data_9O57
# 
_entry.id   9O57 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9O57         pdb_00009o57 10.2210/pdb9o57/pdb 
WWPDB D_1000294900 ?            ?                   
# 
_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       2025-04-16 
_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                        9O57 
_pdbx_database_status.recvd_initial_deposition_date   2025-04-09 
_pdbx_database_status.SG_entry                        Y 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_pdbx_contact_author.id 
_pdbx_contact_author.email 
_pdbx_contact_author.name_first 
_pdbx_contact_author.name_last 
_pdbx_contact_author.name_mi 
_pdbx_contact_author.role 
_pdbx_contact_author.identifier_ORCID 
2 swlovell@ku.edu                    Scott    Lovell ? 'principal investigator/group leader' 0000-0002-3215-4472 
3 isabelle.phan@seattlechildrens.org Isabelle Phan   ? 'principal investigator/group leader' 0000-0001-6873-3401 
4 julie.early@seattlechildrens.org   Julie    Early  ? 'principal investigator/group leader' 0000-0003-1224-2747 
5 peter.myler@seattlechildrens.org   Peter    Myler  ? 'principal investigator/group leader' 0000-0002-0056-0513 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Seattle Structural Genomics Center for Infectious Disease'          1 ? 
'Seattle Structural Genomics Center for Infectious Disease (SSGCID)' 2 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To be published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Crystal structure of Thymidylate kinase (Tmk) from Klebsiella aerogenes.' 
_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 'Liu, L.'        1 0000-0003-0514-281X 
primary 'Lovell, S.'     2 0000-0002-3215-4472 
primary 'Seibold, S.'    3 0000-0001-8297-229X 
primary 'Battaile, K.P.' 4 0000-0003-0833-3259 
# 
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 'Thymidylate kinase' 24838.262 2 2.7.4.9 ? ? ? 
2 non-polymer syn 'CHLORIDE ION'       35.453    2 ?       ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'dTMP kinase' 
# 
_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       
;MAHHHHHHMRSNYIVIEGLEGAGKTTARECVVETLKQLGVSDMVFTREPGGTILAEKLRSLVLDIQSTGDEVINDKAEVL
MFYAARVQLVETVIKPALARGQWVIGDRHDLSTQAYQGGGRGIDQTMLATLRDAVLGDFRPHLTLYLDVTPEVGLKRARA
RGELDRIEQESLDFFNRTRARYLELAAQDPTIRTVDATQPLEAVERDIRAVVNRWVAEQLP
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MAHHHHHHMRSNYIVIEGLEGAGKTTARECVVETLKQLGVSDMVFTREPGGTILAEKLRSLVLDIQSTGDEVINDKAEVL
MFYAARVQLVETVIKPALARGQWVIGDRHDLSTQAYQGGGRGIDQTMLATLRDAVLGDFRPHLTLYLDVTPEVGLKRARA
RGELDRIEQESLDFFNRTRARYLELAAQDPTIRTVDATQPLEAVERDIRAVVNRWVAEQLP
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
_pdbx_entity_nonpoly.entity_id   2 
_pdbx_entity_nonpoly.name        'CHLORIDE ION' 
_pdbx_entity_nonpoly.comp_id     CL 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   ALA n 
1 3   HIS n 
1 4   HIS n 
1 5   HIS n 
1 6   HIS n 
1 7   HIS n 
1 8   HIS n 
1 9   MET n 
1 10  ARG n 
1 11  SER n 
1 12  ASN n 
1 13  TYR n 
1 14  ILE n 
1 15  VAL n 
1 16  ILE n 
1 17  GLU n 
1 18  GLY n 
1 19  LEU n 
1 20  GLU n 
1 21  GLY n 
1 22  ALA n 
1 23  GLY n 
1 24  LYS n 
1 25  THR n 
1 26  THR n 
1 27  ALA n 
1 28  ARG n 
1 29  GLU n 
1 30  CYS n 
1 31  VAL n 
1 32  VAL n 
1 33  GLU n 
1 34  THR n 
1 35  LEU n 
1 36  LYS n 
1 37  GLN n 
1 38  LEU n 
1 39  GLY n 
1 40  VAL n 
1 41  SER n 
1 42  ASP n 
1 43  MET n 
1 44  VAL n 
1 45  PHE n 
1 46  THR n 
1 47  ARG n 
1 48  GLU n 
1 49  PRO n 
1 50  GLY n 
1 51  GLY n 
1 52  THR n 
1 53  ILE n 
1 54  LEU n 
1 55  ALA n 
1 56  GLU n 
1 57  LYS n 
1 58  LEU n 
1 59  ARG n 
1 60  SER n 
1 61  LEU n 
1 62  VAL n 
1 63  LEU n 
1 64  ASP n 
1 65  ILE n 
1 66  GLN n 
1 67  SER n 
1 68  THR n 
1 69  GLY n 
1 70  ASP n 
1 71  GLU n 
1 72  VAL n 
1 73  ILE n 
1 74  ASN n 
1 75  ASP n 
1 76  LYS n 
1 77  ALA n 
1 78  GLU n 
1 79  VAL n 
1 80  LEU n 
1 81  MET n 
1 82  PHE n 
1 83  TYR n 
1 84  ALA n 
1 85  ALA n 
1 86  ARG n 
1 87  VAL n 
1 88  GLN n 
1 89  LEU n 
1 90  VAL n 
1 91  GLU n 
1 92  THR n 
1 93  VAL n 
1 94  ILE n 
1 95  LYS n 
1 96  PRO n 
1 97  ALA n 
1 98  LEU n 
1 99  ALA n 
1 100 ARG n 
1 101 GLY n 
1 102 GLN n 
1 103 TRP n 
1 104 VAL n 
1 105 ILE n 
1 106 GLY n 
1 107 ASP n 
1 108 ARG n 
1 109 HIS n 
1 110 ASP n 
1 111 LEU n 
1 112 SER n 
1 113 THR n 
1 114 GLN n 
1 115 ALA n 
1 116 TYR n 
1 117 GLN n 
1 118 GLY n 
1 119 GLY n 
1 120 GLY n 
1 121 ARG n 
1 122 GLY n 
1 123 ILE n 
1 124 ASP n 
1 125 GLN n 
1 126 THR n 
1 127 MET n 
1 128 LEU n 
1 129 ALA n 
1 130 THR n 
1 131 LEU n 
1 132 ARG n 
1 133 ASP n 
1 134 ALA n 
1 135 VAL n 
1 136 LEU n 
1 137 GLY n 
1 138 ASP n 
1 139 PHE n 
1 140 ARG n 
1 141 PRO n 
1 142 HIS n 
1 143 LEU n 
1 144 THR n 
1 145 LEU n 
1 146 TYR n 
1 147 LEU n 
1 148 ASP n 
1 149 VAL n 
1 150 THR n 
1 151 PRO n 
1 152 GLU n 
1 153 VAL n 
1 154 GLY n 
1 155 LEU n 
1 156 LYS n 
1 157 ARG n 
1 158 ALA n 
1 159 ARG n 
1 160 ALA n 
1 161 ARG n 
1 162 GLY n 
1 163 GLU n 
1 164 LEU n 
1 165 ASP n 
1 166 ARG n 
1 167 ILE n 
1 168 GLU n 
1 169 GLN n 
1 170 GLU n 
1 171 SER n 
1 172 LEU n 
1 173 ASP n 
1 174 PHE n 
1 175 PHE n 
1 176 ASN n 
1 177 ARG n 
1 178 THR n 
1 179 ARG n 
1 180 ALA n 
1 181 ARG n 
1 182 TYR n 
1 183 LEU n 
1 184 GLU n 
1 185 LEU n 
1 186 ALA n 
1 187 ALA n 
1 188 GLN n 
1 189 ASP n 
1 190 PRO n 
1 191 THR n 
1 192 ILE n 
1 193 ARG n 
1 194 THR n 
1 195 VAL n 
1 196 ASP n 
1 197 ALA n 
1 198 THR n 
1 199 GLN n 
1 200 PRO n 
1 201 LEU n 
1 202 GLU n 
1 203 ALA n 
1 204 VAL n 
1 205 GLU n 
1 206 ARG n 
1 207 ASP n 
1 208 ILE n 
1 209 ARG n 
1 210 ALA n 
1 211 VAL n 
1 212 VAL n 
1 213 ASN n 
1 214 ARG n 
1 215 TRP n 
1 216 VAL n 
1 217 ALA n 
1 218 GLU n 
1 219 GLN n 
1 220 LEU n 
1 221 PRO 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                   221 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'tmk, CWM85_24435, N5C89_07930, NP224_17505' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Klebsiella aerogenes KCTC 2190' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     1028307 
_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          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       KlaeA.01628.a.B1 
_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 
CL  non-polymer         . 'CHLORIDE ION'  ? 'Cl -1'          35.453  
CYS 'L-peptide linking' y CYSTEINE        ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE       ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE       ? 'C6 H10 N3 O2 1' 156.162 
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 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   -7  ?   ?   ?   A . n 
A 1 2   ALA 2   -6  ?   ?   ?   A . n 
A 1 3   HIS 3   -5  ?   ?   ?   A . n 
A 1 4   HIS 4   -4  ?   ?   ?   A . n 
A 1 5   HIS 5   -3  ?   ?   ?   A . n 
A 1 6   HIS 6   -2  ?   ?   ?   A . n 
A 1 7   HIS 7   -1  -1  HIS HIS A . n 
A 1 8   HIS 8   0   0   HIS HIS A . n 
A 1 9   MET 9   1   1   MET MET A . n 
A 1 10  ARG 10  2   2   ARG ARG A . n 
A 1 11  SER 11  3   3   SER SER A . n 
A 1 12  ASN 12  4   4   ASN ASN A . n 
A 1 13  TYR 13  5   5   TYR TYR A . n 
A 1 14  ILE 14  6   6   ILE ILE A . n 
A 1 15  VAL 15  7   7   VAL VAL A . n 
A 1 16  ILE 16  8   8   ILE ILE A . n 
A 1 17  GLU 17  9   9   GLU GLU A . n 
A 1 18  GLY 18  10  10  GLY GLY A . n 
A 1 19  LEU 19  11  11  LEU LEU A . n 
A 1 20  GLU 20  12  12  GLU GLU A . n 
A 1 21  GLY 21  13  13  GLY GLY A . n 
A 1 22  ALA 22  14  14  ALA ALA A . n 
A 1 23  GLY 23  15  15  GLY GLY A . n 
A 1 24  LYS 24  16  16  LYS LYS A . n 
A 1 25  THR 25  17  17  THR THR A . n 
A 1 26  THR 26  18  18  THR THR A . n 
A 1 27  ALA 27  19  19  ALA ALA A . n 
A 1 28  ARG 28  20  20  ARG ARG A . n 
A 1 29  GLU 29  21  21  GLU GLU A . n 
A 1 30  CYS 30  22  22  CYS CYS A . n 
A 1 31  VAL 31  23  23  VAL VAL A . n 
A 1 32  VAL 32  24  24  VAL VAL A . n 
A 1 33  GLU 33  25  25  GLU GLU A . n 
A 1 34  THR 34  26  26  THR THR A . n 
A 1 35  LEU 35  27  27  LEU LEU A . n 
A 1 36  LYS 36  28  28  LYS LYS A . n 
A 1 37  GLN 37  29  29  GLN GLN A . n 
A 1 38  LEU 38  30  30  LEU LEU A . n 
A 1 39  GLY 39  31  31  GLY GLY A . n 
A 1 40  VAL 40  32  32  VAL VAL A . n 
A 1 41  SER 41  33  33  SER SER A . n 
A 1 42  ASP 42  34  34  ASP ASP A . n 
A 1 43  MET 43  35  35  MET MET A . n 
A 1 44  VAL 44  36  36  VAL VAL A . n 
A 1 45  PHE 45  37  37  PHE PHE A . n 
A 1 46  THR 46  38  38  THR THR A . n 
A 1 47  ARG 47  39  39  ARG ARG A . n 
A 1 48  GLU 48  40  40  GLU GLU A . n 
A 1 49  PRO 49  41  41  PRO PRO A . n 
A 1 50  GLY 50  42  42  GLY GLY A . n 
A 1 51  GLY 51  43  43  GLY GLY A . n 
A 1 52  THR 52  44  44  THR THR A . n 
A 1 53  ILE 53  45  45  ILE ILE A . n 
A 1 54  LEU 54  46  46  LEU LEU A . n 
A 1 55  ALA 55  47  47  ALA ALA A . n 
A 1 56  GLU 56  48  48  GLU GLU A . n 
A 1 57  LYS 57  49  49  LYS LYS A . n 
A 1 58  LEU 58  50  50  LEU LEU A . n 
A 1 59  ARG 59  51  51  ARG ARG A . n 
A 1 60  SER 60  52  52  SER SER A . n 
A 1 61  LEU 61  53  53  LEU LEU A . n 
A 1 62  VAL 62  54  54  VAL VAL A . n 
A 1 63  LEU 63  55  55  LEU LEU A . n 
A 1 64  ASP 64  56  56  ASP ASP A . n 
A 1 65  ILE 65  57  57  ILE ILE A . n 
A 1 66  GLN 66  58  58  GLN GLN A . n 
A 1 67  SER 67  59  59  SER SER A . n 
A 1 68  THR 68  60  60  THR THR A . n 
A 1 69  GLY 69  61  61  GLY GLY A . n 
A 1 70  ASP 70  62  62  ASP ASP A . n 
A 1 71  GLU 71  63  63  GLU GLU A . n 
A 1 72  VAL 72  64  64  VAL VAL A . n 
A 1 73  ILE 73  65  65  ILE ILE A . n 
A 1 74  ASN 74  66  66  ASN ASN A . n 
A 1 75  ASP 75  67  67  ASP ASP A . n 
A 1 76  LYS 76  68  68  LYS LYS A . n 
A 1 77  ALA 77  69  69  ALA ALA A . n 
A 1 78  GLU 78  70  70  GLU GLU A . n 
A 1 79  VAL 79  71  71  VAL VAL A . n 
A 1 80  LEU 80  72  72  LEU LEU A . n 
A 1 81  MET 81  73  73  MET MET A . n 
A 1 82  PHE 82  74  74  PHE PHE A . n 
A 1 83  TYR 83  75  75  TYR TYR A . n 
A 1 84  ALA 84  76  76  ALA ALA A . n 
A 1 85  ALA 85  77  77  ALA ALA A . n 
A 1 86  ARG 86  78  78  ARG ARG A . n 
A 1 87  VAL 87  79  79  VAL VAL A . n 
A 1 88  GLN 88  80  80  GLN GLN A . n 
A 1 89  LEU 89  81  81  LEU LEU A . n 
A 1 90  VAL 90  82  82  VAL VAL A . n 
A 1 91  GLU 91  83  83  GLU GLU A . n 
A 1 92  THR 92  84  84  THR THR A . n 
A 1 93  VAL 93  85  85  VAL VAL A . n 
A 1 94  ILE 94  86  86  ILE ILE A . n 
A 1 95  LYS 95  87  87  LYS LYS A . n 
A 1 96  PRO 96  88  88  PRO PRO A . n 
A 1 97  ALA 97  89  89  ALA ALA A . n 
A 1 98  LEU 98  90  90  LEU LEU A . n 
A 1 99  ALA 99  91  91  ALA ALA A . n 
A 1 100 ARG 100 92  92  ARG ARG A . n 
A 1 101 GLY 101 93  93  GLY GLY A . n 
A 1 102 GLN 102 94  94  GLN GLN A . n 
A 1 103 TRP 103 95  95  TRP TRP A . n 
A 1 104 VAL 104 96  96  VAL VAL A . n 
A 1 105 ILE 105 97  97  ILE ILE A . n 
A 1 106 GLY 106 98  98  GLY GLY A . n 
A 1 107 ASP 107 99  99  ASP ASP A . n 
A 1 108 ARG 108 100 100 ARG ARG A . n 
A 1 109 HIS 109 101 101 HIS HIS A . n 
A 1 110 ASP 110 102 ?   ?   ?   A . n 
A 1 111 LEU 111 103 ?   ?   ?   A . n 
A 1 112 SER 112 104 ?   ?   ?   A . n 
A 1 113 THR 113 105 ?   ?   ?   A . n 
A 1 114 GLN 114 106 ?   ?   ?   A . n 
A 1 115 ALA 115 107 ?   ?   ?   A . n 
A 1 116 TYR 116 108 ?   ?   ?   A . n 
A 1 117 GLN 117 109 ?   ?   ?   A . n 
A 1 118 GLY 118 110 ?   ?   ?   A . n 
A 1 119 GLY 119 111 ?   ?   ?   A . n 
A 1 120 GLY 120 112 ?   ?   ?   A . n 
A 1 121 ARG 121 113 ?   ?   ?   A . n 
A 1 122 GLY 122 114 ?   ?   ?   A . n 
A 1 123 ILE 123 115 ?   ?   ?   A . n 
A 1 124 ASP 124 116 ?   ?   ?   A . n 
A 1 125 GLN 125 117 ?   ?   ?   A . n 
A 1 126 THR 126 118 118 THR THR A . n 
A 1 127 MET 127 119 119 MET MET A . n 
A 1 128 LEU 128 120 120 LEU LEU A . n 
A 1 129 ALA 129 121 121 ALA ALA A . n 
A 1 130 THR 130 122 122 THR THR A . n 
A 1 131 LEU 131 123 123 LEU LEU A . n 
A 1 132 ARG 132 124 124 ARG ARG A . n 
A 1 133 ASP 133 125 125 ASP ASP A . n 
A 1 134 ALA 134 126 126 ALA ALA A . n 
A 1 135 VAL 135 127 127 VAL VAL A . n 
A 1 136 LEU 136 128 128 LEU LEU A . n 
A 1 137 GLY 137 129 129 GLY GLY A . n 
A 1 138 ASP 138 130 130 ASP ASP A . n 
A 1 139 PHE 139 131 131 PHE PHE A . n 
A 1 140 ARG 140 132 132 ARG ARG A . n 
A 1 141 PRO 141 133 133 PRO PRO A . n 
A 1 142 HIS 142 134 134 HIS HIS A . n 
A 1 143 LEU 143 135 135 LEU LEU A . n 
A 1 144 THR 144 136 136 THR THR A . n 
A 1 145 LEU 145 137 137 LEU LEU A . n 
A 1 146 TYR 146 138 138 TYR TYR A . n 
A 1 147 LEU 147 139 139 LEU LEU A . n 
A 1 148 ASP 148 140 140 ASP ASP A . n 
A 1 149 VAL 149 141 141 VAL VAL A . n 
A 1 150 THR 150 142 142 THR THR A . n 
A 1 151 PRO 151 143 143 PRO PRO A . n 
A 1 152 GLU 152 144 144 GLU GLU A . n 
A 1 153 VAL 153 145 145 VAL VAL A . n 
A 1 154 GLY 154 146 146 GLY GLY A . n 
A 1 155 LEU 155 147 147 LEU LEU A . n 
A 1 156 LYS 156 148 148 LYS LYS A . n 
A 1 157 ARG 157 149 149 ARG ARG A . n 
A 1 158 ALA 158 150 150 ALA ALA A . n 
A 1 159 ARG 159 151 151 ARG ARG A . n 
A 1 160 ALA 160 152 152 ALA ALA A . n 
A 1 161 ARG 161 153 ?   ?   ?   A . n 
A 1 162 GLY 162 154 ?   ?   ?   A . n 
A 1 163 GLU 163 155 ?   ?   ?   A . n 
A 1 164 LEU 164 156 ?   ?   ?   A . n 
A 1 165 ASP 165 157 ?   ?   ?   A . n 
A 1 166 ARG 166 158 ?   ?   ?   A . n 
A 1 167 ILE 167 159 ?   ?   ?   A . n 
A 1 168 GLU 168 160 ?   ?   ?   A . n 
A 1 169 GLN 169 161 ?   ?   ?   A . n 
A 1 170 GLU 170 162 ?   ?   ?   A . n 
A 1 171 SER 171 163 ?   ?   ?   A . n 
A 1 172 LEU 172 164 ?   ?   ?   A . n 
A 1 173 ASP 173 165 165 ASP ASP A . n 
A 1 174 PHE 174 166 166 PHE PHE A . n 
A 1 175 PHE 175 167 167 PHE PHE A . n 
A 1 176 ASN 176 168 168 ASN ASN A . n 
A 1 177 ARG 177 169 169 ARG ARG A . n 
A 1 178 THR 178 170 170 THR THR A . n 
A 1 179 ARG 179 171 171 ARG ARG A . n 
A 1 180 ALA 180 172 172 ALA ALA A . n 
A 1 181 ARG 181 173 173 ARG ARG A . n 
A 1 182 TYR 182 174 174 TYR TYR A . n 
A 1 183 LEU 183 175 175 LEU LEU A . n 
A 1 184 GLU 184 176 176 GLU GLU A . n 
A 1 185 LEU 185 177 177 LEU LEU A . n 
A 1 186 ALA 186 178 178 ALA ALA A . n 
A 1 187 ALA 187 179 179 ALA ALA A . n 
A 1 188 GLN 188 180 180 GLN GLN A . n 
A 1 189 ASP 189 181 181 ASP ASP A . n 
A 1 190 PRO 190 182 182 PRO PRO A . n 
A 1 191 THR 191 183 183 THR THR A . n 
A 1 192 ILE 192 184 184 ILE ILE A . n 
A 1 193 ARG 193 185 185 ARG ARG A . n 
A 1 194 THR 194 186 186 THR THR A . n 
A 1 195 VAL 195 187 187 VAL VAL A . n 
A 1 196 ASP 196 188 188 ASP ASP A . n 
A 1 197 ALA 197 189 189 ALA ALA A . n 
A 1 198 THR 198 190 190 THR THR A . n 
A 1 199 GLN 199 191 191 GLN GLN A . n 
A 1 200 PRO 200 192 192 PRO PRO A . n 
A 1 201 LEU 201 193 193 LEU LEU A . n 
A 1 202 GLU 202 194 194 GLU GLU A . n 
A 1 203 ALA 203 195 195 ALA ALA A . n 
A 1 204 VAL 204 196 196 VAL VAL A . n 
A 1 205 GLU 205 197 197 GLU GLU A . n 
A 1 206 ARG 206 198 198 ARG ARG A . n 
A 1 207 ASP 207 199 199 ASP ASP A . n 
A 1 208 ILE 208 200 200 ILE ILE A . n 
A 1 209 ARG 209 201 201 ARG ARG A . n 
A 1 210 ALA 210 202 202 ALA ALA A . n 
A 1 211 VAL 211 203 203 VAL VAL A . n 
A 1 212 VAL 212 204 204 VAL VAL A . n 
A 1 213 ASN 213 205 205 ASN ASN A . n 
A 1 214 ARG 214 206 206 ARG ARG A . n 
A 1 215 TRP 215 207 207 TRP TRP A . n 
A 1 216 VAL 216 208 208 VAL VAL A . n 
A 1 217 ALA 217 209 209 ALA ALA A . n 
A 1 218 GLU 218 210 210 GLU GLU A . n 
A 1 219 GLN 219 211 211 GLN GLN A . n 
A 1 220 LEU 220 212 ?   ?   ?   A . n 
A 1 221 PRO 221 213 ?   ?   ?   A . n 
B 1 1   MET 1   -7  ?   ?   ?   B . n 
B 1 2   ALA 2   -6  ?   ?   ?   B . n 
B 1 3   HIS 3   -5  ?   ?   ?   B . n 
B 1 4   HIS 4   -4  ?   ?   ?   B . n 
B 1 5   HIS 5   -3  ?   ?   ?   B . n 
B 1 6   HIS 6   -2  ?   ?   ?   B . n 
B 1 7   HIS 7   -1  ?   ?   ?   B . n 
B 1 8   HIS 8   0   ?   ?   ?   B . n 
B 1 9   MET 9   1   1   MET MET B . n 
B 1 10  ARG 10  2   2   ARG ARG B . n 
B 1 11  SER 11  3   3   SER SER B . n 
B 1 12  ASN 12  4   4   ASN ASN B . n 
B 1 13  TYR 13  5   5   TYR TYR B . n 
B 1 14  ILE 14  6   6   ILE ILE B . n 
B 1 15  VAL 15  7   7   VAL VAL B . n 
B 1 16  ILE 16  8   8   ILE ILE B . n 
B 1 17  GLU 17  9   9   GLU GLU B . n 
B 1 18  GLY 18  10  10  GLY GLY B . n 
B 1 19  LEU 19  11  11  LEU LEU B . n 
B 1 20  GLU 20  12  12  GLU GLU B . n 
B 1 21  GLY 21  13  13  GLY GLY B . n 
B 1 22  ALA 22  14  14  ALA ALA B . n 
B 1 23  GLY 23  15  15  GLY GLY B . n 
B 1 24  LYS 24  16  16  LYS LYS B . n 
B 1 25  THR 25  17  17  THR THR B . n 
B 1 26  THR 26  18  18  THR THR B . n 
B 1 27  ALA 27  19  19  ALA ALA B . n 
B 1 28  ARG 28  20  20  ARG ARG B . n 
B 1 29  GLU 29  21  21  GLU GLU B . n 
B 1 30  CYS 30  22  22  CYS CYS B . n 
B 1 31  VAL 31  23  23  VAL VAL B . n 
B 1 32  VAL 32  24  24  VAL VAL B . n 
B 1 33  GLU 33  25  25  GLU GLU B . n 
B 1 34  THR 34  26  26  THR THR B . n 
B 1 35  LEU 35  27  27  LEU LEU B . n 
B 1 36  LYS 36  28  28  LYS LYS B . n 
B 1 37  GLN 37  29  29  GLN GLN B . n 
B 1 38  LEU 38  30  30  LEU LEU B . n 
B 1 39  GLY 39  31  31  GLY GLY B . n 
B 1 40  VAL 40  32  32  VAL VAL B . n 
B 1 41  SER 41  33  33  SER SER B . n 
B 1 42  ASP 42  34  34  ASP ASP B . n 
B 1 43  MET 43  35  35  MET MET B . n 
B 1 44  VAL 44  36  36  VAL VAL B . n 
B 1 45  PHE 45  37  37  PHE PHE B . n 
B 1 46  THR 46  38  38  THR THR B . n 
B 1 47  ARG 47  39  39  ARG ARG B . n 
B 1 48  GLU 48  40  40  GLU GLU B . n 
B 1 49  PRO 49  41  41  PRO PRO B . n 
B 1 50  GLY 50  42  42  GLY GLY B . n 
B 1 51  GLY 51  43  43  GLY GLY B . n 
B 1 52  THR 52  44  44  THR THR B . n 
B 1 53  ILE 53  45  45  ILE ILE B . n 
B 1 54  LEU 54  46  46  LEU LEU B . n 
B 1 55  ALA 55  47  47  ALA ALA B . n 
B 1 56  GLU 56  48  48  GLU GLU B . n 
B 1 57  LYS 57  49  49  LYS LYS B . n 
B 1 58  LEU 58  50  50  LEU LEU B . n 
B 1 59  ARG 59  51  51  ARG ARG B . n 
B 1 60  SER 60  52  52  SER SER B . n 
B 1 61  LEU 61  53  53  LEU LEU B . n 
B 1 62  VAL 62  54  54  VAL VAL B . n 
B 1 63  LEU 63  55  55  LEU LEU B . n 
B 1 64  ASP 64  56  56  ASP ASP B . n 
B 1 65  ILE 65  57  57  ILE ILE B . n 
B 1 66  GLN 66  58  58  GLN GLN B . n 
B 1 67  SER 67  59  59  SER SER B . n 
B 1 68  THR 68  60  60  THR THR B . n 
B 1 69  GLY 69  61  61  GLY GLY B . n 
B 1 70  ASP 70  62  62  ASP ASP B . n 
B 1 71  GLU 71  63  63  GLU GLU B . n 
B 1 72  VAL 72  64  64  VAL VAL B . n 
B 1 73  ILE 73  65  65  ILE ILE B . n 
B 1 74  ASN 74  66  66  ASN ASN B . n 
B 1 75  ASP 75  67  67  ASP ASP B . n 
B 1 76  LYS 76  68  68  LYS LYS B . n 
B 1 77  ALA 77  69  69  ALA ALA B . n 
B 1 78  GLU 78  70  70  GLU GLU B . n 
B 1 79  VAL 79  71  71  VAL VAL B . n 
B 1 80  LEU 80  72  72  LEU LEU B . n 
B 1 81  MET 81  73  73  MET MET B . n 
B 1 82  PHE 82  74  74  PHE PHE B . n 
B 1 83  TYR 83  75  75  TYR TYR B . n 
B 1 84  ALA 84  76  76  ALA ALA B . n 
B 1 85  ALA 85  77  77  ALA ALA B . n 
B 1 86  ARG 86  78  78  ARG ARG B . n 
B 1 87  VAL 87  79  79  VAL VAL B . n 
B 1 88  GLN 88  80  80  GLN GLN B . n 
B 1 89  LEU 89  81  81  LEU LEU B . n 
B 1 90  VAL 90  82  82  VAL VAL B . n 
B 1 91  GLU 91  83  83  GLU GLU B . n 
B 1 92  THR 92  84  84  THR THR B . n 
B 1 93  VAL 93  85  85  VAL VAL B . n 
B 1 94  ILE 94  86  86  ILE ILE B . n 
B 1 95  LYS 95  87  87  LYS LYS B . n 
B 1 96  PRO 96  88  88  PRO PRO B . n 
B 1 97  ALA 97  89  89  ALA ALA B . n 
B 1 98  LEU 98  90  90  LEU LEU B . n 
B 1 99  ALA 99  91  91  ALA ALA B . n 
B 1 100 ARG 100 92  92  ARG ARG B . n 
B 1 101 GLY 101 93  93  GLY GLY B . n 
B 1 102 GLN 102 94  94  GLN GLN B . n 
B 1 103 TRP 103 95  95  TRP TRP B . n 
B 1 104 VAL 104 96  96  VAL VAL B . n 
B 1 105 ILE 105 97  97  ILE ILE B . n 
B 1 106 GLY 106 98  98  GLY GLY B . n 
B 1 107 ASP 107 99  99  ASP ASP B . n 
B 1 108 ARG 108 100 100 ARG ARG B . n 
B 1 109 HIS 109 101 101 HIS HIS B . n 
B 1 110 ASP 110 102 ?   ?   ?   B . n 
B 1 111 LEU 111 103 ?   ?   ?   B . n 
B 1 112 SER 112 104 ?   ?   ?   B . n 
B 1 113 THR 113 105 ?   ?   ?   B . n 
B 1 114 GLN 114 106 ?   ?   ?   B . n 
B 1 115 ALA 115 107 ?   ?   ?   B . n 
B 1 116 TYR 116 108 ?   ?   ?   B . n 
B 1 117 GLN 117 109 ?   ?   ?   B . n 
B 1 118 GLY 118 110 ?   ?   ?   B . n 
B 1 119 GLY 119 111 ?   ?   ?   B . n 
B 1 120 GLY 120 112 ?   ?   ?   B . n 
B 1 121 ARG 121 113 ?   ?   ?   B . n 
B 1 122 GLY 122 114 ?   ?   ?   B . n 
B 1 123 ILE 123 115 ?   ?   ?   B . n 
B 1 124 ASP 124 116 ?   ?   ?   B . n 
B 1 125 GLN 125 117 117 GLN GLN B . n 
B 1 126 THR 126 118 118 THR THR B . n 
B 1 127 MET 127 119 119 MET MET B . n 
B 1 128 LEU 128 120 120 LEU LEU B . n 
B 1 129 ALA 129 121 121 ALA ALA B . n 
B 1 130 THR 130 122 122 THR THR B . n 
B 1 131 LEU 131 123 123 LEU LEU B . n 
B 1 132 ARG 132 124 124 ARG ARG B . n 
B 1 133 ASP 133 125 125 ASP ASP B . n 
B 1 134 ALA 134 126 126 ALA ALA B . n 
B 1 135 VAL 135 127 127 VAL VAL B . n 
B 1 136 LEU 136 128 128 LEU LEU B . n 
B 1 137 GLY 137 129 129 GLY GLY B . n 
B 1 138 ASP 138 130 130 ASP ASP B . n 
B 1 139 PHE 139 131 131 PHE PHE B . n 
B 1 140 ARG 140 132 132 ARG ARG B . n 
B 1 141 PRO 141 133 133 PRO PRO B . n 
B 1 142 HIS 142 134 134 HIS HIS B . n 
B 1 143 LEU 143 135 135 LEU LEU B . n 
B 1 144 THR 144 136 136 THR THR B . n 
B 1 145 LEU 145 137 137 LEU LEU B . n 
B 1 146 TYR 146 138 138 TYR TYR B . n 
B 1 147 LEU 147 139 139 LEU LEU B . n 
B 1 148 ASP 148 140 140 ASP ASP B . n 
B 1 149 VAL 149 141 141 VAL VAL B . n 
B 1 150 THR 150 142 142 THR THR B . n 
B 1 151 PRO 151 143 143 PRO PRO B . n 
B 1 152 GLU 152 144 144 GLU GLU B . n 
B 1 153 VAL 153 145 145 VAL VAL B . n 
B 1 154 GLY 154 146 146 GLY GLY B . n 
B 1 155 LEU 155 147 147 LEU LEU B . n 
B 1 156 LYS 156 148 148 LYS LYS B . n 
B 1 157 ARG 157 149 149 ARG ARG B . n 
B 1 158 ALA 158 150 150 ALA ALA B . n 
B 1 159 ARG 159 151 151 ARG ARG B . n 
B 1 160 ALA 160 152 152 ALA ALA B . n 
B 1 161 ARG 161 153 ?   ?   ?   B . n 
B 1 162 GLY 162 154 ?   ?   ?   B . n 
B 1 163 GLU 163 155 ?   ?   ?   B . n 
B 1 164 LEU 164 156 ?   ?   ?   B . n 
B 1 165 ASP 165 157 ?   ?   ?   B . n 
B 1 166 ARG 166 158 ?   ?   ?   B . n 
B 1 167 ILE 167 159 ?   ?   ?   B . n 
B 1 168 GLU 168 160 ?   ?   ?   B . n 
B 1 169 GLN 169 161 ?   ?   ?   B . n 
B 1 170 GLU 170 162 ?   ?   ?   B . n 
B 1 171 SER 171 163 ?   ?   ?   B . n 
B 1 172 LEU 172 164 164 LEU LEU B . n 
B 1 173 ASP 173 165 165 ASP ASP B . n 
B 1 174 PHE 174 166 166 PHE PHE B . n 
B 1 175 PHE 175 167 167 PHE PHE B . n 
B 1 176 ASN 176 168 168 ASN ASN B . n 
B 1 177 ARG 177 169 169 ARG ARG B . n 
B 1 178 THR 178 170 170 THR THR B . n 
B 1 179 ARG 179 171 171 ARG ARG B . n 
B 1 180 ALA 180 172 172 ALA ALA B . n 
B 1 181 ARG 181 173 173 ARG ARG B . n 
B 1 182 TYR 182 174 174 TYR TYR B . n 
B 1 183 LEU 183 175 175 LEU LEU B . n 
B 1 184 GLU 184 176 176 GLU GLU B . n 
B 1 185 LEU 185 177 177 LEU LEU B . n 
B 1 186 ALA 186 178 178 ALA ALA B . n 
B 1 187 ALA 187 179 179 ALA ALA B . n 
B 1 188 GLN 188 180 180 GLN GLN B . n 
B 1 189 ASP 189 181 181 ASP ASP B . n 
B 1 190 PRO 190 182 182 PRO PRO B . n 
B 1 191 THR 191 183 183 THR THR B . n 
B 1 192 ILE 192 184 184 ILE ILE B . n 
B 1 193 ARG 193 185 185 ARG ARG B . n 
B 1 194 THR 194 186 186 THR THR B . n 
B 1 195 VAL 195 187 187 VAL VAL B . n 
B 1 196 ASP 196 188 188 ASP ASP B . n 
B 1 197 ALA 197 189 189 ALA ALA B . n 
B 1 198 THR 198 190 190 THR THR B . n 
B 1 199 GLN 199 191 191 GLN GLN B . n 
B 1 200 PRO 200 192 192 PRO PRO B . n 
B 1 201 LEU 201 193 193 LEU LEU B . n 
B 1 202 GLU 202 194 194 GLU GLU B . n 
B 1 203 ALA 203 195 195 ALA ALA B . n 
B 1 204 VAL 204 196 196 VAL VAL B . n 
B 1 205 GLU 205 197 197 GLU GLU B . n 
B 1 206 ARG 206 198 198 ARG ARG B . n 
B 1 207 ASP 207 199 199 ASP ASP B . n 
B 1 208 ILE 208 200 200 ILE ILE B . n 
B 1 209 ARG 209 201 201 ARG ARG B . n 
B 1 210 ALA 210 202 202 ALA ALA B . n 
B 1 211 VAL 211 203 203 VAL VAL B . n 
B 1 212 VAL 212 204 204 VAL VAL B . n 
B 1 213 ASN 213 205 205 ASN ASN B . n 
B 1 214 ARG 214 206 206 ARG ARG B . n 
B 1 215 TRP 215 207 207 TRP TRP B . n 
B 1 216 VAL 216 208 208 VAL VAL B . n 
B 1 217 ALA 217 209 209 ALA ALA B . n 
B 1 218 GLU 218 210 210 GLU GLU B . n 
B 1 219 GLN 219 211 211 GLN GLN B . n 
B 1 220 LEU 220 212 ?   ?   ?   B . n 
B 1 221 PRO 221 213 ?   ?   ?   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 CL 1 301 1 CL CL A . 
D 2 CL 1 301 2 CL CL B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A GLU 12  ? CG  ? A GLU 20  CG  
2  1 Y 1 A GLU 12  ? CD  ? A GLU 20  CD  
3  1 Y 1 A GLU 12  ? OE1 ? A GLU 20  OE1 
4  1 Y 1 A GLU 12  ? OE2 ? A GLU 20  OE2 
5  1 Y 1 A ASP 62  ? CG  ? A ASP 70  CG  
6  1 Y 1 A ASP 62  ? OD1 ? A ASP 70  OD1 
7  1 Y 1 A ASP 62  ? OD2 ? A ASP 70  OD2 
8  1 Y 1 B MET 1   ? CG  ? B MET 9   CG  
9  1 Y 1 B MET 1   ? SD  ? B MET 9   SD  
10 1 Y 1 B MET 1   ? CE  ? B MET 9   CE  
11 1 Y 1 B GLN 117 ? CG  ? B GLN 125 CG  
12 1 Y 1 B GLN 117 ? CD  ? B GLN 125 CD  
13 1 Y 1 B GLN 117 ? OE1 ? B GLN 125 OE1 
14 1 Y 1 B GLN 117 ? NE2 ? B GLN 125 NE2 
15 1 Y 1 B PHE 167 ? CG  ? B PHE 175 CG  
16 1 Y 1 B PHE 167 ? CD1 ? B PHE 175 CD1 
17 1 Y 1 B PHE 167 ? CD2 ? B PHE 175 CD2 
18 1 Y 1 B PHE 167 ? CE1 ? B PHE 175 CE1 
19 1 Y 1 B PHE 167 ? CE2 ? B PHE 175 CE2 
20 1 Y 1 B PHE 167 ? CZ  ? B PHE 175 CZ  
21 1 Y 1 B ARG 169 ? CG  ? B ARG 177 CG  
22 1 Y 1 B ARG 169 ? CD  ? B ARG 177 CD  
23 1 Y 1 B ARG 169 ? NE  ? B ARG 177 NE  
24 1 Y 1 B ARG 169 ? CZ  ? B ARG 177 CZ  
25 1 Y 1 B ARG 169 ? NH1 ? B ARG 177 NH1 
26 1 Y 1 B ARG 169 ? NH2 ? B ARG 177 NH2 
# 
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_reference_DOI 
_software.pdbx_ordinal 
? refinement        ? ? ? ? ? ? ? ? ? ? ? PHENIX      ? ? ? dev_5660 ? 1 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? Aimless     ? ? ? .        ? 2 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? XDS         ? ? ? .        ? 3 
? phasing           ? ? ? ? ? ? ? ? ? ? ? PHASER      ? ? ? .        ? 4 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? .        ? 5 
# 
_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                     9O57 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     66.407 
_cell.length_a_esd                 ? 
_cell.length_b                     75.450 
_cell.length_b_esd                 ? 
_cell.length_c                     76.018 
_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                         9O57 
_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                   9O57 
_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             1.92 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          35.83 
_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              5.0 
_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    
;PACT B2: 0.10 M MIB buffer, pH 5.0, 25% PEG 1500. KlaeA.01628.a.B1.PW39187 at 19.7 mg/mL. plate 19509 well B2 drop 2, 2mM UMP added to the protein prior to crystallization but ligand is not bound. Puck: PSL-0313, Cryo: 0.10M MIB buffer, pH 5.0, 35% PEG 1500.
;
_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 XE 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         2025-02-15 
_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                    'Double Crystal Si 111' 
_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   0.9786 
_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                        'NSLS-II BEAMLINE 19-ID' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9786 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   19-ID 
_diffrn_source.pdbx_synchrotron_site       NSLS-II 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9O57 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.85 
_reflns.d_resolution_low                               19.46 
_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                                     9361 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.7 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                8.5 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          10.1 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.99 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.168 
_reflns.pdbx_Rpim_I_all                                0.056 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       79766 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.998 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.158 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.85 
_reflns_shell.d_res_low                                     3.00 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           11261 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1348 
_reflns_shell.percent_possible_obs                          100.0 
_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                               8.4 
_reflns_shell.pdbx_chi_squared                              0.99 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     1.6 
_reflns_shell.pdbx_Rrim_I_all                               1.364 
_reflns_shell.pdbx_Rpim_I_all                               0.460 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.699 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  1.281 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9O57 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.85 
_refine.ls_d_res_low                             19.46 
_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                     9327 
_refine.ls_number_reflns_R_free                  499 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.94 
_refine.ls_percent_reflns_R_free                 5.35 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2396 
_refine.ls_R_factor_R_free                       0.2679 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2378 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.correlation_coeff_I_to_Fcsqd_work        ? 
_refine.correlation_coeff_I_to_Fcsqd_free        ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 30.99 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.26 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.85 
_refine_hist.d_res_low                        19.46 
_refine_hist.number_atoms_solvent             0 
_refine_hist.number_atoms_total               2893 
_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        2891 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         2 
_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_Zscore 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.004  ? 2928 ? f_bond_d           ? ? ? 
'X-RAY DIFFRACTION' ? 0.664  ? 3968 ? f_angle_d          ? ? ? 
'X-RAY DIFFRACTION' ? 12.961 ? 1089 ? f_dihedral_angle_d ? ? ? 
'X-RAY DIFFRACTION' ? 0.041  ? 477  ? f_chiral_restr     ? ? ? 
'X-RAY DIFFRACTION' ? 0.007  ? 510  ? f_plane_restr      ? ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.correlation_coeff_Fo_to_Fc 
_refine_ls_shell.correlation_coeff_Fo_to_Fc_free 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_work 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_free 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.85 3.14  . . 115 2176 100.00 . . . . 0.3065 . . . . . . . . . . . . . . . 0.3336 
'X-RAY DIFFRACTION' 3.14 3.59  . . 116 2182 100.00 . . . . 0.2770 . . . . . . . . . . . . . . . 0.2899 
'X-RAY DIFFRACTION' 3.59 4.51  . . 117 2193 100.00 . . . . 0.2209 . . . . . . . . . . . . . . . 0.2655 
'X-RAY DIFFRACTION' 4.51 19.46 . . 151 2277 100.00 . . . . 0.2185 . . . . . . . . . . . . . . . 0.2509 
# 
_struct.entry_id                     9O57 
_struct.title                        'Crystal structure of Thymidylate kinase (Tmk) from Klebsiella aerogenes.' 
_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        9O57 
_struct_keywords.text            
'SSGCID, STRUCTURAL GENOMICS, SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE, TRANSFERASE, Klebsiella, Thymidylate kinase' 
_struct_keywords.pdbx_keywords   TRANSFERASE 
# 
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 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A0A0J2I384_9ENTR 
_struct_ref.pdbx_db_accession          A0A0J2I384 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MRSNYIVIEGLEGAGKTTARECVVETLKQLGVSDMVFTREPGGTILAEKLRSLVLDIQSTGDEVINDKAEVLMFYAARVQ
LVETVIKPALARGQWVIGDRHDLSTQAYQGGGRGIDQTMLATLRDAVLGDFRPHLTLYLDVTPEVGLKRARARGELDRIE
QESLDFFNRTRARYLELAAQDPTIRTVDATQPLEAVERDIRAVVNRWVAEQLP
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9O57 A 9 ? 221 ? A0A0J2I384 1 ? 213 ? 1 213 
2 1 9O57 B 9 ? 221 ? A0A0J2I384 1 ? 213 ? 1 213 
# 
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 9O57 MET A 1 ? UNP A0A0J2I384 ? ? 'initiating methionine' -7 1  
1 9O57 ALA A 2 ? UNP A0A0J2I384 ? ? 'expression tag'        -6 2  
1 9O57 HIS A 3 ? UNP A0A0J2I384 ? ? 'expression tag'        -5 3  
1 9O57 HIS A 4 ? UNP A0A0J2I384 ? ? 'expression tag'        -4 4  
1 9O57 HIS A 5 ? UNP A0A0J2I384 ? ? 'expression tag'        -3 5  
1 9O57 HIS A 6 ? UNP A0A0J2I384 ? ? 'expression tag'        -2 6  
1 9O57 HIS A 7 ? UNP A0A0J2I384 ? ? 'expression tag'        -1 7  
1 9O57 HIS A 8 ? UNP A0A0J2I384 ? ? 'expression tag'        0  8  
2 9O57 MET B 1 ? UNP A0A0J2I384 ? ? 'initiating methionine' -7 9  
2 9O57 ALA B 2 ? UNP A0A0J2I384 ? ? 'expression tag'        -6 10 
2 9O57 HIS B 3 ? UNP A0A0J2I384 ? ? 'expression tag'        -5 11 
2 9O57 HIS B 4 ? UNP A0A0J2I384 ? ? 'expression tag'        -4 12 
2 9O57 HIS B 5 ? UNP A0A0J2I384 ? ? 'expression tag'        -3 13 
2 9O57 HIS B 6 ? UNP A0A0J2I384 ? ? 'expression tag'        -2 14 
2 9O57 HIS B 7 ? UNP A0A0J2I384 ? ? 'expression tag'        -1 15 
2 9O57 HIS B 8 ? UNP A0A0J2I384 ? ? 'expression tag'        0  16 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 2620  ? 
1 MORE         -38   ? 
1 'SSA (A^2)'  19750 ? 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C 
1 2 B,D 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z           1.0000000000  0.0000000000 0.0000000000 0.0000000000  0.0000000000 
1.0000000000  0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000   
2 'crystal symmetry operation' 2_554 -x+1/2,-y,z-1/2 -1.0000000000 0.0000000000 0.0000000000 33.2035000000 0.0000000000 
-1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 -38.0090000000 
# 
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 23  ? LEU A 38  ? GLY A 15  LEU A 30  1 ? 16 
HELX_P HELX_P2  AA2 THR A 52  ? GLY A 69  ? THR A 44  GLY A 61  1 ? 18 
HELX_P HELX_P3  AA3 ASN A 74  ? VAL A 93  ? ASN A 66  VAL A 85  1 ? 20 
HELX_P HELX_P4  AA4 VAL A 93  ? ARG A 100 ? VAL A 85  ARG A 92  1 ? 8  
HELX_P HELX_P5  AA5 MET A 127 ? LEU A 136 ? MET A 119 LEU A 128 1 ? 10 
HELX_P HELX_P6  AA6 THR A 150 ? ALA A 160 ? THR A 142 ALA A 152 1 ? 11 
HELX_P HELX_P7  AA7 PHE A 174 ? ASP A 189 ? PHE A 166 ASP A 181 1 ? 16 
HELX_P HELX_P8  AA8 PRO A 200 ? GLN A 219 ? PRO A 192 GLN A 211 1 ? 20 
HELX_P HELX_P9  AA9 GLY B 23  ? LEU B 38  ? GLY B 15  LEU B 30  1 ? 16 
HELX_P HELX_P10 AB1 THR B 52  ? GLY B 69  ? THR B 44  GLY B 61  1 ? 18 
HELX_P HELX_P11 AB2 ASN B 74  ? VAL B 93  ? ASN B 66  VAL B 85  1 ? 20 
HELX_P HELX_P12 AB3 VAL B 93  ? ARG B 100 ? VAL B 85  ARG B 92  1 ? 8  
HELX_P HELX_P13 AB4 THR B 126 ? LEU B 136 ? THR B 118 LEU B 128 1 ? 11 
HELX_P HELX_P14 AB5 THR B 150 ? ALA B 160 ? THR B 142 ALA B 152 1 ? 11 
HELX_P HELX_P15 AB6 ASP B 173 ? ASP B 189 ? ASP B 165 ASP B 181 1 ? 17 
HELX_P HELX_P16 AB7 PRO B 200 ? GLU B 218 ? PRO B 192 GLU B 210 1 ? 19 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 5 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel 
AA1 2 3 ? parallel 
AA1 3 4 ? parallel 
AA1 4 5 ? parallel 
AA2 1 2 ? parallel 
AA2 2 3 ? parallel 
AA2 3 4 ? parallel 
AA2 4 5 ? 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 MET A 43  ? ARG A 47  ? MET A 35  ARG A 39  
AA1 2 TRP A 103 ? ASP A 107 ? TRP A 95  ASP A 99  
AA1 3 TYR A 13  ? GLY A 18  ? TYR A 5   GLY A 10  
AA1 4 LEU A 143 ? ASP A 148 ? LEU A 135 ASP A 140 
AA1 5 ILE A 192 ? ASP A 196 ? ILE A 184 ASP A 188 
AA2 1 MET B 43  ? ARG B 47  ? MET B 35  ARG B 39  
AA2 2 TRP B 103 ? ASP B 107 ? TRP B 95  ASP B 99  
AA2 3 TYR B 13  ? GLY B 18  ? TYR B 5   GLY B 10  
AA2 4 LEU B 143 ? ASP B 148 ? LEU B 135 ASP B 140 
AA2 5 ILE B 192 ? ASP B 196 ? ILE B 184 ASP B 188 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N VAL A 44  ? N VAL A 36  O ILE A 105 ? O ILE A 97  
AA1 2 3 O VAL A 104 ? O VAL A 96  N ILE A 14  ? N ILE A 6   
AA1 3 4 N VAL A 15  ? N VAL A 7   O LEU A 145 ? O LEU A 137 
AA1 4 5 N TYR A 146 ? N TYR A 138 O ARG A 193 ? O ARG A 185 
AA2 1 2 N VAL B 44  ? N VAL B 36  O ILE B 105 ? O ILE B 97  
AA2 2 3 O VAL B 104 ? O VAL B 96  N ILE B 14  ? N ILE B 6   
AA2 3 4 N VAL B 15  ? N VAL B 7   O LEU B 145 ? O LEU B 137 
AA2 4 5 N TYR B 146 ? N TYR B 138 O VAL B 195 ? O VAL B 187 
# 
_pdbx_entry_details.entry_id                   9O57 
_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 
# 
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 MET A 1   ? ? -47.59  151.40 
2 1 ASP A 62  ? ? 67.72   -0.20  
3 1 VAL A 85  ? ? -120.65 -58.18 
4 1 ARG A 100 ? ? 72.06   44.97  
5 1 ARG B 2   ? ? -36.78  128.48 
# 
_pdbx_SG_project.id                    1 
_pdbx_SG_project.project_name          'NIAID, National Institute of Allergy and Infectious Diseases' 
_pdbx_SG_project.full_name_of_center   'Seattle Structural Genomics Center for Infectious Disease' 
_pdbx_SG_project.initial_of_center     SSGCID 
# 
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 -8.3051  1.6639  34.1776 0.6558 ? 0.0183  ? -0.0174 ? 0.5321 ? -0.0136 ? 0.5499 ? 3.6360 ? 
-1.6429 ? 0.0171  ? 3.4054 ? 1.3694  ? 0.7452 ? -0.0674 ? -0.4715 ? 0.4414  ? 0.4281  ? -0.5278 ? -0.1866 ? -0.8894 ? 0.8387  ? 
-0.0080 ? 
2  'X-RAY DIFFRACTION' ? refined -0.8644  3.5652  35.2603 0.6758 ? -0.0487 ? 0.0070  ? 0.6028 ? 0.0355  ? 0.6761 ? 1.0620 ? 0.5524 
? 0.7644  ? 0.7634 ? 0.5840  ? 0.6173 ? 0.0559  ? 1.1600  ? 0.6518  ? -0.6535 ? 0.3588  ? -0.5435 ? -1.0731 ? -0.3311 ? 0.0011  ? 
3  'X-RAY DIFFRACTION' ? refined 13.1159  0.9052  18.7456 0.4733 ? -0.0482 ? 0.0568  ? 0.5699 ? 0.0035  ? 0.4245 ? 1.0775 ? 
-0.9848 ? -0.9694 ? 1.6391 ? 1.2055  ? 0.9713 ? 0.3430  ? 0.0210  ? 0.3149  ? -0.0803 ? -0.1076 ? -0.0473 ? -0.9802 ? 0.0280  ? 
0.0008  ? 
4  'X-RAY DIFFRACTION' ? refined 2.8132   -7.2725 30.9523 0.4218 ? -0.0161 ? 0.0439  ? 0.6763 ? -0.0587 ? 0.4640 ? 1.7711 ? 1.5514 
? 0.3450  ? 1.5785 ? 0.0104  ? 0.3193 ? -0.1736 ? 0.0600  ? -0.5237 ? 0.4623  ? 0.3234  ? 0.3141  ? -0.1008 ? 0.7844  ? -0.0301 ? 
5  'X-RAY DIFFRACTION' ? refined -11.5073 -2.4354 15.5494 0.5693 ? 0.1095  ? -0.0987 ? 0.6676 ? -0.1347 ? 0.5075 ? 1.6043 ? 
-0.0866 ? 0.3530  ? 0.1170 ? 0.4233  ? 1.8945 ? 0.3637  ? 0.3668  ? -0.0159 ? 0.1596  ? -0.0467 ? 0.0094  ? 0.0703  ? 0.4724  ? 
-0.0003 ? 
6  'X-RAY DIFFRACTION' ? refined -16.7990 -2.4375 31.3238 0.4355 ? -0.0190 ? -0.0808 ? 0.4825 ? -0.0504 ? 0.6168 ? 0.7288 ? 
-0.3500 ? -0.4566 ? 0.5860 ? -0.6078 ? 1.8392 ? -0.0765 ? -0.2156 ? -0.0940 ? -0.1246 ? 0.1983  ? 0.0479  ? -0.1240 ? -0.3035 ? 
-0.0002 ? 
7  'X-RAY DIFFRACTION' ? refined -1.8637  13.8255 43.0424 0.5207 ? -0.0394 ? 0.0594  ? 0.5608 ? 0.0280  ? 0.5294 ? 2.2278 ? 0.5882 
? 0.8325  ? 2.3391 ? -0.6344 ? 0.7657 ? 0.0918  ? -0.0334 ? -0.6196 ? 0.0899  ? -0.4078 ? 0.5504  ? 0.5115  ? -0.1346 ? -0.0054 ? 
8  'X-RAY DIFFRACTION' ? refined 11.7773  2.4033  59.6683 0.5719 ? 0.0427  ? -0.0711 ? 0.6397 ? 0.0344  ? 0.4864 ? 1.1223 ? 
-0.0383 ? -1.3874 ? 1.2067 ? -0.4572 ? 1.7950 ? 0.0063  ? -0.6844 ? 0.0950  ? 0.0798  ? -0.0260 ? 0.1424  ? 0.1540  ? -0.5635 ? 
-0.0019 ? 
9  'X-RAY DIFFRACTION' ? refined 10.2247  14.2654 47.2904 0.3845 ? 0.1219  ? -0.0256 ? 0.3097 ? -0.0603 ? 0.5541 ? 1.3425 ? 0.1538 
? 0.6556  ? 2.6219 ? -0.0716 ? 1.5051 ? -0.3331 ? 0.2292  ? 0.6491  ? -0.1689 ? 0.4743  ? -0.3593 ? -0.0963 ? 0.7985  ? -0.0723 ? 
10 'X-RAY DIFFRACTION' ? refined -3.5971  22.8756 51.8459 0.4773 ? -0.0930 ? 0.0551  ? 0.4747 ? -0.1042 ? 0.6022 ? 0.3597 ? 
-0.1913 ? 0.9547  ? 3.5833 ? 0.3590  ? 2.6659 ? 0.3307  ? -0.3373 ? 0.3799  ? 0.5167  ? -0.4251 ? 0.3484  ? -0.3875 ? -0.0464 ? 
-0.0004 ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1  'X-RAY DIFFRACTION' 1  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid -1 through 29 )
;
2  'X-RAY DIFFRACTION' 2  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 30 through 44 )
;
3  'X-RAY DIFFRACTION' 3  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 45 through 84 )
;
4  'X-RAY DIFFRACTION' 4  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 85 through 134 )
;
5  'X-RAY DIFFRACTION' 5  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 135 through 180 )
;
6  'X-RAY DIFFRACTION' 6  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 181 through 211 )
;
7  'X-RAY DIFFRACTION' 7  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 1 through 44 )
;
8  'X-RAY DIFFRACTION' 8  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 45 through 84 )
;
9  'X-RAY DIFFRACTION' 9  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 85 through 127 )
;
10 'X-RAY DIFFRACTION' 10 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 128 through 211 )
;
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET -7  ? A MET 1   
2  1 Y 1 A ALA -6  ? A ALA 2   
3  1 Y 1 A HIS -5  ? A HIS 3   
4  1 Y 1 A HIS -4  ? A HIS 4   
5  1 Y 1 A HIS -3  ? A HIS 5   
6  1 Y 1 A HIS -2  ? A HIS 6   
7  1 Y 1 A ASP 102 ? A ASP 110 
8  1 Y 1 A LEU 103 ? A LEU 111 
9  1 Y 1 A SER 104 ? A SER 112 
10 1 Y 1 A THR 105 ? A THR 113 
11 1 Y 1 A GLN 106 ? A GLN 114 
12 1 Y 1 A ALA 107 ? A ALA 115 
13 1 Y 1 A TYR 108 ? A TYR 116 
14 1 Y 1 A GLN 109 ? A GLN 117 
15 1 Y 1 A GLY 110 ? A GLY 118 
16 1 Y 1 A GLY 111 ? A GLY 119 
17 1 Y 1 A GLY 112 ? A GLY 120 
18 1 Y 1 A ARG 113 ? A ARG 121 
19 1 Y 1 A GLY 114 ? A GLY 122 
20 1 Y 1 A ILE 115 ? A ILE 123 
21 1 Y 1 A ASP 116 ? A ASP 124 
22 1 Y 1 A GLN 117 ? A GLN 125 
23 1 Y 1 A ARG 153 ? A ARG 161 
24 1 Y 1 A GLY 154 ? A GLY 162 
25 1 Y 1 A GLU 155 ? A GLU 163 
26 1 Y 1 A LEU 156 ? A LEU 164 
27 1 Y 1 A ASP 157 ? A ASP 165 
28 1 Y 1 A ARG 158 ? A ARG 166 
29 1 Y 1 A ILE 159 ? A ILE 167 
30 1 Y 1 A GLU 160 ? A GLU 168 
31 1 Y 1 A GLN 161 ? A GLN 169 
32 1 Y 1 A GLU 162 ? A GLU 170 
33 1 Y 1 A SER 163 ? A SER 171 
34 1 Y 1 A LEU 164 ? A LEU 172 
35 1 Y 1 A LEU 212 ? A LEU 220 
36 1 Y 1 A PRO 213 ? A PRO 221 
37 1 Y 1 B MET -7  ? B MET 1   
38 1 Y 1 B ALA -6  ? B ALA 2   
39 1 Y 1 B HIS -5  ? B HIS 3   
40 1 Y 1 B HIS -4  ? B HIS 4   
41 1 Y 1 B HIS -3  ? B HIS 5   
42 1 Y 1 B HIS -2  ? B HIS 6   
43 1 Y 1 B HIS -1  ? B HIS 7   
44 1 Y 1 B HIS 0   ? B HIS 8   
45 1 Y 1 B ASP 102 ? B ASP 110 
46 1 Y 1 B LEU 103 ? B LEU 111 
47 1 Y 1 B SER 104 ? B SER 112 
48 1 Y 1 B THR 105 ? B THR 113 
49 1 Y 1 B GLN 106 ? B GLN 114 
50 1 Y 1 B ALA 107 ? B ALA 115 
51 1 Y 1 B TYR 108 ? B TYR 116 
52 1 Y 1 B GLN 109 ? B GLN 117 
53 1 Y 1 B GLY 110 ? B GLY 118 
54 1 Y 1 B GLY 111 ? B GLY 119 
55 1 Y 1 B GLY 112 ? B GLY 120 
56 1 Y 1 B ARG 113 ? B ARG 121 
57 1 Y 1 B GLY 114 ? B GLY 122 
58 1 Y 1 B ILE 115 ? B ILE 123 
59 1 Y 1 B ASP 116 ? B ASP 124 
60 1 Y 1 B ARG 153 ? B ARG 161 
61 1 Y 1 B GLY 154 ? B GLY 162 
62 1 Y 1 B GLU 155 ? B GLU 163 
63 1 Y 1 B LEU 156 ? B LEU 164 
64 1 Y 1 B ASP 157 ? B ASP 165 
65 1 Y 1 B ARG 158 ? B ARG 166 
66 1 Y 1 B ILE 159 ? B ILE 167 
67 1 Y 1 B GLU 160 ? B GLU 168 
68 1 Y 1 B GLN 161 ? B GLN 169 
69 1 Y 1 B GLU 162 ? B GLU 170 
70 1 Y 1 B SER 163 ? B SER 171 
71 1 Y 1 B LEU 212 ? B LEU 220 
72 1 Y 1 B PRO 213 ? B PRO 221 
# 
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  
CL  CL   CL N N 74  
CYS N    N  N N 75  
CYS CA   C  N R 76  
CYS C    C  N N 77  
CYS O    O  N N 78  
CYS CB   C  N N 79  
CYS SG   S  N N 80  
CYS OXT  O  N N 81  
CYS H    H  N N 82  
CYS H2   H  N N 83  
CYS HA   H  N N 84  
CYS HB2  H  N N 85  
CYS HB3  H  N N 86  
CYS HG   H  N N 87  
CYS HXT  H  N N 88  
GLN N    N  N N 89  
GLN CA   C  N S 90  
GLN C    C  N N 91  
GLN O    O  N N 92  
GLN CB   C  N N 93  
GLN CG   C  N N 94  
GLN CD   C  N N 95  
GLN OE1  O  N N 96  
GLN NE2  N  N N 97  
GLN OXT  O  N N 98  
GLN H    H  N N 99  
GLN H2   H  N N 100 
GLN HA   H  N N 101 
GLN HB2  H  N N 102 
GLN HB3  H  N N 103 
GLN HG2  H  N N 104 
GLN HG3  H  N N 105 
GLN HE21 H  N N 106 
GLN HE22 H  N N 107 
GLN HXT  H  N N 108 
GLU N    N  N N 109 
GLU CA   C  N S 110 
GLU C    C  N N 111 
GLU O    O  N N 112 
GLU CB   C  N N 113 
GLU CG   C  N N 114 
GLU CD   C  N N 115 
GLU OE1  O  N N 116 
GLU OE2  O  N N 117 
GLU OXT  O  N N 118 
GLU H    H  N N 119 
GLU H2   H  N N 120 
GLU HA   H  N N 121 
GLU HB2  H  N N 122 
GLU HB3  H  N N 123 
GLU HG2  H  N N 124 
GLU HG3  H  N N 125 
GLU HE2  H  N N 126 
GLU HXT  H  N N 127 
GLY N    N  N N 128 
GLY CA   C  N N 129 
GLY C    C  N N 130 
GLY O    O  N N 131 
GLY OXT  O  N N 132 
GLY H    H  N N 133 
GLY H2   H  N N 134 
GLY HA2  H  N N 135 
GLY HA3  H  N N 136 
GLY HXT  H  N N 137 
HIS N    N  N N 138 
HIS CA   C  N S 139 
HIS C    C  N N 140 
HIS O    O  N N 141 
HIS CB   C  N N 142 
HIS CG   C  Y N 143 
HIS ND1  N  Y N 144 
HIS CD2  C  Y N 145 
HIS CE1  C  Y N 146 
HIS NE2  N  Y N 147 
HIS OXT  O  N N 148 
HIS H    H  N N 149 
HIS H2   H  N N 150 
HIS HA   H  N N 151 
HIS HB2  H  N N 152 
HIS HB3  H  N N 153 
HIS HD1  H  N N 154 
HIS HD2  H  N N 155 
HIS HE1  H  N N 156 
HIS HE2  H  N N 157 
HIS HXT  H  N N 158 
ILE N    N  N N 159 
ILE CA   C  N S 160 
ILE C    C  N N 161 
ILE O    O  N N 162 
ILE CB   C  N S 163 
ILE CG1  C  N N 164 
ILE CG2  C  N N 165 
ILE CD1  C  N N 166 
ILE OXT  O  N N 167 
ILE H    H  N N 168 
ILE H2   H  N N 169 
ILE HA   H  N N 170 
ILE HB   H  N N 171 
ILE HG12 H  N N 172 
ILE HG13 H  N N 173 
ILE HG21 H  N N 174 
ILE HG22 H  N N 175 
ILE HG23 H  N N 176 
ILE HD11 H  N N 177 
ILE HD12 H  N N 178 
ILE HD13 H  N N 179 
ILE HXT  H  N N 180 
LEU N    N  N N 181 
LEU CA   C  N S 182 
LEU C    C  N N 183 
LEU O    O  N N 184 
LEU CB   C  N N 185 
LEU CG   C  N N 186 
LEU CD1  C  N N 187 
LEU CD2  C  N N 188 
LEU OXT  O  N N 189 
LEU H    H  N N 190 
LEU H2   H  N N 191 
LEU HA   H  N N 192 
LEU HB2  H  N N 193 
LEU HB3  H  N N 194 
LEU HG   H  N N 195 
LEU HD11 H  N N 196 
LEU HD12 H  N N 197 
LEU HD13 H  N N 198 
LEU HD21 H  N N 199 
LEU HD22 H  N N 200 
LEU HD23 H  N N 201 
LEU HXT  H  N N 202 
LYS N    N  N N 203 
LYS CA   C  N S 204 
LYS C    C  N N 205 
LYS O    O  N N 206 
LYS CB   C  N N 207 
LYS CG   C  N N 208 
LYS CD   C  N N 209 
LYS CE   C  N N 210 
LYS NZ   N  N N 211 
LYS OXT  O  N N 212 
LYS H    H  N N 213 
LYS H2   H  N N 214 
LYS HA   H  N N 215 
LYS HB2  H  N N 216 
LYS HB3  H  N N 217 
LYS HG2  H  N N 218 
LYS HG3  H  N N 219 
LYS HD2  H  N N 220 
LYS HD3  H  N N 221 
LYS HE2  H  N N 222 
LYS HE3  H  N N 223 
LYS HZ1  H  N N 224 
LYS HZ2  H  N N 225 
LYS HZ3  H  N N 226 
LYS HXT  H  N N 227 
MET N    N  N N 228 
MET CA   C  N S 229 
MET C    C  N N 230 
MET O    O  N N 231 
MET CB   C  N N 232 
MET CG   C  N N 233 
MET SD   S  N N 234 
MET CE   C  N N 235 
MET OXT  O  N N 236 
MET H    H  N N 237 
MET H2   H  N N 238 
MET HA   H  N N 239 
MET HB2  H  N N 240 
MET HB3  H  N N 241 
MET HG2  H  N N 242 
MET HG3  H  N N 243 
MET HE1  H  N N 244 
MET HE2  H  N N 245 
MET HE3  H  N N 246 
MET HXT  H  N N 247 
PHE N    N  N N 248 
PHE CA   C  N S 249 
PHE C    C  N N 250 
PHE O    O  N N 251 
PHE CB   C  N N 252 
PHE CG   C  Y N 253 
PHE CD1  C  Y N 254 
PHE CD2  C  Y N 255 
PHE CE1  C  Y N 256 
PHE CE2  C  Y N 257 
PHE CZ   C  Y N 258 
PHE OXT  O  N N 259 
PHE H    H  N N 260 
PHE H2   H  N N 261 
PHE HA   H  N N 262 
PHE HB2  H  N N 263 
PHE HB3  H  N N 264 
PHE HD1  H  N N 265 
PHE HD2  H  N N 266 
PHE HE1  H  N N 267 
PHE HE2  H  N N 268 
PHE HZ   H  N N 269 
PHE HXT  H  N N 270 
PRO N    N  N N 271 
PRO CA   C  N S 272 
PRO C    C  N N 273 
PRO O    O  N N 274 
PRO CB   C  N N 275 
PRO CG   C  N N 276 
PRO CD   C  N N 277 
PRO OXT  O  N N 278 
PRO H    H  N N 279 
PRO HA   H  N N 280 
PRO HB2  H  N N 281 
PRO HB3  H  N N 282 
PRO HG2  H  N N 283 
PRO HG3  H  N N 284 
PRO HD2  H  N N 285 
PRO HD3  H  N N 286 
PRO HXT  H  N N 287 
SER N    N  N N 288 
SER CA   C  N S 289 
SER C    C  N N 290 
SER O    O  N N 291 
SER CB   C  N N 292 
SER OG   O  N N 293 
SER OXT  O  N N 294 
SER H    H  N N 295 
SER H2   H  N N 296 
SER HA   H  N N 297 
SER HB2  H  N N 298 
SER HB3  H  N N 299 
SER HG   H  N N 300 
SER HXT  H  N N 301 
THR N    N  N N 302 
THR CA   C  N S 303 
THR C    C  N N 304 
THR O    O  N N 305 
THR CB   C  N R 306 
THR OG1  O  N N 307 
THR CG2  C  N N 308 
THR OXT  O  N N 309 
THR H    H  N N 310 
THR H2   H  N N 311 
THR HA   H  N N 312 
THR HB   H  N N 313 
THR HG1  H  N N 314 
THR HG21 H  N N 315 
THR HG22 H  N N 316 
THR HG23 H  N N 317 
THR HXT  H  N N 318 
TRP N    N  N N 319 
TRP CA   C  N S 320 
TRP C    C  N N 321 
TRP O    O  N N 322 
TRP CB   C  N N 323 
TRP CG   C  Y N 324 
TRP CD1  C  Y N 325 
TRP CD2  C  Y N 326 
TRP NE1  N  Y N 327 
TRP CE2  C  Y N 328 
TRP CE3  C  Y N 329 
TRP CZ2  C  Y N 330 
TRP CZ3  C  Y N 331 
TRP CH2  C  Y N 332 
TRP OXT  O  N N 333 
TRP H    H  N N 334 
TRP H2   H  N N 335 
TRP HA   H  N N 336 
TRP HB2  H  N N 337 
TRP HB3  H  N N 338 
TRP HD1  H  N N 339 
TRP HE1  H  N N 340 
TRP HE3  H  N N 341 
TRP HZ2  H  N N 342 
TRP HZ3  H  N N 343 
TRP HH2  H  N N 344 
TRP HXT  H  N N 345 
TYR N    N  N N 346 
TYR CA   C  N S 347 
TYR C    C  N N 348 
TYR O    O  N N 349 
TYR CB   C  N N 350 
TYR CG   C  Y N 351 
TYR CD1  C  Y N 352 
TYR CD2  C  Y N 353 
TYR CE1  C  Y N 354 
TYR CE2  C  Y N 355 
TYR CZ   C  Y N 356 
TYR OH   O  N N 357 
TYR OXT  O  N N 358 
TYR H    H  N N 359 
TYR H2   H  N N 360 
TYR HA   H  N N 361 
TYR HB2  H  N N 362 
TYR HB3  H  N N 363 
TYR HD1  H  N N 364 
TYR HD2  H  N N 365 
TYR HE1  H  N N 366 
TYR HE2  H  N N 367 
TYR HH   H  N N 368 
TYR HXT  H  N N 369 
VAL N    N  N N 370 
VAL CA   C  N S 371 
VAL C    C  N N 372 
VAL O    O  N N 373 
VAL CB   C  N N 374 
VAL CG1  C  N N 375 
VAL CG2  C  N N 376 
VAL OXT  O  N N 377 
VAL H    H  N N 378 
VAL H2   H  N N 379 
VAL HA   H  N N 380 
VAL HB   H  N N 381 
VAL HG11 H  N N 382 
VAL HG12 H  N N 383 
VAL HG13 H  N N 384 
VAL HG21 H  N N 385 
VAL HG22 H  N N 386 
VAL HG23 H  N N 387 
VAL HXT  H  N N 388 
# 
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 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
ILE N   CA   sing N N 150 
ILE N   H    sing N N 151 
ILE N   H2   sing N N 152 
ILE CA  C    sing N N 153 
ILE CA  CB   sing N N 154 
ILE CA  HA   sing N N 155 
ILE C   O    doub N N 156 
ILE C   OXT  sing N N 157 
ILE CB  CG1  sing N N 158 
ILE CB  CG2  sing N N 159 
ILE CB  HB   sing N N 160 
ILE CG1 CD1  sing N N 161 
ILE CG1 HG12 sing N N 162 
ILE CG1 HG13 sing N N 163 
ILE CG2 HG21 sing N N 164 
ILE CG2 HG22 sing N N 165 
ILE CG2 HG23 sing N N 166 
ILE CD1 HD11 sing N N 167 
ILE CD1 HD12 sing N N 168 
ILE CD1 HD13 sing N N 169 
ILE OXT HXT  sing N N 170 
LEU N   CA   sing N N 171 
LEU N   H    sing N N 172 
LEU N   H2   sing N N 173 
LEU CA  C    sing N N 174 
LEU CA  CB   sing N N 175 
LEU CA  HA   sing N N 176 
LEU C   O    doub N N 177 
LEU C   OXT  sing N N 178 
LEU CB  CG   sing N N 179 
LEU CB  HB2  sing N N 180 
LEU CB  HB3  sing N N 181 
LEU CG  CD1  sing N N 182 
LEU CG  CD2  sing N N 183 
LEU CG  HG   sing N N 184 
LEU CD1 HD11 sing N N 185 
LEU CD1 HD12 sing N N 186 
LEU CD1 HD13 sing N N 187 
LEU CD2 HD21 sing N N 188 
LEU CD2 HD22 sing N N 189 
LEU CD2 HD23 sing N N 190 
LEU OXT HXT  sing N N 191 
LYS N   CA   sing N N 192 
LYS N   H    sing N N 193 
LYS N   H2   sing N N 194 
LYS CA  C    sing N N 195 
LYS CA  CB   sing N N 196 
LYS CA  HA   sing N N 197 
LYS C   O    doub N N 198 
LYS C   OXT  sing N N 199 
LYS CB  CG   sing N N 200 
LYS CB  HB2  sing N N 201 
LYS CB  HB3  sing N N 202 
LYS CG  CD   sing N N 203 
LYS CG  HG2  sing N N 204 
LYS CG  HG3  sing N N 205 
LYS CD  CE   sing N N 206 
LYS CD  HD2  sing N N 207 
LYS CD  HD3  sing N N 208 
LYS CE  NZ   sing N N 209 
LYS CE  HE2  sing N N 210 
LYS CE  HE3  sing N N 211 
LYS NZ  HZ1  sing N N 212 
LYS NZ  HZ2  sing N N 213 
LYS NZ  HZ3  sing N N 214 
LYS OXT HXT  sing N N 215 
MET N   CA   sing N N 216 
MET N   H    sing N N 217 
MET N   H2   sing N N 218 
MET CA  C    sing N N 219 
MET CA  CB   sing N N 220 
MET CA  HA   sing N N 221 
MET C   O    doub N N 222 
MET C   OXT  sing N N 223 
MET CB  CG   sing N N 224 
MET CB  HB2  sing N N 225 
MET CB  HB3  sing N N 226 
MET CG  SD   sing N N 227 
MET CG  HG2  sing N N 228 
MET CG  HG3  sing N N 229 
MET SD  CE   sing N N 230 
MET CE  HE1  sing N N 231 
MET CE  HE2  sing N N 232 
MET CE  HE3  sing N N 233 
MET OXT HXT  sing N N 234 
PHE N   CA   sing N N 235 
PHE N   H    sing N N 236 
PHE N   H2   sing N N 237 
PHE CA  C    sing N N 238 
PHE CA  CB   sing N N 239 
PHE CA  HA   sing N N 240 
PHE C   O    doub N N 241 
PHE C   OXT  sing N N 242 
PHE CB  CG   sing N N 243 
PHE CB  HB2  sing N N 244 
PHE CB  HB3  sing N N 245 
PHE CG  CD1  doub Y N 246 
PHE CG  CD2  sing Y N 247 
PHE CD1 CE1  sing Y N 248 
PHE CD1 HD1  sing N N 249 
PHE CD2 CE2  doub Y N 250 
PHE CD2 HD2  sing N N 251 
PHE CE1 CZ   doub Y N 252 
PHE CE1 HE1  sing N N 253 
PHE CE2 CZ   sing Y N 254 
PHE CE2 HE2  sing N N 255 
PHE CZ  HZ   sing N N 256 
PHE OXT HXT  sing N N 257 
PRO N   CA   sing N N 258 
PRO N   CD   sing N N 259 
PRO N   H    sing N N 260 
PRO CA  C    sing N N 261 
PRO CA  CB   sing N N 262 
PRO CA  HA   sing N N 263 
PRO C   O    doub N N 264 
PRO C   OXT  sing N N 265 
PRO CB  CG   sing N N 266 
PRO CB  HB2  sing N N 267 
PRO CB  HB3  sing N N 268 
PRO CG  CD   sing N N 269 
PRO CG  HG2  sing N N 270 
PRO CG  HG3  sing N N 271 
PRO CD  HD2  sing N N 272 
PRO CD  HD3  sing N N 273 
PRO OXT HXT  sing N N 274 
SER N   CA   sing N N 275 
SER N   H    sing N N 276 
SER N   H2   sing N N 277 
SER CA  C    sing N N 278 
SER CA  CB   sing N N 279 
SER CA  HA   sing N N 280 
SER C   O    doub N N 281 
SER C   OXT  sing N N 282 
SER CB  OG   sing N N 283 
SER CB  HB2  sing N N 284 
SER CB  HB3  sing N N 285 
SER OG  HG   sing N N 286 
SER OXT HXT  sing N N 287 
THR N   CA   sing N N 288 
THR N   H    sing N N 289 
THR N   H2   sing N N 290 
THR CA  C    sing N N 291 
THR CA  CB   sing N N 292 
THR CA  HA   sing N N 293 
THR C   O    doub N N 294 
THR C   OXT  sing N N 295 
THR CB  OG1  sing N N 296 
THR CB  CG2  sing N N 297 
THR CB  HB   sing N N 298 
THR OG1 HG1  sing N N 299 
THR CG2 HG21 sing N N 300 
THR CG2 HG22 sing N N 301 
THR CG2 HG23 sing N N 302 
THR OXT HXT  sing N N 303 
TRP N   CA   sing N N 304 
TRP N   H    sing N N 305 
TRP N   H2   sing N N 306 
TRP CA  C    sing N N 307 
TRP CA  CB   sing N N 308 
TRP CA  HA   sing N N 309 
TRP C   O    doub N N 310 
TRP C   OXT  sing N N 311 
TRP CB  CG   sing N N 312 
TRP CB  HB2  sing N N 313 
TRP CB  HB3  sing N N 314 
TRP CG  CD1  doub Y N 315 
TRP CG  CD2  sing Y N 316 
TRP CD1 NE1  sing Y N 317 
TRP CD1 HD1  sing N N 318 
TRP CD2 CE2  doub Y N 319 
TRP CD2 CE3  sing Y N 320 
TRP NE1 CE2  sing Y N 321 
TRP NE1 HE1  sing N N 322 
TRP CE2 CZ2  sing Y N 323 
TRP CE3 CZ3  doub Y N 324 
TRP CE3 HE3  sing N N 325 
TRP CZ2 CH2  doub Y N 326 
TRP CZ2 HZ2  sing N N 327 
TRP CZ3 CH2  sing Y N 328 
TRP CZ3 HZ3  sing N N 329 
TRP CH2 HH2  sing N N 330 
TRP OXT HXT  sing N N 331 
TYR N   CA   sing N N 332 
TYR N   H    sing N N 333 
TYR N   H2   sing N N 334 
TYR CA  C    sing N N 335 
TYR CA  CB   sing N N 336 
TYR CA  HA   sing N N 337 
TYR C   O    doub N N 338 
TYR C   OXT  sing N N 339 
TYR CB  CG   sing N N 340 
TYR CB  HB2  sing N N 341 
TYR CB  HB3  sing N N 342 
TYR CG  CD1  doub Y N 343 
TYR CG  CD2  sing Y N 344 
TYR CD1 CE1  sing Y N 345 
TYR CD1 HD1  sing N N 346 
TYR CD2 CE2  doub Y N 347 
TYR CD2 HD2  sing N N 348 
TYR CE1 CZ   doub Y N 349 
TYR CE1 HE1  sing N N 350 
TYR CE2 CZ   sing Y N 351 
TYR CE2 HE2  sing N N 352 
TYR CZ  OH   sing N N 353 
TYR OH  HH   sing N N 354 
TYR OXT HXT  sing N N 355 
VAL N   CA   sing N N 356 
VAL N   H    sing N N 357 
VAL N   H2   sing N N 358 
VAL CA  C    sing N N 359 
VAL CA  CB   sing N N 360 
VAL CA  HA   sing N N 361 
VAL C   O    doub N N 362 
VAL C   OXT  sing N N 363 
VAL CB  CG1  sing N N 364 
VAL CB  CG2  sing N N 365 
VAL CB  HB   sing N N 366 
VAL CG1 HG11 sing N N 367 
VAL CG1 HG12 sing N N 368 
VAL CG1 HG13 sing N N 369 
VAL CG2 HG21 sing N N 370 
VAL CG2 HG22 sing N N 371 
VAL CG2 HG23 sing N N 372 
VAL OXT HXT  sing N N 373 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 'United States' 75N93022C00036 1 
'National Institutes of Health/Office of the Director'                                            'United States' S10OD030394    2 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   4TMK 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9O57 
_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]   0.015059 
_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]   0.013254 
_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]   0.013155 
_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  
CL 
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . HIS A 1 7   ? -8.043  -2.131  53.548 1.00 125.50 ?  -1  HIS A N   1 
ATOM   2    C  CA  . HIS A 1 7   ? -7.604  -3.511  53.194 1.00 123.36 ?  -1  HIS A CA  1 
ATOM   3    C  C   . HIS A 1 7   ? -6.553  -3.523  52.085 1.00 136.94 ?  -1  HIS A C   1 
ATOM   4    O  O   . HIS A 1 7   ? -5.790  -4.481  51.965 1.00 135.85 ?  -1  HIS A O   1 
ATOM   5    C  CB  . HIS A 1 7   ? -8.808  -4.359  52.773 1.00 121.49 ?  -1  HIS A CB  1 
ATOM   6    C  CG  . HIS A 1 7   ? -9.821  -3.609  51.963 1.00 134.91 ?  -1  HIS A CG  1 
ATOM   7    N  ND1 . HIS A 1 7   ? -11.064 -3.276  52.454 1.00 120.14 ?  -1  HIS A ND1 1 
ATOM   8    C  CD2 . HIS A 1 7   ? -9.774  -3.122  50.702 1.00 133.84 ?  -1  HIS A CD2 1 
ATOM   9    C  CE1 . HIS A 1 7   ? -11.742 -2.620  51.530 1.00 128.31 ?  -1  HIS A CE1 1 
ATOM   10   N  NE2 . HIS A 1 7   ? -10.981 -2.514  50.457 1.00 130.89 ?  -1  HIS A NE2 1 
ATOM   11   N  N   . HIS A 1 8   ? -6.510  -2.459  51.282 1.00 139.29 ?  0   HIS A N   1 
ATOM   12   C  CA  . HIS A 1 8   ? -5.457  -2.262  50.285 1.00 142.44 ?  0   HIS A CA  1 
ATOM   13   C  C   . HIS A 1 8   ? -5.422  -3.427  49.287 1.00 132.69 ?  0   HIS A C   1 
ATOM   14   O  O   . HIS A 1 8   ? -4.499  -4.245  49.254 1.00 136.96 ?  0   HIS A O   1 
ATOM   15   C  CB  . HIS A 1 8   ? -4.101  -2.072  50.980 1.00 123.13 ?  0   HIS A CB  1 
ATOM   16   C  CG  . HIS A 1 8   ? -4.193  -1.410  52.322 1.00 141.98 ?  0   HIS A CG  1 
ATOM   17   N  ND1 . HIS A 1 8   ? -5.023  -0.339  52.573 1.00 146.25 ?  0   HIS A ND1 1 
ATOM   18   C  CD2 . HIS A 1 8   ? -3.565  -1.679  53.492 1.00 134.31 ?  0   HIS A CD2 1 
ATOM   19   C  CE1 . HIS A 1 8   ? -4.900  0.027   53.836 1.00 130.09 ?  0   HIS A CE1 1 
ATOM   20   N  NE2 . HIS A 1 8   ? -4.021  -0.770  54.416 1.00 146.11 ?  0   HIS A NE2 1 
ATOM   21   N  N   . MET A 1 9   ? -6.480  -3.476  48.474 1.00 114.12 ?  1   MET A N   1 
ATOM   22   C  CA  . MET A 1 9   ? -6.707  -4.576  47.543 1.00 104.22 ?  1   MET A CA  1 
ATOM   23   C  C   . MET A 1 9   ? -5.458  -4.922  46.741 1.00 100.29 ?  1   MET A C   1 
ATOM   24   O  O   . MET A 1 9   ? -4.614  -4.069  46.460 1.00 90.45  ?  1   MET A O   1 
ATOM   25   C  CB  . MET A 1 9   ? -7.840  -4.208  46.573 1.00 100.07 ?  1   MET A CB  1 
