18.183 1.00 22.08 ? 220 ARG B CD  1 
ATOM   3526 N  NE  . ARG B 1 195 ? -20.487 -24.596 -18.230 1.00 22.83 ? 220 ARG B NE  1 
ATOM   3527 C  CZ  . ARG B 1 195 ? -19.722 -25.491 -17.612 1.00 23.66 ? 220 ARG B CZ  1 
ATOM   3528 N  NH1 . ARG B 1 195 ? -18.696 -25.112 -16.860 1.00 22.88 ? 220 ARG B NH1 1 
ATOM   3529 N  NH2 . ARG B 1 195 ? -19.998 -26.778 -17.754 1.00 25.55 ? 220 ARG B NH2 1 
ATOM   3530 N  N   . ILE B 1 196 ? -21.863 -18.061 -18.802 1.00 20.38 ? 221 ILE B N   1 
ATOM   3531 C  CA  . ILE B 1 196 ? -21.913 -16.608 -18.688 1.00 21.07 ? 221 ILE B CA  1 
ATOM   3532 C  C   . ILE B 1 196 ? -22.594 -16.005 -19.919 1.00 21.45 ? 221 ILE B C   1 
ATOM   3533 O  O   . ILE B 1 196 ? -23.451 -15.122 -19.788 1.00 21.05 ? 221 ILE B O   1 
ATOM   3534 C  CB  . ILE B 1 196 ? -20.521 -16.010 -18.434 1.00 21.56 ? 221 ILE B CB  1 
ATOM   3535 C  CG1 . ILE B 1 196 ? -20.013 -16.373 -17.039 1.00 21.74 ? 221 ILE B CG1 1 
ATOM   3536 C  CG2 . ILE B 1 196 ? -20.555 -14.486 -18.629 1.00 22.63 ? 221 ILE B CG2 1 
ATOM   3537 C  CD1 . ILE B 1 196 ? -18.538 -16.109 -16.803 1.00 20.40 ? 221 ILE B CD1 1 
ATOM   3538 N  N   . ARG B 1 197 ? -22.291 -16.558 -21.104 1.00 22.57 ? 222 ARG B N   1 
ATOM   3539 C  CA  . ARG B 1 197 ? -22.888 -16.123 -22.358 1.00 22.95 ? 222 ARG B CA  1 
ATOM   3540 C  C   . ARG B 1 197 ? -24.413 -16.113 -22.249 1.00 24.51 ? 222 ARG B C   1 
ATOM   3541 O  O   . ARG B 1 197 ? -25.061 -15.228 -22.828 1.00 25.52 ? 222 ARG B O   1 
ATOM   3542 C  CB  . ARG B 1 197 ? -22.452 -17.061 -23.493 1.00 22.71 ? 222 ARG B CB  1 
ATOM   3543 C  CG  . ARG B 1 197 ? -23.172 -16.912 -24.831 1.00 22.99 ? 222 ARG B CG  1 
ATOM   3544 C  CD  . ARG B 1 197 ? -22.861 -15.602 -25.572 1.00 23.20 ? 222 ARG B CD  1 
ATOM   3545 N  NE  . ARG B 1 197 ? -23.568 -14.429 -25.052 1.00 23.15 ? 222 ARG B NE  1 
ATOM   3546 C  CZ  . ARG B 1 197 ? -23.389 -13.173 -25.456 1.00 24.25 ? 222 ARG B CZ  1 
ATOM   3547 N  NH1 . ARG B 1 197 ? -22.524 -12.918 -26.416 1.00 25.09 ? 222 ARG B NH1 1 
ATOM   3548 N  NH2 . ARG B 1 197 ? -24.084 -12.177 -24.938 1.00 24.43 ? 222 ARG B NH2 1 
ATOM   3549 N  N   . ALA B 1 198 ? -24.990 -17.113 -21.543 1.00 23.62 ? 223 ALA B N   1 
ATOM   3550 C  CA  . ALA B 1 198 ? -26.441 -17.247 -21.443 1.00 25.37 ? 223 ALA B CA  1 
ATOM   3551 C  C   . ALA B 1 198 ? -27.070 -16.206 -20.514 1.00 26.76 ? 223 ALA B C   1 
ATOM   3552 O  O   . ALA B 1 198 ? -28.299 -16.102 -20.456 1.00 29.76 ? 223 ALA B O   1 
ATOM   3553 C  CB  . ALA B 1 198 ? -26.821 -18.650 -20.981 1.00 25.37 ? 223 ALA B CB  1 
ATOM   3554 N  N   . GLY B 1 199 ? -26.268 -15.472 -19.733 1.00 25.72 ? 224 GLY B N   1 
ATOM   3555 C  CA  . GLY B 1 199 ? -26.833 -14.433 -18.874 1.00 25.85 ? 224 GLY B CA  1 
ATOM   3556 C  C   . GLY B 1 199 ? -26.738 -13.013 -19.435 1.00 26.71 ? 224 GLY B C   1 
ATOM   3557 O  O   . GLY B 1 199 ? -27.253 -12.083 -18.808 1.00 28.24 ? 224 GLY B O   1 
ATOM   3558 N  N   . PHE B 1 200 ? -26.071 -12.839 -20.586 1.00 26.64 ? 225 PHE B N   1 
ATOM   3559 C  CA  . PHE B 1 200 ? -25.826 -11.517 -21.146 1.00 25.81 ? 225 PHE B CA  1 
ATOM   3560 C  C   . PHE B 1 200 ? -26.574 -11.329 -22.453 1.00 26.60 ? 225 PHE B C   1 
ATOM   3561 O  O   . PHE B 1 200 ? -26.535 -12.214 -23.291 1.00 26.92 ? 225 PHE B O   1 
ATOM   3562 C  CB  . PHE B 1 200 ? -24.336 -11.291 -21.412 1.00 25.28 ? 225 PHE B CB  1 
ATOM   3563 C  CG  . PHE B 1 200 ? -23.648 -10.799 -20.151 1.00 25.21 ? 225 PHE B CG  1 
ATOM   3564 C  CD1 . PHE B 1 200 ? -23.145 -11.706 -19.232 1.00 24.20 ? 225 PHE B CD1 1 
ATOM   3565 C  CD2 . PHE B 1 200 ? -23.563 -9.438  -19.878 1.00 25.71 ? 225 PHE B CD2 1 
ATOM   3566 C  CE1 . PHE B 1 200 ? -22.557 -11.258 -18.061 1.00 24.17 ? 225 PHE B CE1 1 
ATOM   3567 C  CE2 . PHE B 1 200 ? -22.942 -8.997  -18.720 1.00 24.83 ? 225 PHE B CE2 1 
ATOM   3568 C  CZ  . PHE B 1 200 ? -22.432 -9.903  -17.823 1.00 24.66 ? 225 PHE B CZ  1 
ATOM   3569 N  N   . PRO B 1 201 ? -27.189 -10.151 -22.709 1.00 27.91 ? 226 PRO B N   1 
ATOM   3570 C  CA  . PRO B 1 201 ? -27.902 -9.915  -23.965 1.00 29.54 ? 226 PRO B CA  1 
ATOM   3571 C  C   . PRO B 1 201 ? -27.002 -10.046 -25.184 1.00 29.88 ? 226 PRO B C   1 
ATOM   3572 O  O   . PRO B 1 201 ? -25.779 -9.961  -25.082 1.00 29.10 ? 226 PRO B O   1 
ATOM   3573 C  CB  . PRO B 1 201 ? -28.483 -8.482  -23.802 1.00 30.61 ? 226 PRO B CB  1 
ATOM   3574 C  CG  . PRO B 1 201 ? -28.509 -8.252  -22.316 1.00 29.85 ? 226 PRO B CG  1 
ATOM   3575 C  CD  . PRO B 1 201 ? -27.308 -9.004  -21.792 1.00 28.24 ? 226 PRO B CD  1 
ATOM   3576 N  N   . ALA B 1 202 ? -27.653 -10.250 -26.335 1.00 31.05 ? 227 ALA B N   1 
ATOM   3577 C  CA  . ALA B 1 202 ? -26.982 -10.580 -27.583 1.00 31.87 ? 227 ALA B CA  1 
ATOM   3578 C  C   . ALA B 1 202 ? -26.058 -9.451  -28.042 1.00 33.14 ? 227 ALA B C   1 
ATOM   3579 O  O   . ALA B 1 202 ? -25.058 -9.707  -28.702 1.00 33.65 ? 227 ALA B O   1 
ATOM   3580 C  CB  . ALA B 1 202 ? -28.015 -10.912 -28.638 1.00 32.47 ? 227 ALA B CB  1 
ATOM   3581 N  N   . ASP B 1 203 ? -26.355 -8.204  -27.661 1.00 33.68 ? 228 ASP B N   1 
ATOM   3582 C  CA  . ASP B 1 203 ? -25.504 -7.103  -28.075 1.00 35.26 ? 228 ASP B CA  1 
ATOM   3583 C  C   . ASP B 1 203 ? -24.299 -6.906  -27.151 1.00 34.03 ? 228 ASP B C   1 
ATOM   3584 O  O   . ASP B 1 203 ? -23.595 -5.911  -27.312 1.00 33.65 ? 228 ASP B O   1 
ATOM   3585 C  CB  . ASP B 1 203 ? -26.295 -5.819  -28.249 1.00 36.82 ? 228 ASP B CB  1 
ATOM   3586 C  CG  . ASP B 1 203 ? -27.087 -5.362  -27.040 1.00 37.21 ? 228 ASP B CG  1 
ATOM   3587 O  OD1 . ASP B 1 203 ? -27.110 -6.089  -26.024 1.00 35.08 ? 228 ASP B OD1 1 
ATOM   3588 O  OD2 . ASP B 1 203 ? -27.647 -4.253  -27.123 1.00 39.57 ? 228 ASP B OD2 1 
ATOM   3589 N  N   . TRP B 1 204 ? -24.092 -7.813  -26.183 1.00 32.67 ? 229 TRP B N   1 
ATOM   3590 C  CA  . TRP B 1 204 ? -22.851 -7.886  -25.415 1.00 31.17 ? 229 TRP B CA  1 
ATOM   3591 C  C   . TRP B 1 204 ? -21.950 -8.954  -26.012 1.00 31.21 ? 229 TRP B C   1 
ATOM   3592 O  O   . TRP B 1 204 ? -22.378 -10.094 -26.227 1.00 29.75 ? 229 TRP B O   1 
ATOM   3593 C  CB  . TRP B 1 204 ? -23.102 -8.214  -23.940 1.00 30.93 ? 229 TRP B CB  1 
ATOM   3594 C  CG  . TRP B 1 204 ? -23.757 -7.120  -23.145 1.00 31.28 ? 229 TRP B CG  1 
ATOM   3595 C  CD1 . TRP B 1 204 ? -25.002 -6.605  -23.342 1.00 32.52 ? 229 TRP B CD1 1 
ATOM   3596 C  CD2 . TRP B 1 204 ? -23.208 -6.418  -22.006 1.00 31.44 ? 229 TRP B CD2 1 
ATOM   3597 N  NE1 . TRP B 1 204 ? -25.271 -5.630  -22.422 1.00 33.25 ? 229 TRP B NE1 1 
ATOM   3598 C  CE2 . TRP B 1 204 ? -24.194 -5.498  -21.585 1.00 33.30 ? 229 TRP B CE2 1 
ATOM   3599 C  CE3 . TRP B 1 204 ? -22.001 -6.476  -21.303 1.00 30.12 ? 229 TRP B CE3 1 
ATOM   3600 C  CZ2 . TRP B 1 204 ? -23.995 -4.635  -20.507 1.00 33.67 ? 229 TRP B CZ2 1 
ATOM   3601 C  CZ3 . TRP B 1 204 ? -21.803 -5.616  -20.247 1.00 30.25 ? 229 TRP B CZ3 1 
ATOM   3602 C  CH2 . TRP B 1 204 ? -22.788 -4.724  -19.851 1.00 32.50 ? 229 TRP B CH2 1 
ATOM   3603 N  N   . LYS B 1 205 ? -20.675 -8.597  -26.222 1.00 31.69 ? 230 LYS B N   1 
ATOM   3604 C  CA  . LYS B 1 205 ? -19.693 -9.574  -26.658 1.00 32.18 ? 230 LYS B CA  1 
ATOM   3605 C  C   . LYS B 1 205 ? -19.210 -10.345 -25.433 1.00 29.12 ? 230 LYS B C   1 
ATOM   3606 O  O   . LYS B 1 205 ? -19.048 -9.773  -24.376 1.00 27.01 ? 230 LYS B O   1 
ATOM   3607 C  CB  . LYS B 1 205 ? -18.561 -8.861  -27.408 1.00 36.50 ? 230 LYS B CB  1 
ATOM   3608 C  CG  . LYS B 1 205 ? -17.374 -9.727  -27.815 1.00 41.79 ? 230 LYS B CG  1 
ATOM   3609 C  CD  . LYS B 1 205 ? -16.578 -9.257  -29.038 1.00 50.46 ? 230 LYS B CD  1 
ATOM   3610 C  CE  . LYS B 1 205 ? -15.316 -8.507  -28.700 1.00 55.69 ? 230 LYS B CE  1 
ATOM   3611 N  NZ  . LYS B 1 205 ? -14.341 -8.498  -29.799 1.00 55.31 ? 230 LYS B NZ  1 
ATOM   3612 N  N   . VAL B 1 206 ? -18.968 -11.639 -25.613 1.00 26.93 ? 231 VAL B N   1 
ATOM   3613 C  CA  . VAL B 1 206 ? -18.518 -12.537 -24.568 1.00 25.74 ? 231 VAL B CA  1 
ATOM   3614 C  C   . VAL B 1 206 ? -17.431 -13.433 -25.148 1.00 26.07 ? 231 VAL B C   1 
ATOM   3615 O  O   . VAL B 1 206 ? -17.564 -13.962 -26.264 1.00 26.21 ? 231 VAL B O   1 
ATOM   3616 C  CB  . VAL B 1 206 ? -19.666 -13.397 -24.016 1.00 25.01 ? 231 VAL B CB  1 
ATOM   3617 C  CG1 . VAL B 1 206 ? -19.180 -14.462 -23.039 1.00 24.62 ? 231 VAL B CG1 1 
ATOM   3618 C  CG2 . VAL B 1 206 ? -20.754 -12.534 -23.394 1.00 26.38 ? 231 VAL B CG2 1 
ATOM   3619 N  N   . ILE B 1 207 ? -16.333 -13.558 -24.385 1.00 25.54 ? 232 ILE B N   1 
ATOM   3620 C  CA  . ILE B 1 207 ? -15.336 -14.582 -24.614 1.00 24.36 ? 232 ILE B CA  1 
ATOM   3621 C  C   . ILE B 1 207 ? -15.183 -15.311 -23.287 1.00 23.88 ? 232 ILE B C   1 
ATOM   3622 O  O   . ILE B 1 207 ? -15.260 -14.669 -22.235 1.00 23.00 ? 232 ILE B O   1 
ATOM   3623 C  CB  . ILE B 1 207 ? -14.016 -13.950 -25.107 1.00 25.92 ? 232 ILE B CB  1 
ATOM   3624 C  CG1 . ILE B 1 207 ? -13.205 -13.312 -23.975 1.00 25.82 ? 232 ILE B CG1 1 
ATOM   3625 C  CG2 . ILE B 1 207 ? -14.280 -12.930 -26.221 1.00 26.58 ? 232 ILE B CG2 1 
ATOM   3626 C  CD1 . ILE B 1 207 ? -11.897 -12.683 -24.406 1.00 26.35 ? 232 ILE B CD1 1 
ATOM   3627 N  N   . ASP B 1 208 ? -14.908 -16.620 -23.318 1.00 23.20 ? 233 ASP B N   1 
ATOM   3628 C  CA  . ASP B 1 208 ? -14.851 -17.331 -22.047 1.00 21.92 ? 233 ASP B CA  1 
ATOM   3629 C  C   . ASP B 1 208 ? -14.009 -18.600 -22.121 1.00 20.60 ? 233 ASP B C   1 
ATOM   3630 O  O   . ASP B 1 208 ? -13.659 -19.113 -23.190 1.00 20.55 ? 233 ASP B O   1 
ATOM   3631 C  CB  . ASP B 1 208 ? -16.261 -17.668 -21.565 1.00 23.44 ? 233 ASP B CB  1 
ATOM   3632 C  CG  . ASP B 1 208 ? -16.863 -18.911 -22.191 1.00 24.04 ? 233 ASP B CG  1 
ATOM   3633 O  OD1 . ASP B 1 208 ? -16.953 -18.930 -23.433 1.00 24.73 ? 233 ASP B OD1 1 
ATOM   3634 O  OD2 . ASP B 1 208 ? -17.138 -19.890 -21.442 1.00 22.63 ? 233 ASP B OD2 1 
ATOM   3635 N  N   . LYS B 1 209 ? -13.726 -19.128 -20.919 1.00 20.41 ? 234 LYS B N   1 
ATOM   3636 C  CA  . LYS B 1 209 ? -13.187 -20.468 -20.748 1.00 20.26 ? 234 LYS B CA  1 
ATOM   3637 C  C   . LYS B 1 209 ? -13.957 -21.111 -19.599 1.00 21.44 ? 234 LYS B C   1 
ATOM   3638 O  O   . LYS B 1 209 ? -14.028 -20.545 -18.504 1.00 20.17 ? 234 LYS B O   1 
ATOM   3639 C  CB  . LYS B 1 209 ? -11.679 -20.475 -20.458 1.00 19.87 ? 234 LYS B CB  1 
ATOM   3640 C  CG  . LYS B 1 209 ? -11.109 -21.870 -20.162 1.00 20.69 ? 234 LYS B CG  1 
ATOM   3641 C  CD  . LYS B 1 209 ? -10.938 -22.665 -21.444 1.00 21.93 ? 234 LYS B CD  1 
ATOM   3642 C  CE  . LYS B 1 209 ? -10.896 -24.162 -21.261 1.00 23.48 ? 234 LYS B CE  1 
ATOM   3643 N  NZ  . LYS B 1 209 ? -12.240 -24.729 -21.064 1.00 25.86 ? 234 LYS B NZ  1 
ATOM   3644 N  N   . THR B 1 210 ? -14.488 -22.308 -19.860 1.00 21.68 ? 235 THR B N   1 
ATOM   3645 C  CA  . THR B 1 210 ? -15.272 -23.050 -18.883 1.00 22.27 ? 235 THR B CA  1 
ATOM   3646 C  C   . THR B 1 210 ? -14.378 -23.992 -18.077 1.00 22.54 ? 235 THR B C   1 
ATOM   3647 O  O   . THR B 1 210 ? -13.243 -24.294 -18.442 1.00 21.12 ? 235 THR B O   1 
ATOM   3648 C  CB  . THR B 1 210 ? -16.351 -23.851 -19.610 1.00 23.12 ? 235 THR B CB  1 
ATOM   3649 O  OG1 . THR B 1 210 ? -15.672 -24.813 -20.426 1.00 23.16 ? 235 THR B OG1 1 
ATOM   3650 C  CG2 . THR B 1 210 ? -17.288 -22.984 -20.429 1.00 22.39 ? 235 THR B CG2 1 
ATOM   3651 N  N   . GLY B 1 211 ? -14.919 -24.469 -16.957 1.00 21.64 ? 236 GLY B N   1 
ATOM   3652 C  CA  . GLY B 1 211 ? -14.398 -25.663 -16.319 1.00 21.63 ? 236 GLY B CA  1 
ATOM   3653 C  C   . GLY B 1 211 ? -15.515 -26.470 -15.681 1.00 20.15 ? 236 GLY B C   1 
ATOM   3654 O  O   . GLY B 1 211 ? -16.509 -25.895 -15.241 1.00 19.91 ? 236 GLY B O   1 
ATOM   3655 N  N   . THR B 1 212 ? -15.331 -27.794 -15.642 1.00 20.27 ? 237 THR B N   1 
ATOM   3656 C  CA  . THR B 1 212 ? -16.327 -28.707 -15.112 1.00 21.19 ? 237 THR B CA  1 
ATOM   3657 C  C   . THR B 1 212 ? -15.567 -29.832 -14.410 1.00 22.81 ? 237 THR B C   1 
ATOM   3658 O  O   . THR B 1 212 ? -14.484 -30.228 -14.864 1.00 23.34 ? 237 THR B O   1 
ATOM   3659 C  CB  . THR B 1 212 ? -17.192 -29.253 -16.255 1.00 21.72 ? 237 THR B CB  1 
ATOM   3660 O  OG1 . THR B 1 212 ? -17.652 -28.164 -17.062 1.00 20.23 ? 237 THR B OG1 1 
ATOM   3661 C  CG2 . THR B 1 212 ? -18.378 -30.041 -15.733 1.00 23.02 ? 237 THR B CG2 1 
ATOM   3662 N  N   . GLY B 1 213 ? -16.100 -30.319 -13.290 1.00 22.52 ? 238 GLY B N   1 
ATOM   3663 C  CA  . GLY B 1 213 ? -15.389 -31.345 -12.539 1.00 23.71 ? 238 GLY B CA  1 
ATOM   3664 C  C   . GLY B 1 213 ? -16.333 -32.143 -11.648 1.00 25.09 ? 238 GLY B C   1 
ATOM   3665 O  O   . GLY B 1 213 ? -17.547 -31.956 -11.699 1.00 25.41 ? 238 GLY B O   1 
ATOM   3666 N  N   . ASP B 1 214 ? -15.747 -33.000 -10.806 1.00 26.49 ? 240 ASP B N   1 
ATOM   3667 C  CA  . ASP B 1 214 ? -16.508 -33.795 -9.859  1.00 27.72 ? 240 ASP B CA  1 
ATOM   3668 C  C   . ASP B 1 214 ? -17.073 -32.896 -8.753  1.00 25.82 ? 240 ASP B C   1 
ATOM   3669 O  O   . ASP B 1 214 ? -16.860 -31.684 -8.762  1.00 24.69 ? 240 ASP B O   1 
ATOM   3670 C  CB  . ASP B 1 214 ? -15.667 -34.992 -9.436  1.00 30.55 ? 240 ASP B CB  1 
ATOM   3671 C  CG  . ASP B 1 214 ? -15.337 -35.880 -10.635 1.00 34.11 ? 240 ASP B CG  1 
ATOM   3672 O  OD1 . ASP B 1 214 ? -16.281 -36.508 -11.172 1.00 36.23 ? 240 ASP B OD1 1 
ATOM   3673 O  OD2 . ASP B 1 214 ? -14.174 -35.864 -11.081 1.00 34.55 ? 240 ASP B OD2 1 
ATOM   3674 N  N   . TYR B 1 215 ? -17.871 -33.471 -7.845  1.00 25.55 ? 241 TYR B N   1 
ATOM   3675 C  CA  . TYR B 1 215 ? -18.544 -32.688 -6.806  1.00 26.03 ? 241 TYR B CA  1 
ATOM   3676 C  C   . TYR B 1 215 ? -19.372 -31.542 -7.400  1.00 25.40 ? 241 TYR B C   1 
ATOM   3677 O  O   . TYR B 1 215 ? -19.529 -30.488 -6.777  1.00 23.92 ? 241 TYR B O   1 
ATOM   3678 C  CB  . TYR B 1 215 ? -17.554 -32.164 -5.758  1.00 26.23 ? 241 TYR B CB  1 
ATOM   3679 C  CG  . TYR B 1 215 ? -16.796 -33.287 -5.070  1.00 27.14 ? 241 TYR B CG  1 
ATOM   3680 C  CD1 . TYR B 1 215 ? -17.332 -33.962 -3.979  1.00 28.40 ? 241 TYR B CD1 1 
ATOM   3681 C  CD2 . TYR B 1 215 ? -15.547 -33.680 -5.533  1.00 27.54 ? 241 TYR B CD2 1 
ATOM   3682 C  CE1 . TYR B 1 215 ? -16.646 -35.006 -3.387  1.00 30.05 ? 241 TYR B CE1 1 
ATOM   3683 C  CE2 . TYR B 1 215 ? -14.852 -34.718 -4.950  1.00 29.11 ? 241 TYR B CE2 1 
ATOM   3684 C  CZ  . TYR B 1 215 ? -15.396 -35.374 -3.867  1.00 29.50 ? 241 TYR B CZ  1 
ATOM   3685 O  OH  . TYR B 1 215 ? -14.665 -36.372 -3.303  1.00 31.58 ? 241 TYR B OH  1 
ATOM   3686 N  N   . GLY B 1 216 ? -19.964 -31.777 -8.583  1.00 24.98 ? 242 GLY B N   1 
ATOM   3687 C  CA  . GLY B 1 216 ? -20.844 -30.803 -9.206  1.00 25.04 ? 242 GLY B CA  1 
ATOM   3688 C  C   . GLY B 1 216 ? -20.139 -29.485 -9.557  1.00 25.00 ? 242 GLY B C   1 
ATOM   3689 O  O   . GLY B 1 216 ? -20.793 -28.446 -9.627  1.00 24.43 ? 242 GLY B O   1 
ATOM   3690 N  N   . ARG B 1 217 ? -18.822 -29.538 -9.819  1.00 22.64 ? 243 ARG B N   1 
ATOM   3691 C  CA  . ARG B 1 217 ? -18.061 -28.340 -10.142 1.00 23.09 ? 243 ARG B CA  1 
ATOM   3692 C  C   . ARG B 1 217 ? -18.405 -27.826 -11.547 1.00 22.68 ? 243 ARG B C   1 
ATOM   3693 O  O   . ARG B 1 217 ? -18.423 -28.589 -12.517 1.00 22.54 ? 243 ARG B O   1 
ATOM   3694 C  CB  . ARG B 1 217 ? -16.559 -28.604 -10.040 1.00 22.80 ? 243 ARG B CB  1 
ATOM   3695 C  CG  . ARG B 1 217 ? -16.095 -28.678 -8.591  1.00 24.11 ? 243 ARG B CG  1 
ATOM   3696 C  CD  . ARG B 1 217 ? -14.733 -29.315 -8.394  1.00 23.72 ? 243 ARG B CD  1 
ATOM   3697 N  NE  . ARG B 1 217 ? -14.435 -29.393 -6.958  1.00 25.33 ? 243 ARG B NE  1 
ATOM   3698 C  CZ  . ARG B 1 217 ? -13.783 -30.374 -6.339  1.00 25.60 ? 243 ARG B CZ  1 
ATOM   3699 N  NH1 . ARG B 1 217 ? -13.211 -31.337 -7.025  1.00 24.43 ? 243 ARG B NH1 1 
ATOM   3700 N  NH2 . ARG B 1 217 ? -13.675 -30.361 -5.021  1.00 27.44 ? 243 ARG B NH2 1 
ATOM   3701 N  N   . ALA B 1 218 ? -18.684 -26.522 -11.646 1.00 21.52 ? 244 ALA B N   1 
ATOM   3702 C  CA  . ALA B 1 218 ? -18.945 -25.880 -12.920 1.00 21.21 ? 244 ALA B CA  1 
ATOM   3703 C  C   . ALA B 1 218 ? -18.532 -24.419 -12.790 1.00 21.82 ? 244 ALA B C   1 
ATOM   3704 O  O   . ALA B 1 218 ? -18.991 -23.706 -11.905 1.00 21.44 ? 244 ALA B O   1 
ATOM   3705 C  CB  . ALA B 1 218 ? -20.406 -25.988 -13.316 1.00 22.22 ? 244 ALA B CB  1 
ATOM   3706 N  N   . ASN B 1 219 ? -17.575 -24.016 -13.620 1.00 20.91 ? 245 ASN B N   1 
ATOM   3707 C  CA  . ASN B 1 219 ? -17.014 -22.678 -13.583 1.00 20.28 ? 245 ASN B CA  1 
ATOM   3708 C  C   . ASN B 1 219 ? -17.112 -22.047 -14.965 1.00 19.27 ? 245 ASN B C   1 
ATOM   3709 O  O   . ASN B 1 219 ? -17.216 -22.757 -15.970 1.00 17.27 ? 245 ASN B O   1 
ATOM   3710 C  CB  . ASN B 1 219 ? -15.543 -22.682 -13.192 1.00 19.77 ? 245 ASN B CB  1 
ATOM   3711 C  CG  . ASN B 1 219 ? -15.233 -23.428 -11.916 1.00 21.80 ? 245 ASN B CG  1 
ATOM   3712 O  OD1 . ASN B 1 219 ? -16.012 -23.396 -10.955 1.00 21.28 ? 245 ASN B OD1 1 
ATOM   3713 N  ND2 . ASN B 1 219 ? -14.103 -24.111 -11.891 1.00 20.79 ? 245 ASN B ND2 1 
ATOM   3714 N  N   . ASP B 1 220 ? -16.984 -20.720 -14.994 1.00 19.49 ? 246 ASP B N   1 
ATOM   3715 C  CA  . ASP B 1 220 ? -16.814 -19.997 -16.240 1.00 20.17 ? 246 ASP B CA  1 
ATOM   3716 C  C   . ASP B 1 220 ? -16.087 -18.699 -15.930 1.00 20.90 ? 246 ASP B C   1 
ATOM   3717 O  O   . ASP B 1 220 ? -16.386 -18.058 -14.931 1.00 20.36 ? 246 ASP B O   1 
ATOM   3718 C  CB  . ASP B 1 220 ? -18.142 -19.737 -16.930 1.00 20.65 ? 246 ASP B CB  1 
ATOM   3719 C  CG  . ASP B 1 220 ? -18.046 -19.413 -18.417 1.00 20.87 ? 246 ASP B CG  1 
ATOM   3720 O  OD1 . ASP B 1 220 ? -17.010 -19.735 -19.032 1.00 19.07 ? 246 ASP B OD1 1 
ATOM   3721 O  OD2 . ASP B 1 220 ? -19.014 -18.867 -18.965 1.00 23.47 ? 246 ASP B OD2 1 
ATOM   3722 N  N   . ILE B 1 221 ? -15.080 -18.363 -16.744 1.00 20.40 ? 247 ILE B N   1 
ATOM   3723 C  CA  . ILE B 1 221 ? -14.411 -17.086 -16.639 1.00 21.90 ? 247 ILE B CA  1 
ATOM   3724 C  C   . ILE B 1 221 ? -14.505 -16.421 -18.008 1.00 21.75 ? 247 ILE B C   1 
ATOM   3725 O  O   . ILE B 1 221 ? -14.303 -17.052 -19.039 1.00 21.15 ? 247 ILE B O   1 
ATOM   3726 C  CB  . ILE B 1 221 ? -12.958 -17.208 -16.133 1.00 22.24 ? 247 ILE B CB  1 
ATOM   3727 C  CG1 . ILE B 1 221 ? -12.080 -18.045 -17.078 1.00 22.32 ? 247 ILE B CG1 1 
ATOM   3728 C  CG2 . ILE B 1 221 ? -12.934 -17.740 -14.698 1.00 23.45 ? 247 ILE B CG2 1 
ATOM   3729 C  CD1 . ILE B 1 221 ? -10.602 -18.018 -16.717 1.00 22.16 ? 247 ILE B CD1 1 
ATOM   3730 N  N   . ALA B 1 222 ? -14.814 -15.133 -17.995 1.00 21.47 ? 248 ALA B N   1 
ATOM   3731 C  CA  . ALA B 1 222 ? -15.137 -14.453 -19.231 1.00 20.81 ? 248 ALA B CA  1 
ATOM   3732 C  C   . ALA B 1 222 ? -14.674 -13.008 -19.162 1.00 21.27 ? 248 ALA B C   1 
ATOM   3733 O  O   . ALA B 1 222 ? -14.505 -12.431 -18.087 1.00 22.25 ? 248 ALA B O   1 
ATOM   3734 C  CB  . ALA B 1 222 ? -16.626 -14.528 -19.456 1.00 20.67 ? 248 ALA B CB  1 
ATOM   3735 N  N   . VAL B 1 223 ? -14.480 -12.445 -20.348 1.00 21.94 ? 249 VAL B N   1 
ATOM   3736 C  CA  . VAL B 1 223 ? -14.452 -11.016 -20.525 1.00 22.46 ? 249 VAL B CA  1 
ATOM   3737 C  C   . VAL B 1 223 ? -15.671 -10.705 -21.380 1.00 24.24 ? 249 VAL B C   1 
ATOM   3738 O  O   . VAL B 1 223 ? -15.972 -11.420 -22.337 1.00 24.21 ? 249 VAL B O   1 
ATOM   3739 C  CB  . VAL B 1 223 ? -13.141 -10.532 -21.164 1.00 23.23 ? 249 VAL B CB  1 
ATOM   3740 C  CG1 . VAL B 1 223 ? -13.104 -9.002  -21.216 1.00 24.02 ? 249 VAL B CG1 1 
ATOM   3741 C  CG2 . VAL B 1 223 ? -11.926 -11.126 -20.449 1.00 23.04 ? 249 VAL B CG2 1 
ATOM   3742 N  N   . VAL B 1 224 ? -16.394 -9.655  -21.002 1.00 24.24 ? 250 VAL B N   1 
ATOM   3743 C  CA  . VAL B 1 224 ? -17.575 -9.261  -21.739 1.00 25.51 ? 250 VAL B CA  1 
ATOM   3744 C  C   . VAL B 1 224 ? -17.393 -7.798  -22.100 1.00 26.93 ? 250 VAL B C   1 
ATOM   3745 O  O   . VAL B 1 224 ? -16.647 -7.076  -21.437 1.00 27.63 ? 250 VAL B O   1 
ATOM   3746 C  CB  . VAL B 1 224 ? -18.860 -9.523  -20.917 1.00 26.35 ? 250 VAL B CB  1 
ATOM   3747 C  CG1 . VAL B 1 224 ? -18.864 -10.935 -20.329 1.00 25.32 ? 250 VAL B CG1 1 
ATOM   3748 C  CG2 . VAL B 1 224 ? -19.047 -8.520  -19.789 1.00 27.08 ? 250 VAL B CG2 1 
ATOM   3749 N  N   . TRP B 1 225 ? -18.064 -7.389  -23.170 1.00 27.49 ? 251 TRP B N   1 
ATOM   3750 C  CA  . TRP B 1 225 ? -18.044 -6.015  -23.631 1.00 29.10 ? 251 TRP B CA  1 
ATOM   3751 C  C   . TRP B 1 225 ? -19.479 -5.550  -23.825 1.00 30.37 ? 251 TRP B C   1 
ATOM   3752 O  O   . TRP B 1 225 ? -20.262 -6.247  -24.475 1.00 30.98 ? 251 TRP B O   1 
ATOM   3753 C  CB  . TRP B 1 225 ? -17.274 -5.894  -24.949 1.00 29.96 ? 251 TRP B CB  1 
ATOM   3754 C  CG  . TRP B 1 225 ? -15.773 -5.943  -24.836 1.00 29.55 ? 251 TRP B CG  1 
ATOM   3755 C  CD1 . TRP B 1 225 ? -14.912 -4.883  -24.815 1.00 31.02 ? 251 TRP B CD1 1 
ATOM   3756 C  CD2 . TRP B 1 225 ? -14.948 -7.117  -24.797 1.00 28.73 ? 251 TRP B CD2 1 
ATOM   3757 N  NE1 . TRP B 1 225 ? -13.617 -5.316  -24.758 1.00 30.16 ? 251 TRP B NE1 1 
ATOM   3758 C  CE2 . TRP B 1 225 ? -13.605 -6.676  -24.742 1.00 28.96 ? 251 TRP B CE2 1 
ATOM   3759 C  CE3 . TRP B 1 225 ? -15.214 -8.490  -24.802 1.00 28.60 ? 251 TRP B CE3 1 
ATOM   3760 C  CZ2 . TRP B 1 225 ? -12.534 -7.557  -24.675 1.00 28.24 ? 251 TRP B CZ2 1 
ATOM   3761 C  CZ3 . TRP B 1 225 ? -14.149 -9.363  -24.752 1.00 28.10 ? 251 TRP B CZ3 1 
ATOM   3762 C  CH2 . TRP B 1 225 ? -12.828 -8.902  -24.697 1.00 26.88 ? 251 TRP B CH2 1 
ATOM   3763 N  N   . SER B 1 226 ? -19.798 -4.387  -23.251 1.00 30.12 ? 252 SER B N   1 
ATOM   3764 C  CA  . SER B 1 226 ? -21.124 -3.805  -23.372 1.00 32.49 ? 252 SER B CA  1 
ATOM   3765 C  C   . SER B 1 226 ? -21.348 -3.339  -24.800 1.00 33.64 ? 252 SER B C   1 
ATOM   3766 O  O   . SER B 1 226 ? -20.400 -3.236  -25.573 1.00 33.56 ? 252 SER B O   1 
ATOM   3767 C  CB  . SER B 1 226 ? -21.312 -2.632  -22.429 1.00 32.93 ? 252 SER B CB  1 
ATOM   3768 O  OG  . SER B 1 226 ? -20.721 -1.458  -22.972 1.00 33.60 ? 252 SER B OG  1 
ATOM   3769 N  N   . PRO B 1 227 ? -22.605 -3.028  -25.188 1.00 35.67 ? 254 PRO B N   1 
ATOM   3770 C  CA  . PRO B 1 227 ? -22.883 -2.470  -26.516 1.00 37.46 ? 254 PRO B CA  1 
ATOM   3771 C  C   . PRO B 1 227 ? -22.121 -1.186  -26.860 1.00 39.98 ? 254 PRO B C   1 
ATOM   3772 O  O   . PRO B 1 227 ? -21.940 -0.867  -28.036 1.00 42.35 ? 254 PRO B O   1 
ATOM   3773 C  CB  . PRO B 1 227 ? -24.394 -2.212  -26.476 1.00 38.56 ? 254 PRO B CB  1 
ATOM   3774 C  CG  . PRO B 1 227 ? -24.910 -3.170  -25.444 1.00 36.63 ? 254 PRO B CG  1 
ATOM   3775 C  CD  . PRO B 1 227 ? -23.819 -3.264  -24.399 1.00 35.74 ? 254 PRO B CD  1 
ATOM   3776 N  N   . THR B 1 228 ? -21.681 -0.439  -25.842 1.00 40.46 ? 255 THR B N   1 
ATOM   3777 C  CA  . THR B 1 228 ? -20.857 0.744   -26.061 1.00 42.04 ? 255 THR B CA  1 
ATOM   3778 C  C   . THR B 1 228 ? -19.362 0.414   -25.957 1.00 40.63 ? 255 THR B C   1 
ATOM   3779 O  O   . THR B 1 228 ? -18.540 1.311   -26.022 1.00 40.88 ? 255 THR B O   1 
ATOM   3780 C  CB  . THR B 1 228 ? -21.259 1.828   -25.062 1.00 43.76 ? 255 THR B CB  1 
ATOM   3781 O  OG1 . THR B 1 228 ? -21.031 1.294   -23.768 1.00 41.91 ? 255 THR B OG1 1 
ATOM   3782 C  CG2 . THR B 1 228 ? -22.720 2.229   -25.151 1.00 45.90 ? 255 THR B CG2 1 
ATOM   3783 N  N   . GLY B 1 229 ? -18.994 -0.864  -25.784 1.00 38.68 ? 256 GLY B N   1 
ATOM   3784 C  CA  . GLY B 1 229 ? -17.596 -1.273  -25.854 1.00 37.00 ? 256 GLY B CA  1 
ATOM   3785 C  C   . GLY B 1 229 ? -16.885 -1.284  -24.493 1.00 36.52 ? 256 GLY B C   1 
ATOM   3786 O  O   . GLY B 1 229 ? -15.666 -1.436  -24.437 1.00 37.47 ? 256 GLY B O   1 
ATOM   3787 N  N   . VAL B 1 230 ? -17.630 -1.186  -23.389 1.00 35.30 ? 257 VAL B N   1 
ATOM   3788 C  CA  . VAL B 1 230 ? -17.004 -1.146  -22.076 1.00 33.39 ? 257 VAL B CA  1 
ATOM   3789 C  C   . VAL B 1 230 ? -16.735 -2.575  -21.615 1.00 31.24 ? 257 VAL B C   1 
ATOM   3790 O  O   . VAL B 1 230 ? -17.662 -3.373  -21.538 1.00 28.65 ? 257 VAL B O   1 
ATOM   3791 C  CB  . VAL B 1 230 ? -17.854 -0.405  -21.035 1.00 34.95 ? 257 VAL B CB  1 
ATOM   3792 C  CG1 . VAL B 1 230 ? -17.204 -0.497  -19.655 1.00 33.85 ? 257 VAL B CG1 1 
ATOM   3793 C  CG2 . VAL B 1 230 ? -18.112 1.044   -21.445 1.00 37.11 ? 257 VAL B CG2 1 
ATOM   3794 N  N   . PRO B 1 231 ? -15.477 -2.940  -21.273 1.00 29.68 ? 258 PRO B N   1 
ATOM   3795 C  CA  . PRO B 1 231 ? -15.171 -4.296  -20.815 1.00 28.44 ? 258 PRO B CA  1 
ATOM   3796 C  C   . PRO B 1 231 ? -15.391 -4.539  -19.321 1.00 27.85 ? 258 PRO B C   1 
ATOM   3797 O  O   . PRO B 1 231 ? -15.247 -3.634  -18.496 1.00 29.67 ? 258 PRO B O   1 
ATOM   3798 C  CB  . PRO B 1 231 ? -13.703 -4.456  -21.194 1.00 28.17 ? 258 PRO B CB  1 
ATOM   3799 C  CG  . PRO B 1 231 ? -13.142 -3.065  -21.064 1.00 29.57 ? 258 PRO B CG  1 
ATOM   3800 C  CD  . PRO B 1 231 ? -14.284 -2.090  -21.381 1.00 31.38 ? 258 PRO B CD  1 
ATOM   3801 N  N   . TYR B 1 232 ? -15.775 -5.770  -19.008 1.00 27.17 ? 259 TYR B N   1 
ATOM   3802 C  CA  . TYR B 1 232 ? -15.849 -6.260  -17.638 1.00 27.22 ? 259 TYR B CA  1 
ATOM   3803 C  C   . TYR B 1 232 ? -15.308 -7.682  -17.614 1.00 26.73 ? 259 TYR B C   1 
ATOM   3804 O  O   . TYR B 1 232 ? -15.379 -8.413  -18.622 1.00 25.94 ? 259 TYR B O   1 
ATOM   3805 C  CB  . TYR B 1 232 ? -17.283 -6.306  -17.117 1.00 28.00 ? 259 TYR B CB  1 
ATOM   3806 C  CG  . TYR B 1 232 ? -18.010 -4.980  -17.221 1.00 29.66 ? 259 TYR B CG  1 
ATOM   3807 C  CD1 . TYR B 1 232 ? -18.681 -4.639  -18.379 1.00 30.58 ? 259 TYR B CD1 1 
ATOM   3808 C  CD2 . TYR B 1 232 ? -18.023 -4.079  -16.159 1.00 31.08 ? 259 TYR B CD2 1 
ATOM   3809 C  CE1 . TYR B 1 232 ? -19.338 -3.429  -18.492 1.00 32.89 ? 259 TYR B CE1 1 
ATOM   3810 C  CE2 . TYR B 1 232 ? -18.699 -2.875  -16.247 1.00 33.51 ? 259 TYR B CE2 1 
ATOM   3811 C  CZ  . TYR B 1 232 ? -19.365 -2.557  -17.421 1.00 34.41 ? 259 TYR B CZ  1 
ATOM   3812 O  OH  . TYR B 1 232 ? -20.023 -1.386  -17.601 1.00 37.75 ? 259 TYR B OH  1 
ATOM   3813 N  N   . VAL B 1 233 ? -14.756 -8.066  -16.463 1.00 24.53 ? 260 VAL B N   1 
ATOM   3814 C  CA  . VAL B 1 233 ? -14.310 -9.439  -16.304 1.00 23.89 ? 260 VAL B CA  1 
ATOM   3815 C  C   . VAL B 1 233 ? -15.274 -10.113 -15.339 1.00 24.24 ? 260 VAL B C   1 
ATOM   3816 O  O   . VAL B 1 233 ? -15.631 -9.519  -14.333 1.00 24.15 ? 260 VAL B O   1 
ATOM   3817 C  CB  . VAL B 1 233 ? -12.864 -9.538  -15.800 1.00 24.04 ? 260 VAL B CB  1 
ATOM   3818 C  CG1 . VAL B 1 233 ? -12.467 -10.985 -15.489 1.00 23.87 ? 260 VAL B CG1 1 
ATOM   3819 C  CG2 . VAL B 1 233 ? -11.910 -8.848  -16.752 1.00 26.11 ? 260 VAL B CG2 1 
ATOM   3820 N  N   . VAL B 1 234 ? -15.681 -11.338 -15.683 1.00 23.67 ? 261 VAL B N   1 
ATOM   3821 C  CA  . VAL B 1 234 ? -16.700 -12.038 -14.928 1.00 23.95 ? 261 VAL B CA  1 
ATOM   3822 C  C   . VAL B 1 234 ? -16.187 -13.431 -14.605 1.00 22.23 ? 261 VAL B C   1 
ATOM   3823 O  O   . VAL B 1 234 ? -15.960 -14.229 -15.506 1.00 22.36 ? 261 VAL B O   1 
ATOM   3824 C  CB  . VAL B 1 234 ? -18.040 -12.082 -15.678 1.00 23.84 ? 261 VAL B CB  1 
ATOM   3825 C  CG1 . VAL B 1 234 ? -19.113 -12.807 -14.852 1.00 25.08 ? 261 VAL B CG1 1 
ATOM   3826 C  CG2 . VAL B 1 234 ? -18.488 -10.668 -16.065 1.00 24.31 ? 261 VAL B CG2 1 
ATOM   3827 N  N   . ALA B 1 235 ? -15.981 -13.699 -13.317 1.00 21.15 ? 262 ALA B N   1 
ATOM   3828 C  CA  . ALA B 1 235 ? -15.623 -15.041 -12.868 1.00 21.74 ? 262 ALA B CA  1 
ATOM   3829 C  C   . ALA B 1 235 ? -16.769 -15.613 -12.038 1.00 22.40 ? 262 ALA B C   1 
ATOM   3830 O  O   . ALA B 1 235 ? -17.178 -15.005 -11.066 1.00 22.31 ? 262 ALA B O   1 
ATOM   3831 C  CB  . ALA B 1 235 ? -14.331 -15.010 -12.080 1.00 21.51 ? 262 ALA B CB  1 
ATOM   3832 N  N   . VAL B 1 236 ? -17.268 -16.789 -12.444 1.00 23.19 ? 263 VAL B N   1 
ATOM   3833 C  CA  . VAL B 1 236 ? -18.322 -17.480 -11.735 1.00 23.42 ? 263 VAL B CA  1 
ATOM   3834 C  C   . VAL B 1 236 ? -17.863 -18.920 -11.541 1.00 22.27 ? 263 VAL B C   1 
ATOM   3835 O  O   . VAL B 1 236 ? -17.463 -19.597 -12.489 1.00 21.13 ? 263 VAL B O   1 
ATOM   3836 C  CB  . VAL B 1 236 ? -19.684 -17.408 -12.451 1.00 26.10 ? 263 VAL B CB  1 
ATOM   3837 C  CG1 . VAL B 1 236 ? -20.766 -18.156 -11.683 1.00 28.55 ? 263 VAL B CG1 1 
ATOM   3838 C  CG2 . VAL B 1 236 ? -20.151 -15.975 -12.669 1.00 27.33 ? 263 VAL B CG2 1 
ATOM   3839 N  N   . MET B 1 237 ? -17.850 -19.333 -10.277 1.00 22.84 ? 264 MET B N   1 
ATOM   3840 C  CA  . MET B 1 237 ? -17.366 -20.641 -9.882  1.00 22.46 ? 264 MET B CA  1 
ATOM   3841 C  C   . MET B 1 237 ? -18.447 -21.285 -9.027  1.00 22.14 ? 264 MET B C   1 
ATOM   3842 O  O   . MET B 1 237 ? -19.141 -20.600 -8.294  1.00 20.46 ? 264 MET B O   1 
ATOM   3843 C  CB  . MET B 1 237 ? -16.025 -20.500 -9.147  1.00 23.12 ? 264 MET B CB  1 
ATOM   3844 C  CG  . MET B 1 237 ? -14.994 -19.715 -9.986  1.00 23.03 ? 264 MET B CG  1 
ATOM   3845 S  SD  . MET B 1 237 ? -13.329 -19.830 -9.301  1.00 25.60 ? 264 MET B SD  1 
ATOM   3846 C  CE  . MET B 1 237 ? -12.927 -21.461 -9.968  1.00 24.39 ? 264 MET B CE  1 
ATOM   3847 N  N   . SER B 1 238 ? -18.613 -22.609 -9.137  1.00 21.53 ? 265 SER B N   1 
ATOM   3848 C  CA  . SER B 1 238 ? -19.607 -23.269 -8.318  1.00 21.62 ? 265 SER B CA  1 
ATOM   3849 C  C   . SER B 1 238 ? -19.180 -24.710 -8.082  1.00 22.14 ? 265 SER B C   1 
ATOM   3850 O  O   . SER B 1 238 ? -18.459 -25.312 -8.877  1.00 22.57 ? 265 SER B O   1 
ATOM   3851 C  CB  . SER B 1 238 ? -20.979 -23.214 -8.957  1.00 22.26 ? 265 SER B CB  1 
ATOM   3852 O  OG  . SER B 1 238 ? -21.040 -24.076 -10.084 1.00 22.01 ? 265 SER B OG  1 
ATOM   3853 N  N   . ASP B 1 239 ? -19.672 -25.255 -6.986  1.00 22.64 ? 266 ASP B N   1 
ATOM   3854 C  CA  . ASP B 1 239 ? -19.638 -26.679 -6.764  1.00 24.67 ? 266 ASP B CA  1 
ATOM   3855 C  C   . ASP B 1 239 ? -20.894 -27.065 -6.004  1.00 24.18 ? 266 ASP B C   1 
ATOM   3856 O  O   . ASP B 1 239 ? -21.615 -26.207 -5.526  1.00 24.18 ? 266 ASP B O   1 
ATOM   3857 C  CB  . ASP B 1 239 ? -18.377 -27.129 -6.055  1.00 26.07 ? 266 ASP B CB  1 
ATOM   3858 C  CG  . ASP B 1 239 ? -18.251 -26.668 -4.618  1.00 30.03 ? 266 ASP B CG  1 
ATOM   3859 O  OD1 . ASP B 1 239 ? -19.070 -27.112 -3.772  1.00 34.78 ? 266 ASP B OD1 1 
ATOM   3860 O  OD2 . ASP B 1 239 ? -17.271 -25.973 -4.359  1.00 31.22 ? 266 ASP B OD2 1 
ATOM   3861 N  N   . ARG B 1 240 ? -21.150 -28.372 -5.971  1.00 24.89 ? 267 ARG B N   1 
ATOM   3862 C  CA  . ARG B 1 240 ? -22.296 -28.935 -5.298  1.00 25.25 ? 267 ARG B CA  1 
ATOM   3863 C  C   . ARG B 1 240 ? -21.815 -30.122 -4.490  1.00 26.66 ? 267 ARG B C   1 
ATOM   3864 O  O   . ARG B 1 240 ? -22.342 -31.222 -4.630  1.00 26.41 ? 267 ARG B O   1 
ATOM   3865 C  CB  . ARG B 1 240 ? -23.409 -29.289 -6.286  1.00 26.35 ? 267 ARG B CB  1 
ATOM   3866 C  CG  . ARG B 1 240 ? -23.850 -28.141 -7.182  1.00 25.90 ? 267 ARG B CG  1 
ATOM   3867 C  CD  . ARG B 1 240 ? -24.795 -28.605 -8.274  1.00 27.56 ? 267 ARG B CD  1 
ATOM   3868 N  NE  . ARG B 1 240 ? -26.074 -28.985 -7.675  1.00 30.55 ? 267 ARG B NE  1 
ATOM   3869 C  CZ  . ARG B 1 240 ? -26.625 -30.175 -7.626  1.00 31.06 ? 267 ARG B CZ  1 
ATOM   3870 N  NH1 . ARG B 1 240 ? -26.172 -31.176 -8.353  1.00 30.53 ? 267 ARG B NH1 1 
ATOM   3871 N  NH2 . ARG B 1 240 ? -27.675 -30.338 -6.846  1.00 33.87 ? 267 ARG B NH2 1 
ATOM   3872 N  N   . ALA B 1 241 ? -20.869 -29.863 -3.582  1.00 28.31 ? 268 ALA B N   1 
ATOM   3873 C  CA  . ALA B 1 241 ? -20.305 -30.933 -2.772  1.00 31.23 ? 268 ALA B CA  1 
ATOM   3874 C  C   . ALA B 1 241 ? -21.366 -31.578 -1.876  1.00 32.05 ? 268 ALA B C   1 
ATOM   3875 O  O   . ALA B 1 241 ? -21.207 -32.743 -1.496  1.00 33.81 ? 268 ALA B O   1 
ATOM   3876 C  CB  . ALA B 1 241 ? -19.129 -30.425 -1.969  1.00 34.70 ? 268 ALA B CB  1 
ATOM   3877 N  N   . GLY B 1 242 ? -22.466 -30.854 -1.593  1.00 31.21 ? 269 GLY B N   1 
ATOM   3878 C  CA  . GLY B 1 242 ? -23.664 -31.428 -0.985  1.00 32.21 ? 269 GLY B CA  1 
ATOM   3879 C  C   . GLY B 1 242 ? -24.214 -32.648 -1.740  1.00 33.70 ? 269 GLY B C   1 
ATOM   3880 O  O   . GLY B 1 242 ? -24.894 -33.483 -1.159  1.00 33.28 ? 269 GLY B O   1 
ATOM   3881 N  N   . GLY B 1 243 ? -23.959 -32.765 -3.048  1.00 34.20 ? 270 GLY B N   1 
ATOM   3882 C  CA  . GLY B 1 243 ? -24.413 -33.929 -3.802  1.00 34.97 ? 270 GLY B CA  1 
ATOM   3883 C  C   . GLY B 1 243 ? -23.389 -35.067 -3.849  1.00 34.17 ? 270 GLY B C   1 
ATOM   3884 O  O   . GLY B 1 243 ? -23.618 -36.074 -4.522  1.00 36.22 ? 270 GLY B O   1 
ATOM   3885 N  N   . GLY B 1 244 ? -22.239 -34.890 -3.187  1.00 32.02 ? 271 GLY B N   1 
ATOM   3886 C  CA  . GLY B 1 244 ? -21.153 -35.858 -3.233  1.00 31.34 ? 271 GLY B CA  1 
ATOM   3887 C  C   . GLY B 1 244 ? -20.313 -35.768 -4.508  1.00 30.50 ? 271 GLY B C   1 
ATOM   3888 O  O   . GLY B 1 244 ? -20.516 -34.905 -5.368  1.00 28.54 ? 271 GLY B O   1 
ATOM   3889 N  N   . TYR B 1 245 ? -19.387 -36.727 -4.634  1.00 31.32 ? 272 TYR B N   1 
ATOM   3890 C  CA  . TYR B 1 245 ? -18.461 -36.819 -5.757  1.00 31.19 ? 272 TYR B CA  1 
ATOM   3891 C  C   . TYR B 1 245 ? -19.212 -36.710 -7.086  1.00 29.87 ? 272 TYR B C   1 
ATOM   3892 O  O   . TYR B 1 245 ? -18.784 -35.998 -7.997  1.00 26.65 ? 272 TYR B O   1 
ATOM   3893 C  CB  . TYR B 1 245 ? -17.719 -38.159 -5.618  1.00 31.73 ? 272 TYR B CB  1 
ATOM   3894 C  CG  . TYR B 1 245 ? -16.643 -38.345 -6.665  1.00 30.97 ? 272 TYR B CG  1 
ATOM   3895 C  CD1 . TYR B 1 245 ? -16.964 -38.789 -7.947  1.00 31.08 ? 272 TYR B CD1 1 
ATOM   3896 C  CD2 . TYR B 1 245 ? -15.318 -38.023 -6.397  1.00 30.55 ? 272 TYR B CD2 1 
ATOM   3897 C  CE1 . TYR B 1 245 ? -15.987 -38.940 -8.917  1.00 30.71 ? 272 TYR B CE1 1 
ATOM   3898 C  CE2 . TYR B 1 245 ? -14.335 -38.146 -7.368  1.00 30.97 ? 272 TYR B CE2 1 
ATOM   3899 C  CZ  . TYR B 1 245 ? -14.674 -38.592 -8.638  1.00 30.69 ? 272 TYR B CZ  1 
ATOM   3900 O  OH  . TYR B 1 245 ? -13.725 -38.760 -9.603  1.00 29.40 ? 272 TYR B OH  1 
ATOM   3901 N  N   . ASP B 1 246 ? -20.353 -37.409 -7.172  1.00 31.42 ? 273 ASP B N   1 
ATOM   3902 C  CA  . ASP B 1 246 ? -21.073 -37.575 -8.425  1.00 32.93 ? 273 ASP B CA  1 
ATOM   3903 C  C   . ASP B 1 246 ? -22.187 -36.544 -8.590  1.00 31.94 ? 273 ASP B C   1 
ATOM   3904 O  O   . ASP B 1 246 ? -23.017 -36.673 -9.483  1.00 30.86 ? 273 ASP B O   1 
ATOM   3905 C  CB  . ASP B 1 246 ? -21.673 -38.967 -8.519  1.00 37.01 ? 273 ASP B CB  1 
ATOM   3906 C  CG  . ASP B 1 246 ? -22.683 -39.303 -7.430  1.00 42.37 ? 273 ASP B CG  1 
ATOM   3907 O  OD1 . ASP B 1 246 ? -22.622 -38.683 -6.334  1.00 45.65 ? 273 ASP B OD1 1 
ATOM   3908 O  OD2 . ASP B 1 246 ? -23.530 -40.176 -7.679  1.00 49.03 ? 273 ASP B OD2 1 
ATOM   3909 N  N   . ALA B 1 247 ? -22.201 -35.487 -7.770  1.00 31.92 ? 274 ALA B N   1 
ATOM   3910 C  CA  . ALA B 1 247 ? -23.197 -34.444 -7.948  1.00 30.50 ? 274 ALA B CA  1 
ATOM   3911 C  C   . ALA B 1 247 ? -23.116 -33.936 -9.380  1.00 28.20 ? 274 ALA B C   1 
ATOM   3912 O  O   . ALA B 1 247 ? -22.031 -33.773 -9.927  1.00 25.96 ? 274 ALA B O   1 
ATOM   3913 C  CB  . ALA B 1 247 ? -22.969 -33.320 -6.980  1.00 28.86 ? 274 ALA B CB  1 
ATOM   3914 N  N   A GLU B 1 248 ? -24.283 -33.661 -9.968  0.50 29.13 ? 275 GLU B N   1 
ATOM   3915 N  N   B GLU B 1 248 ? -24.276 -33.673 -9.985  0.50 28.24 ? 275 GLU B N   1 
ATOM   3916 C  CA  A GLU B 1 248 ? -24.356 -33.131 -11.315 0.50 29.09 ? 275 GLU B CA  1 
ATOM   3917 C  CA  B GLU B 1 248 ? -24.303 -33.151 -11.340 0.50 27.51 ? 275 GLU B CA  1 
ATOM   3918 C  C   A GLU B 1 248 ? -23.963 -31.658 -11.290 0.50 27.44 ? 275 GLU B C   1 
ATOM   3919 C  C   B GLU B 1 248 ? -23.951 -31.671 -11.295 0.50 26.59 ? 275 GLU B C   1 
ATOM   3920 O  O   A GLU B 1 248 ? -24.490 -30.902 -10.472 0.50 26.01 ? 275 GLU B O   1 
ATOM   3921 O  O   B GLU B 1 248 ? -24.484 -30.935 -10.467 0.50 25.33 ? 275 GLU B O   1 
ATOM   3922 C  CB  A GLU B 1 248 ? -25.789 -33.256 -11.828 0.50 31.52 ? 275 GLU B CB  1 
ATOM   3923 C  CB  B GLU B 1 248 ? -25.664 -33.309 -12.012 0.50 28.53 ? 275 GLU B CB  1 
ATOM   3924 C  CG  A GLU B 1 248 ? -26.215 -34.700 -12.063 0.50 34.19 ? 275 GLU B CG  1 
ATOM   3925 C  CG  B GLU B 1 248 ? -26.038 -34.766 -12.242 0.50 29.77 ? 275 GLU B CG  1 
ATOM   3926 C  CD  A GLU B 1 248 ? -25.742 -35.312 -13.371 0.50 36.36 ? 275 GLU B CD  1 
ATOM   3927 C  CD  B GLU B 1 248 ? -27.445 -34.958 -12.764 0.50 30.98 ? 275 GLU B CD  1 
ATOM   3928 O  OE1 A GLU B 1 248 ? -25.030 -34.641 -14.159 0.50 35.44 ? 275 GLU B OE1 1 
ATOM   3929 O  OE1 B GLU B 1 248 ? -28.209 -33.967 -12.838 0.50 30.60 ? 275 GLU B OE1 1 
ATOM   3930 O  OE2 A GLU B 1 248 ? -26.113 -36.489 -13.592 0.50 39.83 ? 275 GLU B OE2 1 
ATOM   3931 O  OE2 B GLU B 1 248 ? -27.759 -36.124 -13.086 0.50 31.73 ? 275 GLU B OE2 1 
ATOM   3932 N  N   . PRO B 1 249 ? -23.057 -31.193 -12.185 1.00 25.99 ? 276 PRO B N   1 
ATOM   3933 C  CA  . PRO B 1 249 ? -22.826 -29.752 -12.331 1.00 25.46 ? 276 PRO B CA  1 
ATOM   3934 C  C   . PRO B 1 249 ? -24.092 -29.118 -12.918 1.00 26.91 ? 276 PRO B C   1 
ATOM   3935 O  O   . PRO B 1 249 ? -24.845 -29.794 -13.620 1.00 26.77 ? 276 PRO B O   1 
ATOM   3936 C  CB  . PRO B 1 249 ? -21.624 -29.634 -13.272 1.00 26.32 ? 276 PRO B CB  1 
ATOM   3937 C  CG  . PRO B 1 249 ? -21.163 -31.049 -13.538 1.00 26.73 ? 276 PRO B CG  1 
ATOM   3938 C  CD  . PRO B 1 249 ? -22.267 -32.007 -13.115 1.00 26.95 ? 276 PRO B CD  1 
ATOM   3939 N  N   . ARG B 1 250 ? -24.299 -27.820 -12.661 1.00 26.08 ? 277 ARG B N   1 
ATOM   3940 C  CA  . ARG B 1 250 ? -25.499 -27.127 -13.077 1.00 27.03 ? 277 ARG B CA  1 
ATOM   3941 C  C   . ARG B 1 250 ? -25.108 -25.868 -13.828 1.00 27.43 ? 277 ARG B C   1 
ATOM   3942 O  O   . ARG B 1 250 ? -24.802 -24.837 -13.224 1.00 25.31 ? 277 ARG B O   1 
ATOM   3943 C  CB  . ARG B 1 250 ? -26.353 -26.719 -11.869 1.00 28.87 ? 277 ARG B CB  1 
ATOM   3944 C  CG  . ARG B 1 250 ? -26.981 -27.910 -11.164 1.00 29.39 ? 277 ARG B CG  1 
ATOM   3945 C  CD  . ARG B 1 250 ? -28.080 -28.563 -11.962 1.00 31.51 ? 277 ARG B CD  1 
ATOM   3946 N  NE  . ARG B 1 250 ? -28.748 -29.561 -11.115 1.00 34.32 ? 277 ARG B NE  1 
ATOM   3947 C  CZ  . ARG B 1 250 ? -28.849 -30.858 -11.386 1.00 35.93 ? 277 ARG B CZ  1 
ATOM   3948 N  NH1 . ARG B 1 250 ? -28.556 -31.313 -12.584 1.00 36.67 ? 277 ARG B NH1 1 
ATOM   3949 N  NH2 . ARG B 1 250 ? -29.294 -31.705 -10.473 1.00 37.21 ? 277 ARG B NH2 1 
ATOM   3950 N  N   . GLU B 1 251 ? -25.115 -25.965 -15.161 1.00 26.63 ? 278 GLU B N   1 
ATOM   3951 C  CA  . GLU B 1 251 ? -24.706 -24.827 -15.961 1.00 26.11 ? 278 GLU B CA  1 
ATOM   3952 C  C   . GLU B 1 251 ? -25.651 -23.665 -15.719 1.00 24.78 ? 278 GLU B C   1 
ATOM   3953 O  O   . GLU B 1 251 ? -25.214 -22.513 -15.726 1.00 23.27 ? 278 GLU B O   1 
ATOM   3954 C  CB  . GLU B 1 251 ? -24.698 -25.199 -17.436 1.00 26.34 ? 278 GLU B CB  1 
ATOM   3955 C  CG  . GLU B 1 251 ? -23.591 -26.185 -17.778 1.00 25.48 ? 278 GLU B CG  1 
ATOM   3956 C  CD  . GLU B 1 251 ? -23.431 -26.277 -19.289 1.00 26.33 ? 278 GLU B CD  1 
ATOM   3957 O  OE1 . GLU B 1 251 ? -24.315 -26.855 -19.963 1.00 25.65 ? 278 GLU B OE1 1 
ATOM   3958 O  OE2 . GLU B 1 251 ? -22.426 -25.719 -19.761 1.00 26.13 ? 278 GLU B OE2 1 
ATOM   3959 N  N   . ALA B 1 252 ? -26.933 -23.993 -15.497 1.00 25.43 ? 279 ALA B N   1 
ATOM   3960 C  CA  . ALA B 1 252 ? -27.964 -22.982 -15.334 1.00 25.97 ? 279 ALA B CA  1 
ATOM   3961 C  C   . ALA B 1 252 ? -27.656 -22.095 -14.129 1.00 25.40 ? 279 ALA B C   1 
ATOM   3962 O  O   . ALA B 1 252 ? -28.027 -20.926 -14.145 1.00 26.14 ? 279 ALA B O   1 
ATOM   3963 C  CB  . ALA B 1 252 ? -29.332 -23.628 -15.233 1.00 27.26 ? 279 ALA B CB  1 
ATOM   3964 N  N   . LEU B 1 253 ? -26.987 -22.650 -13.104 1.00 25.11 ? 280 LEU B N   1 
ATOM   3965 C  CA  . LEU B 1 253 ? -26.600 -21.877 -11.928 1.00 25.34 ? 280 LEU B CA  1 
ATOM   3966 C  C   . LEU B 1 253 ? -25.692 -20.722 -12.360 1.00 25.02 ? 280 LEU B C   1 
ATOM   3967 O  O   . LEU B 1 253 ? -25.890 -19.581 -11.936 1.00 23.49 ? 280 LEU B O   1 
ATOM   3968 C  CB  . LEU B 1 253 ? -25.930 -22.796 -10.901 1.00 26.11 ? 280 LEU B CB  1 
ATOM   3969 C  CG  . LEU B 1 253 ? -25.097 -22.119 -9.792  1.00 26.48 ? 280 LEU B CG  1 
ATOM   3970 C  CD1 . LEU B 1 253 ? -25.988 -21.203 -8.962  1.00 26.96 ? 280 LEU B CD1 1 
ATOM   3971 C  CD2 . LEU B 1 253 ? -24.415 -23.155 -8.886  1.00 27.48 ? 280 LEU B CD2 1 
ATOM   3972 N  N   . LEU B 1 254 ? -24.739 -21.010 -13.267 1.00 24.07 ? 281 LEU B N   1 
ATOM   3973 C  CA  . LEU B 1 254 ? -23.810 -20.001 -13.737 1.00 24.27 ? 281 LEU B CA  1 
ATOM   3974 C  C   . LEU B 1 254 ? -24.552 -18.992 -14.625 1.00 24.69 ? 281 LEU B C   1 
ATOM   3975 O  O   . LEU B 1 254 ? -24.289 -17.788 -14.540 1.00 24.37 ? 281 LEU B O   1 
ATOM   3976 C  CB  . LEU B 1 254 ? -22.617 -20.616 -14.471 1.00 24.35 ? 281 LEU B CB  1 
ATOM   3977 C  CG  . LEU B 1 254 ? -21.848 -21.709 -13.727 1.00 25.98 ? 281 LEU B CG  1 
ATOM   3978 C  CD1 . LEU B 1 254 ? -20.815 -22.321 -14.647 1.00 27.13 ? 281 LEU B CD1 1 
ATOM   3979 C  CD2 . LEU B 1 254 ? -21.167 -21.191 -12.468 1.00 26.85 ? 281 LEU B CD2 1 
ATOM   3980 N  N   . ALA B 1 255 ? -25.457 -19.478 -15.489 1.00 23.54 ? 282 ALA B N   1 
ATOM   3981 C  CA  . ALA B 1 255 ? -26.227 -18.596 -16.354 1.00 25.50 ? 282 ALA B CA  1 
ATOM   3982 C  C   . ALA B 1 255 ? -27.050 -17.613 -15.523 1.00 26.33 ? 282 ALA B C   1 
ATOM   3983 O  O   . ALA B 1 255 ? -27.109 -16.424 -15.834 1.00 25.92 ? 282 ALA B O   1 
ATOM   3984 C  CB  . ALA B 1 255 ? -27.127 -19.393 -17.284 1.00 26.23 ? 282 ALA B CB  1 
ATOM   3985 N  N   . GLU B 1 256 ? -27.673 -18.112 -14.453 1.00 27.17 ? 283 GLU B N   1 
ATOM   3986 C  CA  . GLU B 1 256 ? -28.466 -17.273 -13.582 1.00 27.80 ? 283 GLU B CA  1 
ATOM   3987 C  C   . GLU B 1 256 ? -27.585 -16.262 -12.859 1.00 26.94 ? 283 GLU B C   1 
ATOM   3988 O  O   . GLU B 1 256 ? -27.972 -15.102 -12.700 1.00 27.11 ? 283 GLU B O   1 
ATOM   3989 C  CB  . GLU B 1 256 ? -29.204 -18.091 -12.528 1.00 29.70 ? 283 GLU B CB  1 
ATOM   3990 C  CG  . GLU B 1 256 ? -30.412 -18.844 -13.064 1.00 31.36 ? 283 GLU B CG  1 
ATOM   3991 C  CD  . GLU B 1 256 ? -31.091 -19.564 -11.902 1.00 33.56 ? 283 GLU B CD  1 
ATOM   3992 O  OE1 . GLU B 1 256 ? -31.347 -18.901 -10.871 1.00 33.93 ? 283 GLU B OE1 1 
ATOM   3993 O  OE2 . GLU B 1 256 ? -31.347 -20.782 -12.037 1.00 33.89 ? 283 GLU B OE2 1 
ATOM   3994 N  N   . ALA B 1 257 ? -26.425 -16.709 -12.387 1.00 25.05 ? 284 ALA B N   1 
ATOM   3995 C  CA  . ALA B 1 257 ? -25.533 -15.799 -11.696 1.00 25.60 ? 284 ALA B CA  1 
ATOM   3996 C  C   . ALA B 1 257 ? -25.141 -14.679 -12.652 1.00 26.06 ? 284 ALA B C   1 
ATOM   3997 O  O   . ALA B 1 257 ? -25.110 -13.512 -12.277 1.00 25.97 ? 284 ALA B O   1 
ATOM   3998 C  CB  . ALA B 1 257 ? -24.329 -16.534 -11.148 1.00 24.38 ? 284 ALA B CB  1 
ATOM   3999 N  N   . ALA B 1 258 ? -24.826 -15.061 -13.899 1.00 25.87 ? 285 ALA B N   1 
ATOM   4000 C  CA  . ALA B 1 258 ? -24.444 -14.108 -14.934 1.00 24.83 ? 285 ALA B CA  1 
ATOM   4001 C  C   . ALA B 1 258 ? -25.585 -13.138 -15.224 1.00 25.35 ? 285 ALA B C   1 
ATOM   4002 O  O   . ALA B 1 258 ? -25.342 -11.937 -15.359 1.00 25.47 ? 285 ALA B O   1 
ATOM   4003 C  CB  . ALA B 1 258 ? -23.981 -14.871 -16.168 1.00 24.75 ? 285 ALA B CB  1 
ATOM   4004 N  N   . THR B 1 259 ? -26.828 -13.634 -15.258 1.00 26.43 ? 286 THR B N   1 
ATOM   4005 C  CA  . THR B 1 259 ? -27.991 -12.770 -15.452 1.00 29.35 ? 286 THR B CA  1 
ATOM   4006 C  C   . THR B 1 259 ? -28.081 -11.718 -14.339 1.00 31.23 ? 286 THR B C   1 
ATOM   4007 O  O   . THR B 1 259 ? -28.362 -10.549 -14.603 1.00 32.02 ? 286 THR B O   1 
ATOM   4008 C  CB  . THR B 1 259 ? -29.266 -13.611 -15.547 1.00 30.49 ? 286 THR B CB  1 
ATOM   4009 O  OG1 . THR B 1 259 ? -29.052 -14.601 -16.549 1.00 29.92 ? 286 THR B OG1 1 
ATOM   4010 C  CG2 . THR B 1 259 ? -30.491 -12.801 -15.918 1.00 31.48 ? 286 THR B CG2 1 
ATOM   4011 N  N   . CYS B 1 260 ? -27.840 -12.124 -13.077 1.00 31.50 ? 287 CYS B N   1 
ATOM   4012 C  CA  . CYS B 1 260 ? -27.836 -11.171 -11.969 1.00 32.53 ? 287 CYS B CA  1 
ATOM   4013 C  C   . CYS B 1 260 ? -26.788 -10.072 -12.179 1.00 31.42 ? 287 CYS B C   1 
ATOM   4014 O  O   . CYS B 1 260 ? -27.064 -8.873  -11.996 1.00 30.92 ? 287 CYS B O   1 
ATOM   4015 C  CB  . CYS B 1 260 ? -27.590 -11.856 -10.624 1.00 33.99 ? 287 CYS B CB  1 
ATOM   4016 S  SG  . CYS B 1 260 ? -28.901 -13.015 -10.147 1.00 38.59 ? 287 CYS B SG  1 
ATOM   4017 N  N   . VAL B 1 261 ? -25.571 -10.490 -12.531 1.00 29.10 ? 288 VAL B N   1 
ATOM   4018 C  CA  . VAL B 1 261 ? -24.499 -9.553  -12.826 1.00 29.74 ? 288 VAL B CA  1 
ATOM   4019 C  C   . VAL B 1 261 ? -24.885 -8.627  -13.985 1.00 32.09 ? 288 VAL B C   1 
ATOM   4020 O  O   . VAL B 1 261 ? -24.753 -7.397  -13.881 1.00 30.54 ? 288 VAL B O   1 
ATOM   4021 C  CB  . VAL B 1 261 ? -23.204 -10.315 -13.147 1.00 28.87 ? 288 VAL B CB  1 
ATOM   4022 C  CG1 . VAL B 1 261 ? -22.110 -9.385  -13.649 1.00 28.36 ? 288 VAL B CG1 1 
ATOM   4023 C  CG2 . VAL B 1 261 ? -22.709 -11.123 -11.961 1.00 28.67 ? 288 VAL B CG2 1 
ATOM   4024 N  N   . ALA B 1 262 ? -25.342 -9.206  -15.112 1.00 32.07 ? 289 ALA B N   1 
ATOM   4025 C  CA  . ALA B 1 262 ? -25.730 -8.402  -16.264 1.00 32.15 ? 289 ALA B CA  1 
ATOM   4026 C  C   . ALA B 1 262 ? -26.742 -7.316  -15.877 1.00 33.74 ? 289 ALA B C   1 
ATOM   4027 O  O   . ALA B 1 262 ? -26.683 -6.197  -16.376 1.00 34.58 ? 289 ALA B O   1 
ATOM   4028 C  CB  . ALA B 1 262 ? -26.278 -9.309  -17.366 1.00 32.30 ? 289 ALA B CB  1 
ATOM   4029 N  N   . GLY B 1 263 ? -27.712 -7.664  -15.024 1.00 34.16 ? 290 GLY B N   1 
ATOM   4030 C  CA  . GLY B 1 263 ? -28.703 -6.714  -14.547 1.00 36.39 ? 290 GLY B CA  1 
ATOM   4031 C  C   . GLY B 1 263 ? -28.067 -5.498  -13.867 1.00 37.63 ? 290 GLY B C   1 
ATOM   4032 O  O   . GLY B 1 263 ? -28.552 -4.382  -13.994 1.00 38.76 ? 290 GLY B O   1 
ATOM   4033 N  N   . VAL B 1 264 ? -26.990 -5.734  -13.124 1.00 38.34 ? 291 VAL B N   1 
ATOM   4034 C  CA  . VAL B 1 264 ? -26.280 -4.695  -12.404 1.00 41.38 ? 291 VAL B CA  1 
ATOM   4035 C  C   . VAL B 1 264 ? -25.402 -3.888  -13.356 1.00 42.03 ? 291 VAL B C   1 
ATOM   4036 O  O   . VAL B 1 264 ? -25.284 -2.682  -13.188 1.00 42.54 ? 291 VAL B O   1 
ATOM   4037 C  CB  . VAL B 1 264 ? -25.459 -5.377  -11.292 1.00 44.14 ? 291 VAL B CB  1 
ATOM   4038 C  CG1 . VAL B 1 264 ? -24.355 -4.486  -10.724 1.00 46.44 ? 291 VAL B CG1 1 
ATOM   4039 C  CG2 . VAL B 1 264 ? -26.378 -5.888  -10.187 1.00 46.79 ? 291 VAL B CG2 1 
ATOM   4040 N  N   . LEU B 1 265 ? -24.776 -4.552  -14.337 1.00 40.75 ? 292 LEU B N   1 
ATOM   4041 C  CA  . LEU B 1 265 ? -23.884 -3.871  -15.263 1.00 41.70 ? 292 LEU B CA  1 
ATOM   4042 C  C   . LEU B 1 265 ? -24.660 -3.147  -16.368 1.00 41.52 ? 292 LEU B C   1 
ATOM   4043 O  O   . LEU B 1 265 ? -24.100 -2.288  -17.036 1.00 41.38 ? 292 LEU B O   1 
ATOM   4044 C  CB  . LEU B 1 265 ? -22.898 -4.869  -15.860 1.00 40.83 ? 292 LEU B CB  1 
ATOM   4045 C  CG  . LEU B 1 265 ? -21.958 -5.583  -14.885 1.00 39.25 ? 292 LEU B CG  1 
ATOM   4046 C  CD1 . LEU B 1 265 ? -21.033 -6.464  -15.702 1.00 38.56 ? 292 LEU B CD1 1 
ATOM   4047 C  CD2 . LEU B 1 265 ? -21.150 -4.651  -13.996 1.00 39.61 ? 292 LEU B CD2 1 
ATOM   4048 N  N   . ALA B 1 266 ? -25.925 -3.523  -16.576 1.00 43.04 ? 293 ALA B N   1 
ATOM   4049 C  CA  . ALA B 1 266 ? -26.791 -2.813  -17.499 1.00 46.20 ? 293 ALA B CA  1 
ATOM   4050 C  C   . ALA B 1 266 ? -27.063 -1.403  -16.965 1.00 47.28 ? 293 ALA B C   1 
ATOM   4051 O  O   . ALA B 1 266 ? -27.011 -0.527  -17.840 1.00 49.13 ? 293 ALA B O   1 
ATOM   4052 C  CB  . ALA B 1 266 ? -28.079 -3.571  -17.707 1.00 46.62 ? 293 ALA B CB  1 
HETATM 4053 C  C1  . GOL C 2 .   ? 3.504   -18.784 -69.127 1.00 24.26 ? 301 GOL A C1  1 
HETATM 4054 O  O1  . GOL C 2 .   ? 3.894   -19.971 -68.400 1.00 19.47 ? 301 GOL A O1  1 
HETATM 4055 C  C2  . GOL C 2 .   ? 2.268   -18.936 -70.012 1.00 23.34 ? 301 GOL A C2  1 
HETATM 4056 O  O2  . GOL C 2 .   ? 1.094   -19.138 -69.214 1.00 22.51 ? 301 GOL A O2  1 
HETATM 4057 C  C3  . GOL C 2 .   ? 2.064   -17.738 -70.925 1.00 24.13 ? 301 GOL A C3  1 
HETATM 4058 O  O3  . GOL C 2 .   ? 1.015   -17.910 -71.879 1.00 22.48 ? 301 GOL A O3  1 
HETATM 4059 C  C1  . GOL D 2 .   ? -7.951  -27.256 -65.568 1.00 35.13 ? 302 GOL A C1  1 
HETATM 4060 O  O1  . GOL D 2 .   ? -9.215  -27.067 -66.210 1.00 30.43 ? 302 GOL A O1  1 
HETATM 4061 C  C2  . GOL D 2 .   ? -7.388  -25.947 -65.054 1.00 36.30 ? 302 GOL A C2  1 
HETATM 4062 O  O2  . GOL D 2 .   ? -8.014  -25.584 -63.819 1.00 33.98 ? 302 GOL A O2  1 
HETATM 4063 C  C3  . GOL D 2 .   ? -5.875  -25.982 -64.932 1.00 40.43 ? 302 GOL A C3  1 
HETATM 4064 O  O3  . GOL D 2 .   ? -5.408  -25.346 -63.750 1.00 41.17 ? 302 GOL A O3  1 
HETATM 4065 C  C1  . GOL E 2 .   ? -14.479 -28.594 -65.156 1.00 33.58 ? 303 GOL A C1  1 
HETATM 4066 O  O1  . GOL E 2 .   ? -13.925 -29.815 -65.631 1.00 25.85 ? 303 GOL A O1  1 
HETATM 4067 C  C2  . GOL E 2 .   ? -13.424 -27.613 -64.693 1.00 34.24 ? 303 GOL A C2  1 
HETATM 4068 O  O2  . GOL E 2 .   ? -12.822 -28.030 -63.461 1.00 34.06 ? 303 GOL A O2  1 
HETATM 4069 C  C3  . GOL E 2 .   ? -12.338 -27.381 -65.713 1.00 32.04 ? 303 GOL A C3  1 
HETATM 4070 O  O3  . GOL E 2 .   ? -11.349 -26.499 -65.187 1.00 29.47 ? 303 GOL A O3  1 
HETATM 4071 ZN ZN  . ZN  F 3 .   ? -12.100 -10.449 -2.785  1.00 73.05 2 301 ZN  B ZN  1 
HETATM 4072 C  C1  . GOL G 2 .   ? -19.182 -18.902 -25.609 1.00 35.75 ? 302 GOL B C1  1 
HETATM 4073 O  O1  . GOL G 2 .   ? -20.527 -19.023 -26.073 1.00 29.17 ? 302 GOL B O1  1 
HETATM 4074 C  C2  . GOL G 2 .   ? -18.622 -17.520 -25.857 1.00 34.41 ? 302 GOL B C2  1 
HETATM 4075 O  O2  . GOL G 2 .   ? -17.256 -17.409 -25.476 1.00 30.36 ? 302 GOL B O2  1 
HETATM 4076 C  C3  . GOL G 2 .   ? -18.716 -17.069 -27.298 1.00 31.77 ? 302 GOL B C3  1 
HETATM 4077 O  O3  . GOL G 2 .   ? -19.191 -15.731 -27.342 1.00 32.77 ? 302 GOL B O3  1 
HETATM 4078 C  C1  . GOL H 2 .   ? -18.623 -26.501 0.019   1.00 55.01 ? 303 GOL B C1  1 
HETATM 4079 O  O1  . GOL H 2 .   ? -18.922 -26.239 -1.349  1.00 46.59 ? 303 GOL B O1  1 
HETATM 4080 C  C2  . GOL H 2 .   ? -17.283 -27.177 0.135   1.00 58.88 ? 303 GOL B C2  1 
HETATM 4081 O  O2  . GOL H 2 .   ? -16.680 -27.141 -1.153  1.00 53.83 ? 303 GOL B O2  1 
HETATM 4082 C  C3  . GOL H 2 .   ? -16.362 -26.551 1.160   1.00 59.58 ? 303 GOL B C3  1 
HETATM 4083 O  O3  . GOL H 2 .   ? -15.029 -26.482 0.666   1.00 61.47 ? 303 GOL B O3  1 
HETATM 4084 O  O   . HOH I 4 .   ? -11.935 -4.620  -44.382 1.00 28.28 ? 401 HOH A O   1 
HETATM 4085 O  O   . HOH I 4 .   ? 4.836   -15.852 -48.269 1.00 25.03 ? 402 HOH A O   1 
HETATM 4086 O  O   . HOH I 4 .   ? 0.320   -17.554 -56.202 1.00 19.80 ? 403 HOH A O   1 
HETATM 4087 O  O   . HOH I 4 .   ? 18.375  -10.222 -71.245 1.00 32.78 ? 404 HOH A O   1 
HETATM 4088 O  O   . HOH I 4 .   ? -3.183  -20.716 -37.080 1.00 35.50 ? 405 HOH A O   1 
HETATM 4089 O  O   . HOH I 4 .   ? 10.866  -25.053 -71.159 1.00 27.27 ? 406 HOH A O   1 
HETATM 4090 O  O   . HOH I 4 .   ? -12.180 -6.854  -32.132 1.00 39.37 ? 407 HOH A O   1 
HETATM 4091 O  O   . HOH I 4 .   ? 10.087  -18.274 -64.070 1.00 18.35 ? 408 HOH A O   1 
HETATM 4092 O  O   . HOH I 4 .   ? 1.072   7.713   -58.358 1.00 42.20 ? 409 HOH A O   1 
HETATM 4093 O  O   . HOH I 4 .   ? -1.384  -22.647 -66.463 1.00 27.92 ? 410 HOH A O   1 
HETATM 4094 O  O   . HOH I 4 .   ? 3.365   8.668   -53.679 1.00 30.16 ? 411 HOH A O   1 
HETATM 4095 O  O   . HOH I 4 .   ? 3.483   -16.911 -55.790 1.00 18.53 ? 412 HOH A O   1 
HETATM 4096 O  O   . HOH I 4 .   ? -0.686  -12.635 -60.233 1.00 18.12 ? 413 HOH A O   1 
HETATM 4097 O  O   . HOH I 4 .   ? -15.125 -27.105 -36.967 1.00 43.44 ? 414 HOH A O   1 
HETATM 4098 O  O   . HOH I 4 .   ? -10.442 -24.016 -37.164 1.00 28.67 ? 415 HOH A O   1 
HETATM 4099 O  O   . HOH I 4 .   ? -3.347  -24.820 -42.098 1.00 28.37 ? 416 HOH A O   1 
HETATM 4100 O  O   . HOH I 4 .   ? 17.180  -17.252 -53.267 1.00 27.52 ? 417 HOH A O   1 
HETATM 4101 O  O   . HOH I 4 .   ? -3.814  -31.745 -60.255 1.00 29.72 ? 418 HOH A O   1 
HETATM 4102 O  O   . HOH I 4 .   ? 21.119  6.071   -63.880 1.00 45.08 ? 419 HOH A O   1 
HETATM 4103 O  O   . HOH I 4 .   ? 13.166  -23.755 -71.226 1.00 33.95 ? 420 HOH A O   1 
HETATM 4104 O  O   . HOH I 4 .   ? 24.219  12.387  -54.574 1.00 48.32 ? 421 HOH A O   1 
HETATM 4105 O  O   . HOH I 4 .   ? 14.139  -18.878 -50.536 1.00 30.97 ? 422 HOH A O   1 
HETATM 4106 O  O   . HOH I 4 .   ? 20.245  3.418   -49.037 1.00 31.29 ? 423 HOH A O   1 
HETATM 4107 O  O   . HOH I 4 .   ? -14.284 -9.005  -34.737 1.00 41.50 ? 424 HOH A O   1 
HETATM 4108 O  O   . HOH I 4 .   ? 18.148  -12.858 -51.015 1.00 28.37 ? 425 HOH A O   1 
HETATM 4109 O  O   . HOH I 4 .   ? 7.789   3.834   -64.371 1.00 24.73 ? 426 HOH A O   1 
HETATM 4110 O  O   . HOH I 4 .   ? 1.032   -29.487 -53.715 1.00 31.25 ? 427 HOH A O   1 
HETATM 4111 O  O   . HOH I 4 .   ? -21.057 -15.851 -43.152 1.00 36.05 ? 428 HOH A O   1 