ATOM   26   C  CG  . MET A 1 9   ? -9.154  -3.824  47.243 1.00 105.38 ?  1   MET A CG  1 
ATOM   27   S  SD  . MET A 1 9   ? -9.809  -2.220  46.731 1.00 105.97 ?  1   MET A SD  1 
ATOM   28   C  CE  . MET A 1 9   ? -10.842 -2.679  45.341 1.00 99.73  ?  1   MET A CE  1 
ATOM   29   N  N   . ARG A 1 10  ? -5.366  -6.193  46.346 1.00 98.46  ?  2   ARG A N   1 
ATOM   30   C  CA  . ARG A 1 10  ? -4.249  -6.676  45.542 1.00 79.97  ?  2   ARG A CA  1 
ATOM   31   C  C   . ARG A 1 10  ? -4.082  -5.826  44.292 1.00 74.03  ?  2   ARG A C   1 
ATOM   32   O  O   . ARG A 1 10  ? -5.053  -5.513  43.599 1.00 69.29  ?  2   ARG A O   1 
ATOM   33   C  CB  . ARG A 1 10  ? -4.485  -8.148  45.160 1.00 79.46  ?  2   ARG A CB  1 
ATOM   34   C  CG  . ARG A 1 10  ? -3.529  -8.731  44.113 1.00 80.52  ?  2   ARG A CG  1 
ATOM   35   C  CD  . ARG A 1 10  ? -4.295  -9.405  42.964 1.00 83.97  ?  2   ARG A CD  1 
ATOM   36   N  NE  . ARG A 1 10  ? -3.586  -10.547 42.399 1.00 102.80 ?  2   ARG A NE  1 
ATOM   37   C  CZ  . ARG A 1 10  ? -3.968  -11.213 41.317 1.00 107.53 ?  2   ARG A CZ  1 
ATOM   38   N  NH1 . ARG A 1 10  ? -5.023  -10.839 40.611 1.00 105.27 ?  2   ARG A NH1 1 
ATOM   39   N  NH2 . ARG A 1 10  ? -3.277  -12.284 40.935 1.00 104.14 ?  2   ARG A NH2 1 
ATOM   40   N  N   . SER A 1 11  ? -2.838  -5.453  44.012 1.00 67.11  ?  3   SER A N   1 
ATOM   41   C  CA  . SER A 1 11  ? -2.543  -4.673  42.819 1.00 66.46  ?  3   SER A CA  1 
ATOM   42   C  C   . SER A 1 11  ? -2.858  -5.490  41.574 1.00 68.30  ?  3   SER A C   1 
ATOM   43   O  O   . SER A 1 11  ? -2.849  -6.724  41.591 1.00 72.68  ?  3   SER A O   1 
ATOM   44   C  CB  . SER A 1 11  ? -1.076  -4.252  42.825 1.00 59.63  ?  3   SER A CB  1 
ATOM   45   O  OG  . SER A 1 11  ? -0.247  -5.382  43.015 1.00 60.70  ?  3   SER A OG  1 
ATOM   46   N  N   . ASN A 1 12  ? -3.158  -4.791  40.483 1.00 59.56  ?  4   ASN A N   1 
ATOM   47   C  CA  . ASN A 1 12  ? -3.522  -5.460  39.245 1.00 64.93  ?  4   ASN A CA  1 
ATOM   48   C  C   . ASN A 1 12  ? -3.071  -4.624  38.061 1.00 61.08  ?  4   ASN A C   1 
ATOM   49   O  O   . ASN A 1 12  ? -2.784  -3.433  38.187 1.00 55.14  ?  4   ASN A O   1 
ATOM   50   C  CB  . ASN A 1 12  ? -5.030  -5.719  39.161 1.00 63.15  ?  4   ASN A CB  1 
ATOM   51   C  CG  . ASN A 1 12  ? -5.449  -6.946  39.938 1.00 64.25  ?  4   ASN A CG  1 
ATOM   52   O  OD1 . ASN A 1 12  ? -5.183  -8.074  39.529 1.00 63.07  ?  4   ASN A OD1 1 
ATOM   53   N  ND2 . ASN A 1 12  ? -6.112  -6.730  41.068 1.00 76.08  ?  4   ASN A ND2 1 
ATOM   54   N  N   . TYR A 1 13  ? -3.006  -5.272  36.904 1.00 53.89  ?  5   TYR A N   1 
ATOM   55   C  CA  . TYR A 1 13  ? -2.526  -4.648  35.680 1.00 53.93  ?  5   TYR A CA  1 
ATOM   56   C  C   . TYR A 1 13  ? -3.665  -4.649  34.673 1.00 55.75  ?  5   TYR A C   1 
ATOM   57   O  O   . TYR A 1 13  ? -4.159  -5.714  34.291 1.00 54.89  ?  5   TYR A O   1 
ATOM   58   C  CB  . TYR A 1 13  ? -1.308  -5.386  35.133 1.00 58.21  ?  5   TYR A CB  1 
ATOM   59   C  CG  . TYR A 1 13  ? -0.771  -4.815  33.844 1.00 65.23  ?  5   TYR A CG  1 
ATOM   60   C  CD1 . TYR A 1 13  ? -0.912  -3.467  33.535 1.00 64.97  ?  5   TYR A CD1 1 
ATOM   61   C  CD2 . TYR A 1 13  ? -0.129  -5.632  32.925 1.00 64.43  ?  5   TYR A CD2 1 
ATOM   62   C  CE1 . TYR A 1 13  ? -0.420  -2.950  32.348 1.00 67.02  ?  5   TYR A CE1 1 
ATOM   63   C  CE2 . TYR A 1 13  ? 0.364   -5.126  31.737 1.00 69.32  ?  5   TYR A CE2 1 
ATOM   64   C  CZ  . TYR A 1 13  ? 0.215   -3.787  31.452 1.00 77.39  ?  5   TYR A CZ  1 
ATOM   65   O  OH  . TYR A 1 13  ? 0.710   -3.288  30.267 1.00 89.36  ?  5   TYR A OH  1 
ATOM   66   N  N   . ILE A 1 14  ? -4.072  -3.459  34.246 1.00 50.06  ?  6   ILE A N   1 
ATOM   67   C  CA  . ILE A 1 14  ? -5.222  -3.283  33.369 1.00 50.77  ?  6   ILE A CA  1 
ATOM   68   C  C   . ILE A 1 14  ? -4.764  -2.543  32.128 1.00 57.54  ?  6   ILE A C   1 
ATOM   69   O  O   . ILE A 1 14  ? -4.120  -1.494  32.226 1.00 54.18  ?  6   ILE A O   1 
ATOM   70   C  CB  . ILE A 1 14  ? -6.361  -2.521  34.071 1.00 55.31  ?  6   ILE A CB  1 
ATOM   71   C  CG1 . ILE A 1 14  ? -6.759  -3.271  35.339 1.00 52.25  ?  6   ILE A CG1 1 
ATOM   72   C  CG2 . ILE A 1 14  ? -7.545  -2.345  33.136 1.00 54.05  ?  6   ILE A CG2 1 
ATOM   73   C  CD1 . ILE A 1 14  ? -7.874  -2.621  36.082 1.00 52.19  ?  6   ILE A CD1 1 
ATOM   74   N  N   . VAL A 1 15  ? -5.112  -3.080  30.971 1.00 60.29  ?  7   VAL A N   1 
ATOM   75   C  CA  . VAL A 1 15  ? -4.677  -2.541  29.693 1.00 59.85  ?  7   VAL A CA  1 
ATOM   76   C  C   . VAL A 1 15  ? -5.891  -2.008  28.958 1.00 57.50  ?  7   VAL A C   1 
ATOM   77   O  O   . VAL A 1 15  ? -7.007  -2.506  29.114 1.00 58.99  ?  7   VAL A O   1 
ATOM   78   C  CB  . VAL A 1 15  ? -3.947  -3.618  28.864 1.00 68.62  ?  7   VAL A CB  1 
ATOM   79   C  CG1 . VAL A 1 15  ? -3.717  -3.133  27.451 1.00 76.76  ?  7   VAL A CG1 1 
ATOM   80   C  CG2 . VAL A 1 15  ? -2.639  -3.983  29.540 1.00 72.69  ?  7   VAL A CG2 1 
ATOM   81   N  N   . ILE A 1 16  ? -5.667  -0.976  28.156 1.00 63.96  ?  8   ILE A N   1 
ATOM   82   C  CA  . ILE A 1 16  ? -6.707  -0.359  27.344 1.00 66.30  ?  8   ILE A CA  1 
ATOM   83   C  C   . ILE A 1 16  ? -6.242  -0.434  25.899 1.00 68.15  ?  8   ILE A C   1 
ATOM   84   O  O   . ILE A 1 16  ? -5.341  0.310   25.488 1.00 65.78  ?  8   ILE A O   1 
ATOM   85   C  CB  . ILE A 1 16  ? -6.984  1.088   27.772 1.00 71.74  ?  8   ILE A CB  1 
ATOM   86   C  CG1 . ILE A 1 16  ? -7.809  1.103   29.063 1.00 76.06  ?  8   ILE A CG1 1 
ATOM   87   C  CG2 . ILE A 1 16  ? -7.703  1.854   26.678 1.00 70.77  ?  8   ILE A CG2 1 
ATOM   88   C  CD1 . ILE A 1 16  ? -6.990  1.316   30.304 1.00 68.65  ?  8   ILE A CD1 1 
ATOM   89   N  N   . GLU A 1 17  ? -6.837  -1.345  25.138 1.00 65.85  ?  9   GLU A N   1 
ATOM   90   C  CA  . GLU A 1 17  ? -6.526  -1.550  23.734 1.00 68.09  ?  9   GLU A CA  1 
ATOM   91   C  C   . GLU A 1 17  ? -7.659  -1.008  22.875 1.00 59.48  ?  9   GLU A C   1 
ATOM   92   O  O   . GLU A 1 17  ? -8.787  -0.839  23.340 1.00 62.59  ?  9   GLU A O   1 
ATOM   93   C  CB  . GLU A 1 17  ? -6.322  -3.034  23.422 1.00 68.33  ?  9   GLU A CB  1 
ATOM   94   C  CG  . GLU A 1 17  ? -4.972  -3.590  23.806 1.00 74.17  ?  9   GLU A CG  1 
ATOM   95   C  CD  . GLU A 1 17  ? -4.834  -5.045  23.410 1.00 84.73  ?  9   GLU A CD  1 
ATOM   96   O  OE1 . GLU A 1 17  ? -5.873  -5.738  23.360 1.00 80.94  ?  9   GLU A OE1 1 
ATOM   97   O  OE2 . GLU A 1 17  ? -3.700  -5.490  23.136 1.00 94.20  ?  9   GLU A OE2 1 
ATOM   98   N  N   . GLY A 1 18  ? -7.354  -0.746  21.617 1.00 65.53  ?  10  GLY A N   1 
ATOM   99   C  CA  . GLY A 1 18  ? -8.391  -0.333  20.700 1.00 72.53  ?  10  GLY A CA  1 
ATOM   100  C  C   . GLY A 1 18  ? -7.821  0.330   19.474 1.00 68.38  ?  10  GLY A C   1 
ATOM   101  O  O   . GLY A 1 18  ? -6.720  0.888   19.475 1.00 72.93  ?  10  GLY A O   1 
ATOM   102  N  N   . LEU A 1 19  ? -8.607  0.272   18.405 1.00 76.42  ?  11  LEU A N   1 
ATOM   103  C  CA  . LEU A 1 19  ? -8.231  0.863   17.133 1.00 75.94  ?  11  LEU A CA  1 
ATOM   104  C  C   . LEU A 1 19  ? -8.370  2.380   17.181 1.00 74.78  ?  11  LEU A C   1 
ATOM   105  O  O   . LEU A 1 19  ? -9.080  2.947   18.019 1.00 82.49  ?  11  LEU A O   1 
ATOM   106  C  CB  . LEU A 1 19  ? -9.102  0.286   16.012 1.00 75.93  ?  11  LEU A CB  1 
ATOM   107  C  CG  . LEU A 1 19  ? -8.861  -1.198  15.736 1.00 78.34  ?  11  LEU A CG  1 
ATOM   108  C  CD1 . LEU A 1 19  ? -10.095 -1.869  15.160 1.00 83.07  ?  11  LEU A CD1 1 
ATOM   109  C  CD2 . LEU A 1 19  ? -7.672  -1.353  14.788 1.00 78.22  ?  11  LEU A CD2 1 
ATOM   110  N  N   . GLU A 1 20  ? -7.684  3.037   16.246 1.00 77.49  ?  12  GLU A N   1 
ATOM   111  C  CA  . GLU A 1 20  ? -7.602  4.489   16.248 1.00 85.79  ?  12  GLU A CA  1 
ATOM   112  C  C   . GLU A 1 20  ? -8.992  5.107   16.325 1.00 89.94  ?  12  GLU A C   1 
ATOM   113  O  O   . GLU A 1 20  ? -9.935  4.646   15.676 1.00 92.06  ?  12  GLU A O   1 
ATOM   114  C  CB  . GLU A 1 20  ? -6.883  4.975   14.988 1.00 89.61  ?  12  GLU A CB  1 
ATOM   115  N  N   . GLY A 1 21  ? -9.112  6.156   17.132 1.00 103.13 ?  13  GLY A N   1 
ATOM   116  C  CA  . GLY A 1 21  ? -10.383 6.819   17.305 1.00 100.71 ?  13  GLY A CA  1 
ATOM   117  C  C   . GLY A 1 21  ? -11.326 6.131   18.257 1.00 101.87 ?  13  GLY A C   1 
ATOM   118  O  O   . GLY A 1 21  ? -12.516 6.465   18.276 1.00 95.30  ?  13  GLY A O   1 
ATOM   119  N  N   . ALA A 1 22  ? -10.839 5.163   19.028 1.00 91.62  ?  14  ALA A N   1 
ATOM   120  C  CA  . ALA A 1 22  ? -11.634 4.550   20.079 1.00 85.73  ?  14  ALA A CA  1 
ATOM   121  C  C   . ALA A 1 22  ? -11.706 5.409   21.331 1.00 81.98  ?  14  ALA A C   1 
ATOM   122  O  O   . ALA A 1 22  ? -12.478 5.085   22.239 1.00 77.04  ?  14  ALA A O   1 
ATOM   123  C  CB  . ALA A 1 22  ? -11.055 3.178   20.443 1.00 81.14  ?  14  ALA A CB  1 
ATOM   124  N  N   . GLY A 1 23  ? -10.936 6.490   21.398 1.00 88.62  ?  15  GLY A N   1 
ATOM   125  C  CA  . GLY A 1 23  ? -10.849 7.268   22.612 1.00 82.94  ?  15  GLY A CA  1 
ATOM   126  C  C   . GLY A 1 23  ? -10.261 6.438   23.732 1.00 70.15  ?  15  GLY A C   1 
ATOM   127  O  O   . GLY A 1 23  ? -10.922 6.187   24.744 1.00 65.02  ?  15  GLY A O   1 
ATOM   128  N  N   . LYS A 1 24  ? -9.027  5.967   23.540 1.00 73.21  ?  16  LYS A N   1 
ATOM   129  C  CA  . LYS A 1 24  ? -8.382  5.153   24.563 1.00 74.66  ?  16  LYS A CA  1 
ATOM   130  C  C   . LYS A 1 24  ? -7.959  5.998   25.757 1.00 71.17  ?  16  LYS A C   1 
ATOM   131  O  O   . LYS A 1 24  ? -8.168  5.601   26.907 1.00 65.27  ?  16  LYS A O   1 
ATOM   132  C  CB  . LYS A 1 24  ? -7.178  4.421   23.972 1.00 73.84  ?  16  LYS A CB  1 
ATOM   133  C  CG  . LYS A 1 24  ? -7.548  3.217   23.117 1.00 74.57  ?  16  LYS A CG  1 
ATOM   134  C  CD  . LYS A 1 24  ? -6.325  2.550   22.500 1.00 74.90  ?  16  LYS A CD  1 
ATOM   135  C  CE  . LYS A 1 24  ? -5.725  3.403   21.392 1.00 80.42  ?  16  LYS A CE  1 
ATOM   136  N  NZ  . LYS A 1 24  ? -6.736  3.766   20.356 1.00 79.89  ?  16  LYS A NZ  1 
ATOM   137  N  N   . THR A 1 25  ? -7.354  7.161   25.507 1.00 78.72  ?  17  THR A N   1 
ATOM   138  C  CA  . THR A 1 25  ? -6.924  8.015   26.608 1.00 82.48  ?  17  THR A CA  1 
ATOM   139  C  C   . THR A 1 25  ? -8.118  8.490   27.428 1.00 80.29  ?  17  THR A C   1 
ATOM   140  O  O   . THR A 1 25  ? -8.046  8.554   28.663 1.00 74.21  ?  17  THR A O   1 
ATOM   141  C  CB  . THR A 1 25  ? -6.123  9.200   26.069 1.00 84.35  ?  17  THR A CB  1 
ATOM   142  O  OG1 . THR A 1 25  ? -6.881  9.876   25.059 1.00 92.23  ?  17  THR A OG1 1 
ATOM   143  C  CG2 . THR A 1 25  ? -4.795  8.727   25.473 1.00 78.15  ?  17  THR A CG2 1 
ATOM   144  N  N   . THR A 1 26  ? -9.232  8.824   26.761 1.00 74.27  ?  18  THR A N   1 
ATOM   145  C  CA  . THR A 1 26  ? -10.433 9.217   27.490 1.00 72.62  ?  18  THR A CA  1 
ATOM   146  C  C   . THR A 1 26  ? -11.054 8.039   28.232 1.00 67.58  ?  18  THR A C   1 
ATOM   147  O  O   . THR A 1 26  ? -11.600 8.216   29.327 1.00 66.15  ?  18  THR A O   1 
ATOM   148  C  CB  . THR A 1 26  ? -11.455 9.862   26.546 1.00 72.16  ?  18  THR A CB  1 
ATOM   149  O  OG1 . THR A 1 26  ? -12.770 9.756   27.111 1.00 61.94  ?  18  THR A OG1 1 
ATOM   150  C  CG2 . THR A 1 26  ? -11.458 9.225   25.159 1.00 77.14  ?  18  THR A CG2 1 
ATOM   151  N  N   . ALA A 1 27  ? -10.982 6.833   27.661 1.00 65.44  ?  19  ALA A N   1 
ATOM   152  C  CA  . ALA A 1 27  ? -11.465 5.657   28.376 1.00 62.07  ?  19  ALA A CA  1 
ATOM   153  C  C   . ALA A 1 27  ? -10.589 5.334   29.580 1.00 68.64  ?  19  ALA A C   1 
ATOM   154  O  O   . ALA A 1 27  ? -11.097 4.861   30.604 1.00 71.09  ?  19  ALA A O   1 
ATOM   155  C  CB  . ALA A 1 27  ? -11.529 4.452   27.438 1.00 63.58  ?  19  ALA A CB  1 
ATOM   156  N  N   . ARG A 1 28  ? -9.276  5.564   29.469 1.00 69.72  ?  20  ARG A N   1 
ATOM   157  C  CA  . ARG A 1 28  ? -8.401  5.358   30.618 1.00 66.30  ?  20  ARG A CA  1 
ATOM   158  C  C   . ARG A 1 28  ? -8.888  6.173   31.808 1.00 65.17  ?  20  ARG A C   1 
ATOM   159  O  O   . ARG A 1 28  ? -8.943  5.666   32.937 1.00 63.14  ?  20  ARG A O   1 
ATOM   160  C  CB  . ARG A 1 28  ? -6.961  5.728   30.257 1.00 69.27  ?  20  ARG A CB  1 
ATOM   161  C  CG  . ARG A 1 28  ? -5.884  5.204   31.217 1.00 71.55  ?  20  ARG A CG  1 
ATOM   162  C  CD  . ARG A 1 28  ? -5.628  6.137   32.406 1.00 66.99  ?  20  ARG A CD  1 
ATOM   163  N  NE  . ARG A 1 28  ? -5.504  7.528   31.987 1.00 71.54  ?  20  ARG A NE  1 
ATOM   164  C  CZ  . ARG A 1 28  ? -4.496  8.018   31.280 1.00 68.74  ?  20  ARG A CZ  1 
ATOM   165  N  NH1 . ARG A 1 28  ? -3.471  7.261   30.922 1.00 64.02  ?  20  ARG A NH1 1 
ATOM   166  N  NH2 . ARG A 1 28  ? -4.525  9.294   30.905 1.00 72.32  ?  20  ARG A NH2 1 
ATOM   167  N  N   . GLU A 1 29  ? -9.286  7.429   31.566 1.00 70.34  ?  21  GLU A N   1 
ATOM   168  C  CA  . GLU A 1 29  ? -9.797  8.255   32.653 1.00 71.21  ?  21  GLU A CA  1 
ATOM   169  C  C   . GLU A 1 29  ? -10.990 7.587   33.328 1.00 70.22  ?  21  GLU A C   1 
ATOM   170  O  O   . GLU A 1 29  ? -11.095 7.578   34.560 1.00 73.68  ?  21  GLU A O   1 
ATOM   171  C  CB  . GLU A 1 29  ? -10.213 9.638   32.146 1.00 73.77  ?  21  GLU A CB  1 
ATOM   172  C  CG  . GLU A 1 29  ? -9.340  10.258  31.067 1.00 80.55  ?  21  GLU A CG  1 
ATOM   173  C  CD  . GLU A 1 29  ? -7.896  10.436  31.479 1.00 79.45  ?  21  GLU A CD  1 
ATOM   174  O  OE1 . GLU A 1 29  ? -7.359  9.564   32.177 1.00 75.93  ?  21  GLU A OE1 1 
ATOM   175  O  OE2 . GLU A 1 29  ? -7.294  11.457  31.092 1.00 85.55  ?  21  GLU A OE2 1 
ATOM   176  N  N   . CYS A 1 30  ? -11.912 7.039   32.530 1.00 66.51  ?  22  CYS A N   1 
ATOM   177  C  CA  . CYS A 1 30  ? -13.098 6.407   33.098 1.00 70.90  ?  22  CYS A CA  1 
ATOM   178  C  C   . CYS A 1 30  ? -12.729 5.190   33.934 1.00 68.30  ?  22  CYS A C   1 
ATOM   179  O  O   . CYS A 1 30  ? -13.302 4.968   35.007 1.00 68.82  ?  22  CYS A O   1 
ATOM   180  C  CB  . CYS A 1 30  ? -14.068 6.022   31.982 1.00 68.57  ?  22  CYS A CB  1 
ATOM   181  S  SG  . CYS A 1 30  ? -14.924 7.439   31.266 1.00 69.37  ?  22  CYS A SG  1 
ATOM   182  N  N   . VAL A 1 31  ? -11.780 4.386   33.457 1.00 66.12  ?  23  VAL A N   1 
ATOM   183  C  CA  . VAL A 1 31  ? -11.324 3.241   34.236 1.00 67.03  ?  23  VAL A CA  1 
ATOM   184  C  C   . VAL A 1 31  ? -10.770 3.703   35.576 1.00 66.26  ?  23  VAL A C   1 
ATOM   185  O  O   . VAL A 1 31  ? -11.012 3.082   36.616 1.00 63.15  ?  23  VAL A O   1 
ATOM   186  C  CB  . VAL A 1 31  ? -10.280 2.436   33.440 1.00 62.37  ?  23  VAL A CB  1 
ATOM   187  C  CG1 . VAL A 1 31  ? -9.707  1.322   34.297 1.00 62.29  ?  23  VAL A CG1 1 
ATOM   188  C  CG2 . VAL A 1 31  ? -10.895 1.876   32.168 1.00 66.82  ?  23  VAL A CG2 1 
ATOM   189  N  N   . VAL A 1 32  ? -10.011 4.797   35.570 1.00 69.39  ?  24  VAL A N   1 
ATOM   190  C  CA  . VAL A 1 32  ? -9.429  5.297   36.810 1.00 65.93  ?  24  VAL A CA  1 
ATOM   191  C  C   . VAL A 1 32  ? -10.520 5.768   37.760 1.00 67.14  ?  24  VAL A C   1 
ATOM   192  O  O   . VAL A 1 32  ? -10.475 5.485   38.962 1.00 69.99  ?  24  VAL A O   1 
ATOM   193  C  CB  . VAL A 1 32  ? -8.413  6.410   36.494 1.00 61.82  ?  24  VAL A CB  1 
ATOM   194  C  CG1 . VAL A 1 32  ? -7.899  7.071   37.753 1.00 74.31  ?  24  VAL A CG1 1 
ATOM   195  C  CG2 . VAL A 1 32  ? -7.250  5.823   35.708 1.00 64.26  ?  24  VAL A CG2 1 
ATOM   196  N  N   . GLU A 1 33  ? -11.515 6.495   37.247 1.00 67.61  ?  25  GLU A N   1 
ATOM   197  C  CA  . GLU A 1 33  ? -12.563 7.005   38.125 1.00 70.92  ?  25  GLU A CA  1 
ATOM   198  C  C   . GLU A 1 33  ? -13.333 5.868   38.778 1.00 67.81  ?  25  GLU A C   1 
ATOM   199  O  O   . GLU A 1 33  ? -13.627 5.914   39.980 1.00 70.86  ?  25  GLU A O   1 
ATOM   200  C  CB  . GLU A 1 33  ? -13.509 7.914   37.344 1.00 76.78  ?  25  GLU A CB  1 
ATOM   201  C  CG  . GLU A 1 33  ? -12.924 9.276   37.040 1.00 80.54  ?  25  GLU A CG  1 
ATOM   202  C  CD  . GLU A 1 33  ? -13.880 10.151  36.260 1.00 108.58 ?  25  GLU A CD  1 
ATOM   203  O  OE1 . GLU A 1 33  ? -15.096 10.097  36.536 1.00 119.87 ?  25  GLU A OE1 1 
ATOM   204  O  OE2 . GLU A 1 33  ? -13.416 10.884  35.362 1.00 111.09 ?  25  GLU A OE2 1 
ATOM   205  N  N   . THR A 1 34  ? -13.667 4.837   38.003 1.00 61.48  ?  26  THR A N   1 
ATOM   206  C  CA  . THR A 1 34  ? -14.344 3.681   38.574 1.00 61.54  ?  26  THR A CA  1 
ATOM   207  C  C   . THR A 1 34  ? -13.476 3.015   39.634 1.00 65.39  ?  26  THR A C   1 
ATOM   208  O  O   . THR A 1 34  ? -13.950 2.705   40.734 1.00 70.14  ?  26  THR A O   1 
ATOM   209  C  CB  . THR A 1 34  ? -14.710 2.703   37.460 1.00 72.24  ?  26  THR A CB  1 
ATOM   210  O  OG1 . THR A 1 34  ? -13.519 2.267   36.795 1.00 76.34  ?  26  THR A OG1 1 
ATOM   211  C  CG2 . THR A 1 34  ? -15.633 3.375   36.442 1.00 78.70  ?  26  THR A CG2 1 
ATOM   212  N  N   . LEU A 1 35  ? -12.191 2.817   39.334 1.00 65.59  ?  27  LEU A N   1 
ATOM   213  C  CA  . LEU A 1 35  ? -11.298 2.217   40.320 1.00 64.81  ?  27  LEU A CA  1 
ATOM   214  C  C   . LEU A 1 35  ? -11.212 3.062   41.583 1.00 70.49  ?  27  LEU A C   1 
ATOM   215  O  O   . LEU A 1 35  ? -11.063 2.518   42.684 1.00 63.78  ?  27  LEU A O   1 
ATOM   216  C  CB  . LEU A 1 35  ? -9.917  2.010   39.710 1.00 62.31  ?  27  LEU A CB  1 
ATOM   217  C  CG  . LEU A 1 35  ? -9.859  0.949   38.611 1.00 64.53  ?  27  LEU A CG  1 
ATOM   218  C  CD1 . LEU A 1 35  ? -8.427  0.821   38.103 1.00 61.52  ?  27  LEU A CD1 1 
ATOM   219  C  CD2 . LEU A 1 35  ? -10.375 -0.397  39.096 1.00 61.28  ?  27  LEU A CD2 1 
ATOM   220  N  N   . LYS A 1 36  ? -11.301 4.386   41.452 1.00 68.33  ?  28  LYS A N   1 
ATOM   221  C  CA  . LYS A 1 36  ? -11.370 5.226   42.643 1.00 66.60  ?  28  LYS A CA  1 
ATOM   222  C  C   . LYS A 1 36  ? -12.634 4.939   43.445 1.00 69.53  ?  28  LYS A C   1 
ATOM   223  O  O   . LYS A 1 36  ? -12.583 4.814   44.675 1.00 67.86  ?  28  LYS A O   1 
ATOM   224  C  CB  . LYS A 1 36  ? -11.316 6.697   42.249 1.00 65.91  ?  28  LYS A CB  1 
ATOM   225  C  CG  . LYS A 1 36  ? -10.009 7.138   41.631 1.00 66.38  ?  28  LYS A CG  1 
ATOM   226  C  CD  . LYS A 1 36  ? -10.233 8.470   40.935 1.00 75.39  ?  28  LYS A CD  1 
ATOM   227  C  CE  . LYS A 1 36  ? -8.958  9.071   40.355 1.00 76.17  ?  28  LYS A CE  1 
ATOM   228  N  NZ  . LYS A 1 36  ? -7.764  8.961   41.239 1.00 79.57  ?  28  LYS A NZ  1 
ATOM   229  N  N   . GLN A 1 37  ? -13.781 4.826   42.762 1.00 71.25  ?  29  GLN A N   1 
ATOM   230  C  CA  . GLN A 1 37  ? -15.040 4.556   43.449 1.00 70.17  ?  29  GLN A CA  1 
ATOM   231  C  C   . GLN A 1 37  ? -15.018 3.224   44.188 1.00 70.72  ?  29  GLN A C   1 
ATOM   232  O  O   . GLN A 1 37  ? -15.790 3.037   45.135 1.00 78.64  ?  29  GLN A O   1 
ATOM   233  C  CB  . GLN A 1 37  ? -16.212 4.556   42.458 1.00 80.16  ?  29  GLN A CB  1 
ATOM   234  C  CG  . GLN A 1 37  ? -16.664 5.929   41.959 1.00 87.57  ?  29  GLN A CG  1 
ATOM   235  C  CD  . GLN A 1 37  ? -17.311 6.780   43.042 1.00 96.33  ?  29  GLN A CD  1 
ATOM   236  O  OE1 . GLN A 1 37  ? -17.008 7.967   43.171 1.00 102.31 ?  29  GLN A OE1 1 
ATOM   237  N  NE2 . GLN A 1 37  ? -18.211 6.182   43.816 1.00 99.62  ?  29  GLN A NE2 1 
ATOM   238  N  N   . LEU A 1 38  ? -14.169 2.293   43.769 1.00 67.70  ?  30  LEU A N   1 
ATOM   239  C  CA  . LEU A 1 38  ? -14.094 0.975   44.380 1.00 68.40  ?  30  LEU A CA  1 
ATOM   240  C  C   . LEU A 1 38  ? -13.037 0.896   45.468 1.00 71.52  ?  30  LEU A C   1 
ATOM   241  O  O   . LEU A 1 38  ? -12.766 -0.197  45.976 1.00 71.94  ?  30  LEU A O   1 
ATOM   242  C  CB  . LEU A 1 38  ? -13.815 -0.076  43.310 1.00 69.14  ?  30  LEU A CB  1 
ATOM   243  C  CG  . LEU A 1 38  ? -14.956 -0.236  42.309 1.00 68.60  ?  30  LEU A CG  1 
ATOM   244  C  CD1 . LEU A 1 38  ? -14.460 -1.007  41.104 1.00 68.92  ?  30  LEU A CD1 1 
ATOM   245  C  CD2 . LEU A 1 38  ? -16.141 -0.934  42.948 1.00 70.99  ?  30  LEU A CD2 1 
ATOM   246  N  N   . GLY A 1 39  ? -12.440 2.025   45.835 1.00 70.04  ?  31  GLY A N   1 
ATOM   247  C  CA  . GLY A 1 39  ? -11.460 2.057   46.892 1.00 77.50  ?  31  GLY A CA  1 
ATOM   248  C  C   . GLY A 1 39  ? -10.034 1.832   46.453 1.00 74.03  ?  31  GLY A C   1 
ATOM   249  O  O   . GLY A 1 39  ? -9.156  1.685   47.313 1.00 78.57  ?  31  GLY A O   1 
ATOM   250  N  N   . VAL A 1 40  ? -9.780  1.779   45.150 1.00 78.10  ?  32  VAL A N   1 
ATOM   251  C  CA  . VAL A 1 40  ? -8.423  1.699   44.624 1.00 73.09  ?  32  VAL A CA  1 
ATOM   252  C  C   . VAL A 1 40  ? -7.859  3.113   44.595 1.00 71.87  ?  32  VAL A C   1 
ATOM   253  O  O   . VAL A 1 40  ? -8.429  4.008   43.961 1.00 75.53  ?  32  VAL A O   1 
ATOM   254  C  CB  . VAL A 1 40  ? -8.410  1.058   43.229 1.00 72.27  ?  32  VAL A CB  1 
ATOM   255  C  CG1 . VAL A 1 40  ? -6.981  0.889   42.730 1.00 70.26  ?  32  VAL A CG1 1 
ATOM   256  C  CG2 . VAL A 1 40  ? -9.139  -0.283  43.258 1.00 66.41  ?  32  VAL A CG2 1 
ATOM   257  N  N   . SER A 1 41  ? -6.741  3.317   45.283 1.00 70.77  ?  33  SER A N   1 
ATOM   258  C  CA  . SER A 1 41  ? -6.202  4.649   45.508 1.00 73.81  ?  33  SER A CA  1 
ATOM   259  C  C   . SER A 1 41  ? -4.798  4.850   44.963 1.00 70.54  ?  33  SER A C   1 
ATOM   260  O  O   . SER A 1 41  ? -4.456  5.976   44.594 1.00 71.88  ?  33  SER A O   1 
ATOM   261  C  CB  . SER A 1 41  ? -6.198  4.964   47.014 1.00 77.88  ?  33  SER A CB  1 
ATOM   262  O  OG  . SER A 1 41  ? -7.518  5.084   47.517 1.00 83.40  ?  33  SER A OG  1 
ATOM   263  N  N   . ASP A 1 42  ? -3.983  3.802   44.894 1.00 68.08  ?  34  ASP A N   1 
ATOM   264  C  CA  . ASP A 1 42  ? -2.589  3.906   44.482 1.00 69.16  ?  34  ASP A CA  1 
ATOM   265  C  C   . ASP A 1 42  ? -2.405  3.183   43.155 1.00 67.06  ?  34  ASP A C   1 
ATOM   266  O  O   . ASP A 1 42  ? -2.667  1.979   43.063 1.00 63.58  ?  34  ASP A O   1 
ATOM   267  C  CB  . ASP A 1 42  ? -1.667  3.322   45.556 1.00 82.24  ?  34  ASP A CB  1 
ATOM   268  C  CG  . ASP A 1 42  ? -2.118  1.945   46.052 1.00 77.99  ?  34  ASP A CG  1 
ATOM   269  O  OD1 . ASP A 1 42  ? -3.111  1.393   45.536 1.00 69.49  ?  34  ASP A OD1 1 
ATOM   270  O  OD2 . ASP A 1 42  ? -1.464  1.410   46.971 1.00 89.15  ?  34  ASP A OD2 1 
ATOM   271  N  N   . MET A 1 43  ? -1.943  3.907   42.134 1.00 64.89  ?  35  MET A N   1 
ATOM   272  C  CA  . MET A 1 43  ? -1.840  3.314   40.808 1.00 60.35  ?  35  MET A CA  1 
ATOM   273  C  C   . MET A 1 43  ? -0.925  4.143   39.917 1.00 55.29  ?  35  MET A C   1 
ATOM   274  O  O   . MET A 1 43  ? -0.496  5.241   40.273 1.00 57.35  ?  35  MET A O   1 
ATOM   275  C  CB  . MET A 1 43  ? -3.232  3.164   40.177 1.00 60.33  ?  35  MET A CB  1 
ATOM   276  C  CG  . MET A 1 43  ? -3.976  4.476   39.987 1.00 60.85  ?  35  MET A CG  1 
ATOM   277  S  SD  . MET A 1 43  ? -5.632  4.218   39.318 1.00 62.85  ?  35  MET A SD  1 
ATOM   278  C  CE  . MET A 1 43  ? -6.575  3.935   40.820 1.00 69.30  ?  35  MET A CE  1 
ATOM   279  N  N   . VAL A 1 44  ? -0.634  3.582   38.744 1.00 54.18  ?  36  VAL A N   1 
ATOM   280  C  CA  . VAL A 1 44  ? 0.352   4.121   37.809 1.00 61.92  ?  36  VAL A CA  1 
ATOM   281  C  C   . VAL A 1 44  ? -0.224  4.058   36.403 1.00 53.21  ?  36  VAL A C   1 
ATOM   282  O  O   . VAL A 1 44  ? -0.721  3.009   35.983 1.00 52.56  ?  36  VAL A O   1 
ATOM   283  C  CB  . VAL A 1 44  ? 1.672   3.323   37.881 1.00 51.46  ?  36  VAL A CB  1 
ATOM   284  C  CG1 . VAL A 1 44  ? 2.622   3.745   36.778 1.00 59.78  ?  36  VAL A CG1 1 
ATOM   285  C  CG2 . VAL A 1 44  ? 2.316   3.487   39.245 1.00 61.83  ?  36  VAL A CG2 1 
ATOM   286  N  N   . PHE A 1 45  ? -0.155  5.172   35.667 1.00 53.48  ?  37  PHE A N   1 
ATOM   287  C  CA  . PHE A 1 45  ? -0.523  5.193   34.256 1.00 57.58  ?  37  PHE A CA  1 
ATOM   288  C  C   . PHE A 1 45  ? 0.751   5.081   33.422 1.00 57.38  ?  37  PHE A C   1 
ATOM   289  O  O   . PHE A 1 45  ? 1.638   5.937   33.525 1.00 58.81  ?  37  PHE A O   1 
ATOM   290  C  CB  . PHE A 1 45  ? -1.255  6.467   33.829 1.00 58.54  ?  37  PHE A CB  1 
ATOM   291  C  CG  . PHE A 1 45  ? -2.409  6.856   34.696 1.00 57.53  ?  37  PHE A CG  1 
ATOM   292  C  CD1 . PHE A 1 45  ? -2.952  5.982   35.620 1.00 57.96  ?  37  PHE A CD1 1 
ATOM   293  C  CD2 . PHE A 1 45  ? -2.958  8.121   34.575 1.00 59.83  ?  37  PHE A CD2 1 
ATOM   294  C  CE1 . PHE A 1 45  ? -4.011  6.371   36.415 1.00 62.42  ?  37  PHE A CE1 1 
ATOM   295  C  CE2 . PHE A 1 45  ? -4.016  8.514   35.361 1.00 62.28  ?  37  PHE A CE2 1 
ATOM   296  C  CZ  . PHE A 1 45  ? -4.543  7.640   36.283 1.00 63.34  ?  37  PHE A CZ  1 
ATOM   297  N  N   . THR A 1 46  ? 0.825   4.061   32.575 1.00 57.24  ?  38  THR A N   1 
ATOM   298  C  CA  . THR A 1 46  ? 1.945   3.876   31.664 1.00 67.94  ?  38  THR A CA  1 
ATOM   299  C  C   . THR A 1 46  ? 1.454   3.903   30.225 1.00 65.67  ?  38  THR A C   1 
ATOM   300  O  O   . THR A 1 46  ? 0.352   3.427   29.929 1.00 62.41  ?  38  THR A O   1 
ATOM   301  C  CB  . THR A 1 46  ? 2.661   2.553   31.930 1.00 67.60  ?  38  THR A CB  1 
ATOM   302  O  OG1 . THR A 1 46  ? 1.707   1.485   31.909 1.00 63.36  ?  38  THR A OG1 1 
ATOM   303  C  CG2 . THR A 1 46  ? 3.351   2.586   33.278 1.00 64.53  ?  38  THR A CG2 1 
ATOM   304  N  N   . ARG A 1 47  ? 2.270   4.466   29.339 1.00 78.03  ?  39  ARG A N   1 
ATOM   305  C  CA  . ARG A 1 47  ? 2.065   4.364   27.901 1.00 84.79  ?  39  ARG A CA  1 
ATOM   306  C  C   . ARG A 1 47  ? 2.965   3.247   27.385 1.00 92.28  ?  39  ARG A C   1 
ATOM   307  O  O   . ARG A 1 47  ? 4.188   3.308   27.548 1.00 91.55  ?  39  ARG A O   1 
ATOM   308  C  CB  . ARG A 1 47  ? 2.389   5.679   27.199 1.00 92.43  ?  39  ARG A CB  1 
ATOM   309  C  CG  . ARG A 1 47  ? 1.607   6.868   27.716 1.00 111.25 ?  39  ARG A CG  1 
ATOM   310  C  CD  . ARG A 1 47  ? 2.006   8.143   26.988 1.00 126.67 ?  39  ARG A CD  1 
ATOM   311  N  NE  . ARG A 1 47  ? 1.459   9.334   27.628 1.00 122.75 ?  39  ARG A NE  1 
ATOM   312  C  CZ  . ARG A 1 47  ? 1.680   10.575  27.218 1.00 123.52 ?  39  ARG A CZ  1 
ATOM   313  N  NH1 . ARG A 1 47  ? 2.425   10.830  26.155 1.00 138.78 ?  39  ARG A NH1 1 
ATOM   314  N  NH2 . ARG A 1 47  ? 1.143   11.587  27.893 1.00 121.02 ?  39  ARG A NH2 1 
ATOM   315  N  N   . GLU A 1 48  ? 2.367   2.234   26.772 1.00 117.61 ?  40  GLU A N   1 
ATOM   316  C  CA  . GLU A 1 48  ? 3.123   1.050   26.376 1.00 114.75 ?  40  GLU A CA  1 
ATOM   317  C  C   . GLU A 1 48  ? 3.974   1.384   25.155 1.00 119.32 ?  40  GLU A C   1 
ATOM   318  O  O   . GLU A 1 48  ? 5.137   0.967   25.091 1.00 125.88 ?  40  GLU A O   1 
ATOM   319  C  CB  . GLU A 1 48  ? 2.177   -0.122  26.124 1.00 118.71 ?  40  GLU A CB  1 
ATOM   320  C  CG  . GLU A 1 48  ? 1.093   -0.280  27.199 1.00 109.50 ?  40  GLU A CG  1 
ATOM   321  C  CD  . GLU A 1 48  ? 1.636   -0.712  28.552 1.00 102.73 ?  40  GLU A CD  1 
ATOM   322  O  OE1 . GLU A 1 48  ? 2.581   -1.523  28.586 1.00 116.48 ?  40  GLU A OE1 1 
ATOM   323  O  OE2 . GLU A 1 48  ? 1.108   -0.243  29.585 1.00 100.14 ?  40  GLU A OE2 1 
ATOM   324  N  N   . PRO A 1 49  ? 3.450   2.134   24.170 1.00 117.36 ?  41  PRO A N   1 
ATOM   325  C  CA  . PRO A 1 49  ? 4.348   2.753   23.179 1.00 135.12 ?  41  PRO A CA  1 
ATOM   326  C  C   . PRO A 1 49  ? 5.075   3.937   23.798 1.00 127.93 ?  41  PRO A C   1 
ATOM   327  O  O   . PRO A 1 49  ? 4.477   4.997   24.015 1.00 110.13 ?  41  PRO A O   1 
ATOM   328  C  CB  . PRO A 1 49  ? 3.406   3.191   22.046 1.00 124.53 ?  41  PRO A CB  1 
ATOM   329  C  CG  . PRO A 1 49  ? 2.094   2.513   22.322 1.00 115.82 ?  41  PRO A CG  1 
ATOM   330  C  CD  . PRO A 1 49  ? 2.031   2.319   23.811 1.00 97.75  ?  41  PRO A CD  1 
ATOM   331  N  N   . GLY A 1 50  ? 6.364   3.772   24.079 1.00 119.65 ?  42  GLY A N   1 
ATOM   332  C  CA  . GLY A 1 50  ? 7.066   4.684   24.958 1.00 109.06 ?  42  GLY A CA  1 
ATOM   333  C  C   . GLY A 1 50  ? 7.045   4.121   26.364 1.00 98.11  ?  42  GLY A C   1 
ATOM   334  O  O   . GLY A 1 50  ? 7.085   2.900   26.541 1.00 96.81  ?  42  GLY A O   1 
ATOM   335  N  N   . GLY A 1 51  ? 6.972   4.988   27.373 1.00 87.29  ?  43  GLY A N   1 
ATOM   336  C  CA  . GLY A 1 51  ? 6.764   4.566   28.741 1.00 83.35  ?  43  GLY A CA  1 
ATOM   337  C  C   . GLY A 1 51  ? 8.019   4.402   29.568 1.00 69.89  ?  43  GLY A C   1 
ATOM   338  O  O   . GLY A 1 51  ? 7.920   4.301   30.797 1.00 67.81  ?  43  GLY A O   1 
ATOM   339  N  N   . THR A 1 52  ? 9.185   4.354   28.935 1.00 69.14  ?  44  THR A N   1 
ATOM   340  C  CA  . THR A 1 52  ? 10.453  4.311   29.642 1.00 69.78  ?  44  THR A CA  1 
ATOM   341  C  C   . THR A 1 52  ? 11.413  5.243   28.918 1.00 70.23  ?  44  THR A C   1 
ATOM   342  O  O   . THR A 1 52  ? 11.201  5.600   27.756 1.00 73.06  ?  44  THR A O   1 
ATOM   343  C  CB  . THR A 1 52  ? 11.052  2.900   29.697 1.00 64.87  ?  44  THR A CB  1 
ATOM   344  O  OG1 . THR A 1 52  ? 11.177  2.386   28.365 1.00 69.91  ?  44  THR A OG1 1 
ATOM   345  C  CG2 . THR A 1 52  ? 10.194  1.967   30.540 1.00 61.38  ?  44  THR A CG2 1 
ATOM   346  N  N   . ILE A 1 53  ? 12.478  5.638   29.610 1.00 74.02  ?  45  ILE A N   1 
ATOM   347  C  CA  . ILE A 1 53  ? 13.513  6.413   28.938 1.00 74.39  ?  45  ILE A CA  1 
ATOM   348  C  C   . ILE A 1 53  ? 14.119  5.597   27.805 1.00 76.96  ?  45  ILE A C   1 
ATOM   349  O  O   . ILE A 1 53  ? 14.386  6.122   26.720 1.00 73.11  ?  45  ILE A O   1 
ATOM   350  C  CB  . ILE A 1 53  ? 14.577  6.893   29.943 1.00 82.17  ?  45  ILE A CB  1 
ATOM   351  C  CG1 . ILE A 1 53  ? 14.010  8.066   30.750 1.00 78.18  ?  45  ILE A CG1 1 
ATOM   352  C  CG2 . ILE A 1 53  ? 15.851  7.282   29.218 1.00 92.37  ?  45  ILE A CG2 1 
ATOM   353  C  CD1 . ILE A 1 53  ? 15.006  8.745   31.658 1.00 66.22  ?  45  ILE A CD1 1 
ATOM   354  N  N   . LEU A 1 54  ? 14.328  4.297   28.029 1.00 76.10  ?  46  LEU A N   1 
ATOM   355  C  CA  . LEU A 1 54  ? 14.860  3.443   26.972 1.00 70.71  ?  46  LEU A CA  1 
ATOM   356  C  C   . LEU A 1 54  ? 14.013  3.549   25.710 1.00 69.03  ?  46  LEU A C   1 
ATOM   357  O  O   . LEU A 1 54  ? 14.536  3.745   24.610 1.00 71.43  ?  46  LEU A O   1 
ATOM   358  C  CB  . LEU A 1 54  ? 14.925  1.987   27.437 1.00 63.78  ?  46  LEU A CB  1 
ATOM   359  C  CG  . LEU A 1 54  ? 15.285  0.972   26.349 1.00 68.59  ?  46  LEU A CG  1 
ATOM   360  C  CD1 . LEU A 1 54  ? 16.658  1.261   25.758 1.00 69.27  ?  46  LEU A CD1 1 
ATOM   361  C  CD2 . LEU A 1 54  ? 15.234  -0.451  26.891 1.00 59.52  ?  46  LEU A CD2 1 
ATOM   362  N  N   . ALA A 1 55  ? 12.694  3.413   25.853 1.00 70.27  ?  47  ALA A N   1 
ATOM   363  C  CA  . ALA A 1 55  ? 11.821  3.429   24.683 1.00 63.37  ?  47  ALA A CA  1 
ATOM   364  C  C   . ALA A 1 55  ? 11.859  4.786   23.991 1.00 68.30  ?  47  ALA A C   1 
ATOM   365  O  O   . ALA A 1 55  ? 11.793  4.873   22.761 1.00 72.82  ?  47  ALA A O   1 
ATOM   366  C  CB  . ALA A 1 55  ? 10.389  3.068   25.084 1.00 71.21  ?  47  ALA A CB  1 
ATOM   367  N  N   . GLU A 1 56  ? 11.938  5.866   24.773 1.00 68.71  ?  48  GLU A N   1 
ATOM   368  C  CA  . GLU A 1 56  ? 12.047  7.193   24.175 1.00 75.36  ?  48  GLU A CA  1 
ATOM   369  C  C   . GLU A 1 56  ? 13.342  7.333   23.382 1.00 76.02  ?  48  GLU A C   1 
ATOM   370  O  O   . GLU A 1 56  ? 13.342  7.878   22.272 1.00 70.00  ?  48  GLU A O   1 
ATOM   371  C  CB  . GLU A 1 56  ? 11.946  8.261   25.266 1.00 70.27  ?  48  GLU A CB  1 
ATOM   372  C  CG  . GLU A 1 56  ? 10.567  8.331   25.917 1.00 85.13  ?  48  GLU A CG  1 
ATOM   373  C  CD  . GLU A 1 56  ? 10.583  9.018   27.272 1.00 83.95  ?  48  GLU A CD  1 
ATOM   374  O  OE1 . GLU A 1 56  ? 11.533  9.784   27.541 1.00 81.50  ?  48  GLU A OE1 1 
ATOM   375  O  OE2 . GLU A 1 56  ? 9.650   8.782   28.070 1.00 74.12  ?  48  GLU A OE2 1 
ATOM   376  N  N   . LYS A 1 57  ? 14.456  6.834   23.929 1.00 78.42  ?  49  LYS A N   1 
ATOM   377  C  CA  . LYS A 1 57  ? 15.727  6.928   23.215 1.00 73.77  ?  49  LYS A CA  1 
ATOM   378  C  C   . LYS A 1 57  ? 15.745  6.040   21.975 1.00 68.56  ?  49  LYS A C   1 
ATOM   379  O  O   . LYS A 1 57  ? 16.368  6.399   20.971 1.00 70.50  ?  49  LYS A O   1 
ATOM   380  C  CB  . LYS A 1 57  ? 16.888  6.581   24.151 1.00 70.49  ?  49  LYS A CB  1 
ATOM   381  C  CG  . LYS A 1 57  ? 17.128  7.636   25.234 1.00 78.16  ?  49  LYS A CG  1 
ATOM   382  C  CD  . LYS A 1 57  ? 18.383  7.381   26.072 1.00 78.56  ?  49  LYS A CD  1 
ATOM   383  C  CE  . LYS A 1 57  ? 18.601  8.522   27.072 1.00 91.07  ?  49  LYS A CE  1 
ATOM   384  N  NZ  . LYS A 1 57  ? 19.547  8.198   28.181 1.00 104.14 ?  49  LYS A NZ  1 
ATOM   385  N  N   . LEU A 1 58  ? 15.075  4.885   22.016 1.00 67.12  ?  50  LEU A N   1 
ATOM   386  C  CA  . LEU A 1 58  ? 14.960  4.079   20.804 1.00 69.94  ?  50  LEU A CA  1 
ATOM   387  C  C   . LEU A 1 58  ? 14.165  4.819   19.734 1.00 69.00  ?  50  LEU A C   1 
ATOM   388  O  O   . LEU A 1 58  ? 14.483  4.738   18.542 1.00 71.21  ?  50  LEU A O   1 
ATOM   389  C  CB  . LEU A 1 58  ? 14.309  2.732   21.110 1.00 65.24  ?  50  LEU A CB  1 
ATOM   390  C  CG  . LEU A 1 58  ? 15.105  1.728   21.940 1.00 69.32  ?  50  LEU A CG  1 
ATOM   391  C  CD1 . LEU A 1 58  ? 14.232  0.519   22.243 1.00 62.92  ?  50  LEU A CD1 1 
ATOM   392  C  CD2 . LEU A 1 58  ? 16.369  1.297   21.228 1.00 70.96  ?  50  LEU A CD2 1 
ATOM   393  N  N   . ARG A 1 59  ? 13.113  5.536   20.138 1.00 70.22  ?  51  ARG A N   1 
ATOM   394  C  CA  . ARG A 1 59  ? 12.335  6.294   19.164 1.00 72.76  ?  51  ARG A CA  1 
ATOM   395  C  C   . ARG A 1 59  ? 13.172  7.400   18.530 1.00 70.41  ?  51  ARG A C   1 
ATOM   396  O  O   . ARG A 1 59  ? 13.106  7.620   17.315 1.00 78.86  ?  51  ARG A O   1 
ATOM   397  C  CB  . ARG A 1 59  ? 11.086  6.884   19.814 1.00 79.87  ?  51  ARG A CB  1 
ATOM   398  C  CG  . ARG A 1 59  ? 10.276  7.750   18.866 1.00 87.31  ?  51  ARG A CG  1 
ATOM   399  C  CD  . ARG A 1 59  ? 8.922   8.115   19.448 1.00 93.62  ?  51  ARG A CD  1 
ATOM   400  N  NE  . ARG A 1 59  ? 8.068   8.752   18.455 1.00 108.61 ?  51  ARG A NE  1 
ATOM   401  C  CZ  . ARG A 1 59  ? 7.922   10.063  18.315 1.00 108.42 ?  51  ARG A CZ  1 
ATOM   402  N  NH1 . ARG A 1 59  ? 8.545   10.918  19.110 1.00 114.81 ?  51  ARG A NH1 1 
ATOM   403  N  NH2 . ARG A 1 59  ? 7.129   10.527  17.354 1.00 109.74 ?  51  ARG A NH2 1 
ATOM   404  N  N   . SER A 1 60  ? 13.956  8.121   19.338 1.00 68.09  ?  52  SER A N   1 
ATOM   405  C  CA  . SER A 1 60  ? 14.804  9.166   18.776 1.00 77.44  ?  52  SER A CA  1 
ATOM   406  C  C   . SER A 1 60  ? 15.886  8.575   17.884 1.00 74.94  ?  52  SER A C   1 
ATOM   407  O  O   . SER A 1 60  ? 16.273  9.191   16.886 1.00 73.13  ?  52  SER A O   1 
ATOM   408  C  CB  . SER A 1 60  ? 15.439  9.999   19.888 1.00 73.00  ?  52  SER A CB  1 
ATOM   409  O  OG  . SER A 1 60  ? 16.508  9.303   20.502 1.00 75.38  ?  52  SER A OG  1 
ATOM   410  N  N   . LEU A 1 61  ? 16.400  7.395   18.240 1.00 73.37  ?  53  LEU A N   1 
ATOM   411  C  CA  . LEU A 1 61  ? 17.400  6.733   17.407 1.00 71.90  ?  53  LEU A CA  1 
ATOM   412  C  C   . LEU A 1 61  ? 16.833  6.378   16.041 1.00 75.75  ?  53  LEU A C   1 
ATOM   413  O  O   . LEU A 1 61  ? 17.479  6.613   15.013 1.00 79.57  ?  53  LEU A O   1 
ATOM   414  C  CB  . LEU A 1 61  ? 17.908  5.491   18.137 1.00 75.16  ?  53  LEU A CB  1 
ATOM   415  C  CG  . LEU A 1 61  ? 18.793  4.458   17.448 1.00 69.16  ?  53  LEU A CG  1 
ATOM   416  C  CD1 . LEU A 1 61  ? 19.750  3.849   18.471 1.00 70.22  ?  53  LEU A CD1 1 
ATOM   417  C  CD2 . LEU A 1 61  ? 17.946  3.380   16.802 1.00 70.56  ?  53  LEU A CD2 1 
ATOM   418  N  N   . VAL A 1 62  ? 15.616  5.832   16.011 1.00 74.12  ?  54  VAL A N   1 
ATOM   419  C  CA  . VAL A 1 62  ? 15.006  5.454   14.743 1.00 75.74  ?  54  VAL A CA  1 
ATOM   420  C  C   . VAL A 1 62  ? 14.714  6.687   13.901 1.00 77.22  ?  54  VAL A C   1 
ATOM   421  O  O   . VAL A 1 62  ? 14.846  6.663   12.672 1.00 76.13  ?  54  VAL A O   1 
ATOM   422  C  CB  . VAL A 1 62  ? 13.731  4.630   14.995 1.00 71.00  ?  54  VAL A CB  1 
ATOM   423  C  CG1 . VAL A 1 62  ? 12.854  4.632   13.759 1.00 68.10  ?  54  VAL A CG1 1 
ATOM   424  C  CG2 . VAL A 1 62  ? 14.094  3.215   15.385 1.00 63.97  ?  54  VAL A CG2 1 
ATOM   425  N  N   . LEU A 1 63  ? 14.278  7.772   14.539 1.00 78.17  ?  55  LEU A N   1 
ATOM   426  C  CA  . LEU A 1 63  ? 14.047  9.003   13.795 1.00 77.10  ?  55  LEU A CA  1 
ATOM   427  C  C   . LEU A 1 63  ? 15.357  9.634   13.341 1.00 79.33  ?  55  LEU A C   1 
ATOM   428  O  O   . LEU A 1 63  ? 15.408  10.241  12.264 1.00 86.48  ?  55  LEU A O   1 
ATOM   429  C  CB  . LEU A 1 63  ? 13.242  9.983   14.642 1.00 75.80  ?  55  LEU A CB  1 
ATOM   430  C  CG  . LEU A 1 63  ? 11.834  9.511   15.016 1.00 76.85  ?  55  LEU A CG  1 
ATOM   431  C  CD1 . LEU A 1 63  ? 11.084  10.644  15.708 1.00 100.98 ?  55  LEU A CD1 1 
ATOM   432  C  CD2 . LEU A 1 63  ? 11.057  9.014   13.807 1.00 71.93  ?  55  LEU A CD2 1 
ATOM   433  N  N   . ASP A 1 64  ? 16.423  9.510   14.142 1.00 75.40  ?  56  ASP A N   1 
ATOM   434  C  CA  . ASP A 1 64  ? 17.716  10.042  13.721 1.00 76.26  ?  56  ASP A CA  1 
ATOM   435  C  C   . ASP A 1 64  ? 18.245  9.308   12.498 1.00 84.53  ?  56  ASP A C   1 
ATOM   436  O  O   . ASP A 1 64  ? 18.927  9.905   11.657 1.00 78.65  ?  56  ASP A O   1 
ATOM   437  C  CB  . ASP A 1 64  ? 18.733  9.947   14.859 1.00 78.49  ?  56  ASP A CB  1 
ATOM   438  C  CG  . ASP A 1 64  ? 18.474  10.955  15.962 1.00 93.12  ?  56  ASP A CG  1 
ATOM   439  O  OD1 . ASP A 1 64  ? 17.929  12.040  15.666 1.00 95.98  ?  56  ASP A OD1 1 
ATOM   440  O  OD2 . ASP A 1 64  ? 18.821  10.663  17.127 1.00 90.65  ?  56  ASP A OD2 1 
ATOM   441  N  N   . ILE A 1 65  ? 17.958  8.013   12.397 1.00 85.77  ?  57  ILE A N   1 
ATOM   442  C  CA  . ILE A 1 65  ? 18.403  7.230   11.252 1.00 82.84  ?  57  ILE A CA  1 
ATOM   443  C  C   . ILE A 1 65  ? 17.548  7.520   10.028 1.00 88.85  ?  57  ILE A C   1 
ATOM   444  O  O   . ILE A 1 65  ? 18.073  7.706   8.924  1.00 95.78  ?  57  ILE A O   1 
ATOM   445  C  CB  . ILE A 1 65  ? 18.401  5.732   11.618 1.00 82.04  ?  57  ILE A CB  1 
ATOM   446  C  CG1 . ILE A 1 65  ? 19.621  5.429   12.491 1.00 78.77  ?  57  ILE A CG1 1 
ATOM   447  C  CG2 . ILE A 1 65  ? 18.358  4.872   10.373 1.00 84.82  ?  57  ILE A CG2 1 
ATOM   448  C  CD1 . ILE A 1 65  ? 19.751  3.988   12.881 1.00 67.27  ?  57  ILE A CD1 1 
ATOM   449  N  N   . GLN A 1 66  ? 16.224  7.565   10.198 1.00 83.02  ?  58  GLN A N   1 
ATOM   450  C  CA  . GLN A 1 66  ? 15.345  7.762   9.050  1.00 81.99  ?  58  GLN A CA  1 
ATOM   451  C  C   . GLN A 1 66  ? 15.542  9.137   8.421  1.00 89.42  ?  58  GLN A C   1 
ATOM   452  O  O   . GLN A 1 66  ? 15.462  9.280   7.196  1.00 98.62  ?  58  GLN A O   1 
ATOM   453  C  CB  . GLN A 1 66  ? 13.887  7.561   9.466  1.00 79.37  ?  58  GLN A CB  1 
ATOM   454  C  CG  . GLN A 1 66  ? 13.508  6.101   9.670  1.00 79.72  ?  58  GLN A CG  1 
ATOM   455  C  CD  . GLN A 1 66  ? 12.148  5.920   10.322 1.00 81.81  ?  58  GLN A CD  1 
ATOM   456  O  OE1 . GLN A 1 66  ? 11.498  6.888   10.718 1.00 79.45  ?  58  GLN A OE1 1 
ATOM   457  N  NE2 . GLN A 1 66  ? 11.715  4.669   10.441 1.00 77.44  ?  58  GLN A NE2 1 
ATOM   458  N  N   . SER A 1 67  ? 15.790  10.163  9.238  1.00 88.78  ?  59  SER A N   1 
ATOM   459  C  CA  . SER A 1 67  ? 15.991  11.500  8.687  1.00 95.41  ?  59  SER A CA  1 
ATOM   460  C  C   . SER A 1 67  ? 17.219  11.539  7.784  1.00 97.26  ?  59  SER A C   1 
ATOM   461  O  O   . SER A 1 67  ? 17.173  12.089  6.677  1.00 105.92 ?  59  SER A O   1 
ATOM   462  C  CB  . SER A 1 67  ? 16.117  12.527  9.815  1.00 89.13  ?  59  SER A CB  1 
ATOM   463  O  OG  . SER A 1 67  ? 17.421  12.529  10.366 1.00 97.21  ?  59  SER A OG  1 
ATOM   464  N  N   . THR A 1 68  ? 18.329  10.946  8.234  1.00 98.43  ?  60  THR A N   1 
ATOM   465  C  CA  . THR A 1 68  ? 19.531  10.928  7.405  1.00 102.42 ?  60  THR A CA  1 
ATOM   466  C  C   . THR A 1 68  ? 19.298  10.148  6.117  1.00 98.65  ?  60  THR A C   1 
ATOM   467  O  O   . THR A 1 68  ? 19.668  10.603  5.029  1.00 95.86  ?  60  THR A O   1 
ATOM   468  C  CB  . THR A 1 68  ? 20.712  10.321  8.173  1.00 104.01 ?  60  THR A CB  1 
ATOM   469  O  OG1 . THR A 1 68  ? 20.426  8.955   8.508  1.00 103.50 ?  60  THR A OG1 1 
ATOM   470  C  CG2 . THR A 1 68  ? 20.997  11.106  9.448  1.00 108.08 ?  60  THR A CG2 1 
ATOM   471  N  N   . GLY A 1 69  ? 18.671  8.980   6.219  1.00 102.64 ?  61  GLY A N   1 
ATOM   472  C  CA  . GLY A 1 69  ? 18.591  8.088   5.083  1.00 107.17 ?  61  GLY A CA  1 
ATOM   473  C  C   . GLY A 1 69  ? 19.821  7.205   4.994  1.00 109.07 ?  61  GLY A C   1 
ATOM   474  O  O   . GLY A 1 69  ? 20.573  7.027   5.964  1.00 107.71 ?  61  GLY A O   1 
ATOM   475  N  N   . ASP A 1 70  ? 20.030  6.620   3.825  1.00 127.22 ?  62  ASP A N   1 
ATOM   476  C  CA  . ASP A 1 70  ? 21.174  5.767   3.596  1.00 128.99 ?  62  ASP A CA  1 
ATOM   477  C  C   . ASP A 1 70  ? 21.073  4.487   4.412  1.00 121.84 ?  62  ASP A C   1 
ATOM   478  O  O   . ASP A 1 70  ? 21.991  3.648   4.351  1.00 118.15 ?  62  ASP A O   1 
ATOM   479  C  CB  . ASP A 1 70  ? 22.492  6.494   3.919  1.00 127.36 ?  62  ASP A CB  1 
ATOM   480  N  N   . GLU A 1 71  ? 20.018  4.307   5.196  1.00 110.55 ?  63  GLU A N   1 
ATOM   481  C  CA  . GLU A 1 71  ? 19.688  3.010   5.761  1.00 95.93  ?  63  GLU A CA  1 
ATOM   482  C  C   . GLU A 1 71  ? 18.196  2.979   6.070  1.00 87.39  ?  63  GLU A C   1 
ATOM   483  O  O   . GLU A 1 71  ? 17.610  3.992   6.461  1.00 99.52  ?  63  GLU A O   1 
ATOM   484  C  CB  . GLU A 1 71  ? 20.484  2.701   7.031  1.00 89.72  ?  63  GLU A CB  1 
ATOM   485  C  CG  . GLU A 1 71  ? 20.490  1.203   7.355  1.00 86.72  ?  63  GLU A CG  1 
ATOM   486  C  CD  . GLU A 1 71  ? 21.045  0.888   8.729  1.00 71.62  ?  63  GLU A CD  1 
ATOM   487  O  OE1 . GLU A 1 71  ? 20.747  1.642   9.675  1.00 80.48  ?  63  GLU A OE1 1 
ATOM   488  O  OE2 . GLU A 1 71  ? 21.778  -0.115  8.862  1.00 78.89  ?  63  GLU A OE2 1 
ATOM   489  N  N   . VAL A 1 72  ? 17.598  1.807   5.897  1.00 82.86  ?  64  VAL A N   1 
ATOM   490  C  CA  . VAL A 1 72  ? 16.181  1.579   6.147  1.00 83.41  ?  64  VAL A CA  1 
ATOM   491  C  C   . VAL A 1 72  ? 16.066  0.487   7.201  1.00 80.34  ?  64  VAL A C   1 
ATOM   492  O  O   . VAL A 1 72  ? 16.638  -0.598  7.043  1.00 75.07  ?  64  VAL A O   1 
ATOM   493  C  CB  . VAL A 1 72  ? 15.440  1.209   4.847  1.00 88.17  ?  64  VAL A CB  1 
ATOM   494  C  CG1 . VAL A 1 72  ? 16.200  0.131   4.073  1.00 93.34  ?  64  VAL A CG1 1 
ATOM   495  C  CG2 . VAL A 1 72  ? 14.016  0.768   5.141  1.00 86.30  ?  64  VAL A CG2 1 
ATOM   496  N  N   . ILE A 1 73  ? 15.339  0.783   8.278  1.00 80.08  ?  65  ILE A N   1 
ATOM   497  C  CA  . ILE A 1 73  ? 15.211  -0.162  9.381  1.00 74.26  ?  65  ILE A CA  1 
ATOM   498  C  C   . ILE A 1 73  ? 14.319  -1.315  8.941  1.00 65.90  ?  65  ILE A C   1 
ATOM   499  O  O   . ILE A 1 73  ? 13.122  -1.129  8.682  1.00 63.13  ?  65  ILE A O   1 
ATOM   500  C  CB  . ILE A 1 73  ? 14.640  0.520   10.631 1.00 77.29  ?  65  ILE A CB  1 
ATOM   501  C  CG1 . ILE A 1 73  ? 15.461  1.752   11.018 1.00 79.32  ?  65  ILE A CG1 1 
ATOM   502  C  CG2 . ILE A 1 73  ? 14.582  -0.469  11.793 1.00 68.63  ?  65  ILE A CG2 1 
ATOM   503  C  CD1 . ILE A 1 73  ? 16.925  1.476   11.262 1.00 84.69  ?  65  ILE A CD1 1 
ATOM   504  N  N   . ASN A 1 74  ? 14.890  -2.515  8.875  1.00 59.92  ?  66  ASN A N   1 
ATOM   505  C  CA  . ASN A 1 74  ? 14.094  -3.681  8.524  1.00 55.61  ?  66  ASN A CA  1 
ATOM   506  C  C   . ASN A 1 74  ? 12.948  -3.852  9.513  1.00 63.14  ?  66  ASN A C   1 
ATOM   507  O  O   . ASN A 1 74  ? 13.091  -3.574  10.706 1.00 68.69  ?  66  ASN A O   1 
ATOM   508  C  CB  . ASN A 1 74  ? 14.953  -4.940  8.514  1.00 57.64  ?  66  ASN A CB  1 
ATOM   509  C  CG  . ASN A 1 74  ? 14.161  -6.169  8.136  1.00 64.26  ?  66  ASN A CG  1 
ATOM   510  O  OD1 . ASN A 1 74  ? 13.997  -7.091  8.936  1.00 66.11  ?  66  ASN A OD1 1 
ATOM   511  N  ND2 . ASN A 1 74  ? 13.632  -6.176  6.920  1.00 69.77  ?  66  ASN A ND2 1 
ATOM   512  N  N   . ASP A 1 75  ? 11.806  -4.324  9.005  1.00 64.41  ?  67  ASP A N   1 
ATOM   513  C  CA  . ASP A 1 75  ? 10.624  -4.467  9.847  1.00 62.19  ?  67  ASP A CA  1 
ATOM   514  C  C   . ASP A 1 75  ? 10.908  -5.361  11.050 1.00 60.91  ?  67  ASP A C   1 
ATOM   515  O  O   . ASP A 1 75  ? 10.579  -5.010  12.190 1.00 67.85  ?  67  ASP A O   1 
ATOM   516  C  CB  . ASP A 1 75  ? 9.451   -5.018  9.024  1.00 75.26  ?  67  ASP A CB  1 
ATOM   517  C  CG  . ASP A 1 75  ? 9.813   -6.265  8.209  1.00 82.62  ?  67  ASP A CG  1 
ATOM   518  O  OD1 . ASP A 1 75  ? 11.006  -6.623  8.110  1.00 81.62  ?  67  ASP A OD1 1 
ATOM   519  O  OD2 . ASP A 1 75  ? 8.883   -6.890  7.654  1.00 75.71  ?  67  ASP A OD2 1 
ATOM   520  N  N   . LYS A 1 76  ? 11.534  -6.516  10.820 1.00 60.27  ?  68  LYS A N   1 
ATOM   521  C  CA  . LYS A 1 76  ? 11.794  -7.445  11.916 1.00 60.39  ?  68  LYS A CA  1 
ATOM   522  C  C   . LYS A 1 76  ? 12.694  -6.817  12.975 1.00 61.66  ?  68  LYS A C   1 
ATOM   523  O  O   . LYS A 1 76  ? 12.500  -7.040  14.176 1.00 63.03  ?  68  LYS A O   1 
ATOM   524  C  CB  . LYS A 1 76  ? 12.403  -8.734  11.363 1.00 66.66  ?  68  LYS A CB  1 
ATOM   525  C  CG  . LYS A 1 76  ? 11.450  -9.493  10.438 1.00 69.37  ?  68  LYS A CG  1 
ATOM   526  C  CD  . LYS A 1 76  ? 12.171  -10.347 9.402  1.00 79.59  ?  68  LYS A CD  1 
ATOM   527  C  CE  . LYS A 1 76  ? 12.645  -11.669 9.981  1.00 87.23  ?  68  LYS A CE  1 
ATOM   528  N  NZ  . LYS A 1 76  ? 13.047  -12.625 8.908  1.00 88.85  ?  68  LYS A NZ  1 
ATOM   529  N  N   . ALA A 1 77  ? 13.681  -6.024  12.551 1.00 60.79  ?  69  ALA A N   1 
ATOM   530  C  CA  . ALA A 1 77  ? 14.540  -5.348  13.517 1.00 60.31  ?  69  ALA A CA  1 
ATOM   531  C  C   . ALA A 1 77  ? 13.730  -4.416  14.404 1.00 61.60  ?  69  ALA A C   1 
ATOM   532  O  O   . ALA A 1 77  ? 13.960  -4.332  15.617 1.00 60.94  ?  69  ALA A O   1 
ATOM   533  C  CB  . ALA A 1 77  ? 15.635  -4.563  12.797 1.00 59.01  ?  69  ALA A CB  1 
ATOM   534  N  N   . GLU A 1 78  ? 12.784  -3.695  13.807 1.00 58.79  ?  70  GLU A N   1 
ATOM   535  C  CA  . GLU A 1 78  ? 11.953  -2.788  14.582 1.00 59.79  ?  70  GLU A CA  1 
ATOM   536  C  C   . GLU A 1 78  ? 11.107  -3.553  15.587 1.00 60.10  ?  70  GLU A C   1 
ATOM   537  O  O   . GLU A 1 78  ? 10.933  -3.106  16.723 1.00 58.83  ?  70  GLU A O   1 
ATOM   538  C  CB  . GLU A 1 78  ? 11.076  -1.967  13.638 1.00 63.67  ?  70  GLU A CB  1 
ATOM   539  C  CG  . GLU A 1 78  ? 10.418  -0.769  14.279 1.00 74.58  ?  70  GLU A CG  1 
ATOM   540  C  CD  . GLU A 1 78  ? 9.998   0.268   13.253 1.00 87.50  ?  70  GLU A CD  1 
ATOM   541  O  OE1 . GLU A 1 78  ? 10.565  0.271   12.138 1.00 83.48  ?  70  GLU A OE1 1 
ATOM   542  O  OE2 . GLU A 1 78  ? 9.100   1.080   13.558 1.00 95.81  ?  70  GLU A OE2 1 
ATOM   543  N  N   . VAL A 1 79  ? 10.585  -4.717  15.191 1.00 61.30  ?  71  VAL A N   1 
ATOM   544  C  CA  . VAL A 1 79  ? 9.743   -5.491  16.095 1.00 60.70  ?  71  VAL A CA  1 
ATOM   545  C  C   . VAL A 1 79  ? 10.523  -5.887  17.338 1.00 56.06  ?  71  VAL A C   1 
ATOM   546  O  O   . VAL A 1 79  ? 10.079  -5.670  18.469 1.00 61.04  ?  71  VAL A O   1 
ATOM   547  C  CB  . VAL A 1 79  ? 9.179   -6.734  15.385 1.00 66.63  ?  71  VAL A CB  1 
ATOM   548  C  CG1 . VAL A 1 79  ? 8.480   -7.635  16.399 1.00 64.04  ?  71  VAL A CG1 1 
ATOM   549  C  CG2 . VAL A 1 79  ? 8.234   -6.325  14.279 1.00 68.61  ?  71  VAL A CG2 1 
ATOM   550  N  N   . LEU A 1 80  ? 11.698  -6.483  17.148 1.00 51.28  ?  72  LEU A N   1 
ATOM   551  C  CA  . LEU A 1 80  ? 12.498  -6.856  18.307 1.00 54.04  ?  72  LEU A CA  1 
ATOM   552  C  C   . LEU A 1 80  ? 12.784  -5.645  19.181 1.00 55.21  ?  72  LEU A C   1 
ATOM   553  O  O   . LEU A 1 80  ? 12.835  -5.769  20.407 1.00 53.07  ?  72  LEU A O   1 
ATOM   554  C  CB  . LEU A 1 80  ? 13.784  -7.538  17.851 1.00 59.96  ?  72  LEU A CB  1 
ATOM   555  C  CG  . LEU A 1 80  ? 13.502  -8.870  17.149 1.00 65.12  ?  72  LEU A CG  1 
ATOM   556  C  CD1 . LEU A 1 80  ? 14.685  -9.313  16.311 1.00 74.01  ?  72  LEU A CD1 1 
ATOM   557  C  CD2 . LEU A 1 80  ? 13.146  -9.944  18.173 1.00 75.37  ?  72  LEU A CD2 1 
ATOM   558  N  N   . MET A 1 81  ? 12.950  -4.466  18.575 1.00 51.42  ?  73  MET A N   1 
ATOM   559  C  CA  . MET A 1 81  ? 13.116  -3.256  19.370 1.00 50.97  ?  73  MET A CA  1 
ATOM   560  C  C   . MET A 1 81  ? 11.826  -2.887  20.091 1.00 50.91  ?  73  MET A C   1 
ATOM   561  O  O   . MET A 1 81  ? 11.867  -2.364  21.210 1.00 50.35  ?  73  MET A O   1 
ATOM   562  C  CB  . MET A 1 81  ? 13.588  -2.100  18.485 1.00 49.76  ?  73  MET A CB  1 
ATOM   563  C  CG  . MET A 1 81  ? 15.038  -2.219  18.043 1.00 58.30  ?  73  MET A CG  1 
ATOM   564  S  SD  . MET A 1 81  ? 15.688  -0.727  17.263 1.00 60.55  ?  73  MET A SD  1 
ATOM   565  C  CE  . MET A 1 81  ? 14.664  -0.635  15.791 1.00 58.15  ?  73  MET A CE  1 
ATOM   566  N  N   . PHE A 1 82  ? 10.678  -3.141  19.462 1.00 48.62  ?  74  PHE A N   1 
ATOM   567  C  CA  . PHE A 1 82  ? 9.393   -2.949  20.131 1.00 57.08  ?  74  PHE A CA  1 
ATOM   568  C  C   . PHE A 1 82  ? 9.278   -3.853  21.352 1.00 57.18  ?  74  PHE A C   1 
ATOM   569  O  O   . PHE A 1 82  ? 8.900   -3.402  22.439 1.00 48.78  ?  74  PHE A O   1 
ATOM   570  C  CB  . PHE A 1 82  ? 8.270   -3.203  19.114 1.00 59.37  ?  74  PHE A CB  1 
ATOM   571  C  CG  . PHE A 1 82  ? 6.894   -3.354  19.717 1.00 57.35  ?  74  PHE A CG  1 
ATOM   572  C  CD1 . PHE A 1 82  ? 6.502   -4.553  20.297 1.00 72.20  ?  74  PHE A CD1 1 
ATOM   573  C  CD2 . PHE A 1 82  ? 5.976   -2.314  19.663 1.00 66.24  ?  74  PHE A CD2 1 
ATOM   574  C  CE1 . PHE A 1 82  ? 5.232   -4.700  20.844 1.00 81.62  ?  74  PHE A CE1 1 
ATOM   575  C  CE2 . PHE A 1 82  ? 4.703   -2.457  20.204 1.00 72.47  ?  74  PHE A CE2 1 
ATOM   576  C  CZ  . PHE A 1 82  ? 4.331   -3.651  20.792 1.00 78.66  ?  74  PHE A CZ  1 
ATOM   577  N  N   . TYR A 1 83  ? 9.630   -5.131  21.200 1.00 53.24  ?  75  TYR A N   1 
ATOM   578  C  CA  . TYR A 1 83  ? 9.548   -6.050  22.331 1.00 54.66  ?  75  TYR A CA  1 
ATOM   579  C  C   . TYR A 1 83  ? 10.623  -5.764  23.370 1.00 52.84  ?  75  TYR A C   1 
ATOM   580  O  O   . TYR A 1 83  ? 10.430  -6.065  24.553 1.00 53.10  ?  75  TYR A O   1 
ATOM   581  C  CB  . TYR A 1 83  ? 9.643   -7.495  21.845 1.00 59.67  ?  75  TYR A CB  1 
ATOM   582  C  CG  . TYR A 1 83  ? 8.294   -8.160  21.710 1.00 76.36  ?  75  TYR A CG  1 
ATOM   583  C  CD1 . TYR A 1 83  ? 7.552   -8.042  20.542 1.00 82.41  ?  75  TYR A CD1 1 
ATOM   584  C  CD2 . TYR A 1 83  ? 7.757   -8.898  22.755 1.00 90.61  ?  75  TYR A CD2 1 
ATOM   585  C  CE1 . TYR A 1 83  ? 6.316   -8.645  20.419 1.00 91.74  ?  75  TYR A CE1 1 
ATOM   586  C  CE2 . TYR A 1 83  ? 6.522   -9.504  22.641 1.00 99.79  ?  75  TYR A CE2 1 
ATOM   587  C  CZ  . TYR A 1 83  ? 5.805   -9.374  21.471 1.00 101.61 ?  75  TYR A CZ  1 
ATOM   588  O  OH  . TYR A 1 83  ? 4.574   -9.979  21.355 1.00 105.70 ?  75  TYR A OH  1 
ATOM   589  N  N   . ALA A 1 84  ? 11.760  -5.200  22.957 1.00 55.35  ?  76  ALA A N   1 
ATOM   590  C  CA  . ALA A 1 84  ? 12.731  -4.740  23.942 1.00 53.98  ?  76  ALA A CA  1 
ATOM   591  C  C   . ALA A 1 84  ? 12.143  -3.620  24.787 1.00 53.06  ?  76  ALA A C   1 
ATOM   592  O  O   . ALA A 1 84  ? 12.341  -3.579  26.007 1.00 46.91  ?  76  ALA A O   1 
ATOM   593  C  CB  . ALA A 1 84  ? 14.011  -4.276  23.250 1.00 47.64  ?  76  ALA A CB  1 
ATOM   594  N  N   . ALA A 1 85  ? 11.418  -2.698  24.150 1.00 54.68  ?  77  ALA A N   1 
ATOM   595  C  CA  . ALA A 1 85  ? 10.761  -1.632  24.895 1.00 51.42  ?  77  ALA A CA  1 
ATOM   596  C  C   . ALA A 1 85  ? 9.725   -2.197  25.852 1.00 48.15  ?  77  ALA A C   1 
ATOM   597  O  O   . ALA A 1 85  ? 9.647   -1.780  27.013 1.00 51.10  ?  77  ALA A O   1 
ATOM   598  C  CB  . ALA A 1 85  ? 10.109  -0.644  23.932 1.00 49.66  ?  77  ALA A CB  1 
ATOM   599  N  N   . ARG A 1 86  ? 8.912   -3.144  25.379 1.00 49.07  ?  78  ARG A N   1 
ATOM   600  C  CA  . ARG A 1 86  ? 7.862   -3.687  26.230 1.00 52.04  ?  78  ARG A CA  1 
ATOM   601  C  C   . ARG A 1 86  ? 8.454   -4.413  27.429 1.00 57.14  ?  78  ARG A C   1 
ATOM   602  O  O   . ARG A 1 86  ? 7.967   -4.271  28.556 1.00 58.71  ?  78  ARG A O   1 
ATOM   603  C  CB  . ARG A 1 86  ? 6.965   -4.624  25.430 1.00 57.90  ?  78  ARG A CB  1 
ATOM   604  C  CG  . ARG A 1 86  ? 5.909   -5.302  26.282 1.00 71.54  ?  78  ARG A CG  1 
ATOM   605  C  CD  . ARG A 1 86  ? 5.001   -6.182  25.453 1.00 98.54  ?  78  ARG A CD  1 
ATOM   606  N  NE  . ARG A 1 86  ? 4.109   -5.401  24.604 1.00 112.26 ?  78  ARG A NE  1 
ATOM   607  C  CZ  . ARG A 1 86  ? 3.121   -5.917  23.887 1.00 120.23 ?  78  ARG A CZ  1 
ATOM   608  N  NH1 . ARG A 1 86  ? 2.876   -7.216  23.886 1.00 120.24 ?  78  ARG A NH1 1 
ATOM   609  N  NH2 . ARG A 1 86  ? 2.358   -5.109  23.156 1.00 124.42 ?  78  ARG A NH2 1 
ATOM   610  N  N   . VAL A 1 87  ? 9.510   -5.198  27.201 1.00 55.93  ?  79  VAL A N   1 
ATOM   611  C  CA  . VAL A 1 87  ? 10.168  -5.902  28.294 1.00 50.26  ?  79  VAL A CA  1 
ATOM   612  C  C   . VAL A 1 87  ? 10.733  -4.910  29.299 1.00 48.35  ?  79  VAL A C   1 
ATOM   613  O  O   . VAL A 1 87  ? 10.606  -5.094  30.516 1.00 55.22  ?  79  VAL A O   1 
ATOM   614  C  CB  . VAL A 1 87  ? 11.266  -6.830  27.740 1.00 53.88  ?  79  VAL A CB  1 
ATOM   615  C  CG1 . VAL A 1 87  ? 12.121  -7.371  28.872 1.00 54.36  ?  79  VAL A CG1 1 
ATOM   616  C  CG2 . VAL A 1 87  ? 10.648  -7.963  26.934 1.00 61.66  ?  79  VAL A CG2 1 
ATOM   617  N  N   . GLN A 1 88  ? 11.383  -3.853  28.810 1.00 49.58  ?  80  GLN A N   1 
ATOM   618  C  CA  . GLN A 1 88  ? 11.915  -2.842  29.718 1.00 52.04  ?  80  GLN A CA  1 
ATOM   619  C  C   . GLN A 1 88  ? 10.803  -2.265  30.585 1.00 55.54  ?  80  GLN A C   1 
ATOM   620  O  O   . GLN A 1 88  ? 11.002  -2.012  31.778 1.00 50.33  ?  80  GLN A O   1 
ATOM   621  C  CB  . GLN A 1 88  ? 12.617  -1.738  28.925 1.00 48.86  ?  80  GLN A CB  1 
ATOM   622  C  CG  . GLN A 1 88  ? 13.287  -0.660  29.779 1.00 56.34  ?  80  GLN A CG  1 
ATOM   623  C  CD  . GLN A 1 88  ? 14.565  -1.136  30.455 1.00 56.29  ?  80  GLN A CD  1 
ATOM   624  O  OE1 . GLN A 1 88  ? 14.912  -2.313  30.388 1.00 52.21  ?  80  GLN A OE1 1 
ATOM   625  N  NE2 . GLN A 1 88  ? 15.272  -0.215  31.107 1.00 54.71  ?  80  GLN A NE2 1 
ATOM   626  N  N   . LEU A 1 89  ? 9.622   -2.049  29.998 1.00 58.21  ?  81  LEU A N   1 
ATOM   627  C  CA  . LEU A 1 89  ? 8.504   -1.515  30.767 1.00 54.67  ?  81  LEU A CA  1 
ATOM   628  C  C   . LEU A 1 89  ? 7.984   -2.537  31.767 1.00 53.74  ?  81  LEU A C   1 
ATOM   629  O  O   . LEU A 1 89  ? 7.688   -2.195  32.915 1.00 63.69  ?  81  LEU A O   1 
ATOM   630  C  CB  . LEU A 1 89  ? 7.384   -1.075  29.824 1.00 57.75  ?  81  LEU A CB  1 
ATOM   631  C  CG  . LEU A 1 89  ? 6.202   -0.339  30.461 1.00 62.55  ?  81  LEU A CG  1 
ATOM   632  C  CD1 . LEU A 1 89  ? 6.619   1.026   30.988 1.00 59.03  ?  81  LEU A CD1 1 
ATOM   633  C  CD2 . LEU A 1 89  ? 5.064   -0.199  29.459 1.00 69.90  ?  81  LEU A CD2 1 
ATOM   634  N  N   . VAL A 1 90  ? 7.879   -3.799  31.349 1.00 50.76  ?  82  VAL A N   1 
ATOM   635  C  CA  . VAL A 1 90  ? 7.349   -4.830  32.235 1.00 56.44  ?  82  VAL A CA  1 
ATOM   636  C  C   . VAL A 1 90  ? 8.243   -5.000  33.454 1.00 58.99  ?  82  VAL A C   1 
ATOM   637  O  O   . VAL A 1 90  ? 7.761   -5.147  34.580 1.00 54.49  ?  82  VAL A O   1 
ATOM   638  C  CB  . VAL A 1 90  ? 7.186   -6.157  31.471 1.00 56.07  ?  82  VAL A CB  1 
ATOM   639  C  CG1 . VAL A 1 90  ? 6.996   -7.314  32.442 1.00 57.06  ?  82  VAL A CG1 1 
ATOM   640  C  CG2 . VAL A 1 90  ? 6.021   -6.069  30.500 1.00 64.04  ?  82  VAL A CG2 1 
ATOM   641  N  N   . GLU A 1 91  ? 9.553   -4.993  33.251 1.00 58.00  ?  83  GLU A N   1 
ATOM   642  C  CA  . GLU A 1 91  ? 10.470  -5.362  34.320 1.00 54.79  ?  83  GLU A CA  1 
ATOM   643  C  C   . GLU A 1 91  ? 10.867  -4.183  35.196 1.00 46.22  ?  83  GLU A C   1 
ATOM   644  O  O   . GLU A 1 91  ? 11.049  -4.367  36.407 1.00 46.19  ?  83  GLU A O   1 
ATOM   645  C  CB  . GLU A 1 91  ? 11.712  -6.033  33.723 1.00 63.80  ?  83  GLU A CB  1 
ATOM   646  C  CG  . GLU A 1 91  ? 11.414  -7.345  32.986 1.00 61.05  ?  83  GLU A CG  1 
ATOM   647  C  CD  . GLU A 1 91  ? 10.853  -8.421  33.902 1.00 63.64  ?  83  GLU A CD  1 
ATOM   648  O  OE1 . GLU A 1 91  ? 10.897  -8.231  35.138 1.00 71.19  ?  83  GLU A OE1 1 
ATOM   649  O  OE2 . GLU A 1 91  ? 10.368  -9.455  33.392 1.00 60.18  ?  83  GLU A OE2 1 
ATOM   650  N  N   . THR A 1 92  ? 10.976  -2.978  34.630 1.00 53.58  ?  84  THR A N   1 
ATOM   651  C  CA  . THR A 1 92  ? 11.438  -1.836  35.408 1.00 48.65  ?  84  THR A CA  1 
ATOM   652  C  C   . THR A 1 92  ? 10.318  -0.900  35.861 1.00 46.25  ?  84  THR A C   1 
ATOM   653  O  O   . THR A 1 92  ? 10.563  -0.057  36.733 1.00 49.04  ?  84  THR A O   1 
ATOM   654  C  CB  . THR A 1 92  ? 12.447  -0.990  34.618 1.00 54.65  ?  84  THR A CB  1 
ATOM   655  O  OG1 . THR A 1 92  ? 11.739  -0.070  33.769 1.00 57.06  ?  84  THR A OG1 1 
ATOM   656  C  CG2 . THR A 1 92  ? 13.377  -1.856  33.780 1.00 50.69  ?  84  THR A CG2 1 
ATOM   657  N  N   . VAL A 1 93  ? 9.117   -0.996  35.293 1.00 44.53  ?  85  VAL A N   1 
ATOM   658  C  CA  . VAL A 1 93  ? 8.036   -0.120  35.736 1.00 49.48  ?  85  VAL A CA  1 
ATOM   659  C  C   . VAL A 1 93  ? 6.856   -0.924  36.257 1.00 58.33  ?  85  VAL A C   1 
ATOM   660  O  O   . VAL A 1 93  ? 6.444   -0.757  37.410 1.00 53.50  ?  85  VAL A O   1 
ATOM   661  C  CB  . VAL A 1 93  ? 7.579   0.830   34.607 1.00 49.44  ?  85  VAL A CB  1 
ATOM   662  C  CG1 . VAL A 1 93  ? 6.402   1.679   35.069 1.00 50.74  ?  85  VAL A CG1 1 
ATOM   663  C  CG2 . VAL A 1 93  ? 8.730   1.706   34.167 1.00 49.55  ?  85  VAL A CG2 1 
ATOM   664  N  N   . ILE A 1 94  ? 6.302   -1.794  35.412 1.00 48.20  ?  86  ILE A N   1 
ATOM   665  C  CA  . ILE A 1 94  ? 5.034   -2.436  35.742 1.00 56.40  ?  86  ILE A CA  1 
ATOM   666  C  C   . ILE A 1 94  ? 5.214   -3.395  36.911 1.00 55.39  ?  86  ILE A C   1 
ATOM   667  O  O   . ILE A 1 94  ? 4.569   -3.259  37.959 1.00 51.85  ?  86  ILE A O   1 
ATOM   668  C  CB  . ILE A 1 94  ? 4.447   -3.154  34.513 1.00 57.88  ?  86  ILE A CB  1 
ATOM   669  C  CG1 . ILE A 1 94  ? 3.963   -2.140  33.481 1.00 68.00  ?  86  ILE A CG1 1 
ATOM   670  C  CG2 . ILE A 1 94  ? 3.315   -4.076  34.949 1.00 57.74  ?  86  ILE A CG2 1 
ATOM   671  C  CD1 . ILE A 1 94  ? 3.586   -2.748  32.129 1.00 69.65  ?  86  ILE A CD1 1 
ATOM   672  N  N   . LYS A 1 95  ? 6.088   -4.388  36.743 1.00 57.49  ?  87  LYS A N   1 
ATOM   673  C  CA  . LYS A 1 95  ? 6.247   -5.385  37.798 1.00 56.49  ?  87  LYS A CA  1 
ATOM   674  C  C   . LYS A 1 95  ? 6.582   -4.729  39.130 1.00 56.78  ?  87  LYS A C   1 
ATOM   675  O  O   . LYS A 1 95  ? 5.897   -5.019  40.126 1.00 55.26  ?  87  LYS A O   1 
ATOM   676  C  CB  . LYS A 1 95  ? 7.301   -6.419  37.390 1.00 52.30  ?  87  LYS A CB  1 
ATOM   677  C  CG  . LYS A 1 95  ? 6.786   -7.473  36.408 1.00 49.42  ?  87  LYS A CG  1 