HETATM 4112 O  O   . HOH I 4 .   ? 13.694  -23.996 -67.238 1.00 30.63 ? 429 HOH A O   1 
HETATM 4113 O  O   . HOH I 4 .   ? 8.627   7.065   -46.552 1.00 25.64 ? 430 HOH A O   1 
HETATM 4114 O  O   . HOH I 4 .   ? -7.113  -3.370  -40.168 1.00 22.24 ? 431 HOH A O   1 
HETATM 4115 O  O   . HOH I 4 .   ? 14.849  4.056   -64.418 1.00 36.73 ? 432 HOH A O   1 
HETATM 4116 O  O   . HOH I 4 .   ? 16.802  -13.506 -43.040 1.00 31.02 ? 433 HOH A O   1 
HETATM 4117 O  O   . HOH I 4 .   ? 1.172   -9.716  -66.767 1.00 20.44 ? 434 HOH A O   1 
HETATM 4118 O  O   . HOH I 4 .   ? -8.185  2.831   -41.389 1.00 36.80 ? 435 HOH A O   1 
HETATM 4119 O  O   . HOH I 4 .   ? -20.333 -17.526 -57.604 1.00 27.45 ? 436 HOH A O   1 
HETATM 4120 O  O   . HOH I 4 .   ? 7.687   -12.196 -41.951 1.00 33.84 ? 437 HOH A O   1 
HETATM 4121 O  O   . HOH I 4 .   ? -8.415  -25.321 -56.170 1.00 33.40 ? 438 HOH A O   1 
HETATM 4122 O  O   . HOH I 4 .   ? 5.619   5.958   -39.504 1.00 26.10 ? 439 HOH A O   1 
HETATM 4123 O  O   . HOH I 4 .   ? -5.693  -14.424 -66.035 1.00 20.42 ? 440 HOH A O   1 
HETATM 4124 O  O   . HOH I 4 .   ? 12.697  -15.624 -48.811 1.00 22.21 ? 441 HOH A O   1 
HETATM 4125 O  O   . HOH I 4 .   ? -14.033 -13.864 -39.593 1.00 32.08 ? 442 HOH A O   1 
HETATM 4126 O  O   . HOH I 4 .   ? 9.603   -11.979 -40.181 1.00 36.43 ? 443 HOH A O   1 
HETATM 4127 O  O   . HOH I 4 .   ? 22.634  -0.035  -57.059 1.00 27.67 ? 444 HOH A O   1 
HETATM 4128 O  O   . HOH I 4 .   ? 13.061  -11.610 -59.905 1.00 12.87 ? 445 HOH A O   1 
HETATM 4129 O  O   . HOH I 4 .   ? -0.595  2.560   -59.015 1.00 18.09 ? 446 HOH A O   1 
HETATM 4130 O  O   . HOH I 4 .   ? 13.362  6.202   -57.321 1.00 36.16 ? 447 HOH A O   1 
HETATM 4131 O  O   . HOH I 4 .   ? 21.108  -6.966  -38.050 1.00 33.88 ? 448 HOH A O   1 
HETATM 4132 O  O   . HOH I 4 .   ? 22.294  3.757   -62.556 1.00 25.05 ? 449 HOH A O   1 
HETATM 4133 O  O   . HOH I 4 .   ? 7.882   9.769   -38.291 1.00 42.15 ? 450 HOH A O   1 
HETATM 4134 O  O   . HOH I 4 .   ? -3.156  -15.848 -36.491 1.00 29.18 ? 451 HOH A O   1 
HETATM 4135 O  O   . HOH I 4 .   ? -20.612 -14.118 -56.006 1.00 21.73 ? 452 HOH A O   1 
HETATM 4136 O  O   . HOH I 4 .   ? -6.227  -35.635 -60.353 1.00 28.40 ? 453 HOH A O   1 
HETATM 4137 O  O   . HOH I 4 .   ? 10.538  -10.494 -45.971 1.00 15.72 ? 454 HOH A O   1 
HETATM 4138 O  O   . HOH I 4 .   ? -18.379 -26.812 -40.491 1.00 32.42 ? 455 HOH A O   1 
HETATM 4139 O  O   . HOH I 4 .   ? -14.972 -13.938 -60.324 1.00 27.81 ? 456 HOH A O   1 
HETATM 4140 O  O   . HOH I 4 .   ? 2.995   8.383   -50.089 1.00 29.98 ? 457 HOH A O   1 
HETATM 4141 O  O   . HOH I 4 .   ? -16.037 -8.054  -52.221 1.00 36.46 ? 458 HOH A O   1 
HETATM 4142 O  O   . HOH I 4 .   ? -4.410  0.862   -52.820 1.00 27.44 ? 459 HOH A O   1 
HETATM 4143 O  O   . HOH I 4 .   ? -8.346  -37.797 -61.173 1.00 22.39 ? 460 HOH A O   1 
HETATM 4144 O  O   . HOH I 4 .   ? -5.097  -25.694 -56.572 1.00 25.59 ? 461 HOH A O   1 
HETATM 4145 O  O   . HOH I 4 .   ? -7.041  -24.094 -61.366 1.00 32.93 ? 462 HOH A O   1 
HETATM 4146 O  O   . HOH I 4 .   ? 12.377  9.278   -52.155 1.00 32.02 ? 463 HOH A O   1 
HETATM 4147 O  O   . HOH I 4 .   ? 6.150   -9.567  -60.414 1.00 18.87 ? 464 HOH A O   1 
HETATM 4148 O  O   . HOH I 4 .   ? 15.982  -4.098  -67.091 1.00 37.14 ? 465 HOH A O   1 
HETATM 4149 O  O   . HOH I 4 .   ? -13.162 -12.029 -62.029 1.00 37.23 ? 466 HOH A O   1 
HETATM 4150 O  O   . HOH I 4 .   ? 14.973  -10.073 -36.033 1.00 36.55 ? 467 HOH A O   1 
HETATM 4151 O  O   . HOH I 4 .   ? 20.380  -3.306  -43.848 1.00 38.92 ? 468 HOH A O   1 
HETATM 4152 O  O   . HOH I 4 .   ? 6.506   -17.077 -52.880 1.00 12.77 ? 469 HOH A O   1 
HETATM 4153 O  O   . HOH I 4 .   ? 0.025   -11.024 -64.358 1.00 15.12 ? 470 HOH A O   1 
HETATM 4154 O  O   . HOH I 4 .   ? 1.640   -24.012 -58.233 1.00 25.45 ? 471 HOH A O   1 
HETATM 4155 O  O   . HOH I 4 .   ? 0.802   -13.631 -63.896 1.00 16.39 ? 472 HOH A O   1 
HETATM 4156 O  O   . HOH I 4 .   ? 16.466  9.378   -56.763 1.00 43.58 ? 473 HOH A O   1 
HETATM 4157 O  O   . HOH I 4 .   ? 8.347   -0.934  -68.081 1.00 33.12 ? 474 HOH A O   1 
HETATM 4158 O  O   . HOH I 4 .   ? -21.102 -11.293 -41.723 1.00 38.43 ? 475 HOH A O   1 
HETATM 4159 O  O   . HOH I 4 .   ? -12.051 -9.167  -61.036 1.00 35.22 ? 476 HOH A O   1 
HETATM 4160 O  O   . HOH I 4 .   ? 7.848   7.964   -39.766 1.00 35.55 ? 477 HOH A O   1 
HETATM 4161 O  O   . HOH I 4 .   ? 14.518  -15.454 -73.551 1.00 37.52 ? 478 HOH A O   1 
HETATM 4162 O  O   . HOH I 4 .   ? -4.933  -38.568 -56.018 1.00 27.91 ? 479 HOH A O   1 
HETATM 4163 O  O   . HOH I 4 .   ? -1.105  -20.688 -68.059 1.00 21.08 ? 480 HOH A O   1 
HETATM 4164 O  O   . HOH I 4 .   ? -11.579 0.764   -61.082 1.00 26.28 ? 481 HOH A O   1 
HETATM 4165 O  O   . HOH I 4 .   ? 10.077  5.156   -62.014 1.00 34.23 ? 482 HOH A O   1 
HETATM 4166 O  O   . HOH I 4 .   ? -13.987 -18.567 -56.941 1.00 36.49 ? 483 HOH A O   1 
HETATM 4167 O  O   . HOH I 4 .   ? 16.555  -16.307 -55.738 1.00 23.66 ? 484 HOH A O   1 
HETATM 4168 O  O   . HOH I 4 .   ? 8.582   10.886  -53.518 1.00 52.38 ? 485 HOH A O   1 
HETATM 4169 O  O   . HOH I 4 .   ? 3.328   -7.747  -66.833 1.00 30.09 ? 486 HOH A O   1 
HETATM 4170 O  O   . HOH I 4 .   ? 11.640  8.021   -54.704 1.00 24.54 ? 487 HOH A O   1 
HETATM 4171 O  O   . HOH I 4 .   ? 17.134  0.242   -66.061 1.00 29.12 ? 488 HOH A O   1 
HETATM 4172 O  O   . HOH I 4 .   ? -17.350 -27.674 -47.871 1.00 43.97 ? 489 HOH A O   1 
HETATM 4173 O  O   . HOH I 4 .   ? -5.835  1.563   -50.685 1.00 32.85 ? 490 HOH A O   1 
HETATM 4174 O  O   . HOH I 4 .   ? -14.338 -34.720 -50.203 1.00 45.97 ? 491 HOH A O   1 
HETATM 4175 O  O   . HOH I 4 .   ? 6.317   12.030  -50.713 1.00 21.75 ? 492 HOH A O   1 
HETATM 4176 O  O   . HOH I 4 .   ? 5.569   4.392   -62.158 1.00 19.43 ? 493 HOH A O   1 
HETATM 4177 O  O   . HOH I 4 .   ? 19.492  1.311   -66.263 1.00 35.74 ? 494 HOH A O   1 
HETATM 4178 O  O   . HOH I 4 .   ? -4.352  -6.431  -70.675 1.00 21.30 ? 495 HOH A O   1 
HETATM 4179 O  O   . HOH I 4 .   ? -9.008  -9.812  -74.039 1.00 54.46 ? 496 HOH A O   1 
HETATM 4180 O  O   . HOH I 4 .   ? 5.579   3.827   -45.094 1.00 24.79 ? 497 HOH A O   1 
HETATM 4181 O  O   . HOH I 4 .   ? -2.771  -18.247 -66.988 1.00 24.79 ? 498 HOH A O   1 
HETATM 4182 O  O   . HOH I 4 .   ? 10.419  -9.445  -36.980 1.00 30.74 ? 499 HOH A O   1 
HETATM 4183 O  O   . HOH I 4 .   ? 5.275   -8.999  -63.054 1.00 16.87 ? 500 HOH A O   1 
HETATM 4184 O  O   . HOH I 4 .   ? 17.369  -17.007 -65.702 1.00 19.97 ? 501 HOH A O   1 
HETATM 4185 O  O   . HOH I 4 .   ? 21.218  -12.480 -62.225 1.00 40.31 ? 502 HOH A O   1 
HETATM 4186 O  O   . HOH I 4 .   ? 2.539   -21.573 -61.079 1.00 35.71 ? 503 HOH A O   1 
HETATM 4187 O  O   . HOH I 4 .   ? -16.453 -22.709 -33.076 1.00 35.25 ? 504 HOH A O   1 
HETATM 4188 O  O   . HOH I 4 .   ? 5.914   -9.545  -66.034 1.00 10.50 ? 505 HOH A O   1 
HETATM 4189 O  O   . HOH I 4 .   ? -13.131 -17.002 -59.250 1.00 32.15 ? 506 HOH A O   1 
HETATM 4190 O  O   . HOH I 4 .   ? 0.807   -21.511 -54.796 1.00 37.39 ? 507 HOH A O   1 
HETATM 4191 O  O   . HOH I 4 .   ? -8.463  -19.457 -63.519 1.00 31.67 ? 508 HOH A O   1 
HETATM 4192 O  O   . HOH I 4 .   ? -18.915 -21.467 -51.442 1.00 48.38 ? 509 HOH A O   1 
HETATM 4193 O  O   . HOH I 4 .   ? 18.915  0.618   -37.258 1.00 46.31 ? 510 HOH A O   1 
HETATM 4194 O  O   . HOH I 4 .   ? 11.466  -11.309 -38.493 1.00 34.84 ? 511 HOH A O   1 
HETATM 4195 O  O   . HOH I 4 .   ? -5.369  -26.107 -36.728 1.00 42.30 ? 512 HOH A O   1 
HETATM 4196 O  O   . HOH I 4 .   ? 7.440   5.715   -59.674 1.00 19.33 ? 513 HOH A O   1 
HETATM 4197 O  O   . HOH I 4 .   ? -20.427 -15.376 -52.111 1.00 35.22 ? 514 HOH A O   1 
HETATM 4198 O  O   . HOH I 4 .   ? -10.967 -7.600  -62.865 1.00 35.01 ? 515 HOH A O   1 
HETATM 4199 O  O   . HOH I 4 .   ? -18.306 -5.178  -42.317 1.00 41.91 ? 516 HOH A O   1 
HETATM 4200 O  O   . HOH I 4 .   ? 9.598   -2.638  -32.604 1.00 45.42 ? 517 HOH A O   1 
HETATM 4201 O  O   . HOH I 4 .   ? -10.765 -25.867 -56.695 1.00 48.72 ? 518 HOH A O   1 
HETATM 4202 O  O   . HOH I 4 .   ? 22.750  -0.510  -54.231 1.00 27.14 ? 519 HOH A O   1 
HETATM 4203 O  O   . HOH I 4 .   ? 3.483   -30.074 -51.638 1.00 18.85 ? 520 HOH A O   1 
HETATM 4204 O  O   . HOH I 4 .   ? -8.439  -2.101  -69.240 1.00 42.30 ? 521 HOH A O   1 
HETATM 4205 O  O   . HOH I 4 .   ? 10.978  -13.652 -42.585 1.00 28.03 ? 522 HOH A O   1 
HETATM 4206 O  O   . HOH I 4 .   ? -9.336  -30.730 -39.698 1.00 44.66 ? 523 HOH A O   1 
HETATM 4207 O  O   . HOH I 4 .   ? -11.870 -22.953 -65.791 1.00 39.70 ? 524 HOH A O   1 
HETATM 4208 O  O   . HOH I 4 .   ? -13.406 -38.499 -59.637 1.00 39.08 ? 525 HOH A O   1 
HETATM 4209 O  O   . HOH I 4 .   ? -13.070 3.599   -49.891 1.00 46.12 ? 526 HOH A O   1 
HETATM 4210 O  O   . HOH I 4 .   ? 21.617  5.489   -47.938 1.00 50.29 ? 527 HOH A O   1 
HETATM 4211 O  O   . HOH I 4 .   ? -2.690  -36.335 -41.937 1.00 41.11 ? 528 HOH A O   1 
HETATM 4212 O  O   . HOH I 4 .   ? -8.263  -15.127 -66.705 1.00 35.83 ? 529 HOH A O   1 
HETATM 4213 O  O   . HOH I 4 .   ? -4.087  -34.495 -59.419 1.00 40.52 ? 530 HOH A O   1 
HETATM 4214 O  O   . HOH I 4 .   ? 14.041  8.476   -55.568 1.00 46.89 ? 531 HOH A O   1 
HETATM 4215 O  O   . HOH I 4 .   ? -2.572  3.389   -57.035 1.00 30.01 ? 532 HOH A O   1 
HETATM 4216 O  O   . HOH I 4 .   ? 11.491  4.820   -63.886 1.00 45.80 ? 533 HOH A O   1 
HETATM 4217 O  O   . HOH I 4 .   ? -12.516 -18.041 -61.602 1.00 47.30 ? 534 HOH A O   1 
HETATM 4218 O  O   . HOH I 4 .   ? 2.520   11.733  -38.467 1.00 39.19 ? 535 HOH A O   1 
HETATM 4219 O  O   . HOH I 4 .   ? -3.924  -27.076 -40.693 1.00 39.93 ? 536 HOH A O   1 
HETATM 4220 O  O   . HOH I 4 .   ? 24.756  1.625   -56.854 1.00 35.07 ? 537 HOH A O   1 
HETATM 4221 O  O   . HOH I 4 .   ? 12.617  -14.313 -40.465 1.00 38.45 ? 538 HOH A O   1 
HETATM 4222 O  O   . HOH J 4 .   ? -24.043 -38.183 -4.487  1.00 30.17 ? 401 HOH B O   1 
HETATM 4223 O  O   . HOH J 4 .   ? -12.424 -9.025  -28.557 1.00 45.42 ? 402 HOH B O   1 
HETATM 4224 O  O   . HOH J 4 .   ? -21.087 -14.630 -28.332 1.00 30.32 ? 403 HOH B O   1 
HETATM 4225 O  O   . HOH J 4 .   ? -1.769  -36.646 -20.909 1.00 28.54 ? 404 HOH B O   1 
HETATM 4226 O  O   . HOH J 4 .   ? -31.805 -15.446 -6.492  1.00 28.64 ? 405 HOH B O   1 
HETATM 4227 O  O   . HOH J 4 .   ? -8.606  -27.079 -31.733 1.00 31.49 ? 406 HOH B O   1 
HETATM 4228 O  O   . HOH J 4 .   ? -10.067 -29.707 -16.418 1.00 28.61 ? 407 HOH B O   1 
HETATM 4229 O  O   . HOH J 4 .   ? 6.584   -19.942 -37.542 1.00 27.76 ? 408 HOH B O   1 
HETATM 4230 O  O   . HOH J 4 .   ? -17.492 -19.390 -29.729 1.00 32.04 ? 409 HOH B O   1 
HETATM 4231 O  O   . HOH J 4 .   ? -13.818 -23.977 -22.833 1.00 25.06 ? 410 HOH B O   1 
HETATM 4232 O  O   . HOH J 4 .   ? -29.270 -8.076  -11.137 1.00 41.31 ? 411 HOH B O   1 
HETATM 4233 O  O   . HOH J 4 .   ? -3.585  -34.927 -37.703 1.00 36.50 ? 412 HOH B O   1 
HETATM 4234 O  O   . HOH J 4 .   ? -23.637 -27.636 -22.269 1.00 34.31 ? 413 HOH B O   1 
HETATM 4235 O  O   . HOH J 4 .   ? 7.014   -36.088 -27.889 1.00 43.22 ? 414 HOH B O   1 
HETATM 4236 O  O   . HOH J 4 .   ? -8.965  -6.581  -6.278  1.00 32.30 ? 415 HOH B O   1 
HETATM 4237 O  O   . HOH J 4 .   ? 1.295   -30.515 -5.038  1.00 35.89 ? 416 HOH B O   1 
HETATM 4238 O  O   . HOH J 4 .   ? 2.595   -12.369 -18.719 1.00 32.61 ? 417 HOH B O   1 
HETATM 4239 O  O   . HOH J 4 .   ? 0.269   -7.617  -15.971 1.00 44.03 ? 418 HOH B O   1 
HETATM 4240 O  O   . HOH J 4 .   ? -21.956 -18.258 -28.060 1.00 27.65 ? 419 HOH B O   1 
HETATM 4241 O  O   . HOH J 4 .   ? -17.763 -22.013 2.079   1.00 37.18 ? 420 HOH B O   1 
HETATM 4242 O  O   . HOH J 4 .   ? -32.065 -16.403 -11.081 1.00 36.78 ? 421 HOH B O   1 
HETATM 4243 O  O   . HOH J 4 .   ? -9.061  -27.940 -10.349 1.00 20.59 ? 422 HOH B O   1 
HETATM 4244 O  O   . HOH J 4 .   ? -10.487 -3.433  -11.791 1.00 43.63 ? 423 HOH B O   1 
HETATM 4245 O  O   . HOH J 4 .   ? -25.716 -7.628  -2.106  1.00 36.78 ? 424 HOH B O   1 
HETATM 4246 O  O   . HOH J 4 .   ? -27.630 -22.766 -18.729 1.00 28.48 ? 425 HOH B O   1 
HETATM 4247 O  O   . HOH J 4 .   ? -3.302  -44.799 -31.662 1.00 39.32 ? 426 HOH B O   1 
HETATM 4248 O  O   . HOH J 4 .   ? -1.583  -5.705  -16.687 1.00 39.27 ? 427 HOH B O   1 
HETATM 4249 O  O   . HOH J 4 .   ? -26.740 -27.623 -19.218 1.00 37.92 ? 428 HOH B O   1 
HETATM 4250 O  O   . HOH J 4 .   ? -4.083  -32.627 -6.639  1.00 30.69 ? 429 HOH B O   1 
HETATM 4251 O  O   . HOH J 4 .   ? -19.089 -34.148 -0.677  1.00 34.56 ? 430 HOH B O   1 
HETATM 4252 O  O   . HOH J 4 .   ? -21.982 -24.075 -21.886 1.00 23.88 ? 431 HOH B O   1 
HETATM 4253 O  O   . HOH J 4 .   ? 11.503  -21.393 -26.704 1.00 31.24 ? 432 HOH B O   1 
HETATM 4254 O  O   . HOH J 4 .   ? -19.863 -18.192 -21.411 1.00 22.31 ? 433 HOH B O   1 
HETATM 4255 O  O   . HOH J 4 .   ? -27.934 -31.796 -4.034  1.00 26.64 ? 434 HOH B O   1 
HETATM 4256 O  O   . HOH J 4 .   ? -4.810  -36.653 -21.090 1.00 30.06 ? 435 HOH B O   1 
HETATM 4257 O  O   . HOH J 4 .   ? 10.696  -25.206 -18.695 1.00 47.32 ? 436 HOH B O   1 
HETATM 4258 O  O   . HOH J 4 .   ? -21.261 -24.465 -25.706 1.00 25.88 ? 437 HOH B O   1 
HETATM 4259 O  O   . HOH J 4 .   ? 6.719   -20.342 -14.985 1.00 34.50 ? 438 HOH B O   1 
HETATM 4260 O  O   . HOH J 4 .   ? 6.224   -12.846 -24.333 1.00 30.04 ? 439 HOH B O   1 
HETATM 4261 O  O   . HOH J 4 .   ? 0.860   -24.362 -35.912 1.00 31.18 ? 440 HOH B O   1 
HETATM 4262 O  O   . HOH J 4 .   ? -23.594 -28.289 -2.209  1.00 26.61 ? 441 HOH B O   1 
HETATM 4263 O  O   . HOH J 4 .   ? -13.113 -32.217 -32.762 1.00 50.20 ? 442 HOH B O   1 
HETATM 4264 O  O   . HOH J 4 .   ? -12.390 -6.463  -4.309  1.00 37.15 ? 443 HOH B O   1 
HETATM 4265 O  O   . HOH J 4 .   ? -17.418 -28.710 -27.564 1.00 34.14 ? 444 HOH B O   1 
HETATM 4266 O  O   . HOH J 4 .   ? -13.096 -28.867 -16.764 1.00 26.24 ? 445 HOH B O   1 
HETATM 4267 O  O   . HOH J 4 .   ? -19.277 -21.809 -26.711 1.00 28.42 ? 446 HOH B O   1 
HETATM 4268 O  O   . HOH J 4 .   ? 3.093   -34.571 -38.383 1.00 28.31 ? 447 HOH B O   1 
HETATM 4269 O  O   . HOH J 4 .   ? -15.727 -25.212 -8.806  1.00 25.64 ? 448 HOH B O   1 
HETATM 4270 O  O   . HOH J 4 .   ? -1.963  -8.884  -21.927 1.00 21.66 ? 449 HOH B O   1 
HETATM 4271 O  O   . HOH J 4 .   ? -10.791 -28.777 -3.601  1.00 27.59 ? 450 HOH B O   1 
HETATM 4272 O  O   . HOH J 4 .   ? -7.428  -20.758 1.513   1.00 45.71 ? 451 HOH B O   1 
HETATM 4273 O  O   . HOH J 4 .   ? -3.887  -39.391 -35.664 1.00 34.01 ? 452 HOH B O   1 
HETATM 4274 O  O   . HOH J 4 .   ? -22.667 -26.609 -10.457 1.00 25.16 ? 453 HOH B O   1 
HETATM 4275 O  O   . HOH J 4 .   ? -10.177 -30.645 -7.904  1.00 22.75 ? 454 HOH B O   1 
HETATM 4276 O  O   . HOH J 4 .   ? -31.405 -15.421 0.093   1.00 35.08 ? 455 HOH B O   1 
HETATM 4277 O  O   . HOH J 4 .   ? -11.712 -4.698  -8.176  1.00 29.50 ? 456 HOH B O   1 
HETATM 4278 O  O   . HOH J 4 .   ? 5.202   -29.298 -11.116 1.00 30.31 ? 457 HOH B O   1 
HETATM 4279 O  O   . HOH J 4 .   ? -16.928 -16.064 2.185   1.00 36.21 ? 458 HOH B O   1 
HETATM 4280 O  O   . HOH J 4 .   ? 2.300   -37.832 -32.263 1.00 26.90 ? 459 HOH B O   1 
HETATM 4281 O  O   . HOH J 4 .   ? -26.143 -28.233 -16.483 1.00 26.17 ? 460 HOH B O   1 
HETATM 4282 O  O   . HOH J 4 .   ? -6.393  -27.717 -32.508 1.00 27.81 ? 461 HOH B O   1 
HETATM 4283 O  O   . HOH J 4 .   ? -22.402 -4.820  -29.642 1.00 48.82 ? 462 HOH B O   1 
HETATM 4284 O  O   . HOH J 4 .   ? 6.799   -23.259 -22.804 1.00 38.78 ? 463 HOH B O   1 
HETATM 4285 O  O   . HOH J 4 .   ? 8.780   -28.855 -34.896 1.00 33.25 ? 464 HOH B O   1 
HETATM 4286 O  O   . HOH J 4 .   ? -19.145 -13.302 0.331   1.00 34.09 ? 465 HOH B O   1 
HETATM 4287 O  O   . HOH J 4 .   ? -8.617  -14.249 -3.269  1.00 25.22 ? 466 HOH B O   1 
HETATM 4288 O  O   . HOH J 4 .   ? -14.730 -5.972  -14.507 1.00 26.84 ? 467 HOH B O   1 
HETATM 4289 O  O   . HOH J 4 .   ? -16.507 -12.249 -1.184  1.00 31.75 ? 468 HOH B O   1 
HETATM 4290 O  O   . HOH J 4 .   ? 2.866   -27.057 -8.350  1.00 48.69 ? 469 HOH B O   1 
HETATM 4291 O  O   . HOH J 4 .   ? -30.482 -10.835 -26.283 1.00 31.91 ? 470 HOH B O   1 
HETATM 4292 O  O   . HOH J 4 .   ? 11.109  -26.711 -15.109 1.00 30.09 ? 471 HOH B O   1 
HETATM 4293 O  O   . HOH J 4 .   ? -15.564 -27.397 -19.107 1.00 16.24 ? 472 HOH B O   1 
HETATM 4294 O  O   . HOH J 4 .   ? -0.927  -44.023 -30.447 1.00 32.50 ? 473 HOH B O   1 
HETATM 4295 O  O   . HOH J 4 .   ? -27.850 -4.370  -21.944 1.00 45.10 ? 474 HOH B O   1 
HETATM 4296 O  O   . HOH J 4 .   ? -20.763 -7.344  -4.239  1.00 35.20 ? 475 HOH B O   1 
HETATM 4297 O  O   . HOH J 4 .   ? -21.533 -28.957 -18.956 1.00 33.45 ? 476 HOH B O   1 
HETATM 4298 O  O   . HOH J 4 .   ? 4.873   -36.357 -25.371 1.00 39.54 ? 477 HOH B O   1 
HETATM 4299 O  O   . HOH J 4 .   ? -17.235 -13.005 -29.015 1.00 32.07 ? 478 HOH B O   1 
HETATM 4300 O  O   . HOH J 4 .   ? -26.866 -34.211 -8.693  1.00 33.65 ? 479 HOH B O   1 
HETATM 4301 O  O   . HOH J 4 .   ? -15.447 -28.237 -3.857  1.00 22.84 ? 480 HOH B O   1 
HETATM 4302 O  O   . HOH J 4 .   ? 7.410   -33.653 -28.957 1.00 34.84 ? 481 HOH B O   1 
HETATM 4303 O  O   . HOH J 4 .   ? 5.013   -31.456 -24.551 1.00 25.91 ? 482 HOH B O   1 
HETATM 4304 O  O   . HOH J 4 .   ? -2.097  -35.630 -12.015 1.00 35.27 ? 483 HOH B O   1 
HETATM 4305 O  O   . HOH J 4 .   ? -7.572  -8.321  -25.975 1.00 36.20 ? 484 HOH B O   1 
HETATM 4306 O  O   . HOH J 4 .   ? -14.737 -26.168 -6.183  1.00 22.23 ? 485 HOH B O   1 
HETATM 4307 O  O   . HOH J 4 .   ? 3.473   -31.051 -14.045 1.00 36.48 ? 486 HOH B O   1 
HETATM 4308 O  O   . HOH J 4 .   ? -20.629 -25.208 0.876   1.00 40.50 ? 487 HOH B O   1 
HETATM 4309 O  O   . HOH J 4 .   ? 4.627   -17.756 -28.290 1.00 27.50 ? 488 HOH B O   1 
HETATM 4310 O  O   . HOH J 4 .   ? -18.960 -38.231 -2.076  1.00 40.72 ? 489 HOH B O   1 
HETATM 4311 O  O   . HOH J 4 .   ? 4.247   -31.437 -16.497 1.00 37.19 ? 490 HOH B O   1 
HETATM 4312 O  O   . HOH J 4 .   ? 8.904   -13.583 -27.769 1.00 39.00 ? 491 HOH B O   1 
HETATM 4313 O  O   . HOH J 4 .   ? -9.721  -28.609 -6.152  1.00 21.95 ? 492 HOH B O   1 
HETATM 4314 O  O   . HOH J 4 .   ? -19.406 -12.356 -28.526 1.00 31.44 ? 493 HOH B O   1 
HETATM 4315 O  O   . HOH J 4 .   ? -2.965  -12.475 -5.043  1.00 28.87 ? 494 HOH B O   1 
HETATM 4316 O  O   . HOH J 4 .   ? -12.033 -21.504 0.957   1.00 33.94 ? 495 HOH B O   1 
HETATM 4317 O  O   . HOH J 4 .   ? -11.114 -39.699 -8.267  1.00 47.46 ? 496 HOH B O   1 
HETATM 4318 O  O   . HOH J 4 .   ? -15.442 -1.432  -5.466  1.00 34.50 ? 497 HOH B O   1 
HETATM 4319 O  O   . HOH J 4 .   ? -30.555 -22.672 -21.202 1.00 41.21 ? 498 HOH B O   1 
HETATM 4320 O  O   . HOH J 4 .   ? -15.024 -14.555 0.351   1.00 23.07 ? 499 HOH B O   1 
HETATM 4321 O  O   . HOH J 4 .   ? -13.266 -27.064 -2.401  1.00 36.46 ? 500 HOH B O   1 
HETATM 4322 O  O   . HOH J 4 .   ? 0.280   -30.977 -37.247 1.00 36.42 ? 501 HOH B O   1 
HETATM 4323 O  O   . HOH J 4 .   ? -35.868 -21.685 -3.277  1.00 37.12 ? 502 HOH B O   1 
HETATM 4324 O  O   . HOH J 4 .   ? -10.416 -32.439 -20.137 1.00 40.87 ? 503 HOH B O   1 
HETATM 4325 O  O   . HOH J 4 .   ? 0.283   -7.630  -10.919 1.00 46.50 ? 504 HOH B O   1 
HETATM 4326 O  O   . HOH J 4 .   ? 11.746  -16.460 -25.096 1.00 42.09 ? 505 HOH B O   1 
HETATM 4327 O  O   . HOH J 4 .   ? -1.424  -33.896 -6.729  1.00 44.58 ? 506 HOH B O   1 
HETATM 4328 O  O   . HOH J 4 .   ? -6.275  -7.510  -27.947 1.00 42.92 ? 507 HOH B O   1 
HETATM 4329 O  O   . HOH J 4 .   ? -30.129 -11.494 -21.798 1.00 31.18 ? 508 HOH B O   1 
HETATM 4330 O  O   . HOH J 4 .   ? -26.976 -19.733 1.323   1.00 46.66 ? 509 HOH B O   1 
HETATM 4331 O  O   . HOH J 4 .   ? -16.059 7.375   -15.765 1.00 47.99 ? 510 HOH B O   1 
HETATM 4332 O  O   . HOH J 4 .   ? 7.307   -30.389 -24.717 1.00 33.84 ? 511 HOH B O   1 
HETATM 4333 O  O   . HOH J 4 .   ? -20.922 -22.636 -28.934 1.00 40.90 ? 512 HOH B O   1 
HETATM 4334 O  O   . HOH J 4 .   ? -21.696 -23.056 1.229   1.00 42.31 ? 513 HOH B O   1 
HETATM 4335 O  O   . HOH J 4 .   ? -26.607 -24.531 0.157   1.00 45.54 ? 514 HOH B O   1 
HETATM 4336 O  O   . HOH J 4 .   ? -33.269 -4.743  -2.371  1.00 43.49 ? 515 HOH B O   1 
HETATM 4337 O  O   . HOH J 4 .   ? -12.127 -17.159 2.865   1.00 50.45 ? 516 HOH B O   1 
HETATM 4338 O  O   . HOH J 4 .   ? 7.165   -14.538 -9.151  1.00 29.81 ? 517 HOH B O   1 
HETATM 4339 O  O   . HOH J 4 .   ? -7.100  -12.671 -4.460  1.00 41.76 ? 518 HOH B O   1 
HETATM 4340 O  O   . HOH J 4 .   ? -7.292  -21.297 -37.006 1.00 34.37 ? 519 HOH B O   1 
HETATM 4341 O  O   . HOH J 4 .   ? -27.503 -14.517 -26.499 1.00 54.29 ? 520 HOH B O   1 
HETATM 4342 O  O   . HOH J 4 .   ? 5.570   -10.570 -16.302 1.00 43.47 ? 521 HOH B O   1 
HETATM 4343 O  O   . HOH J 4 .   ? 5.399   -33.951 -24.224 1.00 42.84 ? 522 HOH B O   1 
HETATM 4344 O  O   . HOH J 4 .   ? 2.833   -37.466 -9.418  1.00 44.65 ? 523 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   . GLY A 1   ? 0.7632 0.6669 0.7863 -0.0975 0.0296  -0.0124 27  GLY A N   
2    C CA  . GLY A 1   ? 0.7322 0.6450 0.7606 -0.1109 0.0253  -0.0201 27  GLY A CA  
3    C C   . GLY A 1   ? 0.6942 0.6366 0.7284 -0.1085 0.0184  -0.0223 27  GLY A C   
4    O O   . GLY A 1   ? 0.5716 0.5293 0.6092 -0.0996 0.0187  -0.0162 27  GLY A O   
5    N N   . ASP A 2   ? 0.6653 0.6145 0.6994 -0.1163 0.0121  -0.0311 28  ASP A N   
6    C CA  . ASP A 2   ? 0.6394 0.6177 0.6809 -0.1160 0.0051  -0.0326 28  ASP A CA  
7    C C   . ASP A 2   ? 0.5232 0.5089 0.5598 -0.1006 0.0034  -0.0302 28  ASP A C   
8    O O   . ASP A 2   ? 0.4464 0.4528 0.4912 -0.0953 0.0026  -0.0253 28  ASP A O   
9    C CB  . ASP A 2   ? 0.7012 0.6845 0.7413 -0.1269 -0.0022 -0.0423 28  ASP A CB  
10   C CG  . ASP A 2   ? 0.7979 0.7936 0.8508 -0.1433 -0.0040 -0.0433 28  ASP A CG  
11   O OD1 . ASP A 2   ? 0.7938 0.7867 0.8548 -0.1479 0.0023  -0.0371 28  ASP A OD1 
12   O OD2 . ASP A 2   ? 0.9166 0.9263 0.9714 -0.1518 -0.0118 -0.0499 28  ASP A OD2 
13   N N   . LEU A 3   ? 0.5015 0.4697 0.5251 -0.0937 0.0038  -0.0337 29  LEU A N   
14   C CA  . LEU A 3   ? 0.4421 0.4173 0.4610 -0.0808 0.0018  -0.0321 29  LEU A CA  
15   C C   . LEU A 3   ? 0.3796 0.3570 0.4016 -0.0717 0.0067  -0.0233 29  LEU A C   
16   O O   . LEU A 3   ? 0.3454 0.3383 0.3702 -0.0643 0.0049  -0.0204 29  LEU A O   
17   C CB  . LEU A 3   ? 0.4736 0.4298 0.4787 -0.0768 0.0020  -0.0379 29  LEU A CB  
18   C CG  . LEU A 3   ? 0.4999 0.4650 0.4990 -0.0676 -0.0021 -0.0390 29  LEU A CG  
19   C CD1 . LEU A 3   ? 0.4968 0.4854 0.5007 -0.0703 -0.0096 -0.0408 29  LEU A CD1 
20   C CD2 . LEU A 3   ? 0.5301 0.4757 0.5153 -0.0658 -0.0008 -0.0455 29  LEU A CD2 
21   N N   . ALA A 4   ? 0.3473 0.3087 0.3682 -0.0725 0.0128  -0.0191 30  ALA A N   
22   C CA  . ALA A 4   ? 0.3175 0.2813 0.3399 -0.0652 0.0170  -0.0106 30  ALA A CA  
23   C C   . ALA A 4   ? 0.3002 0.2864 0.3329 -0.0671 0.0169  -0.0068 30  ALA A C   
24   O O   . ALA A 4   ? 0.3049 0.3013 0.3377 -0.0590 0.0174  -0.0034 30  ALA A O   
25   C CB  . ALA A 4   ? 0.3225 0.2667 0.3423 -0.0668 0.0230  -0.0057 30  ALA A CB  
26   N N   . ASP A 5   ? 0.3000 0.2942 0.3416 -0.0780 0.0165  -0.0081 31  ASP A N   
27   C CA  . ASP A 5   ? 0.2947 0.3121 0.3483 -0.0801 0.0173  -0.0045 31  ASP A CA  
28   C C   . ASP A 5   ? 0.2728 0.3100 0.3298 -0.0732 0.0121  -0.0068 31  ASP A C   
29   O O   . ASP A 5   ? 0.2633 0.3148 0.3251 -0.0671 0.0142  -0.0028 31  ASP A O   
30   C CB  . ASP A 5   ? 0.3075 0.3307 0.3715 -0.0940 0.0179  -0.0051 31  ASP A CB  
31   C CG  . ASP A 5   ? 0.3355 0.3402 0.3980 -0.1014 0.0242  -0.0010 31  ASP A CG  
32   O OD1 . ASP A 5   ? 0.3739 0.3721 0.4324 -0.0956 0.0297  0.0060  31  ASP A OD1 
33   O OD2 . ASP A 5   ? 0.3781 0.3746 0.4429 -0.1131 0.0236  -0.0047 31  ASP A OD2 
34   N N   . ARG A 6   ? 0.2807 0.3177 0.3342 -0.0740 0.0057  -0.0130 32  ARG A N   
35   C CA  . ARG A 6   ? 0.3024 0.3564 0.3581 -0.0672 0.0005  -0.0143 32  ARG A CA  
36   C C   . ARG A 6   ? 0.2694 0.3190 0.3178 -0.0542 0.0027  -0.0113 32  ARG A C   
37   O O   . ARG A 6   ? 0.2397 0.3040 0.2932 -0.0476 0.0027  -0.0088 32  ARG A O   
38   C CB  . ARG A 6   ? 0.3424 0.3956 0.3930 -0.0706 -0.0068 -0.0211 32  ARG A CB  
39   C CG  . ARG A 6   ? 0.4484 0.5118 0.5078 -0.0843 -0.0105 -0.0245 32  ARG A CG  
40   C CD  . ARG A 6   ? 0.5271 0.5910 0.5800 -0.0896 -0.0184 -0.0319 32  ARG A CD  
41   N NE  . ARG A 6   ? 0.6155 0.6957 0.6682 -0.0807 -0.0242 -0.0310 32  ARG A NE  
42   C CZ  . ARG A 6   ? 0.7005 0.7802 0.7435 -0.0808 -0.0307 -0.0359 32  ARG A CZ  
43   N NH1 . ARG A 6   ? 0.7169 0.7823 0.7500 -0.0903 -0.0326 -0.0435 32  ARG A NH1 
44   N NH2 . ARG A 6   ? 0.7333 0.8254 0.7753 -0.0712 -0.0347 -0.0332 32  ARG A NH2 
45   N N   . PHE A 7   ? 0.2639 0.2932 0.3009 -0.0508 0.0048  -0.0116 33  PHE A N   
46   C CA  . PHE A 7   ? 0.2466 0.2714 0.2766 -0.0403 0.0065  -0.0092 33  PHE A CA  
47   C C   . PHE A 7   ? 0.2280 0.2585 0.2615 -0.0374 0.0117  -0.0036 33  PHE A C   
48   O O   . PHE A 7   ? 0.2195 0.2552 0.2512 -0.0298 0.0125  -0.0021 33  PHE A O   
49   C CB  . PHE A 7   ? 0.2519 0.2563 0.2712 -0.0380 0.0077  -0.0101 33  PHE A CB  
50   C CG  . PHE A 7   ? 0.2661 0.2642 0.2787 -0.0379 0.0036  -0.0159 33  PHE A CG  
51   C CD1 . PHE A 7   ? 0.2656 0.2747 0.2776 -0.0346 -0.0013 -0.0181 33  PHE A CD1 
52   C CD2 . PHE A 7   ? 0.2864 0.2664 0.2923 -0.0404 0.0052  -0.0187 33  PHE A CD2 
53   C CE1 . PHE A 7   ? 0.2830 0.2863 0.2870 -0.0350 -0.0047 -0.0232 33  PHE A CE1 
54   C CE2 . PHE A 7   ? 0.3014 0.2752 0.2997 -0.0404 0.0024  -0.0246 33  PHE A CE2 
55   C CZ  . PHE A 7   ? 0.2982 0.2838 0.2948 -0.0379 -0.0026 -0.0268 33  PHE A CZ  
56   N N   . ALA A 8   ? 0.2237 0.2521 0.2610 -0.0439 0.0158  -0.0006 34  ALA A N   
57   C CA  . ALA A 8   ? 0.2171 0.2517 0.2564 -0.0420 0.0213  0.0048  34  ALA A CA  
58   C C   . ALA A 8   ? 0.2036 0.2593 0.2526 -0.0399 0.0217  0.0048  34  ALA A C   
59   O O   . ALA A 8   ? 0.2067 0.2675 0.2541 -0.0339 0.0254  0.0072  34  ALA A O   
60   C CB  . ALA A 8   ? 0.2255 0.2537 0.2668 -0.0498 0.0258  0.0088  34  ALA A CB  
61   N N   . GLU A 9   ? 0.1988 0.2674 0.2582 -0.0450 0.0181  0.0024  35  GLU A N   
62   C CA  . GLU A 9   ? 0.1967 0.2874 0.2676 -0.0420 0.0182  0.0032  35  GLU A CA  
63   C C   . GLU A 9   ? 0.1933 0.2854 0.2595 -0.0308 0.0158  0.0018  35  GLU A C   
64   O O   . GLU A 9   ? 0.1917 0.2954 0.2629 -0.0242 0.0190  0.0036  35  GLU A O   
65   C CB  . GLU A 9   ? 0.1994 0.3050 0.2828 -0.0506 0.0135  0.0012  35  GLU A CB  
66   C CG  . GLU A 9   ? 0.2011 0.3332 0.3000 -0.0480 0.0140  0.0034  35  GLU A CG  
67   C CD  . GLU A 9   ? 0.1960 0.3376 0.2962 -0.0389 0.0085  0.0021  35  GLU A CD  
68   O OE1 . GLU A 9   ? 0.1943 0.3232 0.2836 -0.0364 0.0035  -0.0009 35  GLU A OE1 
69   O OE2 . GLU A 9   ? 0.1997 0.3614 0.3120 -0.0334 0.0101  0.0049  35  GLU A OE2 
70   N N   . LEU A 10  ? 0.1977 0.2777 0.2545 -0.0285 0.0108  -0.0013 36  LEU A N   
71   C CA  . LEU A 10  ? 0.2112 0.2896 0.2623 -0.0185 0.0092  -0.0018 36  LEU A CA  
72   C C   . LEU A 10  ? 0.2050 0.2761 0.2493 -0.0126 0.0152  0.0002  36  LEU A C   
73   O O   . LEU A 10  ? 0.2040 0.2804 0.2491 -0.0051 0.0170  0.0006  36  LEU A O   
74   C CB  . LEU A 10  ? 0.2290 0.2941 0.2700 -0.0181 0.0043  -0.0049 36  LEU A CB  
75   C CG  . LEU A 10  ? 0.2526 0.3264 0.2962 -0.0189 -0.0027 -0.0073 36  LEU A CG  
76   C CD1 . LEU A 10  ? 0.2695 0.3579 0.3244 -0.0273 -0.0052 -0.0080 36  LEU A CD1 
77   C CD2 . LEU A 10  ? 0.2659 0.3238 0.2973 -0.0198 -0.0057 -0.0107 36  LEU A CD2 
78   N N   . GLU A 11  ? 0.1962 0.2549 0.2335 -0.0161 0.0180  0.0014  37  GLU A N   
79   C CA  . GLU A 11  ? 0.2043 0.2566 0.2334 -0.0118 0.0226  0.0032  37  GLU A CA  
80   C C   . GLU A 11  ? 0.2062 0.2712 0.2410 -0.0100 0.0285  0.0049  37  GLU A C   
81   O O   . GLU A 11  ? 0.1990 0.2633 0.2287 -0.0036 0.0316  0.0043  37  GLU A O   
82   C CB  . GLU A 11  ? 0.2091 0.2485 0.2305 -0.0156 0.0242  0.0057  37  GLU A CB  
83   C CG  . GLU A 11  ? 0.2208 0.2467 0.2353 -0.0148 0.0200  0.0042  37  GLU A CG  
84   C CD  . GLU A 11  ? 0.2193 0.2335 0.2274 -0.0166 0.0217  0.0077  37  GLU A CD  
85   O OE1 . GLU A 11  ? 0.2554 0.2687 0.2664 -0.0219 0.0245  0.0108  37  GLU A OE1 
86   O OE2 . GLU A 11  ? 0.2153 0.2215 0.2164 -0.0129 0.0200  0.0077  37  GLU A OE2 
87   N N   . ARG A 12  ? 0.2111 0.2872 0.2563 -0.0159 0.0306  0.0069  38  ARG A N   
88   C CA  . ARG A 12  ? 0.2114 0.3015 0.2634 -0.0146 0.0373  0.0089  38  ARG A CA  
89   C C   . ARG A 12  ? 0.2068 0.3091 0.2662 -0.0064 0.0370  0.0071  38  ARG A C   
90   O O   . ARG A 12  ? 0.2149 0.3197 0.2721 0.0002  0.0427  0.0069  38  ARG A O   
91   C CB  . ARG A 12  ? 0.2184 0.3200 0.2823 -0.0236 0.0398  0.0118  38  ARG A CB  
92   C CG  . ARG A 12  ? 0.2304 0.3194 0.2875 -0.0312 0.0418  0.0150  38  ARG A CG  
93   C CD  . ARG A 12  ? 0.2368 0.3370 0.3048 -0.0398 0.0466  0.0188  38  ARG A CD  
94   N NE  . ARG A 12  ? 0.2496 0.3620 0.3322 -0.0461 0.0423  0.0171  38  ARG A NE  
95   C CZ  . ARG A 12  ? 0.2732 0.3767 0.3565 -0.0543 0.0373  0.0155  38  ARG A CZ  
96   N NH1 . ARG A 12  ? 0.2879 0.3697 0.3588 -0.0554 0.0364  0.0156  38  ARG A NH1 
97   N NH2 . ARG A 12  ? 0.2917 0.4084 0.3880 -0.0613 0.0332  0.0134  38  ARG A NH2 
98   N N   . ARG A 13  ? 0.1794 0.2890 0.2471 -0.0066 0.0305  0.0060  39  ARG A N   
99   C CA  . ARG A 13  ? 0.1837 0.3069 0.2605 0.0015  0.0298  0.0059  39  ARG A CA  
100  C C   . ARG A 13  ? 0.1981 0.3087 0.2639 0.0114  0.0304  0.0042  39  ARG A C   
101  O O   . ARG A 13  ? 0.2208 0.3373 0.2902 0.0198  0.0347  0.0045  39  ARG A O   
102  C CB  . ARG A 13  ? 0.1766 0.3111 0.2633 -0.0023 0.0217  0.0058  39  ARG A CB  
103  C CG  . ARG A 13  ? 0.1816 0.3322 0.2788 0.0066  0.0199  0.0073  39  ARG A CG  
104  C CD  . ARG A 13  ? 0.1862 0.3575 0.2984 0.0004  0.0133  0.0085  39  ARG A CD  
105  N NE  . ARG A 13  ? 0.1880 0.3499 0.2932 -0.0095 0.0061  0.0055  39  ARG A NE  
106  C CZ  . ARG A 13  ? 0.2044 0.3525 0.2974 -0.0076 0.0004  0.0031  39  ARG A CZ  
107  N NH1 . ARG A 13  ? 0.1943 0.3405 0.2835 0.0028  -0.0011 0.0042  39  ARG A NH1 
108  N NH2 . ARG A 13  ? 0.2083 0.3446 0.2933 -0.0165 -0.0035 -0.0003 39  ARG A NH2 
109  N N   . TYR A 14  ? 0.2080 0.3007 0.2606 0.0104  0.0268  0.0023  40  TYR A N   
110  C CA  . TYR A 14  ? 0.2188 0.2993 0.2613 0.0182  0.0271  0.0007  40  TYR A CA  
111  C C   . TYR A 14  ? 0.2405 0.3091 0.2711 0.0189  0.0328  -0.0006 40  TYR A C   
112  O O   . TYR A 14  ? 0.2434 0.3009 0.2650 0.0241  0.0337  -0.0026 40  TYR A O   
113  C CB  . TYR A 14  ? 0.1985 0.2678 0.2338 0.0166  0.0202  -0.0005 40  TYR A CB  
114  C CG  . TYR A 14  ? 0.2040 0.2829 0.2467 0.0189  0.0143  0.0003  40  TYR A CG  
115  C CD1 . TYR A 14  ? 0.2101 0.2900 0.2537 0.0278  0.0140  0.0014  40  TYR A CD1 
116  C CD2 . TYR A 14  ? 0.1919 0.2782 0.2400 0.0119  0.0090  0.0002  40  TYR A CD2 
117  C CE1 . TYR A 14  ? 0.2093 0.2994 0.2592 0.0303  0.0081  0.0034  40  TYR A CE1 
118  C CE2 . TYR A 14  ? 0.2120 0.3082 0.2653 0.0132  0.0028  0.0009  40  TYR A CE2 
119  C CZ  . TYR A 14  ? 0.2162 0.3155 0.2706 0.0228  0.0021  0.0030  40  TYR A CZ  
120  O OH  . TYR A 14  ? 0.2466 0.3560 0.3049 0.0246  -0.0046 0.0048  40  TYR A OH  
121  N N   . ASP A 15  ? 0.2399 0.3105 0.2697 0.0130  0.0364  0.0007  41  ASP A N   
122  C CA  . ASP A 15  ? 0.2695 0.3300 0.2865 0.0122  0.0406  0.0001  41  ASP A CA  
123  C C   . ASP A 15  ? 0.2619 0.3066 0.2670 0.0119  0.0359  -0.0014 41  ASP A C   
124  O O   . ASP A 15  ? 0.2684 0.3045 0.2643 0.0157  0.0372  -0.0039 41  ASP A O   
125  C CB  . ASP A 15  ? 0.2996 0.3628 0.3144 0.0184  0.0480  -0.0018 41  ASP A CB  
126  C CG  . ASP A 15  ? 0.3571 0.4120 0.3573 0.0164  0.0527  -0.0028 41  ASP A CG  
127  O OD1 . ASP A 15  ? 0.3452 0.3990 0.3417 0.0098  0.0519  0.0001  41  ASP A OD1 
128  O OD2 . ASP A 15  ? 0.4129 0.4616 0.4049 0.0215  0.0568  -0.0066 41  ASP A OD2 
129  N N   . ALA A 16  ? 0.2082 0.2492 0.2139 0.0071  0.0308  0.0001  42  ALA A N   
130  C CA  . ALA A 16  ? 0.2069 0.2363 0.2053 0.0073  0.0261  -0.0008 42  ALA A CA  
131  C C   . ALA A 16  ? 0.2071 0.2313 0.2033 0.0016  0.0242  0.0018  42  ALA A C   
132  O O   . ALA A 16  ? 0.2232 0.2522 0.2253 -0.0028 0.0255  0.0038  42  ALA A O   
133  C CB  . ALA A 16  ? 0.1993 0.2298 0.2026 0.0099  0.0215  -0.0021 42  ALA A CB  
134  N N   . ARG A 17  ? 0.1972 0.2118 0.1861 0.0019  0.0215  0.0018  43  ARG A N   
135  C CA  . ARG A 17  ? 0.2125 0.2212 0.2008 -0.0013 0.0193  0.0042  43  ARG A CA  
136  C C   . ARG A 17  ? 0.2146 0.2199 0.2050 -0.0002 0.0154  0.0019  43  ARG A C   
137  O O   . ARG A 17  ? 0.1890 0.1924 0.1763 0.0034  0.0138  0.0000  43  ARG A O   
138  C CB  . ARG A 17  ? 0.2226 0.2257 0.2026 -0.0014 0.0193  0.0068  43  ARG A CB  
139  C CG  . ARG A 17  ? 0.2330 0.2302 0.2133 -0.0032 0.0179  0.0105  43  ARG A CG  
140  C CD  . ARG A 17  ? 0.2440 0.2391 0.2177 -0.0027 0.0171  0.0142  43  ARG A CD  
141  N NE  . ARG A 17  ? 0.2415 0.2356 0.2114 -0.0004 0.0144  0.0118  43  ARG A NE  
142  C CZ  . ARG A 17  ? 0.2230 0.2145 0.1927 0.0008  0.0119  0.0136  43  ARG A CZ  
143  N NH1 . ARG A 17  ? 0.2113 0.2000 0.1840 0.0011  0.0117  0.0179  43  ARG A NH1 
144  N NH2 . ARG A 17  ? 0.2176 0.2092 0.1845 0.0016  0.0100  0.0111  43  ARG A NH2 
145  N N   . LEU A 18  ? 0.2043 0.2081 0.1989 -0.0036 0.0143  0.0019  44  LEU A N   
146  C CA  . LEU A 18  ? 0.2050 0.2060 0.2002 -0.0033 0.0110  -0.0009 44  LEU A CA  
147  C C   . LEU A 18  ? 0.2101 0.2008 0.2024 -0.0047 0.0110  -0.0001 44  LEU A C   
148  O O   . LEU A 18  ? 0.1967 0.1837 0.1905 -0.0079 0.0131  0.0024  44  LEU A O   
149  C CB  . LEU A 18  ? 0.1998 0.2087 0.2020 -0.0066 0.0095  -0.0030 44  LEU A CB  
150  C CG  . LEU A 18  ? 0.2045 0.2106 0.2057 -0.0082 0.0058  -0.0065 44  LEU A CG  
151  C CD1 . LEU A 18  ? 0.2189 0.2256 0.2158 -0.0029 0.0033  -0.0076 44  LEU A CD1 
152  C CD2 . LEU A 18  ? 0.2208 0.2363 0.2294 -0.0136 0.0038  -0.0084 44  LEU A CD2 
153  N N   . GLY A 19  ? 0.2014 0.1873 0.1900 -0.0020 0.0093  -0.0018 45  GLY A N   
154  C CA  . GLY A 19  ? 0.2100 0.1865 0.1966 -0.0020 0.0100  -0.0017 45  GLY A CA  
155  C C   . GLY A 19  ? 0.2132 0.1871 0.1976 -0.0024 0.0082  -0.0064 45  GLY A C   
156  O O   . GLY A 19  ? 0.2277 0.2061 0.2100 -0.0001 0.0060  -0.0080 45  GLY A O   
157  N N   . VAL A 20  ? 0.2001 0.1655 0.1840 -0.0053 0.0094  -0.0085 46  VAL A N   
158  C CA  . VAL A 20  ? 0.2119 0.1737 0.1917 -0.0069 0.0080  -0.0141 46  VAL A CA  
159  C C   . VAL A 20  ? 0.2272 0.1754 0.2034 -0.0058 0.0115  -0.0154 46  VAL A C   
160  O O   . VAL A 20  ? 0.2345 0.1747 0.2132 -0.0071 0.0145  -0.0133 46  VAL A O   
161  C CB  . VAL A 20  ? 0.2297 0.1958 0.2122 -0.0138 0.0055  -0.0178 46  VAL A CB  
162  C CG1 . VAL A 20  ? 0.2378 0.2011 0.2137 -0.0159 0.0030  -0.0240 46  VAL A CG1 
163  C CG2 . VAL A 20  ? 0.2248 0.2057 0.2133 -0.0140 0.0030  -0.0157 46  VAL A CG2 
164  N N   . TYR A 21  ? 0.2432 0.1881 0.2133 -0.0029 0.0118  -0.0184 47  TYR A N   
165  C CA  . TYR A 21  ? 0.2344 0.1658 0.2003 -0.0018 0.0159  -0.0214 47  TYR A CA  
166  C C   . TYR A 21  ? 0.2508 0.1803 0.2078 -0.0030 0.0149  -0.0282 47  TYR A C   
167  O O   . TYR A 21  ? 0.2375 0.1747 0.1911 -0.0003 0.0129  -0.0278 47  TYR A O   
168  C CB  . TYR A 21  ? 0.2375 0.1661 0.2052 0.0053  0.0199  -0.0166 47  TYR A CB  
169  C CG  . TYR A 21  ? 0.2593 0.1730 0.2253 0.0075  0.0255  -0.0185 47  TYR A CG  
170  C CD1 . TYR A 21  ? 0.2743 0.1780 0.2438 0.0057  0.0280  -0.0166 47  TYR A CD1 
171  C CD2 . TYR A 21  ? 0.2728 0.1813 0.2331 0.0115  0.0290  -0.0221 47  TYR A CD2 
172  C CE1 . TYR A 21  ? 0.3057 0.1934 0.2737 0.0088  0.0339  -0.0180 47  TYR A CE1 
173  C CE2 . TYR A 21  ? 0.2914 0.1851 0.2501 0.0146  0.0352  -0.0241 47  TYR A CE2 
174  C CZ  . TYR A 21  ? 0.3188 0.2014 0.2816 0.0136  0.0377  -0.0220 47  TYR A CZ  
175  O OH  . TYR A 21  ? 0.3685 0.2340 0.3298 0.0173  0.0445  -0.0239 47  TYR A OH  
176  N N   . VAL A 22  ? 0.2724 0.1904 0.2248 -0.0074 0.0166  -0.0343 48  VAL A N   
177  C CA  . VAL A 22  ? 0.2926 0.2048 0.2339 -0.0086 0.0170  -0.0417 48  VAL A CA  
178  C C   . VAL A 22  ? 0.3155 0.2088 0.2533 -0.0069 0.0241  -0.0451 48  VAL A C   
179  O O   . VAL A 22  ? 0.3256 0.2084 0.2658 -0.0115 0.0256  -0.0467 48  VAL A O   
180  C CB  . VAL A 22  ? 0.2985 0.2154 0.2360 -0.0175 0.0112  -0.0477 48  VAL A CB  
181  C CG1 . VAL A 22  ? 0.3128 0.2241 0.2361 -0.0194 0.0111  -0.0558 48  VAL A CG1 
182  C CG2 . VAL A 22  ? 0.2813 0.2171 0.2248 -0.0181 0.0047  -0.0433 48  VAL A CG2 
183  N N   . PRO A 23  ? 0.3369 0.2251 0.2695 -0.0002 0.0292  -0.0459 49  PRO A N   
184  C CA  . PRO A 23  ? 0.3631 0.2330 0.2926 0.0033  0.0372  -0.0491 49  PRO A CA  
185  C C   . PRO A 23  ? 0.3873 0.2424 0.3065 -0.0046 0.0377  -0.0596 49  PRO A C   
186  O O   . PRO A 23  ? 0.3909 0.2520 0.3021 -0.0114 0.0322  -0.0655 49  PRO A O   
187  C CB  . PRO A 23  ? 0.3651 0.2375 0.2903 0.0112  0.0418  -0.0488 49  PRO A CB  
188  C CG  . PRO A 23  ? 0.3429 0.2346 0.2730 0.0127  0.0365  -0.0421 49  PRO A CG  
189  C CD  . PRO A 23  ? 0.3267 0.2266 0.2570 0.0049  0.0284  -0.0431 49  PRO A CD  
190  N N   . ALA A 24  ? 0.4114 0.2471 0.3311 -0.0038 0.0442  -0.0616 50  ALA A N   
191  C CA  . ALA A 24  ? 0.4395 0.2565 0.3475 -0.0108 0.0467  -0.0728 50  ALA A CA  
192  C C   . ALA A 24  ? 0.4488 0.2631 0.3417 -0.0086 0.0494  -0.0811 50  ALA A C   
193  O O   . ALA A 24  ? 0.4165 0.2367 0.3097 0.0007  0.0533  -0.0774 50  ALA A O   
194  C CB  . ALA A 24  ? 0.4634 0.2570 0.3745 -0.0082 0.0549  -0.0726 50  ALA A CB  
195  N N   . THR A 25  ? 0.4957 0.3006 0.3751 -0.0180 0.0477  -0.0924 51  THR A N   
196  C CA  . THR A 25  ? 0.5347 0.3308 0.3963 -0.0170 0.0520  -0.1023 51  THR A CA  
197  C C   . THR A 25  ? 0.5748 0.3425 0.4270 -0.0218 0.0586  -0.1131 51  THR A C   
198  O O   . THR A 25  ? 0.5979 0.3539 0.4589 -0.0251 0.0598  -0.1112 51  THR A O   
199  C CB  . THR A 25  ? 0.5389 0.3515 0.3894 -0.0244 0.0429  -0.1067 51  THR A CB  
200  O OG1 . THR A 25  ? 0.5647 0.3747 0.4132 -0.0376 0.0362  -0.1129 51  THR A OG1 
201  C CG2 . THR A 25  ? 0.5222 0.3605 0.3830 -0.0204 0.0362  -0.0957 51  THR A CG2 
202  N N   . GLY A 26  ? 0.5910 0.3466 0.4244 -0.0227 0.0633  -0.1245 52  GLY A N   
203  C CA  . GLY A 26  ? 0.6453 0.3712 0.4668 -0.0278 0.0702  -0.1367 52  GLY A CA  
204  C C   . GLY A 26  ? 0.6423 0.3632 0.4620 -0.0442 0.0625  -0.1431 52  GLY A C   
205  O O   . GLY A 26  ? 0.6755 0.3697 0.4899 -0.0495 0.0681  -0.1511 52  GLY A O   
206  N N   . THR A 27  ? 0.6093 0.3553 0.4331 -0.0523 0.0501  -0.1398 53  THR A N   
207  C CA  . THR A 27  ? 0.6318 0.3782 0.4550 -0.0685 0.0419  -0.1456 53  THR A CA  
208  C C   . THR A 27  ? 0.5959 0.3644 0.4397 -0.0713 0.0337  -0.1338 53  THR A C   
209  O O   . THR A 27  ? 0.6161 0.3882 0.4629 -0.0846 0.0271  -0.1370 53  THR A O   
210  C CB  . THR A 27  ? 0.6722 0.4279 0.4766 -0.0782 0.0343  -0.1563 53  THR A CB  
211  O OG1 . THR A 27  ? 0.6716 0.4560 0.4796 -0.0719 0.0276  -0.1476 53  THR A OG1 
212  C CG2 . THR A 27  ? 0.7133 0.4451 0.4946 -0.0772 0.0430  -0.1699 53  THR A CG2 
213  N N   . THR A 28  ? 0.5638 0.3469 0.4219 -0.0595 0.0344  -0.1206 54  THR A N   
214  C CA  . THR A 28  ? 0.5452 0.3472 0.4215 -0.0613 0.0281  -0.1099 54  THR A CA  
215  C C   . THR A 28  ? 0.5152 0.3113 0.4053 -0.0506 0.0350  -0.0988 54  THR A C   
216  O O   . THR A 28  ? 0.5154 0.3078 0.4048 -0.0386 0.0412  -0.0953 54  THR A O   
217  C CB  . THR A 28  ? 0.5243 0.3561 0.4032 -0.0597 0.0189  -0.1048 54  THR A CB  
218  O OG1 . THR A 28  ? 0.5221 0.3571 0.3984 -0.0469 0.0232  -0.1002 54  THR A OG1 
219  C CG2 . THR A 28  ? 0.5461 0.3864 0.4121 -0.0703 0.0108  -0.1141 54  THR A CG2 
220  N N   . ALA A 29  ? 0.4978 0.2949 0.4008 -0.0554 0.0336  -0.0929 55  ALA A N   
221  C CA  . ALA A 29  ? 0.4868 0.2831 0.4029 -0.0464 0.0380  -0.0810 55  ALA A CA  
222  C C   . ALA A 29  ? 0.4477 0.2702 0.3723 -0.0391 0.0331  -0.0715 55  ALA A C   
223  O O   . ALA A 29  ? 0.4305 0.2725 0.3546 -0.0431 0.0255  -0.0725 55  ALA A O   
224  C CB  . ALA A 29  ? 0.4854 0.2749 0.4106 -0.0547 0.0382  -0.0777 55  ALA A CB  
225  N N   . ALA A 30  ? 0.4417 0.2640 0.3740 -0.0284 0.0376  -0.0621 56  ALA A N   
226  C CA  . ALA A 30  ? 0.4101 0.2540 0.3508 -0.0223 0.0337  -0.0529 56  ALA A CA  
227  C C   . ALA A 30  ? 0.3760 0.2351 0.3247 -0.0300 0.0273  -0.0496 56  ALA A C   
228  O O   . ALA A 30  ? 0.3779 0.2296 0.3303 -0.0373 0.0279  -0.0497 56  ALA A O   
229  C CB  . ALA A 30  ? 0.3998 0.2397 0.3478 -0.0118 0.0392  -0.0436 56  ALA A CB  
230  N N   . ILE A 31  ? 0.3568 0.2368 0.3083 -0.0281 0.0216  -0.0465 57  ILE A N   
231  C CA  . ILE A 31  ? 0.3381 0.2341 0.2990 -0.0320 0.0170  -0.0414 57  ILE A CA  
232  C C   . ILE A 31  ? 0.3198 0.2229 0.2873 -0.0235 0.0187  -0.0319 57  ILE A C   
233  O O   . ILE A 31  ? 0.3031 0.2110 0.2682 -0.0163 0.0187  -0.0302 57  ILE A O   
234  C CB  . ILE A 31  ? 0.3337 0.2475 0.2932 -0.0358 0.0098  -0.0448 57  ILE A CB  
235  C CG1 . ILE A 31  ? 0.3565 0.2648 0.3080 -0.0451 0.0071  -0.0546 57  ILE A CG1 
236  C CG2 . ILE A 31  ? 0.3242 0.2554 0.2947 -0.0380 0.0062  -0.0391 57  ILE A CG2 
237  C CD1 . ILE A 31  ? 0.3582 0.2844 0.3065 -0.0470 -0.0004 -0.0572 57  ILE A CD1 
238  N N   . GLU A 32  ? 0.3106 0.2137 0.2855 -0.0251 0.0202  -0.0257 59  GLU A N   
239  C CA  . GLU A 32  ? 0.3282 0.2358 0.3076 -0.0178 0.0219  -0.0169 59  GLU A CA  
240  C C   . GLU A 32  ? 0.2830 0.2025 0.2691 -0.0216 0.0201  -0.0120 59  GLU A C   
241  O O   . GLU A 32  ? 0.2798 0.1947 0.2689 -0.0283 0.0215  -0.0116 59  GLU A O   
242  C CB  . GLU A 32  ? 0.3810 0.2730 0.3613 -0.0141 0.0276  -0.0121 59  GLU A CB  
243  C CG  . GLU A 32  ? 0.4538 0.3297 0.4286 -0.0099 0.0319  -0.0164 59  GLU A CG  
244  C CD  . GLU A 32  ? 0.5198 0.3785 0.4969 -0.0065 0.0380  -0.0114 59  GLU A CD  
245  O OE1 . GLU A 32  ? 0.5703 0.4163 0.5474 -0.0130 0.0401  -0.0127 59  GLU A OE1 
246  O OE2 . GLU A 32  ? 0.6140 0.4721 0.5934 0.0026  0.0407  -0.0056 59  GLU A OE2 
247  N N   . TYR A 33  ? 0.2492 0.1830 0.2370 -0.0174 0.0178  -0.0084 60  TYR A N   
248  C CA  . TYR A 33  ? 0.2451 0.1891 0.2379 -0.0194 0.0176  -0.0035 60  TYR A CA  
249  C C   . TYR A 33  ? 0.2253 0.1754 0.2169 -0.0125 0.0174  0.0016  60  TYR A C   
250  O O   . TYR A 33  ? 0.2353 0.1919 0.2248 -0.0089 0.0150  -0.0003 60  TYR A O   
251  C CB  . TYR A 33  ? 0.2341 0.1912 0.2306 -0.0243 0.0142  -0.0072 60  TYR A CB  
252  C CG  . TYR A 33  ? 0.2159 0.1835 0.2183 -0.0267 0.0154  -0.0027 60  TYR A CG  
253  C CD1 . TYR A 33  ? 0.2360 0.2008 0.2429 -0.0338 0.0180  -0.0008 60  TYR A CD1 
254  C CD2 . TYR A 33  ? 0.2073 0.1863 0.2101 -0.0220 0.0148  -0.0003 60  TYR A CD2 
255  C CE1 . TYR A 33  ? 0.2312 0.2063 0.2432 -0.0360 0.0202  0.0037  60  TYR A CE1 
256  C CE2 . TYR A 33  ? 0.2086 0.1967 0.2156 -0.0238 0.0171  0.0033  60  TYR A CE2 
257  C CZ  . TYR A 33  ? 0.2211 0.2080 0.2327 -0.0305 0.0199  0.0056  60  TYR A CZ  
258  O OH  . TYR A 33  ? 0.2177 0.2148 0.2333 -0.0323 0.0231  0.0095  60  TYR A OH  
259  N N   . ARG A 34  ? 0.2345 0.1819 0.2268 -0.0112 0.0199  0.0083  61  ARG A N   
260  C CA  . ARG A 34  ? 0.2238 0.1765 0.2142 -0.0057 0.0193  0.0131  61  ARG A CA  
261  C C   . ARG A 34  ? 0.2158 0.1660 0.2041 -0.0004 0.0183  0.0113  61  ARG A C   
262  O O   . ARG A 34  ? 0.2031 0.1607 0.1900 0.0028  0.0165  0.0124  61  ARG A O   
263  C CB  . ARG A 34  ? 0.2251 0.1906 0.2148 -0.0062 0.0176  0.0130  61  ARG A CB  
264  C CG  . ARG A 34  ? 0.2389 0.2092 0.2310 -0.0109 0.0194  0.0148  61  ARG A CG  
265  C CD  . ARG A 34  ? 0.2292 0.2102 0.2191 -0.0094 0.0190  0.0151  61  ARG A CD  
266  N NE  . ARG A 34  ? 0.2308 0.2187 0.2236 -0.0133 0.0216  0.0162  61  ARG A NE  
267  C CZ  . ARG A 34  ? 0.2364 0.2236 0.2284 -0.0160 0.0248  0.0217  61  ARG A CZ  
268  N NH1 . ARG A 34  ? 0.2449 0.2254 0.2328 -0.0146 0.0253  0.0274  61  ARG A NH1 
269  N NH2 . ARG A 34  ? 0.2374 0.2321 0.2332 -0.0199 0.0278  0.0221  61  ARG A NH2 
270  N N   . ALA A 35  ? 0.2325 0.1717 0.2204 0.0003  0.0203  0.0085  62  ALA A N   
271  C CA  . ALA A 35  ? 0.2227 0.1597 0.2086 0.0048  0.0205  0.0057  62  ALA A CA  
272  C C   . ALA A 35  ? 0.2104 0.1502 0.1982 0.0109  0.0212  0.0120  62  ALA A C   
273  O O   . ALA A 35  ? 0.2190 0.1629 0.2063 0.0144  0.0207  0.0110  62  ALA A O   
274  C CB  . ALA A 35  ? 0.2452 0.1683 0.2290 0.0037  0.0234  0.0007  62  ALA A CB  
275  N N   . ASP A 36  ? 0.2201 0.1588 0.2105 0.0120  0.0222  0.0191  63  ASP A N   
276  C CA  . ASP A 36  ? 0.2252 0.1689 0.2185 0.0177  0.0221  0.0260  63  ASP A CA  
277  C C   . ASP A 36  ? 0.2238 0.1802 0.2160 0.0161  0.0184  0.0304  63  ASP A C   
278  O O   . ASP A 36  ? 0.2395 0.2022 0.2340 0.0196  0.0171  0.0368  63  ASP A O   
279  C CB  . ASP A 36  ? 0.2551 0.1885 0.2518 0.0217  0.0258  0.0321  63  ASP A CB  
280  C CG  . ASP A 36  ? 0.2861 0.2050 0.2828 0.0242  0.0305  0.0272  63  ASP A CG  
281  O OD1 . ASP A 36  ? 0.2724 0.1940 0.2691 0.0275  0.0312  0.0233  63  ASP A OD1 
282  O OD2 . ASP A 36  ? 0.2968 0.2013 0.2931 0.0226  0.0340  0.0272  63  ASP A OD2 
283  N N   . GLU A 37  ? 0.2262 0.1869 0.2150 0.0112  0.0166  0.0267  64  GLU A N   
284  C CA  . GLU A 37  ? 0.2263 0.1976 0.2121 0.0097  0.0138  0.0287  64  GLU A CA  
285  C C   . GLU A 37  ? 0.2208 0.1981 0.2056 0.0106  0.0114  0.0250  64  GLU A C   
286  O O   . GLU A 37  ? 0.2221 0.1966 0.2070 0.0109  0.0119  0.0196  64  GLU A O   
287  C CB  . GLU A 37  ? 0.2267 0.2001 0.2095 0.0050  0.0141  0.0261  64  GLU A CB  
288  C CG  . GLU A 37  ? 0.2358 0.2048 0.2193 0.0027  0.0167  0.0305  64  GLU A CG  
289  C CD  . GLU A 37  ? 0.2309 0.2050 0.2122 -0.0017 0.0177  0.0291  64  GLU A CD  
290  O OE1 . GLU A 37  ? 0.2436 0.2251 0.2217 -0.0019 0.0164  0.0259  64  GLU A OE1 
291  O OE2 . GLU A 37  ? 0.2406 0.2108 0.2239 -0.0049 0.0205  0.0310  64  GLU A OE2 
292  N N   . ARG A 38  ? 0.2150 0.2007 0.1981 0.0103  0.0088  0.0281  65  ARG A N   
293  C CA  . ARG A 38  ? 0.2086 0.1993 0.1906 0.0098  0.0067  0.0250  65  ARG A CA  
294  C C   . ARG A 38  ? 0.2158 0.2058 0.1928 0.0069  0.0065  0.0190  65  ARG A C   
295  O O   . ARG A 38  ? 0.2308 0.2216 0.2039 0.0046  0.0068  0.0185  65  ARG A O   
296  C CB  . ARG A 38  ? 0.2013 0.2013 0.1832 0.0093  0.0035  0.0302  65  ARG A CB  
297  C CG  . ARG A 38  ? 0.1877 0.1912 0.1772 0.0137  0.0036  0.0363  65  ARG A CG  
298  C CD  . ARG A 38  ? 0.2001 0.2161 0.1904 0.0125  -0.0008 0.0423  65  ARG A CD  
299  N NE  . ARG A 38  ? 0.2003 0.2218 0.2003 0.0180  -0.0004 0.0488  65  ARG A NE  
300  C CZ  . ARG A 38  ? 0.2182 0.2430 0.2252 0.0205  0.0009  0.0480  65  ARG A CZ  
301  N NH1 . ARG A 38  ? 0.2196 0.2430 0.2241 0.0172  0.0013  0.0415  65  ARG A NH1 
302  N NH2 . ARG A 38  ? 0.2191 0.2490 0.2358 0.0267  0.0023  0.0546  65  ARG A NH2 
303  N N   . PHE A 39  ? 0.2021 0.1908 0.1791 0.0074  0.0063  0.0151  66  PHE A N   
304  C CA  . PHE A 39  ? 0.2107 0.1984 0.1837 0.0060  0.0061  0.0104  66  PHE A CA  
305  C C   . PHE A 39  ? 0.2051 0.1936 0.1772 0.0056  0.0050  0.0096  66  PHE A C   
306  O O   . PHE A 39  ? 0.2065 0.1960 0.1823 0.0071  0.0053  0.0113  66  PHE A O   
307  C CB  . PHE A 39  ? 0.2083 0.1922 0.1824 0.0072  0.0074  0.0068  66  PHE A CB  
308  C CG  . PHE A 39  ? 0.2187 0.2021 0.1947 0.0063  0.0086  0.0066  66  PHE A CG  
309  C CD1 . PHE A 39  ? 0.2113 0.1915 0.1902 0.0063  0.0097  0.0087  66  PHE A CD1 
310  C CD2 . PHE A 39  ? 0.2025 0.1883 0.1778 0.0055  0.0092  0.0042  66  PHE A CD2 
311  C CE1 . PHE A 39  ? 0.2327 0.2119 0.2136 0.0040  0.0110  0.0085  66  PHE A CE1 
312  C CE2 . PHE A 39  ? 0.2062 0.1936 0.1847 0.0038  0.0105  0.0043  66  PHE A CE2 
313  C CZ  . PHE A 39  ? 0.2157 0.1995 0.1967 0.0024  0.0112  0.0064  66  PHE A CZ  
314  N N   . ALA A 40  ? 0.2068 0.1944 0.1741 0.0034  0.0045  0.0069  67  ALA A N   
315  C CA  . ALA A 40  ? 0.2103 0.1966 0.1762 0.0018  0.0038  0.0059  67  ALA A CA  
316  C C   . ALA A 40  ? 0.2050 0.1882 0.1731 0.0046  0.0052  0.0053  67  ALA A C   
317  O O   . ALA A 40  ? 0.2112 0.1910 0.1784 0.0069  0.0061  0.0032  67  ALA A O   
318  C CB  . ALA A 40  ? 0.2189 0.2005 0.1782 -0.0003 0.0042  0.0020  67  ALA A CB  
319  N N   . PHE A 41  ? 0.2034 0.1888 0.1741 0.0040  0.0053  0.0073  68  PHE A N   
320  C CA  . PHE A 41  ? 0.2217 0.2040 0.1923 0.0061  0.0070  0.0069  68  PHE A CA  
321  C C   . PHE A 41  ? 0.2254 0.2009 0.1906 0.0062  0.0073  0.0045  68  PHE A C   
322  O O   . PHE A 41  ? 0.2285 0.2012 0.1920 0.0091  0.0080  0.0038  68  PHE A O   
323  C CB  . PHE A 41  ? 0.2329 0.2193 0.2066 0.0043  0.0077  0.0096  68  PHE A CB  
324  C CG  . PHE A 41  ? 0.2256 0.2188 0.2060 0.0065  0.0091  0.0128  68  PHE A CG  
325  C CD1 . PHE A 41  ? 0.2260 0.2168 0.2063 0.0106  0.0122  0.0122  68  PHE A CD1 
326  C CD2 . PHE A 41  ? 0.2446 0.2469 0.2311 0.0049  0.0076  0.0164  68  PHE A CD2 
327  C CE1 . PHE A 41  ? 0.2483 0.2440 0.2346 0.0135  0.0148  0.0148  68  PHE A CE1 
328  C CE2 . PHE A 41  ? 0.2328 0.2420 0.2270 0.0083  0.0096  0.0201  68  PHE A CE2 
329  C CZ  . PHE A 41  ? 0.2396 0.2447 0.2338 0.0130  0.0138  0.0191  68  PHE A CZ  
330  N N   . CYS A 42  ? 0.2228 0.1954 0.1851 0.0029  0.0068  0.0035  69  CYS A N   
331  C CA  . CYS A 42  ? 0.2337 0.1980 0.1915 0.0030  0.0080  0.0025  69  CYS A CA  
332  C C   . CYS A 42  ? 0.2329 0.1968 0.1913 0.0039  0.0093  0.0051  69  CYS A C   
333  O O   . CYS A 42  ? 0.2432 0.2130 0.2054 0.0022  0.0097  0.0073  69  CYS A O   
334  C CB  . CYS A 42  ? 0.2339 0.1941 0.1893 0.0069  0.0085  0.0002  69  CYS A CB  
335  S SG  . CYS A 42  ? 0.2540 0.2158 0.2080 0.0053  0.0083  -0.0027 69  CYS A SG  
336  N N   A SER A 43  ? 0.2333 0.1910 0.1879 0.0070  0.0103  0.0056  70  SER A N   
337  N N   B SER A 43  ? 0.2518 0.2095 0.2064 0.0070  0.0103  0.0056  70  SER A N   
338  C CA  A SER A 43  ? 0.2207 0.1767 0.1735 0.0072  0.0120  0.0086  70  SER A CA  
339  C CA  B SER A 43  ? 0.2508 0.2069 0.2036 0.0072  0.0120  0.0086  70  SER A CA  
340  C C   A SER A 43  ? 0.2224 0.1848 0.1763 0.0098  0.0124  0.0093  70  SER A C   
341  C C   B SER A 43  ? 0.2387 0.2010 0.1926 0.0098  0.0124  0.0093  70  SER A C   
342  O O   A SER A 43  ? 0.2246 0.1867 0.1762 0.0101  0.0145  0.0117  70  SER A O   
343  O O   B SER A 43  ? 0.2392 0.2014 0.1908 0.0101  0.0145  0.0117  70  SER A O   
344  C CB  A SER A 43  ? 0.2285 0.1755 0.1760 0.0097  0.0129  0.0101  70  SER A CB  
345  C CB  B SER A 43  ? 0.2825 0.2293 0.2300 0.0096  0.0129  0.0101  70  SER A CB  
346  O OG  A SER A 43  ? 0.2218 0.1602 0.1674 0.0055  0.0143  0.0104  70  SER A OG  
347  O OG  B SER A 43  ? 0.3133 0.2605 0.2596 0.0150  0.0114  0.0094  70  SER A OG  
348  N N   . THR A 44  ? 0.2145 0.1815 0.1713 0.0114  0.0112  0.0071  71  THR A N   
349  C CA  . THR A 44  ? 0.2046 0.1749 0.1615 0.0135  0.0123  0.0067  71  THR A CA  
350  C C   . THR A 44  ? 0.2082 0.1825 0.1684 0.0123  0.0153  0.0090  71  THR A C   
351  O O   . THR A 44  ? 0.2388 0.2140 0.1969 0.0143  0.0179  0.0091  71  THR A O   
352  C CB  . THR A 44  ? 0.2102 0.1826 0.1697 0.0146  0.0109  0.0040  71  THR A CB  
353  O OG1 . THR A 44  ? 0.2021 0.1777 0.1672 0.0128  0.0108  0.0049  71  THR A OG1 
354  C CG2 . THR A 44  ? 0.2135 0.1847 0.1710 0.0157  0.0084  0.0021  71  THR A CG2 
355  N N   . PHE A 45  ? 0.2142 0.1919 0.1795 0.0088  0.0151  0.0109  72  PHE A N   
356  C CA  . PHE A 45  ? 0.2208 0.2058 0.1921 0.0078  0.0177  0.0138  72  PHE A CA  
357  C C   . PHE A 45  ? 0.2310 0.2148 0.1991 0.0070  0.0211  0.0161  72  PHE A C   
358  O O   . PHE A 45  ? 0.2470 0.2375 0.2197 0.0073  0.0247  0.0186  72  PHE A O   
359  C CB  . PHE A 45  ? 0.2367 0.2276 0.2142 0.0031  0.0154  0.0155  72  PHE A CB  
360  C CG  . PHE A 45  ? 0.2394 0.2275 0.2151 -0.0028 0.0151  0.0164  72  PHE A CG  
361  C CD1 . PHE A 45  ? 0.2290 0.2074 0.1982 -0.0046 0.0134  0.0139  72  PHE A CD1 
362  C CD2 . PHE A 45  ? 0.2498 0.2449 0.2310 -0.0066 0.0171  0.0199  72  PHE A CD2 
363  C CE1 . PHE A 45  ? 0.2613 0.2342 0.2283 -0.0102 0.0137  0.0143  72  PHE A CE1 
364  C CE2 . PHE A 45  ? 0.2469 0.2381 0.2264 -0.0133 0.0170  0.0206  72  PHE A CE2 
365  C CZ  . PHE A 45  ? 0.2590 0.2377 0.2308 -0.0151 0.0154  0.0176  72  PHE A CZ  
366  N N   . LYS A 46  ? 0.2563 0.2321 0.2171 0.0065  0.0206  0.0161  73  LYS A N   
367  C CA  . LYS A 46  ? 0.2633 0.2367 0.2201 0.0052  0.0239  0.0195  73  LYS A CA  
368  C C   . LYS A 46  ? 0.2700 0.2461 0.2229 0.0091  0.0276  0.0198  73  LYS A C   
369  O O   . LYS A 46  ? 0.2676 0.2461 0.2197 0.0079  0.0320  0.0232  73  LYS A O   
370  C CB  . LYS A 46  ? 0.2679 0.2307 0.2175 0.0048  0.0226  0.0204  73  LYS A CB  
371  C CG  . LYS A 46  ? 0.2907 0.2493 0.2432 -0.0003 0.0211  0.0200  73  LYS A CG  
372  C CD  . LYS A 46  ? 0.3092 0.2553 0.2553 0.0008  0.0201  0.0198  73  LYS A CD  
373  C CE  . LYS A 46  ? 0.3251 0.2656 0.2727 -0.0045 0.0191  0.0177  73  LYS A CE  
374  N NZ  . LYS A 46  ? 0.3363 0.2632 0.2780 -0.0021 0.0193  0.0171  73  LYS A NZ  
375  N N   . ALA A 47  ? 0.2697 0.2451 0.2196 0.0131  0.0262  0.0160  74  ALA A N   
376  C CA  . ALA A 47  ? 0.2888 0.2651 0.2328 0.0164  0.0298  0.0147  74  ALA A CA  
377  C C   . ALA A 47  ? 0.2660 0.2496 0.2177 0.0172  0.0349  0.0157  74  ALA A C   
378  O O   . ALA A 47  ? 0.2628 0.2491 0.2123 0.0175  0.0402  0.0180  74  ALA A O   
379  C CB  . ALA A 47  ? 0.3185 0.2915 0.2574 0.0190  0.0268  0.0098  74  ALA A CB  
380  N N   . PRO A 48  ? 0.2476 0.2353 0.2086 0.0182  0.0342  0.0146  75  PRO A N   
381  C CA  . PRO A 48  ? 0.2369 0.2333 0.2073 0.0200  0.0390  0.0170  75  PRO A CA  
382  C C   . PRO A 48  ? 0.2280 0.2333 0.2062 0.0158  0.0407  0.0224  75  PRO A C   
383  O O   . PRO A 48  ? 0.2344 0.2484 0.2192 0.0174  0.0461  0.0251  75  PRO A O   
384  C CB  . PRO A 48  ? 0.2379 0.2359 0.2161 0.0219  0.0364  0.0159  75  PRO A CB  
385  C CG  . PRO A 48  ? 0.2332 0.2255 0.2078 0.0188  0.0299  0.0141  75  PRO A CG  
386  C CD  . PRO A 48  ? 0.2472 0.2319 0.2102 0.0185  0.0293  0.0117  75  PRO A CD  
387  N N   . LEU A 49  ? 0.2276 0.2306 0.2053 0.0101  0.0364  0.0238  76  LEU A N   
388  C CA  . LEU A 49  ? 0.2342 0.2438 0.2180 0.0043  0.0379  0.0284  76  LEU A CA  
389  C C   . LEU A 49  ? 0.2393 0.2489 0.2180 0.0045  0.0443  0.0311  76  LEU A C   
390  O O   . LEU A 49  ? 0.2460 0.2663 0.2330 0.0028  0.0490  0.0351  76  LEU A O   
391  C CB  . LEU A 49  ? 0.2338 0.2364 0.2149 -0.0018 0.0328  0.0281  76  LEU A CB  
392  C CG  . LEU A 49  ? 0.2385 0.2442 0.2237 -0.0096 0.0342  0.0321  76  LEU A CG  
393  C CD1 . LEU A 49  ? 0.2389 0.2616 0.2389 -0.0130 0.0342  0.0349  76  LEU A CD1 
394  C CD2 . LEU A 49  ? 0.2488 0.2425 0.2282 -0.0148 0.0302  0.0305  76  LEU A CD2 
395  N N   . VAL A 50  ? 0.2321 0.2307 0.1973 0.0065  0.0443  0.0296  77  VAL A N   
396  C CA  . VAL A 50  ? 0.2691 0.2666 0.2264 0.0068  0.0501  0.0325  77  VAL A CA  
397  C C   . VAL A 50  ? 0.2652 0.2706 0.2243 0.0118  0.0568  0.0316  77  VAL A C   
398  O O   . VAL A 50  ? 0.2629 0.2750 0.2239 0.0108  0.0635  0.0355  77  VAL A O   
399  C CB  . VAL A 50  ? 0.2716 0.2570 0.2136 0.0085  0.0475  0.0316  77  VAL A CB  
400  C CG1 . VAL A 50  ? 0.2864 0.2710 0.2170 0.0103  0.0533  0.0341  77  VAL A CG1 
401  C CG2 . VAL A 50  ? 0.2740 0.2516 0.2154 0.0041  0.0435  0.0342  77  VAL A CG2 
402  N N   . ALA A 51  ? 0.2716 0.2756 0.2308 0.0170  0.0556  0.0264  78  ALA A N   
403  C CA  . ALA A 51  ? 0.2748 0.2839 0.2361 0.0225  0.0625  0.0247  78  ALA A CA  
404  C C   . ALA A 51  ? 0.2821 0.3060 0.2604 0.0221  0.0668  0.0296  78  ALA A C   
405  O O   . ALA A 51  ? 0.2777 0.3086 0.2580 0.0252  0.0752  0.0312  78  ALA A O   
406  C CB  . ALA A 51  ? 0.2676 0.2706 0.2274 0.0272  0.0600  0.0186  78  ALA A CB  
407  N N   . ALA A 52  ? 0.2542 0.2843 0.2448 0.0184  0.0612  0.0320  79  ALA A N   
408  C CA  . ALA A 52  ? 0.2557 0.3028 0.2638 0.0175  0.0637  0.0372  79  ALA A CA  
409  C C   . ALA A 52  ? 0.2618 0.3167 0.2724 0.0123  0.0690  0.0423  79  ALA A C   
410  O O   . ALA A 52  ? 0.2573 0.3266 0.2789 0.0144  0.0760  0.0461  79  ALA A O   
411  C CB  . ALA A 52  ? 0.2267 0.2785 0.2445 0.0133  0.0556  0.0384  79  ALA A CB  
412  N N   . VAL A 53  ? 0.2737 0.3196 0.2753 0.0056  0.0660  0.0431  80  VAL A N   
413  C CA  . VAL A 53  ? 0.2733 0.3244 0.2765 -0.0007 0.0709  0.0487  80  VAL A CA  
414  C C   . VAL A 53  ? 0.2832 0.3343 0.2777 0.0043  0.0804  0.0494  80  VAL A C   
415  O O   . VAL A 53  ? 0.2932 0.3566 0.2953 0.0026  0.0880  0.0543  80  VAL A O   
416  C CB  . VAL A 53  ? 0.2768 0.3141 0.2708 -0.0081 0.0656  0.0492  80  VAL A CB  
417  C CG1 . VAL A 53  ? 0.2863 0.3230 0.2770 -0.0140 0.0714  0.0551  80  VAL A CG1 
418  C CG2 . VAL A 53  ? 0.2580 0.2968 0.2608 -0.0143 0.0577  0.0484  80  VAL A CG2 
419  N N   . LEU A 54  ? 0.2890 0.3271 0.2673 0.0100  0.0802  0.0443  81  LEU A N   
420  C CA  . LEU A 54  ? 0.3149 0.3523 0.2822 0.0149  0.0890  0.0436  81  LEU A CA  
421  C C   . LEU A 54  ? 0.3377 0.3889 0.3176 0.0209  0.0970  0.0436  81  LEU A C   
422  O O   . LEU A 54  ? 0.3211 0.3812 0.3024 0.0216  0.1065  0.0470  81  LEU A O   
423  C CB  . LEU A 54  ? 0.3233 0.3459 0.2720 0.0195  0.0859  0.0370  81  LEU A CB  
424  C CG  . LEU A 54  ? 0.3251 0.3357 0.2588 0.0157  0.0805  0.0385  81  LEU A CG  
425  C CD1 . LEU A 54  ? 0.3173 0.3170 0.2375 0.0196  0.0750  0.0318  81  LEU A CD1 
426  C CD2 . LEU A 54  ? 0.3499 0.3608 0.2734 0.0134  0.0874  0.0442  81  LEU A CD2 
427  N N   . HIS A 55  ? 0.3211 0.3740 0.3103 0.0256  0.0937  0.0401  82  HIS A N   
428  C CA  . HIS A 55  ? 0.3408 0.4037 0.3408 0.0336  0.1014  0.0396  82  HIS A CA  
429  C C   . HIS A 55  ? 0.3356 0.4202 0.3558 0.0314  0.1065  0.0475  82  HIS A C   
430  O O   . HIS A 55  ? 0.3459 0.4401 0.3711 0.0371  0.1171  0.0489  82  HIS A O   
431  C CB  . HIS A 55  ? 0.3458 0.4044 0.3516 0.0385  0.0957  0.0358  82  HIS A CB  
432  C CG  . HIS A 55  ? 0.3803 0.4491 0.4002 0.0474  0.1029  0.0367  82  HIS A CG  
433  N ND1 . HIS A 55  ? 0.4124 0.4742 0.4245 0.0561  0.1122  0.0317  82  HIS A ND1 
434  C CD2 . HIS A 55  ? 0.3806 0.4655 0.4216 0.0493  0.1019  0.0423  82  HIS A CD2 
435  C CE1 . HIS A 55  ? 0.4253 0.4984 0.4545 0.0639  0.1178  0.0347  82  HIS A CE1 
436  N NE2 . HIS A 55  ? 0.4131 0.5013 0.4606 0.0600  0.1110  0.0416  82  HIS A NE2 
437  N N   . GLN A 56  ? 0.3402 0.4326 0.3714 0.0227  0.0993  0.0523  83  GLN A N   
438  C CA  . GLN A 56  ? 0.3785 0.4939 0.4321 0.0190  0.1012  0.0595  83  GLN A CA  
439  C C   . GLN A 56  ? 0.3812 0.5052 0.4353 0.0139  0.1099  0.0649  83  GLN A C   
440  O O   . GLN A 56  ? 0.3908 0.5366 0.4642 0.0119  0.1142  0.0711  83  GLN A O   
441  C CB  . GLN A 56  ? 0.4158 0.5334 0.4770 0.0100  0.0894  0.0611  83  GLN A CB  
442  C CG  . GLN A 56  ? 0.4834 0.6257 0.5676 0.0037  0.0883  0.0682  83  GLN A CG  
443  C CD  . GLN A 56  ? 0.5136 0.6556 0.6008 -0.0077 0.0771  0.0687  83  GLN A CD  
444  O OE1 . GLN A 56  ? 0.6198 0.7519 0.6984 -0.0176 0.0750  0.0687  83  GLN A OE1 
445  N NE2 . GLN A 56  ? 0.5602 0.7132 0.6595 -0.0067 0.0701  0.0696  83  GLN A NE2 
446  N N   . ASN A 57  ? 0.3681 0.4765 0.4020 0.0116  0.1123  0.0632  86  ASN A N   
447  C CA  . ASN A 57  ? 0.3811 0.4952 0.4139 0.0047  0.1192  0.0694  86  ASN A CA  
448  C C   . ASN A 57  ? 0.3904 0.4951 0.4033 0.0099  0.1286  0.0676  86  ASN A C   
449  O O   . ASN A 57  ? 0.3740 0.4625 0.3689 0.0157  0.1266  0.0610  86  ASN A O   
450  C CB  . ASN A 57  ? 0.3809 0.4842 0.4077 -0.0069 0.1116  0.0718  86  ASN A CB  
451  C CG  . ASN A 57  ? 0.3602 0.4708 0.4030 -0.0141 0.1021  0.0727  86  ASN A CG  
452  O OD1 . ASN A 57  ? 0.3755 0.5041 0.4359 -0.0213 0.1037  0.0784  86  ASN A OD1 
453  N ND2 . ASN A 57  ? 0.3593 0.4566 0.3957 -0.0132 0.0923  0.0674  86  ASN A ND2 
454  N N   . PRO A 58  ? 0.3907 0.5056 0.4050 0.0069  0.1390  0.0738  87  PRO A N   
455  C CA  . PRO A 58  ? 0.4162 0.5211 0.4081 0.0100  0.1472  0.0730  87  PRO A CA  
456  C C   . PRO A 58  ? 0.4110 0.4952 0.3820 0.0046  0.1398  0.0730  87  PRO A C   
457  O O   . PRO A 58  ? 0.3866 0.4652 0.3621 -0.0028 0.1306  0.0750  87  PRO A O   
458  C CB  . PRO A 58  ? 0.4324 0.5558 0.4343 0.0069  0.1599  0.0809  87  PRO A CB  
459  C CG  . PRO A 58  ? 0.4193 0.5595 0.4474 -0.0020 0.1554  0.0870  87  PRO A CG  
460  C CD  . PRO A 58  ? 0.4092 0.5469 0.4465 0.0002  0.1434  0.0819  87  PRO A CD  
461  N N   . LEU A 59  ? 0.4351 0.5079 0.3828 0.0092  0.1436  0.0702  88  LEU A N   
462  C CA  . LEU A 59  ? 0.4665 0.5215 0.3930 0.0060  0.1376  0.0712  88  LEU A CA  
463  C C   . LEU A 59  ? 0.4633 0.5170 0.3923 -0.0042 0.1375  0.0811  88  LEU A C   
464  O O   . LEU A 59  ? 0.4852 0.5242 0.4058 -0.0077 0.1291  0.0823  88  LEU A O   
465  C CB  . LEU A 59  ? 0.5201 0.5688 0.4222 0.0119  0.1442  0.0683  88  LEU A CB  
466  C CG  . LEU A 59  ? 0.5627 0.6021 0.4524 0.0198  0.1401  0.0573  88  LEU A CG  
467  C CD1 . LEU A 59  ? 0.5881 0.6222 0.4517 0.0231  0.1470  0.0555  88  LEU A CD1 
468  C CD2 . LEU A 59  ? 0.5592 0.5858 0.4459 0.0187  0.1259  0.0537  88  LEU A CD2 
469  N N   . THR A 60  ? 0.4449 0.5132 0.3852 -0.0090 0.1474  0.0882  89  THR A N   
470  C CA  . THR A 60  ? 0.4452 0.5116 0.3882 -0.0199 0.1485  0.0979  89  THR A CA  
471  C C   . THR A 60  ? 0.4330 0.4967 0.3920 -0.0279 0.1382  0.0980  89  THR A C   
472  O O   . THR A 60  ? 0.4185 0.4729 0.3761 -0.0370 0.1363  0.1040  89  THR A O   
473  C CB  . THR A 60  ? 0.4684 0.5543 0.4230 -0.0236 0.1619  0.1050  89  THR A CB  
474  O OG1 . THR A 60  ? 0.4701 0.5750 0.4483 -0.0207 0.1624  0.1013  89  THR A OG1 
475  C CG2 . THR A 60  ? 0.4912 0.5779 0.4268 -0.0173 0.1736  0.1060  89  THR A CG2 
476  N N   . HIS A 61  ? 0.4045 0.4751 0.3774 -0.0245 0.1318  0.0913  90  HIS A N   
477  C CA  . HIS A 61  ? 0.3899 0.4583 0.3758 -0.0316 0.1217  0.0902  90  HIS A CA  
478  C C   . HIS A 61  ? 0.3715 0.4160 0.3415 -0.0321 0.1124  0.0877  90  HIS A C   
479  O O   . HIS A 61  ? 0.3757 0.4132 0.3514 -0.0396 0.1057  0.0880  90  HIS A O   
480  C CB  . HIS A 61  ? 0.3936 0.4750 0.3956 -0.0264 0.1172  0.0841  90  HIS A CB  
481  C CG  . HIS A 61  ? 0.3659 0.4483 0.3812 -0.0338 0.1071  0.0828  90  HIS A CG  
482  N ND1 . HIS A 61  ? 0.3605 0.4566 0.3936 -0.0448 0.1071  0.0877  90  HIS A ND1 
483  C CD2 . HIS A 61  ? 0.3610 0.4334 0.3739 -0.0319 0.0970  0.0768  90  HIS A CD2 
484  C CE1 . HIS A 61  ? 0.3713 0.4648 0.4107 -0.0493 0.0969  0.0841  90  HIS A CE1 
485  N NE2 . HIS A 61  ? 0.3725 0.4513 0.3996 -0.0413 0.0910  0.0777  90  HIS A NE2 
486  N N   . LEU A 62  ? 0.3729 0.4053 0.3230 -0.0240 0.1118  0.0849  91  LEU A N   
487  C CA  . LEU A 62  ? 0.3735 0.3855 0.3094 -0.0234 0.1038  0.0839  91  LEU A CA  
488  C C   . LEU A 62  ? 0.3763 0.3767 0.3068 -0.0317 0.1057  0.0926  91  LEU A C   
489  O O   . LEU A 62  ? 0.3694 0.3530 0.2932 -0.0326 0.0990  0.0926  91  LEU A O   
490  C CB  . LEU A 62  ? 0.3920 0.3974 0.3085 -0.0138 0.1033  0.0801  91  LEU A CB  
491  C CG  . LEU A 62  ? 0.4046 0.4161 0.3239 -0.0060 0.1008  0.0707  91  LEU A CG  
492  C CD1 . LEU A 62  ? 0.4338 0.4382 0.3317 0.0013  0.1009  0.0672  91  LEU A CD1 
493  C CD2 . LEU A 62  ? 0.3921 0.3995 0.3207 -0.0062 0.0907  0.0654  91  LEU A CD2 
494  N N   . ASP A 63  ? 0.3810 0.3897 0.3148 -0.0373 0.1152  0.1001  92  ASP A N   
495  C CA  . ASP A 63  ? 0.4016 0.3985 0.3304 -0.0459 0.1183  0.1093  92  ASP A CA  
496  C C   . ASP A 63  ? 0.3934 0.3937 0.3410 -0.0586 0.1175  0.1113  92  ASP A C   
497  O O   . ASP A 63  ? 0.3935 0.3832 0.3390 -0.0675 0.1205  0.1186  92  ASP A O   
498  C CB  . ASP A 63  ? 0.4263 0.4260 0.3422 -0.0447 0.1289  0.1171  92  ASP A CB  
499  C CG  . ASP A 63  ? 0.4547 0.4460 0.3479 -0.0338 0.1269  0.1149  92  ASP A CG  
500  O OD1 . ASP A 63  ? 0.4332 0.4078 0.3165 -0.0309 0.1185  0.1140  92  ASP A OD1 
501  O OD2 . ASP A 63  ? 0.4724 0.4747 0.3586 -0.0278 0.1332  0.1130  92  ASP A OD2 
502  N N   . LYS A 64  ? 0.3815 0.3960 0.3469 -0.0599 0.1131  0.1050  93  LYS A N   
503  C CA  . LYS A 64  ? 0.3905 0.4101 0.3732 -0.0726 0.1107  0.1058  93  LYS A CA  
504  C C   . LYS A 64  ? 0.3816 0.3775 0.3577 -0.0771 0.1026  0.1032  93  LYS A C   
505  O O   . LYS A 64  ? 0.3528 0.3395 0.3222 -0.0695 0.0951  0.0965  93  LYS A O   
506  C CB  . LYS A 64  ? 0.4040 0.4459 0.4058 -0.0711 0.1070  0.0999  93  LYS A CB  
507  C CG  . LYS A 64  ? 0.4327 0.4852 0.4535 -0.0847 0.1039  0.1007  93  LYS A CG  
508  C CD  . LYS A 64  ? 0.4574 0.5303 0.4946 -0.0815 0.0982  0.0952  93  LYS A CD  
509  C CE  . LYS A 64  ? 0.4817 0.5611 0.5333 -0.0946 0.0912  0.0938  93  LYS A CE  
510  N NZ  . LYS A 64  ? 0.5220 0.6096 0.5836 -0.1085 0.0972  0.1011  93  LYS A NZ  
511  N N   . LEU A 65  ? 0.4027 0.3885 0.3810 -0.0898 0.1047  0.1084  94  LEU A N   
512  C CA  . LEU A 65  ? 0.4131 0.3735 0.3842 -0.0943 0.0987  0.1060  94  LEU A CA  
513  C C   . LEU A 65  ? 0.4107 0.3770 0.3951 -0.1013 0.0907  0.0979  94  LEU A C   
514  O O   . LEU A 65  ? 0.4061 0.3909 0.4070 -0.1116 0.0918  0.0988  94  LEU A O   
515  C CB  . LEU A 65  ? 0.4322 0.3764 0.3986 -0.1051 0.1050  0.1149  94  LEU A CB  
516  C CG  . LEU A 65  ? 0.4547 0.3674 0.4105 -0.1078 0.1009  0.1135  94  LEU A CG  
517  C CD1 . LEU A 65  ? 0.4522 0.3483 0.3900 -0.0925 0.0979  0.1131  94  LEU A CD1 
518  C CD2 . LEU A 65  ? 0.4874 0.3846 0.4417 -0.1210 0.1077  0.1221  94  LEU A CD2 
519  N N   . ILE A 66  ? 0.4013 0.3525 0.3783 -0.0961 0.0829  0.0906  95  ILE A N   
520  C CA  . ILE A 66  ? 0.4064 0.3594 0.3919 -0.1027 0.0752  0.0826  95  ILE A CA  
521  C C   . ILE A 66  ? 0.4338 0.3576 0.4099 -0.1098 0.0735  0.0809  95  ILE A C   
522  O O   . ILE A 66  ? 0.4375 0.3403 0.3995 -0.1011 0.0729  0.0805  95  ILE A O   
523  C CB  . ILE A 66  ? 0.3990 0.3589 0.3837 -0.0908 0.0684  0.0750  95  ILE A CB  
524  C CG1 . ILE A 66  ? 0.3951 0.3786 0.3864 -0.0817 0.0709  0.0763  95  ILE A CG1 
525  C CG2 . ILE A 66  ? 0.3994 0.3625 0.3916 -0.0977 0.0605  0.0674  95  ILE A CG2 
526  C CD1 . ILE A 66  ? 0.4046 0.4148 0.4149 -0.0893 0.0737  0.0793  95  ILE A CD1 
527  N N   A THR A 67  ? 0.4589 0.3812 0.4428 -0.1256 0.0726  0.0794  96  THR A N   
528  N N   B THR A 67  ? 0.4476 0.3705 0.4317 -0.1256 0.0725  0.0794  96  THR A N   
529  C CA  A THR A 67  ? 0.4935 0.3859 0.4678 -0.1327 0.0713  0.0761  96  THR A CA  
530  C CA  B THR A 67  ? 0.4732 0.3670 0.4485 -0.1335 0.0712  0.0760  96  THR A CA  
531  C C   A THR A 67  ? 0.4893 0.3821 0.4652 -0.1349 0.0626  0.0649  96  THR A C   
532  C C   B THR A 67  ? 0.4773 0.3705 0.4534 -0.1348 0.0625  0.0648  96  THR A C   
533  O O   A THR A 67  ? 0.4659 0.3839 0.4530 -0.1353 0.0578  0.0614  96  THR A O   
534  O O   B THR A 67  ? 0.4563 0.3744 0.4433 -0.1350 0.0575  0.0612  96  THR A O   
535  C CB  A THR A 67  ? 0.5272 0.4113 0.5052 -0.1497 0.0768  0.0815  96  THR A CB  
536  C CB  B THR A 67  ? 0.4882 0.3781 0.4696 -0.1517 0.0759  0.0807  96  THR A CB  
537  O OG1 A THR A 67  ? 0.5442 0.4363 0.5224 -0.1461 0.0848  0.0923  96  THR A OG1 
538  O OG1 B THR A 67  ? 0.4633 0.3854 0.4633 -0.1606 0.0737  0.0800  96  THR A OG1 
539  C CG2 A THR A 67  ? 0.5579 0.4041 0.5220 -0.1539 0.0785  0.0805  96  THR A CG2 
540  C CG2 B THR A 67  ? 0.5047 0.3857 0.4803 -0.1503 0.0853  0.0923  96  THR A CG2 
541  N N   . TYR A 68  ? 0.5156 0.3797 0.4793 -0.1350 0.0613  0.0598  97  TYR A N   
542  C CA  . TYR A 68  ? 0.5256 0.3851 0.4866 -0.1358 0.0542  0.0489  97  TYR A CA  
543  C C   . TYR A 68  ? 0.5810 0.4042 0.5289 -0.1407 0.0565  0.0453  97  TYR A C   
544  O O   . TYR A 68  ? 0.5876 0.3922 0.5305 -0.1426 0.0631  0.0524  97  TYR A O   
545  C CB  . TYR A 68  ? 0.4829 0.3511 0.4410 -0.1187 0.0505  0.0462  97  TYR A CB  
546  C CG  . TYR A 68  ? 0.4714 0.3229 0.4180 -0.1040 0.0542  0.0507  97  TYR A CG  
547  C CD1 . TYR A 68  ? 0.4622 0.3234 0.4093 -0.0965 0.0584  0.0593  97  TYR A CD1 
548  C CD2 . TYR A 68  ? 0.4852 0.3125 0.4204 -0.0973 0.0536  0.0464  97  TYR A CD2 
549  C CE1 . TYR A 68  ? 0.4518 0.2998 0.3879 -0.0838 0.0607  0.0638  97  TYR A CE1 
550  C CE2 . TYR A 68  ? 0.4799 0.2944 0.4061 -0.0839 0.0562  0.0515  97  TYR A CE2 
551  C CZ  . TYR A 68  ? 0.4600 0.2855 0.3865 -0.0775 0.0592  0.0603  97  TYR A CZ  
552  O OH  . TYR A 68  ? 0.4510 0.2658 0.3682 -0.0648 0.0607  0.0654  97  TYR A OH  
553  N N   . THR A 69  ? 0.6020 0.4145 0.5441 -0.1427 0.0518  0.0347  98  THR A N   
554  C CA  . THR A 69  ? 0.6394 0.4155 0.5684 -0.1464 0.0548  0.0301  98  THR A CA  
555  C C   . THR A 69  ? 0.5996 0.3640 0.5188 -0.1329 0.0525  0.0227  98  THR A C   
556  O O   . THR A 69  ? 0.5384 0.3236 0.4615 -0.1230 0.0479  0.0211  98  THR A O   
557  C CB  . THR A 69  ? 0.7124 0.4826 0.6430 -0.1675 0.0532  0.0234  98  THR A CB  
558  O OG1 . THR A 69  ? 0.7552 0.4863 0.6734 -0.1709 0.0593  0.0224  98  THR A OG1 
559  C CG2 . THR A 69  ? 0.7136 0.4991 0.6457 -0.1725 0.0448  0.0123  98  THR A CG2 
560  N N   . SER A 70  ? 0.6162 0.3466 0.5232 -0.1317 0.0564  0.0190  99  SER A N   
561  C CA  . SER A 70  ? 0.6300 0.3498 0.5287 -0.1174 0.0556  0.0132  99  SER A CA  
562  C C   . SER A 70  ? 0.6027 0.3367 0.5018 -0.1221 0.0489  0.0017  99  SER A C   
563  O O   . SER A 70  ? 0.5810 0.3197 0.4775 -0.1099 0.0468  -0.0019 99  SER A O   
564  C CB  . SER A 70  ? 0.6460 0.3271 0.5326 -0.1132 0.0623  0.0125  99  SER A CB  
565  O OG  . SER A 70  ? 0.6983 0.3571 0.5777 -0.1277 0.0637  0.0028  99  SER A OG  
566  N N   . ASP A 71  ? 0.6062 0.3501 0.5095 -0.1396 0.0452  -0.0029 100 ASP A N   
567  C CA  . ASP A 71  ? 0.6151 0.3755 0.5185 -0.1448 0.0381  -0.0124 100 ASP A CA  
568  C C   . ASP A 71  ? 0.5660 0.3611 0.4803 -0.1352 0.0328  -0.0083 100 ASP A C   
569  O O   . ASP A 71  ? 0.5266 0.3351 0.4401 -0.1345 0.0272  -0.0146 100 ASP A O   
570  C CB  . ASP A 71  ? 0.6386 0.4036 0.5442 -0.1665 0.0344  -0.0177 100 ASP A CB  
571  C CG  . ASP A 71  ? 0.7292 0.4578 0.6214 -0.1781 0.0387  -0.0256 100 ASP A CG  
572  O OD1 . ASP A 71  ? 0.7899 0.4944 0.6690 -0.1692 0.0419  -0.0323 100 ASP A OD1 
573  O OD2 . ASP A 71  ? 0.7765 0.5015 0.6719 -0.1958 0.0392  -0.0251 100 ASP A OD2 
574  N N   . ASP A 72  ? 0.5351 0.3436 0.4585 -0.1283 0.0349  0.0022  101 ASP A N   
575  C CA  . ASP A 72  ? 0.4951 0.3335 0.4283 -0.1189 0.0311  0.0062  101 ASP A CA  
576  C C   . ASP A 72  ? 0.4607 0.2940 0.3882 -0.1011 0.0319  0.0060  101 ASP A C   
577  O O   . ASP A 72  ? 0.4386 0.2929 0.3720 -0.0930 0.0286  0.0074  101 ASP A O   
578  C CB  . ASP A 72  ? 0.5209 0.3754 0.4650 -0.1189 0.0338  0.0166  101 ASP A CB  
579  C CG  . ASP A 72  ? 0.5400 0.4098 0.4948 -0.1356 0.0325  0.0184  101 ASP A CG  
580  O OD1 . ASP A 72  ? 0.5593 0.4503 0.5213 -0.1413 0.0262  0.0147  101 ASP A OD1 
581  O OD2 . ASP A 72  ? 0.5967 0.4574 0.5528 -0.1430 0.0378  0.0239  101 ASP A OD2 
582  N N   . ILE A 73  ? 0.4680 0.2739 0.3850 -0.0949 0.0365  0.0050  102 ILE A N   
583  C CA  . ILE A 73  ? 0.4370 0.2395 0.3500 -0.0784 0.0372  0.0053  102 ILE A CA  
584  C C   . ILE A 73  ? 0.4368 0.2345 0.3434 -0.0775 0.0348  -0.0049 102 ILE A C   
585  O O   . ILE A 73  ? 0.4432 0.2170 0.3404 -0.0815 0.0378  -0.0110 102 ILE A O   
586  C CB  . ILE A 73  ? 0.4596 0.2381 0.3660 -0.0704 0.0434  0.0110  102 ILE A CB  
587  C CG1 . ILE A 73  ? 0.4831 0.2663 0.3939 -0.0721 0.0462  0.0216  102 ILE A CG1 
588  C CG2 . ILE A 73  ? 0.4501 0.2275 0.3538 -0.0535 0.0434  0.0115  102 ILE A CG2 
589  C CD1 . ILE A 73  ? 0.5267 0.2847 0.4301 -0.0659 0.0522  0.0284  102 ILE A CD1 
590  N N   . ARG A 74  ? 0.4095 0.2295 0.3209 -0.0729 0.0299  -0.0067 103 ARG A N   
591  C CA  . ARG A 74  ? 0.4092 0.2292 0.3148 -0.0725 0.0273  -0.0155 103 ARG A CA  
592  C C   . ARG A 74  ? 0.3998 0.2288 0.3070 -0.0578 0.0268  -0.0143 103 ARG A C   
593  O O   . ARG A 74  ? 0.3820 0.2185 0.2871 -0.0565 0.0242  -0.0196 103 ARG A O   
594  C CB  . ARG A 74  ? 0.4106 0.2508 0.3204 -0.0840 0.0211  -0.0188 103 ARG A CB  
595  C CG  . ARG A 74  ? 0.4397 0.2742 0.3497 -0.1001 0.0209  -0.0197 103 ARG A CG  
596  C CD  . ARG A 74  ? 0.4412 0.2965 0.3556 -0.1125 0.0140  -0.0226 103 ARG A CD  
597  N NE  . ARG A 74  ? 0.4389 0.2911 0.3556 -0.1288 0.0137  -0.0228 103 ARG A NE  
598  C CZ  . ARG A 74  ? 0.4503 0.3211 0.3720 -0.1422 0.0073  -0.0247 103 ARG A CZ  
599  N NH1 . ARG A 74  ? 0.4466 0.3364 0.3687 -0.1412 0.0009  -0.0275 103 ARG A NH1 
600  N NH2 . ARG A 74  ? 0.4762 0.3479 0.4030 -0.1570 0.0070  -0.0234 103 ARG A NH2 
601  N N   . SER A 75  ? 0.3852 0.2155 0.2964 -0.0477 0.0289  -0.0069 104 SER A N   
602  C CA  . SER A 75  ? 0.3826 0.2231 0.2966 -0.0349 0.0279  -0.0049 104 SER A CA  
603  C C   . SER A 75  ? 0.3998 0.2294 0.3127 -0.0254 0.0316  0.0016  104 SER A C   
604  O O   . SER A 75  ? 0.4044 0.2233 0.3158 -0.0293 0.0344  0.0060  104 SER A O   
605  C CB  . SER A 75  ? 0.3606 0.2263 0.2835 -0.0343 0.0236  -0.0017 104 SER A CB  
606  O OG  . SER A 75  ? 0.3480 0.2192 0.2757 -0.0371 0.0245  0.0050  104 SER A OG  
607  N N   . ARG A 76  ? 0.4325 0.2664 0.3465 -0.0137 0.0314  0.0026  105 ARG A N   
608  C CA  . ARG A 76  ? 0.4514 0.2796 0.3650 -0.0035 0.0334  0.0094  105 ARG A CA  
609  C C   . ARG A 76  ? 0.4077 0.2444 0.3238 -0.0054 0.0326  0.0170  105 ARG A C   
610  O O   . ARG A 76  ? 0.3644 0.2201 0.2855 -0.0055 0.0294  0.0178  105 ARG A O   
611  C CB  . ARG A 76  ? 0.4962 0.3362 0.4133 0.0071  0.0313  0.0086  105 ARG A CB  
612  C CG  . ARG A 76  ? 0.5198 0.3598 0.4378 0.0183  0.0316  0.0157  105 ARG A CG  
613  C CD  . ARG A 76  ? 0.5684 0.3861 0.4815 0.0229  0.0365  0.0186  105 ARG A CD  
614  N NE  . ARG A 76  ? 0.6329 0.4411 0.5447 0.0265  0.0394  0.0120  105 ARG A NE  
615  C CZ  . ARG A 76  ? 0.6298 0.4159 0.5371 0.0309  0.0449  0.0118  105 ARG A CZ  
616  N NH1 . ARG A 76  ? 0.6430 0.4143 0.5474 0.0336  0.0476  0.0194  105 ARG A NH1 
617  N NH2 . ARG A 76  ? 0.6087 0.3871 0.5139 0.0328  0.0482  0.0041  105 ARG A NH2 
618  N N   . SER A 77  ? 0.3927 0.2139 0.3047 -0.0067 0.0364  0.0226  106 SER A N   
619  C CA  . SER A 77  ? 0.3826 0.2096 0.2956 -0.0108 0.0371  0.0296  106 SER A CA  
620  C C   . SER A 77  ? 0.3871 0.2002 0.2946 -0.0041 0.0404  0.0383  106 SER A C   
621  O O   . SER A 77  ? 0.3835 0.1793 0.2871 -0.0092 0.0446  0.0418  106 SER A O   
622  C CB  . SER A 77  ? 0.3843 0.2086 0.2988 -0.0247 0.0384  0.0275  106 SER A CB  
623  O OG  . SER A 77  ? 0.3571 0.1952 0.2764 -0.0301 0.0346  0.0203  106 SER A OG  
624  N N   . PRO A 78  ? 0.3994 0.2196 0.3062 0.0074  0.0384  0.0425  107 PRO A N   
625  C CA  . PRO A 78  ? 0.4268 0.2341 0.3281 0.0155  0.0408  0.0515  107 PRO A CA  
626  C C   . PRO A 78  ? 0.4279 0.2315 0.3247 0.0110  0.0438  0.0603  107 PRO A C   
627  O O   . PRO A 78  ? 0.4789 0.2649 0.3701 0.0139  0.0474  0.0678  107 PRO A O   
628  C CB  . PRO A 78  ? 0.4235 0.2465 0.3266 0.0268  0.0362  0.0532  107 PRO A CB  
629  C CG  . PRO A 78  ? 0.4161 0.2528 0.3256 0.0252  0.0329  0.0435  107 PRO A CG  
630  C CD  . PRO A 78  ? 0.3995 0.2396 0.3108 0.0129  0.0336  0.0391  107 PRO A CD  
631  N N   . VAL A 79  ? 0.4045 0.2242 0.3037 0.0042  0.0430  0.0599  108 VAL A N   
632  C CA  . VAL A 79  ? 0.4131 0.2315 0.3084 -0.0006 0.0467  0.0681  108 VAL A CA  
633  C C   . VAL A 79  ? 0.4168 0.2249 0.3146 -0.0138 0.0508  0.0666  108 VAL A C   
634  O O   . VAL A 79  ? 0.4309 0.2219 0.3240 -0.0175 0.0557  0.0734  108 VAL A O   
635  C CB  . VAL A 79  ? 0.3881 0.2293 0.2842 0.0001  0.0449  0.0690  108 VAL A CB  
636  C CG1 . VAL A 79  ? 0.3996 0.2406 0.2909 -0.0045 0.0498  0.0776  108 VAL A CG1 
637  C CG2 . VAL A 79  ? 0.4033 0.2540 0.2962 0.0115  0.0402  0.0696  108 VAL A CG2 
638  N N   . ALA A 80  ? 0.4110 0.2296 0.3163 -0.0214 0.0487  0.0580  109 ALA A N   
639  C CA  . ALA A 80  ? 0.4465 0.2619 0.3558 -0.0354 0.0513  0.0566  109 ALA A CA  
640  C C   . ALA A 80  ? 0.4887 0.2759 0.3927 -0.0399 0.0548  0.0561  109 ALA A C   
641  O O   . ALA A 80  ? 0.5029 0.2812 0.4072 -0.0508 0.0587  0.0591  109 ALA A O   
642  C CB  . ALA A 80  ? 0.4368 0.2697 0.3549 -0.0414 0.0472  0.0479  109 ALA A CB  
643  N N   . GLN A 81  ? 0.5173 0.2907 0.4171 -0.0313 0.0539  0.0526  110 GLN A N   
644  C CA  . GLN A 81  ? 0.5883 0.3316 0.4817 -0.0323 0.0582  0.0520  110 GLN A CA  
645  C C   . GLN A 81  ? 0.6175 0.3439 0.5056 -0.0342 0.0639  0.0631  110 GLN A C   
646  O O   . GLN A 81  ? 0.6387 0.3426 0.5236 -0.0434 0.0684  0.0630  110 GLN A O   
647  C CB  . GLN A 81  ? 0.6259 0.3615 0.5161 -0.0173 0.0574  0.0512  110 GLN A CB  
648  C CG  . GLN A 81  ? 0.7224 0.4297 0.6075 -0.0171 0.0614  0.0458  110 GLN A CG  
649  C CD  . GLN A 81  ? 0.7295 0.4395 0.6160 -0.0259 0.0593  0.0326  110 GLN A CD  
650  O OE1 . GLN A 81  ? 0.8297 0.5547 0.7192 -0.0207 0.0554  0.0264  110 GLN A OE1 
651  N NE2 . GLN A 81  ? 0.7556 0.4520 0.6396 -0.0405 0.0617  0.0285  110 GLN A NE2 
652  N N   . GLN A 82  ? 0.5790 0.3155 0.4653 -0.0256 0.0637  0.0728  111 GLN A N   
653  C CA  . GLN A 82  ? 0.6135 0.3338 0.4928 -0.0241 0.0689  0.0850  111 GLN A CA  
654  C C   . GLN A 82  ? 0.5711 0.2970 0.4520 -0.0372 0.0726  0.0901  111 GLN A C   
655  O O   . GLN A 82  ? 0.5642 0.2785 0.4391 -0.0373 0.0775  0.1012  111 GLN A O   
656  C CB  . GLN A 82  ? 0.6587 0.3866 0.5335 -0.0084 0.0665  0.0931  111 GLN A CB  
657  C CG  . GLN A 82  ? 0.7400 0.4526 0.6126 0.0045  0.0658  0.0926  111 GLN A CG  
658  C CD  . GLN A 82  ? 0.8011 0.5340 0.6790 0.0133  0.0594  0.0853  111 GLN A CD  
659  O OE1 . GLN A 82  ? 0.7531 0.4813 0.6343 0.0149  0.0586  0.0761  111 GLN A OE1 
660  N NE2 . GLN A 82  ? 0.8539 0.6097 0.7317 0.0184  0.0551  0.0891  111 GLN A NE2 
661  N N   . HIS A 83  ? 0.5319 0.2770 0.4214 -0.0479 0.0706  0.0833  112 HIS A N   
662  C CA  . HIS A 83  ? 0.5326 0.2897 0.4260 -0.0584 0.0741  0.0889  112 HIS A CA  
663  C C   . HIS A 83  ? 0.5393 0.2978 0.4410 -0.0754 0.0746  0.0823  112 HIS A C   
664  O O   . HIS A 83  ? 0.5246 0.3004 0.4336 -0.0845 0.0764  0.0851  112 HIS A O   
665  C CB  . HIS A 83  ? 0.5057 0.2925 0.4021 -0.0523 0.0716  0.0904  112 HIS A CB  
666  C CG  . HIS A 83  ? 0.5173 0.3017 0.4035 -0.0392 0.0721  0.0991  112 HIS A CG  
667  N ND1 . HIS A 83  ? 0.5325 0.3255 0.4163 -0.0263 0.0666  0.0962  112 HIS A ND1 
668  C CD2 . HIS A 83  ? 0.5493 0.3236 0.4268 -0.0376 0.0771  0.1110  112 HIS A CD2 
669  C CE1 . HIS A 83  ? 0.5298 0.3196 0.4038 -0.0174 0.0676  0.1060  112 HIS A CE1 
670  N NE2 . HIS A 83  ? 0.5617 0.3398 0.4312 -0.0237 0.0740  0.1153  112 HIS A NE2 
671  N N   . VAL A 84  ? 0.5607 0.3005 0.4610 -0.0801 0.0735  0.0742  113 VAL A N   
672  C CA  . VAL A 84  ? 0.6006 0.3420 0.5077 -0.0973 0.0728  0.0672  113 VAL A CA  
673  C C   . VAL A 84  ? 0.6183 0.3555 0.5280 -0.1111 0.0789  0.0753  113 VAL A C   
674  O O   . VAL A 84  ? 0.6059 0.3616 0.5260 -0.1242 0.0781  0.0738  113 VAL A O   
675  C CB  . VAL A 84  ? 0.6612 0.3768 0.5622 -0.1003 0.0721  0.0574  113 VAL A CB  
676  C CG1 . VAL A 84  ? 0.6751 0.3900 0.5810 -0.1202 0.0712  0.0502  113 VAL A CG1 
677  C CG2 . VAL A 84  ? 0.6265 0.3494 0.5263 -0.0881 0.0665  0.0490  113 VAL A CG2 
678  N N   . GLN A 85  ? 0.6618 0.3749 0.5626 -0.1084 0.0852  0.0849  114 GLN A N   
679  C CA  . GLN A 85  ? 0.7287 0.4340 0.6315 -0.1234 0.0916  0.0922  114 GLN A CA  
680  C C   . GLN A 85  ? 0.6966 0.4295 0.6058 -0.1240 0.0943  0.1016  114 GLN A C   
681  O O   . GLN A 85  ? 0.6998 0.4395 0.6164 -0.1389 0.0982  0.1052  114 GLN A O   
682  C CB  . GLN A 85  ? 0.8169 0.4851 0.7079 -0.1213 0.0984  0.1005  114 GLN A CB  
683  C CG  . GLN A 85  ? 0.8880 0.5488 0.7802 -0.1355 0.1061  0.1108  114 GLN A CG  
684  C CD  . GLN A 85  ? 0.9785 0.5978 0.8588 -0.1349 0.1127  0.1176  114 GLN A CD  
685  O OE1 . GLN A 85  ? 1.0550 0.6533 0.9268 -0.1219 0.1117  0.1152  114 GLN A OE1 
686  N NE2 . GLN A 85  ? 1.0111 0.6187 0.8919 -0.1491 0.1199  0.1259  114 GLN A NE2 
687  N N   . THR A 86  ? 0.6432 0.3905 0.5486 -0.1082 0.0928  0.1056  115 THR A N   
688  C CA  . THR A 86  ? 0.6375 0.4064 0.5449 -0.1066 0.0967  0.1148  115 THR A CA  
689  C C   . THR A 86  ? 0.5697 0.3737 0.4900 -0.1078 0.0927  0.1083  115 THR A C   
690  O O   . THR A 86  ? 0.5678 0.3921 0.4948 -0.1122 0.0970  0.1136  115 THR A O   
691  C CB  . THR A 86  ? 0.6507 0.4148 0.5450 -0.0895 0.0972  0.1225  115 THR A CB  
692  O OG1 . THR A 86  ? 0.6566 0.4296 0.5505 -0.0770 0.0897  0.1141  115 THR A OG1 
693  C CG2 . THR A 86  ? 0.6914 0.4215 0.5736 -0.0870 0.1015  0.1310  115 THR A CG2 
694  N N   . GLY A 87  ? 0.5064 0.3170 0.4302 -0.1029 0.0852  0.0974  116 GLY A N   
695  C CA  . GLY A 87  ? 0.4726 0.3137 0.4055 -0.0983 0.0810  0.0924  116 GLY A CA  
696  C C   . GLY A 87  ? 0.4447 0.2920 0.3690 -0.0817 0.0803  0.0951  116 GLY A C   
697  O O   . GLY A 87  ? 0.4490 0.2796 0.3610 -0.0743 0.0825  0.1016  116 GLY A O   
698  N N   . MET A 88  ? 0.4039 0.2753 0.3350 -0.0763 0.0768  0.0901  117 MET A N   
699  C CA  . MET A 88  ? 0.3841 0.2651 0.3084 -0.0627 0.0760  0.0911  117 MET A CA  
700  C C   . MET A 88  ? 0.3684 0.2763 0.3019 -0.0635 0.0788  0.0912  117 MET A C   
701  O O   . MET A 88  ? 0.3568 0.2791 0.3044 -0.0712 0.0778  0.0874  117 MET A O   
702  C CB  . MET A 88  ? 0.3722 0.2515 0.2948 -0.0535 0.0683  0.0825  117 MET A CB  
703  C CG  . MET A 88  ? 0.3898 0.2436 0.3032 -0.0498 0.0664  0.0827  117 MET A CG  
704  S SD  . MET A 88  ? 0.3968 0.2508 0.3099 -0.0397 0.0584  0.0729  117 MET A SD  
705  C CE  . MET A 88  ? 0.3711 0.2441 0.2801 -0.0284 0.0573  0.0749  117 MET A CE  
706  N N   . THR A 89  ? 0.3631 0.2781 0.2883 -0.0552 0.0823  0.0955  118 THR A N   
707  C CA  . THR A 89  ? 0.3505 0.2897 0.2833 -0.0537 0.0858  0.0945  118 THR A CA  
708  C C   . THR A 89  ? 0.3246 0.2745 0.2624 -0.0463 0.0793  0.0851  118 THR A C   
709  O O   . THR A 89  ? 0.3197 0.2594 0.2515 -0.0403 0.0729  0.0804  118 THR A O   
710  C CB  . THR A 89  ? 0.3648 0.3073 0.2855 -0.0482 0.0927  0.1014  118 THR A CB  
711  O OG1 . THR A 89  ? 0.3636 0.2982 0.2699 -0.0370 0.0880  0.0991  118 THR A OG1 
712  C CG2 . THR A 89  ? 0.3955 0.3271 0.3106 -0.0556 0.0997  0.1121  118 THR A CG2 
713  N N   . ILE A 90  ? 0.3148 0.2858 0.2640 -0.0462 0.0817  0.0830  119 ILE A N   
714  C CA  . ILE A 90  ? 0.2977 0.2793 0.2519 -0.0389 0.0770  0.0753  119 ILE A CA  
715  C C   . ILE A 90  ? 0.2950 0.2683 0.2337 -0.0280 0.0747  0.0727  119 ILE A C   
716  O O   . ILE A 90  ? 0.2739 0.2437 0.2118 -0.0232 0.0680  0.0665  119 ILE A O   
717  C CB  . ILE A 90  ? 0.2985 0.3032 0.2662 -0.0386 0.0820  0.0753  119 ILE A CB  
718  C CG1 . ILE A 90  ? 0.3081 0.3248 0.2941 -0.0496 0.0816  0.0770  119 ILE A CG1 
719  C CG2 . ILE A 90  ? 0.2773 0.2892 0.2464 -0.0288 0.0787  0.0683  119 ILE A CG2 
720  C CD1 . ILE A 90  ? 0.3033 0.3193 0.2965 -0.0518 0.0722  0.0707  119 ILE A CD1 
721  N N   . GLY A 91  ? 0.3121 0.2823 0.2379 -0.0250 0.0801  0.0780  120 GLY A N   
722  C CA  . GLY A 91  ? 0.3166 0.2807 0.2266 -0.0158 0.0776  0.0761  120 GLY A CA  
723  C C   . GLY A 91  ? 0.3186 0.2661 0.2217 -0.0138 0.0702  0.0758  120 GLY A C   
724  O O   . GLY A 91  ? 0.3053 0.2513 0.2045 -0.0074 0.0643  0.0704  120 GLY A O   
725  N N   . GLN A 92  ? 0.3278 0.2625 0.2304 -0.0194 0.0712  0.0817  121 GLN A N   
726  C CA  . GLN A 92  ? 0.3374 0.2554 0.2347 -0.0167 0.0655  0.0818  121 GLN A CA  
727  C C   . GLN A 92  ? 0.3175 0.2361 0.2248 -0.0166 0.0590  0.0730  121 GLN A C   
728  O O   . GLN A 92  ? 0.3125 0.2244 0.2156 -0.0105 0.0537  0.0701  121 GLN A O   
729  C CB  . GLN A 92  ? 0.3660 0.2682 0.2614 -0.0234 0.0692  0.0896  121 GLN A CB  
730  C CG  . GLN A 92  ? 0.3981 0.2970 0.2809 -0.0223 0.0752  0.0998  121 GLN A CG  
731  C CD  . GLN A 92  ? 0.4306 0.3147 0.3132 -0.0307 0.0805  0.1082  121 GLN A CD  
732  O OE1 . GLN A 92  ? 0.4235 0.3034 0.3171 -0.0399 0.0810  0.1058  121 GLN A OE1 
733  N NE2 . GLN A 92  ? 0.4671 0.3443 0.3366 -0.0285 0.0848  0.1183  121 GLN A NE2 
734  N N   . LEU A 93  ? 0.3096 0.2377 0.2302 -0.0235 0.0597  0.0693  122 LEU A N   
735  C CA  . LEU A 93  ? 0.2972 0.2278 0.2263 -0.0239 0.0538  0.0615  122 LEU A CA  
736  C C   . LEU A 93  ? 0.2820 0.2216 0.2101 -0.0154 0.0501  0.0558  122 LEU A C   
737  O O   . LEU A 93  ? 0.2689 0.2044 0.1972 -0.0121 0.0447  0.0509  122 LEU A O   
738  C CB  . LEU A 93  ? 0.2966 0.2381 0.2396 -0.0333 0.0550  0.0603  122 LEU A CB  
739  C CG  . LEU A 93  ? 0.3145 0.2454 0.2595 -0.0441 0.0574  0.0639  122 LEU A CG  
740  C CD1 . LEU A 93  ? 0.3235 0.2709 0.2831 -0.0539 0.0589  0.0641  122 LEU A CD1 
741  C CD2 . LEU A 93  ? 0.3236 0.2369 0.2652 -0.0456 0.0528  0.0596  122 LEU A CD2 
742  N N   . CYS A 94  ? 0.2924 0.2438 0.2192 -0.0119 0.0535  0.0563  123 CYS A N   
743  C CA  . CYS A 94  ? 0.2765 0.2341 0.2009 -0.0046 0.0506  0.0506  123 CYS A CA  
744  C C   . CYS A 94  ? 0.2850 0.2328 0.1979 0.0014  0.0460  0.0501  123 CYS A C   
745  O O   . CYS A 94  ? 0.2859 0.2338 0.2002 0.0049  0.0407  0.0447  123 CYS A O   
746  C CB  . CYS A 94  ? 0.2747 0.2433 0.1970 -0.0019 0.0563  0.0509  123 CYS A CB  
747  S SG  . CYS A 94  ? 0.2801 0.2650 0.2197 -0.0062 0.0614  0.0509  123 CYS A SG  
748  N N   . ASP A 95  ? 0.3227 0.2632 0.2246 0.0024  0.0481  0.0567  124 ASP A N   
749  C CA  . ASP A 95  ? 0.3284 0.2618 0.2198 0.0084  0.0436  0.0581  124 ASP A CA  
750  C C   . ASP A 95  ? 0.3297 0.2546 0.2265 0.0094  0.0385  0.0559  124 ASP A C   
751  O O   . ASP A 95  ? 0.3389 0.2652 0.2350 0.0144  0.0333  0.0521  124 ASP A O   
752  C CB  . ASP A 95  ? 0.3724 0.2993 0.2521 0.0087  0.0474  0.0673  124 ASP A CB  
753  C CG  . ASP A 95  ? 0.4216 0.3424 0.2899 0.0154  0.0428  0.0715  124 ASP A CG  
754  O OD1 . ASP A 95  ? 0.4788 0.3928 0.3507 0.0182  0.0382  0.0708  124 ASP A OD1 
755  O OD2 . ASP A 95  ? 0.4874 0.4104 0.3431 0.0176  0.0444  0.0765  124 ASP A OD2 
756  N N   . ALA A 96  ? 0.3293 0.2454 0.2316 0.0039  0.0405  0.0576  125 ALA A N   
757  C CA  . ALA A 96  ? 0.3249 0.2305 0.2306 0.0045  0.0371  0.0551  125 ALA A CA  
758  C C   . ALA A 96  ? 0.3019 0.2156 0.2158 0.0050  0.0330  0.0466  125 ALA A C   
759  O O   . ALA A 96  ? 0.3119 0.2221 0.2261 0.0095  0.0292  0.0437  125 ALA A O   
760  C CB  . ALA A 96  ? 0.3349 0.2287 0.2434 -0.0031 0.0408  0.0578  125 ALA A CB  
761  N N   . ALA A 97  ? 0.2932 0.2182 0.2142 0.0007  0.0342  0.0434  126 ALA A N   
762  C CA  . ALA A 97  ? 0.2812 0.2140 0.2100 0.0005  0.0308  0.0366  126 ALA A CA  
763  C C   . ALA A 97  ? 0.2924 0.2303 0.2184 0.0075  0.0273  0.0334  126 ALA A C   
764  O O   . ALA A 97  ? 0.2785 0.2165 0.2076 0.0094  0.0237  0.0291  126 ALA A O   
765  C CB  . ALA A 97  ? 0.2819 0.2265 0.2193 -0.0044 0.0330  0.0358  126 ALA A CB  
766  N N   . ILE A 98  ? 0.2877 0.2299 0.2071 0.0108  0.0286  0.0352  127 ILE A N   
767  C CA  . ILE A 98  ? 0.2934 0.2403 0.2091 0.0159  0.0249  0.0316  127 ILE A CA  
768  C C   . ILE A 98  ? 0.3013 0.2428 0.2115 0.0205  0.0210  0.0339  127 ILE A C   
769  O O   . ILE A 98  ? 0.2914 0.2358 0.2044 0.0232  0.0168  0.0301  127 ILE A O   
770  C CB  . ILE A 98  ? 0.3088 0.2622 0.2184 0.0169  0.0278  0.0313  127 ILE A CB  
771  C CG1 . ILE A 98  ? 0.3216 0.2821 0.2399 0.0146  0.0310  0.0279  127 ILE A CG1 
772  C CG2 . ILE A 98  ? 0.3035 0.2597 0.2061 0.0210  0.0236  0.0280  127 ILE A CG2 
773  C CD1 . ILE A 98  ? 0.3678 0.3335 0.2811 0.0159  0.0359  0.0273  127 ILE A CD1 
774  N N   . ARG A 99  ? 0.3165 0.2511 0.2195 0.0216  0.0226  0.0407  128 ARG A N   
775  C CA  . ARG A 99  ? 0.3449 0.2773 0.2418 0.0275  0.0189  0.0445  128 ARG A CA  
776  C C   . ARG A 99  ? 0.3784 0.3015 0.2803 0.0300  0.0177  0.0456  128 ARG A C   
777  O O   . ARG A 99  ? 0.3961 0.3205 0.2975 0.0359  0.0139  0.0472  128 ARG A O   
778  C CB  . ARG A 99  ? 0.3692 0.2992 0.2543 0.0290  0.0209  0.0523  128 ARG A CB  
779  C CG  . ARG A 99  ? 0.3745 0.3135 0.2510 0.0281  0.0221  0.0510  128 ARG A CG  
780  C CD  . ARG A 99  ? 0.4135 0.3498 0.2761 0.0297  0.0243  0.0599  128 ARG A CD  
781  N NE  . ARG A 99  ? 0.4887 0.4210 0.3464 0.0354  0.0198  0.0668  128 ARG A NE  
782  C CZ  . ARG A 99  ? 0.5563 0.4764 0.4143 0.0372  0.0215  0.0748  128 ARG A CZ  
783  N NH1 . ARG A 99  ? 0.5243 0.4344 0.3841 0.0322  0.0281  0.0781  128 ARG A NH1 
784  N NH2 . ARG A 99  ? 0.5399 0.4577 0.3971 0.0440  0.0169  0.0799  128 ARG A NH2 
785  N N   . TYR A 100 ? 0.3890 0.3030 0.2955 0.0254  0.0211  0.0450  129 TYR A N   
786  C CA  . TYR A 100 ? 0.4405 0.3434 0.3506 0.0272  0.0211  0.0445  129 TYR A CA  
787  C C   . TYR A 100 ? 0.4133 0.3178 0.3313 0.0228  0.0209  0.0368  129 TYR A C   
788  O O   . TYR A 100 ? 0.4862 0.3812 0.4062 0.0230  0.0217  0.0346  129 TYR A O   
789  C CB  . TYR A 100 ? 0.4513 0.3378 0.3573 0.0253  0.0256  0.0506  129 TYR A CB  
790  C CG  . TYR A 100 ? 0.4733 0.3569 0.3710 0.0316  0.0253  0.0596  129 TYR A CG  
791  C CD1 . TYR A 100 ? 0.5170 0.3978 0.4145 0.0405  0.0226  0.0627  129 TYR A CD1 
792  C CD2 . TYR A 100 ? 0.4833 0.3692 0.3736 0.0293  0.0275  0.0653  129 TYR A CD2 
793  C CE1 . TYR A 100 ? 0.5194 0.3997 0.4095 0.0469  0.0213  0.0718  129 TYR A CE1 
794  C CE2 . TYR A 100 ? 0.5231 0.4075 0.4044 0.0351  0.0267  0.0740  129 TYR A CE2 
795  C CZ  . TYR A 100 ? 0.5180 0.3997 0.3991 0.0439  0.0231  0.0775  129 TYR A CZ  
796  O OH  . TYR A 100 ? 0.5528 0.4345 0.4251 0.0500  0.0216  0.0871  129 TYR A OH  
797  N N   . SER A 101 ? 0.4189 0.3349 0.3404 0.0190  0.0202  0.0327  130 SER A N   
798  C CA  . SER A 101 ? 0.4153 0.3340 0.3436 0.0144  0.0198  0.0268  130 SER A CA  
799  C C   . SER A 101 ? 0.3938 0.3009 0.3224 0.0084  0.0225  0.0268  130 SER A C   
800  O O   . SER A 101 ? 0.4193 0.3232 0.3503 0.0060  0.0218  0.0220  130 SER A O   
801  C CB  . SER A 101 ? 0.4269 0.3495 0.3584 0.0186  0.0166  0.0224  130 SER A CB  
802  O OG  . SER A 101 ? 0.3542 0.2849 0.2911 0.0148  0.0156  0.0177  130 SER A OG  
803  N N   . ASP A 102 ? 0.3601 0.2613 0.2856 0.0047  0.0258  0.0317  131 ASP A N   
804  C CA  . ASP A 102 ? 0.3206 0.2091 0.2456 -0.0022 0.0286  0.0321  131 ASP A CA  
805  C C   . ASP A 102 ? 0.3084 0.2051 0.2401 -0.0105 0.0275  0.0272  131 ASP A C   
806  O O   . ASP A 102 ? 0.3050 0.2155 0.2415 -0.0130 0.0275  0.0281  131 ASP A O   
807  C CB  . ASP A 102 ? 0.3219 0.2042 0.2426 -0.0045 0.0326  0.0396  131 ASP A CB  
808  C CG  . ASP A 102 ? 0.3215 0.1878 0.2409 -0.0126 0.0360  0.0408  131 ASP A CG  
809  O OD1 . ASP A 102 ? 0.3204 0.1904 0.2452 -0.0216 0.0358  0.0367  131 ASP A OD1 
810  O OD2 . ASP A 102 ? 0.3341 0.1843 0.2472 -0.0100 0.0389  0.0462  131 ASP A OD2 
811  N N   . GLY A 103 ? 0.2943 0.1829 0.2257 -0.0145 0.0268  0.0221  132 GLY A N   
812  C CA  . GLY A 103 ? 0.2711 0.1688 0.2078 -0.0222 0.0245  0.0175  132 GLY A CA  
813  C C   . GLY A 103 ? 0.2662 0.1666 0.2066 -0.0327 0.0260  0.0198  132 GLY A C   
814  O O   . GLY A 103 ? 0.2486 0.1656 0.1966 -0.0367 0.0242  0.0199  132 GLY A O   
815  N N   . THR A 104 ? 0.2848 0.1691 0.2206 -0.0374 0.0294  0.0221  133 THR A N   
816  C CA  . THR A 104 ? 0.3021 0.1892 0.2423 -0.0486 0.0312  0.0248  133 THR A CA  
817  C C   . THR A 104 ? 0.2916 0.1950 0.2378 -0.0468 0.0332  0.0313  133 THR A C   
818  O O   . THR A 104 ? 0.2847 0.2023 0.2394 -0.0542 0.0333  0.0326  133 THR A O   
819  C CB  . THR A 104 ? 0.3377 0.2017 0.2711 -0.0537 0.0353  0.0266  133 THR A CB  
820  O OG1 . THR A 104 ? 0.3586 0.2079 0.2862 -0.0546 0.0340  0.0193  133 THR A OG1 
821  C CG2 . THR A 104 ? 0.3504 0.2177 0.2891 -0.0673 0.0371  0.0290  133 THR A CG2 
822  N N   . ALA A 105 ? 0.2897 0.1914 0.2311 -0.0372 0.0351  0.0353  134 ALA A N   
823  C CA  . ALA A 105 ? 0.2736 0.1897 0.2181 -0.0347 0.0376  0.0403  134 ALA A CA  
824  C C   . ALA A 105 ? 0.2613 0.1979 0.2154 -0.0340 0.0350  0.0372  134 ALA A C   
825  O O   . ALA A 105 ? 0.2639 0.2148 0.2258 -0.0375 0.0374  0.0400  134 ALA A O   
826  C CB  . ALA A 105 ? 0.2732 0.1842 0.2089 -0.0245 0.0385  0.0434  134 ALA A CB  
827  N N   . ALA A 106 ? 0.2541 0.1924 0.2081 -0.0294 0.0305  0.0318  135 ALA A N   
828  C CA  . ALA A 106 ? 0.2452 0.2006 0.2076 -0.0280 0.0280  0.0295  135 ALA A CA  
829  C C   . ALA A 106 ? 0.2454 0.2109 0.2171 -0.0377 0.0265  0.0293  135 ALA A C   
830  O O   . ALA A 106 ? 0.2573 0.2399 0.2388 -0.0382 0.0272  0.0316  135 ALA A O   
831  C CB  . ALA A 106 ? 0.2390 0.1925 0.1987 -0.0220 0.0241  0.0246  135 ALA A CB  
832  N N   . ASN A 107 ? 0.2625 0.2177 0.2314 -0.0457 0.0248  0.0267  136 ASN A N   
833  C CA  . ASN A 107 ? 0.2473 0.2133 0.2244 -0.0565 0.0224  0.0262  136 ASN A CA  
834  C C   . ASN A 107 ? 0.2432 0.2192 0.2286 -0.0623 0.0264  0.0323  136 ASN A C   
835  O O   . ASN A 107 ? 0.2324 0.2277 0.2296 -0.0671 0.0249  0.0341  136 ASN A O   
836  C CB  . ASN A 107 ? 0.2567 0.2082 0.2273 -0.0653 0.0200  0.0211  136 ASN A CB  
837  C CG  . ASN A 107 ? 0.2579 0.2054 0.2227 -0.0616 0.0158  0.0148  136 ASN A CG  
838  O OD1 . ASN A 107 ? 0.2396 0.1973 0.2070 -0.0537 0.0138  0.0146  136 ASN A OD1 
839  N ND2 . ASN A 107 ? 0.2794 0.2108 0.2358 -0.0673 0.0151  0.0094  136 ASN A ND2 
840  N N   . LEU A 108 ? 0.2546 0.2185 0.2342 -0.0620 0.0318  0.0361  137 LEU A N   
841  C CA  . LEU A 108 ? 0.2559 0.2285 0.2426 -0.0680 0.0368  0.0424  137 LEU A CA  
842  C C   . LEU A 108 ? 0.2475 0.2402 0.2423 -0.0605 0.0395  0.0459  137 LEU A C   
843  O O   . LEU A 108 ? 0.2413 0.2517 0.2482 -0.0652 0.0420  0.0499  137 LEU A O   
844  C CB  . LEU A 108 ? 0.2678 0.2208 0.2446 -0.0692 0.0421  0.0465  137 LEU A CB  
845  C CG  . LEU A 108 ? 0.2873 0.2187 0.2573 -0.0781 0.0412  0.0437  137 LEU A CG  
846  C CD1 . LEU A 108 ? 0.3066 0.2164 0.2656 -0.0753 0.0463  0.0484  137 LEU A CD1 
847  C CD2 . LEU A 108 ? 0.2988 0.2379 0.2783 -0.0936 0.0406  0.0438  137 LEU A CD2 
848  N N   . LEU A 109 ? 0.2458 0.2360 0.2345 -0.0488 0.0393  0.0441  138 LEU A N   
849  C CA  . LEU A 109 ? 0.2517 0.2577 0.2463 -0.0413 0.0423  0.0459  138 LEU A CA  
850  C C   . LEU A 109 ? 0.2503 0.2750 0.2585 -0.0419 0.0386  0.0448  138 LEU A C   
851  O O   . LEU A 109 ? 0.2399 0.2825 0.2597 -0.0411 0.0420  0.0485  138 LEU A O   
852  C CB  . LEU A 109 ? 0.2418 0.2389 0.2255 -0.0303 0.0425  0.0435  138 LEU A CB  
853  C CG  . LEU A 109 ? 0.2683 0.2518 0.2392 -0.0281 0.0466  0.0466  138 LEU A CG  
854  C CD1 . LEU A 109 ? 0.2582 0.2330 0.2182 -0.0187 0.0442  0.0432  138 LEU A CD1 
855  C CD2 . LEU A 109 ? 0.2747 0.2673 0.2473 -0.0282 0.0541  0.0520  138 LEU A CD2 
856  N N   . LEU A 110 ? 0.2495 0.2705 0.2563 -0.0430 0.0318  0.0401  139 LEU A N   
857  C CA  . LEU A 110 ? 0.2348 0.2730 0.2531 -0.0449 0.0272  0.0399  139 LEU A CA  
858  C C   . LEU A 110 ? 0.2396 0.2947 0.2714 -0.0549 0.0278  0.0444  139 LEU A C   
859  O O   . LEU A 110 ? 0.2270 0.3030 0.2725 -0.0527 0.0282  0.0481  139 LEU A O   
860  C CB  . LEU A 110 ? 0.2327 0.2624 0.2446 -0.0471 0.0203  0.0345  139 LEU A CB  
861  C CG  . LEU A 110 ? 0.2303 0.2511 0.2341 -0.0370 0.0190  0.0308  139 LEU A CG  
862  C CD1 . LEU A 110 ? 0.2354 0.2455 0.2310 -0.0398 0.0138  0.0254  139 LEU A CD1 
863  C CD2 . LEU A 110 ? 0.2263 0.2616 0.2387 -0.0293 0.0190  0.0328  139 LEU A CD2 
864  N N   . ALA A 111 ? 0.2537 0.2999 0.2821 -0.0658 0.0280  0.0443  140 ALA A N   
865  C CA  . ALA A 111 ? 0.2620 0.3237 0.3032 -0.0777 0.0282  0.0482  140 ALA A CA  
866  C C   . ALA A 111 ? 0.2695 0.3460 0.3209 -0.0746 0.0361  0.0551  140 ALA A C   
867  O O   . ALA A 111 ? 0.2615 0.3613 0.3295 -0.0794 0.0365  0.0596  140 ALA A O   
868  C CB  . ALA A 111 ? 0.2841 0.3283 0.3173 -0.0901 0.0275  0.0460  140 ALA A CB  
869  N N   . ASP A 112 ? 0.2802 0.3441 0.3217 -0.0669 0.0427  0.0562  141 ASP A N   
870  C CA  . ASP A 112 ? 0.2903 0.3669 0.3388 -0.0632 0.0512  0.0620  141 ASP A CA  
871  C C   . ASP A 112 ? 0.2854 0.3819 0.3456 -0.0532 0.0518  0.0629  141 ASP A C   
872  O O   . ASP A 112 ? 0.3113 0.4287 0.3862 -0.0528 0.0568  0.0680  141 ASP A O   
873  C CB  . ASP A 112 ? 0.3011 0.3600 0.3340 -0.0567 0.0575  0.0626  141 ASP A CB  
874  C CG  . ASP A 112 ? 0.3002 0.3709 0.3377 -0.0543 0.0674  0.0686  141 ASP A CG  
875  O OD1 . ASP A 112 ? 0.3393 0.4182 0.3852 -0.0642 0.0709  0.0737  141 ASP A OD1 
876  O OD2 . ASP A 112 ? 0.2929 0.3649 0.3257 -0.0432 0.0718  0.0679  141 ASP A OD2 
877  N N   . LEU A 113 ? 0.2662 0.3558 0.3204 -0.0451 0.0470  0.0580  142 LEU A N   
878  C CA  . LEU A 113 ? 0.2589 0.3618 0.3216 -0.0343 0.0481  0.0586  142 LEU A CA  
879  C C   . LEU A 113 ? 0.2506 0.3771 0.3319 -0.0381 0.0433  0.0620  142 LEU A C   
880  O O   . LEU A 113 ? 0.2500 0.3957 0.3457 -0.0323 0.0475  0.0666  142 LEU A O   
881  C CB  . LEU A 113 ? 0.2448 0.3315 0.2948 -0.0258 0.0445  0.0528  142 LEU A CB  
882  C CG  . LEU A 113 ? 0.2438 0.3381 0.2992 -0.0141 0.0468  0.0528  142 LEU A CG  
883  C CD1 . LEU A 113 ? 0.2565 0.3494 0.3083 -0.0071 0.0566  0.0536  142 LEU A CD1 
884  C CD2 . LEU A 113 ? 0.2512 0.3314 0.2965 -0.0094 0.0411  0.0474  142 LEU A CD2 
885  N N   . GLY A 114 ? 0.2461 0.3716 0.3268 -0.0473 0.0346  0.0599  143 GLY A N   
886  C CA  . GLY A 114 ? 0.2438 0.3905 0.3388 -0.0499 0.0277  0.0625  143 GLY A CA  
887  C C   . GLY A 114 ? 0.2667 0.4244 0.3692 -0.0658 0.0228  0.0639  143 GLY A C   
888  O O   . GLY A 114 ? 0.2550 0.4321 0.3688 -0.0702 0.0157  0.0661  143 GLY A O   
889  N N   . GLY A 115 ? 0.2824 0.4282 0.3787 -0.0751 0.0263  0.0631  144 GLY A N   
890  C CA  . GLY A 115 ? 0.3215 0.4728 0.4223 -0.0919 0.0219  0.0631  144 GLY A CA  
891  C C   . GLY A 115 ? 0.3636 0.4962 0.4494 -0.0987 0.0138  0.0555  144 GLY A C   
892  O O   . GLY A 115 ? 0.3281 0.4458 0.4015 -0.0900 0.0116  0.0509  144 GLY A O   
893  N N   . PRO A 116 ? 0.4257 0.5585 0.5121 -0.1150 0.0095  0.0536  145 PRO A N   
894  C CA  . PRO A 116 ? 0.4843 0.6017 0.5569 -0.1223 0.0019  0.0457  145 PRO A CA  
895  C C   . PRO A 116 ? 0.4576 0.5956 0.5367 -0.1189 -0.0065 0.0462  145 PRO A C   
896  O O   . PRO A 116 ? 0.5728 0.7404 0.6700 -0.1223 -0.0097 0.0521  145 PRO A O   
897  C CB  . PRO A 116 ? 0.5168 0.6331 0.5915 -0.1414 0.0006  0.0446  145 PRO A CB  
898  C CG  . PRO A 116 ? 0.5136 0.6610 0.6112 -0.1448 0.0032  0.0535  145 PRO A CG  
899  C CD  . PRO A 116 ? 0.4677 0.6160 0.5681 -0.1277 0.0120  0.0586  145 PRO A CD  
900  N N   . GLY A 117 A 0.4074 0.5311 0.4728 -0.1114 -0.0095 0.0411  145 GLY A N   
901  C CA  . GLY A 117 A 0.3787 0.5190 0.4476 -0.1080 -0.0172 0.0420  145 GLY A CA  
902  C C   . GLY A 117 A 0.3341 0.4831 0.4100 -0.0907 -0.0142 0.0473  145 GLY A C   
903  O O   . GLY A 117 A 0.3367 0.4881 0.4089 -0.0848 -0.0189 0.0468  145 GLY A O   
904  N N   . GLY A 118 B 0.3023 0.4555 0.3875 -0.0831 -0.0060 0.0522  145 GLY A N   
905  C CA  . GLY A 118 B 0.2688 0.4330 0.3632 -0.0680 -0.0026 0.0574  145 GLY A CA  
906  C C   . GLY A 118 B 0.2505 0.3920 0.3327 -0.0561 0.0044  0.0542  145 GLY A C   
907  O O   . GLY A 118 B 0.2421 0.3879 0.3291 -0.0437 0.0079  0.0570  145 GLY A O   
908  N N   . GLY A 119 C 0.2523 0.3694 0.3186 -0.0597 0.0063  0.0483  145 GLY A N   
909  C CA  . GLY A 119 C 0.2448 0.3426 0.3001 -0.0499 0.0124  0.0458  145 GLY A CA  
910  C C   . GLY A 119 C 0.2357 0.3276 0.2855 -0.0390 0.0108  0.0437  145 GLY A C   
911  O O   . GLY A 119 C 0.2312 0.3210 0.2815 -0.0287 0.0160  0.0447  145 GLY A O   
912  N N   . THR A 120 D 0.2465 0.3344 0.2898 -0.0417 0.0041  0.0403  145 THR A N   
913  C CA  . THR A 120 D 0.2435 0.3237 0.2804 -0.0328 0.0029  0.0383  145 THR A CA  
914  C C   . THR A 120 D 0.2247 0.3219 0.2746 -0.0244 0.0034  0.0443  145 THR A C   
915  O O   . THR A 120 D 0.2026 0.2927 0.2502 -0.0147 0.0068  0.0439  145 THR A O   
916  C CB  . THR A 120 D 0.2605 0.3329 0.2868 -0.0380 -0.0033 0.0336  145 THR A CB  
917  O OG1 . THR A 120 D 0.2592 0.3489 0.2925 -0.0456 -0.0096 0.0362  145 THR A OG1 
918  C CG2 . THR A 120 D 0.2831 0.3363 0.2966 -0.0443 -0.0025 0.0275  145 THR A CG2 
919  N N   . ALA A 121 ? 0.2153 0.3346 0.2791 -0.0283 0.0003  0.0499  146 ALA A N   
920  C CA  . ALA A 121 ? 0.2202 0.3568 0.2986 -0.0193 0.0016  0.0569  146 ALA A CA  
921  C C   . ALA A 121 ? 0.2101 0.3450 0.2936 -0.0106 0.0112  0.0583  146 ALA A C   
922  O O   . ALA A 121 ? 0.1866 0.3192 0.2724 0.0005  0.0151  0.0599  146 ALA A O   
923  C CB  . ALA A 121 ? 0.2226 0.3858 0.3162 -0.0256 -0.0039 0.0633  146 ALA A CB  
924  N N   . ALA A 122 ? 0.2110 0.3456 0.2952 -0.0159 0.0157  0.0577  147 ALA A N   
925  C CA  . ALA A 122 ? 0.2035 0.3371 0.2908 -0.0082 0.0254  0.0589  147 ALA A CA  
926  C C   . ALA A 122 ? 0.2021 0.3123 0.2736 -0.0009 0.0289  0.0529  147 ALA A C   
927  O O   . ALA A 122 ? 0.2015 0.3091 0.2738 0.0088  0.0355  0.0530  147 ALA A O   
928  C CB  . ALA A 122 ? 0.2077 0.3458 0.2978 -0.0164 0.0293  0.0601  147 ALA A CB  
929  N N   . PHE A 123 ? 0.2020 0.2949 0.2587 -0.0059 0.0249  0.0474  148 PHE A N   
930  C CA  . PHE A 123 ? 0.2023 0.2755 0.2450 -0.0001 0.0272  0.0421  148 PHE A CA  
931  C C   . PHE A 123 ? 0.2039 0.2763 0.2486 0.0084  0.0266  0.0421  148 PHE A C   
932  O O   . PHE A 123 ? 0.2106 0.2746 0.2513 0.0160  0.0316  0.0400  148 PHE A O   
933  C CB  . PHE A 123 ? 0.2165 0.2741 0.2458 -0.0062 0.0228  0.0371  148 PHE A CB  
934  C CG  . PHE A 123 ? 0.2136 0.2550 0.2311 -0.0004 0.0230  0.0322  148 PHE A CG  
935  C CD1 . PHE A 123 ? 0.2253 0.2568 0.2346 0.0035  0.0278  0.0300  148 PHE A CD1 
936  C CD2 . PHE A 123 ? 0.2282 0.2663 0.2434 0.0014  0.0186  0.0304  148 PHE A CD2 
937  C CE1 . PHE A 123 ? 0.2230 0.2425 0.2231 0.0081  0.0274  0.0256  148 PHE A CE1 
938  C CE2 . PHE A 123 ? 0.2212 0.2466 0.2277 0.0059  0.0189  0.0263  148 PHE A CE2 
939  C CZ  . PHE A 123 ? 0.2080 0.2245 0.2072 0.0088  0.0229  0.0237  148 PHE A CZ  
940  N N   . THR A 124 ? 0.1797 0.2601 0.2295 0.0067  0.0204  0.0446  149 THR A N   
941  C CA  . THR A 124 ? 0.1872 0.2660 0.2386 0.0141  0.0194  0.0458  149 THR A CA  
942  C C   . THR A 124 ? 0.1914 0.2786 0.2544 0.0235  0.0260  0.0502  149 THR A C   
943  O O   . THR A 124 ? 0.2059 0.2830 0.2661 0.0313  0.0297  0.0487  149 THR A O   
944  C CB  . THR A 124 ? 0.1882 0.2762 0.2424 0.0097  0.0114  0.0489  149 THR A CB  
945  O OG1 . THR A 124 ? 0.1932 0.2701 0.2347 0.0020  0.0072  0.0433  149 THR A OG1 
946  C CG2 . THR A 124 ? 0.1886 0.2748 0.2444 0.0172  0.0106  0.0517  149 THR A CG2 
947  N N   . GLY A 125 ? 0.1731 0.2785 0.2493 0.0223  0.0279  0.0554  150 GLY A N   
948  C CA  . GLY A 125 ? 0.1909 0.3067 0.2798 0.0315  0.0353  0.0599  150 GLY A CA  
949  C C   . GLY A 125 ? 0.1976 0.2982 0.2775 0.0374  0.0445  0.0546  150 GLY A C   
950  O O   . GLY A 125 ? 0.2089 0.3070 0.2925 0.0474  0.0508  0.0553  150 GLY A O   
951  N N   . TYR A 126 ? 0.1978 0.2876 0.2650 0.0314  0.0453  0.0494  151 TYR A N   
952  C CA  . TYR A 126 ? 0.2207 0.2964 0.2768 0.0359  0.0527  0.0441  151 TYR A CA  
953  C C   . TYR A 126 ? 0.2278 0.2863 0.2745 0.0415  0.0522  0.0392  151 TYR A C   
954  O O   . TYR A 126 ? 0.2173 0.2684 0.2614 0.0490  0.0593  0.0365  151 TYR A O   
955  C CB  . TYR A 126 ? 0.2200 0.2887 0.2643 0.0282  0.0525  0.0411  151 TYR A CB  
956  C CG  . TYR A 126 ? 0.2318 0.2876 0.2631 0.0327  0.0595  0.0361  151 TYR A CG  
957  C CD1 . TYR A 126 ? 0.2390 0.3011 0.2744 0.0385  0.0691  0.0374  151 TYR A CD1 
958  C CD2 . TYR A 126 ? 0.2232 0.2616 0.2382 0.0315  0.0567  0.0300  151 TYR A CD2 
959  C CE1 . TYR A 126 ? 0.2516 0.3014 0.2728 0.0423  0.0756  0.0321  151 TYR A CE1 
960  C CE2 . TYR A 126 ? 0.2452 0.2731 0.2474 0.0349  0.0621  0.0252  151 TYR A CE2 
961  C CZ  . TYR A 126 ? 0.2529 0.2858 0.2569 0.0400  0.0715  0.0260  151 TYR A CZ  
962  O OH  . TYR A 126 ? 0.2913 0.3136 0.2805 0.0428  0.0768  0.0206  151 TYR A OH  
963  N N   . LEU A 127 ? 0.2161 0.2679 0.2575 0.0373  0.0444  0.0376  152 LEU A N   
964  C CA  . LEU A 127 ? 0.2310 0.2679 0.2651 0.0413  0.0438  0.0336  152 LEU A CA  
965  C C   . LEU A 127 ? 0.2245 0.2648 0.2693 0.0502  0.0475  0.0378  152 LEU A C   
966  O O   . LEU A 127 ? 0.2373 0.2643 0.2773 0.0560  0.0523  0.0341  152 LEU A O   
967  C CB  . LEU A 127 ? 0.2238 0.2560 0.2524 0.0354  0.0355  0.0324  152 LEU A CB  
968  C CG  . LEU A 127 ? 0.2406 0.2670 0.2587 0.0280  0.0321  0.0284  152 LEU A CG  
969  C CD1 . LEU A 127 ? 0.2354 0.2561 0.2482 0.0242  0.0256  0.0266  152 LEU A CD1 
970  C CD2 . LEU A 127 ? 0.2445 0.2594 0.2515 0.0297  0.0365  0.0229  152 LEU A CD2 
971  N N   . ARG A 128 ? 0.2178 0.2760 0.2775 0.0514  0.0455  0.0456  153 ARG A N   
972  C CA  . ARG A 128 ? 0.2145 0.2776 0.2862 0.0612  0.0492  0.0513  153 ARG A CA  
973  C C   . ARG A 128 ? 0.2392 0.2989 0.3129 0.0698  0.0603  0.0494  153 ARG A C   
974  O O   . ARG A 128 ? 0.2319 0.2826 0.3078 0.0788  0.0656  0.0497  153 ARG A O   
975  C CB  . ARG A 128 ? 0.2121 0.2995 0.3010 0.0611  0.0448  0.0611  153 ARG A CB  
976  C CG  . ARG A 128 ? 0.2090 0.3003 0.2949 0.0530  0.0341  0.0630  153 ARG A CG  
977  C CD  . ARG A 128 ? 0.2066 0.2891 0.2906 0.0577  0.0316  0.0655  153 ARG A CD  
978  N NE  . ARG A 128 ? 0.2027 0.2892 0.2816 0.0493  0.0220  0.0666  153 ARG A NE  
979  C CZ  . ARG A 128 ? 0.1863 0.2599 0.2509 0.0421  0.0184  0.0600  153 ARG A CZ  
980  N NH1 . ARG A 128 ? 0.1812 0.2368 0.2349 0.0421  0.0225  0.0522  153 ARG A NH1 
981  N NH2 . ARG A 128 ? 0.1879 0.2676 0.2490 0.0351  0.0107  0.0615  153 ARG A NH2 
982  N N   . SER A 129 ? 0.2416 0.3076 0.3142 0.0668  0.0643  0.0477  154 SER A N   
983  C CA  . SER A 129 ? 0.2561 0.3201 0.3290 0.0742  0.0757  0.0455  154 SER A CA  