ATOM   678  C  CD  . LYS A 1 95  ? 7.807   -8.591  36.180 1.00 51.60  ?  87  LYS A CD  1 
ATOM   679  C  CE  . LYS A 1 95  ? 7.200   -9.755  35.401 1.00 60.14  ?  87  LYS A CE  1 
ATOM   680  N  NZ  . LYS A 1 95  ? 8.210   -10.773 34.985 1.00 74.94  ?  87  LYS A NZ  1 
ATOM   681  N  N   . PRO A 1 96  ? 7.568   -3.830  39.224 1.00 62.23  ?  88  PRO A N   1 
ATOM   682  C  CA  . PRO A 1 96  ? 7.795   -3.165  40.519 1.00 57.49  ?  88  PRO A CA  1 
ATOM   683  C  C   . PRO A 1 96  ? 6.571   -2.426  41.029 1.00 54.16  ?  88  PRO A C   1 
ATOM   684  O  O   . PRO A 1 96  ? 6.268   -2.497  42.226 1.00 61.15  ?  88  PRO A O   1 
ATOM   685  C  CB  . PRO A 1 96  ? 8.965   -2.214  40.227 1.00 57.99  ?  88  PRO A CB  1 
ATOM   686  C  CG  . PRO A 1 96  ? 9.670   -2.825  39.055 1.00 54.58  ?  88  PRO A CG  1 
ATOM   687  C  CD  . PRO A 1 96  ? 8.589   -3.468  38.220 1.00 54.93  ?  88  PRO A CD  1 
ATOM   688  N  N   . ALA A 1 97  ? 5.842   -1.733  40.150 1.00 61.25  ?  89  ALA A N   1 
ATOM   689  C  CA  . ALA A 1 97  ? 4.666   -0.996  40.597 1.00 56.34  ?  89  ALA A CA  1 
ATOM   690  C  C   . ALA A 1 97  ? 3.671   -1.932  41.266 1.00 52.88  ?  89  ALA A C   1 
ATOM   691  O  O   . ALA A 1 97  ? 3.195   -1.666  42.375 1.00 53.89  ?  89  ALA A O   1 
ATOM   692  C  CB  . ALA A 1 97  ? 4.014   -0.271  39.422 1.00 52.40  ?  89  ALA A CB  1 
ATOM   693  N  N   . LEU A 1 98  ? 3.362   -3.052  40.608 1.00 52.14  ?  90  LEU A N   1 
ATOM   694  C  CA  . LEU A 1 98  ? 2.491   -4.043  41.225 1.00 52.70  ?  90  LEU A CA  1 
ATOM   695  C  C   . LEU A 1 98  ? 3.061   -4.506  42.558 1.00 52.95  ?  90  LEU A C   1 
ATOM   696  O  O   . LEU A 1 98  ? 2.321   -4.697  43.529 1.00 53.56  ?  90  LEU A O   1 
ATOM   697  C  CB  . LEU A 1 98  ? 2.310   -5.238  40.292 1.00 56.49  ?  90  LEU A CB  1 
ATOM   698  C  CG  . LEU A 1 98  ? 1.683   -4.950  38.929 1.00 55.18  ?  90  LEU A CG  1 
ATOM   699  C  CD1 . LEU A 1 98  ? 1.743   -6.183  38.044 1.00 55.99  ?  90  LEU A CD1 1 
ATOM   700  C  CD2 . LEU A 1 98  ? 0.249   -4.486  39.098 1.00 53.00  ?  90  LEU A CD2 1 
ATOM   701  N  N   . ALA A 1 99  ? 4.380   -4.682  42.626 1.00 56.53  ?  91  ALA A N   1 
ATOM   702  C  CA  . ALA A 1 99  ? 4.982   -5.229  43.833 1.00 50.35  ?  91  ALA A CA  1 
ATOM   703  C  C   . ALA A 1 99  ? 4.837   -4.278  45.014 1.00 52.85  ?  91  ALA A C   1 
ATOM   704  O  O   . ALA A 1 99  ? 4.689   -4.736  46.153 1.00 53.93  ?  91  ALA A O   1 
ATOM   705  C  CB  . ALA A 1 99  ? 6.453   -5.564  43.575 1.00 50.81  ?  91  ALA A CB  1 
ATOM   706  N  N   . ARG A 1 100 ? 4.856   -2.965  44.769 1.00 52.03  ?  92  ARG A N   1 
ATOM   707  C  CA  . ARG A 1 100 ? 4.655   -2.001  45.843 1.00 51.43  ?  92  ARG A CA  1 
ATOM   708  C  C   . ARG A 1 100 ? 3.199   -1.871  46.272 1.00 56.70  ?  92  ARG A C   1 
ATOM   709  O  O   . ARG A 1 100 ? 2.918   -1.153  47.236 1.00 58.86  ?  92  ARG A O   1 
ATOM   710  C  CB  . ARG A 1 100 ? 5.153   -0.616  45.427 1.00 55.15  ?  92  ARG A CB  1 
ATOM   711  C  CG  . ARG A 1 100 ? 6.617   -0.536  45.095 1.00 60.00  ?  92  ARG A CG  1 
ATOM   712  C  CD  . ARG A 1 100 ? 7.064   0.914   45.075 1.00 64.46  ?  92  ARG A CD  1 
ATOM   713  N  NE  . ARG A 1 100 ? 6.384   1.687   44.043 1.00 65.10  ?  92  ARG A NE  1 
ATOM   714  C  CZ  . ARG A 1 100 ? 6.814   1.795   42.792 1.00 62.33  ?  92  ARG A CZ  1 
ATOM   715  N  NH1 . ARG A 1 100 ? 7.900   1.163   42.379 1.00 56.62  ?  92  ARG A NH1 1 
ATOM   716  N  NH2 . ARG A 1 100 ? 6.140   2.559   41.936 1.00 68.14  ?  92  ARG A NH2 1 
ATOM   717  N  N   . GLY A 1 101 ? 2.276   -2.526  45.578 1.00 59.91  ?  93  GLY A N   1 
ATOM   718  C  CA  . GLY A 1 101 ? 0.863   -2.371  45.834 1.00 54.87  ?  93  GLY A CA  1 
ATOM   719  C  C   . GLY A 1 101 ? 0.156   -1.393  44.932 1.00 57.97  ?  93  GLY A C   1 
ATOM   720  O  O   . GLY A 1 101 ? -1.005  -1.059  45.198 1.00 56.61  ?  93  GLY A O   1 
ATOM   721  N  N   . GLN A 1 102 ? 0.814   -0.926  43.876 1.00 57.11  ?  94  GLN A N   1 
ATOM   722  C  CA  . GLN A 1 102 ? 0.221   0.025   42.951 1.00 58.84  ?  94  GLN A CA  1 
ATOM   723  C  C   . GLN A 1 102 ? -0.413  -0.705  41.775 1.00 54.30  ?  94  GLN A C   1 
ATOM   724  O  O   . GLN A 1 102 ? 0.242   -1.508  41.105 1.00 54.63  ?  94  GLN A O   1 
ATOM   725  C  CB  . GLN A 1 102 ? 1.274   1.006   42.432 1.00 57.61  ?  94  GLN A CB  1 
ATOM   726  C  CG  . GLN A 1 102 ? 1.584   2.155   43.366 1.00 66.26  ?  94  GLN A CG  1 
ATOM   727  C  CD  . GLN A 1 102 ? 2.703   3.033   42.844 1.00 67.03  ?  94  GLN A CD  1 
ATOM   728  O  OE1 . GLN A 1 102 ? 3.459   2.629   41.966 1.00 58.32  ?  94  GLN A OE1 1 
ATOM   729  N  NE2 . GLN A 1 102 ? 2.807   4.244   43.379 1.00 72.92  ?  94  GLN A NE2 1 
ATOM   730  N  N   . TRP A 1 103 ? -1.687  -0.423  41.525 1.00 58.23  ?  95  TRP A N   1 
ATOM   731  C  CA  . TRP A 1 103 ? -2.295  -0.832  40.266 1.00 58.77  ?  95  TRP A CA  1 
ATOM   732  C  C   . TRP A 1 103 ? -1.566  -0.140  39.120 1.00 53.55  ?  95  TRP A C   1 
ATOM   733  O  O   . TRP A 1 103 ? -0.809  0.813   39.318 1.00 52.95  ?  95  TRP A O   1 
ATOM   734  C  CB  . TRP A 1 103 ? -3.787  -0.501  40.265 1.00 63.62  ?  95  TRP A CB  1 
ATOM   735  C  CG  . TRP A 1 103 ? -4.584  -1.387  41.183 1.00 65.48  ?  95  TRP A CG  1 
ATOM   736  C  CD1 . TRP A 1 103 ? -4.337  -1.630  42.502 1.00 65.43  ?  95  TRP A CD1 1 
ATOM   737  C  CD2 . TRP A 1 103 ? -5.766  -2.134  40.854 1.00 68.93  ?  95  TRP A CD2 1 
ATOM   738  N  NE1 . TRP A 1 103 ? -5.278  -2.493  43.011 1.00 67.68  ?  95  TRP A NE1 1 
ATOM   739  C  CE2 . TRP A 1 103 ? -6.170  -2.813  42.022 1.00 70.43  ?  95  TRP A CE2 1 
ATOM   740  C  CE3 . TRP A 1 103 ? -6.520  -2.294  39.687 1.00 65.47  ?  95  TRP A CE3 1 
ATOM   741  C  CZ2 . TRP A 1 103 ? -7.293  -3.639  42.056 1.00 70.00  ?  95  TRP A CZ2 1 
ATOM   742  C  CZ3 . TRP A 1 103 ? -7.635  -3.117  39.723 1.00 64.95  ?  95  TRP A CZ3 1 
ATOM   743  C  CH2 . TRP A 1 103 ? -8.009  -3.779  40.900 1.00 67.22  ?  95  TRP A CH2 1 
ATOM   744  N  N   . VAL A 1 104 ? -1.786  -0.640  37.906 1.00 55.37  ?  96  VAL A N   1 
ATOM   745  C  CA  . VAL A 1 104 ? -1.144  -0.097  36.711 1.00 55.72  ?  96  VAL A CA  1 
ATOM   746  C  C   . VAL A 1 104 ? -2.149  -0.121  35.567 1.00 47.96  ?  96  VAL A C   1 
ATOM   747  O  O   . VAL A 1 104 ? -2.613  -1.194  35.176 1.00 48.52  ?  96  VAL A O   1 
ATOM   748  C  CB  . VAL A 1 104 ? 0.121   -0.890  36.327 1.00 54.63  ?  96  VAL A CB  1 
ATOM   749  C  CG1 . VAL A 1 104 ? 0.798   -0.253  35.134 1.00 55.23  ?  96  VAL A CG1 1 
ATOM   750  C  CG2 . VAL A 1 104 ? 1.075   -0.998  37.514 1.00 53.33  ?  96  VAL A CG2 1 
ATOM   751  N  N   . ILE A 1 105 ? -2.463  1.053   35.014 1.00 51.80  ?  97  ILE A N   1 
ATOM   752  C  CA  . ILE A 1 105 ? -3.407  1.200   33.903 1.00 54.91  ?  97  ILE A CA  1 
ATOM   753  C  C   . ILE A 1 105 ? -2.612  1.639   32.679 1.00 47.74  ?  97  ILE A C   1 
ATOM   754  O  O   . ILE A 1 105 ? -1.963  2.689   32.716 1.00 53.49  ?  97  ILE A O   1 
ATOM   755  C  CB  . ILE A 1 105 ? -4.494  2.245   34.204 1.00 61.59  ?  97  ILE A CB  1 
ATOM   756  C  CG1 . ILE A 1 105 ? -4.963  2.166   35.654 1.00 57.39  ?  97  ILE A CG1 1 
ATOM   757  C  CG2 . ILE A 1 105 ? -5.663  2.087   33.235 1.00 55.27  ?  97  ILE A CG2 1 
ATOM   758  C  CD1 . ILE A 1 105 ? -5.575  0.850   36.029 1.00 58.42  ?  97  ILE A CD1 1 
ATOM   759  N  N   . GLY A 1 106 ? -2.669  0.895   31.583 1.00 58.33  ?  98  GLY A N   1 
ATOM   760  C  CA  . GLY A 1 106 ? -1.817  1.119   30.426 1.00 66.08  ?  98  GLY A CA  1 
ATOM   761  C  C   . GLY A 1 106 ? -2.599  1.338   29.139 1.00 66.53  ?  98  GLY A C   1 
ATOM   762  O  O   . GLY A 1 106 ? -3.704  0.845   28.958 1.00 66.12  ?  98  GLY A O   1 
ATOM   763  N  N   . ASP A 1 107 ? -1.955  2.073   28.217 1.00 83.79  ?  99  ASP A N   1 
ATOM   764  C  CA  . ASP A 1 107 ? -2.520  2.336   26.893 1.00 81.06  ?  99  ASP A CA  1 
ATOM   765  C  C   . ASP A 1 107 ? -1.759  1.553   25.825 1.00 87.30  ?  99  ASP A C   1 
ATOM   766  O  O   . ASP A 1 107 ? -0.554  1.760   25.645 1.00 87.17  ?  99  ASP A O   1 
ATOM   767  C  CB  . ASP A 1 107 ? -2.474  3.828   26.538 1.00 76.71  ?  99  ASP A CB  1 
ATOM   768  C  CG  . ASP A 1 107 ? -3.427  4.662   27.358 1.00 74.64  ?  99  ASP A CG  1 
ATOM   769  O  OD1 . ASP A 1 107 ? -4.450  4.121   27.821 1.00 79.79  ?  99  ASP A OD1 1 
ATOM   770  O  OD2 . ASP A 1 107 ? -3.148  5.869   27.527 1.00 69.33  ?  99  ASP A OD2 1 
ATOM   771  N  N   . ARG A 1 108 ? -2.477  0.694   25.091 1.00 87.50  ?  100 ARG A N   1 
ATOM   772  C  CA  . ARG A 1 108 ? -1.986  0.055   23.865 1.00 90.44  ?  100 ARG A CA  1 
ATOM   773  C  C   . ARG A 1 108 ? -0.925  -1.021  24.122 1.00 98.64  ?  100 ARG A C   1 
ATOM   774  O  O   . ARG A 1 108 ? 0.089   -1.080  23.421 1.00 117.98 ?  100 ARG A O   1 
ATOM   775  C  CB  . ARG A 1 108 ? -1.442  1.100   22.880 1.00 93.00  ?  100 ARG A CB  1 
ATOM   776  C  CG  . ARG A 1 108 ? -2.348  2.303   22.597 1.00 89.13  ?  100 ARG A CG  1 
ATOM   777  C  CD  . ARG A 1 108 ? -1.550  3.452   21.957 1.00 93.43  ?  100 ARG A CD  1 
ATOM   778  N  NE  . ARG A 1 108 ? -2.351  4.657   21.764 1.00 96.94  ?  100 ARG A NE  1 
ATOM   779  C  CZ  . ARG A 1 108 ? -2.511  5.612   22.671 1.00 100.37 ?  100 ARG A CZ  1 
ATOM   780  N  NH1 . ARG A 1 108 ? -1.931  5.545   23.858 1.00 93.82  ?  100 ARG A NH1 1 
ATOM   781  N  NH2 . ARG A 1 108 ? -3.274  6.661   22.379 1.00 105.24 ?  100 ARG A NH2 1 
ATOM   782  N  N   . HIS A 1 109 ? -1.147  -1.891  25.106 1.00 101.24 ?  101 HIS A N   1 
ATOM   783  C  CA  . HIS A 1 109 ? -0.263  -3.045  25.319 1.00 107.77 ?  101 HIS A CA  1 
ATOM   784  C  C   . HIS A 1 109 ? -0.599  -4.148  24.314 1.00 119.36 ?  101 HIS A C   1 
ATOM   785  O  O   . HIS A 1 109 ? -1.251  -5.137  24.658 1.00 116.43 ?  101 HIS A O   1 
ATOM   786  C  CB  . HIS A 1 109 ? -0.378  -3.597  26.746 1.00 101.23 ?  101 HIS A CB  1 
ATOM   787  C  CG  . HIS A 1 109 ? 0.699   -4.583  27.114 1.00 112.38 ?  101 HIS A CG  1 
ATOM   788  N  ND1 . HIS A 1 109 ? 1.963   -4.195  27.506 1.00 119.75 ?  101 HIS A ND1 1 
ATOM   789  C  CD2 . HIS A 1 109 ? 0.689   -5.937  27.177 1.00 115.10 ?  101 HIS A CD2 1 
ATOM   790  C  CE1 . HIS A 1 109 ? 2.687   -5.266  27.782 1.00 122.03 ?  101 HIS A CE1 1 
ATOM   791  N  NE2 . HIS A 1 109 ? 1.938   -6.336  27.591 1.00 120.65 ?  101 HIS A NE2 1 
ATOM   792  N  N   . THR A 1 126 ? 2.366   -15.412 14.275 1.00 108.52 ?  118 THR A N   1 
ATOM   793  C  CA  . THR A 1 126 ? 2.909   -16.572 14.969 1.00 118.56 ?  118 THR A CA  1 
ATOM   794  C  C   . THR A 1 126 ? 4.240   -16.210 15.602 1.00 109.96 ?  118 THR A C   1 
ATOM   795  O  O   . THR A 1 126 ? 4.590   -16.688 16.681 1.00 109.05 ?  118 THR A O   1 
ATOM   796  C  CB  . THR A 1 126 ? 3.135   -17.762 14.031 1.00 114.96 ?  118 THR A CB  1 
ATOM   797  O  OG1 . THR A 1 126 ? 1.924   -18.062 13.330 1.00 111.69 ?  118 THR A OG1 1 
ATOM   798  C  CG2 . THR A 1 126 ? 3.582   -18.984 14.828 1.00 123.68 ?  118 THR A CG2 1 
ATOM   799  N  N   . MET A 1 127 ? 4.998   -15.380 14.886 1.00 106.08 ?  119 MET A N   1 
ATOM   800  C  CA  . MET A 1 127 ? 6.305   -14.962 15.370 1.00 108.62 ?  119 MET A CA  1 
ATOM   801  C  C   . MET A 1 127 ? 6.172   -13.990 16.533 1.00 103.04 ?  119 MET A C   1 
ATOM   802  O  O   . MET A 1 127 ? 7.014   -13.989 17.439 1.00 93.64  ?  119 MET A O   1 
ATOM   803  C  CB  . MET A 1 127 ? 7.097   -14.350 14.215 1.00 118.38 ?  119 MET A CB  1 
ATOM   804  C  CG  . MET A 1 127 ? 7.282   -15.281 13.001 1.00 132.40 ?  119 MET A CG  1 
ATOM   805  S  SD  . MET A 1 127 ? 5.844   -15.520 11.927 1.00 127.61 ?  119 MET A SD  1 
ATOM   806  C  CE  . MET A 1 127 ? 6.442   -16.831 10.858 1.00 118.53 ?  119 MET A CE  1 
ATOM   807  N  N   . LEU A 1 128 ? 5.122   -13.169 16.529 1.00 99.35  ?  120 LEU A N   1 
ATOM   808  C  CA  . LEU A 1 128 ? 4.841   -12.316 17.679 1.00 94.50  ?  120 LEU A CA  1 
ATOM   809  C  C   . LEU A 1 128 ? 4.539   -13.149 18.918 1.00 96.25  ?  120 LEU A C   1 
ATOM   810  O  O   . LEU A 1 128 ? 5.010   -12.835 20.018 1.00 96.39  ?  120 LEU A O   1 
ATOM   811  C  CB  . LEU A 1 128 ? 3.673   -11.386 17.354 1.00 98.54  ?  120 LEU A CB  1 
ATOM   812  C  CG  . LEU A 1 128 ? 3.960   -10.333 16.282 1.00 97.75  ?  120 LEU A CG  1 
ATOM   813  C  CD1 . LEU A 1 128 ? 2.691   -9.683  15.760 1.00 104.67 ?  120 LEU A CD1 1 
ATOM   814  C  CD2 . LEU A 1 128 ? 4.904   -9.280  16.854 1.00 96.33  ?  120 LEU A CD2 1 
ATOM   815  N  N   . ALA A 1 129 ? 3.752   -14.216 18.758 1.00 96.41  ?  121 ALA A N   1 
ATOM   816  C  CA  . ALA A 1 129 ? 3.389   -15.049 19.899 1.00 96.07  ?  121 ALA A CA  1 
ATOM   817  C  C   . ALA A 1 129 ? 4.597   -15.786 20.458 1.00 96.58  ?  121 ALA A C   1 
ATOM   818  O  O   . ALA A 1 129 ? 4.739   -15.925 21.678 1.00 103.22 ?  121 ALA A O   1 
ATOM   819  C  CB  . ALA A 1 129 ? 2.297   -16.042 19.497 1.00 105.94 ?  121 ALA A CB  1 
ATOM   820  N  N   . THR A 1 130 ? 5.474   -16.278 19.580 1.00 99.27  ?  122 THR A N   1 
ATOM   821  C  CA  . THR A 1 130 ? 6.663   -16.978 20.049 1.00 102.37 ?  122 THR A CA  1 
ATOM   822  C  C   . THR A 1 130 ? 7.571   -16.042 20.836 1.00 95.96  ?  122 THR A C   1 
ATOM   823  O  O   . THR A 1 130 ? 8.120   -16.426 21.876 1.00 95.04  ?  122 THR A O   1 
ATOM   824  C  CB  . THR A 1 130 ? 7.419   -17.581 18.867 1.00 108.55 ?  122 THR A CB  1 
ATOM   825  O  OG1 . THR A 1 130 ? 6.487   -18.141 17.931 1.00 120.80 ?  122 THR A OG1 1 
ATOM   826  C  CG2 . THR A 1 130 ? 8.363   -18.674 19.346 1.00 133.64 ?  122 THR A CG2 1 
ATOM   827  N  N   . LEU A 1 131 ? 7.740   -14.808 20.356 1.00 92.57  ?  123 LEU A N   1 
ATOM   828  C  CA  . LEU A 1 131 ? 8.563   -13.845 21.077 1.00 88.92  ?  123 LEU A CA  1 
ATOM   829  C  C   . LEU A 1 131 ? 7.994   -13.570 22.461 1.00 91.88  ?  123 LEU A C   1 
ATOM   830  O  O   . LEU A 1 131 ? 8.726   -13.556 23.456 1.00 87.73  ?  123 LEU A O   1 
ATOM   831  C  CB  . LEU A 1 131 ? 8.664   -12.545 20.288 1.00 93.19  ?  123 LEU A CB  1 
ATOM   832  C  CG  . LEU A 1 131 ? 9.416   -12.596 18.964 1.00 94.81  ?  123 LEU A CG  1 
ATOM   833  C  CD1 . LEU A 1 131 ? 9.139   -11.316 18.197 1.00 90.71  ?  123 LEU A CD1 1 
ATOM   834  C  CD2 . LEU A 1 131 ? 10.898  -12.783 19.202 1.00 104.13 ?  123 LEU A CD2 1 
ATOM   835  N  N   . ARG A 1 132 ? 6.681   -13.346 22.544 1.00 90.94  ?  124 ARG A N   1 
ATOM   836  C  CA  . ARG A 1 132 ? 6.072   -13.040 23.833 1.00 88.53  ?  124 ARG A CA  1 
ATOM   837  C  C   . ARG A 1 132 ? 6.295   -14.179 24.820 1.00 87.81  ?  124 ARG A C   1 
ATOM   838  O  O   . ARG A 1 132 ? 6.779   -13.963 25.938 1.00 85.87  ?  124 ARG A O   1 
ATOM   839  C  CB  . ARG A 1 132 ? 4.577   -12.763 23.667 1.00 90.20  ?  124 ARG A CB  1 
ATOM   840  C  CG  . ARG A 1 132 ? 3.920   -12.276 24.954 1.00 94.30  ?  124 ARG A CG  1 
ATOM   841  C  CD  . ARG A 1 132 ? 2.423   -12.023 24.806 1.00 92.85  ?  124 ARG A CD  1 
ATOM   842  N  NE  . ARG A 1 132 ? 1.851   -11.457 26.024 1.00 107.87 ?  124 ARG A NE  1 
ATOM   843  C  CZ  . ARG A 1 132 ? 1.530   -10.179 26.187 1.00 106.88 ?  124 ARG A CZ  1 
ATOM   844  N  NH1 . ARG A 1 132 ? 1.668   -9.299  25.210 1.00 116.07 ?  124 ARG A NH1 1 
ATOM   845  N  NH2 . ARG A 1 132 ? 1.053   -9.775  27.361 1.00 88.89  ?  124 ARG A NH2 1 
ATOM   846  N  N   . ASP A 1 133 ? 5.980   -15.411 24.409 1.00 86.65  ?  125 ASP A N   1 
ATOM   847  C  CA  . ASP A 1 133 ? 6.126   -16.548 25.311 1.00 84.06  ?  125 ASP A CA  1 
ATOM   848  C  C   . ASP A 1 133 ? 7.570   -16.733 25.759 1.00 85.13  ?  125 ASP A C   1 
ATOM   849  O  O   . ASP A 1 133 ? 7.816   -17.411 26.762 1.00 90.14  ?  125 ASP A O   1 
ATOM   850  C  CB  . ASP A 1 133 ? 5.623   -17.825 24.636 1.00 92.13  ?  125 ASP A CB  1 
ATOM   851  C  CG  . ASP A 1 133 ? 4.178   -17.715 24.180 1.00 102.72 ?  125 ASP A CG  1 
ATOM   852  O  OD1 . ASP A 1 133 ? 3.345   -17.198 24.953 1.00 101.97 ?  125 ASP A OD1 1 
ATOM   853  O  OD2 . ASP A 1 133 ? 3.880   -18.139 23.042 1.00 105.59 ?  125 ASP A OD2 1 
ATOM   854  N  N   . ALA A 1 134 ? 8.526   -16.154 25.034 1.00 92.77  ?  126 ALA A N   1 
ATOM   855  C  CA  . ALA A 1 134 ? 9.934   -16.246 25.394 1.00 91.04  ?  126 ALA A CA  1 
ATOM   856  C  C   . ALA A 1 134 ? 10.350  -15.143 26.362 1.00 88.00  ?  126 ALA A C   1 
ATOM   857  O  O   . ALA A 1 134 ? 10.885  -15.425 27.440 1.00 85.19  ?  126 ALA A O   1 
ATOM   858  C  CB  . ALA A 1 134 ? 10.801  -16.182 24.130 1.00 89.55  ?  126 ALA A CB  1 
ATOM   859  N  N   . VAL A 1 135 ? 10.089  -13.884 25.988 1.00 88.22  ?  127 VAL A N   1 
ATOM   860  C  CA  . VAL A 1 135 ? 10.636  -12.752 26.727 1.00 82.51  ?  127 VAL A CA  1 
ATOM   861  C  C   . VAL A 1 135 ? 9.783   -12.436 27.952 1.00 86.14  ?  127 VAL A C   1 
ATOM   862  O  O   . VAL A 1 135 ? 10.313  -12.181 29.042 1.00 88.56  ?  127 VAL A O   1 
ATOM   863  C  CB  . VAL A 1 135 ? 10.773  -11.537 25.795 1.00 81.37  ?  127 VAL A CB  1 
ATOM   864  C  CG1 . VAL A 1 135 ? 11.653  -11.887 24.598 1.00 78.77  ?  127 VAL A CG1 1 
ATOM   865  C  CG2 . VAL A 1 135 ? 9.406   -11.047 25.323 1.00 98.08  ?  127 VAL A CG2 1 
ATOM   866  N  N   . LEU A 1 136 ? 8.455   -12.432 27.799 1.00 86.16  ?  128 LEU A N   1 
ATOM   867  C  CA  . LEU A 1 136 ? 7.567   -12.163 28.923 1.00 86.23  ?  128 LEU A CA  1 
ATOM   868  C  C   . LEU A 1 136 ? 7.169   -13.423 29.682 1.00 82.83  ?  128 LEU A C   1 
ATOM   869  O  O   . LEU A 1 136 ? 6.722   -13.324 30.831 1.00 87.19  ?  128 LEU A O   1 
ATOM   870  C  CB  . LEU A 1 136 ? 6.294   -11.458 28.447 1.00 88.31  ?  128 LEU A CB  1 
ATOM   871  C  CG  . LEU A 1 136 ? 6.452   -10.062 27.848 1.00 83.90  ?  128 LEU A CG  1 
ATOM   872  C  CD1 . LEU A 1 136 ? 5.080   -9.467  27.527 1.00 90.62  ?  128 LEU A CD1 1 
ATOM   873  C  CD2 . LEU A 1 136 ? 7.233   -9.135  28.766 1.00 77.94  ?  128 LEU A CD2 1 
ATOM   874  N  N   . GLY A 1 137 ? 7.330   -14.598 29.077 1.00 83.59  ?  129 GLY A N   1 
ATOM   875  C  CA  . GLY A 1 137 ? 6.870   -15.806 29.727 1.00 82.57  ?  129 GLY A CA  1 
ATOM   876  C  C   . GLY A 1 137 ? 5.373   -15.760 29.931 1.00 88.43  ?  129 GLY A C   1 
ATOM   877  O  O   . GLY A 1 137 ? 4.610   -15.366 29.041 1.00 90.11  ?  129 GLY A O   1 
ATOM   878  N  N   . ASP A 1 138 ? 4.941   -16.144 31.132 1.00 85.36  ?  130 ASP A N   1 
ATOM   879  C  CA  . ASP A 1 138 ? 3.518   -16.205 31.439 1.00 81.93  ?  130 ASP A CA  1 
ATOM   880  C  C   . ASP A 1 138 ? 2.930   -14.859 31.846 1.00 77.48  ?  130 ASP A C   1 
ATOM   881  O  O   . ASP A 1 138 ? 1.721   -14.785 32.089 1.00 75.40  ?  130 ASP A O   1 
ATOM   882  C  CB  . ASP A 1 138 ? 3.265   -17.234 32.552 1.00 87.95  ?  130 ASP A CB  1 
ATOM   883  C  CG  . ASP A 1 138 ? 4.124   -16.993 33.792 1.00 95.83  ?  130 ASP A CG  1 
ATOM   884  O  OD1 . ASP A 1 138 ? 4.990   -16.094 33.766 1.00 95.49  ?  130 ASP A OD1 1 
ATOM   885  O  OD2 . ASP A 1 138 ? 3.932   -17.709 34.798 1.00 96.78  ?  130 ASP A OD2 1 
ATOM   886  N  N   . PHE A 1 139 ? 3.732   -13.797 31.915 1.00 77.93  ?  131 PHE A N   1 
ATOM   887  C  CA  . PHE A 1 139 ? 3.227   -12.514 32.389 1.00 75.66  ?  131 PHE A CA  1 
ATOM   888  C  C   . PHE A 1 139 ? 2.210   -11.944 31.406 1.00 78.09  ?  131 PHE A C   1 
ATOM   889  O  O   . PHE A 1 139 ? 2.521   -11.734 30.232 1.00 85.70  ?  131 PHE A O   1 
ATOM   890  C  CB  . PHE A 1 139 ? 4.373   -11.524 32.583 1.00 72.42  ?  131 PHE A CB  1 
ATOM   891  C  CG  . PHE A 1 139 ? 3.914   -10.136 32.934 1.00 68.15  ?  131 PHE A CG  1 
ATOM   892  C  CD1 . PHE A 1 139 ? 3.747   -9.767  34.256 1.00 59.64  ?  131 PHE A CD1 1 
ATOM   893  C  CD2 . PHE A 1 139 ? 3.636   -9.207  31.945 1.00 72.52  ?  131 PHE A CD2 1 
ATOM   894  C  CE1 . PHE A 1 139 ? 3.316   -8.496  34.585 1.00 59.15  ?  131 PHE A CE1 1 
ATOM   895  C  CE2 . PHE A 1 139 ? 3.203   -7.935  32.268 1.00 66.11  ?  131 PHE A CE2 1 
ATOM   896  C  CZ  . PHE A 1 139 ? 3.044   -7.580  33.589 1.00 57.06  ?  131 PHE A CZ  1 
ATOM   897  N  N   . ARG A 1 140 ? 1.011   -11.657 31.893 1.00 73.36  ?  132 ARG A N   1 
ATOM   898  C  CA  . ARG A 1 140 ? -0.067  -11.103 31.094 1.00 68.57  ?  132 ARG A CA  1 
ATOM   899  C  C   . ARG A 1 140 ? -0.783  -10.039 31.915 1.00 61.79  ?  132 ARG A C   1 
ATOM   900  O  O   . ARG A 1 140 ? -0.690  -10.032 33.147 1.00 70.80  ?  132 ARG A O   1 
ATOM   901  C  CB  . ARG A 1 140 ? -1.068  -12.186 30.665 1.00 70.35  ?  132 ARG A CB  1 
ATOM   902  C  CG  . ARG A 1 140 ? -0.450  -13.397 29.956 1.00 82.31  ?  132 ARG A CG  1 
ATOM   903  C  CD  . ARG A 1 140 ? -0.095  -13.092 28.498 1.00 88.34  ?  132 ARG A CD  1 
ATOM   904  N  NE  . ARG A 1 140 ? 0.526   -14.215 27.799 1.00 88.52  ?  132 ARG A NE  1 
ATOM   905  C  CZ  . ARG A 1 140 ? 1.830   -14.353 27.598 1.00 92.29  ?  132 ARG A CZ  1 
ATOM   906  N  NH1 . ARG A 1 140 ? 2.704   -13.482 28.078 1.00 92.43  ?  132 ARG A NH1 1 
ATOM   907  N  NH2 . ARG A 1 140 ? 2.270   -15.391 26.890 1.00 91.53  ?  132 ARG A NH2 1 
ATOM   908  N  N   . PRO A 1 141 ? -1.496  -9.124  31.259 1.00 60.99  ?  133 PRO A N   1 
ATOM   909  C  CA  . PRO A 1 141 ? -2.374  -8.219  32.011 1.00 63.78  ?  133 PRO A CA  1 
ATOM   910  C  C   . PRO A 1 141 ? -3.461  -9.005  32.726 1.00 56.73  ?  133 PRO A C   1 
ATOM   911  O  O   . PRO A 1 141 ? -3.882  -10.074 32.283 1.00 58.06  ?  133 PRO A O   1 
ATOM   912  C  CB  . PRO A 1 141 ? -2.958  -7.298  30.931 1.00 62.01  ?  133 PRO A CB  1 
ATOM   913  C  CG  . PRO A 1 141 ? -2.001  -7.394  29.785 1.00 62.44  ?  133 PRO A CG  1 
ATOM   914  C  CD  . PRO A 1 141 ? -1.481  -8.807  29.817 1.00 63.37  ?  133 PRO A CD  1 
ATOM   915  N  N   . HIS A 1 142 ? -3.898  -8.473  33.864 1.00 58.73  ?  134 HIS A N   1 
ATOM   916  C  CA  . HIS A 1 142 ? -4.976  -9.109  34.610 1.00 60.76  ?  134 HIS A CA  1 
ATOM   917  C  C   . HIS A 1 142 ? -6.326  -8.860  33.962 1.00 52.50  ?  134 HIS A C   1 
ATOM   918  O  O   . HIS A 1 142 ? -7.186  -9.746  33.958 1.00 50.89  ?  134 HIS A O   1 
ATOM   919  C  CB  . HIS A 1 142 ? -4.973  -8.607  36.046 1.00 59.15  ?  134 HIS A CB  1 
ATOM   920  C  CG  . HIS A 1 142 ? -3.752  -9.010  36.799 1.00 56.95  ?  134 HIS A CG  1 
ATOM   921  N  ND1 . HIS A 1 142 ? -2.515  -8.454  36.555 1.00 58.47  ?  134 HIS A ND1 1 
ATOM   922  C  CD2 . HIS A 1 142 ? -3.563  -9.952  37.752 1.00 70.95  ?  134 HIS A CD2 1 
ATOM   923  C  CE1 . HIS A 1 142 ? -1.622  -9.019  37.346 1.00 72.79  ?  134 HIS A CE1 1 
ATOM   924  N  NE2 . HIS A 1 142 ? -2.232  -9.928  38.084 1.00 81.79  ?  134 HIS A NE2 1 
ATOM   925  N  N   . LEU A 1 143 ? -6.529  -7.662  33.435 1.00 53.60  ?  135 LEU A N   1 
ATOM   926  C  CA  . LEU A 1 143 ? -7.700  -7.358  32.637 1.00 54.79  ?  135 LEU A CA  1 
ATOM   927  C  C   . LEU A 1 143 ? -7.241  -6.584  31.415 1.00 53.86  ?  135 LEU A C   1 
ATOM   928  O  O   . LEU A 1 143 ? -6.371  -5.713  31.509 1.00 54.97  ?  135 LEU A O   1 
ATOM   929  C  CB  . LEU A 1 143 ? -8.734  -6.548  33.419 1.00 53.11  ?  135 LEU A CB  1 
ATOM   930  C  CG  . LEU A 1 143 ? -10.044 -6.310  32.669 1.00 50.03  ?  135 LEU A CG  1 
ATOM   931  C  CD1 . LEU A 1 143 ? -10.753 -7.639  32.435 1.00 54.11  ?  135 LEU A CD1 1 
ATOM   932  C  CD2 . LEU A 1 143 ? -10.950 -5.346  33.408 1.00 55.30  ?  135 LEU A CD2 1 
ATOM   933  N  N   . THR A 1 144 ? -7.823  -6.918  30.269 1.00 55.91  ?  136 THR A N   1 
ATOM   934  C  CA  . THR A 1 144 ? -7.596  -6.181  29.034 1.00 56.66  ?  136 THR A CA  1 
ATOM   935  C  C   . THR A 1 144 ? -8.936  -5.667  28.543 1.00 49.86  ?  136 THR A C   1 
ATOM   936  O  O   . THR A 1 144 ? -9.844  -6.458  28.270 1.00 56.65  ?  136 THR A O   1 
ATOM   937  C  CB  . THR A 1 144 ? -6.936  -7.051  27.967 1.00 58.23  ?  136 THR A CB  1 
ATOM   938  O  OG1 . THR A 1 144 ? -5.802  -7.710  28.534 1.00 61.71  ?  136 THR A OG1 1 
ATOM   939  C  CG2 . THR A 1 144 ? -6.500  -6.186  26.799 1.00 62.30  ?  136 THR A CG2 1 
ATOM   940  N  N   . LEU A 1 145 ? -9.047  -4.354  28.426 1.00 52.23  ?  137 LEU A N   1 
ATOM   941  C  CA  . LEU A 1 145 ? -10.274 -3.684  28.020 1.00 55.25  ?  137 LEU A CA  1 
ATOM   942  C  C   . LEU A 1 145 ? -10.110 -3.281  26.562 1.00 54.20  ?  137 LEU A C   1 
ATOM   943  O  O   . LEU A 1 145 ? -9.335  -2.374  26.252 1.00 50.84  ?  137 LEU A O   1 
ATOM   944  C  CB  . LEU A 1 145 ? -10.515 -2.475  28.915 1.00 54.89  ?  137 LEU A CB  1 
ATOM   945  C  CG  . LEU A 1 145 ? -11.945 -1.993  29.137 1.00 59.78  ?  137 LEU A CG  1 
ATOM   946  C  CD1 . LEU A 1 145 ? -12.839 -2.336  27.966 1.00 64.55  ?  137 LEU A CD1 1 
ATOM   947  C  CD2 . LEU A 1 145 ? -12.478 -2.582  30.434 1.00 53.94  ?  137 LEU A CD2 1 
ATOM   948  N  N   . TYR A 1 146 ? -10.823 -3.962  25.669 1.00 58.80  ?  138 TYR A N   1 
ATOM   949  C  CA  . TYR A 1 146 ? -10.742 -3.673  24.245 1.00 63.64  ?  138 TYR A CA  1 
ATOM   950  C  C   . TYR A 1 146 ? -11.868 -2.725  23.860 1.00 59.90  ?  138 TYR A C   1 
ATOM   951  O  O   . TYR A 1 146 ? -13.045 -3.038  24.068 1.00 62.75  ?  138 TYR A O   1 
ATOM   952  C  CB  . TYR A 1 146 ? -10.828 -4.935  23.389 1.00 68.50  ?  138 TYR A CB  1 
ATOM   953  C  CG  . TYR A 1 146 ? -11.033 -4.611  21.924 1.00 69.53  ?  138 TYR A CG  1 
ATOM   954  C  CD1 . TYR A 1 146 ? -10.084 -3.881  21.218 1.00 67.27  ?  138 TYR A CD1 1 
ATOM   955  C  CD2 . TYR A 1 146 ? -12.176 -5.020  21.248 1.00 74.71  ?  138 TYR A CD2 1 
ATOM   956  C  CE1 . TYR A 1 146 ? -10.264 -3.571  19.882 1.00 63.38  ?  138 TYR A CE1 1 
ATOM   957  C  CE2 . TYR A 1 146 ? -12.361 -4.720  19.908 1.00 73.50  ?  138 TYR A CE2 1 
ATOM   958  C  CZ  . TYR A 1 146 ? -11.403 -3.996  19.231 1.00 68.17  ?  138 TYR A CZ  1 
ATOM   959  O  OH  . TYR A 1 146 ? -11.585 -3.695  17.900 1.00 68.02  ?  138 TYR A OH  1 
ATOM   960  N  N   . LEU A 1 147 ? -11.507 -1.581  23.293 1.00 57.36  ?  139 LEU A N   1 
ATOM   961  C  CA  . LEU A 1 147 ? -12.478 -0.601  22.827 1.00 61.86  ?  139 LEU A CA  1 
ATOM   962  C  C   . LEU A 1 147 ? -12.727 -0.865  21.351 1.00 63.67  ?  139 LEU A C   1 
ATOM   963  O  O   . LEU A 1 147 ? -11.874 -0.572  20.507 1.00 70.38  ?  139 LEU A O   1 
ATOM   964  C  CB  . LEU A 1 147 ? -11.971 0.813   23.060 1.00 72.86  ?  139 LEU A CB  1 
ATOM   965  C  CG  . LEU A 1 147 ? -11.730 1.194   24.520 1.00 58.60  ?  139 LEU A CG  1 
ATOM   966  C  CD1 . LEU A 1 147 ? -11.273 2.643   24.548 1.00 65.66  ?  139 LEU A CD1 1 
ATOM   967  C  CD2 . LEU A 1 147 ? -12.959 0.985   25.373 1.00 65.87  ?  139 LEU A CD2 1 
ATOM   968  N  N   . ASP A 1 148 ? -13.881 -1.444  21.049 1.00 65.21  ?  140 ASP A N   1 
ATOM   969  C  CA  . ASP A 1 148 ? -14.245 -1.723  19.673 1.00 68.26  ?  140 ASP A CA  1 
ATOM   970  C  C   . ASP A 1 148 ? -14.778 -0.458  19.018 1.00 65.49  ?  140 ASP A C   1 
ATOM   971  O  O   . ASP A 1 148 ? -15.527 0.308   19.631 1.00 58.91  ?  140 ASP A O   1 
ATOM   972  C  CB  . ASP A 1 148 ? -15.292 -2.832  19.622 1.00 66.63  ?  140 ASP A CB  1 
ATOM   973  C  CG  . ASP A 1 148 ? -15.664 -3.210  18.213 1.00 67.14  ?  140 ASP A CG  1 
ATOM   974  O  OD1 . ASP A 1 148 ? -14.746 -3.484  17.418 1.00 73.27  ?  140 ASP A OD1 1 
ATOM   975  O  OD2 . ASP A 1 148 ? -16.875 -3.240  17.909 1.00 73.48  ?  140 ASP A OD2 1 
ATOM   976  N  N   . VAL A 1 149 ? -14.358 -0.220  17.781 1.00 68.34  ?  141 VAL A N   1 
ATOM   977  C  CA  . VAL A 1 149 ? -14.932 0.828   16.950 1.00 70.44  ?  141 VAL A CA  1 
ATOM   978  C  C   . VAL A 1 149 ? -15.210 0.234   15.579 1.00 75.03  ?  141 VAL A C   1 
ATOM   979  O  O   . VAL A 1 149 ? -14.407 -0.542  15.050 1.00 79.09  ?  141 VAL A O   1 
ATOM   980  C  CB  . VAL A 1 149 ? -14.023 2.069   16.831 1.00 72.60  ?  141 VAL A CB  1 
ATOM   981  C  CG1 . VAL A 1 149 ? -14.135 2.917   18.091 1.00 76.12  ?  141 VAL A CG1 1 
ATOM   982  C  CG2 . VAL A 1 149 ? -12.586 1.664   16.573 1.00 78.13  ?  141 VAL A CG2 1 
ATOM   983  N  N   . THR A 1 150 ? -16.348 0.593   15.015 1.00 80.76  ?  142 THR A N   1 
ATOM   984  C  CA  . THR A 1 150 ? -16.781 0.089   13.727 1.00 81.74  ?  142 THR A CA  1 
ATOM   985  C  C   . THR A 1 150 ? -16.081 0.822   12.589 1.00 80.32  ?  142 THR A C   1 
ATOM   986  O  O   . THR A 1 150 ? -15.515 1.902   12.782 1.00 80.05  ?  142 THR A O   1 
ATOM   987  C  CB  . THR A 1 150 ? -18.289 0.260   13.599 1.00 83.40  ?  142 THR A CB  1 
ATOM   988  O  OG1 . THR A 1 150 ? -18.591 1.661   13.605 1.00 83.83  ?  142 THR A OG1 1 
ATOM   989  C  CG2 . THR A 1 150 ? -18.996 -0.419  14.762 1.00 75.37  ?  142 THR A CG2 1 
ATOM   990  N  N   . PRO A 1 151 ? -16.115 0.250   11.382 1.00 85.35  ?  143 PRO A N   1 
ATOM   991  C  CA  . PRO A 1 151 ? -15.441 0.908   10.249 1.00 84.61  ?  143 PRO A CA  1 
ATOM   992  C  C   . PRO A 1 151 ? -15.943 2.313   9.965  1.00 82.88  ?  143 PRO A C   1 
ATOM   993  O  O   . PRO A 1 151 ? -15.145 3.179   9.585  1.00 82.81  ?  143 PRO A O   1 
ATOM   994  C  CB  . PRO A 1 151 ? -15.728 -0.038  9.070  1.00 83.20  ?  143 PRO A CB  1 
ATOM   995  C  CG  . PRO A 1 151 ? -16.050 -1.350  9.695  1.00 89.74  ?  143 PRO A CG  1 
ATOM   996  C  CD  . PRO A 1 151 ? -16.713 -1.044  11.008 1.00 86.26  ?  143 PRO A CD  1 
ATOM   997  N  N   . GLU A 1 152 ? -17.244 2.570   10.119 1.00 79.31  ?  144 GLU A N   1 
ATOM   998  C  CA  . GLU A 1 152 ? -17.730 3.937   9.964  1.00 81.10  ?  144 GLU A CA  1 
ATOM   999  C  C   . GLU A 1 152 ? -17.028 4.860   10.951 1.00 87.01  ?  144 GLU A C   1 
ATOM   1000 O  O   . GLU A 1 152 ? -16.504 5.913   10.573 1.00 89.98  ?  144 GLU A O   1 
ATOM   1001 C  CB  . GLU A 1 152 ? -19.248 3.996   10.151 1.00 81.86  ?  144 GLU A CB  1 
ATOM   1002 C  CG  . GLU A 1 152 ? -19.992 4.788   9.058  1.00 84.30  ?  144 GLU A CG  1 
ATOM   1003 C  CD  . GLU A 1 152 ? -20.387 6.201   9.482  1.00 101.20 ?  144 GLU A CD  1 
ATOM   1004 O  OE1 . GLU A 1 152 ? -20.748 6.394   10.660 1.00 108.71 ?  144 GLU A OE1 1 
ATOM   1005 O  OE2 . GLU A 1 152 ? -20.345 7.119   8.630  1.00 103.96 ?  144 GLU A OE2 1 
ATOM   1006 N  N   . VAL A 1 153 ? -16.971 4.459   12.224 1.00 86.37  ?  145 VAL A N   1 
ATOM   1007 C  CA  . VAL A 1 153 ? -16.375 5.327   13.235 1.00 87.25  ?  145 VAL A CA  1 
ATOM   1008 C  C   . VAL A 1 153 ? -14.923 5.621   12.894 1.00 91.94  ?  145 VAL A C   1 
ATOM   1009 O  O   . VAL A 1 153 ? -14.477 6.773   12.971 1.00 96.73  ?  145 VAL A O   1 
ATOM   1010 C  CB  . VAL A 1 153 ? -16.514 4.698   14.633 1.00 87.62  ?  145 VAL A CB  1 
ATOM   1011 C  CG1 . VAL A 1 153 ? -15.647 5.439   15.637 1.00 86.47  ?  145 VAL A CG1 1 
ATOM   1012 C  CG2 . VAL A 1 153 ? -17.971 4.709   15.065 1.00 90.41  ?  145 VAL A CG2 1 
ATOM   1013 N  N   . GLY A 1 154 ? -14.172 4.599   12.489 1.00 89.06  ?  146 GLY A N   1 
ATOM   1014 C  CA  . GLY A 1 154 ? -12.794 4.829   12.093 1.00 89.90  ?  146 GLY A CA  1 
ATOM   1015 C  C   . GLY A 1 154 ? -12.679 5.824   10.954 1.00 99.96  ?  146 GLY A C   1 
ATOM   1016 O  O   . GLY A 1 154 ? -11.741 6.623   10.910 1.00 105.93 ?  146 GLY A O   1 
ATOM   1017 N  N   . LEU A 1 155 ? -13.628 5.784   10.014 1.00 97.51  ?  147 LEU A N   1 
ATOM   1018 C  CA  . LEU A 1 155 ? -13.585 6.698   8.879  1.00 92.78  ?  147 LEU A CA  1 
ATOM   1019 C  C   . LEU A 1 155 ? -13.872 8.136   9.294  1.00 94.80  ?  147 LEU A C   1 
ATOM   1020 O  O   . LEU A 1 155 ? -13.296 9.066   8.717  1.00 100.56 ?  147 LEU A O   1 
ATOM   1021 C  CB  . LEU A 1 155 ? -14.577 6.239   7.807  1.00 102.10 ?  147 LEU A CB  1 
ATOM   1022 C  CG  . LEU A 1 155 ? -14.172 5.039   6.948  1.00 103.49 ?  147 LEU A CG  1 
ATOM   1023 C  CD1 . LEU A 1 155 ? -15.319 4.625   6.025  1.00 92.83  ?  147 LEU A CD1 1 
ATOM   1024 C  CD2 . LEU A 1 155 ? -12.918 5.344   6.137  1.00 83.97  ?  147 LEU A CD2 1 
ATOM   1025 N  N   . LYS A 1 156 ? -14.751 8.343   10.275 1.00 91.26  ?  148 LYS A N   1 
ATOM   1026 C  CA  . LYS A 1 156 ? -14.987 9.695   10.771 1.00 103.24 ?  148 LYS A CA  1 
ATOM   1027 C  C   . LYS A 1 156 ? -13.724 10.273  11.397 1.00 109.38 ?  148 LYS A C   1 
ATOM   1028 O  O   . LYS A 1 156 ? -13.399 11.449  11.194 1.00 115.89 ?  148 LYS A O   1 
ATOM   1029 C  CB  . LYS A 1 156 ? -16.122 9.690   11.795 1.00 103.67 ?  148 LYS A CB  1 
ATOM   1030 C  CG  . LYS A 1 156 ? -17.484 9.301   11.241 1.00 104.69 ?  148 LYS A CG  1 
ATOM   1031 C  CD  . LYS A 1 156 ? -18.378 8.745   12.347 1.00 107.71 ?  148 LYS A CD  1 
ATOM   1032 C  CE  . LYS A 1 156 ? -19.836 9.130   12.150 1.00 100.44 ?  148 LYS A CE  1 
ATOM   1033 N  NZ  . LYS A 1 156 ? -20.746 8.164   12.831 1.00 84.93  ?  148 LYS A NZ  1 
ATOM   1034 N  N   . ARG A 1 157 ? -13.000 9.456   12.163 1.00 100.32 ?  149 ARG A N   1 
ATOM   1035 C  CA  . ARG A 1 157 ? -11.812 9.937   12.857 1.00 105.62 ?  149 ARG A CA  1 
ATOM   1036 C  C   . ARG A 1 157 ? -10.650 10.165  11.901 1.00 115.34 ?  149 ARG A C   1 
ATOM   1037 O  O   . ARG A 1 157 ? -9.826  11.056  12.135 1.00 126.65 ?  149 ARG A O   1 
ATOM   1038 C  CB  . ARG A 1 157 ? -11.419 8.939   13.945 1.00 105.92 ?  149 ARG A CB  1 
ATOM   1039 C  CG  . ARG A 1 157 ? -12.566 8.536   14.852 1.00 113.44 ?  149 ARG A CG  1 
ATOM   1040 C  CD  . ARG A 1 157 ? -13.148 9.733   15.589 1.00 112.88 ?  149 ARG A CD  1 
ATOM   1041 N  NE  . ARG A 1 157 ? -14.110 9.313   16.600 1.00 110.53 ?  149 ARG A NE  1 
ATOM   1042 C  CZ  . ARG A 1 157 ? -15.393 9.078   16.363 1.00 110.39 ?  149 ARG A CZ  1 
ATOM   1043 N  NH1 . ARG A 1 157 ? -15.908 9.209   15.151 1.00 126.86 ?  149 ARG A NH1 1 
ATOM   1044 N  NH2 . ARG A 1 157 ? -16.181 8.704   17.367 1.00 104.85 ?  149 ARG A NH2 1 
ATOM   1045 N  N   . ALA A 1 158 ? -10.560 9.374   10.830 1.00 120.57 ?  150 ALA A N   1 
ATOM   1046 C  CA  . ALA A 1 158 ? -9.473  9.552   9.874  1.00 124.90 ?  150 ALA A CA  1 
ATOM   1047 C  C   . ALA A 1 158 ? -9.556  10.915  9.197  1.00 119.63 ?  150 ALA A C   1 
ATOM   1048 O  O   . ALA A 1 158 ? -8.532  11.574  8.982  1.00 109.04 ?  150 ALA A O   1 
ATOM   1049 C  CB  . ALA A 1 158 ? -9.496  8.431   8.836  1.00 109.08 ?  150 ALA A CB  1 
ATOM   1050 N  N   . ARG A 1 159 ? -10.770 11.356  8.854  1.00 111.06 ?  151 ARG A N   1 
ATOM   1051 C  CA  . ARG A 1 159 ? -10.933 12.666  8.230  1.00 108.53 ?  151 ARG A CA  1 
ATOM   1052 C  C   . ARG A 1 159 ? -10.360 13.764  9.119  1.00 107.86 ?  151 ARG A C   1 
ATOM   1053 O  O   . ARG A 1 159 ? -9.646  14.655  8.644  1.00 118.93 ?  151 ARG A O   1 
ATOM   1054 C  CB  . ARG A 1 159 ? -12.413 12.923  7.936  1.00 104.97 ?  151 ARG A CB  1 
ATOM   1055 C  CG  . ARG A 1 159 ? -12.984 12.064  6.813  1.00 103.03 ?  151 ARG A CG  1 
ATOM   1056 C  CD  . ARG A 1 159 ? -14.509 12.114  6.772  1.00 103.10 ?  151 ARG A CD  1 
ATOM   1057 N  NE  . ARG A 1 159 ? -15.026 13.458  6.543  1.00 106.98 ?  151 ARG A NE  1 
ATOM   1058 C  CZ  . ARG A 1 159 ? -16.315 13.767  6.497  1.00 109.24 ?  151 ARG A CZ  1 
ATOM   1059 N  NH1 . ARG A 1 159 ? -17.253 12.850  6.667  1.00 109.83 ?  151 ARG A NH1 1 
ATOM   1060 N  NH2 . ARG A 1 159 ? -16.672 15.029  6.274  1.00 109.40 ?  151 ARG A NH2 1 
ATOM   1061 N  N   . ALA A 1 160 ? -10.653 13.710  10.414 1.00 115.77 ?  152 ALA A N   1 
ATOM   1062 C  CA  . ALA A 1 160 ? -10.129 14.692  11.356 1.00 116.13 ?  152 ALA A CA  1 
ATOM   1063 C  C   . ALA A 1 160 ? -8.611  14.570  11.464 1.00 118.54 ?  152 ALA A C   1 
ATOM   1064 O  O   . ALA A 1 160 ? -8.083  14.179  12.505 1.00 124.31 ?  152 ALA A O   1 
ATOM   1065 C  CB  . ALA A 1 160 ? -10.775 14.517  12.720 1.00 138.59 ?  152 ALA A CB  1 
ATOM   1066 N  N   . ASP A 1 173 ? -9.976  -1.084  3.599  1.00 98.04  ?  165 ASP A N   1 
ATOM   1067 C  CA  . ASP A 1 173 ? -9.986  -1.180  5.050  1.00 105.29 ?  165 ASP A CA  1 
ATOM   1068 C  C   . ASP A 1 173 ? -9.251  -2.417  5.572  1.00 104.41 ?  165 ASP A C   1 
ATOM   1069 O  O   . ASP A 1 173 ? -9.879  -3.384  6.007  1.00 105.53 ?  165 ASP A O   1 
ATOM   1070 C  CB  . ASP A 1 173 ? -11.434 -1.198  5.579  1.00 97.11  ?  165 ASP A CB  1 
ATOM   1071 C  CG  . ASP A 1 173 ? -11.985 0.195   5.864  1.00 95.61  ?  165 ASP A CG  1 
ATOM   1072 O  OD1 . ASP A 1 173 ? -11.262 1.185   5.637  1.00 90.66  ?  165 ASP A OD1 1 
ATOM   1073 O  OD2 . ASP A 1 173 ? -13.144 0.300   6.325  1.00 89.60  ?  165 ASP A OD2 1 
ATOM   1074 N  N   . PHE A 1 174 ? -7.914  -2.378  5.546  1.00 114.26 ?  166 PHE A N   1 
ATOM   1075 C  CA  . PHE A 1 174 ? -7.136  -3.389  6.251  1.00 114.57 ?  166 PHE A CA  1 
ATOM   1076 C  C   . PHE A 1 174 ? -7.551  -3.492  7.713  1.00 116.39 ?  166 PHE A C   1 
ATOM   1077 O  O   . PHE A 1 174 ? -7.316  -4.520  8.357  1.00 110.12 ?  166 PHE A O   1 
ATOM   1078 C  CB  . PHE A 1 174 ? -5.651  -3.043  6.227  1.00 116.67 ?  166 PHE A CB  1 
ATOM   1079 C  CG  . PHE A 1 174 ? -5.200  -2.297  7.458  1.00 123.01 ?  166 PHE A CG  1 
ATOM   1080 C  CD1 . PHE A 1 174 ? -5.491  -0.950  7.612  1.00 127.62 ?  166 PHE A CD1 1 
ATOM   1081 C  CD2 . PHE A 1 174 ? -4.512  -2.948  8.472  1.00 120.39 ?  166 PHE A CD2 1 
ATOM   1082 C  CE1 . PHE A 1 174 ? -5.091  -0.262  8.746  1.00 132.01 ?  166 PHE A CE1 1 
ATOM   1083 C  CE2 . PHE A 1 174 ? -4.108  -2.263  9.609  1.00 122.75 ?  166 PHE A CE2 1 
ATOM   1084 C  CZ  . PHE A 1 174 ? -4.399  -0.919  9.744  1.00 129.70 ?  166 PHE A CZ  1 
ATOM   1085 N  N   . PHE A 1 175 ? -8.130  -2.416  8.249  1.00 107.33 ?  167 PHE A N   1 
ATOM   1086 C  CA  . PHE A 1 175 ? -8.466  -2.312  9.666  1.00 96.35  ?  167 PHE A CA  1 
ATOM   1087 C  C   . PHE A 1 175 ? -9.491  -3.353  10.082 1.00 93.84  ?  167 PHE A C   1 
ATOM   1088 O  O   . PHE A 1 175 ? -9.498  -3.770  11.243 1.00 97.04  ?  167 PHE A O   1 
ATOM   1089 C  CB  . PHE A 1 175 ? -8.902  -0.849  9.904  1.00 97.62  ?  167 PHE A CB  1 
ATOM   1090 C  CG  . PHE A 1 175 ? -10.168 -0.669  10.701 1.00 95.88  ?  167 PHE A CG  1 
ATOM   1091 C  CD1 . PHE A 1 175 ? -11.392 -1.145  10.251 1.00 96.29  ?  167 PHE A CD1 1 
ATOM   1092 C  CD2 . PHE A 1 175 ? -10.139 0.062   11.876 1.00 100.21 ?  167 PHE A CD2 1 
ATOM   1093 C  CE1 . PHE A 1 175 ? -12.539 -0.954  10.998 1.00 98.84  ?  167 PHE A CE1 1 
ATOM   1094 C  CE2 . PHE A 1 175 ? -11.284 0.267   12.619 1.00 97.94  ?  167 PHE A CE2 1 
ATOM   1095 C  CZ  . PHE A 1 175 ? -12.485 -0.239  12.178 1.00 92.46  ?  167 PHE A CZ  1 
ATOM   1096 N  N   . ASN A 1 176 ? -10.337 -3.808  9.158  1.00 97.75  ?  168 ASN A N   1 
ATOM   1097 C  CA  . ASN A 1 176 ? -11.326 -4.820  9.513  1.00 91.69  ?  168 ASN A CA  1 
ATOM   1098 C  C   . ASN A 1 176 ? -10.672 -6.142  9.884  1.00 86.11  ?  168 ASN A C   1 
ATOM   1099 O  O   . ASN A 1 176 ? -11.244 -6.924  10.653 1.00 77.87  ?  168 ASN A O   1 
ATOM   1100 C  CB  . ASN A 1 176 ? -12.303 -5.028  8.360  1.00 88.99  ?  168 ASN A CB  1 
ATOM   1101 C  CG  . ASN A 1 176 ? -13.339 -3.936  8.282  1.00 90.61  ?  168 ASN A CG  1 
ATOM   1102 O  OD1 . ASN A 1 176 ? -13.827 -3.464  9.306  1.00 88.77  ?  168 ASN A OD1 1 
ATOM   1103 N  ND2 . ASN A 1 176 ? -13.675 -3.518  7.067  1.00 98.26  ?  168 ASN A ND2 1 
ATOM   1104 N  N   . ARG A 1 177 ? -9.488  -6.426  9.343  1.00 92.58  ?  169 ARG A N   1 
ATOM   1105 C  CA  . ARG A 1 177 ? -8.809  -7.664  9.707  1.00 95.42  ?  169 ARG A CA  1 
ATOM   1106 C  C   . ARG A 1 177 ? -8.238  -7.578  11.121 1.00 88.02  ?  169 ARG A C   1 
ATOM   1107 O  O   . ARG A 1 177 ? -8.393  -8.506  11.921 1.00 86.03  ?  169 ARG A O   1 
ATOM   1108 C  CB  . ARG A 1 177 ? -7.716  -7.983  8.694  1.00 93.43  ?  169 ARG A CB  1 
ATOM   1109 C  CG  . ARG A 1 177 ? -7.151  -9.383  8.828  1.00 99.20  ?  169 ARG A CG  1 
ATOM   1110 C  CD  . ARG A 1 177 ? -6.124  -9.642  7.746  1.00 111.80 ?  169 ARG A CD  1 
ATOM   1111 N  NE  . ARG A 1 177 ? -6.753  -9.842  6.448  1.00 120.45 ?  169 ARG A NE  1 
ATOM   1112 C  CZ  . ARG A 1 177 ? -6.811  -11.006 5.816  1.00 126.66 ?  169 ARG A CZ  1 
ATOM   1113 N  NH1 . ARG A 1 177 ? -6.237  -12.091 6.310  1.00 127.09 ?  169 ARG A NH1 1 
ATOM   1114 N  NH2 . ARG A 1 177 ? -7.453  -11.081 4.654  1.00 127.96 ?  169 ARG A NH2 1 
ATOM   1115 N  N   . THR A 1 178 ? -7.576  -6.464  11.454 1.00 90.15  ?  170 THR A N   1 
ATOM   1116 C  CA  . THR A 1 178 ? -7.068  -6.298  12.814 1.00 91.60  ?  170 THR A CA  1 
ATOM   1117 C  C   . THR A 1 178 ? -8.219  -6.291  13.811 1.00 87.15  ?  170 THR A C   1 
ATOM   1118 O  O   . THR A 1 178 ? -8.176  -6.971  14.845 1.00 83.05  ?  170 THR A O   1 
ATOM   1119 C  CB  . THR A 1 178 ? -6.260  -5.004  12.938 1.00 98.97  ?  170 THR A CB  1 
ATOM   1120 O  OG1 . THR A 1 178 ? -7.080  -3.887  12.571 1.00 103.44 ?  170 THR A OG1 1 
ATOM   1121 C  CG2 . THR A 1 178 ? -5.031  -5.047  12.051 1.00 90.50  ?  170 THR A CG2 1 
ATOM   1122 N  N   . ARG A 1 179 ? -9.267  -5.525  13.500 1.00 86.39  ?  171 ARG A N   1 
ATOM   1123 C  CA  . ARG A 1 179 ? -10.469 -5.536  14.322 1.00 82.17  ?  171 ARG A CA  1 
ATOM   1124 C  C   . ARG A 1 179 ? -10.969 -6.953  14.546 1.00 80.38  ?  171 ARG A C   1 
ATOM   1125 O  O   . ARG A 1 179 ? -11.387 -7.306  15.655 1.00 84.18  ?  171 ARG A O   1 
ATOM   1126 C  CB  . ARG A 1 179 ? -11.547 -4.694  13.647 1.00 85.92  ?  171 ARG A CB  1 
ATOM   1127 C  CG  . ARG A 1 179 ? -12.869 -4.725  14.357 1.00 85.07  ?  171 ARG A CG  1 
ATOM   1128 C  CD  . ARG A 1 179 ? -13.779 -3.639  13.831 1.00 88.26  ?  171 ARG A CD  1 
ATOM   1129 N  NE  . ARG A 1 179 ? -14.998 -3.553  14.622 1.00 78.91  ?  171 ARG A NE  1 
ATOM   1130 C  CZ  . ARG A 1 179 ? -16.198 -3.938  14.204 1.00 77.25  ?  171 ARG A CZ  1 
ATOM   1131 N  NH1 . ARG A 1 179 ? -16.391 -4.393  12.975 1.00 83.07  ?  171 ARG A NH1 1 
ATOM   1132 N  NH2 . ARG A 1 179 ? -17.230 -3.855  15.037 1.00 77.10  ?  171 ARG A NH2 1 
ATOM   1133 N  N   . ALA A 1 180 ? -10.941 -7.779  13.501 1.00 83.18  ?  172 ALA A N   1 
ATOM   1134 C  CA  . ALA A 1 180 ? -11.409 -9.152  13.645 1.00 82.36  ?  172 ALA A CA  1 
ATOM   1135 C  C   . ALA A 1 180 ? -10.551 -9.926  14.636 1.00 84.66  ?  172 ALA A C   1 
ATOM   1136 O  O   . ALA A 1 180 ? -11.078 -10.666 15.475 1.00 87.73  ?  172 ALA A O   1 
ATOM   1137 C  CB  . ALA A 1 180 ? -11.425 -9.847  12.283 1.00 76.51  ?  172 ALA A CB  1 
ATOM   1138 N  N   . ARG A 1 181 ? -9.227  -9.765  14.563 1.00 83.27  ?  173 ARG A N   1 
ATOM   1139 C  CA  . ARG A 1 181 ? -8.349  -10.498 15.470 1.00 84.96  ?  173 ARG A CA  1 
ATOM   1140 C  C   . ARG A 1 181 ? -8.642  -10.133 16.919 1.00 86.14  ?  173 ARG A C   1 
ATOM   1141 O  O   . ARG A 1 181 ? -8.799  -11.013 17.774 1.00 87.44  ?  173 ARG A O   1 
ATOM   1142 C  CB  . ARG A 1 181 ? -6.885  -10.218 15.136 1.00 86.84  ?  173 ARG A CB  1 
ATOM   1143 C  CG  . ARG A 1 181 ? -5.908  -11.194 15.783 1.00 84.87  ?  173 ARG A CG  1 
ATOM   1144 C  CD  . ARG A 1 181 ? -4.464  -10.728 15.634 1.00 87.89  ?  173 ARG A CD  1 
ATOM   1145 N  NE  . ARG A 1 181 ? -4.097  -9.736  16.639 1.00 96.52  ?  173 ARG A NE  1 
ATOM   1146 C  CZ  . ARG A 1 181 ? -3.404  -9.997  17.740 1.00 106.33 ?  173 ARG A CZ  1 
ATOM   1147 N  NH1 . ARG A 1 181 ? -2.965  -11.216 18.010 1.00 102.93 ?  173 ARG A NH1 1 
ATOM   1148 N  NH2 . ARG A 1 181 ? -3.139  -9.008  18.589 1.00 112.06 ?  173 ARG A NH2 1 
ATOM   1149 N  N   . TYR A 1 182 ? -8.725  -8.832  17.214 1.00 81.44  ?  174 TYR A N   1 
ATOM   1150 C  CA  . TYR A 1 182 ? -9.087  -8.406  18.561 1.00 83.56  ?  174 TYR A CA  1 
ATOM   1151 C  C   . TYR A 1 182 ? -10.364 -9.101  19.019 1.00 83.16  ?  174 TYR A C   1 
ATOM   1152 O  O   . TYR A 1 182 ? -10.471 -9.543  20.170 1.00 85.11  ?  174 TYR A O   1 
ATOM   1153 C  CB  . TYR A 1 182 ? -9.287  -6.892  18.603 1.00 77.93  ?  174 TYR A CB  1 
ATOM   1154 C  CG  . TYR A 1 182 ? -8.037  -6.047  18.738 1.00 80.29  ?  174 TYR A CG  1 
ATOM   1155 C  CD1 . TYR A 1 182 ? -6.937  -6.483  19.465 1.00 85.69  ?  174 TYR A CD1 1 
ATOM   1156 C  CD2 . TYR A 1 182 ? -7.974  -4.793  18.148 1.00 78.23  ?  174 TYR A CD2 1 
ATOM   1157 C  CE1 . TYR A 1 182 ? -5.806  -5.694  19.589 1.00 79.59  ?  174 TYR A CE1 1 
ATOM   1158 C  CE2 . TYR A 1 182 ? -6.855  -3.999  18.270 1.00 76.20  ?  174 TYR A CE2 1 
ATOM   1159 C  CZ  . TYR A 1 182 ? -5.773  -4.452  18.987 1.00 81.64  ?  174 TYR A CZ  1 
ATOM   1160 O  OH  . TYR A 1 182 ? -4.657  -3.655  19.100 1.00 86.69  ?  174 TYR A OH  1 
ATOM   1161 N  N   . LEU A 1 183 ? -11.351 -9.202  18.124 1.00 81.80  ?  175 LEU A N   1 
ATOM   1162 C  CA  . LEU A 1 183 ? -12.640 -9.774  18.495 1.00 83.22  ?  175 LEU A CA  1 
ATOM   1163 C  C   . LEU A 1 183 ? -12.551 -11.282 18.707 1.00 81.22  ?  175 LEU A C   1 
ATOM   1164 O  O   . LEU A 1 183 ? -13.334 -11.841 19.485 1.00 78.70  ?  175 LEU A O   1 
ATOM   1165 C  CB  . LEU A 1 183 ? -13.684 -9.436  17.428 1.00 87.86  ?  175 LEU A CB  1 
ATOM   1166 C  CG  . LEU A 1 183 ? -14.216 -8.003  17.402 1.00 79.03  ?  175 LEU A CG  1 
ATOM   1167 C  CD1 . LEU A 1 183 ? -15.088 -7.753  16.181 1.00 81.39  ?  175 LEU A CD1 1 
ATOM   1168 C  CD2 . LEU A 1 183 ? -15.011 -7.707  18.665 1.00 80.62  ?  175 LEU A CD2 1 
ATOM   1169 N  N   . GLU A 1 184 ? -11.626 -11.960 18.023 1.00 83.33  ?  176 GLU A N   1 
ATOM   1170 C  CA  . GLU A 1 184 ? -11.425 -13.383 18.287 1.00 86.10  ?  176 GLU A CA  1 
ATOM   1171 C  C   . GLU A 1 184 ? -10.790 -13.593 19.656 1.00 89.90  ?  176 GLU A C   1 
ATOM   1172 O  O   . GLU A 1 184 ? -11.258 -14.412 20.456 1.00 90.95  ?  176 GLU A O   1 
ATOM   1173 C  CB  . GLU A 1 184 ? -10.553 -14.008 17.198 1.00 90.61  ?  176 GLU A CB  1 
ATOM   1174 C  CG  . GLU A 1 184 ? -10.389 -15.516 17.337 1.00 107.61 ?  176 GLU A CG  1 
ATOM   1175 C  CD  . GLU A 1 184 ? -9.262  -16.071 16.484 1.00 122.03 ?  176 GLU A CD  1 
ATOM   1176 O  OE1 . GLU A 1 184 ? -8.630  -15.290 15.740 1.00 119.39 ?  176 GLU A OE1 1 
ATOM   1177 O  OE2 . GLU A 1 184 ? -9.003  -17.292 16.561 1.00 125.68 ?  176 GLU A OE2 1 
ATOM   1178 N  N   . LEU A 1 185 ? -9.725  -12.843 19.942 1.00 92.11  ?  177 LEU A N   1 
ATOM   1179 C  CA  . LEU A 1 185 ? -9.059  -12.948 21.236 1.00 92.49  ?  177 LEU A CA  1 
ATOM   1180 C  C   . LEU A 1 185 ? -10.019 -12.638 22.377 1.00 84.11  ?  177 LEU A C   1 
ATOM   1181 O  O   . LEU A 1 185 ? -9.921  -13.224 23.462 1.00 81.78  ?  177 LEU A O   1 
ATOM   1182 C  CB  . LEU A 1 185 ? -7.863  -12.002 21.275 1.00 96.66  ?  177 LEU A CB  1 
ATOM   1183 C  CG  . LEU A 1 185 ? -6.759  -12.310 20.267 1.00 88.73  ?  177 LEU A CG  1 
ATOM   1184 C  CD1 . LEU A 1 185 ? -5.746  -11.180 20.240 1.00 103.86 ?  177 LEU A CD1 1 
ATOM   1185 C  CD2 . LEU A 1 185 ? -6.092  -13.631 20.609 1.00 76.67  ?  177 LEU A CD2 1 
ATOM   1186 N  N   . ALA A 1 186 ? -10.941 -11.695 22.164 1.00 83.11  ?  178 ALA A N   1 
ATOM   1187 C  CA  . ALA A 1 186 ? -11.896 -11.362 23.218 1.00 84.83  ?  178 ALA A CA  1 
ATOM   1188 C  C   . ALA A 1 186 ? -12.824 -12.537 23.511 1.00 85.20  ?  178 ALA A C   1 
ATOM   1189 O  O   . ALA A 1 186 ? -13.174 -12.787 24.670 1.00 88.59  ?  178 ALA A O   1 
ATOM   1190 C  CB  . ALA A 1 186 ? -12.699 -10.121 22.830 1.00 87.87  ?  178 ALA A CB  1 
ATOM   1191 N  N   . ALA A 1 187 ? -13.240 -13.266 22.473 1.00 84.60  ?  179 ALA A N   1 
ATOM   1192 C  CA  . ALA A 1 187 ? -14.115 -14.414 22.686 1.00 88.86  ?  179 ALA A CA  1 
ATOM   1193 C  C   . ALA A 1 187 ? -13.374 -15.557 23.369 1.00 86.46  ?  179 ALA A C   1 
ATOM   1194 O  O   . ALA A 1 187 ? -13.939 -16.243 24.229 1.00 91.38  ?  179 ALA A O   1 
ATOM   1195 C  CB  . ALA A 1 187 ? -14.707 -14.878 21.355 1.00 93.02  ?  179 ALA A CB  1 
ATOM   1196 N  N   . GLN A 1 188 ? -12.108 -15.776 22.999 1.00 81.67  ?  180 GLN A N   1 
ATOM   1197 C  CA  . GLN A 1 188 ? -11.357 -16.917 23.514 1.00 84.28  ?  180 GLN A CA  1 
ATOM   1198 C  C   . GLN A 1 188 ? -10.718 -16.656 24.872 1.00 83.03  ?  180 GLN A C   1 
ATOM   1199 O  O   . GLN A 1 188 ? -10.414 -17.616 25.588 1.00 91.04  ?  180 GLN A O   1 
ATOM   1200 C  CB  . GLN A 1 188 ? -10.263 -17.312 22.518 1.00 87.76  ?  180 GLN A CB  1 
ATOM   1201 C  CG  . GLN A 1 188 ? -10.756 -18.160 21.360 1.00 101.76 ?  180 GLN A CG  1 
ATOM   1202 C  CD  . GLN A 1 188 ? -9.652  -18.531 20.386 1.00 113.28 ?  180 GLN A CD  1 
ATOM   1203 O  OE1 . GLN A 1 188 ? -8.665  -17.809 20.242 1.00 109.39 ?  180 GLN A OE1 1 
ATOM   1204 N  NE2 . GLN A 1 188 ? -9.815  -19.664 19.713 1.00 110.66 ?  180 GLN A NE2 1 
ATOM   1205 N  N   . ASP A 1 189 ? -10.515 -15.394 25.244 1.00 82.91  ?  181 ASP A N   1 
ATOM   1206 C  CA  . ASP A 1 189 ? -9.732  -15.041 26.419 1.00 71.89  ?  181 ASP A CA  1 
ATOM   1207 C  C   . ASP A 1 189 ? -10.635 -14.518 27.524 1.00 71.79  ?  181 ASP A C   1 
ATOM   1208 O  O   . ASP A 1 189 ? -11.354 -13.533 27.305 1.00 72.81  ?  181 ASP A O   1 
ATOM   1209 C  CB  . ASP A 1 189 ? -8.684  -13.991 26.041 1.00 69.32  ?  181 ASP A CB  1 
ATOM   1210 C  CG  . ASP A 1 189 ? -7.664  -13.762 27.132 1.00 70.81  ?  181 ASP A CG  1 
ATOM   1211 O  OD1 . ASP A 1 189 ? -7.976  -14.048 28.303 1.00 75.20  ?  181 ASP A OD1 1 
ATOM   1212 O  OD2 . ASP A 1 189 ? -6.550  -13.298 26.816 1.00 67.19  ?  181 ASP A OD2 1 
ATOM   1213 N  N   . PRO A 1 190 ? -10.642 -15.132 28.712 1.00 69.89  ?  182 PRO A N   1 
ATOM   1214 C  CA  . PRO A 1 190 ? -11.524 -14.631 29.782 1.00 70.14  ?  182 PRO A CA  1 
ATOM   1215 C  C   . PRO A 1 190 ? -11.048 -13.338 30.422 1.00 67.34  ?  182 PRO A C   1 
ATOM   1216 O  O   . PRO A 1 190 ? -11.856 -12.664 31.071 1.00 67.65  ?  182 PRO A O   1 
ATOM   1217 C  CB  . PRO A 1 190 ? -11.541 -15.782 30.795 1.00 71.11  ?  182 PRO A CB  1 
ATOM   1218 C  CG  . PRO A 1 190 ? -10.218 -16.451 30.606 1.00 77.06  ?  182 PRO A CG  1 
ATOM   1219 C  CD  . PRO A 1 190 ? -9.918  -16.354 29.123 1.00 74.81  ?  182 PRO A CD  1 
ATOM   1220 N  N   . THR A 1 191 ? -9.775  -12.972 30.271 1.00 68.07  ?  183 THR A N   1 
ATOM   1221 C  CA  . THR A 1 191 ? -9.277  -11.712 30.802 1.00 64.82  ?  183 THR A CA  1 
ATOM   1222 C  C   . THR A 1 191 ? -9.425  -10.562 29.815 1.00 61.96  ?  183 THR A C   1 
ATOM   1223 O  O   . THR A 1 191 ? -8.843  -9.499  30.037 1.00 58.10  ?  183 THR A O   1 
ATOM   1224 C  CB  . THR A 1 191 ? -7.800  -11.824 31.198 1.00 62.29  ?  183 THR A CB  1 
ATOM   1225 O  OG1 . THR A 1 191 ? -6.998  -11.930 30.014 1.00 59.67  ?  183 THR A OG1 1 
ATOM   1226 C  CG2 . THR A 1 191 ? -7.569  -13.029 32.089 1.00 64.02  ?  183 THR A CG2 1 
ATOM   1227 N  N   . ILE A 1 192 ? -10.153 -10.754 28.718 1.00 65.78  ?  184 ILE A N   1 
ATOM   1228 C  CA  . ILE A 1 192 ? -10.442 -9.679  27.778 1.00 66.04  ?  184 ILE A CA  1 
ATOM   1229 C  C   . ILE A 1 192 ? -11.927 -9.362  27.846 1.00 63.02  ?  184 ILE A C   1 
ATOM   1230 O  O   . ILE A 1 192 ? -12.771 -10.255 27.698 1.00 64.96  ?  184 ILE A O   1 
ATOM   1231 C  CB  . ILE A 1 192 ? -10.035 -10.029 26.337 1.00 72.71  ?  184 ILE A CB  1 
ATOM   1232 C  CG1 . ILE A 1 192 ? -8.542  -10.320 26.268 1.00 67.07  ?  184 ILE A CG1 1 
ATOM   1233 C  CG2 . ILE A 1 192 ? -10.427 -8.877  25.414 1.00 72.46  ?  184 ILE A CG2 1 
ATOM   1234 C  CD1 . ILE A 1 192 ? -8.080  -10.738 24.902 1.00 70.41  ?  184 ILE A CD1 1 
ATOM   1235 N  N   . ARG A 1 193 ? -12.238 -8.089  28.060 1.00 59.10  ?  185 ARG A N   1 
ATOM   1236 C  CA  . ARG A 1 193 ? -13.600 -7.582  28.060 1.00 63.25  ?  185 ARG A CA  1 
ATOM   1237 C  C   . ARG A 1 193 ? -13.696 -6.499  26.999 1.00 64.30  ?  185 ARG A C   1 
ATOM   1238 O  O   . ARG A 1 193 ? -12.795 -5.665  26.872 1.00 59.93  ?  185 ARG A O   1 
ATOM   1239 C  CB  . ARG A 1 193 ? -13.983 -7.009  29.416 1.00 60.26  ?  185 ARG A CB  1 
ATOM   1240 C  CG  . ARG A 1 193 ? -13.735 -7.963  30.557 1.00 56.57  ?  185 ARG A CG  1 
ATOM   1241 C  CD  . ARG A 1 193 ? -14.616 -9.193  30.451 1.00 69.45  ?  185 ARG A CD  1 
ATOM   1242 N  NE  . ARG A 1 193 ? -14.209 -10.222 31.401 1.00 70.80  ?  185 ARG A NE  1 
ATOM   1243 C  CZ  . ARG A 1 193 ? -14.522 -10.220 32.690 1.00 75.08  ?  185 ARG A CZ  1 
ATOM   1244 N  NH1 . ARG A 1 193 ? -15.263 -9.260  33.220 1.00 78.09  ?  185 ARG A NH1 1 
ATOM   1245 N  NH2 . ARG A 1 193 ? -14.076 -11.202 33.467 1.00 78.07  ?  185 ARG A NH2 1 
ATOM   1246 N  N   . THR A 1 194 ? -14.784 -6.509  26.245 1.00 72.91  ?  186 THR A N   1 
ATOM   1247 C  CA  . THR A 1 194 ? -14.986 -5.554  25.168 1.00 69.92  ?  186 THR A CA  1 
ATOM   1248 C  C   . THR A 1 194 ? -15.979 -4.482  25.594 1.00 61.94  ?  186 THR A C   1 
ATOM   1249 O  O   . THR A 1 194 ? -16.936 -4.758  26.325 1.00 57.51  ?  186 THR A O   1 
ATOM   1250 C  CB  . THR A 1 194 ? -15.484 -6.261  23.907 1.00 77.34  ?  186 THR A CB  1 
ATOM   1251 O  OG1 . THR A 1 194 ? -14.604 -7.346  23.588 1.00 83.08  ?  186 THR A OG1 1 
ATOM   1252 C  CG2 . THR A 1 194 ? -15.527 -5.292  22.743 1.00 71.29  ?  186 THR A CG2 1 
ATOM   1253 N  N   . VAL A 1 195 ? -15.730 -3.255  25.142 1.00 60.02  ?  187 VAL A N   1 
ATOM   1254 C  CA  . VAL A 1 195 ? -16.657 -2.141  25.315 1.00 62.33  ?  187 VAL A CA  1 
ATOM   1255 C  C   . VAL A 1 195 ? -16.865 -1.496  23.952 1.00 64.25  ?  187 VAL A C   1 
ATOM   1256 O  O   . VAL A 1 195 ? -15.896 -1.081  23.303 1.00 60.46  ?  187 VAL A O   1 
ATOM   1257 C  CB  . VAL A 1 195 ? -16.144 -1.110  26.332 1.00 63.06  ?  187 VAL A CB  1 
ATOM   1258 C  CG1 . VAL A 1 195 ? -16.869 0.216   26.169 1.00 64.67  ?  187 VAL A CG1 1 
ATOM   1259 C  CG2 . VAL A 1 195 ? -16.310 -1.642  27.749 1.00 66.00  ?  187 VAL A CG2 1 
ATOM   1260 N  N   . ASP A 1 196 ? -18.121 -1.403  23.519 1.00 65.03  ?  188 ASP A N   1 
ATOM   1261 C  CA  . ASP A 1 196 ? -18.445 -0.687  22.287 1.00 63.73  ?  188 ASP A CA  1 
ATOM   1262 C  C   . ASP A 1 196 ? -18.159 0.797   22.493 1.00 66.18  ?  188 ASP A C   1 
ATOM   1263 O  O   . ASP A 1 196 ? -18.875 1.479   23.234 1.00 68.95  ?  188 ASP A O   1 
ATOM   1264 C  CB  . ASP A 1 196 ? -19.903 -0.914  21.901 1.00 62.81  ?  188 ASP A CB  1 
ATOM   1265 C  CG  . ASP A 1 196 ? -20.314 -0.120  20.670 1.00 68.64  ?  188 ASP A CG  1 
ATOM   1266 O  OD1 . ASP A 1 196 ? -19.428 0.453   20.003 1.00 69.69  ?  188 ASP A OD1 1 
ATOM   1267 O  OD2 . ASP A 1 196 ? -21.524 -0.066  20.371 1.00 78.01  ?  188 ASP A OD2 1 
ATOM   1268 N  N   . ALA A 1 197 ? -17.111 1.298   21.834 1.00 67.35  ?  189 ALA A N   1 
ATOM   1269 C  CA  . ALA A 1 197 ? -16.673 2.676   22.000 1.00 64.77  ?  189 ALA A CA  1 
ATOM   1270 C  C   . ALA A 1 197 ? -17.384 3.654   21.075 1.00 65.65  ?  189 ALA A C   1 
ATOM   1271 O  O   . ALA A 1 197 ? -17.156 4.864   21.189 1.00 67.70  ?  189 ALA A O   1 
ATOM   1272 C  CB  . ALA A 1 197 ? -15.160 2.770   21.757 1.00 67.04  ?  189 ALA A CB  1 
ATOM   1273 N  N   . THR A 1 198 ? -18.232 3.167   20.172 1.00 70.08  ?  190 THR A N   1 
ATOM   1274 C  CA  . THR A 1 198 ? -18.887 4.017   19.189 1.00 70.54  ?  190 THR A CA  1 
ATOM   1275 C  C   . THR A 1 198 ? -20.047 4.819   19.762 1.00 73.33  ?  190 THR A C   1 
ATOM   1276 O  O   . THR A 1 198 ? -20.509 5.761   19.108 1.00 78.53  ?  190 THR A O   1 
ATOM   1277 C  CB  . THR A 1 198 ? -19.403 3.163   18.027 1.00 73.42  ?  190 THR A CB  1 
ATOM   1278 O  OG1 . THR A 1 198 ? -20.470 2.322   18.488 1.00 65.32  ?  190 THR A OG1 1 
ATOM   1279 C  CG2 . THR A 1 198 ? -18.291 2.289   17.464 1.00 72.38  ?  190 THR A CG2 1 
ATOM   1280 N  N   . GLN A 1 199 ? -20.522 4.472   20.947 1.00 74.12  ?  191 GLN A N   1 
ATOM   1281 C  CA  . GLN A 1 199 ? -21.712 5.069   21.535 1.00 69.78  ?  191 GLN A CA  1 
ATOM   1282 C  C   . GLN A 1 199 ? -21.340 6.286   22.364 1.00 65.79  ?  191 GLN A C   1 
ATOM   1283 O  O   . GLN A 1 199 ? -20.169 6.514   22.682 1.00 71.61  ?  191 GLN A O   1 
ATOM   1284 C  CB  . GLN A 1 199 ? -22.437 4.027   22.380 1.00 67.25  ?  191 GLN A CB  1 
ATOM   1285 C  CG  . GLN A 1 199 ? -21.591 3.474   23.504 1.00 71.86  ?  191 GLN A CG  1 
ATOM   1286 C  CD  . GLN A 1 199 ? -22.159 2.200   24.088 1.00 70.43  ?  191 GLN A CD  1 
ATOM   1287 O  OE1 . GLN A 1 199 ? -23.230 1.741   23.690 1.00 75.40  ?  191 GLN A OE1 1 
ATOM   1288 N  NE2 . GLN A 1 199 ? -21.439 1.615   25.038 1.00 69.00  ?  191 GLN A NE2 1 
ATOM   1289 N  N   . PRO A 1 200 ? -22.325 7.107   22.732 1.00 66.63  ?  192 PRO A N   1 
ATOM   1290 C  CA  . PRO A 1 200 ? -22.014 8.391   23.375 1.00 74.21  ?  192 PRO A CA  1 
ATOM   1291 C  C   . PRO A 1 200 ? -21.174 8.223   24.631 1.00 72.73  ?  192 PRO A C   1 
ATOM   1292 O  O   . PRO A 1 200 ? -21.075 7.140   25.210 1.00 69.52  ?  192 PRO A O   1 
ATOM   1293 C  CB  . PRO A 1 200 ? -23.397 8.973   23.703 1.00 80.11  ?  192 PRO A CB  1 
ATOM   1294 C  CG  . PRO A 1 200 ? -24.312 8.341   22.704 1.00 79.73  ?  192 PRO A CG  1 
ATOM   1295 C  CD  . PRO A 1 200 ? -23.773 6.943   22.496 1.00 76.65  ?  192 PRO A CD  1 
ATOM   1296 N  N   . LEU A 1 201 ? -20.564 9.334   25.053 1.00 68.21  ?  193 LEU A N   1 
ATOM   1297 C  CA  . LEU A 1 201 ? -19.603 9.283   26.151 1.00 68.27  ?  193 LEU A CA  1 
ATOM   1298 C  C   . LEU A 1 201 ? -20.209 8.633   27.388 1.00 69.21  ?  193 LEU A C   1 
ATOM   1299 O  O   . LEU A 1 201 ? -19.656 7.672   27.930 1.00 69.36  ?  193 LEU A O   1 
ATOM   1300 C  CB  . LEU A 1 201 ? -19.112 10.695  26.487 1.00 73.20  ?  193 LEU A CB  1 
ATOM   1301 C  CG  . LEU A 1 201 ? -18.201 10.832  27.709 1.00 74.51  ?  193 LEU A CG  1 
ATOM   1302 C  CD1 . LEU A 1 201 ? -16.845 10.179  27.443 1.00 67.61  ?  193 LEU A CD1 1 
ATOM   1303 C  CD2 . LEU A 1 201 ? -18.029 12.293  28.127 1.00 81.45  ?  193 LEU A CD2 1 
ATOM   1304 N  N   . GLU A 1 202 ? -21.362 9.132   27.837 1.00 67.84  ?  194 GLU A N   1 
ATOM   1305 C  CA  . GLU A 1 202 ? -21.952 8.615   29.066 1.00 67.75  ?  194 GLU A CA  1 
ATOM   1306 C  C   . GLU A 1 202 ? -22.313 7.142   28.946 1.00 65.86  ?  194 GLU A C   1 
ATOM   1307 O  O   . GLU A 1 202 ? -22.371 6.444   29.965 1.00 61.24  ?  194 GLU A O   1 
ATOM   1308 C  CB  . GLU A 1 202 ? -23.181 9.443   29.438 1.00 63.26  ?  194 GLU A CB  1 
ATOM   1309 C  CG  . GLU A 1 202 ? -22.873 10.917  29.673 1.00 62.32  ?  194 GLU A CG  1 
ATOM   1310 C  CD  . GLU A 1 202 ? -21.836 11.133  30.766 1.00 68.82  ?  194 GLU A CD  1 
ATOM   1311 O  OE1 . GLU A 1 202 ? -21.800 10.327  31.719 1.00 69.70  ?  194 GLU A OE1 1 
ATOM   1312 O  OE2 . GLU A 1 202 ? -21.055 12.104  30.664 1.00 69.53  ?  194 GLU A OE2 1 
ATOM   1313 N  N   . ALA A 1 203 ? -22.555 6.659   27.724 1.00 69.54  ?  195 ALA A N   1 
ATOM   1314 C  CA  . ALA A 1 203 ? -22.815 5.238   27.526 1.00 70.52  ?  195 ALA A CA  1 
ATOM   1315 C  C   . ALA A 1 203 ? -21.542 4.419   27.702 1.00 66.47  ?  195 ALA A C   1 
ATOM   1316 O  O   . ALA A 1 203 ? -21.559 3.358   28.340 1.00 61.03  ?  195 ALA A O   1 
ATOM   1317 C  CB  . ALA A 1 203 ? -23.416 5.004   26.143 1.00 71.10  ?  195 ALA A CB  1 
ATOM   1318 N  N   . VAL A 1 204 ? -20.428 4.894   27.140 1.00 71.13  ?  196 VAL A N   1 
ATOM   1319 C  CA  . VAL A 1 204 ? -19.158 4.205   27.333 1.00 68.81  ?  196 VAL A CA  1 
ATOM   1320 C  C   . VAL A 1 204 ? -18.779 4.210   28.807 1.00 61.32  ?  196 VAL A C   1 
ATOM   1321 O  O   . VAL A 1 204 ? -18.286 3.210   29.338 1.00 62.21  ?  196 VAL A O   1 
ATOM   1322 C  CB  . VAL A 1 204 ? -18.059 4.842   26.464 1.00 67.43  ?  196 VAL A CB  1 
ATOM   1323 C  CG1 . VAL A 1 204 ? -16.728 4.138   26.695 1.00 65.07  ?  196 VAL A CG1 1 
ATOM   1324 C  CG2 . VAL A 1 204 ? -18.445 4.785   24.994 1.00 66.80  ?  196 VAL A CG2 1 
ATOM   1325 N  N   . GLU A 1 205 ? -18.991 5.337   29.488 1.00 59.48  ?  197 GLU A N   1 
ATOM   1326 C  CA  . GLU A 1 205 ? -18.692 5.400   30.916 1.00 61.15  ?  197 GLU A CA  1 
ATOM   1327 C  C   . GLU A 1 205 ? -19.527 4.393   31.694 1.00 60.15  ?  197 GLU A C   1 
ATOM   1328 O  O   . GLU A 1 205 ? -19.010 3.671   32.554 1.00 56.50  ?  197 GLU A O   1 
ATOM   1329 C  CB  . GLU A 1 205 ? -18.932 6.816   31.434 1.00 66.65  ?  197 GLU A CB  1 