984  C C   . SER A 129 ? 0.2771 0.3160 0.3317 0.0762  0.0798  0.0357  154 SER A C   
985  O O   . SER A 129 ? 0.2829 0.3148 0.3353 0.0839  0.0896  0.0326  154 SER A O   
986  C CB  . SER A 129 ? 0.2452 0.3222 0.3199 0.0693  0.0789  0.0465  154 SER A CB  
987  O OG  . SER A 129 ? 0.2298 0.2938 0.2864 0.0618  0.0771  0.0397  154 SER A OG  
988  N N   . LEU A 130 ? 0.2870 0.3130 0.3282 0.0690  0.0725  0.0307  155 LEU A N   
989  C CA  . LEU A 130 ? 0.3086 0.3129 0.3333 0.0692  0.0745  0.0216  155 LEU A CA  
990  C C   . LEU A 130 ? 0.3338 0.3255 0.3596 0.0732  0.0735  0.0212  155 LEU A C   
991  O O   . LEU A 130 ? 0.3458 0.3195 0.3588 0.0719  0.0742  0.0137  155 LEU A O   
992  C CB  . LEU A 130 ? 0.3025 0.3011 0.3136 0.0597  0.0676  0.0169  155 LEU A CB  
993  C CG  . LEU A 130 ? 0.2922 0.2999 0.3000 0.0547  0.0678  0.0178  155 LEU A CG  
994  C CD1 . LEU A 130 ? 0.2813 0.2823 0.2773 0.0466  0.0600  0.0145  155 LEU A CD1 
995  C CD2 . LEU A 130 ? 0.3239 0.3285 0.3245 0.0587  0.0774  0.0142  155 LEU A CD2 
996  N N   . GLY A 131 ? 0.3331 0.3346 0.3738 0.0775  0.0716  0.0296  156 GLY A N   
997  C CA  . GLY A 131 ? 0.3406 0.3301 0.3826 0.0814  0.0709  0.0309  156 GLY A CA  
998  C C   . GLY A 131 ? 0.3261 0.3128 0.3630 0.0732  0.0610  0.0312  156 GLY A C   
999  O O   . GLY A 131 ? 0.3246 0.3003 0.3610 0.0749  0.0601  0.0323  156 GLY A O   
1000 N N   . ASP A 132 ? 0.2928 0.2894 0.3268 0.0648  0.0541  0.0309  157 ASP A N   
1001 C CA  . ASP A 132 ? 0.2886 0.2855 0.3195 0.0579  0.0455  0.0320  157 ASP A CA  
1002 C C   . ASP A 132 ? 0.2677 0.2817 0.3111 0.0586  0.0408  0.0416  157 ASP A C   
1003 O O   . ASP A 132 ? 0.2326 0.2626 0.2816 0.0552  0.0380  0.0447  157 ASP A O   
1004 C CB  . ASP A 132 ? 0.2747 0.2716 0.2957 0.0493  0.0411  0.0268  157 ASP A CB  
1005 C CG  . ASP A 132 ? 0.2679 0.2665 0.2859 0.0425  0.0331  0.0275  157 ASP A CG  
1006 O OD1 . ASP A 132 ? 0.2491 0.2498 0.2719 0.0437  0.0305  0.0325  157 ASP A OD1 
1007 O OD2 . ASP A 132 ? 0.2513 0.2483 0.2615 0.0367  0.0301  0.0233  157 ASP A OD2 
1008 N N   . THR A 133 ? 0.2531 0.2636 0.3002 0.0623  0.0396  0.0466  158 THR A N   
1009 C CA  . THR A 133 ? 0.2532 0.2805 0.3114 0.0638  0.0348  0.0566  158 THR A CA  
1010 C C   . THR A 133 ? 0.2477 0.2767 0.2991 0.0556  0.0264  0.0572  158 THR A C   
1011 O O   . THR A 133 ? 0.2461 0.2876 0.3037 0.0559  0.0215  0.0651  158 THR A O   
1012 C CB  . THR A 133 ? 0.2828 0.3064 0.3498 0.0743  0.0391  0.0637  158 THR A CB  
1013 O OG1 . THR A 133 ? 0.2933 0.2968 0.3508 0.0735  0.0397  0.0606  158 THR A OG1 
1014 C CG2 . THR A 133 ? 0.3087 0.3306 0.3826 0.0835  0.0487  0.0629  158 THR A CG2 
1015 N N   . VAL A 134 ? 0.2285 0.2459 0.2675 0.0489  0.0249  0.0492  159 VAL A N   
1016 C CA  . VAL A 134 ? 0.2440 0.2601 0.2758 0.0425  0.0189  0.0489  159 VAL A CA  
1017 C C   . VAL A 134 ? 0.2255 0.2485 0.2520 0.0342  0.0142  0.0448  159 VAL A C   
1018 O O   . VAL A 134 ? 0.2340 0.2645 0.2585 0.0294  0.0087  0.0471  159 VAL A O   
1019 C CB  . VAL A 134 ? 0.2663 0.2639 0.2899 0.0421  0.0214  0.0439  159 VAL A CB  
1020 C CG1 . VAL A 134 ? 0.2884 0.2834 0.3029 0.0345  0.0170  0.0402  159 VAL A CG1 
1021 C CG2 . VAL A 134 ? 0.2788 0.2695 0.3069 0.0484  0.0242  0.0502  159 VAL A CG2 
1022 N N   . SER A 135 ? 0.2232 0.2419 0.2459 0.0324  0.0168  0.0386  160 SER A N   
1023 C CA  . SER A 135 ? 0.2146 0.2354 0.2312 0.0252  0.0134  0.0345  160 SER A CA  
1024 C C   . SER A 135 ? 0.2066 0.2433 0.2296 0.0217  0.0098  0.0389  160 SER A C   
1025 O O   . SER A 135 ? 0.2381 0.2859 0.2718 0.0254  0.0114  0.0442  160 SER A O   
1026 C CB  . SER A 135 ? 0.2345 0.2478 0.2460 0.0250  0.0170  0.0287  160 SER A CB  
1027 O OG  . SER A 135 ? 0.2389 0.2389 0.2439 0.0269  0.0193  0.0240  160 SER A OG  
1028 N N   . ARG A 136 ? 0.2040 0.2420 0.2209 0.0142  0.0054  0.0364  161 ARG A N   
1029 C CA  . ARG A 136 ? 0.2000 0.2516 0.2214 0.0086  0.0016  0.0390  161 ARG A CA  
1030 C C   . ARG A 136 ? 0.2097 0.2547 0.2221 0.0010  0.0002  0.0331  161 ARG A C   
1031 O O   . ARG A 136 ? 0.2100 0.2443 0.2125 -0.0007 -0.0007 0.0285  161 ARG A O   
1032 C CB  . ARG A 136 ? 0.2025 0.2651 0.2264 0.0072  -0.0039 0.0445  161 ARG A CB  
1033 C CG  . ARG A 136 ? 0.2201 0.2731 0.2325 0.0050  -0.0062 0.0414  161 ARG A CG  
1034 C CD  . ARG A 136 ? 0.2372 0.3007 0.2500 0.0039  -0.0114 0.0474  161 ARG A CD  
1035 N NE  . ARG A 136 ? 0.2437 0.3200 0.2564 -0.0041 -0.0170 0.0478  161 ARG A NE  
1036 C CZ  . ARG A 136 ? 0.2832 0.3730 0.2959 -0.0070 -0.0231 0.0531  161 ARG A CZ  
1037 N NH1 . ARG A 136 ? 0.2725 0.3641 0.2853 -0.0018 -0.0240 0.0593  161 ARG A NH1 
1038 N NH2 . ARG A 136 ? 0.2870 0.3887 0.2996 -0.0155 -0.0285 0.0525  161 ARG A NH2 
1039 N N   . LEU A 137 ? 0.2083 0.2599 0.2249 -0.0032 0.0005  0.0337  162 LEU A N   
1040 C CA  . LEU A 137 ? 0.2038 0.2497 0.2132 -0.0112 -0.0010 0.0293  162 LEU A CA  
1041 C C   . LEU A 137 ? 0.2213 0.2811 0.2353 -0.0192 -0.0061 0.0319  162 LEU A C   
1042 O O   . LEU A 137 ? 0.2112 0.2870 0.2373 -0.0193 -0.0065 0.0374  162 LEU A O   
1043 C CB  . LEU A 137 ? 0.2108 0.2500 0.2194 -0.0109 0.0039  0.0276  162 LEU A CB  
1044 C CG  . LEU A 137 ? 0.2138 0.2414 0.2131 -0.0173 0.0036  0.0232  162 LEU A CG  
1045 C CD1 . LEU A 137 ? 0.2272 0.2406 0.2160 -0.0145 0.0034  0.0184  162 LEU A CD1 
1046 C CD2 . LEU A 137 ? 0.2322 0.2560 0.2320 -0.0176 0.0083  0.0239  162 LEU A CD2 
1047 N N   . ASP A 138 ? 0.2196 0.2734 0.2237 -0.0261 -0.0098 0.0274  163 ASP A N   
1048 C CA  . ASP A 138 ? 0.2480 0.3137 0.2529 -0.0348 -0.0159 0.0284  163 ASP A CA  
1049 C C   . ASP A 138 ? 0.2762 0.3335 0.2739 -0.0450 -0.0164 0.0228  163 ASP A C   
1050 O O   . ASP A 138 ? 0.3276 0.3966 0.3299 -0.0538 -0.0203 0.0241  163 ASP A O   
1051 C CB  . ASP A 138 ? 0.2464 0.3135 0.2442 -0.0344 -0.0201 0.0283  163 ASP A CB  
1052 C CG  . ASP A 138 ? 0.2422 0.3180 0.2482 -0.0251 -0.0198 0.0353  163 ASP A CG  
1053 O OD1 . ASP A 138 ? 0.2661 0.3599 0.2822 -0.0252 -0.0234 0.0421  163 ASP A OD1 
1054 O OD2 . ASP A 138 ? 0.2283 0.2926 0.2313 -0.0178 -0.0157 0.0342  163 ASP A OD2 
1055 N N   . ALA A 139 ? 0.2513 0.2886 0.2382 -0.0440 -0.0128 0.0169  164 ALA A N   
1056 C CA  . ALA A 139 ? 0.2552 0.2806 0.2344 -0.0526 -0.0123 0.0115  164 ALA A CA  
1057 C C   . ALA A 139 ? 0.2582 0.2717 0.2379 -0.0493 -0.0064 0.0116  164 ALA A C   
1058 O O   . ALA A 139 ? 0.2348 0.2468 0.2170 -0.0402 -0.0030 0.0137  164 ALA A O   
1059 C CB  . ALA A 139 ? 0.2618 0.2732 0.2265 -0.0541 -0.0130 0.0047  164 ALA A CB  
1060 N N   . GLU A 140 ? 0.2744 0.2779 0.2499 -0.0571 -0.0052 0.0088  165 GLU A N   
1061 C CA  . GLU A 140 ? 0.3021 0.2917 0.2753 -0.0541 0.0004  0.0092  165 GLU A CA  
1062 C C   . GLU A 140 ? 0.2922 0.2609 0.2527 -0.0510 0.0025  0.0036  165 GLU A C   
1063 O O   . GLU A 140 ? 0.2725 0.2388 0.2269 -0.0496 0.0004  -0.0004 165 GLU A O   
1064 C CB  . GLU A 140 ? 0.3401 0.3331 0.3189 -0.0636 0.0014  0.0116  165 GLU A CB  
1065 C CG  . GLU A 140 ? 0.4078 0.3909 0.3794 -0.0759 -0.0007 0.0064  165 GLU A CG  
1066 C CD  . GLU A 140 ? 0.4662 0.4533 0.4449 -0.0859 0.0007  0.0097  165 GLU A CD  
1067 O OE1 . GLU A 140 ? 0.5051 0.5007 0.4929 -0.0822 0.0044  0.0160  165 GLU A OE1 
1068 O OE2 . GLU A 140 ? 0.5129 0.4954 0.4877 -0.0981 -0.0019 0.0056  165 GLU A OE2 
1069 N N   . GLU A 141 ? 0.2812 0.2360 0.2385 -0.0487 0.0070  0.0044  166 GLU A N   
1070 C CA  . GLU A 141 ? 0.2809 0.2165 0.2283 -0.0441 0.0096  0.0006  166 GLU A CA  
1071 C C   . GLU A 141 ? 0.2840 0.2065 0.2234 -0.0534 0.0094  -0.0050 166 GLU A C   
1072 O O   . GLU A 141 ? 0.2838 0.2068 0.2254 -0.0633 0.0089  -0.0043 166 GLU A O   
1073 C CB  . GLU A 141 ? 0.2877 0.2128 0.2339 -0.0397 0.0141  0.0044  166 GLU A CB  
1074 C CG  . GLU A 141 ? 0.2828 0.2170 0.2333 -0.0304 0.0150  0.0087  166 GLU A CG  
1075 C CD  . GLU A 141 ? 0.2987 0.2307 0.2460 -0.0215 0.0143  0.0063  166 GLU A CD  
1076 O OE1 . GLU A 141 ? 0.2826 0.2075 0.2251 -0.0216 0.0136  0.0016  166 GLU A OE1 
1077 O OE2 . GLU A 141 ? 0.3091 0.2476 0.2590 -0.0150 0.0146  0.0089  166 GLU A OE2 
1078 N N   . PRO A 142 ? 0.2824 0.1920 0.2124 -0.0511 0.0103  -0.0110 167 PRO A N   
1079 C CA  . PRO A 142 ? 0.2832 0.1935 0.2118 -0.0401 0.0111  -0.0117 167 PRO A CA  
1080 C C   . PRO A 142 ? 0.2725 0.1963 0.2015 -0.0396 0.0075  -0.0135 167 PRO A C   
1081 O O   . PRO A 142 ? 0.2728 0.1976 0.2012 -0.0316 0.0085  -0.0139 167 PRO A O   
1082 C CB  . PRO A 142 ? 0.3037 0.1923 0.2226 -0.0383 0.0153  -0.0166 167 PRO A CB  
1083 C CG  . PRO A 142 ? 0.3210 0.2023 0.2330 -0.0505 0.0142  -0.0224 167 PRO A CG  
1084 C CD  . PRO A 142 ? 0.3158 0.2074 0.2356 -0.0589 0.0117  -0.0176 167 PRO A CD  
1085 N N   . GLU A 143 ? 0.2861 0.2205 0.2161 -0.0484 0.0032  -0.0142 168 GLU A N   
1086 C CA  . GLU A 143 ? 0.2986 0.2442 0.2264 -0.0494 -0.0005 -0.0158 168 GLU A CA  
1087 C C   . GLU A 143 ? 0.2644 0.2227 0.2000 -0.0405 -0.0012 -0.0106 168 GLU A C   
1088 O O   . GLU A 143 ? 0.2531 0.2142 0.1852 -0.0373 -0.0017 -0.0119 168 GLU A O   
1089 C CB  . GLU A 143 ? 0.3324 0.2900 0.2613 -0.0606 -0.0060 -0.0158 168 GLU A CB  
1090 C CG  . GLU A 143 ? 0.3951 0.3393 0.3121 -0.0712 -0.0062 -0.0235 168 GLU A CG  
1091 C CD  . GLU A 143 ? 0.4332 0.3631 0.3503 -0.0766 -0.0031 -0.0245 168 GLU A CD  
1092 O OE1 . GLU A 143 ? 0.4571 0.3918 0.3847 -0.0740 -0.0017 -0.0180 168 GLU A OE1 
1093 O OE2 . GLU A 143 ? 0.5178 0.4306 0.4233 -0.0835 -0.0015 -0.0319 168 GLU A OE2 
1094 N N   . LEU A 144 ? 0.2438 0.2083 0.1890 -0.0366 -0.0004 -0.0051 169 LEU A N   
1095 C CA  . LEU A 144 ? 0.2174 0.1919 0.1697 -0.0290 -0.0005 -0.0008 169 LEU A CA  
1096 C C   . LEU A 144 ? 0.2155 0.1825 0.1637 -0.0215 0.0020  -0.0030 169 LEU A C   
1097 O O   . LEU A 144 ? 0.2055 0.1796 0.1576 -0.0168 0.0015  -0.0008 169 LEU A O   
1098 C CB  . LEU A 144 ? 0.2233 0.2039 0.1846 -0.0264 0.0009  0.0042  169 LEU A CB  
1099 C CG  . LEU A 144 ? 0.2293 0.1985 0.1887 -0.0232 0.0049  0.0044  169 LEU A CG  
1100 C CD1 . LEU A 144 ? 0.2293 0.1955 0.1878 -0.0145 0.0065  0.0043  169 LEU A CD1 
1101 C CD2 . LEU A 144 ? 0.2315 0.2066 0.1975 -0.0252 0.0065  0.0088  169 LEU A CD2 
1102 N N   . ASN A 145 ? 0.2182 0.1714 0.1596 -0.0204 0.0048  -0.0070 170 ASN A N   
1103 C CA  . ASN A 145 ? 0.2209 0.1696 0.1605 -0.0131 0.0073  -0.0085 170 ASN A CA  
1104 C C   . ASN A 145 ? 0.2296 0.1774 0.1626 -0.0142 0.0076  -0.0127 170 ASN A C   
1105 O O   . ASN A 145 ? 0.2347 0.1805 0.1671 -0.0087 0.0101  -0.0140 170 ASN A O   
1106 C CB  . ASN A 145 ? 0.2384 0.1741 0.1755 -0.0093 0.0107  -0.0095 170 ASN A CB  
1107 C CG  . ASN A 145 ? 0.2624 0.1980 0.2036 -0.0085 0.0109  -0.0052 170 ASN A CG  
1108 O OD1 . ASN A 145 ? 0.2480 0.1906 0.1941 -0.0039 0.0104  -0.0021 170 ASN A OD1 
1109 N ND2 . ASN A 145 ? 0.2651 0.1924 0.2036 -0.0136 0.0119  -0.0051 170 ASN A ND2 
1110 N N   . ARG A 146 ? 0.2404 0.1900 0.1682 -0.0217 0.0053  -0.0149 171 ARG A N   
1111 C CA  . ARG A 146 ? 0.2511 0.1953 0.1684 -0.0241 0.0066  -0.0205 171 ARG A CA  
1112 C C   . ARG A 146 ? 0.2580 0.2147 0.1729 -0.0278 0.0029  -0.0192 171 ARG A C   
1113 O O   . ARG A 146 ? 0.2726 0.2265 0.1767 -0.0322 0.0030  -0.0239 171 ARG A O   
1114 C CB  . ARG A 146 ? 0.2762 0.2072 0.1847 -0.0310 0.0075  -0.0262 171 ARG A CB  
1115 C CG  . ARG A 146 ? 0.2863 0.2030 0.1962 -0.0270 0.0116  -0.0265 171 ARG A CG  
1116 C CD  . ARG A 146 ? 0.3162 0.2176 0.2176 -0.0346 0.0129  -0.0317 171 ARG A CD  
1117 N NE  . ARG A 146 ? 0.3234 0.2097 0.2261 -0.0298 0.0173  -0.0306 171 ARG A NE  
1118 C CZ  . ARG A 146 ? 0.3497 0.2182 0.2456 -0.0351 0.0199  -0.0344 171 ARG A CZ  
1119 N NH1 . ARG A 146 ? 0.3524 0.2175 0.2405 -0.0463 0.0180  -0.0398 171 ARG A NH1 
1120 N NH2 . ARG A 146 ? 0.3654 0.2193 0.2619 -0.0293 0.0243  -0.0324 171 ARG A NH2 
1121 N N   . ASP A 147 ? 0.2413 0.2113 0.1651 -0.0263 -0.0003 -0.0127 172 ASP A N   
1122 C CA  . ASP A 147 ? 0.2413 0.2234 0.1633 -0.0293 -0.0042 -0.0099 172 ASP A CA  
1123 C C   . ASP A 147 ? 0.2449 0.2259 0.1613 -0.0255 -0.0012 -0.0110 172 ASP A C   
1124 O O   . ASP A 147 ? 0.2353 0.2124 0.1558 -0.0192 0.0027  -0.0110 172 ASP A O   
1125 C CB  . ASP A 147 ? 0.2449 0.2399 0.1785 -0.0269 -0.0073 -0.0020 172 ASP A CB  
1126 C CG  . ASP A 147 ? 0.2594 0.2605 0.2005 -0.0306 -0.0102 0.0007  172 ASP A CG  
1127 O OD1 . ASP A 147 ? 0.3201 0.3290 0.2592 -0.0377 -0.0146 0.0011  172 ASP A OD1 
1128 O OD2 . ASP A 147 ? 0.2740 0.2728 0.2227 -0.0268 -0.0080 0.0024  172 ASP A OD2 
1129 N N   . PRO A 148 ? 0.2519 0.2383 0.1593 -0.0295 -0.0031 -0.0112 173 PRO A N   
1130 C CA  . PRO A 148 ? 0.2757 0.2625 0.1779 -0.0263 0.0004  -0.0114 173 PRO A CA  
1131 C C   . PRO A 148 ? 0.2520 0.2458 0.1650 -0.0206 0.0007  -0.0040 173 PRO A C   
1132 O O   . PRO A 148 ? 0.2410 0.2417 0.1629 -0.0199 -0.0028 0.0019  173 PRO A O   
1133 C CB  . PRO A 148 ? 0.2980 0.2904 0.1874 -0.0329 -0.0028 -0.0121 173 PRO A CB  
1134 C CG  . PRO A 148 ? 0.2997 0.2931 0.1870 -0.0405 -0.0080 -0.0144 173 PRO A CG  
1135 C CD  . PRO A 148 ? 0.2759 0.2698 0.1777 -0.0379 -0.0090 -0.0110 173 PRO A CD  
1136 N N   . PRO A 149 ? 0.2781 0.2697 0.1916 -0.0163 0.0056  -0.0045 174 PRO A N   
1137 C CA  . PRO A 149 ? 0.2754 0.2722 0.1978 -0.0125 0.0062  0.0019  174 PRO A CA  
1138 C C   . PRO A 149 ? 0.2669 0.2724 0.1877 -0.0147 0.0024  0.0090  174 PRO A C   
1139 O O   . PRO A 149 ? 0.2675 0.2765 0.1774 -0.0188 0.0009  0.0086  174 PRO A O   
1140 C CB  . PRO A 149 ? 0.3183 0.3132 0.2385 -0.0101 0.0119  -0.0005 174 PRO A CB  
1141 C CG  . PRO A 149 ? 0.3471 0.3337 0.2622 -0.0096 0.0148  -0.0083 174 PRO A CG  
1142 C CD  . PRO A 149 ? 0.3072 0.2918 0.2128 -0.0153 0.0111  -0.0110 174 PRO A CD  
1143 N N   . GLY A 150 ? 0.2537 0.2623 0.1849 -0.0117 0.0009  0.0154  175 GLY A N   
1144 C CA  . GLY A 150 ? 0.2755 0.2918 0.2072 -0.0120 -0.0025 0.0236  175 GLY A CA  
1145 C C   . GLY A 150 ? 0.2674 0.2905 0.2035 -0.0133 -0.0079 0.0263  175 GLY A C   
1146 O O   . GLY A 150 ? 0.2712 0.3011 0.2128 -0.0112 -0.0106 0.0342  175 GLY A O   
1147 N N   . ASP A 151 ? 0.2774 0.2991 0.2114 -0.0167 -0.0094 0.0204  176 ASP A N   
1148 C CA  . ASP A 151 ? 0.2774 0.3074 0.2169 -0.0189 -0.0144 0.0231  176 ASP A CA  
1149 C C   . ASP A 151 ? 0.2483 0.2778 0.2016 -0.0133 -0.0128 0.0264  176 ASP A C   
1150 O O   . ASP A 151 ? 0.2298 0.2501 0.1856 -0.0106 -0.0089 0.0223  176 ASP A O   
1151 C CB  . ASP A 151 ? 0.2985 0.3251 0.2319 -0.0251 -0.0155 0.0156  176 ASP A CB  
1152 C CG  . ASP A 151 ? 0.3488 0.3860 0.2857 -0.0305 -0.0213 0.0176  176 ASP A CG  
1153 O OD1 . ASP A 151 ? 0.2939 0.3413 0.2426 -0.0276 -0.0235 0.0248  176 ASP A OD1 
1154 O OD2 . ASP A 151 ? 0.3942 0.4287 0.3223 -0.0378 -0.0229 0.0114  176 ASP A OD2 
1155 N N   . GLU A 152 ? 0.2426 0.2826 0.2047 -0.0113 -0.0159 0.0339  177 GLU A N   
1156 C CA  . GLU A 152 ? 0.2210 0.2600 0.1952 -0.0055 -0.0134 0.0365  177 GLU A CA  
1157 C C   . GLU A 152 ? 0.2181 0.2579 0.1965 -0.0078 -0.0134 0.0327  177 GLU A C   
1158 O O   . GLU A 152 ? 0.2091 0.2455 0.1947 -0.0035 -0.0101 0.0326  177 GLU A O   
1159 C CB  . GLU A 152 ? 0.2415 0.2914 0.2251 -0.0011 -0.0155 0.0462  177 GLU A CB  
1160 C CG  . GLU A 152 ? 0.2493 0.2957 0.2311 0.0029  -0.0141 0.0518  177 GLU A CG  
1161 C CD  . GLU A 152 ? 0.2620 0.3137 0.2547 0.0101  -0.0138 0.0614  177 GLU A CD  
1162 O OE1 . GLU A 152 ? 0.2610 0.3236 0.2634 0.0120  -0.0157 0.0651  177 GLU A OE1 
1163 O OE2 . GLU A 152 ? 0.2697 0.3139 0.2615 0.0138  -0.0111 0.0653  177 GLU A OE2 
1164 N N   . ARG A 153 ? 0.2083 0.2516 0.1812 -0.0151 -0.0167 0.0293  178 ARG A N   
1165 C CA  . ARG A 153 ? 0.2191 0.2622 0.1958 -0.0183 -0.0164 0.0263  178 ARG A CA  
1166 C C   . ARG A 153 ? 0.2084 0.2370 0.1832 -0.0154 -0.0111 0.0209  178 ARG A C   
1167 O O   . ARG A 153 ? 0.2059 0.2244 0.1732 -0.0144 -0.0089 0.0166  178 ARG A O   
1168 C CB  . ARG A 153 ? 0.2552 0.3010 0.2244 -0.0280 -0.0204 0.0224  178 ARG A CB  
1169 C CG  . ARG A 153 ? 0.2928 0.3569 0.2657 -0.0324 -0.0270 0.0281  178 ARG A CG  
1170 C CD  . ARG A 153 ? 0.3314 0.3949 0.2934 -0.0435 -0.0309 0.0219  178 ARG A CD  
1171 N NE  . ARG A 153 ? 0.4302 0.5125 0.3932 -0.0489 -0.0385 0.0269  178 ARG A NE  
1172 C CZ  . ARG A 153 ? 0.5434 0.6319 0.4994 -0.0482 -0.0419 0.0304  178 ARG A CZ  
1173 N NH1 . ARG A 153 ? 0.5969 0.6748 0.5461 -0.0420 -0.0377 0.0299  178 ARG A NH1 
1174 N NH2 . ARG A 153 ? 0.5925 0.6992 0.5487 -0.0539 -0.0497 0.0349  178 ARG A NH2 
1175 N N   . ASP A 154 ? 0.2043 0.2337 0.1868 -0.0135 -0.0089 0.0219  179 ASP A N   
1176 C CA  . ASP A 154 ? 0.2122 0.2299 0.1925 -0.0114 -0.0047 0.0177  179 ASP A CA  
1177 C C   . ASP A 154 ? 0.2055 0.2158 0.1847 -0.0050 -0.0018 0.0168  179 ASP A C   
1178 O O   . ASP A 154 ? 0.2110 0.2117 0.1856 -0.0038 0.0004  0.0127  179 ASP A O   
1179 C CB  . ASP A 154 ? 0.2251 0.2338 0.1964 -0.0170 -0.0049 0.0121  179 ASP A CB  
1180 C CG  . ASP A 154 ? 0.2294 0.2442 0.2012 -0.0252 -0.0080 0.0122  179 ASP A CG  
1181 O OD1 . ASP A 154 ? 0.2413 0.2648 0.2221 -0.0260 -0.0080 0.0160  179 ASP A OD1 
1182 O OD2 . ASP A 154 ? 0.2245 0.2354 0.1876 -0.0312 -0.0101 0.0080  179 ASP A OD2 
1183 N N   . THR A 155 ? 0.1932 0.2081 0.1774 -0.0008 -0.0017 0.0211  180 THR A N   
1184 C CA  . THR A 155 ? 0.1981 0.2056 0.1815 0.0037  0.0010  0.0200  180 THR A CA  
1185 C C   . THR A 155 ? 0.1959 0.2028 0.1860 0.0090  0.0041  0.0221  180 THR A C   
1186 O O   . THR A 155 ? 0.2137 0.2283 0.2108 0.0107  0.0044  0.0262  180 THR A O   
1187 C CB  . THR A 155 ? 0.1915 0.2000 0.1726 0.0038  -0.0002 0.0224  180 THR A CB  
1188 O OG1 . THR A 155 ? 0.2032 0.2206 0.1903 0.0054  -0.0019 0.0291  180 THR A OG1 
1189 C CG2 . THR A 155 ? 0.1864 0.1946 0.1590 -0.0011 -0.0022 0.0194  180 THR A CG2 
1190 N N   . THR A 156 ? 0.1877 0.1857 0.1752 0.0114  0.0066  0.0187  181 THR A N   
1191 C CA  . THR A 156 ? 0.2021 0.1959 0.1930 0.0160  0.0100  0.0191  181 THR A CA  
1192 C C   . THR A 156 ? 0.2066 0.1936 0.1954 0.0163  0.0105  0.0182  181 THR A C   
1193 O O   . THR A 156 ? 0.1988 0.1871 0.1850 0.0135  0.0085  0.0186  181 THR A O   
1194 C CB  . THR A 156 ? 0.2149 0.2049 0.2034 0.0169  0.0124  0.0152  181 THR A CB  
1195 O OG1 . THR A 156 ? 0.2205 0.2061 0.2109 0.0212  0.0163  0.0147  181 THR A OG1 
1196 C CG2 . THR A 156 ? 0.2154 0.1993 0.1970 0.0150  0.0115  0.0103  181 THR A CG2 
1197 N N   . THR A 157 ? 0.2054 0.1849 0.1949 0.0190  0.0137  0.0165  182 THR A N   
1198 C CA  . THR A 157 ? 0.2078 0.1798 0.1954 0.0178  0.0144  0.0145  182 THR A CA  
1199 C C   . THR A 157 ? 0.2061 0.1717 0.1899 0.0174  0.0158  0.0083  182 THR A C   
1200 O O   . THR A 157 ? 0.2110 0.1761 0.1939 0.0197  0.0175  0.0067  182 THR A O   
1201 C CB  . THR A 157 ? 0.2125 0.1797 0.2041 0.0205  0.0167  0.0191  182 THR A CB  
1202 O OG1 . THR A 157 ? 0.2147 0.1763 0.2083 0.0249  0.0206  0.0181  182 THR A OG1 
1203 C CG2 . THR A 157 ? 0.2157 0.1912 0.2108 0.0216  0.0147  0.0266  182 THR A CG2 
1204 N N   . PRO A 158 ? 0.2076 0.1696 0.1890 0.0141  0.0149  0.0048  183 PRO A N   
1205 C CA  . PRO A 158 ? 0.2046 0.1617 0.1819 0.0130  0.0153  -0.0011 183 PRO A CA  
1206 C C   . PRO A 158 ? 0.2291 0.1776 0.2053 0.0158  0.0194  -0.0029 183 PRO A C   
1207 O O   . PRO A 158 ? 0.2352 0.1820 0.2065 0.0167  0.0204  -0.0068 183 PRO A O   
1208 C CB  . PRO A 158 ? 0.2098 0.1661 0.1876 0.0084  0.0138  -0.0030 183 PRO A CB  
1209 C CG  . PRO A 158 ? 0.1966 0.1601 0.1770 0.0076  0.0123  0.0010  183 PRO A CG  
1210 C CD  . PRO A 158 ? 0.1974 0.1616 0.1798 0.0109  0.0135  0.0063  183 PRO A CD  
1211 N N   . HIS A 159 ? 0.2346 0.1770 0.2146 0.0176  0.0222  0.0002  184 HIS A N   
1212 C CA  . HIS A 159 ? 0.2558 0.1881 0.2355 0.0215  0.0272  -0.0010 184 HIS A CA  
1213 C C   . HIS A 159 ? 0.2659 0.2036 0.2470 0.0269  0.0296  0.0007  184 HIS A C   
1214 O O   . HIS A 159 ? 0.2505 0.1828 0.2270 0.0288  0.0331  -0.0039 184 HIS A O   
1215 C CB  . HIS A 159 ? 0.2654 0.1909 0.2503 0.0234  0.0296  0.0043  184 HIS A CB  
1216 C CG  . HIS A 159 ? 0.2912 0.2030 0.2763 0.0279  0.0357  0.0033  184 HIS A CG  
1217 N ND1 . HIS A 159 ? 0.3097 0.2125 0.2992 0.0303  0.0386  0.0086  184 HIS A ND1 
1218 C CD2 . HIS A 159 ? 0.3045 0.2092 0.2858 0.0311  0.0402  -0.0019 184 HIS A CD2 
1219 C CE1 . HIS A 159 ? 0.3312 0.2206 0.3199 0.0352  0.0449  0.0061  184 HIS A CE1 
1220 N NE2 . HIS A 159 ? 0.3139 0.2044 0.2971 0.0355  0.0460  -0.0008 184 HIS A NE2 
1221 N N   . ALA A 160 ? 0.2481 0.1969 0.2352 0.0288  0.0277  0.0071  185 ALA A N   
1222 C CA  . ALA A 160 ? 0.2433 0.1994 0.2342 0.0331  0.0300  0.0098  185 ALA A CA  
1223 C C   . ALA A 160 ? 0.2398 0.1986 0.2245 0.0312  0.0298  0.0053  185 ALA A C   
1224 O O   . ALA A 160 ? 0.2442 0.2022 0.2278 0.0346  0.0343  0.0039  185 ALA A O   
1225 C CB  . ALA A 160 ? 0.2304 0.1992 0.2287 0.0335  0.0269  0.0172  185 ALA A CB  
1226 N N   . ILE A 161 ? 0.2343 0.1963 0.2148 0.0265  0.0251  0.0036  186 ILE A N   
1227 C CA  . ILE A 161 ? 0.2544 0.2195 0.2296 0.0251  0.0245  0.0014  186 ILE A CA  
1228 C C   . ILE A 161 ? 0.2544 0.2113 0.2207 0.0250  0.0264  -0.0049 186 ILE A C   
1229 O O   . ILE A 161 ? 0.2307 0.1884 0.1918 0.0260  0.0286  -0.0063 186 ILE A O   
1230 C CB  . ILE A 161 ? 0.2391 0.2091 0.2129 0.0212  0.0195  0.0022  186 ILE A CB  
1231 C CG1 . ILE A 161 ? 0.2681 0.2410 0.2377 0.0206  0.0195  0.0021  186 ILE A CG1 
1232 C CG2 . ILE A 161 ? 0.2332 0.1995 0.2036 0.0184  0.0165  -0.0012 186 ILE A CG2 
1233 C CD1 . ILE A 161 ? 0.3071 0.2857 0.2810 0.0220  0.0226  0.0059  186 ILE A CD1 
1234 N N   . ALA A 162 ? 0.2621 0.2114 0.2263 0.0230  0.0257  -0.0086 187 ALA A N   
1235 C CA  . ALA A 162 ? 0.2853 0.2264 0.2403 0.0219  0.0273  -0.0155 187 ALA A CA  
1236 C C   . ALA A 162 ? 0.2963 0.2318 0.2492 0.0267  0.0343  -0.0170 187 ALA A C   
1237 O O   . ALA A 162 ? 0.3125 0.2464 0.2562 0.0270  0.0364  -0.0210 187 ALA A O   
1238 C CB  . ALA A 162 ? 0.2827 0.2165 0.2370 0.0178  0.0256  -0.0192 187 ALA A CB  
1239 N N   . LEU A 163 ? 0.2869 0.2194 0.2477 0.0311  0.0384  -0.0136 188 LEU A N   
1240 C CA  . LEU A 163 ? 0.3048 0.2324 0.2654 0.0372  0.0462  -0.0145 188 LEU A CA  
1241 C C   . LEU A 163 ? 0.2999 0.2388 0.2618 0.0399  0.0483  -0.0113 188 LEU A C   
1242 O O   . LEU A 163 ? 0.3036 0.2394 0.2601 0.0432  0.0545  -0.0144 188 LEU A O   
1243 C CB  . LEU A 163 ? 0.3258 0.2482 0.2959 0.0425  0.0501  -0.0103 188 LEU A CB  
1244 C CG  . LEU A 163 ? 0.3601 0.2679 0.3279 0.0396  0.0497  -0.0136 188 LEU A CG  
1245 C CD1 . LEU A 163 ? 0.3618 0.2641 0.3391 0.0458  0.0540  -0.0077 188 LEU A CD1 
1246 C CD2 . LEU A 163 ? 0.4050 0.2986 0.3597 0.0367  0.0527  -0.0240 188 LEU A CD2 
1247 N N   . VAL A 164 ? 0.2546 0.2059 0.2232 0.0382  0.0440  -0.0053 189 VAL A N   
1248 C CA  . VAL A 164 ? 0.2699 0.2315 0.2397 0.0389  0.0456  -0.0022 189 VAL A CA  
1249 C C   . VAL A 164 ? 0.2735 0.2320 0.2297 0.0362  0.0457  -0.0071 189 VAL A C   
1250 O O   . VAL A 164 ? 0.2857 0.2457 0.2379 0.0387  0.0514  -0.0076 189 VAL A O   
1251 C CB  . VAL A 164 ? 0.2590 0.2317 0.2364 0.0355  0.0399  0.0038  189 VAL A CB  
1252 C CG1 . VAL A 164 ? 0.2437 0.2238 0.2191 0.0332  0.0401  0.0059  189 VAL A CG1 
1253 C CG2 . VAL A 164 ? 0.2505 0.2304 0.2411 0.0387  0.0405  0.0100  189 VAL A CG2 
1254 N N   . LEU A 165 ? 0.2737 0.2292 0.2232 0.0315  0.0396  -0.0099 190 LEU A N   
1255 C CA  . LEU A 165 ? 0.2863 0.2409 0.2235 0.0291  0.0381  -0.0130 190 LEU A CA  
1256 C C   . LEU A 165 ? 0.3024 0.2483 0.2287 0.0305  0.0430  -0.0199 190 LEU A C   
1257 O O   . LEU A 165 ? 0.2928 0.2391 0.2088 0.0309  0.0457  -0.0214 190 LEU A O   
1258 C CB  . LEU A 165 ? 0.2683 0.2235 0.2029 0.0247  0.0304  -0.0138 190 LEU A CB  
1259 C CG  . LEU A 165 ? 0.2783 0.2352 0.2016 0.0229  0.0276  -0.0148 190 LEU A CG  
1260 C CD1 . LEU A 165 ? 0.2911 0.2532 0.2140 0.0239  0.0293  -0.0092 190 LEU A CD1 
1261 C CD2 . LEU A 165 ? 0.2734 0.2322 0.1964 0.0198  0.0204  -0.0153 190 LEU A CD2 
1262 N N   . GLN A 166 ? 0.3067 0.2435 0.2344 0.0312  0.0447  -0.0240 191 GLN A N   
1263 C CA  . GLN A 166 ? 0.3320 0.2574 0.2486 0.0321  0.0499  -0.0318 191 GLN A CA  
1264 C C   . GLN A 166 ? 0.3387 0.2652 0.2543 0.0382  0.0591  -0.0309 191 GLN A C   
1265 O O   . GLN A 166 ? 0.3406 0.2628 0.2424 0.0383  0.0631  -0.0363 191 GLN A O   
1266 C CB  . GLN A 166 ? 0.3505 0.2641 0.2708 0.0319  0.0510  -0.0353 191 GLN A CB  
1267 C CG  . GLN A 166 ? 0.4063 0.3048 0.3141 0.0323  0.0570  -0.0447 191 GLN A CG  
1268 C CD  . GLN A 166 ? 0.4875 0.3713 0.3973 0.0305  0.0578  -0.0488 191 GLN A CD  
1269 O OE1 . GLN A 166 ? 0.6030 0.4784 0.5196 0.0365  0.0646  -0.0473 191 GLN A OE1 
1270 N NE2 . GLN A 166 ? 0.5235 0.4045 0.4281 0.0224  0.0511  -0.0533 191 GLN A NE2 
1271 N N   . GLN A 167 ? 0.3378 0.2707 0.2680 0.0432  0.0627  -0.0242 192 GLN A N   
1272 C CA  . GLN A 167 ? 0.3615 0.2980 0.2939 0.0495  0.0721  -0.0226 192 GLN A CA  
1273 C C   . GLN A 167 ? 0.3324 0.2784 0.2581 0.0475  0.0726  -0.0202 192 GLN A C   
1274 O O   . GLN A 167 ? 0.3416 0.2874 0.2605 0.0508  0.0807  -0.0223 192 GLN A O   
1275 C CB  . GLN A 167 ? 0.3953 0.3418 0.3468 0.0548  0.0746  -0.0142 192 GLN A CB  
1276 C CG  . GLN A 167 ? 0.4964 0.4352 0.4568 0.0585  0.0751  -0.0135 192 GLN A CG  
1277 C CD  . GLN A 167 ? 0.6111 0.5314 0.5619 0.0617  0.0820  -0.0220 192 GLN A CD  
1278 O OE1 . GLN A 167 ? 0.7256 0.6428 0.6758 0.0686  0.0918  -0.0237 192 GLN A OE1 
1279 N NE2 . GLN A 167 ? 0.7304 0.6380 0.6734 0.0564  0.0773  -0.0277 192 GLN A NE2 
1280 N N   . LEU A 168 ? 0.3047 0.2589 0.2332 0.0427  0.0650  -0.0153 193 LEU A N   
1281 C CA  . LEU A 168 ? 0.3034 0.2657 0.2273 0.0406  0.0652  -0.0114 193 LEU A CA  
1282 C C   . LEU A 168 ? 0.3202 0.2764 0.2242 0.0383  0.0649  -0.0168 193 LEU A C   
1283 O O   . LEU A 168 ? 0.3395 0.2987 0.2354 0.0392  0.0703  -0.0156 193 LEU A O   
1284 C CB  . LEU A 168 ? 0.2877 0.2568 0.2191 0.0361  0.0572  -0.0054 193 LEU A CB  
1285 C CG  . LEU A 168 ? 0.2852 0.2632 0.2346 0.0371  0.0570  0.0007  193 LEU A CG  
1286 C CD1 . LEU A 168 ? 0.2850 0.2667 0.2380 0.0319  0.0494  0.0046  193 LEU A CD1 
1287 C CD2 . LEU A 168 ? 0.2856 0.2732 0.2424 0.0402  0.0649  0.0051  193 LEU A CD2 
1288 N N   . VAL A 169 ? 0.3198 0.2688 0.2162 0.0349  0.0584  -0.0222 194 VAL A N   
1289 C CA  . VAL A 169 ? 0.3528 0.2988 0.2312 0.0316  0.0552  -0.0263 194 VAL A CA  
1290 C C   . VAL A 169 ? 0.3706 0.3060 0.2354 0.0322  0.0601  -0.0361 194 VAL A C   
1291 O O   . VAL A 169 ? 0.4154 0.3498 0.2637 0.0316  0.0627  -0.0391 194 VAL A O   
1292 C CB  . VAL A 169 ? 0.3341 0.2815 0.2132 0.0270  0.0445  -0.0259 194 VAL A CB  
1293 C CG1 . VAL A 169 ? 0.3626 0.3089 0.2240 0.0236  0.0401  -0.0301 194 VAL A CG1 
1294 C CG2 . VAL A 169 ? 0.3231 0.2787 0.2128 0.0265  0.0406  -0.0172 194 VAL A CG2 
1295 N N   . LEU A 170 ? 0.3651 0.2916 0.2356 0.0333  0.0619  -0.0410 195 LEU A N   
1296 C CA  . LEU A 170 ? 0.3795 0.2923 0.2365 0.0330  0.0664  -0.0515 195 LEU A CA  
1297 C C   . LEU A 170 ? 0.4032 0.3100 0.2633 0.0404  0.0787  -0.0532 195 LEU A C   
1298 O O   . LEU A 170 ? 0.4051 0.3006 0.2502 0.0412  0.0851  -0.0621 195 LEU A O   
1299 C CB  . LEU A 170 ? 0.3916 0.2956 0.2506 0.0283  0.0604  -0.0568 195 LEU A CB  
1300 C CG  . LEU A 170 ? 0.3836 0.2942 0.2395 0.0210  0.0487  -0.0563 195 LEU A CG  
1301 C CD1 . LEU A 170 ? 0.3831 0.2858 0.2427 0.0159  0.0440  -0.0614 195 LEU A CD1 
1302 C CD2 . LEU A 170 ? 0.4025 0.3153 0.2387 0.0177  0.0464  -0.0604 195 LEU A CD2 
1303 N N   . GLY A 171 ? 0.3788 0.2940 0.2572 0.0459  0.0823  -0.0449 196 GLY A N   
1304 C CA  . GLY A 171 ? 0.3902 0.3029 0.2741 0.0542  0.0942  -0.0449 196 GLY A CA  
1305 C C   . GLY A 171 ? 0.3787 0.3050 0.2645 0.0575  0.1005  -0.0388 196 GLY A C   
1306 O O   . GLY A 171 ? 0.3801 0.3137 0.2573 0.0530  0.0968  -0.0364 196 GLY A O   
1307 N N   . ASN A 172 ? 0.3939 0.3245 0.2928 0.0655  0.1100  -0.0353 197 ASN A N   
1308 C CA  . ASN A 172 ? 0.3938 0.3364 0.2946 0.0694  0.1190  -0.0308 197 ASN A CA  
1309 C C   . ASN A 172 ? 0.3807 0.3419 0.3056 0.0714  0.1181  -0.0191 197 ASN A C   
1310 O O   . ASN A 172 ? 0.3859 0.3579 0.3200 0.0769  0.1274  -0.0148 197 ASN A O   
1311 C CB  . ASN A 172 ? 0.4253 0.3590 0.3201 0.0776  0.1329  -0.0374 197 ASN A CB  
1312 C CG  . ASN A 172 ? 0.4396 0.3571 0.3070 0.0738  0.1339  -0.0492 197 ASN A CG  
1313 O OD1 . ASN A 172 ? 0.4543 0.3762 0.3070 0.0679  0.1302  -0.0493 197 ASN A OD1 
1314 N ND2 . ASN A 172 ? 0.4543 0.3530 0.3148 0.0761  0.1374  -0.0588 197 ASN A ND2 
1315 N N   . ALA A 173 ? 0.3723 0.3379 0.3071 0.0665  0.1070  -0.0142 198 ALA A N   
1316 C CA  . ALA A 173 ? 0.3506 0.3339 0.3050 0.0658  0.1043  -0.0039 198 ALA A CA  
1317 C C   . ALA A 173 ? 0.3415 0.3371 0.2940 0.0625  0.1074  0.0010  198 ALA A C   
1318 O O   . ALA A 173 ? 0.3157 0.3271 0.2842 0.0642  0.1112  0.0084  198 ALA A O   
1319 C CB  . ALA A 173 ? 0.3297 0.3129 0.2889 0.0597  0.0920  -0.0015 198 ALA A CB  
1320 N N   . LEU A 174 ? 0.3623 0.3514 0.2959 0.0575  0.1050  -0.0024 199 LEU A N   
1321 C CA  . LEU A 174 ? 0.3656 0.3630 0.2935 0.0544  0.1088  0.0022  199 LEU A CA  
1322 C C   . LEU A 174 ? 0.3978 0.3890 0.3071 0.0578  0.1188  -0.0037 199 LEU A C   
1323 O O   . LEU A 174 ? 0.3986 0.3757 0.2921 0.0587  0.1182  -0.0127 199 LEU A O   
1324 C CB  . LEU A 174 ? 0.3405 0.3351 0.2599 0.0466  0.0984  0.0042  199 LEU A CB  
1325 C CG  . LEU A 174 ? 0.3283 0.3285 0.2632 0.0424  0.0894  0.0097  199 LEU A CG  
1326 C CD1 . LEU A 174 ? 0.3260 0.3193 0.2499 0.0367  0.0801  0.0096  199 LEU A CD1 
1327 C CD2 . LEU A 174 ? 0.3316 0.3473 0.2830 0.0408  0.0929  0.0182  199 LEU A CD2 
1328 N N   . PRO A 175 ? 0.4150 0.4167 0.3244 0.0588  0.1280  0.0010  200 PRO A N   
1329 C CA  . PRO A 175 ? 0.4390 0.4350 0.3264 0.0603  0.1366  -0.0040 200 PRO A CA  
1330 C C   . PRO A 175 ? 0.4511 0.4377 0.3166 0.0537  0.1275  -0.0066 200 PRO A C   
1331 O O   . PRO A 175 ? 0.4360 0.4243 0.3057 0.0481  0.1172  -0.0015 200 PRO A O   
1332 C CB  . PRO A 175 ? 0.4586 0.4705 0.3531 0.0607  0.1467  0.0042  200 PRO A CB  
1333 C CG  . PRO A 175 ? 0.4268 0.4531 0.3474 0.0577  0.1415  0.0138  200 PRO A CG  
1334 C CD  . PRO A 175 ? 0.4038 0.4235 0.3334 0.0572  0.1302  0.0113  200 PRO A CD  
1335 N N   . PRO A 176 ? 0.4901 0.4666 0.3314 0.0543  0.1310  -0.0147 201 PRO A N   
1336 C CA  . PRO A 176 ? 0.4937 0.4625 0.3145 0.0485  0.1211  -0.0176 201 PRO A CA  
1337 C C   . PRO A 176 ? 0.4811 0.4570 0.2997 0.0432  0.1152  -0.0074 201 PRO A C   
1338 O O   . PRO A 176 ? 0.4758 0.4480 0.2890 0.0390  0.1037  -0.0066 201 PRO A O   
1339 C CB  . PRO A 176 ? 0.5234 0.4842 0.3186 0.0504  0.1292  -0.0266 201 PRO A CB  
1340 C CG  . PRO A 176 ? 0.5318 0.4898 0.3362 0.0579  0.1412  -0.0321 201 PRO A CG  
1341 C CD  . PRO A 176 ? 0.5044 0.4772 0.3363 0.0607  0.1448  -0.0215 201 PRO A CD  
1342 N N   . ASP A 177 ? 0.4957 0.4815 0.3188 0.0434  0.1235  0.0008  202 ASP A N   
1343 C CA  . ASP A 177 ? 0.5241 0.5144 0.3442 0.0383  0.1196  0.0110  202 ASP A CA  
1344 C C   . ASP A 177 ? 0.4860 0.4783 0.3258 0.0348  0.1097  0.0166  202 ASP A C   
1345 O O   . ASP A 177 ? 0.4929 0.4817 0.3272 0.0310  0.1010  0.0208  202 ASP A O   
1346 C CB  . ASP A 177 ? 0.5724 0.5718 0.3907 0.0383  0.1317  0.0180  202 ASP A CB  
1347 C CG  . ASP A 177 ? 0.6255 0.6369 0.4665 0.0413  0.1418  0.0210  202 ASP A CG  
1348 O OD1 . ASP A 177 ? 0.6557 0.6682 0.5145 0.0443  0.1396  0.0175  202 ASP A OD1 
1349 O OD2 . ASP A 177 ? 0.6262 0.6467 0.4668 0.0408  0.1521  0.0273  202 ASP A OD2 
1350 N N   . LYS A 178 ? 0.4253 0.4232 0.2873 0.0366  0.1112  0.0166  203 LYS A N   
1351 C CA  . LYS A 178 ? 0.3802 0.3798 0.2596 0.0332  0.1022  0.0205  203 LYS A CA  
1352 C C   . LYS A 178 ? 0.3802 0.3700 0.2554 0.0332  0.0915  0.0141  203 LYS A C   
1353 O O   . LYS A 178 ? 0.3490 0.3364 0.2265 0.0296  0.0826  0.0172  203 LYS A O   
1354 C CB  . LYS A 178 ? 0.3640 0.3749 0.2671 0.0348  0.1068  0.0232  203 LYS A CB  
1355 C CG  . LYS A 178 ? 0.3633 0.3869 0.2739 0.0335  0.1165  0.0308  203 LYS A CG  
1356 C CD  . LYS A 178 ? 0.3532 0.3914 0.2896 0.0342  0.1193  0.0347  203 LYS A CD  
1357 C CE  . LYS A 178 ? 0.3719 0.4247 0.3168 0.0323  0.1293  0.0421  203 LYS A CE  
1358 N NZ  . LYS A 178 ? 0.3580 0.4281 0.3292 0.0332  0.1315  0.0461  203 LYS A NZ  
1359 N N   . ARG A 179 ? 0.3835 0.3671 0.2520 0.0370  0.0929  0.0051  204 ARG A N   
1360 C CA  . ARG A 179 ? 0.3833 0.3583 0.2479 0.0360  0.0835  -0.0012 204 ARG A CA  
1361 C C   . ARG A 179 ? 0.3923 0.3640 0.2416 0.0323  0.0755  0.0002  204 ARG A C   
1362 O O   . ARG A 179 ? 0.3759 0.3454 0.2288 0.0302  0.0661  0.0002  204 ARG A O   
1363 C CB  . ARG A 179 ? 0.3914 0.3584 0.2480 0.0397  0.0878  -0.0115 204 ARG A CB  
1364 C CG  . ARG A 179 ? 0.3895 0.3478 0.2422 0.0375  0.0786  -0.0184 204 ARG A CG  
1365 C CD  . ARG A 179 ? 0.4062 0.3547 0.2548 0.0407  0.0841  -0.0281 204 ARG A CD  
1366 N NE  . ARG A 179 ? 0.4529 0.3976 0.2809 0.0417  0.0915  -0.0334 204 ARG A NE  
1367 C CZ  . ARG A 179 ? 0.4861 0.4216 0.3056 0.0451  0.0999  -0.0421 204 ARG A CZ  
1368 N NH1 . ARG A 179 ? 0.5066 0.4359 0.3389 0.0493  0.1036  -0.0454 204 ARG A NH1 
1369 N NH2 . ARG A 179 ? 0.5075 0.4395 0.3047 0.0446  0.1049  -0.0473 204 ARG A NH2 
1370 N N   . ALA A 180 ? 0.4226 0.3946 0.2544 0.0320  0.0796  0.0017  205 ALA A N   
1371 C CA  . ALA A 180 ? 0.4218 0.3917 0.2378 0.0294  0.0721  0.0039  205 ALA A CA  
1372 C C   . ALA A 180 ? 0.4024 0.3748 0.2277 0.0272  0.0669  0.0140  205 ALA A C   
1373 O O   . ALA A 180 ? 0.3883 0.3586 0.2094 0.0261  0.0579  0.0156  205 ALA A O   
1374 C CB  . ALA A 180 ? 0.4591 0.4293 0.2535 0.0299  0.0785  0.0039  205 ALA A CB  
1375 N N   . LEU A 181 ? 0.3919 0.3686 0.2303 0.0264  0.0726  0.0207  206 LEU A N   
1376 C CA  . LEU A 181 ? 0.3895 0.3657 0.2362 0.0235  0.0681  0.0292  206 LEU A CA  
1377 C C   . LEU A 181 ? 0.3681 0.3417 0.2268 0.0231  0.0592  0.0263  206 LEU A C   
1378 O O   . LEU A 181 ? 0.3594 0.3293 0.2159 0.0224  0.0522  0.0295  206 LEU A O   
1379 C CB  . LEU A 181 ? 0.3823 0.3639 0.2416 0.0210  0.0755  0.0360  206 LEU A CB  
1380 C CG  . LEU A 181 ? 0.4135 0.3983 0.2617 0.0205  0.0849  0.0414  206 LEU A CG  
1381 C CD1 . LEU A 181 ? 0.4043 0.3978 0.2680 0.0178  0.0933  0.0465  206 LEU A CD1 
1382 C CD2 . LEU A 181 ? 0.4316 0.4101 0.2658 0.0188  0.0810  0.0490  206 LEU A CD2 
1383 N N   . LEU A 182 ? 0.3550 0.3308 0.2263 0.0241  0.0601  0.0208  207 LEU A N   
1384 C CA  . LEU A 182 ? 0.3416 0.3156 0.2240 0.0236  0.0527  0.0179  207 LEU A CA  
1385 C C   . LEU A 182 ? 0.3459 0.3157 0.2178 0.0243  0.0450  0.0140  207 LEU A C   
1386 O O   . LEU A 182 ? 0.3139 0.2820 0.1894 0.0235  0.0382  0.0160  207 LEU A O   
1387 C CB  . LEU A 182 ? 0.3285 0.3051 0.2227 0.0254  0.0556  0.0129  207 LEU A CB  
1388 C CG  . LEU A 182 ? 0.3292 0.3038 0.2330 0.0251  0.0487  0.0096  207 LEU A CG  
1389 C CD1 . LEU A 182 ? 0.3371 0.3132 0.2512 0.0220  0.0446  0.0149  207 LEU A CD1 
1390 C CD2 . LEU A 182 ? 0.3420 0.3180 0.2553 0.0277  0.0520  0.0055  207 LEU A CD2 
1391 N N   . THR A 183 ? 0.3668 0.3353 0.2262 0.0255  0.0464  0.0079  208 THR A N   
1392 C CA  . THR A 183 ? 0.3829 0.3494 0.2324 0.0250  0.0390  0.0031  208 THR A CA  
1393 C C   . THR A 183 ? 0.3710 0.3388 0.2121 0.0247  0.0332  0.0097  208 THR A C   
1394 O O   . THR A 183 ? 0.3450 0.3139 0.1883 0.0245  0.0251  0.0095  208 THR A O   
1395 C CB  . THR A 183 ? 0.4642 0.4283 0.2990 0.0254  0.0433  -0.0046 208 THR A CB  
1396 O OG1 . THR A 183 ? 0.4778 0.4387 0.3226 0.0264  0.0470  -0.0110 208 THR A OG1 
1397 C CG2 . THR A 183 ? 0.5053 0.4689 0.3264 0.0233  0.0357  -0.0095 208 THR A CG2 
1398 N N   A ASP A 184 ? 0.3609 0.3291 0.1927 0.0251  0.0378  0.0162  209 ASP A N   
1399 N N   B ASP A 184 ? 0.3763 0.3445 0.2082 0.0251  0.0378  0.0162  209 ASP A N   
1400 C CA  A ASP A 184 ? 0.3615 0.3299 0.1841 0.0257  0.0334  0.0242  209 ASP A CA  
1401 C CA  B ASP A 184 ? 0.3878 0.3563 0.2105 0.0257  0.0332  0.0241  209 ASP A CA  
1402 C C   A ASP A 184 ? 0.3581 0.3242 0.1945 0.0261  0.0292  0.0301  209 ASP A C   
1403 C C   B ASP A 184 ? 0.3728 0.3389 0.2092 0.0261  0.0292  0.0301  209 ASP A C   
1404 O O   A ASP A 184 ? 0.3635 0.3300 0.1979 0.0279  0.0222  0.0334  209 ASP A O   
1405 O O   B ASP A 184 ? 0.3765 0.3430 0.2110 0.0279  0.0222  0.0334  209 ASP A O   
1406 C CB  A ASP A 184 ? 0.3673 0.3354 0.1785 0.0256  0.0408  0.0308  209 ASP A CB  
1407 C CB  B ASP A 184 ? 0.4151 0.3836 0.2242 0.0257  0.0402  0.0299  209 ASP A CB  
1408 C CG  A ASP A 184 ? 0.3667 0.3335 0.1688 0.0267  0.0372  0.0412  209 ASP A CG  
1409 C CG  B ASP A 184 ? 0.4444 0.4147 0.2344 0.0257  0.0427  0.0238  209 ASP A CG  
1410 O OD1 A ASP A 184 ? 0.3753 0.3449 0.1636 0.0279  0.0312  0.0411  209 ASP A OD1 
1411 O OD1 B ASP A 184 ? 0.4405 0.4114 0.2272 0.0251  0.0377  0.0150  209 ASP A OD1 
1412 O OD2 A ASP A 184 ? 0.3518 0.3145 0.1614 0.0262  0.0400  0.0492  209 ASP A OD2 
1413 O OD2 B ASP A 184 ? 0.4563 0.4272 0.2347 0.0258  0.0502  0.0275  209 ASP A OD2 
1414 N N   . TRP A 185 ? 0.3466 0.3107 0.1968 0.0246  0.0338  0.0315  210 TRP A N   
1415 C CA  . TRP A 185 ? 0.3389 0.2990 0.2007 0.0243  0.0308  0.0358  210 TRP A CA  
1416 C C   . TRP A 185 ? 0.3316 0.2929 0.2005 0.0256  0.0234  0.0306  210 TRP A C   
1417 O O   . TRP A 185 ? 0.3360 0.2951 0.2071 0.0274  0.0187  0.0341  210 TRP A O   
1418 C CB  . TRP A 185 ? 0.3136 0.2728 0.1882 0.0210  0.0364  0.0370  210 TRP A CB  
1419 C CG  . TRP A 185 ? 0.3221 0.2794 0.1933 0.0186  0.0429  0.0446  210 TRP A CG  
1420 C CD1 . TRP A 185 ? 0.3356 0.2871 0.1975 0.0190  0.0431  0.0527  210 TRP A CD1 
1421 C CD2 . TRP A 185 ? 0.3164 0.2783 0.1945 0.0153  0.0505  0.0454  210 TRP A CD2 
1422 N NE1 . TRP A 185 ? 0.3427 0.2938 0.2046 0.0153  0.0506  0.0584  210 TRP A NE1 
1423 C CE2 . TRP A 185 ? 0.3324 0.2910 0.2050 0.0129  0.0552  0.0540  210 TRP A CE2 
1424 C CE3 . TRP A 185 ? 0.3114 0.2806 0.2007 0.0145  0.0539  0.0407  210 TRP A CE3 
1425 C CZ2 . TRP A 185 ? 0.3416 0.3053 0.2199 0.0088  0.0633  0.0574  210 TRP A CZ2 
1426 C CZ3 . TRP A 185 ? 0.3187 0.2940 0.2143 0.0116  0.0616  0.0443  210 TRP A CZ3 
1427 C CH2 . TRP A 185 ? 0.3250 0.2982 0.2156 0.0083  0.0662  0.0523  210 TRP A CH2 
1428 N N   . MET A 186 ? 0.3315 0.2963 0.2036 0.0249  0.0229  0.0225  211 MET A N   
1429 C CA  . MET A 186 ? 0.3461 0.3127 0.2246 0.0253  0.0166  0.0178  211 MET A CA  
1430 C C   . MET A 186 ? 0.3648 0.3352 0.2339 0.0270  0.0100  0.0185  211 MET A C   
1431 O O   . MET A 186 ? 0.3804 0.3529 0.2556 0.0284  0.0044  0.0195  211 MET A O   
1432 C CB  . MET A 186 ? 0.3338 0.3015 0.2170 0.0239  0.0184  0.0098  211 MET A CB  
1433 C CG  . MET A 186 ? 0.3318 0.2986 0.2271 0.0229  0.0233  0.0102  211 MET A CG  
1434 S SD  . MET A 186 ? 0.3207 0.2878 0.2221 0.0228  0.0258  0.0026  211 MET A SD  
1435 C CE  . MET A 186 ? 0.3234 0.2908 0.2302 0.0218  0.0179  -0.0004 211 MET A CE  
1436 N N   . ALA A 187 ? 0.4117 0.3838 0.2658 0.0268  0.0106  0.0182  212 ALA A N   
1437 C CA  . ALA A 187 ? 0.4194 0.3973 0.2633 0.0278  0.0035  0.0193  212 ALA A CA  
1438 C C   . ALA A 187 ? 0.4388 0.4170 0.2839 0.0317  -0.0001 0.0292  212 ALA A C   
1439 O O   . ALA A 187 ? 0.4451 0.4300 0.2902 0.0336  -0.0074 0.0309  212 ALA A O   
1440 C CB  . ALA A 187 ? 0.4511 0.4300 0.2767 0.0264  0.0058  0.0171  212 ALA A CB  
1441 N N   . ARG A 188 ? 0.4299 0.4007 0.2769 0.0328  0.0053  0.0361  213 ARG A N   
1442 C CA  . ARG A 188 ? 0.4471 0.4144 0.2940 0.0368  0.0035  0.0461  213 ARG A CA  
1443 C C   . ARG A 188 ? 0.4386 0.4005 0.3011 0.0383  0.0034  0.0468  213 ARG A C   
1444 O O   . ARG A 188 ? 0.4329 0.3875 0.2968 0.0413  0.0043  0.0544  213 ARG A O   
1445 C CB  . ARG A 188 ? 0.4637 0.4244 0.3011 0.0362  0.0102  0.0535  213 ARG A CB  
1446 C CG  . ARG A 188 ? 0.5057 0.4723 0.3247 0.0359  0.0097  0.0540  213 ARG A CG  
1447 C CD  . ARG A 188 ? 0.5580 0.5193 0.3654 0.0364  0.0149  0.0640  213 ARG A CD  
1448 N NE  . ARG A 188 ? 0.5831 0.5390 0.3950 0.0325  0.0244  0.0636  213 ARG A NE  
1449 C CZ  . ARG A 188 ? 0.6318 0.5795 0.4458 0.0315  0.0299  0.0719  213 ARG A CZ  
1450 N NH1 . ARG A 188 ? 0.6402 0.5812 0.4519 0.0348  0.0275  0.0816  213 ARG A NH1 
1451 N NH2 . ARG A 188 ? 0.6605 0.6068 0.4795 0.0271  0.0381  0.0708  213 ARG A NH2 
1452 N N   A ASN A 189 ? 0.3904 0.3548 0.2637 0.0362  0.0026  0.0389  214 ASN A N   
1453 N N   B ASN A 189 ? 0.4215 0.3855 0.2949 0.0359  0.0030  0.0388  214 ASN A N   
1454 C CA  A ASN A 189 ? 0.3686 0.3278 0.2549 0.0366  0.0035  0.0383  214 ASN A CA  
1455 C CA  B ASN A 189 ? 0.4241 0.3853 0.3101 0.0377  0.0016  0.0384  214 ASN A CA  
1456 C C   A ASN A 189 ? 0.3471 0.3069 0.2372 0.0424  -0.0011 0.0429  214 ASN A C   
1457 C C   B ASN A 189 ? 0.4025 0.3736 0.2912 0.0410  -0.0056 0.0375  214 ASN A C   
1458 O O   A ASN A 189 ? 0.3279 0.2971 0.2151 0.0452  -0.0068 0.0440  214 ASN A O   
1459 O O   B ASN A 189 ? 0.3718 0.3514 0.2579 0.0385  -0.0089 0.0319  214 ASN A O   
1460 C CB  A ASN A 189 ? 0.3478 0.3107 0.2425 0.0330  0.0037  0.0295  214 ASN A CB  
1461 C CB  B ASN A 189 ? 0.4169 0.3769 0.3134 0.0338  0.0042  0.0314  214 ASN A CB  
1462 C CG  A ASN A 189 ? 0.3313 0.2897 0.2376 0.0326  0.0048  0.0280  214 ASN A CG  
1463 C CG  B ASN A 189 ? 0.4297 0.3973 0.3333 0.0340  -0.0004 0.0256  214 ASN A CG  
1464 O OD1 A ASN A 189 ? 0.3433 0.2943 0.2511 0.0347  0.0059  0.0327  214 ASN A OD1 
1465 O OD1 B ASN A 189 ? 0.4189 0.3864 0.3304 0.0365  -0.0022 0.0263  214 ASN A OD1 
1466 N ND2 A ASN A 189 ? 0.3378 0.2997 0.2512 0.0301  0.0045  0.0217  214 ASN A ND2 
1467 N ND2 B ASN A 189 ? 0.4425 0.4164 0.3427 0.0315  -0.0021 0.0202  214 ASN A ND2 
1468 N N   A THR A 190 ? 0.3502 0.3007 0.2476 0.0441  0.0014  0.0451  215 THR A N   
1469 N N   B THR A 190 ? 0.3907 0.3602 0.2851 0.0463  -0.0075 0.0427  215 THR A N   
1470 C CA  A THR A 190 ? 0.3416 0.2912 0.2432 0.0510  -0.0013 0.0499  215 THR A CA  
1471 C CA  B THR A 190 ? 0.4009 0.3816 0.3021 0.0498  -0.0137 0.0423  215 THR A CA  
1472 C C   A THR A 190 ? 0.3286 0.2813 0.2424 0.0520  -0.0023 0.0443  215 THR A C   
1473 C C   B THR A 190 ? 0.3749 0.3524 0.2895 0.0510  -0.0116 0.0392  215 THR A C   
1474 O O   A THR A 190 ? 0.3387 0.2897 0.2575 0.0583  -0.0030 0.0479  215 THR A O   
1475 O O   B THR A 190 ? 0.3885 0.3748 0.3114 0.0545  -0.0152 0.0392  215 THR A O   
1476 C CB  A THR A 190 ? 0.3591 0.2932 0.2575 0.0537  0.0031  0.0578  215 THR A CB  
1477 C CB  B THR A 190 ? 0.4392 0.4227 0.3358 0.0568  -0.0173 0.0522  215 THR A CB  
1478 O OG1 A THR A 190 ? 0.3308 0.2537 0.2356 0.0502  0.0078  0.0538  215 THR A OG1 
1479 O OG1 B THR A 190 ? 0.4654 0.4340 0.3641 0.0605  -0.0120 0.0578  215 THR A OG1 
1480 C CG2 A THR A 190 ? 0.3665 0.2968 0.2528 0.0518  0.0054  0.0641  215 THR A CG2 
1481 C CG2 B THR A 190 ? 0.4634 0.4493 0.3442 0.0557  -0.0189 0.0561  215 THR A CG2 
1482 N N   A THR A 191 ? 0.3155 0.2732 0.2343 0.0468  -0.0022 0.0362  216 THR A N   
1483 N N   B THR A 191 ? 0.3666 0.3321 0.2828 0.0479  -0.0057 0.0370  216 THR A N   
1484 C CA  A THR A 191 ? 0.3077 0.2671 0.2370 0.0474  -0.0021 0.0317  216 THR A CA  
1485 C CA  B THR A 191 ? 0.3297 0.2907 0.2556 0.0478  -0.0032 0.0334  216 THR A CA  
1486 C C   A THR A 191 ? 0.2875 0.2606 0.2220 0.0453  -0.0061 0.0261  216 THR A C   
1487 C C   B THR A 191 ? 0.3023 0.2755 0.2358 0.0460  -0.0064 0.0272  216 THR A C   
1488 O O   A THR A 191 ? 0.2554 0.2310 0.1985 0.0457  -0.0056 0.0230  216 THR A O   
1489 O O   B THR A 191 ? 0.2755 0.2503 0.2175 0.0478  -0.0059 0.0253  216 THR A O   
1490 C CB  A THR A 191 ? 0.3076 0.2570 0.2394 0.0428  0.0028  0.0277  216 THR A CB  
1491 C CB  B THR A 191 ? 0.3234 0.2737 0.2487 0.0422  0.0021  0.0306  216 THR A CB  
1492 O OG1 A THR A 191 ? 0.3253 0.2789 0.2562 0.0368  0.0031  0.0233  216 THR A OG1 
1493 O OG1 B THR A 191 ? 0.3273 0.2838 0.2533 0.0369  0.0019  0.0249  216 THR A OG1 
1494 C CG2 A THR A 191 ? 0.3240 0.2587 0.2511 0.0422  0.0072  0.0319  216 THR A CG2 
1495 C CG2 B THR A 191 ? 0.3261 0.2668 0.2434 0.0410  0.0055  0.0359  216 THR A CG2 
1496 N N   . GLY A 192 ? 0.2853 0.2663 0.2146 0.0423  -0.0093 0.0243  217 GLY A N   
1497 C CA  . GLY A 192 ? 0.2760 0.2663 0.2105 0.0385  -0.0119 0.0180  217 GLY A CA  
1498 C C   . GLY A 192 ? 0.2740 0.2786 0.2111 0.0399  -0.0184 0.0186  217 GLY A C   
1499 O O   . GLY A 192 ? 0.2814 0.2930 0.2213 0.0352  -0.0207 0.0132  217 GLY A O   
1500 N N   . ALA A 193 ? 0.2689 0.2780 0.2053 0.0459  -0.0214 0.0253  218 ALA A N   
1501 C CA  . ALA A 193 ? 0.2832 0.3087 0.2215 0.0470  -0.0287 0.0269  218 ALA A CA  
1502 C C   . ALA A 193 ? 0.2761 0.3137 0.2283 0.0454  -0.0307 0.0232  218 ALA A C   
1503 O O   . ALA A 193 ? 0.2654 0.3172 0.2193 0.0420  -0.0367 0.0213  218 ALA A O   
1504 C CB  . ALA A 193 ? 0.3126 0.3406 0.2492 0.0551  -0.0311 0.0364  218 ALA A CB  
1505 N N   . LYS A 194 ? 0.2892 0.3217 0.2507 0.0472  -0.0257 0.0219  219 LYS A N   
1506 C CA  . LYS A 194 ? 0.2915 0.3361 0.2664 0.0465  -0.0266 0.0197  219 LYS A CA  
1507 C C   . LYS A 194 ? 0.2674 0.3087 0.2441 0.0385  -0.0240 0.0122  219 LYS A C   
1508 O O   . LYS A 194 ? 0.2442 0.2929 0.2315 0.0374  -0.0229 0.0105  219 LYS A O   
1509 C CB  . LYS A 194 ? 0.3386 0.3809 0.3224 0.0543  -0.0221 0.0232  219 LYS A CB  
1510 C CG  . LYS A 194 ? 0.4128 0.4568 0.3968 0.0640  -0.0236 0.0315  219 LYS A CG  
1511 C CD  . LYS A 194 ? 0.4930 0.5581 0.4817 0.0653  -0.0318 0.0354  219 LYS A CD  
1512 C CE  . LYS A 194 ? 0.5492 0.6324 0.5548 0.0670  -0.0328 0.0351  219 LYS A CE  
1513 N NZ  . LYS A 194 ? 0.6148 0.7146 0.6285 0.0758  -0.0377 0.0436  219 LYS A NZ  
1514 N N   . ARG A 195 ? 0.2455 0.2761 0.2122 0.0335  -0.0224 0.0086  220 ARG A N   
1515 C CA  . ARG A 195 ? 0.2328 0.2583 0.2008 0.0272  -0.0194 0.0028  220 ARG A CA  
1516 C C   . ARG A 195 ? 0.2259 0.2553 0.1897 0.0204  -0.0231 -0.0019 220 ARG A C   
1517 O O   . ARG A 195 ? 0.2249 0.2673 0.1930 0.0182  -0.0282 -0.0025 220 ARG A O   
1518 C CB  . ARG A 195 ? 0.2296 0.2403 0.1930 0.0277  -0.0137 0.0027  220 ARG A CB  
1519 C CG  . ARG A 195 ? 0.2284 0.2356 0.1968 0.0326  -0.0103 0.0054  220 ARG A CG  
1520 C CD  . ARG A 195 ? 0.2323 0.2263 0.1961 0.0319  -0.0056 0.0051  220 ARG A CD  
1521 N NE  . ARG A 195 ? 0.2529 0.2417 0.2190 0.0363  -0.0025 0.0071  220 ARG A NE  
1522 C CZ  . ARG A 195 ? 0.2543 0.2334 0.2185 0.0350  0.0014  0.0059  220 ARG A CZ  
1523 N NH1 . ARG A 195 ? 0.2734 0.2496 0.2358 0.0298  0.0025  0.0035  220 ARG A NH1 
1524 N NH2 . ARG A 195 ? 0.2648 0.2370 0.2290 0.0390  0.0043  0.0072  220 ARG A NH2 
1525 N N   . ILE A 196 ? 0.2279 0.2465 0.1835 0.0169  -0.0204 -0.0056 221 ILE A N   
1526 C CA  . ILE A 196 ? 0.2386 0.2575 0.1892 0.0104  -0.0225 -0.0113 221 ILE A CA  
1527 C C   . ILE A 196 ? 0.2445 0.2726 0.1880 0.0098  -0.0289 -0.0109 221 ILE A C   
1528 O O   . ILE A 196 ? 0.2407 0.2769 0.1849 0.0040  -0.0335 -0.0148 221 ILE A O   
1529 C CB  . ILE A 196 ? 0.2571 0.2621 0.1999 0.0088  -0.0174 -0.0147 221 ILE A CB  
1530 C CG1 . ILE A 196 ? 0.2501 0.2487 0.2004 0.0083  -0.0126 -0.0150 221 ILE A CG1 
1531 C CG2 . ILE A 196 ? 0.2689 0.2716 0.2029 0.0031  -0.0191 -0.0211 221 ILE A CG2 
1532 C CD1 . ILE A 196 ? 0.2417 0.2289 0.1869 0.0090  -0.0074 -0.0160 221 ILE A CD1 
1533 N N   . ARG A 197 ? 0.2362 0.2640 0.1728 0.0154  -0.0295 -0.0057 222 ARG A N   
1534 C CA  . ARG A 197 ? 0.2458 0.2834 0.1749 0.0160  -0.0359 -0.0033 222 ARG A CA  
1535 C C   . ARG A 197 ? 0.2509 0.3066 0.1907 0.0149  -0.0428 -0.0021 222 ARG A C   
1536 O O   . ARG A 197 ? 0.2524 0.3184 0.1869 0.0105  -0.0495 -0.0041 222 ARG A O   
1537 C CB  . ARG A 197 ? 0.2481 0.2827 0.1719 0.0237  -0.0349 0.0047  222 ARG A CB  
1538 C CG  . ARG A 197 ? 0.2692 0.3150 0.1859 0.0263  -0.0417 0.0099  222 ARG A CG  
1539 C CD  . ARG A 197 ? 0.2779 0.3244 0.1779 0.0209  -0.0448 0.0056  222 ARG A CD  
1540 N NE  . ARG A 197 ? 0.2856 0.3402 0.1862 0.0125  -0.0497 -0.0024 222 ARG A NE  
1541 C CZ  . ARG A 197 ? 0.3149 0.3692 0.2006 0.0062  -0.0524 -0.0086 222 ARG A CZ  
1542 N NH1 . ARG A 197 ? 0.3284 0.3754 0.1974 0.0081  -0.0499 -0.0073 222 ARG A NH1 
1543 N NH2 . ARG A 197 ? 0.3216 0.3820 0.2079 -0.0024 -0.0569 -0.0163 222 ARG A NH2 
1544 N N   . ALA A 198 ? 0.2393 0.2998 0.1939 0.0186  -0.0411 0.0010  223 ALA A N   
1545 C CA  . ALA A 198 ? 0.2483 0.3281 0.2157 0.0186  -0.0466 0.0033  223 ALA A CA  
1546 C C   . ALA A 198 ? 0.2479 0.3346 0.2210 0.0085  -0.0489 -0.0037 223 ALA A C   
1547 O O   . ALA A 198 ? 0.2608 0.3663 0.2443 0.0064  -0.0545 -0.0024 223 ALA A O   
1548 C CB  . ALA A 198 ? 0.2466 0.3283 0.2272 0.0264  -0.0425 0.0085  223 ALA A CB  
1549 N N   . GLY A 199 ? 0.2406 0.3127 0.2076 0.0022  -0.0447 -0.0105 224 GLY A N   
1550 C CA  . GLY A 199 ? 0.2537 0.3284 0.2243 -0.0080 -0.0463 -0.0171 224 GLY A CA  
1551 C C   . GLY A 199 ? 0.2770 0.3496 0.2339 -0.0160 -0.0508 -0.0239 224 GLY A C   
1552 O O   . GLY A 199 ? 0.2926 0.3670 0.2518 -0.0257 -0.0527 -0.0300 224 GLY A O   
1553 N N   . PHE A 200 ? 0.2855 0.3540 0.2276 -0.0127 -0.0522 -0.0230 225 PHE A N   
1554 C CA  . PHE A 200 ? 0.2881 0.3526 0.2141 -0.0200 -0.0554 -0.0303 225 PHE A CA  
1555 C C   . PHE A 200 ? 0.2947 0.3767 0.2146 -0.0200 -0.0649 -0.0272 225 PHE A C   
1556 O O   . PHE A 200 ? 0.2973 0.3850 0.2173 -0.0110 -0.0660 -0.0186 225 PHE A O   
1557 C CB  . PHE A 200 ? 0.2878 0.3323 0.1989 -0.0169 -0.0483 -0.0327 225 PHE A CB  
1558 C CG  . PHE A 200 ? 0.2826 0.3101 0.1957 -0.0204 -0.0408 -0.0387 225 PHE A CG  
1559 C CD1 . PHE A 200 ? 0.2934 0.3116 0.1974 -0.0289 -0.0403 -0.0483 225 PHE A CD1 
1560 C CD2 . PHE A 200 ? 0.2711 0.2923 0.1952 -0.0154 -0.0346 -0.0347 225 PHE A CD2 
1561 C CE1 . PHE A 200 ? 0.2961 0.2981 0.2027 -0.0312 -0.0332 -0.0528 225 PHE A CE1 
1562 C CE2 . PHE A 200 ? 0.2771 0.2844 0.2034 -0.0182 -0.0284 -0.0390 225 PHE A CE2 
1563 C CZ  . PHE A 200 ? 0.2872 0.2846 0.2054 -0.0255 -0.0276 -0.0474 225 PHE A CZ  
1564 N N   . PRO A 201 ? 0.3145 0.4042 0.2271 -0.0300 -0.0719 -0.0339 226 PRO A N   
1565 C CA  . PRO A 201 ? 0.3211 0.4295 0.2263 -0.0306 -0.0822 -0.0307 226 PRO A CA  
1566 C C   . PRO A 201 ? 0.3278 0.4287 0.2148 -0.0234 -0.0807 -0.0266 226 PRO A C   
1567 O O   . PRO A 201 ? 0.3208 0.4013 0.1975 -0.0214 -0.0721 -0.0298 226 PRO A O   
1568 C CB  . PRO A 201 ? 0.3452 0.4572 0.2422 -0.0450 -0.0884 -0.0414 226 PRO A CB  
1569 C CG  . PRO A 201 ? 0.3434 0.4446 0.2522 -0.0513 -0.0824 -0.0477 226 PRO A CG  
1570 C CD  . PRO A 201 ? 0.3229 0.4043 0.2338 -0.0420 -0.0710 -0.0447 226 PRO A CD  
1571 N N   . ALA A 202 ? 0.3351 0.4538 0.2195 -0.0194 -0.0889 -0.0188 227 ALA A N   
1572 C CA  . ALA A 202 ? 0.3633 0.4773 0.2327 -0.0113 -0.0877 -0.0118 227 ALA A CA  
1573 C C   . ALA A 202 ? 0.3803 0.4808 0.2243 -0.0170 -0.0854 -0.0202 227 ALA A C   
1574 O O   . ALA A 202 ? 0.3974 0.4862 0.2294 -0.0110 -0.0795 -0.0166 227 ALA A O   
1575 C CB  . ALA A 202 ? 0.3829 0.5202 0.2557 -0.0060 -0.0977 -0.0010 227 ALA A CB  
1576 N N   . ASP A 203 ? 0.3823 0.4829 0.2180 -0.0288 -0.0889 -0.0317 228 ASP A N   
1577 C CA  . ASP A 203 ? 0.4075 0.4934 0.2183 -0.0338 -0.0854 -0.0408 228 ASP A CA  
1578 C C   . ASP A 203 ? 0.4036 0.4641 0.2134 -0.0337 -0.0725 -0.0483 228 ASP A C   
1579 O O   . ASP A 203 ? 0.4313 0.4781 0.2218 -0.0377 -0.0681 -0.0572 228 ASP A O   
1580 C CB  . ASP A 203 ? 0.4286 0.5235 0.2269 -0.0467 -0.0946 -0.0507 228 ASP A CB  
1581 C CG  . ASP A 203 ? 0.4216 0.5187 0.2342 -0.0573 -0.0971 -0.0592 228 ASP A CG  
1582 O OD1 . ASP A 203 ? 0.4038 0.4971 0.2368 -0.0541 -0.0920 -0.0566 228 ASP A OD1 
1583 O OD2 . ASP A 203 ? 0.4434 0.5450 0.2450 -0.0692 -0.1038 -0.0686 228 ASP A OD2 
1584 N N   . TRP A 204 ? 0.3889 0.4438 0.2187 -0.0289 -0.0666 -0.0448 229 TRP A N   
1585 C CA  . TRP A 204 ? 0.3735 0.4070 0.2044 -0.0259 -0.0547 -0.0481 229 TRP A CA  
1586 C C   . TRP A 204 ? 0.3802 0.4099 0.2116 -0.0151 -0.0489 -0.0382 229 TRP A C   
1587 O O   . TRP A 204 ? 0.3878 0.4273 0.2313 -0.0089 -0.0517 -0.0284 229 TRP A O   
1588 C CB  . TRP A 204 ? 0.3597 0.3896 0.2109 -0.0279 -0.0519 -0.0498 229 TRP A CB  
1589 C CG  . TRP A 204 ? 0.3620 0.3897 0.2133 -0.0394 -0.0546 -0.0603 229 TRP A CG  
1590 C CD1 . TRP A 204 ? 0.3790 0.4225 0.2307 -0.0480 -0.0647 -0.0632 229 TRP A CD1 
1591 C CD2 . TRP A 204 ? 0.3704 0.3794 0.2235 -0.0437 -0.0471 -0.0685 229 TRP A CD2 
1592 N NE1 . TRP A 204 ? 0.3841 0.4187 0.2365 -0.0586 -0.0639 -0.0735 229 TRP A NE1 
1593 C CE2 . TRP A 204 ? 0.3828 0.3952 0.2358 -0.0558 -0.0529 -0.0767 229 TRP A CE2 
1594 C CE3 . TRP A 204 ? 0.3621 0.3523 0.2172 -0.0386 -0.0363 -0.0692 229 TRP A CE3 
1595 C CZ2 . TRP A 204 ? 0.3988 0.3935 0.2524 -0.0627 -0.0474 -0.0855 229 TRP A CZ2 
1596 C CZ3 . TRP A 204 ? 0.3738 0.3480 0.2297 -0.0444 -0.0313 -0.0774 229 TRP A CZ3 
1597 C CH2 . TRP A 204 ? 0.3862 0.3615 0.2416 -0.0560 -0.0364 -0.0852 229 TRP A CH2 