ATOM   1330 C  CG  . GLU A 1 205 ? -18.871 6.950   32.942 1.00 69.79  ?  197 GLU A CG  1 
ATOM   1331 C  CD  . GLU A 1 205 ? -19.095 8.376   33.400 1.00 78.50  ?  197 GLU A CD  1 
ATOM   1332 O  OE1 . GLU A 1 205 ? -19.112 9.279   32.536 1.00 74.11  ?  197 GLU A OE1 1 
ATOM   1333 O  OE2 . GLU A 1 205 ? -19.254 8.596   34.618 1.00 95.38  ?  197 GLU A OE2 1 
ATOM   1334 N  N   . ARG A 1 206 ? -20.824 4.329   31.398 1.00 62.06  ?  198 ARG A N   1 
ATOM   1335 C  CA  . ARG A 1 206 ? -21.682 3.326   32.019 1.00 58.67  ?  198 ARG A CA  1 
ATOM   1336 C  C   . ARG A 1 206 ? -21.087 1.934   31.858 1.00 59.47  ?  198 ARG A C   1 
ATOM   1337 O  O   . ARG A 1 206 ? -20.974 1.176   32.829 1.00 59.46  ?  198 ARG A O   1 
ATOM   1338 C  CB  . ARG A 1 206 ? -23.084 3.410   31.400 1.00 67.06  ?  198 ARG A CB  1 
ATOM   1339 C  CG  . ARG A 1 206 ? -24.033 2.265   31.730 1.00 73.12  ?  198 ARG A CG  1 
ATOM   1340 C  CD  . ARG A 1 206 ? -24.644 2.369   33.127 1.00 95.53  ?  198 ARG A CD  1 
ATOM   1341 N  NE  . ARG A 1 206 ? -25.422 3.585   33.341 1.00 104.51 ?  198 ARG A NE  1 
ATOM   1342 C  CZ  . ARG A 1 206 ? -26.327 3.737   34.298 1.00 98.71  ?  198 ARG A CZ  1 
ATOM   1343 N  NH1 . ARG A 1 206 ? -26.652 2.742   35.107 1.00 98.39  ?  198 ARG A NH1 1 
ATOM   1344 N  NH2 . ARG A 1 206 ? -26.924 4.917   34.446 1.00 93.28  ?  198 ARG A NH2 1 
ATOM   1345 N  N   . ASP A 1 207 ? -20.685 1.585   30.633 1.00 57.76  ?  199 ASP A N   1 
ATOM   1346 C  CA  . ASP A 1 207 ? -20.259 0.216   30.360 1.00 56.41  ?  199 ASP A CA  1 
ATOM   1347 C  C   . ASP A 1 207 ? -18.902 -0.081  30.985 1.00 58.73  ?  199 ASP A C   1 
ATOM   1348 O  O   . ASP A 1 207 ? -18.708 -1.148  31.577 1.00 61.81  ?  199 ASP A O   1 
ATOM   1349 C  CB  . ASP A 1 207 ? -20.221 -0.035  28.851 1.00 58.94  ?  199 ASP A CB  1 
ATOM   1350 C  CG  . ASP A 1 207 ? -21.614 -0.160  28.241 1.00 65.93  ?  199 ASP A CG  1 
ATOM   1351 O  OD1 . ASP A 1 207 ? -22.613 0.004   28.971 1.00 69.90  ?  199 ASP A OD1 1 
ATOM   1352 O  OD2 . ASP A 1 207 ? -21.711 -0.428  27.025 1.00 69.60  ?  199 ASP A OD2 1 
ATOM   1353 N  N   . ILE A 1 208 ? -17.945 0.840   30.851 1.00 61.36  ?  200 ILE A N   1 
ATOM   1354 C  CA  . ILE A 1 208 ? -16.649 0.638   31.492 1.00 62.56  ?  200 ILE A CA  1 
ATOM   1355 C  C   . ILE A 1 208 ? -16.838 0.446   32.989 1.00 62.10  ?  200 ILE A C   1 
ATOM   1356 O  O   . ILE A 1 208 ? -16.285 -0.480  33.595 1.00 63.73  ?  200 ILE A O   1 
ATOM   1357 C  CB  . ILE A 1 208 ? -15.710 1.819   31.192 1.00 60.93  ?  200 ILE A CB  1 
ATOM   1358 C  CG1 . ILE A 1 208 ? -15.354 1.839   29.703 1.00 55.63  ?  200 ILE A CG1 1 
ATOM   1359 C  CG2 . ILE A 1 208 ? -14.460 1.736   32.048 1.00 63.13  ?  200 ILE A CG2 1 
ATOM   1360 C  CD1 . ILE A 1 208 ? -14.450 2.986   29.306 1.00 64.29  ?  200 ILE A CD1 1 
ATOM   1361 N  N   . ARG A 1 209 ? -17.643 1.317   33.601 1.00 63.34  ?  201 ARG A N   1 
ATOM   1362 C  CA  . ARG A 1 209 ? -17.913 1.214   35.028 1.00 59.70  ?  201 ARG A CA  1 
ATOM   1363 C  C   . ARG A 1 209 ? -18.540 -0.127  35.380 1.00 58.18  ?  201 ARG A C   1 
ATOM   1364 O  O   . ARG A 1 209 ? -18.270 -0.673  36.457 1.00 57.18  ?  201 ARG A O   1 
ATOM   1365 C  CB  . ARG A 1 209 ? -18.812 2.379   35.441 1.00 62.39  ?  201 ARG A CB  1 
ATOM   1366 C  CG  . ARG A 1 209 ? -19.095 2.496   36.918 1.00 79.22  ?  201 ARG A CG  1 
ATOM   1367 C  CD  . ARG A 1 209 ? -19.359 3.949   37.301 1.00 93.05  ?  201 ARG A CD  1 
ATOM   1368 N  NE  . ARG A 1 209 ? -19.747 4.077   38.699 1.00 124.25 ?  201 ARG A NE  1 
ATOM   1369 C  CZ  . ARG A 1 209 ? -19.867 5.228   39.345 1.00 115.70 ?  201 ARG A CZ  1 
ATOM   1370 N  NH1 . ARG A 1 209 ? -19.630 6.385   38.750 1.00 124.72 ?  201 ARG A NH1 1 
ATOM   1371 N  NH2 . ARG A 1 209 ? -20.228 5.217   40.624 1.00 108.52 ?  201 ARG A NH2 1 
ATOM   1372 N  N   . ALA A 1 210 ? -19.355 -0.685  34.481 1.00 59.47  ?  202 ALA A N   1 
ATOM   1373 C  CA  . ALA A 1 210 ? -19.980 -1.976  34.748 1.00 58.64  ?  202 ALA A CA  1 
ATOM   1374 C  C   . ALA A 1 210 ? -18.985 -3.121  34.615 1.00 57.35  ?  202 ALA A C   1 
ATOM   1375 O  O   . ALA A 1 210 ? -18.980 -4.048  35.433 1.00 54.25  ?  202 ALA A O   1 
ATOM   1376 C  CB  . ALA A 1 210 ? -21.159 -2.191  33.800 1.00 56.31  ?  202 ALA A CB  1 
ATOM   1377 N  N   . VAL A 1 211 ? -18.150 -3.083  33.576 1.00 58.90  ?  203 VAL A N   1 
ATOM   1378 C  CA  . VAL A 1 211 ? -17.167 -4.144  33.378 1.00 61.87  ?  203 VAL A CA  1 
ATOM   1379 C  C   . VAL A 1 211 ? -16.205 -4.189  34.550 1.00 60.46  ?  203 VAL A C   1 
ATOM   1380 O  O   . VAL A 1 211 ? -15.799 -5.265  35.007 1.00 57.71  ?  203 VAL A O   1 
ATOM   1381 C  CB  . VAL A 1 211 ? -16.419 -3.930  32.051 1.00 64.54  ?  203 VAL A CB  1 
ATOM   1382 C  CG1 . VAL A 1 211 ? -15.224 -4.861  31.957 1.00 60.78  ?  203 VAL A CG1 1 
ATOM   1383 C  CG2 . VAL A 1 211 ? -17.360 -4.131  30.880 1.00 70.57  ?  203 VAL A CG2 1 
ATOM   1384 N  N   . VAL A 1 212 ? -15.807 -3.017  35.034 1.00 57.12  ?  204 VAL A N   1 
ATOM   1385 C  CA  . VAL A 1 212 ? -14.852 -2.945  36.129 1.00 59.53  ?  204 VAL A CA  1 
ATOM   1386 C  C   . VAL A 1 212 ? -15.481 -3.446  37.421 1.00 62.59  ?  204 VAL A C   1 
ATOM   1387 O  O   . VAL A 1 212 ? -14.876 -4.236  38.152 1.00 58.22  ?  204 VAL A O   1 
ATOM   1388 C  CB  . VAL A 1 212 ? -14.322 -1.507  36.272 1.00 62.07  ?  204 VAL A CB  1 
ATOM   1389 C  CG1 . VAL A 1 212 ? -13.514 -1.378  37.541 1.00 66.64  ?  204 VAL A CG1 1 
ATOM   1390 C  CG2 . VAL A 1 212 ? -13.492 -1.130  35.051 1.00 65.69  ?  204 VAL A CG2 1 
ATOM   1391 N  N   . ASN A 1 213 ? -16.702 -2.998  37.724 1.00 61.45  ?  205 ASN A N   1 
ATOM   1392 C  CA  . ASN A 1 213 ? -17.375 -3.462  38.934 1.00 58.45  ?  205 ASN A CA  1 
ATOM   1393 C  C   . ASN A 1 213 ? -17.522 -4.977  38.931 1.00 63.24  ?  205 ASN A C   1 
ATOM   1394 O  O   . ASN A 1 213 ? -17.129 -5.655  39.888 1.00 67.70  ?  205 ASN A O   1 
ATOM   1395 C  CB  . ASN A 1 213 ? -18.748 -2.806  39.064 1.00 60.77  ?  205 ASN A CB  1 
ATOM   1396 C  CG  . ASN A 1 213 ? -18.664 -1.332  39.372 1.00 67.70  ?  205 ASN A CG  1 
ATOM   1397 O  OD1 . ASN A 1 213 ? -17.593 -0.733  39.299 1.00 75.36  ?  205 ASN A OD1 1 
ATOM   1398 N  ND2 . ASN A 1 213 ? -19.799 -0.734  39.714 1.00 74.85  ?  205 ASN A ND2 1 
ATOM   1399 N  N   . ARG A 1 214 ? -18.086 -5.527  37.852 1.00 64.54  ?  206 ARG A N   1 
ATOM   1400 C  CA  . ARG A 1 214 ? -18.241 -6.974  37.759 1.00 65.88  ?  206 ARG A CA  1 
ATOM   1401 C  C   . ARG A 1 214 ? -16.898 -7.673  37.929 1.00 68.59  ?  206 ARG A C   1 
ATOM   1402 O  O   . ARG A 1 214 ? -16.785 -8.664  38.659 1.00 75.02  ?  206 ARG A O   1 
ATOM   1403 C  CB  . ARG A 1 214 ? -18.873 -7.354  36.416 1.00 73.01  ?  206 ARG A CB  1 
ATOM   1404 C  CG  . ARG A 1 214 ? -19.171 -8.843  36.284 1.00 82.32  ?  206 ARG A CG  1 
ATOM   1405 C  CD  . ARG A 1 214 ? -19.664 -9.236  34.888 1.00 95.38  ?  206 ARG A CD  1 
ATOM   1406 N  NE  . ARG A 1 214 ? -21.019 -8.774  34.607 1.00 111.06 ?  206 ARG A NE  1 
ATOM   1407 C  CZ  . ARG A 1 214 ? -21.358 -7.992  33.589 1.00 120.65 ?  206 ARG A CZ  1 
ATOM   1408 N  NH1 . ARG A 1 214 ? -20.462 -7.569  32.711 1.00 118.17 ?  206 ARG A NH1 1 
ATOM   1409 N  NH2 . ARG A 1 214 ? -22.630 -7.636  33.442 1.00 126.23 ?  206 ARG A NH2 1 
ATOM   1410 N  N   . TRP A 1 215 ? -15.863 -7.165  37.259 1.00 66.65  ?  207 TRP A N   1 
ATOM   1411 C  CA  . TRP A 1 215 ? -14.557 -7.813  37.325 1.00 67.85  ?  207 TRP A CA  1 
ATOM   1412 C  C   . TRP A 1 215 ? -14.005 -7.786  38.745 1.00 66.03  ?  207 TRP A C   1 
ATOM   1413 O  O   . TRP A 1 215 ? -13.576 -8.816  39.280 1.00 63.91  ?  207 TRP A O   1 
ATOM   1414 C  CB  . TRP A 1 215 ? -13.595 -7.136  36.349 1.00 68.29  ?  207 TRP A CB  1 
ATOM   1415 C  CG  . TRP A 1 215 ? -12.244 -7.741  36.378 1.00 61.97  ?  207 TRP A CG  1 
ATOM   1416 C  CD1 . TRP A 1 215 ? -11.868 -8.927  35.824 1.00 63.81  ?  207 TRP A CD1 1 
ATOM   1417 C  CD2 . TRP A 1 215 ? -11.081 -7.203  37.010 1.00 59.04  ?  207 TRP A CD2 1 
ATOM   1418 N  NE1 . TRP A 1 215 ? -10.539 -9.163  36.070 1.00 60.19  ?  207 TRP A NE1 1 
ATOM   1419 C  CE2 . TRP A 1 215 ? -10.031 -8.116  36.795 1.00 58.74  ?  207 TRP A CE2 1 
ATOM   1420 C  CE3 . TRP A 1 215 ? -10.822 -6.034  37.733 1.00 67.52  ?  207 TRP A CE3 1 
ATOM   1421 C  CZ2 . TRP A 1 215 ? -8.743  -7.898  37.277 1.00 60.63  ?  207 TRP A CZ2 1 
ATOM   1422 C  CZ3 . TRP A 1 215 ? -9.544  -5.821  38.211 1.00 66.83  ?  207 TRP A CZ3 1 
ATOM   1423 C  CH2 . TRP A 1 215 ? -8.521  -6.749  37.981 1.00 65.94  ?  207 TRP A CH2 1 
ATOM   1424 N  N   . VAL A 1 216 ? -14.044 -6.614  39.380 1.00 67.80  ?  208 VAL A N   1 
ATOM   1425 C  CA  . VAL A 1 216 ? -13.519 -6.460  40.735 1.00 66.10  ?  208 VAL A CA  1 
ATOM   1426 C  C   . VAL A 1 216 ? -14.237 -7.402  41.699 1.00 70.59  ?  208 VAL A C   1 
ATOM   1427 O  O   . VAL A 1 216 ? -13.608 -8.085  42.514 1.00 71.87  ?  208 VAL A O   1 
ATOM   1428 C  CB  . VAL A 1 216 ? -13.641 -4.990  41.176 1.00 62.39  ?  208 VAL A CB  1 
ATOM   1429 C  CG1 . VAL A 1 216 ? -13.511 -4.846  42.678 1.00 64.27  ?  208 VAL A CG1 1 
ATOM   1430 C  CG2 . VAL A 1 216 ? -12.603 -4.133  40.446 1.00 56.75  ?  208 VAL A CG2 1 
ATOM   1431 N  N   . ALA A 1 217 ? -15.568 -7.456  41.613 1.00 68.29  ?  209 ALA A N   1 
ATOM   1432 C  CA  . ALA A 1 217 ? -16.322 -8.329  42.509 1.00 72.25  ?  209 ALA A CA  1 
ATOM   1433 C  C   . ALA A 1 217 ? -15.900 -9.784  42.351 1.00 76.69  ?  209 ALA A C   1 
ATOM   1434 O  O   . ALA A 1 217 ? -15.832 -10.528 43.335 1.00 87.39  ?  209 ALA A O   1 
ATOM   1435 C  CB  . ALA A 1 217 ? -17.823 -8.176  42.257 1.00 79.86  ?  209 ALA A CB  1 
ATOM   1436 N  N   . GLU A 1 218 ? -15.605 -10.210 41.122 1.00 72.90  ?  210 GLU A N   1 
ATOM   1437 C  CA  . GLU A 1 218 ? -15.186 -11.593 40.914 1.00 74.67  ?  210 GLU A CA  1 
ATOM   1438 C  C   . GLU A 1 218 ? -13.872 -11.897 41.626 1.00 76.96  ?  210 GLU A C   1 
ATOM   1439 O  O   . GLU A 1 218 ? -13.599 -13.055 41.963 1.00 78.97  ?  210 GLU A O   1 
ATOM   1440 C  CB  . GLU A 1 218 ? -15.060 -11.890 39.420 1.00 71.24  ?  210 GLU A CB  1 
ATOM   1441 C  CG  . GLU A 1 218 ? -16.398 -11.933 38.706 1.00 75.89  ?  210 GLU A CG  1 
ATOM   1442 C  CD  . GLU A 1 218 ? -16.269 -11.971 37.194 1.00 79.31  ?  210 GLU A CD  1 
ATOM   1443 O  OE1 . GLU A 1 218 ? -15.138 -11.844 36.681 1.00 68.96  ?  210 GLU A OE1 1 
ATOM   1444 O  OE2 . GLU A 1 218 ? -17.309 -12.125 36.518 1.00 83.18  ?  210 GLU A OE2 1 
ATOM   1445 N  N   . GLN A 1 219 ? -13.044 -10.881 41.865 1.00 78.69  ?  211 GLN A N   1 
ATOM   1446 C  CA  . GLN A 1 219 ? -11.761 -11.077 42.542 1.00 78.49  ?  211 GLN A CA  1 
ATOM   1447 C  C   . GLN A 1 219 ? -11.909 -11.056 44.063 1.00 77.16  ?  211 GLN A C   1 
ATOM   1448 O  O   . GLN A 1 219 ? -11.973 -9.993  44.682 1.00 72.44  ?  211 GLN A O   1 
ATOM   1449 C  CB  . GLN A 1 219 ? -10.760 -10.001 42.106 1.00 77.29  ?  211 GLN A CB  1 
ATOM   1450 C  CG  . GLN A 1 219 ? -10.691 -9.790  40.601 1.00 69.53  ?  211 GLN A CG  1 
ATOM   1451 C  CD  . GLN A 1 219 ? -10.344 -11.060 39.847 1.00 79.72  ?  211 GLN A CD  1 
ATOM   1452 O  OE1 . GLN A 1 219 ? -9.384  -11.754 40.181 1.00 85.07  ?  211 GLN A OE1 1 
ATOM   1453 N  NE2 . GLN A 1 219 ? -11.131 -11.371 38.822 1.00 76.38  ?  211 GLN A NE2 1 
ATOM   1454 N  N   . MET B 1 9   ? 5.088   18.872  27.652 1.00 71.93  ?  1   MET B N   1 
ATOM   1455 C  CA  . MET B 1 9   ? 4.883   19.663  28.899 1.00 75.84  ?  1   MET B CA  1 
ATOM   1456 C  C   . MET B 1 9   ? 5.705   19.060  30.032 1.00 68.51  ?  1   MET B C   1 
ATOM   1457 O  O   . MET B 1 9   ? 5.398   17.970  30.515 1.00 71.64  ?  1   MET B O   1 
ATOM   1458 C  CB  . MET B 1 9   ? 3.406   19.702  29.286 1.00 65.66  ?  1   MET B CB  1 
ATOM   1459 N  N   . ARG B 1 10  ? 6.741   19.786  30.447 1.00 66.60  ?  2   ARG B N   1 
ATOM   1460 C  CA  . ARG B 1 10  ? 7.619   19.360  31.531 1.00 73.03  ?  2   ARG B CA  1 
ATOM   1461 C  C   . ARG B 1 10  ? 6.836   18.644  32.622 1.00 63.20  ?  2   ARG B C   1 
ATOM   1462 O  O   . ARG B 1 10  ? 5.828   19.154  33.117 1.00 57.48  ?  2   ARG B O   1 
ATOM   1463 C  CB  . ARG B 1 10  ? 8.328   20.591  32.116 1.00 80.18  ?  2   ARG B CB  1 
ATOM   1464 C  CG  . ARG B 1 10  ? 9.373   20.320  33.195 1.00 95.55  ?  2   ARG B CG  1 
ATOM   1465 C  CD  . ARG B 1 10  ? 9.543   21.558  34.096 1.00 102.37 ?  2   ARG B CD  1 
ATOM   1466 N  NE  . ARG B 1 10  ? 9.022   22.753  33.440 1.00 110.91 ?  2   ARG B NE  1 
ATOM   1467 C  CZ  . ARG B 1 10  ? 9.760   23.726  32.923 1.00 129.11 ?  2   ARG B CZ  1 
ATOM   1468 N  NH1 . ARG B 1 10  ? 11.067  23.781  33.115 1.00 130.75 ?  2   ARG B NH1 1 
ATOM   1469 N  NH2 . ARG B 1 10  ? 9.170   24.670  32.194 1.00 126.03 ?  2   ARG B NH2 1 
ATOM   1470 N  N   . SER B 1 11  ? 7.307   17.455  32.990 1.00 63.21  ?  3   SER B N   1 
ATOM   1471 C  CA  . SER B 1 11  ? 6.697   16.723  34.090 1.00 61.58  ?  3   SER B CA  1 
ATOM   1472 C  C   . SER B 1 11  ? 6.737   17.557  35.366 1.00 59.03  ?  3   SER B C   1 
ATOM   1473 O  O   . SER B 1 11  ? 7.592   18.433  35.533 1.00 63.01  ?  3   SER B O   1 
ATOM   1474 C  CB  . SER B 1 11  ? 7.430   15.400  34.302 1.00 58.82  ?  3   SER B CB  1 
ATOM   1475 O  OG  . SER B 1 11  ? 8.799   15.631  34.578 1.00 58.97  ?  3   SER B OG  1 
ATOM   1476 N  N   . ASN B 1 12  ? 5.795   17.287  36.274 1.00 51.48  ?  4   ASN B N   1 
ATOM   1477 C  CA  . ASN B 1 12  ? 5.742   18.027  37.521 1.00 52.65  ?  4   ASN B CA  1 
ATOM   1478 C  C   . ASN B 1 12  ? 5.328   17.140  38.681 1.00 56.31  ?  4   ASN B C   1 
ATOM   1479 O  O   . ASN B 1 12  ? 4.643   16.132  38.520 1.00 53.49  ?  4   ASN B O   1 
ATOM   1480 C  CB  . ASN B 1 12  ? 4.774   19.218  37.453 1.00 54.14  ?  4   ASN B CB  1 
ATOM   1481 C  CG  . ASN B 1 12  ? 5.411   20.442  36.871 1.00 54.75  ?  4   ASN B CG  1 
ATOM   1482 O  OD1 . ASN B 1 12  ? 6.154   21.151  37.545 1.00 53.50  ?  4   ASN B OD1 1 
ATOM   1483 N  ND2 . ASN B 1 12  ? 5.127   20.703  35.601 1.00 64.24  ?  4   ASN B ND2 1 
ATOM   1484 N  N   . TYR B 1 13  ? 5.732   17.578  39.869 1.00 57.92  ?  5   TYR B N   1 
ATOM   1485 C  CA  . TYR B 1 13  ? 5.520   16.859  41.117 1.00 50.39  ?  5   TYR B CA  1 
ATOM   1486 C  C   . TYR B 1 13  ? 4.628   17.714  42.000 1.00 48.54  ?  5   TYR B C   1 
ATOM   1487 O  O   . TYR B 1 13  ? 5.005   18.826  42.381 1.00 50.70  ?  5   TYR B O   1 
ATOM   1488 C  CB  . TYR B 1 13  ? 6.860   16.567  41.792 1.00 58.71  ?  5   TYR B CB  1 
ATOM   1489 C  CG  . TYR B 1 13  ? 6.750   15.910  43.138 1.00 61.55  ?  5   TYR B CG  1 
ATOM   1490 C  CD1 . TYR B 1 13  ? 5.677   15.085  43.450 1.00 61.34  ?  5   TYR B CD1 1 
ATOM   1491 C  CD2 . TYR B 1 13  ? 7.717   16.123  44.110 1.00 59.42  ?  5   TYR B CD2 1 
ATOM   1492 C  CE1 . TYR B 1 13  ? 5.576   14.488  44.688 1.00 66.94  ?  5   TYR B CE1 1 
ATOM   1493 C  CE2 . TYR B 1 13  ? 7.625   15.531  45.352 1.00 69.62  ?  5   TYR B CE2 1 
ATOM   1494 C  CZ  . TYR B 1 13  ? 6.555   14.713  45.633 1.00 72.00  ?  5   TYR B CZ  1 
ATOM   1495 O  OH  . TYR B 1 13  ? 6.461   14.125  46.871 1.00 78.93  ?  5   TYR B OH  1 
ATOM   1496 N  N   . ILE B 1 14  ? 3.442   17.200  42.308 1.00 46.12  ?  6   ILE B N   1 
ATOM   1497 C  CA  . ILE B 1 14  ? 2.464   17.895  43.134 1.00 50.05  ?  6   ILE B CA  1 
ATOM   1498 C  C   . ILE B 1 14  ? 2.263   17.063  44.388 1.00 53.95  ?  6   ILE B C   1 
ATOM   1499 O  O   . ILE B 1 14  ? 2.115   15.840  44.304 1.00 52.95  ?  6   ILE B O   1 
ATOM   1500 C  CB  . ILE B 1 14  ? 1.135   18.101  42.388 1.00 51.62  ?  6   ILE B CB  1 
ATOM   1501 C  CG1 . ILE B 1 14  ? 1.370   18.912  41.113 1.00 52.59  ?  6   ILE B CG1 1 
ATOM   1502 C  CG2 . ILE B 1 14  ? 0.134   18.811  43.276 1.00 52.66  ?  6   ILE B CG2 1 
ATOM   1503 C  CD1 . ILE B 1 14  ? 0.224   18.838  40.134 1.00 56.12  ?  6   ILE B CD1 1 
ATOM   1504 N  N   . VAL B 1 15  ? 2.285   17.720  45.542 1.00 58.65  ?  7   VAL B N   1 
ATOM   1505 C  CA  . VAL B 1 15  ? 2.121   17.077  46.836 1.00 61.17  ?  7   VAL B CA  1 
ATOM   1506 C  C   . VAL B 1 15  ? 0.835   17.603  47.451 1.00 57.14  ?  7   VAL B C   1 
ATOM   1507 O  O   . VAL B 1 15  ? 0.495   18.773  47.270 1.00 58.52  ?  7   VAL B O   1 
ATOM   1508 C  CB  . VAL B 1 15  ? 3.327   17.356  47.757 1.00 62.79  ?  7   VAL B CB  1 
ATOM   1509 C  CG1 . VAL B 1 15  ? 3.020   16.961  49.182 1.00 77.21  ?  7   VAL B CG1 1 
ATOM   1510 C  CG2 . VAL B 1 15  ? 4.549   16.612  47.253 1.00 72.54  ?  7   VAL B CG2 1 
ATOM   1511 N  N   . ILE B 1 16  ? 0.118   16.741  48.166 1.00 63.98  ?  8   ILE B N   1 
ATOM   1512 C  CA  . ILE B 1 16  ? -1.124  17.115  48.836 1.00 72.04  ?  8   ILE B CA  1 
ATOM   1513 C  C   . ILE B 1 16  ? -0.921  16.893  50.330 1.00 75.37  ?  8   ILE B C   1 
ATOM   1514 O  O   . ILE B 1 16  ? -0.820  15.747  50.786 1.00 71.52  ?  8   ILE B O   1 
ATOM   1515 C  CB  . ILE B 1 16  ? -2.327  16.322  48.303 1.00 69.48  ?  8   ILE B CB  1 
ATOM   1516 C  CG1 . ILE B 1 16  ? -2.537  16.654  46.817 1.00 69.94  ?  8   ILE B CG1 1 
ATOM   1517 C  CG2 . ILE B 1 16  ? -3.579  16.627  49.102 1.00 75.22  ?  8   ILE B CG2 1 
ATOM   1518 C  CD1 . ILE B 1 16  ? -3.748  15.998  46.196 1.00 77.21  ?  8   ILE B CD1 1 
ATOM   1519 N  N   . GLU B 1 17  ? -0.865  17.986  51.085 1.00 81.03  ?  9   GLU B N   1 
ATOM   1520 C  CA  . GLU B 1 17  ? -0.589  17.972  52.511 1.00 80.25  ?  9   GLU B CA  1 
ATOM   1521 C  C   . GLU B 1 17  ? -1.833  18.368  53.290 1.00 76.58  ?  9   GLU B C   1 
ATOM   1522 O  O   . GLU B 1 17  ? -2.741  19.011  52.762 1.00 81.09  ?  9   GLU B O   1 
ATOM   1523 C  CB  . GLU B 1 17  ? 0.546   18.938  52.860 1.00 90.44  ?  9   GLU B CB  1 
ATOM   1524 C  CG  . GLU B 1 17  ? 1.938   18.409  52.616 1.00 100.68 ?  9   GLU B CG  1 
ATOM   1525 C  CD  . GLU B 1 17  ? 2.993   19.447  52.932 1.00 102.00 ?  9   GLU B CD  1 
ATOM   1526 O  OE1 . GLU B 1 17  ? 2.613   20.584  53.283 1.00 101.38 ?  9   GLU B OE1 1 
ATOM   1527 O  OE2 . GLU B 1 17  ? 4.196   19.129  52.830 1.00 104.47 ?  9   GLU B OE2 1 
ATOM   1528 N  N   . GLY B 1 18  ? -1.863  17.998  54.558 1.00 86.06  ?  10  GLY B N   1 
ATOM   1529 C  CA  . GLY B 1 18  ? -2.965  18.409  55.399 1.00 83.89  ?  10  GLY B CA  1 
ATOM   1530 C  C   . GLY B 1 18  ? -3.088  17.543  56.625 1.00 80.41  ?  10  GLY B C   1 
ATOM   1531 O  O   . GLY B 1 18  ? -2.631  16.402  56.675 1.00 79.63  ?  10  GLY B O   1 
ATOM   1532 N  N   . LEU B 1 19  ? -3.722  18.111  57.642 1.00 89.47  ?  11  LEU B N   1 
ATOM   1533 C  CA  . LEU B 1 19  ? -3.959  17.388  58.881 1.00 90.34  ?  11  LEU B CA  1 
ATOM   1534 C  C   . LEU B 1 19  ? -4.954  16.257  58.633 1.00 88.99  ?  11  LEU B C   1 
ATOM   1535 O  O   . LEU B 1 19  ? -5.697  16.250  57.648 1.00 88.77  ?  11  LEU B O   1 
ATOM   1536 C  CB  . LEU B 1 19  ? -4.461  18.347  59.967 1.00 88.35  ?  11  LEU B CB  1 
ATOM   1537 C  CG  . LEU B 1 19  ? -3.479  19.466  60.330 1.00 96.77  ?  11  LEU B CG  1 
ATOM   1538 C  CD1 . LEU B 1 19  ? -4.171  20.643  61.011 1.00 103.03 ?  11  LEU B CD1 1 
ATOM   1539 C  CD2 . LEU B 1 19  ? -2.359  18.940  61.231 1.00 95.17  ?  11  LEU B CD2 1 
ATOM   1540 N  N   . GLU B 1 20  ? -4.940  15.275  59.530 1.00 88.03  ?  12  GLU B N   1 
ATOM   1541 C  CA  . GLU B 1 20  ? -5.823  14.127  59.389 1.00 94.40  ?  12  GLU B CA  1 
ATOM   1542 C  C   . GLU B 1 20  ? -7.267  14.589  59.249 1.00 95.46  ?  12  GLU B C   1 
ATOM   1543 O  O   . GLU B 1 20  ? -7.690  15.561  59.880 1.00 100.72 ?  12  GLU B O   1 
ATOM   1544 C  CB  . GLU B 1 20  ? -5.693  13.203  60.598 1.00 101.59 ?  12  GLU B CB  1 
ATOM   1545 C  CG  . GLU B 1 20  ? -6.121  13.846  61.901 1.00 111.18 ?  12  GLU B CG  1 
ATOM   1546 C  CD  . GLU B 1 20  ? -5.982  12.906  63.075 1.00 115.30 ?  12  GLU B CD  1 
ATOM   1547 O  OE1 . GLU B 1 20  ? -5.871  11.684  62.843 1.00 123.30 ?  12  GLU B OE1 1 
ATOM   1548 O  OE2 . GLU B 1 20  ? -5.978  13.388  64.228 1.00 115.92 ?  12  GLU B OE2 1 
ATOM   1549 N  N   . GLY B 1 21  ? -8.021  13.888  58.411 1.00 93.62  ?  13  GLY B N   1 
ATOM   1550 C  CA  . GLY B 1 21  ? -9.386  14.273  58.148 1.00 88.34  ?  13  GLY B CA  1 
ATOM   1551 C  C   . GLY B 1 21  ? -9.531  15.419  57.180 1.00 92.33  ?  13  GLY B C   1 
ATOM   1552 O  O   . GLY B 1 21  ? -10.662 15.851  56.921 1.00 94.12  ?  13  GLY B O   1 
ATOM   1553 N  N   . ALA B 1 22  ? -8.421  15.949  56.664 1.00 90.85  ?  14  ALA B N   1 
ATOM   1554 C  CA  . ALA B 1 22  ? -8.482  16.900  55.566 1.00 84.97  ?  14  ALA B CA  1 
ATOM   1555 C  C   . ALA B 1 22  ? -8.942  16.247  54.273 1.00 80.79  ?  14  ALA B C   1 
ATOM   1556 O  O   . ALA B 1 22  ? -9.268  16.962  53.320 1.00 86.58  ?  14  ALA B O   1 
ATOM   1557 C  CB  . ALA B 1 22  ? -7.112  17.547  55.348 1.00 82.97  ?  14  ALA B CB  1 
ATOM   1558 N  N   . GLY B 1 23  ? -8.974  14.919  54.222 1.00 78.76  ?  15  GLY B N   1 
ATOM   1559 C  CA  . GLY B 1 23  ? -9.405  14.209  53.039 1.00 87.92  ?  15  GLY B CA  1 
ATOM   1560 C  C   . GLY B 1 23  ? -8.448  14.398  51.886 1.00 79.06  ?  15  GLY B C   1 
ATOM   1561 O  O   . GLY B 1 23  ? -8.832  14.892  50.822 1.00 75.12  ?  15  GLY B O   1 
ATOM   1562 N  N   . LYS B 1 24  ? -7.187  14.015  52.096 1.00 79.70  ?  16  LYS B N   1 
ATOM   1563 C  CA  . LYS B 1 24  ? -6.170  14.206  51.068 1.00 80.77  ?  16  LYS B CA  1 
ATOM   1564 C  C   . LYS B 1 24  ? -6.355  13.228  49.914 1.00 84.74  ?  16  LYS B C   1 
ATOM   1565 O  O   . LYS B 1 24  ? -6.126  13.584  48.753 1.00 80.66  ?  16  LYS B O   1 
ATOM   1566 C  CB  . LYS B 1 24  ? -4.777  14.063  51.688 1.00 79.46  ?  16  LYS B CB  1 
ATOM   1567 C  CG  . LYS B 1 24  ? -4.444  15.173  52.685 1.00 83.15  ?  16  LYS B CG  1 
ATOM   1568 C  CD  . LYS B 1 24  ? -3.191  14.889  53.519 1.00 85.57  ?  16  LYS B CD  1 
ATOM   1569 C  CE  . LYS B 1 24  ? -3.459  13.926  54.684 1.00 93.91  ?  16  LYS B CE  1 
ATOM   1570 N  NZ  . LYS B 1 24  ? -4.474  14.402  55.673 1.00 82.46  ?  16  LYS B NZ  1 
ATOM   1571 N  N   . THR B 1 25  ? -6.771  11.994  50.211 1.00 90.53  ?  17  THR B N   1 
ATOM   1572 C  CA  . THR B 1 25  ? -6.951  11.007  49.153 1.00 88.12  ?  17  THR B CA  1 
ATOM   1573 C  C   . THR B 1 25  ? -8.027  11.441  48.166 1.00 80.90  ?  17  THR B C   1 
ATOM   1574 O  O   . THR B 1 25  ? -7.854  11.306  46.948 1.00 78.58  ?  17  THR B O   1 
ATOM   1575 C  CB  . THR B 1 25  ? -7.305  9.650   49.758 1.00 95.80  ?  17  THR B CB  1 
ATOM   1576 O  OG1 . THR B 1 25  ? -8.371  9.810   50.703 1.00 107.28 ?  17  THR B OG1 1 
ATOM   1577 C  CG2 . THR B 1 25  ? -6.097  9.045   50.454 1.00 95.68  ?  17  THR B CG2 1 
ATOM   1578 N  N   . THR B 1 26  ? -9.153  11.957  48.667 1.00 91.79  ?  18  THR B N   1 
ATOM   1579 C  CA  . THR B 1 26  ? -10.192 12.426  47.758 1.00 83.84  ?  18  THR B CA  1 
ATOM   1580 C  C   . THR B 1 26  ? -9.717  13.641  46.971 1.00 75.46  ?  18  THR B C   1 
ATOM   1581 O  O   . THR B 1 26  ? -10.093 13.811  45.806 1.00 80.04  ?  18  THR B O   1 
ATOM   1582 C  CB  . THR B 1 26  ? -11.477 12.761  48.522 1.00 77.47  ?  18  THR B CB  1 
ATOM   1583 O  OG1 . THR B 1 26  ? -11.383 14.080  49.075 1.00 80.86  ?  18  THR B OG1 1 
ATOM   1584 C  CG2 . THR B 1 26  ? -11.731 11.752  49.641 1.00 77.39  ?  18  THR B CG2 1 
ATOM   1585 N  N   . ALA B 1 27  ? -8.894  14.494  47.588 1.00 74.42  ?  19  ALA B N   1 
ATOM   1586 C  CA  . ALA B 1 27  ? -8.320  15.621  46.863 1.00 80.49  ?  19  ALA B CA  1 
ATOM   1587 C  C   . ALA B 1 27  ? -7.411  15.135  45.743 1.00 74.44  ?  19  ALA B C   1 
ATOM   1588 O  O   . ALA B 1 27  ? -7.391  15.710  44.648 1.00 69.25  ?  19  ALA B O   1 
ATOM   1589 C  CB  . ALA B 1 27  ? -7.549  16.525  47.822 1.00 82.24  ?  19  ALA B CB  1 
ATOM   1590 N  N   . ARG B 1 28  ? -6.647  14.072  46.005 1.00 81.51  ?  20  ARG B N   1 
ATOM   1591 C  CA  . ARG B 1 28  ? -5.725  13.543  45.006 1.00 72.79  ?  20  ARG B CA  1 
ATOM   1592 C  C   . ARG B 1 28  ? -6.469  13.116  43.748 1.00 70.91  ?  20  ARG B C   1 
ATOM   1593 O  O   . ARG B 1 28  ? -5.981  13.331  42.630 1.00 69.93  ?  20  ARG B O   1 
ATOM   1594 C  CB  . ARG B 1 28  ? -4.942  12.380  45.617 1.00 70.43  ?  20  ARG B CB  1 
ATOM   1595 C  CG  . ARG B 1 28  ? -3.699  11.947  44.859 1.00 71.80  ?  20  ARG B CG  1 
ATOM   1596 C  CD  . ARG B 1 28  ? -4.026  10.976  43.731 1.00 77.56  ?  20  ARG B CD  1 
ATOM   1597 N  NE  . ARG B 1 28  ? -4.972  9.946   44.149 1.00 80.08  ?  20  ARG B NE  1 
ATOM   1598 C  CZ  . ARG B 1 28  ? -4.713  8.996   45.038 1.00 84.36  ?  20  ARG B CZ  1 
ATOM   1599 N  NH1 . ARG B 1 28  ? -3.526  8.890   45.611 1.00 78.66  ?  20  ARG B NH1 1 
ATOM   1600 N  NH2 . ARG B 1 28  ? -5.675  8.140   45.368 1.00 92.18  ?  20  ARG B NH2 1 
ATOM   1601 N  N   . GLU B 1 29  ? -7.668  12.533  43.904 1.00 72.26  ?  21  GLU B N   1 
ATOM   1602 C  CA  . GLU B 1 29  ? -8.456  12.184  42.728 1.00 72.63  ?  21  GLU B CA  1 
ATOM   1603 C  C   . GLU B 1 29  ? -8.827  13.435  41.935 1.00 71.80  ?  21  GLU B C   1 
ATOM   1604 O  O   . GLU B 1 29  ? -8.792  13.435  40.700 1.00 72.07  ?  21  GLU B O   1 
ATOM   1605 C  CB  . GLU B 1 29  ? -9.740  11.437  43.106 1.00 73.07  ?  21  GLU B CB  1 
ATOM   1606 C  CG  . GLU B 1 29  ? -9.776  10.739  44.459 1.00 80.16  ?  21  GLU B CG  1 
ATOM   1607 C  CD  . GLU B 1 29  ? -8.821  9.574   44.550 1.00 79.16  ?  21  GLU B CD  1 
ATOM   1608 O  OE1 . GLU B 1 29  ? -7.767  9.627   43.896 1.00 76.07  ?  21  GLU B OE1 1 
ATOM   1609 O  OE2 . GLU B 1 29  ? -9.123  8.607   45.281 1.00 85.75  ?  21  GLU B OE2 1 
ATOM   1610 N  N   . CYS B 1 30  ? -9.206  14.509  42.633 1.00 71.91  ?  22  CYS B N   1 
ATOM   1611 C  CA  . CYS B 1 30  ? -9.667  15.714  41.953 1.00 74.17  ?  22  CYS B CA  1 
ATOM   1612 C  C   . CYS B 1 30  ? -8.520  16.468  41.295 1.00 66.88  ?  22  CYS B C   1 
ATOM   1613 O  O   . CYS B 1 30  ? -8.731  17.144  40.282 1.00 62.19  ?  22  CYS B O   1 
ATOM   1614 C  CB  . CYS B 1 30  ? -10.411 16.612  42.940 1.00 79.18  ?  22  CYS B CB  1 
ATOM   1615 S  SG  . CYS B 1 30  ? -11.954 15.887  43.560 1.00 85.81  ?  22  CYS B SG  1 
ATOM   1616 N  N   . VAL B 1 31  ? -7.309  16.378  41.843 1.00 66.70  ?  23  VAL B N   1 
ATOM   1617 C  CA  . VAL B 1 31  ? -6.163  16.950  41.141 1.00 70.74  ?  23  VAL B CA  1 
ATOM   1618 C  C   . VAL B 1 31  ? -5.948  16.219  39.824 1.00 69.92  ?  23  VAL B C   1 
ATOM   1619 O  O   . VAL B 1 31  ? -5.678  16.833  38.784 1.00 60.56  ?  23  VAL B O   1 
ATOM   1620 C  CB  . VAL B 1 31  ? -4.902  16.902  42.022 1.00 68.96  ?  23  VAL B CB  1 
ATOM   1621 C  CG1 . VAL B 1 31  ? -3.679  17.323  41.211 1.00 67.51  ?  23  VAL B CG1 1 
ATOM   1622 C  CG2 . VAL B 1 31  ? -5.081  17.789  43.239 1.00 75.06  ?  23  VAL B CG2 1 
ATOM   1623 N  N   . VAL B 1 32  ? -6.075  14.896  39.848 1.00 71.06  ?  24  VAL B N   1 
ATOM   1624 C  CA  . VAL B 1 32  ? -5.836  14.108  38.648 1.00 66.05  ?  24  VAL B CA  1 
ATOM   1625 C  C   . VAL B 1 32  ? -6.823  14.497  37.555 1.00 66.08  ?  24  VAL B C   1 
ATOM   1626 O  O   . VAL B 1 32  ? -6.441  14.716  36.401 1.00 62.18  ?  24  VAL B O   1 
ATOM   1627 C  CB  . VAL B 1 32  ? -5.911  12.607  38.976 1.00 68.33  ?  24  VAL B CB  1 
ATOM   1628 C  CG1 . VAL B 1 32  ? -5.771  11.790  37.716 1.00 70.45  ?  24  VAL B CG1 1 
ATOM   1629 C  CG2 . VAL B 1 32  ? -4.828  12.240  39.982 1.00 71.66  ?  24  VAL B CG2 1 
ATOM   1630 N  N   . GLU B 1 33  ? -8.103  14.612  37.903 1.00 70.95  ?  25  GLU B N   1 
ATOM   1631 C  CA  . GLU B 1 33  ? -9.105  14.893  36.879 1.00 71.43  ?  25  GLU B CA  1 
ATOM   1632 C  C   . GLU B 1 33  ? -8.862  16.250  36.228 1.00 65.57  ?  25  GLU B C   1 
ATOM   1633 O  O   . GLU B 1 33  ? -9.093  16.415  35.025 1.00 70.79  ?  25  GLU B O   1 
ATOM   1634 C  CB  . GLU B 1 33  ? -10.505 14.814  37.484 1.00 78.61  ?  25  GLU B CB  1 
ATOM   1635 C  CG  . GLU B 1 33  ? -10.911 13.395  37.871 1.00 86.42  ?  25  GLU B CG  1 
ATOM   1636 C  CD  . GLU B 1 33  ? -12.263 13.332  38.550 1.00 103.43 ?  25  GLU B CD  1 
ATOM   1637 O  OE1 . GLU B 1 33  ? -13.021 14.319  38.456 1.00 111.29 ?  25  GLU B OE1 1 
ATOM   1638 O  OE2 . GLU B 1 33  ? -12.567 12.297  39.183 1.00 104.10 ?  25  GLU B OE2 1 
ATOM   1639 N  N   . THR B 1 34  ? -8.392  17.233  37.000 1.00 60.13  ?  26  THR B N   1 
ATOM   1640 C  CA  . THR B 1 34  ? -8.087  18.530  36.407 1.00 61.37  ?  26  THR B CA  1 
ATOM   1641 C  C   . THR B 1 34  ? -6.922  18.426  35.432 1.00 61.17  ?  26  THR B C   1 
ATOM   1642 O  O   . THR B 1 34  ? -6.929  19.064  34.373 1.00 66.18  ?  26  THR B O   1 
ATOM   1643 C  CB  . THR B 1 34  ? -7.753  19.553  37.488 1.00 75.19  ?  26  THR B CB  1 
ATOM   1644 O  OG1 . THR B 1 34  ? -6.554  19.156  38.164 1.00 73.45  ?  26  THR B OG1 1 
ATOM   1645 C  CG2 . THR B 1 34  ? -8.878  19.640  38.478 1.00 78.48  ?  26  THR B CG2 1 
ATOM   1646 N  N   . LEU B 1 35  ? -5.899  17.652  35.794 1.00 64.04  ?  27  LEU B N   1 
ATOM   1647 C  CA  . LEU B 1 35  ? -4.769  17.464  34.896 1.00 64.60  ?  27  LEU B CA  1 
ATOM   1648 C  C   . LEU B 1 35  ? -5.196  16.734  33.630 1.00 62.97  ?  27  LEU B C   1 
ATOM   1649 O  O   . LEU B 1 35  ? -4.736  17.068  32.533 1.00 60.14  ?  27  LEU B O   1 
ATOM   1650 C  CB  . LEU B 1 35  ? -3.652  16.714  35.616 1.00 62.84  ?  27  LEU B CB  1 
ATOM   1651 C  CG  . LEU B 1 35  ? -3.100  17.414  36.869 1.00 60.84  ?  27  LEU B CG  1 
ATOM   1652 C  CD1 . LEU B 1 35  ? -1.957  16.610  37.487 1.00 52.23  ?  27  LEU B CD1 1 
ATOM   1653 C  CD2 . LEU B 1 35  ? -2.658  18.841  36.544 1.00 58.05  ?  27  LEU B CD2 1 
ATOM   1654 N  N   . LYS B 1 36  ? -6.083  15.743  33.756 1.00 66.08  ?  28  LYS B N   1 
ATOM   1655 C  CA  . LYS B 1 36  ? -6.562  15.045  32.567 1.00 62.98  ?  28  LYS B CA  1 
ATOM   1656 C  C   . LYS B 1 36  ? -7.253  16.011  31.611 1.00 64.48  ?  28  LYS B C   1 
ATOM   1657 O  O   . LYS B 1 36  ? -7.095  15.911  30.387 1.00 56.18  ?  28  LYS B O   1 
ATOM   1658 C  CB  . LYS B 1 36  ? -7.526  13.922  32.947 1.00 65.63  ?  28  LYS B CB  1 
ATOM   1659 C  CG  . LYS B 1 36  ? -6.950  12.747  33.724 1.00 66.53  ?  28  LYS B CG  1 
ATOM   1660 C  CD  . LYS B 1 36  ? -8.127  11.969  34.322 1.00 75.54  ?  28  LYS B CD  1 
ATOM   1661 C  CE  . LYS B 1 36  ? -7.739  10.679  35.020 1.00 73.05  ?  28  LYS B CE  1 
ATOM   1662 N  NZ  . LYS B 1 36  ? -8.879  10.186  35.862 1.00 79.12  ?  28  LYS B NZ  1 
ATOM   1663 N  N   . GLN B 1 37  ? -8.045  16.943  32.151 1.00 65.85  ?  29  GLN B N   1 
ATOM   1664 C  CA  . GLN B 1 37  ? -8.713  17.918  31.295 1.00 67.16  ?  29  GLN B CA  1 
ATOM   1665 C  C   . GLN B 1 37  ? -7.695  18.830  30.619 1.00 63.91  ?  29  GLN B C   1 
ATOM   1666 O  O   . GLN B 1 37  ? -7.851  19.196  29.449 1.00 71.71  ?  29  GLN B O   1 
ATOM   1667 C  CB  . GLN B 1 37  ? -9.715  18.749  32.090 1.00 67.62  ?  29  GLN B CB  1 
ATOM   1668 C  CG  . GLN B 1 37  ? -10.867 17.960  32.690 1.00 73.39  ?  29  GLN B CG  1 
ATOM   1669 C  CD  . GLN B 1 37  ? -11.464 16.953  31.728 1.00 82.92  ?  29  GLN B CD  1 
ATOM   1670 O  OE1 . GLN B 1 37  ? -11.725 17.257  30.563 1.00 85.14  ?  29  GLN B OE1 1 
ATOM   1671 N  NE2 . GLN B 1 37  ? -11.671 15.736  32.214 1.00 87.72  ?  29  GLN B NE2 1 
ATOM   1672 N  N   . LEU B 1 38  ? -6.649  19.217  31.342 1.00 66.50  ?  30  LEU B N   1 
ATOM   1673 C  CA  . LEU B 1 38  ? -5.602  20.053  30.774 1.00 64.67  ?  30  LEU B CA  1 
ATOM   1674 C  C   . LEU B 1 38  ? -4.655  19.276  29.869 1.00 61.45  ?  30  LEU B C   1 
ATOM   1675 O  O   . LEU B 1 38  ? -3.628  19.826  29.458 1.00 63.19  ?  30  LEU B O   1 
ATOM   1676 C  CB  . LEU B 1 38  ? -4.820  20.736  31.898 1.00 65.94  ?  30  LEU B CB  1 
ATOM   1677 C  CG  . LEU B 1 38  ? -5.630  21.772  32.675 1.00 58.73  ?  30  LEU B CG  1 
ATOM   1678 C  CD1 . LEU B 1 38  ? -5.067  21.972  34.065 1.00 69.47  ?  30  LEU B CD1 1 
ATOM   1679 C  CD2 . LEU B 1 38  ? -5.650  23.095  31.923 1.00 60.96  ?  30  LEU B CD2 1 
ATOM   1680 N  N   . GLY B 1 39  ? -4.977  18.025  29.549 1.00 58.75  ?  31  GLY B N   1 
ATOM   1681 C  CA  . GLY B 1 39  ? -4.191  17.244  28.619 1.00 61.47  ?  31  GLY B CA  1 
ATOM   1682 C  C   . GLY B 1 39  ? -3.032  16.473  29.205 1.00 63.52  ?  31  GLY B C   1 
ATOM   1683 O  O   . GLY B 1 39  ? -2.260  15.879  28.440 1.00 70.82  ?  31  GLY B O   1 
ATOM   1684 N  N   . VAL B 1 40  ? -2.876  16.463  30.525 1.00 63.12  ?  32  VAL B N   1 
ATOM   1685 C  CA  . VAL B 1 40  ? -1.849  15.654  31.174 1.00 66.64  ?  32  VAL B CA  1 
ATOM   1686 C  C   . VAL B 1 40  ? -2.353  14.216  31.232 1.00 61.62  ?  32  VAL B C   1 
ATOM   1687 O  O   . VAL B 1 40  ? -3.409  13.944  31.811 1.00 67.05  ?  32  VAL B O   1 
ATOM   1688 C  CB  . VAL B 1 40  ? -1.531  16.186  32.579 1.00 61.10  ?  32  VAL B CB  1 
ATOM   1689 C  CG1 . VAL B 1 40  ? -0.381  15.407  33.187 1.00 53.26  ?  32  VAL B CG1 1 
ATOM   1690 C  CG2 . VAL B 1 40  ? -1.229  17.675  32.524 1.00 57.47  ?  32  VAL B CG2 1 
ATOM   1691 N  N   . SER B 1 41  ? -1.588  13.287  30.656 1.00 61.77  ?  33  SER B N   1 
ATOM   1692 C  CA  . SER B 1 41  ? -2.105  11.949  30.407 1.00 75.97  ?  33  SER B CA  1 
ATOM   1693 C  C   . SER B 1 41  ? -1.377  10.827  31.132 1.00 73.67  ?  33  SER B C   1 
ATOM   1694 O  O   . SER B 1 41  ? -2.022  9.845   31.499 1.00 74.23  ?  33  SER B O   1 
ATOM   1695 C  CB  . SER B 1 41  ? -2.089  11.650  28.898 1.00 89.56  ?  33  SER B CB  1 
ATOM   1696 O  OG  . SER B 1 41  ? -3.173  12.284  28.243 1.00 83.79  ?  33  SER B OG  1 
ATOM   1697 N  N   . ASP B 1 42  ? -0.068  10.924  31.341 1.00 87.63  ?  34  ASP B N   1 
ATOM   1698 C  CA  . ASP B 1 42  ? 0.687   9.883   32.030 1.00 87.95  ?  34  ASP B CA  1 
ATOM   1699 C  C   . ASP B 1 42  ? 1.193   10.441  33.354 1.00 71.20  ?  34  ASP B C   1 
ATOM   1700 O  O   . ASP B 1 42  ? 1.882   11.468  33.375 1.00 69.48  ?  34  ASP B O   1 
ATOM   1701 C  CB  . ASP B 1 42  ? 1.845   9.371   31.168 1.00 101.36 ?  34  ASP B CB  1 
ATOM   1702 C  CG  . ASP B 1 42  ? 2.754   10.484  30.668 1.00 112.47 ?  34  ASP B CG  1 
ATOM   1703 O  OD1 . ASP B 1 42  ? 2.519   11.661  31.005 1.00 116.29 ?  34  ASP B OD1 1 
ATOM   1704 O  OD2 . ASP B 1 42  ? 3.711   10.174  29.927 1.00 107.20 ?  34  ASP B OD2 1 
ATOM   1705 N  N   . MET B 1 43  ? 0.852   9.775   34.454 1.00 67.23  ?  35  MET B N   1 
ATOM   1706 C  CA  . MET B 1 43  ? 1.223   10.284  35.767 1.00 67.12  ?  35  MET B CA  1 
ATOM   1707 C  C   . MET B 1 43  ? 1.152   9.161   36.789 1.00 56.06  ?  35  MET B C   1 
ATOM   1708 O  O   . MET B 1 43  ? 0.673   8.060   36.509 1.00 52.63  ?  35  MET B O   1 
ATOM   1709 C  CB  . MET B 1 43  ? 0.332   11.466  36.166 1.00 67.85  ?  35  MET B CB  1 
ATOM   1710 C  CG  . MET B 1 43  ? -1.147  11.145  36.276 1.00 61.21  ?  35  MET B CG  1 
ATOM   1711 S  SD  . MET B 1 43  ? -2.153  12.643  36.306 1.00 62.54  ?  35  MET B SD  1 
ATOM   1712 C  CE  . MET B 1 43  ? -2.521  12.838  34.561 1.00 65.07  ?  35  MET B CE  1 
ATOM   1713 N  N   . VAL B 1 44  ? 1.649   9.466   37.987 1.00 57.99  ?  36  VAL B N   1 
ATOM   1714 C  CA  . VAL B 1 44  ? 1.911   8.477   39.024 1.00 61.34  ?  36  VAL B CA  1 
ATOM   1715 C  C   . VAL B 1 44  ? 1.374   8.993   40.347 1.00 56.43  ?  36  VAL B C   1 
ATOM   1716 O  O   . VAL B 1 44  ? 1.630   10.143  40.711 1.00 54.92  ?  36  VAL B O   1 
ATOM   1717 C  CB  . VAL B 1 44  ? 3.422   8.188   39.145 1.00 61.64  ?  36  VAL B CB  1 
ATOM   1718 C  CG1 . VAL B 1 44  ? 3.721   7.442   40.433 1.00 66.73  ?  36  VAL B CG1 1 
ATOM   1719 C  CG2 . VAL B 1 44  ? 3.912   7.427   37.932 1.00 54.38  ?  36  VAL B CG2 1 
ATOM   1720 N  N   . PHE B 1 45  ? 0.655   8.144   41.077 1.00 58.34  ?  37  PHE B N   1 
ATOM   1721 C  CA  . PHE B 1 45  ? 0.250   8.468   42.437 1.00 63.88  ?  37  PHE B CA  1 
ATOM   1722 C  C   . PHE B 1 45  ? 1.233   7.804   43.395 1.00 58.98  ?  37  PHE B C   1 
ATOM   1723 O  O   . PHE B 1 45  ? 1.697   6.685   43.148 1.00 64.74  ?  37  PHE B O   1 
ATOM   1724 C  CB  . PHE B 1 45  ? -1.171  8.005   42.761 1.00 65.39  ?  37  PHE B CB  1 
ATOM   1725 C  CG  . PHE B 1 45  ? -2.185  8.345   41.708 1.00 66.26  ?  37  PHE B CG  1 
ATOM   1726 C  CD1 . PHE B 1 45  ? -1.938  9.322   40.758 1.00 68.16  ?  37  PHE B CD1 1 
ATOM   1727 C  CD2 . PHE B 1 45  ? -3.393  7.671   41.669 1.00 70.87  ?  37  PHE B CD2 1 
ATOM   1728 C  CE1 . PHE B 1 45  ? -2.875  9.612   39.785 1.00 63.49  ?  37  PHE B CE1 1 
ATOM   1729 C  CE2 . PHE B 1 45  ? -4.333  7.961   40.702 1.00 69.28  ?  37  PHE B CE2 1 
ATOM   1730 C  CZ  . PHE B 1 45  ? -4.075  8.931   39.760 1.00 67.14  ?  37  PHE B CZ  1 
ATOM   1731 N  N   . THR B 1 46  ? 1.556   8.506   44.479 1.00 62.56  ?  38  THR B N   1 
ATOM   1732 C  CA  . THR B 1 46  ? 2.426   7.978   45.516 1.00 70.43  ?  38  THR B CA  1 
ATOM   1733 C  C   . THR B 1 46  ? 1.831   8.319   46.876 1.00 68.91  ?  38  THR B C   1 
ATOM   1734 O  O   . THR B 1 46  ? 1.215   9.373   47.053 1.00 67.83  ?  38  THR B O   1 
ATOM   1735 C  CB  . THR B 1 46  ? 3.845   8.551   45.428 1.00 65.71  ?  38  THR B CB  1 
ATOM   1736 O  OG1 . THR B 1 46  ? 3.782   9.983   45.385 1.00 66.26  ?  38  THR B OG1 1 
ATOM   1737 C  CG2 . THR B 1 46  ? 4.564   8.043   44.190 1.00 64.37  ?  38  THR B CG2 1 
ATOM   1738 N  N   . ARG B 1 47  ? 2.018   7.410   47.831 1.00 76.54  ?  39  ARG B N   1 
ATOM   1739 C  CA  . ARG B 1 47  ? 1.687   7.630   49.233 1.00 69.81  ?  39  ARG B CA  1 
ATOM   1740 C  C   . ARG B 1 47  ? 3.001   7.785   49.988 1.00 73.22  ?  39  ARG B C   1 
ATOM   1741 O  O   . ARG B 1 47  ? 3.797   6.842   50.052 1.00 75.97  ?  39  ARG B O   1 
ATOM   1742 C  CB  . ARG B 1 47  ? 0.867   6.472   49.799 1.00 70.83  ?  39  ARG B CB  1 
ATOM   1743 C  CG  . ARG B 1 47  ? 1.370   5.087   49.400 1.00 78.16  ?  39  ARG B CG  1 
ATOM   1744 C  CD  . ARG B 1 47  ? 0.731   4.620   48.091 1.00 94.46  ?  39  ARG B CD  1 
ATOM   1745 N  NE  . ARG B 1 47  ? 1.599   3.747   47.306 1.00 91.26  ?  39  ARG B NE  1 
ATOM   1746 C  CZ  . ARG B 1 47  ? 1.675   2.430   47.443 1.00 95.10  ?  39  ARG B CZ  1 
ATOM   1747 N  NH1 . ARG B 1 47  ? 0.972   1.789   48.362 1.00 93.05  ?  39  ARG B NH1 1 
ATOM   1748 N  NH2 . ARG B 1 47  ? 2.479   1.738   46.639 1.00 89.08  ?  39  ARG B NH2 1 
ATOM   1749 N  N   . GLU B 1 48  ? 3.235   8.969   50.540 1.00 75.69  ?  40  GLU B N   1 
ATOM   1750 C  CA  . GLU B 1 48  ? 4.564   9.307   51.039 1.00 85.44  ?  40  GLU B CA  1 
ATOM   1751 C  C   . GLU B 1 48  ? 4.890   8.485   52.279 1.00 85.06  ?  40  GLU B C   1 
ATOM   1752 O  O   . GLU B 1 48  ? 6.010   7.972   52.398 1.00 89.64  ?  40  GLU B O   1 
ATOM   1753 C  CB  . GLU B 1 48  ? 4.656   10.809  51.299 1.00 89.52  ?  40  GLU B CB  1 
ATOM   1754 C  CG  . GLU B 1 48  ? 5.347   11.601  50.171 1.00 96.86  ?  40  GLU B CG  1 
ATOM   1755 C  CD  . GLU B 1 48  ? 4.746   11.375  48.780 1.00 82.17  ?  40  GLU B CD  1 
ATOM   1756 O  OE1 . GLU B 1 48  ? 3.861   10.514  48.615 1.00 90.57  ?  40  GLU B OE1 1 
ATOM   1757 O  OE2 . GLU B 1 48  ? 5.177   12.072  47.836 1.00 67.93  ?  40  GLU B OE2 1 
ATOM   1758 N  N   . PRO B 1 49  ? 3.963   8.334   53.222 1.00 78.20  ?  41  PRO B N   1 
ATOM   1759 C  CA  . PRO B 1 49  ? 4.116   7.260   54.217 1.00 88.28  ?  41  PRO B CA  1 
ATOM   1760 C  C   . PRO B 1 49  ? 3.919   5.916   53.532 1.00 78.91  ?  41  PRO B C   1 
ATOM   1761 O  O   . PRO B 1 49  ? 2.806   5.597   53.101 1.00 76.35  ?  41  PRO B O   1 
ATOM   1762 C  CB  . PRO B 1 49  ? 3.021   7.548   55.250 1.00 89.27  ?  41  PRO B CB  1 
ATOM   1763 C  CG  . PRO B 1 49  ? 2.575   8.954   54.985 1.00 89.61  ?  41  PRO B CG  1 
ATOM   1764 C  CD  . PRO B 1 49  ? 2.813   9.207   53.519 1.00 84.70  ?  41  PRO B CD  1 
ATOM   1765 N  N   . GLY B 1 50  ? 4.985   5.129   53.414 1.00 76.16  ?  42  GLY B N   1 
ATOM   1766 C  CA  . GLY B 1 50  ? 4.962   3.965   52.551 1.00 72.77  ?  42  GLY B CA  1 
ATOM   1767 C  C   . GLY B 1 50  ? 5.444   4.355   51.170 1.00 72.33  ?  42  GLY B C   1 
ATOM   1768 O  O   . GLY B 1 50  ? 6.260   5.270   51.040 1.00 65.29  ?  42  GLY B O   1 
ATOM   1769 N  N   . GLY B 1 51  ? 4.946   3.690   50.132 1.00 68.76  ?  43  GLY B N   1 
ATOM   1770 C  CA  . GLY B 1 51  ? 5.247   4.058   48.764 1.00 71.69  ?  43  GLY B CA  1 
ATOM   1771 C  C   . GLY B 1 51  ? 6.386   3.297   48.125 1.00 67.48  ?  43  GLY B C   1 
ATOM   1772 O  O   . GLY B 1 51  ? 6.636   3.482   46.928 1.00 59.74  ?  43  GLY B O   1 
ATOM   1773 N  N   . THR B 1 52  ? 7.085   2.463   48.888 1.00 68.19  ?  44  THR B N   1 
ATOM   1774 C  CA  . THR B 1 52  ? 8.144   1.622   48.352 1.00 63.94  ?  44  THR B CA  1 
ATOM   1775 C  C   . THR B 1 52  ? 8.125   0.320   49.141 1.00 61.39  ?  44  THR B C   1 
ATOM   1776 O  O   . THR B 1 52  ? 7.601   0.263   50.257 1.00 61.34  ?  44  THR B O   1 
ATOM   1777 C  CB  . THR B 1 52  ? 9.519   2.297   48.454 1.00 62.99  ?  44  THR B CB  1 
ATOM   1778 O  OG1 . THR B 1 52  ? 9.774   2.678   49.813 1.00 67.61  ?  44  THR B OG1 1 
ATOM   1779 C  CG2 . THR B 1 52  ? 9.588   3.535   47.564 1.00 60.50  ?  44  THR B CG2 1 
ATOM   1780 N  N   . ILE B 1 53  ? 8.691   -0.732  48.550 1.00 61.07  ?  45  ILE B N   1 
ATOM   1781 C  CA  . ILE B 1 53  ? 8.884   -1.956  49.320 1.00 65.59  ?  45  ILE B CA  1 
ATOM   1782 C  C   . ILE B 1 53  ? 9.744   -1.664  50.541 1.00 64.34  ?  45  ILE B C   1 
ATOM   1783 O  O   . ILE B 1 53  ? 9.480   -2.167  51.639 1.00 62.07  ?  45  ILE B O   1 
ATOM   1784 C  CB  . ILE B 1 53  ? 9.504   -3.064  48.450 1.00 65.92  ?  45  ILE B CB  1 
ATOM   1785 C  CG1 . ILE B 1 53  ? 8.519   -3.507  47.369 1.00 60.42  ?  45  ILE B CG1 1 
ATOM   1786 C  CG2 . ILE B 1 53  ? 9.912   -4.246  49.327 1.00 59.10  ?  45  ILE B CG2 1 
ATOM   1787 C  CD1 . ILE B 1 53  ? 9.124   -4.433  46.332 1.00 72.99  ?  45  ILE B CD1 1 
ATOM   1788 N  N   . LEU B 1 54  ? 10.784  -0.844  50.371 1.00 63.34  ?  46  LEU B N   1 
ATOM   1789 C  CA  . LEU B 1 54  ? 11.638  -0.499  51.501 1.00 66.29  ?  46  LEU B CA  1 
ATOM   1790 C  C   . LEU B 1 54  ? 10.816  0.084   52.640 1.00 59.31  ?  46  LEU B C   1 
ATOM   1791 O  O   . LEU B 1 54  ? 10.880  -0.397  53.775 1.00 58.25  ?  46  LEU B O   1 
ATOM   1792 C  CB  . LEU B 1 54  ? 12.713  0.494   51.066 1.00 68.25  ?  46  LEU B CB  1 
ATOM   1793 C  CG  . LEU B 1 54  ? 13.681  0.939   52.161 1.00 59.57  ?  46  LEU B CG  1 
ATOM   1794 C  CD1 . LEU B 1 54  ? 14.456  -0.250  52.695 1.00 65.06  ?  46  LEU B CD1 1 
ATOM   1795 C  CD2 . LEU B 1 54  ? 14.629  1.996   51.626 1.00 55.60  ?  46  LEU B CD2 1 
ATOM   1796 N  N   . ALA B 1 55  ? 10.017  1.110   52.348 1.00 56.66  ?  47  ALA B N   1 
ATOM   1797 C  CA  . ALA B 1 55  ? 9.207   1.723   53.393 1.00 57.36  ?  47  ALA B CA  1 
ATOM   1798 C  C   . ALA B 1 55  ? 8.297   0.691   54.042 1.00 59.68  ?  47  ALA B C   1 
ATOM   1799 O  O   . ALA B 1 55  ? 8.132   0.680   55.266 1.00 55.39  ?  47  ALA B O   1 
ATOM   1800 C  CB  . ALA B 1 55  ? 8.393   2.881   52.815 1.00 58.81  ?  47  ALA B CB  1 
ATOM   1801 N  N   . GLU B 1 56  ? 7.712   -0.197  53.236 1.00 61.35  ?  48  GLU B N   1 
ATOM   1802 C  CA  . GLU B 1 56  ? 6.809   -1.207  53.776 1.00 62.39  ?  48  GLU B CA  1 
ATOM   1803 C  C   . GLU B 1 56  ? 7.526   -2.113  54.767 1.00 61.73  ?  48  GLU B C   1 
ATOM   1804 O  O   . GLU B 1 56  ? 7.010   -2.399  55.853 1.00 64.90  ?  48  GLU B O   1 
ATOM   1805 C  CB  . GLU B 1 56  ? 6.218   -2.036  52.635 1.00 61.14  ?  48  GLU B CB  1 
ATOM   1806 C  CG  . GLU B 1 56  ? 5.332   -1.260  51.677 1.00 66.16  ?  48  GLU B CG  1 
ATOM   1807 C  CD  . GLU B 1 56  ? 5.017   -2.046  50.417 1.00 69.16  ?  48  GLU B CD  1 
ATOM   1808 O  OE1 . GLU B 1 56  ? 4.879   -3.284  50.506 1.00 78.12  ?  48  GLU B OE1 1 
ATOM   1809 O  OE2 . GLU B 1 56  ? 4.925   -1.429  49.333 1.00 61.54  ?  48  GLU B OE2 1 
ATOM   1810 N  N   . LYS B 1 57  ? 8.719   -2.580  54.405 1.00 62.33  ?  49  LYS B N   1 
ATOM   1811 C  CA  . LYS B 1 57  ? 9.469   -3.478  55.275 1.00 58.46  ?  49  LYS B CA  1 
ATOM   1812 C  C   . LYS B 1 57  ? 10.099  -2.748  56.450 1.00 61.36  ?  49  LYS B C   1 
ATOM   1813 O  O   . LYS B 1 57  ? 10.409  -3.387  57.459 1.00 65.88  ?  49  LYS B O   1 
ATOM   1814 C  CB  . LYS B 1 57  ? 10.523  -4.221  54.450 1.00 59.09  ?  49  LYS B CB  1 
ATOM   1815 C  CG  . LYS B 1 57  ? 9.897   -5.083  53.358 1.00 57.99  ?  49  LYS B CG  1 
ATOM   1816 C  CD  . LYS B 1 57  ? 10.646  -6.384  53.117 1.00 69.42  ?  49  LYS B CD  1 
ATOM   1817 C  CE  . LYS B 1 57  ? 9.733   -7.380  52.405 1.00 85.00  ?  49  LYS B CE  1 
ATOM   1818 N  NZ  . LYS B 1 57  ? 10.375  -8.702  52.181 1.00 87.23  ?  49  LYS B NZ  1 
ATOM   1819 N  N   . LEU B 1 58  ? 10.284  -1.431  56.349 1.00 58.48  ?  50  LEU B N   1 
ATOM   1820 C  CA  . LEU B 1 58  ? 10.704  -0.668  57.516 1.00 62.10  ?  50  LEU B CA  1 
ATOM   1821 C  C   . LEU B 1 58  ? 9.558   -0.528  58.513 1.00 60.80  ?  50  LEU B C   1 
ATOM   1822 O  O   . LEU B 1 58  ? 9.767   -0.628  59.728 1.00 58.93  ?  50  LEU B O   1 
ATOM   1823 C  CB  . LEU B 1 58  ? 11.231  0.701   57.097 1.00 57.82  ?  50  LEU B CB  1 
ATOM   1824 C  CG  . LEU B 1 58  ? 12.546  0.734   56.317 1.00 56.66  ?  50  LEU B CG  1 
ATOM   1825 C  CD1 . LEU B 1 58  ? 12.896  2.187   55.997 1.00 61.37  ?  50  LEU B CD1 1 
ATOM   1826 C  CD2 . LEU B 1 58  ? 13.699  0.079   57.052 1.00 55.64  ?  50  LEU B CD2 1 
ATOM   1827 N  N   . ARG B 1 59  ? 8.337   -0.308  58.021 1.00 63.06  ?  51  ARG B N   1 
ATOM   1828 C  CA  . ARG B 1 59  ? 7.191   -0.222  58.922 1.00 61.51  ?  51  ARG B CA  1 
ATOM   1829 C  C   . ARG B 1 59  ? 6.976   -1.543  59.647 1.00 66.85  ?  51  ARG B C   1 
ATOM   1830 O  O   . ARG B 1 59  ? 6.834   -1.580  60.873 1.00 68.60  ?  51  ARG B O   1 
ATOM   1831 C  CB  . ARG B 1 59  ? 5.937   0.179   58.142 1.00 64.27  ?  51  ARG B CB  1 
ATOM   1832 C  CG  . ARG B 1 59  ? 4.657   0.305   58.971 1.00 82.75  ?  51  ARG B CG  1 
ATOM   1833 C  CD  . ARG B 1 59  ? 3.950   -1.038  59.224 1.00 90.04  ?  51  ARG B CD  1 
ATOM   1834 N  NE  . ARG B 1 59  ? 4.088   -1.974  58.113 1.00 92.32  ?  51  ARG B NE  1 
ATOM   1835 C  CZ  . ARG B 1 59  ? 3.514   -1.826  56.927 1.00 88.62  ?  51  ARG B CZ  1 
ATOM   1836 N  NH1 . ARG B 1 59  ? 2.748   -0.782  56.657 1.00 91.72  ?  51  ARG B NH1 1 
ATOM   1837 N  NH2 . ARG B 1 59  ? 3.725   -2.740  55.985 1.00 85.20  ?  51  ARG B NH2 1 
ATOM   1838 N  N   . SER B 1 60  ? 6.962   -2.649  58.900 1.00 66.99  ?  52  SER B N   1 
ATOM   1839 C  CA  . SER B 1 60  ? 6.792   -3.950  59.534 1.00 69.71  ?  52  SER B CA  1 
ATOM   1840 C  C   . SER B 1 60  ? 7.953   -4.263  60.469 1.00 67.36  ?  52  SER B C   1 
ATOM   1841 O  O   . SER B 1 60  ? 7.777   -4.986  61.455 1.00 69.84  ?  52  SER B O   1 
ATOM   1842 C  CB  . SER B 1 60  ? 6.664   -5.045  58.475 1.00 68.27  ?  52  SER B CB  1 
ATOM   1843 O  OG  . SER B 1 60  ? 7.932   -5.391  57.949 1.00 63.88  ?  52  SER B OG  1 
ATOM   1844 N  N   . LEU B 1 61  ? 9.147   -3.738  60.177 1.00 67.64  ?  53  LEU B N   1 
ATOM   1845 C  CA  . LEU B 1 61  ? 10.288  -3.971  61.057 1.00 70.64  ?  53  LEU B CA  1 
ATOM   1846 C  C   . LEU B 1 61  ? 10.099  -3.281  62.401 1.00 66.36  ?  53  LEU B C   1 
ATOM   1847 O  O   . LEU B 1 61  ? 10.438  -3.846  63.448 1.00 65.52  ?  53  LEU B O   1 
ATOM   1848 C  CB  . LEU B 1 61  ? 11.575  -3.492  60.387 1.00 69.43  ?  53  LEU B CB  1 
ATOM   1849 C  CG  . LEU B 1 61  ? 12.811  -3.350  61.277 1.00 64.74  ?  53  LEU B CG  1 
ATOM   1850 C  CD1 . LEU B 1 61  ? 13.257  -4.679  61.861 1.00 69.01  ?  53  LEU B CD1 1 
ATOM   1851 C  CD2 . LEU B 1 61  ? 13.945  -2.698  60.480 1.00 71.47  ?  53  LEU B CD2 1 
ATOM   1852 N  N   . VAL B 1 62  ? 9.581   -2.052  62.392 1.00 67.48  ?  54  VAL B N   1 
ATOM   1853 C  CA  . VAL B 1 62  ? 9.373   -1.328  63.641 1.00 71.31  ?  54  VAL B CA  1 
ATOM   1854 C  C   . VAL B 1 62  ? 8.322   -2.022  64.496 1.00 71.75  ?  54  VAL B C   1 
ATOM   1855 O  O   . VAL B 1 62  ? 8.479   -2.142  65.718 1.00 74.76  ?  54  VAL B O   1 
ATOM   1856 C  CB  . VAL B 1 62  ? 8.993   0.132   63.339 1.00 73.08  ?  54  VAL B CB  1 
ATOM   1857 C  CG1 . VAL B 1 62  ? 8.488   0.832   64.585 1.00 80.54  ?  54  VAL B CG1 1 
ATOM   1858 C  CG2 . VAL B 1 62  ? 10.189  0.878   62.780 1.00 69.12  ?  54  VAL B CG2 1 
ATOM   1859 N  N   . LEU B 1 63  ? 7.237   -2.491  63.874 1.00 71.22  ?  55  LEU B N   1 
ATOM   1860 C  CA  . LEU B 1 63  ? 6.172   -3.134  64.634 1.00 73.04  ?  55  LEU B CA  1 
ATOM   1861 C  C   . LEU B 1 63  ? 6.623   -4.475  65.203 1.00 72.43  ?  55  LEU B C   1 
ATOM   1862 O  O   . LEU B 1 63  ? 6.265   -4.825  66.333 1.00 73.57  ?  55  LEU B O   1 
ATOM   1863 C  CB  . LEU B 1 63  ? 4.937   -3.314  63.759 1.00 81.03  ?  55  LEU B CB  1 
ATOM   1864 C  CG  . LEU B 1 63  ? 4.243   -2.025  63.310 1.00 85.18  ?  55  LEU B CG  1 
ATOM   1865 C  CD1 . LEU B 1 63  ? 2.998   -2.344  62.501 1.00 68.17  ?  55  LEU B CD1 1 
ATOM   1866 C  CD2 . LEU B 1 63  ? 3.905   -1.156  64.508 1.00 71.19  ?  55  LEU B CD2 1 
ATOM   1867 N  N   . ASP B 1 64  ? 7.400   -5.246  64.435 1.00 68.88  ?  56  ASP B N   1 
ATOM   1868 C  CA  . ASP B 1 64  ? 7.893   -6.521  64.951 1.00 69.90  ?  56  ASP B CA  1 
ATOM   1869 C  C   . ASP B 1 64  ? 8.778   -6.305  66.171 1.00 74.06  ?  56  ASP B C   1 
ATOM   1870 O  O   . ASP B 1 64  ? 8.781   -7.111  67.108 1.00 73.76  ?  56  ASP B O   1 
ATOM   1871 C  CB  . ASP B 1 64  ? 8.659   -7.285  63.872 1.00 68.46  ?  56  ASP B CB  1 
ATOM   1872 C  CG  . ASP B 1 64  ? 7.750   -7.862  62.814 1.00 75.32  ?  56  ASP B CG  1 
ATOM   1873 O  OD1 . ASP B 1 64  ? 6.544   -8.031  63.087 1.00 78.46  ?  56  ASP B OD1 1 
ATOM   1874 O  OD2 . ASP B 1 64  ? 8.244   -8.148  61.704 1.00 83.98  ?  56  ASP B OD2 1 
ATOM   1875 N  N   . ILE B 1 65  ? 9.567   -5.226  66.166 1.00 72.06  ?  57  ILE B N   1 
ATOM   1876 C  CA  . ILE B 1 65  ? 10.382  -4.924  67.336 1.00 73.82  ?  57  ILE B CA  1 
ATOM   1877 C  C   . ILE B 1 65  ? 9.518   -4.436  68.490 1.00 75.85  ?  57  ILE B C   1 
ATOM   1878 O  O   . ILE B 1 65  ? 9.869   -4.626  69.661 1.00 79.16  ?  57  ILE B O   1 
ATOM   1879 C  CB  . ILE B 1 65  ? 11.483  -3.907  66.980 1.00 69.08  ?  57  ILE B CB  1 
ATOM   1880 C  CG1 . ILE B 1 65  ? 12.589  -4.628  66.212 1.00 70.25  ?  57  ILE B CG1 1 
ATOM   1881 C  CG2 . ILE B 1 65  ? 12.011  -3.240  68.233 1.00 69.48  ?  57  ILE B CG2 1 
ATOM   1882 C  CD1 . ILE B 1 65  ? 13.704  -3.737  65.758 1.00 69.00  ?  57  ILE B CD1 1 
ATOM   1883 N  N   . GLN B 1 66  ? 8.392   -3.789  68.196 1.00 70.61  ?  58  GLN B N   1 
ATOM   1884 C  CA  . GLN B 1 66  ? 7.541   -3.298  69.277 1.00 77.73  ?  58  GLN B CA  1 
ATOM   1885 C  C   . GLN B 1 66  ? 6.799   -4.441  69.957 1.00 73.20  ?  58  GLN B C   1 
ATOM   1886 O  O   . GLN B 1 66  ? 6.697   -4.476  71.189 1.00 69.54  ?  58  GLN B O   1 
ATOM   1887 C  CB  . GLN B 1 66  ? 6.568   -2.249  68.738 1.00 73.27  ?  58  GLN B CB  1 
ATOM   1888 C  CG  . GLN B 1 66  ? 7.247   -0.917  68.453 1.00 76.40  ?  58  GLN B CG  1 
ATOM   1889 C  CD  . GLN B 1 66  ? 6.366   0.065   67.706 1.00 84.46  ?  58  GLN B CD  1 
ATOM   1890 O  OE1 . GLN B 1 66  ? 5.228   -0.241  67.355 1.00 86.84  ?  58  GLN B OE1 1 
ATOM   1891 N  NE2 . GLN B 1 66  ? 6.897   1.256   67.456 1.00 96.06  ?  58  GLN B NE2 1 
ATOM   1892 N  N   . SER B 1 67  ? 6.305   -5.405  69.177 1.00 75.36  ?  59  SER B N   1 
ATOM   1893 C  CA  . SER B 1 67  ? 5.516   -6.495  69.742 1.00 73.64  ?  59  SER B CA  1 
ATOM   1894 C  C   . SER B 1 67  ? 6.353   -7.452  70.583 1.00 71.96  ?  59  SER B C   1 
ATOM   1895 O  O   . SER B 1 67  ? 5.785   -8.184  71.399 1.00 77.35  ?  59  SER B O   1 
ATOM   1896 C  CB  . SER B 1 67  ? 4.805   -7.258  68.619 1.00 70.81  ?  59  SER B CB  1 
ATOM   1897 O  OG  . SER B 1 67  ? 5.690   -8.129  67.941 1.00 76.14  ?  59  SER B OG  1 
ATOM   1898 N  N   . THR B 1 68  ? 7.681   -7.473  70.403 1.00 78.88  ?  60  THR B N   1 
ATOM   1899 C  CA  . THR B 1 68  ? 8.529   -8.256  71.298 1.00 78.05  ?  60  THR B CA  1 
ATOM   1900 C  C   . THR B 1 68  ? 8.599   -7.610  72.680 1.00 83.76  ?  60  THR B C   1 
ATOM   1901 O  O   . THR B 1 68  ? 8.477   -8.288  73.706 1.00 87.60  ?  60  THR B O   1 
ATOM   1902 C  CB  . THR B 1 68  ? 9.948   -8.408  70.733 1.00 80.29  ?  60  THR B CB  1 
ATOM   1903 O  OG1 . THR B 1 68  ? 10.566  -7.117  70.618 1.00 76.48  ?  60  THR B OG1 1 
ATOM   1904 C  CG2 . THR B 1 68  ? 9.942   -9.111  69.377 1.00 80.50  ?  60  THR B CG2 1 
ATOM   1905 N  N   . GLY B 1 69  ? 8.810   -6.296  72.724 1.00 80.00  ?  61  GLY B N   1 
ATOM   1906 C  CA  . GLY B 1 69  ? 8.952   -5.598  73.983 1.00 81.42  ?  61  GLY B CA  1 
ATOM   1907 C  C   . GLY B 1 69  ? 10.294  -5.748  74.654 1.00 91.49  ?  61  GLY B C   1 
ATOM   1908 O  O   . GLY B 1 69  ? 10.447  -5.302  75.796 1.00 94.37  ?  61  GLY B O   1 
ATOM   1909 N  N   . ASP B 1 70  ? 11.270  -6.364  73.987 1.00 103.68 ?  62  ASP B N   1 
ATOM   1910 C  CA  . ASP B 1 70  ? 12.608  -6.538  74.533 1.00 90.88  ?  62  ASP B CA  1 
ATOM   1911 C  C   . ASP B 1 70  ? 13.647  -5.634  73.879 1.00 93.60  ?  62  ASP B C   1 
ATOM   1912 O  O   . ASP B 1 70  ? 14.827  -5.716  74.239 1.00 95.16  ?  62  ASP B O   1 
ATOM   1913 C  CB  . ASP B 1 70  ? 13.062  -7.999  74.396 1.00 90.74  ?  62  ASP B CB  1 
ATOM   1914 C  CG  . ASP B 1 70  ? 12.873  -8.801  75.674 1.00 98.33  ?  62  ASP B CG  1 
ATOM   1915 O  OD1 . ASP B 1 70  ? 12.409  -8.237  76.690 1.00 98.42  ?  62  ASP B OD1 1 
ATOM   1916 O  OD2 . ASP B 1 70  ? 13.195  -10.008 75.660 1.00 101.35 ?  62  ASP B OD2 1 
ATOM   1917 N  N   . GLU B 1 71  ? 13.259  -4.799  72.915 1.00 84.14  ?  63  GLU B N   1 
ATOM   1918 C  CA  . GLU B 1 71  ? 14.183  -3.831  72.341 1.00 84.88  ?  63  GLU B CA  1 
ATOM   1919 C  C   . GLU B 1 71  ? 13.467  -2.506  72.132 1.00 79.05  ?  63  GLU B C   1 
ATOM   1920 O  O   . GLU B 1 71  ? 12.296  -2.472  71.741 1.00 84.45  ?  63  GLU B O   1 
ATOM   1921 C  CB  . GLU B 1 71  ? 14.785  -4.311  71.008 1.00 88.09  ?  63  GLU B CB  1 
ATOM   1922 C  CG  . GLU B 1 71  ? 16.034  -3.518  70.593 1.00 98.70  ?  63  GLU B CG  1 
ATOM   1923 C  CD  . GLU B 1 71  ? 16.784  -4.132  69.419 1.00 89.93  ?  63  GLU B CD  1 
ATOM   1924 O  OE1 . GLU B 1 71  ? 16.265  -5.096  68.821 1.00 99.05  ?  63  GLU B OE1 1 
ATOM   1925 O  OE2 . GLU B 1 71  ? 17.894  -3.651  69.095 1.00 80.18  ?  63  GLU B OE2 1 
ATOM   1926 N  N   . VAL B 1 72  ? 14.186  -1.418  72.394 1.00 77.45  ?  64  VAL B N   1 
ATOM   1927 C  CA  . VAL B 1 72  ? 13.693  -0.059  72.206 1.00 74.48  ?  64  VAL B CA  1 
ATOM   1928 C  C   . VAL B 1 72  ? 14.449  0.554   71.038 1.00 77.74  ?  64  VAL B C   1 
ATOM   1929 O  O   . VAL B 1 72  ? 15.678  0.446   70.963 1.00 81.60  ?  64  VAL B O   1 
ATOM   1930 C  CB  . VAL B 1 72  ? 13.867  0.783   73.483 1.00 82.05  ?  64  VAL B CB  1 
ATOM   1931 C  CG1 . VAL B 1 72  ? 14.226  2.224   73.139 1.00 82.56  ?  64  VAL B CG1 1 
ATOM   1932 C  CG2 . VAL B 1 72  ? 12.598  0.724   74.321 1.00 104.48 ?  64  VAL B CG2 1 
ATOM   1933 N  N   . ILE B 1 73  ? 13.720  1.201   70.138 1.00 71.26  ?  65  ILE B N   1 
ATOM   1934 C  CA  . ILE B 1 73  ? 14.319  1.865   68.988 1.00 66.43  ?  65  ILE B CA  1 
ATOM   1935 C  C   . ILE B 1 73  ? 14.550  3.327   69.344 1.00 62.43  ?  65  ILE B C   1 
ATOM   1936 O  O   . ILE B 1 73  ? 13.599  4.061   69.631 1.00 65.52  ?  65  ILE B O   1 
ATOM   1937 C  CB  . ILE B 1 73  ? 13.430  1.725   67.743 1.00 65.68  ?  65  ILE B CB  1 
ATOM   1938 C  CG1 . ILE B 1 73  ? 13.413  0.263   67.293 1.00 68.50  ?  65  ILE B CG1 1 
ATOM   1939 C  CG2 . ILE B 1 73  ? 13.918  2.649   66.638 1.00 63.31  ?  65  ILE B CG2 1 
ATOM   1940 C  CD1 . ILE B 1 73  ? 12.267  -0.085  66.380 1.00 77.74  ?  65  ILE B CD1 1 
ATOM   1941 N  N   . ASN B 1 74  ? 15.814  3.746   69.325 1.00 61.63  ?  66  ASN B N   1 
ATOM   1942 C  CA  . ASN B 1 74  ? 16.144  5.136   69.609 1.00 61.06  ?  66  ASN B CA  1 
ATOM   1943 C  C   . ASN B 1 74  ? 15.364  6.047   68.670 1.00 58.03  ?  66  ASN B C   1 
ATOM   1944 O  O   . ASN B 1 74  ? 15.152  5.719   67.500 1.00 57.28  ?  66  ASN B O   1 
ATOM   1945 C  CB  . ASN B 1 74  ? 17.646  5.371   69.451 1.00 58.04  ?  66  ASN B CB  1 
ATOM   1946 C  CG  . ASN B 1 74  ? 18.082  6.730   69.962 1.00 62.65  ?  66  ASN B CG  1 
ATOM   1947 O  OD1 . ASN B 1 74  ? 18.194  6.945   71.171 1.00 70.18  ?  66  ASN B OD1 1 
ATOM   1948 N  ND2 . ASN B 1 74  ? 18.338  7.655   69.044 1.00 63.33  ?  66  ASN B ND2 1 
ATOM   1949 N  N   . ASP B 1 75  ? 14.920  7.194   69.190 1.00 61.88  ?  67  ASP B N   1 
ATOM   1950 C  CA  . ASP B 1 75  ? 14.116  8.097   68.373 1.00 60.76  ?  67  ASP B CA  1 
ATOM   1951 C  C   . ASP B 1 75  ? 14.891  8.558   67.140 1.00 60.92  ?  67  ASP B C   1 
ATOM   1952 O  O   . ASP B 1 75  ? 14.381  8.498   66.016 1.00 55.88  ?  67  ASP B O   1 
ATOM   1953 C  CB  . ASP B 1 75  ? 13.634  9.294   69.203 1.00 64.29  ?  67  ASP B CB  1 
ATOM   1954 C  CG  . ASP B 1 75  ? 14.743  9.958   70.018 1.00 75.08  ?  67  ASP B CG  1 
ATOM   1955 O  OD1 . ASP B 1 75  ? 15.881  9.447   70.058 1.00 77.99  ?  67  ASP B OD1 1 
ATOM   1956 O  OD2 . ASP B 1 75  ? 14.463  11.010  70.633 1.00 81.18  ?  67  ASP B OD2 1 
ATOM   1957 N  N   . LYS B 1 76  ? 16.139  8.996   67.325 1.00 75.38  ?  68  LYS B N   1 
ATOM   1958 C  CA  . LYS B 1 76  ? 16.904  9.514   66.191 1.00 63.93  ?  68  LYS B CA  1 
ATOM   1959 C  C   . LYS B 1 76  ? 17.097  8.450   65.116 1.00 60.47  ?  68  LYS B C   1 
ATOM   1960 O  O   . LYS B 1 76  ? 16.920  8.725   63.924 1.00 62.15  ?  68  LYS B O   1 
ATOM   1961 C  CB  . LYS B 1 76  ? 18.247  10.068  66.669 1.00 60.87  ?  68  LYS B CB  1 
ATOM   1962 C  CG  . LYS B 1 76  ? 18.098  11.302  67.556 1.00 77.71  ?  68  LYS B CG  1 
ATOM   1963 C  CD  . LYS B 1 76  ? 19.406  12.047  67.795 1.00 87.05  ?  68  LYS B CD  1 
ATOM   1964 C  CE  . LYS B 1 76  ? 19.121  13.437  68.364 1.00 109.98 ?  68  LYS B CE  1 
ATOM   1965 N  NZ  . LYS B 1 76  ? 20.350  14.217  68.673 1.00 135.43 ?  68  LYS B NZ  1 
ATOM   1966 N  N   . ALA B 1 77  ? 17.434  7.222   65.517 1.00 57.65  ?  69  ALA B N   1 
ATOM   1967 C  CA  . ALA B 1 77  ? 17.572  6.150   64.536 1.00 55.49  ?  69  ALA B CA  1 
ATOM   1968 C  C   . ALA B 1 77  ? 16.281  5.963   63.748 1.00 57.34  ?  69  ALA B C   1 
ATOM   1969 O  O   . ALA B 1 77  ? 16.309  5.792   62.524 1.00 56.85  ?  69  ALA B O   1 
ATOM   1970 C  CB  . ALA B 1 77  ? 17.966  4.840   65.221 1.00 56.25  ?  69  ALA B CB  1 
ATOM   1971 N  N   . GLU B 1 78  ? 15.135  5.998   64.434 1.00 63.01  ?  70  GLU B N   1 
ATOM   1972 C  CA  . GLU B 1 78  ? 13.869  5.809   63.735 1.00 61.57  ?  70  GLU B CA  1 
ATOM   1973 C  C   . GLU B 1 78  ? 13.662  6.892   62.683 1.00 61.51  ?  70  GLU B C   1 
ATOM   1974 O  O   . GLU B 1 78  ? 13.251  6.599   61.557 1.00 56.92  ?  70  GLU B O   1 
ATOM   1975 C  CB  . GLU B 1 78  ? 12.705  5.799   64.725 1.00 56.71  ?  70  GLU B CB  1 
ATOM   1976 C  CG  . GLU B 1 78  ? 11.371  5.441   64.080 1.00 68.97  ?  70  GLU B CG  1 
ATOM   1977 C  CD  . GLU B 1 78  ? 10.308  5.064   65.093 1.00 81.63  ?  70  GLU B CD  1 
ATOM   1978 O  OE1 . GLU B 1 78  ? 10.625  5.024   66.299 1.00 72.72  ?  70  GLU B OE1 1 
ATOM   1979 O  OE2 . GLU B 1 78  ? 9.157   4.804   64.679 1.00 83.78  ?  70  GLU B OE2 1 
ATOM   1980 N  N   . VAL B 1 79  ? 13.957  8.149   63.028 1.00 62.75  ?  71  VAL B N   1 