1598 N N   . LYS A 205 ? 0.3856 0.4001 0.2053 -0.0128 -0.0400 -0.0410 230 LYS A N   
1599 C CA  . LYS A 205 ? 0.4022 0.4118 0.2238 -0.0041 -0.0334 -0.0323 230 LYS A CA  
1600 C C   . LYS A 205 ? 0.3725 0.3745 0.2126 -0.0011 -0.0272 -0.0309 230 LYS A C   
1601 O O   . LYS A 205 ? 0.3495 0.3437 0.1947 -0.0050 -0.0242 -0.0381 230 LYS A O   
1602 C CB  . LYS A 205 ? 0.4650 0.4640 0.2672 -0.0034 -0.0261 -0.0357 230 LYS A CB  
1603 C CG  . LYS A 205 ? 0.5130 0.5070 0.3161 0.0040  -0.0185 -0.0272 230 LYS A CG  
1604 C CD  . LYS A 205 ? 0.6243 0.6096 0.4088 0.0043  -0.0105 -0.0310 230 LYS A CD  
1605 C CE  . LYS A 205 ? 0.7141 0.7034 0.4759 -0.0004 -0.0152 -0.0363 230 LYS A CE  
1606 N NZ  . LYS A 205 ? 0.8425 0.8208 0.5870 -0.0009 -0.0057 -0.0434 230 LYS A NZ  
1607 N N   . VAL A 206 ? 0.3516 0.3559 0.2014 0.0055  -0.0260 -0.0213 231 VAL A N   
1608 C CA  . VAL A 206 ? 0.3247 0.3236 0.1909 0.0083  -0.0211 -0.0192 231 VAL A CA  
1609 C C   . VAL A 206 ? 0.3226 0.3162 0.1883 0.0141  -0.0153 -0.0119 231 VAL A C   
1610 O O   . VAL A 206 ? 0.3697 0.3679 0.2310 0.0176  -0.0179 -0.0046 231 VAL A O   
1611 C CB  . VAL A 206 ? 0.3009 0.3095 0.1830 0.0088  -0.0265 -0.0159 231 VAL A CB  
1612 C CG1 . VAL A 206 ? 0.2842 0.2867 0.1805 0.0115  -0.0212 -0.0137 231 VAL A CG1 
1613 C CG2 . VAL A 206 ? 0.2964 0.3121 0.1810 0.0018  -0.0324 -0.0225 231 VAL A CG2 
1614 N N   . ILE A 207 ? 0.3094 0.2937 0.1798 0.0149  -0.0077 -0.0134 232 ILE A N   
1615 C CA  . ILE A 207 ? 0.3077 0.2884 0.1820 0.0190  -0.0027 -0.0065 232 ILE A CA  
1616 C C   . ILE A 207 ? 0.2878 0.2656 0.1777 0.0192  -0.0004 -0.0067 232 ILE A C   
1617 O O   . ILE A 207 ? 0.2807 0.2558 0.1749 0.0168  0.0009  -0.0124 232 ILE A O   
1618 C CB  . ILE A 207 ? 0.3245 0.2995 0.1885 0.0198  0.0046  -0.0067 232 ILE A CB  
1619 C CG1 . ILE A 207 ? 0.3327 0.3015 0.2002 0.0186  0.0108  -0.0133 232 ILE A CG1 
1620 C CG2 . ILE A 207 ? 0.3471 0.3250 0.1929 0.0190  0.0024  -0.0071 232 ILE A CG2 
1621 C CD1 . ILE A 207 ? 0.3364 0.3012 0.1948 0.0200  0.0189  -0.0141 232 ILE A CD1 
1622 N N   . ASP A 208 ? 0.2850 0.2623 0.1821 0.0218  0.0005  -0.0005 233 ASP A N   
1623 C CA  . ASP A 208 ? 0.2647 0.2407 0.1749 0.0216  0.0013  -0.0009 233 ASP A CA  
1624 C C   . ASP A 208 ? 0.2710 0.2432 0.1856 0.0232  0.0047  0.0045  233 ASP A C   
1625 O O   . ASP A 208 ? 0.2644 0.2347 0.1735 0.0247  0.0058  0.0096  233 ASP A O   
1626 C CB  . ASP A 208 ? 0.2490 0.2309 0.1659 0.0215  -0.0043 -0.0013 233 ASP A CB  
1627 C CG  . ASP A 208 ? 0.2590 0.2431 0.1782 0.0254  -0.0066 0.0049  233 ASP A CG  
1628 O OD1 . ASP A 208 ? 0.2624 0.2476 0.1732 0.0276  -0.0081 0.0089  233 ASP A OD1 
1629 O OD2 . ASP A 208 ? 0.2417 0.2249 0.1701 0.0266  -0.0060 0.0061  233 ASP A OD2 
1630 N N   . LYS A 209 ? 0.2624 0.2333 0.1868 0.0221  0.0061  0.0035  234 LYS A N   
1631 C CA  . LYS A 209 ? 0.2550 0.2227 0.1845 0.0222  0.0078  0.0072  234 LYS A CA  
1632 C C   . LYS A 209 ? 0.2506 0.2195 0.1884 0.0219  0.0057  0.0055  234 LYS A C   
1633 O O   . LYS A 209 ? 0.2476 0.2185 0.1899 0.0203  0.0057  0.0021  234 LYS A O   
1634 C CB  . LYS A 209 ? 0.2586 0.2249 0.1906 0.0203  0.0126  0.0081  234 LYS A CB  
1635 C CG  . LYS A 209 ? 0.2566 0.2201 0.1938 0.0185  0.0137  0.0110  234 LYS A CG  
1636 C CD  . LYS A 209 ? 0.2711 0.2294 0.2029 0.0190  0.0147  0.0158  234 LYS A CD  
1637 C CE  . LYS A 209 ? 0.2897 0.2421 0.2249 0.0168  0.0152  0.0175  234 LYS A CE  
1638 N NZ  . LYS A 209 ? 0.3384 0.2877 0.2738 0.0198  0.0124  0.0168  234 LYS A NZ  
1639 N N   . THR A 210 ? 0.2456 0.2123 0.1848 0.0237  0.0048  0.0081  235 THR A N   
1640 C CA  . THR A 210 ? 0.2677 0.2353 0.2134 0.0240  0.0037  0.0065  235 THR A CA  
1641 C C   . THR A 210 ? 0.2634 0.2265 0.2120 0.0212  0.0063  0.0063  235 THR A C   
1642 O O   . THR A 210 ? 0.2685 0.2278 0.2151 0.0192  0.0086  0.0082  235 THR A O   
1643 C CB  . THR A 210 ? 0.2688 0.2360 0.2145 0.0283  0.0021  0.0092  235 THR A CB  
1644 O OG1 . THR A 210 ? 0.2843 0.2425 0.2263 0.0293  0.0045  0.0128  235 THR A OG1 
1645 C CG2 . THR A 210 ? 0.2776 0.2514 0.2203 0.0309  -0.0016 0.0106  235 THR A CG2 
1646 N N   . GLY A 211 ? 0.2447 0.2095 0.1978 0.0206  0.0060  0.0040  236 GLY A N   
1647 C CA  . GLY A 211 ? 0.2362 0.1968 0.1902 0.0181  0.0076  0.0035  236 GLY A CA  
1648 C C   . GLY A 211 ? 0.2381 0.1983 0.1939 0.0199  0.0077  0.0016  236 GLY A C   
1649 O O   . GLY A 211 ? 0.2328 0.1994 0.1921 0.0216  0.0065  0.0006  236 GLY A O   
1650 N N   . THR A 212 ? 0.2463 0.1989 0.1995 0.0192  0.0097  0.0010  237 THR A N   
1651 C CA  . THR A 212 ? 0.2513 0.2018 0.2049 0.0215  0.0113  -0.0013 237 THR A CA  
1652 C C   . THR A 212 ? 0.2658 0.2095 0.2150 0.0167  0.0130  -0.0039 237 THR A C   
1653 O O   . THR A 212 ? 0.2639 0.2019 0.2102 0.0129  0.0131  -0.0032 237 THR A O   
1654 C CB  . THR A 212 ? 0.2658 0.2110 0.2188 0.0277  0.0125  0.0006  237 THR A CB  
1655 O OG1 . THR A 212 ? 0.2535 0.2062 0.2091 0.0310  0.0097  0.0036  237 THR A OG1 
1656 C CG2 . THR A 212 ? 0.2796 0.2247 0.2347 0.0318  0.0151  -0.0016 237 THR A CG2 
1657 N N   . GLY A 213 ? 0.2543 0.1995 0.2030 0.0162  0.0143  -0.0071 238 GLY A N   
1658 C CA  . GLY A 213 ? 0.2561 0.1959 0.1989 0.0107  0.0152  -0.0102 238 GLY A CA  
1659 C C   . GLY A 213 ? 0.2543 0.1928 0.1939 0.0121  0.0182  -0.0141 238 GLY A C   
1660 O O   . GLY A 213 ? 0.2540 0.1957 0.1974 0.0178  0.0201  -0.0139 238 GLY A O   
1661 N N   . ASP A 214 ? 0.2536 0.1889 0.1861 0.0063  0.0184  -0.0175 240 ASP A N   
1662 C CA  . ASP A 214 ? 0.2598 0.1944 0.1870 0.0066  0.0217  -0.0217 240 ASP A CA  
1663 C C   . ASP A 214 ? 0.2354 0.1834 0.1677 0.0080  0.0210  -0.0193 240 ASP A C   
1664 O O   . ASP A 214 ? 0.2241 0.1804 0.1635 0.0082  0.0179  -0.0152 240 ASP A O   
1665 C CB  . ASP A 214 ? 0.2681 0.1965 0.1846 -0.0010 0.0213  -0.0261 240 ASP A CB  
1666 C CG  . ASP A 214 ? 0.3153 0.2267 0.2249 -0.0027 0.0238  -0.0302 240 ASP A CG  
1667 O OD1 . ASP A 214 ? 0.3239 0.2282 0.2378 0.0025  0.0256  -0.0281 240 ASP A OD1 
1668 O OD2 . ASP A 214 ? 0.3142 0.2197 0.2140 -0.0098 0.0237  -0.0350 240 ASP A OD2 
1669 N N   . TYR A 215 ? 0.2433 0.1924 0.1714 0.0089  0.0248  -0.0223 241 TYR A N   
1670 C CA  . TYR A 215 ? 0.2360 0.1967 0.1684 0.0097  0.0254  -0.0198 241 TYR A CA  
1671 C C   . TYR A 215 ? 0.2359 0.2039 0.1804 0.0148  0.0249  -0.0163 241 TYR A C   
1672 O O   . TYR A 215 ? 0.2284 0.2057 0.1785 0.0137  0.0237  -0.0132 241 TYR A O   
1673 C CB  . TYR A 215 ? 0.2442 0.2111 0.1743 0.0036  0.0212  -0.0170 241 TYR A CB  
1674 C CG  . TYR A 215 ? 0.2514 0.2141 0.1690 -0.0020 0.0210  -0.0206 241 TYR A CG  
1675 C CD1 . TYR A 215 ? 0.2665 0.2302 0.1756 -0.0028 0.0248  -0.0234 241 TYR A CD1 
1676 C CD2 . TYR A 215 ? 0.2717 0.2296 0.1855 -0.0069 0.0173  -0.0217 241 TYR A CD2 
1677 C CE1 . TYR A 215 ? 0.2872 0.2465 0.1826 -0.0086 0.0245  -0.0277 241 TYR A CE1 
1678 C CE2 . TYR A 215 ? 0.2832 0.2376 0.1850 -0.0133 0.0165  -0.0257 241 TYR A CE2 
1679 C CZ  . TYR A 215 ? 0.3009 0.2558 0.1927 -0.0141 0.0198  -0.0290 241 TYR A CZ  
1680 O OH  . TYR A 215 ? 0.3023 0.2542 0.1804 -0.0211 0.0186  -0.0335 241 TYR A OH  
1681 N N   . GLY A 216 ? 0.2419 0.2056 0.1899 0.0202  0.0263  -0.0168 242 GLY A N   
1682 C CA  . GLY A 216 ? 0.2454 0.2173 0.2042 0.0248  0.0250  -0.0135 242 GLY A CA  
1683 C C   . GLY A 216 ? 0.2360 0.2120 0.1987 0.0219  0.0197  -0.0102 242 GLY A C   
1684 O O   . GLY A 216 ? 0.2439 0.2288 0.2141 0.0227  0.0181  -0.0082 242 GLY A O   
1685 N N   . ARG A 217 ? 0.2245 0.1943 0.1822 0.0182  0.0173  -0.0100 243 ARG A N   
1686 C CA  . ARG A 217 ? 0.2157 0.1885 0.1763 0.0161  0.0135  -0.0073 243 ARG A CA  
1687 C C   . ARG A 217 ? 0.2232 0.1958 0.1871 0.0199  0.0120  -0.0058 243 ARG A C   
1688 O O   . ARG A 217 ? 0.2234 0.1891 0.1846 0.0227  0.0129  -0.0057 243 ARG A O   
1689 C CB  . ARG A 217 ? 0.2258 0.1940 0.1816 0.0117  0.0120  -0.0070 243 ARG A CB  
1690 C CG  . ARG A 217 ? 0.2231 0.1953 0.1767 0.0076  0.0116  -0.0068 243 ARG A CG  
1691 C CD  . ARG A 217 ? 0.2358 0.2057 0.1847 0.0030  0.0098  -0.0067 243 ARG A CD  
1692 N NE  . ARG A 217 ? 0.2298 0.2051 0.1760 -0.0005 0.0088  -0.0057 243 ARG A NE  
1693 C CZ  . ARG A 217 ? 0.2519 0.2264 0.1910 -0.0051 0.0078  -0.0072 243 ARG A CZ  
1694 N NH1 . ARG A 217 ? 0.2591 0.2266 0.1936 -0.0079 0.0077  -0.0104 243 ARG A NH1 
1695 N NH2 . ARG A 217 ? 0.2752 0.2558 0.2110 -0.0075 0.0068  -0.0055 243 ARG A NH2 
1696 N N   . ALA A 218 ? 0.2053 0.1848 0.1740 0.0198  0.0097  -0.0045 244 ALA A N   
1697 C CA  . ALA A 218 ? 0.2088 0.1894 0.1787 0.0224  0.0074  -0.0030 244 ALA A CA  
1698 C C   . ALA A 218 ? 0.1959 0.1797 0.1669 0.0194  0.0051  -0.0029 244 ALA A C   
1699 O O   . ALA A 218 ? 0.2084 0.1972 0.1833 0.0171  0.0050  -0.0037 244 ALA A O   
1700 C CB  . ALA A 218 ? 0.2099 0.1970 0.1850 0.0270  0.0073  -0.0025 244 ALA A CB  
1701 N N   . ASN A 219 ? 0.1983 0.1782 0.1654 0.0192  0.0043  -0.0020 245 ASN A N   
1702 C CA  . ASN A 219 ? 0.2091 0.1896 0.1757 0.0170  0.0034  -0.0026 245 ASN A CA  
1703 C C   . ASN A 219 ? 0.2164 0.1971 0.1793 0.0188  0.0017  -0.0022 245 ASN A C   
1704 O O   . ASN A 219 ? 0.2030 0.1820 0.1632 0.0216  0.0014  -0.0001 245 ASN A O   
1705 C CB  . ASN A 219 ? 0.2124 0.1891 0.1775 0.0152  0.0050  -0.0016 245 ASN A CB  
1706 C CG  . ASN A 219 ? 0.2281 0.2052 0.1950 0.0133  0.0060  -0.0012 245 ASN A CG  
1707 O OD1 . ASN A 219 ? 0.2048 0.1847 0.1742 0.0125  0.0061  -0.0018 245 ASN A OD1 
1708 N ND2 . ASN A 219 ? 0.2285 0.2035 0.1937 0.0119  0.0066  0.0001  245 ASN A ND2 
1709 N N   . ASP A 220 ? 0.2077 0.1893 0.1692 0.0170  0.0009  -0.0040 246 ASP A N   
1710 C CA  . ASP A 220 ? 0.2295 0.2105 0.1846 0.0179  -0.0003 -0.0041 246 ASP A CA  
1711 C C   . ASP A 220 ? 0.2315 0.2094 0.1840 0.0156  0.0014  -0.0070 246 ASP A C   
1712 O O   . ASP A 220 ? 0.2352 0.2128 0.1912 0.0132  0.0015  -0.0094 246 ASP A O   
1713 C CB  . ASP A 220 ? 0.2198 0.2077 0.1747 0.0187  -0.0044 -0.0044 246 ASP A CB  
1714 C CG  . ASP A 220 ? 0.2369 0.2251 0.1834 0.0206  -0.0061 -0.0027 246 ASP A CG  
1715 O OD1 . ASP A 220 ? 0.2456 0.2281 0.1873 0.0220  -0.0035 -0.0004 246 ASP A OD1 
1716 O OD2 . ASP A 220 ? 0.2413 0.2364 0.1862 0.0203  -0.0103 -0.0034 246 ASP A OD2 
1717 N N   . ILE A 221 ? 0.2365 0.2110 0.1830 0.0167  0.0035  -0.0064 247 ILE A N   
1718 C CA  . ILE A 221 ? 0.2340 0.2047 0.1769 0.0158  0.0061  -0.0096 247 ILE A CA  
1719 C C   . ILE A 221 ? 0.2391 0.2099 0.1717 0.0162  0.0053  -0.0110 247 ILE A C   
1720 O O   . ILE A 221 ? 0.2360 0.2083 0.1646 0.0181  0.0049  -0.0074 247 ILE A O   
1721 C CB  . ILE A 221 ? 0.2280 0.1959 0.1741 0.0171  0.0108  -0.0076 247 ILE A CB  
1722 C CG1 . ILE A 221 ? 0.2464 0.2155 0.1904 0.0185  0.0124  -0.0037 247 ILE A CG1 
1723 C CG2 . ILE A 221 ? 0.2190 0.1879 0.1738 0.0163  0.0106  -0.0061 247 ILE A CG2 
1724 C CD1 . ILE A 221 ? 0.2610 0.2305 0.2093 0.0192  0.0168  -0.0014 247 ILE A CD1 
1725 N N   . ALA A 222 ? 0.2403 0.2089 0.1677 0.0140  0.0050  -0.0163 248 ALA A N   
1726 C CA  . ALA A 222 ? 0.2526 0.2222 0.1683 0.0134  0.0032  -0.0185 248 ALA A CA  
1727 C C   . ALA A 222 ? 0.2685 0.2308 0.1765 0.0117  0.0069  -0.0249 248 ALA A C   
1728 O O   . ALA A 222 ? 0.2828 0.2391 0.1955 0.0104  0.0094  -0.0282 248 ALA A O   
1729 C CB  . ALA A 222 ? 0.2543 0.2316 0.1702 0.0112  -0.0037 -0.0190 248 ALA A CB  
1730 N N   . VAL A 223 ? 0.2664 0.2284 0.1613 0.0119  0.0074  -0.0266 249 VAL A N   
1731 C CA  . VAL A 223 ? 0.2722 0.2279 0.1557 0.0090  0.0091  -0.0345 249 VAL A CA  
1732 C C   . VAL A 223 ? 0.2922 0.2549 0.1668 0.0051  0.0014  -0.0365 249 VAL A C   
1733 O O   . VAL A 223 ? 0.2960 0.2669 0.1681 0.0070  -0.0025 -0.0308 249 VAL A O   
1734 C CB  . VAL A 223 ? 0.2919 0.2422 0.1662 0.0125  0.0168  -0.0351 249 VAL A CB  
1735 C CG1 . VAL A 223 ? 0.3116 0.2530 0.1724 0.0099  0.0198  -0.0446 249 VAL A CG1 
1736 C CG2 . VAL A 223 ? 0.2830 0.2307 0.1694 0.0167  0.0234  -0.0312 249 VAL A CG2 
1737 N N   . VAL A 224 ? 0.3105 0.2700 0.1808 -0.0006 -0.0010 -0.0443 250 VAL A N   
1738 C CA  . VAL A 224 ? 0.3261 0.2942 0.1883 -0.0057 -0.0093 -0.0470 250 VAL A CA  
1739 C C   . VAL A 224 ? 0.3435 0.3027 0.1883 -0.0103 -0.0072 -0.0569 250 VAL A C   
1740 O O   . VAL A 224 ? 0.3572 0.3026 0.2002 -0.0102 0.0002  -0.0625 250 VAL A O   
1741 C CB  . VAL A 224 ? 0.3119 0.2879 0.1870 -0.0104 -0.0158 -0.0471 250 VAL A CB  
1742 C CG1 . VAL A 224 ? 0.3022 0.2835 0.1937 -0.0055 -0.0154 -0.0389 250 VAL A CG1 
1743 C CG2 . VAL A 224 ? 0.3200 0.2853 0.1972 -0.0165 -0.0133 -0.0552 250 VAL A CG2 
1744 N N   . TRP A 225 ? 0.3511 0.3184 0.1825 -0.0138 -0.0137 -0.0586 251 TRP A N   
1745 C CA  . TRP A 225 ? 0.3785 0.3383 0.1903 -0.0194 -0.0129 -0.0689 251 TRP A CA  
1746 C C   . TRP A 225 ? 0.3746 0.3458 0.1830 -0.0281 -0.0240 -0.0727 251 TRP A C   
1747 O O   . TRP A 225 ? 0.3688 0.3567 0.1804 -0.0270 -0.0321 -0.0653 251 TRP A O   
1748 C CB  . TRP A 225 ? 0.3977 0.3571 0.1915 -0.0153 -0.0092 -0.0673 251 TRP A CB  
1749 C CG  . TRP A 225 ? 0.4123 0.3608 0.2069 -0.0081 0.0027  -0.0656 251 TRP A CG  
1750 C CD1 . TRP A 225 ? 0.4335 0.3679 0.2168 -0.0074 0.0121  -0.0735 251 TRP A CD1 
1751 C CD2 . TRP A 225 ? 0.3980 0.3505 0.2051 -0.0007 0.0063  -0.0548 251 TRP A CD2 
1752 N NE1 . TRP A 225 ? 0.4333 0.3649 0.2233 0.0004  0.0212  -0.0676 251 TRP A NE1 
1753 C CE2 . TRP A 225 ? 0.4127 0.3551 0.2169 0.0038  0.0175  -0.0564 251 TRP A CE2 
1754 C CE3 . TRP A 225 ? 0.3925 0.3553 0.2130 0.0024  0.0016  -0.0446 251 TRP A CE3 
1755 C CZ2 . TRP A 225 ? 0.3939 0.3385 0.2090 0.0100  0.0231  -0.0479 251 TRP A CZ2 
1756 C CZ3 . TRP A 225 ? 0.3802 0.3423 0.2091 0.0083  0.0074  -0.0369 251 TRP A CZ3 
1757 C CH2 . TRP A 225 ? 0.3993 0.3533 0.2256 0.0115  0.0176  -0.0385 251 TRP A CH2 
1758 N N   . SER A 226 ? 0.3757 0.3374 0.1781 -0.0368 -0.0242 -0.0840 252 SER A N   
1759 C CA  . SER A 226 ? 0.3946 0.3671 0.1932 -0.0473 -0.0348 -0.0892 252 SER A CA  
1760 C C   . SER A 226 ? 0.4166 0.3983 0.1937 -0.0489 -0.0405 -0.0902 252 SER A C   
1761 O O   . SER A 226 ? 0.4175 0.3926 0.1802 -0.0431 -0.0343 -0.0893 252 SER A O   
1762 C CB  . SER A 226 ? 0.4054 0.3625 0.2003 -0.0572 -0.0326 -0.1018 252 SER A CB  
1763 O OG  . SER A 226 ? 0.4407 0.3835 0.2115 -0.0600 -0.0280 -0.1123 252 SER A OG  
1764 N N   . PRO A 227 ? 0.4414 0.4394 0.2152 -0.0575 -0.0525 -0.0921 254 PRO A N   
1765 C CA  . PRO A 227 ? 0.4672 0.4746 0.2184 -0.0603 -0.0590 -0.0936 254 PRO A CA  
1766 C C   . PRO A 227 ? 0.4982 0.4868 0.2226 -0.0637 -0.0518 -0.1058 254 PRO A C   
1767 O O   . PRO A 227 ? 0.5110 0.5042 0.2150 -0.0622 -0.0533 -0.1048 254 PRO A O   
1768 C CB  . PRO A 227 ? 0.4797 0.5065 0.2356 -0.0713 -0.0729 -0.0959 254 PRO A CB  
1769 C CG  . PRO A 227 ? 0.4444 0.4787 0.2297 -0.0690 -0.0737 -0.0889 254 PRO A CG  
1770 C CD  . PRO A 227 ? 0.4303 0.4408 0.2225 -0.0646 -0.0605 -0.0918 254 PRO A CD  
1771 N N   . THR A 228 ? 0.5142 0.4812 0.2380 -0.0680 -0.0437 -0.1170 255 THR A N   
1772 C CA  . THR A 228 ? 0.5494 0.4958 0.2487 -0.0699 -0.0348 -0.1292 255 THR A CA  
1773 C C   . THR A 228 ? 0.5384 0.4692 0.2409 -0.0577 -0.0200 -0.1257 255 THR A C   
1774 O O   . THR A 228 ? 0.5718 0.4841 0.2577 -0.0570 -0.0100 -0.1351 255 THR A O   
1775 C CB  . THR A 228 ? 0.5811 0.5117 0.2752 -0.0824 -0.0346 -0.1446 255 THR A CB  
1776 O OG1 . THR A 228 ? 0.5664 0.4864 0.2836 -0.0797 -0.0287 -0.1424 255 THR A OG1 
1777 C CG2 . THR A 228 ? 0.6024 0.5502 0.2937 -0.0962 -0.0497 -0.1487 255 THR A CG2 
1778 N N   . GLY A 229 ? 0.4984 0.4367 0.2221 -0.0482 -0.0182 -0.1126 256 GLY A N   
1779 C CA  . GLY A 229 ? 0.4894 0.4183 0.2162 -0.0370 -0.0058 -0.1075 256 GLY A CA  
1780 C C   . GLY A 229 ? 0.4806 0.3931 0.2237 -0.0338 0.0034  -0.1098 256 GLY A C   
1781 O O   . GLY A 229 ? 0.4688 0.3730 0.2148 -0.0252 0.0142  -0.1069 256 GLY A O   
1782 N N   . VAL A 230 ? 0.4627 0.3727 0.2182 -0.0404 -0.0010 -0.1131 257 VAL A N   
1783 C CA  . VAL A 230 ? 0.4562 0.3506 0.2265 -0.0376 0.0072  -0.1142 257 VAL A CA  
1784 C C   . VAL A 230 ? 0.4221 0.3267 0.2155 -0.0295 0.0073  -0.1007 257 VAL A C   
1785 O O   . VAL A 230 ? 0.3923 0.3125 0.1975 -0.0316 -0.0015 -0.0941 257 VAL A O   
1786 C CB  . VAL A 230 ? 0.4686 0.3540 0.2422 -0.0483 0.0037  -0.1228 257 VAL A CB  
1787 C CG1 . VAL A 230 ? 0.4645 0.3340 0.2540 -0.0441 0.0124  -0.1215 257 VAL A CG1 
1788 C CG2 . VAL A 230 ? 0.5087 0.3818 0.2582 -0.0579 0.0035  -0.1378 257 VAL A CG2 
1789 N N   . PRO A 231 ? 0.4245 0.3213 0.2252 -0.0201 0.0174  -0.0963 258 PRO A N   
1790 C CA  . PRO A 231 ? 0.3906 0.2975 0.2110 -0.0133 0.0172  -0.0841 258 PRO A CA  
1791 C C   . PRO A 231 ? 0.3799 0.2822 0.2189 -0.0139 0.0176  -0.0819 258 PRO A C   
1792 O O   . PRO A 231 ? 0.3866 0.2729 0.2250 -0.0156 0.0229  -0.0884 258 PRO A O   
1793 C CB  . PRO A 231 ? 0.3873 0.2902 0.2052 -0.0041 0.0274  -0.0808 258 PRO A CB  
1794 C CG  . PRO A 231 ? 0.4178 0.3016 0.2232 -0.0047 0.0361  -0.0920 258 PRO A CG  
1795 C CD  . PRO A 231 ? 0.4397 0.3199 0.2294 -0.0153 0.0294  -0.1026 258 PRO A CD  
1796 N N   . TYR A 232 ? 0.3524 0.2681 0.2068 -0.0119 0.0127  -0.0725 259 TYR A N   
1797 C CA  . TYR A 232 ? 0.3414 0.2550 0.2132 -0.0108 0.0138  -0.0681 259 TYR A CA  
1798 C C   . TYR A 232 ? 0.3212 0.2457 0.2048 -0.0038 0.0138  -0.0574 259 TYR A C   
1799 O O   . TYR A 232 ? 0.3385 0.2733 0.2184 -0.0016 0.0109  -0.0531 259 TYR A O   
1800 C CB  . TYR A 232 ? 0.3389 0.2588 0.2172 -0.0190 0.0059  -0.0694 259 TYR A CB  
1801 C CG  . TYR A 232 ? 0.3553 0.2662 0.2224 -0.0283 0.0042  -0.0803 259 TYR A CG  
1802 C CD1 . TYR A 232 ? 0.3686 0.2620 0.2375 -0.0317 0.0094  -0.0857 259 TYR A CD1 
1803 C CD2 . TYR A 232 ? 0.3698 0.2892 0.2240 -0.0340 -0.0027 -0.0850 259 TYR A CD2 
1804 C CE1 . TYR A 232 ? 0.3876 0.2705 0.2455 -0.0414 0.0081  -0.0966 259 TYR A CE1 
1805 C CE2 . TYR A 232 ? 0.3904 0.3015 0.2328 -0.0440 -0.0047 -0.0960 259 TYR A CE2 
1806 C CZ  . TYR A 232 ? 0.3986 0.2907 0.2431 -0.0480 0.0009  -0.1022 259 TYR A CZ  
1807 O OH  . TYR A 232 ? 0.4285 0.3099 0.2615 -0.0587 -0.0006 -0.1137 259 TYR A OH  
1808 N N   . VAL A 233 ? 0.3074 0.2284 0.2040 -0.0006 0.0174  -0.0530 260 VAL A N   
1809 C CA  . VAL A 233 ? 0.2968 0.2272 0.2043 0.0045  0.0171  -0.0438 260 VAL A CA  
1810 C C   . VAL A 233 ? 0.2977 0.2335 0.2170 0.0015  0.0125  -0.0406 260 VAL A C   
1811 O O   . VAL A 233 ? 0.2967 0.2252 0.2198 -0.0020 0.0134  -0.0433 260 VAL A O   
1812 C CB  . VAL A 233 ? 0.3126 0.2377 0.2252 0.0111  0.0249  -0.0404 260 VAL A CB  
1813 C CG1 . VAL A 233 ? 0.3089 0.2439 0.2326 0.0145  0.0237  -0.0317 260 VAL A CG1 
1814 C CG2 . VAL A 233 ? 0.3442 0.2650 0.2457 0.0145  0.0308  -0.0436 260 VAL A CG2 
1815 N N   . VAL A 234 ? 0.2834 0.2310 0.2080 0.0029  0.0083  -0.0348 261 VAL A N   
1816 C CA  . VAL A 234 ? 0.2719 0.2264 0.2065 0.0004  0.0043  -0.0320 261 VAL A CA  
1817 C C   . VAL A 234 ? 0.2552 0.2146 0.1974 0.0051  0.0053  -0.0250 261 VAL A C   
1818 O O   . VAL A 234 ? 0.2495 0.2140 0.1894 0.0081  0.0043  -0.0218 261 VAL A O   
1819 C CB  . VAL A 234 ? 0.2762 0.2411 0.2092 -0.0036 -0.0026 -0.0335 261 VAL A CB  
1820 C CG1 . VAL A 234 ? 0.2687 0.2421 0.2134 -0.0055 -0.0056 -0.0304 261 VAL A CG1 
1821 C CG2 . VAL A 234 ? 0.2866 0.2472 0.2105 -0.0096 -0.0044 -0.0413 261 VAL A CG2 
1822 N N   . ALA A 235 ? 0.2360 0.1935 0.1866 0.0051  0.0071  -0.0225 262 ALA A N   
1823 C CA  . ALA A 235 ? 0.2367 0.1993 0.1937 0.0078  0.0072  -0.0168 262 ALA A CA  
1824 C C   . ALA A 235 ? 0.2320 0.2003 0.1956 0.0051  0.0046  -0.0156 262 ALA A C   
1825 O O   . ALA A 235 ? 0.2335 0.1985 0.2005 0.0019  0.0055  -0.0167 262 ALA A O   
1826 C CB  . ALA A 235 ? 0.2341 0.1918 0.1942 0.0106  0.0116  -0.0140 262 ALA A CB  
1827 N N   . VAL A 236 ? 0.2245 0.2003 0.1901 0.0067  0.0024  -0.0131 263 VAL A N   
1828 C CA  . VAL A 236 ? 0.2166 0.1986 0.1888 0.0054  0.0013  -0.0116 263 VAL A CA  
1829 C C   . VAL A 236 ? 0.2036 0.1868 0.1769 0.0085  0.0026  -0.0080 263 VAL A C   
1830 O O   . VAL A 236 ? 0.2265 0.2095 0.1965 0.0114  0.0021  -0.0069 263 VAL A O   
1831 C CB  . VAL A 236 ? 0.2288 0.2196 0.2029 0.0039  -0.0025 -0.0131 263 VAL A CB  
1832 C CG1 . VAL A 236 ? 0.2558 0.2453 0.2277 -0.0011 -0.0044 -0.0175 263 VAL A CG1 
1833 C CG2 . VAL A 236 ? 0.2651 0.2596 0.2355 0.0080  -0.0047 -0.0116 263 VAL A CG2 
1834 N N   . MET A 237 ? 0.1966 0.1799 0.1735 0.0074  0.0043  -0.0062 264 MET A N   
1835 C CA  . MET A 237 ? 0.1933 0.1772 0.1698 0.0091  0.0054  -0.0038 264 MET A CA  
1836 C C   . MET A 237 ? 0.1946 0.1836 0.1745 0.0081  0.0062  -0.0034 264 MET A C   
1837 O O   . MET A 237 ? 0.1866 0.1780 0.1704 0.0053  0.0066  -0.0037 264 MET A O   
1838 C CB  . MET A 237 ? 0.2052 0.1851 0.1809 0.0089  0.0069  -0.0015 264 MET A CB  
1839 C CG  . MET A 237 ? 0.1989 0.1750 0.1725 0.0104  0.0074  -0.0020 264 MET A CG  
1840 S SD  . MET A 237 ? 0.2349 0.2101 0.2100 0.0117  0.0090  0.0018  264 MET A SD  
1841 C CE  . MET A 237 ? 0.2131 0.1915 0.1858 0.0113  0.0078  0.0027  264 MET A CE  
1842 N N   . SER A 238 ? 0.2033 0.1937 0.1819 0.0100  0.0071  -0.0031 265 SER A N   
1843 C CA  . SER A 238 ? 0.1884 0.1838 0.1696 0.0097  0.0091  -0.0030 265 SER A CA  
1844 C C   . SER A 238 ? 0.2004 0.1928 0.1764 0.0109  0.0109  -0.0031 265 SER A C   
1845 O O   . SER A 238 ? 0.1878 0.1752 0.1598 0.0124  0.0103  -0.0037 265 SER A O   
1846 C CB  . SER A 238 ? 0.1828 0.1856 0.1695 0.0115  0.0085  -0.0040 265 SER A CB  
1847 O OG  . SER A 238 ? 0.1868 0.1883 0.1716 0.0162  0.0080  -0.0043 265 SER A OG  
1848 N N   . ASP A 239 ? 0.2091 0.2045 0.1848 0.0098  0.0136  -0.0029 266 ASP A N   
1849 C CA  . ASP A 239 ? 0.2135 0.2064 0.1833 0.0109  0.0161  -0.0046 266 ASP A CA  
1850 C C   . ASP A 239 ? 0.2243 0.2235 0.1965 0.0117  0.0201  -0.0051 266 ASP A C   
1851 O O   . ASP A 239 ? 0.2284 0.2342 0.2069 0.0099  0.0206  -0.0033 266 ASP A O   
1852 C CB  . ASP A 239 ? 0.2307 0.2199 0.1934 0.0077  0.0153  -0.0037 266 ASP A CB  
1853 C CG  . ASP A 239 ? 0.2559 0.2492 0.2185 0.0046  0.0159  -0.0005 266 ASP A CG  
1854 O OD1 . ASP A 239 ? 0.2947 0.2911 0.2546 0.0039  0.0192  -0.0008 266 ASP A OD1 
1855 O OD2 . ASP A 239 ? 0.3068 0.3000 0.2723 0.0034  0.0139  0.0024  266 ASP A OD2 
1856 N N   . ARG A 240 ? 0.2299 0.2262 0.1970 0.0141  0.0236  -0.0078 267 ARG A N   
1857 C CA  . ARG A 240 ? 0.2340 0.2360 0.2020 0.0155  0.0290  -0.0087 267 ARG A CA  
1858 C C   . ARG A 240 ? 0.2502 0.2463 0.2058 0.0138  0.0320  -0.0114 267 ARG A C   
1859 O O   . ARG A 240 ? 0.2572 0.2502 0.2085 0.0170  0.0369  -0.0151 267 ARG A O   
1860 C CB  . ARG A 240 ? 0.2481 0.2537 0.2235 0.0218  0.0312  -0.0099 267 ARG A CB  
1861 C CG  . ARG A 240 ? 0.2580 0.2695 0.2434 0.0228  0.0266  -0.0075 267 ARG A CG  
1862 C CD  . ARG A 240 ? 0.2711 0.2879 0.2642 0.0296  0.0275  -0.0073 267 ARG A CD  
1863 N NE  . ARG A 240 ? 0.2798 0.3079 0.2803 0.0318  0.0326  -0.0071 267 ARG A NE  
1864 C CZ  . ARG A 240 ? 0.3063 0.3338 0.3063 0.0378  0.0388  -0.0088 267 ARG A CZ  
1865 N NH1 . ARG A 240 ? 0.3058 0.3208 0.2991 0.0430  0.0406  -0.0110 267 ARG A NH1 
1866 N NH2 . ARG A 240 ? 0.3185 0.3580 0.3257 0.0388  0.0440  -0.0082 267 ARG A NH2 
1867 N N   . ALA A 241 ? 0.2612 0.2561 0.2109 0.0087  0.0291  -0.0093 268 ALA A N   
1868 C CA  . ALA A 241 ? 0.2592 0.2490 0.1959 0.0055  0.0296  -0.0116 268 ALA A CA  
1869 C C   . ALA A 241 ? 0.2646 0.2568 0.1943 0.0057  0.0358  -0.0138 268 ALA A C   
1870 O O   . ALA A 241 ? 0.2613 0.2474 0.1786 0.0041  0.0375  -0.0182 268 ALA A O   
1871 C CB  . ALA A 241 ? 0.2682 0.2599 0.2027 0.0009  0.0246  -0.0072 268 ALA A CB  
1872 N N   . GLY A 242 ? 0.2662 0.2673 0.2035 0.0069  0.0394  -0.0110 269 GLY A N   
1873 C CA  . GLY A 242 ? 0.2743 0.2797 0.2073 0.0080  0.0468  -0.0127 269 GLY A CA  
1874 C C   . GLY A 242 ? 0.2914 0.2906 0.2205 0.0134  0.0523  -0.0194 269 GLY A C   
1875 O O   . GLY A 242 ? 0.3096 0.3079 0.2290 0.0139  0.0588  -0.0229 269 GLY A O   
1876 N N   . GLY A 243 ? 0.2870 0.2810 0.2228 0.0178  0.0502  -0.0210 270 GLY A N   
1877 C CA  . GLY A 243 ? 0.3120 0.2981 0.2452 0.0240  0.0556  -0.0264 270 GLY A CA  
1878 C C   . GLY A 243 ? 0.3320 0.3021 0.2501 0.0213  0.0547  -0.0320 270 GLY A C   
1879 O O   . GLY A 243 ? 0.3571 0.3165 0.2707 0.0259  0.0597  -0.0372 270 GLY A O   
1880 N N   . GLY A 244 ? 0.3100 0.2783 0.2205 0.0137  0.0485  -0.0309 271 GLY A N   
1881 C CA  . GLY A 244 ? 0.3092 0.2645 0.2067 0.0094  0.0465  -0.0360 271 GLY A CA  
1882 C C   . GLY A 244 ? 0.2909 0.2387 0.1944 0.0102  0.0420  -0.0351 271 GLY A C   
1883 O O   . GLY A 244 ? 0.2544 0.2075 0.1709 0.0143  0.0399  -0.0305 271 GLY A O   
1884 N N   . TYR A 245 ? 0.2877 0.2231 0.1805 0.0056  0.0406  -0.0398 272 TYR A N   
1885 C CA  . TYR A 245 ? 0.2937 0.2230 0.1903 0.0036  0.0357  -0.0382 272 TYR A CA  
1886 C C   . TYR A 245 ? 0.2967 0.2195 0.2018 0.0121  0.0389  -0.0374 272 TYR A C   
1887 O O   . TYR A 245 ? 0.3015 0.2245 0.2141 0.0128  0.0350  -0.0332 272 TYR A O   
1888 C CB  . TYR A 245 ? 0.2989 0.2165 0.1824 -0.0044 0.0340  -0.0437 272 TYR A CB  
1889 C CG  . TYR A 245 ? 0.3183 0.2169 0.1939 -0.0018 0.0405  -0.0509 272 TYR A CG  
1890 C CD1 . TYR A 245 ? 0.3330 0.2252 0.1973 -0.0003 0.0474  -0.0577 272 TYR A CD1 
1891 C CD2 . TYR A 245 ? 0.3234 0.2099 0.2030 0.0004  0.0407  -0.0503 272 TYR A CD2 
1892 C CE1 . TYR A 245 ? 0.3678 0.2409 0.2254 0.0037  0.0546  -0.0643 272 TYR A CE1 
1893 C CE2 . TYR A 245 ? 0.3552 0.2222 0.2279 0.0037  0.0473  -0.0561 272 TYR A CE2 
1894 C CZ  . TYR A 245 ? 0.3659 0.2257 0.2280 0.0058  0.0544  -0.0634 272 TYR A CZ  
1895 O OH  . TYR A 245 ? 0.4501 0.2891 0.3056 0.0103  0.0620  -0.0693 272 TYR A OH  
1896 N N   . ASP A 246 ? 0.2971 0.2147 0.2008 0.0188  0.0463  -0.0409 273 ASP A N   
1897 C CA  . ASP A 246 ? 0.3086 0.2204 0.2203 0.0279  0.0496  -0.0395 273 ASP A CA  
1898 C C   . ASP A 246 ? 0.3010 0.2293 0.2272 0.0351  0.0502  -0.0341 273 ASP A C   
1899 O O   . ASP A 246 ? 0.2969 0.2243 0.2306 0.0440  0.0538  -0.0327 273 ASP A O   
1900 C CB  . ASP A 246 ? 0.3373 0.2317 0.2398 0.0321  0.0578  -0.0463 273 ASP A CB  
1901 C CG  . ASP A 246 ? 0.3675 0.2661 0.2652 0.0348  0.0650  -0.0507 273 ASP A CG  
1902 O OD1 . ASP A 246 ? 0.3788 0.2897 0.2733 0.0287  0.0627  -0.0502 273 ASP A OD1 
1903 O OD2 . ASP A 246 ? 0.3954 0.2844 0.2919 0.0430  0.0733  -0.0543 273 ASP A OD2 
1904 N N   . ALA A 247 ? 0.2914 0.2350 0.2224 0.0312  0.0466  -0.0307 274 ALA A N   
1905 C CA  . ALA A 247 ? 0.2782 0.2377 0.2234 0.0358  0.0463  -0.0259 274 ALA A CA  
1906 C C   . ALA A 247 ? 0.2609 0.2206 0.2151 0.0400  0.0421  -0.0216 274 ALA A C   
1907 O O   . ALA A 247 ? 0.2560 0.2090 0.2071 0.0366  0.0375  -0.0206 274 ALA A O   
1908 C CB  . ALA A 247 ? 0.2560 0.2279 0.2038 0.0295  0.0425  -0.0228 274 ALA A CB  
1909 N N   . GLU A 248 ? 0.2686 0.2383 0.2345 0.0472  0.0437  -0.0187 275 GLU A N   
1910 C CA  . GLU A 248 ? 0.2807 0.2526 0.2545 0.0517  0.0394  -0.0141 275 GLU A CA  
1911 C C   . GLU A 248 ? 0.2621 0.2443 0.2404 0.0459  0.0322  -0.0108 275 GLU A C   
1912 O O   . GLU A 248 ? 0.2631 0.2579 0.2472 0.0428  0.0315  -0.0100 275 GLU A O   
1913 C CB  . GLU A 248 ? 0.3061 0.2882 0.2918 0.0614  0.0426  -0.0113 275 GLU A CB  
1914 C CG  . GLU A 248 ? 0.3850 0.3561 0.3672 0.0691  0.0512  -0.0146 275 GLU A CG  
1915 C CD  . GLU A 248 ? 0.4608 0.4437 0.4565 0.0801  0.0555  -0.0114 275 GLU A CD  
1916 O OE1 . GLU A 248 ? 0.4703 0.4729 0.4796 0.0813  0.0511  -0.0064 275 GLU A OE1 
1917 O OE2 . GLU A 248 ? 0.5677 0.5399 0.5604 0.0876  0.0636  -0.0143 275 GLU A OE2 
1918 N N   . PRO A 249 ? 0.2635 0.2398 0.2391 0.0441  0.0273  -0.0088 276 PRO A N   
1919 C CA  . PRO A 249 ? 0.2438 0.2291 0.2235 0.0400  0.0213  -0.0061 276 PRO A CA  
1920 C C   . PRO A 249 ? 0.2413 0.2408 0.2321 0.0444  0.0192  -0.0030 276 PRO A C   
1921 O O   . PRO A 249 ? 0.2200 0.2208 0.2151 0.0520  0.0213  -0.0013 276 PRO A O   
1922 C CB  . PRO A 249 ? 0.2686 0.2434 0.2417 0.0383  0.0183  -0.0050 276 PRO A CB  
1923 C CG  . PRO A 249 ? 0.3114 0.2728 0.2796 0.0430  0.0221  -0.0056 276 PRO A CG  
1924 C CD  . PRO A 249 ? 0.2872 0.2474 0.2552 0.0458  0.0280  -0.0091 276 PRO A CD  
1925 N N   . ARG A 250 ? 0.2316 0.2415 0.2271 0.0397  0.0149  -0.0021 277 ARG A N   
1926 C CA  . ARG A 250 ? 0.2385 0.2637 0.2444 0.0418  0.0117  0.0005  277 ARG A CA  
1927 C C   . ARG A 250 ? 0.2195 0.2459 0.2231 0.0381  0.0053  0.0014  277 ARG A C   
1928 O O   . ARG A 250 ? 0.1979 0.2266 0.2013 0.0314  0.0033  -0.0002 277 ARG A O   
1929 C CB  . ARG A 250 ? 0.2461 0.2843 0.2605 0.0379  0.0133  -0.0003 277 ARG A CB  
1930 C CG  . ARG A 250 ? 0.2720 0.3119 0.2891 0.0421  0.0204  -0.0012 277 ARG A CG  
1931 C CD  . ARG A 250 ? 0.2726 0.3216 0.2992 0.0514  0.0219  0.0015  277 ARG A CD  
1932 N NE  . ARG A 250 ? 0.3025 0.3523 0.3311 0.0556  0.0301  -0.0001 277 ARG A NE  
1933 C CZ  . ARG A 250 ? 0.2882 0.3285 0.3135 0.0636  0.0358  -0.0011 277 ARG A CZ  
1934 N NH1 . ARG A 250 ? 0.3019 0.3310 0.3229 0.0690  0.0341  0.0004  277 ARG A NH1 
1935 N NH2 . ARG A 250 ? 0.2979 0.3387 0.3232 0.0663  0.0438  -0.0036 277 ARG A NH2 
1936 N N   . GLU A 251 ? 0.2351 0.2590 0.2361 0.0427  0.0027  0.0042  278 GLU A N   
1937 C CA  . GLU A 251 ? 0.2346 0.2602 0.2318 0.0397  -0.0029 0.0050  278 GLU A CA  
1938 C C   . GLU A 251 ? 0.2080 0.2495 0.2127 0.0355  -0.0073 0.0044  278 GLU A C   
1939 O O   . GLU A 251 ? 0.1987 0.2393 0.1990 0.0296  -0.0105 0.0021  278 GLU A O   
1940 C CB  . GLU A 251 ? 0.2564 0.2804 0.2507 0.0462  -0.0051 0.0095  278 GLU A CB  
1941 C CG  . GLU A 251 ? 0.2660 0.2725 0.2516 0.0487  -0.0012 0.0103  278 GLU A CG  
1942 C CD  . GLU A 251 ? 0.2682 0.2711 0.2487 0.0533  -0.0036 0.0154  278 GLU A CD  
1943 O OE1 . GLU A 251 ? 0.2712 0.2795 0.2569 0.0607  -0.0042 0.0198  278 GLU A OE1 
1944 O OE2 . GLU A 251 ? 0.2647 0.2609 0.2367 0.0497  -0.0047 0.0155  278 GLU A OE2 
1945 N N   . ALA A 252 ? 0.1881 0.2437 0.2042 0.0386  -0.0071 0.0061  279 ALA A N   
1946 C CA  . ALA A 252 ? 0.1995 0.2725 0.2245 0.0341  -0.0117 0.0059  279 ALA A CA  
1947 C C   . ALA A 252 ? 0.1853 0.2562 0.2099 0.0244  -0.0109 0.0016  279 ALA A C   
1948 O O   . ALA A 252 ? 0.1666 0.2449 0.1932 0.0178  -0.0154 -0.0002 279 ALA A O   
1949 C CB  . ALA A 252 ? 0.2022 0.2924 0.2416 0.0397  -0.0107 0.0093  279 ALA A CB  
1950 N N   . LEU A 253 ? 0.1912 0.2514 0.2127 0.0235  -0.0050 0.0000  280 LEU A N   
1951 C CA  . LEU A 253 ? 0.1844 0.2404 0.2048 0.0154  -0.0036 -0.0028 280 LEU A CA  
1952 C C   . LEU A 253 ? 0.1954 0.2421 0.2068 0.0109  -0.0072 -0.0052 280 LEU A C   
1953 O O   . LEU A 253 ? 0.1864 0.2342 0.1989 0.0038  -0.0089 -0.0076 280 LEU A O   
1954 C CB  . LEU A 253 ? 0.1933 0.2397 0.2098 0.0163  0.0025  -0.0029 280 LEU A CB  
1955 C CG  . LEU A 253 ? 0.2042 0.2422 0.2165 0.0097  0.0040  -0.0043 280 LEU A CG  
1956 C CD1 . LEU A 253 ? 0.2040 0.2498 0.2239 0.0027  0.0038  -0.0047 280 LEU A CD1 
1957 C CD2 . LEU A 253 ? 0.2138 0.2441 0.2210 0.0114  0.0090  -0.0038 280 LEU A CD2 
1958 N N   . LEU A 254 ? 0.1954 0.2326 0.1979 0.0150  -0.0077 -0.0046 281 LEU A N   
1959 C CA  . LEU A 254 ? 0.2133 0.2419 0.2069 0.0119  -0.0098 -0.0068 281 LEU A CA  
1960 C C   . LEU A 254 ? 0.2130 0.2504 0.2063 0.0092  -0.0156 -0.0081 281 LEU A C   
1961 O O   . LEU A 254 ? 0.2219 0.2554 0.2106 0.0034  -0.0171 -0.0119 281 LEU A O   
1962 C CB  . LEU A 254 ? 0.2164 0.2344 0.2016 0.0166  -0.0081 -0.0052 281 LEU A CB  
1963 C CG  . LEU A 254 ? 0.2229 0.2327 0.2071 0.0183  -0.0034 -0.0044 281 LEU A CG  
1964 C CD1 . LEU A 254 ? 0.2340 0.2349 0.2108 0.0214  -0.0026 -0.0029 281 LEU A CD1 
1965 C CD2 . LEU A 254 ? 0.2279 0.2332 0.2122 0.0136  -0.0011 -0.0060 281 LEU A CD2 
1966 N N   . ALA A 255 ? 0.2133 0.2624 0.2110 0.0137  -0.0189 -0.0049 282 ALA A N   
1967 C CA  . ALA A 255 ? 0.2193 0.2805 0.2172 0.0112  -0.0257 -0.0053 282 ALA A CA  
1968 C C   . ALA A 255 ? 0.2310 0.3008 0.2360 0.0023  -0.0278 -0.0090 282 ALA A C   
1969 O O   . ALA A 255 ? 0.2175 0.2880 0.2173 -0.0043 -0.0320 -0.0130 282 ALA A O   
1970 C CB  . ALA A 255 ? 0.2176 0.2920 0.2217 0.0186  -0.0287 0.0003  282 ALA A CB  
1971 N N   . GLU A 256 ? 0.2287 0.3042 0.2449 0.0015  -0.0242 -0.0080 283 GLU A N   
1972 C CA  . GLU A 256 ? 0.2359 0.3190 0.2599 -0.0077 -0.0253 -0.0108 283 GLU A CA  
1973 C C   . GLU A 256 ? 0.2246 0.2909 0.2404 -0.0149 -0.0230 -0.0157 283 GLU A C   
1974 O O   . GLU A 256 ? 0.2569 0.3247 0.2726 -0.0236 -0.0260 -0.0198 283 GLU A O   
1975 C CB  . GLU A 256 ? 0.2497 0.3416 0.2866 -0.0068 -0.0206 -0.0080 283 GLU A CB  
1976 C CG  . GLU A 256 ? 0.2640 0.3766 0.3130 -0.0009 -0.0229 -0.0036 283 GLU A CG  
1977 C CD  . GLU A 256 ? 0.2928 0.4144 0.3543 -0.0009 -0.0171 -0.0016 283 GLU A CD  
1978 O OE1 . GLU A 256 ? 0.3213 0.4447 0.3873 -0.0102 -0.0159 -0.0036 283 GLU A OE1 
1979 O OE2 . GLU A 256 ? 0.3142 0.4398 0.3801 0.0084  -0.0134 0.0019  283 GLU A OE2 
1980 N N   . ALA A 257 ? 0.2191 0.2698 0.2285 -0.0113 -0.0176 -0.0151 284 ALA A N   
1981 C CA  . ALA A 257 ? 0.2309 0.2658 0.2336 -0.0163 -0.0149 -0.0186 284 ALA A CA  
1982 C C   . ALA A 257 ? 0.2340 0.2632 0.2262 -0.0190 -0.0186 -0.0233 284 ALA A C   
1983 O O   . ALA A 257 ? 0.2419 0.2636 0.2309 -0.0262 -0.0185 -0.0280 284 ALA A O   
1984 C CB  . ALA A 257 ? 0.2235 0.2456 0.2217 -0.0112 -0.0094 -0.0163 284 ALA A CB  
1985 N N   . ALA A 258 ? 0.2206 0.2524 0.2067 -0.0132 -0.0212 -0.0218 285 ALA A N   
1986 C CA  . ALA A 258 ? 0.2241 0.2520 0.1984 -0.0150 -0.0245 -0.0257 285 ALA A CA  
1987 C C   . ALA A 258 ? 0.2426 0.2814 0.2182 -0.0231 -0.0309 -0.0297 285 ALA A C   
1988 O O   . ALA A 258 ? 0.2521 0.2828 0.2182 -0.0294 -0.0319 -0.0360 285 ALA A O   
1989 C CB  . ALA A 258 ? 0.2176 0.2469 0.1860 -0.0070 -0.0255 -0.0216 285 ALA A CB  
1990 N N   . THR A 259 ? 0.2298 0.2875 0.2175 -0.0236 -0.0349 -0.0263 286 THR A N   
1991 C CA  . THR A 259 ? 0.2494 0.3215 0.2412 -0.0323 -0.0417 -0.0294 286 THR A CA  
1992 C C   . THR A 259 ? 0.2686 0.3311 0.2614 -0.0431 -0.0393 -0.0355 286 THR A C   
1993 O O   . THR A 259 ? 0.2749 0.3370 0.2617 -0.0523 -0.0437 -0.0419 286 THR A O   
1994 C CB  . THR A 259 ? 0.2365 0.3321 0.2444 -0.0295 -0.0451 -0.0235 286 THR A CB  
1995 O OG1 . THR A 259 ? 0.2267 0.3262 0.2322 -0.0184 -0.0461 -0.0176 286 THR A OG1 
1996 C CG2 . THR A 259 ? 0.2483 0.3634 0.2627 -0.0388 -0.0533 -0.0257 286 THR A CG2 
1997 N N   . CYS A 260 ? 0.2739 0.3284 0.2736 -0.0426 -0.0326 -0.0335 287 CYS A N   
1998 C CA  . CYS A 260 ? 0.2930 0.3352 0.2931 -0.0521 -0.0293 -0.0380 287 CYS A CA  
1999 C C   . CYS A 260 ? 0.3016 0.3225 0.2857 -0.0544 -0.0276 -0.0448 287 CYS A C   
2000 O O   . CYS A 260 ? 0.2872 0.3013 0.2673 -0.0644 -0.0289 -0.0515 287 CYS A O   
2001 C CB  . CYS A 260 ? 0.3085 0.3437 0.3158 -0.0496 -0.0219 -0.0335 287 CYS A CB  
2002 S SG  . CYS A 260 ? 0.3435 0.4016 0.3688 -0.0471 -0.0214 -0.0264 287 CYS A SG  
2003 N N   . VAL A 261 ? 0.2912 0.3011 0.2666 -0.0453 -0.0240 -0.0432 288 VAL A N   
2004 C CA  . VAL A 261 ? 0.3120 0.3034 0.2728 -0.0454 -0.0213 -0.0490 288 VAL A CA  
2005 C C   . VAL A 261 ? 0.3170 0.3128 0.2671 -0.0511 -0.0276 -0.0556 288 VAL A C   
2006 O O   . VAL A 261 ? 0.3153 0.2983 0.2565 -0.0586 -0.0268 -0.0636 288 VAL A O   
2007 C CB  . VAL A 261 ? 0.2942 0.2789 0.2501 -0.0344 -0.0169 -0.0448 288 VAL A CB  
2008 C CG1 . VAL A 261 ? 0.3094 0.2799 0.2503 -0.0329 -0.0143 -0.0501 288 VAL A CG1 
2009 C CG2 . VAL A 261 ? 0.2825 0.2608 0.2465 -0.0303 -0.0109 -0.0395 288 VAL A CG2 
2010 N N   . ALA A 262 ? 0.2971 0.3102 0.2468 -0.0476 -0.0338 -0.0523 289 ALA A N   
2011 C CA  . ALA A 262 ? 0.3197 0.3394 0.2581 -0.0525 -0.0407 -0.0574 289 ALA A CA  
2012 C C   . ALA A 262 ? 0.3450 0.3690 0.2857 -0.0663 -0.0455 -0.0643 289 ALA A C   
2013 O O   . ALA A 262 ? 0.3442 0.3617 0.2711 -0.0737 -0.0482 -0.0728 289 ALA A O   
2014 C CB  . ALA A 262 ? 0.3057 0.3457 0.2468 -0.0459 -0.0469 -0.0503 289 ALA A CB  
2015 N N   . GLY A 263 ? 0.3479 0.3833 0.3060 -0.0703 -0.0464 -0.0609 290 GLY A N   
2016 C CA  . GLY A 263 ? 0.3722 0.4123 0.3352 -0.0845 -0.0503 -0.0666 290 GLY A CA  
2017 C C   . GLY A 263 ? 0.3934 0.4065 0.3460 -0.0923 -0.0446 -0.0756 290 GLY A C   
2018 O O   . GLY A 263 ? 0.4000 0.4108 0.3466 -0.1048 -0.0486 -0.0841 290 GLY A O   
2019 N N   . VAL A 264 ? 0.3863 0.3791 0.3368 -0.0849 -0.0353 -0.0737 291 VAL A N   
2020 C CA  . VAL A 264 ? 0.4260 0.3914 0.3679 -0.0894 -0.0284 -0.0805 291 VAL A CA  
2021 C C   . VAL A 264 ? 0.4430 0.3947 0.3645 -0.0886 -0.0279 -0.0889 291 VAL A C   
2022 O O   . VAL A 264 ? 0.4447 0.3786 0.3558 -0.0971 -0.0259 -0.0985 291 VAL A O   
2023 C CB  . VAL A 264 ? 0.4486 0.4014 0.3971 -0.0800 -0.0193 -0.0735 291 VAL A CB  
2024 C CG1 . VAL A 264 ? 0.4994 0.4229 0.4379 -0.0794 -0.0111 -0.0786 291 VAL A CG1 
2025 C CG2 . VAL A 264 ? 0.4577 0.4201 0.4235 -0.0835 -0.0187 -0.0671 291 VAL A CG2 
2026 N N   . LEU A 265 ? 0.4263 0.3852 0.3413 -0.0784 -0.0289 -0.0853 292 LEU A N   
2027 C CA  . LEU A 265 ? 0.4706 0.4170 0.3658 -0.0763 -0.0269 -0.0921 292 LEU A CA  
2028 C C   . LEU A 265 ? 0.5002 0.4583 0.3834 -0.0853 -0.0363 -0.0990 292 LEU A C   
2029 O O   . LEU A 265 ? 0.5504 0.4964 0.4145 -0.0867 -0.0347 -0.1072 292 LEU A O   
2030 C CB  . LEU A 265 ? 0.4533 0.4009 0.3465 -0.0622 -0.0229 -0.0849 292 LEU A CB  
2031 C CG  . LEU A 265 ? 0.4582 0.3963 0.3621 -0.0534 -0.0147 -0.0780 292 LEU A CG  
2032 C CD1 . LEU A 265 ? 0.4456 0.3879 0.3464 -0.0420 -0.0125 -0.0719 292 LEU A CD1 
2033 C CD2 . LEU A 265 ? 0.4825 0.3957 0.3831 -0.0547 -0.0061 -0.0831 292 LEU A CD2 
2034 N N   A ALA A 266 ? 0.4987 0.4808 0.3927 -0.0914 -0.0457 -0.0959 293 ALA A N   
2035 N N   B ALA A 266 ? 0.4995 0.4819 0.3935 -0.0910 -0.0458 -0.0957 293 ALA A N   
2036 C CA  A ALA A 266 ? 0.5213 0.5188 0.4053 -0.0997 -0.0561 -0.1009 293 ALA A CA  
2037 C CA  B ALA A 266 ? 0.5240 0.5215 0.4080 -0.0996 -0.0561 -0.1009 293 ALA A CA  
2038 C C   A ALA A 266 ? 0.5504 0.5316 0.4205 -0.1142 -0.0565 -0.1150 293 ALA A C   
2039 C C   B ALA A 266 ? 0.5566 0.5354 0.4248 -0.1129 -0.0554 -0.1152 293 ALA A C   
2040 O O   A ALA A 266 ? 0.5521 0.5133 0.4262 -0.1188 -0.0494 -0.1191 293 ALA A O   
2041 O O   B ALA A 266 ? 0.5688 0.5427 0.4161 -0.1134 -0.0569 -0.1217 293 ALA A O   
2042 C CB  A ALA A 266 ? 0.5196 0.5474 0.4216 -0.1029 -0.0657 -0.0939 293 ALA A CB  
2043 C CB  B ALA A 266 ? 0.5233 0.5498 0.4252 -0.1046 -0.0656 -0.0950 293 ALA A CB  
2044 O OXT A ALA A 266 ? 0.5670 0.5560 0.4220 -0.1206 -0.0640 -0.1212 293 ALA A OXT 
2045 N N   . ASP B 2   ? 0.6069 0.5736 0.5128 0.0748  0.1065  -0.0575 28  ASP B N   
2046 C CA  . ASP B 2   ? 0.6234 0.5706 0.5191 0.0707  0.1015  -0.0584 28  ASP B CA  
2047 C C   . ASP B 2   ? 0.5814 0.5344 0.4731 0.0615  0.0919  -0.0526 28  ASP B C   
2048 O O   . ASP B 2   ? 0.5430 0.5123 0.4386 0.0579  0.0899  -0.0487 28  ASP B O   
2049 C CB  . ASP B 2   ? 0.6890 0.6194 0.5708 0.0676  0.1069  -0.0690 28  ASP B CB  
2050 C CG  . ASP B 2   ? 0.7676 0.7012 0.6341 0.0574  0.1057  -0.0740 28  ASP B CG  
2051 O OD1 . ASP B 2   ? 0.7924 0.7416 0.6585 0.0533  0.1033  -0.0693 28  ASP B OD1 
2052 O OD2 . ASP B 2   ? 0.8773 0.7978 0.7321 0.0535  0.1072  -0.0826 28  ASP B OD2 
2053 N N   . LEU B 3   ? 0.5743 0.5126 0.4589 0.0578  0.0870  -0.0524 29  LEU B N   
2054 C CA  . LEU B 3   ? 0.5635 0.5049 0.4468 0.0516  0.0780  -0.0461 29  LEU B CA  
2055 C C   . LEU B 3   ? 0.5183 0.4679 0.3930 0.0426  0.0760  -0.0470 29  LEU B C   
2056 O O   . LEU B 3   ? 0.4767 0.4373 0.3554 0.0392  0.0714  -0.0411 29  LEU B O   
2057 C CB  . LEU B 3   ? 0.6058 0.5288 0.4834 0.0500  0.0753  -0.0469 29  LEU B CB  
2058 C CG  . LEU B 3   ? 0.6329 0.5569 0.5122 0.0473  0.0669  -0.0392 29  LEU B CG  
2059 C CD1 . LEU B 3   ? 0.6292 0.5652 0.5210 0.0544  0.0643  -0.0316 29  LEU B CD1 
2060 C CD2 . LEU B 3   ? 0.6628 0.5675 0.5371 0.0462  0.0667  -0.0406 29  LEU B CD2 
2061 N N   . ALA B 4   ? 0.5197 0.4632 0.3821 0.0390  0.0795  -0.0544 30  ALA B N   
2062 C CA  . ALA B 4   ? 0.5212 0.4717 0.3730 0.0320  0.0782  -0.0547 30  ALA B CA  
2063 C C   . ALA B 4   ? 0.4972 0.4638 0.3551 0.0326  0.0817  -0.0504 30  ALA B C   
2064 O O   . ALA B 4   ? 0.4938 0.4675 0.3503 0.0275  0.0785  -0.0450 30  ALA B O   
2065 C CB  . ALA B 4   ? 0.5409 0.4847 0.3788 0.0299  0.0822  -0.0643 30  ALA B CB  
2066 N N   . ASP B 5   ? 0.4990 0.4713 0.3651 0.0389  0.0889  -0.0526 31  ASP B N   
2067 C CA  . ASP B 5   ? 0.5139 0.5026 0.3879 0.0392  0.0934  -0.0492 31  ASP B CA  
2068 C C   . ASP B 5   ? 0.4920 0.4912 0.3802 0.0380  0.0879  -0.0415 31  ASP B C   
2069 O O   . ASP B 5   ? 0.4591 0.4690 0.3501 0.0330  0.0885  -0.0375 31  ASP B O   
2070 C CB  . ASP B 5   ? 0.5472 0.5406 0.4283 0.0469  0.1026  -0.0538 31  ASP B CB  
2071 C CG  . ASP B 5   ? 0.5968 0.5910 0.4653 0.0458  0.1109  -0.0601 31  ASP B CG  
2072 O OD1 . ASP B 5   ? 0.6226 0.6078 0.4742 0.0411  0.1089  -0.0639 31  ASP B OD1 
2073 O OD2 . ASP B 5   ? 0.6185 0.6236 0.4945 0.0499  0.1190  -0.0612 31  ASP B OD2 
2074 N N   . ARG B 6   ? 0.4899 0.4856 0.3866 0.0425  0.0829  -0.0395 32  ARG B N   
2075 C CA  . ARG B 6   ? 0.4810 0.4873 0.3897 0.0414  0.0767  -0.0334 32  ARG B CA  
2076 C C   . ARG B 6   ? 0.4607 0.4639 0.3618 0.0323  0.0706  -0.0301 32  ARG B C   
2077 O O   . ARG B 6   ? 0.4470 0.4613 0.3555 0.0278  0.0689  -0.0266 32  ARG B O   
2078 C CB  . ARG B 6   ? 0.5130 0.5158 0.4295 0.0490  0.0725  -0.0313 32  ARG B CB  
2079 C CG  . ARG B 6   ? 0.5594 0.5683 0.4868 0.0594  0.0787  -0.0331 32  ARG B CG  
2080 C CD  . ARG B 6   ? 0.6258 0.6239 0.5557 0.0689  0.0773  -0.0316 32  ARG B CD  
2081 N NE  . ARG B 6   ? 0.7006 0.7030 0.6358 0.0699  0.0686  -0.0250 32  ARG B NE  
2082 C CZ  . ARG B 6   ? 0.7508 0.7426 0.6858 0.0773  0.0663  -0.0215 32  ARG B CZ  
2083 N NH1 . ARG B 6   ? 0.7790 0.7530 0.7094 0.0833  0.0723  -0.0242 32  ARG B NH1 
2084 N NH2 . ARG B 6   ? 0.7836 0.7819 0.7224 0.0786  0.0585  -0.0154 32  ARG B NH2 
2085 N N   . PHE B 7   ? 0.4272 0.4155 0.3146 0.0295  0.0676  -0.0316 33  PHE B N   
2086 C CA  . PHE B 7   ? 0.4106 0.3953 0.2903 0.0221  0.0622  -0.0286 33  PHE B CA  
2087 C C   . PHE B 7   ? 0.4049 0.3962 0.2798 0.0171  0.0664  -0.0272 33  PHE B C   
2088 O O   . PHE B 7   ? 0.3781 0.3722 0.2540 0.0118  0.0639  -0.0228 33  PHE B O   
2089 C CB  . PHE B 7   ? 0.4101 0.3802 0.2773 0.0206  0.0590  -0.0315 33  PHE B CB  
2090 C CG  . PHE B 7   ? 0.4129 0.3740 0.2833 0.0236  0.0546  -0.0310 33  PHE B CG  
2091 C CD1 . PHE B 7   ? 0.4100 0.3760 0.2899 0.0251  0.0500  -0.0260 33  PHE B CD1 
2092 C CD2 . PHE B 7   ? 0.4333 0.3809 0.2965 0.0245  0.0555  -0.0359 33  PHE B CD2 
2093 C CE1 . PHE B 7   ? 0.4130 0.3703 0.2938 0.0282  0.0466  -0.0245 33  PHE B CE1 
2094 C CE2 . PHE B 7   ? 0.4341 0.3719 0.2999 0.0269  0.0528  -0.0346 33  PHE B CE2 
2095 C CZ  . PHE B 7   ? 0.4193 0.3618 0.2932 0.0293  0.0485  -0.0282 33  PHE B CZ  
2096 N N   . ALA B 8   ? 0.4242 0.4168 0.2931 0.0189  0.0736  -0.0309 34  ALA B N   
2097 C CA  . ALA B 8   ? 0.4291 0.4275 0.2919 0.0150  0.0788  -0.0286 34  ALA B CA  
2098 C C   . ALA B 8   ? 0.4131 0.4246 0.2910 0.0130  0.0821  -0.0245 34  ALA B C   
2099 O O   . ALA B 8   ? 0.4088 0.4229 0.2846 0.0077  0.0845  -0.0201 34  ALA B O   
2100 C CB  . ALA B 8   ? 0.4488 0.4470 0.3015 0.0179  0.0863  -0.0340 34  ALA B CB  
2101 N N   . GLU B 9   ? 0.4091 0.4294 0.3025 0.0174  0.0830  -0.0261 35  GLU B N   
2102 C CA  . GLU B 9   ? 0.4105 0.4463 0.3206 0.0151  0.0855  -0.0237 35  GLU B CA  
2103 C C   . GLU B 9   ? 0.4006 0.4363 0.3157 0.0091  0.0783  -0.0199 35  GLU B C   
2104 O O   . GLU B 9   ? 0.3809 0.4243 0.3032 0.0030  0.0811  -0.0175 35  GLU B O   
2105 C CB  . GLU B 9   ? 0.4255 0.4730 0.3514 0.0225  0.0873  -0.0265 35  GLU B CB  
2106 C CG  . GLU B 9   ? 0.4291 0.4967 0.3738 0.0197  0.0909  -0.0253 35  GLU B CG  
2107 C CD  . GLU B 9   ? 0.4227 0.4977 0.3794 0.0160  0.0826  -0.0232 35  GLU B CD  
2108 O OE1 . GLU B 9   ? 0.4119 0.4780 0.3639 0.0185  0.0741  -0.0226 35  GLU B OE1 
2109 O OE2 . GLU B 9   ? 0.4127 0.5017 0.3824 0.0098  0.0851  -0.0227 35  GLU B OE2 
2110 N N   . LEU B 10  ? 0.4143 0.4409 0.3255 0.0106  0.0699  -0.0198 36  LEU B N   
2111 C CA  . LEU B 10  ? 0.4126 0.4374 0.3258 0.0052  0.0632  -0.0170 36  LEU B CA  
2112 C C   . LEU B 10  ? 0.4023 0.4203 0.3058 -0.0016 0.0659  -0.0137 36  LEU B C   
2113 O O   . LEU B 10  ? 0.4024 0.4240 0.3125 -0.0077 0.0663  -0.0115 36  LEU B O   
2114 C CB  . LEU B 10  ? 0.4337 0.4477 0.3408 0.0079  0.0552  -0.0171 36  LEU B CB  
2115 C CG  . LEU B 10  ? 0.4382 0.4550 0.3524 0.0157  0.0520  -0.0184 36  LEU B CG  
2116 C CD1 . LEU B 10  ? 0.4428 0.4486 0.3506 0.0161  0.0446  -0.0171 36  LEU B CD1 
2117 C CD2 . LEU B 10  ? 0.4435 0.4784 0.3748 0.0176  0.0515  -0.0183 36  LEU B CD2 
2118 N N   . GLU B 11  ? 0.4121 0.4205 0.2998 -0.0004 0.0679  -0.0136 37  GLU B N   
2119 C CA  . GLU B 11  ? 0.4067 0.4084 0.2830 -0.0048 0.0700  -0.0094 37  GLU B CA  
2120 C C   . GLU B 11  ? 0.4067 0.4161 0.2887 -0.0088 0.0788  -0.0063 37  GLU B C   
2121 O O   . GLU B 11  ? 0.4156 0.4218 0.2982 -0.0142 0.0801  -0.0017 37  GLU B O   
2122 C CB  . GLU B 11  ? 0.4134 0.4075 0.2718 -0.0020 0.0706  -0.0105 37  GLU B CB  
2123 C CG  . GLU B 11  ? 0.3954 0.3807 0.2476 0.0000  0.0625  -0.0133 37  GLU B CG  
2124 C CD  . GLU B 11  ? 0.4067 0.3868 0.2425 0.0015  0.0624  -0.0157 37  GLU B CD  
2125 O OE1 . GLU B 11  ? 0.4127 0.3958 0.2430 0.0040  0.0681  -0.0193 37  GLU B OE1 
2126 O OE2 . GLU B 11  ? 0.3969 0.3709 0.2257 0.0002  0.0566  -0.0147 37  GLU B OE2 
2127 N N   . ARG B 12  ? 0.4065 0.4251 0.2930 -0.0062 0.0857  -0.0088 38  ARG B N   
2128 C CA  . ARG B 12  ? 0.4281 0.4548 0.3208 -0.0102 0.0954  -0.0060 38  ARG B CA  
2129 C C   . ARG B 12  ? 0.3915 0.4266 0.3035 -0.0162 0.0946  -0.0056 38  ARG B C   
2130 O O   . ARG B 12  ? 0.3789 0.4126 0.2931 -0.0229 0.0999  -0.0015 38  ARG B O   
2131 C CB  . ARG B 12  ? 0.4520 0.4890 0.3478 -0.0060 0.1036  -0.0094 38  ARG B CB  
2132 C CG  . ARG B 12  ? 0.4936 0.5237 0.3696 -0.0013 0.1065  -0.0110 38  ARG B CG  
2133 C CD  . ARG B 12  ? 0.5290 0.5700 0.4087 0.0017  0.1170  -0.0139 38  ARG B CD  
2134 N NE  . ARG B 12  ? 0.5245 0.5756 0.4216 0.0066  0.1162  -0.0194 38  ARG B NE  
2135 C CZ  . ARG B 12  ? 0.5386 0.5856 0.4333 0.0136  0.1127  -0.0250 38  ARG B CZ  
2136 N NH1 . ARG B 12  ? 0.5520 0.5856 0.4293 0.0153  0.1086  -0.0271 38  ARG B NH1 
2137 N NH2 . ARG B 12  ? 0.5494 0.6060 0.4601 0.0192  0.1135  -0.0286 38  ARG B NH2 
2138 N N   . ARG B 13  ? 0.3662 0.4098 0.2916 -0.0139 0.0883  -0.0099 39  ARG B N   
2139 C CA  . ARG B 13  ? 0.3585 0.4142 0.3031 -0.0196 0.0872  -0.0112 39  ARG B CA  
2140 C C   . ARG B 13  ? 0.3532 0.3989 0.2954 -0.0264 0.0829  -0.0089 39  ARG B C   
2141 O O   . ARG B 13  ? 0.3561 0.4062 0.3091 -0.0344 0.0869  -0.0087 39  ARG B O   
2142 C CB  . ARG B 13  ? 0.3528 0.4212 0.3102 -0.0138 0.0805  -0.0157 39  ARG B CB  
2143 C CG  . ARG B 13  ? 0.3418 0.4251 0.3180 -0.0191 0.0767  -0.0183 39  ARG B CG  
2144 C CD  . ARG B 13  ? 0.3460 0.4486 0.3373 -0.0121 0.0743  -0.0219 39  ARG B CD  
2145 N NE  . ARG B 13  ? 0.3528 0.4473 0.3342 -0.0015 0.0696  -0.0215 39  ARG B NE  
2146 C CZ  . ARG B 13  ? 0.3725 0.4575 0.3463 0.0016  0.0606  -0.0208 39  ARG B CZ  
2147 N NH1 . ARG B 13  ? 0.3677 0.4554 0.3455 -0.0035 0.0540  -0.0212 39  ARG B NH1 
2148 N NH2 . ARG B 13  ? 0.3788 0.4523 0.3419 0.0097  0.0588  -0.0201 39  ARG B NH2 
2149 N N   . TYR B 14  ? 0.3395 0.3717 0.2685 -0.0235 0.0755  -0.0078 40  TYR B N   
2150 C CA  . TYR B 14  ? 0.3497 0.3722 0.2763 -0.0287 0.0714  -0.0061 40  TYR B CA  
2151 C C   . TYR B 14  ? 0.3559 0.3641 0.2688 -0.0311 0.0767  0.0000  40  TYR B C   
2152 O O   . TYR B 14  ? 0.3608 0.3592 0.2711 -0.0348 0.0748  0.0023  40  TYR B O   
2153 C CB  . TYR B 14  ? 0.3517 0.3680 0.2719 -0.0241 0.0613  -0.0076 40  TYR B CB  
2154 C CG  . TYR B 14  ? 0.3421 0.3707 0.2752 -0.0225 0.0548  -0.0120 40  TYR B CG  
2155 C CD1 . TYR B 14  ? 0.3361 0.3698 0.2790 -0.0283 0.0513  -0.0143 40  TYR B CD1 
2156 C CD2 . TYR B 14  ? 0.3311 0.3655 0.2655 -0.0146 0.0520  -0.0139 40  TYR B CD2 
2157 C CE1 . TYR B 14  ? 0.3275 0.3741 0.2802 -0.0261 0.0444  -0.0182 40  TYR B CE1 
2158 C CE2 . TYR B 14  ? 0.3248 0.3706 0.2695 -0.0116 0.0458  -0.0164 40  TYR B CE2 
2159 C CZ  . TYR B 14  ? 0.3321 0.3853 0.2856 -0.0172 0.0416  -0.0185 40  TYR B CZ  
2160 O OH  . TYR B 14  ? 0.3429 0.4093 0.3051 -0.0136 0.0348  -0.0208 40  TYR B OH  
2161 N N   . ASP B 15  ? 0.3613 0.3688 0.2650 -0.0283 0.0835  0.0028  41  ASP B N   
2162 C CA  . ASP B 15  ? 0.3810 0.3763 0.2685 -0.0282 0.0877  0.0094  41  ASP B CA  
2163 C C   . ASP B 15  ? 0.3795 0.3634 0.2553 -0.0252 0.0789  0.0105  41  ASP B C   
2164 O O   . ASP B 15  ? 0.4037 0.3779 0.2762 -0.0278 0.0788  0.0149  41  ASP B O   
2165 C CB  . ASP B 15  ? 0.3803 0.3722 0.2733 -0.0354 0.0964  0.0144  41  ASP B CB  
2166 C CG  . ASP B 15  ? 0.4053 0.3854 0.2807 -0.0337 0.1022  0.0231  41  ASP B CG  
2167 O OD1 . ASP B 15  ? 0.4081 0.3895 0.2693 -0.0278 0.1026  0.0241  41  ASP B OD1 
2168 O OD2 . ASP B 15  ? 0.4125 0.3826 0.2886 -0.0381 0.1063  0.0285  41  ASP B OD2 
2169 N N   . ALA B 16  ? 0.3794 0.3643 0.2495 -0.0197 0.0725  0.0064  42  ALA B N   
2170 C CA  . ALA B 16  ? 0.3733 0.3501 0.2363 -0.0175 0.0639  0.0058  42  ALA B CA  
2171 C C   . ALA B 16  ? 0.3849 0.3599 0.2341 -0.0122 0.0617  0.0039  42  ALA B C   
2172 O O   . ALA B 16  ? 0.3850 0.3653 0.2318 -0.0098 0.0661  0.0015  42  ALA B O   
2173 C CB  . ALA B 16  ? 0.3627 0.3436 0.2376 -0.0178 0.0575  0.0010  42  ALA B CB  
2174 N N   . ARG B 17  ? 0.3709 0.3391 0.2119 -0.0108 0.0553  0.0043  43  ARG B N   
2175 C CA  . ARG B 17  ? 0.3836 0.3508 0.2149 -0.0071 0.0515  0.0000  43  ARG B CA  
2176 C C   . ARG B 17  ? 0.3767 0.3418 0.2154 -0.0067 0.0450  -0.0043 43  ARG B C   
2177 O O   . ARG B 17  ? 0.3763 0.3380 0.2193 -0.0086 0.0410  -0.0024 43  ARG B O   
2178 C CB  . ARG B 17  ? 0.3862 0.3498 0.2037 -0.0059 0.0492  0.0036  43  ARG B CB  
2179 C CG  . ARG B 17  ? 0.3923 0.3570 0.1997 -0.0032 0.0457  -0.0022 43  ARG B CG  
2180 C CD  . ARG B 17  ? 0.4078 0.3730 0.2020 -0.0016 0.0430  0.0013  43  ARG B CD  
2181 N NE  . ARG B 17  ? 0.4042 0.3651 0.2016 -0.0023 0.0380  0.0053  43  ARG B NE  
2182 C CZ  . ARG B 17  ? 0.3926 0.3537 0.1872 -0.0016 0.0315  0.0033  43  ARG B CZ  
2183 N NH1 . ARG B 17  ? 0.4042 0.3696 0.1924 -0.0009 0.0284  -0.0034 43  ARG B NH1 
2184 N NH2 . ARG B 17  ? 0.4070 0.3643 0.2062 -0.0019 0.0285  0.0073  43  ARG B NH2 
2185 N N   . LEU B 18  ? 0.3896 0.3556 0.2287 -0.0038 0.0446  -0.0099 44  LEU B N   
2186 C CA  . LEU B 18  ? 0.3792 0.3422 0.2245 -0.0026 0.0399  -0.0130 44  LEU B CA  
2187 C C   . LEU B 18  ? 0.3855 0.3429 0.2225 -0.0011 0.0376  -0.0177 44  LEU B C   
2188 O O   . LEU B 18  ? 0.4003 0.3586 0.2302 0.0003  0.0409  -0.0215 44  LEU B O   
2189 C CB  . LEU B 18  ? 0.3905 0.3592 0.2468 0.0001  0.0426  -0.0149 44  LEU B CB  
2190 C CG  . LEU B 18  ? 0.3814 0.3464 0.2425 0.0034  0.0390  -0.0172 44  LEU B CG  
2191 C CD1 . LEU B 18  ? 0.3769 0.3409 0.2423 0.0012  0.0334  -0.0143 44  LEU B CD1 
2192 C CD2 . LEU B 18  ? 0.3850 0.3567 0.2556 0.0080  0.0425  -0.0187 44  LEU B CD2 
2193 N N   . GLY B 19  ? 0.3705 0.3227 0.2087 -0.0019 0.0325  -0.0181 45  GLY B N   
2194 C CA  . GLY B 19  ? 0.3805 0.3270 0.2135 -0.0019 0.0305  -0.0232 45  GLY B CA  
2195 C C   . GLY B 19  ? 0.3709 0.3115 0.2109 -0.0004 0.0291  -0.0242 45  GLY B C   
2196 O O   . GLY B 19  ? 0.3494 0.2900 0.1948 -0.0008 0.0262  -0.0203 45  GLY B O   
2197 N N   . VAL B 20  ? 0.3758 0.3106 0.2148 0.0014  0.0316  -0.0295 46  VAL B N   
2198 C CA  . VAL B 20  ? 0.3755 0.3027 0.2202 0.0039  0.0318  -0.0296 46  VAL B CA  
2199 C C   . VAL B 20  ? 0.3811 0.2986 0.2217 0.0019  0.0328  -0.0358 46  VAL B C   
2200 O O   . VAL B 20  ? 0.3882 0.3049 0.2235 0.0011  0.0357  -0.0422 46  VAL B O   
2201 C CB  . VAL B 20  ? 0.3964 0.3251 0.2475 0.0097  0.0360  -0.0292 46  VAL B CB  
2202 C CG1 . VAL B 20  ? 0.4047 0.3251 0.2608 0.0138  0.0362  -0.0275 46  VAL B CG1 
2203 C CG2 . VAL B 20  ? 0.3845 0.3253 0.2415 0.0105  0.0354  -0.0245 46  VAL B CG2 
2204 N N   . TYR B 21  ? 0.3788 0.2891 0.2216 0.0007  0.0309  -0.0343 47  TYR B N   
2205 C CA  . TYR B 21  ? 0.3831 0.2823 0.2248 -0.0013 0.0335  -0.0401 47  TYR B CA  
2206 C C   . TYR B 21  ? 0.3846 0.2738 0.2314 0.0017  0.0350  -0.0356 47  TYR B C   
2207 O O   . TYR B 21  ? 0.3725 0.2641 0.2212 0.0018  0.0315  -0.0294 47  TYR B O   
2208 C CB  . TYR B 21  ? 0.3861 0.2871 0.2240 -0.0080 0.0302  -0.0440 47  TYR B CB  
2209 C CG  . TYR B 21  ? 0.4091 0.3006 0.2462 -0.0117 0.0338  -0.0529 47  TYR B CG  
2210 C CD1 . TYR B 21  ? 0.4346 0.3260 0.2673 -0.0122 0.0370  -0.0614 47  TYR B CD1 
2211 C CD2 . TYR B 21  ? 0.4120 0.2942 0.2528 -0.0150 0.0347  -0.0535 47  TYR B CD2 
2212 C CE1 . TYR B 21  ? 0.4418 0.3243 0.2741 -0.0167 0.0406  -0.0713 47  TYR B CE1 
2213 C CE2 . TYR B 21  ? 0.4291 0.3015 0.2705 -0.0195 0.0390  -0.0623 47  TYR B CE2 
2214 C CZ  . TYR B 21  ? 0.4513 0.3238 0.2888 -0.0206 0.0418  -0.0718 47  TYR B CZ  
2215 O OH  . TYR B 21  ? 0.4896 0.3518 0.3283 -0.0261 0.0464  -0.0820 47  TYR B OH  
2216 N N   . VAL B 22  ? 0.3941 0.2714 0.2421 0.0043  0.0407  -0.0390 48  VAL B N   
2217 C CA  . VAL B 22  ? 0.4148 0.2790 0.2660 0.0070  0.0438  -0.0352 48  VAL B CA  
2218 C C   . VAL B 22  ? 0.4315 0.2815 0.2816 0.0023  0.0492  -0.0435 48  VAL B C   
2219 O O   . VAL B 22  ? 0.4262 0.2716 0.2755 0.0033  0.0538  -0.0504 48  VAL B O   
2220 C CB  . VAL B 22  ? 0.4274 0.2892 0.2828 0.0168  0.0469  -0.0297 48  VAL B CB  
2221 C CG1 . VAL B 22  ? 0.4379 0.2857 0.2950 0.0208  0.0501  -0.0237 48  VAL B CG1 
2222 C CG2 . VAL B 22  ? 0.4148 0.2931 0.2728 0.0204  0.0418  -0.0238 48  VAL B CG2 
2223 N N   . PRO B 23  ? 0.4267 0.2703 0.2773 -0.0037 0.0491  -0.0441 49  PRO B N   
2224 C CA  . PRO B 23  ? 0.4398 0.2699 0.2911 -0.0097 0.0548  -0.0528 49  PRO B CA  
2225 C C   . PRO B 23  ? 0.4595 0.2711 0.3132 -0.0037 0.0635  -0.0524 49  PRO B C   
2226 O O   . PRO B 23  ? 0.4565 0.2643 0.3119 0.0050  0.0648  -0.0428 49  PRO B O   
2227 C CB  . PRO B 23  ? 0.4431 0.2712 0.2963 -0.0159 0.0534  -0.0504 49  PRO B CB  
2228 C CG  . PRO B 23  ? 0.4263 0.2710 0.2780 -0.0147 0.0454  -0.0436 49  PRO B CG  
2229 C CD  . PRO B 23  ? 0.4163 0.2660 0.2671 -0.0058 0.0441  -0.0374 49  PRO B CD  
2230 N N   . ALA B 24  ? 0.4751 0.2758 0.3290 -0.0083 0.0695  -0.0634 50  ALA B N   
2231 C CA  . ALA B 24  ? 0.4968 0.2759 0.3536 -0.0037 0.0794  -0.0643 50  ALA B CA  
2232 C C   . ALA B 24  ? 0.5127 0.2767 0.3723 -0.0027 0.0834  -0.0552 50  ALA B C   
2233 O O   . ALA B 24  ? 0.4886 0.2559 0.3487 -0.0100 0.0805  -0.0541 50  ALA B O   
2234 C CB  . ALA B 24  ? 0.5075 0.2776 0.3639 -0.0112 0.0850  -0.0796 50  ALA B CB  
2235 N N   . THR B 25  ? 0.5405 0.2891 0.4020 0.0072  0.0901  -0.0479 51  THR B N   
2236 C CA  . THR B 25  ? 0.5650 0.2967 0.4277 0.0102  0.0956  -0.0379 51  THR B CA  
2237 C C   . THR B 25  ? 0.5928 0.2980 0.4584 0.0131  0.1081  -0.0416 51  THR B C   
2238 O O   . THR B 25  ? 0.5904 0.2927 0.4568 0.0116  0.1114  -0.0531 51  THR B O   
2239 C CB  . THR B 25  ? 0.5484 0.2889 0.4094 0.0219  0.0909  -0.0226 51  THR B CB  
2240 O OG1 . THR B 25  ? 0.5684 0.3063 0.4313 0.0335  0.0941  -0.0206 51  THR B OG1 
2241 C CG2 . THR B 25  ? 0.5346 0.3010 0.3934 0.0199  0.0793  -0.0206 51  THR B CG2 
2242 N N   . GLY B 26  ? 0.6080 0.2935 0.4744 0.0177  0.1155  -0.0314 52  GLY B N   
2243 C CA  . GLY B 26  ? 0.6489 0.3060 0.5182 0.0220  0.1287  -0.0326 52  GLY B CA  
2244 C C   . GLY B 26  ? 0.6797 0.3354 0.5498 0.0370  0.1309  -0.0288 52  GLY B C   
2245 O O   . GLY B 26  ? 0.7432 0.3750 0.6161 0.0417  0.1423  -0.0309 52  GLY B O   
2246 N N   . THR B 27  ? 0.7017 0.3819 0.5706 0.0447  0.1211  -0.0233 53  THR B N   
2247 C CA  . THR B 27  ? 0.7334 0.4156 0.6050 0.0591  0.1230  -0.0197 53  THR B CA  
2248 C C   . THR B 27  ? 0.7170 0.4234 0.5889 0.0575  0.1156  -0.0284 53  THR B C   
2249 O O   . THR B 27  ? 0.7387 0.4469 0.6140 0.0673  0.1186  -0.0291 53  THR B O   
2250 C CB  . THR B 27  ? 0.7852 0.4733 0.6564 0.0732  0.1197  -0.0016 53  THR B CB  
2251 O OG1 . THR B 27  ? 0.7964 0.5107 0.6647 0.0693  0.1072  0.0021  53  THR B OG1 
2252 C CG2 . THR B 27  ? 0.8206 0.4843 0.6897 0.0763  0.1277  0.0090  53  THR B CG2 
2253 N N   . THR B 28  ? 0.6655 0.3902 0.5342 0.0461  0.1067  -0.0342 54  THR B N   
2254 C CA  . THR B 28  ? 0.6238 0.3718 0.4918 0.0452  0.0999  -0.0399 54  THR B CA  
2255 C C   . THR B 28  ? 0.5885 0.3411 0.4525 0.0310  0.0978  -0.0541 54  THR B C   
2256 O O   . THR B 28  ? 0.5659 0.3159 0.4282 0.0210  0.0958  -0.0563 54  THR B O   
2257 C CB  . THR B 28  ? 0.6245 0.3957 0.4924 0.0488  0.0894  -0.0293 54  THR B CB  
2258 O OG1 . THR B 28  ? 0.6120 0.3855 0.4765 0.0400  0.0842  -0.0270 54  THR B OG1 
2259 C CG2 . THR B 28  ? 0.6420 0.4138 0.5140 0.0636  0.0902  -0.0166 54  THR B CG2 
2260 N N   . ALA B 29  ? 0.5482 0.3100 0.4108 0.0309  0.0980  -0.0633 55  ALA B N   
2261 C CA  . ALA B 29  ? 0.5323 0.3050 0.3895 0.0195  0.0940  -0.0752 55  ALA B CA  
2262 C C   . ALA B 29  ? 0.5004 0.2960 0.3550 0.0165  0.0829  -0.0690 55  ALA B C   
2263 O O   . ALA B 29  ? 0.4884 0.2940 0.3455 0.0236  0.0788  -0.0580 55  ALA B O   
2264 C CB  . ALA B 29  ? 0.5385 0.3142 0.3932 0.0212  0.0983  -0.0860 55  ALA B CB  
2265 N N   . ALA B 30  ? 0.4866 0.2911 0.3365 0.0060  0.0781  -0.0766 56  ALA B N   
2266 C CA  . ALA B 30  ? 0.4737 0.2988 0.3207 0.0034  0.0686  -0.0717 56  ALA B CA  
2267 C C   . ALA B 30  ? 0.4696 0.3088 0.3160 0.0103  0.0671  -0.0682 56  ALA B C   
2268 O O   . ALA B 30  ? 0.4675 0.3053 0.3126 0.0134  0.0722  -0.0745 56  ALA B O   
2269 C CB  . ALA B 30  ? 0.4713 0.3043 0.3132 -0.0072 0.0645  -0.0811 56  ALA B CB  
2270 N N   . ILE B 31  ? 0.4563 0.3086 0.3042 0.0125  0.0606  -0.0584 57  ILE B N   
2271 C CA  . ILE B 31  ? 0.4606 0.3284 0.3086 0.0164  0.0588  -0.0556 57  ILE B CA  
2272 C C   . ILE B 31  ? 0.4601 0.3411 0.3018 0.0094  0.0527  -0.0569 57  ILE B C   
2273 O O   . ILE B 31  ? 0.4393 0.3219 0.2807 0.0051  0.0475  -0.0534 57  ILE B O   
2274 C CB  . ILE B 31  ? 0.4619 0.3352 0.3172 0.0239  0.0568  -0.0447 57  ILE B CB  
2275 C CG1 . ILE B 31  ? 0.4694 0.3306 0.3304 0.0327  0.0630  -0.0425 57  ILE B CG1 
2276 C CG2 . ILE B 31  ? 0.4587 0.3498 0.3156 0.0257  0.0545  -0.0420 57  ILE B CG2 
2277 C CD1 . ILE B 31  ? 0.4740 0.3399 0.3411 0.0399  0.0598  -0.0314 57  ILE B CD1 
2278 N N   . GLU B 32  ? 0.4678 0.3572 0.3039 0.0085  0.0540  -0.0623 59  GLU B N   
2279 C CA  . GLU B 32  ? 0.4896 0.3909 0.3184 0.0031  0.0488  -0.0628 59  GLU B CA  
2280 C C   . GLU B 32  ? 0.4596 0.3731 0.2860 0.0061  0.0502  -0.0600 59  GLU B C   
2281 O O   . GLU B 32  ? 0.4340 0.3474 0.2595 0.0095  0.0561  -0.0645 59  GLU B O   
2282 C CB  . GLU B 32  ? 0.5456 0.4459 0.3664 -0.0033 0.0480  -0.0728 59  GLU B CB  
2283 C CG  . GLU B 32  ? 0.6441 0.5323 0.4643 -0.0037 0.0547  -0.0837 59  GLU B CG  
2284 C CD  . GLU B 32  ? 0.7198 0.6087 0.5335 -0.0116 0.0529  -0.0950 59  GLU B CD  
2285 O OE1 . GLU B 32  ? 0.7321 0.6185 0.5488 -0.0171 0.0494  -0.0957 59  GLU B OE1 
2286 O OE2 . GLU B 32  ? 0.8366 0.7306 0.6422 -0.0122 0.0552  -0.1035 59  GLU B OE2 
2287 N N   . TYR B 33  ? 0.4248 0.3480 0.2511 0.0047  0.0455  -0.0526 60  TYR B N   
2288 C CA  . TYR B 33  ? 0.4170 0.3512 0.2404 0.0059  0.0473  -0.0496 60  TYR B CA  
2289 C C   . TYR B 33  ? 0.4078 0.3485 0.2254 0.0019  0.0419  -0.0451 60  TYR B C   
2290 O O   . TYR B 33  ? 0.3975 0.3378 0.2201 0.0007  0.0377  -0.0393 60  TYR B O   
2291 C CB  . TYR B 33  ? 0.4216 0.3597 0.2556 0.0105  0.0498  -0.0438 60  TYR B CB  
2292 C CG  . TYR B 33  ? 0.4146 0.3637 0.2471 0.0110  0.0536  -0.0415 60  TYR B CG  
2293 C CD1 . TYR B 33  ? 0.4292 0.3806 0.2587 0.0139  0.0604  -0.0466 60  TYR B CD1 
2294 C CD2 . TYR B 33  ? 0.3976 0.3538 0.2310 0.0083  0.0512  -0.0345 60  TYR B CD2 
2295 C CE1 . TYR B 33  ? 0.4276 0.3889 0.2550 0.0140  0.0650  -0.0442 60  TYR B CE1 
2296 C CE2 . TYR B 33  ? 0.4050 0.3696 0.2369 0.0081  0.0559  -0.0319 60  TYR B CE2 
2297 C CZ  . TYR B 33  ? 0.4163 0.3841 0.2452 0.0109  0.0629  -0.0364 60  TYR B CZ  
2298 O OH  . TYR B 33  ? 0.4196 0.3960 0.2472 0.0107  0.0687  -0.0334 60  TYR B OH  
2299 N N   . ARG B 34  ? 0.4140 0.3603 0.2202 0.0003  0.0422  -0.0484 61  ARG B N   
2300 C CA  . ARG B 34  ? 0.4099 0.3623 0.2093 -0.0022 0.0372  -0.0442 61  ARG B CA  
2301 C C   . ARG B 34  ? 0.4143 0.3625 0.2176 -0.0051 0.0312  -0.0444 61  ARG B C   
2302 O O   . ARG B 34  ? 0.4035 0.3546 0.2074 -0.0061 0.0269  -0.0383 61  ARG B O   
2303 C CB  . ARG B 34  ? 0.3963 0.3535 0.1981 -0.0011 0.0381  -0.0343 61  ARG B CB  
2304 C CG  . ARG B 34  ? 0.4053 0.3675 0.2044 0.0012  0.0450  -0.0333 61  ARG B CG  
2305 C CD  . ARG B 34  ? 0.4094 0.3755 0.2092 0.0006  0.0460  -0.0237 61  ARG B CD  
2306 N NE  . ARG B 34  ? 0.4142 0.3852 0.2148 0.0019  0.0537  -0.0215 61  ARG B NE  
2307 C CZ  . ARG B 34  ? 0.4352 0.4111 0.2246 0.0031  0.0586  -0.0217 61  ARG B CZ  
2308 N NH1 . ARG B 34  ? 0.4486 0.4263 0.2234 0.0035  0.0560  -0.0245 61  ARG B NH1 
2309 N NH2 . ARG B 34  ? 0.4531 0.4334 0.2459 0.0039  0.0663  -0.0195 61  ARG B NH2 
2310 N N   . ALA B 35  ? 0.4149 0.3557 0.2211 -0.0065 0.0317  -0.0518 62  ALA B N   
2311 C CA  . ALA B 35  ? 0.4125 0.3479 0.2244 -0.0094 0.0278  -0.0517 62  ALA B CA  
2312 C C   . ALA B 35  ? 0.4018 0.3448 0.2083 -0.0130 0.0223  -0.0535 62  ALA B C   
2313 O O   . ALA B 35  ? 0.3998 0.3416 0.2114 -0.0152 0.0186  -0.0513 62  ALA B O   
2314 C CB  . ALA B 35  ? 0.4180 0.3418 0.2343 -0.0101 0.0313  -0.0585 62  ALA B CB  
2315 N N   . ASP B 36  ? 0.4037 0.3554 0.2001 -0.0133 0.0217  -0.0577 63  ASP B N   
2316 C CA  . ASP B 36  ? 0.4252 0.3869 0.2166 -0.0158 0.0158  -0.0597 63  ASP B CA  
2317 C C   . ASP B 36  ? 0.4329 0.4045 0.2174 -0.0121 0.0134  -0.0507 63  ASP B C   
2318 O O   . ASP B 36  ? 0.4348 0.4172 0.2133 -0.0123 0.0084  -0.0511 63  ASP B O   
2319 C CB  . ASP B 36  ? 0.4645 0.4310 0.2491 -0.0191 0.0155  -0.0722 63  ASP B CB  
2320 C CG  . ASP B 36  ? 0.4708 0.4255 0.2625 -0.0234 0.0189  -0.0818 63  ASP B CG  
2321 O OD1 . ASP B 36  ? 0.4299 0.3785 0.2311 -0.0262 0.0176  -0.0806 63  ASP B OD1 
2322 O OD2 . ASP B 36  ? 0.5011 0.4526 0.2882 -0.0239 0.0235  -0.0908 63  ASP B OD2 
2323 N N   . GLU B 37  ? 0.4260 0.3942 0.2117 -0.0089 0.0171  -0.0425 64  GLU B N   
2324 C CA  . GLU B 37  ? 0.4189 0.3924 0.2000 -0.0058 0.0163  -0.0325 64  GLU B CA  
2325 C C   . GLU B 37  ? 0.4217 0.3923 0.2113 -0.0062 0.0127  -0.0261 64  GLU B C   
2326 O O   . GLU B 37  ? 0.4079 0.3709 0.2074 -0.0079 0.0130  -0.0268 64  GLU B O   
2327 C CB  . GLU B 37  ? 0.4107 0.3818 0.1911 -0.0034 0.0227  -0.0270 64  GLU B CB  
2328 C CG  . GLU B 37  ? 0.4149 0.3901 0.1854 -0.0022 0.0273  -0.0321 64  GLU B CG  
2329 C CD  . GLU B 37  ? 0.4153 0.3902 0.1854 0.0000  0.0342  -0.0256 64  GLU B CD  
2330 O OE1 . GLU B 37  ? 0.4132 0.3863 0.1876 0.0004  0.0351  -0.0162 64  GLU B OE1 
2331 O OE2 . GLU B 37  ? 0.4244 0.4005 0.1911 0.0008  0.0395  -0.0303 64  GLU B OE2 
2332 N N   . ARG B 38  ? 0.4132 0.3898 0.1983 -0.0037 0.0099  -0.0196 65  ARG B N   
2333 C CA  . ARG B 38  ? 0.4083 0.3822 0.2009 -0.0034 0.0071  -0.0140 65  ARG B CA  
2334 C C   . ARG B 38  ? 0.3833 0.3489 0.1814 -0.0028 0.0114  -0.0068 65  ARG B C   
2335 O O   . ARG B 38  ? 0.3818 0.3468 0.1755 -0.0012 0.0159  -0.0021 65  ARG B O   
2336 C CB  . ARG B 38  ? 0.4190 0.4022 0.2056 0.0001  0.0027  -0.0093 65  ARG B CB  
2337 C CG  . ARG B 38  ? 0.4190 0.4131 0.2043 -0.0016 -0.0031 -0.0174 65  ARG B CG  
2338 C CD  . ARG B 38  ? 0.4255 0.4321 0.2042 0.0034  -0.0078 -0.0122 65  ARG B CD  
2339 N NE  . ARG B 38  ? 0.4271 0.4470 0.2069 0.0011  -0.0142 -0.0209 65  ARG B NE  
2340 C CZ  . ARG B 38  ? 0.4447 0.4665 0.2355 -0.0024 -0.0173 -0.0253 65  ARG B CZ  
2341 N NH1 . ARG B 38  ? 0.4250 0.4364 0.2258 -0.0028 -0.0153 -0.0207 65  ARG B NH1 
2342 N NH2 . ARG B 38  ? 0.4487 0.4835 0.2405 -0.0059 -0.0221 -0.0350 65  ARG B NH2 
2343 N N   . PHE B 39  ? 0.3599 0.3195 0.1677 -0.0046 0.0103  -0.0064 66  PHE B N   
2344 C CA  . PHE B 39  ? 0.3408 0.2940 0.1548 -0.0048 0.0132  -0.0009 66  PHE B CA  
2345 C C   . PHE B 39  ? 0.3401 0.2913 0.1589 -0.0047 0.0102  0.0018  66  PHE B C   
2346 O O   . PHE B 39  ? 0.3517 0.3048 0.1728 -0.0057 0.0066  -0.0022 66  PHE B O   
2347 C CB  . PHE B 39  ? 0.3410 0.2901 0.1623 -0.0070 0.0153  -0.0044 66  PHE B CB  
2348 C CG  . PHE B 39  ? 0.3491 0.2997 0.1684 -0.0066 0.0195  -0.0067 66  PHE B CG  
2349 C CD1 . PHE B 39  ? 0.3598 0.3123 0.1747 -0.0064 0.0195  -0.0131 66  PHE B CD1 
2350 C CD2 . PHE B 39  ? 0.3619 0.3123 0.1852 -0.0069 0.0241  -0.0035 66  PHE B CD2 
2351 C CE1 . PHE B 39  ? 0.3725 0.3261 0.1860 -0.0055 0.0240  -0.0157 66  PHE B CE1 
2352 C CE2 . PHE B 39  ? 0.3706 0.3237 0.1935 -0.0062 0.0284  -0.0057 66  PHE B CE2 
2353 C CZ  . PHE B 39  ? 0.3782 0.3327 0.1960 -0.0050 0.0285  -0.0116 66  PHE B CZ  
2354 N N   . ALA B 40  ? 0.3393 0.2859 0.1603 -0.0038 0.0127  0.0079  67  ALA B N   
2355 C CA  . ALA B 40  ? 0.3452 0.2883 0.1716 -0.0036 0.0111  0.0097  67  ALA B CA  
2356 C C   . ALA B 40  ? 0.3404 0.2812 0.1737 -0.0067 0.0093  0.0045  67  ALA B C   
2357 O O   . ALA B 40  ? 0.3387 0.2771 0.1754 -0.0089 0.0111  0.0026  67  ALA B O   
2358 C CB  . ALA B 40  ? 0.3584 0.2944 0.1869 -0.0033 0.0156  0.0155  67  ALA B CB  
2359 N N   . PHE B 41  ? 0.3278 0.2703 0.1634 -0.0066 0.0061  0.0028  68  PHE B N   
2360 C CA  . PHE B 41  ? 0.3367 0.2763 0.1777 -0.0090 0.0053  -0.0005 68  PHE B CA  
2361 C C   . PHE B 41  ? 0.3377 0.2716 0.1827 -0.0102 0.0075  0.0009  68  PHE B C   
2362 O O   . PHE B 41  ? 0.3526 0.2850 0.2002 -0.0120 0.0075  -0.0015 68  PHE B O   
2363 C CB  . PHE B 41  ? 0.3356 0.2776 0.1791 -0.0084 0.0030  -0.0009 68  PHE B CB  
2364 C CG  . PHE B 41  ? 0.3337 0.2821 0.1774 -0.0095 0.0003  -0.0052 68  PHE B CG  
2365 C CD1 . PHE B 41  ? 0.3418 0.2875 0.1878 -0.0128 0.0007  -0.0095 68  PHE B CD1 
2366 C CD2 . PHE B 41  ? 0.3497 0.3068 0.1923 -0.0074 -0.0024 -0.0048 68  PHE B CD2 
2367 C CE1 . PHE B 41  ? 0.3491 0.2993 0.1969 -0.0152 -0.0007 -0.0141 68  PHE B CE1 
2368 C CE2 . PHE B 41  ? 0.3547 0.3194 0.1993 -0.0098 -0.0049 -0.0101 68  PHE B CE2 
2369 C CZ  . PHE B 41  ? 0.3552 0.3156 0.2028 -0.0143 -0.0037 -0.0151 68  PHE B CZ  
2370 N N   . CYS B 42  ? 0.3393 0.2701 0.1849 -0.0090 0.0093  0.0046  69  CYS B N   
2371 C CA  . CYS B 42  ? 0.3488 0.2743 0.1988 -0.0108 0.0111  0.0041  69  CYS B CA  
2372 C C   . CYS B 42  ? 0.3506 0.2770 0.2026 -0.0117 0.0087  0.0006  69  CYS B C   
2373 O O   . CYS B 42  ? 0.3435 0.2730 0.1948 -0.0104 0.0068  0.0002  69  CYS B O   
2374 C CB  . CYS B 42  ? 0.3658 0.2900 0.2182 -0.0137 0.0137  0.0035  69  CYS B CB  
2375 S SG  . CYS B 42  ? 0.3640 0.2873 0.2133 -0.0127 0.0180  0.0084  69  CYS B SG  
2376 N N   . SER B 43  ? 0.3232 0.2478 0.1776 -0.0140 0.0091  -0.0019 70  SER B N   
2377 C CA  . SER B 43  ? 0.3339 0.2587 0.1887 -0.0145 0.0078  -0.0043 70  SER B CA  
2378 C C   . SER B 43  ? 0.3218 0.2492 0.1749 -0.0143 0.0060  -0.0053 70  SER B C   
2379 O O   . SER B 43  ? 0.3182 0.2453 0.1709 -0.0146 0.0057  -0.0063 70  SER B O   
2380 C CB  . SER B 43  ? 0.3283 0.2520 0.1847 -0.0167 0.0084  -0.0070 70  SER B CB  
2381 O OG  . SER B 43  ? 0.3555 0.2743 0.2137 -0.0170 0.0109  -0.0073 70  SER B OG  
2382 N N   . THR B 44  ? 0.3273 0.2564 0.1792 -0.0140 0.0056  -0.0051 71  THR B N   
2383 C CA  . THR B 44  ? 0.3297 0.2588 0.1806 -0.0141 0.0050  -0.0065 71  THR B CA  
2384 C C   . THR B 44  ? 0.3339 0.2639 0.1854 -0.0147 0.0047  -0.0073 71  THR B C   
2385 O O   . THR B 44  ? 0.3452 0.2732 0.1968 -0.0158 0.0054  -0.0084 71  THR B O   
2386 C CB  . THR B 44  ? 0.3288 0.2586 0.1783 -0.0136 0.0055  -0.0072 71  THR B CB  
2387 O OG1 . THR B 44  ? 0.3294 0.2620 0.1771 -0.0133 0.0051  -0.0072 71  THR B OG1 
2388 C CG2 . THR B 44  ? 0.3257 0.2565 0.1766 -0.0129 0.0062  -0.0067 71  THR B CG2 
2389 N N   . PHE B 45  ? 0.3292 0.2622 0.1817 -0.0139 0.0041  -0.0065 72  PHE B N   
2390 C CA  . PHE B 45  ? 0.3192 0.2564 0.1742 -0.0143 0.0034  -0.0078 72  PHE B CA  
2391 C C   . PHE B 45  ? 0.3234 0.2586 0.1804 -0.0152 0.0050  -0.0081 72  PHE B C   
2392 O O   . PHE B 45  ? 0.3288 0.2671 0.1889 -0.0167 0.0055  -0.0097 72  PHE B O   
2393 C CB  . PHE B 45  ? 0.3279 0.2704 0.1838 -0.0116 0.0021  -0.0059 72  PHE B CB  
2394 C CG  . PHE B 45  ? 0.3327 0.2732 0.1908 -0.0092 0.0034  -0.0035 72  PHE B CG  
2395 C CD1 . PHE B 45  ? 0.3314 0.2655 0.1880 -0.0083 0.0052  -0.0015 72  PHE B CD1 
2396 C CD2 . PHE B 45  ? 0.3390 0.2836 0.2015 -0.0082 0.0036  -0.0041 72  PHE B CD2 
2397 C CE1 . PHE B 45  ? 0.3468 0.2771 0.2055 -0.0065 0.0073  -0.0004 72  PHE B CE1 
2398 C CE2 . PHE B 45  ? 0.3447 0.2863 0.2093 -0.0055 0.0057  -0.0026 72  PHE B CE2 
2399 C CZ  . PHE B 45  ? 0.3446 0.2782 0.2070 -0.0048 0.0077  -0.0010 72  PHE B CZ  
2400 N N   . LYS B 46  ? 0.3204 0.2515 0.1758 -0.0147 0.0060  -0.0072 73  LYS B N   
2401 C CA  . LYS B 46  ? 0.3374 0.2672 0.1930 -0.0151 0.0077  -0.0077 73  LYS B CA  
2402 C C   . LYS B 46  ? 0.3536 0.2819 0.2079 -0.0168 0.0091  -0.0079 73  LYS B C   
2403 O O   . LYS B 46  ? 0.3595 0.2881 0.2144 -0.0176 0.0114  -0.0081 73  LYS B O   
2404 C CB  . LYS B 46  ? 0.3178 0.2448 0.1711 -0.0147 0.0081  -0.0081 73  LYS B CB  
2405 C CG  . LYS B 46  ? 0.3404 0.2662 0.1959 -0.0134 0.0086  -0.0078 73  LYS B CG  
2406 C CD  . LYS B 46  ? 0.3520 0.2744 0.2067 -0.0144 0.0094  -0.0095 73  LYS B CD  
2407 C CE  . LYS B 46  ? 0.3710 0.2896 0.2285 -0.0132 0.0114  -0.0086 73  LYS B CE  
2408 N NZ  . LYS B 46  ? 0.3950 0.3097 0.2530 -0.0158 0.0129  -0.0113 73  LYS B NZ  
2409 N N   . ALA B 47  ? 0.3616 0.2873 0.2141 -0.0172 0.0087  -0.0076 74  ALA B N   
2410 C CA  . ALA B 47  ? 0.3788 0.3003 0.2300 -0.0184 0.0112  -0.0070 74  ALA B CA  
2411 C C   . ALA B 47  ? 0.3712 0.2946 0.2271 -0.0216 0.0129  -0.0092 74  ALA B C   
2412 O O   . ALA B 47  ? 0.3806 0.3030 0.2376 -0.0232 0.0160  -0.0087 74  ALA B O   
2413 C CB  . ALA B 47  ? 0.3950 0.3125 0.2439 -0.0170 0.0109  -0.0061 74  ALA B CB  
2414 N N   . PRO B 48  ? 0.3429 0.2701 0.2020 -0.0230 0.0111  -0.0121 75  PRO B N   
2415 C CA  . PRO B 48  ? 0.3367 0.2692 0.2017 -0.0266 0.0120  -0.0155 75  PRO B CA  
2416 C C   . PRO B 48  ? 0.3359 0.2763 0.2056 -0.0262 0.0118  -0.0154 75  PRO B C   
2417 O O   . PRO B 48  ? 0.3445 0.2895 0.2203 -0.0295 0.0138  -0.0177 75  PRO B O   
2418 C CB  . PRO B 48  ? 0.3335 0.2705 0.1990 -0.0273 0.0090  -0.0189 75  PRO B CB  
2419 C CG  . PRO B 48  ? 0.3339 0.2694 0.1942 -0.0232 0.0067  -0.0161 75  PRO B CG  
2420 C CD  . PRO B 48  ? 0.3378 0.2653 0.1947 -0.0216 0.0087  -0.0128 75  PRO B CD  
2421 N N   . LEU B 49  ? 0.3325 0.2745 0.2005 -0.0222 0.0101  -0.0130 76  LEU B N   
2422 C CA  . LEU B 49  ? 0.3261 0.2739 0.1984 -0.0206 0.0108  -0.0127 76  LEU B CA  
2423 C C   . LEU B 49  ? 0.3224 0.2672 0.1948 -0.0225 0.0154  -0.0124 76  LEU B C   
2424 O O   . LEU B 49  ? 0.3214 0.2727 0.2003 -0.0239 0.0176  -0.0138 76  LEU B O   
2425 C CB  . LEU B 49  ? 0.3240 0.2700 0.1937 -0.0162 0.0096  -0.0104 76  LEU B CB  
2426 C CG  . LEU B 49  ? 0.3313 0.2805 0.2049 -0.0135 0.0115  -0.0102 76  LEU B CG  
2427 C CD1 . LEU B 49  ? 0.3473 0.3082 0.2291 -0.0123 0.0102  -0.0110 76  LEU B CD1 
2428 C CD2 . LEU B 49  ? 0.3387 0.2824 0.2094 -0.0099 0.0116  -0.0086 76  LEU B CD2 
2429 N N   . VAL B 50  ? 0.3214 0.2577 0.1867 -0.0221 0.0170  -0.0104 77  VAL B N   
2430 C CA  . VAL B 50  ? 0.3400 0.2731 0.2025 -0.0231 0.0215  -0.0090 77  VAL B CA  
2431 C C   . VAL B 50  ? 0.3520 0.2844 0.2187 -0.0275 0.0253  -0.0096 77  VAL B C   
2432 O O   . VAL B 50  ? 0.3391 0.2739 0.2091 -0.0296 0.0297  -0.0097 77  VAL B O   
2433 C CB  . VAL B 50  ? 0.3439 0.2701 0.1970 -0.0209 0.0213  -0.0064 77  VAL B CB  
2434 C CG1 . VAL B 50  ? 0.3580 0.2800 0.2057 -0.0215 0.0261  -0.0036 77  VAL B CG1 
2435 C CG2 . VAL B 50  ? 0.3450 0.2729 0.1958 -0.0182 0.0191  -0.0075 77  VAL B CG2 
2436 N N   . ALA B 51  ? 0.3420 0.2713 0.2096 -0.0295 0.0240  -0.0107 78  ALA B N   
2437 C CA  . ALA B 51  ? 0.3363 0.2636 0.2090 -0.0349 0.0281  -0.0126 78  ALA B CA  
2438 C C   . ALA B 51  ? 0.3306 0.2703 0.2142 -0.0383 0.0283  -0.0169 78  ALA B C   
2439 O O   . ALA B 51  ? 0.3359 0.2764 0.2251 -0.0430 0.0336  -0.0180 78  ALA B O   
2440 C CB  . ALA B 51  ? 0.3331 0.2551 0.2050 -0.0362 0.0266  -0.0146 78  ALA B CB  
2441 N N   . ALA B 52  ? 0.3219 0.2720 0.2089 -0.0358 0.0228  -0.0190 79  ALA B N   
2442 C CA  . ALA B 52  ? 0.3199 0.2847 0.2179 -0.0378 0.0219  -0.0228 79  ALA B CA  
2443 C C   . ALA B 52  ? 0.3285 0.2972 0.2305 -0.0371 0.0264  -0.0213 79  ALA B C   
2444 O O   . ALA B 52  ? 0.3297 0.3071 0.2416 -0.0413 0.0296  -0.0242 79  ALA B O   
2445 C CB  . ALA B 52  ? 0.3141 0.2883 0.2128 -0.0333 0.0152  -0.0235 79  ALA B CB  
2446 N N   . VAL B 53  ? 0.3213 0.2846 0.2161 -0.0319 0.0268  -0.0176 80  VAL B N   
2447 C CA  . VAL B 53  ? 0.3348 0.3012 0.2319 -0.0307 0.0315  -0.0168 80  VAL B CA  
2448 C C   . VAL B 53  ? 0.3396 0.2999 0.2351 -0.0356 0.0388  -0.0155 80  VAL B C   
2449 O O   . VAL B 53  ? 0.3446 0.3115 0.2472 -0.0380 0.0441  -0.0166 80  VAL B O   
2450 C CB  . VAL B 53  ? 0.3307 0.2912 0.2191 -0.0248 0.0305  -0.0144 80  VAL B CB  
2451 C CG1 . VAL B 53  ? 0.3359 0.2966 0.2231 -0.0238 0.0363  -0.0141 80  VAL B CG1 
2452 C CG2 . VAL B 53  ? 0.3225 0.2885 0.2141 -0.0200 0.0252  -0.0149 80  VAL B CG2 
2453 N N   . LEU B 54  ? 0.3585 0.3062 0.2448 -0.0366 0.0398  -0.0128 81  LEU B N   
2454 C CA  . LEU B 54  ? 0.3870 0.3267 0.2707 -0.0405 0.0473  -0.0101 81  LEU B CA  
2455 C C   . LEU B 54  ? 0.4004 0.3458 0.2970 -0.0479 0.0509  -0.0141 81  LEU B C   
2456 O O   . LEU B 54  ? 0.4160 0.3637 0.3176 -0.0516 0.0582  -0.0138 81  LEU B O   
2457 C CB  . LEU B 54  ? 0.3918 0.3174 0.2645 -0.0391 0.0471  -0.0060 81  LEU B CB  
2458 C CG  . LEU B 54  ? 0.3803 0.3012 0.2401 -0.0329 0.0449  -0.0019 81  LEU B CG  
2459 C CD1 . LEU B 54  ? 0.3744 0.2853 0.2267 -0.0308 0.0430  0.0014  81  LEU B CD1 
2460 C CD2 . LEU B 54  ? 0.3971 0.3166 0.2502 -0.0319 0.0512  0.0016  81  LEU B CD2 
2461 N N   . HIS B 55  ? 0.4091 0.3579 0.3114 -0.0503 0.0462  -0.0185 82  HIS B N   
2462 C CA  . HIS B 55  ? 0.4218 0.3753 0.3360 -0.0586 0.0493  -0.0238 82  HIS B CA  
2463 C C   . HIS B 55  ? 0.4112 0.3830 0.3393 -0.0611 0.0505  -0.0278 82  HIS B C   
2464 O O   . HIS B 55  ? 0.3965 0.3714 0.3345 -0.0686 0.0570  -0.0305 82  HIS B O   
2465 C CB  . HIS B 55  ? 0.4172 0.3718 0.3327 -0.0601 0.0431  -0.0288 82  HIS B CB  
2466 C CG  . HIS B 55  ? 0.4341 0.3949 0.3620 -0.0693 0.0456  -0.0363 82  HIS B CG  
2467 N ND1 . HIS B 55  ? 0.4227 0.4041 0.3627 -0.0717 0.0407  -0.0431 82  HIS B ND1 
2468 C CD2 . HIS B 55  ? 0.4502 0.3997 0.3809 -0.0769 0.0527  -0.0384 82  HIS B CD2 
2469 C CE1 . HIS B 55  ? 0.4655 0.4497 0.4158 -0.0814 0.0443  -0.0503 82  HIS B CE1 
2470 N NE2 . HIS B 55  ? 0.4680 0.4314 0.4129 -0.0850 0.0521  -0.0477 82  HIS B NE2 
2471 N N   . GLN B 56  ? 0.4243 0.4083 0.3542 -0.0548 0.0447  -0.0280 83  GLN B N   
2472 C CA  . GLN B 56  ? 0.4571 0.4617 0.4020 -0.0556 0.0439  -0.0322 83  GLN B CA  
2473 C C   . GLN B 56  ? 0.4466 0.4543 0.3951 -0.0552 0.0516  -0.0300 83  GLN B C   
2474 O O   . GLN B 56  ? 0.4509 0.4761 0.4137 -0.0566 0.0528  -0.0335 83  GLN B O   
2475 C CB  . GLN B 56  ? 0.5232 0.5385 0.4684 -0.0480 0.0347  -0.0326 83  GLN B CB  
2476 C CG  . GLN B 56  ? 0.6079 0.6256 0.5523 -0.0498 0.0278  -0.0363 83  GLN B CG  
2477 C CD  . GLN B 56  ? 0.7115 0.7413 0.6687 -0.0589 0.0282  -0.0441 83  GLN B CD  
2478 O OE1 . GLN B 56  ? 0.7128 0.7327 0.6712 -0.0670 0.0343  -0.0463 83  GLN B OE1 
2479 N NE2 . GLN B 56  ? 0.7293 0.7803 0.6959 -0.0575 0.0215  -0.0485 83  GLN B NE2 
2480 N N   . ASN B 57  ? 0.4164 0.4084 0.3521 -0.0533 0.0569  -0.0245 86  ASN B N   
2481 C CA  . ASN B 57  ? 0.4346 0.4287 0.3703 -0.0517 0.0642  -0.0222 86  ASN B CA  
2482 C C   . ASN B 57  ? 0.4389 0.4189 0.3665 -0.0561 0.0737  -0.0179 86  ASN B C   
2483 O O   . ASN B 57  ? 0.4350 0.3994 0.3518 -0.0570 0.0737  -0.0144 86  ASN B O   
2484 C CB  . ASN B 57  ? 0.4158 0.4069 0.3412 -0.0426 0.0612  -0.0196 86  ASN B CB  
2485 C CG  . ASN B 57  ? 0.3940 0.3968 0.3265 -0.0369 0.0535  -0.0222 86  ASN B CG  
2486 O OD1 . ASN B 57  ? 0.3976 0.4152 0.3419 -0.0347 0.0547  -0.0245 86  ASN B OD1 
2487 N ND2 . ASN B 57  ? 0.3801 0.3769 0.3055 -0.0337 0.0461  -0.0214 86  ASN B ND2 
2488 N N   . PRO B 58  ? 0.4652 0.4501 0.3970 -0.0580 0.0827  -0.0170 87  PRO B N   
2489 C CA  . PRO B 58  ? 0.4750 0.4459 0.3955 -0.0600 0.0922  -0.0110 87  PRO B CA  
2490 C C   . PRO B 58  ? 0.4639 0.4224 0.3638 -0.0523 0.0896  -0.0056 87  PRO B C   
2491 O O   . PRO B 58  ? 0.4230 0.3850 0.3189 -0.0459 0.0825  -0.0073 87  PRO B O   
2492 C CB  . PRO B 58  ? 0.4827 0.4653 0.4132 -0.0628 0.1017  -0.0121 87  PRO B CB  
2493 C CG  . PRO B 58  ? 0.4835 0.4844 0.4253 -0.0579 0.0956  -0.0175 87  PRO B CG  
2494 C CD  . PRO B 58  ? 0.4633 0.4678 0.4105 -0.0576 0.0846  -0.0212 87  PRO B CD  
2495 N N   . LEU B 59  ? 0.4725 0.4167 0.3596 -0.0531 0.0957  0.0009  88  LEU B N   
2496 C CA  . LEU B 59  ? 0.4961 0.4301 0.3633 -0.0462 0.0933  0.0062  88  LEU B CA  
2497 C C   . LEU B 59  ? 0.4922 0.4335 0.3531 -0.0409 0.0939  0.0048  88  LEU B C   
2498 O O   . LEU B 59  ? 0.5145 0.4533 0.3638 -0.0351 0.0878  0.0048  88  LEU B O   
2499 C CB  . LEU B 59  ? 0.5212 0.4409 0.3779 -0.0480 0.1018  0.0143  88  LEU B CB  
2500 C CG  . LEU B 59  ? 0.5460 0.4527 0.3859 -0.0424 0.0976  0.0205  88  LEU B CG  
2501 C CD1 . LEU B 59  ? 0.5415 0.4465 0.3866 -0.0420 0.0879  0.0170  88  LEU B CD1 
2502 C CD2 . LEU B 59  ? 0.5542 0.4467 0.3872 -0.0445 0.1080  0.0293  88  LEU B CD2 
2503 N N   . THR B 60  ? 0.4872 0.4380 0.3565 -0.0431 0.1015  0.0027  89  THR B N   
2504 C CA  . THR B 60  ? 0.4851 0.4424 0.3488 -0.0381 0.1037  0.0006  89  THR B CA  
2505 C C   . THR B 60  ? 0.4413 0.4057 0.3111 -0.0333 0.0946  -0.0057 89  THR B C   
2506 O O   . THR B 60  ? 0.4334 0.3994 0.2960 -0.0283 0.0946  -0.0082 89  THR B O   
2507 C CB  . THR B 60  ? 0.5138 0.4806 0.3876 -0.0417 0.1147  -0.0004 89  THR B CB  
2508 O OG1 . THR B 60  ? 0.5294 0.5072 0.4250 -0.0462 0.1125  -0.0051 89  THR B OG1 
2509 C CG2 . THR B 60  ? 0.5711 0.5291 0.4365 -0.0460 0.1257  0.0069  89  THR B CG2 
2510 N N   . HIS B 61  ? 0.4200 0.3884 0.3025 -0.0349 0.0875  -0.0083 90  HIS B N   
2511 C CA  . HIS B 61  ? 0.3965 0.3704 0.2844 -0.0300 0.0794  -0.0126 90  HIS B CA  
2512 C C   . HIS B 61  ? 0.3733 0.3370 0.2460 -0.0254 0.0732  -0.0119 90  HIS B C   
2513 O O   . HIS B 61  ? 0.3626 0.3280 0.2364 -0.0209 0.0690  -0.0151 90  HIS B O   
2514 C CB  . HIS B 61  ? 0.3998 0.3803 0.3020 -0.0327 0.0732  -0.0146 90  HIS B CB  
2515 C CG  . HIS B 61  ? 0.3846 0.3716 0.2931 -0.0273 0.0657  -0.0176 90  HIS B CG  
2516 N ND1 . HIS B 61  ? 0.3863 0.3857 0.3062 -0.0233 0.0669  -0.0205 90  HIS B ND1 
2517 C CD2 . HIS B 61  ? 0.3820 0.3646 0.2872 -0.0249 0.0574  -0.0174 90  HIS B CD2 
2518 C CE1 . HIS B 61  ? 0.3979 0.3990 0.3203 -0.0182 0.0596  -0.0213 90  HIS B CE1 
2519 N NE2 . HIS B 61  ? 0.3736 0.3646 0.2870 -0.0195 0.0539  -0.0195 90  HIS B NE2 
2520 N N   . LEU B 62  ? 0.3824 0.3357 0.2417 -0.0265 0.0729  -0.0076 91  LEU B N   
2521 C CA  . LEU B 62  ? 0.3861 0.3324 0.2316 -0.0226 0.0673  -0.0073 91  LEU B CA  
2522 C C   . LEU B 62  ? 0.3944 0.3424 0.2314 -0.0189 0.0700  -0.0106 91  LEU B C   
2523 O O   . LEU B 62  ? 0.3790 0.3238 0.2083 -0.0161 0.0648  -0.0131 91  LEU B O   
2524 C CB  . LEU B 62  ? 0.4137 0.3510 0.2477 -0.0236 0.0676  -0.0012 91  LEU B CB  
2525 C CG  . LEU B 62  ? 0.4260 0.3591 0.2668 -0.0268 0.0645  0.0010  91  LEU B CG  
2526 C CD1 . LEU B 62  ? 0.4567 0.3796 0.2854 -0.0265 0.0669  0.0079  91  LEU B CD1 
2527 C CD2 . LEU B 62  ? 0.4409 0.3748 0.2857 -0.0251 0.0555  -0.0022 91  LEU B CD2 
2528 N N   . ASP B 63  ? 0.3955 0.3485 0.2341 -0.0193 0.0784  -0.0112 92  ASP B N   
2529 C CA  . ASP B 63  ? 0.4227 0.3771 0.2523 -0.0160 0.0823  -0.0152 92  ASP B CA  
2530 C C   . ASP B 63  ? 0.4178 0.3787 0.2603 -0.0132 0.0834  -0.0213 92  ASP B C   
2531 O O   . ASP B 63  ? 0.4074 0.3693 0.2449 -0.0103 0.0876  -0.0258 92  ASP B O   
2532 C CB  . ASP B 63  ? 0.4583 0.4128 0.2770 -0.0171 0.0914  -0.0114 92  ASP B CB  
2533 C CG  . ASP B 63  ? 0.4923 0.4390 0.2956 -0.0175 0.0895  -0.0046 92  ASP B CG  
2534 O OD1 . ASP B 63  ? 0.5039 0.4476 0.2972 -0.0149 0.0822  -0.0059 92  ASP B OD1 
2535 O OD2 . ASP B 63  ? 0.5416 0.4852 0.3449 -0.0205 0.0949  0.0022  92  ASP B OD2 
2536 N N   . LYS B 64  ? 0.4034 0.3689 0.2621 -0.0134 0.0796  -0.0216 93  LYS B N   
2537 C CA  . LYS B 64  ? 0.4264 0.3980 0.2974 -0.0090 0.0802  -0.0260 93  LYS B CA  
2538 C C   . LYS B 64  ? 0.4138 0.3774 0.2785 -0.0051 0.0753  -0.0297 93  LYS B C   
2539 O O   . LYS B 64  ? 0.3974 0.3551 0.2588 -0.0061 0.0681  -0.0282 93  LYS B O   
2540 C CB  . LYS B 64  ? 0.4473 0.4275 0.3356 -0.0101 0.0764  -0.0244 93  LYS B CB  
2541 C CG  . LYS B 64  ? 0.4882 0.4715 0.3868 -0.0047 0.0713  -0.0262 93  LYS B CG  
2542 C CD  . LYS B 64  ? 0.5443 0.5382 0.4563 0.0006  0.0761  -0.0288 93  LYS B CD  
2543 C CE  . LYS B 64  ? 0.5784 0.5801 0.5039 0.0044  0.0697  -0.0275 93  LYS B CE  
2544 N NZ  . LYS B 64  ? 0.6365 0.6480 0.5746 0.0115  0.0739  -0.0294 93  LYS B NZ  
2545 N N   . LEU B 65  ? 0.4118 0.3749 0.2761 -0.0010 0.0800  -0.0350 94  LEU B N   
2546 C CA  . LEU B 65  ? 0.4024 0.3564 0.2616 0.0019  0.0772  -0.0397 94  LEU B CA  
2547 C C   . LEU B 65  ? 0.3810 0.3349 0.2541 0.0061  0.0735  -0.0388 94  LEU B C   
2548 O O   . LEU B 65  ? 0.3697 0.3318 0.2560 0.0099  0.0766  -0.0382 94  LEU B O   
2549 C CB  . LEU B 65  ? 0.4096 0.3614 0.2622 0.0045  0.0846  -0.0467 94  LEU B CB  
2550 C CG  . LEU B 65  ? 0.4175 0.3584 0.2637 0.0059  0.0829  -0.0534 94  LEU B CG  
2551 C CD1 . LEU B 65  ? 0.4147 0.3508 0.2461 0.0013  0.0769  -0.0542 94  LEU B CD1 
2552 C CD2 . LEU B 65  ? 0.4340 0.3732 0.2774 0.0091  0.0913  -0.0614 94  LEU B CD2 
2553 N N   . ILE B 66  ? 0.3672 0.3127 0.2372 0.0057  0.0672  -0.0384 95  ILE B N   
2554 C CA  . ILE B 66  ? 0.3646 0.3075 0.2445 0.0101  0.0642  -0.0369 95  ILE B CA  
2555 C C   . ILE B 66  ? 0.3750 0.3056 0.2509 0.0126  0.0669  -0.0425 95  ILE B C   
2556 O O   . ILE B 66  ? 0.3922 0.3150 0.2574 0.0085  0.0648  -0.0459 95  ILE B O   
2557 C CB  . ILE B 66  ? 0.3531 0.2952 0.2330 0.0073  0.0561  -0.0318 95  ILE B CB  
2558 C CG1 . ILE B 66  ? 0.3470 0.2990 0.2297 0.0035  0.0539  -0.0278 95  ILE B CG1 
2559 C CG2 . ILE B 66  ? 0.3567 0.2965 0.2452 0.0125  0.0535  -0.0291 95  ILE B CG2 
2560 C CD1 . ILE B 66  ? 0.3573 0.3225 0.2538 0.0060  0.0567  -0.0266 95  ILE B CD1 
2561 N N   . THR B 67  ? 0.3726 0.3017 0.2579 0.0193  0.0716  -0.0437 96  THR B N   
2562 C CA  . THR B 67  ? 0.3859 0.3009 0.2691 0.0218  0.0754  -0.0491 96  THR B CA  
2563 C C   . THR B 67  ? 0.3875 0.2946 0.2764 0.0247  0.0716  -0.0442 96  THR B C   
2564 O O   . THR B 67  ? 0.3833 0.2984 0.2801 0.0278  0.0674  -0.0368 96  THR B O   
2565 C CB  . THR B 67  ? 0.3962 0.3113 0.2852 0.0281  0.0843  -0.0536 96  THR B CB  
2566 O OG1 . THR B 67  ? 0.3953 0.3217 0.2987 0.0348  0.0844  -0.0473 96  THR B OG1 
2567 C CG2 . THR B 67  ? 0.3978 0.3196 0.2790 0.0250  0.0892  -0.0588 96  THR B CG2 
2568 N N   . TYR B 68  ? 0.3880 0.2801 0.2722 0.0229  0.0731  -0.0487 97  TYR B N   
2569 C CA  . TYR B 68  ? 0.4019 0.2843 0.2900 0.0250  0.0709  -0.0438 97  TYR B CA  
2570 C C   . TYR B 68  ? 0.4232 0.2877 0.3087 0.0237  0.0769  -0.0513 97  TYR B C   
2571 O O   . TYR B 68  ? 0.4278 0.2900 0.3082 0.0214  0.0815  -0.0605 97  TYR B O   
2572 C CB  . TYR B 68  ? 0.3858 0.2729 0.2697 0.0193  0.0625  -0.0390 97  TYR B CB  
2573 C CG  . TYR B 68  ? 0.3858 0.2717 0.2587 0.0105  0.0600  -0.0451 97  TYR B CG  
2574 C CD1 . TYR B 68  ? 0.3913 0.2878 0.2578 0.0070  0.0581  -0.0466 97  TYR B CD1 
2575 C CD2 . TYR B 68  ? 0.3902 0.2657 0.2598 0.0059  0.0592  -0.0484 97  TYR B CD2 
2576 C CE1 . TYR B 68  ? 0.3874 0.2842 0.2434 0.0005  0.0554  -0.0513 97  TYR B CE1 
2577 C CE2 . TYR B 68  ? 0.4020 0.2795 0.2627 -0.0015 0.0561  -0.0541 97  TYR B CE2 
2578 C CZ  . TYR B 68  ? 0.3939 0.2824 0.2472 -0.0036 0.0539  -0.0554 97  TYR B CZ  
2579 O OH  . TYR B 68  ? 0.3872 0.2790 0.2314 -0.0096 0.0501  -0.0600 97  TYR B OH  
2580 N N   . THR B 69  ? 0.4350 0.2869 0.3241 0.0253  0.0776  -0.0477 98  THR B N   
2581 C CA  . THR B 69  ? 0.4664 0.2993 0.3545 0.0233  0.0844  -0.0552 98  THR B CA  
2582 C C   . THR B 69  ? 0.4693 0.2941 0.3550 0.0164  0.0812  -0.0541 98  THR B C   
2583 O O   . THR B 69  ? 0.4507 0.2838 0.3356 0.0151  0.0742  -0.0466 98  THR B O   
2584 C CB  . THR B 69  ? 0.4773 0.2980 0.3744 0.0336  0.0928  -0.0526 98  THR B CB  
2585 O OG1 . THR B 69  ? 0.4855 0.3012 0.3867 0.0373  0.0906  -0.0418 98  THR B OG1 
2586 C CG2 . THR B 69  ? 0.4827 0.3152 0.3855 0.0421  0.0953  -0.0511 98  THR B CG2 
2587 N N   . SER B 70  ? 0.4952 0.3032 0.3805 0.0120  0.0872  -0.0623 99  SER B N   
2588 C CA  . SER B 70  ? 0.5279 0.3277 0.4128 0.0049  0.0858  -0.0621 99  SER B CA  
2589 C C   . SER B 70  ? 0.5070 0.3022 0.3974 0.0113  0.0854  -0.0483 99  SER B C   
2590 O O   . SER B 70  ? 0.4855 0.2813 0.3749 0.0067  0.0816  -0.0442 99  SER B O   
2591 C CB  . SER B 70  ? 0.5747 0.3563 0.4606 -0.0009 0.0939  -0.0737 99  SER B CB  
2592 O OG  . SER B 70  ? 0.6413 0.4304 0.5199 -0.0094 0.0917  -0.0870 99  SER B OG  
2593 N N   . ASP B 71  ? 0.4969 0.2884 0.3930 0.0226  0.0896  -0.0413 100 ASP B N   
2594 C CA  . ASP B 71  ? 0.5034 0.2921 0.4035 0.0307  0.0893  -0.0276 100 ASP B CA  
2595 C C   . ASP B 71  ? 0.4910 0.2999 0.3884 0.0307  0.0789  -0.0197 100 ASP B C   
2596 O O   . ASP B 71  ? 0.4868 0.2959 0.3850 0.0351  0.0769  -0.0092 100 ASP B O   
2597 C CB  . ASP B 71  ? 0.5046 0.2872 0.4116 0.0439  0.0958  -0.0223 100 ASP B CB  
2598 C CG  . ASP B 71  ? 0.5248 0.2812 0.4353 0.0456  0.1077  -0.0263 100 ASP B CG  
2599 O OD1 . ASP B 71  ? 0.5316 0.2761 0.4394 0.0349  0.1110  -0.0362 100 ASP B OD1 
2600 O OD2 . ASP B 71  ? 0.5227 0.2711 0.4393 0.0579  0.1138  -0.0195 100 ASP B OD2 
2601 N N   . ASP B 72  ? 0.4855 0.3108 0.3793 0.0262  0.0729  -0.0247 101 ASP B N   
2602 C CA  . ASP B 72  ? 0.4820 0.3250 0.3736 0.0253  0.0639  -0.0189 101 ASP B CA  
2603 C C   . ASP B 72  ? 0.4743 0.3177 0.3605 0.0161  0.0594  -0.0203 101 ASP B C   
2604 O O   . ASP B 72  ? 0.4638 0.3190 0.3479 0.0151  0.0527  -0.0154 101 ASP B O   
2605 C CB  . ASP B 72  ? 0.4748 0.3337 0.3656 0.0247  0.0607  -0.0226 101 ASP B CB  
2606 C CG  . ASP B 72  ? 0.4855 0.3504 0.3837 0.0343  0.0637  -0.0198 101 ASP B CG  
2607 O OD1 . ASP B 72  ? 0.5214 0.3923 0.4247 0.0417  0.0614  -0.0109 101 ASP B OD1 
2608 O OD2 . ASP B 72  ? 0.4782 0.3423 0.3770 0.0347  0.0685  -0.0267 101 ASP B OD2 
2609 N N   . ILE B 73  ? 0.4684 0.3001 0.3528 0.0090  0.0632  -0.0279 102 ILE B N   
2610 C CA  . ILE B 73  ? 0.4920 0.3264 0.3728 0.0002  0.0590  -0.0303 102 ILE B CA  
2611 C C   . ILE B 73  ? 0.5038 0.3272 0.3872 0.0005  0.0619  -0.0237 102 ILE B C   
2612 O O   . ILE B 73  ? 0.4824 0.2894 0.3688 -0.0013 0.0694  -0.0268 102 ILE B O   
2613 C CB  . ILE B 73  ? 0.5103 0.3429 0.3880 -0.0083 0.0602  -0.0430 102 ILE B CB  
2614 C CG1 . ILE B 73  ? 0.5330 0.3774 0.4061 -0.0074 0.0576  -0.0477 102 ILE B CG1 
2615 C CG2 . ILE B 73  ? 0.5181 0.3557 0.3939 -0.0169 0.0557  -0.0455 102 ILE B CG2 
2616 C CD1 . ILE B 73  ? 0.5289 0.3726 0.3973 -0.0137 0.0593  -0.0603 102 ILE B CD1 
2617 N N   . ARG B 74  ? 0.5195 0.3513 0.4015 0.0027  0.0569  -0.0148 103 ARG B N   
2618 C CA  . ARG B 74  ? 0.5803 0.4035 0.4631 0.0041  0.0597  -0.0067 103 ARG B CA  
2619 C C   . ARG B 74  ? 0.5557 0.3877 0.4356 -0.0024 0.0545  -0.0060 103 ARG B C   
2620 O O   . ARG B 74  ? 0.5159 0.3446 0.3951 -0.0012 0.0558  0.0015  103 ARG B O   
2621 C CB  . ARG B 74  ? 0.6495 0.4760 0.5325 0.0151  0.0588  0.0049  103 ARG B CB  
2622 C CG  . ARG B 74  ? 0.7343 0.5592 0.6212 0.0241  0.0617  0.0060  103 ARG B CG  
2623 C CD  . ARG B 74  ? 0.7964 0.6362 0.6831 0.0332  0.0560  0.0154  103 ARG B CD  
2624 N NE  . ARG B 74  ? 0.8398 0.6750 0.7240 0.0383  0.0571  0.0264  103 ARG B NE  
2625 C CZ  . ARG B 74  ? 0.8187 0.6650 0.6981 0.0385  0.0512  0.0322  103 ARG B CZ  
2626 N NH1 . ARG B 74  ? 0.7710 0.6346 0.6486 0.0345  0.0434  0.0285  103 ARG B NH1 
2627 N NH2 . ARG B 74  ? 0.8338 0.6732 0.7099 0.0430  0.0541  0.0418  103 ARG B NH2 
2628 N N   . SER B 75  ? 0.5031 0.3462 0.3809 -0.0084 0.0491  -0.0134 104 SER B N   
2629 C CA  . SER B 75  ? 0.5075 0.3602 0.3832 -0.0138 0.0441  -0.0138 104 SER B CA  
2630 C C   . SER B 75  ? 0.4878 0.3456 0.3630 -0.0212 0.0419  -0.0243 104 SER B C   
2631 O O   . SER B 75  ? 0.5038 0.3605 0.3782 -0.0211 0.0430  -0.0303 104 SER B O   
2632 C CB  . SER B 75  ? 0.4818 0.3478 0.3540 -0.0098 0.0375  -0.0083 104 SER B CB  
2633 O OG  . SER B 75  ? 0.4710 0.3444 0.3419 -0.0083 0.0345  -0.0118 104 SER B OG  
2634 N N   . ARG B 76  ? 0.4889 0.3536 0.3643 -0.0269 0.0389  -0.0261 105 ARG B N   
2635 C CA  . ARG B 76  ? 0.5088 0.3823 0.3835 -0.0330 0.0353  -0.0350 105 ARG B CA  
2636 C C   . ARG B 76  ? 0.4699 0.3524 0.3387 -0.0299 0.0307  -0.0364 105 ARG B C   
2637 O O   . ARG B 76  ? 0.4624 0.3524 0.3283 -0.0263 0.0265  -0.0308 105 ARG B O   
2638 C CB  . ARG B 76  ? 0.5552 0.4376 0.4316 -0.0366 0.0320  -0.0335 105 ARG B CB  
2639 C CG  . ARG B 76  ? 0.6244 0.5184 0.5011 -0.0423 0.0277  -0.0419 105 ARG B CG  
2640 C CD  . ARG B 76  ? 0.6942 0.5968 0.5752 -0.0457 0.0257  -0.0409 105 ARG B CD  
2641 N NE  . ARG B 76  ? 0.7619 0.6756 0.6455 -0.0517 0.0226  -0.0504 105 ARG B NE  
2642 C CZ  . ARG B 76  ? 0.7798 0.7053 0.6581 -0.0501 0.0165  -0.0534 105 ARG B CZ  
2643 N NH1 . ARG B 76  ? 0.7654 0.6942 0.6370 -0.0436 0.0129  -0.0468 105 ARG B NH1 
2644 N NH2 . ARG B 76  ? 0.8210 0.7559 0.7007 -0.0553 0.0141  -0.0630 105 ARG B NH2 
2645 N N   . SER B 77  ? 0.4622 0.3433 0.3291 -0.0316 0.0322  -0.0441 106 SER B N   
2646 C CA  . SER B 77  ? 0.4394 0.3264 0.3005 -0.0282 0.0301  -0.0450 106 SER B CA  
2647 C C   . SER B 77  ? 0.4450 0.3377 0.3015 -0.0328 0.0287  -0.0550 106 SER B C   
2648 O O   . SER B 77  ? 0.4473 0.3348 0.3024 -0.0333 0.0327  -0.0615 106 SER B O   
2649 C CB  . SER B 77  ? 0.4261 0.3047 0.2888 -0.0227 0.0351  -0.0427 106 SER B CB  
2650 O OG  . SER B 77  ? 0.4358 0.3113 0.3022 -0.0181 0.0356  -0.0336 106 SER B OG  
2651 N N   . PRO B 78  ? 0.4784 0.3830 0.3323 -0.0358 0.0230  -0.0565 107 PRO B N   
2652 C CA  . PRO B 78  ? 0.4868 0.3996 0.3361 -0.0401 0.0207  -0.0662 107 PRO B CA  
2653 C C   . PRO B 78  ? 0.4811 0.3968 0.3212 -0.0373 0.0211  -0.0689 107 PRO B C   
2654 O O   . PRO B 78  ? 0.5248 0.4423 0.3608 -0.0406 0.0220  -0.0787 107 PRO B O   
2655 C CB  . PRO B 78  ? 0.4894 0.4162 0.3380 -0.0410 0.0139  -0.0638 107 PRO B CB  
2656 C CG  . PRO B 78  ? 0.4910 0.4137 0.3461 -0.0393 0.0143  -0.0552 107 PRO B CG  
2657 C CD  . PRO B 78  ? 0.4685 0.3800 0.3235 -0.0345 0.0186  -0.0492 107 PRO B CD  
2658 N N   . VAL B 79  ? 0.4347 0.3507 0.2716 -0.0316 0.0211  -0.0608 108 VAL B N   
2659 C CA  . VAL B 79  ? 0.4418 0.3609 0.2701 -0.0288 0.0224  -0.0619 108 VAL B CA  
2660 C C   . VAL B 79  ? 0.4281 0.3368 0.2597 -0.0265 0.0293  -0.0636 108 VAL B C   
2661 O O   . VAL B 79  ? 0.4454 0.3531 0.2723 -0.0271 0.0327  -0.0710 108 VAL B O   
2662 C CB  . VAL B 79  ? 0.4408 0.3663 0.2646 -0.0248 0.0195  -0.0528 108 VAL B CB  
2663 C CG1 . VAL B 79  ? 0.4330 0.3613 0.2480 -0.0222 0.0221  -0.0530 108 VAL B CG1 
2664 C CG2 . VAL B 79  ? 0.4653 0.4002 0.2862 -0.0257 0.0132  -0.0507 108 VAL B CG2 
2665 N N   . ALA B 80  ? 0.4012 0.3028 0.2408 -0.0233 0.0315  -0.0570 109 ALA B N   
2666 C CA  . ALA B 80  ? 0.4013 0.2956 0.2447 -0.0191 0.0376  -0.0568 109 ALA B CA  
2667 C C   . ALA B 80  ? 0.4180 0.3021 0.2632 -0.0215 0.0430  -0.0662 109 ALA B C   
2668 O O   . ALA B 80  ? 0.4127 0.2926 0.2572 -0.0188 0.0484  -0.0702 109 ALA B O   
2669 C CB  . ALA B 80  ? 0.4105 0.3014 0.2620 -0.0148 0.0379  -0.0478 109 ALA B CB  
2670 N N   . GLN B 81  ? 0.4248 0.3053 0.2724 -0.0270 0.0420  -0.0706 110 GLN B N   
2671 C CA  . GLN B 81  ? 0.4908 0.3604 0.3409 -0.0309 0.0477  -0.0807 110 GLN B CA  
2672 C C   . GLN B 81  ? 0.4952 0.3705 0.3363 -0.0333 0.0483  -0.0915 110 GLN B C   
2673 O O   . GLN B 81  ? 0.5024 0.3682 0.3440 -0.0336 0.0549  -0.0998 110 GLN B O   
2674 C CB  . GLN B 81  ? 0.5585 0.4245 0.4143 -0.0374 0.0467  -0.0829 110 GLN B CB  
2675 C CG  . GLN B 81  ? 0.6641 0.5188 0.5234 -0.0436 0.0529  -0.0951 110 GLN B CG  
2676 C CD  . GLN B 81  ? 0.7672 0.6028 0.6320 -0.0390 0.0623  -0.0941 110 GLN B CD  
2677 O OE1 . GLN B 81  ? 0.8288 0.6534 0.7006 -0.0362 0.0657  -0.0858 110 GLN B OE1 
2678 N NE2 . GLN B 81  ? 0.8005 0.6320 0.6617 -0.0377 0.0670  -0.1024 110 GLN B NE2 
2679 N N   . GLN B 82  ? 0.4864 0.3767 0.3186 -0.0342 0.0419  -0.0913 111 GLN B N   
2680 C CA  . GLN B 82  ? 0.5242 0.4220 0.3456 -0.0364 0.0417  -0.1012 111 GLN B CA  
2681 C C   . GLN B 82  ? 0.4991 0.3963 0.3150 -0.0307 0.0466  -0.1000 111 GLN B C   
2682 O O   . GLN B 82  ? 0.4977 0.3984 0.3043 -0.0320 0.0487  -0.1091 111 GLN B O   
2683 C CB  . GLN B 82  ? 0.5736 0.4883 0.3863 -0.0379 0.0332  -0.0994 111 GLN B CB  
2684 C CG  . GLN B 82  ? 0.6259 0.5464 0.4435 -0.0435 0.0276  -0.1018 111 GLN B CG  
2685 C CD  . GLN B 82  ? 0.7368 0.6732 0.5484 -0.0417 0.0194  -0.0952 111 GLN B CD  
2686 O OE1 . GLN B 82  ? 0.7919 0.7327 0.5957 -0.0363 0.0184  -0.0875 111 GLN B OE1 
2687 N NE2 . GLN B 82  ? 0.7889 0.7337 0.6047 -0.0461 0.0142  -0.0981 111 GLN B NE2 
2688 N N   . HIS B 83  ? 0.4713 0.3654 0.2929 -0.0247 0.0486  -0.0894 112 HIS B N   
2689 C CA  . HIS B 83  ? 0.4818 0.3783 0.3001 -0.0195 0.0531  -0.0872 112 HIS B CA  
2690 C C   . HIS B 83  ? 0.4644 0.3502 0.2935 -0.0143 0.0601  -0.0852 112 HIS B C   
2691 O O   . HIS B 83  ? 0.4523 0.3414 0.2832 -0.0092 0.0635  -0.0809 112 HIS B O   
2692 C CB  . HIS B 83  ? 0.4930 0.4000 0.3078 -0.0171 0.0489  -0.0766 112 HIS B CB  
2693 C CG  . HIS B 83  ? 0.5356 0.4527 0.3397 -0.0203 0.0425  -0.0770 112 HIS B CG  
2694 N ND1 . HIS B 83  ? 0.5799 0.5036 0.3710 -0.0215 0.0431  -0.0839 112 HIS B ND1 
2695 C CD2 . HIS B 83  ? 0.5258 0.4479 0.3298 -0.0221 0.0356  -0.0722 112 HIS B CD2 
2696 C CE1 . HIS B 83  ? 0.5889 0.5223 0.3723 -0.0232 0.0362  -0.0823 112 HIS B CE1 
2697 N NE2 . HIS B 83  ? 0.5650 0.4973 0.3567 -0.0235 0.0318  -0.0752 112 HIS B NE2 
2698 N N   . VAL B 84  ? 0.4608 0.3340 0.2978 -0.0152 0.0628  -0.0880 113 VAL B N   
2699 C CA  . VAL B 84  ? 0.4661 0.3294 0.3135 -0.0085 0.0689  -0.0838 113 VAL B CA  
2700 C C   . VAL B 84  ? 0.4679 0.3298 0.3139 -0.0042 0.0766  -0.0897 113 VAL B C   
2701 O O   . VAL B 84  ? 0.4482 0.3102 0.3017 0.0031  0.0804  -0.0839 113 VAL B O   
2702 C CB  . VAL B 84  ? 0.4959 0.3436 0.3509 -0.0100 0.0717  -0.0851 113 VAL B CB  
2703 C CG1 . VAL B 84  ? 0.5183 0.3565 0.3702 -0.0164 0.0762  -0.0993 113 VAL B CG1 
2704 C CG2 . VAL B 84  ? 0.5213 0.3598 0.3866 -0.0012 0.0772  -0.0778 113 VAL B CG2 
2705 N N   . GLN B 85  ? 0.4612 0.3228 0.2980 -0.0084 0.0793  -0.1017 114 GLN B N   
2706 C CA  . GLN B 85  ? 0.4973 0.3563 0.3328 -0.0041 0.0879  -0.1082 114 GLN B CA  
2707 C C   . GLN B 85  ? 0.4726 0.3463 0.3026 -0.0010 0.0878  -0.1036 114 GLN B C   
2708 O O   . GLN B 85  ? 0.4740 0.3476 0.3071 0.0046  0.0951  -0.1050 114 GLN B O   
2709 C CB  . GLN B 85  ? 0.5430 0.3963 0.3698 -0.0098 0.0916  -0.1241 114 GLN B CB  
2710 C CG  . GLN B 85  ? 0.5999 0.4363 0.4336 -0.0139 0.0942  -0.1306 114 GLN B CG  
2711 C CD  . GLN B 85  ? 0.6653 0.4842 0.5110 -0.0067 0.1038  -0.1293 114 GLN B CD  
2712 O OE1 . GLN B 85  ? 0.7052 0.5149 0.5612 -0.0038 0.1038  -0.1204 114 GLN B OE1 
2713 N NE2 . GLN B 85  ? 0.7432 0.5569 0.5871 -0.0033 0.1126  -0.1382 114 GLN B NE2 
2714 N N   . THR B 86  ? 0.4529 0.3390 0.2749 -0.0044 0.0804  -0.0985 115 THR B N   
2715 C CA  . THR B 86  ? 0.4482 0.3467 0.2639 -0.0025 0.0813  -0.0940 115 THR B CA  
2716 C C   . THR B 86  ? 0.4253 0.3295 0.2516 0.0011  0.0792  -0.0813 115 THR B C   
2717 O O   . THR B 86  ? 0.4309 0.3432 0.2585 0.0039  0.0829  -0.0776 115 THR B O   
2718 C CB  . THR B 86  ? 0.4519 0.3597 0.2520 -0.0076 0.0755  -0.0951 115 THR B CB  
2719 O OG1 . THR B 86  ? 0.4309 0.3397 0.2338 -0.0105 0.0670  -0.0888 115 THR B OG1 
2720 C CG2 . THR B 86  ? 0.4659 0.3722 0.2542 -0.0114 0.0772  -0.1089 115 THR B CG2 
2721 N N   . GLY B 87  ? 0.4045 0.3050 0.2386 0.0006  0.0735  -0.0755 116 GLY B N   
2722 C CA  . GLY B 87  ? 0.3884 0.2960 0.2295 0.0020  0.0692  -0.0646 116 GLY B CA  
2723 C C   . GLY B 87  ? 0.3863 0.3010 0.2175 -0.0027 0.0631  -0.0610 116 GLY B C   
2724 O O   . GLY B 87  ? 0.3816 0.2971 0.2007 -0.0061 0.0619  -0.0663 116 GLY B O   
2725 N N   . MET B 88  ? 0.3675 0.2873 0.2043 -0.0025 0.0591  -0.0522 117 MET B N   
2726 C CA  . MET B 88  ? 0.3678 0.2929 0.1970 -0.0058 0.0543  -0.0474 117 MET B CA  
2727 C C   . MET B 88  ? 0.3541 0.2862 0.1889 -0.0050 0.0561  -0.0407 117 MET B C   
2728 O O   . MET B 88  ? 0.3466 0.2807 0.1936 -0.0023 0.0575  -0.0386 117 MET B O   
2729 C CB  . MET B 88  ? 0.3598 0.2819 0.1907 -0.0080 0.0471  -0.0447 117 MET B CB  
2730 C CG  . MET B 88  ? 0.3705 0.2866 0.1978 -0.0103 0.0455  -0.0517 117 MET B CG  
2731 S SD  . MET B 88  ? 0.3815 0.2954 0.2120 -0.0132 0.0382  -0.0488 117 MET B SD  
2732 C CE  . MET B 88  ? 0.3823 0.3047 0.2059 -0.0140 0.0334  -0.0418 117 MET B CE  
2733 N N   . THR B 89  ? 0.3575 0.2935 0.1838 -0.0072 0.0564  -0.0372 118 THR B N   
2734 C CA  . THR B 89  ? 0.3544 0.2956 0.1870 -0.0079 0.0584  -0.0310 118 THR B CA  
2735 C C   . THR B 89  ? 0.3522 0.2927 0.1915 -0.0094 0.0521  -0.0262 118 THR B C   
2736 O O   . THR B 89  ? 0.3480 0.2842 0.1837 -0.0100 0.0464  -0.0263 118 THR B O   
2737 C CB  . THR B 89  ? 0.3642 0.3074 0.1853 -0.0097 0.0623  -0.0279 118 THR B CB  
2738 O OG1 . THR B 89  ? 0.3730 0.3131 0.1836 -0.0108 0.0566  -0.0254 118 THR B OG1 
2739 C CG2 . THR B 89  ? 0.3822 0.3272 0.1945 -0.0082 0.0689  -0.0326 118 THR B CG2 
2740 N N   . ILE B 90  ? 0.3621 0.3077 0.2110 -0.0105 0.0536  -0.0226 119 ILE B N   
2741 C CA  . ILE B 90  ? 0.3618 0.3075 0.2162 -0.0124 0.0483  -0.0190 119 ILE B CA  
2742 C C   . ILE B 90  ? 0.3582 0.2981 0.2017 -0.0144 0.0451  -0.0160 119 ILE B C   
2743 O O   . ILE B 90  ? 0.3520 0.2891 0.1957 -0.0145 0.0395  -0.0152 119 ILE B O   
2744 C CB  . ILE B 90  ? 0.3773 0.3305 0.2430 -0.0147 0.0511  -0.0171 119 ILE B CB  
2745 C CG1 . ILE B 90  ? 0.3717 0.3333 0.2506 -0.0114 0.0520  -0.0195 119 ILE B CG1 
2746 C CG2 . ILE B 90  ? 0.3713 0.3233 0.2396 -0.0179 0.0465  -0.0142 119 ILE B CG2 
2747 C CD1 . ILE B 90  ? 0.3715 0.3331 0.2559 -0.0083 0.0455  -0.0194 119 ILE B CD1 
2748 N N   . GLY B 91  ? 0.3655 0.3041 0.1987 -0.0151 0.0489  -0.0142 120 GLY B N   
2749 C CA  . GLY B 91  ? 0.3707 0.3048 0.1932 -0.0153 0.0461  -0.0104 120 GLY B CA  
2750 C C   . GLY B 91  ? 0.3644 0.2973 0.1803 -0.0137 0.0402  -0.0136 120 GLY B C   
2751 O O   . GLY B 91  ? 0.3585 0.2895 0.1731 -0.0136 0.0352  -0.0115 120 GLY B O   
2752 N N   . GLN B 92  ? 0.3650 0.2993 0.1780 -0.0126 0.0414  -0.0194 121 GLN B N   
2753 C CA  . GLN B 92  ? 0.3730 0.3065 0.1819 -0.0124 0.0365  -0.0241 121 GLN B CA  
2754 C C   . GLN B 92  ? 0.3606 0.2915 0.1801 -0.0130 0.0322  -0.0245 121 GLN B C   
2755 O O   . GLN B 92  ? 0.3653 0.2957 0.1832 -0.0138 0.0273  -0.0253 121 GLN B O   
2756 C CB  . GLN B 92  ? 0.3836 0.3178 0.1883 -0.0119 0.0399  -0.0315 121 GLN B CB  
2757 C CG  . GLN B 92  ? 0.3974 0.3353 0.1886 -0.0111 0.0437  -0.0316 121 GLN B CG  
2758 C CD  . GLN B 92  ? 0.4180 0.3564 0.2057 -0.0106 0.0484  -0.0399 121 GLN B CD  
2759 O OE1 . GLN B 92  ? 0.3967 0.3321 0.1943 -0.0100 0.0515  -0.0437 121 GLN B OE1 
2760 N NE2 . GLN B 92  ? 0.4495 0.3919 0.2223 -0.0104 0.0490  -0.0430 121 GLN B NE2 
2761 N N   . LEU B 93  ? 0.3464 0.2768 0.1766 -0.0124 0.0342  -0.0238 122 LEU B N   
2762 C CA  . LEU B 93  ? 0.3425 0.2710 0.1812 -0.0121 0.0305  -0.0229 122 LEU B CA  
2763 C C   . LEU B 93  ? 0.3283 0.2570 0.1672 -0.0134 0.0263  -0.0184 122 LEU B C   
2764 O O   . LEU B 93  ? 0.3331 0.2600 0.1732 -0.0138 0.0226  -0.0185 122 LEU B O   
2765 C CB  . LEU B 93  ? 0.3397 0.2702 0.1889 -0.0100 0.0332  -0.0225 122 LEU B CB  
2766 C CG  . LEU B 93  ? 0.3458 0.2744 0.1969 -0.0074 0.0376  -0.0272 122 LEU B CG  
2767 C CD1 . LEU B 93  ? 0.3456 0.2793 0.2076 -0.0042 0.0403  -0.0255 122 LEU B CD1 
2768 C CD2 . LEU B 93  ? 0.3561 0.2774 0.2075 -0.0069 0.0361  -0.0301 122 LEU B CD2 
2769 N N   . CYS B 94  ? 0.3437 0.2739 0.1814 -0.0144 0.0279  -0.0147 123 CYS B N   
2770 C CA  . CYS B 94  ? 0.3429 0.2716 0.1802 -0.0154 0.0251  -0.0109 123 CYS B CA  
2771 C C   . CYS B 94  ? 0.3611 0.2885 0.1905 -0.0146 0.0216  -0.0105 123 CYS B C   
2772 O O   . CYS B 94  ? 0.3641 0.2908 0.1956 -0.0146 0.0178  -0.0098 123 CYS B O   
2773 C CB  . CYS B 94  ? 0.3451 0.2732 0.1821 -0.0169 0.0291  -0.0074 123 CYS B CB  
2774 S SG  . CYS B 94  ? 0.3678 0.3010 0.2173 -0.0190 0.0323  -0.0085 123 CYS B SG  
2775 N N   . ASP B 95  ? 0.3739 0.3026 0.1943 -0.0137 0.0227  -0.0113 124 ASP B N   
2776 C CA  . ASP B 95  ? 0.3854 0.3166 0.1983 -0.0125 0.0188  -0.0115 124 ASP B CA  
2777 C C   . ASP B 95  ? 0.3640 0.2965 0.1816 -0.0137 0.0148  -0.0162 124 ASP B C   
2778 O O   . ASP B 95  ? 0.3680 0.3021 0.1868 -0.0134 0.0110  -0.0150 124 ASP B O   
2779 C CB  . ASP B 95  ? 0.4058 0.3402 0.2076 -0.0112 0.0208  -0.0125 124 ASP B CB  
2780 C CG  . ASP B 95  ? 0.4372 0.3776 0.2301 -0.0094 0.0161  -0.0131 124 ASP B CG  
2781 O OD1 . ASP B 95  ? 0.4592 0.4031 0.2555 -0.0108 0.0118  -0.0180 124 ASP B OD1 
2782 O OD2 . ASP B 95  ? 0.4817 0.4242 0.2641 -0.0066 0.0172  -0.0089 124 ASP B OD2 
2783 N N   . ALA B 96  ? 0.3498 0.2808 0.1712 -0.0150 0.0166  -0.0212 125 ALA B N   
2784 C CA  . ALA B 96  ? 0.3323 0.2624 0.1581 -0.0168 0.0145  -0.0258 125 ALA B CA  
2785 C C   . ALA B 96  ? 0.3319 0.2596 0.1656 -0.0169 0.0128  -0.0225 125 ALA B C   
2786 O O   . ALA B 96  ? 0.3171 0.2458 0.1533 -0.0184 0.0103  -0.0238 125 ALA B O   
2787 C CB  . ALA B 96  ? 0.3406 0.2670 0.1688 -0.0173 0.0183  -0.0309 125 ALA B CB  
2788 N N   . ALA B 97  ? 0.3224 0.2483 0.1601 -0.0157 0.0145  -0.0188 126 ALA B N   
2789 C CA  . ALA B 97  ? 0.3273 0.2519 0.1709 -0.0155 0.0131  -0.0160 126 ALA B CA  
2790 C C   . ALA B 97  ? 0.3442 0.2704 0.1861 -0.0157 0.0100  -0.0136 126 ALA B C   
2791 O O   . ALA B 97  ? 0.3283 0.2545 0.1733 -0.0162 0.0084  -0.0133 126 ALA B O   
2792 C CB  . ALA B 97  ? 0.3173 0.2426 0.1652 -0.0144 0.0149  -0.0138 126 ALA B CB  
2793 N N   . ILE B 98  ? 0.3556 0.2830 0.1926 -0.0149 0.0101  -0.0114 127 ILE B N   
2794 C CA  . ILE B 98  ? 0.3715 0.2997 0.2071 -0.0138 0.0079  -0.0086 127 ILE B CA  
2795 C C   . ILE B 98  ? 0.3884 0.3217 0.2215 -0.0133 0.0048  -0.0105 127 ILE B C   
2796 O O   . ILE B 98  ? 0.3734 0.3089 0.2100 -0.0132 0.0026  -0.0104 127 ILE B O   
2797 C CB  . ILE B 98  ? 0.3879 0.3134 0.2197 -0.0125 0.0100  -0.0046 127 ILE B CB  
2798 C CG1 . ILE B 98  ? 0.4139 0.3364 0.2510 -0.0142 0.0123  -0.0041 127 ILE B CG1 
2799 C CG2 . ILE B 98  ? 0.3957 0.3214 0.2245 -0.0097 0.0083  -0.0014 127 ILE B CG2 
2800 C CD1 . ILE B 98  ? 0.4601 0.3785 0.2955 -0.0146 0.0161  -0.0011 127 ILE B CD1 
2801 N N   . ARG B 99  ? 0.3785 0.3152 0.2060 -0.0132 0.0045  -0.0128 128 ARG B N   
2802 C CA  . ARG B 99  ? 0.4029 0.3476 0.2270 -0.0123 0.0008  -0.0144 128 ARG B CA  
2803 C C   . ARG B 99  ? 0.3956 0.3441 0.2250 -0.0160 -0.0009 -0.0209 128 ARG B C   
2804 O O   . ARG B 99  ? 0.3984 0.3552 0.2294 -0.0162 -0.0045 -0.0228 128 ARG B O   
2805 C CB  . ARG B 99  ? 0.4236 0.3718 0.2374 -0.0103 0.0010  -0.0141 128 ARG B CB  
2806 C CG  . ARG B 99  ? 0.4537 0.3986 0.2612 -0.0062 0.0031  -0.0065 128 ARG B CG  
2807 C CD  . ARG B 99  ? 0.4789 0.4284 0.2742 -0.0036 0.0034  -0.0054 128 ARG B CD  
2808 N NE  . ARG B 99  ? 0.5160 0.4777 0.3074 -0.0027 -0.0021 -0.0096 128 ARG B NE  
2809 C CZ  . ARG B 99  ? 0.5493 0.5171 0.3381 -0.0058 -0.0034 -0.0176 128 ARG B CZ  
2810 N NH1 . ARG B 99  ? 0.5514 0.5139 0.3383 -0.0084 0.0011  -0.0214 128 ARG B NH1 
2811 N NH2 . ARG B 99  ? 0.5662 0.5462 0.3550 -0.0063 -0.0090 -0.0227 128 ARG B NH2 
2812 N N   . TYR B 100 ? 0.3883 0.3309 0.2212 -0.0189 0.0021  -0.0244 129 TYR B N   
2813 C CA  . TYR B 100 ? 0.4085 0.3512 0.2473 -0.0229 0.0023  -0.0302 129 TYR B CA  
2814 C C   . TYR B 100 ? 0.4105 0.3452 0.2563 -0.0238 0.0050  -0.0280 129 TYR B C   
2815 O O   . TYR B 100 ? 0.4219 0.3534 0.2727 -0.0270 0.0070  -0.0316 129 TYR B O   
2816 C CB  . TYR B 100 ? 0.4374 0.3785 0.2730 -0.0252 0.0043  -0.0370 129 TYR B CB  
2817 C CG  . TYR B 100 ? 0.4693 0.4211 0.2974 -0.0251 0.0007  -0.0407 129 TYR B CG  
2818 C CD1 . TYR B 100 ? 0.5012 0.4624 0.3322 -0.0283 -0.0029 -0.0463 129 TYR B CD1 
2819 C CD2 . TYR B 100 ? 0.4978 0.4514 0.3160 -0.0217 0.0011  -0.0384 129 TYR B CD2 
2820 C CE1 . TYR B 100 ? 0.5211 0.4949 0.3450 -0.0278 -0.0072 -0.0500 129 TYR B CE1 
2821 C CE2 . TYR B 100 ? 0.5096 0.4740 0.3192 -0.0208 -0.0024 -0.0411 129 TYR B CE2 
2822 C CZ  . TYR B 100 ? 0.5224 0.4977 0.3347 -0.0235 -0.0071 -0.0469 129 TYR B CZ  
2823 O OH  . TYR B 100 ? 0.5714 0.5602 0.3753 -0.0222 -0.0117 -0.0499 129 TYR B OH  
2824 N N   . SER B 101 ? 0.3936 0.3253 0.2396 -0.0209 0.0055  -0.0222 130 SER B N   