ATOM   1981 C  CA  . VAL B 1 79  ? 13.784  9.232   62.065 1.00 56.81  ?  71  VAL B CA  1 
ATOM   1982 C  C   . VAL B 1 79  ? 14.677  9.010   60.853 1.00 58.19  ?  71  VAL B C   1 
ATOM   1983 O  O   . VAL B 1 79  ? 14.264  9.239   59.713 1.00 65.76  ?  71  VAL B O   1 
ATOM   1984 C  CB  . VAL B 1 79  ? 14.058  10.597  62.721 1.00 56.01  ?  71  VAL B CB  1 
ATOM   1985 C  CG1 . VAL B 1 79  ? 14.011  11.704  61.672 1.00 68.65  ?  71  VAL B CG1 1 
ATOM   1986 C  CG2 . VAL B 1 79  ? 13.052  10.859  63.823 1.00 57.20  ?  71  VAL B CG2 1 
ATOM   1987 N  N   . LEU B 1 80  ? 15.922  8.585   61.077 1.00 54.80  ?  72  LEU B N   1 
ATOM   1988 C  CA  . LEU B 1 80  ? 16.776  8.235   59.947 1.00 59.89  ?  72  LEU B CA  1 
ATOM   1989 C  C   . LEU B 1 80  ? 16.144  7.125   59.116 1.00 59.00  ?  72  LEU B C   1 
ATOM   1990 O  O   . LEU B 1 80  ? 16.270  7.114   57.886 1.00 60.67  ?  72  LEU B O   1 
ATOM   1991 C  CB  . LEU B 1 80  ? 18.163  7.825   60.436 1.00 59.24  ?  72  LEU B CB  1 
ATOM   1992 C  CG  . LEU B 1 80  ? 19.066  8.937   60.977 1.00 54.48  ?  72  LEU B CG  1 
ATOM   1993 C  CD1 . LEU B 1 80  ? 20.278  8.353   61.688 1.00 62.74  ?  72  LEU B CD1 1 
ATOM   1994 C  CD2 . LEU B 1 80  ? 19.517  9.862   59.858 1.00 66.17  ?  72  LEU B CD2 1 
ATOM   1995 N  N   . MET B 1 81  ? 15.462  6.178   59.767 1.00 56.20  ?  73  MET B N   1 
ATOM   1996 C  CA  . MET B 1 81  ? 14.742  5.154   59.023 1.00 55.84  ?  73  MET B CA  1 
ATOM   1997 C  C   . MET B 1 81  ? 13.514  5.721   58.326 1.00 56.31  ?  73  MET B C   1 
ATOM   1998 O  O   . MET B 1 81  ? 13.050  5.141   57.339 1.00 56.82  ?  73  MET B O   1 
ATOM   1999 C  CB  . MET B 1 81  ? 14.319  4.011   59.947 1.00 56.13  ?  73  MET B CB  1 
ATOM   2000 C  CG  . MET B 1 81  ? 15.445  3.082   60.365 1.00 59.33  ?  73  MET B CG  1 
ATOM   2001 S  SD  . MET B 1 81  ? 14.832  1.668   61.306 1.00 57.91  ?  73  MET B SD  1 
ATOM   2002 C  CE  . MET B 1 81  ? 14.566  2.422   62.908 1.00 60.11  ?  73  MET B CE  1 
ATOM   2003 N  N   . PHE B 1 82  ? 12.970  6.824   58.836 1.00 60.41  ?  74  PHE B N   1 
ATOM   2004 C  CA  . PHE B 1 82  ? 11.885  7.507   58.144 1.00 61.30  ?  74  PHE B CA  1 
ATOM   2005 C  C   . PHE B 1 82  ? 12.400  8.250   56.921 1.00 64.41  ?  74  PHE B C   1 
ATOM   2006 O  O   . PHE B 1 82  ? 11.800  8.169   55.842 1.00 68.94  ?  74  PHE B O   1 
ATOM   2007 C  CB  . PHE B 1 82  ? 11.187  8.456   59.120 1.00 62.10  ?  74  PHE B CB  1 
ATOM   2008 C  CG  . PHE B 1 82  ? 10.276  9.451   58.465 1.00 69.49  ?  74  PHE B CG  1 
ATOM   2009 C  CD1 . PHE B 1 82  ? 8.929   9.174   58.297 1.00 71.63  ?  74  PHE B CD1 1 
ATOM   2010 C  CD2 . PHE B 1 82  ? 10.760  10.681  58.045 1.00 75.17  ?  74  PHE B CD2 1 
ATOM   2011 C  CE1 . PHE B 1 82  ? 8.084   10.099  57.707 1.00 76.18  ?  74  PHE B CE1 1 
ATOM   2012 C  CE2 . PHE B 1 82  ? 9.922   11.607  57.453 1.00 81.42  ?  74  PHE B CE2 1 
ATOM   2013 C  CZ  . PHE B 1 82  ? 8.582   11.316  57.285 1.00 77.99  ?  74  PHE B CZ  1 
ATOM   2014 N  N   . TYR B 1 83  ? 13.516  8.972   57.069 1.00 64.99  ?  75  TYR B N   1 
ATOM   2015 C  CA  . TYR B 1 83  ? 14.094  9.666   55.925 1.00 71.28  ?  75  TYR B CA  1 
ATOM   2016 C  C   . TYR B 1 83  ? 14.693  8.696   54.920 1.00 62.92  ?  75  TYR B C   1 
ATOM   2017 O  O   . TYR B 1 83  ? 14.806  9.037   53.739 1.00 64.73  ?  75  TYR B O   1 
ATOM   2018 C  CB  . TYR B 1 83  ? 15.146  10.672  56.389 1.00 74.27  ?  75  TYR B CB  1 
ATOM   2019 C  CG  . TYR B 1 83  ? 14.644  12.098  56.330 1.00 86.11  ?  75  TYR B CG  1 
ATOM   2020 C  CD1 . TYR B 1 83  ? 13.938  12.652  57.392 1.00 93.26  ?  75  TYR B CD1 1 
ATOM   2021 C  CD2 . TYR B 1 83  ? 14.852  12.883  55.203 1.00 98.63  ?  75  TYR B CD2 1 
ATOM   2022 C  CE1 . TYR B 1 83  ? 13.464  13.952  57.337 1.00 95.62  ?  75  TYR B CE1 1 
ATOM   2023 C  CE2 . TYR B 1 83  ? 14.382  14.185  55.139 1.00 106.66 ?  75  TYR B CE2 1 
ATOM   2024 C  CZ  . TYR B 1 83  ? 13.688  14.713  56.210 1.00 95.57  ?  75  TYR B CZ  1 
ATOM   2025 O  OH  . TYR B 1 83  ? 13.217  16.005  56.156 1.00 100.76 ?  75  TYR B OH  1 
ATOM   2026 N  N   . ALA B 1 84  ? 15.078  7.497   55.358 1.00 60.75  ?  76  ALA B N   1 
ATOM   2027 C  CA  . ALA B 1 84  ? 15.559  6.499   54.411 1.00 62.77  ?  76  ALA B CA  1 
ATOM   2028 C  C   . ALA B 1 84  ? 14.452  6.084   53.454 1.00 60.22  ?  76  ALA B C   1 
ATOM   2029 O  O   . ALA B 1 84  ? 14.697  5.888   52.257 1.00 56.17  ?  76  ALA B O   1 
ATOM   2030 C  CB  . ALA B 1 84  ? 16.111  5.290   55.160 1.00 58.79  ?  76  ALA B CB  1 
ATOM   2031 N  N   . ALA B 1 85  ? 13.230  5.938   53.964 1.00 65.21  ?  77  ALA B N   1 
ATOM   2032 C  CA  . ALA B 1 85  ? 12.106  5.627   53.090 1.00 63.65  ?  77  ALA B CA  1 
ATOM   2033 C  C   . ALA B 1 85  ? 11.811  6.786   52.147 1.00 57.53  ?  77  ALA B C   1 
ATOM   2034 O  O   . ALA B 1 85  ? 11.597  6.577   50.948 1.00 56.35  ?  77  ALA B O   1 
ATOM   2035 C  CB  . ALA B 1 85  ? 10.871  5.280   53.921 1.00 64.69  ?  77  ALA B CB  1 
ATOM   2036 N  N   . ARG B 1 86  ? 11.803  8.017   52.666 1.00 61.10  ?  78  ARG B N   1 
ATOM   2037 C  CA  . ARG B 1 86  ? 11.512  9.163   51.813 1.00 67.14  ?  78  ARG B CA  1 
ATOM   2038 C  C   . ARG B 1 86  ? 12.538  9.283   50.695 1.00 63.33  ?  78  ARG B C   1 
ATOM   2039 O  O   . ARG B 1 86  ? 12.185  9.572   49.544 1.00 64.11  ?  78  ARG B O   1 
ATOM   2040 C  CB  . ARG B 1 86  ? 11.475  10.451  52.636 1.00 74.47  ?  78  ARG B CB  1 
ATOM   2041 C  CG  . ARG B 1 86  ? 11.380  11.711  51.778 1.00 86.35  ?  78  ARG B CG  1 
ATOM   2042 C  CD  . ARG B 1 86  ? 11.162  12.970  52.606 1.00 91.45  ?  78  ARG B CD  1 
ATOM   2043 N  NE  . ARG B 1 86  ? 9.860   12.974  53.263 1.00 103.52 ?  78  ARG B NE  1 
ATOM   2044 C  CZ  . ARG B 1 86  ? 9.334   14.020  53.885 1.00 124.17 ?  78  ARG B CZ  1 
ATOM   2045 N  NH1 . ARG B 1 86  ? 9.967   15.180  53.944 1.00 126.91 ?  78  ARG B NH1 1 
ATOM   2046 N  NH2 . ARG B 1 86  ? 8.142   13.901  54.461 1.00 122.41 ?  78  ARG B NH2 1 
ATOM   2047 N  N   . VAL B 1 87  ? 13.817  9.079   51.019 1.00 66.11  ?  79  VAL B N   1 
ATOM   2048 C  CA  . VAL B 1 87  ? 14.863  9.165   50.002 1.00 64.82  ?  79  VAL B CA  1 
ATOM   2049 C  C   . VAL B 1 87  ? 14.678  8.072   48.959 1.00 62.45  ?  79  VAL B C   1 
ATOM   2050 O  O   . VAL B 1 87  ? 14.807  8.310   47.752 1.00 58.69  ?  79  VAL B O   1 
ATOM   2051 C  CB  . VAL B 1 87  ? 16.250  9.084   50.666 1.00 64.72  ?  79  VAL B CB  1 
ATOM   2052 C  CG1 . VAL B 1 87  ? 17.325  8.903   49.615 1.00 66.20  ?  79  VAL B CG1 1 
ATOM   2053 C  CG2 . VAL B 1 87  ? 16.505  10.330  51.495 1.00 77.90  ?  79  VAL B CG2 1 
ATOM   2054 N  N   . GLN B 1 88  ? 14.379  6.854   49.414 1.00 59.67  ?  80  GLN B N   1 
ATOM   2055 C  CA  . GLN B 1 88  ? 14.104  5.757   48.494 1.00 55.91  ?  80  GLN B CA  1 
ATOM   2056 C  C   . GLN B 1 88  ? 12.946  6.096   47.567 1.00 60.15  ?  80  GLN B C   1 
ATOM   2057 O  O   . GLN B 1 88  ? 12.987  5.785   46.370 1.00 55.36  ?  80  GLN B O   1 
ATOM   2058 C  CB  . GLN B 1 88  ? 13.802  4.492   49.298 1.00 55.73  ?  80  GLN B CB  1 
ATOM   2059 C  CG  . GLN B 1 88  ? 13.528  3.255   48.476 1.00 56.38  ?  80  GLN B CG  1 
ATOM   2060 C  CD  . GLN B 1 88  ? 14.771  2.741   47.794 1.00 60.82  ?  80  GLN B CD  1 
ATOM   2061 O  OE1 . GLN B 1 88  ? 15.823  3.372   47.860 1.00 59.17  ?  80  GLN B OE1 1 
ATOM   2062 N  NE2 . GLN B 1 88  ? 14.661  1.594   47.135 1.00 66.25  ?  80  GLN B NE2 1 
ATOM   2063 N  N   . LEU B 1 89  ? 11.893  6.719   48.102 1.00 61.38  ?  81  LEU B N   1 
ATOM   2064 C  CA  . LEU B 1 89  ? 10.742  7.052   47.271 1.00 55.94  ?  81  LEU B CA  1 
ATOM   2065 C  C   . LEU B 1 89  ? 11.093  8.113   46.240 1.00 58.58  ?  81  LEU B C   1 
ATOM   2066 O  O   . LEU B 1 89  ? 10.641  8.050   45.093 1.00 59.52  ?  81  LEU B O   1 
ATOM   2067 C  CB  . LEU B 1 89  ? 9.587   7.545   48.137 1.00 55.57  ?  81  LEU B CB  1 
ATOM   2068 C  CG  . LEU B 1 89  ? 8.324   7.855   47.328 1.00 57.58  ?  81  LEU B CG  1 
ATOM   2069 C  CD1 . LEU B 1 89  ? 7.696   6.559   46.835 1.00 54.49  ?  81  LEU B CD1 1 
ATOM   2070 C  CD2 . LEU B 1 89  ? 7.355   8.665   48.159 1.00 62.01  ?  81  LEU B CD2 1 
ATOM   2071 N  N   . VAL B 1 90  ? 11.867  9.116   46.647 1.00 60.25  ?  82  VAL B N   1 
ATOM   2072 C  CA  . VAL B 1 90  ? 12.212  10.195  45.736 1.00 62.01  ?  82  VAL B CA  1 
ATOM   2073 C  C   . VAL B 1 90  ? 13.147  9.701   44.644 1.00 63.39  ?  82  VAL B C   1 
ATOM   2074 O  O   . VAL B 1 90  ? 13.064  10.145  43.495 1.00 58.02  ?  82  VAL B O   1 
ATOM   2075 C  CB  . VAL B 1 90  ? 12.823  11.372  46.519 1.00 67.29  ?  82  VAL B CB  1 
ATOM   2076 C  CG1 . VAL B 1 90  ? 13.548  12.313  45.578 1.00 75.23  ?  82  VAL B CG1 1 
ATOM   2077 C  CG2 . VAL B 1 90  ? 11.738  12.105  47.289 1.00 75.64  ?  82  VAL B CG2 1 
ATOM   2078 N  N   . GLU B 1 91  ? 14.054  8.787   44.978 1.00 65.79  ?  83  GLU B N   1 
ATOM   2079 C  CA  . GLU B 1 91  ? 15.123  8.436   44.053 1.00 57.76  ?  83  GLU B CA  1 
ATOM   2080 C  C   . GLU B 1 91  ? 14.785  7.251   43.160 1.00 56.35  ?  83  GLU B C   1 
ATOM   2081 O  O   . GLU B 1 91  ? 15.329  7.151   42.054 1.00 63.15  ?  83  GLU B O   1 
ATOM   2082 C  CB  . GLU B 1 91  ? 16.410  8.141   44.828 1.00 59.68  ?  83  GLU B CB  1 
ATOM   2083 C  CG  . GLU B 1 91  ? 17.668  8.643   44.136 1.00 65.76  ?  83  GLU B CG  1 
ATOM   2084 C  CD  . GLU B 1 91  ? 17.742  10.160  44.084 1.00 69.99  ?  83  GLU B CD  1 
ATOM   2085 O  OE1 . GLU B 1 91  ? 17.465  10.808  45.118 1.00 59.79  ?  83  GLU B OE1 1 
ATOM   2086 O  OE2 . GLU B 1 91  ? 18.072  10.704  43.008 1.00 72.51  ?  83  GLU B OE2 1 
ATOM   2087 N  N   . THR B 1 92  ? 13.901  6.352   43.603 1.00 55.00  ?  84  THR B N   1 
ATOM   2088 C  CA  . THR B 1 92  ? 13.519  5.211   42.785 1.00 59.40  ?  84  THR B CA  1 
ATOM   2089 C  C   . THR B 1 92  ? 12.131  5.319   42.168 1.00 48.52  ?  84  THR B C   1 
ATOM   2090 O  O   . THR B 1 92  ? 11.849  4.598   41.208 1.00 48.21  ?  84  THR B O   1 
ATOM   2091 C  CB  . THR B 1 92  ? 13.562  3.902   43.595 1.00 63.20  ?  84  THR B CB  1 
ATOM   2092 O  OG1 . THR B 1 92  ? 12.355  3.779   44.362 1.00 64.72  ?  84  THR B OG1 1 
ATOM   2093 C  CG2 . THR B 1 92  ? 14.759  3.868   44.520 1.00 59.24  ?  84  THR B CG2 1 
ATOM   2094 N  N   . VAL B 1 93  ? 11.254  6.174   42.691 1.00 50.46  ?  85  VAL B N   1 
ATOM   2095 C  CA  . VAL B 1 93  ? 9.888   6.304   42.183 1.00 56.37  ?  85  VAL B CA  1 
ATOM   2096 C  C   . VAL B 1 93  ? 9.652   7.680   41.559 1.00 55.43  ?  85  VAL B C   1 
ATOM   2097 O  O   . VAL B 1 93  ? 9.304   7.783   40.383 1.00 51.57  ?  85  VAL B O   1 
ATOM   2098 C  CB  . VAL B 1 93  ? 8.845   6.004   43.286 1.00 58.09  ?  85  VAL B CB  1 
ATOM   2099 C  CG1 . VAL B 1 93  ? 7.436   6.206   42.739 1.00 59.81  ?  85  VAL B CG1 1 
ATOM   2100 C  CG2 . VAL B 1 93  ? 9.023   4.591   43.814 1.00 59.32  ?  85  VAL B CG2 1 
ATOM   2101 N  N   . ILE B 1 94  ? 9.822   8.748   42.337 1.00 57.39  ?  86  ILE B N   1 
ATOM   2102 C  CA  . ILE B 1 94  ? 9.416   10.074  41.873 1.00 53.47  ?  86  ILE B CA  1 
ATOM   2103 C  C   . ILE B 1 94  ? 10.342  10.562  40.766 1.00 55.05  ?  86  ILE B C   1 
ATOM   2104 O  O   . ILE B 1 94  ? 9.906   10.813  39.636 1.00 52.35  ?  86  ILE B O   1 
ATOM   2105 C  CB  . ILE B 1 94  ? 9.364   11.064  43.052 1.00 54.98  ?  86  ILE B CB  1 
ATOM   2106 C  CG1 . ILE B 1 94  ? 8.238   10.663  44.010 1.00 55.02  ?  86  ILE B CG1 1 
ATOM   2107 C  CG2 . ILE B 1 94  ? 9.176   12.485  42.542 1.00 57.75  ?  86  ILE B CG2 1 
ATOM   2108 C  CD1 . ILE B 1 94  ? 8.213   11.448  45.302 1.00 62.23  ?  86  ILE B CD1 1 
ATOM   2109 N  N   . LYS B 1 95  ? 11.634  10.705  41.073 1.00 58.52  ?  87  LYS B N   1 
ATOM   2110 C  CA  . LYS B 1 95  ? 12.549  11.260  40.078 1.00 55.62  ?  87  LYS B CA  1 
ATOM   2111 C  C   . LYS B 1 95  ? 12.521  10.466  38.778 1.00 53.53  ?  87  LYS B C   1 
ATOM   2112 O  O   . LYS B 1 95  ? 12.459  11.085  37.700 1.00 56.55  ?  87  LYS B O   1 
ATOM   2113 C  CB  . LYS B 1 95  ? 13.970  11.333  40.649 1.00 58.55  ?  87  LYS B CB  1 
ATOM   2114 C  CG  . LYS B 1 95  ? 14.229  12.549  41.543 1.00 64.67  ?  87  LYS B CG  1 
ATOM   2115 C  CD  . LYS B 1 95  ? 15.673  12.594  42.061 1.00 67.16  ?  87  LYS B CD  1 
ATOM   2116 C  CE  . LYS B 1 95  ? 15.930  13.841  42.915 1.00 72.68  ?  87  LYS B CE  1 
ATOM   2117 N  NZ  . LYS B 1 95  ? 17.292  13.864  43.532 1.00 77.19  ?  87  LYS B NZ  1 
ATOM   2118 N  N   . PRO B 1 96  ? 12.577  9.130   38.789 1.00 48.51  ?  88  PRO B N   1 
ATOM   2119 C  CA  . PRO B 1 96  ? 12.447  8.399   37.515 1.00 51.38  ?  88  PRO B CA  1 
ATOM   2120 C  C   . PRO B 1 96  ? 11.153  8.699   36.785 1.00 54.56  ?  88  PRO B C   1 
ATOM   2121 O  O   . PRO B 1 96  ? 11.156  8.822   35.555 1.00 61.29  ?  88  PRO B O   1 
ATOM   2122 C  CB  . PRO B 1 96  ? 12.534  6.930   37.952 1.00 45.59  ?  88  PRO B CB  1 
ATOM   2123 C  CG  . PRO B 1 96  ? 13.383  6.969   39.184 1.00 50.86  ?  88  PRO B CG  1 
ATOM   2124 C  CD  . PRO B 1 96  ? 12.975  8.244   39.901 1.00 55.01  ?  88  PRO B CD  1 
ATOM   2125 N  N   . ALA B 1 97  ? 10.043  8.839   37.511 1.00 58.06  ?  89  ALA B N   1 
ATOM   2126 C  CA  . ALA B 1 97  ? 8.772   9.128   36.856 1.00 50.41  ?  89  ALA B CA  1 
ATOM   2127 C  C   . ALA B 1 97  ? 8.828   10.466  36.129 1.00 51.98  ?  89  ALA B C   1 
ATOM   2128 O  O   . ALA B 1 97  ? 8.561   10.545  34.925 1.00 56.98  ?  89  ALA B O   1 
ATOM   2129 C  CB  . ALA B 1 97  ? 7.642   9.117   37.886 1.00 59.57  ?  89  ALA B CB  1 
ATOM   2130 N  N   . LEU B 1 98  ? 9.219   11.527  36.840 1.00 56.97  ?  90  LEU B N   1 
ATOM   2131 C  CA  . LEU B 1 98  ? 9.362   12.827  36.198 1.00 55.84  ?  90  LEU B CA  1 
ATOM   2132 C  C   . LEU B 1 98  ? 10.299  12.744  35.000 1.00 55.72  ?  90  LEU B C   1 
ATOM   2133 O  O   . LEU B 1 98  ? 10.093  13.420  33.985 1.00 63.23  ?  90  LEU B O   1 
ATOM   2134 C  CB  . LEU B 1 98  ? 9.901   13.854  37.194 1.00 58.35  ?  90  LEU B CB  1 
ATOM   2135 C  CG  . LEU B 1 98  ? 9.125   14.099  38.484 1.00 54.62  ?  90  LEU B CG  1 
ATOM   2136 C  CD1 . LEU B 1 98  ? 9.977   14.964  39.407 1.00 50.29  ?  90  LEU B CD1 1 
ATOM   2137 C  CD2 . LEU B 1 98  ? 7.788   14.752  38.206 1.00 52.99  ?  90  LEU B CD2 1 
ATOM   2138 N  N   . ALA B 1 99  ? 11.351  11.933  35.111 1.00 55.96  ?  91  ALA B N   1 
ATOM   2139 C  CA  . ALA B 1 99  ? 12.309  11.819  34.018 1.00 57.97  ?  91  ALA B CA  1 
ATOM   2140 C  C   . ALA B 1 99  ? 11.680  11.176  32.791 1.00 56.75  ?  91  ALA B C   1 
ATOM   2141 O  O   . ALA B 1 99  ? 12.063  11.497  31.659 1.00 55.66  ?  91  ALA B O   1 
ATOM   2142 C  CB  . ALA B 1 99  ? 13.531  11.024  34.476 1.00 65.36  ?  91  ALA B CB  1 
ATOM   2143 N  N   . ARG B 1 100 ? 10.716  10.279  32.991 1.00 62.25  ?  92  ARG B N   1 
ATOM   2144 C  CA  . ARG B 1 100 ? 9.976   9.681   31.889 1.00 55.96  ?  92  ARG B CA  1 
ATOM   2145 C  C   . ARG B 1 100 ? 8.904   10.605  31.327 1.00 56.58  ?  92  ARG B C   1 
ATOM   2146 O  O   . ARG B 1 100 ? 8.195   10.210  30.394 1.00 60.13  ?  92  ARG B O   1 
ATOM   2147 C  CB  . ARG B 1 100 ? 9.321   8.375   32.344 1.00 56.39  ?  92  ARG B CB  1 
ATOM   2148 C  CG  . ARG B 1 100 ? 10.302  7.316   32.802 1.00 64.22  ?  92  ARG B CG  1 
ATOM   2149 C  CD  . ARG B 1 100 ? 9.630   5.959   32.920 1.00 63.06  ?  92  ARG B CD  1 
ATOM   2150 N  NE  . ARG B 1 100 ? 8.676   5.899   34.023 1.00 55.11  ?  92  ARG B NE  1 
ATOM   2151 C  CZ  . ARG B 1 100 ? 8.973   5.484   35.247 1.00 54.33  ?  92  ARG B CZ  1 
ATOM   2152 N  NH1 . ARG B 1 100 ? 10.201  5.118   35.572 1.00 44.16  ?  92  ARG B NH1 1 
ATOM   2153 N  NH2 . ARG B 1 100 ? 8.011   5.430   36.164 1.00 68.48  ?  92  ARG B NH2 1 
ATOM   2154 N  N   . GLY B 1 101 ? 8.763   11.813  31.867 1.00 54.52  ?  93  GLY B N   1 
ATOM   2155 C  CA  . GLY B 1 101 ? 7.690   12.692  31.470 1.00 56.84  ?  93  GLY B CA  1 
ATOM   2156 C  C   . GLY B 1 101 ? 6.375   12.434  32.165 1.00 60.23  ?  93  GLY B C   1 
ATOM   2157 O  O   . GLY B 1 101 ? 5.374   13.081  31.823 1.00 56.62  ?  93  GLY B O   1 
ATOM   2158 N  N   . GLN B 1 102 ? 6.335   11.491  33.100 1.00 60.12  ?  94  GLN B N   1 
ATOM   2159 C  CA  . GLN B 1 102 ? 5.168   11.304  33.944 1.00 59.49  ?  94  GLN B CA  1 
ATOM   2160 C  C   . GLN B 1 102 ? 5.102   12.399  35.002 1.00 52.54  ?  94  GLN B C   1 
ATOM   2161 O  O   . GLN B 1 102 ? 6.120   12.771  35.596 1.00 49.15  ?  94  GLN B O   1 
ATOM   2162 C  CB  . GLN B 1 102 ? 5.221   9.940   34.633 1.00 60.26  ?  94  GLN B CB  1 
ATOM   2163 C  CG  . GLN B 1 102 ? 5.165   8.727   33.719 1.00 63.63  ?  94  GLN B CG  1 
ATOM   2164 C  CD  . GLN B 1 102 ? 5.389   7.435   34.489 1.00 60.01  ?  94  GLN B CD  1 
ATOM   2165 O  OE1 . GLN B 1 102 ? 6.163   7.404   35.444 1.00 63.47  ?  94  GLN B OE1 1 
ATOM   2166 N  NE2 . GLN B 1 102 ? 4.699   6.371   34.090 1.00 60.96  ?  94  GLN B NE2 1 
ATOM   2167 N  N   . TRP B 1 103 ? 3.899   12.914  35.238 1.00 53.52  ?  95  TRP B N   1 
ATOM   2168 C  CA  . TRP B 1 103 ? 3.670   13.736  36.416 1.00 57.51  ?  95  TRP B CA  1 
ATOM   2169 C  C   . TRP B 1 103 ? 3.545   12.842  37.643 1.00 54.63  ?  95  TRP B C   1 
ATOM   2170 O  O   . TRP B 1 103 ? 3.260   11.646  37.542 1.00 54.78  ?  95  TRP B O   1 
ATOM   2171 C  CB  . TRP B 1 103 ? 2.405   14.573  36.274 1.00 55.18  ?  95  TRP B CB  1 
ATOM   2172 C  CG  . TRP B 1 103 ? 2.554   15.706  35.334 1.00 51.43  ?  95  TRP B CG  1 
ATOM   2173 C  CD1 . TRP B 1 103 ? 3.079   15.660  34.079 1.00 53.74  ?  95  TRP B CD1 1 
ATOM   2174 C  CD2 . TRP B 1 103 ? 2.160   17.065  35.557 1.00 48.79  ?  95  TRP B CD2 1 
ATOM   2175 N  NE1 . TRP B 1 103 ? 3.044   16.905  33.508 1.00 53.17  ?  95  TRP B NE1 1 
ATOM   2176 C  CE2 . TRP B 1 103 ? 2.483   17.786  34.392 1.00 48.48  ?  95  TRP B CE2 1 
ATOM   2177 C  CE3 . TRP B 1 103 ? 1.565   17.741  36.628 1.00 53.47  ?  95  TRP B CE3 1 
ATOM   2178 C  CZ2 . TRP B 1 103 ? 2.234   19.151  34.266 1.00 52.03  ?  95  TRP B CZ2 1 
ATOM   2179 C  CZ3 . TRP B 1 103 ? 1.319   19.097  36.500 1.00 54.40  ?  95  TRP B CZ3 1 
ATOM   2180 C  CH2 . TRP B 1 103 ? 1.655   19.787  35.328 1.00 56.79  ?  95  TRP B CH2 1 
ATOM   2181 N  N   . VAL B 1 104 ? 3.757   13.431  38.814 1.00 49.87  ?  96  VAL B N   1 
ATOM   2182 C  CA  . VAL B 1 104 ? 3.633   12.698  40.065 1.00 59.12  ?  96  VAL B CA  1 
ATOM   2183 C  C   . VAL B 1 104 ? 2.725   13.479  40.997 1.00 52.03  ?  96  VAL B C   1 
ATOM   2184 O  O   . VAL B 1 104 ? 2.916   14.683  41.189 1.00 49.68  ?  96  VAL B O   1 
ATOM   2185 C  CB  . VAL B 1 104 ? 5.008   12.439  40.710 1.00 59.09  ?  96  VAL B CB  1 
ATOM   2186 C  CG1 . VAL B 1 104 ? 4.850   11.558  41.926 1.00 59.31  ?  96  VAL B CG1 1 
ATOM   2187 C  CG2 . VAL B 1 104 ? 5.940   11.803  39.695 1.00 56.39  ?  96  VAL B CG2 1 
ATOM   2188 N  N   . ILE B 1 105 ? 1.725   12.792  41.546 1.00 54.55  ?  97  ILE B N   1 
ATOM   2189 C  CA  . ILE B 1 105 ? 0.846   13.324  42.580 1.00 58.13  ?  97  ILE B CA  1 
ATOM   2190 C  C   . ILE B 1 105 ? 1.123   12.527  43.843 1.00 54.75  ?  97  ILE B C   1 
ATOM   2191 O  O   . ILE B 1 105 ? 0.964   11.301  43.852 1.00 55.28  ?  97  ILE B O   1 
ATOM   2192 C  CB  . ILE B 1 105 ? -0.639  13.214  42.200 1.00 59.71  ?  97  ILE B CB  1 
ATOM   2193 C  CG1 . ILE B 1 105 ? -0.833  13.409  40.699 1.00 54.55  ?  97  ILE B CG1 1 
ATOM   2194 C  CG2 . ILE B 1 105 ? -1.455  14.215  43.009 1.00 60.87  ?  97  ILE B CG2 1 
ATOM   2195 C  CD1 . ILE B 1 105 ? -0.478  14.779  40.203 1.00 59.04  ?  97  ILE B CD1 1 
ATOM   2196 N  N   . GLY B 1 106 ? 1.519   13.218  44.907 1.00 59.20  ?  98  GLY B N   1 
ATOM   2197 C  CA  . GLY B 1 106 ? 1.852   12.543  46.142 1.00 69.70  ?  98  GLY B CA  1 
ATOM   2198 C  C   . GLY B 1 106 ? 0.942   12.964  47.272 1.00 67.62  ?  98  GLY B C   1 
ATOM   2199 O  O   . GLY B 1 106 ? 0.319   14.026  47.204 1.00 53.63  ?  98  GLY B O   1 
ATOM   2200 N  N   . ASP B 1 107 ? 0.856   12.145  48.315 1.00 81.26  ?  99  ASP B N   1 
ATOM   2201 C  CA  . ASP B 1 107 ? 0.021   12.425  49.475 1.00 86.65  ?  99  ASP B CA  1 
ATOM   2202 C  C   . ASP B 1 107 ? 0.906   12.462  50.714 1.00 85.53  ?  99  ASP B C   1 
ATOM   2203 O  O   . ASP B 1 107 ? 1.516   11.449  51.074 1.00 85.90  ?  99  ASP B O   1 
ATOM   2204 C  CB  . ASP B 1 107 ? -1.080  11.364  49.610 1.00 85.90  ?  99  ASP B CB  1 
ATOM   2205 C  CG  . ASP B 1 107 ? -2.156  11.749  50.606 1.00 92.70  ?  99  ASP B CG  1 
ATOM   2206 O  OD1 . ASP B 1 107 ? -1.839  12.442  51.595 1.00 100.03 ?  99  ASP B OD1 1 
ATOM   2207 O  OD2 . ASP B 1 107 ? -3.323  11.348  50.404 1.00 94.57  ?  99  ASP B OD2 1 
ATOM   2208 N  N   . ARG B 1 108 ? 0.935   13.621  51.387 1.00 87.51  ?  100 ARG B N   1 
ATOM   2209 C  CA  . ARG B 1 108 ? 1.552   13.782  52.711 1.00 96.86  ?  100 ARG B CA  1 
ATOM   2210 C  C   . ARG B 1 108 ? 3.079   13.664  52.690 1.00 100.74 ?  100 ARG B C   1 
ATOM   2211 O  O   . ARG B 1 108 ? 3.676   12.912  53.461 1.00 108.87 ?  100 ARG B O   1 
ATOM   2212 C  CB  . ARG B 1 108 ? 0.939   12.755  53.677 1.00 95.93  ?  100 ARG B CB  1 
ATOM   2213 C  CG  . ARG B 1 108 ? 1.220   12.995  55.148 1.00 94.61  ?  100 ARG B CG  1 
ATOM   2214 C  CD  . ARG B 1 108 ? 0.129   12.380  56.026 1.00 93.43  ?  100 ARG B CD  1 
ATOM   2215 N  NE  . ARG B 1 108 ? -0.052  10.951  55.792 1.00 85.49  ?  100 ARG B NE  1 
ATOM   2216 C  CZ  . ARG B 1 108 ? -0.982  10.425  55.005 1.00 79.09  ?  100 ARG B CZ  1 
ATOM   2217 N  NH1 . ARG B 1 108 ? -1.833  11.186  54.332 1.00 83.64  ?  100 ARG B NH1 1 
ATOM   2218 N  NH2 . ARG B 1 108 ? -1.064  9.102   54.895 1.00 74.43  ?  100 ARG B NH2 1 
ATOM   2219 N  N   . HIS B 1 109 ? 3.711   14.473  51.842 1.00 109.64 ?  101 HIS B N   1 
ATOM   2220 C  CA  . HIS B 1 109 ? 5.170   14.622  51.826 1.00 119.24 ?  101 HIS B CA  1 
ATOM   2221 C  C   . HIS B 1 109 ? 5.635   15.455  53.022 1.00 119.82 ?  101 HIS B C   1 
ATOM   2222 O  O   . HIS B 1 109 ? 5.764   16.678  52.930 1.00 118.87 ?  101 HIS B O   1 
ATOM   2223 C  CB  . HIS B 1 109 ? 5.625   15.281  50.516 1.00 127.01 ?  101 HIS B CB  1 
ATOM   2224 C  CG  . HIS B 1 109 ? 7.080   15.089  50.195 1.00 138.76 ?  101 HIS B CG  1 
ATOM   2225 N  ND1 . HIS B 1 109 ? 7.589   13.899  49.720 1.00 140.22 ?  101 HIS B ND1 1 
ATOM   2226 C  CD2 . HIS B 1 109 ? 8.125   15.949  50.243 1.00 145.30 ?  101 HIS B CD2 1 
ATOM   2227 C  CE1 . HIS B 1 109 ? 8.886   14.029  49.506 1.00 138.18 ?  101 HIS B CE1 1 
ATOM   2228 N  NE2 . HIS B 1 109 ? 9.237   15.263  49.817 1.00 144.13 ?  101 HIS B NE2 1 
ATOM   2229 N  N   . GLN B 1 125 ? 13.258  20.297  66.273 1.00 141.92 ?  117 GLN B N   1 
ATOM   2230 C  CA  . GLN B 1 125 ? 12.466  20.027  65.078 1.00 177.59 ?  117 GLN B CA  1 
ATOM   2231 C  C   . GLN B 1 125 ? 13.074  20.720  63.863 1.00 170.15 ?  117 GLN B C   1 
ATOM   2232 O  O   . GLN B 1 125 ? 12.872  20.290  62.730 1.00 134.39 ?  117 GLN B O   1 
ATOM   2233 C  CB  . GLN B 1 125 ? 11.021  20.480  65.272 1.00 135.22 ?  117 GLN B CB  1 
ATOM   2234 N  N   . THR B 1 126 ? 13.813  21.808  64.104 1.00 143.92 ?  118 THR B N   1 
ATOM   2235 C  CA  . THR B 1 126 ? 14.600  22.404  63.030 1.00 147.77 ?  118 THR B CA  1 
ATOM   2236 C  C   . THR B 1 126 ? 15.597  21.397  62.470 1.00 140.68 ?  118 THR B C   1 
ATOM   2237 O  O   . THR B 1 126 ? 16.005  21.502  61.307 1.00 134.70 ?  118 THR B O   1 
ATOM   2238 C  CB  . THR B 1 126 ? 15.331  23.650  63.536 1.00 153.20 ?  118 THR B CB  1 
ATOM   2239 O  OG1 . THR B 1 126 ? 14.378  24.610  64.011 1.00 148.69 ?  118 THR B OG1 1 
ATOM   2240 C  CG2 . THR B 1 126 ? 16.171  24.278  62.428 1.00 151.79 ?  118 THR B CG2 1 
ATOM   2241 N  N   . MET B 1 127 ? 15.994  20.414  63.284 1.00 135.78 ?  119 MET B N   1 
ATOM   2242 C  CA  . MET B 1 127 ? 16.936  19.391  62.846 1.00 130.38 ?  119 MET B CA  1 
ATOM   2243 C  C   . MET B 1 127 ? 16.315  18.423  61.847 1.00 128.04 ?  119 MET B C   1 
ATOM   2244 O  O   . MET B 1 127 ? 17.051  17.793  61.079 1.00 123.78 ?  119 MET B O   1 
ATOM   2245 C  CB  . MET B 1 127 ? 17.467  18.632  64.067 1.00 131.77 ?  119 MET B CB  1 
ATOM   2246 C  CG  . MET B 1 127 ? 18.242  19.491  65.075 1.00 131.73 ?  119 MET B CG  1 
ATOM   2247 S  SD  . MET B 1 127 ? 17.257  20.673  66.033 1.00 136.57 ?  119 MET B SD  1 
ATOM   2248 C  CE  . MET B 1 127 ? 16.919  19.754  67.535 1.00 127.26 ?  119 MET B CE  1 
ATOM   2249 N  N   . LEU B 1 128 ? 14.986  18.295  61.838 1.00 134.26 ?  120 LEU B N   1 
ATOM   2250 C  CA  . LEU B 1 128 ? 14.329  17.507  60.802 1.00 121.62 ?  120 LEU B CA  1 
ATOM   2251 C  C   . LEU B 1 128 ? 14.641  18.062  59.417 1.00 125.91 ?  120 LEU B C   1 
ATOM   2252 O  O   . LEU B 1 128 ? 14.911  17.303  58.477 1.00 123.75 ?  120 LEU B O   1 
ATOM   2253 C  CB  . LEU B 1 128 ? 12.818  17.495  61.033 1.00 130.02 ?  120 LEU B CB  1 
ATOM   2254 C  CG  . LEU B 1 128 ? 12.193  16.374  61.867 1.00 118.66 ?  120 LEU B CG  1 
ATOM   2255 C  CD1 . LEU B 1 128 ? 11.905  15.168  60.974 1.00 112.96 ?  120 LEU B CD1 1 
ATOM   2256 C  CD2 . LEU B 1 128 ? 13.073  15.986  63.042 1.00 109.40 ?  120 LEU B CD2 1 
ATOM   2257 N  N   . ALA B 1 129 ? 14.608  19.389  59.272 1.00 120.73 ?  121 ALA B N   1 
ATOM   2258 C  CA  . ALA B 1 129 ? 14.836  19.998  57.967 1.00 113.31 ?  121 ALA B CA  1 
ATOM   2259 C  C   . ALA B 1 129 ? 16.299  19.918  57.551 1.00 126.09 ?  121 ALA B C   1 
ATOM   2260 O  O   . ALA B 1 129 ? 16.598  19.875  56.352 1.00 114.54 ?  121 ALA B O   1 
ATOM   2261 C  CB  . ALA B 1 129 ? 14.372  21.455  57.980 1.00 113.55 ?  121 ALA B CB  1 
ATOM   2262 N  N   . THR B 1 130 ? 17.221  19.902  58.513 1.00 142.69 ?  122 THR B N   1 
ATOM   2263 C  CA  . THR B 1 130 ? 18.636  19.843  58.163 1.00 151.45 ?  122 THR B CA  1 
ATOM   2264 C  C   . THR B 1 130 ? 18.988  18.528  57.477 1.00 137.03 ?  122 THR B C   1 
ATOM   2265 O  O   . THR B 1 130 ? 19.873  18.504  56.614 1.00 140.93 ?  122 THR B O   1 
ATOM   2266 C  CB  . THR B 1 130 ? 19.489  20.042  59.414 1.00 167.89 ?  122 THR B CB  1 
ATOM   2267 O  OG1 . THR B 1 130 ? 19.176  19.025  60.373 1.00 125.06 ?  122 THR B OG1 1 
ATOM   2268 C  CG2 . THR B 1 130 ? 19.224  21.414  60.026 1.00 138.67 ?  122 THR B CG2 1 
ATOM   2269 N  N   . LEU B 1 131 ? 18.321  17.430  57.847 1.00 132.29 ?  123 LEU B N   1 
ATOM   2270 C  CA  . LEU B 1 131 ? 18.498  16.188  57.104 1.00 131.44 ?  123 LEU B CA  1 
ATOM   2271 C  C   . LEU B 1 131 ? 18.029  16.345  55.664 1.00 126.81 ?  123 LEU B C   1 
ATOM   2272 O  O   . LEU B 1 131 ? 18.707  15.899  54.729 1.00 125.37 ?  123 LEU B O   1 
ATOM   2273 C  CB  . LEU B 1 131 ? 17.728  15.055  57.772 1.00 117.25 ?  123 LEU B CB  1 
ATOM   2274 C  CG  . LEU B 1 131 ? 18.253  14.487  59.085 1.00 110.35 ?  123 LEU B CG  1 
ATOM   2275 C  CD1 . LEU B 1 131 ? 17.261  13.452  59.597 1.00 118.48 ?  123 LEU B CD1 1 
ATOM   2276 C  CD2 . LEU B 1 131 ? 19.623  13.877  58.914 1.00 91.61  ?  123 LEU B CD2 1 
ATOM   2277 N  N   . ARG B 1 132 ? 16.870  16.974  55.468 1.00 105.63 ?  124 ARG B N   1 
ATOM   2278 C  CA  . ARG B 1 132 ? 16.348  17.176  54.121 1.00 104.07 ?  124 ARG B CA  1 
ATOM   2279 C  C   . ARG B 1 132 ? 17.360  17.914  53.255 1.00 101.73 ?  124 ARG B C   1 
ATOM   2280 O  O   . ARG B 1 132 ? 17.686  17.474  52.147 1.00 104.80 ?  124 ARG B O   1 
ATOM   2281 C  CB  . ARG B 1 132 ? 15.027  17.944  54.193 1.00 102.39 ?  124 ARG B CB  1 
ATOM   2282 C  CG  . ARG B 1 132 ? 14.377  18.212  52.845 1.00 102.42 ?  124 ARG B CG  1 
ATOM   2283 C  CD  . ARG B 1 132 ? 13.012  18.878  52.993 1.00 112.08 ?  124 ARG B CD  1 
ATOM   2284 N  NE  . ARG B 1 132 ? 12.316  18.959  51.713 1.00 123.07 ?  124 ARG B NE  1 
ATOM   2285 C  CZ  . ARG B 1 132 ? 11.445  18.062  51.270 1.00 127.28 ?  124 ARG B CZ  1 
ATOM   2286 N  NH1 . ARG B 1 132 ? 11.094  17.018  52.003 1.00 122.87 ?  124 ARG B NH1 1 
ATOM   2287 N  NH2 . ARG B 1 132 ? 10.915  18.216  50.060 1.00 113.80 ?  124 ARG B NH2 1 
ATOM   2288 N  N   . ASP B 1 133 ? 17.899  19.027  53.762 1.00 114.92 ?  125 ASP B N   1 
ATOM   2289 C  CA  . ASP B 1 133 ? 18.854  19.812  52.986 1.00 109.89 ?  125 ASP B CA  1 
ATOM   2290 C  C   . ASP B 1 133 ? 20.137  19.044  52.704 1.00 105.77 ?  125 ASP B C   1 
ATOM   2291 O  O   . ASP B 1 133 ? 20.886  19.419  51.796 1.00 104.38 ?  125 ASP B O   1 
ATOM   2292 C  CB  . ASP B 1 133 ? 19.179  21.116  53.723 1.00 109.84 ?  125 ASP B CB  1 
ATOM   2293 C  CG  . ASP B 1 133 ? 17.949  21.970  53.967 1.00 103.62 ?  125 ASP B CG  1 
ATOM   2294 O  OD1 . ASP B 1 133 ? 16.987  21.876  53.175 1.00 103.92 ?  125 ASP B OD1 1 
ATOM   2295 O  OD2 . ASP B 1 133 ? 17.943  22.740  54.953 1.00 110.52 ?  125 ASP B OD2 1 
ATOM   2296 N  N   . ALA B 1 134 ? 20.407  17.981  53.458 1.00 125.39 ?  126 ALA B N   1 
ATOM   2297 C  CA  . ALA B 1 134 ? 21.604  17.175  53.259 1.00 134.22 ?  126 ALA B CA  1 
ATOM   2298 C  C   . ALA B 1 134 ? 21.393  16.087  52.210 1.00 132.38 ?  126 ALA B C   1 
ATOM   2299 O  O   . ALA B 1 134 ? 22.221  15.923  51.308 1.00 166.51 ?  126 ALA B O   1 
ATOM   2300 C  CB  . ALA B 1 134 ? 22.032  16.541  54.589 1.00 110.75 ?  126 ALA B CB  1 
ATOM   2301 N  N   . VAL B 1 135 ? 20.286  15.354  52.306 1.00 109.79 ?  127 VAL B N   1 
ATOM   2302 C  CA  . VAL B 1 135 ? 20.068  14.182  51.465 1.00 105.68 ?  127 VAL B CA  1 
ATOM   2303 C  C   . VAL B 1 135 ? 19.321  14.539  50.184 1.00 100.35 ?  127 VAL B C   1 
ATOM   2304 O  O   . VAL B 1 135 ? 19.712  14.119  49.093 1.00 91.02  ?  127 VAL B O   1 
ATOM   2305 C  CB  . VAL B 1 135 ? 19.327  13.090  52.269 1.00 103.74 ?  127 VAL B CB  1 
ATOM   2306 C  CG1 . VAL B 1 135 ? 20.123  12.714  53.519 1.00 101.53 ?  127 VAL B CG1 1 
ATOM   2307 C  CG2 . VAL B 1 135 ? 17.929  13.544  52.661 1.00 107.87 ?  127 VAL B CG2 1 
ATOM   2308 N  N   . LEU B 1 136 ? 18.242  15.321  50.280 1.00 104.08 ?  128 LEU B N   1 
ATOM   2309 C  CA  . LEU B 1 136 ? 17.469  15.687  49.099 1.00 103.95 ?  128 LEU B CA  1 
ATOM   2310 C  C   . LEU B 1 136 ? 17.984  16.939  48.403 1.00 91.99  ?  128 LEU B C   1 
ATOM   2311 O  O   . LEU B 1 136 ? 17.684  17.143  47.220 1.00 89.94  ?  128 LEU B O   1 
ATOM   2312 C  CB  . LEU B 1 136 ? 16.000  15.913  49.469 1.00 103.53 ?  128 LEU B CB  1 
ATOM   2313 C  CG  . LEU B 1 136 ? 15.282  14.723  50.100 1.00 96.62  ?  128 LEU B CG  1 
ATOM   2314 C  CD1 . LEU B 1 136 ? 13.833  15.075  50.407 1.00 99.92  ?  128 LEU B CD1 1 
ATOM   2315 C  CD2 . LEU B 1 136 ? 15.368  13.504  49.194 1.00 112.75 ?  128 LEU B CD2 1 
ATOM   2316 N  N   . GLY B 1 137 ? 18.738  17.786  49.107 1.00 91.33  ?  129 GLY B N   1 
ATOM   2317 C  CA  . GLY B 1 137 ? 19.250  18.987  48.476 1.00 86.50  ?  129 GLY B CA  1 
ATOM   2318 C  C   . GLY B 1 137 ? 18.136  19.951  48.118 1.00 89.22  ?  129 GLY B C   1 
ATOM   2319 O  O   . GLY B 1 137 ? 17.207  20.188  48.895 1.00 94.17  ?  129 GLY B O   1 
ATOM   2320 N  N   . ASP B 1 138 ? 18.225  20.510  46.913 1.00 85.35  ?  130 ASP B N   1 
ATOM   2321 C  CA  . ASP B 1 138 ? 17.277  21.526  46.474 1.00 85.70  ?  130 ASP B CA  1 
ATOM   2322 C  C   . ASP B 1 138 ? 15.975  20.936  45.950 1.00 80.60  ?  130 ASP B C   1 
ATOM   2323 O  O   . ASP B 1 138 ? 15.096  21.694  45.528 1.00 82.15  ?  130 ASP B O   1 
ATOM   2324 C  CB  . ASP B 1 138 ? 17.912  22.402  45.392 1.00 80.81  ?  130 ASP B CB  1 
ATOM   2325 C  CG  . ASP B 1 138 ? 18.335  21.606  44.178 1.00 79.33  ?  130 ASP B CG  1 
ATOM   2326 O  OD1 . ASP B 1 138 ? 18.101  20.378  44.164 1.00 83.97  ?  130 ASP B OD1 1 
ATOM   2327 O  OD2 . ASP B 1 138 ? 18.901  22.204  43.242 1.00 84.97  ?  130 ASP B OD2 1 
ATOM   2328 N  N   . PHE B 1 139 ? 15.836  19.613  45.961 1.00 77.43  ?  131 PHE B N   1 
ATOM   2329 C  CA  . PHE B 1 139 ? 14.620  18.983  45.470 1.00 78.07  ?  131 PHE B CA  1 
ATOM   2330 C  C   . PHE B 1 139 ? 13.421  19.398  46.311 1.00 72.36  ?  131 PHE B C   1 
ATOM   2331 O  O   . PHE B 1 139 ? 13.422  19.250  47.534 1.00 78.90  ?  131 PHE B O   1 
ATOM   2332 C  CB  . PHE B 1 139 ? 14.778  17.462  45.489 1.00 85.01  ?  131 PHE B CB  1 
ATOM   2333 C  CG  . PHE B 1 139 ? 13.565  16.720  45.012 1.00 79.75  ?  131 PHE B CG  1 
ATOM   2334 C  CD1 . PHE B 1 139 ? 13.428  16.378  43.679 1.00 82.60  ?  131 PHE B CD1 1 
ATOM   2335 C  CD2 . PHE B 1 139 ? 12.562  16.364  45.897 1.00 81.43  ?  131 PHE B CD2 1 
ATOM   2336 C  CE1 . PHE B 1 139 ? 12.313  15.696  43.235 1.00 77.75  ?  131 PHE B CE1 1 
ATOM   2337 C  CE2 . PHE B 1 139 ? 11.445  15.682  45.458 1.00 84.99  ?  131 PHE B CE2 1 
ATOM   2338 C  CZ  . PHE B 1 139 ? 11.321  15.348  44.125 1.00 78.56  ?  131 PHE B CZ  1 
ATOM   2339 N  N   . ARG B 1 140 ? 12.392  19.910  45.644 1.00 69.92  ?  132 ARG B N   1 
ATOM   2340 C  CA  . ARG B 1 140 ? 11.145  20.323  46.266 1.00 68.72  ?  132 ARG B CA  1 
ATOM   2341 C  C   . ARG B 1 140 ? 9.997   19.975  45.333 1.00 69.50  ?  132 ARG B C   1 
ATOM   2342 O  O   . ARG B 1 140 ? 10.170  19.980  44.109 1.00 69.03  ?  132 ARG B O   1 
ATOM   2343 C  CB  . ARG B 1 140 ? 11.106  21.833  46.540 1.00 69.07  ?  132 ARG B CB  1 
ATOM   2344 C  CG  . ARG B 1 140 ? 12.244  22.368  47.379 1.00 74.54  ?  132 ARG B CG  1 
ATOM   2345 C  CD  . ARG B 1 140 ? 12.029  22.087  48.856 1.00 81.92  ?  132 ARG B CD  1 
ATOM   2346 N  NE  . ARG B 1 140 ? 13.058  22.726  49.666 1.00 86.03  ?  132 ARG B NE  1 
ATOM   2347 C  CZ  . ARG B 1 140 ? 14.235  22.184  49.950 1.00 96.41  ?  132 ARG B CZ  1 
ATOM   2348 N  NH1 . ARG B 1 140 ? 14.553  20.967  49.538 1.00 96.60  ?  132 ARG B NH1 1 
ATOM   2349 N  NH2 . ARG B 1 140 ? 15.117  22.883  50.661 1.00 95.98  ?  132 ARG B NH2 1 
ATOM   2350 N  N   . PRO B 1 141 ? 8.807   19.709  45.873 1.00 67.78  ?  133 PRO B N   1 
ATOM   2351 C  CA  . PRO B 1 141 ? 7.642   19.566  44.995 1.00 59.31  ?  133 PRO B CA  1 
ATOM   2352 C  C   . PRO B 1 141 ? 7.427   20.860  44.233 1.00 52.15  ?  133 PRO B C   1 
ATOM   2353 O  O   . PRO B 1 141 ? 7.734   21.951  44.717 1.00 55.42  ?  133 PRO B O   1 
ATOM   2354 C  CB  . PRO B 1 141 ? 6.482   19.275  45.961 1.00 60.35  ?  133 PRO B CB  1 
ATOM   2355 C  CG  . PRO B 1 141 ? 7.130   18.899  47.250 1.00 67.35  ?  133 PRO B CG  1 
ATOM   2356 C  CD  . PRO B 1 141 ? 8.420   19.664  47.296 1.00 65.54  ?  133 PRO B CD  1 
ATOM   2357 N  N   . HIS B 1 142 ? 6.929   20.730  43.011 1.00 55.52  ?  134 HIS B N   1 
ATOM   2358 C  CA  . HIS B 1 142 ? 6.651   21.921  42.220 1.00 55.58  ?  134 HIS B CA  1 
ATOM   2359 C  C   . HIS B 1 142 ? 5.472   22.683  42.786 1.00 51.64  ?  134 HIS B C   1 
ATOM   2360 O  O   . HIS B 1 142 ? 5.477   23.919  42.818 1.00 50.17  ?  134 HIS B O   1 
ATOM   2361 C  CB  . HIS B 1 142 ? 6.398   21.520  40.782 1.00 55.54  ?  134 HIS B CB  1 
ATOM   2362 C  CG  . HIS B 1 142 ? 7.606   20.947  40.131 1.00 52.48  ?  134 HIS B CG  1 
ATOM   2363 N  ND1 . HIS B 1 142 ? 8.107   19.707  40.460 1.00 58.14  ?  134 HIS B ND1 1 
ATOM   2364 C  CD2 . HIS B 1 142 ? 8.456   21.470  39.219 1.00 64.71  ?  134 HIS B CD2 1 
ATOM   2365 C  CE1 . HIS B 1 142 ? 9.195   19.477  39.751 1.00 73.63  ?  134 HIS B CE1 1 
ATOM   2366 N  NE2 . HIS B 1 142 ? 9.425   20.529  38.986 1.00 80.47  ?  134 HIS B NE2 1 
ATOM   2367 N  N   . LEU B 1 143 ? 4.456   21.959  43.227 1.00 54.00  ?  135 LEU B N   1 
ATOM   2368 C  CA  . LEU B 1 143 ? 3.289   22.531  43.867 1.00 54.12  ?  135 LEU B CA  1 
ATOM   2369 C  C   . LEU B 1 143 ? 2.998   21.706  45.106 1.00 53.37  ?  135 LEU B C   1 
ATOM   2370 O  O   . LEU B 1 143 ? 2.991   20.474  45.042 1.00 52.42  ?  135 LEU B O   1 
ATOM   2371 C  CB  . LEU B 1 143 ? 2.083   22.521  42.936 1.00 57.08  ?  135 LEU B CB  1 
ATOM   2372 C  CG  . LEU B 1 143 ? 0.774   22.960  43.592 1.00 56.57  ?  135 LEU B CG  1 
ATOM   2373 C  CD1 . LEU B 1 143 ? 0.846   24.422  44.006 1.00 58.04  ?  135 LEU B CD1 1 
ATOM   2374 C  CD2 . LEU B 1 143 ? -0.380  22.704  42.637 1.00 62.50  ?  135 LEU B CD2 1 
ATOM   2375 N  N   . THR B 1 144 ? 2.779   22.384  46.225 1.00 60.22  ?  136 THR B N   1 
ATOM   2376 C  CA  . THR B 1 144 ? 2.218   21.773  47.420 1.00 60.51  ?  136 THR B CA  1 
ATOM   2377 C  C   . THR B 1 144 ? 0.795   22.291  47.558 1.00 58.32  ?  136 THR B C   1 
ATOM   2378 O  O   . THR B 1 144 ? 0.558   23.497  47.434 1.00 54.97  ?  136 THR B O   1 
ATOM   2379 C  CB  . THR B 1 144 ? 3.035   22.106  48.665 1.00 62.68  ?  136 THR B CB  1 
ATOM   2380 O  OG1 . THR B 1 144 ? 4.430   22.109  48.337 1.00 63.96  ?  136 THR B OG1 1 
ATOM   2381 C  CG2 . THR B 1 144 ? 2.787   21.068  49.757 1.00 70.32  ?  136 THR B CG2 1 
ATOM   2382 N  N   . LEU B 1 145 ? -0.143  21.385  47.771 1.00 64.80  ?  137 LEU B N   1 
ATOM   2383 C  CA  . LEU B 1 145 ? -1.557  21.721  47.908 1.00 65.93  ?  137 LEU B CA  1 
ATOM   2384 C  C   . LEU B 1 145 ? -1.928  21.460  49.362 1.00 68.14  ?  137 LEU B C   1 
ATOM   2385 O  O   . LEU B 1 145 ? -2.115  20.311  49.767 1.00 65.90  ?  137 LEU B O   1 
ATOM   2386 C  CB  . LEU B 1 145 ? -2.409  20.896  46.961 1.00 68.74  ?  137 LEU B CB  1 
ATOM   2387 C  CG  . LEU B 1 145 ? -3.918  21.048  47.142 1.00 77.70  ?  137 LEU B CG  1 
ATOM   2388 C  CD1 . LEU B 1 145 ? -4.335  22.483  46.881 1.00 84.37  ?  137 LEU B CD1 1 
ATOM   2389 C  CD2 . LEU B 1 145 ? -4.650  20.089  46.220 1.00 81.15  ?  137 LEU B CD2 1 
ATOM   2390 N  N   . TYR B 1 146 ? -2.035  22.532  50.142 1.00 71.13  ?  138 TYR B N   1 
ATOM   2391 C  CA  . TYR B 1 146 ? -2.347  22.431  51.561 1.00 74.84  ?  138 TYR B CA  1 
ATOM   2392 C  C   . TYR B 1 146 ? -3.861  22.436  51.735 1.00 75.56  ?  138 TYR B C   1 
ATOM   2393 O  O   . TYR B 1 146 ? -4.539  23.357  51.268 1.00 71.17  ?  138 TYR B O   1 
ATOM   2394 C  CB  . TYR B 1 146 ? -1.710  23.574  52.343 1.00 70.91  ?  138 TYR B CB  1 
ATOM   2395 C  CG  . TYR B 1 146 ? -2.117  23.604  53.799 1.00 79.72  ?  138 TYR B CG  1 
ATOM   2396 C  CD1 . TYR B 1 146 ? -2.100  22.447  54.566 1.00 83.09  ?  138 TYR B CD1 1 
ATOM   2397 C  CD2 . TYR B 1 146 ? -2.511  24.788  54.409 1.00 79.72  ?  138 TYR B CD2 1 
ATOM   2398 C  CE1 . TYR B 1 146 ? -2.470  22.466  55.897 1.00 89.46  ?  138 TYR B CE1 1 
ATOM   2399 C  CE2 . TYR B 1 146 ? -2.880  24.817  55.741 1.00 86.32  ?  138 TYR B CE2 1 
ATOM   2400 C  CZ  . TYR B 1 146 ? -2.860  23.652  56.480 1.00 91.33  ?  138 TYR B CZ  1 
ATOM   2401 O  OH  . TYR B 1 146 ? -3.227  23.675  57.806 1.00 89.11  ?  138 TYR B OH  1 
ATOM   2402 N  N   . LEU B 1 147 ? -4.385  21.409  52.395 1.00 81.98  ?  139 LEU B N   1 
ATOM   2403 C  CA  . LEU B 1 147 ? -5.798  21.322  52.742 1.00 82.29  ?  139 LEU B CA  1 
ATOM   2404 C  C   . LEU B 1 147 ? -5.929  21.730  54.205 1.00 82.30  ?  139 LEU B C   1 
ATOM   2405 O  O   . LEU B 1 147 ? -5.525  20.984  55.102 1.00 88.52  ?  139 LEU B O   1 
ATOM   2406 C  CB  . LEU B 1 147 ? -6.335  19.912  52.512 1.00 86.19  ?  139 LEU B CB  1 
ATOM   2407 C  CG  . LEU B 1 147 ? -6.317  19.408  51.070 1.00 75.91  ?  139 LEU B CG  1 
ATOM   2408 C  CD1 . LEU B 1 147 ? -6.796  17.967  50.971 1.00 73.59  ?  139 LEU B CD1 1 
ATOM   2409 C  CD2 . LEU B 1 147 ? -7.167  20.308  50.183 1.00 84.64  ?  139 LEU B CD2 1 
ATOM   2410 N  N   . ASP B 1 148 ? -6.482  22.912  54.444 1.00 88.99  ?  140 ASP B N   1 
ATOM   2411 C  CA  . ASP B 1 148 ? -6.548  23.471  55.785 1.00 83.37  ?  140 ASP B CA  1 
ATOM   2412 C  C   . ASP B 1 148 ? -7.853  23.066  56.458 1.00 92.65  ?  140 ASP B C   1 
ATOM   2413 O  O   . ASP B 1 148 ? -8.939  23.395  55.971 1.00 97.39  ?  140 ASP B O   1 
ATOM   2414 C  CB  . ASP B 1 148 ? -6.428  24.995  55.736 1.00 90.82  ?  140 ASP B CB  1 
ATOM   2415 C  CG  . ASP B 1 148 ? -6.574  25.629  57.098 1.00 101.19 ?  140 ASP B CG  1 
ATOM   2416 O  OD1 . ASP B 1 148 ? -5.577  25.642  57.849 1.00 100.15 ?  140 ASP B OD1 1 
ATOM   2417 O  OD2 . ASP B 1 148 ? -7.687  26.099  57.417 1.00 108.79 ?  140 ASP B OD2 1 
ATOM   2418 N  N   . VAL B 1 149 ? -7.744  22.357  57.577 1.00 104.50 ?  141 VAL B N   1 
ATOM   2419 C  CA  . VAL B 1 149 ? -8.869  22.121  58.474 1.00 111.72 ?  141 VAL B CA  1 
ATOM   2420 C  C   . VAL B 1 149 ? -8.450  22.548  59.874 1.00 119.46 ?  141 VAL B C   1 
ATOM   2421 O  O   . VAL B 1 149 ? -7.290  22.368  60.265 1.00 114.42 ?  141 VAL B O   1 
ATOM   2422 C  CB  . VAL B 1 149 ? -9.333  20.649  58.488 1.00 122.43 ?  141 VAL B CB  1 
ATOM   2423 C  CG1 . VAL B 1 149 ? -10.133 20.330  57.241 1.00 116.05 ?  141 VAL B CG1 1 
ATOM   2424 C  CG2 . VAL B 1 149 ? -8.145  19.714  58.623 1.00 116.82 ?  141 VAL B CG2 1 
ATOM   2425 N  N   . THR B 1 150 ? -9.382  23.138  60.617 1.00 128.96 ?  142 THR B N   1 
ATOM   2426 C  CA  . THR B 1 150 ? -9.135  23.403  62.021 1.00 121.61 ?  142 THR B CA  1 
ATOM   2427 C  C   . THR B 1 150 ? -9.009  22.073  62.761 1.00 126.68 ?  142 THR B C   1 
ATOM   2428 O  O   . THR B 1 150 ? -9.768  21.142  62.484 1.00 134.36 ?  142 THR B O   1 
ATOM   2429 C  CB  . THR B 1 150 ? -10.270 24.226  62.618 1.00 114.77 ?  142 THR B CB  1 
ATOM   2430 O  OG1 . THR B 1 150 ? -11.304 23.346  63.076 1.00 123.94 ?  142 THR B OG1 1 
ATOM   2431 C  CG2 . THR B 1 150 ? -10.857 25.191  61.591 1.00 97.18  ?  142 THR B CG2 1 
ATOM   2432 N  N   . PRO B 1 151 ? -8.075  21.948  63.709 1.00 115.92 ?  143 PRO B N   1 
ATOM   2433 C  CA  . PRO B 1 151 ? -7.899  20.638  64.365 1.00 119.20 ?  143 PRO B CA  1 
ATOM   2434 C  C   . PRO B 1 151 ? -9.197  20.076  64.921 1.00 121.27 ?  143 PRO B C   1 
ATOM   2435 O  O   . PRO B 1 151 ? -9.331  18.852  65.052 1.00 122.85 ?  143 PRO B O   1 
ATOM   2436 C  CB  . PRO B 1 151 ? -6.880  20.932  65.477 1.00 117.58 ?  143 PRO B CB  1 
ATOM   2437 C  CG  . PRO B 1 151 ? -6.137  22.139  65.004 1.00 115.79 ?  143 PRO B CG  1 
ATOM   2438 C  CD  . PRO B 1 151 ? -7.146  22.965  64.240 1.00 115.10 ?  143 PRO B CD  1 
ATOM   2439 N  N   . GLU B 1 152 ? -10.162 20.938  65.254 1.00 127.08 ?  144 GLU B N   1 
ATOM   2440 C  CA  . GLU B 1 152 ? -11.476 20.455  65.667 1.00 127.77 ?  144 GLU B CA  1 
ATOM   2441 C  C   . GLU B 1 152 ? -12.184 19.748  64.519 1.00 126.64 ?  144 GLU B C   1 
ATOM   2442 O  O   . GLU B 1 152 ? -12.578 18.582  64.646 1.00 133.95 ?  144 GLU B O   1 
ATOM   2443 C  CB  . GLU B 1 152 ? -12.317 21.631  66.174 1.00 134.09 ?  144 GLU B CB  1 
ATOM   2444 C  CG  . GLU B 1 152 ? -13.517 21.253  67.040 1.00 147.07 ?  144 GLU B CG  1 
ATOM   2445 C  CD  . GLU B 1 152 ? -14.807 21.085  66.249 1.00 151.73 ?  144 GLU B CD  1 
ATOM   2446 O  OE1 . GLU B 1 152 ? -14.812 21.351  65.029 1.00 150.11 ?  144 GLU B OE1 1 
ATOM   2447 O  OE2 . GLU B 1 152 ? -15.824 20.685  66.857 1.00 155.08 ?  144 GLU B OE2 1 
ATOM   2448 N  N   . VAL B 1 153 ? -12.306 20.418  63.373 1.00 172.62 ?  145 VAL B N   1 
ATOM   2449 C  CA  . VAL B 1 153 ? -13.045 19.848  62.251 1.00 174.98 ?  145 VAL B CA  1 
ATOM   2450 C  C   . VAL B 1 153 ? -12.353 18.592  61.740 1.00 163.78 ?  145 VAL B C   1 
ATOM   2451 O  O   . VAL B 1 153 ? -13.007 17.591  61.420 1.00 153.32 ?  145 VAL B O   1 
ATOM   2452 C  CB  . VAL B 1 153 ? -13.210 20.901  61.138 1.00 145.88 ?  145 VAL B CB  1 
ATOM   2453 C  CG1 . VAL B 1 153 ? -13.734 20.260  59.866 1.00 130.63 ?  145 VAL B CG1 1 
ATOM   2454 C  CG2 . VAL B 1 153 ? -14.142 22.016  61.601 1.00 114.62 ?  145 VAL B CG2 1 
ATOM   2455 N  N   . GLY B 1 154 ? -11.023 18.622  61.651 1.00 160.78 ?  146 GLY B N   1 
ATOM   2456 C  CA  . GLY B 1 154 ? -10.304 17.471  61.132 1.00 163.31 ?  146 GLY B CA  1 
ATOM   2457 C  C   . GLY B 1 154 ? -10.461 16.237  61.997 1.00 142.91 ?  146 GLY B C   1 
ATOM   2458 O  O   . GLY B 1 154 ? -10.622 15.125  61.489 1.00 135.15 ?  146 GLY B O   1 
ATOM   2459 N  N   . LEU B 1 155 ? -10.402 16.413  63.318 1.00 146.74 ?  147 LEU B N   1 
ATOM   2460 C  CA  . LEU B 1 155 ? -10.544 15.266  64.209 1.00 140.71 ?  147 LEU B CA  1 
ATOM   2461 C  C   . LEU B 1 155 ? -11.950 14.684  64.140 1.00 109.60 ?  147 LEU B C   1 
ATOM   2462 O  O   . LEU B 1 155 ? -12.121 13.461  64.203 1.00 122.28 ?  147 LEU B O   1 
ATOM   2463 C  CB  . LEU B 1 155 ? -10.186 15.663  65.640 1.00 160.70 ?  147 LEU B CB  1 
ATOM   2464 C  CG  . LEU B 1 155 ? -8.741  15.353  66.042 1.00 160.16 ?  147 LEU B CG  1 
ATOM   2465 C  CD1 . LEU B 1 155 ? -7.758  16.126  65.176 1.00 130.70 ?  147 LEU B CD1 1 
ATOM   2466 C  CD2 . LEU B 1 155 ? -8.509  15.653  67.517 1.00 123.51 ?  147 LEU B CD2 1 
ATOM   2467 N  N   . LYS B 1 156 ? -12.969 15.539  64.011 1.00 126.06 ?  148 LYS B N   1 
ATOM   2468 C  CA  . LYS B 1 156 ? -14.332 15.032  63.882 1.00 111.07 ?  148 LYS B CA  1 
ATOM   2469 C  C   . LYS B 1 156 ? -14.464 14.128  62.663 1.00 126.99 ?  148 LYS B C   1 
ATOM   2470 O  O   . LYS B 1 156 ? -15.065 13.049  62.743 1.00 137.17 ?  148 LYS B O   1 
ATOM   2471 C  CB  . LYS B 1 156 ? -15.324 16.193  63.790 1.00 117.09 ?  148 LYS B CB  1 
ATOM   2472 C  CG  . LYS B 1 156 ? -15.445 17.006  65.072 1.00 130.76 ?  148 LYS B CG  1 
ATOM   2473 C  CD  . LYS B 1 156 ? -16.799 17.697  65.205 1.00 128.29 ?  148 LYS B CD  1 
ATOM   2474 C  CE  . LYS B 1 156 ? -17.247 17.699  66.663 1.00 209.91 ?  148 LYS B CE  1 
ATOM   2475 N  NZ  . LYS B 1 156 ? -18.166 18.825  66.985 1.00 174.85 ?  148 LYS B NZ  1 
ATOM   2476 N  N   . ARG B 1 157 ? -13.902 14.545  61.531 1.00 131.69 ?  149 ARG B N   1 
ATOM   2477 C  CA  . ARG B 1 157 ? -13.990 13.741  60.320 1.00 123.84 ?  149 ARG B CA  1 
ATOM   2478 C  C   . ARG B 1 157 ? -13.180 12.458  60.433 1.00 122.20 ?  149 ARG B C   1 
ATOM   2479 O  O   . ARG B 1 157 ? -13.590 11.426  59.890 1.00 119.72 ?  149 ARG B O   1 
ATOM   2480 C  CB  . ARG B 1 157 ? -13.532 14.579  59.129 1.00 122.84 ?  149 ARG B CB  1 
ATOM   2481 C  CG  . ARG B 1 157 ? -14.475 15.733  58.813 1.00 115.02 ?  149 ARG B CG  1 
ATOM   2482 C  CD  . ARG B 1 157 ? -13.723 16.903  58.207 1.00 113.56 ?  149 ARG B CD  1 
ATOM   2483 N  NE  . ARG B 1 157 ? -14.610 17.834  57.524 1.00 108.43 ?  149 ARG B NE  1 
ATOM   2484 C  CZ  . ARG B 1 157 ? -14.272 18.526  56.445 1.00 104.27 ?  149 ARG B CZ  1 
ATOM   2485 N  NH1 . ARG B 1 157 ? -13.080 18.393  55.884 1.00 109.21 ?  149 ARG B NH1 1 
ATOM   2486 N  NH2 . ARG B 1 157 ? -15.153 19.366  55.909 1.00 112.52 ?  149 ARG B NH2 1 
ATOM   2487 N  N   . ALA B 1 158 ? -12.048 12.496  61.135 1.00 134.04 ?  150 ALA B N   1 
ATOM   2488 C  CA  . ALA B 1 158 ? -11.270 11.279  61.335 1.00 139.37 ?  150 ALA B CA  1 
ATOM   2489 C  C   . ALA B 1 158 ? -12.062 10.253  62.135 1.00 105.28 ?  150 ALA B C   1 
ATOM   2490 O  O   . ALA B 1 158 ? -12.013 9.052   61.842 1.00 111.39 ?  150 ALA B O   1 
ATOM   2491 C  CB  . ALA B 1 158 ? -9.953  11.612  62.036 1.00 116.44 ?  150 ALA B CB  1 
ATOM   2492 N  N   . ARG B 1 159 ? -12.794 10.711  63.157 1.00 119.69 ?  151 ARG B N   1 
ATOM   2493 C  CA  . ARG B 1 159 ? -13.640 9.813   63.936 1.00 127.46 ?  151 ARG B CA  1 
ATOM   2494 C  C   . ARG B 1 159 ? -14.727 9.191   63.071 1.00 122.76 ?  151 ARG B C   1 
ATOM   2495 O  O   . ARG B 1 159 ? -15.088 8.022   63.255 1.00 117.76 ?  151 ARG B O   1 
ATOM   2496 C  CB  . ARG B 1 159 ? -14.271 10.575  65.101 1.00 130.05 ?  151 ARG B CB  1 
ATOM   2497 C  CG  . ARG B 1 159 ? -13.293 11.091  66.139 1.00 132.23 ?  151 ARG B CG  1 
ATOM   2498 C  CD  . ARG B 1 159 ? -13.893 12.267  66.898 1.00 131.86 ?  151 ARG B CD  1 
ATOM   2499 N  NE  . ARG B 1 159 ? -13.411 12.333  68.271 1.00 139.58 ?  151 ARG B NE  1 
ATOM   2500 C  CZ  . ARG B 1 159 ? -13.926 11.639  69.277 1.00 132.92 ?  151 ARG B CZ  1 
ATOM   2501 N  NH1 . ARG B 1 159 ? -14.940 10.809  69.095 1.00 122.08 ?  151 ARG B NH1 1 
ATOM   2502 N  NH2 . ARG B 1 159 ? -13.409 11.779  70.494 1.00 128.60 ?  151 ARG B NH2 1 
ATOM   2503 N  N   . ALA B 1 160 ? -15.280 9.964   62.142 1.00 116.26 ?  152 ALA B N   1 
ATOM   2504 C  CA  . ALA B 1 160 ? -16.295 9.468   61.221 1.00 109.94 ?  152 ALA B CA  1 
ATOM   2505 C  C   . ALA B 1 160 ? -15.651 8.634   60.119 1.00 107.56 ?  152 ALA B C   1 
ATOM   2506 O  O   . ALA B 1 160 ? -16.320 7.838   59.459 1.00 102.35 ?  152 ALA B O   1 
ATOM   2507 C  CB  . ALA B 1 160 ? -17.076 10.626  60.619 1.00 99.59  ?  152 ALA B CB  1 
ATOM   2508 N  N   . LEU B 1 172 ? -6.175  19.367  70.218 1.00 140.38 ?  164 LEU B N   1 
ATOM   2509 C  CA  . LEU B 1 172 ? -4.878  18.990  70.770 1.00 143.38 ?  164 LEU B CA  1 
ATOM   2510 C  C   . LEU B 1 172 ? -3.842  20.080  70.486 1.00 161.21 ?  164 LEU B C   1 
ATOM   2511 O  O   . LEU B 1 172 ? -3.900  20.742  69.451 1.00 160.65 ?  164 LEU B O   1 
ATOM   2512 C  CB  . LEU B 1 172 ? -4.417  17.653  70.189 1.00 139.82 ?  164 LEU B CB  1 
ATOM   2513 C  CG  . LEU B 1 172 ? -3.146  17.073  70.806 1.00 176.27 ?  164 LEU B CG  1 
ATOM   2514 C  CD1 . LEU B 1 172 ? -3.460  16.001  71.842 1.00 176.83 ?  164 LEU B CD1 1 
ATOM   2515 C  CD2 . LEU B 1 172 ? -2.241  16.516  69.719 1.00 138.35 ?  164 LEU B CD2 1 
ATOM   2516 N  N   . ASP B 1 173 ? -2.901  20.263  71.419 1.00 137.27 ?  165 ASP B N   1 
ATOM   2517 C  CA  . ASP B 1 173 ? -1.885  21.301  71.260 1.00 134.61 ?  165 ASP B CA  1 
ATOM   2518 C  C   . ASP B 1 173 ? -0.932  20.991  70.109 1.00 139.49 ?  165 ASP B C   1 
ATOM   2519 O  O   . ASP B 1 173 ? -0.558  21.891  69.350 1.00 138.06 ?  165 ASP B O   1 
ATOM   2520 C  CB  . ASP B 1 173 ? -1.097  21.471  72.560 1.00 139.10 ?  165 ASP B CB  1 
ATOM   2521 C  CG  . ASP B 1 173 ? -1.906  22.139  73.654 1.00 139.42 ?  165 ASP B CG  1 
ATOM   2522 O  OD1 . ASP B 1 173 ? -2.745  23.008  73.334 1.00 152.26 ?  165 ASP B OD1 1 
ATOM   2523 O  OD2 . ASP B 1 173 ? -1.699  21.798  74.837 1.00 139.49 ?  165 ASP B OD2 1 
ATOM   2524 N  N   . PHE B 1 174 ? -0.515  19.729  69.972 1.00 153.83 ?  166 PHE B N   1 
ATOM   2525 C  CA  . PHE B 1 174 ? 0.358   19.354  68.862 1.00 143.95 ?  166 PHE B CA  1 
ATOM   2526 C  C   . PHE B 1 174 ? -0.300  19.684  67.528 1.00 143.27 ?  166 PHE B C   1 
ATOM   2527 O  O   . PHE B 1 174 ? 0.366   20.139  66.591 1.00 140.37 ?  166 PHE B O   1 
ATOM   2528 C  CB  . PHE B 1 174 ? 0.695   17.861  68.953 1.00 142.69 ?  166 PHE B CB  1 
ATOM   2529 C  CG  . PHE B 1 174 ? 1.932   17.448  68.186 1.00 143.01 ?  166 PHE B CG  1 
ATOM   2530 C  CD1 . PHE B 1 174 ? 1.862   17.150  66.835 1.00 137.01 ?  166 PHE B CD1 1 
ATOM   2531 C  CD2 . PHE B 1 174 ? 3.155   17.324  68.828 1.00 138.99 ?  166 PHE B CD2 1 
ATOM   2532 C  CE1 . PHE B 1 174 ? 2.991   16.756  66.134 1.00 132.54 ?  166 PHE B CE1 1 
ATOM   2533 C  CE2 . PHE B 1 174 ? 4.287   16.931  68.132 1.00 134.87 ?  166 PHE B CE2 1 
ATOM   2534 C  CZ  . PHE B 1 174 ? 4.203   16.646  66.785 1.00 132.87 ?  166 PHE B CZ  1 
ATOM   2535 N  N   . PHE B 1 175 ? -1.616  19.474  67.431 1.00 160.67 ?  167 PHE B N   1 
ATOM   2536 C  CA  . PHE B 1 175 ? -2.331  19.766  66.193 1.00 163.64 ?  167 PHE B CA  1 
ATOM   2537 C  C   . PHE B 1 175 ? -2.429  21.266  65.943 1.00 153.03 ?  167 PHE B C   1 
ATOM   2538 O  O   . PHE B 1 175 ? -2.294  21.719  64.800 1.00 143.91 ?  167 PHE B O   1 
ATOM   2539 C  CB  . PHE B 1 175 ? -3.726  19.140  66.237 1.00 139.08 ?  167 PHE B CB  1 
ATOM   2540 N  N   . ASN B 1 176 ? -2.675  22.056  66.993 1.00 154.39 ?  168 ASN B N   1 
ATOM   2541 C  CA  . ASN B 1 176 ? -2.779  23.500  66.809 1.00 157.03 ?  168 ASN B CA  1 
ATOM   2542 C  C   . ASN B 1 176 ? -1.446  24.112  66.403 1.00 149.95 ?  168 ASN B C   1 
ATOM   2543 O  O   . ASN B 1 176 ? -1.418  25.082  65.637 1.00 140.03 ?  168 ASN B O   1 
ATOM   2544 C  CB  . ASN B 1 176 ? -3.287  24.174  68.087 1.00 166.30 ?  168 ASN B CB  1 
ATOM   2545 C  CG  . ASN B 1 176 ? -4.752  23.902  68.344 1.00 150.68 ?  168 ASN B CG  1 
ATOM   2546 O  OD1 . ASN B 1 176 ? -5.615  24.295  67.558 1.00 165.64 ?  168 ASN B OD1 1 
ATOM   2547 N  ND2 . ASN B 1 176 ? -5.045  23.240  69.454 1.00 137.91 ?  168 ASN B ND2 1 
ATOM   2548 N  N   . ARG B 1 177 ? -0.337  23.583  66.923 1.00 152.79 ?  169 ARG B N   1 
ATOM   2549 C  CA  . ARG B 1 177 ? 0.970   24.107  66.543 1.00 152.57 ?  169 ARG B CA  1 
ATOM   2550 C  C   . ARG B 1 177 ? 1.308   23.754  65.099 1.00 136.44 ?  169 ARG B C   1 
ATOM   2551 O  O   . ARG B 1 177 ? 1.785   24.607  64.340 1.00 119.83 ?  169 ARG B O   1 
ATOM   2552 C  CB  . ARG B 1 177 ? 2.043   23.578  67.493 1.00 157.29 ?  169 ARG B CB  1 
ATOM   2553 N  N   . THR B 1 178 ? 1.055   22.504  64.701 1.00 135.69 ?  170 THR B N   1 
ATOM   2554 C  CA  . THR B 1 178 ? 1.399   22.075  63.350 1.00 116.60 ?  170 THR B CA  1 
ATOM   2555 C  C   . THR B 1 178 ? 0.565   22.804  62.302 1.00 111.25 ?  170 THR B C   1 
ATOM   2556 O  O   . THR B 1 178 ? 1.058   23.096  61.206 1.00 120.90 ?  170 THR B O   1 
ATOM   2557 C  CB  . THR B 1 178 ? 1.222   20.561  63.216 1.00 154.25 ?  170 THR B CB  1 
ATOM   2558 O  OG1 . THR B 1 178 ? -0.045  20.172  63.763 1.00 138.75 ?  170 THR B OG1 1 
ATOM   2559 C  CG2 . THR B 1 178 ? 2.343   19.824  63.942 1.00 153.33 ?  170 THR B CG2 1 
ATOM   2560 N  N   . ARG B 1 179 ? -0.702  23.101  62.609 1.00 120.23 ?  171 ARG B N   1 
ATOM   2561 C  CA  . ARG B 1 179 ? -1.513  23.867  61.666 1.00 103.93 ?  171 ARG B CA  1 
ATOM   2562 C  C   . ARG B 1 179 ? -0.914  25.248  61.429 1.00 108.72 ?  171 ARG B C   1 
ATOM   2563 O  O   . ARG B 1 179 ? -0.871  25.726  60.290 1.00 109.86 ?  171 ARG B O   1 
ATOM   2564 C  CB  . ARG B 1 179 ? -2.954  23.991  62.165 1.00 98.45  ?  171 ARG B CB  1 
ATOM   2565 C  CG  . ARG B 1 179 ? -3.857  24.762  61.199 1.00 111.29 ?  171 ARG B CG  1 
ATOM   2566 C  CD  . ARG B 1 179 ? -5.343  24.679  61.552 1.00 120.95 ?  171 ARG B CD  1 
ATOM   2567 N  NE  . ARG B 1 179 ? -6.140  25.479  60.628 1.00 116.92 ?  171 ARG B NE  1 
ATOM   2568 C  CZ  . ARG B 1 179 ? -6.915  26.499  60.976 1.00 121.79 ?  171 ARG B CZ  1 
ATOM   2569 N  NH1 . ARG B 1 179 ? -7.135  26.802  62.246 1.00 135.68 ?  171 ARG B NH1 1 
ATOM   2570 N  NH2 . ARG B 1 179 ? -7.484  27.232  60.023 1.00 127.92 ?  171 ARG B NH2 1 
ATOM   2571 N  N   . ALA B 1 180 ? -0.442  25.902  62.494 1.00 125.89 ?  172 ALA B N   1 
ATOM   2572 C  CA  . ALA B 1 180 ? 0.163   27.221  62.340 1.00 139.32 ?  172 ALA B CA  1 
ATOM   2573 C  C   . ALA B 1 180 ? 1.385   27.160  61.434 1.00 130.78 ?  172 ALA B C   1 
ATOM   2574 O  O   . ALA B 1 180 ? 1.593   28.044  60.596 1.00 129.78 ?  172 ALA B O   1 
ATOM   2575 C  CB  . ALA B 1 180 ? 0.545   27.788  63.708 1.00 175.54 ?  172 ALA B CB  1 
ATOM   2576 N  N   . ARG B 1 181 ? 2.207   26.121  61.590 1.00 128.89 ?  173 ARG B N   1 
ATOM   2577 C  CA  . ARG B 1 181 ? 3.392   25.977  60.752 1.00 124.19 ?  173 ARG B CA  1 
ATOM   2578 C  C   . ARG B 1 181 ? 3.015   25.833  59.284 1.00 111.79 ?  173 ARG B C   1 
ATOM   2579 O  O   . ARG B 1 181 ? 3.646   26.442  58.412 1.00 109.34 ?  173 ARG B O   1 
ATOM   2580 C  CB  . ARG B 1 181 ? 4.206   24.773  61.226 1.00 126.83 ?  173 ARG B CB  1 
ATOM   2581 C  CG  . ARG B 1 181 ? 5.545   24.587  60.538 1.00 128.10 ?  173 ARG B CG  1 
ATOM   2582 C  CD  . ARG B 1 181 ? 6.213   23.303  61.020 1.00 129.05 ?  173 ARG B CD  1 
ATOM   2583 N  NE  . ARG B 1 181 ? 5.316   22.160  60.894 1.00 128.91 ?  173 ARG B NE  1 
ATOM   2584 C  CZ  . ARG B 1 181 ? 5.241   21.376  59.827 1.00 136.83 ?  173 ARG B CZ  1 
ATOM   2585 N  NH1 . ARG B 1 181 ? 6.045   21.541  58.790 1.00 139.86 ?  173 ARG B NH1 1 
ATOM   2586 N  NH2 . ARG B 1 181 ? 4.334   20.403  59.798 1.00 134.52 ?  173 ARG B NH2 1 
ATOM   2587 N  N   . TYR B 1 182 ? 1.989   25.030  58.990 1.00 113.65 ?  174 TYR B N   1 
ATOM   2588 C  CA  . TYR B 1 182 ? 1.544   24.881  57.609 1.00 106.38 ?  174 TYR B CA  1 
ATOM   2589 C  C   . TYR B 1 182 ? 1.008   26.197  57.055 1.00 104.35 ?  174 TYR B C   1 
ATOM   2590 O  O   . TYR B 1 182 ? 1.262   26.541  55.895 1.00 103.22 ?  174 TYR B O   1 
ATOM   2591 C  CB  . TYR B 1 182 ? 0.466   23.802  57.508 1.00 106.22 ?  174 TYR B CB  1 
ATOM   2592 C  CG  . TYR B 1 182 ? 0.977   22.380  57.497 1.00 112.48 ?  174 TYR B CG  1 
ATOM   2593 C  CD1 . TYR B 1 182 ? 2.156   22.042  56.844 1.00 129.32 ?  174 TYR B CD1 1 
ATOM   2594 C  CD2 . TYR B 1 182 ? 0.270   21.370  58.133 1.00 112.52 ?  174 TYR B CD2 1 
ATOM   2595 C  CE1 . TYR B 1 182 ? 2.618   20.742  56.834 1.00 134.22 ?  174 TYR B CE1 1 
ATOM   2596 C  CE2 . TYR B 1 182 ? 0.723   20.070  58.128 1.00 111.58 ?  174 TYR B CE2 1 
ATOM   2597 C  CZ  . TYR B 1 182 ? 1.896   19.760  57.477 1.00 131.01 ?  174 TYR B CZ  1 
ATOM   2598 O  OH  . TYR B 1 182 ? 2.346   18.461  57.473 1.00 123.72 ?  174 TYR B OH  1 
ATOM   2599 N  N   . LEU B 1 183 ? 0.239   26.935  57.862 1.00 103.89 ?  175 LEU B N   1 
ATOM   2600 C  CA  . LEU B 1 183 ? -0.376  28.159  57.360 1.00 104.60 ?  175 LEU B CA  1 
ATOM   2601 C  C   . LEU B 1 183 ? 0.658   29.253  57.126 1.00 103.14 ?  175 LEU B C   1 
ATOM   2602 O  O   . LEU B 1 183 ? 0.519   30.040  56.184 1.00 106.32 ?  175 LEU B O   1 
ATOM   2603 C  CB  . LEU B 1 183 ? -1.457  28.643  58.326 1.00 119.28 ?  175 LEU B CB  1 
ATOM   2604 C  CG  . LEU B 1 183 ? -2.780  27.877  58.269 1.00 114.35 ?  175 LEU B CG  1 
ATOM   2605 C  CD1 . LEU B 1 183 ? -3.704  28.309  59.397 1.00 128.86 ?  175 LEU B CD1 1 
ATOM   2606 C  CD2 . LEU B 1 183 ? -3.468  28.070  56.923 1.00 104.82 ?  175 LEU B CD2 1 
ATOM   2607 N  N   . GLU B 1 184 ? 1.691   29.324  57.970 1.00 99.16  ?  176 GLU B N   1 
ATOM   2608 C  CA  . GLU B 1 184 ? 2.749   30.306  57.753 1.00 93.50  ?  176 GLU B CA  1 
ATOM   2609 C  C   . GLU B 1 184 ? 3.509   30.007  56.468 1.00 94.89  ?  176 GLU B C   1 
ATOM   2610 O  O   . GLU B 1 184 ? 3.709   30.893  55.630 1.00 90.49  ?  176 GLU B O   1 
ATOM   2611 C  CB  . GLU B 1 184 ? 3.709   30.326  58.943 1.00 104.38 ?  176 GLU B CB  1 
ATOM   2612 C  CG  . GLU B 1 184 ? 4.835   31.350  58.814 1.00 111.12 ?  176 GLU B CG  1 
ATOM   2613 C  CD  . GLU B 1 184 ? 6.033   31.011  59.684 1.00 113.52 ?  176 GLU B CD  1 
ATOM   2614 O  OE1 . GLU B 1 184 ? 5.893   30.143  60.571 1.00 119.28 ?  176 GLU B OE1 1 
ATOM   2615 O  OE2 . GLU B 1 184 ? 7.114   31.600  59.477 1.00 119.05 ?  176 GLU B OE2 1 
ATOM   2616 N  N   . LEU B 1 185 ? 3.953   28.759  56.305 1.00 98.70  ?  177 LEU B N   1 
ATOM   2617 C  CA  . LEU B 1 185 ? 4.615   28.374  55.065 1.00 89.95  ?  177 LEU B CA  1 
ATOM   2618 C  C   . LEU B 1 185 ? 3.699   28.589  53.871 1.00 87.62  ?  177 LEU B C   1 
ATOM   2619 O  O   . LEU B 1 185 ? 4.168   28.943  52.783 1.00 84.12  ?  177 LEU B O   1 
ATOM   2620 C  CB  . LEU B 1 185 ? 5.061   26.916  55.145 1.00 90.02  ?  177 LEU B CB  1 
ATOM   2621 C  CG  . LEU B 1 185 ? 6.126   26.603  56.199 1.00 108.39 ?  177 LEU B CG  1 
ATOM   2622 C  CD1 . LEU B 1 185 ? 6.276   25.103  56.383 1.00 120.93 ?  177 LEU B CD1 1 
ATOM   2623 C  CD2 . LEU B 1 185 ? 7.455   27.234  55.809 1.00 103.50 ?  177 LEU B CD2 1 
ATOM   2624 N  N   . ALA B 1 186 ? 2.393   28.389  54.055 1.00 89.95  ?  178 ALA B N   1 
ATOM   2625 C  CA  . ALA B 1 186 ? 1.452   28.624  52.965 1.00 87.63  ?  178 ALA B CA  1 
ATOM   2626 C  C   . ALA B 1 186 ? 1.465   30.086  52.540 1.00 86.25  ?  178 ALA B C   1 
ATOM   2627 O  O   . ALA B 1 186 ? 1.500   30.400  51.345 1.00 86.04  ?  178 ALA B O   1 
ATOM   2628 C  CB  . ALA B 1 186 ? 0.048   28.198  53.395 1.00 95.66  ?  178 ALA B CB  1 
ATOM   2629 N  N   . ALA B 1 187 ? 1.448   30.998  53.513 1.00 89.86  ?  179 ALA B N   1 
ATOM   2630 C  CA  . ALA B 1 187 ? 1.476   32.418  53.192 1.00 92.35  ?  179 ALA B CA  1 
ATOM   2631 C  C   . ALA B 1 187 ? 2.814   32.839  52.604 1.00 87.16  ?  179 ALA B C   1 
ATOM   2632 O  O   . ALA B 1 187 ? 2.852   33.720  51.736 1.00 85.05  ?  179 ALA B O   1 
ATOM   2633 C  CB  . ALA B 1 187 ? 1.170   33.238  54.448 1.00 98.72  ?  179 ALA B CB  1 
ATOM   2634 N  N   . GLN B 1 188 ? 3.908   32.223  53.049 1.00 87.48  ?  180 GLN B N   1 
ATOM   2635 C  CA  . GLN B 1 188 ? 5.242   32.646  52.656 1.00 82.26  ?  180 GLN B CA  1 
ATOM   2636 C  C   . GLN B 1 188 ? 5.794   31.923  51.433 1.00 72.22  ?  180 GLN B C   1 
ATOM   2637 O  O   . GLN B 1 188 ? 6.796   32.380  50.875 1.00 75.75  ?  180 GLN B O   1 
ATOM   2638 C  CB  . GLN B 1 188 ? 6.223   32.438  53.820 1.00 81.31  ?  180 GLN B CB  1 
ATOM   2639 C  CG  . GLN B 1 188 ? 6.113   33.460  54.928 1.00 85.55  ?  180 GLN B CG  1 
ATOM   2640 C  CD  . GLN B 1 188 ? 6.935   33.083  56.143 1.00 94.29  ?  180 GLN B CD  1 
ATOM   2641 O  OE1 . GLN B 1 188 ? 7.540   32.011  56.189 1.00 89.64  ?  180 GLN B OE1 1 
ATOM   2642 N  NE2 . GLN B 1 188 ? 6.958   33.960  57.139 1.00 108.13 ?  180 GLN B NE2 1 
ATOM   2643 N  N   . ASP B 1 189 ? 5.183   30.823  51.002 1.00 74.51  ?  181 ASP B N   1 
ATOM   2644 C  CA  . ASP B 1 189 ? 5.772   29.984  49.959 1.00 71.71  ?  181 ASP B CA  1 
ATOM   2645 C  C   . ASP B 1 189 ? 4.961   30.060  48.675 1.00 71.07  ?  181 ASP B C   1 
ATOM   2646 O  O   . ASP B 1 189 ? 3.816   29.583  48.646 1.00 66.05  ?  181 ASP B O   1 
ATOM   2647 C  CB  . ASP B 1 189 ? 5.864   28.533  50.448 1.00 70.94  ?  181 ASP B CB  1 
ATOM   2648 C  CG  . ASP B 1 189 ? 6.778   27.674  49.591 1.00 68.15  ?  181 ASP B CG  1 
ATOM   2649 O  OD1 . ASP B 1 189 ? 7.063   28.066  48.443 1.00 67.94  ?  181 ASP B OD1 1 
ATOM   2650 O  OD2 . ASP B 1 189 ? 7.204   26.598  50.069 1.00 63.34  ?  181 ASP B OD2 1 
ATOM   2651 N  N   . PRO B 1 190 ? 5.494   30.638  47.593 1.00 67.84  ?  182 PRO B N   1 
ATOM   2652 C  CA  . PRO B 1 190 ? 4.695   30.758  46.361 1.00 65.08  ?  182 PRO B CA  1 
ATOM   2653 C  C   . PRO B 1 190 ? 4.334   29.426  45.740 1.00 64.41  ?  182 PRO B C   1 
ATOM   2654 O  O   . PRO B 1 190 ? 3.346   29.354  44.997 1.00 65.54  ?  182 PRO B O   1 
ATOM   2655 C  CB  . PRO B 1 190 ? 5.597   31.582  45.429 1.00 71.77  ?  182 PRO B CB  1 
ATOM   2656 C  CG  . PRO B 1 190 ? 6.982   31.298  45.901 1.00 69.52  ?  182 PRO B CG  1 
ATOM   2657 C  CD  . PRO B 1 190 ? 6.885   31.100  47.398 1.00 70.57  ?  182 PRO B CD  1 
ATOM   2658 N  N   . THR B 1 191 ? 5.108   28.375  46.002 1.00 66.81  ?  183 THR B N   1 
ATOM   2659 C  CA  . THR B 1 191 ? 4.811   27.052  45.480 1.00 61.72  ?  183 THR B CA  1 
ATOM   2660 C  C   . THR B 1 191 ? 3.816   26.302  46.348 1.00 57.42  ?  183 THR B C   1 
ATOM   2661 O  O   . THR B 1 191 ? 3.590   25.113  46.114 1.00 53.77  ?  183 THR B O   1 
ATOM   2662 C  CB  . THR B 1 191 ? 6.087   26.216  45.340 1.00 57.64  ?  183 THR B CB  1 
ATOM   2663 O  OG1 . THR B 1 191 ? 6.664   25.977  46.629 1.00 64.95  ?  183 THR B OG1 1 
ATOM   2664 C  CG2 . THR B 1 191 ? 7.098   26.930  44.464 1.00 57.67  ?  183 THR B CG2 1 
ATOM   2665 N  N   . ILE B 1 192 ? 3.244   26.956  47.356 1.00 59.12  ?  184 ILE B N   1 
ATOM   2666 C  CA  . ILE B 1 192 ? 2.199   26.371  48.180 1.00 61.05  ?  184 ILE B CA  1 
ATOM   2667 C  C   . ILE B 1 192 ? 0.913   27.146  47.938 1.00 59.59  ?  184 ILE B C   1 
ATOM   2668 O  O   . ILE B 1 192 ? 0.893   28.380  48.032 1.00 63.14  ?  184 ILE B O   1 
ATOM   2669 C  CB  . ILE B 1 192 ? 2.556   26.384  49.675 1.00 68.35  ?  184 ILE B CB  1 
ATOM   2670 C  CG1 . ILE B 1 192 ? 3.833   25.598  49.946 1.00 72.57  ?  184 ILE B CG1 1 
ATOM   2671 C  CG2 . ILE B 1 192 ? 1.389   25.804  50.468 1.00 65.50  ?  184 ILE B CG2 1 
ATOM   2672 C  CD1 . ILE B 1 192 ? 4.292   25.641  51.405 1.00 70.97  ?  184 ILE B CD1 1 
ATOM   2673 N  N   . ARG B 1 193 ? -0.156  26.420  47.640 1.00 57.51  ?  185 ARG B N   1 
ATOM   2674 C  CA  . ARG B 1 193 ? -1.491  26.980  47.522 1.00 58.36  ?  185 ARG B CA  1 
ATOM   2675 C  C   . ARG B 1 193 ? -2.392  26.257  48.506 1.00 58.58  ?  185 ARG B C   1 
ATOM   2676 O  O   . ARG B 1 193 ? -2.260  25.046  48.705 1.00 55.63  ?  185 ARG B O   1 
ATOM   2677 C  CB  . ARG B 1 193 ? -2.038  26.832  46.113 1.00 64.12  ?  185 ARG B CB  1 
ATOM   2678 C  CG  . ARG B 1 193 ? -1.171  27.480  45.066 1.00 68.24  ?  185 ARG B CG  1 
ATOM   2679 C  CD  . ARG B 1 193 ? -1.151  28.984  45.232 1.00 78.17  ?  185 ARG B CD  1 
ATOM   2680 N  NE  . ARG B 1 193 ? -0.120  29.587  44.394 1.00 77.42  ?  185 ARG B NE  1 
ATOM   2681 C  CZ  . ARG B 1 193 ? -0.223  29.747  43.082 1.00 80.40  ?  185 ARG B CZ  1 
ATOM   2682 N  NH1 . ARG B 1 193 ? -1.303  29.359  42.422 1.00 83.05  ?  185 ARG B NH1 1 
ATOM   2683 N  NH2 . ARG B 1 193 ? 0.784   30.307  42.413 1.00 74.68  ?  185 ARG B NH2 1 
ATOM   2684 N  N   . THR B 1 194 ? -3.307  27.001  49.108 1.00 63.43  ?  186 THR B N   1 
ATOM   2685 C  CA  . THR B 1 194 ? -4.154  26.488  50.167 1.00 69.93  ?  186 THR B CA  1 
ATOM   2686 C  C   . THR B 1 194 ? -5.595  26.393  49.692 1.00 72.42  ?  186 THR B C   1 
ATOM   2687 O  O   . THR B 1 194 ? -6.093  27.280  48.993 1.00 72.32  ?  186 THR B O   1 
ATOM   2688 C  CB  . THR B 1 194 ? -4.089  27.382  51.407 1.00 65.41  ?  186 THR B CB  1 
ATOM   2689 O  OG1 . THR B 1 194 ? -2.729  27.530  51.825 1.00 73.99  ?  186 THR B OG1 1 
ATOM   2690 C  CG2 . THR B 1 194 ? -4.901  26.772  52.533 1.00 73.74  ?  186 THR B CG2 1 
ATOM   2691 N  N   . VAL B 1 195 ? -6.249  25.304  50.078 1.00 75.55  ?  187 VAL B N   1 
ATOM   2692 C  CA  . VAL B 1 195 ? -7.677  25.110  49.883 1.00 83.44  ?  187 VAL B CA  1 
ATOM   2693 C  C   . VAL B 1 195 ? -8.284  24.890  51.256 1.00 91.74  ?  187 VAL B C   1 
ATOM   2694 O  O   . VAL B 1 195 ? -7.869  23.977  51.980 1.00 90.16  ?  187 VAL B O   1 
ATOM   2695 C  CB  . VAL B 1 195 ? -7.969  23.918  48.959 1.00 88.64  ?  187 VAL B CB  1 
ATOM   2696 C  CG1 . VAL B 1 195 ? -9.406  23.457  49.133 1.00 96.86  ?  187 VAL B CG1 1 
ATOM   2697 C  CG2 . VAL B 1 195 ? -7.689  24.291  47.516 1.00 96.96  ?  187 VAL B CG2 1 
ATOM   2698 N  N   . ASP B 1 196 ? -9.254  25.719  51.622 1.00 93.88  ?  188 ASP B N   1 
ATOM   2699 C  CA  . ASP B 1 196 ? -9.969  25.487  52.868 1.00 99.51  ?  188 ASP B CA  1 
ATOM   2700 C  C   . ASP B 1 196 ? -10.793 24.213  52.724 1.00 97.41  ?  188 ASP B C   1 
ATOM   2701 O  O   . ASP B 1 196 ? -11.677 24.129  51.864 1.00 92.37  ?  188 ASP B O   1 
ATOM   2702 C  CB  . ASP B 1 196 ? -10.863 26.666  53.222 1.00 107.29 ?  188 ASP B CB  1 
ATOM   2703 C  CG  . ASP B 1 196 ? -11.599 26.455  54.531 1.00 113.46 ?  188 ASP B CG  1 
ATOM   2704 O  OD1 . ASP B 1 196 ? -10.937 26.434  55.592 1.00 108.28 ?  188 ASP B OD1 1 
ATOM   2705 O  OD2 . ASP B 1 196 ? -12.837 26.298  54.496 1.00 112.23 ?  188 ASP B OD2 1 
ATOM   2706 N  N   . ALA B 1 197 ? -10.487 23.214  53.548 1.00 99.67  ?  189 ALA B N   1 
ATOM   2707 C  CA  . ALA B 1 197 ? -11.189 21.942  53.512 1.00 108.46 ?  189 ALA B CA  1 
ATOM   2708 C  C   . ALA B 1 197 ? -12.321 21.849  54.527 1.00 114.08 ?  189 ALA B C   1 
ATOM   2709 O  O   . ALA B 1 197 ? -13.072 20.868  54.494 1.00 110.65 ?  189 ALA B O   1 
ATOM   2710 C  CB  . ALA B 1 197 ? -10.190 20.794  53.740 1.00 110.33 ?  189 ALA B CB  1 
ATOM   2711 N  N   . THR B 1 198 ? -12.479 22.842  55.409 1.00 112.79 ?  190 THR B N   1 
ATOM   2712 C  CA  . THR B 1 198 ? -13.537 22.778  56.410 1.00 113.86 ?  190 THR B CA  1 
ATOM   2713 C  C   . THR B 1 198 ? -14.929 22.915  55.805 1.00 108.51 ?  190 THR B C   1 
ATOM   2714 O  O   . THR B 1 198 ? -15.919 22.658  56.499 1.00 117.29 ?  190 THR B O   1 
ATOM   2715 C  CB  . THR B 1 198 ? -13.372 23.872  57.472 1.00 120.85 ?  190 THR B CB  1 
ATOM   2716 O  OG1 . THR B 1 198 ? -13.703 25.148  56.906 1.00 115.68 ?  190 THR B OG1 1 
ATOM   2717 C  CG2 . THR B 1 198 ? -11.953 23.903  58.011 1.00 115.79 ?  190 THR B CG2 1 
ATOM   2718 N  N   . GLN B 1 199 ? -15.025 23.337  54.549 1.00 110.08 ?  191 GLN B N   1 
ATOM   2719 C  CA  . GLN B 1 199 ? -16.297 23.537  53.883 1.00 112.92 ?  191 GLN B CA  1 
ATOM   2720 C  C   . GLN B 1 199 ? -16.807 22.218  53.318 1.00 113.95 ?  191 GLN B C   1 
ATOM   2721 O  O   . GLN B 1 199 ? -16.131 21.192  53.402 1.00 108.72 ?  191 GLN B O   1 
ATOM   2722 C  CB  . GLN B 1 199 ? -16.126 24.593  52.792 1.00 108.43 ?  191 GLN B CB  1 
ATOM   2723 C  CG  . GLN B 1 199 ? -15.136 24.209  51.711 1.00 104.90 ?  191 GLN B CG  1 
ATOM   2724 C  CD  . GLN B 1 199 ? -14.727 25.383  50.845 1.00 101.13 ?  191 GLN B CD  1 
ATOM   2725 O  OE1 . GLN B 1 199 ? -15.327 26.455  50.907 1.00 88.93  ?  191 GLN B OE1 1 
ATOM   2726 N  NE2 . GLN B 1 199 ? -13.693 25.186  50.035 1.00 102.15 ?  191 GLN B NE2 1 
ATOM   2727 N  N   . PRO B 1 200 ? -18.018 22.204  52.763 1.00 116.49 ?  192 PRO B N   1 
ATOM   2728 C  CA  . PRO B 1 200 ? -18.565 20.945  52.240 1.00 118.37 ?  192 PRO B CA  1 
ATOM   2729 C  C   . PRO B 1 200 ? -17.734 20.394  51.090 1.00 112.92 ?  192 PRO B C   1 
ATOM   2730 O  O   . PRO B 1 200 ? -17.025 21.117  50.389 1.00 108.84 ?  192 PRO B O   1 
ATOM   2731 C  CB  . PRO B 1 200 ? -19.976 21.329  51.773 1.00 128.27 ?  192 PRO B CB  1 
ATOM   2732 C  CG  . PRO B 1 200 ? -20.316 22.548  52.562 1.00 114.51 ?  192 PRO B CG  1 
ATOM   2733 C  CD  . PRO B 1 200 ? -19.016 23.289  52.739 1.00 111.01 ?  192 PRO B CD  1 
ATOM   2734 N  N   . LEU B 1 201 ? -17.858 19.080  50.893 1.00 109.49 ?  193 LEU B N   1 
ATOM   2735 C  CA  . LEU B 1 201 ? -17.019 18.381  49.924 1.00 104.21 ?  193 LEU B CA  1 
ATOM   2736 C  C   . LEU B 1 201 ? -17.192 18.944  48.519 1.00 106.43 ?  193 LEU B C   1 
ATOM   2737 O  O   . LEU B 1 201 ? -16.208 19.117  47.792 1.00 108.53 ?  193 LEU B O   1 
ATOM   2738 C  CB  . LEU B 1 201 ? -17.346 16.888  49.955 1.00 110.00 ?  193 LEU B CB  1 
ATOM   2739 C  CG  . LEU B 1 201 ? -16.428 15.915  49.219 1.00 99.30  ?  193 LEU B CG  1 
ATOM   2740 C  CD1 . LEU B 1 201 ? -14.989 16.056  49.673 1.00 110.59 ?  193 LEU B CD1 1 
ATOM   2741 C  CD2 . LEU B 1 201 ? -16.932 14.487  49.437 1.00 91.32  ?  193 LEU B CD2 1 
ATOM   2742 N  N   . GLU B 1 202 ? -18.433 19.231  48.111 1.00 108.96 ?  194 GLU B N   1 
ATOM   2743 C  CA  . GLU B 1 202 ? -18.651 19.772  46.771 1.00 111.46 ?  194 GLU B CA  1 
ATOM   2744 C  C   . GLU B 1 202 ? -17.917 21.094  46.586 1.00 110.29 ?  194 GLU B C   1 
ATOM   2745 O  O   . GLU B 1 202 ? -17.444 21.397  45.484 1.00 108.68 ?  194 GLU B O   1 
ATOM   2746 C  CB  . GLU B 1 202 ? -20.146 19.959  46.504 1.00 122.72 ?  194 GLU B CB  1 
ATOM   2747 C  CG  . GLU B 1 202 ? -20.487 20.364  45.068 1.00 129.95 ?  194 GLU B CG  1 
ATOM   2748 C  CD  . GLU B 1 202 ? -20.567 19.177  44.120 1.00 132.87 ?  194 GLU B CD  1 
ATOM   2749 O  OE1 . GLU B 1 202 ? -21.103 18.125  44.526 1.00 137.65 ?  194 GLU B OE1 1 
ATOM   2750 O  OE2 . GLU B 1 202 ? -20.093 19.296  42.969 1.00 131.62 ?  194 GLU B OE2 1 
ATOM   2751 N  N   . ALA B 1 203 ? -17.828 21.900  47.646 1.00 107.65 ?  195 ALA B N   1 
ATOM   2752 C  CA  . ALA B 1 203 ? -17.074 23.145  47.569 1.00 98.84  ?  195 ALA B CA  1 
ATOM   2753 C  C   . ALA B 1 203 ? -15.579 22.876  47.465 1.00 98.07  ?  195 ALA B C   1 
ATOM   2754 O  O   . ALA B 1 203 ? -14.877 23.536  46.689 1.00 99.42  ?  195 ALA B O   1 
ATOM   2755 C  CB  . ALA B 1 203 ? -17.382 24.012  48.788 1.00 91.31  ?  195 ALA B CB  1 
ATOM   2756 N  N   . VAL B 1 204 ? -15.075 21.908  48.236 1.00 98.05  ?  196 VAL B N   1 
ATOM   2757 C  CA  . VAL B 1 204 ? -13.658 21.570  48.159 1.00 96.77  ?  196 VAL B CA  1 
ATOM   2758 C  C   . VAL B 1 204 ? -13.308 21.111  46.750 1.00 96.71  ?  196 VAL B C   1 
ATOM   2759 O  O   . VAL B 1 204 ? -12.232 21.418  46.226 1.00 86.68  ?  196 VAL B O   1 
ATOM   2760 C  CB  . VAL B 1 204 ? -13.303 20.495  49.201 1.00 94.87  ?  196 VAL B CB  1 
ATOM   2761 C  CG1 . VAL B 1 204 ? -11.806 20.202  49.173 1.00 88.02  ?  196 VAL B CG1 1 
ATOM   2762 C  CG2 . VAL B 1 204 ? -13.732 20.929  50.591 1.00 96.49  ?  196 VAL B CG2 1 
ATOM   2763 N  N   . GLU B 1 205 ? -14.210 20.360  46.118 1.00 99.35  ?  197 GLU B N   1 
ATOM   2764 C  CA  . GLU B 1 205 ? -13.966 19.907  44.753 1.00 96.81  ?  197 GLU B CA  1 
ATOM   2765 C  C   . GLU B 1 205 ? -13.849 21.083  43.793 1.00 87.63  ?  197 GLU B C   1 
ATOM   2766 O  O   . GLU B 1 205 ? -12.978 21.090  42.914 1.00 89.72  ?  197 GLU B O   1 
ATOM   2767 C  CB  . GLU B 1 205 ? -15.086 18.962  44.324 1.00 113.71 ?  197 GLU B CB  1 
ATOM   2768 C  CG  . GLU B 1 205 ? -15.060 18.542  42.870 1.00 98.80  ?  197 GLU B CG  1 
ATOM   2769 C  CD  . GLU B 1 205 ? -16.329 17.810  42.479 1.00 96.36  ?  197 GLU B CD  1 
ATOM   2770 O  OE1 . GLU B 1 205 ? -17.229 17.690  43.339 1.00 112.95 ?  197 GLU B OE1 1 
ATOM   2771 O  OE2 . GLU B 1 205 ? -16.432 17.357  41.322 1.00 87.01  ?  197 GLU B OE2 1 
ATOM   2772 N  N   . ARG B 1 206 ? -14.718 22.086  43.936 1.00 87.56  ?  198 ARG B N   1 
ATOM   2773 C  CA  . ARG B 1 206 ? -14.639 23.236  43.042 1.00 83.85  ?  198 ARG B CA  1 
ATOM   2774 C  C   . ARG B 1 206 ? -13.299 23.943  43.186 1.00 84.49  ?  198 ARG B C   1 
ATOM   2775 O  O   . ARG B 1 206 ? -12.704 24.377  42.192 1.00 76.31  ?  198 ARG B O   1 
ATOM   2776 C  CB  . ARG B 1 206 ? -15.777 24.221  43.316 1.00 86.19  ?  198 ARG B CB  1 
ATOM   2777 C  CG  . ARG B 1 206 ? -15.555 25.613  42.702 1.00 87.93  ?  198 ARG B CG  1 
ATOM   2778 C  CD  . ARG B 1 206 ? -15.413 25.574  41.175 1.00 93.70  ?  198 ARG B CD  1 
ATOM   2779 N  NE  . ARG B 1 206 ? -16.688 25.330  40.508 1.00 104.59 ?  198 ARG B NE  1 
ATOM   2780 C  CZ  . ARG B 1 206 ? -16.875 25.358  39.195 1.00 88.87  ?  198 ARG B CZ  1 
ATOM   2781 N  NH1 . ARG B 1 206 ? -15.881 25.617  38.358 1.00 88.21  ?  198 ARG B NH1 1 
ATOM   2782 N  NH2 . ARG B 1 206 ? -18.090 25.125  38.708 1.00 83.31  ?  198 ARG B NH2 1 
ATOM   2783 N  N   . ASP B 1 207 ? -12.823 24.088  44.424 1.00 90.87  ?  199 ASP B N   1 
ATOM   2784 C  CA  . ASP B 1 207 ? -11.643 24.903  44.682 1.00 91.69  ?  199 ASP B CA  1 
ATOM   2785 C  C   . ASP B 1 207 ? -10.363 24.166  44.322 1.00 83.85  ?  199 ASP B C   1 
ATOM   2786 O  O   . ASP B 1 207 ? -9.489  24.729  43.661 1.00 76.88  ?  199 ASP B O   1 
ATOM   2787 C  CB  . ASP B 1 207 ? -11.611 25.336  46.147 1.00 94.75  ?  199 ASP B CB  1 
ATOM   2788 C  CG  . ASP B 1 207 ? -12.562 26.479  46.433 1.00 98.55  ?  199 ASP B CG  1 
ATOM   2789 O  OD1 . ASP B 1 207 ? -12.818 27.292  45.518 1.00 96.03  ?  199 ASP B OD1 1 
ATOM   2790 O  OD2 . ASP B 1 207 ? -13.053 26.572  47.575 1.00 107.72 ?  199 ASP B OD2 1 
ATOM   2791 N  N   . ILE B 1 208 ? -10.222 22.915  44.767 1.00 84.43  ?  200 ILE B N   1 
ATOM   2792 C  CA  . ILE B 1 208 ? -9.094  22.102  44.318 1.00 85.38  ?  200 ILE B CA  1 
ATOM   2793 C  C   . ILE B 1 208 ? -8.976  22.182  42.805 1.00 83.00  ?  200 ILE B C   1 
ATOM   2794 O  O   . ILE B 1 208 ? -7.921  22.511  42.254 1.00 82.35  ?  200 ILE B O   1 
ATOM   2795 C  CB  . ILE B 1 208 ? -9.258  20.642  44.777 1.00 86.58  ?  200 ILE B CB  1 
ATOM   2796 C  CG1 . ILE B 1 208 ? -9.030  20.537  46.282 1.00 88.16  ?  200 ILE B CG1 1 
ATOM   2797 C  CG2 . ILE B 1 208 ? -8.303  19.734  44.005 1.00 84.68  ?  200 ILE B CG2 1 
ATOM   2798 C  CD1 . ILE B 1 208 ? -9.254  19.153  46.829 1.00 87.34  ?  200 ILE B CD1 1 
ATOM   2799 N  N   . ARG B 1 209 ? -10.077 21.892  42.113 1.00 85.94  ?  201 ARG B N   1 
ATOM   2800 C  CA  . ARG B 1 209 ? -10.071 21.910  40.654 1.00 78.37  ?  201 ARG B CA  1 
ATOM   2801 C  C   . ARG B 1 209 ? -9.636  23.269  40.128 1.00 75.93  ?  201 ARG B C   1 
ATOM   2802 O  O   . ARG B 1 209 ? -8.887  23.351  39.148 1.00 79.00  ?  201 ARG B O   1 
ATOM   2803 C  CB  . ARG B 1 209 ? -11.466 21.537  40.148 1.00 79.09  ?  201 ARG B CB  1 
ATOM   2804 C  CG  . ARG B 1 209 ? -11.633 21.528  38.642 1.00 83.55  ?  201 ARG B CG  1 
ATOM   2805 C  CD  . ARG B 1 209 ? -12.480 20.334  38.227 1.00 78.23  ?  201 ARG B CD  1 
ATOM   2806 N  NE  . ARG B 1 209 ? -12.431 20.065  36.796 1.00 89.93  ?  201 ARG B NE  1 
ATOM   2807 C  CZ  . ARG B 1 209 ? -13.022 19.029  36.216 1.00 86.58  ?  201 ARG B CZ  1 
ATOM   2808 N  NH1 . ARG B 1 209 ? -13.714 18.146  36.918 1.00 93.48  ?  201 ARG B NH1 1 
ATOM   2809 N  NH2 . ARG B 1 209 ? -12.916 18.874  34.900 1.00 94.86  ?  201 ARG B NH2 1 
ATOM   2810 N  N   . ALA B 1 210 ? -10.081 24.348  40.775 1.00 79.64  ?  202 ALA B N   1 
ATOM   2811 C  CA  . ALA B 1 210 ? -9.701  25.681  40.323 1.00 77.17  ?  202 ALA B CA  1 
ATOM   2812 C  C   . ALA B 1 210 ? -8.235  25.968  40.609 1.00 78.55  ?  202 ALA B C   1 
ATOM   2813 O  O   . ALA B 1 210 ? -7.556  26.610  39.800 1.00 81.40  ?  202 ALA B O   1 
ATOM   2814 C  CB  . ALA B 1 210 ? -10.586 26.732  40.992 1.00 77.31  ?  202 ALA B CB  1 
ATOM   2815 N  N   . VAL B 1 211 ? -7.743  25.536  41.772 1.00 77.18  ?  203 VAL B N   1 
ATOM   2816 C  CA  . VAL B 1 211 ? -6.381  25.873  42.171 1.00 74.20  ?  203 VAL B CA  1 
ATOM   2817 C  C   . VAL B 1 211 ? -5.374  25.245  41.221 1.00 78.85  ?  203 VAL B C   1 
ATOM   2818 O  O   . VAL B 1 211 ? -4.480  25.920  40.698 1.00 81.87  ?  203 VAL B O   1 
ATOM   2819 C  CB  . VAL B 1 211 ? -6.118  25.427  43.620 1.00 79.71  ?  203 VAL B CB  1 
ATOM   2820 C  CG1 . VAL B 1 211 ? -4.619  25.445  43.908 1.00 77.14  ?  203 VAL B CG1 1 
ATOM   2821 C  CG2 . VAL B 1 211 ? -6.879  26.301  44.599 1.00 77.27  ?  203 VAL B CG2 1 
ATOM   2822 N  N   . VAL B 1 212 ? -5.504  23.941  40.989 1.00 80.86  ?  204 VAL B N   1 
ATOM   2823 C  CA  . VAL B 1 212 ? -4.587  23.262  40.084 1.00 76.87  ?  204 VAL B CA  1 
ATOM   2824 C  C   . VAL B 1 212 ? -4.686  23.874  38.699 1.00 73.61  ?  204 VAL B C   1 
ATOM   2825 O  O   . VAL B 1 212 ? -3.671  24.123  38.040 1.00 77.93  ?  204 VAL B O   1 
ATOM   2826 C  CB  . VAL B 1 212 ? -4.881  21.752  40.061 1.00 82.10  ?  204 VAL B CB  1 
ATOM   2827 C  CG1 . VAL B 1 212 ? -4.113  21.079  38.937 1.00 89.96  ?  204 VAL B CG1 1 
ATOM   2828 C  CG2 . VAL B 1 212 ? -4.516  21.138  41.400 1.00 83.01  ?  204 VAL B CG2 1 
ATOM   2829 N  N   . ASN B 1 213 ? -5.910  24.143  38.241 1.00 79.40  ?  205 ASN B N   1 
ATOM   2830 C  CA  . ASN B 1 213 ? -6.075  24.762  36.934 1.00 81.64  ?  205 ASN B CA  1 
ATOM   2831 C  C   . ASN B 1 213 ? -5.362  26.105  36.872 1.00 78.88  ?  205 ASN B C   1 
ATOM   2832 O  O   . ASN B 1 213 ? -4.677  26.405  35.885 1.00 75.16  ?  205 ASN B O   1 
ATOM   2833 C  CB  . ASN B 1 213 ? -7.563  24.932  36.629 1.00 79.04  ?  205 ASN B CB  1 
ATOM   2834 C  CG  . ASN B 1 213 ? -7.809  25.527  35.264 1.00 88.41  ?  205 ASN B CG  1 
ATOM   2835 O  OD1 . ASN B 1 213 ? -6.932  25.498  34.398 1.00 93.18  ?  205 ASN B OD1 1 
ATOM   2836 N  ND2 . ASN B 1 213 ? -9.000  26.073  35.059 1.00 89.86  ?  205 ASN B ND2 1 
ATOM   2837 N  N   . ARG B 1 214 ? -5.510  26.925  37.915 1.00 78.25  ?  206 ARG B N   1 
ATOM   2838 C  CA  . ARG B 1 214 ? -4.863  28.232  37.918 1.00 80.93  ?  206 ARG B CA  1 
ATOM   2839 C  C   . ARG B 1 214 ? -3.347  28.094  37.914 1.00 80.71  ?  206 ARG B C   1 
ATOM   2840 O  O   . ARG B 1 214 ? -2.654  28.813  37.184 1.00 78.81  ?  206 ARG B O   1 
ATOM   2841 C  CB  . ARG B 1 214 ? -5.321  29.043  39.131 1.00 77.82  ?  206 ARG B CB  1 
ATOM   2842 C  CG  . ARG B 1 214 ? -4.628  30.397  39.279 1.00 83.55  ?  206 ARG B CG  1 
ATOM   2843 C  CD  . ARG B 1 214 ? -4.961  31.335  38.122 1.00 87.38  ?  206 ARG B CD  1 
ATOM   2844 N  NE  . ARG B 1 214 ? -3.812  32.134  37.710 1.00 89.39  ?  206 ARG B NE  1 
ATOM   2845 C  CZ  . ARG B 1 214 ? -3.701  32.738  36.534 1.00 105.46 ?  206 ARG B CZ  1 
ATOM   2846 N  NH1 . ARG B 1 214 ? -4.651  32.648  35.620 1.00 107.27 ?  206 ARG B NH1 1 
ATOM   2847 N  NH2 . ARG B 1 214 ? -2.605  33.443  36.268 1.00 102.18 ?  206 ARG B NH2 1 
ATOM   2848 N  N   . TRP B 1 215 ? -2.817  27.182  38.726 1.00 76.29  ?  207 TRP B N   1 
ATOM   2849 C  CA  . TRP B 1 215 ? -1.371  27.016  38.801 1.00 74.68  ?  207 TRP B CA  1 
ATOM   2850 C  C   . TRP B 1 215 ? -0.806  26.560  37.465 1.00 72.94  ?  207 TRP B C   1 
ATOM   2851 O  O   . TRP B 1 215 ? 0.204   27.094  36.988 1.00 73.42  ?  207 TRP B O   1 
ATOM   2852 C  CB  . TRP B 1 215 ? -1.020  26.017  39.900 1.00 74.16  ?  207 TRP B CB  1 
ATOM   2853 C  CG  . TRP B 1 215 ? 0.445   25.804  40.038 1.00 72.63  ?  207 TRP B CG  1 
ATOM   2854 C  CD1 . TRP B 1 215 ? 1.342   26.650  40.618 1.00 67.07  ?  207 TRP B CD1 1 
ATOM   2855 C  CD2 . TRP B 1 215 ? 1.193   24.669  39.591 1.00 66.11  ?  207 TRP B CD2 1 
ATOM   2856 N  NE1 . TRP B 1 215 ? 2.605   26.114  40.560 1.00 60.93  ?  207 TRP B NE1 1 
ATOM   2857 C  CE2 . TRP B 1 215 ? 2.541   24.897  39.934 1.00 62.38  ?  207 TRP B CE2 1 
ATOM   2858 C  CE3 . TRP B 1 215 ? 0.855   23.482  38.933 1.00 65.68  ?  207 TRP B CE3 1 
ATOM   2859 C  CZ2 . TRP B 1 215 ? 3.550   23.982  39.644 1.00 65.68  ?  207 TRP B CZ2 1 
ATOM   2860 C  CZ3 . TRP B 1 215 ? 1.858   22.576  38.647 1.00 65.09  ?  207 TRP B CZ3 1 
ATOM   2861 C  CH2 . TRP B 1 215 ? 3.188   22.831  39.001 1.00 64.59  ?  207 TRP B CH2 1 
ATOM   2862 N  N   . VAL B 1 216 ? -1.457  25.578  36.838 1.00 74.52  ?  208 VAL B N   1 
ATOM   2863 C  CA  . VAL B 1 216 ? -0.955  25.037  35.579 1.00 76.05  ?  208 VAL B CA  1 
ATOM   2864 C  C   . VAL B 1 216 ? -0.858  26.137  34.531 1.00 72.77  ?  208 VAL B C   1 
ATOM   2865 O  O   . VAL B 1 216 ? 0.073   26.163  33.718 1.00 70.93  ?  208 VAL B O   1 
ATOM   2866 C  CB  . VAL B 1 216 ? -1.857  23.884  35.101 1.00 75.09  ?  208 VAL B CB  1 
ATOM   2867 C  CG1 . VAL B 1 216 ? -1.542  23.537  33.658 1.00 68.82  ?  208 VAL B CG1 1 
ATOM   2868 C  CG2 . VAL B 1 216 ? -1.684  22.663  35.992 1.00 73.28  ?  208 VAL B CG2 1 
ATOM   2869 N  N   . ALA B 1 217 ? -1.828  27.054  34.523 1.00 73.81  ?  209 ALA B N   1 
ATOM   2870 C  CA  . ALA B 1 217 ? -1.777  28.178  33.597 1.00 75.94  ?  209 ALA B CA  1 
ATOM   2871 C  C   . ALA B 1 217 ? -0.562  29.052  33.869 1.00 74.90  ?  209 ALA B C   1 
ATOM   2872 O  O   . ALA B 1 217 ? 0.063   29.573  32.938 1.00 70.61  ?  209 ALA B O   1 
ATOM   2873 C  CB  . ALA B 1 217 ? -3.061  29.000  33.699 1.00 83.88  ?  209 ALA B CB  1 
ATOM   2874 N  N   . GLU B 1 218 ? -0.208  29.215  35.143 1.00 73.63  ?  210 GLU B N   1 
ATOM   2875 C  CA  . GLU B 1 218 ? 0.938   30.027  35.521 1.00 75.33  ?  210 GLU B CA  1 
ATOM   2876 C  C   . GLU B 1 218 ? 2.268   29.403  35.124 1.00 68.11  ?  210 GLU B C   1 
ATOM   2877 O  O   . GLU B 1 218 ? 3.304   30.059  35.277 1.00 62.67  ?  210 GLU B O   1 
ATOM   2878 C  CB  . GLU B 1 218 ? 0.940   30.265  37.030 1.00 76.33  ?  210 GLU B CB  1 
ATOM   2879 C  CG  . GLU B 1 218 ? -0.253  31.021  37.565 1.00 79.42  ?  210 GLU B CG  1 
ATOM   2880 C  CD  . GLU B 1 218 ? -0.208  31.124  39.073 1.00 82.45  ?  210 GLU B CD  1 
ATOM   2881 O  OE1 . GLU B 1 218 ? 0.875   30.866  39.635 1.00 78.88  ?  210 GLU B OE1 1 
ATOM   2882 O  OE2 . GLU B 1 218 ? -1.244  31.449  39.691 1.00 81.44  ?  210 GLU B OE2 1 
ATOM   2883 N  N   . GLN B 1 219 ? 2.277   28.155  34.663 1.00 70.87  ?  211 GLN B N   1 
ATOM   2884 C  CA  . GLN B 1 219 ? 3.514   27.527  34.213 1.00 82.92  ?  211 GLN B CA  1 
ATOM   2885 C  C   . GLN B 1 219 ? 3.686   27.727  32.708 1.00 85.79  ?  211 GLN B C   1 
ATOM   2886 O  O   . GLN B 1 219 ? 3.495   26.792  31.927 1.00 92.26  ?  211 GLN B O   1 
ATOM   2887 C  CB  . GLN B 1 219 ? 3.534   26.033  34.533 1.00 78.95  ?  211 GLN B CB  1 
ATOM   2888 C  CG  . GLN B 1 219 ? 3.226   25.681  35.980 1.00 73.28  ?  211 GLN B CG  1 
ATOM   2889 C  CD  . GLN B 1 219 ? 4.148   26.369  36.966 1.00 75.69  ?  211 GLN B CD  1 
ATOM   2890 O  OE1 . GLN B 1 219 ? 5.347   26.094  37.017 1.00 72.06  ?  211 GLN B OE1 1 
ATOM   2891 N  NE2 . GLN B 1 219 ? 3.586   27.273  37.761 1.00 74.87  ?  211 GLN B NE2 1 
HETATM 2892 CL CL  . CL  C 2 .   ? -7.679  7.346   20.132 1.00 70.80  -1 301 CL  A CL  1 
HETATM 2893 CL CL  . CL  D 2 .   ? -6.880  12.756  55.205 1.00 58.98  -1 301 CL  B CL  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   . HIS A 7   ? 1.8496 1.8424 1.0765 0.1038  -0.0075 -0.0476 -1  HIS A N   
2    C CA  . HIS A 7   ? 1.8016 1.8251 1.0603 0.1172  0.0091  -0.0017 -1  HIS A CA  
3    C C   . HIS A 7   ? 1.9404 1.9954 1.2671 0.0982  -0.0188 0.0113  -1  HIS A C   
4    O O   . HIS A 7   ? 1.9084 1.9994 1.2541 0.1062  -0.0214 0.0452  -1  HIS A O   
5    C CB  . HIS A 7   ? 1.7755 1.7750 1.0658 0.1327  0.0623  0.0115  -1  HIS A CB  
6    C CG  . HIS A 7   ? 1.9451 1.9061 1.2746 0.1208  0.0751  -0.0205 -1  HIS A CG  
7    N ND1 . HIS A 7   ? 1.7806 1.7020 1.0822 0.1291  0.1039  -0.0457 -1  HIS A ND1 
8    C CD2 . HIS A 7   ? 1.9123 1.8679 1.3050 0.1028  0.0627  -0.0314 -1  HIS A CD2 
9    C CE1 . HIS A 7   ? 1.8779 1.7711 1.2262 0.1169  0.1065  -0.0721 -1  HIS A CE1 
10   N NE2 . HIS A 7   ? 1.8866 1.7989 1.2877 0.1017  0.0817  -0.0629 -1  HIS A NE2 
11   N N   . HIS A 8   ? 1.9627 2.0037 1.3261 0.0738  -0.0385 -0.0149 0   HIS A N   
12   C CA  . HIS A 8   ? 1.9735 2.0428 1.3958 0.0533  -0.0664 -0.0059 0   HIS A CA  
13   C C   . HIS A 8   ? 1.8233 1.9123 1.3058 0.0619  -0.0422 0.0283  0   HIS A C   
14   O O   . HIS A 8   ? 1.8581 1.9885 1.3573 0.0668  -0.0511 0.0573  0   HIS A O   
15   C CB  . HIS A 8   ? 1.7238 1.8322 1.1224 0.0467  -0.1088 -0.0032 0   HIS A CB  
16   C CG  . HIS A 8   ? 1.9915 2.0886 1.3145 0.0521  -0.1265 -0.0302 0   HIS A CG  
17   N ND1 . HIS A 8   ? 2.0674 2.1237 1.3657 0.0446  -0.1256 -0.0684 0   HIS A ND1 
18   C CD2 . HIS A 8   ? 1.9053 2.0273 1.1704 0.0665  -0.1463 -0.0257 0   HIS A CD2 
19   C CE1 . HIS A 8   ? 1.8852 1.9434 1.1144 0.0538  -0.1436 -0.0875 0   HIS A CE1 
20   N NE2 . HIS A 8   ? 2.0828 2.1803 1.2883 0.0680  -0.1568 -0.0620 0   HIS A NE2 
21   N N   . MET A 9   ? 1.5869 1.6454 1.1038 0.0652  -0.0125 0.0212  1   MET A N   
22   C CA  . MET A 9   ? 1.4379 1.5095 1.0124 0.0775  0.0146  0.0467  1   MET A CA  
23   C C   . MET A 9   ? 1.3569 1.4737 0.9799 0.0672  -0.0071 0.0699  1   MET A C   
24   O O   . MET A 9   ? 1.2260 1.3539 0.8569 0.0450  -0.0394 0.0608  1   MET A O   
25   C CB  . MET A 9   ? 1.3859 1.4191 0.9974 0.0769  0.0358  0.0260  1   MET A CB  
26   C CG  . MET A 9   ? 1.4809 1.4681 1.0551 0.0861  0.0591  -0.0010 1   MET A CG  
27   S SD  . MET A 9   ? 1.5040 1.4436 1.0789 0.0670  0.0442  -0.0453 1   MET A SD  
28   C CE  . MET A 9   ? 1.4089 1.3284 1.0522 0.0793  0.0736  -0.0483 1   MET A CE  
29   N N   . ARG A 10  ? 1.3123 1.4552 0.9734 0.0836  0.0127  0.0992  2   ARG A N   
30   C CA  . ARG A 10  ? 1.0457 1.2343 0.7583 0.0771  -0.0031 0.1219  2   ARG A CA  
31   C C   . ARG A 10  ? 0.9585 1.1411 0.7131 0.0568  -0.0151 0.1078  2   ARG A C   
32   O O   . ARG A 10  ? 0.9043 1.0531 0.6756 0.0593  0.0027  0.0917  2   ARG A O   
33   C CB  . ARG A 10  ? 1.0182 1.2272 0.7740 0.1001  0.0260  0.1495  2   ARG A CB  
34   C CG  . ARG A 10  ? 0.9949 1.2497 0.8148 0.0963  0.0160  0.1699  2   ARG A CG  
35   C CD  . ARG A 10  ? 1.0196 1.2700 0.9006 0.1103  0.0450  0.1716  2   ARG A CD  
36   N NE  . ARG A 10  ? 1.2241 1.5219 1.1600 0.1202  0.0470  0.1982  2   ARG A NE  
37   C CZ  . ARG A 10  ? 1.2605 1.5675 1.2577 0.1327  0.0656  0.2006  2   ARG A CZ  
38   N NH1 . ARG A 10  ? 1.2381 1.5109 1.2507 0.1370  0.0821  0.1779  2   ARG A NH1 
39   N NH2 . ARG A 10  ? 1.1863 1.5388 1.2317 0.1425  0.0660  0.2241  2   ARG A NH2 
40   N N   . SER A 11  ? 0.8541 1.0694 0.6262 0.0378  -0.0452 0.1143  3   SER A N   
41   C CA  . SER A 11  ? 0.8337 1.0459 0.6454 0.0183  -0.0550 0.1066  3   SER A CA  
42   C C   . SER A 11  ? 0.8349 1.0584 0.7019 0.0317  -0.0313 0.1209  3   SER A C   
43   O O   . SER A 11  ? 0.8745 1.1245 0.7627 0.0512  -0.0156 0.1412  3   SER A O   
44   C CB  . SER A 11  ? 0.7295 0.9801 0.5561 -0.0039 -0.0884 0.1135  3   SER A CB  
45   O OG  . SER A 11  ? 0.7199 1.0205 0.5660 0.0066  -0.0915 0.1402  3   SER A OG  
46   N N   . ASN A 12  ? 0.7236 0.9256 0.6138 0.0229  -0.0291 0.1094  4   ASN A N   
47   C CA  . ASN A 12  ? 0.7727 0.9830 0.7113 0.0381  -0.0088 0.1179  4   ASN A CA  
48   C C   . ASN A 12  ? 0.7165 0.9248 0.6793 0.0212  -0.0192 0.1161  4   ASN A C   
49   O O   . ASN A 12  ? 0.6551 0.8422 0.5976 -0.0015 -0.0373 0.1044  4   ASN A O   
50   C CB  . ASN A 12  ? 0.7649 0.9347 0.6998 0.0600  0.0184  0.1009  4   ASN A CB  
51   C CG  . ASN A 12  ? 0.7749 0.9566 0.7095 0.0824  0.0392  0.1120  4   ASN A CG  
52   O OD1 . ASN A 12  ? 0.7341 0.9513 0.7109 0.0973  0.0501  0.1316  4   ASN A OD1 
53   N ND2 . ASN A 12  ? 0.9505 1.1020 0.8383 0.0857  0.0461  0.0998  4   ASN A ND2 
54   N N   . TYR A 13  ? 0.6031 0.8340 0.6107 0.0336  -0.0067 0.1281  5   TYR A N   
55   C CA  . TYR A 13  ? 0.5946 0.8290 0.6256 0.0219  -0.0121 0.1321  5   TYR A CA  
56   C C   . TYR A 13  ? 0.6250 0.8271 0.6660 0.0424  0.0061  0.1187  5   TYR A C   
57   O O   . TYR A 13  ? 0.5995 0.8173 0.6688 0.0681  0.0235  0.1209  5   TYR A O   
58   C CB  . TYR A 13  ? 0.6140 0.9096 0.6883 0.0196  -0.0156 0.1576  5   TYR A CB  
59   C CG  . TYR A 13  ? 0.6925 0.9952 0.7907 0.0089  -0.0167 0.1649  5   TYR A CG  
60   C CD1 . TYR A 13  ? 0.7106 0.9709 0.7870 -0.0094 -0.0239 0.1542  5   TYR A CD1 
61   C CD2 . TYR A 13  ? 0.6513 1.0025 0.7941 0.0183  -0.0091 0.1832  5   TYR A CD2 
62   C CE1 . TYR A 13  ? 0.7289 0.9932 0.8243 -0.0179 -0.0215 0.1648  5   TYR A CE1 
63   C CE2 . TYR A 13  ? 0.7050 1.0632 0.8656 0.0103  -0.0068 0.1916  5   TYR A CE2 
64   C CZ  . TYR A 13  ? 0.8304 1.1441 0.9657 -0.0077 -0.0120 0.1839  5   TYR A CZ  
65   O OH  . TYR A 13  ? 0.9755 1.2940 1.1257 -0.0146 -0.0066 0.1960  5   TYR A OH  
66   N N   . ILE A 14  ? 0.5748 0.7319 0.5953 0.0320  0.0007  0.1036  6   ILE A N   
67   C CA  . ILE A 14  ? 0.5959 0.7148 0.6184 0.0521  0.0135  0.0865  6   ILE A CA  
68   C C   . ILE A 14  ? 0.6808 0.7946 0.7109 0.0438  0.0084  0.0950  6   ILE A C   
69   O O   . ILE A 14  ? 0.6476 0.7487 0.6625 0.0167  -0.0060 0.0993  6   ILE A O   
70   C CB  . ILE A 14  ? 0.6853 0.7456 0.6708 0.0520  0.0134  0.0578  6   ILE A CB  
71   C CG1 . ILE A 14  ? 0.6480 0.7149 0.6222 0.0603  0.0221  0.0528  6   ILE A CG1 
72   C CG2 . ILE A 14  ? 0.6802 0.7017 0.6717 0.0744  0.0241  0.0378  6   ILE A CG2 
73   C CD1 . ILE A 14  ? 0.6764 0.6906 0.6159 0.0615  0.0251  0.0240  6   ILE A CD1 
74   N N   . VAL A 15  ? 0.7045 0.8274 0.7588 0.0683  0.0206  0.0967  7   VAL A N   
75   C CA  . VAL A 15  ? 0.6973 0.8199 0.7568 0.0664  0.0197  0.1083  7   VAL A CA  
76   C C   . VAL A 15  ? 0.6911 0.7605 0.7332 0.0870  0.0238  0.0867  7   VAL A C   
77   O O   . VAL A 15  ? 0.7144 0.7664 0.7606 0.1113  0.0315  0.0643  7   VAL A O   
78   C CB  . VAL A 15  ? 0.7746 0.9580 0.8745 0.0805  0.0287  0.1287  7   VAL A CB  
79   C CG1 . VAL A 15  ? 0.8792 1.0585 0.9788 0.0863  0.0323  0.1384  7   VAL A CG1 
80   C CG2 . VAL A 15  ? 0.8034 1.0375 0.9210 0.0574  0.0213  0.1502  7   VAL A CG2 
81   N N   . ILE A 16  ? 0.7877 0.8301 0.8124 0.0775  0.0186  0.0936  8   ILE A N   
82   C CA  . ILE A 16  ? 0.8415 0.8316 0.8459 0.0976  0.0194  0.0761  8   ILE A CA  
83   C C   . ILE A 16  ? 0.8564 0.8652 0.8679 0.1117  0.0256  0.0954  8   ILE A C   
84   O O   . ILE A 16  ? 0.8293 0.8382 0.8320 0.0899  0.0236  0.1187  8   ILE A O   
85   C CB  . ILE A 16  ? 0.9423 0.8718 0.9116 0.0749  0.0069  0.0658  8   ILE A CB  
86   C CG1 . ILE A 16  ? 1.0090 0.9137 0.9671 0.0720  0.0031  0.0381  8   ILE A CG1 
87   C CG2 . ILE A 16  ? 0.9537 0.8333 0.9019 0.0926  0.0058  0.0581  8   ILE A CG2 
88   C CD1 . ILE A 16  ? 0.9109 0.8333 0.8640 0.0396  -0.0061 0.0452  8   ILE A CD1 
89   N N   . GLU A 17  ? 0.8155 0.8415 0.8451 0.1487  0.0342  0.0852  9   GLU A N   
90   C CA  . GLU A 17  ? 0.8356 0.8822 0.8692 0.1699  0.0406  0.0989  9   GLU A CA  
91   C C   . GLU A 17  ? 0.7532 0.7470 0.7600 0.1996  0.0372  0.0781  9   GLU A C   
92   O O   . GLU A 17  ? 0.8084 0.7614 0.8083 0.2103  0.0319  0.0483  9   GLU A O   
93   C CB  . GLU A 17  ? 0.8027 0.9130 0.8804 0.1940  0.0500  0.0998  9   GLU A CB  
94   C CG  . GLU A 17  ? 0.8473 1.0182 0.9525 0.1704  0.0534  0.1271  9   GLU A CG  
95   C CD  . GLU A 17  ? 0.9456 1.1768 1.0970 0.1972  0.0620  0.1261  9   GLU A CD  
96   O OE1 . GLU A 17  ? 0.8937 1.1188 1.0629 0.2279  0.0647  0.1002  9   GLU A OE1 
97   O OE2 . GLU A 17  ? 1.0400 1.3247 1.2146 0.1879  0.0661  0.1495  9   GLU A OE2 
98   N N   . GLY A 18  ? 0.8345 0.8298 0.8256 0.2144  0.0406  0.0937  10  GLY A N   
99   C CA  . GLY A 18  ? 0.9474 0.8971 0.9114 0.2486  0.0356  0.0746  10  GLY A CA  
100  C C   . GLY A 18  ? 0.9087 0.8496 0.8399 0.2539  0.0396  0.1019  10  GLY A C   
101  O O   . GLY A 18  ? 0.9658 0.9158 0.8894 0.2220  0.0456  0.1351  10  GLY A O   
102  N N   . LEU A 19  ? 1.0231 0.9452 0.9352 0.2966  0.0366  0.0867  11  LEU A N   
103  C CA  . LEU A 19  ? 1.0346 0.9438 0.9070 0.3108  0.0413  0.1113  11  LEU A CA  
104  C C   . LEU A 19  ? 1.0593 0.8957 0.8864 0.2903  0.0351  0.1231  11  LEU A C   
105  O O   . LEU A 19  ? 1.1736 0.9636 0.9970 0.2774  0.0232  0.1016  11  LEU A O   
106  C CB  . LEU A 19  ? 1.0356 0.9491 0.9003 0.3613  0.0363  0.0853  11  LEU A CB  
107  C CG  . LEU A 19  ? 1.0258 1.0143 0.9365 0.3533  0.0410  0.0705  11  LEU A CG  
108  C CD1 . LEU A 19  ? 1.0816 1.0690 1.0057 0.3449  0.0263  0.0275  11  LEU A CD1 
109  C CD2 . LEU A 19  ? 1.0140 1.0452 0.9128 0.3698  0.0573  0.1082  11  LEU A CD2 
110  N N   . GLU A 20  ? 1.1081 0.9346 0.9016 0.2886  0.0447  0.1581  12  GLU A N   
111  C CA  . GLU A 20  ? 1.2475 1.0083 1.0038 0.2650  0.0423  0.1773  12  GLU A CA  
112  C C   . GLU A 20  ? 1.3324 1.0231 1.0618 0.2868  0.0231  0.1439  12  GLU A C   
113  O O   . GLU A 20  ? 1.3652 1.0495 1.0832 0.3333  0.0148  0.1173  12  GLU A O   
114  C CB  . GLU A 20  ? 1.3092 1.0664 1.0291 0.2734  0.0582  0.2181  12  GLU A CB  
115  N N   . GLY A 21  ? 1.5188 1.1581 1.2417 0.2536  0.0147  0.1426  13  GLY A N   
116  C CA  . GLY A 21  ? 1.5178 1.0897 1.2192 0.2697  -0.0040 0.1101  13  GLY A CA  
117  C C   . GLY A 21  ? 1.5187 1.0993 1.2525 0.2773  -0.0146 0.0639  13  GLY A C   
118  O O   . GLY A 21  ? 1.4558 0.9878 1.1775 0.2998  -0.0295 0.0304  13  GLY A O   
119  N N   . ALA A 22  ? 1.3549 0.9956 1.1305 0.2607  -0.0066 0.0614  14  ALA A N   
120  C CA  . ALA A 22  ? 1.2673 0.9154 1.0745 0.2620  -0.0123 0.0229  14  ALA A CA  
121  C C   . ALA A 22  ? 1.2326 0.8440 1.0383 0.2229  -0.0201 0.0144  14  ALA A C   
122  O O   . ALA A 22  ? 1.1655 0.7721 0.9896 0.2240  -0.0241 -0.0186 14  ALA A O   
123  C CB  . ALA A 22  ? 1.1692 0.8939 1.0197 0.2602  -0.0001 0.0268  14  ALA A CB  
124  N N   . GLY A 23  ? 1.3315 0.9175 1.1181 0.1895  -0.0213 0.0421  15  GLY A N   
125  C CA  . GLY A 23  ? 1.2672 0.8269 1.0573 0.1508  -0.0297 0.0338  15  GLY A CA  
126  C C   . GLY A 23  ? 1.0754 0.6920 0.8982 0.1277  -0.0242 0.0326  15  GLY A C   
127  O O   . GLY A 23  ? 1.0085 0.6207 0.8412 0.1258  -0.0287 0.0025  15  GLY A O   
128  N N   . LYS A 24  ? 1.0904 0.7614 0.9297 0.1123  -0.0135 0.0654  16  LYS A N   
129  C CA  . LYS A 24  ? 1.0802 0.8071 0.9496 0.0921  -0.0100 0.0670  16  LYS A CA  
130  C C   . LYS A 24  ? 1.0421 0.7515 0.9107 0.0509  -0.0208 0.0642  16  LYS A C   
131  O O   . LYS A 24  ? 0.9596 0.6830 0.8373 0.0427  -0.0247 0.0449  16  LYS A O   
132  C CB  . LYS A 24  ? 1.0414 0.8321 0.9319 0.0889  0.0028  0.1008  16  LYS A CB  
133  C CG  . LYS A 24  ? 1.0344 0.8618 0.9372 0.1300  0.0128  0.0966  16  LYS A CG  
134  C CD  . LYS A 24  ? 1.0102 0.9012 0.9344 0.1266  0.0255  0.1293  16  LYS A CD  
135  C CE  . LYS A 24  ? 1.0941 0.9667 0.9949 0.1224  0.0321  0.1595  16  LYS A CE  
136  N NZ  . LYS A 24  ? 1.1150 0.9400 0.9804 0.1599  0.0300  0.1483  16  LYS A NZ  
137  N N   . THR A 25  ? 1.1509 0.8302 1.0099 0.0255  -0.0254 0.0832  17  THR A N   
138  C CA  . THR A 25  ? 1.2023 0.8657 1.0660 -0.0132 -0.0381 0.0772  17  THR A CA  
139  C C   . THR A 25  ? 1.1969 0.8107 1.0430 -0.0086 -0.0511 0.0375  17  THR A C   
140  O O   . THR A 25  ? 1.1158 0.7371 0.9667 -0.0283 -0.0600 0.0200  17  THR A O   
141  C CB  . THR A 25  ? 1.2350 0.8710 1.0990 -0.0393 -0.0389 0.1043  17  THR A CB  
142  O OG1 . THR A 25  ? 1.3635 0.9414 1.1993 -0.0176 -0.0378 0.1056  17  THR A OG1 
143  C CG2 . THR A 25  ? 1.1296 0.8220 1.0179 -0.0504 -0.0244 0.1425  17  THR A CG2 
144  N N   . THR A 26  ? 1.1444 0.7081 0.9694 0.0191  -0.0527 0.0214  18  THR A N   
145  C CA  . THR A 26  ? 1.1428 0.6611 0.9552 0.0262  -0.0635 -0.0191 18  THR A CA  
146  C C   . THR A 26  ? 1.0642 0.6163 0.8874 0.0437  -0.0567 -0.0436 18  THR A C   
147  O O   . THR A 26  ? 1.0525 0.5892 0.8717 0.0357  -0.0626 -0.0722 18  THR A O   
148  C CB  . THR A 26  ? 1.1649 0.6216 0.9554 0.0532  -0.0685 -0.0310 18  THR A CB  
149  O OG1 . THR A 26  ? 1.0460 0.4748 0.8328 0.0720  -0.0741 -0.0742 18  THR A OG1 
150  C CG2 . THR A 26  ? 1.2240 0.6974 1.0097 0.0866  -0.0575 -0.0111 18  THR A CG2 
151  N N   . ALA A 27  ? 1.0168 0.6146 0.8550 0.0680  -0.0431 -0.0329 19  ALA A N   
152  C CA  . ALA A 27  ? 0.9569 0.5894 0.8123 0.0827  -0.0338 -0.0515 19  ALA A CA  
153  C C   . ALA A 27  ? 1.0236 0.6975 0.8871 0.0537  -0.0338 -0.0419 19  ALA A C   
154  O O   . ALA A 27  ? 1.0519 0.7326 0.9167 0.0560  -0.0303 -0.0627 19  ALA A O   
155  C CB  . ALA A 27  ? 0.9555 0.6285 0.8316 0.1154  -0.0205 -0.0423 19  ALA A CB  
156  N N   . ARG A 28  ? 1.0256 0.7282 0.8951 0.0279  -0.0371 -0.0108 20  ARG A N   
157  C CA  . ARG A 28  ? 0.9675 0.7077 0.8440 0.0008  -0.0418 -0.0041 20  ARG A CA  
158  C C   . ARG A 28  ? 0.9725 0.6751 0.8287 -0.0157 -0.0547 -0.0329 20  ARG A C   
159  O O   . ARG A 28  ? 0.9410 0.6649 0.7932 -0.0188 -0.0543 -0.0446 20  ARG A O   
160  C CB  . ARG A 28  ? 0.9911 0.7592 0.8817 -0.0264 -0.0460 0.0291  20  ARG A CB  
161  C CG  . ARG A 28  ? 0.9963 0.8195 0.9030 -0.0479 -0.0506 0.0403  20  ARG A CG  
162  C CD  . ARG A 28  ? 0.9487 0.7526 0.8440 -0.0777 -0.0696 0.0239  20  ARG A CD  
163  N NE  . ARG A 28  ? 1.0230 0.7796 0.9156 -0.0974 -0.0795 0.0240  20  ARG A NE  
164  C CZ  . ARG A 28  ? 0.9775 0.7431 0.8911 -0.1166 -0.0793 0.0511  20  ARG A CZ  
165  N NH1 . ARG A 28  ? 0.8900 0.7131 0.8295 -0.1200 -0.0710 0.0786  20  ARG A NH1 
166  N NH2 . ARG A 28  ? 1.0404 0.7556 0.9518 -0.1323 -0.0861 0.0509  20  ARG A NH2 
167  N N   . GLU A 29  ? 1.0619 0.7071 0.9035 -0.0242 -0.0659 -0.0452 21  GLU A N   
168  C CA  . GLU A 29  ? 1.0912 0.6993 0.9153 -0.0385 -0.0791 -0.0763 21  GLU A CA  
169  C C   . GLU A 29  ? 1.0839 0.6859 0.8981 -0.0150 -0.0697 -0.1071 21  GLU A C   
170  O O   . GLU A 29  ? 1.1301 0.7374 0.9320 -0.0247 -0.0733 -0.1252 21  GLU A O   
171  C CB  . GLU A 29  ? 1.1486 0.6916 0.9628 -0.0455 -0.0913 -0.0866 21  GLU A CB  
172  C CG  . GLU A 29  ? 1.2333 0.7696 1.0577 -0.0584 -0.0929 -0.0531 21  GLU A CG  
173  C CD  . GLU A 29  ? 1.1998 0.7750 1.0440 -0.0926 -0.0990 -0.0303 21  GLU A CD  
174  O OE1 . GLU A 29  ? 1.1345 0.7634 0.9872 -0.0965 -0.0966 -0.0265 21  GLU A OE1 
175  O OE2 . GLU A 29  ? 1.2817 0.8329 1.1358 -0.1149 -0.1061 -0.0159 21  GLU A OE2 
176  N N   . CYS A 30  ? 1.0387 0.6292 0.8593 0.0170  -0.0572 -0.1145 22  CYS A N   
177  C CA  . CYS A 30  ? 1.0968 0.6798 0.9171 0.0398  -0.0453 -0.1449 22  CYS A CA  
178  C C   . CYS A 30  ? 1.0429 0.6807 0.8716 0.0413  -0.0316 -0.1353 22  CYS A C   
179  O O   . CYS A 30  ? 1.0542 0.6884 0.8723 0.0432  -0.0250 -0.1566 22  CYS A O   
180  C CB  . CYS A 30  ? 1.0689 0.6333 0.9032 0.0749  -0.0365 -0.1552 22  CYS A CB  
181  S SG  . CYS A 30  ? 1.1100 0.5976 0.9280 0.0807  -0.0529 -0.1779 22  CYS A SG  
182  N N   . VAL A 31  ? 0.9922 0.6806 0.8393 0.0416  -0.0261 -0.1027 23  VAL A N   
183  C CA  . VAL A 31  ? 0.9834 0.7240 0.8393 0.0426  -0.0151 -0.0900 23  VAL A CA  
184  C C   . VAL A 31  ? 0.9804 0.7263 0.8110 0.0161  -0.0271 -0.0935 23  VAL A C   
185  O O   . VAL A 31  ? 0.9393 0.7006 0.7595 0.0210  -0.0180 -0.1007 23  VAL A O   
186  C CB  . VAL A 31  ? 0.8980 0.6917 0.7803 0.0448  -0.0110 -0.0547 23  VAL A CB  
187  C CG1 . VAL A 31  ? 0.8764 0.7228 0.7676 0.0439  -0.0029 -0.0399 23  VAL A CG1 
188  C CG2 . VAL A 31  ? 0.9469 0.7391 0.8528 0.0758  0.0006  -0.0556 23  VAL A CG2 
189  N N   . VAL A 32  ? 1.0273 0.7608 0.8485 -0.0111 -0.0474 -0.0884 24  VAL A N   
190  C CA  . VAL A 32  ? 0.9881 0.7285 0.7884 -0.0354 -0.0630 -0.0955 24  VAL A CA  
191  C C   . VAL A 32  ? 1.0264 0.7264 0.7982 -0.0310 -0.0630 -0.1328 24  VAL A C   
192  O O   . VAL A 32  ? 1.0645 0.7806 0.8143 -0.0333 -0.0628 -0.1415 24  VAL A O   
193  C CB  . VAL A 32  ? 0.9358 0.6696 0.7434 -0.0654 -0.0846 -0.0847 24  VAL A CB  
194  C CG1 . VAL A 32  ? 1.0992 0.8353 0.8890 -0.0893 -0.1050 -0.0999 24  VAL A CG1 
195  C CG2 . VAL A 32  ? 0.9408 0.7230 0.7776 -0.0704 -0.0815 -0.0472 24  VAL A CG2 
196  N N   . GLU A 33  ? 1.0505 0.6977 0.8207 -0.0231 -0.0630 -0.1558 25  GLU A N   
197  C CA  . GLU A 33  ? 1.1132 0.7215 0.8597 -0.0195 -0.0629 -0.1940 25  GLU A CA  
198  C C   . GLU A 33  ? 1.0699 0.6950 0.8116 0.0036  -0.0380 -0.2027 25  GLU A C   
199  O O   . GLU A 33  ? 1.1182 0.7412 0.8329 0.0012  -0.0355 -0.2214 25  GLU A O   
200  C CB  . GLU A 33  ? 1.2056 0.7549 0.9568 -0.0123 -0.0677 -0.2166 25  GLU A CB  
201  C CG  . GLU A 33  ? 1.2635 0.7832 1.0134 -0.0378 -0.0924 -0.2154 25  GLU A CG  
202  C CD  . GLU A 33  ? 1.6381 1.0967 1.3907 -0.0280 -0.0976 -0.2357 25  GLU A CD  
203  O OE1 . GLU A 33  ? 1.7813 1.2333 1.5402 -0.0108 -0.0835 -0.2606 25  GLU A OE1 
204  O OE2 . GLU A 33  ? 1.6737 1.1119 1.4352 -0.0380 -0.1090 -0.2190 25  GLU A OE2 
205  N N   . THR A 34  ? 0.9749 0.6172 0.7440 0.0270  -0.0184 -0.1895 26  THR A N   
206  C CA  . THR A 34  ? 0.9680 0.6279 0.7422 0.0486  0.0081  -0.1943 26  THR A CA  
207  C C   . THR A 34  ? 1.0079 0.7134 0.7634 0.0397  0.0105  -0.1733 26  THR A C   
208  O O   . THR A 34  ? 1.0759 0.7807 0.8083 0.0454  0.0239  -0.1857 26  THR A O   
209  C CB  . THR A 34  ? 1.0849 0.7593 0.9006 0.0742  0.0251  -0.1834 26  THR A CB  
210  O OG1 . THR A 34  ? 1.1175 0.8344 0.9487 0.0678  0.0181  -0.1472 26  THR A OG1 
211  C CG2 . THR A 34  ? 1.1778 0.8052 1.0073 0.0873  0.0202  -0.2072 26  THR A CG2 
212  N N   . LEU A 35  ? 0.9946 0.7393 0.7581 0.0263  -0.0025 -0.1419 27  LEU A N   
213  C CA  . LEU A 35  ? 0.9760 0.7645 0.7219 0.0189  -0.0047 -0.1224 27  LEU A CA  
214  C C   . LEU A 35  ? 1.0681 0.8413 0.7689 0.0028  -0.0205 -0.1434 27  LEU A C   
215  O O   . LEU A 35  ? 0.9852 0.7801 0.6582 0.0072  -0.0146 -0.1397 27  LEU A O   
216  C CB  . LEU A 35  ? 0.9229 0.7541 0.6906 0.0055  -0.0193 -0.0894 27  LEU A CB  
217  C CG  . LEU A 35  ? 0.9276 0.7866 0.7376 0.0239  -0.0027 -0.0664 27  LEU A CG  
218  C CD1 . LEU A 35  ? 0.8681 0.7711 0.6980 0.0084  -0.0173 -0.0354 27  LEU A CD1 
219  C CD2 . LEU A 35  ? 0.8766 0.7571 0.6949 0.0479  0.0233  -0.0605 27  LEU A CD2 
220  N N   . LYS A 36  ? 1.0558 0.7917 0.7485 -0.0142 -0.0409 -0.1656 28  LYS A N   
221  C CA  . LYS A 36  ? 1.0530 0.7715 0.7058 -0.0267 -0.0560 -0.1926 28  LYS A CA  
222  C C   . LYS A 36  ? 1.1064 0.8019 0.7336 -0.0073 -0.0326 -0.2182 28  LYS A C   
223  O O   . LYS A 36  ? 1.0947 0.8015 0.6823 -0.0062 -0.0317 -0.2261 28  LYS A O   
224  C CB  . LYS A 36  ? 1.0556 0.7348 0.7137 -0.0474 -0.0809 -0.2129 28  LYS A CB  
225  C CG  . LYS A 36  ? 1.0467 0.7464 0.7293 -0.0705 -0.1035 -0.1896 28  LYS A CG  
226  C CD  . LYS A 36  ? 1.1723 0.8231 0.8690 -0.0851 -0.1189 -0.2055 28  LYS A CD  
227  C CE  . LYS A 36  ? 1.1683 0.8334 0.8926 -0.1109 -0.1393 -0.1838 28  LYS A CE  
228  N NZ  . LYS A 36  ? 1.1974 0.9081 0.9179 -0.1278 -0.1572 -0.1765 28  LYS A NZ  
229  N N   . GLN A 37  ? 1.1313 0.7949 0.7808 0.0093  -0.0131 -0.2322 29  GLN A N   
230  C CA  . GLN A 37  ? 1.1303 0.7711 0.7649 0.0275  0.0125  -0.2583 29  GLN A CA  
231  C C   . GLN A 37  ? 1.1288 0.8057 0.7527 0.0438  0.0397  -0.2377 29  GLN A C   
232  O O   . GLN A 37  ? 1.2417 0.9069 0.8394 0.0546  0.0602  -0.2551 29  GLN A O   
233  C CB  . GLN A 37  ? 1.2561 0.8615 0.9280 0.0444  0.0277  -0.2761 29  GLN A CB  
234  C CG  . GLN A 37  ? 1.3658 0.9212 1.0403 0.0345  0.0063  -0.3060 29  GLN A CG  
235  C CD  . GLN A 37  ? 1.4820 1.0323 1.1459 0.0254  0.0049  -0.3358 29  GLN A CD  
236  O OE1 . GLN A 37  ? 1.5642 1.1014 1.2218 0.0052  -0.0190 -0.3476 29  GLN A OE1 
237  N NE2 . GLN A 37  ? 1.5128 1.0844 1.1878 0.0402  0.0308  -0.3449 29  GLN A NE2 
238  N N   . LEU A 38  ? 0.8422 0.9058 0.8243 0.1797  -0.1894 0.0486  30  LEU A N   
239  C CA  . LEU A 38  ? 0.8348 0.9264 0.8376 0.1535  -0.1880 0.0238  30  LEU A CA  
240  C C   . LEU A 38  ? 0.8746 0.9390 0.9039 0.1431  -0.1924 0.0009  30  LEU A C   
241  O O   . LEU A 38  ? 0.8704 0.9492 0.9140 0.1198  -0.1881 -0.0189 30  LEU A O   
242  C CB  . LEU A 38  ? 0.8346 0.9601 0.8322 0.1393  -0.1874 0.0212  30  LEU A CB  
243  C CG  . LEU A 38  ? 0.8276 0.9763 0.8027 0.1423  -0.1830 0.0386  30  LEU A CG  
244  C CD1 . LEU A 38  ? 0.8264 0.9998 0.7925 0.1329  -0.1830 0.0375  30  LEU A CD1 
245  C CD2 . LEU A 38  ? 0.8519 1.0103 0.8349 0.1280  -0.1767 0.0329  30  LEU A CD2 
246  N N   . GLY A 39  ? 0.8691 0.8864 0.9056 0.1576  -0.1973 0.0054  31  GLY A N   
247  C CA  . GLY A 39  ? 0.9644 0.9487 1.0317 0.1452  -0.2012 -0.0156 31  GLY A CA  
248  C C   . GLY A 39  ? 0.9198 0.8874 1.0056 0.1254  -0.1953 -0.0255 31  GLY A C   
249  O O   . GLY A 39  ? 0.9754 0.9196 1.0904 0.1090  -0.1960 -0.0459 31  GLY A O   
250  N N   . VAL A 40  ? 0.9732 0.9533 1.0408 0.1210  -0.1835 -0.0124 32  VAL A N   
251  C CA  . VAL A 40  ? 0.9110 0.8745 0.9914 0.0975  -0.1681 -0.0200 32  VAL A CA  
252  C C   . VAL A 40  ? 0.9163 0.8221 0.9921 0.1012  -0.1500 -0.0031 32  VAL A C   
253  O O   . VAL A 40  ? 0.9764 0.8701 1.0234 0.1186  -0.1429 0.0243  32  VAL A O   
254  C CB  . VAL A 40  ? 0.8936 0.8970 0.9552 0.0907  -0.1627 -0.0135 32  VAL A CB  
255  C CG1 . VAL A 40  ? 0.8668 0.8576 0.9449 0.0646  -0.1471 -0.0252 32  VAL A CG1 
256  C CG2 . VAL A 40  ? 0.7995 0.8606 0.8632 0.0906  -0.1824 -0.0277 32  VAL A CG2 
257  N N   . SER A 41  ? 0.9052 0.7743 1.0096 0.0847  -0.1436 -0.0192 33  SER A N   
258  C CA  . SER A 41  ? 0.9628 0.7738 1.0679 0.0880  -0.1289 -0.0064 33  SER A CA  
259  C C   . SER A 41  ? 0.9259 0.7120 1.0421 0.0649  -0.1097 -0.0102 33  SER A C   
260  O O   . SER A 41  ? 0.9603 0.7063 1.0644 0.0681  -0.0940 0.0093  33  SER A O   
261  C CB  . SER A 41  ? 1.0161 0.7972 1.1459 0.0923  -0.1383 -0.0206 33  SER A CB  
262  O OG  . SER A 41  ? 1.0851 0.8816 1.2022 0.1159  -0.1529 -0.0134 33  SER A OG  
263  N N   . ASP A 42  ? 0.8796 0.6885 1.0188 0.0417  -0.1108 -0.0350 34  ASP A N   
264  C CA  . ASP A 42  ? 0.8949 0.6828 1.0501 0.0180  -0.0932 -0.0436 34  ASP A CA  
265  C C   . ASP A 42  ? 0.8587 0.6889 1.0004 0.0062  -0.0862 -0.0427 34  ASP A C   
266  O O   . ASP A 42  ? 0.7965 0.6736 0.9455 0.0010  -0.0995 -0.0594 34  ASP A O   
267  C CB  . ASP A 42  ? 1.0502 0.8262 1.2483 -0.0005 -0.1003 -0.0764 34  ASP A CB  
268  C CG  . ASP A 42  ? 0.9761 0.7979 1.1894 -0.0040 -0.1230 -0.0996 34  ASP A CG  
269  O OD1 . ASP A 42  ? 0.8611 0.7263 1.0529 0.0072  -0.1325 -0.0915 34  ASP A OD1 
270  O OD2 . ASP A 42  ? 1.1068 0.9469 1.3334 -0.0138 -0.1198 -0.1115 34  ASP A OD2 
271  N N   . MET A 43  ? 0.8433 0.6572 0.9652 0.0012  -0.0657 -0.0236 35  MET A N   
272  C CA  . MET A 43  ? 0.7779 0.6325 0.8825 -0.0090 -0.0577 -0.0201 35  MET A CA  
273  C C   . MET A 43  ? 0.7271 0.5538 0.8200 -0.0227 -0.0327 -0.0059 35  MET A C   
274  O O   . MET A 43  ? 0.7698 0.5451 0.8642 -0.0215 -0.0221 0.0051  35  MET A O   
275  C CB  . MET A 43  ? 0.7779 0.6683 0.8460 0.0126  -0.0674 0.0013  35  MET A CB  
276  C CG  . MET A 43  ? 0.8064 0.6638 0.8418 0.0350  -0.0624 0.0359  35  MET A CG  
277  S SD  . MET A 43  ? 0.8300 0.7315 0.8263 0.0608  -0.0762 0.0580  35  MET A SD  
278  C CE  . MET A 43  ? 0.9042 0.8094 0.9194 0.0798  -0.1005 0.0445  35  MET A CE  
279  N N   . VAL A 44  ? 0.7049 0.5678 0.7860 -0.0364 -0.0234 -0.0068 36  VAL A N   
280  C CA  . VAL A 44  ? 0.8111 0.6580 0.8836 -0.0551 0.0008  0.0012  36  VAL A CA  
281  C C   . VAL A 44  ? 0.7032 0.5841 0.7344 -0.0518 0.0074  0.0237  36  VAL A C   
282  O O   . VAL A 44  ? 0.6788 0.6120 0.7063 -0.0509 -0.0030 0.0142  36  VAL A O   
283  C CB  . VAL A 44  ? 0.6616 0.5205 0.7732 -0.0837 0.0073  -0.0335 36  VAL A CB  
284  C CG1 . VAL A 44  ? 0.7725 0.6258 0.8732 -0.1044 0.0328  -0.0264 36  VAL A CG1 
285  C CG2 . VAL A 44  ? 0.7926 0.6126 0.9439 -0.0881 0.0018  -0.0540 36  VAL A CG2 
286  N N   . PHE A 45  ? 0.7270 0.5782 0.7267 -0.0506 0.0241  0.0538  37  PHE A N   
287  C CA  . PHE A 45  ? 0.7831 0.6621 0.7424 -0.0517 0.0331  0.0758  37  PHE A CA  
288  C C   . PHE A 45  ? 0.7767 0.6615 0.7418 -0.0821 0.0555  0.0658  37  PHE A C   
289  O O   . PHE A 45  ? 0.8075 0.6483 0.7789 -0.0944 0.0716  0.0703  37  PHE A O   
290  C CB  . PHE A 45  ? 0.8207 0.6657 0.7379 -0.0332 0.0370  0.1169  37  PHE A CB  
291  C CG  . PHE A 45  ? 0.8147 0.6437 0.7275 -0.0031 0.0178  0.1285  37  PHE A CG  
292  C CD1 . PHE A 45  ? 0.8034 0.6580 0.7406 0.0073  -0.0023 0.1061  37  PHE A CD1 
293  C CD2 . PHE A 45  ? 0.8672 0.6550 0.7510 0.0145  0.0197  0.1620  37  PHE A CD2 
294  C CE1 . PHE A 45  ? 0.8658 0.7071 0.7987 0.0341  -0.0188 0.1161  37  PHE A CE1 
295  C CE2 . PHE A 45  ? 0.9038 0.6777 0.7850 0.0425  0.0024  0.1714  37  PHE A CE2 
296  C CZ  . PHE A 45  ? 0.8998 0.7013 0.8054 0.0521  -0.0161 0.1481  37  PHE A CZ  
297  N N   . THR A 46  ? 0.7578 0.6970 0.7199 -0.0941 0.0567  0.0526  38  THR A N   
298  C CA  . THR A 46  ? 0.8876 0.8410 0.8527 -0.1229 0.0780  0.0422  38  THR A CA  
299  C C   . THR A 46  ? 0.8638 0.8485 0.7828 -0.1237 0.0865  0.0661  38  THR A C   
300  O O   . THR A 46  ? 0.8184 0.8369 0.7162 -0.1062 0.0719  0.0753  38  THR A O   
301  C CB  . THR A 46  ? 0.8556 0.8485 0.8646 -0.1407 0.0729  -0.0008 38  THR A CB  
302  O OG1 . THR A 46  ? 0.7859 0.8283 0.7930 -0.1274 0.0523  -0.0094 38  THR A OG1 
303  C CG2 . THR A 46  ? 0.8129 0.7710 0.8678 -0.1447 0.0672  -0.0249 38  THR A CG2 
304  N N   . ARG A 47  ? 1.0296 1.0029 0.9324 -0.1445 0.1101  0.0763  39  ARG A N   
305  C CA  . ARG A 47  ? 1.1170 1.1247 0.9799 -0.1526 0.1211  0.0931  39  ARG A CA  
306  C C   . ARG A 47  ? 1.1869 1.2441 1.0752 -0.1789 0.1300  0.0581  39  ARG A C   
307  O O   . ARG A 47  ? 1.1725 1.2162 1.0898 -0.2018 0.1448  0.0377  39  ARG A O   
308  C CB  . ARG A 47  ? 1.2398 1.2058 1.0664 -0.1609 0.1414  0.1269  39  ARG A CB  
309  C CG  . ARG A 47  ? 1.5034 1.4156 1.3080 -0.1360 0.1329  0.1605  39  ARG A CG  
310  C CD  . ARG A 47  ? 1.7244 1.5944 1.4941 -0.1467 0.1524  0.1933  39  ARG A CD  
311  N NE  . ARG A 47  ? 1.6982 1.5099 1.4557 -0.1249 0.1446  0.2211  39  ARG A NE  
312  C CZ  . ARG A 47  ? 1.7332 1.4977 1.4623 -0.1293 0.1569  0.2523  39  ARG A CZ  
313  N NH1 . ARG A 47  ? 1.9328 1.7006 1.6398 -0.1556 0.1783  0.2617  39  ARG A NH1 
314  N NH2 . ARG A 47  ? 1.7207 1.4337 1.4437 -0.1074 0.1470  0.2742  39  ARG A NH2 
315  N N   . GLU A 48  ? 1.4917 1.6062 1.3706 -0.1753 0.1206  0.0503  40  GLU A N   
316  C CA  . GLU A 48  ? 1.4289 1.5945 1.3367 -0.1973 0.1249  0.0134  40  GLU A CA  
317  C C   . GLU A 48  ? 1.4905 1.6653 1.3779 -0.2241 0.1522  0.0190  40  GLU A C   
318  O O   . GLU A 48  ? 1.5584 1.7459 1.4787 -0.2490 0.1649  -0.0113 40  GLU A O   
319  C CB  . GLU A 48  ? 1.4611 1.6843 1.3652 -0.1843 0.1051  0.0039  40  GLU A CB  
320  C CG  . GLU A 48  ? 1.3453 1.5585 1.2567 -0.1553 0.0783  0.0078  40  GLU A CG  
321  C CD  . GLU A 48  ? 1.2472 1.4439 1.2121 -0.1575 0.0666  -0.0243 40  GLU A CD  
322  O OE1 . GLU A 48  ? 1.4012 1.6212 1.4033 -0.1783 0.0698  -0.0592 40  GLU A OE1 
323  O OE2 . GLU A 48  ? 1.2247 1.3857 1.1946 -0.1386 0.0536  -0.0150 40  GLU A OE2 
324  N N   . PRO A 49  ? 1.4853 1.6544 1.3193 -0.2207 0.1619  0.0565  41  PRO A N   
325  C CA  . PRO A 49  ? 1.7198 1.8816 1.5327 -0.2475 0.1898  0.0665  41  PRO A CA  
326  C C   . PRO A 49  ? 1.6478 1.7436 1.4693 -0.2540 0.2020  0.0774  41  PRO A C   
327  O O   . PRO A 49  ? 1.4474 1.4965 1.2407 -0.2371 0.1985  0.1121  41  PRO A O   
328  C CB  . PRO A 49  ? 1.6026 1.7752 1.3539 -0.2387 0.1916  0.1059  41  PRO A CB  
329  C CG  . PRO A 49  ? 1.4849 1.6851 1.2308 -0.2098 0.1652  0.1083  41  PRO A CG  
330  C CD  . PRO A 49  ? 1.2491 1.4255 1.0394 -0.1946 0.1475  0.0889  41  PRO A CD  
331  N N   . GLY A 50  ? 1.5312 1.6226 1.3923 -0.2782 0.2159  0.0475  42  GLY A N   
332  C CA  . GLY A 50  ? 1.4103 1.4410 1.2926 -0.2820 0.2227  0.0491  42  GLY A CA  
333  C C   . GLY A 50  ? 1.2579 1.2798 1.1901 -0.2684 0.2024  0.0208  42  GLY A C   
334  O O   . GLY A 50  ? 1.2161 1.2833 1.1790 -0.2703 0.1910  -0.0121 42  GLY A O   
335  N N   . GLY A 51  ? 1.1373 1.1015 1.0778 -0.2551 0.1969  0.0331  43  GLY A N   
336  C CA  . GLY A 51  ? 1.0781 1.0301 1.0586 -0.2392 0.1757  0.0121  43  GLY A CA  
337  C C   . GLY A 51  ? 0.8963 0.8295 0.9297 -0.2573 0.1813  -0.0220 43  GLY A C   
338  O O   . GLY A 51  ? 0.8673 0.7774 0.9317 -0.2449 0.1652  -0.0352 43  GLY A O   
339  N N   . THR A 52  ? 0.8795 0.8229 0.9244 -0.2865 0.2033  -0.0375 44  THR A N   
340  C CA  . THR A 52  ? 0.8782 0.8008 0.9723 -0.3052 0.2110  -0.0685 44  THR A CA  
341  C C   . THR A 52  ? 0.8970 0.7953 0.9762 -0.3294 0.2403  -0.0558 44  THR A C   
342  O O   . THR A 52  ? 0.9425 0.8550 0.9783 -0.3363 0.2544  -0.0313 44  THR A O   
343  C CB  . THR A 52  ? 0.7838 0.7579 0.9229 -0.3198 0.2048  -0.1150 44  THR A CB  
344  O OG1 . THR A 52  ? 0.8367 0.8635 0.9560 -0.3357 0.2179  -0.1182 44  THR A OG1 
345  C CG2 . THR A 52  ? 0.7266 0.7206 0.8848 -0.2979 0.1745  -0.1296 44  THR A CG2 
346  N N   . ILE A 53  ? 1.0001 0.9636 0.8487 -0.1065 0.0883  -0.0671 45  ILE A N   
347  C CA  . ILE A 53  ? 1.0119 0.9585 0.8561 -0.1224 0.0955  -0.0718 45  ILE A CA  
348  C C   . ILE A 53  ? 1.0295 1.0016 0.8930 -0.1249 0.0891  -0.0653 45  ILE A C   
349  O O   . ILE A 53  ? 0.9883 0.9422 0.8473 -0.1266 0.0976  -0.0605 45  ILE A O   
350  C CB  . ILE A 53  ? 1.1128 1.0566 0.9528 -0.1430 0.0956  -0.0894 45  ILE A CB  
351  C CG1 . ILE A 53  ? 1.0821 0.9893 0.8992 -0.1415 0.1068  -0.0955 45  ILE A CG1 
352  C CG2 . ILE A 53  ? 1.2409 1.1810 1.0876 -0.1619 0.1005  -0.0963 45  ILE A CG2 
353  C CD1 . ILE A 53  ? 0.9347 0.8347 0.7468 -0.1612 0.1090  -0.1151 45  ILE A CD1 
354  N N   . LEU A 54  ? 0.9982 1.0111 0.8822 -0.1241 0.0749  -0.0645 46  LEU A N   
355  C CA  . LEU A 54  ? 0.9143 0.9540 0.8184 -0.1259 0.0682  -0.0583 46  LEU A CA  
356  C C   . LEU A 54  ? 0.8974 0.9259 0.7995 -0.1089 0.0733  -0.0448 46  LEU A C   
357  O O   . LEU A 54  ? 0.9296 0.9520 0.8323 -0.1127 0.0773  -0.0408 46  LEU A O   
358  C CB  . LEU A 54  ? 0.8049 0.8881 0.7303 -0.1230 0.0535  -0.0575 46  LEU A CB  
359  C CG  . LEU A 54  ? 0.8480 0.9618 0.7965 -0.1219 0.0459  -0.0500 46  LEU A CG  
360  C CD1 . LEU A 54  ? 0.8551 0.9692 0.8078 -0.1414 0.0469  -0.0561 46  LEU A CD1 
361  C CD2 . LEU A 54  ? 0.7132 0.8666 0.6815 -0.1175 0.0336  -0.0489 46  LEU A CD2 
362  N N   . ALA A 55  ? 0.9147 0.9406 0.8144 -0.0890 0.0733  -0.0384 47  ALA A N   
363  C CA  . ALA A 55  ? 0.8294 0.8496 0.7289 -0.0697 0.0756  -0.0276 47  ALA A CA  
364  C C   . ALA A 55  ? 0.9153 0.8911 0.7885 -0.0686 0.0897  -0.0250 47  ALA A C   
365  O O   . ALA A 55  ? 0.9758 0.9452 0.8457 -0.0594 0.0923  -0.0169 47  ALA A O   
366  C CB  . ALA A 55  ? 0.9248 0.9516 0.8293 -0.0490 0.0733  -0.0248 47  ALA A CB  
367  N N   . GLU A 56  ? 0.9384 0.8812 0.7911 -0.0767 0.1000  -0.0317 48  GLU A N   
368  C CA  . GLU A 56  ? 1.0465 0.9434 0.8733 -0.0771 0.1162  -0.0296 48  GLU A CA  
369  C C   . GLU A 56  ? 1.0556 0.9486 0.8842 -0.0941 0.1215  -0.0307 48  GLU A C   
370  O O   . GLU A 56  ? 0.9928 0.8603 0.8066 -0.0869 0.1318  -0.0227 48  GLU A O   
371  C CB  . GLU A 56  ? 0.9989 0.8640 0.8069 -0.0847 0.1263  -0.0385 48  GLU A CB  
372  C CG  . GLU A 56  ? 1.1910 1.0510 0.9927 -0.0660 0.1248  -0.0363 48  GLU A CG  
373  C CD  . GLU A 56  ? 1.1858 1.0280 0.9758 -0.0764 0.1301  -0.0473 48  GLU A CD  
374  O OE1 . GLU A 56  ? 1.1643 0.9870 0.9454 -0.0954 0.1386  -0.0563 48  GLU A OE1 
375  O OE2 . GLU A 56  ? 1.0591 0.9073 0.8499 -0.0655 0.1262  -0.0479 48  GLU A OE2 
376  N N   . LYS A 57  ? 1.0718 0.9898 0.9180 -0.1156 0.1149  -0.0410 49  LYS A N   
377  C CA  . LYS A 57  ? 1.0114 0.9282 0.8633 -0.1333 0.1202  -0.0442 49  LYS A CA  
378  C C   . LYS A 57  ? 0.9335 0.8733 0.7982 -0.1237 0.1132  -0.0328 49  LYS A C   
379  O O   . LYS A 57  ? 0.9657 0.8887 0.8244 -0.1288 0.1232  -0.0294 49  LYS A O   
380  C CB  . LYS A 57  ? 0.9557 0.8972 0.8254 -0.1572 0.1129  -0.0603 49  LYS A CB  
381  C CG  . LYS A 57  ? 1.0660 0.9813 0.9224 -0.1699 0.1222  -0.0747 49  LYS A CG  
382  C CD  . LYS A 57  ? 1.0572 0.9967 0.9309 -0.1929 0.1150  -0.0936 49  LYS A CD  
383  C CE  . LYS A 57  ? 1.2293 1.1412 1.0898 -0.2048 0.1252  -0.1096 49  LYS A CE  
384  N NZ  . LYS A 57  ? 1.3803 1.3208 1.2557 -0.2212 0.1137  -0.1299 49  LYS A NZ  
385  N N   . LEU A 58  ? 0.8970 0.8740 0.7794 -0.1100 0.0975  -0.0273 50  LEU A N   
386  C CA  . LEU A 58  ? 0.9215 0.9199 0.8160 -0.0985 0.0910  -0.0171 50  LEU A CA  
387  C C   . LEU A 58  ? 0.9288 0.8936 0.7994 -0.0775 0.1013  -0.0061 50  LEU A C   
388  O O   . LEU A 58  ? 0.9587 0.9205 0.8265 -0.0733 0.1042  0.0011  50  LEU A O   
389  C CB  . LEU A 58  ? 0.8385 0.8819 0.7583 -0.0873 0.0741  -0.0149 50  LEU A CB  
390  C CG  . LEU A 58  ? 0.8693 0.9512 0.8134 -0.1036 0.0621  -0.0229 50  LEU A CG  
391  C CD1 . LEU A 58  ? 0.7693 0.8870 0.7344 -0.0890 0.0499  -0.0194 50  LEU A CD1 
392  C CD2 . LEU A 58  ? 0.8797 0.9787 0.8378 -0.1194 0.0595  -0.0243 50  LEU A CD2 
393  N N   . ARG A 59  ? 0.9590 0.8981 0.8110 -0.0627 0.1068  -0.0046 51  ARG A N   
394  C CA  . ARG A 59  ? 1.0110 0.9163 0.8372 -0.0403 0.1163  0.0053  51  ARG A CA  
395  C C   . ARG A 59  ? 1.0048 0.8652 0.8052 -0.0503 0.1357  0.0073  51  ARG A C   
396  O O   . ARG A 59  ? 1.1229 0.9660 0.9074 -0.0366 0.1419  0.0170  51  ARG A O   
397  C CB  . ARG A 59  ? 1.1122 0.9983 0.9242 -0.0236 0.1187  0.0049  51  ARG A CB  
398  C CG  . ARG A 59  ? 1.2287 1.0775 1.0110 0.0015  0.1285  0.0143  51  ARG A CG  
399  C CD  . ARG A 59  ? 1.3146 1.1535 1.0891 0.0210  0.1274  0.0133  51  ARG A CD  
400  N NE  . ARG A 59  ? 1.5222 1.3332 1.2712 0.0496  0.1328  0.0219  51  ARG A NE  
401  C CZ  . ARG A 59  ? 1.5491 1.3078 1.2624 0.0557  0.1497  0.0256  51  ARG A CZ  
402  N NH1 . ARG A 59  ? 1.6443 1.3727 1.3452 0.0341  0.1637  0.0205  51  ARG A NH1 
403  N NH2 . ARG A 59  ? 1.5812 1.3178 1.2707 0.0851  0.1528  0.0338  51  ARG A NH2 
404  N N   . SER A 60  ? 0.9840 0.8239 0.7793 -0.0735 0.1464  -0.0026 52  SER A N   
405  C CA  . SER A 60  ? 1.1239 0.9204 0.8982 -0.0855 0.1677  -0.0027 52  SER A CA  
406  C C   . SER A 60  ? 1.0818 0.8953 0.8702 -0.0976 0.1672  -0.0014 52  SER A C   
407  O O   . SER A 60  ? 1.0769 0.8564 0.8454 -0.0960 0.1839  0.0051  52  SER A O   
408  C CB  . SER A 60  ? 1.0752 0.8513 0.8472 -0.1093 0.1787  -0.0171 52  SER A CB  
409  O OG  . SER A 60  ? 1.0835 0.8961 0.8846 -0.1338 0.1688  -0.0299 52  SER A OG  
410  N N   . LEU A 61  ? 1.0341 0.8981 0.8556 -0.1095 0.1494  -0.0074 53  LEU A N   
411  C CA  . LEU A 61  ? 1.0032 0.8877 0.8409 -0.1205 0.1472  -0.0064 53  LEU A CA  
412  C C   . LEU A 61  ? 1.0552 0.9397 0.8834 -0.0964 0.1453  0.0088  53  LEU A C   
413  O O   . LEU A 61  ? 1.1130 0.9792 0.9312 -0.0992 0.1569  0.0139  53  LEU A O   
414  C CB  . LEU A 61  ? 1.0139 0.9538 0.8879 -0.1343 0.1269  -0.0153 53  LEU A CB  