2825 C CA  . SER B 101 ? 0.4216 0.3479 0.2725 -0.0207 0.0076  -0.0196 130 SER B CA  
2826 C C   . SER B 101 ? 0.4141 0.3337 0.2672 -0.0214 0.0112  -0.0220 130 SER B C   
2827 O O   . SER B 101 ? 0.4141 0.3288 0.2713 -0.0219 0.0134  -0.0210 130 SER B O   
2828 C CB  . SER B 101 ? 0.4177 0.3460 0.2725 -0.0221 0.0067  -0.0189 130 SER B CB  
2829 O OG  . SER B 101 ? 0.3943 0.3197 0.2505 -0.0204 0.0076  -0.0145 130 SER B OG  
2830 N N   . ASP B 102 ? 0.4001 0.3189 0.2502 -0.0207 0.0126  -0.0244 131 ASP B N   
2831 C CA  . ASP B 102 ? 0.3968 0.3090 0.2490 -0.0207 0.0167  -0.0276 131 ASP B CA  
2832 C C   . ASP B 102 ? 0.3787 0.2865 0.2351 -0.0170 0.0187  -0.0224 131 ASP B C   
2833 O O   . ASP B 102 ? 0.3664 0.2780 0.2225 -0.0144 0.0177  -0.0190 131 ASP B O   
2834 C CB  . ASP B 102 ? 0.3828 0.2967 0.2301 -0.0204 0.0179  -0.0316 131 ASP B CB  
2835 C CG  . ASP B 102 ? 0.3852 0.2919 0.2344 -0.0203 0.0228  -0.0364 131 ASP B CG  
2836 O OD1 . ASP B 102 ? 0.3659 0.2674 0.2199 -0.0168 0.0258  -0.0331 131 ASP B OD1 
2837 O OD2 . ASP B 102 ? 0.4022 0.3092 0.2481 -0.0233 0.0235  -0.0437 131 ASP B OD2 
2838 N N   . GLY B 103 ? 0.3669 0.2673 0.2274 -0.0168 0.0218  -0.0218 132 GLY B N   
2839 C CA  . GLY B 103 ? 0.3545 0.2520 0.2180 -0.0122 0.0232  -0.0157 132 GLY B CA  
2840 C C   . GLY B 103 ? 0.3447 0.2419 0.2101 -0.0076 0.0255  -0.0153 132 GLY B C   
2841 O O   . GLY B 103 ? 0.3269 0.2299 0.1939 -0.0038 0.0239  -0.0110 132 GLY B O   
2842 N N   . THR B 104 ? 0.3458 0.2371 0.2115 -0.0080 0.0295  -0.0205 133 THR B N   
2843 C CA  . THR B 104 ? 0.3491 0.2404 0.2174 -0.0032 0.0326  -0.0207 133 THR B CA  
2844 C C   . THR B 104 ? 0.3434 0.2458 0.2101 -0.0031 0.0300  -0.0206 133 THR B C   
2845 O O   . THR B 104 ? 0.3366 0.2442 0.2076 0.0012  0.0307  -0.0179 133 THR B O   
2846 C CB  . THR B 104 ? 0.3607 0.2433 0.2289 -0.0044 0.0380  -0.0278 133 THR B CB  
2847 O OG1 . THR B 104 ? 0.3744 0.2457 0.2452 -0.0054 0.0410  -0.0275 133 THR B OG1 
2848 C CG2 . THR B 104 ? 0.3696 0.2521 0.2412 0.0014  0.0422  -0.0281 133 THR B CG2 
2849 N N   . ALA B 105 ? 0.3352 0.2415 0.1961 -0.0076 0.0275  -0.0233 134 ALA B N   
2850 C CA  . ALA B 105 ? 0.3358 0.2501 0.1944 -0.0079 0.0262  -0.0224 134 ALA B CA  
2851 C C   . ALA B 105 ? 0.3387 0.2589 0.2017 -0.0062 0.0235  -0.0169 134 ALA B C   
2852 O O   . ALA B 105 ? 0.3276 0.2541 0.1944 -0.0047 0.0245  -0.0159 134 ALA B O   
2853 C CB  . ALA B 105 ? 0.3384 0.2548 0.1895 -0.0118 0.0237  -0.0244 134 ALA B CB  
2854 N N   . ALA B 106 ? 0.3227 0.2418 0.1859 -0.0068 0.0204  -0.0142 135 ALA B N   
2855 C CA  . ALA B 106 ? 0.3172 0.2424 0.1832 -0.0057 0.0176  -0.0104 135 ALA B CA  
2856 C C   . ALA B 106 ? 0.3231 0.2519 0.1955 -0.0006 0.0185  -0.0080 135 ALA B C   
2857 O O   . ALA B 106 ? 0.3342 0.2721 0.2106 0.0003  0.0171  -0.0071 135 ALA B O   
2858 C CB  . ALA B 106 ? 0.3239 0.2470 0.1875 -0.0070 0.0149  -0.0084 135 ALA B CB  
2859 N N   . ASN B 107 ? 0.3135 0.2355 0.1874 0.0030  0.0213  -0.0071 136 ASN B N   
2860 C CA  . ASN B 107 ? 0.3190 0.2445 0.1989 0.0096  0.0224  -0.0037 136 ASN B CA  
2861 C C   . ASN B 107 ? 0.3149 0.2479 0.2001 0.0112  0.0245  -0.0061 136 ASN B C   
2862 O O   . ASN B 107 ? 0.3091 0.2529 0.2008 0.0152  0.0231  -0.0038 136 ASN B O   
2863 C CB  . ASN B 107 ? 0.3214 0.2353 0.2020 0.0137  0.0265  -0.0017 136 ASN B CB  
2864 C CG  . ASN B 107 ? 0.3437 0.2524 0.2209 0.0136  0.0252  0.0029  136 ASN B CG  
2865 O OD1 . ASN B 107 ? 0.3431 0.2582 0.2175 0.0114  0.0209  0.0046  136 ASN B OD1 
2866 N ND2 . ASN B 107 ? 0.3562 0.2521 0.2338 0.0156  0.0300  0.0045  136 ASN B ND2 
2867 N N   . LEU B 108 ? 0.3178 0.2468 0.2003 0.0081  0.0278  -0.0110 137 LEU B N   
2868 C CA  . LEU B 108 ? 0.3124 0.2480 0.1992 0.0093  0.0311  -0.0134 137 LEU B CA  
2869 C C   . LEU B 108 ? 0.3188 0.2660 0.2078 0.0058  0.0285  -0.0129 137 LEU B C   
2870 O O   . LEU B 108 ? 0.3080 0.2659 0.2050 0.0076  0.0298  -0.0130 137 LEU B O   
2871 C CB  . LEU B 108 ? 0.3212 0.2495 0.2024 0.0070  0.0356  -0.0188 137 LEU B CB  
2872 C CG  . LEU B 108 ? 0.3318 0.2483 0.2126 0.0099  0.0398  -0.0214 137 LEU B CG  
2873 C CD1 . LEU B 108 ? 0.3309 0.2416 0.2040 0.0057  0.0428  -0.0283 137 LEU B CD1 
2874 C CD2 . LEU B 108 ? 0.3377 0.2561 0.2274 0.0175  0.0439  -0.0200 137 LEU B CD2 
2875 N N   . LEU B 109 ? 0.3099 0.2552 0.1929 0.0007  0.0254  -0.0127 138 LEU B N   
2876 C CA  . LEU B 109 ? 0.3085 0.2619 0.1937 -0.0032 0.0238  -0.0126 138 LEU B CA  
2877 C C   . LEU B 109 ? 0.3099 0.2737 0.2026 -0.0011 0.0200  -0.0107 138 LEU B C   
2878 O O   . LEU B 109 ? 0.3032 0.2783 0.2034 -0.0025 0.0202  -0.0120 138 LEU B O   
2879 C CB  . LEU B 109 ? 0.3185 0.2656 0.1955 -0.0078 0.0220  -0.0124 138 LEU B CB  
2880 C CG  . LEU B 109 ? 0.3237 0.2646 0.1927 -0.0099 0.0250  -0.0141 138 LEU B CG  
2881 C CD1 . LEU B 109 ? 0.3328 0.2684 0.1943 -0.0124 0.0221  -0.0131 138 LEU B CD1 
2882 C CD2 . LEU B 109 ? 0.3295 0.2747 0.1998 -0.0119 0.0293  -0.0146 138 LEU B CD2 
2883 N N   . LEU B 110 ? 0.3173 0.2787 0.2083 0.0022  0.0168  -0.0080 139 LEU B N   
2884 C CA  . LEU B 110 ? 0.3154 0.2880 0.2118 0.0056  0.0128  -0.0058 139 LEU B CA  
2885 C C   . LEU B 110 ? 0.3215 0.3056 0.2281 0.0106  0.0143  -0.0057 139 LEU B C   
2886 O O   . LEU B 110 ? 0.3247 0.3240 0.2388 0.0100  0.0116  -0.0069 139 LEU B O   
2887 C CB  . LEU B 110 ? 0.3148 0.2809 0.2060 0.0096  0.0108  -0.0016 139 LEU B CB  
2888 C CG  . LEU B 110 ? 0.3216 0.2817 0.2050 0.0051  0.0084  -0.0016 139 LEU B CG  
2889 C CD1 . LEU B 110 ? 0.3215 0.2729 0.2000 0.0089  0.0088  0.0029  139 LEU B CD1 
2890 C CD2 . LEU B 110 ? 0.3153 0.2865 0.1998 0.0023  0.0042  -0.0032 139 LEU B CD2 
2891 N N   . ALA B 111 ? 0.3410 0.3186 0.2488 0.0155  0.0187  -0.0049 140 ALA B N   
2892 C CA  . ALA B 111 ? 0.3473 0.3352 0.2654 0.0215  0.0211  -0.0048 140 ALA B CA  
2893 C C   . ALA B 111 ? 0.3476 0.3464 0.2726 0.0165  0.0234  -0.0091 140 ALA B C   
2894 O O   . ALA B 111 ? 0.3526 0.3678 0.2890 0.0194  0.0231  -0.0096 140 ALA B O   
2895 C CB  . ALA B 111 ? 0.3665 0.3421 0.2836 0.0271  0.0267  -0.0041 140 ALA B CB  
2896 N N   . ASP B 112 ? 0.3408 0.3311 0.2591 0.0095  0.0263  -0.0120 141 ASP B N   
2897 C CA  . ASP B 112 ? 0.3511 0.3495 0.2745 0.0044  0.0299  -0.0151 141 ASP B CA  
2898 C C   . ASP B 112 ? 0.3555 0.3668 0.2855 -0.0003 0.0256  -0.0162 141 ASP B C   
2899 O O   . ASP B 112 ? 0.3414 0.3669 0.2825 -0.0024 0.0273  -0.0186 141 ASP B O   
2900 C CB  . ASP B 112 ? 0.3541 0.3402 0.2670 -0.0012 0.0338  -0.0166 141 ASP B CB  
2901 C CG  . ASP B 112 ? 0.3644 0.3567 0.2816 -0.0059 0.0394  -0.0186 141 ASP B CG  
2902 O OD1 . ASP B 112 ? 0.3918 0.3901 0.3153 -0.0027 0.0443  -0.0200 141 ASP B OD1 
2903 O OD2 . ASP B 112 ? 0.3621 0.3530 0.2768 -0.0125 0.0396  -0.0186 141 ASP B OD2 
2904 N N   . LEU B 113 ? 0.3437 0.3505 0.2673 -0.0022 0.0203  -0.0151 142 LEU B N   
2905 C CA  . LEU B 113 ? 0.3506 0.3671 0.2784 -0.0076 0.0166  -0.0175 142 LEU B CA  
2906 C C   . LEU B 113 ? 0.3492 0.3857 0.2881 -0.0033 0.0120  -0.0180 142 LEU B C   
2907 O O   . LEU B 113 ? 0.3505 0.4021 0.2998 -0.0079 0.0115  -0.0221 142 LEU B O   
2908 C CB  . LEU B 113 ? 0.3332 0.3392 0.2503 -0.0101 0.0129  -0.0167 142 LEU B CB  
2909 C CG  . LEU B 113 ? 0.3338 0.3464 0.2537 -0.0169 0.0103  -0.0207 142 LEU B CG  
2910 C CD1 . LEU B 113 ? 0.3389 0.3474 0.2611 -0.0247 0.0159  -0.0235 142 LEU B CD1 
2911 C CD2 . LEU B 113 ? 0.3374 0.3408 0.2471 -0.0174 0.0067  -0.0197 142 LEU B CD2 
2912 N N   . GLY B 114 ? 0.3597 0.3965 0.2965 0.0054  0.0089  -0.0136 143 GLY B N   
2913 C CA  . GLY B 114 ? 0.3786 0.4343 0.3226 0.0107  0.0029  -0.0127 143 GLY B CA  
2914 C C   . GLY B 114 ? 0.3922 0.4545 0.3431 0.0216  0.0040  -0.0084 143 GLY B C   
2915 O O   . GLY B 114 ? 0.3798 0.4581 0.3358 0.0283  -0.0012 -0.0060 143 GLY B O   
2916 N N   . GLY B 115 ? 0.4086 0.4591 0.3591 0.0240  0.0107  -0.0076 144 GLY B N   
2917 C CA  . GLY B 115 ? 0.4429 0.4954 0.3990 0.0351  0.0131  -0.0035 144 GLY B CA  
2918 C C   . GLY B 115 ? 0.4746 0.5114 0.4206 0.0420  0.0123  0.0029  144 GLY B C   
2919 O O   . GLY B 115 ? 0.5011 0.5281 0.4364 0.0382  0.0095  0.0041  144 GLY B O   
2920 N N   . PRO B 116 ? 0.5866 0.6192 0.5359 0.0524  0.0159  0.0072  145 PRO B N   
2921 C CA  . PRO B 116 ? 0.6016 0.6200 0.5430 0.0597  0.0160  0.0143  145 PRO B CA  
2922 C C   . PRO B 116 ? 0.5987 0.6338 0.5406 0.0648  0.0081  0.0194  145 PRO B C   
2923 O O   . PRO B 116 ? 0.6609 0.7185 0.6136 0.0702  0.0045  0.0199  145 PRO B O   
2924 C CB  . PRO B 116 ? 0.6490 0.6607 0.5967 0.0694  0.0228  0.0166  145 PRO B CB  
2925 C CG  . PRO B 116 ? 0.6556 0.6900 0.6179 0.0714  0.0227  0.0131  145 PRO B CG  
2926 C CD  . PRO B 116 ? 0.6262 0.6673 0.5877 0.0579  0.0209  0.0057  145 PRO B CD  
2927 N N   . GLY B 117 A 0.5402 0.5664 0.4704 0.0625  0.0051  0.0225  145 GLY B N   
2928 C CA  . GLY B 117 A 0.5173 0.5584 0.4449 0.0674  -0.0021 0.0273  145 GLY B CA  
2929 C C   . GLY B 117 A 0.4676 0.5215 0.3932 0.0571  -0.0083 0.0207  145 GLY B C   
2930 O O   . GLY B 117 A 0.4792 0.5372 0.3967 0.0577  -0.0132 0.0232  145 GLY B O   
2931 N N   . GLY B 118 B 0.4166 0.4755 0.3491 0.0479  -0.0072 0.0123  145 GLY B N   
2932 C CA  . GLY B 118 B 0.3990 0.4711 0.3326 0.0384  -0.0121 0.0053  145 GLY B CA  
2933 C C   . GLY B 118 B 0.3763 0.4313 0.3016 0.0273  -0.0094 0.0007  145 GLY B C   
2934 O O   . GLY B 118 B 0.3524 0.4140 0.2778 0.0192  -0.0122 -0.0052 145 GLY B O   
2935 N N   . GLY B 119 C 0.3697 0.4029 0.2880 0.0270  -0.0040 0.0030  145 GLY B N   
2936 C CA  . GLY B 119 C 0.3419 0.3608 0.2537 0.0178  -0.0013 -0.0009 145 GLY B CA  
2937 C C   . GLY B 119 C 0.3392 0.3557 0.2422 0.0135  -0.0051 -0.0017 145 GLY B C   
2938 O O   . GLY B 119 C 0.3269 0.3429 0.2293 0.0055  -0.0053 -0.0069 145 GLY B O   
2939 N N   . THR B 120 D 0.3405 0.3543 0.2364 0.0191  -0.0073 0.0038  145 THR B N   
2940 C CA  . THR B 120 D 0.3354 0.3463 0.2221 0.0156  -0.0099 0.0032  145 THR B CA  
2941 C C   . THR B 120 D 0.3287 0.3579 0.2184 0.0123  -0.0153 -0.0022 145 THR B C   
2942 O O   . THR B 120 D 0.3356 0.3619 0.2215 0.0053  -0.0158 -0.0072 145 THR B O   
2943 C CB  . THR B 120 D 0.3493 0.3525 0.2274 0.0221  -0.0095 0.0107  145 THR B CB  
2944 O OG1 . THR B 120 D 0.3658 0.3820 0.2464 0.0310  -0.0125 0.0158  145 THR B OG1 
2945 C CG2 . THR B 120 D 0.3673 0.3515 0.2437 0.0232  -0.0035 0.0141  145 THR B CG2 
2946 N N   . ALA B 121 ? 0.3219 0.3700 0.2194 0.0169  -0.0190 -0.0021 146 ALA B N   
2947 C CA  . ALA B 121 ? 0.3291 0.3977 0.2321 0.0127  -0.0243 -0.0091 146 ALA B CA  
2948 C C   . ALA B 121 ? 0.3203 0.3869 0.2305 0.0020  -0.0212 -0.0175 146 ALA B C   
2949 O O   . ALA B 121 ? 0.3084 0.3778 0.2175 -0.0056 -0.0228 -0.0243 146 ALA B O   
2950 C CB  . ALA B 121 ? 0.3304 0.4215 0.2425 0.0203  -0.0286 -0.0072 146 ALA B CB  
2951 N N   . ALA B 122 ? 0.3242 0.3850 0.2415 0.0012  -0.0160 -0.0170 147 ALA B N   
2952 C CA  . ALA B 122 ? 0.3191 0.3773 0.2426 -0.0083 -0.0120 -0.0234 147 ALA B CA  
2953 C C   . ALA B 122 ? 0.3112 0.3499 0.2248 -0.0143 -0.0091 -0.0246 147 ALA B C   
2954 O O   . ALA B 122 ? 0.3159 0.3533 0.2314 -0.0226 -0.0076 -0.0305 147 ALA B O   
2955 C CB  . ALA B 122 ? 0.3273 0.3835 0.2583 -0.0068 -0.0067 -0.0218 147 ALA B CB  
2956 N N   . PHE B 123 ? 0.3084 0.3318 0.2120 -0.0101 -0.0078 -0.0189 148 PHE B N   
2957 C CA  . PHE B 123 ? 0.3144 0.3216 0.2094 -0.0144 -0.0055 -0.0194 148 PHE B CA  
2958 C C   . PHE B 123 ? 0.3202 0.3319 0.2117 -0.0180 -0.0090 -0.0239 148 PHE B C   
2959 O O   . PHE B 123 ? 0.3357 0.3406 0.2264 -0.0244 -0.0067 -0.0284 148 PHE B O   
2960 C CB  . PHE B 123 ? 0.3074 0.3010 0.1939 -0.0095 -0.0042 -0.0134 148 PHE B CB  
2961 C CG  . PHE B 123 ? 0.3274 0.3088 0.2058 -0.0127 -0.0032 -0.0139 148 PHE B CG  
2962 C CD1 . PHE B 123 ? 0.3410 0.3118 0.2182 -0.0167 0.0005  -0.0151 148 PHE B CD1 
2963 C CD2 . PHE B 123 ? 0.3507 0.3323 0.2226 -0.0112 -0.0058 -0.0131 148 PHE B CD2 
2964 C CE1 . PHE B 123 ? 0.3449 0.3062 0.2158 -0.0186 0.0012  -0.0153 148 PHE B CE1 
2965 C CE2 . PHE B 123 ? 0.3526 0.3244 0.2184 -0.0137 -0.0044 -0.0138 148 PHE B CE2 
2966 C CZ  . PHE B 123 ? 0.3445 0.3064 0.2105 -0.0171 -0.0011 -0.0150 148 PHE B CZ  
2967 N N   . THR B 124 ? 0.3392 0.3619 0.2279 -0.0132 -0.0139 -0.0226 149 THR B N   
2968 C CA  . THR B 124 ? 0.3392 0.3673 0.2226 -0.0159 -0.0173 -0.0272 149 THR B CA  
2969 C C   . THR B 124 ? 0.3419 0.3806 0.2340 -0.0239 -0.0180 -0.0367 149 THR B C   
2970 O O   . THR B 124 ? 0.3324 0.3663 0.2219 -0.0300 -0.0170 -0.0428 149 THR B O   
2971 C CB  . THR B 124 ? 0.3406 0.3804 0.2185 -0.0083 -0.0225 -0.0230 149 THR B CB  
2972 O OG1 . THR B 124 ? 0.3347 0.3619 0.2053 -0.0019 -0.0202 -0.0142 149 THR B OG1 
2973 C CG2 . THR B 124 ? 0.3474 0.3948 0.2184 -0.0108 -0.0261 -0.0285 149 THR B CG2 
2974 N N   . GLY B 125 ? 0.3436 0.3961 0.2473 -0.0242 -0.0188 -0.0382 150 GLY B N   
2975 C CA  . GLY B 125 ? 0.3483 0.4121 0.2631 -0.0328 -0.0186 -0.0474 150 GLY B CA  
2976 C C   . GLY B 125 ? 0.3529 0.3990 0.2688 -0.0412 -0.0114 -0.0507 150 GLY B C   
2977 O O   . GLY B 125 ? 0.3608 0.4081 0.2803 -0.0495 -0.0103 -0.0591 150 GLY B O   
2978 N N   . TYR B 126 ? 0.3642 0.3935 0.2765 -0.0388 -0.0064 -0.0441 151 TYR B N   
2979 C CA  . TYR B 126 ? 0.3722 0.3845 0.2838 -0.0450 0.0004  -0.0453 151 TYR B CA  
2980 C C   . TYR B 126 ? 0.3897 0.3912 0.2932 -0.0475 0.0005  -0.0484 151 TYR B C   
2981 O O   . TYR B 126 ? 0.4041 0.3987 0.3105 -0.0548 0.0047  -0.0540 151 TYR B O   
2982 C CB  . TYR B 126 ? 0.3642 0.3636 0.2720 -0.0408 0.0047  -0.0375 151 TYR B CB  
2983 C CG  . TYR B 126 ? 0.3570 0.3396 0.2626 -0.0457 0.0115  -0.0372 151 TYR B CG  
2984 C CD1 . TYR B 126 ? 0.3694 0.3531 0.2839 -0.0529 0.0168  -0.0409 151 TYR B CD1 
2985 C CD2 . TYR B 126 ? 0.3528 0.3195 0.2481 -0.0430 0.0129  -0.0329 151 TYR B CD2 
2986 C CE1 . TYR B 126 ? 0.3786 0.3456 0.2901 -0.0566 0.0238  -0.0393 151 TYR B CE1 
2987 C CE2 . TYR B 126 ? 0.3729 0.3250 0.2656 -0.0459 0.0189  -0.0314 151 TYR B CE2 
2988 C CZ  . TYR B 126 ? 0.3770 0.3283 0.2772 -0.0524 0.0246  -0.0341 151 TYR B CZ  
2989 O OH  . TYR B 126 ? 0.4213 0.3564 0.3177 -0.0543 0.0312  -0.0312 151 TYR B OH  
2990 N N   . LEU B 127 ? 0.3859 0.3851 0.2795 -0.0415 -0.0031 -0.0448 152 LEU B N   
2991 C CA  . LEU B 127 ? 0.3946 0.3858 0.2807 -0.0431 -0.0030 -0.0482 152 LEU B CA  
2992 C C   . LEU B 127 ? 0.3974 0.4002 0.2876 -0.0495 -0.0052 -0.0587 152 LEU B C   
2993 O O   . LEU B 127 ? 0.4207 0.4140 0.3100 -0.0549 -0.0017 -0.0647 152 LEU B O   
2994 C CB  . LEU B 127 ? 0.3967 0.3867 0.2727 -0.0358 -0.0061 -0.0426 152 LEU B CB  
2995 C CG  . LEU B 127 ? 0.3826 0.3614 0.2549 -0.0306 -0.0039 -0.0338 152 LEU B CG  
2996 C CD1 . LEU B 127 ? 0.3751 0.3525 0.2387 -0.0251 -0.0060 -0.0296 152 LEU B CD1 
2997 C CD2 . LEU B 127 ? 0.3961 0.3591 0.2680 -0.0333 0.0015  -0.0331 152 LEU B CD2 
2998 N N   . ARG B 128 ? 0.3719 0.3955 0.2671 -0.0489 -0.0108 -0.0615 153 ARG B N   
2999 C CA  . ARG B 128 ? 0.3834 0.4216 0.2833 -0.0556 -0.0138 -0.0729 153 ARG B CA  
3000 C C   . ARG B 128 ? 0.3901 0.4226 0.3009 -0.0662 -0.0077 -0.0806 153 ARG B C   
3001 O O   . ARG B 128 ? 0.3769 0.4094 0.2893 -0.0738 -0.0066 -0.0910 153 ARG B O   
3002 C CB  . ARG B 128 ? 0.3734 0.4383 0.2784 -0.0523 -0.0214 -0.0739 153 ARG B CB  
3003 C CG  . ARG B 128 ? 0.3737 0.4441 0.2673 -0.0416 -0.0268 -0.0660 153 ARG B CG  
3004 C CD  . ARG B 128 ? 0.3689 0.4431 0.2510 -0.0417 -0.0302 -0.0711 153 ARG B CD  
3005 N NE  . ARG B 128 ? 0.3513 0.4298 0.2224 -0.0311 -0.0342 -0.0616 153 ARG B NE  
3006 C CZ  . ARG B 128 ? 0.3572 0.4192 0.2182 -0.0259 -0.0310 -0.0533 153 ARG B CZ  
3007 N NH1 . ARG B 128 ? 0.3643 0.4053 0.2239 -0.0293 -0.0247 -0.0531 153 ARG B NH1 
3008 N NH2 . ARG B 128 ? 0.3627 0.4290 0.2155 -0.0167 -0.0337 -0.0442 153 ARG B NH2 
3009 N N   . SER B 129 ? 0.3836 0.4113 0.3020 -0.0668 -0.0031 -0.0756 154 SER B N   
3010 C CA  . SER B 129 ? 0.3875 0.4081 0.3161 -0.0765 0.0043  -0.0807 154 SER B CA  
3011 C C   . SER B 129 ? 0.3985 0.3937 0.3204 -0.0795 0.0113  -0.0810 154 SER B C   
3012 O O   . SER B 129 ? 0.4107 0.3980 0.3396 -0.0884 0.0178  -0.0873 154 SER B O   
3013 C CB  . SER B 129 ? 0.3719 0.3932 0.3080 -0.0754 0.0082  -0.0742 154 SER B CB  
3014 O OG  . SER B 129 ? 0.3564 0.3573 0.2835 -0.0701 0.0128  -0.0643 154 SER B OG  
3015 N N   . LEU B 130 ? 0.3954 0.3779 0.3048 -0.0719 0.0107  -0.0740 155 LEU B N   
3016 C CA  . LEU B 130 ? 0.4265 0.3869 0.3294 -0.0725 0.0166  -0.0735 155 LEU B CA  
3017 C C   . LEU B 130 ? 0.4555 0.4163 0.3526 -0.0736 0.0142  -0.0814 155 LEU B C   
3018 O O   . LEU B 130 ? 0.4944 0.4382 0.3849 -0.0716 0.0183  -0.0802 155 LEU B O   
3019 C CB  . LEU B 130 ? 0.4290 0.3768 0.3231 -0.0638 0.0176  -0.0618 155 LEU B CB  
3020 C CG  . LEU B 130 ? 0.4421 0.3875 0.3392 -0.0621 0.0205  -0.0540 155 LEU B CG  
3021 C CD1 . LEU B 130 ? 0.4375 0.3743 0.3251 -0.0535 0.0197  -0.0443 155 LEU B CD1 
3022 C CD2 . LEU B 130 ? 0.4546 0.3883 0.3578 -0.0689 0.0291  -0.0554 155 LEU B CD2 
3023 N N   . GLY B 131 ? 0.4473 0.4283 0.3463 -0.0759 0.0077  -0.0894 156 GLY B N   
3024 C CA  . GLY B 131 ? 0.4436 0.4268 0.3365 -0.0779 0.0058  -0.0986 156 GLY B CA  
3025 C C   . GLY B 131 ? 0.4428 0.4282 0.3226 -0.0684 0.0011  -0.0926 156 GLY B C   
3026 O O   . GLY B 131 ? 0.4382 0.4240 0.3107 -0.0687 0.0002  -0.0991 156 GLY B O   
3027 N N   . ASP B 132 ? 0.4153 0.4015 0.2920 -0.0603 -0.0012 -0.0806 157 ASP B N   
3028 C CA  . ASP B 132 ? 0.4044 0.3923 0.2701 -0.0520 -0.0046 -0.0742 157 ASP B CA  
3029 C C   . ASP B 132 ? 0.3959 0.4064 0.2598 -0.0490 -0.0124 -0.0747 157 ASP B C   
3030 O O   . ASP B 132 ? 0.3804 0.4000 0.2489 -0.0457 -0.0153 -0.0688 157 ASP B O   
3031 C CB  . ASP B 132 ? 0.3946 0.3711 0.2582 -0.0456 -0.0024 -0.0622 157 ASP B CB  
3032 C CG  . ASP B 132 ? 0.3983 0.3767 0.2524 -0.0378 -0.0052 -0.0550 157 ASP B CG  
3033 O OD1 . ASP B 132 ? 0.3934 0.3821 0.2410 -0.0364 -0.0087 -0.0582 157 ASP B OD1 
3034 O OD2 . ASP B 132 ? 0.3964 0.3660 0.2494 -0.0335 -0.0034 -0.0467 157 ASP B OD2 
3035 N N   . THR B 133 ? 0.4125 0.4322 0.2690 -0.0495 -0.0156 -0.0816 158 THR B N   
3036 C CA  . THR B 133 ? 0.4174 0.4604 0.2706 -0.0461 -0.0234 -0.0823 158 THR B CA  
3037 C C   . THR B 133 ? 0.4126 0.4556 0.2529 -0.0365 -0.0252 -0.0724 158 THR B C   
3038 O O   . THR B 133 ? 0.4147 0.4751 0.2489 -0.0320 -0.0311 -0.0712 158 THR B O   
3039 C CB  . THR B 133 ? 0.4442 0.5006 0.2968 -0.0531 -0.0263 -0.0969 158 THR B CB  
3040 O OG1 . THR B 133 ? 0.4466 0.4915 0.2883 -0.0530 -0.0228 -0.1005 158 THR B OG1 
3041 C CG2 . THR B 133 ? 0.4499 0.5058 0.3166 -0.0639 -0.0235 -0.1075 158 THR B CG2 
3042 N N   . VAL B 134 ? 0.4024 0.4266 0.2386 -0.0334 -0.0199 -0.0652 159 VAL B N   
3043 C CA  . VAL B 134 ? 0.4241 0.4455 0.2488 -0.0264 -0.0195 -0.0575 159 VAL B CA  
3044 C C   . VAL B 134 ? 0.4082 0.4249 0.2346 -0.0201 -0.0190 -0.0448 159 VAL B C   
3045 O O   . VAL B 134 ? 0.3983 0.4221 0.2182 -0.0137 -0.0214 -0.0376 159 VAL B O   
3046 C CB  . VAL B 134 ? 0.4626 0.4679 0.2831 -0.0283 -0.0134 -0.0605 159 VAL B CB  
3047 C CG1 . VAL B 134 ? 0.4765 0.4767 0.2880 -0.0218 -0.0112 -0.0517 159 VAL B CG1 
3048 C CG2 . VAL B 134 ? 0.4840 0.4928 0.3010 -0.0338 -0.0130 -0.0736 159 VAL B CG2 
3049 N N   . SER B 135 ? 0.3755 0.3794 0.2099 -0.0220 -0.0153 -0.0422 160 SER B N   
3050 C CA  . SER B 135 ? 0.3770 0.3739 0.2131 -0.0172 -0.0139 -0.0321 160 SER B CA  
3051 C C   . SER B 135 ? 0.3701 0.3793 0.2098 -0.0132 -0.0179 -0.0278 160 SER B C   
3052 O O   . SER B 135 ? 0.3709 0.3932 0.2164 -0.0156 -0.0215 -0.0331 160 SER B O   
3053 C CB  . SER B 135 ? 0.3820 0.3653 0.2250 -0.0204 -0.0097 -0.0317 160 SER B CB  
3054 O OG  . SER B 135 ? 0.3810 0.3534 0.2215 -0.0229 -0.0059 -0.0351 160 SER B OG  
3055 N N   . ARG B 136 ? 0.3676 0.3725 0.2047 -0.0071 -0.0169 -0.0184 161 ARG B N   
3056 C CA  . ARG B 136 ? 0.3726 0.3861 0.2137 -0.0018 -0.0195 -0.0131 161 ARG B CA  
3057 C C   . ARG B 136 ? 0.3687 0.3689 0.2110 0.0018  -0.0154 -0.0050 161 ARG B C   
3058 O O   . ARG B 136 ? 0.3840 0.3735 0.2206 0.0028  -0.0121 -0.0010 161 ARG B O   
3059 C CB  . ARG B 136 ? 0.3994 0.4282 0.2333 0.0040  -0.0242 -0.0104 161 ARG B CB  
3060 C CG  . ARG B 136 ? 0.4166 0.4383 0.2383 0.0077  -0.0216 -0.0046 161 ARG B CG  
3061 C CD  . ARG B 136 ? 0.4390 0.4759 0.2511 0.0141  -0.0259 -0.0011 161 ARG B CD  
3062 N NE  . ARG B 136 ? 0.4291 0.4724 0.2443 0.0221  -0.0280 0.0073  161 ARG B NE  
3063 C CZ  . ARG B 136 ? 0.4625 0.5214 0.2712 0.0299  -0.0326 0.0122  161 ARG B CZ  
3064 N NH1 . ARG B 136 ? 0.4662 0.5377 0.2639 0.0303  -0.0362 0.0089  161 ARG B NH1 
3065 N NH2 . ARG B 136 ? 0.4651 0.5276 0.2781 0.0381  -0.0334 0.0206  161 ARG B NH2 
3066 N N   . LEU B 137 ? 0.3479 0.3495 0.1984 0.0032  -0.0153 -0.0035 162 LEU B N   
3067 C CA  . LEU B 137 ? 0.3551 0.3463 0.2070 0.0074  -0.0118 0.0034  162 LEU B CA  
3068 C C   . LEU B 137 ? 0.3571 0.3580 0.2110 0.0154  -0.0139 0.0091  162 LEU B C   
3069 O O   . LEU B 137 ? 0.3565 0.3719 0.2167 0.0162  -0.0176 0.0062  162 LEU B O   
3070 C CB  . LEU B 137 ? 0.3562 0.3391 0.2151 0.0033  -0.0087 0.0006  162 LEU B CB  
3071 C CG  . LEU B 137 ? 0.3547 0.3248 0.2142 0.0057  -0.0044 0.0052  162 LEU B CG  
3072 C CD1 . LEU B 137 ? 0.3679 0.3269 0.2214 0.0039  -0.0017 0.0068  162 LEU B CD1 
3073 C CD2 . LEU B 137 ? 0.3663 0.3325 0.2318 0.0025  -0.0021 0.0019  162 LEU B CD2 
3074 N N   . ASP B 138 ? 0.3693 0.3613 0.2187 0.0214  -0.0109 0.0174  163 ASP B N   
3075 C CA  . ASP B 138 ? 0.3904 0.3894 0.2390 0.0309  -0.0123 0.0250  163 ASP B CA  
3076 C C   . ASP B 138 ? 0.4035 0.3891 0.2562 0.0355  -0.0068 0.0308  163 ASP B C   
3077 O O   . ASP B 138 ? 0.4350 0.4270 0.2925 0.0430  -0.0076 0.0350  163 ASP B O   
3078 C CB  . ASP B 138 ? 0.4099 0.4113 0.2469 0.0352  -0.0131 0.0309  163 ASP B CB  
3079 C CG  . ASP B 138 ? 0.4033 0.4209 0.2360 0.0318  -0.0190 0.0241  163 ASP B CG  
3080 O OD1 . ASP B 138 ? 0.4046 0.4407 0.2389 0.0362  -0.0247 0.0239  163 ASP B OD1 
3081 O OD2 . ASP B 138 ? 0.3778 0.3899 0.2072 0.0245  -0.0178 0.0182  163 ASP B OD2 
3082 N N   . ALA B 139 ? 0.3966 0.3645 0.2479 0.0312  -0.0013 0.0308  164 ALA B N   
3083 C CA  . ALA B 139 ? 0.4014 0.3548 0.2564 0.0340  0.0046  0.0344  164 ALA B CA  
3084 C C   . ALA B 139 ? 0.3875 0.3338 0.2481 0.0268  0.0068  0.0269  164 ALA B C   
3085 O O   . ALA B 139 ? 0.3690 0.3182 0.2291 0.0199  0.0047  0.0208  164 ALA B O   
3086 C CB  . ALA B 139 ? 0.4162 0.3554 0.2646 0.0351  0.0099  0.0408  164 ALA B CB  
3087 N N   . GLU B 140 ? 0.4124 0.3484 0.2774 0.0289  0.0115  0.0278  165 GLU B N   
3088 C CA  . GLU B 140 ? 0.4141 0.3424 0.2823 0.0226  0.0142  0.0211  165 GLU B CA  
3089 C C   . GLU B 140 ? 0.4097 0.3229 0.2747 0.0187  0.0188  0.0213  165 GLU B C   
3090 O O   . GLU B 140 ? 0.3901 0.2990 0.2507 0.0199  0.0202  0.0263  165 GLU B O   
3091 C CB  . GLU B 140 ? 0.4394 0.3691 0.3147 0.0266  0.0161  0.0198  165 GLU B CB  
3092 C CG  . GLU B 140 ? 0.5101 0.4283 0.3873 0.0336  0.0217  0.0249  165 GLU B CG  
3093 C CD  . GLU B 140 ? 0.5764 0.4951 0.4610 0.0370  0.0246  0.0219  165 GLU B CD  
3094 O OE1 . GLU B 140 ? 0.5573 0.4873 0.4455 0.0340  0.0219  0.0167  165 GLU B OE1 
3095 O OE2 . GLU B 140 ? 0.6187 0.5251 0.5054 0.0421  0.0305  0.0245  165 GLU B OE2 
3096 N N   . GLU B 141 ? 0.4147 0.3215 0.2818 0.0134  0.0210  0.0150  166 GLU B N   
3097 C CA  . GLU B 141 ? 0.4097 0.3050 0.2757 0.0082  0.0248  0.0127  166 GLU B CA  
3098 C C   . GLU B 141 ? 0.4199 0.3019 0.2882 0.0120  0.0313  0.0161  166 GLU B C   
3099 O O   . GLU B 141 ? 0.4284 0.3094 0.3003 0.0169  0.0330  0.0161  166 GLU B O   
3100 C CB  . GLU B 141 ? 0.4206 0.3156 0.2879 0.0024  0.0247  0.0046  166 GLU B CB  
3101 C CG  . GLU B 141 ? 0.4185 0.3231 0.2833 -0.0017 0.0197  0.0016  166 GLU B CG  
3102 C CD  . GLU B 141 ? 0.4404 0.3447 0.3027 -0.0057 0.0188  0.0018  166 GLU B CD  
3103 O OE1 . GLU B 141 ? 0.4189 0.3165 0.2814 -0.0059 0.0220  0.0044  166 GLU B OE1 
3104 O OE2 . GLU B 141 ? 0.4479 0.3586 0.3083 -0.0083 0.0153  -0.0004 166 GLU B OE2 
3105 N N   . PRO B 142 ? 0.4111 0.2821 0.2785 0.0097  0.0360  0.0184  167 PRO B N   
3106 C CA  . PRO B 142 ? 0.4129 0.2864 0.2774 0.0040  0.0347  0.0181  167 PRO B CA  
3107 C C   . PRO B 142 ? 0.4216 0.2993 0.2808 0.0078  0.0337  0.0261  167 PRO B C   
3108 O O   . PRO B 142 ? 0.4383 0.3185 0.2953 0.0034  0.0332  0.0256  167 PRO B O   
3109 C CB  . PRO B 142 ? 0.4261 0.2857 0.2940 -0.0014 0.0415  0.0150  167 PRO B CB  
3110 C CG  . PRO B 142 ? 0.4401 0.2868 0.3096 0.0052  0.0478  0.0209  167 PRO B CG  
3111 C CD  . PRO B 142 ? 0.4297 0.2841 0.2999 0.0118  0.0440  0.0206  167 PRO B CD  
3112 N N   . GLU B 143 ? 0.4232 0.3029 0.2804 0.0163  0.0332  0.0333  168 GLU B N   
3113 C CA  . GLU B 143 ? 0.4409 0.3242 0.2915 0.0213  0.0329  0.0419  168 GLU B CA  
3114 C C   . GLU B 143 ? 0.4184 0.3156 0.2643 0.0183  0.0267  0.0391  168 GLU B C   
3115 O O   . GLU B 143 ? 0.4249 0.3229 0.2649 0.0182  0.0280  0.0432  168 GLU B O   
3116 C CB  . GLU B 143 ? 0.4724 0.3593 0.3218 0.0321  0.0320  0.0496  168 GLU B CB  
3117 C CG  . GLU B 143 ? 0.5066 0.3766 0.3592 0.0372  0.0399  0.0551  168 GLU B CG  
3118 C CD  . GLU B 143 ? 0.5347 0.3996 0.3954 0.0364  0.0415  0.0483  168 GLU B CD  
3119 O OE1 . GLU B 143 ? 0.5038 0.3793 0.3676 0.0326  0.0363  0.0403  168 GLU B OE1 
3120 O OE2 . GLU B 143 ? 0.5922 0.4410 0.4559 0.0398  0.0491  0.0515  168 GLU B OE2 
3121 N N   . LEU B 144 ? 0.4084 0.3152 0.2571 0.0151  0.0213  0.0318  169 LEU B N   
3122 C CA  . LEU B 144 ? 0.3966 0.3151 0.2417 0.0125  0.0161  0.0285  169 LEU B CA  
3123 C C   . LEU B 144 ? 0.4041 0.3187 0.2472 0.0067  0.0184  0.0266  169 LEU B C   
3124 O O   . LEU B 144 ? 0.3888 0.3110 0.2280 0.0053  0.0157  0.0248  169 LEU B O   
3125 C CB  . LEU B 144 ? 0.3948 0.3213 0.2439 0.0099  0.0115  0.0215  169 LEU B CB  
3126 C CG  . LEU B 144 ? 0.4024 0.3234 0.2561 0.0042  0.0128  0.0154  169 LEU B CG  
3127 C CD1 . LEU B 144 ? 0.4099 0.3318 0.2619 -0.0012 0.0118  0.0115  169 LEU B CD1 
3128 C CD2 . LEU B 144 ? 0.4149 0.3413 0.2726 0.0043  0.0104  0.0115  169 LEU B CD2 
3129 N N   . ASN B 145 ? 0.4028 0.3067 0.2496 0.0030  0.0236  0.0260  170 ASN B N   
3130 C CA  . ASN B 145 ? 0.4389 0.3418 0.2861 -0.0026 0.0256  0.0236  170 ASN B CA  
3131 C C   . ASN B 145 ? 0.4420 0.3407 0.2850 -0.0013 0.0310  0.0305  170 ASN B C   
3132 O O   . ASN B 145 ? 0.4562 0.3550 0.3003 -0.0058 0.0336  0.0291  170 ASN B O   
3133 C CB  . ASN B 145 ? 0.4186 0.3159 0.2728 -0.0086 0.0279  0.0179  170 ASN B CB  
3134 C CG  . ASN B 145 ? 0.4162 0.3175 0.2727 -0.0095 0.0234  0.0119  170 ASN B CG  
3135 O OD1 . ASN B 145 ? 0.4350 0.3441 0.2905 -0.0107 0.0192  0.0086  170 ASN B OD1 
3136 N ND2 . ASN B 145 ? 0.4083 0.3036 0.2678 -0.0087 0.0251  0.0106  170 ASN B ND2 
3137 N N   . ARG B 146 ? 0.4502 0.3452 0.2887 0.0052  0.0330  0.0385  171 ARG B N   
3138 C CA  . ARG B 146 ? 0.4695 0.3550 0.3048 0.0068  0.0404  0.0466  171 ARG B CA  
3139 C C   . ARG B 146 ? 0.4735 0.3659 0.2979 0.0138  0.0393  0.0545  171 ARG B C   
3140 O O   . ARG B 146 ? 0.4998 0.3844 0.3194 0.0170  0.0457  0.0634  171 ARG B O   
3141 C CB  . ARG B 146 ? 0.4869 0.3580 0.3262 0.0095  0.0460  0.0506  171 ARG B CB  
3142 C CG  . ARG B 146 ? 0.5106 0.3763 0.3595 0.0032  0.0464  0.0416  171 ARG B CG  
3143 C CD  . ARG B 146 ? 0.5445 0.3936 0.3980 0.0043  0.0537  0.0439  171 ARG B CD  
3144 N NE  . ARG B 146 ? 0.5704 0.4160 0.4320 -0.0032 0.0540  0.0334  171 ARG B NE  
3145 C CZ  . ARG B 146 ? 0.5933 0.4246 0.4602 -0.0043 0.0602  0.0314  171 ARG B CZ  
3146 N NH1 . ARG B 146 ? 0.6111 0.4292 0.4765 0.0022  0.0667  0.0402  171 ARG B NH1 
3147 N NH2 . ARG B 146 ? 0.6078 0.4381 0.4807 -0.0113 0.0598  0.0208  171 ARG B NH2 
3148 N N   . ASP B 147 ? 0.4614 0.3682 0.2811 0.0158  0.0317  0.0513  172 ASP B N   
3149 C CA  . ASP B 147 ? 0.4629 0.3784 0.2715 0.0226  0.0298  0.0577  172 ASP B CA  
3150 C C   . ASP B 147 ? 0.4489 0.3628 0.2508 0.0204  0.0353  0.0609  172 ASP B C   
3151 O O   . ASP B 147 ? 0.4338 0.3466 0.2404 0.0134  0.0372  0.0549  172 ASP B O   
3152 C CB  . ASP B 147 ? 0.4715 0.4034 0.2776 0.0233  0.0209  0.0513  172 ASP B CB  
3153 C CG  . ASP B 147 ? 0.4714 0.4091 0.2834 0.0263  0.0153  0.0488  172 ASP B CG  
3154 O OD1 . ASP B 147 ? 0.5158 0.4572 0.3246 0.0342  0.0140  0.0557  172 ASP B OD1 
3155 O OD2 . ASP B 147 ? 0.4795 0.4181 0.2990 0.0211  0.0126  0.0406  172 ASP B OD2 
3156 N N   . PRO B 148 ? 0.4801 0.3949 0.2706 0.0270  0.0381  0.0707  173 PRO B N   
3157 C CA  . PRO B 148 ? 0.4778 0.3926 0.2605 0.0252  0.0438  0.0738  173 PRO B CA  
3158 C C   . PRO B 148 ? 0.4604 0.3884 0.2404 0.0214  0.0389  0.0643  173 PRO B C   
3159 O O   . PRO B 148 ? 0.4348 0.3741 0.2135 0.0226  0.0307  0.0581  173 PRO B O   
3160 C CB  . PRO B 148 ? 0.5111 0.4268 0.2801 0.0349  0.0459  0.0865  173 PRO B CB  
3161 C CG  . PRO B 148 ? 0.5131 0.4246 0.2861 0.0414  0.0436  0.0913  173 PRO B CG  
3162 C CD  . PRO B 148 ? 0.5012 0.4191 0.2851 0.0371  0.0357  0.0795  173 PRO B CD  
3163 N N   . PRO B 149 ? 0.4653 0.3921 0.2455 0.0162  0.0446  0.0623  174 PRO B N   
3164 C CA  . PRO B 149 ? 0.4514 0.3895 0.2274 0.0141  0.0416  0.0544  174 PRO B CA  
3165 C C   . PRO B 149 ? 0.4517 0.4016 0.2124 0.0205  0.0371  0.0563  174 PRO B C   
3166 O O   . PRO B 149 ? 0.4675 0.4166 0.2183 0.0266  0.0398  0.0665  174 PRO B O   
3167 C CB  . PRO B 149 ? 0.4712 0.4051 0.2485 0.0098  0.0508  0.0559  174 PRO B CB  
3168 C CG  . PRO B 149 ? 0.4742 0.3949 0.2635 0.0060  0.0562  0.0591  174 PRO B CG  
3169 C CD  . PRO B 149 ? 0.4686 0.3832 0.2540 0.0122  0.0547  0.0671  174 PRO B CD  
3170 N N   . GLY B 150 ? 0.4533 0.4141 0.2127 0.0192  0.0302  0.0463  175 GLY B N   
3171 C CA  . GLY B 150 ? 0.4726 0.4472 0.2190 0.0240  0.0246  0.0452  175 GLY B CA  
3172 C C   . GLY B 150 ? 0.4639 0.4454 0.2131 0.0272  0.0160  0.0441  175 GLY B C   
3173 O O   . GLY B 150 ? 0.4604 0.4559 0.2036 0.0287  0.0094  0.0386  175 GLY B O   
3174 N N   . ASP B 151 ? 0.4590 0.4318 0.2181 0.0280  0.0163  0.0486  176 ASP B N   
3175 C CA  . ASP B 151 ? 0.4432 0.4232 0.2057 0.0321  0.0093  0.0488  176 ASP B CA  
3176 C C   . ASP B 151 ? 0.4303 0.4162 0.2022 0.0260  0.0033  0.0362  176 ASP B C   
3177 O O   . ASP B 151 ? 0.4187 0.3955 0.1998 0.0198  0.0057  0.0310  176 ASP B O   
3178 C CB  . ASP B 151 ? 0.4417 0.4091 0.2120 0.0350  0.0130  0.0571  176 ASP B CB  
3179 C CG  . ASP B 151 ? 0.4287 0.4034 0.2011 0.0421  0.0075  0.0609  176 ASP B CG  
3180 O OD1 . ASP B 151 ? 0.4083 0.3932 0.1872 0.0400  0.0007  0.0525  176 ASP B OD1 
3181 O OD2 . ASP B 151 ? 0.4401 0.4099 0.2083 0.0500  0.0107  0.0725  176 ASP B OD2 
3182 N N   . GLU B 152 ? 0.4198 0.4208 0.1903 0.0280  -0.0043 0.0318  177 GLU B N   
3183 C CA  . GLU B 152 ? 0.4271 0.4335 0.2059 0.0216  -0.0089 0.0196  177 GLU B CA  
3184 C C   . GLU B 152 ? 0.4078 0.4095 0.2002 0.0204  -0.0101 0.0194  177 GLU B C   
3185 O O   . GLU B 152 ? 0.3997 0.4004 0.2005 0.0145  -0.0115 0.0110  177 GLU B O   
3186 C CB  . GLU B 152 ? 0.4601 0.4858 0.2335 0.0220  -0.0161 0.0125  177 GLU B CB  
3187 C CG  . GLU B 152 ? 0.4972 0.5281 0.2566 0.0220  -0.0149 0.0098  177 GLU B CG  
3188 C CD  . GLU B 152 ? 0.5417 0.5924 0.2947 0.0212  -0.0219 0.0005  177 GLU B CD  
3189 O OE1 . GLU B 152 ? 0.5133 0.5754 0.2743 0.0195  -0.0282 -0.0055 177 GLU B OE1 
3190 O OE2 . GLU B 152 ? 0.5652 0.6206 0.3048 0.0222  -0.0206 -0.0010 177 GLU B OE2 
3191 N N   . ARG B 153 ? 0.4089 0.4071 0.2030 0.0265  -0.0088 0.0286  178 ARG B N   
3192 C CA  . ARG B 153 ? 0.4130 0.4062 0.2191 0.0261  -0.0090 0.0285  178 ARG B CA  
3193 C C   . ARG B 153 ? 0.3886 0.3672 0.2018 0.0190  -0.0045 0.0243  178 ARG B C   
3194 O O   . ARG B 153 ? 0.4009 0.3692 0.2112 0.0171  0.0006  0.0265  178 ARG B O   
3195 C CB  . ARG B 153 ? 0.4400 0.4285 0.2457 0.0346  -0.0065 0.0398  178 ARG B CB  
3196 C CG  . ARG B 153 ? 0.4882 0.4944 0.2889 0.0431  -0.0123 0.0442  178 ARG B CG  
3197 C CD  . ARG B 153 ? 0.5266 0.5273 0.3270 0.0532  -0.0094 0.0565  178 ARG B CD  
3198 N NE  . ARG B 153 ? 0.5685 0.5542 0.3598 0.0560  -0.0019 0.0662  178 ARG B NE  
3199 C CZ  . ARG B 153 ? 0.6207 0.5891 0.4148 0.0597  0.0054  0.0748  178 ARG B CZ  
3200 N NH1 . ARG B 153 ? 0.6590 0.6242 0.4629 0.0635  0.0055  0.0761  178 ARG B NH1 
3201 N NH2 . ARG B 153 ? 0.6168 0.5709 0.4041 0.0595  0.0132  0.0819  178 ARG B NH2 
3202 N N   . ASP B 154 ? 0.3694 0.3488 0.1920 0.0153  -0.0065 0.0183  179 ASP B N   
3203 C CA  . ASP B 154 ? 0.3613 0.3285 0.1904 0.0099  -0.0031 0.0152  179 ASP B CA  
3204 C C   . ASP B 154 ? 0.3490 0.3129 0.1754 0.0046  -0.0016 0.0102  179 ASP B C   
3205 O O   . ASP B 154 ? 0.3403 0.2946 0.1694 0.0018  0.0019  0.0101  179 ASP B O   
3206 C CB  . ASP B 154 ? 0.3691 0.3239 0.2001 0.0122  0.0019  0.0217  179 ASP B CB  
3207 C CG  . ASP B 154 ? 0.3695 0.3258 0.2033 0.0187  0.0016  0.0271  179 ASP B CG  
3208 O OD1 . ASP B 154 ? 0.3400 0.3036 0.1799 0.0186  -0.0016 0.0233  179 ASP B OD1 
3209 O OD2 . ASP B 154 ? 0.3716 0.3214 0.2020 0.0239  0.0053  0.0352  179 ASP B OD2 
3210 N N   . THR B 155 ? 0.3414 0.3142 0.1634 0.0034  -0.0045 0.0052  180 THR B N   
3211 C CA  . THR B 155 ? 0.3609 0.3303 0.1802 -0.0005 -0.0025 0.0004  180 THR B CA  
3212 C C   . THR B 155 ? 0.3533 0.3254 0.1767 -0.0052 -0.0047 -0.0083 180 THR B C   
3213 O O   . THR B 155 ? 0.3529 0.3335 0.1791 -0.0058 -0.0084 -0.0115 180 THR B O   
3214 C CB  . THR B 155 ? 0.3750 0.3494 0.1837 0.0018  -0.0017 0.0017  180 THR B CB  
3215 O OG1 . THR B 155 ? 0.4119 0.3997 0.2158 0.0031  -0.0066 -0.0017 180 THR B OG1 
3216 C CG2 . THR B 155 ? 0.3838 0.3537 0.1881 0.0061  0.0021  0.0113  180 THR B CG2 
3217 N N   . THR B 156 ? 0.3548 0.3195 0.1789 -0.0082 -0.0017 -0.0119 181 THR B N   
3218 C CA  . THR B 156 ? 0.3596 0.3239 0.1856 -0.0123 -0.0019 -0.0200 181 THR B CA  
3219 C C   . THR B 156 ? 0.3724 0.3345 0.1926 -0.0123 0.0011  -0.0227 181 THR B C   
3220 O O   . THR B 156 ? 0.3583 0.3218 0.1728 -0.0093 0.0027  -0.0182 181 THR B O   
3221 C CB  . THR B 156 ? 0.3528 0.3087 0.1867 -0.0149 -0.0004 -0.0206 181 THR B CB  
3222 O OG1 . THR B 156 ? 0.3803 0.3341 0.2165 -0.0189 0.0003  -0.0277 181 THR B OG1 
3223 C CG2 . THR B 156 ? 0.3591 0.3064 0.1940 -0.0137 0.0028  -0.0168 181 THR B CG2 
3224 N N   . THR B 157 ? 0.3651 0.3232 0.1869 -0.0154 0.0027  -0.0299 182 THR B N   
3225 C CA  . THR B 157 ? 0.3685 0.3223 0.1869 -0.0147 0.0067  -0.0325 182 THR B CA  
3226 C C   . THR B 157 ? 0.3658 0.3087 0.1912 -0.0156 0.0098  -0.0332 182 THR B C   
3227 O O   . THR B 157 ? 0.3559 0.2949 0.1865 -0.0178 0.0089  -0.0341 182 THR B O   
3228 C CB  . THR B 157 ? 0.3745 0.3334 0.1866 -0.0165 0.0065  -0.0411 182 THR B CB  
3229 O OG1 . THR B 157 ? 0.3858 0.3404 0.2035 -0.0211 0.0065  -0.0483 182 THR B OG1 
3230 C CG2 . THR B 157 ? 0.3724 0.3446 0.1765 -0.0150 0.0024  -0.0403 182 THR B CG2 
3231 N N   . PRO B 158 ? 0.3689 0.3074 0.1944 -0.0132 0.0136  -0.0325 183 PRO B N   
3232 C CA  . PRO B 158 ? 0.3745 0.3039 0.2060 -0.0125 0.0163  -0.0327 183 PRO B CA  
3233 C C   . PRO B 158 ? 0.3959 0.3184 0.2290 -0.0156 0.0176  -0.0392 183 PRO B C   
3234 O O   . PRO B 158 ? 0.4046 0.3200 0.2425 -0.0162 0.0182  -0.0374 183 PRO B O   
3235 C CB  . PRO B 158 ? 0.3793 0.3088 0.2102 -0.0090 0.0203  -0.0324 183 PRO B CB  
3236 C CG  . PRO B 158 ? 0.3677 0.3056 0.1945 -0.0083 0.0195  -0.0283 183 PRO B CG  
3237 C CD  . PRO B 158 ? 0.3765 0.3194 0.1971 -0.0106 0.0159  -0.0304 183 PRO B CD  
3238 N N   . HIS B 159 ? 0.4019 0.3266 0.2305 -0.0180 0.0182  -0.0470 184 HIS B N   
3239 C CA  . HIS B 159 ? 0.4176 0.3359 0.2481 -0.0224 0.0202  -0.0552 184 HIS B CA  
3240 C C   . HIS B 159 ? 0.4086 0.3290 0.2435 -0.0267 0.0170  -0.0549 184 HIS B C   
3241 O O   . HIS B 159 ? 0.3953 0.3061 0.2356 -0.0291 0.0198  -0.0559 184 HIS B O   
3242 C CB  . HIS B 159 ? 0.4323 0.3560 0.2562 -0.0246 0.0206  -0.0648 184 HIS B CB  
3243 C CG  . HIS B 159 ? 0.4597 0.3759 0.2856 -0.0298 0.0239  -0.0755 184 HIS B CG  
3244 N ND1 . HIS B 159 ? 0.5010 0.4199 0.3208 -0.0321 0.0254  -0.0862 184 HIS B ND1 
3245 C CD2 . HIS B 159 ? 0.4835 0.3890 0.3164 -0.0338 0.0265  -0.0779 184 HIS B CD2 
3246 C CE1 . HIS B 159 ? 0.5081 0.4176 0.3323 -0.0378 0.0290  -0.0955 184 HIS B CE1 
3247 N NE2 . HIS B 159 ? 0.5006 0.4017 0.3330 -0.0390 0.0299  -0.0902 184 HIS B NE2 
3248 N N   . ALA B 160 ? 0.3907 0.3238 0.2238 -0.0272 0.0117  -0.0529 185 ALA B N   
3249 C CA  . ALA B 160 ? 0.3835 0.3214 0.2217 -0.0310 0.0087  -0.0535 185 ALA B CA  
3250 C C   . ALA B 160 ? 0.3825 0.3128 0.2262 -0.0298 0.0101  -0.0462 185 ALA B C   
3251 O O   . ALA B 160 ? 0.3563 0.2820 0.2056 -0.0336 0.0119  -0.0479 185 ALA B O   
3252 C CB  . ALA B 160 ? 0.3831 0.3368 0.2181 -0.0298 0.0029  -0.0519 185 ALA B CB  
3253 N N   . ILE B 161 ? 0.3838 0.3133 0.2259 -0.0249 0.0096  -0.0385 186 ILE B N   
3254 C CA  . ILE B 161 ? 0.3754 0.3004 0.2213 -0.0237 0.0100  -0.0323 186 ILE B CA  
3255 C C   . ILE B 161 ? 0.3808 0.2933 0.2286 -0.0233 0.0146  -0.0320 186 ILE B C   
3256 O O   . ILE B 161 ? 0.3833 0.2910 0.2340 -0.0241 0.0159  -0.0291 186 ILE B O   
3257 C CB  . ILE B 161 ? 0.3705 0.2991 0.2148 -0.0197 0.0081  -0.0255 186 ILE B CB  
3258 C CG1 . ILE B 161 ? 0.3979 0.3244 0.2455 -0.0193 0.0077  -0.0209 186 ILE B CG1 
3259 C CG2 . ILE B 161 ? 0.3772 0.3027 0.2196 -0.0163 0.0101  -0.0237 186 ILE B CG2 
3260 C CD1 . ILE B 161 ? 0.4157 0.3466 0.2665 -0.0221 0.0063  -0.0221 186 ILE B CD1 
3261 N N   . ALA B 162 ? 0.3681 0.2751 0.2141 -0.0215 0.0175  -0.0345 187 ALA B N   
3262 C CA  . ALA B 162 ? 0.3737 0.2680 0.2217 -0.0199 0.0225  -0.0336 187 ALA B CA  
3263 C C   . ALA B 162 ? 0.3957 0.2822 0.2468 -0.0254 0.0258  -0.0380 187 ALA B C   
3264 O O   . ALA B 162 ? 0.4161 0.2936 0.2692 -0.0248 0.0290  -0.0337 187 ALA B O   
3265 C CB  . ALA B 162 ? 0.3822 0.2725 0.2285 -0.0164 0.0256  -0.0361 187 ALA B CB  
3266 N N   . LEU B 163 ? 0.4052 0.2960 0.2568 -0.0310 0.0252  -0.0466 188 LEU B N   
3267 C CA  . LEU B 163 ? 0.4221 0.3071 0.2786 -0.0379 0.0287  -0.0522 188 LEU B CA  
3268 C C   . LEU B 163 ? 0.4222 0.3117 0.2828 -0.0403 0.0272  -0.0479 188 LEU B C   
3269 O O   . LEU B 163 ? 0.4125 0.2927 0.2774 -0.0439 0.0321  -0.0478 188 LEU B O   
3270 C CB  . LEU B 163 ? 0.4377 0.3293 0.2945 -0.0440 0.0277  -0.0639 188 LEU B CB  
3271 C CG  . LEU B 163 ? 0.4502 0.3357 0.3026 -0.0423 0.0309  -0.0700 188 LEU B CG  
3272 C CD1 . LEU B 163 ? 0.4822 0.3759 0.3338 -0.0491 0.0294  -0.0828 188 LEU B CD1 
3273 C CD2 . LEU B 163 ? 0.4645 0.3294 0.3188 -0.0402 0.0391  -0.0688 188 LEU B CD2 
3274 N N   . VAL B 164 ? 0.3964 0.2993 0.2558 -0.0383 0.0212  -0.0444 189 VAL B N   
3275 C CA  . VAL B 164 ? 0.3891 0.2964 0.2524 -0.0396 0.0203  -0.0404 189 VAL B CA  
3276 C C   . VAL B 164 ? 0.3981 0.2942 0.2600 -0.0360 0.0239  -0.0323 189 VAL B C   
3277 O O   . VAL B 164 ? 0.3830 0.2743 0.2481 -0.0389 0.0277  -0.0308 189 VAL B O   
3278 C CB  . VAL B 164 ? 0.3749 0.2968 0.2370 -0.0370 0.0140  -0.0380 189 VAL B CB  
3279 C CG1 . VAL B 164 ? 0.3647 0.2886 0.2293 -0.0358 0.0137  -0.0322 189 VAL B CG1 
3280 C CG2 . VAL B 164 ? 0.3823 0.3178 0.2466 -0.0407 0.0102  -0.0452 189 VAL B CG2 
3281 N N   . LEU B 165 ? 0.3827 0.2763 0.2398 -0.0297 0.0228  -0.0272 190 LEU B N   
3282 C CA  . LEU B 165 ? 0.3954 0.2818 0.2503 -0.0254 0.0250  -0.0197 190 LEU B CA  
3283 C C   . LEU B 165 ? 0.4299 0.3013 0.2854 -0.0260 0.0318  -0.0190 190 LEU B C   
3284 O O   . LEU B 165 ? 0.4168 0.2819 0.2713 -0.0250 0.0352  -0.0134 190 LEU B O   
3285 C CB  . LEU B 165 ? 0.3901 0.2794 0.2414 -0.0191 0.0221  -0.0158 190 LEU B CB  
3286 C CG  . LEU B 165 ? 0.3873 0.2735 0.2358 -0.0139 0.0225  -0.0085 190 LEU B CG  
3287 C CD1 . LEU B 165 ? 0.3995 0.2905 0.2472 -0.0153 0.0210  -0.0058 190 LEU B CD1 
3288 C CD2 . LEU B 165 ? 0.3944 0.2860 0.2417 -0.0087 0.0196  -0.0064 190 LEU B CD2 
3289 N N   . GLN B 166 ? 0.4185 0.2836 0.2752 -0.0275 0.0346  -0.0246 191 GLN B N   
3290 C CA  . GLN B 166 ? 0.4289 0.2772 0.2867 -0.0281 0.0423  -0.0244 191 GLN B CA  
3291 C C   . GLN B 166 ? 0.4235 0.2677 0.2858 -0.0354 0.0467  -0.0258 191 GLN B C   
3292 O O   . GLN B 166 ? 0.4180 0.2495 0.2795 -0.0343 0.0529  -0.0200 191 GLN B O   
3293 C CB  . GLN B 166 ? 0.4498 0.2924 0.3087 -0.0296 0.0449  -0.0326 191 GLN B CB  
3294 C CG  . GLN B 166 ? 0.4723 0.2944 0.3329 -0.0298 0.0542  -0.0326 191 GLN B CG  
3295 C CD  . GLN B 166 ? 0.5179 0.3339 0.3793 -0.0310 0.0572  -0.0418 191 GLN B CD  
3296 O OE1 . GLN B 166 ? 0.5538 0.3739 0.4180 -0.0391 0.0569  -0.0525 191 GLN B OE1 
3297 N NE2 . GLN B 166 ? 0.5349 0.3432 0.3938 -0.0227 0.0597  -0.0382 191 GLN B NE2 
3298 N N   . GLN B 167 ? 0.4130 0.2687 0.2801 -0.0425 0.0437  -0.0332 192 GLN B N   
3299 C CA  . GLN B 167 ? 0.4337 0.2884 0.3072 -0.0502 0.0479  -0.0355 192 GLN B CA  
3300 C C   . GLN B 167 ? 0.4231 0.2803 0.2948 -0.0477 0.0481  -0.0267 192 GLN B C   
3301 O O   . GLN B 167 ? 0.4364 0.2856 0.3108 -0.0513 0.0548  -0.0243 192 GLN B O   
3302 C CB  . GLN B 167 ? 0.4530 0.3237 0.3331 -0.0576 0.0437  -0.0452 192 GLN B CB  
3303 C CG  . GLN B 167 ? 0.4938 0.3643 0.3757 -0.0622 0.0437  -0.0563 192 GLN B CG  
3304 C CD  . GLN B 167 ? 0.5183 0.4087 0.4059 -0.0685 0.0379  -0.0653 192 GLN B CD  
3305 O OE1 . GLN B 167 ? 0.5436 0.4385 0.4402 -0.0765 0.0404  -0.0703 192 GLN B OE1 
3306 N NE2 . GLN B 167 ? 0.5179 0.4215 0.4006 -0.0646 0.0304  -0.0669 192 GLN B NE2 
3307 N N   . LEU B 168 ? 0.4067 0.2751 0.2742 -0.0422 0.0414  -0.0227 193 LEU B N   
3308 C CA  . LEU B 168 ? 0.4093 0.2813 0.2745 -0.0398 0.0412  -0.0158 193 LEU B CA  
3309 C C   . LEU B 168 ? 0.4226 0.2812 0.2810 -0.0345 0.0462  -0.0069 193 LEU B C   
3310 O O   . LEU B 168 ? 0.4215 0.2767 0.2788 -0.0355 0.0508  -0.0023 193 LEU B O   
3311 C CB  . LEU B 168 ? 0.3907 0.2757 0.2528 -0.0353 0.0334  -0.0145 193 LEU B CB  
3312 C CG  . LEU B 168 ? 0.3773 0.2766 0.2447 -0.0384 0.0283  -0.0207 193 LEU B CG  
3313 C CD1 . LEU B 168 ? 0.3691 0.2767 0.2327 -0.0331 0.0225  -0.0178 193 LEU B CD1 
3314 C CD2 . LEU B 168 ? 0.3671 0.2728 0.2420 -0.0442 0.0307  -0.0234 193 LEU B CD2 
3315 N N   . VAL B 169 ? 0.4078 0.2603 0.2615 -0.0283 0.0452  -0.0041 194 VAL B N   
3316 C CA  . VAL B 169 ? 0.4422 0.2859 0.2888 -0.0210 0.0481  0.0053  194 VAL B CA  
3317 C C   . VAL B 169 ? 0.4495 0.2743 0.2965 -0.0212 0.0570  0.0076  194 VAL B C   
3318 O O   . VAL B 169 ? 0.4760 0.2916 0.3182 -0.0182 0.0624  0.0158  194 VAL B O   
3319 C CB  . VAL B 169 ? 0.4507 0.3008 0.2932 -0.0134 0.0418  0.0075  194 VAL B CB  
3320 C CG1 . VAL B 169 ? 0.4581 0.3013 0.2939 -0.0049 0.0440  0.0168  194 VAL B CG1 
3321 C CG2 . VAL B 169 ? 0.4410 0.3069 0.2829 -0.0135 0.0346  0.0060  194 VAL B CG2 
3322 N N   . LEU B 170 ? 0.4596 0.2781 0.3116 -0.0244 0.0591  0.0006  195 LEU B N   
3323 C CA  . LEU B 170 ? 0.4809 0.2793 0.3338 -0.0240 0.0682  0.0019  195 LEU B CA  
3324 C C   . LEU B 170 ? 0.4903 0.2811 0.3511 -0.0352 0.0751  -0.0056 195 LEU B C   
3325 O O   . LEU B 170 ? 0.5286 0.3001 0.3908 -0.0365 0.0847  -0.0042 195 LEU B O   
3326 C CB  . LEU B 170 ? 0.4895 0.2852 0.3424 -0.0191 0.0665  -0.0016 195 LEU B CB  
3327 C CG  . LEU B 170 ? 0.4972 0.2993 0.3443 -0.0077 0.0613  0.0061  195 LEU B CG  
3328 C CD1 . LEU B 170 ? 0.4991 0.2995 0.3478 -0.0033 0.0607  0.0021  195 LEU B CD1 
3329 C CD2 . LEU B 170 ? 0.5156 0.3079 0.3565 0.0000  0.0657  0.0185  195 LEU B CD2 
3330 N N   . GLY B 171 ? 0.4620 0.2677 0.3287 -0.0434 0.0708  -0.0137 196 GLY B N   
3331 C CA  . GLY B 171 ? 0.4783 0.2811 0.3544 -0.0549 0.0762  -0.0228 196 GLY B CA  
3332 C C   . GLY B 171 ? 0.4825 0.2917 0.3627 -0.0605 0.0787  -0.0207 196 GLY B C   
3333 O O   . GLY B 171 ? 0.4886 0.2979 0.3624 -0.0550 0.0791  -0.0107 196 GLY B O   
3334 N N   . ASN B 172 ? 0.4926 0.3099 0.3835 -0.0714 0.0796  -0.0310 197 ASN B N   
3335 C CA  . ASN B 172 ? 0.4899 0.3129 0.3878 -0.0783 0.0839  -0.0305 197 ASN B CA  
3336 C C   . ASN B 172 ? 0.4744 0.3232 0.3781 -0.0807 0.0751  -0.0360 197 ASN B C   
3337 O O   . ASN B 172 ? 0.4796 0.3372 0.3934 -0.0887 0.0780  -0.0401 197 ASN B O   
3338 C CB  . ASN B 172 ? 0.5313 0.3428 0.4398 -0.0898 0.0942  -0.0378 197 ASN B CB  
3339 C CG  . ASN B 172 ? 0.5363 0.3591 0.4540 -0.0982 0.0897  -0.0532 197 ASN B CG  
3340 O OD1 . ASN B 172 ? 0.5162 0.3518 0.4304 -0.0941 0.0797  -0.0575 197 ASN B OD1 
3341 N ND2 . ASN B 172 ? 0.5630 0.3820 0.4927 -0.1105 0.0973  -0.0621 197 ASN B ND2 
3342 N N   . ALA B 173 ? 0.4573 0.3184 0.3553 -0.0736 0.0649  -0.0354 198 ALA B N   
3343 C CA  . ALA B 173 ? 0.4391 0.3227 0.3413 -0.0738 0.0571  -0.0383 198 ALA B CA  
3344 C C   . ALA B 173 ? 0.4476 0.3350 0.3505 -0.0729 0.0602  -0.0316 198 ALA B C   
3345 O O   . ALA B 173 ? 0.4319 0.3352 0.3438 -0.0769 0.0588  -0.0355 198 ALA B O   
3346 C CB  . ALA B 173 ? 0.4190 0.3101 0.3134 -0.0655 0.0478  -0.0366 198 ALA B CB  
3347 N N   . LEU B 174 ? 0.4455 0.3199 0.3383 -0.0667 0.0641  -0.0216 199 LEU B N   
3348 C CA  . LEU B 174 ? 0.4431 0.3201 0.3333 -0.0647 0.0673  -0.0148 199 LEU B CA  
3349 C C   . LEU B 174 ? 0.4586 0.3186 0.3475 -0.0679 0.0791  -0.0092 199 LEU B C   
3350 O O   . LEU B 174 ? 0.4600 0.3026 0.3438 -0.0661 0.0834  -0.0058 199 LEU B O   
3351 C CB  . LEU B 174 ? 0.4329 0.3108 0.3108 -0.0546 0.0617  -0.0077 199 LEU B CB  
3352 C CG  . LEU B 174 ? 0.4307 0.3237 0.3092 -0.0511 0.0516  -0.0116 199 LEU B CG  
3353 C CD1 . LEU B 174 ? 0.4213 0.3117 0.2881 -0.0424 0.0473  -0.0054 199 LEU B CD1 
3354 C CD2 . LEU B 174 ? 0.4223 0.3310 0.3090 -0.0538 0.0507  -0.0147 199 LEU B CD2 
3355 N N   . PRO B 175 ? 0.4628 0.3271 0.3557 -0.0717 0.0852  -0.0072 200 PRO B N   
3356 C CA  . PRO B 175 ? 0.4830 0.3310 0.3711 -0.0726 0.0970  0.0011  200 PRO B CA  
3357 C C   . PRO B 175 ? 0.4936 0.3311 0.3642 -0.0614 0.0957  0.0121  200 PRO B C   
3358 O O   . PRO B 175 ? 0.4929 0.3404 0.3568 -0.0543 0.0866  0.0130  200 PRO B O   
3359 C CB  . PRO B 175 ? 0.4829 0.3422 0.3770 -0.0769 0.1020  0.0014  200 PRO B CB  
3360 C CG  . PRO B 175 ? 0.4710 0.3533 0.3765 -0.0793 0.0931  -0.0084 200 PRO B CG  
3361 C CD  . PRO B 175 ? 0.4493 0.3344 0.3513 -0.0744 0.0819  -0.0121 200 PRO B CD  
3362 N N   . PRO B 176 ? 0.5065 0.3242 0.3697 -0.0593 0.1048  0.0209  201 PRO B N   
3363 C CA  . PRO B 176 ? 0.5261 0.3350 0.3735 -0.0478 0.1026  0.0311  201 PRO B CA  
3364 C C   . PRO B 176 ? 0.5343 0.3556 0.3703 -0.0403 0.0969  0.0361  201 PRO B C   
3365 O O   . PRO B 176 ? 0.5318 0.3553 0.3583 -0.0315 0.0897  0.0395  201 PRO B O   
3366 C CB  . PRO B 176 ? 0.5506 0.3371 0.3932 -0.0477 0.1159  0.0407  201 PRO B CB  
3367 C CG  . PRO B 176 ? 0.5608 0.3412 0.4191 -0.0606 0.1242  0.0326  201 PRO B CG  
3368 C CD  . PRO B 176 ? 0.5345 0.3378 0.4051 -0.0680 0.1179  0.0214  201 PRO B CD  
3369 N N   . ASP B 177 ? 0.5558 0.3853 0.3933 -0.0440 0.1010  0.0360  202 ASP B N   
3370 C CA  . ASP B 177 ? 0.5683 0.4085 0.3947 -0.0378 0.0972  0.0397  202 ASP B CA  
3371 C C   . ASP B 177 ? 0.5104 0.3663 0.3398 -0.0355 0.0848  0.0319  202 ASP B C   
3372 O O   . ASP B 177 ? 0.5285 0.3893 0.3474 -0.0283 0.0784  0.0343  202 ASP B O   
3373 C CB  . ASP B 177 ? 0.6109 0.4546 0.4378 -0.0421 0.1062  0.0416  202 ASP B CB  
3374 C CG  . ASP B 177 ? 0.6538 0.5069 0.4990 -0.0524 0.1094  0.0326  202 ASP B CG  
3375 O OD1 . ASP B 177 ? 0.6192 0.4773 0.4770 -0.0569 0.1040  0.0240  202 ASP B OD1 
3376 O OD2 . ASP B 177 ? 0.7387 0.5955 0.5855 -0.0559 0.1176  0.0342  202 ASP B OD2 
3377 N N   . LYS B 178 ? 0.4888 0.3530 0.3326 -0.0419 0.0817  0.0226  203 LYS B N   
3378 C CA  . LYS B 178 ? 0.4601 0.3374 0.3071 -0.0397 0.0710  0.0160  203 LYS B CA  
3379 C C   . LYS B 178 ? 0.4420 0.3141 0.2849 -0.0351 0.0645  0.0164  203 LYS B C   
3380 O O   . LYS B 178 ? 0.4253 0.3040 0.2633 -0.0300 0.0569  0.0158  203 LYS B O   
3381 C CB  . LYS B 178 ? 0.4505 0.3394 0.3130 -0.0467 0.0697  0.0072  203 LYS B CB  
3382 C CG  . LYS B 178 ? 0.4496 0.3472 0.3178 -0.0503 0.0755  0.0063  203 LYS B CG  
3383 C CD  . LYS B 178 ? 0.4412 0.3526 0.3264 -0.0567 0.0742  -0.0022 203 LYS B CD  
3384 C CE  . LYS B 178 ? 0.4477 0.3682 0.3403 -0.0603 0.0810  -0.0029 203 LYS B CE  
3385 N NZ  . LYS B 178 ? 0.4442 0.3817 0.3543 -0.0653 0.0786  -0.0112 203 LYS B NZ  
3386 N N   . ARG B 179 ? 0.4351 0.2949 0.2804 -0.0370 0.0683  0.0172  204 ARG B N   
3387 C CA  . ARG B 179 ? 0.4453 0.2997 0.2872 -0.0322 0.0634  0.0177  204 ARG B CA  
3388 C C   . ARG B 179 ? 0.4496 0.3032 0.2785 -0.0228 0.0604  0.0254  204 ARG B C   
3389 O O   . ARG B 179 ? 0.4453 0.3043 0.2722 -0.0182 0.0529  0.0241  204 ARG B O   
3390 C CB  . ARG B 179 ? 0.4635 0.3019 0.3091 -0.0352 0.0704  0.0180  204 ARG B CB  
3391 C CG  . ARG B 179 ? 0.4618 0.2961 0.3063 -0.0308 0.0658  0.0165  204 ARG B CG  
3392 C CD  . ARG B 179 ? 0.4804 0.2984 0.3302 -0.0350 0.0735  0.0146  204 ARG B CD  
3393 N NE  . ARG B 179 ? 0.4955 0.2956 0.3377 -0.0296 0.0816  0.0248  204 ARG B NE  
3394 C CZ  . ARG B 179 ? 0.5164 0.2984 0.3607 -0.0299 0.0887  0.0254  204 ARG B CZ  
3395 N NH1 . ARG B 179 ? 0.5265 0.3060 0.3804 -0.0368 0.0893  0.0149  204 ARG B NH1 
3396 N NH2 . ARG B 179 ? 0.5249 0.2910 0.3613 -0.0227 0.0954  0.0364  204 ARG B NH2 
3397 N N   . ALA B 180 ? 0.4668 0.3150 0.2869 -0.0201 0.0662  0.0334  205 ALA B N   
3398 C CA  . ALA B 180 ? 0.4618 0.3110 0.2687 -0.0109 0.0633  0.0409  205 ALA B CA  
3399 C C   . ALA B 180 ? 0.4497 0.3150 0.2535 -0.0091 0.0550  0.0367  205 ALA B C   
3400 O O   . ALA B 180 ? 0.4675 0.3384 0.2653 -0.0030 0.0486  0.0381  205 ALA B O   
3401 C CB  . ALA B 180 ? 0.5008 0.3406 0.2981 -0.0087 0.0723  0.0506  205 ALA B CB  
3402 N N   . LEU B 181 ? 0.4355 0.3087 0.2443 -0.0144 0.0555  0.0313  206 LEU B N   
3403 C CA  . LEU B 181 ? 0.4313 0.3174 0.2381 -0.0129 0.0489  0.0266  206 LEU B CA  
3404 C C   . LEU B 181 ? 0.4256 0.3167 0.2382 -0.0123 0.0407  0.0214  206 LEU B C   
3405 O O   . LEU B 181 ? 0.4149 0.3126 0.2227 -0.0085 0.0348  0.0205  206 LEU B O   
3406 C CB  . LEU B 181 ? 0.4332 0.3259 0.2461 -0.0180 0.0516  0.0217  206 LEU B CB  
3407 C CG  . LEU B 181 ? 0.4543 0.3452 0.2607 -0.0185 0.0599  0.0261  206 LEU B CG  
3408 C CD1 . LEU B 181 ? 0.4405 0.3384 0.2569 -0.0239 0.0633  0.0207  206 LEU B CD1 
3409 C CD2 . LEU B 181 ? 0.4705 0.3659 0.2621 -0.0125 0.0574  0.0289  206 LEU B CD2 
3410 N N   . LEU B 182 ? 0.4338 0.3227 0.2568 -0.0165 0.0407  0.0173  207 LEU B N   
3411 C CA  . LEU B 182 ? 0.4213 0.3146 0.2492 -0.0160 0.0341  0.0128  207 LEU B CA  
3412 C C   . LEU B 182 ? 0.4195 0.3101 0.2416 -0.0102 0.0311  0.0167  207 LEU B C   
3413 O O   . LEU B 182 ? 0.3947 0.2925 0.2160 -0.0077 0.0253  0.0147  207 LEU B O   
3414 C CB  . LEU B 182 ? 0.4293 0.3203 0.2670 -0.0210 0.0352  0.0083  207 LEU B CB  
3415 C CG  . LEU B 182 ? 0.4377 0.3322 0.2789 -0.0202 0.0294  0.0044  207 LEU B CG  
3416 C CD1 . LEU B 182 ? 0.4447 0.3497 0.2876 -0.0200 0.0244  0.0012  207 LEU B CD1 
3417 C CD2 . LEU B 182 ? 0.4482 0.3398 0.2966 -0.0247 0.0308  0.0000  207 LEU B CD2 
3418 N N   . THR B 183 ? 0.4194 0.2994 0.2387 -0.0080 0.0359  0.0221  208 THR B N   
3419 C CA  . THR B 183 ? 0.4276 0.3048 0.2425 -0.0013 0.0341  0.0267  208 THR B CA  
3420 C C   . THR B 183 ? 0.4281 0.3149 0.2342 0.0044  0.0293  0.0298  208 THR B C   
3421 O O   . THR B 183 ? 0.4324 0.3261 0.2388 0.0084  0.0238  0.0291  208 THR B O   
3422 C CB  . THR B 183 ? 0.4555 0.3177 0.2678 0.0007  0.0418  0.0334  208 THR B CB  
3423 O OG1 . THR B 183 ? 0.4539 0.3079 0.2752 -0.0056 0.0460  0.0286  208 THR B OG1 
3424 C CG2 . THR B 183 ? 0.4650 0.3243 0.2728 0.0095  0.0403  0.0394  208 THR B CG2 
3425 N N   A ASP B 184 ? 0.4261 0.3142 0.2246 0.0046  0.0320  0.0328  209 ASP B N   
3426 N N   B ASP B 184 ? 0.4333 0.3217 0.2318 0.0046  0.0318  0.0326  209 ASP B N   
3427 C CA  A ASP B 184 ? 0.4261 0.3241 0.2146 0.0094  0.0278  0.0347  209 ASP B CA  
3428 C CA  B ASP B 184 ? 0.4381 0.3365 0.2268 0.0098  0.0274  0.0348  209 ASP B CA  
3429 C C   A ASP B 184 ? 0.4240 0.3346 0.2165 0.0071  0.0207  0.0265  209 ASP B C   
3430 C C   B ASP B 184 ? 0.4307 0.3416 0.2232 0.0071  0.0205  0.0264  209 ASP B C   
3431 O O   A ASP B 184 ? 0.4243 0.3446 0.2139 0.0108  0.0149  0.0258  209 ASP B O   
3432 O O   B ASP B 184 ? 0.4298 0.3504 0.2193 0.0108  0.0148  0.0257  209 ASP B O   
3433 C CB  A ASP B 184 ? 0.4337 0.3303 0.2130 0.0091  0.0331  0.0384  209 ASP B CB  
3434 C CB  B ASP B 184 ? 0.4579 0.3538 0.2360 0.0110  0.0329  0.0403  209 ASP B CB  
3435 C CG  A ASP B 184 ? 0.4241 0.3328 0.1922 0.0130  0.0287  0.0383  209 ASP B CG  
3436 C CG  B ASP B 184 ? 0.4732 0.3568 0.2448 0.0161  0.0393  0.0509  209 ASP B CG  
3437 O OD1 A ASP B 184 ? 0.4205 0.3325 0.1803 0.0203  0.0261  0.0443  209 ASP B OD1 
3438 O OD1 B ASP B 184 ? 0.4613 0.3412 0.2346 0.0212  0.0376  0.0543  209 ASP B OD1 