415  C CG  . LEU A 61  ? 0.9177 0.8934 0.8165 -0.1437 0.1179  -0.0148 53  LEU A CG  
416  C CD1 . LEU A 61  ? 0.9104 0.9209 0.8367 -0.1672 0.1069  -0.0299 53  LEU A CD1 
417  C CD2 . LEU A 61  ? 0.9211 0.9291 0.8309 -0.1212 0.1025  -0.0034 53  LEU A CD2 
418  N N   . VAL A 62  ? 1.0270 0.9312 0.8579 -0.0718 0.1315  0.0153  54  VAL A N   
419  C CA  . VAL A 62  ? 1.0484 0.9573 0.8721 -0.0464 0.1272  0.0273  54  VAL A CA  
420  C C   . VAL A 62  ? 1.1001 0.9521 0.8817 -0.0305 0.1470  0.0365  54  VAL A C   
421  O O   . VAL A 62  ? 1.0944 0.9360 0.8621 -0.0183 0.1516  0.0457  54  VAL A O   
422  C CB  . VAL A 62  ? 0.9713 0.9153 0.8112 -0.0242 0.1087  0.0285  54  VAL A CB  
423  C CG1 . VAL A 62  ? 0.9421 0.8794 0.7661 0.0074  0.1069  0.0388  54  VAL A CG1 
424  C CG2 . VAL A 62  ? 0.8498 0.8505 0.7302 -0.0358 0.0907  0.0231  54  VAL A CG2 
425  N N   . LEU A 63  ? 1.1327 0.9460 0.8914 -0.0287 0.1592  0.0346  55  LEU A N   
426  C CA  . LEU A 63  ? 1.1529 0.9076 0.8691 -0.0139 0.1804  0.0436  55  LEU A CA  
427  C C   . LEU A 63  ? 1.1962 0.9172 0.9007 -0.0359 0.2024  0.0429  55  LEU A C   
428  O O   . LEU A 63  ? 1.3106 0.9919 0.9834 -0.0223 0.2188  0.0535  55  LEU A O   
429  C CB  . LEU A 63  ? 1.1535 0.8762 0.8502 -0.0070 0.1882  0.0411  55  LEU A CB  
430  C CG  . LEU A 63  ? 1.1555 0.9040 0.8603 0.0175  0.1700  0.0417  55  LEU A CG  
431  C CD1 . LEU A 63  ? 1.4827 1.1913 1.1627 0.0253  0.1813  0.0405  55  LEU A CD1 
432  C CD2 . LEU A 63  ? 1.0912 0.8523 0.7894 0.0497  0.1601  0.0516  55  LEU A CD2 
433  N N   . ASP A 64  ? 1.1335 0.8689 0.8626 -0.0687 0.2039  0.0297  56  ASP A N   
434  C CA  . ASP A 64  ? 1.1550 0.8629 0.8796 -0.0917 0.2251  0.0260  56  ASP A CA  
435  C C   . ASP A 64  ? 1.2526 0.9765 0.9828 -0.0883 0.2224  0.0339  56  ASP A C   
436  O O   . ASP A 64  ? 1.1973 0.8832 0.9081 -0.0930 0.2445  0.0382  56  ASP A O   
437  C CB  . ASP A 64  ? 1.1663 0.8948 0.9213 -0.1263 0.2234  0.0071  56  ASP A CB  
438  C CG  . ASP A 64  ? 1.3646 1.0647 1.1089 -0.1337 0.2335  -0.0023 56  ASP A CG  
439  O OD1 . ASP A 64  ? 1.4295 1.0780 1.1392 -0.1201 0.2525  0.0051  56  ASP A OD1 
440  O OD2 . ASP A 64  ? 1.3154 1.0442 1.0846 -0.1523 0.2226  -0.0172 56  ASP A OD2 
441  N N   . ILE A 65  ? 1.2410 1.0198 0.9980 -0.0807 0.1970  0.0354  57  ILE A N   
442  C CA  . ILE A 65  ? 1.1949 0.9934 0.9594 -0.0764 0.1924  0.0425  57  ILE A CA  
443  C C   . ILE A 65  ? 1.2919 1.0631 1.0208 -0.0418 0.1973  0.0586  57  ILE A C   
444  O O   . ILE A 65  ? 1.3936 1.1412 1.1042 -0.0383 0.2109  0.0664  57  ILE A O   
445  C CB  . ILE A 65  ? 1.1476 1.0146 0.9548 -0.0809 0.1642  0.0374  57  ILE A CB  
446  C CG1 . ILE A 65  ? 1.0881 0.9783 0.9265 -0.1161 0.1624  0.0222  57  ILE A CG1 
447  C CG2 . ILE A 65  ? 1.1738 1.0636 0.9853 -0.0654 0.1553  0.0471  57  ILE A CG2 
448  C CD1 . ILE A 65  ? 0.9081 0.8616 0.7862 -0.1218 0.1373  0.0174  57  ILE A CD1 
449  N N   . GLN A 66  ? 1.2208 0.9946 0.9389 -0.0146 0.1865  0.0629  58  GLN A N   
450  C CA  . GLN A 66  ? 1.2252 0.9791 0.9110 0.0219  0.1874  0.0763  58  GLN A CA  
451  C C   . GLN A 66  ? 1.3596 1.0418 0.9961 0.0294  0.2172  0.0852  58  GLN A C   
452  O O   . GLN A 66  ? 1.4935 1.1529 1.1008 0.0512  0.2247  0.0968  58  GLN A O   
453  C CB  . GLN A 66  ? 1.1848 0.9579 0.8731 0.0482  0.1698  0.0759  58  GLN A CB  
454  C CG  . GLN A 66  ? 1.1517 0.9933 0.8838 0.0506  0.1420  0.0703  58  GLN A CG  
455  C CD  . GLN A 66  ? 1.1686 1.0297 0.9100 0.0703  0.1273  0.0663  58  GLN A CD  
456  O OE1 . GLN A 66  ? 1.1591 0.9843 0.8753 0.0808  0.1365  0.0672  58  GLN A OE1 
457  N NE2 . GLN A 66  ? 1.0819 0.9996 0.8609 0.0750  0.1055  0.0612  58  GLN A NE2 
458  N N   . SER A 67  ? 1.3678 1.0122 0.9931 0.0127  0.2354  0.0797  59  SER A N   
459  C CA  . SER A 67  ? 1.4913 1.0639 1.0701 0.0187  0.2669  0.0878  59  SER A CA  
460  C C   . SER A 67  ? 1.5232 1.0760 1.0961 0.0036  0.2858  0.0911  59  SER A C   
461  O O   . SER A 67  ? 1.6616 1.1694 1.1935 0.0240  0.3039  0.1044  59  SER A O   
462  C CB  . SER A 67  ? 1.4238 0.9642 0.9987 -0.0006 0.2829  0.0786  59  SER A CB  
463  O OG  . SER A 67  ? 1.5151 1.0614 1.1169 -0.0399 0.2926  0.0654  59  SER A OG  
464  N N   . THR A 68  ? 1.5139 1.0996 1.1265 -0.0310 0.2822  0.0789  60  THR A N   
465  C CA  . THR A 68  ? 1.5698 1.1402 1.1816 -0.0473 0.3001  0.0802  60  THR A CA  
466  C C   . THR A 68  ? 1.5197 1.1068 1.1218 -0.0224 0.2894  0.0933  60  THR A C   
467  O O   . THR A 68  ? 1.5094 1.0541 1.0787 -0.0133 0.3111  0.1039  60  THR A O   
468  C CB  . THR A 68  ? 1.5599 1.1710 1.2209 -0.0873 0.2937  0.0625  60  THR A CB  
469  O OG1 . THR A 68  ? 1.5176 1.1986 1.2163 -0.0858 0.2596  0.0589  60  THR A OG1 
470  C CG2 . THR A 68  ? 1.6132 1.2091 1.2842 -0.1117 0.3038  0.0473  60  THR A CG2 
471  N N   . GLY A 69  ? 1.5409 1.1883 1.1704 -0.0106 0.2573  0.0924  61  GLY A N   
472  C CA  . GLY A 69  ? 1.5896 1.2629 1.2196 0.0079  0.2448  0.1010  61  GLY A CA  
473  C C   . GLY A 69  ? 1.5885 1.2987 1.2569 -0.0219 0.2404  0.0935  61  GLY A C   
474  O O   . GLY A 69  ? 1.5527 1.2843 1.2555 -0.0547 0.2385  0.0797  61  GLY A O   
475  N N   . ASP A 70  ? 1.8171 1.5369 1.4800 -0.0096 0.2378  0.1018  62  ASP A N   
476  C CA  . ASP A 70  ? 1.8169 1.5703 1.5139 -0.0351 0.2341  0.0959  62  ASP A CA  
477  C C   . ASP A 70  ? 1.6842 1.5111 1.4340 -0.0469 0.2026  0.0852  62  ASP A C   
478  O O   . ASP A 70  ? 1.6143 1.4771 1.3978 -0.0685 0.1956  0.0789  62  ASP A O   
479  C CB  . ASP A 70  ? 1.8060 1.5260 1.5070 -0.0709 0.2614  0.0872  62  ASP A CB  
480  N N   . GLU A 71  ? 1.5311 1.3801 1.2894 -0.0340 0.1846  0.0825  63  GLU A N   
481  C CA  . GLU A 71  ? 1.3088 1.2250 1.1112 -0.0363 0.1552  0.0756  63  GLU A CA  
482  C C   . GLU A 71  ? 1.1997 1.1256 0.9953 -0.0073 0.1405  0.0779  63  GLU A C   
483  O O   . GLU A 71  ? 1.3755 1.2623 1.1434 0.0021  0.1513  0.0796  63  GLU A O   
484  C CB  . GLU A 71  ? 1.2085 1.1518 1.0485 -0.0713 0.1502  0.0610  63  GLU A CB  
485  C CG  . GLU A 71  ? 1.1326 1.1443 1.0182 -0.0765 0.1233  0.0554  63  GLU A CG  
486  C CD  . GLU A 71  ? 0.9215 0.9603 0.8394 -0.1042 0.1156  0.0415  63  GLU A CD  
487  O OE1 . GLU A 71  ? 1.0443 1.0616 0.9520 -0.1082 0.1212  0.0365  63  GLU A OE1 
488  O OE2 . GLU A 71  ? 0.9879 1.0694 0.9402 -0.1207 0.1036  0.0355  63  GLU A OE2 
489  N N   . VAL A 72  ? 1.1156 1.0940 0.9387 0.0063  0.1168  0.0769  64  VAL A N   
490  C CA  . VAL A 72  ? 1.1155 1.1124 0.9412 0.0334  0.1010  0.0764  64  VAL A CA  
491  C C   . VAL A 72  ? 1.0419 1.0949 0.9158 0.0187  0.0814  0.0660  64  VAL A C   
492  O O   . VAL A 72  ? 0.9501 1.0455 0.8568 0.0066  0.0703  0.0630  64  VAL A O   
493  C CB  . VAL A 72  ? 1.1771 1.1831 0.9897 0.0683  0.0923  0.0837  64  VAL A CB  
494  C CG1 . VAL A 72  ? 1.2220 1.2651 1.0593 0.0601  0.0839  0.0840  64  VAL A CG1 
495  C CG2 . VAL A 72  ? 1.1384 1.1751 0.9654 0.0940  0.0734  0.0790  64  VAL A CG2 
496  N N   . ILE A 73  ? 1.0382 1.0894 0.9151 0.0202  0.0785  0.0608  65  ILE A N   
497  C CA  . ILE A 73  ? 0.9355 1.0330 0.8531 0.0069  0.0630  0.0515  65  ILE A CA  
498  C C   . ILE A 73  ? 0.8049 0.9498 0.7493 0.0283  0.0440  0.0505  65  ILE A C   
499  O O   . ILE A 73  ? 0.7740 0.9158 0.7088 0.0561  0.0397  0.0513  65  ILE A O   
500  C CB  . ILE A 73  ? 0.9826 1.0614 0.8927 0.0042  0.0668  0.0465  65  ILE A CB  
501  C CG1 . ILE A 73  ? 1.0337 1.0633 0.9168 -0.0154 0.0870  0.0460  65  ILE A CG1 
502  C CG2 . ILE A 73  ? 0.8451 0.9685 0.7939 -0.0094 0.0528  0.0376  65  ILE A CG2 
503  C CD1 . ILE A 73  ? 1.0925 1.1324 0.9931 -0.0479 0.0905  0.0403  65  ILE A CD1 
504  N N   . ASN A 74  ? 0.7021 0.8922 0.6824 0.0154  0.0328  0.0473  66  ASN A N   
505  C CA  . ASN A 74  ? 0.6212 0.8592 0.6326 0.0328  0.0158  0.0444  66  ASN A CA  
506  C C   . ASN A 74  ? 0.7069 0.9589 0.7333 0.0425  0.0092  0.0377  66  ASN A C   
507  O O   . ASN A 74  ? 0.7799 1.0226 0.8074 0.0264  0.0133  0.0342  66  ASN A O   
508  C CB  . ASN A 74  ? 0.6193 0.9023 0.6686 0.0137  0.0064  0.0414  66  ASN A CB  
509  C CG  . ASN A 74  ? 0.6750 1.0075 0.7591 0.0305  -0.0093 0.0373  66  ASN A CG  
510  O OD1 . ASN A 74  ? 0.6751 1.0432 0.7937 0.0224  -0.0175 0.0311  66  ASN A OD1 
511  N ND2 . ASN A 74  ? 0.7474 1.0815 0.8219 0.0555  -0.0128 0.0400  66  ASN A ND2 
512  N N   . ASP A 75  ? 0.7110 0.9861 0.7500 0.0694  -0.0008 0.0348  67  ASP A N   
513  C CA  . ASP A 75  ? 0.6736 0.9611 0.7281 0.0809  -0.0055 0.0274  67  ASP A CA  
514  C C   . ASP A 75  ? 0.6357 0.9537 0.7250 0.0588  -0.0095 0.0216  67  ASP A C   
515  O O   . ASP A 75  ? 0.7288 1.0342 0.8151 0.0528  -0.0051 0.0185  67  ASP A O   
516  C CB  . ASP A 75  ? 0.8240 1.1402 0.8953 0.1118  -0.0168 0.0220  67  ASP A CB  
517  C CG  . ASP A 75  ? 0.8911 1.2530 0.9952 0.1114  -0.0277 0.0199  67  ASP A CG  
518  O OD1 . ASP A 75  ? 0.8750 1.2424 0.9836 0.0890  -0.0260 0.0245  67  ASP A OD1 
519  O OD2 . ASP A 75  ? 0.7854 1.1791 0.9123 0.1341  -0.0380 0.0122  67  ASP A OD2 
520  N N   . LYS A 76  ? 0.6042 0.9610 0.7248 0.0474  -0.0171 0.0204  68  LYS A N   
521  C CA  . LYS A 76  ? 0.5856 0.9715 0.7376 0.0294  -0.0207 0.0156  68  LYS A CA  
522  C C   . LYS A 76  ? 0.6166 0.9759 0.7503 0.0049  -0.0128 0.0169  68  LYS A C   
523  O O   . LYS A 76  ? 0.6290 0.9935 0.7722 -0.0027 -0.0124 0.0127  68  LYS A O   
524  C CB  . LYS A 76  ? 0.6393 1.0684 0.8249 0.0220  -0.0294 0.0150  68  LYS A CB  
525  C CG  . LYS A 76  ? 0.6696 1.1005 0.8656 0.0428  -0.0355 0.0097  68  LYS A CG  
526  C CD  . LYS A 76  ? 0.8038 1.2220 0.9983 0.0359  -0.0382 0.0104  68  LYS A CD  
527  C CE  . LYS A 76  ? 0.9069 1.2982 1.1092 0.0186  -0.0374 0.0064  68  LYS A CE  
528  N NZ  . LYS A 76  ? 0.9325 1.3078 1.1355 0.0177  -0.0399 0.0056  68  LYS A NZ  
529  N N   . ALA A 77  ? 0.6241 0.9543 0.7315 -0.0071 -0.0056 0.0217  69  ALA A N   
530  C CA  . ALA A 77  ? 0.6317 0.9368 0.7231 -0.0300 0.0022  0.0201  69  ALA A CA  
531  C C   . ALA A 77  ? 0.6653 0.9395 0.7356 -0.0231 0.0091  0.0180  69  ALA A C   
532  O O   . ALA A 77  ? 0.6577 0.9288 0.7289 -0.0370 0.0106  0.0133  69  ALA A O   
533  C CB  . ALA A 77  ? 0.6329 0.9087 0.7006 -0.0423 0.0115  0.0241  69  ALA A CB  
534  N N   . GLU A 78  ? 0.6445 0.8951 0.6942 -0.0007 0.0132  0.0212  70  GLU A N   
535  C CA  . GLU A 78  ? 0.6738 0.8945 0.7035 0.0074  0.0199  0.0193  70  GLU A CA  
536  C C   . GLU A 78  ? 0.6598 0.9081 0.7157 0.0117  0.0134  0.0130  70  GLU A C   
537  O O   . GLU A 78  ? 0.6520 0.8840 0.6991 0.0049  0.0183  0.0097  70  GLU A O   
538  C CB  . GLU A 78  ? 0.7406 0.9341 0.7443 0.0338  0.0242  0.0238  70  GLU A CB  
539  C CG  . GLU A 78  ? 0.9021 1.0545 0.8771 0.0408  0.0341  0.0234  70  GLU A CG  
540  C CD  . GLU A 78  ? 1.0905 1.2047 1.0294 0.0624  0.0418  0.0299  70  GLU A CD  
541  O OE1 . GLU A 78  ? 1.0446 1.1540 0.9733 0.0653  0.0433  0.0359  70  GLU A OE1 
542  O OE2 . GLU A 78  ? 1.2111 1.2988 1.1305 0.0774  0.0469  0.0293  70  GLU A OE2 
543  N N   . VAL A 79  ? 0.6503 0.9398 0.7390 0.0228  0.0035  0.0108  71  VAL A N   
544  C CA  . VAL A 79  ? 0.6254 0.9399 0.7410 0.0275  0.0002  0.0044  71  VAL A CA  
545  C C   . VAL A 79  ? 0.5624 0.8831 0.6845 0.0044  0.0012  0.0026  71  VAL A C   
546  O O   . VAL A 79  ? 0.6308 0.9405 0.7481 0.0030  0.0055  -0.0008 71  VAL A O   
547  C CB  . VAL A 79  ? 0.6730 1.0322 0.8265 0.0411  -0.0091 0.0010  71  VAL A CB  
548  C CG1 . VAL A 79  ? 0.6216 1.0060 0.8057 0.0418  -0.0093 -0.0058 71  VAL A CG1 
549  C CG2 . VAL A 79  ? 0.7017 1.0564 0.8487 0.0680  -0.0115 -0.0001 71  VAL A CG2 
550  N N   . LEU A 80  ? 0.4924 0.8311 0.6248 -0.0128 -0.0031 0.0043  72  LEU A N   
551  C CA  . LEU A 80  ? 0.5238 0.8693 0.6603 -0.0327 -0.0037 0.0017  72  LEU A CA  
552  C C   . LEU A 80  ? 0.5622 0.8686 0.6667 -0.0425 0.0043  -0.0003 72  LEU A C   
553  O O   . LEU A 80  ? 0.5356 0.8416 0.6390 -0.0498 0.0051  -0.0043 72  LEU A O   
554  C CB  . LEU A 80  ? 0.5866 0.9550 0.7368 -0.0490 -0.0097 0.0030  72  LEU A CB  
555  C CG  . LEU A 80  ? 0.6262 1.0367 0.8116 -0.0404 -0.0176 0.0039  72  LEU A CG  
556  C CD1 . LEU A 80  ? 0.7360 1.1514 0.9246 -0.0516 -0.0221 0.0063  72  LEU A CD1 
557  C CD2 . LEU A 80  ? 0.7508 1.1638 0.9489 -0.0384 -0.0184 0.0006  72  LEU A CD2 
558  N N   . MET A 81  ? 0.5349 0.8069 0.6121 -0.0419 0.0111  0.0022  73  MET A N   
559  C CA  . MET A 81  ? 0.5519 0.7850 0.5999 -0.0502 0.0202  -0.0006 73  MET A CA  
560  C C   . MET A 81  ? 0.5583 0.7773 0.5988 -0.0349 0.0241  -0.0023 73  MET A C   
561  O O   . MET A 81  ? 0.5619 0.7627 0.5885 -0.0428 0.0286  -0.0067 73  MET A O   
562  C CB  . MET A 81  ? 0.5575 0.7547 0.5786 -0.0526 0.0293  0.0029  73  MET A CB  
563  C CG  . MET A 81  ? 0.6624 0.8653 0.6873 -0.0733 0.0292  0.0020  73  MET A CG  
564  S SD  . MET A 81  ? 0.7193 0.8715 0.7100 -0.0800 0.0456  0.0044  73  MET A SD  
565  C CE  . MET A 81  ? 0.6952 0.8390 0.6752 -0.0504 0.0466  0.0154  73  MET A CE  
566  N N   . PHE A 82  ? 0.5231 0.7509 0.5732 -0.0127 0.0222  -0.0001 74  PHE A N   
567  C CA  . PHE A 82  ? 0.6331 0.8532 0.6826 0.0025  0.0254  -0.0033 74  PHE A CA  
568  C C   . PHE A 82  ? 0.6203 0.8628 0.6895 -0.0041 0.0234  -0.0078 74  PHE A C   
569  O O   . PHE A 82  ? 0.5243 0.7484 0.5808 -0.0053 0.0291  -0.0110 74  PHE A O   
570  C CB  . PHE A 82  ? 0.6534 0.8863 0.7161 0.0278  0.0219  -0.0027 74  PHE A CB  
571  C CG  . PHE A 82  ? 0.6222 0.8597 0.6970 0.0441  0.0236  -0.0084 74  PHE A CG  
572  C CD1 . PHE A 82  ? 0.7877 1.0592 0.8961 0.0442  0.0209  -0.0132 74  PHE A CD1 
573  C CD2 . PHE A 82  ? 0.7519 0.9593 0.8056 0.0602  0.0292  -0.0094 74  PHE A CD2 
574  C CE1 . PHE A 82  ? 0.9015 1.1764 1.0234 0.0586  0.0247  -0.0196 74  PHE A CE1 
575  C CE2 . PHE A 82  ? 0.8245 1.0372 0.8919 0.0751  0.0312  -0.0160 74  PHE A CE2 
576  C CZ  . PHE A 82  ? 0.8799 1.1265 0.9823 0.0738  0.0294  -0.0215 74  PHE A CZ  
577  N N   . TYR A 83  ? 0.5480 0.8286 0.6464 -0.0081 0.0162  -0.0077 75  TYR A N   
578  C CA  . TYR A 83  ? 0.5540 0.8539 0.6689 -0.0128 0.0159  -0.0108 75  TYR A CA  
579  C C   . TYR A 83  ? 0.5414 0.8289 0.6375 -0.0323 0.0164  -0.0124 75  TYR A C   
580  O O   . TYR A 83  ? 0.5452 0.8327 0.6399 -0.0337 0.0190  -0.0152 75  TYR A O   
581  C CB  . TYR A 83  ? 0.5911 0.9337 0.7422 -0.0111 0.0093  -0.0102 75  TYR A CB  
582  C CG  . TYR A 83  ? 0.7873 1.1484 0.9658 0.0078  0.0116  -0.0137 75  TYR A CG  
583  C CD1 . TYR A 83  ? 0.8579 1.2260 1.0472 0.0245  0.0089  -0.0151 75  TYR A CD1 
584  C CD2 . TYR A 83  ? 0.9596 1.3304 1.1529 0.0097  0.0172  -0.0169 75  TYR A CD2 
585  C CE1 . TYR A 83  ? 0.9598 1.3477 1.1781 0.0418  0.0107  -0.0215 75  TYR A CE1 
586  C CE2 . TYR A 83  ? 1.0607 1.4483 1.2827 0.0258  0.0215  -0.0223 75  TYR A CE2 
587  C CZ  . TYR A 83  ? 1.0755 1.4732 1.3119 0.0414  0.0177  -0.0256 75  TYR A CZ  
588  O OH  . TYR A 83  ? 1.1125 1.5249 1.3788 0.0568  0.0214  -0.0335 75  TYR A OH  
589  N N   . ALA A 84  ? 0.5814 0.8584 0.6632 -0.0468 0.0144  -0.0119 76  ALA A N   
590  C CA  . ALA A 84  ? 0.5747 0.8381 0.6383 -0.0643 0.0150  -0.0168 76  ALA A CA  
591  C C   . ALA A 84  ? 0.5839 0.8113 0.6210 -0.0613 0.0236  -0.0201 76  ALA A C   
592  O O   . ALA A 84  ? 0.5110 0.7332 0.5381 -0.0675 0.0243  -0.0252 76  ALA A O   
593  C CB  . ALA A 84  ? 0.4984 0.7564 0.5551 -0.0806 0.0133  -0.0177 76  ALA A CB  
594  N N   . ALA A 85  ? 0.6173 0.8190 0.6411 -0.0506 0.0301  -0.0175 77  ALA A N   
595  C CA  . ALA A 85  ? 0.5956 0.7627 0.5953 -0.0462 0.0388  -0.0203 77  ALA A CA  
596  C C   . ALA A 85  ? 0.5484 0.7240 0.5569 -0.0349 0.0402  -0.0220 77  ALA A C   
597  O O   . ALA A 85  ? 0.5969 0.7555 0.5892 -0.0388 0.0446  -0.0265 77  ALA A O   
598  C CB  . ALA A 85  ? 0.5875 0.7271 0.5722 -0.0334 0.0453  -0.0163 77  ALA A CB  
599  N N   . ARG A 86  ? 0.5428 0.7441 0.5775 -0.0206 0.0376  -0.0194 78  ARG A N   
600  C CA  . ARG A 86  ? 0.5745 0.7824 0.6203 -0.0096 0.0419  -0.0218 78  ARG A CA  
601  C C   . ARG A 86  ? 0.6352 0.8545 0.6816 -0.0201 0.0409  -0.0238 78  ARG A C   
602  O O   . ARG A 86  ? 0.6635 0.8688 0.6986 -0.0173 0.0474  -0.0266 78  ARG A O   
603  C CB  . ARG A 86  ? 0.6281 0.8647 0.7071 0.0063  0.0400  -0.0210 78  ARG A CB  
604  C CG  . ARG A 86  ? 0.7924 1.0377 0.8882 0.0165  0.0468  -0.0248 78  ARG A CG  
605  C CD  . ARG A 86  ? 1.1122 1.3871 1.2450 0.0319  0.0457  -0.0271 78  ARG A CD  
606  N NE  . ARG A 86  ? 1.2903 1.5540 1.4210 0.0479  0.0457  -0.0295 78  ARG A NE  
607  C CZ  . ARG A 86  ? 1.3738 1.6598 1.5347 0.0649  0.0446  -0.0349 78  ARG A CZ  
608  N NH1 . ARG A 86  ? 1.3502 1.6705 1.5480 0.0668  0.0450  -0.0385 78  ARG A NH1 
609  N NH2 . ARG A 86  ? 1.4332 1.7069 1.5872 0.0812  0.0435  -0.0376 78  ARG A NH2 
610  N N   . VAL A 87  ? 0.6077 0.8517 0.6656 -0.0310 0.0330  -0.0224 79  VAL A N   
611  C CA  . VAL A 87  ? 0.5329 0.7882 0.5887 -0.0393 0.0307  -0.0243 79  VAL A CA  
612  C C   . VAL A 87  ? 0.5286 0.7563 0.5520 -0.0494 0.0321  -0.0298 79  VAL A C   
613  O O   . VAL A 87  ? 0.6215 0.8435 0.6332 -0.0478 0.0351  -0.0325 79  VAL A O   
614  C CB  . VAL A 87  ? 0.5623 0.8489 0.6360 -0.0490 0.0208  -0.0223 79  VAL A CB  
615  C CG1 . VAL A 87  ? 0.5685 0.8632 0.6335 -0.0574 0.0169  -0.0253 79  VAL A CG1 
616  C CG2 . VAL A 87  ? 0.6395 0.9558 0.7474 -0.0384 0.0202  -0.0181 79  VAL A CG2 
617  N N   . GLN A 88  ? 0.5552 0.7651 0.5636 -0.0597 0.0308  -0.0323 80  GLN A N   
618  C CA  . GLN A 88  ? 0.6042 0.7882 0.5847 -0.0700 0.0330  -0.0399 80  GLN A CA  
619  C C   . GLN A 88  ? 0.6627 0.8209 0.6267 -0.0593 0.0424  -0.0412 80  GLN A C   
620  O O   . GLN A 88  ? 0.6067 0.7536 0.5522 -0.0629 0.0436  -0.0472 80  GLN A O   
621  C CB  . GLN A 88  ? 0.5739 0.7390 0.5438 -0.0817 0.0342  -0.0425 80  GLN A CB  
622  C CG  . GLN A 88  ? 0.6851 0.8252 0.6303 -0.0947 0.0370  -0.0530 80  GLN A CG  
623  C CD  . GLN A 88  ? 0.6770 0.8375 0.6242 -0.1088 0.0274  -0.0620 80  GLN A CD  
624  O OE1 . GLN A 88  ? 0.6089 0.8010 0.5737 -0.1078 0.0190  -0.0592 80  GLN A OE1 
625  N NE2 . GLN A 88  ? 0.6687 0.8117 0.5985 -0.1213 0.0287  -0.0741 80  GLN A NE2 
626  N N   . LEU A 89  ? 0.6973 0.8465 0.6677 -0.0452 0.0488  -0.0365 81  LEU A N   
627  C CA  . LEU A 89  ? 0.6648 0.7903 0.6223 -0.0344 0.0582  -0.0381 81  LEU A CA  
628  C C   . LEU A 89  ? 0.6457 0.7849 0.6114 -0.0268 0.0609  -0.0380 81  LEU A C   
629  O O   . LEU A 89  ? 0.7842 0.9047 0.7308 -0.0253 0.0668  -0.0417 81  LEU A O   
630  C CB  . LEU A 89  ? 0.7047 0.8203 0.6693 -0.0197 0.0633  -0.0345 81  LEU A CB  
631  C CG  . LEU A 89  ? 0.7790 0.8673 0.7303 -0.0083 0.0733  -0.0370 81  LEU A CG  
632  C CD1 . LEU A 89  ? 0.7572 0.8096 0.6760 -0.0178 0.0778  -0.0412 81  LEU A CD1 
633  C CD2 . LEU A 89  ? 0.8675 0.9557 0.8328 0.0094  0.0758  -0.0345 81  LEU A CD2 
634  N N   . VAL A 90  ? 0.5883 0.7586 0.5817 -0.0218 0.0579  -0.0339 82  VAL A N   
635  C CA  . VAL A 90  ? 0.6536 0.8349 0.6560 -0.0137 0.0636  -0.0331 82  VAL A CA  
636  C C   . VAL A 90  ? 0.6945 0.8724 0.6744 -0.0219 0.0609  -0.0359 82  VAL A C   
637  O O   . VAL A 90  ? 0.6460 0.8115 0.6127 -0.0154 0.0689  -0.0370 82  VAL A O   
638  C CB  . VAL A 90  ? 0.6252 0.8414 0.6637 -0.0084 0.0614  -0.0290 82  VAL A CB  
639  C CG1 . VAL A 90  ? 0.6319 0.8589 0.6770 -0.0033 0.0680  -0.0277 82  VAL A CG1 
640  C CG2 . VAL A 90  ? 0.7172 0.9372 0.7788 0.0045  0.0655  -0.0290 82  VAL A CG2 
641  N N   . GLU A 91  ? 0.6798 0.8689 0.6549 -0.0353 0.0498  -0.0377 83  GLU A N   
642  C CA  . GLU A 91  ? 0.6435 0.8370 0.6014 -0.0408 0.0445  -0.0416 83  GLU A CA  
643  C C   . GLU A 91  ? 0.5547 0.7214 0.4801 -0.0477 0.0441  -0.0505 83  GLU A C   
644  O O   . GLU A 91  ? 0.5628 0.7241 0.4680 -0.0447 0.0445  -0.0542 83  GLU A O   
645  C CB  . GLU A 91  ? 0.7431 0.9659 0.7151 -0.0512 0.0319  -0.0414 83  GLU A CB  
646  C CG  . GLU A 91  ? 0.6877 0.9398 0.6921 -0.0446 0.0320  -0.0334 83  GLU A CG  
647  C CD  . GLU A 91  ? 0.7182 0.9754 0.7242 -0.0323 0.0399  -0.0296 83  GLU A CD  
648  O OE1 . GLU A 91  ? 0.8286 1.0689 0.8074 -0.0292 0.0431  -0.0327 83  GLU A OE1 
649  O OE2 . GLU A 91  ? 0.6584 0.9356 0.6924 -0.0254 0.0440  -0.0240 83  GLU A OE2 
650  N N   . THR A 92  ? 0.6561 0.8047 0.5749 -0.0557 0.0445  -0.0542 84  THR A N   
651  C CA  . THR A 92  ? 0.6111 0.7354 0.5021 -0.0641 0.0446  -0.0644 84  THR A CA  
652  C C   . THR A 92  ? 0.5971 0.6884 0.4717 -0.0561 0.0565  -0.0649 84  THR A C   
653  O O   . THR A 92  ? 0.6474 0.7181 0.4976 -0.0609 0.0580  -0.0737 84  THR A O   
654  C CB  . THR A 92  ? 0.6878 0.8090 0.5796 -0.0805 0.0395  -0.0705 84  THR A CB  
655  O OG1 . THR A 92  ? 0.7259 0.8243 0.6179 -0.0783 0.0481  -0.0665 84  THR A OG1 
656  C CG2 . THR A 92  ? 0.6195 0.7728 0.5339 -0.0878 0.0294  -0.0681 84  THR A CG2 
657  N N   . VAL A 93  ? 0.5380 0.8595 0.2945 -0.0853 0.0099  -0.0622 85  VAL A N   
658  C CA  . VAL A 93  ? 0.6198 0.8989 0.3612 -0.0925 0.0239  -0.0534 85  VAL A CA  
659  C C   . VAL A 93  ? 0.7377 0.9789 0.4996 -0.0763 0.0392  -0.0423 85  VAL A C   
660  O O   . VAL A 93  ? 0.6952 0.9034 0.4343 -0.0732 0.0515  -0.0320 85  VAL A O   
661  C CB  . VAL A 93  ? 0.6147 0.8976 0.3662 -0.1106 0.0209  -0.0599 85  VAL A CB  
662  C CG1 . VAL A 93  ? 0.6485 0.8863 0.3931 -0.1165 0.0358  -0.0509 85  VAL A CG1 
663  C CG2 . VAL A 93  ? 0.6123 0.9309 0.3395 -0.1285 0.0062  -0.0698 85  VAL A CG2 
664  N N   . ILE A 94  ? 0.5938 0.8396 0.3980 -0.0672 0.0389  -0.0448 86  ILE A N   
665  C CA  . ILE A 94  ? 0.7025 0.9110 0.5293 -0.0541 0.0536  -0.0345 86  ILE A CA  
666  C C   . ILE A 94  ? 0.6965 0.8928 0.5154 -0.0369 0.0581  -0.0247 86  ILE A C   
667  O O   . ILE A 94  ? 0.6698 0.8297 0.4707 -0.0342 0.0722  -0.0135 86  ILE A O   
668  C CB  . ILE A 94  ? 0.7026 0.9207 0.5761 -0.0495 0.0509  -0.0398 86  ILE A CB  
669  C CG1 . ILE A 94  ? 0.8279 1.0471 0.7085 -0.0687 0.0483  -0.0447 86  ILE A CG1 
670  C CG2 . ILE A 94  ? 0.7040 0.8878 0.6021 -0.0324 0.0644  -0.0287 86  ILE A CG2 
671  C CD1 . ILE A 94  ? 0.8296 1.0659 0.7511 -0.0696 0.0422  -0.0516 86  ILE A CD1 
672  N N   . LYS A 95  ? 0.7079 0.9347 0.5417 -0.0261 0.0459  -0.0288 87  LYS A N   
673  C CA  . LYS A 95  ? 0.6997 0.9155 0.5313 -0.0099 0.0474  -0.0177 87  LYS A CA  
674  C C   . LYS A 95  ? 0.7257 0.9237 0.5078 -0.0169 0.0516  -0.0081 87  LYS A C   
675  O O   . LYS A 95  ? 0.7218 0.8851 0.4929 -0.0110 0.0640  0.0050  87  LYS A O   
676  C CB  . LYS A 95  ? 0.6249 0.8802 0.4819 0.0009  0.0313  -0.0250 87  LYS A CB  
677  C CG  . LYS A 95  ? 0.5685 0.8318 0.4775 0.0130  0.0309  -0.0311 87  LYS A CG  
678  C CD  . LYS A 95  ? 0.5747 0.8736 0.5123 0.0256  0.0168  -0.0382 87  LYS A CD  
679  C CE  . LYS A 95  ? 0.6652 0.9657 0.6543 0.0394  0.0186  -0.0428 87  LYS A CE  
680  N NZ  . LYS A 95  ? 0.8282 1.1672 0.8518 0.0501  0.0054  -0.0542 87  LYS A NZ  
681  N N   . PRO A 96  ? 0.7988 1.0175 0.5482 -0.0306 0.0428  -0.0138 88  PRO A N   
682  C CA  . PRO A 96  ? 0.7620 0.9605 0.4620 -0.0391 0.0484  -0.0047 88  PRO A CA  
683  C C   . PRO A 96  ? 0.7399 0.8939 0.4240 -0.0462 0.0693  0.0009  88  PRO A C   
684  O O   . PRO A 96  ? 0.8467 0.9721 0.5045 -0.0456 0.0802  0.0119  88  PRO A O   
685  C CB  . PRO A 96  ? 0.7663 0.9969 0.4401 -0.0543 0.0351  -0.0146 88  PRO A CB  
686  C CG  . PRO A 96  ? 0.6964 0.9704 0.4069 -0.0488 0.0195  -0.0267 88  PRO A CG  
687  C CD  . PRO A 96  ? 0.6897 0.9527 0.4448 -0.0393 0.0270  -0.0288 88  PRO A CD  
688  N N   . ALA A 97  ? 0.8260 0.9736 0.5275 -0.0536 0.0751  -0.0064 89  ALA A N   
689  C CA  . ALA A 97  ? 0.7805 0.8864 0.4736 -0.0603 0.0951  -0.0022 89  ALA A CA  
690  C C   . ALA A 97  ? 0.7428 0.8160 0.4506 -0.0462 0.1101  0.0091  89  ALA A C   
691  O O   . ALA A 97  ? 0.7751 0.8162 0.4562 -0.0496 0.1260  0.0162  89  ALA A O   
692  C CB  . ALA A 97  ? 0.7216 0.8278 0.4416 -0.0690 0.0957  -0.0101 89  ALA A CB  
693  N N   . LEU A 98  ? 0.7166 0.7981 0.4662 -0.0311 0.1055  0.0102  90  LEU A N   
694  C CA  . LEU A 98  ? 0.7282 0.7813 0.4928 -0.0169 0.1176  0.0217  90  LEU A CA  
695  C C   . LEU A 98  ? 0.7450 0.7917 0.4751 -0.0141 0.1174  0.0324  90  LEU A C   
696  O O   . LEU A 98  ? 0.7684 0.7812 0.4853 -0.0126 0.1333  0.0425  90  LEU A O   
697  C CB  . LEU A 98  ? 0.7545 0.8236 0.5682 -0.0012 0.1091  0.0204  90  LEU A CB  
698  C CG  . LEU A 98  ? 0.7237 0.7990 0.5740 -0.0046 0.1083  0.0115  90  LEU A CG  
699  C CD1 . LEU A 98  ? 0.7124 0.8090 0.6061 0.0095  0.0981  0.0083  90  LEU A CD1 
700  C CD2 . LEU A 98  ? 0.7066 0.7408 0.5662 -0.0074 0.1280  0.0170  90  LEU A CD2 
701  N N   . ALA A 99  ? 0.7845 0.8639 0.4996 -0.0146 0.0990  0.0306  91  ALA A N   
702  C CA  . ALA A 99  ? 0.7169 0.7929 0.4032 -0.0121 0.0947  0.0428  91  ALA A CA  
703  C C   . ALA A 99  ? 0.7755 0.8239 0.4087 -0.0282 0.1087  0.0476  91  ALA A C   
704  O O   . ALA A 99  ? 0.8038 0.8311 0.4140 -0.0278 0.1149  0.0606  91  ALA A O   
705  C CB  . ALA A 99  ? 0.7083 0.8272 0.3949 -0.0099 0.0708  0.0391  91  ALA A CB  
706  N N   . ARG A 100 ? 0.7720 0.8196 0.3854 -0.0435 0.1140  0.0374  92  ARG A N   
707  C CA  . ARG A 100 ? 0.7895 0.8098 0.3549 -0.0597 0.1295  0.0394  92  ARG A CA  
708  C C   . ARG A 100 ? 0.8686 0.8455 0.4402 -0.0602 0.1557  0.0422  92  ARG A C   
709  O O   . ARG A 100 ? 0.9171 0.8682 0.4510 -0.0737 0.1721  0.0428  92  ARG A O   
710  C CB  . ARG A 100 ? 0.8389 0.8722 0.3841 -0.0761 0.1262  0.0269  92  ARG A CB  
711  C CG  . ARG A 100 ? 0.8907 0.9658 0.4233 -0.0792 0.1024  0.0229  92  ARG A CG  
712  C CD  . ARG A 100 ? 0.9567 1.0364 0.4562 -0.0984 0.1025  0.0135  92  ARG A CD  
713  N NE  . ARG A 100 ? 0.9570 1.0335 0.4832 -0.1031 0.1077  0.0030  92  ARG A NE  
714  C CZ  . ARG A 100 ? 0.9022 1.0110 0.4549 -0.1029 0.0922  -0.0058 92  ARG A CZ  
715  N NH1 . ARG A 100 ? 0.8149 0.9623 0.3742 -0.0970 0.0723  -0.0075 92  ARG A NH1 
716  N NH2 . ARG A 100 ? 0.9708 1.0734 0.5448 -0.1100 0.0966  -0.0130 92  ARG A NH2 
717  N N   . GLY A 101 ? 0.8962 0.8652 0.5149 -0.0468 0.1606  0.0430  93  GLY A N   
718  C CA  . GLY A 101 ? 0.8409 0.7711 0.4729 -0.0468 0.1850  0.0445  93  GLY A CA  
719  C C   . GLY A 101 ? 0.8739 0.7972 0.5314 -0.0530 0.1925  0.0337  93  GLY A C   
720  O O   . GLY A 101 ? 0.8643 0.7542 0.5325 -0.0553 0.2141  0.0336  93  GLY A O   
721  N N   . GLN A 102 ? 0.8489 0.8029 0.5180 -0.0565 0.1752  0.0248  94  GLN A N   
722  C CA  . GLN A 102 ? 0.8638 0.8139 0.5577 -0.0645 0.1782  0.0161  94  GLN A CA  
723  C C   . GLN A 102 ? 0.7860 0.7432 0.5340 -0.0524 0.1723  0.0167  94  GLN A C   
724  O O   . GLN A 102 ? 0.7747 0.7627 0.5382 -0.0436 0.1546  0.0159  94  GLN A O   
725  C CB  . GLN A 102 ? 0.8451 0.8246 0.5191 -0.0783 0.1620  0.0067  94  GLN A CB  
726  C CG  . GLN A 102 ? 0.9747 0.9406 0.6022 -0.0948 0.1712  0.0033  94  GLN A CG  
727  C CD  . GLN A 102 ? 0.9806 0.9780 0.5882 -0.1077 0.1531  -0.0051 94  GLN A CD  
728  O OE1 . GLN A 102 ? 0.8538 0.8871 0.4752 -0.1037 0.1328  -0.0078 94  GLN A OE1 
729  N NE2 . GLN A 102 ? 1.0700 1.0544 0.6461 -0.1239 0.1610  -0.0102 94  GLN A NE2 
730  N N   . TRP A 103 ? 0.8352 0.7640 0.6131 -0.0526 0.1874  0.0175  95  TRP A N   
731  C CA  . TRP A 103 ? 0.8229 0.7590 0.6510 -0.0461 0.1803  0.0170  95  TRP A CA  
732  C C   . TRP A 103 ? 0.7443 0.7136 0.5767 -0.0577 0.1603  0.0080  95  TRP A C   
733  O O   . TRP A 103 ? 0.7438 0.7240 0.5442 -0.0711 0.1552  0.0023  95  TRP A O   
734  C CB  . TRP A 103 ? 0.8867 0.7851 0.7455 -0.0466 0.1998  0.0202  95  TRP A CB  
735  C CG  . TRP A 103 ? 0.9187 0.7878 0.7814 -0.0341 0.2183  0.0291  95  TRP A CG  
736  C CD1 . TRP A 103 ? 0.9354 0.7911 0.7596 -0.0331 0.2296  0.0333  95  TRP A CD1 
737  C CD2 . TRP A 103 ? 0.9543 0.8039 0.8607 -0.0224 0.2272  0.0356  95  TRP A CD2 
738  N NE1 . TRP A 103 ? 0.9670 0.7968 0.8077 -0.0219 0.2449  0.0419  95  TRP A NE1 
739  C CE2 . TRP A 103 ? 0.9864 0.8117 0.8780 -0.0145 0.2441  0.0433  95  TRP A CE2 
740  C CE3 . TRP A 103 ? 0.8940 0.7441 0.8494 -0.0193 0.2220  0.0363  95  TRP A CE3 
741  C CZ2 . TRP A 103 ? 0.9774 0.7797 0.9026 -0.0026 0.2563  0.0511  95  TRP A CZ2 
742  C CZ3 . TRP A 103 ? 0.8840 0.7109 0.8731 -0.0071 0.2339  0.0443  95  TRP A CZ3 
743  C CH2 . TRP A 103 ? 0.9255 0.7288 0.8997 0.0016  0.2511  0.0513  95  TRP A CH2 
744  N N   . VAL A 104 ? 0.7489 0.7349 0.6202 -0.0536 0.1488  0.0066  96  VAL A N   
745  C CA  . VAL A 104 ? 0.7400 0.7595 0.6177 -0.0661 0.1294  -0.0019 96  VAL A CA  
746  C C   . VAL A 104 ? 0.6283 0.6414 0.5525 -0.0685 0.1274  -0.0004 96  VAL A C   
747  O O   . VAL A 104 ? 0.6254 0.6383 0.5797 -0.0557 0.1275  0.0029  96  VAL A O   
748  C CB  . VAL A 104 ? 0.7145 0.7766 0.5845 -0.0605 0.1113  -0.0078 96  VAL A CB  
749  C CG1 . VAL A 104 ? 0.7096 0.8066 0.5823 -0.0762 0.0929  -0.0178 96  VAL A CG1 
750  C CG2 . VAL A 104 ? 0.7108 0.7776 0.5381 -0.0570 0.1121  -0.0065 96  VAL A CG2 
751  N N   . ILE A 105 ? 0.6763 0.6847 0.6072 -0.0856 0.1241  -0.0023 97  ILE A N   
752  C CA  . ILE A 105 ? 0.7034 0.7053 0.6776 -0.0920 0.1197  0.0007  97  ILE A CA  
753  C C   . ILE A 105 ? 0.6001 0.6406 0.5733 -0.1087 0.0967  -0.0066 97  ILE A C   
754  O O   . ILE A 105 ? 0.6779 0.7291 0.6253 -0.1238 0.0897  -0.0112 97  ILE A O   
755  C CB  . ILE A 105 ? 0.7958 0.7597 0.7848 -0.1004 0.1330  0.0060  97  ILE A CB  
756  C CG1 . ILE A 105 ? 0.7593 0.6884 0.7326 -0.0896 0.1575  0.0093  97  ILE A CG1 
757  C CG2 . ILE A 105 ? 0.7031 0.6539 0.7432 -0.1021 0.1309  0.0128  97  ILE A CG2 
758  C CD1 . ILE A 105 ? 0.7715 0.6863 0.7619 -0.0699 0.1688  0.0158  97  ILE A CD1 
759  N N   . GLY A 106 ? 0.7183 0.7796 0.7185 -0.1081 0.0851  -0.0083 98  GLY A N   
760  C CA  . GLY A 106 ? 0.8039 0.9064 0.8005 -0.1242 0.0641  -0.0171 98  GLY A CA  
761  C C   . GLY A 106 ? 0.7976 0.9004 0.8300 -0.1388 0.0540  -0.0134 98  GLY A C   
762  O O   . GLY A 106 ? 0.7890 0.8679 0.8554 -0.1314 0.0612  -0.0054 98  GLY A O   
763  N N   . ASP A 107 ? 1.0095 1.1417 1.0323 -0.1612 0.0358  -0.0193 99  ASP A N   
764  C CA  . ASP A 107 ? 0.9632 1.1019 1.0147 -0.1803 0.0220  -0.0159 99  ASP A CA  
765  C C   . ASP A 107 ? 1.0274 1.2099 1.0797 -0.1865 0.0080  -0.0273 99  ASP A C   
766  O O   . ASP A 107 ? 1.0232 1.2413 1.0475 -0.1952 -0.0017 -0.0388 99  ASP A O   
767  C CB  . ASP A 107 ? 0.9112 1.0490 0.9544 -0.2056 0.0102  -0.0125 99  ASP A CB  
768  C CG  . ASP A 107 ? 0.8964 0.9892 0.9504 -0.2030 0.0233  -0.0017 99  ASP A CG  
769  O OD1 . ASP A 107 ? 0.9636 1.0243 1.0436 -0.1867 0.0389  0.0058  99  ASP A OD1 
770  O OD2 . ASP A 107 ? 0.8353 0.9256 0.8733 -0.2178 0.0183  -0.0014 99  ASP A OD2 
771  N N   . ARG A 108 ? 1.0195 1.1998 1.1052 -0.1836 0.0073  -0.0249 100 ARG A N   
772  C CA  . ARG A 108 ? 1.0414 1.2604 1.1344 -0.1951 -0.0059 -0.0358 100 ARG A CA  
773  C C   . ARG A 108 ? 1.1394 1.3887 1.2199 -0.1785 -0.0026 -0.0511 100 ARG A C   
774  O O   . ARG A 108 ? 1.3746 1.6658 1.4421 -0.1914 -0.0140 -0.0655 100 ARG A O   
775  C CB  . ARG A 108 ? 1.0694 1.3163 1.1477 -0.2276 -0.0255 -0.0396 100 ARG A CB  
776  C CG  . ARG A 108 ? 1.0252 1.2452 1.1161 -0.2470 -0.0326 -0.0241 100 ARG A CG  
777  C CD  . ARG A 108 ? 1.0863 1.3177 1.1457 -0.2587 -0.0475 -0.0258 100 ARG A CD  
778  N NE  . ARG A 108 ? 1.1390 1.3363 1.2082 -0.2628 -0.0528 -0.0108 100 ARG A NE  
779  C CZ  . ARG A 108 ? 1.1900 1.3691 1.2544 -0.2679 -0.0487 -0.0051 100 ARG A CZ  
780  N NH1 . ARG A 108 ? 1.1097 1.2999 1.1551 -0.2719 -0.0386 -0.0124 100 ARG A NH1 
781  N NH2 . ARG A 108 ? 1.2563 1.4061 1.3362 -0.2687 -0.0539 0.0068  100 ARG A NH2 
782  N N   . HIS A 109 ? 1.1769 1.4063 1.2634 -0.1508 0.0124  -0.0481 101 HIS A N   
783  C CA  . HIS A 109 ? 1.2519 1.5072 1.3359 -0.1336 0.0146  -0.0607 101 HIS A CA  
784  C C   . HIS A 109 ? 1.3830 1.6520 1.5003 -0.1323 0.0120  -0.0671 101 HIS A C   
785  O O   . HIS A 109 ? 1.3448 1.5933 1.4856 -0.1120 0.0221  -0.0620 101 HIS A O   
786  C CB  . HIS A 109 ? 1.1798 1.4085 1.2581 -0.1061 0.0298  -0.0535 101 HIS A CB  
787  C CG  . HIS A 109 ? 1.3139 1.5698 1.3861 -0.0899 0.0292  -0.0647 101 HIS A CG  
788  N ND1 . HIS A 109 ? 1.4088 1.6912 1.4500 -0.0931 0.0231  -0.0731 101 HIS A ND1 
789  C CD2 . HIS A 109 ? 1.3392 1.5990 1.4352 -0.0703 0.0333  -0.0680 101 HIS A CD2 
790  C CE1 . HIS A 109 ? 1.4289 1.7308 1.4770 -0.0762 0.0231  -0.0809 101 HIS A CE1 
791  N NE2 . HIS A 109 ? 1.4046 1.6931 1.4863 -0.0621 0.0291  -0.0782 101 HIS A NE2 
792  N N   . THR A 126 ? 1.0912 1.6077 1.4244 -0.1446 0.0165  -0.2606 118 THR A N   
793  C CA  . THR A 126 ? 1.1978 1.7342 1.5728 -0.1194 0.0226  -0.2782 118 THR A CA  
794  C C   . THR A 126 ? 1.0846 1.6471 1.4462 -0.1126 0.0208  -0.2880 118 THR A C   
795  O O   . THR A 126 ? 1.0605 1.6327 1.4502 -0.0888 0.0219  -0.2893 118 THR A O   
796  C CB  . THR A 126 ? 1.1426 1.6882 1.5370 -0.1185 0.0293  -0.3009 118 THR A CB  
797  O OG1 . THR A 126 ? 1.1066 1.6285 1.5087 -0.1274 0.0303  -0.2915 118 THR A OG1 
798  C CG2 . THR A 126 ? 1.2338 1.7904 1.6751 -0.0888 0.0341  -0.3137 118 THR A CG2 
799  N N   . MET A 127 ? 1.0472 1.6186 1.3648 -0.1322 0.0187  -0.2927 119 MET A N   
800  C CA  . MET A 127 ? 1.0768 1.6724 1.3779 -0.1284 0.0173  -0.3017 119 MET A CA  
801  C C   . MET A 127 ? 1.0131 1.6019 1.3002 -0.1245 0.0104  -0.2820 119 MET A C   
802  O O   . MET A 127 ? 0.8859 1.4939 1.1780 -0.1111 0.0084  -0.2866 119 MET A O   
803  C CB  . MET A 127 ? 1.2108 1.8158 1.4712 -0.1489 0.0205  -0.3096 119 MET A CB  
804  C CG  . MET A 127 ? 1.3808 1.9967 1.6529 -0.1548 0.0294  -0.3314 119 MET A CG  
805  S SD  . MET A 127 ? 1.3296 1.9171 1.6018 -0.1691 0.0300  -0.3199 119 MET A SD  
806  C CE  . MET A 127 ? 1.1995 1.8112 1.4930 -0.1697 0.0424  -0.3541 119 MET A CE  
807  N N   . LEU A 128 ? 0.9810 1.5424 1.2516 -0.1362 0.0065  -0.2598 120 LEU A N   
808  C CA  . LEU A 128 ? 0.9248 1.4785 1.1872 -0.1325 0.0015  -0.2422 120 LEU A CA  
809  C C   . LEU A 128 ? 0.9341 1.4862 1.2367 -0.1031 0.0062  -0.2381 120 LEU A C   
810  O O   . LEU A 128 ? 0.9442 1.4877 1.2305 -0.0876 0.0055  -0.2280 120 LEU A O   
811  C CB  . LEU A 128 ? 0.9937 1.5134 1.2370 -0.1497 -0.0024 -0.2196 120 LEU A CB  
812  C CG  . LEU A 128 ? 1.0040 1.5106 1.1996 -0.1717 -0.0065 -0.2121 120 LEU A CG  
813  C CD1 . LEU A 128 ? 1.1060 1.5767 1.2942 -0.1856 -0.0118 -0.1899 120 LEU A CD1 
814  C CD2 . LEU A 128 ? 0.9945 1.5093 1.1565 -0.1738 -0.0095 -0.2086 120 LEU A CD2 
815  N N   . ALA A 129 ? 0.9307 1.4647 1.2676 -0.0892 0.0128  -0.2369 121 ALA A N   
816  C CA  . ALA A 129 ? 0.9304 1.4328 1.2871 -0.0548 0.0192  -0.2224 121 ALA A CA  
817  C C   . ALA A 129 ? 0.9226 1.4514 1.2957 -0.0349 0.0190  -0.2369 121 ALA A C   
818  O O   . ALA A 129 ? 1.0146 1.5237 1.3837 -0.0121 0.0197  -0.2219 121 ALA A O   
819  C CB  . ALA A 129 ? 1.0514 1.5311 1.4427 -0.0464 0.0254  -0.2192 121 ALA A CB  
820  N N   . THR A 130 ? 0.9349 1.5087 1.3281 -0.0442 0.0181  -0.2661 122 THR A N   
821  C CA  . THR A 130 ? 0.9576 1.5592 1.3727 -0.0261 0.0172  -0.2812 122 THR A CA  
822  C C   . THR A 130 ? 0.8848 1.4963 1.2649 -0.0273 0.0105  -0.2747 122 THR A C   
823  O O   . THR A 130 ? 0.8720 1.4796 1.2594 -0.0045 0.0086  -0.2678 122 THR A O   
824  C CB  . THR A 130 ? 1.0261 1.6497 1.4487 -0.0378 0.0186  -0.3089 122 THR A CB  
825  O OG1 . THR A 130 ? 1.1827 1.7891 1.6181 -0.0456 0.0239  -0.3122 122 THR A OG1 
826  C CG2 . THR A 130 ? 1.3296 1.9636 1.7843 -0.0137 0.0186  -0.3202 122 THR A CG2 
827  N N   . LEU A 131 ? 0.8505 1.4745 1.1923 -0.0547 0.0059  -0.2758 123 LEU A N   
828  C CA  . LEU A 131 ? 0.8135 1.4457 1.1195 -0.0576 -0.0006 -0.2692 123 LEU A CA  
829  C C   . LEU A 131 ? 0.8729 1.4588 1.1595 -0.0380 0.0003  -0.2388 123 LEU A C   
830  O O   . LEU A 131 ? 0.8226 1.4102 1.1005 -0.0236 -0.0030 -0.2330 123 LEU A O   
831  C CB  . LEU A 131 ? 0.8792 1.5192 1.1424 -0.0902 -0.0052 -0.2708 123 LEU A CB  
832  C CG  . LEU A 131 ? 0.9035 1.5507 1.1482 -0.1053 -0.0009 -0.2881 123 LEU A CG  
833  C CD1 . LEU A 131 ? 0.8747 1.5007 1.0713 -0.1298 -0.0006 -0.2743 123 LEU A CD1 
834  C CD2 . LEU A 131 ? 1.0119 1.6882 1.2562 -0.0977 -0.0014 -0.3037 123 LEU A CD2 
835  N N   . ARG A 132 ? 0.8770 1.4212 1.1569 -0.0385 0.0049  -0.2192 124 ARG A N   
836  C CA  . ARG A 132 ? 0.8678 1.3675 1.1283 -0.0225 0.0080  -0.1918 124 ARG A CA  
837  C C   . ARG A 132 ? 0.8538 1.3433 1.1392 0.0081  0.0102  -0.1862 124 ARG A C   
838  O O   . ARG A 132 ? 0.8385 1.3195 1.1045 0.0192  0.0078  -0.1746 124 ARG A O   
839  C CB  . ARG A 132 ? 0.9033 1.3617 1.1622 -0.0272 0.0139  -0.1742 124 ARG A CB  
840  C CG  . ARG A 132 ? 0.9780 1.3911 1.2137 -0.0149 0.0189  -0.1478 124 ARG A CG  
841  C CD  . ARG A 132 ? 0.9721 1.3444 1.2116 -0.0186 0.0256  -0.1310 124 ARG A CD  
842  N NE  . ARG A 132 ? 1.1835 1.5151 1.3998 -0.0095 0.0320  -0.1086 124 ARG A NE  
843  C CZ  . ARG A 132 ? 1.1861 1.5020 1.3728 -0.0250 0.0320  -0.0988 124 ARG A CZ  
844  N NH1 . ARG A 132 ? 1.2995 1.6349 1.4756 -0.0507 0.0244  -0.1067 124 ARG A NH1 
845  N NH2 . ARG A 132 ? 0.9766 1.2563 1.1445 -0.0154 0.0400  -0.0810 124 ARG A NH2 
846  N N   . ASP A 133 ? 0.8243 1.3151 1.1529 0.0208  0.0139  -0.1944 125 ASP A N   
847  C CA  . ASP A 133 ? 0.7859 1.2655 1.1424 0.0495  0.0146  -0.1876 125 ASP A CA  
848  C C   . ASP A 133 ? 0.7869 1.3002 1.1473 0.0567  0.0065  -0.1983 125 ASP A C   
849  O O   . ASP A 133 ? 0.8500 1.3517 1.2232 0.0786  0.0039  -0.1871 125 ASP A O   
850  C CB  . ASP A 133 ? 0.8716 1.3517 1.2772 0.0596  0.0192  -0.1981 125 ASP A CB  
851  C CG  . ASP A 133 ? 1.0170 1.4638 1.4221 0.0529  0.0264  -0.1868 125 ASP A CG  
852  O OD1 . ASP A 133 ? 1.0287 1.4357 1.4100 0.0566  0.0301  -0.1625 125 ASP A OD1 
853  O OD2 . ASP A 133 ? 1.0407 1.5014 1.4699 0.0428  0.0286  -0.2027 125 ASP A OD2 
854  N N   . ALA A 134 ? 0.8730 1.4281 1.2237 0.0379  0.0017  -0.2190 126 ALA A N   
855  C CA  . ALA A 134 ? 0.8380 1.4279 1.1932 0.0428  -0.0064 -0.2302 126 ALA A CA  
856  C C   . ALA A 134 ? 0.8190 1.3995 1.1251 0.0381  -0.0118 -0.2133 126 ALA A C   
857  O O   . ALA A 134 ? 0.7855 1.3605 1.0907 0.0544  -0.0172 -0.2019 126 ALA A O   
858  C CB  . ALA A 134 ? 0.7969 1.4389 1.1668 0.0238  -0.0079 -0.2625 126 ALA A CB  
859  N N   . VAL A 135 ? 0.8364 1.4140 1.1016 0.0149  -0.0112 -0.2111 127 VAL A N   
860  C CA  . VAL A 135 ? 0.7800 1.3561 0.9988 0.0066  -0.0166 -0.2004 127 VAL A CA  
861  C C   . VAL A 135 ? 0.8519 1.3773 1.0436 0.0171  -0.0122 -0.1712 127 VAL A C   
862  O O   . VAL A 135 ? 0.8927 1.4110 1.0613 0.0242  -0.0164 -0.1591 127 VAL A O   
863  C CB  . VAL A 135 ? 0.7688 1.3651 0.9579 -0.0235 -0.0187 -0.2110 127 VAL A CB  
864  C CG1 . VAL A 135 ? 0.7099 1.3584 0.9246 -0.0358 -0.0219 -0.2415 127 VAL A CG1 
865  C CG2 . VAL A 135 ? 0.9948 1.5584 1.1735 -0.0353 -0.0123 -0.2003 127 VAL A CG2 
866  N N   . LEU A 136 ? 0.8635 1.3531 1.0571 0.0171  -0.0034 -0.1598 128 LEU A N   
867  C CA  . LEU A 136 ? 0.8881 1.3292 1.0590 0.0262  0.0032  -0.1340 128 LEU A CA  
868  C C   . LEU A 136 ? 0.8432 1.2612 1.0426 0.0521  0.0066  -0.1224 128 LEU A C   
869  O O   . LEU A 136 ? 0.9169 1.2999 1.0960 0.0612  0.0108  -0.1015 128 LEU A O   
870  C CB  . LEU A 136 ? 0.9277 1.3397 1.0878 0.0129  0.0111  -0.1260 128 LEU A CB  
871  C CG  . LEU A 136 ? 0.8786 1.3026 1.0066 -0.0139 0.0073  -0.1311 128 LEU A CG  
872  C CD1 . LEU A 136 ? 0.9766 1.3657 1.1007 -0.0240 0.0145  -0.1192 128 LEU A CD1 
873  C CD2 . LEU A 136 ? 0.8165 1.2423 0.9025 -0.0184 0.0032  -0.1248 128 LEU A CD2 
874  N N   . GLY A 137 ? 0.8311 1.2681 1.0769 0.0630  0.0050  -0.1357 129 GLY A N   
875  C CA  . GLY A 137 ? 0.8160 1.2296 1.0916 0.0867  0.0075  -0.1240 129 GLY A CA  
876  C C   . GLY A 137 ? 0.9073 1.2746 1.1780 0.0893  0.0189  -0.1062 129 GLY A C   
877  O O   . GLY A 137 ? 0.9298 1.2918 1.2021 0.0763  0.0243  -0.1109 129 GLY A O   
878  N N   . ASP A 138 ? 0.8819 1.2153 1.1461 0.1048  0.0221  -0.0848 130 ASP A N   
879  C CA  . ASP A 138 ? 0.8539 1.1424 1.1165 0.1092  0.0339  -0.0675 130 ASP A CA  
880  C C   . ASP A 138 ? 0.8213 1.0837 1.0390 0.0943  0.0417  -0.0558 130 ASP A C   
881  O O   . ASP A 138 ? 0.8077 1.0329 1.0244 0.0962  0.0527  -0.0422 130 ASP A O   
882  C CB  . ASP A 138 ? 0.9344 1.1975 1.2099 0.1309  0.0348  -0.0497 130 ASP A CB  
883  C CG  . ASP A 138 ? 1.0445 1.3078 1.2890 0.1339  0.0281  -0.0384 130 ASP A CG  
884  O OD1 . ASP A 138 ? 1.0421 1.3279 1.2582 0.1208  0.0225  -0.0459 130 ASP A OD1 
885  O OD2 . ASP A 138 ? 1.0629 1.3038 1.3107 0.1481  0.0277  -0.0212 130 ASP A OD2 
886  N N   . PHE A 139 ? 0.8323 1.1131 1.0155 0.0795  0.0366  -0.0611 131 PHE A N   
887  C CA  . PHE A 139 ? 0.8258 1.0812 0.9678 0.0659  0.0438  -0.0503 131 PHE A CA  
888  C C   . PHE A 139 ? 0.8575 1.1017 1.0079 0.0523  0.0500  -0.0531 131 PHE A C   
889  O O   . PHE A 139 ? 0.9403 1.2138 1.1020 0.0392  0.0435  -0.0690 131 PHE A O   
890  C CB  . PHE A 139 ? 0.7885 1.0690 0.8940 0.0522  0.0356  -0.0568 131 PHE A CB  
891  C CG  . PHE A 139 ? 0.7553 1.0130 0.8211 0.0362  0.0425  -0.0489 131 PHE A CG  
892  C CD1 . PHE A 139 ? 0.6683 0.8963 0.7013 0.0393  0.0495  -0.0331 131 PHE A CD1 
893  C CD2 . PHE A 139 ? 0.8093 1.0746 0.8716 0.0171  0.0418  -0.0571 131 PHE A CD2 
894  C CE1 . PHE A 139 ? 0.6804 0.8870 0.6801 0.0247  0.0571  -0.0277 131 PHE A CE1 
895  C CE2 . PHE A 139 ? 0.7459 0.9894 0.7767 0.0028  0.0475  -0.0499 131 PHE A CE2 
896  C CZ  . PHE A 139 ? 0.6512 0.8653 0.6518 0.0072  0.0559  -0.0361 131 PHE A CZ  
897  N N   . ARG A 140 ? 0.8136 1.0158 0.9581 0.0537  0.0623  -0.0375 132 ARG A N   
898  C CA  . ARG A 140 ? 0.7548 0.9408 0.9098 0.0415  0.0679  -0.0364 132 ARG A CA  
899  C C   . ARG A 140 ? 0.6907 0.8402 0.8168 0.0348  0.0790  -0.0222 132 ARG A C   
900  O O   . ARG A 140 ? 0.8188 0.9493 0.9219 0.0430  0.0854  -0.0119 132 ARG A O   
901  C CB  . ARG A 140 ? 0.7689 0.9386 0.9653 0.0538  0.0733  -0.0326 132 ARG A CB  
902  C CG  . ARG A 140 ? 0.8986 1.1002 1.1285 0.0631  0.0647  -0.0469 132 ARG A CG  
903  C CD  . ARG A 140 ? 0.9598 1.1963 1.2005 0.0445  0.0561  -0.0657 132 ARG A CD  
904  N NE  . ARG A 140 ? 0.9403 1.2091 1.2139 0.0517  0.0498  -0.0826 132 ARG A NE  
905  C CZ  . ARG A 140 ? 0.9751 1.2841 1.2473 0.0500  0.0407  -0.0991 132 ARG A CZ  
906  N NH1 . ARG A 140 ? 0.9838 1.3064 1.2215 0.0421  0.0358  -0.0999 132 ARG A NH1 
907  N NH2 . ARG A 140 ? 0.9444 1.2810 1.2524 0.0560  0.0370  -0.1161 132 ARG A NH2 
908  N N   . PRO A 141 ? 0.6835 0.8227 0.8112 0.0186  0.0811  -0.0217 133 PRO A N   
909  C CA  . PRO A 141 ? 0.7375 0.8377 0.8482 0.0141  0.0940  -0.0088 133 PRO A CA  
910  C C   . PRO A 141 ? 0.6548 0.7172 0.7833 0.0312  0.1086  0.0050  133 PRO A C   
911  O O   . PRO A 141 ? 0.6607 0.7231 0.8223 0.0425  0.1081  0.0055  133 PRO A O   
912  C CB  . PRO A 141 ? 0.7112 0.8113 0.8334 -0.0058 0.0903  -0.0112 133 PRO A CB  
913  C CG  . PRO A 141 ? 0.7001 0.8457 0.8265 -0.0167 0.0737  -0.0271 133 PRO A CG  
914  C CD  . PRO A 141 ? 0.7001 0.8637 0.8442 0.0016  0.0712  -0.0332 133 PRO A CD  
915  N N   . HIS A 142 ? 0.6984 0.7291 0.8039 0.0322  0.1221  0.0155  134 HIS A N   
916  C CA  . HIS A 142 ? 0.7320 0.7253 0.8513 0.0460  0.1378  0.0287  134 HIS A CA  
917  C C   . HIS A 142 ? 0.6246 0.5938 0.7762 0.0416  0.1455  0.0335  134 HIS A C   
918  O O   . HIS A 142 ? 0.6009 0.5514 0.7812 0.0539  0.1524  0.0409  134 HIS A O   
919  C CB  . HIS A 142 ? 0.7323 0.7009 0.8143 0.0460  0.1509  0.0366  134 HIS A CB  
920  C CG  . HIS A 142 ? 0.7077 0.6959 0.7602 0.0515  0.1430  0.0356  134 HIS A CG  
921  N ND1 . HIS A 142 ? 0.7237 0.7450 0.7529 0.0418  0.1292  0.0254  134 HIS A ND1 
922  C CD2 . HIS A 142 ? 0.8901 0.8705 0.9351 0.0652  0.1453  0.0444  134 HIS A CD2 
923  C CE1 . HIS A 142 ? 0.9079 0.9404 0.9173 0.0497  0.1235  0.0280  134 HIS A CE1 
924  N NE2 . HIS A 142 ? 1.0271 1.0349 1.0455 0.0636  0.1324  0.0400  134 HIS A NE2 
925  N N   . LEU A 143 ? 0.7696 0.7088 0.5582 0.0554  -0.1788 -0.1493 135 LEU A N   
926  C CA  . LEU A 143 ? 0.7861 0.7121 0.5838 0.0501  -0.1702 -0.1439 135 LEU A CA  
927  C C   . LEU A 143 ? 0.7612 0.7113 0.5740 0.0537  -0.1621 -0.1508 135 LEU A C   
928  O O   . LEU A 143 ? 0.7652 0.7402 0.5831 0.0498  -0.1542 -0.1573 135 LEU A O   
929  C CB  . LEU A 143 ? 0.7683 0.6837 0.5661 0.0322  -0.1555 -0.1368 135 LEU A CB  
930  C CG  . LEU A 143 ? 0.7313 0.6325 0.5372 0.0276  -0.1475 -0.1308 135 LEU A CG  
931  C CD1 . LEU A 143 ? 0.7937 0.6699 0.5923 0.0343  -0.1615 -0.1248 135 LEU A CD1 
932  C CD2 . LEU A 143 ? 0.7991 0.6956 0.6065 0.0112  -0.1321 -0.1261 135 LEU A CD2 
933  N N   . THR A 144 ? 0.7871 0.7305 0.6067 0.0606  -0.1643 -0.1494 136 THR A N   
934  C CA  . THR A 144 ? 0.7849 0.7495 0.6186 0.0631  -0.1559 -0.1536 136 THR A CA  
935  C C   . THR A 144 ? 0.7011 0.6514 0.5419 0.0552  -0.1444 -0.1460 136 THR A C   
936  O O   . THR A 144 ? 0.7947 0.7246 0.6332 0.0589  -0.1511 -0.1414 136 THR A O   
937  C CB  . THR A 144 ? 0.7998 0.7767 0.6360 0.0815  -0.1698 -0.1608 136 THR A CB  
938  O OG1 . THR A 144 ? 0.8436 0.8300 0.6710 0.0909  -0.1829 -0.1677 136 THR A OG1 
939  C CG2 . THR A 144 ? 0.8371 0.8428 0.6872 0.0828  -0.1602 -0.1653 136 THR A CG2 
940  N N   . LEU A 145 ? 0.7248 0.6857 0.5741 0.0446  -0.1278 -0.1451 137 LEU A N   
941  C CA  . LEU A 145 ? 0.7645 0.7141 0.6207 0.0372  -0.1155 -0.1382 137 LEU A CA  
942  C C   . LEU A 145 ? 0.7414 0.7084 0.6094 0.0441  -0.1114 -0.1399 137 LEU A C   
943  O O   . LEU A 145 ? 0.6900 0.6774 0.5642 0.0409  -0.1031 -0.1431 137 LEU A O   
944  C CB  . LEU A 145 ? 0.7604 0.7079 0.6172 0.0216  -0.1002 -0.1361 137 LEU A CB  
945  C CG  . LEU A 145 ? 0.8279 0.7569 0.6864 0.0128  -0.0900 -0.1289 137 LEU A CG  
946  C CD1 . LEU A 145 ? 0.8883 0.8115 0.7528 0.0202  -0.0913 -0.1247 137 LEU A CD1 
947  C CD2 . LEU A 145 ? 0.7635 0.6755 0.6104 0.0065  -0.0947 -0.1256 137 LEU A CD2 
948  N N   . TYR A 146 ? 0.8012 0.7610 0.6720 0.0529  -0.1174 -0.1377 138 TYR A N   
949  C CA  . TYR A 146 ? 0.8529 0.8306 0.7345 0.0605  -0.1144 -0.1389 138 TYR A CA  
950  C C   . TYR A 146 ? 0.8057 0.7760 0.6941 0.0530  -0.0996 -0.1313 138 TYR A C   
951  O O   . TYR A 146 ? 0.8492 0.7997 0.7355 0.0506  -0.0995 -0.1263 138 TYR A O   
952  C CB  . TYR A 146 ? 0.9144 0.8921 0.7961 0.0759  -0.1296 -0.1425 138 TYR A CB  
953  C CG  . TYR A 146 ? 0.9178 0.9131 0.8107 0.0829  -0.1252 -0.1425 138 TYR A CG  
954  C CD1 . TYR A 146 ? 0.8771 0.9019 0.7770 0.0847  -0.1195 -0.1458 138 TYR A CD1 
955  C CD2 . TYR A 146 ? 0.9860 0.9704 0.8823 0.0869  -0.1266 -0.1391 138 TYR A CD2 
956  C CE1 . TYR A 146 ? 0.8187 0.8614 0.7281 0.0908  -0.1154 -0.1447 138 TYR A CE1 
957  C CE2 . TYR A 146 ? 0.9612 0.9640 0.8675 0.0938  -0.1227 -0.1390 138 TYR A CE2 
958  C CZ  . TYR A 146 ? 0.8820 0.9137 0.7945 0.0960  -0.1171 -0.1414 138 TYR A CZ  
959  O OH  . TYR A 146 ? 0.8704 0.9220 0.7920 0.1026  -0.1132 -0.1403 138 TYR A OH  
960  N N   . LEU A 147 ? 0.7656 0.7522 0.6617 0.0492  -0.0876 -0.1303 139 LEU A N   
961  C CA  . LEU A 147 ? 0.8223 0.8030 0.7250 0.0439  -0.0737 -0.1230 139 LEU A CA  
962  C C   . LEU A 147 ? 0.8383 0.8323 0.7484 0.0555  -0.0762 -0.1220 139 LEU A C   
963  O O   . LEU A 147 ? 0.9136 0.9314 0.8290 0.0599  -0.0754 -0.1242 139 LEU A O   
964  C CB  . LEU A 147 ? 0.9584 0.9457 0.8643 0.0328  -0.0595 -0.1217 139 LEU A CB  
965  C CG  . LEU A 147 ? 0.7835 0.7600 0.6830 0.0208  -0.0558 -0.1239 139 LEU A CG  
966  C CD1 . LEU A 147 ? 0.8693 0.8518 0.7736 0.0100  -0.0415 -0.1231 139 LEU A CD1 
967  C CD2 . LEU A 147 ? 0.8854 0.8376 0.7798 0.0163  -0.0547 -0.1201 139 LEU A CD2 
968  N N   . ASP A 148 ? 0.8620 0.8432 0.7725 0.0600  -0.0795 -0.1189 140 ASP A N   
969  C CA  . ASP A 148 ? 0.8939 0.8880 0.8117 0.0711  -0.0819 -0.1184 140 ASP A CA  
970  C C   . ASP A 148 ? 0.8548 0.8540 0.7796 0.0676  -0.0666 -0.1108 140 ASP A C   
971  O O   . ASP A 148 ? 0.7773 0.7600 0.7009 0.0586  -0.0562 -0.1054 140 ASP A O   
972  C CB  . ASP A 148 ? 0.8791 0.8578 0.7947 0.0763  -0.0915 -0.1188 140 ASP A CB  
973  C CG  . ASP A 148 ? 0.8780 0.8717 0.8012 0.0883  -0.0951 -0.1199 140 ASP A CG  
974  O OD1 . ASP A 148 ? 0.9472 0.9630 0.8739 0.0979  -0.1013 -0.1255 140 ASP A OD1 
975  O OD2 . ASP A 148 ? 0.9602 0.9457 0.8860 0.0884  -0.0920 -0.1159 140 ASP A OD2 
976  N N   . VAL A 149 ? 0.8809 0.9034 0.8124 0.0752  -0.0654 -0.1104 141 VAL A N   
977  C CA  . VAL A 149 ? 0.9036 0.9315 0.8413 0.0747  -0.0527 -0.1021 141 VAL A CA  
978  C C   . VAL A 149 ? 0.9533 1.0005 0.8970 0.0884  -0.0587 -0.1030 141 VAL A C   
979  O O   . VAL A 149 ? 0.9978 1.0645 0.9428 0.0971  -0.0694 -0.1103 141 VAL A O   
980  C CB  . VAL A 149 ? 0.9265 0.9657 0.8662 0.0668  -0.0417 -0.0984 141 VAL A CB  
981  C CG1 . VAL A 149 ? 0.9800 0.9968 0.9153 0.0528  -0.0324 -0.0962 141 VAL A CG1 
982  C CG2 . VAL A 149 ? 0.9880 1.0526 0.9280 0.0699  -0.0493 -0.1057 141 VAL A CG2 
983  N N   . THR A 150 ? 1.0260 1.0692 0.9733 0.0910  -0.0523 -0.0965 142 THR A N   
984  C CA  . THR A 150 ? 1.0303 1.0920 0.9836 0.1037  -0.0570 -0.0972 142 THR A CA  
985  C C   . THR A 150 ? 1.0011 1.0910 0.9597 0.1077  -0.0511 -0.0931 142 THR A C   
986  O O   . THR A 150 ? 0.9979 1.0880 0.9557 0.0990  -0.0408 -0.0872 142 THR A O   
987  C CB  . THR A 150 ? 1.0550 1.1038 1.0099 0.1047  -0.0516 -0.0917 142 THR A CB  
988  O OG1 . THR A 150 ? 1.0621 1.1053 1.0178 0.0987  -0.0365 -0.0817 142 THR A OG1 
989  C CG2 . THR A 150 ? 0.9639 0.9868 0.9132 0.0986  -0.0566 -0.0949 142 THR A CG2 
990  N N   . PRO A 151 ? 1.0549 1.1693 1.0188 0.1204  -0.0574 -0.0960 143 PRO A N   
991  C CA  . PRO A 151 ? 1.0336 1.1788 1.0023 0.1242  -0.0521 -0.0915 143 PRO A CA  
992  C C   . PRO A 151 ? 1.0133 1.1530 0.9827 0.1182  -0.0362 -0.0774 143 PRO A C   
993  O O   . PRO A 151 ? 1.0075 1.1615 0.9775 0.1134  -0.0288 -0.0714 143 PRO A O   
994  C CB  . PRO A 151 ? 1.0056 1.1754 0.9800 0.1397  -0.0620 -0.0978 143 PRO A CB  
995  C CG  . PRO A 151 ? 1.0949 1.2480 1.0668 0.1434  -0.0757 -0.1087 143 PRO A CG  
996  C CD  . PRO A 151 ? 1.0650 1.1815 1.0309 0.1312  -0.0703 -0.1043 143 PRO A CD  
997  N N   . GLU A 152 ? 0.9747 1.0947 0.9439 0.1185  -0.0310 -0.0720 144 GLU A N   
998  C CA  . GLU A 152 ? 1.0007 1.1111 0.9696 0.1137  -0.0164 -0.0589 144 GLU A CA  
999  C C   . GLU A 152 ? 1.0832 1.1753 1.0475 0.0989  -0.0084 -0.0558 144 GLU A C   
1000 O O   . GLU A 152 ? 1.1190 1.2163 1.0834 0.0936  0.0009  -0.0471 144 GLU A O   
1001 C CB  . GLU A 152 ? 1.0166 1.1083 0.9855 0.1168  -0.0131 -0.0557 144 GLU A CB  
1002 C CG  . GLU A 152 ? 1.0430 1.1451 1.0150 0.1245  -0.0046 -0.0447 144 GLU A CG  
1003 C CD  . GLU A 152 ? 1.2660 1.3446 1.2346 0.1174  0.0092  -0.0335 144 GLU A CD  
1004 O OE1 . GLU A 152 ? 1.3713 1.4230 1.3364 0.1092  0.0117  -0.0358 144 GLU A OE1 
1005 O OE2 . GLU A 152 ? 1.2979 1.3849 1.2671 0.1202  0.0171  -0.0222 144 GLU A OE2 
1006 N N   . VAL A 153 ? 1.0834 1.1547 1.0436 0.0916  -0.0122 -0.0629 145 VAL A N   
1007 C CA  . VAL A 153 ? 1.1016 1.1555 1.0577 0.0775  -0.0046 -0.0613 145 VAL A CA  
1008 C C   . VAL A 153 ? 1.1536 1.2292 1.1104 0.0728  -0.0042 -0.0620 145 VAL A C   
1009 O O   . VAL A 153 ? 1.2161 1.2869 1.1722 0.0628  0.0062  -0.0551 145 VAL A O   
1010 C CB  . VAL A 153 ? 1.1150 1.1479 1.0663 0.0716  -0.0103 -0.0697 145 VAL A CB  
1011 C CG1 . VAL A 153 ? 1.1052 1.1273 1.0528 0.0577  -0.0045 -0.0708 145 VAL A CG1 
1012 C CG2 . VAL A 153 ? 1.1579 1.1692 1.1081 0.0728  -0.0074 -0.0674 145 VAL A CG2 
1013 N N   . GLY A 154 ? 1.1083 1.2087 1.0668 0.0799  -0.0157 -0.0706 146 GLY A N   
1014 C CA  . GLY A 154 ? 1.1097 1.2367 1.0694 0.0763  -0.0158 -0.0722 146 GLY A CA  
1015 C C   . GLY A 154 ? 1.2305 1.3743 1.1933 0.0756  -0.0059 -0.0604 146 GLY A C   
1016 O O   . GLY A 154 ? 1.3031 1.4564 1.2654 0.0651  0.0008  -0.0566 146 GLY A O   
1017 N N   . LEU A 155 ? 1.1969 1.3454 1.1627 0.0862  -0.0048 -0.0542 147 LEU A N   
1018 C CA  . LEU A 155 ? 1.1308 1.2957 1.0986 0.0868  0.0042  -0.0415 147 LEU A CA  
1019 C C   . LEU A 155 ? 1.1671 1.3035 1.1315 0.0745  0.0184  -0.0291 147 LEU A C   
1020 O O   . LEU A 155 ? 1.2368 1.3831 1.2008 0.0676  0.0265  -0.0191 147 LEU A O   
1021 C CB  . LEU A 155 ? 1.2433 1.4213 1.2149 0.1024  0.0010  -0.0387 147 LEU A CB  
1022 C CG  . LEU A 155 ? 1.2471 1.4618 1.2234 0.1157  -0.0116 -0.0489 147 LEU A CG  
1023 C CD1 . LEU A 155 ? 1.1079 1.3312 1.0879 0.1302  -0.0141 -0.0470 147 LEU A CD1 
1024 C CD2 . LEU A 155 ? 0.9870 1.2387 0.9649 0.1135  -0.0104 -0.0469 147 LEU A CD2 
1025 N N   . LYS A 156 ? 1.1347 1.2362 1.0964 0.0714  0.0214  -0.0297 148 LYS A N   
1026 C CA  . LYS A 156 ? 1.2973 1.3697 1.2557 0.0603  0.0340  -0.0202 148 LYS A CA  
1027 C C   . LYS A 156 ? 1.3762 1.4473 1.3326 0.0439  0.0378  -0.0222 148 LYS A C   
1028 O O   . LYS A 156 ? 1.4617 1.5250 1.4166 0.0341  0.0480  -0.0121 148 LYS A O   
1029 C CB  . LYS A 156 ? 1.3145 1.3539 1.2707 0.0607  0.0351  -0.0233 148 LYS A CB  
1030 C CG  . LYS A 156 ? 1.3270 1.3657 1.2851 0.0751  0.0332  -0.0207 148 LYS A CG  
1031 C CD  . LYS A 156 ? 1.3730 1.3901 1.3295 0.0754  0.0295  -0.0290 148 LYS A CD  
1032 C CE  . LYS A 156 ? 1.2853 1.2890 1.2421 0.0836  0.0345  -0.0232 148 LYS A CE  
1033 N NZ  . LYS A 156 ? 1.0911 1.0880 1.0478 0.0871  0.0276  -0.0322 148 LYS A NZ  
1034 N N   . ARG A 157 ? 1.2591 1.3376 1.2151 0.0407  0.0295  -0.0351 149 ARG A N   
1035 C CA  . ARG A 157 ? 1.3265 1.4059 1.2807 0.0253  0.0326  -0.0390 149 ARG A CA  
1036 C C   . ARG A 157 ? 1.4373 1.5514 1.3937 0.0215  0.0336  -0.0355 149 ARG A C   
1037 O O   . ARG A 157 ? 1.5812 1.6944 1.5364 0.0063  0.0411  -0.0325 149 ARG A O   
1038 C CB  . ARG A 157 ? 1.3310 1.4100 1.2835 0.0248  0.0226  -0.0537 149 ARG A CB  
1039 C CG  . ARG A 157 ? 1.4367 1.4866 1.3868 0.0287  0.0202  -0.0573 149 ARG A CG  
1040 C CD  . ARG A 157 ? 1.4415 1.4582 1.3892 0.0184  0.0319  -0.0518 149 ARG A CD  
1041 N NE  . ARG A 157 ? 1.4204 1.4139 1.3655 0.0205  0.0293  -0.0571 149 ARG A NE  
1042 C CZ  . ARG A 157 ? 1.4218 1.4050 1.3674 0.0304  0.0289  -0.0537 149 ARG A CZ  
1043 N NH1 . ARG A 157 ? 1.6261 1.6192 1.5749 0.0402  0.0307  -0.0453 149 ARG A NH1 
1044 N NH2 . ARG A 157 ? 1.3587 1.3234 1.3016 0.0301  0.0266  -0.0589 149 ARG A NH2 
1045 N N   . ALA A 158 ? 1.4917 1.6381 1.4514 0.0346  0.0262  -0.0364 150 ALA A N   
1046 C CA  . ALA A 158 ? 1.5330 1.7176 1.4950 0.0317  0.0270  -0.0335 150 ALA A CA  
1047 C C   . ALA A 158 ? 1.4687 1.6471 1.4295 0.0226  0.0403  -0.0161 150 ALA A C   
1048 O O   . ALA A 158 ? 1.3295 1.5237 1.2897 0.0093  0.0457  -0.0121 150 ALA A O   
1049 C CB  . ALA A 158 ? 1.3195 1.5397 1.2855 0.0494  0.0162  -0.0387 150 ALA A CB  
1050 N N   . ARG A 159 ? 1.3682 1.5237 1.3279 0.0294  0.0454  -0.0055 151 ARG A N   
1051 C CA  . ARG A 159 ? 1.3406 1.4852 1.2979 0.0221  0.0576  0.0122  151 ARG A CA  
1052 C C   . ARG A 159 ? 1.3421 1.4601 1.2960 0.0016  0.0667  0.0147  151 ARG A C   
1053 O O   . ARG A 159 ? 1.4804 1.6056 1.4327 -0.0111 0.0743  0.0250  151 ARG A O   
1054 C CB  . ARG A 159 ? 1.3040 1.4240 1.2603 0.0341  0.0607  0.0211  151 ARG A CB  
1055 C CG  . ARG A 159 ? 1.2686 1.4177 1.2284 0.0531  0.0537  0.0216  151 ARG A CG  
1056 C CD  . ARG A 159 ? 1.2777 1.4028 1.2370 0.0656  0.0551  0.0260  151 ARG A CD  
1057 N NE  . ARG A 159 ? 1.3368 1.4360 1.2918 0.0617  0.0667  0.0426  151 ARG A NE  
1058 C CZ  . ARG A 159 ? 1.3734 1.4503 1.3271 0.0718  0.0697  0.0484  151 ARG A CZ  
1059 N NH1 . ARG A 159 ? 1.3794 1.4577 1.3360 0.0848  0.0627  0.0391  151 ARG A NH1 
1060 N NH2 . ARG A 159 ? 1.3850 1.4377 1.3341 0.0687  0.0798  0.0636  151 ARG A NH2 
1061 N N   . ALA A 160 ? 1.4527 1.5406 1.4053 -0.0026 0.0660  0.0052  152 ALA A N   
1062 C CA  . ALA A 160 ? 1.4667 1.5293 1.4165 -0.0217 0.0738  0.0048  152 ALA A CA  
1063 C C   . ALA A 160 ? 1.4866 1.5796 1.4377 -0.0349 0.0721  -0.0022 152 ALA A C   
1064 O O   . ALA A 160 ? 1.5598 1.6522 1.5110 -0.0409 0.0680  -0.0157 152 ALA A O   
1065 C CB  . ALA A 160 ? 1.7624 1.7926 1.7109 -0.0215 0.0722  -0.0057 152 ALA A CB  
1066 N N   . ASP A 173 ? 1.1053 1.5166 1.1030 0.1843  -0.0878 -0.1283 165 ASP A N   
1067 C CA  . ASP A 173 ? 1.2132 1.5830 1.2045 0.1745  -0.0888 -0.1300 165 ASP A CA  
1068 C C   . ASP A 173 ? 1.2019 1.5736 1.1915 0.1832  -0.1056 -0.1480 165 ASP A C   
1069 O O   . ASP A 173 ? 1.2251 1.5713 1.2132 0.1899  -0.1161 -0.1556 165 ASP A O   
1070 C CB  . ASP A 173 ? 1.1246 1.4515 1.1138 0.1719  -0.0857 -0.1238 165 ASP A CB  
1071 C CG  . ASP A 173 ? 1.1133 1.4193 1.1000 0.1576  -0.0681 -0.1061 165 ASP A CG  
1072 O OD1 . ASP A 173 ? 1.0455 1.3672 1.0319 0.1488  -0.0583 -0.0978 165 ASP A OD1 
1073 O OD2 . ASP A 173 ? 1.0487 1.3222 1.0336 0.1550  -0.0644 -0.1009 165 ASP A OD2 
1074 N N   . PHE A 174 ? 1.3166 1.7185 1.3062 0.1829  -0.1084 -0.1545 166 PHE A N   
1075 C CA  . PHE A 174 ? 1.3224 1.7220 1.3088 0.1897  -0.1232 -0.1702 166 PHE A CA  
1076 C C   . PHE A 174 ? 1.3645 1.7145 1.3433 0.1801  -0.1234 -0.1680 166 PHE A C   
1077 O O   . PHE A 174 ? 1.2911 1.6270 1.2659 0.1874  -0.1373 -0.1796 166 PHE A O   
1078 C CB  . PHE A 174 ? 1.3365 1.7734 1.3230 0.1863  -0.1225 -0.1749 166 PHE A CB  
1079 C CG  . PHE A 174 ? 1.4263 1.8410 1.4066 0.1685  -0.1140 -0.1690 166 PHE A CG  
1080 C CD1 . PHE A 174 ? 1.4890 1.8914 1.4686 0.1505  -0.0962 -0.1525 166 PHE A CD1 
1081 C CD2 . PHE A 174 ? 1.3981 1.8029 1.3731 0.1704  -0.1243 -0.1801 166 PHE A CD2 
1082 C CE1 . PHE A 174 ? 1.5531 1.9352 1.5275 0.1341  -0.0887 -0.1484 166 PHE A CE1 
1083 C CE2 . PHE A 174 ? 1.4358 1.8225 1.4055 0.1541  -0.1165 -0.1754 166 PHE A CE2 
1084 C CZ  . PHE A 174 ? 1.5276 1.9032 1.4974 0.1357  -0.0986 -0.1601 166 PHE A CZ  
1085 N N   . PHE A 175 ? 1.2592 1.5834 1.2355 0.1639  -0.1082 -0.1533 167 PHE A N   
1086 C CA  . PHE A 175 ? 1.1367 1.4182 1.1058 0.1526  -0.1060 -0.1502 167 PHE A CA  
1087 C C   . PHE A 175 ? 1.1167 1.3656 1.0831 0.1596  -0.1162 -0.1545 167 PHE A C   
1088 O O   . PHE A 175 ? 1.1690 1.3893 1.1286 0.1553  -0.1213 -0.1573 167 PHE A O   
1089 C CB  . PHE A 175 ? 1.1580 1.4247 1.1266 0.1356  -0.0870 -0.1341 167 PHE A CB  
1090 C CG  . PHE A 175 ? 1.1517 1.3747 1.1167 0.1288  -0.0818 -0.1267 167 PHE A CG  
1091 C CD1 . PHE A 175 ? 1.1602 1.3710 1.1274 0.1368  -0.0846 -0.1251 167 PHE A CD1 
1092 C CD2 . PHE A 175 ? 1.2170 1.4138 1.1768 0.1136  -0.0733 -0.1215 167 PHE A CD2 
1093 C CE1 . PHE A 175 ? 1.2056 1.3802 1.1696 0.1299  -0.0794 -0.1188 167 PHE A CE1 
1094 C CE2 . PHE A 175 ? 1.2015 1.3618 1.1581 0.1074  -0.0682 -0.1153 167 PHE A CE2 
1095 C CZ  . PHE A 175 ? 1.1349 1.2848 1.0936 0.1155  -0.0712 -0.1138 167 PHE A CZ  
1096 N N   . ASN A 176 ? 1.1630 1.4167 1.1344 0.1700  -0.1197 -0.1552 168 ASN A N   
1097 C CA  . ASN A 176 ? 1.0970 1.3206 1.0661 0.1752  -0.1296 -0.1596 168 ASN A CA  
1098 C C   . ASN A 176 ? 1.0286 1.2492 0.9940 0.1859  -0.1483 -0.1745 168 ASN A C   
1099 O O   . ASN A 176 ? 0.9373 1.1241 0.8971 0.1854  -0.1564 -0.1769 168 ASN A O   
1100 C CB  . ASN A 176 ? 1.0569 1.2913 1.0330 0.1843  -0.1296 -0.1587 168 ASN A CB  
1101 C CG  . ASN A 176 ? 1.0809 1.3035 1.0584 0.1743  -0.1133 -0.1435 168 ASN A CG  
1102 O OD1 . ASN A 176 ? 1.0699 1.2609 1.0422 0.1620  -0.1060 -0.1360 168 ASN A OD1 
1103 N ND2 . ASN A 176 ? 1.1668 1.4156 1.1509 0.1804  -0.1077 -0.1391 168 ASN A ND2 
1104 N N   . ARG A 177 ? 1.0981 1.3536 1.0659 0.1960  -0.1557 -0.1847 169 ARG A N   