3439 O OD2 A ASP B 184 ? 0.4038 0.3196 0.1722 0.0090  0.0274  0.0315  209 ASP B OD2 
3440 O OD2 B ASP B 184 ? 0.4861 0.3634 0.2515 0.0151  0.0466  0.0557  209 ASP B OD2 
3441 N N   . TRP B 185 ? 0.4154 0.3263 0.2152 0.0009  0.0214  0.0202  210 TRP B N   
3442 C CA  . TRP B 185 ? 0.4150 0.3347 0.2191 -0.0015 0.0162  0.0130  210 TRP B CA  
3443 C C   . TRP B 185 ? 0.3935 0.3161 0.2033 -0.0002 0.0115  0.0115  210 TRP B C   
3444 O O   . TRP B 185 ? 0.3835 0.3149 0.1934 0.0004  0.0067  0.0082  210 TRP B O   
3445 C CB  . TRP B 185 ? 0.3924 0.3109 0.2036 -0.0068 0.0185  0.0080  210 TRP B CB  
3446 C CG  . TRP B 185 ? 0.3935 0.3132 0.1999 -0.0079 0.0223  0.0074  210 TRP B CG  
3447 C CD1 . TRP B 185 ? 0.4038 0.3286 0.2006 -0.0059 0.0218  0.0069  210 TRP B CD1 
3448 C CD2 . TRP B 185 ? 0.3811 0.2983 0.1924 -0.0113 0.0276  0.0066  210 TRP B CD2 
3449 N NE1 . TRP B 185 ? 0.3963 0.3207 0.1910 -0.0076 0.0270  0.0059  210 TRP B NE1 
3450 C CE2 . TRP B 185 ? 0.3901 0.3103 0.1945 -0.0109 0.0307  0.0060  210 TRP B CE2 
3451 C CE3 . TRP B 185 ? 0.3699 0.2843 0.1911 -0.0148 0.0298  0.0056  210 TRP B CE3 
3452 C CZ2 . TRP B 185 ? 0.3958 0.3159 0.2039 -0.0135 0.0365  0.0050  210 TRP B CZ2 
3453 C CZ3 . TRP B 185 ? 0.3717 0.2875 0.1972 -0.0177 0.0348  0.0044  210 TRP B CZ3 
3454 C CH2 . TRP B 185 ? 0.3847 0.3033 0.2044 -0.0169 0.0383  0.0043  210 TRP B CH2 
3455 N N   . MET B 186 ? 0.3979 0.3135 0.2127 -0.0001 0.0133  0.0134  211 MET B N   
3456 C CA  . MET B 186 ? 0.4107 0.3288 0.2308 0.0014  0.0100  0.0122  211 MET B CA  
3457 C C   . MET B 186 ? 0.4231 0.3469 0.2387 0.0080  0.0072  0.0163  211 MET B C   
3458 O O   . MET B 186 ? 0.4177 0.3505 0.2372 0.0090  0.0027  0.0136  211 MET B O   
3459 C CB  . MET B 186 ? 0.4194 0.3287 0.2450 -0.0001 0.0133  0.0122  211 MET B CB  
3460 C CG  . MET B 186 ? 0.3987 0.3071 0.2299 -0.0060 0.0142  0.0073  211 MET B CG  
3461 S SD  . MET B 186 ? 0.3941 0.2951 0.2311 -0.0085 0.0170  0.0052  211 MET B SD  
3462 C CE  . MET B 186 ? 0.3813 0.2872 0.2203 -0.0051 0.0132  0.0041  211 MET B CE  
3463 N N   . ALA B 187 ? 0.4318 0.3515 0.2395 0.0125  0.0098  0.0229  212 ALA B N   
3464 C CA  . ALA B 187 ? 0.4442 0.3704 0.2466 0.0203  0.0069  0.0282  212 ALA B CA  
3465 C C   . ALA B 187 ? 0.4479 0.3903 0.2475 0.0203  0.0005  0.0240  212 ALA B C   
3466 O O   . ALA B 187 ? 0.4792 0.4330 0.2795 0.0251  -0.0044 0.0246  212 ALA B O   
3467 C CB  . ALA B 187 ? 0.4643 0.3814 0.2571 0.0255  0.0120  0.0373  212 ALA B CB  
3468 N N   . ARG B 188 ? 0.4560 0.4002 0.2533 0.0149  0.0007  0.0189  213 ARG B N   
3469 C CA  . ARG B 188 ? 0.4443 0.4022 0.2380 0.0139  -0.0044 0.0135  213 ARG B CA  
3470 C C   . ARG B 188 ? 0.4396 0.4019 0.2433 0.0075  -0.0069 0.0046  213 ARG B C   
3471 O O   . ARG B 188 ? 0.4360 0.4063 0.2384 0.0043  -0.0095 -0.0019 213 ARG B O   
3472 C CB  . ARG B 188 ? 0.4689 0.4249 0.2525 0.0126  -0.0014 0.0134  213 ARG B CB  
3473 C CG  . ARG B 188 ? 0.4938 0.4470 0.2655 0.0195  0.0013  0.0231  213 ARG B CG  
3474 C CD  . ARG B 188 ? 0.5197 0.4671 0.2825 0.0176  0.0071  0.0246  213 ARG B CD  
3475 N NE  . ARG B 188 ? 0.5538 0.5100 0.3135 0.0136  0.0050  0.0158  213 ARG B NE  
3476 C CZ  . ARG B 188 ? 0.6187 0.5695 0.3798 0.0085  0.0098  0.0117  213 ARG B CZ  
3477 N NH1 . ARG B 188 ? 0.6413 0.5804 0.4054 0.0069  0.0166  0.0160  213 ARG B NH1 
3478 N NH2 . ARG B 188 ? 0.6787 0.6360 0.4392 0.0048  0.0080  0.0027  213 ARG B NH2 
3479 N N   . ASN B 189 ? 0.4353 0.3921 0.2484 0.0057  -0.0058 0.0042  214 ASN B N   
3480 C CA  . ASN B 189 ? 0.4284 0.3872 0.2502 0.0001  -0.0068 -0.0025 214 ASN B CA  
3481 C C   . ASN B 189 ? 0.4263 0.3996 0.2512 -0.0007 -0.0120 -0.0075 214 ASN B C   
3482 O O   . ASN B 189 ? 0.4105 0.3929 0.2353 0.0042  -0.0152 -0.0048 214 ASN B O   
3483 C CB  . ASN B 189 ? 0.4316 0.3832 0.2608 -0.0004 -0.0046 -0.0009 214 ASN B CB  
3484 C CG  . ASN B 189 ? 0.4397 0.3930 0.2767 -0.0054 -0.0051 -0.0063 214 ASN B CG  
3485 O OD1 . ASN B 189 ? 0.4264 0.3800 0.2635 -0.0094 -0.0049 -0.0107 214 ASN B OD1 
3486 N ND2 . ASN B 189 ? 0.4342 0.3883 0.2774 -0.0050 -0.0050 -0.0059 214 ASN B ND2 
3487 N N   . THR B 190 ? 0.4097 0.3853 0.2384 -0.0067 -0.0123 -0.0150 215 THR B N   
3488 C CA  . THR B 190 ? 0.4262 0.4156 0.2597 -0.0094 -0.0165 -0.0215 215 THR B CA  
3489 C C   . THR B 190 ? 0.4127 0.4035 0.2583 -0.0130 -0.0159 -0.0238 215 THR B C   
3490 O O   . THR B 190 ? 0.4315 0.4349 0.2833 -0.0158 -0.0189 -0.0293 215 THR B O   
3491 C CB  . THR B 190 ? 0.4315 0.4225 0.2618 -0.0146 -0.0164 -0.0295 215 THR B CB  
3492 O OG1 . THR B 190 ? 0.4172 0.3975 0.2538 -0.0201 -0.0122 -0.0330 215 THR B OG1 
3493 C CG2 . THR B 190 ? 0.4370 0.4253 0.2548 -0.0116 -0.0154 -0.0274 215 THR B CG2 
3494 N N   . THR B 191 ? 0.4008 0.3802 0.2498 -0.0132 -0.0120 -0.0203 216 THR B N   
3495 C CA  . THR B 191 ? 0.3830 0.3622 0.2416 -0.0174 -0.0102 -0.0229 216 THR B CA  
3496 C C   . THR B 191 ? 0.3592 0.3421 0.2230 -0.0139 -0.0103 -0.0190 216 THR B C   
3497 O O   . THR B 191 ? 0.3447 0.3283 0.2159 -0.0171 -0.0082 -0.0205 216 THR B O   
3498 C CB  . THR B 191 ? 0.3914 0.3569 0.2502 -0.0205 -0.0056 -0.0226 216 THR B CB  
3499 O OG1 . THR B 191 ? 0.3921 0.3500 0.2479 -0.0167 -0.0041 -0.0168 216 THR B OG1 
3500 C CG2 . THR B 191 ? 0.4036 0.3638 0.2580 -0.0230 -0.0044 -0.0261 216 THR B CG2 
3501 N N   . GLY B 192 ? 0.3397 0.3237 0.1994 -0.0072 -0.0117 -0.0138 217 GLY B N   
3502 C CA  . GLY B 192 ? 0.3287 0.3103 0.1918 -0.0034 -0.0098 -0.0098 217 GLY B CA  
3503 C C   . GLY B 192 ? 0.3439 0.3396 0.2123 0.0015  -0.0128 -0.0090 217 GLY B C   
3504 O O   . GLY B 192 ? 0.3733 0.3672 0.2443 0.0059  -0.0109 -0.0057 217 GLY B O   
3505 N N   . ALA B 193 ? 0.3336 0.3444 0.2042 0.0008  -0.0174 -0.0125 218 ALA B N   
3506 C CA  . ALA B 193 ? 0.3426 0.3695 0.2173 0.0073  -0.0214 -0.0108 218 ALA B CA  
3507 C C   . ALA B 193 ? 0.3484 0.3825 0.2353 0.0075  -0.0196 -0.0117 218 ALA B C   
3508 O O   . ALA B 193 ? 0.3462 0.3890 0.2367 0.0151  -0.0209 -0.0082 218 ALA B O   
3509 C CB  . ALA B 193 ? 0.3435 0.3878 0.2184 0.0055  -0.0273 -0.0159 218 ALA B CB  
3510 N N   . LYS B 194 ? 0.3502 0.3807 0.2433 -0.0003 -0.0159 -0.0160 219 LYS B N   
3511 C CA  . LYS B 194 ? 0.3465 0.3859 0.2515 -0.0013 -0.0135 -0.0176 219 LYS B CA  
3512 C C   . LYS B 194 ? 0.3356 0.3606 0.2386 0.0002  -0.0076 -0.0141 219 LYS B C   
3513 O O   . LYS B 194 ? 0.3121 0.3415 0.2232 -0.0016 -0.0041 -0.0154 219 LYS B O   
3514 C CB  . LYS B 194 ? 0.3771 0.4227 0.2907 -0.0114 -0.0122 -0.0246 219 LYS B CB  
3515 C CG  . LYS B 194 ? 0.4331 0.4939 0.3500 -0.0153 -0.0177 -0.0309 219 LYS B CG  
3516 C CD  . LYS B 194 ? 0.4932 0.5758 0.4144 -0.0084 -0.0241 -0.0307 219 LYS B CD  
3517 C CE  . LYS B 194 ? 0.5642 0.6641 0.5007 -0.0077 -0.0233 -0.0322 219 LYS B CE  
3518 N NZ  . LYS B 194 ? 0.5787 0.6985 0.5277 -0.0161 -0.0259 -0.0414 219 LYS B NZ  
3519 N N   . ARG B 195 ? 0.3147 0.3236 0.2072 0.0031  -0.0063 -0.0102 220 ARG B N   
3520 C CA  . ARG B 195 ? 0.3156 0.3115 0.2051 0.0039  -0.0013 -0.0082 220 ARG B CA  
3521 C C   . ARG B 195 ? 0.3032 0.2952 0.1903 0.0125  -0.0005 -0.0041 220 ARG B C   
3522 O O   . ARG B 195 ? 0.3061 0.3091 0.1997 0.0180  -0.0013 -0.0032 220 ARG B O   
3523 C CB  . ARG B 195 ? 0.3164 0.2984 0.1984 -0.0013 0.0003  -0.0086 220 ARG B CB  
3524 C CG  . ARG B 195 ? 0.3297 0.3147 0.2159 -0.0087 0.0011  -0.0121 220 ARG B CG  
3525 C CD  . ARG B 195 ? 0.3288 0.3013 0.2087 -0.0126 0.0027  -0.0119 220 ARG B CD  
3526 N NE  . ARG B 195 ? 0.3364 0.3105 0.2206 -0.0189 0.0040  -0.0149 220 ARG B NE  
3527 C CZ  . ARG B 195 ? 0.3508 0.3154 0.2326 -0.0222 0.0071  -0.0143 220 ARG B CZ  
3528 N NH1 . ARG B 195 ? 0.3462 0.3018 0.2214 -0.0199 0.0084  -0.0110 220 ARG B NH1 
3529 N NH2 . ARG B 195 ? 0.3733 0.3378 0.2597 -0.0277 0.0091  -0.0170 220 ARG B NH2 
3530 N N   . ILE B 196 ? 0.3063 0.2829 0.1851 0.0136  0.0016  -0.0019 221 ILE B N   
3531 C CA  . ILE B 196 ? 0.3181 0.2874 0.1950 0.0209  0.0041  0.0014  221 ILE B CA  
3532 C C   . ILE B 196 ? 0.3201 0.2973 0.1977 0.0286  0.0008  0.0058  221 ILE B C   
3533 O O   . ILE B 196 ? 0.3124 0.2929 0.1944 0.0363  0.0022  0.0082  221 ILE B O   
3534 C CB  . ILE B 196 ? 0.3329 0.2847 0.2016 0.0191  0.0070  0.0021  221 ILE B CB  
3535 C CG1 . ILE B 196 ? 0.3371 0.2836 0.2052 0.0136  0.0100  -0.0019 221 ILE B CG1 
3536 C CG2 . ILE B 196 ? 0.3503 0.2925 0.2170 0.0264  0.0101  0.0058  221 ILE B CG2 
3537 C CD1 . ILE B 196 ? 0.3266 0.2605 0.1881 0.0099  0.0114  -0.0028 221 ILE B CD1 
3538 N N   . ARG B 197 ? 0.3340 0.3161 0.2076 0.0272  -0.0036 0.0066  222 ARG B N   
3539 C CA  . ARG B 197 ? 0.3358 0.3280 0.2081 0.0345  -0.0077 0.0108  222 ARG B CA  
3540 C C   . ARG B 197 ? 0.3456 0.3568 0.2288 0.0394  -0.0101 0.0100  222 ARG B C   
3541 O O   . ARG B 197 ? 0.3561 0.3734 0.2400 0.0493  -0.0116 0.0153  222 ARG B O   
3542 C CB  . ARG B 197 ? 0.3325 0.3308 0.1995 0.0301  -0.0123 0.0091  222 ARG B CB  
3543 C CG  . ARG B 197 ? 0.3314 0.3455 0.1964 0.0366  -0.0181 0.0119  222 ARG B CG  
3544 C CD  . ARG B 197 ? 0.3401 0.3456 0.1959 0.0465  -0.0167 0.0211  222 ARG B CD  
3545 N NE  . ARG B 197 ? 0.3387 0.3416 0.1993 0.0557  -0.0138 0.0262  222 ARG B NE  
3546 C CZ  . ARG B 197 ? 0.3584 0.3501 0.2127 0.0650  -0.0106 0.0348  222 ARG B CZ  
3547 N NH1 . ARG B 197 ? 0.3760 0.3589 0.2184 0.0660  -0.0100 0.0398  222 ARG B NH1 
3548 N NH2 . ARG B 197 ? 0.3598 0.3487 0.2196 0.0736  -0.0073 0.0387  222 ARG B NH2 
3549 N N   . ALA B 198 ? 0.3279 0.3492 0.2203 0.0326  -0.0102 0.0039  223 ALA B N   
3550 C CA  . ALA B 198 ? 0.3390 0.3811 0.2440 0.0355  -0.0123 0.0020  223 ALA B CA  
3551 C C   . ALA B 198 ? 0.3554 0.3952 0.2660 0.0429  -0.0074 0.0045  223 ALA B C   
3552 O O   . ALA B 198 ? 0.3837 0.4415 0.3056 0.0474  -0.0086 0.0038  223 ALA B O   
3553 C CB  . ALA B 198 ? 0.3329 0.3848 0.2462 0.0250  -0.0124 -0.0053 223 ALA B CB  
3554 N N   . GLY B 199 ? 0.3514 0.3704 0.2554 0.0437  -0.0017 0.0062  224 GLY B N   
3555 C CA  . GLY B 199 ? 0.3528 0.3680 0.2613 0.0508  0.0037  0.0075  224 GLY B CA  
3556 C C   . GLY B 199 ? 0.3687 0.3737 0.2725 0.0621  0.0052  0.0144  224 GLY B C   
3557 O O   . GLY B 199 ? 0.3881 0.3890 0.2961 0.0692  0.0101  0.0155  224 GLY B O   
3558 N N   . PHE B 200 ? 0.3725 0.3723 0.2674 0.0638  0.0019  0.0191  225 PHE B N   
3559 C CA  . PHE B 200 ? 0.3685 0.3550 0.2572 0.0738  0.0047  0.0268  225 PHE B CA  
3560 C C   . PHE B 200 ? 0.3730 0.3756 0.2621 0.0837  -0.0013 0.0334  225 PHE B C   
3561 O O   . PHE B 200 ? 0.3734 0.3894 0.2601 0.0796  -0.0078 0.0321  225 PHE B O   
3562 C CB  . PHE B 200 ? 0.3729 0.3380 0.2496 0.0686  0.0073  0.0283  225 PHE B CB  
3563 C CG  . PHE B 200 ? 0.3786 0.3246 0.2544 0.0639  0.0146  0.0240  225 PHE B CG  
3564 C CD1 . PHE B 200 ? 0.3656 0.3118 0.2420 0.0532  0.0146  0.0166  225 PHE B CD1 
3565 C CD2 . PHE B 200 ? 0.3912 0.3200 0.2657 0.0707  0.0214  0.0271  225 PHE B CD2 
3566 C CE1 . PHE B 200 ? 0.3706 0.3023 0.2455 0.0493  0.0204  0.0121  225 PHE B CE1 
3567 C CE2 . PHE B 200 ? 0.3857 0.2985 0.2594 0.0655  0.0277  0.0214  225 PHE B CE2 
3568 C CZ  . PHE B 200 ? 0.3826 0.2982 0.2561 0.0549  0.0267  0.0138  225 PHE B CZ  
3569 N N   . PRO B 201 ? 0.3897 0.3905 0.2803 0.0972  0.0010  0.0408  226 PRO B N   
3570 C CA  . PRO B 201 ? 0.4049 0.4226 0.2948 0.1084  -0.0051 0.0484  226 PRO B CA  
3571 C C   . PRO B 201 ? 0.4158 0.4281 0.2914 0.1070  -0.0082 0.0533  226 PRO B C   
3572 O O   . PRO B 201 ? 0.4161 0.4069 0.2826 0.1000  -0.0037 0.0530  226 PRO B O   
3573 C CB  . PRO B 201 ? 0.4205 0.4293 0.3134 0.1236  0.0007  0.0564  226 PRO B CB  
3574 C CG  . PRO B 201 ? 0.4124 0.4093 0.3127 0.1192  0.0083  0.0495  226 PRO B CG  
3575 C CD  . PRO B 201 ? 0.3985 0.3823 0.2922 0.1033  0.0096  0.0421  226 PRO B CD  
3576 N N   . ALA B 202 ? 0.4239 0.4579 0.2979 0.1141  -0.0160 0.0575  227 ALA B N   
3577 C CA  . ALA B 202 ? 0.4384 0.4737 0.2987 0.1127  -0.0203 0.0609  227 ALA B CA  
3578 C C   . ALA B 202 ? 0.4677 0.4767 0.3145 0.1189  -0.0133 0.0715  227 ALA B C   
3579 O O   . ALA B 202 ? 0.4812 0.4814 0.3160 0.1135  -0.0130 0.0727  227 ALA B O   
3580 C CB  . ALA B 202 ? 0.4351 0.5017 0.2970 0.1203  -0.0302 0.0628  227 ALA B CB  
3581 N N   . ASP B 203 ? 0.4785 0.4734 0.3277 0.1297  -0.0067 0.0789  228 ASP B N   
3582 C CA  . ASP B 203 ? 0.5115 0.4793 0.3489 0.1351  0.0014  0.0891  228 ASP B CA  
3583 C C   . ASP B 203 ? 0.5056 0.4455 0.3421 0.1233  0.0103  0.0835  228 ASP B C   
3584 O O   . ASP B 203 ? 0.5114 0.4265 0.3407 0.1263  0.0187  0.0905  228 ASP B O   
3585 C CB  . ASP B 203 ? 0.5323 0.4954 0.3713 0.1529  0.0053  0.1007  228 ASP B CB  
3586 C CG  . ASP B 203 ? 0.5328 0.4942 0.3867 0.1566  0.0095  0.0965  228 ASP B CG  
3587 O OD1 . ASP B 203 ? 0.5012 0.4674 0.3641 0.1452  0.0088  0.0844  228 ASP B OD1 
3588 O OD2 . ASP B 203 ? 0.5647 0.5185 0.4203 0.1715  0.0142  0.1059  228 ASP B OD2 
3589 N N   . TRP B 204 ? 0.4845 0.4285 0.3283 0.1104  0.0089  0.0713  229 TRP B N   
3590 C CA  . TRP B 204 ? 0.4730 0.3964 0.3148 0.0979  0.0149  0.0649  229 TRP B CA  
3591 C C   . TRP B 204 ? 0.4742 0.4028 0.3090 0.0875  0.0106  0.0613  229 TRP B C   
3592 O O   . TRP B 204 ? 0.4479 0.3973 0.2853 0.0835  0.0029  0.0561  229 TRP B O   
3593 C CB  . TRP B 204 ? 0.4662 0.3903 0.3188 0.0911  0.0165  0.0546  229 TRP B CB  
3594 C CG  . TRP B 204 ? 0.4715 0.3859 0.3309 0.0993  0.0230  0.0559  229 TRP B CG  
3595 C CD1 . TRP B 204 ? 0.4817 0.4068 0.3471 0.1126  0.0220  0.0613  229 TRP B CD1 
3596 C CD2 . TRP B 204 ? 0.4802 0.3729 0.3413 0.0950  0.0317  0.0508  229 TRP B CD2 
3597 N NE1 . TRP B 204 ? 0.4941 0.4044 0.3650 0.1174  0.0301  0.0603  229 TRP B NE1 
3598 C CE2 . TRP B 204 ? 0.5024 0.3924 0.3703 0.1063  0.0362  0.0533  229 TRP B CE2 
3599 C CE3 . TRP B 204 ? 0.4698 0.3467 0.3279 0.0830  0.0359  0.0438  229 TRP B CE3 
3600 C CZ2 . TRP B 204 ? 0.5127 0.3830 0.3834 0.1054  0.0452  0.0485  229 TRP B CZ2 
3601 C CZ3 . TRP B 204 ? 0.4764 0.3357 0.3373 0.0819  0.0439  0.0390  229 TRP B CZ3 
3602 C CH2 . TRP B 204 ? 0.5042 0.3597 0.3710 0.0925  0.0487  0.0408  229 TRP B CH2 
3603 N N   . LYS B 205 ? 0.4894 0.3984 0.3162 0.0823  0.0164  0.0632  230 LYS B N   
3604 C CA  . LYS B 205 ? 0.4966 0.4085 0.3177 0.0721  0.0137  0.0590  230 LYS B CA  
3605 C C   . LYS B 205 ? 0.4557 0.3666 0.2842 0.0602  0.0138  0.0478  230 LYS B C   
3606 O O   . LYS B 205 ? 0.4314 0.3301 0.2649 0.0583  0.0189  0.0447  230 LYS B O   
3607 C CB  . LYS B 205 ? 0.5609 0.4543 0.3716 0.0719  0.0204  0.0660  230 LYS B CB  
3608 C CG  . LYS B 205 ? 0.6295 0.5233 0.4349 0.0616  0.0197  0.0618  230 LYS B CG  
3609 C CD  . LYS B 205 ? 0.7465 0.6312 0.5396 0.0639  0.0241  0.0705  230 LYS B CD  
3610 C CE  . LYS B 205 ? 0.8203 0.6823 0.6135 0.0575  0.0340  0.0710  230 LYS B CE  
3611 N NZ  . LYS B 205 ? 0.8206 0.6777 0.6033 0.0556  0.0378  0.0762  230 LYS B NZ  
3612 N N   . VAL B 206 ? 0.4238 0.3472 0.2521 0.0528  0.0083  0.0419  231 VAL B N   
3613 C CA  . VAL B 206 ? 0.4066 0.3308 0.2406 0.0425  0.0078  0.0327  231 VAL B CA  
3614 C C   . VAL B 206 ? 0.4124 0.3370 0.2410 0.0350  0.0065  0.0302  231 VAL B C   
3615 O O   . VAL B 206 ? 0.4127 0.3473 0.2359 0.0365  0.0025  0.0318  231 VAL B O   
3616 C CB  . VAL B 206 ? 0.3886 0.3303 0.2313 0.0419  0.0027  0.0274  231 VAL B CB  
3617 C CG1 . VAL B 206 ? 0.3821 0.3244 0.2290 0.0318  0.0024  0.0194  231 VAL B CG1 
3618 C CG2 . VAL B 206 ? 0.4034 0.3462 0.2528 0.0497  0.0045  0.0294  231 VAL B CG2 
3619 N N   . ILE B 207 ? 0.4087 0.3229 0.2388 0.0274  0.0101  0.0259  232 ILE B N   
3620 C CA  . ILE B 207 ? 0.3938 0.3099 0.2218 0.0200  0.0089  0.0219  232 ILE B CA  
3621 C C   . ILE B 207 ? 0.3848 0.3025 0.2199 0.0137  0.0082  0.0149  232 ILE B C   
3622 O O   . ILE B 207 ? 0.3745 0.2858 0.2134 0.0136  0.0110  0.0135  232 ILE B O   
3623 C CB  . ILE B 207 ? 0.4196 0.3228 0.2423 0.0178  0.0143  0.0249  232 ILE B CB  
3624 C CG1 . ILE B 207 ? 0.4208 0.3119 0.2483 0.0130  0.0193  0.0218  232 ILE B CG1 
3625 C CG2 . ILE B 207 ? 0.4323 0.3304 0.2474 0.0255  0.0169  0.0339  232 ILE B CG2 
3626 C CD1 . ILE B 207 ? 0.4322 0.3119 0.2570 0.0095  0.0253  0.0238  232 ILE B CD1 
3627 N N   . ASP B 208 ? 0.3736 0.2985 0.2096 0.0087  0.0052  0.0106  233 ASP B N   
3628 C CA  . ASP B 208 ? 0.3550 0.2813 0.1967 0.0041  0.0048  0.0055  233 ASP B CA  
3629 C C   . ASP B 208 ? 0.3376 0.2660 0.1792 -0.0013 0.0038  0.0021  233 ASP B C   
3630 O O   . ASP B 208 ? 0.3373 0.2681 0.1752 -0.0018 0.0028  0.0023  233 ASP B O   
3631 C CB  . ASP B 208 ? 0.3693 0.3051 0.2163 0.0060  0.0024  0.0041  233 ASP B CB  
3632 C CG  . ASP B 208 ? 0.3724 0.3199 0.2212 0.0042  -0.0015 0.0016  233 ASP B CG  
3633 O OD1 . ASP B 208 ? 0.3810 0.3330 0.2255 0.0063  -0.0038 0.0031  233 ASP B OD1 
3634 O OD2 . ASP B 208 ? 0.3516 0.3028 0.2053 0.0001  -0.0018 -0.0021 233 ASP B OD2 
3635 N N   . LYS B 209 ? 0.3342 0.2618 0.1795 -0.0047 0.0043  -0.0009 234 LYS B N   
3636 C CA  . LYS B 209 ? 0.3311 0.2609 0.1777 -0.0085 0.0035  -0.0035 234 LYS B CA  
3637 C C   . LYS B 209 ? 0.3435 0.2767 0.1943 -0.0096 0.0031  -0.0052 234 LYS B C   
3638 O O   . LYS B 209 ? 0.3278 0.2590 0.1795 -0.0091 0.0045  -0.0053 234 LYS B O   
3639 C CB  . LYS B 209 ? 0.3280 0.2529 0.1740 -0.0108 0.0052  -0.0041 234 LYS B CB  
3640 C CG  . LYS B 209 ? 0.3372 0.2639 0.1850 -0.0132 0.0048  -0.0059 234 LYS B CG  
3641 C CD  . LYS B 209 ? 0.3530 0.2811 0.1991 -0.0136 0.0045  -0.0068 234 LYS B CD  
3642 C CE  . LYS B 209 ? 0.3717 0.3003 0.2202 -0.0153 0.0047  -0.0090 234 LYS B CE  
3643 N NZ  . LYS B 209 ? 0.3999 0.3317 0.2509 -0.0163 0.0037  -0.0104 234 LYS B NZ  
3644 N N   . THR B 210 ? 0.3442 0.2821 0.1975 -0.0115 0.0021  -0.0069 235 THR B N   
3645 C CA  . THR B 210 ? 0.3493 0.2900 0.2069 -0.0132 0.0029  -0.0080 235 THR B CA  
3646 C C   . THR B 210 ? 0.3544 0.2904 0.2116 -0.0153 0.0047  -0.0078 235 THR B C   
3647 O O   . THR B 210 ? 0.3383 0.2707 0.1934 -0.0156 0.0048  -0.0077 235 THR B O   
3648 C CB  . THR B 210 ? 0.3562 0.3043 0.2179 -0.0151 0.0016  -0.0105 235 THR B CB  
3649 O OG1 . THR B 210 ? 0.3580 0.3037 0.2181 -0.0176 0.0014  -0.0126 235 THR B OG1 
3650 C CG2 . THR B 210 ? 0.3442 0.3001 0.2065 -0.0118 -0.0011 -0.0102 235 THR B CG2 
3651 N N   . GLY B 211 ? 0.3420 0.2787 0.2013 -0.0162 0.0066  -0.0072 236 GLY B N   
3652 C CA  . GLY B 211 ? 0.3433 0.2760 0.2024 -0.0176 0.0087  -0.0060 236 GLY B CA  
3653 C C   . GLY B 211 ? 0.3227 0.2570 0.1858 -0.0197 0.0116  -0.0056 236 GLY B C   
3654 O O   . GLY B 211 ? 0.3174 0.2566 0.1825 -0.0194 0.0121  -0.0059 236 GLY B O   
3655 N N   . THR B 212 ? 0.3254 0.2548 0.1900 -0.0218 0.0143  -0.0050 237 THR B N   
3656 C CA  . THR B 212 ? 0.3358 0.2646 0.2049 -0.0250 0.0185  -0.0045 237 THR B CA  
3657 C C   . THR B 212 ? 0.3601 0.2797 0.2268 -0.0242 0.0224  -0.0002 237 THR B C   
3658 O O   . THR B 212 ? 0.3691 0.2837 0.2338 -0.0224 0.0216  0.0001  237 THR B O   
3659 C CB  . THR B 212 ? 0.3389 0.2713 0.2149 -0.0297 0.0183  -0.0099 237 THR B CB  
3660 O OG1 . THR B 212 ? 0.3168 0.2583 0.1934 -0.0284 0.0136  -0.0127 237 THR B OG1 
3661 C CG2 . THR B 212 ? 0.3526 0.2864 0.2356 -0.0343 0.0231  -0.0105 237 THR B CG2 
3662 N N   . GLY B 213 ? 0.3571 0.2747 0.2236 -0.0246 0.0271  0.0036  238 GLY B N   
3663 C CA  . GLY B 213 ? 0.3765 0.2851 0.2394 -0.0223 0.0312  0.0095  238 GLY B CA  
3664 C C   . GLY B 213 ? 0.3946 0.2993 0.2592 -0.0248 0.0383  0.0133  238 GLY B C   
3665 O O   . GLY B 213 ? 0.3949 0.3051 0.2653 -0.0293 0.0400  0.0102  238 GLY B O   
3666 N N   . ASP B 214 ? 0.4169 0.3129 0.2766 -0.0214 0.0426  0.0206  240 ASP B N   
3667 C CA  . ASP B 214 ? 0.4344 0.3249 0.2940 -0.0230 0.0507  0.0261  240 ASP B CA  
3668 C C   . ASP B 214 ? 0.4090 0.3088 0.2632 -0.0215 0.0506  0.0282  240 ASP B C   
3669 O O   . ASP B 214 ? 0.3926 0.3018 0.2438 -0.0193 0.0444  0.0247  240 ASP B O   
3670 C CB  . ASP B 214 ? 0.4760 0.3533 0.3316 -0.0187 0.0556  0.0340  240 ASP B CB  
3671 C CG  . ASP B 214 ? 0.5220 0.3894 0.3848 -0.0215 0.0570  0.0298  240 ASP B CG  
3672 O OD1 . ASP B 214 ? 0.5475 0.4102 0.4189 -0.0291 0.0620  0.0252  240 ASP B OD1 
3673 O OD2 . ASP B 214 ? 0.5287 0.3949 0.3891 -0.0166 0.0529  0.0298  240 ASP B OD2 
3674 N N   . TYR B 215 ? 0.4068 0.3034 0.2604 -0.0231 0.0585  0.0332  241 TYR B N   
3675 C CA  . TYR B 215 ? 0.4116 0.3172 0.2603 -0.0221 0.0599  0.0345  241 TYR B CA  
3676 C C   . TYR B 215 ? 0.3971 0.3147 0.2531 -0.0253 0.0556  0.0258  241 TYR B C   
3677 O O   . TYR B 215 ? 0.3774 0.3032 0.2283 -0.0225 0.0535  0.0246  241 TYR B O   
3678 C CB  . TYR B 215 ? 0.4178 0.3264 0.2522 -0.0143 0.0565  0.0396  241 TYR B CB  
3679 C CG  . TYR B 215 ? 0.4353 0.3340 0.2618 -0.0094 0.0608  0.0498  241 TYR B CG  
3680 C CD1 . TYR B 215 ? 0.4548 0.3489 0.2754 -0.0085 0.0695  0.0583  241 TYR B CD1 
3681 C CD2 . TYR B 215 ? 0.4424 0.3364 0.2676 -0.0050 0.0566  0.0516  241 TYR B CD2 
3682 C CE1 . TYR B 215 ? 0.4817 0.3655 0.2946 -0.0028 0.0739  0.0690  241 TYR B CE1 
3683 C CE2 . TYR B 215 ? 0.4674 0.3524 0.2861 0.0009  0.0605  0.0616  241 TYR B CE2 
3684 C CZ  . TYR B 215 ? 0.4764 0.3559 0.2884 0.0024  0.0690  0.0707  241 TYR B CZ  
3685 O OH  . TYR B 215 ? 0.5083 0.3784 0.3131 0.0097  0.0729  0.0819  241 TYR B OH  
3686 N N   . GLY B 216 ? 0.3875 0.3063 0.2554 -0.0310 0.0548  0.0196  242 GLY B N   
3687 C CA  . GLY B 216 ? 0.3816 0.3126 0.2573 -0.0332 0.0510  0.0124  242 GLY B CA  
3688 C C   . GLY B 216 ? 0.3812 0.3173 0.2516 -0.0281 0.0427  0.0095  242 GLY B C   
3689 O O   . GLY B 216 ? 0.3700 0.3152 0.2431 -0.0272 0.0405  0.0059  242 GLY B O   
3690 N N   . ARG B 217 ? 0.3555 0.2854 0.2194 -0.0249 0.0386  0.0109  243 ARG B N   
3691 C CA  . ARG B 217 ? 0.3614 0.2949 0.2209 -0.0211 0.0319  0.0082  243 ARG B CA  
3692 C C   . ARG B 217 ? 0.3525 0.2903 0.2191 -0.0230 0.0275  0.0025  243 ARG B C   
3693 O O   . ARG B 217 ? 0.3498 0.2853 0.2214 -0.0261 0.0272  0.0005  243 ARG B O   
3694 C CB  . ARG B 217 ? 0.3621 0.2898 0.2145 -0.0177 0.0292  0.0112  243 ARG B CB  
3695 C CG  . ARG B 217 ? 0.3820 0.3094 0.2247 -0.0138 0.0312  0.0166  243 ARG B CG  
3696 C CD  . ARG B 217 ? 0.3803 0.3034 0.2177 -0.0099 0.0296  0.0211  243 ARG B CD  
3697 N NE  . ARG B 217 ? 0.4032 0.3285 0.2305 -0.0056 0.0312  0.0266  243 ARG B NE  
3698 C CZ  . ARG B 217 ? 0.4100 0.3310 0.2317 -0.0014 0.0333  0.0341  243 ARG B CZ  
3699 N NH1 . ARG B 217 ? 0.3963 0.3095 0.2223 -0.0006 0.0342  0.0366  243 ARG B NH1 
3700 N NH2 . ARG B 217 ? 0.4354 0.3603 0.2467 0.0027  0.0347  0.0392  243 ARG B NH2 
3701 N N   . ALA B 218 ? 0.3357 0.2797 0.2021 -0.0206 0.0245  -0.0002 244 ALA B N   
3702 C CA  . ALA B 218 ? 0.3288 0.2773 0.1999 -0.0206 0.0202  -0.0040 244 ALA B CA  
3703 C C   . ALA B 218 ? 0.3379 0.2868 0.2042 -0.0163 0.0174  -0.0047 244 ALA B C   
3704 O O   . ALA B 218 ? 0.3328 0.2841 0.1978 -0.0143 0.0194  -0.0048 244 ALA B O   
3705 C CB  . ALA B 218 ? 0.3352 0.2929 0.2160 -0.0230 0.0213  -0.0067 244 ALA B CB  
3706 N N   . ASN B 219 ? 0.3285 0.2739 0.1921 -0.0152 0.0138  -0.0054 245 ASN B N   
3707 C CA  . ASN B 219 ? 0.3225 0.2659 0.1820 -0.0122 0.0121  -0.0062 245 ASN B CA  
3708 C C   . ASN B 219 ? 0.3089 0.2531 0.1704 -0.0108 0.0093  -0.0070 245 ASN B C   
3709 O O   . ASN B 219 ? 0.2821 0.2283 0.1460 -0.0125 0.0077  -0.0074 245 ASN B O   
3710 C CB  . ASN B 219 ? 0.3197 0.2580 0.1733 -0.0122 0.0111  -0.0056 245 ASN B CB  
3711 C CG  . ASN B 219 ? 0.3468 0.2850 0.1966 -0.0124 0.0130  -0.0036 245 ASN B CG  
3712 O OD1 . ASN B 219 ? 0.3397 0.2804 0.1885 -0.0120 0.0158  -0.0032 245 ASN B OD1 
3713 N ND2 . ASN B 219 ? 0.3356 0.2715 0.1830 -0.0125 0.0119  -0.0019 245 ASN B ND2 
3714 N N   . ASP B 220 ? 0.3131 0.2548 0.1727 -0.0078 0.0092  -0.0073 246 ASP B N   
3715 C CA  . ASP B 220 ? 0.3224 0.2625 0.1815 -0.0057 0.0073  -0.0065 246 ASP B CA  
3716 C C   . ASP B 220 ? 0.3354 0.2678 0.1909 -0.0041 0.0088  -0.0068 246 ASP B C   
3717 O O   . ASP B 220 ? 0.3291 0.2601 0.1844 -0.0029 0.0111  -0.0084 246 ASP B O   
3718 C CB  . ASP B 220 ? 0.3244 0.2721 0.1882 -0.0026 0.0062  -0.0059 246 ASP B CB  
3719 C CG  . ASP B 220 ? 0.3273 0.2760 0.1894 -0.0002 0.0035  -0.0041 246 ASP B CG  
3720 O OD1 . ASP B 220 ? 0.3074 0.2516 0.1653 -0.0024 0.0027  -0.0039 246 ASP B OD1 
3721 O OD2 . ASP B 220 ? 0.3573 0.3123 0.2220 0.0042  0.0022  -0.0027 246 ASP B OD2 
3722 N N   . ILE B 221 ? 0.3317 0.2590 0.1846 -0.0047 0.0082  -0.0060 247 ILE B N   
3723 C CA  . ILE B 221 ? 0.3540 0.2731 0.2048 -0.0041 0.0105  -0.0065 247 ILE B CA  
3724 C C   . ILE B 221 ? 0.3537 0.2693 0.2032 -0.0010 0.0108  -0.0029 247 ILE B C   
3725 O O   . ILE B 221 ? 0.3456 0.2643 0.1938 -0.0014 0.0087  -0.0010 247 ILE B O   
3726 C CB  . ILE B 221 ? 0.3598 0.2762 0.2089 -0.0084 0.0107  -0.0090 247 ILE B CB  
3727 C CG1 . ILE B 221 ? 0.3605 0.2784 0.2092 -0.0103 0.0090  -0.0075 247 ILE B CG1 
3728 C CG2 . ILE B 221 ? 0.3740 0.2946 0.2225 -0.0100 0.0103  -0.0118 247 ILE B CG2 
3729 C CD1 . ILE B 221 ? 0.3586 0.2757 0.2075 -0.0138 0.0093  -0.0097 247 ILE B CD1 
3730 N N   . ALA B 222 ? 0.3525 0.2612 0.2019 0.0025  0.0138  -0.0017 248 ALA B N   
3731 C CA  . ALA B 222 ? 0.3459 0.2515 0.1933 0.0074  0.0145  0.0035  248 ALA B CA  
3732 C C   . ALA B 222 ? 0.3568 0.2484 0.2029 0.0087  0.0199  0.0045  248 ALA B C   
3733 O O   . ALA B 222 ? 0.3705 0.2565 0.2185 0.0068  0.0229  0.0001  248 ALA B O   
3734 C CB  . ALA B 222 ? 0.3402 0.2547 0.1905 0.0132  0.0124  0.0056  248 ALA B CB  
3735 N N   . VAL B 223 ? 0.3683 0.2545 0.2109 0.0118  0.0216  0.0101  249 VAL B N   
3736 C CA  . VAL B 223 ? 0.3800 0.2519 0.2216 0.0155  0.0276  0.0135  249 VAL B CA  
3737 C C   . VAL B 223 ? 0.4018 0.2775 0.2417 0.0253  0.0263  0.0207  249 VAL B C   
3738 O O   . VAL B 223 ? 0.3987 0.2853 0.2357 0.0274  0.0217  0.0240  249 VAL B O   
3739 C CB  . VAL B 223 ? 0.3943 0.2554 0.2328 0.0113  0.0320  0.0152  249 VAL B CB  
3740 C CG1 . VAL B 223 ? 0.4104 0.2536 0.2486 0.0142  0.0399  0.0183  249 VAL B CG1 
3741 C CG2 . VAL B 223 ? 0.3902 0.2539 0.2314 0.0019  0.0312  0.0080  249 VAL B CG2 
3742 N N   . VAL B 224 ? 0.4035 0.2716 0.2457 0.0315  0.0303  0.0224  250 VAL B N   
3743 C CA  . VAL B 224 ? 0.4182 0.2910 0.2599 0.0423  0.0291  0.0297  250 VAL B CA  
3744 C C   . VAL B 224 ? 0.4435 0.2970 0.2825 0.0481  0.0370  0.0361  250 VAL B C   
3745 O O   . VAL B 224 ? 0.4575 0.2948 0.2976 0.0432  0.0436  0.0322  250 VAL B O   
3746 C CB  . VAL B 224 ? 0.4225 0.3073 0.2714 0.0462  0.0265  0.0264  250 VAL B CB  
3747 C CG1 . VAL B 224 ? 0.4036 0.3030 0.2555 0.0384  0.0211  0.0195  250 VAL B CG1 
3748 C CG2 . VAL B 224 ? 0.4346 0.3068 0.2875 0.0477  0.0331  0.0228  250 VAL B CG2 
3749 N N   . TRP B 225 ? 0.4512 0.3067 0.2864 0.0585  0.0364  0.0458  251 TRP B N   
3750 C CA  . TRP B 225 ? 0.4791 0.3157 0.3109 0.0662  0.0443  0.0542  251 TRP B CA  
3751 C C   . TRP B 225 ? 0.4919 0.3356 0.3265 0.0802  0.0429  0.0606  251 TRP B C   
3752 O O   . TRP B 225 ? 0.4929 0.3574 0.3268 0.0853  0.0350  0.0636  251 TRP B O   
3753 C CB  . TRP B 225 ? 0.4950 0.3261 0.3171 0.0667  0.0460  0.0626  251 TRP B CB  
3754 C CG  . TRP B 225 ? 0.4942 0.3136 0.3147 0.0546  0.0506  0.0582  251 TRP B CG  
3755 C CD1 . TRP B 225 ? 0.5208 0.3175 0.3405 0.0516  0.0607  0.0601  251 TRP B CD1 
3756 C CD2 . TRP B 225 ? 0.4802 0.3108 0.3005 0.0442  0.0457  0.0513  251 TRP B CD2 
3757 N NE1 . TRP B 225 ? 0.5102 0.3056 0.3301 0.0398  0.0619  0.0545  251 TRP B NE1 
3758 C CE2 . TRP B 225 ? 0.4881 0.3040 0.3082 0.0357  0.0527  0.0494  251 TRP B CE2 
3759 C CE3 . TRP B 225 ? 0.4714 0.3226 0.2926 0.0413  0.0366  0.0465  251 TRP B CE3 
3760 C CZ2 . TRP B 225 ? 0.4764 0.2991 0.2974 0.0256  0.0504  0.0432  251 TRP B CZ2 
3761 C CZ3 . TRP B 225 ? 0.4638 0.3190 0.2849 0.0315  0.0350  0.0408  251 TRP B CZ3 
3762 C CH2 . TRP B 225 ? 0.4528 0.2947 0.2738 0.0243  0.0415  0.0394  251 TRP B CH2 
3763 N N   . SER B 226 ? 0.4930 0.3200 0.3313 0.0859  0.0508  0.0618  252 SER B N   
3764 C CA  . SER B 226 ? 0.5201 0.3521 0.3623 0.1005  0.0509  0.0683  252 SER B CA  
3765 C C   . SER B 226 ? 0.5376 0.3690 0.3714 0.1123  0.0507  0.0827  252 SER B C   
3766 O O   . SER B 226 ? 0.5430 0.3642 0.3678 0.1087  0.0533  0.0875  252 SER B O   
3767 C CB  . SER B 226 ? 0.5307 0.3419 0.3784 0.1040  0.0608  0.0658  252 SER B CB  
3768 O OG  . SER B 226 ? 0.5499 0.3349 0.3920 0.1079  0.0706  0.0739  252 SER B OG  
3769 N N   . PRO B 227 ? 0.5585 0.4018 0.3950 0.1272  0.0478  0.0903  254 PRO B N   
3770 C CA  . PRO B 227 ? 0.5842 0.4272 0.4117 0.1407  0.0478  0.1055  254 PRO B CA  
3771 C C   . PRO B 227 ? 0.6296 0.4397 0.4498 0.1444  0.0603  0.1148  254 PRO B C   
3772 O O   . PRO B 227 ? 0.6643 0.4711 0.4735 0.1517  0.0613  0.1274  254 PRO B O   
3773 C CB  . PRO B 227 ? 0.5899 0.4499 0.4255 0.1562  0.0440  0.1098  254 PRO B CB  
3774 C CG  . PRO B 227 ? 0.5549 0.4345 0.4023 0.1478  0.0380  0.0961  254 PRO B CG  
3775 C CD  . PRO B 227 ? 0.5497 0.4101 0.3980 0.1320  0.0440  0.0850  254 PRO B CD  
3776 N N   . THR B 228 ? 0.6419 0.4276 0.4679 0.1390  0.0704  0.1086  255 THR B N   
3777 C CA  . THR B 228 ? 0.6747 0.4270 0.4956 0.1393  0.0836  0.1151  255 THR B CA  
3778 C C   . THR B 228 ? 0.6615 0.4032 0.4790 0.1214  0.0867  0.1077  255 THR B C   
3779 O O   . THR B 228 ? 0.6745 0.3891 0.4896 0.1179  0.0981  0.1104  255 THR B O   
3780 C CB  . THR B 228 ? 0.7007 0.4318 0.5304 0.1440  0.0938  0.1118  255 THR B CB  
3781 O OG1 . THR B 228 ? 0.6728 0.4089 0.5108 0.1306  0.0918  0.0947  255 THR B OG1 
3782 C CG2 . THR B 228 ? 0.7228 0.4640 0.5573 0.1629  0.0919  0.1196  255 THR B CG2 
3783 N N   . GLY B 229 ? 0.6296 0.3924 0.4477 0.1099  0.0771  0.0982  256 GLY B N   
3784 C CA  . GLY B 229 ? 0.6113 0.3682 0.4261 0.0948  0.0789  0.0926  256 GLY B CA  
3785 C C   . GLY B 229 ? 0.6053 0.3535 0.4288 0.0808  0.0823  0.0775  256 GLY B C   
3786 O O   . GLY B 229 ? 0.6197 0.3613 0.4426 0.0684  0.0852  0.0724  256 GLY B O   
3787 N N   . VAL B 230 ? 0.5862 0.3372 0.4179 0.0825  0.0815  0.0697  257 VAL B N   
3788 C CA  . VAL B 230 ? 0.5621 0.3061 0.4005 0.0701  0.0846  0.0553  257 VAL B CA  
3789 C C   . VAL B 230 ? 0.5264 0.2941 0.3663 0.0603  0.0741  0.0460  257 VAL B C   
3790 O O   . VAL B 230 ? 0.4863 0.2744 0.3278 0.0649  0.0659  0.0459  257 VAL B O   
3791 C CB  . VAL B 230 ? 0.5822 0.3179 0.4276 0.0757  0.0894  0.0502  257 VAL B CB  
3792 C CG1 . VAL B 230 ? 0.5678 0.3003 0.4182 0.0623  0.0911  0.0341  257 VAL B CG1 
3793 C CG2 . VAL B 230 ? 0.6187 0.3280 0.4633 0.0861  0.1011  0.0594  257 VAL B CG2 
3794 N N   . PRO B 231 ? 0.5073 0.2730 0.3475 0.0466  0.0745  0.0381  258 PRO B N   
3795 C CA  . PRO B 231 ? 0.4841 0.2706 0.3256 0.0383  0.0653  0.0302  258 PRO B CA  
3796 C C   . PRO B 231 ? 0.4730 0.2649 0.3202 0.0334  0.0636  0.0183  258 PRO B C   
3797 O O   . PRO B 231 ? 0.4999 0.2772 0.3501 0.0312  0.0705  0.0121  258 PRO B O   
3798 C CB  . PRO B 231 ? 0.4830 0.2647 0.3225 0.0278  0.0673  0.0285  258 PRO B CB  
3799 C CG  . PRO B 231 ? 0.5086 0.2651 0.3499 0.0255  0.0789  0.0282  258 PRO B CG  
3800 C CD  . PRO B 231 ? 0.5359 0.2803 0.3759 0.0390  0.0840  0.0370  258 PRO B CD  
3801 N N   . TYR B 232 ? 0.4573 0.2699 0.3053 0.0320  0.0550  0.0153  259 TYR B N   
3802 C CA  . TYR B 232 ? 0.4541 0.2748 0.3055 0.0265  0.0526  0.0048  259 TYR B CA  
3803 C C   . TYR B 232 ? 0.4426 0.2800 0.2929 0.0195  0.0448  0.0023  259 TYR B C   
3804 O O   . TYR B 232 ? 0.4304 0.2768 0.2783 0.0214  0.0402  0.0083  259 TYR B O   
3805 C CB  . TYR B 232 ? 0.4600 0.2890 0.3147 0.0346  0.0513  0.0049  259 TYR B CB  
3806 C CG  . TYR B 232 ? 0.4853 0.2995 0.3420 0.0442  0.0587  0.0087  259 TYR B CG  
3807 C CD1 . TYR B 232 ? 0.4975 0.3113 0.3531 0.0550  0.0587  0.0200  259 TYR B CD1 
3808 C CD2 . TYR B 232 ? 0.5070 0.3079 0.3661 0.0431  0.0659  0.0010  259 TYR B CD2 
3809 C CE1 . TYR B 232 ? 0.5309 0.3305 0.3883 0.0653  0.0659  0.0248  259 TYR B CE1 
3810 C CE2 . TYR B 232 ? 0.5421 0.3276 0.4034 0.0526  0.0736  0.0045  259 TYR B CE2 
3811 C CZ  . TYR B 232 ? 0.5540 0.3387 0.4148 0.0643  0.0737  0.0171  259 TYR B CZ  
3812 O OH  . TYR B 232 ? 0.6007 0.3701 0.4636 0.0754  0.0814  0.0224  259 TYR B OH  
3813 N N   . VAL B 233 ? 0.4131 0.2543 0.2645 0.0119  0.0437  -0.0068 260 VAL B N   
3814 C CA  . VAL B 233 ? 0.4003 0.2566 0.2509 0.0066  0.0369  -0.0087 260 VAL B CA  
3815 C C   . VAL B 233 ? 0.4003 0.2683 0.2522 0.0085  0.0339  -0.0118 260 VAL B C   
3816 O O   . VAL B 233 ? 0.4002 0.2643 0.2530 0.0090  0.0373  -0.0170 260 VAL B O   
3817 C CB  . VAL B 233 ? 0.4026 0.2576 0.2532 -0.0028 0.0371  -0.0152 260 VAL B CB  
3818 C CG1 . VAL B 233 ? 0.3956 0.2659 0.2456 -0.0066 0.0304  -0.0167 260 VAL B CG1 
3819 C CG2 . VAL B 233 ? 0.4326 0.2762 0.2832 -0.0055 0.0413  -0.0123 260 VAL B CG2 
3820 N N   . VAL B 234 ? 0.3885 0.2700 0.2406 0.0091  0.0283  -0.0088 261 VAL B N   
3821 C CA  . VAL B 234 ? 0.3877 0.2805 0.2420 0.0109  0.0263  -0.0104 261 VAL B CA  
3822 C C   . VAL B 234 ? 0.3630 0.2657 0.2160 0.0053  0.0218  -0.0119 261 VAL B C   
3823 O O   . VAL B 234 ? 0.3632 0.2704 0.2160 0.0043  0.0184  -0.0085 261 VAL B O   
3824 C CB  . VAL B 234 ? 0.3827 0.2826 0.2406 0.0184  0.0250  -0.0049 261 VAL B CB  
3825 C CG1 . VAL B 234 ? 0.3929 0.3053 0.2548 0.0192  0.0240  -0.0071 261 VAL B CG1 
3826 C CG2 . VAL B 234 ? 0.3919 0.2808 0.2507 0.0257  0.0298  -0.0019 261 VAL B CG2 
3827 N N   . ALA B 235 ? 0.3490 0.2542 0.2004 0.0020  0.0223  -0.0169 262 ALA B N   
3828 C CA  . ALA B 235 ? 0.3540 0.2680 0.2039 -0.0018 0.0189  -0.0171 262 ALA B CA  
3829 C C   . ALA B 235 ? 0.3593 0.2813 0.2105 -0.0001 0.0198  -0.0173 262 ALA B C   
3830 O O   . ALA B 235 ? 0.3589 0.2798 0.2088 0.0012  0.0230  -0.0208 262 ALA B O   
3831 C CB  . ALA B 235 ? 0.3529 0.2655 0.1991 -0.0066 0.0185  -0.0215 262 ALA B CB  
3832 N N   . VAL B 236 ? 0.3660 0.2956 0.2197 -0.0005 0.0175  -0.0140 263 VAL B N   
3833 C CA  . VAL B 236 ? 0.3654 0.3029 0.2215 0.0000  0.0190  -0.0137 263 VAL B CA  
3834 C C   . VAL B 236 ? 0.3502 0.2911 0.2047 -0.0040 0.0174  -0.0119 263 VAL B C   
3835 O O   . VAL B 236 ? 0.3353 0.2762 0.1913 -0.0056 0.0146  -0.0099 263 VAL B O   
3836 C CB  . VAL B 236 ? 0.3945 0.3387 0.2583 0.0036  0.0192  -0.0118 263 VAL B CB  
3837 C CG1 . VAL B 236 ? 0.4211 0.3745 0.2890 0.0029  0.0217  -0.0120 263 VAL B CG1 
3838 C CG2 . VAL B 236 ? 0.4109 0.3510 0.2765 0.0093  0.0213  -0.0122 263 VAL B CG2 
3839 N N   . MET B 237 ? 0.3582 0.3011 0.2087 -0.0051 0.0195  -0.0125 264 MET B N   
3840 C CA  . MET B 237 ? 0.3538 0.2981 0.2015 -0.0077 0.0191  -0.0098 264 MET B CA  
3841 C C   . MET B 237 ? 0.3477 0.2970 0.1964 -0.0078 0.0233  -0.0082 264 MET B C   
3842 O O   . MET B 237 ? 0.3259 0.2776 0.1739 -0.0060 0.0265  -0.0103 264 MET B O   
3843 C CB  . MET B 237 ? 0.3655 0.3076 0.2054 -0.0082 0.0174  -0.0110 264 MET B CB  
3844 C CG  . MET B 237 ? 0.3656 0.3032 0.2062 -0.0089 0.0144  -0.0133 264 MET B CG  
3845 S SD  . MET B 237 ? 0.3996 0.3387 0.2344 -0.0105 0.0115  -0.0149 264 MET B SD  
3846 C CE  . MET B 237 ? 0.3833 0.3231 0.2203 -0.0106 0.0099  -0.0090 264 MET B CE  
3847 N N   . SER B 238 ? 0.3390 0.2892 0.1899 -0.0102 0.0243  -0.0047 265 SER B N   
3848 C CA  . SER B 238 ? 0.3384 0.2924 0.1907 -0.0112 0.0296  -0.0027 265 SER B CA  
3849 C C   . SER B 238 ? 0.3469 0.2972 0.1970 -0.0135 0.0313  0.0021  265 SER B C   
3850 O O   . SER B 238 ? 0.3535 0.2995 0.2048 -0.0147 0.0284  0.0031  265 SER B O   
3851 C CB  . SER B 238 ? 0.3405 0.3013 0.2040 -0.0121 0.0312  -0.0042 265 SER B CB  
3852 O OG  . SER B 238 ? 0.3350 0.2959 0.2052 -0.0154 0.0291  -0.0038 265 SER B OG  
3853 N N   . ASP B 239 ? 0.3540 0.3055 0.2007 -0.0138 0.0369  0.0054  266 ASP B N   
3854 C CA  . ASP B 239 ? 0.3813 0.3281 0.2278 -0.0160 0.0408  0.0109  266 ASP B CA  
3855 C C   . ASP B 239 ? 0.3729 0.3234 0.2225 -0.0180 0.0486  0.0128  266 ASP B C   
3856 O O   . ASP B 239 ? 0.3705 0.3277 0.2204 -0.0167 0.0504  0.0100  266 ASP B O   
3857 C CB  . ASP B 239 ? 0.4045 0.3464 0.2397 -0.0129 0.0397  0.0157  266 ASP B CB  
3858 C CG  . ASP B 239 ? 0.4573 0.4030 0.2808 -0.0094 0.0416  0.0173  266 ASP B CG  
3859 O OD1 . ASP B 239 ? 0.5179 0.4646 0.3390 -0.0098 0.0484  0.0209  266 ASP B OD1 
3860 O OD2 . ASP B 239 ? 0.4740 0.4218 0.2904 -0.0066 0.0365  0.0150  266 ASP B OD2 
3861 N N   . ARG B 240 ? 0.3825 0.3279 0.2352 -0.0215 0.0538  0.0173  267 ARG B N   
3862 C CA  . ARG B 240 ? 0.3850 0.3327 0.2418 -0.0247 0.0626  0.0199  267 ARG B CA  
3863 C C   . ARG B 240 ? 0.4089 0.3466 0.2573 -0.0242 0.0686  0.0287  267 ARG B C   
3864 O O   . ARG B 240 ? 0.4053 0.3374 0.2607 -0.0291 0.0752  0.0315  267 ARG B O   
3865 C CB  . ARG B 240 ? 0.3916 0.3444 0.2653 -0.0310 0.0643  0.0153  267 ARG B CB  
3866 C CG  . ARG B 240 ? 0.3798 0.3430 0.2613 -0.0299 0.0577  0.0080  267 ARG B CG  
3867 C CD  . ARG B 240 ? 0.3932 0.3633 0.2907 -0.0359 0.0576  0.0032  267 ARG B CD  
3868 N NE  . ARG B 240 ? 0.4254 0.4033 0.3321 -0.0401 0.0658  0.0034  267 ARG B NE  
3869 C CZ  . ARG B 240 ? 0.4300 0.4056 0.3447 -0.0472 0.0728  0.0044  267 ARG B CZ  
3870 N NH1 . ARG B 240 ? 0.4254 0.3919 0.3426 -0.0518 0.0722  0.0039  267 ARG B NH1 
3871 N NH2 . ARG B 240 ? 0.4611 0.4436 0.3821 -0.0501 0.0812  0.0055  267 ARG B NH2 
3872 N N   . ALA B 241 ? 0.4354 0.3716 0.2688 -0.0182 0.0667  0.0329  268 ALA B N   
3873 C CA  . ALA B 241 ? 0.4785 0.4060 0.3019 -0.0155 0.0716  0.0427  268 ALA B CA  
3874 C C   . ALA B 241 ? 0.4896 0.4157 0.3125 -0.0180 0.0830  0.0484  268 ALA B C   
3875 O O   . ALA B 241 ? 0.5166 0.4322 0.3360 -0.0178 0.0897  0.0572  268 ALA B O   
3876 C CB  . ALA B 241 ? 0.5268 0.4571 0.3345 -0.0082 0.0661  0.0452  268 ALA B CB  
3877 N N   . GLY B 242 ? 0.4740 0.4101 0.3016 -0.0204 0.0861  0.0437  269 GLY B N   
3878 C CA  . GLY B 242 ? 0.4850 0.4218 0.3170 -0.0247 0.0977  0.0473  269 GLY B CA  
3879 C C   . GLY B 242 ? 0.5016 0.4303 0.3484 -0.0325 0.1037  0.0485  269 GLY B C   
3880 O O   . GLY B 242 ? 0.4972 0.4214 0.3458 -0.0362 0.1149  0.0543  269 GLY B O   
3881 N N   . GLY B 243 ? 0.5049 0.4317 0.3626 -0.0356 0.0971  0.0424  270 GLY B N   
3882 C CA  . GLY B 243 ? 0.5128 0.4317 0.3841 -0.0436 0.1025  0.0418  270 GLY B CA  
3883 C C   . GLY B 243 ? 0.5109 0.4118 0.3755 -0.0417 0.1045  0.0491  270 GLY B C   
3884 O O   . GLY B 243 ? 0.5364 0.4279 0.4117 -0.0482 0.1091  0.0479  270 GLY B O   
3885 N N   . GLY B 244 ? 0.4906 0.3875 0.3387 -0.0327 0.1008  0.0559  271 GLY B N   
3886 C CA  . GLY B 244 ? 0.4892 0.3708 0.3308 -0.0285 0.1015  0.0633  271 GLY B CA  
3887 C C   . GLY B 244 ? 0.4773 0.3572 0.3244 -0.0282 0.0922  0.0566  271 GLY B C   
3888 O O   . GLY B 244 ? 0.4466 0.3369 0.3010 -0.0308 0.0846  0.0468  271 GLY B O   
3889 N N   . TYR B 245 ? 0.4935 0.3593 0.3371 -0.0246 0.0939  0.0627  272 TYR B N   
3890 C CA  . TYR B 245 ? 0.4917 0.3540 0.3393 -0.0233 0.0867  0.0578  272 TYR B CA  
3891 C C   . TYR B 245 ? 0.4686 0.3347 0.3315 -0.0326 0.0847  0.0457  272 TYR B C   
3892 O O   . TYR B 245 ? 0.4247 0.2982 0.2899 -0.0321 0.0756  0.0383  272 TYR B O   
3893 C CB  . TYR B 245 ? 0.5057 0.3496 0.3503 -0.0193 0.0932  0.0669  272 TYR B CB  
3894 C CG  . TYR B 245 ? 0.4965 0.3361 0.3440 -0.0166 0.0870  0.0628  272 TYR B CG  
3895 C CD1 . TYR B 245 ? 0.4956 0.3296 0.3557 -0.0242 0.0878  0.0535  272 TYR B CD1 
3896 C CD2 . TYR B 245 ? 0.4931 0.3364 0.3311 -0.0066 0.0800  0.0672  272 TYR B CD2 
3897 C CE1 . TYR B 245 ? 0.4913 0.3219 0.3534 -0.0216 0.0828  0.0494  272 TYR B CE1 
3898 C CE2 . TYR B 245 ? 0.4980 0.3390 0.3397 -0.0042 0.0749  0.0632  272 TYR B CE2 
3899 C CZ  . TYR B 245 ? 0.4928 0.3270 0.3461 -0.0115 0.0765  0.0544  272 TYR B CZ  
3900 O OH  . TYR B 245 ? 0.4764 0.3079 0.3327 -0.0091 0.0726  0.0502  272 TYR B OH  
3901 N N   . ASP B 246 ? 0.4861 0.3481 0.3594 -0.0412 0.0934  0.0439  273 ASP B N   
3902 C CA  . ASP B 246 ? 0.4991 0.3645 0.3876 -0.0506 0.0924  0.0325  273 ASP B CA  
3903 C C   . ASP B 246 ? 0.4776 0.3623 0.3735 -0.0548 0.0886  0.0250  273 ASP B C   
3904 O O   . ASP B 246 ? 0.4574 0.3485 0.3667 -0.0629 0.0882  0.0159  273 ASP B O   
3905 C CB  . ASP B 246 ? 0.5525 0.4032 0.4506 -0.0588 0.1041  0.0330  273 ASP B CB  
3906 C CG  . ASP B 246 ? 0.6201 0.4698 0.5200 -0.0627 0.1152  0.0391  273 ASP B CG  
3907 O OD1 . ASP B 246 ? 0.6634 0.5189 0.5521 -0.0562 0.1152  0.0467  273 ASP B OD1 
3908 O OD2 . ASP B 246 ? 0.7024 0.5458 0.6148 -0.0727 0.1242  0.0357  273 ASP B OD2 
3909 N N   . ALA B 247 ? 0.4768 0.3718 0.3644 -0.0490 0.0853  0.0281  274 ALA B N   
3910 C CA  . ALA B 247 ? 0.4504 0.3631 0.3451 -0.0514 0.0817  0.0213  274 ALA B CA  
3911 C C   . ALA B 247 ? 0.4163 0.3368 0.3182 -0.0530 0.0723  0.0117  274 ALA B C   
3912 O O   . ALA B 247 ? 0.3917 0.3074 0.2872 -0.0487 0.0659  0.0114  274 ALA B O   
3913 C CB  . ALA B 247 ? 0.4311 0.3513 0.3143 -0.0439 0.0787  0.0249  274 ALA B CB  
3914 N N   A GLU B 248 ? 0.4192 0.3533 0.3343 -0.0587 0.0715  0.0041  275 GLU B N   
3915 N N   B GLU B 248 ? 0.4079 0.3419 0.3230 -0.0588 0.0714  0.0041  275 GLU B N   
3916 C CA  A GLU B 248 ? 0.4134 0.3575 0.3345 -0.0597 0.0625  -0.0045 275 GLU B CA  
3917 C CA  B GLU B 248 ? 0.3937 0.3372 0.3145 -0.0596 0.0624  -0.0044 275 GLU B CA  
3918 C C   A GLU B 248 ? 0.3924 0.3446 0.3057 -0.0514 0.0545  -0.0040 275 GLU B C   
3919 C C   B GLU B 248 ? 0.3816 0.3336 0.2948 -0.0514 0.0545  -0.0040 275 GLU B C   
3920 O O   A GLU B 248 ? 0.3721 0.3317 0.2842 -0.0485 0.0560  -0.0021 275 GLU B O   
3921 O O   B GLU B 248 ? 0.3636 0.3229 0.2757 -0.0486 0.0562  -0.0020 275 GLU B O   
3922 C CB  A GLU B 248 ? 0.4335 0.3927 0.3714 -0.0674 0.0640  -0.0121 275 GLU B CB  
3923 C CB  B GLU B 248 ? 0.3961 0.3543 0.3336 -0.0675 0.0630  -0.0127 275 GLU B CB  
3924 C CG  A GLU B 248 ? 0.4665 0.4181 0.4146 -0.0777 0.0718  -0.0152 275 GLU B CG  
3925 C CG  B GLU B 248 ? 0.4113 0.3612 0.3585 -0.0775 0.0708  -0.0157 275 GLU B CG  
3926 C CD  A GLU B 248 ? 0.4946 0.4415 0.4453 -0.0815 0.0676  -0.0224 275 GLU B CD  
3927 C CD  B GLU B 248 ? 0.4148 0.3819 0.3804 -0.0867 0.0721  -0.0247 275 GLU B CD  
3928 O OE1 A GLU B 248 ? 0.4844 0.4340 0.4282 -0.0760 0.0584  -0.0244 275 GLU B OE1 
3929 O OE1 B GLU B 248 ? 0.4017 0.3882 0.3727 -0.0842 0.0674  -0.0273 275 GLU B OE1 
3930 O OE2 A GLU B 248 ? 0.5379 0.4777 0.4977 -0.0907 0.0745  -0.0264 275 GLU B OE2 
3931 O OE2 B GLU B 248 ? 0.4233 0.3841 0.3982 -0.0963 0.0782  -0.0292 275 GLU B OE2 
3932 N N   . PRO B 249 ? 0.3763 0.3268 0.2843 -0.0477 0.0466  -0.0062 276 PRO B N   
3933 C CA  . PRO B 249 ? 0.3688 0.3269 0.2718 -0.0412 0.0397  -0.0068 276 PRO B CA  
3934 C C   . PRO B 249 ? 0.3779 0.3527 0.2919 -0.0425 0.0372  -0.0122 276 PRO B C   
3935 O O   . PRO B 249 ? 0.3702 0.3517 0.2950 -0.0487 0.0377  -0.0172 276 PRO B O   
3936 C CB  . PRO B 249 ? 0.3838 0.3356 0.2805 -0.0386 0.0336  -0.0078 276 PRO B CB  
3937 C CG  . PRO B 249 ? 0.3924 0.3330 0.2902 -0.0430 0.0373  -0.0076 276 PRO B CG  
3938 C CD  . PRO B 249 ? 0.3919 0.3331 0.2992 -0.0499 0.0449  -0.0084 276 PRO B CD  
3939 N N   . ARG B 250 ? 0.3658 0.3476 0.2775 -0.0364 0.0343  -0.0116 277 ARG B N   
3940 C CA  . ARG B 250 ? 0.3689 0.3672 0.2909 -0.0355 0.0323  -0.0154 277 ARG B CA  
3941 C C   . ARG B 250 ? 0.3747 0.3754 0.2920 -0.0285 0.0251  -0.0158 277 ARG B C   
3942 O O   . ARG B 250 ? 0.3512 0.3485 0.2619 -0.0226 0.0252  -0.0133 277 ARG B O   
3943 C CB  . ARG B 250 ? 0.3892 0.3934 0.3143 -0.0339 0.0383  -0.0136 277 ARG B CB  
3944 C CG  . ARG B 250 ? 0.3937 0.3976 0.3253 -0.0412 0.0467  -0.0128 277 ARG B CG  
3945 C CD  . ARG B 250 ? 0.4104 0.4279 0.3587 -0.0483 0.0470  -0.0187 277 ARG B CD  
3946 N NE  . ARG B 250 ? 0.4440 0.4606 0.3993 -0.0554 0.0570  -0.0174 277 ARG B NE  
3947 C CZ  . ARG B 250 ? 0.4640 0.4753 0.4257 -0.0644 0.0613  -0.0194 277 ARG B CZ  
3948 N NH1 . ARG B 250 ? 0.4726 0.4833 0.4373 -0.0679 0.0558  -0.0248 277 ARG B NH1 
3949 N NH2 . ARG B 250 ? 0.4807 0.4869 0.4461 -0.0701 0.0718  -0.0163 277 ARG B NH2 
3950 N N   . GLU B 251 ? 0.3617 0.3679 0.2820 -0.0293 0.0194  -0.0191 278 GLU B N   
3951 C CA  . GLU B 251 ? 0.3568 0.3638 0.2716 -0.0226 0.0134  -0.0183 278 GLU B CA  
3952 C C   . GLU B 251 ? 0.3345 0.3524 0.2545 -0.0162 0.0131  -0.0176 278 GLU B C   
3953 O O   . GLU B 251 ? 0.3194 0.3320 0.2327 -0.0095 0.0116  -0.0150 278 GLU B O   
3954 C CB  . GLU B 251 ? 0.3569 0.3703 0.2735 -0.0245 0.0077  -0.0220 278 GLU B CB  
3955 C CG  . GLU B 251 ? 0.3525 0.3531 0.2627 -0.0291 0.0081  -0.0228 278 GLU B CG  
3956 C CD  . GLU B 251 ? 0.3618 0.3680 0.2706 -0.0294 0.0022  -0.0265 278 GLU B CD  
3957 O OE1 . GLU B 251 ? 0.3461 0.3653 0.2633 -0.0337 0.0003  -0.0322 278 GLU B OE1 
3958 O OE2 . GLU B 251 ? 0.3652 0.3634 0.2642 -0.0252 -0.0002 -0.0238 278 GLU B OE2 
3959 N N   . ALA B 252 ? 0.3337 0.3663 0.2662 -0.0187 0.0154  -0.0202 279 ALA B N   
3960 C CA  . ALA B 252 ? 0.3337 0.3794 0.2737 -0.0121 0.0154  -0.0199 279 ALA B CA  
3961 C C   . ALA B 252 ? 0.3322 0.3675 0.2651 -0.0070 0.0203  -0.0166 279 ALA B C   
3962 O O   . ALA B 252 ? 0.3402 0.3789 0.2741 0.0009  0.0196  -0.0155 279 ALA B O   
3963 C CB  . ALA B 252 ? 0.3383 0.4028 0.2946 -0.0169 0.0177  -0.0239 279 ALA B CB  
3964 N N   . LEU B 253 ? 0.3353 0.3581 0.2608 -0.0111 0.0252  -0.0153 280 LEU B N   
3965 C CA  . LEU B 253 ? 0.3441 0.3576 0.2610 -0.0071 0.0294  -0.0134 280 LEU B CA  
3966 C C   . LEU B 253 ? 0.3464 0.3500 0.2542 -0.0011 0.0254  -0.0123 280 LEU B C   
3967 O O   . LEU B 253 ? 0.3280 0.3301 0.2345 0.0049  0.0273  -0.0124 280 LEU B O   
3968 C CB  . LEU B 253 ? 0.3599 0.3632 0.2690 -0.0123 0.0340  -0.0116 280 LEU B CB  
3969 C CG  . LEU B 253 ? 0.3725 0.3649 0.2686 -0.0090 0.0364  -0.0102 280 LEU B CG  
3970 C CD1 . LEU B 253 ? 0.3756 0.3742 0.2744 -0.0044 0.0411  -0.0117 280 LEU B CD1 
3971 C CD2 . LEU B 253 ? 0.3906 0.3750 0.2784 -0.0132 0.0399  -0.0072 280 LEU B CD2 
3972 N N   . LEU B 254 ? 0.3384 0.3353 0.2409 -0.0029 0.0206  -0.0116 281 LEU B N   
3973 C CA  . LEU B 254 ? 0.3469 0.3338 0.2413 0.0015  0.0176  -0.0103 281 LEU B CA  
3974 C C   . LEU B 254 ? 0.3481 0.3423 0.2478 0.0085  0.0151  -0.0095 281 LEU B C   
3975 O O   . LEU B 254 ? 0.3478 0.3345 0.2436 0.0143  0.0161  -0.0082 281 LEU B O   
3976 C CB  . LEU B 254 ? 0.3527 0.3318 0.2408 -0.0021 0.0141  -0.0096 281 LEU B CB  
3977 C CG  . LEU B 254 ? 0.3771 0.3495 0.2605 -0.0077 0.0162  -0.0094 281 LEU B CG  
3978 C CD1 . LEU B 254 ? 0.3948 0.3616 0.2744 -0.0103 0.0128  -0.0091 281 LEU B CD1 
3979 C CD2 . LEU B 254 ? 0.3934 0.3578 0.2689 -0.0065 0.0192  -0.0089 281 LEU B CD2 
3980 N N   . ALA B 255 ? 0.3256 0.3345 0.2343 0.0082  0.0118  -0.0102 282 ALA B N   
3981 C CA  . ALA B 255 ? 0.3454 0.3643 0.2592 0.0161  0.0086  -0.0086 282 ALA B CA  
3982 C C   . ALA B 255 ? 0.3532 0.3749 0.2722 0.0228  0.0132  -0.0081 282 ALA B C   
3983 O O   . ALA B 255 ? 0.3498 0.3676 0.2672 0.0313  0.0132  -0.0052 282 ALA B O   
3984 C CB  . ALA B 255 ? 0.3449 0.3830 0.2685 0.0138  0.0040  -0.0108 282 ALA B CB  
3985 N N   . GLU B 256 ? 0.3600 0.3874 0.2850 0.0193  0.0180  -0.0107 283 GLU B N   
3986 C CA  . GLU B 256 ? 0.3652 0.3959 0.2952 0.0253  0.0234  -0.0111 283 GLU B CA  
3987 C C   . GLU B 256 ? 0.3645 0.3761 0.2832 0.0285  0.0272  -0.0108 283 GLU B C   
3988 O O   . GLU B 256 ? 0.3669 0.3760 0.2871 0.0366  0.0299  -0.0103 283 GLU B O   
3989 C CB  . GLU B 256 ? 0.3840 0.4236 0.3209 0.0198  0.0289  -0.0139 283 GLU B CB  
3990 C CG  . GLU B 256 ? 0.3923 0.4543 0.3450 0.0173  0.0271  -0.0156 283 GLU B CG  
3991 C CD  . GLU B 256 ? 0.4158 0.4842 0.3750 0.0116  0.0346  -0.0178 283 GLU B CD  
3992 O OE1 . GLU B 256 ? 0.4220 0.4875 0.3797 0.0158  0.0409  -0.0179 283 GLU B OE1 
3993 O OE2 . GLU B 256 ? 0.4156 0.4910 0.3810 0.0028  0.0349  -0.0195 283 GLU B OE2 
3994 N N   . ALA B 257 ? 0.3484 0.3470 0.2564 0.0222  0.0276  -0.0116 284 ALA B N   
3995 C CA  . ALA B 257 ? 0.3641 0.3465 0.2620 0.0238  0.0306  -0.0128 284 ALA B CA  
3996 C C   . ALA B 257 ? 0.3736 0.3473 0.2692 0.0298  0.0284  -0.0104 284 ALA B C   
3997 O O   . ALA B 257 ? 0.3763 0.3406 0.2699 0.0350  0.0324  -0.0114 284 ALA B O   
3998 C CB  . ALA B 257 ? 0.3549 0.3285 0.2428 0.0163  0.0301  -0.0138 284 ALA B CB  
3999 N N   . ALA B 258 ? 0.3706 0.3464 0.2660 0.0290  0.0227  -0.0073 285 ALA B N   
4000 C CA  . ALA B 258 ? 0.3611 0.3291 0.2534 0.0347  0.0209  -0.0035 285 ALA B CA  
4001 C C   . ALA B 258 ? 0.3631 0.3372 0.2628 0.0452  0.0224  -0.0008 285 ALA B C   
4002 O O   . ALA B 258 ? 0.3700 0.3313 0.2665 0.0515  0.0255  0.0014  285 ALA B O   
4003 C CB  . ALA B 258 ? 0.3595 0.3314 0.2495 0.0315  0.0148  -0.0010 285 ALA B CB  
4004 N N   . THR B 259 ? 0.3669 0.3602 0.2773 0.0472  0.0210  -0.0012 286 THR B N   
4005 C CA  . THR B 259 ? 0.3977 0.4002 0.3171 0.0582  0.0224  0.0012  286 THR B CA  
4006 C C   . THR B 259 ? 0.4260 0.4161 0.3446 0.0627  0.0305  -0.0010 286 THR B C   
4007 O O   . THR B 259 ? 0.4377 0.4213 0.3576 0.0728  0.0333  0.0023  286 THR B O   
4008 C CB  . THR B 259 ? 0.3993 0.4272 0.3321 0.0576  0.0198  -0.0003 286 THR B CB  
4009 O OG1 . THR B 259 ? 0.3892 0.4262 0.3214 0.0519  0.0127  0.0000  286 THR B OG1 
4010 C CG2 . THR B 259 ? 0.4034 0.4454 0.3472 0.0698  0.0198  0.0027  286 THR B CG2 
4011 N N   . CYS B 260 ? 0.4316 0.4179 0.3475 0.0558  0.0349  -0.0065 287 CYS B N   
4012 C CA  . CYS B 260 ? 0.4494 0.4239 0.3627 0.0590  0.0427  -0.0103 287 CYS B CA  
4013 C C   . CYS B 260 ? 0.4461 0.3978 0.3501 0.0609  0.0447  -0.0098 287 CYS B C   
4014 O O   . CYS B 260 ? 0.4426 0.3842 0.3479 0.0688  0.0503  -0.0101 287 CYS B O   
4015 C CB  . CYS B 260 ? 0.4693 0.4439 0.3781 0.0507  0.0462  -0.0161 287 CYS B CB  
4016 S SG  . CYS B 260 ? 0.5158 0.5144 0.4362 0.0481  0.0473  -0.0170 287 CYS B SG  
4017 N N   . VAL B 261 ? 0.4224 0.3656 0.3178 0.0534  0.0409  -0.0095 288 VAL B N   
4018 C CA  . VAL B 261 ? 0.4398 0.3627 0.3276 0.0534  0.0429  -0.0091 288 VAL B CA  
4019 C C   . VAL B 261 ? 0.4700 0.3885 0.3608 0.0636  0.0430  -0.0019 288 VAL B C   
4020 O O   . VAL B 261 ? 0.4564 0.3583 0.3458 0.0690  0.0491  -0.0017 288 VAL B O   
4021 C CB  . VAL B 261 ? 0.4325 0.3517 0.3127 0.0438  0.0382  -0.0093 288 VAL B CB  
4022 C CG1 . VAL B 261 ? 0.4343 0.3346 0.3085 0.0433  0.0402  -0.0082 288 VAL B CG1 
4023 C CG2 . VAL B 261 ? 0.4305 0.3523 0.3064 0.0352  0.0384  -0.0154 288 VAL B CG2 
4024 N N   . ALA B 262 ? 0.4639 0.3965 0.3581 0.0665  0.0366  0.0043  289 ALA B N   
4025 C CA  . ALA B 262 ? 0.4650 0.3960 0.3606 0.0773  0.0359  0.0124  289 ALA B CA  
4026 C C   . ALA B 262 ? 0.4835 0.4123 0.3862 0.0891  0.0420  0.0137  289 ALA B C   
4027 O O   . ALA B 262 ? 0.4994 0.4140 0.4003 0.0979  0.0460  0.0192  289 ALA B O   
4028 C CB  . ALA B 262 ? 0.4587 0.4110 0.3577 0.0786  0.0274  0.0169  289 ALA B CB  
4029 N N   . GLY B 263 ? 0.4811 0.4244 0.3925 0.0900  0.0434  0.0091  290 GLY B N   
4030 C CA  . GLY B 263 ? 0.5068 0.4498 0.4261 0.1012  0.0499  0.0091  290 GLY B CA  
4031 C C   . GLY B 263 ? 0.5337 0.4493 0.4470 0.1025  0.0592  0.0057  290 GLY B C   
4032 O O   . GLY B 263 ? 0.5498 0.4560 0.4667 0.1140  0.0650  0.0090  290 GLY B O   
4033 N N   . VAL B 264 ? 0.5495 0.4531 0.4542 0.0906  0.0608  -0.0015 291 VAL B N   
4034 C CA  . VAL B 264 ? 0.5979 0.4772 0.4969 0.0889  0.0690  -0.0074 291 VAL B CA  
4035 C C   . VAL B 264 ? 0.6150 0.4737 0.5084 0.0904  0.0705  -0.0018 291 VAL B C   
4036 O O   . VAL B 264 ? 0.6284 0.4664 0.5213 0.0953  0.0788  -0.0027 291 VAL B O   
4037 C CB  . VAL B 264 ? 0.6353 0.5145 0.5273 0.0755  0.0686  -0.0172 291 VAL B CB  
4038 C CG1 . VAL B 264 ? 0.6748 0.5305 0.5593 0.0699  0.0746  -0.0244 291 VAL B CG1 
4039 C CG2 . VAL B 264 ? 0.6623 0.5570 0.5586 0.0755  0.0705  -0.0227 291 VAL B CG2 
4040 N N   . LEU B 265 ? 0.5985 0.4620 0.4877 0.0859  0.0633  0.0038  292 LEU B N   
4041 C CA  . LEU B 265 ? 0.6188 0.4637 0.5021 0.0863  0.0652  0.0097  292 LEU B CA  
4042 C C   . LEU B 265 ? 0.6159 0.4595 0.5022 0.1011  0.0662  0.0215  292 LEU B C   
4043 O O   . LEU B 265 ? 0.6222 0.4463 0.5038 0.1043  0.0708  0.0274  292 LEU B O   
4044 C CB  . LEU B 265 ? 0.6077 0.4588 0.4849 0.0761  0.0579  0.0107  292 LEU B CB  
4045 C CG  . LEU B 265 ? 0.5887 0.4406 0.4621 0.0623  0.0564  0.0007  292 LEU B CG  
4046 C CD1 . LEU B 265 ? 0.5798 0.4368 0.4484 0.0550  0.0499  0.0037  292 LEU B CD1 
4047 C CD2 . LEU B 265 ? 0.6010 0.4325 0.4716 0.0570  0.0642  -0.0075 292 LEU B CD2 
4048 N N   . ALA B 266 ? 0.6253 0.4906 0.5193 0.1101  0.0619  0.0252  293 ALA B N   
4049 C CA  . ALA B 266 ? 0.6634 0.5309 0.5612 0.1261  0.0625  0.0363  293 ALA B CA  
4050 C C   . ALA B 266 ? 0.6836 0.5287 0.5842 0.1354  0.0740  0.0362  293 ALA B C   
4051 O O   . ALA B 266 ? 0.7127 0.5437 0.6105 0.1454  0.0775  0.0465  293 ALA B O   
4052 C CB  . ALA B 266 ? 0.6550 0.5539 0.5625 0.1323  0.0550  0.0382  293 ALA B CB  
# 