1105 C CA  . ARG A 177 ? 1.1365 1.3890 1.1002 0.2080  -0.1743 -0.1995 169 ARG A CA  
1106 C C   . ARG A 177 ? 1.0534 1.2832 1.0078 0.1984  -0.1748 -0.1982 169 ARG A C   
1107 O O   . ARG A 177 ? 1.0405 1.2404 0.9877 0.2015  -0.1867 -0.2030 169 ARG A O   
1108 C CB  . ARG A 177 ? 1.0934 1.3938 1.0629 0.2231  -0.1824 -0.2120 169 ARG A CB  
1109 C CG  . ARG A 177 ? 1.1681 1.4666 1.1344 0.2401  -0.2038 -0.2293 169 ARG A CG  
1110 C CD  . ARG A 177 ? 1.3081 1.6588 1.2811 0.2560  -0.2112 -0.2427 169 ARG A CD  
1111 N NE  . ARG A 177 ? 1.4077 1.7791 1.3896 0.2657  -0.2121 -0.2456 169 ARG A NE  
1112 C CZ  . ARG A 177 ? 1.4831 1.8613 1.4680 0.2844  -0.2289 -0.2612 169 ARG A CZ  
1113 N NH1 . ARG A 177 ? 1.4953 1.8585 1.4751 0.2956  -0.2448 -0.2744 169 ARG A NH1 
1114 N NH2 . ARG A 177 ? 1.4902 1.8883 1.4835 0.2916  -0.2280 -0.2630 169 ARG A NH2 
1115 N N   . THR A 178 ? 1.0760 1.3194 1.0300 0.1861  -0.1619 -0.1915 170 THR A N   
1116 C CA  . THR A 178 ? 1.1037 1.3275 1.0492 0.1760  -0.1611 -0.1904 170 THR A CA  
1117 C C   . THR A 178 ? 1.0650 1.2420 1.0045 0.1651  -0.1572 -0.1813 170 THR A C   
1118 O O   . THR A 178 ? 1.0244 1.1756 0.9554 0.1648  -0.1662 -0.1842 170 THR A O   
1119 C CB  . THR A 178 ? 1.1889 1.4353 1.1362 0.1627  -0.1464 -0.1845 170 THR A CB  
1120 O OG1 . THR A 178 ? 1.2460 1.4866 1.1975 0.1509  -0.1295 -0.1707 170 THR A OG1 
1121 C CG2 . THR A 178 ? 1.0633 1.3594 1.0159 0.1721  -0.1507 -0.1940 170 THR A CG2 
1122 N N   . ARG A 179 ? 1.0572 1.2245 1.0007 0.1566  -0.1439 -0.1700 171 ARG A N   
1123 C CA  . ARG A 179 ? 1.0186 1.1460 0.9574 0.1472  -0.1402 -0.1621 171 ARG A CA  
1124 C C   . ARG A 179 ? 1.0050 1.1097 0.9393 0.1564  -0.1567 -0.1689 171 ARG A C   
1125 O O   . ARG A 179 ? 1.0665 1.1391 0.9926 0.1493  -0.1595 -0.1662 171 ARG A O   
1126 C CB  . ARG A 179 ? 1.0643 1.1911 1.0093 0.1422  -0.1264 -0.1516 171 ARG A CB  
1127 C CG  . ARG A 179 ? 1.0666 1.1578 1.0080 0.1339  -0.1226 -0.1446 171 ARG A CG  
1128 C CD  . ARG A 179 ? 1.1046 1.1973 1.0515 0.1281  -0.1070 -0.1337 171 ARG A CD  
1129 N NE  . ARG A 179 ? 0.9980 1.0593 0.9411 0.1193  -0.1022 -0.1274 171 ARG A NE  
1130 C CZ  . ARG A 179 ? 0.9786 1.0321 0.9244 0.1227  -0.1033 -0.1258 171 ARG A CZ  
1131 N NH1 . ARG A 179 ? 1.0434 1.1169 0.9959 0.1349  -0.1086 -0.1298 171 ARG A NH1 
1132 N NH2 . ARG A 179 ? 0.9868 1.0141 0.9287 0.1136  -0.0990 -0.1207 171 ARG A NH2 
1133 N N   . ALA A 180 ? 1.0334 1.1543 0.9727 0.1718  -0.1678 -0.1778 172 ALA A N   
1134 C CA  . ALA A 180 ? 1.0322 1.1296 0.9674 0.1804  -0.1844 -0.1850 172 ALA A CA  
1135 C C   . ALA A 180 ? 1.0695 1.1525 0.9947 0.1837  -0.1977 -0.1916 172 ALA A C   
1136 O O   . ALA A 180 ? 1.1229 1.1706 1.0397 0.1805  -0.2055 -0.1901 172 ALA A O   
1137 C CB  . ALA A 180 ? 0.9475 1.0685 0.8908 0.1973  -0.1942 -0.1953 172 ALA A CB  
1138 N N   . ARG A 181 ? 1.0425 1.1534 0.9680 0.1899  -0.2004 -0.1986 173 ARG A N   
1139 C CA  . ARG A 181 ? 1.0706 1.1711 0.9863 0.1951  -0.2136 -0.2056 173 ARG A CA  
1140 C C   . ARG A 181 ? 1.0992 1.1686 1.0053 0.1788  -0.2070 -0.1955 173 ARG A C   
1141 O O   . ARG A 181 ? 1.1291 1.1680 1.0252 0.1798  -0.2184 -0.1961 173 ARG A O   
1142 C CB  . ARG A 181 ? 1.0797 1.2214 0.9982 0.2031  -0.2153 -0.2146 173 ARG A CB  
1143 C CG  . ARG A 181 ? 1.0590 1.1969 0.9686 0.2151  -0.2329 -0.2255 173 ARG A CG  
1144 C CD  . ARG A 181 ? 1.0820 1.2632 0.9941 0.2196  -0.2318 -0.2333 173 ARG A CD  
1145 N NE  . ARG A 181 ? 1.1929 1.3732 1.1011 0.2024  -0.2187 -0.2253 173 ARG A NE  
1146 C CZ  . ARG A 181 ? 1.3231 1.4953 1.2217 0.2020  -0.2250 -0.2282 173 ARG A CZ  
1147 N NH1 . ARG A 181 ? 1.2857 1.4484 1.1768 0.2185  -0.2446 -0.2380 173 ARG A NH1 
1148 N NH2 . ARG A 181 ? 1.3959 1.5694 1.2923 0.1852  -0.2117 -0.2213 173 ARG A NH2 
1149 N N   . TYR A 182 ? 1.0364 1.1127 0.9451 0.1635  -0.1888 -0.1861 174 TYR A N   
1150 C CA  . TYR A 182 ? 1.0751 1.1241 0.9757 0.1477  -0.1814 -0.1772 174 TYR A CA  
1151 C C   . TYR A 182 ? 1.0846 1.0954 0.9798 0.1437  -0.1858 -0.1716 174 TYR A C   
1152 O O   . TYR A 182 ? 1.1214 1.1062 1.0060 0.1381  -0.1910 -0.1688 174 TYR A O   
1153 C CB  . TYR A 182 ? 0.9988 1.0574 0.9049 0.1324  -0.1607 -0.1681 174 TYR A CB  
1154 C CG  . TYR A 182 ? 1.0187 1.1055 0.9265 0.1283  -0.1539 -0.1709 174 TYR A CG  
1155 C CD1 . TYR A 182 ? 1.0871 1.1806 0.9880 0.1321  -0.1633 -0.1785 174 TYR A CD1 
1156 C CD2 . TYR A 182 ? 0.9833 1.0899 0.8991 0.1201  -0.1380 -0.1655 174 TYR A CD2 
1157 C CE1 . TYR A 182 ? 0.9997 1.1216 0.9026 0.1271  -0.1567 -0.1817 174 TYR A CE1 
1158 C CE2 . TYR A 182 ? 0.9487 1.0806 0.8661 0.1141  -0.1314 -0.1677 174 TYR A CE2 
1159 C CZ  . TYR A 182 ? 1.0167 1.1574 0.9280 0.1173  -0.1406 -0.1763 174 TYR A CZ  
1160 O OH  . TYR A 182 ? 1.0706 1.2392 0.9840 0.1103  -0.1337 -0.1793 174 TYR A OH  
1161 N N   . LEU A 183 ? 1.0656 1.0746 0.9677 0.1460  -0.1838 -0.1697 175 LEU A N   
1162 C CA  . LEU A 183 ? 1.0959 1.0722 0.9940 0.1401  -0.1863 -0.1641 175 LEU A CA  
1163 C C   . LEU A 183 ? 1.0803 1.0352 0.9705 0.1500  -0.2068 -0.1709 175 LEU A C   
1164 O O   . LEU A 183 ? 1.0618 0.9845 0.9439 0.1421  -0.2108 -0.1655 175 LEU A O   
1165 C CB  . LEU A 183 ? 1.1486 1.1329 1.0569 0.1404  -0.1784 -0.1612 175 LEU A CB  
1166 C CG  . LEU A 183 ? 1.0322 1.0245 0.9459 0.1284  -0.1580 -0.1512 175 LEU A CG  
1167 C CD1 . LEU A 183 ? 1.0543 1.0598 0.9782 0.1327  -0.1522 -0.1496 175 LEU A CD1 
1168 C CD2 . LEU A 183 ? 1.0643 1.0282 0.9706 0.1127  -0.1509 -0.1423 175 LEU A CD2 
1169 N N   . GLU A 184 ? 1.1007 1.0727 0.9929 0.1671  -0.2201 -0.1828 176 GLU A N   
1170 C CA  . GLU A 184 ? 1.1463 1.0953 1.0298 0.1777  -0.2408 -0.1899 176 GLU A CA  
1171 C C   . GLU A 184 ? 1.2050 1.1359 1.0751 0.1734  -0.2459 -0.1870 176 GLU A C   
1172 O O   . GLU A 184 ? 1.2336 1.1292 1.0928 0.1696  -0.2552 -0.1828 176 GLU A O   
1173 C CB  . GLU A 184 ? 1.1929 1.1675 1.0823 0.1988  -0.2540 -0.2049 176 GLU A CB  
1174 C CG  . GLU A 184 ? 1.4196 1.3684 1.3006 0.2121  -0.2767 -0.2136 176 GLU A CG  
1175 C CD  . GLU A 184 ? 1.5914 1.5684 1.4766 0.2345  -0.2905 -0.2301 176 GLU A CD  
1176 O OE1 . GLU A 184 ? 1.5407 1.5601 1.4356 0.2388  -0.2819 -0.2344 176 GLU A OE1 
1177 O OE2 . GLU A 184 ? 1.6466 1.6035 1.5250 0.2480  -0.3103 -0.2389 176 GLU A OE2 
1178 N N   . LEU A 185 ? 1.2245 1.1805 1.0949 0.1733  -0.2397 -0.1888 177 LEU A N   
1179 C CA  . LEU A 185 ? 1.2372 1.1816 1.0955 0.1695  -0.2436 -0.1867 177 LEU A CA  
1180 C C   . LEU A 185 ? 1.1435 1.0581 0.9943 0.1503  -0.2347 -0.1733 177 LEU A C   
1181 O O   . LEU A 185 ? 1.1263 1.0169 0.9641 0.1476  -0.2429 -0.1698 177 LEU A O   
1182 C CB  . LEU A 185 ? 1.2765 1.2573 1.1387 0.1696  -0.2352 -0.1908 177 LEU A CB  
1183 C CG  . LEU A 185 ? 1.1624 1.1781 1.0310 0.1884  -0.2446 -0.2048 177 LEU A CG  
1184 C CD1 . LEU A 185 ? 1.3393 1.3936 1.2133 0.1837  -0.2325 -0.2069 177 LEU A CD1 
1185 C CD2 . LEU A 185 ? 1.0173 1.0202 0.8756 0.2053  -0.2668 -0.2139 177 LEU A CD2 
1186 N N   . ALA A 186 ? 1.1274 1.0447 0.9858 0.1372  -0.2177 -0.1656 178 ALA A N   
1187 C CA  . ALA A 186 ? 1.1594 1.0523 1.0115 0.1194  -0.2087 -0.1540 178 ALA A CA  
1188 C C   . ALA A 186 ? 1.1785 1.0364 1.0223 0.1181  -0.2205 -0.1502 178 ALA A C   
1189 O O   . ALA A 186 ? 1.2331 1.0674 1.0656 0.1075  -0.2219 -0.1425 178 ALA A O   
1190 C CB  . ALA A 186 ? 1.1906 1.0948 1.0530 0.1082  -0.1889 -0.1479 178 ALA A CB  
1191 N N   . ALA A 187 ? 1.1700 1.0250 1.0193 0.1278  -0.2292 -0.1554 179 ALA A N   
1192 C CA  . ALA A 187 ? 1.2378 1.0588 1.0797 0.1256  -0.2411 -0.1524 179 ALA A CA  
1193 C C   . ALA A 187 ? 1.2195 1.0182 1.0474 0.1339  -0.2603 -0.1550 179 ALA A C   
1194 O O   . ALA A 187 ? 1.2967 1.0627 1.1127 0.1251  -0.2668 -0.1472 179 ALA A O   
1195 C CB  . ALA A 187 ? 1.2855 1.1111 1.1377 0.1343  -0.2456 -0.1589 179 ALA A CB  
1196 N N   . GLN A 188 ? 1.1526 0.9694 0.9813 0.1509  -0.2697 -0.1657 180 GLN A N   
1197 C CA  . GLN A 188 ? 1.1967 0.9933 1.0123 0.1626  -0.2897 -0.1698 180 GLN A CA  
1198 C C   . GLN A 188 ? 1.1864 0.9788 0.9897 0.1563  -0.2883 -0.1636 180 GLN A C   
1199 O O   . GLN A 188 ? 1.3013 1.0676 1.0903 0.1613  -0.3038 -0.1620 180 GLN A O   
1200 C CB  . GLN A 188 ? 1.2306 1.0515 1.0524 0.1856  -0.3016 -0.1856 180 GLN A CB  
1201 C CG  . GLN A 188 ? 1.4080 1.2218 1.2365 0.1968  -0.3126 -0.1941 180 GLN A CG  
1202 C CD  . GLN A 188 ? 1.5425 1.3842 1.3774 0.2204  -0.3243 -0.2110 180 GLN A CD  
1203 O OE1 . GLN A 188 ? 1.4795 1.3575 1.3192 0.2258  -0.3182 -0.2161 180 GLN A OE1 
1204 N NE2 . GLN A 188 ? 1.5147 1.3404 1.3497 0.2342  -0.3415 -0.2205 180 GLN A NE2 
1205 N N   . ASP A 189 ? 1.0520 0.9062 1.1921 -0.0847 -0.0456 -0.0415 181 ASP A N   
1206 C CA  . ASP A 189 ? 0.9008 0.7768 1.0539 -0.0742 -0.0413 -0.0389 181 ASP A CA  
1207 C C   . ASP A 189 ? 0.8846 0.7901 1.0530 -0.0733 -0.0467 -0.0359 181 ASP A C   
1208 O O   . ASP A 189 ? 0.8935 0.8089 1.0640 -0.0754 -0.0536 -0.0393 181 ASP A O   
1209 C CB  . ASP A 189 ? 0.8684 0.7455 1.0201 -0.0681 -0.0396 -0.0446 181 ASP A CB  
1210 C CG  . ASP A 189 ? 0.8769 0.7739 1.0397 -0.0585 -0.0346 -0.0423 181 ASP A CG  
1211 O OD1 . ASP A 189 ? 0.9225 0.8385 1.0961 -0.0556 -0.0346 -0.0372 181 ASP A OD1 
1212 O OD2 . ASP A 189 ? 0.8325 0.7271 0.9931 -0.0540 -0.0308 -0.0452 181 ASP A OD2 
1213 N N   . PRO A 190 ? 0.8523 0.7726 1.0307 -0.0692 -0.0434 -0.0290 182 PRO A N   
1214 C CA  . PRO A 190 ? 0.8414 0.7902 1.0336 -0.0672 -0.0482 -0.0257 182 PRO A CA  
1215 C C   . PRO A 190 ? 0.7966 0.7661 0.9959 -0.0587 -0.0496 -0.0297 182 PRO A C   
1216 O O   . PRO A 190 ? 0.7912 0.7809 0.9982 -0.0568 -0.0545 -0.0288 182 PRO A O   
1217 C CB  . PRO A 190 ? 0.8492 0.8044 1.0481 -0.0647 -0.0428 -0.0168 182 PRO A CB  
1218 C CG  . PRO A 190 ? 0.9325 0.8712 1.1242 -0.0597 -0.0340 -0.0165 182 PRO A CG  
1219 C CD  . PRO A 190 ? 0.9184 0.8293 1.0949 -0.0654 -0.0346 -0.0231 182 PRO A CD  
1220 N N   . THR A 191 ? 0.8083 0.7733 1.0046 -0.0536 -0.0454 -0.0339 183 THR A N   
1221 C CA  . THR A 191 ? 0.7599 0.7418 0.9612 -0.0477 -0.0471 -0.0388 183 THR A CA  
1222 C C   . THR A 191 ? 0.7294 0.7015 0.9233 -0.0510 -0.0515 -0.0466 183 THR A C   
1223 O O   . THR A 191 ? 0.6778 0.6572 0.8727 -0.0475 -0.0519 -0.0517 183 THR A O   
1224 C CB  . THR A 191 ? 0.7258 0.7119 0.9292 -0.0414 -0.0408 -0.0389 183 THR A CB  
1225 O OG1 . THR A 191 ? 0.7033 0.6673 0.8967 -0.0438 -0.0373 -0.0422 183 THR A OG1 
1226 C CG2 . THR A 191 ? 0.7431 0.7372 0.9522 -0.0367 -0.0351 -0.0304 183 THR A CG2 
1227 N N   . ILE A 192 ? 0.7862 0.7414 0.9719 -0.0580 -0.0544 -0.0476 184 ILE A N   
1228 C CA  . ILE A 192 ? 0.7947 0.7416 0.9730 -0.0603 -0.0585 -0.0539 184 ILE A CA  
1229 C C   . ILE A 192 ? 0.7522 0.7096 0.9327 -0.0629 -0.0652 -0.0517 184 ILE A C   
1230 O O   . ILE A 192 ? 0.7770 0.7330 0.9580 -0.0687 -0.0673 -0.0467 184 ILE A O   
1231 C CB  . ILE A 192 ? 0.8925 0.8125 1.0578 -0.0653 -0.0567 -0.0570 184 ILE A CB  
1232 C CG1 . ILE A 192 ? 0.8243 0.7361 0.9878 -0.0615 -0.0494 -0.0578 184 ILE A CG1 
1233 C CG2 . ILE A 192 ? 0.8937 0.8074 1.0518 -0.0668 -0.0609 -0.0626 184 ILE A CG2 
1234 C CD1 . ILE A 192 ? 0.8802 0.7650 1.0299 -0.0647 -0.0465 -0.0601 184 ILE A CD1 
1235 N N   . ARG A 193 ? 0.6988 0.6665 0.8800 -0.0587 -0.0681 -0.0550 185 ARG A N   
1236 C CA  . ARG A 193 ? 0.7474 0.7263 0.9296 -0.0588 -0.0738 -0.0527 185 ARG A CA  
1237 C C   . ARG A 193 ? 0.7681 0.7352 0.9399 -0.0588 -0.0757 -0.0584 185 ARG A C   
1238 O O   . ARG A 193 ? 0.7167 0.6761 0.8842 -0.0554 -0.0728 -0.0644 185 ARG A O   
1239 C CB  . ARG A 193 ? 0.6988 0.7013 0.8896 -0.0510 -0.0745 -0.0501 185 ARG A CB  
1240 C CG  . ARG A 193 ? 0.6444 0.6597 0.8453 -0.0491 -0.0718 -0.0445 185 ARG A CG  
1241 C CD  . ARG A 193 ? 0.8055 0.8227 1.0107 -0.0558 -0.0733 -0.0367 185 ARG A CD  
1242 N NE  . ARG A 193 ? 0.8175 0.8418 1.0307 -0.0541 -0.0690 -0.0312 185 ARG A NE  
1243 C CZ  . ARG A 193 ? 0.8610 0.9076 1.0839 -0.0475 -0.0686 -0.0261 185 ARG A CZ  
1244 N NH1 . ARG A 193 ? 0.8926 0.9564 1.1181 -0.0418 -0.0720 -0.0257 185 ARG A NH1 
1245 N NH2 . ARG A 193 ? 0.8952 0.9467 1.1244 -0.0456 -0.0639 -0.0208 185 ARG A NH2 
1246 N N   . THR A 194 ? 0.8786 0.8452 1.0466 -0.0629 -0.0804 -0.0562 186 THR A N   
1247 C CA  . THR A 194 ? 0.8477 0.8038 1.0052 -0.0623 -0.0821 -0.0605 186 THR A CA  
1248 C C   . THR A 194 ? 0.7406 0.7136 0.8993 -0.0554 -0.0849 -0.0584 186 THR A C   
1249 O O   . THR A 194 ? 0.6750 0.6682 0.8420 -0.0542 -0.0877 -0.0517 186 THR A O   
1250 C CB  . THR A 194 ? 0.9483 0.8919 1.0983 -0.0711 -0.0854 -0.0597 186 THR A CB  
1251 O OG1 . THR A 194 ? 1.0278 0.9539 1.1748 -0.0765 -0.0820 -0.0611 186 THR A OG1 
1252 C CG2 . THR A 194 ? 0.8797 0.8112 1.0179 -0.0695 -0.0863 -0.0643 186 THR A CG2 
1253 N N   . VAL A 195 ? 0.7221 0.6862 0.8721 -0.0502 -0.0834 -0.0635 187 VAL A N   
1254 C CA  . VAL A 195 ? 0.7489 0.7237 0.8957 -0.0423 -0.0849 -0.0616 187 VAL A CA  
1255 C C   . VAL A 195 ? 0.7819 0.7426 0.9167 -0.0425 -0.0855 -0.0641 187 VAL A C   
1256 O O   . VAL A 195 ? 0.7432 0.6838 0.8701 -0.0432 -0.0819 -0.0705 187 VAL A O   
1257 C CB  . VAL A 195 ? 0.7576 0.7345 0.9037 -0.0336 -0.0811 -0.0654 187 VAL A CB  
1258 C CG1 . VAL A 195 ? 0.7810 0.7584 0.9177 -0.0247 -0.0807 -0.0654 187 VAL A CG1 
1259 C CG2 . VAL A 195 ? 0.7844 0.7813 0.9420 -0.0311 -0.0814 -0.0611 187 VAL A CG2 
1260 N N   . ASP A 196 ? 0.7882 0.7610 0.9217 -0.0416 -0.0899 -0.0585 188 ASP A N   
1261 C CA  . ASP A 196 ? 0.7790 0.7419 0.9006 -0.0397 -0.0905 -0.0597 188 ASP A CA  
1262 C C   . ASP A 196 ? 0.8155 0.7705 0.9286 -0.0287 -0.0854 -0.0634 188 ASP A C   
1263 O O   . ASP A 196 ? 0.8456 0.8147 0.9593 -0.0197 -0.0849 -0.0596 188 ASP A O   
1264 C CB  . ASP A 196 ? 0.7602 0.7430 0.8835 -0.0407 -0.0967 -0.0517 188 ASP A CB  
1265 C CG  . ASP A 196 ? 0.8404 0.8165 0.9512 -0.0370 -0.0973 -0.0520 188 ASP A CG  
1266 O OD1 . ASP A 196 ? 0.8647 0.8178 0.9652 -0.0353 -0.0929 -0.0587 188 ASP A OD1 
1267 O OD2 . ASP A 196 ? 0.9524 0.9477 1.0638 -0.0356 -0.1019 -0.0449 188 ASP A OD2 
1268 N N   . ALA A 197 ? 0.8411 0.7726 0.9453 -0.0294 -0.0810 -0.0705 189 ALA A N   
1269 C CA  . ALA A 197 ? 0.8155 0.7348 0.9105 -0.0211 -0.0754 -0.0750 189 ALA A CA  
1270 C C   . ALA A 197 ? 0.8326 0.7466 0.9151 -0.0138 -0.0744 -0.0730 189 ALA A C   
1271 O O   . ALA A 197 ? 0.8659 0.7678 0.9386 -0.0061 -0.0691 -0.0760 189 ALA A O   
1272 C CB  . ALA A 197 ? 0.8523 0.7502 0.9449 -0.0260 -0.0708 -0.0828 189 ALA A CB  
1273 N N   . THR A 198 ? 0.8863 0.8084 0.9679 -0.0162 -0.0791 -0.0681 190 THR A N   
1274 C CA  . THR A 198 ? 0.8974 0.8161 0.9668 -0.0090 -0.0782 -0.0655 190 THR A CA  
1275 C C   . THR A 198 ? 0.9274 0.8639 0.9949 0.0032  -0.0778 -0.0586 190 THR A C   
1276 O O   . THR A 198 ? 0.9987 0.9307 1.0544 0.0124  -0.0750 -0.0563 190 THR A O   
1277 C CB  . THR A 198 ? 0.9324 0.8560 1.0011 -0.0165 -0.0843 -0.0626 190 THR A CB  
1278 O OG1 . THR A 198 ? 0.8172 0.7679 0.8969 -0.0202 -0.0912 -0.0554 190 THR A OG1 
1279 C CG2 . THR A 198 ? 0.9255 0.8303 0.9943 -0.0275 -0.0841 -0.0688 190 THR A CG2 
1280 N N   . GLN A 199 ? 0.9273 0.8837 1.0053 0.0046  -0.0799 -0.0546 191 GLN A N   
1281 C CA  . GLN A 199 ? 0.8657 0.8428 0.9430 0.0167  -0.0798 -0.0464 191 GLN A CA  
1282 C C   . GLN A 199 ? 0.8228 0.7865 0.8905 0.0282  -0.0722 -0.0502 191 GLN A C   
1283 O O   . GLN A 199 ? 0.9043 0.8471 0.9694 0.0245  -0.0685 -0.0590 191 GLN A O   
1284 C CB  . GLN A 199 ? 0.8186 0.8245 0.9122 0.0122  -0.0857 -0.0394 191 GLN A CB  
1285 C CG  . GLN A 199 ? 0.8750 0.8778 0.9777 0.0071  -0.0847 -0.0442 191 GLN A CG  
1286 C CD  . GLN A 199 ? 0.8432 0.8706 0.9624 -0.0005 -0.0905 -0.0376 191 GLN A CD  
1287 O OE1 . GLN A 199 ? 0.8976 0.9454 1.0218 -0.0029 -0.0958 -0.0294 191 GLN A OE1 
1288 N NE2 . GLN A 199 ? 0.8226 0.8487 0.9502 -0.0047 -0.0896 -0.0408 191 GLN A NE2 
1289 N N   . PRO A 200 ? 0.8319 0.8069 0.8930 0.0424  -0.0697 -0.0434 192 PRO A N   
1290 C CA  . PRO A 200 ? 0.9387 0.8954 0.9855 0.0542  -0.0616 -0.0474 192 PRO A CA  
1291 C C   . PRO A 200 ? 0.9200 0.8713 0.9719 0.0503  -0.0606 -0.0543 192 PRO A C   
1292 O O   . PRO A 200 ? 0.8688 0.8365 0.9363 0.0419  -0.0657 -0.0532 192 PRO A O   
1293 C CB  . PRO A 200 ? 1.0083 0.9855 1.0502 0.0704  -0.0601 -0.0365 192 PRO A CB  
1294 C CG  . PRO A 200 ? 0.9935 0.9933 1.0425 0.0673  -0.0663 -0.0276 192 PRO A CG  
1295 C CD  . PRO A 200 ? 0.9476 0.9522 1.0125 0.0485  -0.0737 -0.0312 192 PRO A CD  
1296 N N   . LEU A 201 ? 0.8756 0.8030 0.9129 0.0564  -0.0537 -0.0612 193 LEU A N   
1297 C CA  . LEU A 201 ? 0.8781 0.7978 0.9180 0.0514  -0.0528 -0.0693 193 LEU A CA  
1298 C C   . LEU A 201 ? 0.8771 0.8240 0.9287 0.0545  -0.0564 -0.0638 193 LEU A C   
1299 O O   . LEU A 201 ? 0.8710 0.8274 0.9368 0.0449  -0.0603 -0.0659 193 LEU A O   
1300 C CB  . LEU A 201 ? 0.9567 0.8480 0.9764 0.0587  -0.0451 -0.0767 193 LEU A CB  
1301 C CG  . LEU A 201 ? 0.9761 0.8598 0.9953 0.0546  -0.0442 -0.0853 193 LEU A CG  
1302 C CD1 . LEU A 201 ? 0.8874 0.7639 0.9174 0.0381  -0.0467 -0.0930 193 LEU A CD1 
1303 C CD2 . LEU A 201 ? 1.0807 0.9373 1.0767 0.0634  -0.0366 -0.0913 193 LEU A CD2 
1304 N N   . GLU A 202 ? 0.8571 0.8176 0.9028 0.0690  -0.0546 -0.0557 194 GLU A N   
1305 C CA  . GLU A 202 ? 0.8442 0.8303 0.8998 0.0737  -0.0570 -0.0497 194 GLU A CA  
1306 C C   . GLU A 202 ? 0.8036 0.8173 0.8814 0.0632  -0.0645 -0.0429 194 GLU A C   
1307 O O   . GLU A 202 ? 0.7354 0.7667 0.8249 0.0618  -0.0669 -0.0404 194 GLU A O   
1308 C CB  . GLU A 202 ? 0.7877 0.7840 0.8321 0.0925  -0.0529 -0.0407 194 GLU A CB  
1309 C CG  . GLU A 202 ? 0.7943 0.7600 0.8135 0.1039  -0.0444 -0.0474 194 GLU A CG  
1310 C CD  . GLU A 202 ? 0.8836 0.8332 0.8980 0.1000  -0.0429 -0.0586 194 GLU A CD  
1311 O OE1 . GLU A 202 ? 0.8835 0.8532 0.9116 0.0968  -0.0469 -0.0572 194 GLU A OE1 
1312 O OE2 . GLU A 202 ? 0.9092 0.8265 0.9060 0.0996  -0.0377 -0.0686 194 GLU A OE2 
1313 N N   . ALA A 203 ? 0.8477 0.8642 0.9303 0.0558  -0.0681 -0.0399 195 ALA A N   
1314 C CA  . ALA A 203 ? 0.8468 0.8843 0.9482 0.0437  -0.0752 -0.0347 195 ALA A CA  
1315 C C   . ALA A 203 ? 0.7969 0.8223 0.9063 0.0301  -0.0765 -0.0432 195 ALA A C   
1316 O O   . ALA A 203 ? 0.7179 0.7594 0.8416 0.0239  -0.0799 -0.0401 195 ALA A O   
1317 C CB  . ALA A 203 ? 0.8527 0.8946 0.9540 0.0394  -0.0788 -0.0300 195 ALA A CB  
1318 N N   . VAL A 204 ? 0.8683 0.8660 0.9684 0.0259  -0.0734 -0.0532 196 VAL A N   
1319 C CA  . VAL A 204 ? 0.8400 0.8274 0.9471 0.0146  -0.0738 -0.0606 196 VAL A CA  
1320 C C   . VAL A 204 ? 0.7414 0.7360 0.8525 0.0179  -0.0724 -0.0627 196 VAL A C   
1321 O O   . VAL A 204 ? 0.7457 0.7489 0.8691 0.0108  -0.0745 -0.0628 196 VAL A O   
1322 C CB  . VAL A 204 ? 0.8359 0.7940 0.9320 0.0104  -0.0701 -0.0699 196 VAL A CB  
1323 C CG1 . VAL A 204 ? 0.8059 0.7566 0.9098 -0.0002 -0.0700 -0.0764 196 VAL A CG1 
1324 C CG2 . VAL A 204 ? 0.8315 0.7834 0.9232 0.0079  -0.0714 -0.0675 196 VAL A CG2 
1325 N N   . GLU A 205 ? 0.7235 0.7137 0.8228 0.0293  -0.0685 -0.0644 197 GLU A N   
1326 C CA  . GLU A 205 ? 0.7418 0.7391 0.8427 0.0333  -0.0675 -0.0666 197 GLU A CA  
1327 C C   . GLU A 205 ? 0.7140 0.7415 0.8301 0.0352  -0.0711 -0.0567 197 GLU A C   
1328 O O   . GLU A 205 ? 0.6612 0.6982 0.7874 0.0313  -0.0723 -0.0576 197 GLU A O   
1329 C CB  . GLU A 205 ? 0.8217 0.8067 0.9039 0.0462  -0.0625 -0.0697 197 GLU A CB  
1330 C CG  . GLU A 205 ? 0.8588 0.8529 0.9399 0.0527  -0.0616 -0.0710 197 GLU A CG  
1331 C CD  . GLU A 205 ? 0.9822 0.9594 1.0411 0.0654  -0.0561 -0.0749 197 GLU A CD  
1332 O OE1 . GLU A 205 ? 0.9387 0.8940 0.9832 0.0678  -0.0524 -0.0776 197 GLU A OE1 
1333 O OE2 . GLU A 205 ? 1.1950 1.1793 1.2495 0.0734  -0.0551 -0.0751 197 GLU A OE2 
1334 N N   . ARG A 206 ? 0.7318 0.7762 0.8501 0.0412  -0.0727 -0.0465 198 ARG A N   
1335 C CA  . ARG A 206 ? 0.6736 0.7480 0.8077 0.0413  -0.0762 -0.0358 198 ARG A CA  
1336 C C   . ARG A 206 ? 0.6774 0.7553 0.8268 0.0267  -0.0799 -0.0362 198 ARG A C   
1337 O O   . ARG A 206 ? 0.6688 0.7611 0.8292 0.0255  -0.0806 -0.0334 198 ARG A O   
1338 C CB  . ARG A 206 ? 0.7737 0.8656 0.9088 0.0466  -0.0781 -0.0247 198 ARG A CB  
1339 C CG  . ARG A 206 ? 0.8338 0.9574 0.9871 0.0429  -0.0827 -0.0126 198 ARG A CG  
1340 C CD  . ARG A 206 ? 1.1092 1.2544 1.2662 0.0550  -0.0807 -0.0054 198 ARG A CD  
1341 N NE  . ARG A 206 ? 1.2263 1.3747 1.3697 0.0723  -0.0766 -0.0014 198 ARG A NE  
1342 C CZ  . ARG A 206 ? 1.1444 1.3162 1.2900 0.0852  -0.0748 0.0085  198 ARG A CZ  
1343 N NH1 . ARG A 206 ? 1.1265 1.3228 1.2889 0.0822  -0.0772 0.0161  198 ARG A NH1 
1344 N NH2 . ARG A 206 ? 1.0815 1.2513 1.2113 0.1023  -0.0698 0.0113  198 ARG A NH2 
1345 N N   . ASP A 207 ? 0.6606 0.7244 0.8096 0.0161  -0.0816 -0.0396 199 ASP A N   
1346 C CA  . ASP A 207 ? 0.6389 0.7043 0.8002 0.0029  -0.0846 -0.0389 199 ASP A CA  
1347 C C   . ASP A 207 ? 0.6711 0.7260 0.8346 -0.0008 -0.0821 -0.0464 199 ASP A C   
1348 O O   . ASP A 207 ? 0.7026 0.7681 0.8778 -0.0054 -0.0829 -0.0431 199 ASP A O   
1349 C CB  . ASP A 207 ? 0.6767 0.7284 0.8342 -0.0062 -0.0869 -0.0406 199 ASP A CB  
1350 C CG  . ASP A 207 ? 0.7588 0.8276 0.9184 -0.0059 -0.0912 -0.0313 199 ASP A CG  
1351 O OD1 . ASP A 207 ? 0.7999 0.8918 0.9642 0.0021  -0.0918 -0.0229 199 ASP A OD1 
1352 O OD2 . ASP A 207 ? 0.8092 0.8696 0.9655 -0.0135 -0.0939 -0.0320 199 ASP A OD2 
1353 N N   . ILE A 208 ? 0.7147 0.7495 0.8673 0.0009  -0.0788 -0.0560 200 ILE A N   
1354 C CA  . ILE A 208 ? 0.7311 0.7597 0.8862 -0.0025 -0.0767 -0.0627 200 ILE A CA  
1355 C C   . ILE A 208 ? 0.7165 0.7649 0.8780 0.0041  -0.0765 -0.0593 200 ILE A C   
1356 O O   . ILE A 208 ? 0.7309 0.7878 0.9027 0.0003  -0.0765 -0.0581 200 ILE A O   
1357 C CB  . ILE A 208 ? 0.7224 0.7286 0.8642 -0.0019 -0.0734 -0.0730 200 ILE A CB  
1358 C CG1 . ILE A 208 ? 0.6633 0.6502 0.8002 -0.0090 -0.0730 -0.0759 200 ILE A CG1 
1359 C CG2 . ILE A 208 ? 0.7495 0.7550 0.8942 -0.0046 -0.0718 -0.0791 200 ILE A CG2 
1360 C CD1 . ILE A 208 ? 0.7848 0.7490 0.9092 -0.0093 -0.0693 -0.0850 200 ILE A CD1 
1361 N N   . ARG A 209 ? 0.7320 0.7878 0.8867 0.0152  -0.0757 -0.0571 201 ARG A N   
1362 C CA  . ARG A 209 ? 0.6783 0.7530 0.8372 0.0232  -0.0753 -0.0536 201 ARG A CA  
1363 C C   . ARG A 209 ? 0.6458 0.7434 0.8215 0.0205  -0.0776 -0.0429 201 ARG A C   
1364 O O   . ARG A 209 ? 0.6260 0.7371 0.8094 0.0226  -0.0770 -0.0408 201 ARG A O   
1365 C CB  . ARG A 209 ? 0.7158 0.7926 0.8622 0.0367  -0.0735 -0.0519 201 ARG A CB  
1366 C CG  . ARG A 209 ? 0.9234 1.0167 1.0698 0.0472  -0.0723 -0.0491 201 ARG A CG  
1367 C CD  . ARG A 209 ? 1.1093 1.1907 1.2356 0.0596  -0.0689 -0.0536 201 ARG A CD  
1368 N NE  . ARG A 209 ? 1.4998 1.5970 1.6241 0.0712  -0.0676 -0.0504 201 ARG A NE  
1369 C CZ  . ARG A 209 ? 1.4012 1.4883 1.5067 0.0828  -0.0643 -0.0549 201 ARG A CZ  
1370 N NH1 . ARG A 209 ? 1.5306 1.5908 1.6175 0.0842  -0.0615 -0.0629 201 ARG A NH1 
1371 N NH2 . ARG A 209 ? 1.3054 1.4083 1.4095 0.0935  -0.0633 -0.0513 201 ARG A NH2 
1372 N N   . ALA A 210 ? 0.6587 0.7608 0.8400 0.0153  -0.0802 -0.0360 202 ALA A N   
1373 C CA  . ALA A 210 ? 0.6365 0.7583 0.8332 0.0107  -0.0824 -0.0258 202 ALA A CA  
1374 C C   . ALA A 210 ? 0.6202 0.7341 0.8246 -0.0001 -0.0820 -0.0282 202 ALA A C   
1375 O O   . ALA A 210 ? 0.5728 0.7006 0.7880 -0.0007 -0.0813 -0.0225 202 ALA A O   
1376 C CB  . ALA A 210 ? 0.6036 0.7328 0.8029 0.0068  -0.0859 -0.0182 202 ALA A CB  
1377 N N   . VAL A 211 ? 0.6493 0.7409 0.8476 -0.0078 -0.0817 -0.0358 203 VAL A N   
1378 C CA  . VAL A 211 ? 0.6883 0.7707 0.8918 -0.0166 -0.0804 -0.0377 203 VAL A CA  
1379 C C   . VAL A 211 ? 0.6674 0.7555 0.8741 -0.0119 -0.0773 -0.0405 203 VAL A C   
1380 O O   . VAL A 211 ? 0.6278 0.7217 0.8433 -0.0146 -0.0757 -0.0368 203 VAL A O   
1381 C CB  . VAL A 211 ? 0.7334 0.7908 0.9280 -0.0237 -0.0800 -0.0453 203 VAL A CB  
1382 C CG1 . VAL A 211 ? 0.6880 0.7353 0.8860 -0.0300 -0.0772 -0.0478 203 VAL A CG1 
1383 C CG2 . VAL A 211 ? 0.8119 0.8653 1.0041 -0.0295 -0.0836 -0.0418 203 VAL A CG2 
1384 N N   . VAL A 212 ? 0.6286 0.7145 0.8271 -0.0050 -0.0762 -0.0473 204 VAL A N   
1385 C CA  . VAL A 212 ? 0.6566 0.7487 0.8565 -0.0012 -0.0741 -0.0511 204 VAL A CA  
1386 C C   . VAL A 212 ? 0.6845 0.8008 0.8931 0.0062  -0.0740 -0.0429 204 VAL A C   
1387 O O   . VAL A 212 ? 0.6232 0.7492 0.8397 0.0063  -0.0722 -0.0406 204 VAL A O   
1388 C CB  . VAL A 212 ? 0.6968 0.7780 0.8836 0.0027  -0.0735 -0.0611 204 VAL A CB  
1389 C CG1 . VAL A 212 ? 0.7509 0.8427 0.9386 0.0068  -0.0724 -0.0646 204 VAL A CG1 
1390 C CG2 . VAL A 212 ? 0.7526 0.8106 0.9326 -0.0052 -0.0727 -0.0686 204 VAL A CG2 
1391 N N   . ASN A 213 ? 0.6667 0.7942 0.8738 0.0133  -0.0753 -0.0375 205 ASN A N   
1392 C CA  . ASN A 213 ? 0.6178 0.7695 0.8333 0.0211  -0.0748 -0.0286 205 ASN A CA  
1393 C C   . ASN A 213 ? 0.6707 0.8315 0.9007 0.0145  -0.0744 -0.0196 205 ASN A C   
1394 O O   . ASN A 213 ? 0.7206 0.8936 0.9581 0.0174  -0.0722 -0.0161 205 ASN A O   
1395 C CB  . ASN A 213 ? 0.6447 0.8074 0.8569 0.0296  -0.0759 -0.0225 205 ASN A CB  
1396 C CG  . ASN A 213 ? 0.7408 0.8949 0.9367 0.0391  -0.0749 -0.0303 205 ASN A CG  
1397 O OD1 . ASN A 213 ? 0.8464 0.9838 1.0332 0.0368  -0.0741 -0.0413 205 ASN A OD1 
1398 N ND2 . ASN A 213 ? 0.8291 0.9943 1.0206 0.0498  -0.0746 -0.0243 205 ASN A ND2 
1399 N N   . ARG A 214 ? 0.6883 0.8424 0.9215 0.0054  -0.0763 -0.0157 206 ARG A N   
1400 C CA  . ARG A 214 ? 0.7003 0.8583 0.9447 -0.0025 -0.0757 -0.0077 206 ARG A CA  
1401 C C   . ARG A 214 ? 0.7373 0.8857 0.9832 -0.0055 -0.0721 -0.0116 206 ARG A C   
1402 O O   . ARG A 214 ? 0.8124 0.9709 1.0671 -0.0047 -0.0693 -0.0048 206 ARG A O   
1403 C CB  . ARG A 214 ? 0.7944 0.9414 1.0381 -0.0136 -0.0789 -0.0058 206 ARG A CB  
1404 C CG  . ARG A 214 ? 0.9087 1.0572 1.1620 -0.0233 -0.0785 0.0024  206 ARG A CG  
1405 C CD  . ARG A 214 ? 1.0798 1.2143 1.3298 -0.0360 -0.0822 0.0024  206 ARG A CD  
1406 N NE  . ARG A 214 ? 1.2727 1.4226 1.5246 -0.0360 -0.0869 0.0081  206 ARG A NE  
1407 C CZ  . ARG A 214 ? 1.3994 1.5420 1.6428 -0.0376 -0.0904 0.0040  206 ARG A CZ  
1408 N NH1 . ARG A 214 ? 1.3797 1.4983 1.6120 -0.0400 -0.0898 -0.0063 206 ARG A NH1 
1409 N NH2 . ARG A 214 ? 1.4629 1.6240 1.7094 -0.0364 -0.0943 0.0111  206 ARG A NH2 
1410 N N   . TRP A 215 ? 0.7219 0.8514 0.9592 -0.0085 -0.0716 -0.0216 207 TRP A N   
1411 C CA  . TRP A 215 ? 0.7393 0.8610 0.9779 -0.0109 -0.0678 -0.0245 207 TRP A CA  
1412 C C   . TRP A 215 ? 0.7087 0.8486 0.9517 -0.0018 -0.0654 -0.0235 207 TRP A C   
1413 O O   . TRP A 215 ? 0.6772 0.8238 0.9274 -0.0010 -0.0619 -0.0180 207 TRP A O   
1414 C CB  . TRP A 215 ? 0.7550 0.8558 0.9839 -0.0153 -0.0678 -0.0348 207 TRP A CB  
1415 C CG  . TRP A 215 ? 0.6763 0.7714 0.9068 -0.0169 -0.0637 -0.0369 207 TRP A CG  
1416 C CD1 . TRP A 215 ? 0.7026 0.7868 0.9351 -0.0224 -0.0605 -0.0330 207 TRP A CD1 
1417 C CD2 . TRP A 215 ? 0.6377 0.7384 0.8671 -0.0128 -0.0621 -0.0426 207 TRP A CD2 
1418 N NE1 . TRP A 215 ? 0.6567 0.7405 0.8898 -0.0204 -0.0563 -0.0352 207 TRP A NE1 
1419 C CE2 . TRP A 215 ? 0.6348 0.7303 0.8670 -0.0153 -0.0577 -0.0410 207 TRP A CE2 
1420 C CE3 . TRP A 215 ? 0.7437 0.8528 0.9688 -0.0077 -0.0639 -0.0491 207 TRP A CE3 
1421 C CZ2 . TRP A 215 ? 0.6560 0.7586 0.8891 -0.0127 -0.0554 -0.0448 207 TRP A CZ2 
1422 C CZ3 . TRP A 215 ? 0.7332 0.8475 0.9586 -0.0068 -0.0622 -0.0538 207 TRP A CZ3 
1423 C CH2 . TRP A 215 ? 0.7207 0.8336 0.9510 -0.0093 -0.0582 -0.0513 207 TRP A CH2 
1424 N N   . VAL A 216 ? 0.7305 0.8780 0.9678 0.0055  -0.0672 -0.0287 208 VAL A N   
1425 C CA  . VAL A 216 ? 0.7025 0.8673 0.9417 0.0142  -0.0657 -0.0292 208 VAL A CA  
1426 C C   . VAL A 216 ? 0.7488 0.9344 0.9987 0.0198  -0.0639 -0.0174 208 VAL A C   
1427 O O   . VAL A 216 ? 0.7592 0.9564 1.0151 0.0235  -0.0608 -0.0139 208 VAL A O   
1428 C CB  . VAL A 216 ? 0.6589 0.8246 0.8870 0.0205  -0.0682 -0.0370 208 VAL A CB  
1429 C CG1 . VAL A 216 ? 0.6756 0.8619 0.9045 0.0307  -0.0675 -0.0358 208 VAL A CG1 
1430 C CG2 . VAL A 216 ? 0.5972 0.7436 0.8155 0.0146  -0.0688 -0.0488 208 VAL A CG2 
1431 N N   . ALA A 217 ? 0.7166 0.9085 0.9695 0.0207  -0.0656 -0.0102 209 ALA A N   
1432 C CA  . ALA A 217 ? 0.7564 0.9687 1.0201 0.0255  -0.0636 0.0020  209 ALA A CA  
1433 C C   . ALA A 217 ? 0.8110 1.0194 1.0834 0.0192  -0.0598 0.0084  209 ALA A C   
1434 O O   . ALA A 217 ? 0.9389 1.1626 1.2189 0.0248  -0.0562 0.0160  209 ALA A O   
1435 C CB  . ALA A 217 ? 0.8493 1.0693 1.1157 0.0255  -0.0662 0.0094  209 ALA A CB  
1436 N N   . GLU A 218 ? 0.7710 0.9579 1.0409 0.0081  -0.0600 0.0055  210 GLU A N   
1437 C CA  . GLU A 218 ? 0.7944 0.9731 1.0694 0.0025  -0.0555 0.0112  210 GLU A CA  
1438 C C   . GLU A 218 ? 0.8217 1.0048 1.0974 0.0088  -0.0507 0.0097  210 GLU A C   
1439 O O   . GLU A 218 ? 0.8451 1.0293 1.1262 0.0094  -0.0454 0.0173  210 GLU A O   
1440 C CB  . GLU A 218 ? 0.7618 0.9141 1.0307 -0.0097 -0.0566 0.0071  210 GLU A CB  
1441 C CG  . GLU A 218 ? 0.8212 0.9714 1.0911 -0.0176 -0.0611 0.0111  210 GLU A CG  
1442 C CD  . GLU A 218 ? 0.8758 1.0005 1.1371 -0.0287 -0.0633 0.0050  210 GLU A CD  
1443 O OE1 . GLU A 218 ? 0.7526 0.8607 1.0067 -0.0295 -0.0611 -0.0025 210 GLU A OE1 
1444 O OE2 . GLU A 218 ? 0.9254 1.0480 1.1870 -0.0367 -0.0672 0.0083  210 GLU A OE2 
1445 N N   . GLN A 219 ? 0.8447 1.0304 1.1146 0.0134  -0.0523 0.0003  211 GLN A N   
1446 C CA  . GLN A 219 ? 0.8392 1.0329 1.1100 0.0190  -0.0486 -0.0013 211 GLN A CA  
1447 C C   . GLN A 219 ? 0.8117 1.0323 1.0876 0.0305  -0.0476 0.0037  211 GLN A C   
1448 O O   . GLN A 219 ? 0.7499 0.9813 1.0213 0.0362  -0.0511 -0.0020 211 GLN A O   
1449 C CB  . GLN A 219 ? 0.8295 1.0151 1.0920 0.0169  -0.0511 -0.0137 211 GLN A CB  
1450 C CG  . GLN A 219 ? 0.7420 0.9017 0.9981 0.0067  -0.0526 -0.0193 211 GLN A CG  
1451 C CD  . GLN A 219 ? 0.8755 1.0201 1.1334 0.0012  -0.0478 -0.0141 211 GLN A CD  
1452 O OE1 . GLN A 219 ? 0.9412 1.0895 1.2017 0.0045  -0.0427 -0.0111 211 GLN A OE1 
1453 N NE2 . GLN A 219 ? 0.8399 0.9670 1.0950 -0.0068 -0.0492 -0.0128 211 GLN A NE2 
1454 N N   . MET B 9   ? 0.9083 1.1178 0.7071 0.1191  -0.0700 -0.0018 1   MET B N   
1455 C CA  . MET B 9   ? 0.9468 1.1635 0.7711 0.1103  -0.0730 0.0146  1   MET B CA  
1456 C C   . MET B 9   ? 0.8577 1.0589 0.6865 0.1161  -0.0546 0.0296  1   MET B C   
1457 O O   . MET B 9   ? 0.9042 1.0781 0.7397 0.1136  -0.0432 0.0186  1   MET B O   
1458 C CB  . MET B 9   ? 0.8128 1.0203 0.6617 0.0938  -0.0816 -0.0025 1   MET B CB  
1459 N N   . ARG B 10  ? 0.8285 1.0470 0.6550 0.1227  -0.0536 0.0559  2   ARG B N   
1460 C CA  . ARG B 10  ? 0.9125 1.1189 0.7433 0.1276  -0.0393 0.0745  2   ARG B CA  
1461 C C   . ARG B 10  ? 0.7914 0.9711 0.6387 0.1160  -0.0316 0.0655  2   ARG B C   
1462 O O   . ARG B 10  ? 0.7133 0.8950 0.5756 0.1024  -0.0391 0.0588  2   ARG B O   
1463 C CB  . ARG B 10  ? 0.9941 1.2233 0.8289 0.1280  -0.0469 0.1025  2   ARG B CB  
1464 C CG  . ARG B 10  ? 1.1911 1.4110 1.0285 0.1328  -0.0357 0.1262  2   ARG B CG  
1465 C CD  . ARG B 10  ? 1.2702 1.4946 1.1249 0.1200  -0.0434 0.1396  2   ARG B CD  
1466 N NE  . ARG B 10  ? 1.3710 1.6062 1.2368 0.1097  -0.0567 0.1285  2   ARG B NE  
1467 C CZ  . ARG B 10  ? 1.5978 1.8332 1.4748 0.1041  -0.0591 0.1306  2   ARG B CZ  
1468 N NH1 . ARG B 10  ? 1.6189 1.8476 1.5014 0.1057  -0.0507 0.1417  2   ARG B NH1 
1469 N NH2 . ARG B 10  ? 1.5546 1.7960 1.4378 0.0965  -0.0710 0.1213  2   ARG B NH2 
1470 N N   . SER B 11  ? 0.8000 0.9556 0.6463 0.1213  -0.0164 0.0660  3   SER B N   
1471 C CA  . SER B 11  ? 0.7826 0.9131 0.6439 0.1100  -0.0083 0.0620  3   SER B CA  
1472 C C   . SER B 11  ? 0.7450 0.8831 0.6149 0.1005  -0.0103 0.0815  3   SER B C   
1473 O O   . SER B 11  ? 0.7914 0.9475 0.6553 0.1060  -0.0150 0.1027  3   SER B O   
1474 C CB  . SER B 11  ? 0.7565 0.8618 0.6164 0.1186  0.0066  0.0652  3   SER B CB  
1475 O OG  . SER B 11  ? 0.7575 0.8715 0.6115 0.1301  0.0113  0.0912  3   SER B OG  
1476 N N   . ASN B 12  ? 0.6495 0.7734 0.5332 0.0858  -0.0066 0.0742  4   ASN B N   
1477 C CA  . ASN B 12  ? 0.6609 0.7898 0.5498 0.0758  -0.0069 0.0895  4   ASN B CA  
1478 C C   . ASN B 12  ? 0.7127 0.8171 0.6096 0.0640  0.0056  0.0900  4   ASN B C   
1479 O O   . ASN B 12  ? 0.6800 0.7666 0.5858 0.0594  0.0116  0.0738  4   ASN B O   
1480 C CB  . ASN B 12  ? 0.6695 0.8187 0.5688 0.0668  -0.0191 0.0797  4   ASN B CB  
1481 C CG  . ASN B 12  ? 0.6709 0.8465 0.5628 0.0751  -0.0329 0.0914  4   ASN B CG  
1482 O OD1 . ASN B 12  ? 0.6542 0.8376 0.5411 0.0765  -0.0354 0.1124  4   ASN B OD1 
1483 N ND2 . ASN B 12  ? 0.7869 0.9762 0.6776 0.0800  -0.0434 0.0789  4   ASN B ND2 
1484 N N   . TYR B 13  ? 0.7344 0.8387 0.6275 0.0581  0.0083  0.1096  5   TYR B N   
1485 C CA  . TYR B 13  ? 0.6451 0.7284 0.5410 0.0458  0.0198  0.1163  5   TYR B CA  
1486 C C   . TYR B 13  ? 0.6170 0.7093 0.5180 0.0310  0.0193  0.1126  5   TYR B C   
1487 O O   . TYR B 13  ? 0.6420 0.7492 0.5353 0.0314  0.0123  0.1240  5   TYR B O   
1488 C CB  . TYR B 13  ? 0.7579 0.8312 0.6417 0.0512  0.0236  0.1443  5   TYR B CB  
1489 C CG  . TYR B 13  ? 0.8010 0.8534 0.6842 0.0372  0.0335  0.1556  5   TYR B CG  
1490 C CD1 . TYR B 13  ? 0.7992 0.8367 0.6945 0.0246  0.0422  0.1406  5   TYR B CD1 
1491 C CD2 . TYR B 13  ? 0.7797 0.8277 0.6503 0.0355  0.0332  0.1828  5   TYR B CD2 
1492 C CE1 . TYR B 13  ? 0.8767 0.8965 0.7702 0.0105  0.0513  0.1528  5   TYR B CE1 
1493 C CE2 . TYR B 13  ? 0.9164 0.9454 0.7834 0.0212  0.0412  0.1946  5   TYR B CE2 
1494 C CZ  . TYR B 13  ? 0.9474 0.9628 0.8253 0.0087  0.0508  0.1798  5   TYR B CZ  
1495 O OH  . TYR B 13  ? 1.0427 1.0405 0.9159 -0.0069 0.0589  0.1934  5   TYR B OH  
1496 N N   . ILE B 14  ? 0.5844 0.6681 0.5000 0.0181  0.0268  0.0961  6   ILE B N   
1497 C CA  . ILE B 14  ? 0.6284 0.7208 0.5525 0.0039  0.0297  0.0892  6   ILE B CA  
1498 C C   . ILE B 14  ? 0.6850 0.7578 0.6070 -0.0101 0.0447  0.0975  6   ILE B C   
1499 O O   . ILE B 14  ? 0.6764 0.7304 0.6051 -0.0127 0.0517  0.0950  6   ILE B O   
1500 C CB  . ILE B 14  ? 0.6366 0.7402 0.5843 -0.0003 0.0254  0.0629  6   ILE B CB  
1501 C CG1 . ILE B 14  ? 0.6425 0.7653 0.5901 0.0124  0.0088  0.0568  6   ILE B CG1 
1502 C CG2 . ILE B 14  ? 0.6422 0.7559 0.6028 -0.0140 0.0306  0.0555  6   ILE B CG2 
1503 C CD1 . ILE B 14  ? 0.6781 0.8072 0.6470 0.0099  0.0019  0.0323  6   ILE B CD1 
1504 N N   . VAL B 15  ? 0.7468 0.8233 0.6582 -0.0195 0.0490  0.1079  7   VAL B N   
1505 C CA  . VAL B 15  ? 0.7865 0.8468 0.6908 -0.0347 0.0631  0.1182  7   VAL B CA  
1506 C C   . VAL B 15  ? 0.7278 0.7992 0.6441 -0.0488 0.0716  0.1024  7   VAL B C   
1507 O O   . VAL B 15  ? 0.7371 0.8280 0.6583 -0.0462 0.0651  0.0923  7   VAL B O   
1508 C CB  . VAL B 15  ? 0.8186 0.8718 0.6953 -0.0347 0.0615  0.1455  7   VAL B CB  
1509 C CG1 . VAL B 15  ? 1.0093 1.0497 0.8747 -0.0532 0.0751  0.1551  7   VAL B CG1 
1510 C CG2 . VAL B 15  ? 0.9483 0.9886 0.8192 -0.0219 0.0563  0.1623  7   VAL B CG2 
1511 N N   . ILE B 16  ? 0.8158 0.8757 0.7394 -0.0638 0.0863  0.1007  8   ILE B N   
1512 C CA  . ILE B 16  ? 0.9098 0.9807 0.8467 -0.0782 0.0981  0.0867  8   ILE B CA  
1513 C C   . ILE B 16  ? 0.9634 1.0235 0.8767 -0.0932 0.1121  0.1039  8   ILE B C   
1514 O O   . ILE B 16  ? 0.9218 0.9636 0.8321 -0.1021 0.1202  0.1159  8   ILE B O   
1515 C CB  . ILE B 16  ? 0.8664 0.9368 0.8366 -0.0845 0.1036  0.0680  8   ILE B CB  
1516 C CG1 . ILE B 16  ? 0.8623 0.9436 0.8516 -0.0706 0.0877  0.0506  8   ILE B CG1 
1517 C CG2 . ILE B 16  ? 0.9296 1.0121 0.9162 -0.1001 0.1187  0.0562  8   ILE B CG2 
1518 C CD1 . ILE B 16  ? 0.9431 1.0244 0.9662 -0.0766 0.0892  0.0310  8   ILE B CD1 
1519 N N   . GLU B 17  ? 1.0372 1.1081 0.9336 -0.0965 0.1139  0.1052  9   GLU B N   
1520 C CA  . GLU B 17  ? 1.0404 1.1019 0.9070 -0.1105 0.1252  0.1213  9   GLU B CA  
1521 C C   . GLU B 17  ? 0.9868 1.0611 0.8619 -0.1249 0.1429  0.1051  9   GLU B C   
1522 O O   . GLU B 17  ? 1.0283 1.1215 0.9311 -0.1213 0.1430  0.0823  9   GLU B O   
1523 C CB  . GLU B 17  ? 1.1798 1.2412 1.0154 -0.1035 0.1130  0.1361  9   GLU B CB  
1524 C CG  . GLU B 17  ? 1.3202 1.3654 1.1396 -0.0946 0.1007  0.1609  9   GLU B CG  
1525 C CD  . GLU B 17  ? 1.3451 1.3923 1.1381 -0.0882 0.0872  0.1754  9   GLU B CD  
1526 O OE1 . GLU B 17  ? 1.3348 1.3949 1.1221 -0.0900 0.0866  0.1642  9   GLU B OE1 
1527 O OE2 . GLU B 17  ? 1.3844 1.4201 1.1648 -0.0812 0.0768  0.1980  9   GLU B OE2 
1528 N N   . GLY B 18  ? 1.1179 1.1827 0.9693 -0.1416 0.1579  0.1176  10  GLY B N   
1529 C CA  . GLY B 18  ? 1.0848 1.1628 0.9398 -0.1554 0.1774  0.1032  10  GLY B CA  
1530 C C   . GLY B 18  ? 1.0523 1.1175 0.8856 -0.1760 0.1955  0.1192  10  GLY B C   
1531 O O   . GLY B 18  ? 1.0499 1.0968 0.8789 -0.1810 0.1939  0.1382  10  GLY B O   
1532 N N   . LEU B 19  ? 1.1680 1.2435 0.9878 -0.1885 0.2132  0.1113  11  LEU B N   
1533 C CA  . LEU B 19  ? 1.1896 1.2566 0.9863 -0.2104 0.2328  0.1255  11  LEU B CA  
1534 C C   . LEU B 19  ? 1.1591 1.2288 0.9933 -0.2201 0.2455  0.1218  11  LEU B C   
1535 O O   . LEU B 19  ? 1.1375 1.2197 1.0155 -0.2116 0.2427  0.1026  11  LEU B O   
1536 C CB  . LEU B 19  ? 1.1682 1.2477 0.9410 -0.2202 0.2504  0.1141  11  LEU B CB  
1537 C CG  . LEU B 19  ? 1.2894 1.3629 1.0246 -0.2106 0.2354  0.1178  11  LEU B CG  
1538 C CD1 . LEU B 19  ? 1.3661 1.4558 1.0928 -0.2131 0.2494  0.0952  11  LEU B CD1 
1539 C CD2 . LEU B 19  ? 1.2886 1.3360 0.9916 -0.2075 0.2209  0.1448  11  LEU B CD2 
1540 N N   . GLU B 20  ? 1.1570 1.2140 0.9739 -0.2391 0.2577  0.1420  12  GLU B N   
1541 C CA  . GLU B 20  ? 1.2259 1.2832 1.0775 -0.2504 0.2686  0.1424  12  GLU B CA  
1542 C C   . GLU B 20  ? 1.2177 1.3023 1.1070 -0.2532 0.2858  0.1151  12  GLU B C   
1543 O O   . GLU B 20  ? 1.2828 1.3842 1.1599 -0.2562 0.2998  0.1021  12  GLU B O   
1544 C CB  . GLU B 20  ? 1.3279 1.3721 1.1600 -0.2638 0.2745  0.1664  12  GLU B CB  
1545 C CG  . GLU B 20  ? 1.4528 1.5092 1.2625 -0.2677 0.2874  0.1620  12  GLU B CG  
1546 C CD  . GLU B 20  ? 1.5143 1.5585 1.3082 -0.2773 0.2898  0.1854  12  GLU B CD  
1547 O OE1 . GLU B 20  ? 1.6143 1.6450 1.4257 -0.2832 0.2854  0.2020  12  GLU B OE1 
1548 O OE2 . GLU B 20  ? 1.5308 1.5783 1.2952 -0.2793 0.2961  0.1867  12  GLU B OE2 
1549 N N   . GLY B 21  ? 1.1773 1.2657 1.1143 -0.2520 0.2841  0.1061  13  GLY B N   
1550 C CA  . GLY B 21  ? 1.0873 1.2014 1.0678 -0.2537 0.2973  0.0813  13  GLY B CA  
1551 C C   . GLY B 21  ? 1.1256 1.2549 1.1274 -0.2337 0.2840  0.0567  13  GLY B C   
1552 O O   . GLY B 21  ? 1.1275 1.2794 1.1693 -0.2339 0.2930  0.0353  13  GLY B O   
1553 N N   . ALA B 22  ? 1.1183 1.2371 1.0964 -0.2172 0.2626  0.0604  14  ALA B N   
1554 C CA  . ALA B 22  ? 1.0320 1.1633 1.0330 -0.1981 0.2455  0.0404  14  ALA B CA  
1555 C C   . ALA B 22  ? 0.9650 1.0954 1.0093 -0.1912 0.2322  0.0313  14  ALA B C   
1556 O O   . ALA B 22  ? 1.0251 1.1687 1.0959 -0.1784 0.2194  0.0130  14  ALA B O   
1557 C CB  . ALA B 22  ? 1.0229 1.1429 0.9868 -0.1833 0.2257  0.0504  14  ALA B CB  
1558 N N   . GLY B 23  ? 0.9423 1.0562 0.9939 -0.1999 0.2337  0.0438  15  GLY B N   
1559 C CA  . GLY B 23  ? 1.0471 1.1564 1.1368 -0.1947 0.2207  0.0348  15  GLY B CA  
1560 C C   . GLY B 23  ? 0.9417 1.0405 1.0216 -0.1746 0.1955  0.0337  15  GLY B C   
1561 O O   . GLY B 23  ? 0.8797 0.9895 0.9852 -0.1635 0.1821  0.0157  15  GLY B O   
1562 N N   . LYS B 24  ? 0.9689 1.0472 1.0122 -0.1702 0.1888  0.0540  16  LYS B N   
1563 C CA  . LYS B 24  ? 0.9892 1.0590 1.0208 -0.1507 0.1672  0.0551  16  LYS B CA  
1564 C C   . LYS B 24  ? 1.0351 1.0924 1.0923 -0.1450 0.1554  0.0478  16  LYS B C   
1565 O O   . LYS B 24  ? 0.9803 1.0408 1.0437 -0.1296 0.1387  0.0364  16  LYS B O   
1566 C CB  . LYS B 24  ? 0.9926 1.0450 0.9814 -0.1481 0.1645  0.0802  16  LYS B CB  
1567 C CG  . LYS B 24  ? 1.0461 1.1089 1.0045 -0.1511 0.1710  0.0861  16  LYS B CG  
1568 C CD  . LYS B 24  ? 1.0968 1.1406 1.0138 -0.1540 0.1698  0.1139  16  LYS B CD  
1569 C CE  . LYS B 24  ? 1.2098 1.2413 1.1171 -0.1753 0.1868  0.1300  16  LYS B CE  
1570 N NZ  . LYS B 24  ? 1.0598 1.1076 0.9658 -0.1915 0.2075  0.1214  16  LYS B NZ  
1571 N N   . THR B 25  ? 1.1087 1.1511 1.1799 -0.1579 0.1632  0.0542  17  THR B N   
1572 C CA  . THR B 25  ? 1.0755 1.1025 1.1703 -0.1531 0.1514  0.0463  17  THR B CA  
1573 C C   . THR B 25  ? 0.9665 1.0103 1.0968 -0.1498 0.1436  0.0207  17  THR B C   
1574 O O   . THR B 25  ? 0.9371 0.9747 1.0740 -0.1371 0.1265  0.0093  17  THR B O   
1575 C CB  . THR B 25  ? 1.1747 1.1833 1.2820 -0.1698 0.1610  0.0583  17  THR B CB  
1576 O OG1 . THR B 25  ? 1.3094 1.3346 1.4322 -0.1885 0.1798  0.0578  17  THR B OG1 
1577 C CG2 . THR B 25  ? 1.1913 1.1779 1.2663 -0.1706 0.1622  0.0845  17  THR B CG2 
1578 N N   . THR B 26  ? 1.0894 1.1546 1.2435 -0.1615 0.1560  0.0114  18  THR B N   
1579 C CA  . THR B 26  ? 0.9704 1.0528 1.1624 -0.1590 0.1473  -0.0115 18  THR B CA  
1580 C C   . THR B 26  ? 0.8636 0.9594 1.0442 -0.1415 0.1317  -0.0213 18  THR B C   
1581 O O   . THR B 26  ? 0.9133 1.0135 1.1142 -0.1340 0.1151  -0.0369 18  THR B O   
1582 C CB  . THR B 26  ? 0.8717 0.9765 1.0954 -0.1746 0.1655  -0.0185 18  THR B CB  
1583 O OG1 . THR B 26  ? 0.9120 1.0379 1.1226 -0.1709 0.1729  -0.0215 18  THR B OG1 
1584 C CG2 . THR B 26  ? 0.8740 0.9690 1.0975 -0.1934 0.1853  -0.0024 18  THR B CG2 
1585 N N   . ALA B 27  ? 0.8592 0.9611 1.0073 -0.1359 0.1356  -0.0114 19  ALA B N   
1586 C CA  . ALA B 27  ? 0.9363 1.0496 1.0724 -0.1196 0.1194  -0.0172 19  ALA B CA  
1587 C C   . ALA B 27  ? 0.8703 0.9673 0.9908 -0.1052 0.1012  -0.0146 19  ALA B C   
1588 O O   . ALA B 27  ? 0.7994 0.9055 0.9262 -0.0939 0.0841  -0.0259 19  ALA B O   
1589 C CB  . ALA B 27  ? 0.9673 1.0868 1.0705 -0.1175 0.1264  -0.0049 19  ALA B CB  
1590 N N   . ARG B 28  ? 0.9745 1.0476 1.0750 -0.1058 0.1048  0.0006  20  ARG B N   
1591 C CA  . ARG B 28  ? 0.8745 0.9313 0.9600 -0.0913 0.0905  0.0028  20  ARG B CA  
1592 C C   . ARG B 28  ? 0.8427 0.8971 0.9543 -0.0887 0.0776  -0.0174 20  ARG B C   
1593 O O   . ARG B 28  ? 0.8335 0.8879 0.9357 -0.0745 0.0622  -0.0242 20  ARG B O   
1594 C CB  . ARG B 28  ? 0.8592 0.8899 0.9272 -0.0944 0.0982  0.0219  20  ARG B CB  
1595 C CG  . ARG B 28  ? 0.8889 0.9034 0.9359 -0.0777 0.0873  0.0288  20  ARG B CG  
1596 C CD  . ARG B 28  ? 0.9615 0.9602 1.0254 -0.0732 0.0780  0.0134  20  ARG B CD  
1597 N NE  . ARG B 28  ? 0.9893 0.9746 1.0789 -0.0894 0.0856  0.0102  20  ARG B NE  
1598 C CZ  . ARG B 28  ? 1.0505 1.0167 1.1379 -0.0989 0.0957  0.0270  20  ARG B CZ  
1599 N NH1 . ARG B 28  ? 0.9903 0.9468 1.0515 -0.0937 0.0990  0.0482  20  ARG B NH1 
1600 N NH2 . ARG B 28  ? 1.1436 1.1008 1.2579 -0.1148 0.1015  0.0241  20  ARG B NH2 
1601 N N   . GLU B 29  ? 0.8494 0.9024 0.9937 -0.1030 0.0833  -0.0269 21  GLU B N   
1602 C CA  . GLU B 29  ? 0.8462 0.8969 1.0167 -0.1022 0.0690  -0.0465 21  GLU B CA  
1603 C C   . GLU B 29  ? 0.8243 0.8995 1.0043 -0.0951 0.0552  -0.0605 21  GLU B C   
1604 O O   . GLU B 29  ? 0.8286 0.9013 1.0082 -0.0863 0.0373  -0.0723 21  GLU B O   
1605 C CB  . GLU B 29  ? 0.8399 0.8877 1.0487 -0.1202 0.0769  -0.0526 21  GLU B CB  
1606 C CG  . GLU B 29  ? 0.9328 0.9719 1.1410 -0.1347 0.0975  -0.0355 21  GLU B CG  
1607 C CD  . GLU B 29  ? 0.9375 0.9462 1.1239 -0.1316 0.0974  -0.0217 21  GLU B CD  
1608 O OE1 . GLU B 29  ? 0.9104 0.9095 1.0703 -0.1153 0.0869  -0.0203 21  GLU B OE1 
1609 O OE2 . GLU B 29  ? 1.0217 1.0169 1.2195 -0.1456 0.1079  -0.0116 21  GLU B OE2 
1610 N N   . CYS B 30  ? 0.8149 0.9136 1.0037 -0.0993 0.0630  -0.0596 22  CYS B N   
1611 C CA  . CYS B 30  ? 0.8302 0.9526 1.0352 -0.0941 0.0493  -0.0725 22  CYS B CA  
1612 C C   . CYS B 30  ? 0.7474 0.8739 0.9200 -0.0773 0.0352  -0.0672 22  CYS B C   
1613 O O   . CYS B 30  ? 0.6808 0.8199 0.8623 -0.0709 0.0171  -0.0775 22  CYS B O   
1614 C CB  . CYS B 30  ? 0.8789 1.0240 1.1057 -0.1030 0.0629  -0.0742 22  CYS B CB  
1615 S SG  . CYS B 30  ? 0.9459 1.0942 1.2203 -0.1231 0.0790  -0.0823 22  CYS B SG  
1616 N N   . VAL B 31  ? 0.7603 0.8772 0.8968 -0.0706 0.0423  -0.0497 23  VAL B N   
1617 C CA  . VAL B 31  ? 0.8202 0.9401 0.9276 -0.0545 0.0289  -0.0430 23  VAL B CA  
1618 C C   . VAL B 31  ? 0.8161 0.9230 0.9178 -0.0463 0.0152  -0.0514 23  VAL B C   
1619 O O   . VAL B 31  ? 0.6964 0.8139 0.7908 -0.0362 -0.0012 -0.0564 23  VAL B O   
1620 C CB  . VAL B 31  ? 0.8120 0.9228 0.8852 -0.0498 0.0389  -0.0211 23  VAL B CB  
1621 C CG1 . VAL B 31  ? 0.8018 0.9151 0.8481 -0.0328 0.0256  -0.0128 23  VAL B CG1 
1622 C CG2 . VAL B 31  ? 0.8847 1.0091 0.9582 -0.0573 0.0499  -0.0147 23  VAL B CG2 
1623 N N   . VAL B 32  ? 0.8375 0.9208 0.9418 -0.0509 0.0215  -0.0533 24  VAL B N   
1624 C CA  . VAL B 32  ? 0.7821 0.8493 0.8782 -0.0428 0.0098  -0.0631 24  VAL B CA  
1625 C C   . VAL B 32  ? 0.7716 0.8501 0.8891 -0.0451 -0.0077 -0.0831 24  VAL B C   
1626 O O   . VAL B 32  ? 0.7267 0.8074 0.8284 -0.0346 -0.0229 -0.0896 24  VAL B O   
1627 C CB  . VAL B 32  ? 0.8192 0.8573 0.9198 -0.0490 0.0193  -0.0623 24  VAL B CB  
1628 C CG1 . VAL B 32  ? 0.8545 0.8740 0.9481 -0.0409 0.0068  -0.0764 24  VAL B CG1 
1629 C CG2 . VAL B 32  ? 0.8726 0.8991 0.9509 -0.0462 0.0337  -0.0404 24  VAL B CG2 
1630 N N   . GLU B 33  ? 0.8182 0.9052 0.9724 -0.0593 -0.0061 -0.0920 25  GLU B N   
1631 C CA  . GLU B 33  ? 0.8130 0.9089 0.9922 -0.0631 -0.0244 -0.1101 25  GLU B CA  
1632 C C   . GLU B 33  ? 0.7330 0.8533 0.9052 -0.0546 -0.0397 -0.1106 25  GLU B C   
1633 O O   . GLU B 33  ? 0.7982 0.9214 0.9702 -0.0516 -0.0595 -0.1217 25  GLU B O   
1634 C CB  . GLU B 33  ? 0.8862 0.9894 1.1114 -0.0800 -0.0181 -0.1172 25  GLU B CB  
1635 C CG  . GLU B 33  ? 0.9892 1.0679 1.2266 -0.0903 -0.0082 -0.1182 25  GLU B CG  
1636 C CD  . GLU B 33  ? 1.1855 1.2745 1.4700 -0.1075 0.0005  -0.1225 25  GLU B CD  
1637 O OE1 . GLU B 33  ? 1.2676 1.3812 1.5798 -0.1108 -0.0050 -0.1294 25  GLU B OE1 
1638 O OE2 . GLU B 33  ? 1.1953 1.2685 1.4914 -0.1179 0.0130  -0.1183 25  GLU B OE2 
1639 N N   . THR B 34  ? 0.6605 0.7980 0.8261 -0.0512 -0.0322 -0.0981 26  THR B N   
1640 C CA  . THR B 34  ? 0.6707 0.8306 0.8306 -0.0430 -0.0480 -0.0964 26  THR B CA  
1641 C C   . THR B 34  ? 0.6832 0.8373 0.8038 -0.0287 -0.0584 -0.0911 26  THR B C   
1642 O O   . THR B 34  ? 0.7435 0.9103 0.8609 -0.0240 -0.0777 -0.0958 26  THR B O   
1643 C CB  . THR B 34  ? 0.8405 1.0166 0.9998 -0.0422 -0.0379 -0.0842 26  THR B CB  
1644 O OG1 . THR B 34  ? 0.8344 0.9975 0.9588 -0.0357 -0.0243 -0.0674 26  THR B OG1 
1645 C CG2 . THR B 34  ? 0.8677 1.0505 1.0636 -0.0557 -0.0245 -0.0904 26  THR B CG2 
1646 N N   . LEU B 35  ? 0.7352 0.8713 0.8266 -0.0218 -0.0454 -0.0803 27  LEU B N   
1647 C CA  . LEU B 35  ? 0.7558 0.8867 0.8120 -0.0073 -0.0520 -0.0756 27  LEU B CA  
1648 C C   . LEU B 35  ? 0.7400 0.8586 0.7939 -0.0069 -0.0647 -0.0936 27  LEU B C   
1649 O O   . LEU B 35  ? 0.7087 0.8346 0.7417 0.0021  -0.0782 -0.0960 27  LEU B O   
1650 C CB  . LEU B 35  ? 0.7474 0.8606 0.7796 -0.0005 -0.0349 -0.0603 27  LEU B CB  
1651 C CG  . LEU B 35  ? 0.7202 0.8432 0.7483 -0.0011 -0.0238 -0.0409 27  LEU B CG  
1652 C CD1 . LEU B 35  ? 0.6252 0.7293 0.6301 0.0052  -0.0098 -0.0243 27  LEU B CD1 
1653 C CD2 . LEU B 35  ? 0.6786 0.8276 0.6996 0.0060  -0.0366 -0.0330 27  LEU B CD2 
1654 N N   . LYS B 36  ? 0.7788 0.8787 0.8531 -0.0173 -0.0612 -0.1063 28  LYS B N   
1655 C CA  . LYS B 36  ? 0.7450 0.8307 0.8174 -0.0182 -0.0753 -0.1250 28  LYS B CA  
1656 C C   . LYS B 36  ? 0.7533 0.8600 0.8367 -0.0216 -0.0978 -0.1343 28  LYS B C   
1657 O O   . LYS B 36  ? 0.6563 0.7597 0.7187 -0.0165 -0.1130 -0.1438 28  LYS B O   
1658 C CB  . LYS B 36  ? 0.7768 0.8406 0.8764 -0.0311 -0.0699 -0.1357 28  LYS B CB  
1659 C CG  . LYS B 36  ? 0.7996 0.8377 0.8905 -0.0296 -0.0513 -0.1283 28  LYS B CG  
1660 C CD  . LYS B 36  ? 0.9055 0.9309 1.0338 -0.0464 -0.0464 -0.1350 28  LYS B CD  
1661 C CE  . LYS B 36  ? 0.8843 0.8815 1.0096 -0.0479 -0.0313 -0.1284 28  LYS B CE  
1662 N NZ  . LYS B 36  ? 0.9494 0.9426 1.1141 -0.0663 -0.0239 -0.1288 28  LYS B NZ  
1663 N N   . GLN B 37  ? 0.7524 0.8803 0.8693 -0.0307 -0.1005 -0.1320 29  GLN B N   
1664 C CA  . GLN B 37  ? 0.7567 0.9054 0.8896 -0.0344 -0.1235 -0.1389 29  GLN B CA  
1665 C C   . GLN B 37  ? 0.7207 0.8862 0.8214 -0.0220 -0.1339 -0.1286 29  GLN B C   
1666 O O   . GLN B 37  ? 0.8197 0.9929 0.9122 -0.0216 -0.1550 -0.1348 29  GLN B O   
1667 C CB  . GLN B 37  ? 0.7406 0.9090 0.9198 -0.0452 -0.1224 -0.1383 29  GLN B CB  
1668 C CG  . GLN B 37  ? 0.8046 0.9618 1.0220 -0.0592 -0.1133 -0.1481 29  GLN B CG  
1669 C CD  . GLN B 37  ? 0.9313 1.0681 1.1513 -0.0650 -0.1269 -0.1637 29  GLN B CD  
1670 O OE1 . GLN B 37  ? 0.9591 1.1002 1.1756 -0.0652 -0.1502 -0.1722 29  GLN B OE1 
1671 N NE2 . GLN B 37  ? 0.9982 1.1116 1.2234 -0.0705 -0.1134 -0.1672 29  GLN B NE2 
1672 N N   . LEU B 38  ? 0.7575 0.9294 0.8398 -0.0128 -0.1202 -0.1114 30  LEU B N   
1673 C CA  . LEU B 38  ? 0.7385 0.9269 0.7918 -0.0010 -0.1287 -0.0986 30  LEU B CA  
1674 C C   . LEU B 38  ? 0.7162 0.8908 0.7276 0.0105  -0.1278 -0.0999 30  LEU B C   
1675 O O   . LEU B 38  ? 0.7429 0.9306 0.7275 0.0215  -0.1306 -0.0871 30  LEU B O   
1676 C CB  . LEU B 38  ? 0.7519 0.9511 0.8024 0.0042  -0.1155 -0.0792 30  LEU B CB  
1677 C CG  . LEU B 38  ? 0.6421 0.8593 0.7299 -0.0047 -0.1182 -0.0782 30  LEU B CG  
1678 C CD1 . LEU B 38  ? 0.7796 0.9958 0.8643 -0.0031 -0.0991 -0.0641 30  LEU B CD1 
1679 C CD2 . LEU B 38  ? 0.6597 0.9026 0.7538 -0.0027 -0.1412 -0.0741 30  LEU B CD2 
1680 N N   . GLY B 39  ? 0.6922 0.8411 0.6988 0.0082  -0.1238 -0.1151 31  GLY B N   
1681 C CA  . GLY B 39  ? 0.7444 0.8785 0.7129 0.0192  -0.1231 -0.1208 31  GLY B CA  
1682 C C   . GLY B 39  ? 0.7825 0.9008 0.7300 0.0310  -0.1013 -0.1107 31  GLY B C   
1683 O O   . GLY B 39  ? 0.8889 0.9968 0.8052 0.0425  -0.0987 -0.1149 31  GLY B O   
1684 N N   . VAL B 40  ? 0.7729 0.8891 0.7362 0.0286  -0.0858 -0.0975 32  VAL B N   
1685 C CA  . VAL B 40  ? 0.8282 0.9272 0.7764 0.0378  -0.0664 -0.0865 32  VAL B CA  
1686 C C   . VAL B 40  ? 0.7728 0.8396 0.7291 0.0329  -0.0598 -0.1019 32  VAL B C   
1687 O O   . VAL B 40  ? 0.8341 0.8938 0.8197 0.0187  -0.0591 -0.1086 32  VAL B O   
1688 C CB  . VAL B 40  ? 0.7512 0.8589 0.7113 0.0349  -0.0544 -0.0659 32  VAL B CB  
1689 C CG1 . VAL B 40  ? 0.6630 0.7539 0.6068 0.0444  -0.0373 -0.0518 32  VAL B CG1 
1690 C CG2 . VAL B 40  ? 0.6957 0.8342 0.6535 0.0376  -0.0644 -0.0530 32  VAL B CG2 
1691 N N   . SER B 41  ? 0.7890 0.8365 0.7216 0.0447  -0.0543 -0.1073 33  SER B N   
1692 C CA  . SER B 41  ? 0.9775 0.9932 0.9160 0.0409  -0.0532 -0.1260 33  SER B CA  
1693 C C   . SER B 41  ? 0.9571 0.9472 0.8949 0.0468  -0.0355 -0.1185 33  SER B C   
1694 O O   . SER B 41  ? 0.9659 0.9316 0.9230 0.0377  -0.0329 -0.1272 33  SER B O   
1695 C CB  . SER B 41  ? 1.1603 1.1692 1.0734 0.0480  -0.0657 -0.1467 33  SER B CB  
1696 O OG  . SER B 41  ? 1.0798 1.1015 1.0025 0.0366  -0.0854 -0.1588 33  SER B OG  
1697 N N   . ASP B 42  ? 1.1387 1.1333 1.0577 0.0612  -0.0246 -0.1016 34  ASP B N   
1698 C CA  . ASP B 42  ? 1.1500 1.1206 1.0710 0.0672  -0.0092 -0.0923 34  ASP B CA  
1699 C C   . ASP B 42  ? 0.9311 0.9142 0.8601 0.0640  0.0008  -0.0645 34  ASP B C   
1700 O O   . ASP B 42  ? 0.9052 0.9131 0.8214 0.0709  0.0000  -0.0493 34  ASP B O   
1701 C CB  . ASP B 42  ? 1.3312 1.2935 1.2264 0.0873  -0.0041 -0.0962 34  ASP B CB  
1702 C CG  . ASP B 42  ? 1.4693 1.4627 1.3413 0.0995  -0.0054 -0.0836 34  ASP B CG  
1703 O OD1 . ASP B 42  ? 1.5075 1.5273 1.3838 0.0926  -0.0118 -0.0713 34  ASP B OD1 
1704 O OD2 . ASP B 42  ? 1.4102 1.4017 1.2610 0.1163  0.0002  -0.0860 34  ASP B OD2 
1705 N N   . MET B 43  ? 0.8798 0.8455 0.8290 0.0529  0.0093  -0.0573 35  MET B N   
1706 C CA  . MET B 43  ? 0.8735 0.8492 0.8277 0.0472  0.0181  -0.0320 35  MET B CA  
1707 C C   . MET B 43  ? 0.7370 0.6860 0.7070 0.0384  0.0287  -0.0237 35  MET B C   
1708 O O   . MET B 43  ? 0.6978 0.6221 0.6797 0.0352  0.0281  -0.0382 35  MET B O   
1709 C CB  . MET B 43  ? 0.8708 0.8717 0.8356 0.0344  0.0124  -0.0313 35  MET B CB  
1710 C CG  . MET B 43  ? 0.7801 0.7747 0.7710 0.0175  0.0090  -0.0481 35  MET B CG  
1711 S SD  . MET B 43  ? 0.7812 0.8090 0.7862 0.0074  -0.0006 -0.0527 35  MET B SD  
1712 C CE  . MET B 43  ? 0.8136 0.8473 0.8113 0.0143  -0.0200 -0.0758 35  MET B CE  
1713 N N   . VAL B 44  ? 0.7600 0.7138 0.7295 0.0338  0.0371  0.0006  36  VAL B N   
1714 C CA  . VAL B 44  ? 0.8071 0.7374 0.7863 0.0269  0.0471  0.0157  36  VAL B CA  
1715 C C   . VAL B 44  ? 0.7392 0.6793 0.7257 0.0090  0.0530  0.0303  36  VAL B C   
1716 O O   . VAL B 44  ? 0.7163 0.6791 0.6912 0.0092  0.0523  0.0409  36  VAL B O   
1717 C CB  . VAL B 44  ? 0.8177 0.7406 0.7838 0.0423  0.0520  0.0352  36  VAL B CB  
1718 C CG1 . VAL B 44  ? 0.8854 0.7890 0.8609 0.0323  0.0604  0.0572  36  VAL B CG1 
1719 C CG2 . VAL B 44  ? 0.7320 0.6405 0.6939 0.0596  0.0499  0.0191  36  VAL B CG2 
1720 N N   . PHE B 45  ? 0.7630 0.6857 0.7678 -0.0067 0.0589  0.0311  37  PHE B N   
1721 C CA  . PHE B 45  ? 0.8297 0.7592 0.8384 -0.0242 0.0676  0.0469  37  PHE B CA  
1722 C C   . PHE B 45  ? 0.7761 0.6875 0.7773 -0.0254 0.0747  0.0732  37  PHE B C   
1723 O O   . PHE B 45  ? 0.8549 0.7418 0.8629 -0.0197 0.0743  0.0749  37  PHE B O   
1724 C CB  . PHE B 45  ? 0.8416 0.7668 0.8760 -0.0431 0.0710  0.0351  37  PHE B CB  
1725 C CG  . PHE B 45  ? 0.8443 0.7806 0.8927 -0.0425 0.0616  0.0083  37  PHE B CG  
1726 C CD1 . PHE B 45  ? 0.8662 0.8218 0.9017 -0.0292 0.0517  -0.0018 37  PHE B CD1 
1727 C CD2 . PHE B 45  ? 0.8964 0.8238 0.9725 -0.0563 0.0613  -0.0051 37  PHE B CD2 
1728 C CE1 . PHE B 45  ? 0.7997 0.7645 0.8481 -0.0300 0.0409  -0.0250 37  PHE B CE1 
1729 C CE2 . PHE B 45  ? 0.8683 0.8049 0.9591 -0.0568 0.0505  -0.0285 37  PHE B CE2 
1730 C CZ  . PHE B 45  ? 0.8400 0.7949 0.9163 -0.0438 0.0400  -0.0384 37  PHE B CZ  
1731 N N   . THR B 46  ? 0.8223 0.7450 0.8097 -0.0329 0.0801  0.0936  38  THR B N   
1732 C CA  . THR B 46  ? 0.9299 0.8369 0.9090 -0.0374 0.0853  0.1213  38  THR B CA  
1733 C C   . THR B 46  ? 0.9100 0.8235 0.8846 -0.0588 0.0943  0.1337  38  THR B C   
1734 O O   . THR B 46  ? 0.8905 0.8264 0.8602 -0.0640 0.0961  0.1256  38  THR B O   
1735 C CB  . THR B 46  ? 0.8750 0.7883 0.8336 -0.0215 0.0808  0.1387  38  THR B CB  
1736 O OG1 . THR B 46  ? 0.8776 0.8185 0.8215 -0.0192 0.0775  0.1361  38  THR B OG1 
1737 C CG2 . THR B 46  ? 0.8594 0.7644 0.8220 -0.0003 0.0752  0.1294  38  THR B CG2 
1738 N N   . ARG B 47  ? 1.0127 0.9062 0.9895 -0.0713 0.1000  0.1534  39  ARG B N   
1739 C CA  . ARG B 47  ? 0.9299 0.8269 0.8958 -0.0920 0.1095  0.1703  39  ARG B CA  
1740 C C   . ARG B 47  ? 0.9834 0.8736 0.9251 -0.0897 0.1069  0.1998  39  ARG B C   
1741 O O   . ARG B 47  ? 1.0238 0.8921 0.9707 -0.0861 0.1034  0.2159  39  ARG B O   
1742 C CB  . ARG B 47  ? 0.9416 0.8217 0.9277 -0.1109 0.1169  0.1733  39  ARG B CB  
1743 C CG  . ARG B 47  ? 1.0385 0.8891 1.0423 -0.1052 0.1110  0.1790  39  ARG B CG  
1744 C CD  . ARG B 47  ? 1.2382 1.0840 1.2668 -0.0952 0.1053  0.1499  39  ARG B CD  
1745 N NE  . ARG B 47  ? 1.2026 1.0257 1.2393 -0.0782 0.0971  0.1491  39  ARG B NE  
1746 C CZ  . ARG B 47  ? 1.2540 1.0488 1.3106 -0.0828 0.0955  0.1560  39  ARG B CZ  
1747 N NH1 . ARG B 47  ? 1.2266 1.0122 1.2966 -0.1050 0.1007  0.1675  39  ARG B NH1 
1748 N NH2 . ARG B 47  ? 1.1816 0.9572 1.2460 -0.0645 0.0886  0.1515  39  ARG B NH2 
1749 N N   . GLU B 48  ? 1.0168 0.9248 0.9342 -0.0916 0.1074  0.2067  40  GLU B N   
1750 C CA  . GLU B 48  ? 1.1493 1.0534 1.0438 -0.0862 0.1011  0.2327  40  GLU B CA  
1751 C C   . GLU B 48  ? 1.1541 1.0374 1.0405 -0.1037 0.1048  0.2607  40  GLU B C   
1752 O O   . GLU B 48  ? 1.2178 1.0853 1.1027 -0.0975 0.0977  0.2827  40  GLU B O   
1753 C CB  . GLU B 48  ? 1.2009 1.1281 1.0722 -0.0846 0.0989  0.2312  40  GLU B CB  
1754 C CG  . GLU B 48  ? 1.2892 1.2309 1.1602 -0.0618 0.0876  0.2235  40  GLU B CG  
1755 C CD  . GLU B 48  ? 1.0933 1.0411 0.9878 -0.0492 0.0858  0.1957  40  GLU B CD  
1756 O OE1 . GLU B 48  ? 1.1964 1.1345 1.1102 -0.0567 0.0917  0.1823  40  GLU B OE1 
1757 O OE2 . GLU B 48  ? 0.9086 0.8710 0.8015 -0.0324 0.0773  0.1880  40  GLU B OE2 
1758 N N   . PRO B 49  ? 1.0685 0.9520 0.9508 -0.1258 0.1158  0.2620  41  PRO B N   
1759 C CA  . PRO B 49  ? 1.2038 1.0651 1.0854 -0.1436 0.1189  0.2870  41  PRO B CA  
1760 C C   . PRO B 49  ? 1.0800 0.9218 0.9962 -0.1397 0.1169  0.2812  41  PRO B C   
1761 O O   . PRO B 49  ? 1.0392 0.8847 0.9770 -0.1440 0.1228  0.2597  41  PRO B O   
1762 C CB  . PRO B 49  ? 1.2170 1.0887 1.0861 -0.1675 0.1332  0.2850  41  PRO B CB  
1763 C CG  . PRO B 49  ? 1.2163 1.1148 1.0738 -0.1609 0.1362  0.2634  41  PRO B CG  
1764 C CD  . PRO B 49  ? 1.1454 1.0507 1.0221 -0.1362 0.1259  0.2435  41  PRO B CD  
1765 N N   . GLY B 50  ? 1.0496 0.8703 0.9736 -0.1311 0.1078  0.2997  42  GLY B N   
1766 C CA  . GLY B 50  ? 1.0019 0.8036 0.9592 -0.1214 0.1039  0.2900  42  GLY B CA  
1767 C C   . GLY B 50  ? 0.9915 0.8011 0.9555 -0.0940 0.0975  0.2694  42  GLY B C   
1768 O O   . GLY B 50  ? 0.9041 0.7272 0.8493 -0.0819 0.0932  0.2754  42  GLY B O   
1769 N N   . GLY B 51  ? 0.9406 0.7422 0.9299 -0.0847 0.0964  0.2455  43  GLY B N   
1770 C CA  . GLY B 51  ? 0.9736 0.7840 0.9662 -0.0605 0.0916  0.2228  43  GLY B CA  
1771 C C   . GLY B 51  ? 0.9223 0.7142 0.9275 -0.0409 0.0856  0.2283  43  GLY B C   
1772 O O   . GLY B 51  ? 0.8214 0.6194 0.8290 -0.0205 0.0829  0.2083  43  GLY B O   
1773 N N   . THR B 52  ? 0.9357 0.7059 0.9493 -0.0466 0.0837  0.2551  44  THR B N   
1774 C CA  . THR B 52  ? 0.8823 0.6328 0.9145 -0.0283 0.0788  0.2609  44  THR B CA  
1775 C C   . THR B 52  ? 0.8525 0.5730 0.9071 -0.0430 0.0768  0.2799  44  THR B C   
1776 O O   . THR B 52  ? 0.8546 0.5733 0.9025 -0.0671 0.0788  0.2969  44  THR B O   
1777 C CB  . THR B 52  ? 0.8713 0.6325 0.8895 -0.0145 0.0752  0.2822  44  THR B CB  
1778 O OG1 . THR B 52  ? 0.9350 0.6983 0.9357 -0.0331 0.0736  0.3134  44  THR B OG1 
1779 C CG2 . THR B 52  ? 0.8362 0.6268 0.8358 0.0012  0.0758  0.2639  44  THR B CG2 
1780 N N   . ILE B 53  ? 0.8492 0.7421 0.7293 -0.0135 -0.1039 0.0727  45  ILE B N   
1781 C CA  . ILE B 53  ? 0.9126 0.7996 0.7799 -0.0310 -0.0970 0.0814  45  ILE B CA  
1782 C C   . ILE B 53  ? 0.8943 0.7840 0.7663 -0.0195 -0.0914 0.0807  45  ILE B C   
1783 O O   . ILE B 53  ? 0.8572 0.7714 0.7298 -0.0270 -0.0866 0.0840  45  ILE B O   
1784 C CB  . ILE B 53  ? 0.9428 0.7768 0.7850 -0.0457 -0.0937 0.0907  45  ILE B CB  
1785 C CG1 . ILE B 53  ? 0.8746 0.7116 0.7096 -0.0623 -0.0992 0.0908  45  ILE B CG1 
1786 C CG2 . ILE B 53  ? 0.8647 0.6873 0.6935 -0.0592 -0.0836 0.1010  45  ILE B CG2 
1787 C CD1 . ILE B 53  ? 1.0617 0.8417 0.8698 -0.0755 -0.0958 0.0978  45  ILE B CD1 
1788 N N   . LEU B 54  ? 0.8886 0.7542 0.7638 -0.0015 -0.0918 0.0762  46  LEU B N   
1789 C CA  . LEU B 54  ? 0.9228 0.7934 0.8027 0.0087  -0.0877 0.0742  46  LEU B CA  
1790 C C   . LEU B 54  ? 0.8116 0.7349 0.7069 0.0128  -0.0874 0.0665  46  LEU B C   
1791 O O   . LEU B 54  ? 0.7932 0.7343 0.6856 0.0074  -0.0830 0.0703  46  LEU B O   
1792 C CB  . LEU B 54  ? 0.9551 0.7979 0.8401 0.0273  -0.0888 0.0676  46  LEU B CB  
1793 C CG  . LEU B 54  ? 0.8416 0.6898 0.7318 0.0372  -0.0856 0.0640  46  LEU B CG  
1794 C CD1 . LEU B 54  ? 0.9217 0.7532 0.7972 0.0269  -0.0809 0.0777  46  LEU B CD1 
1795 C CD2 . LEU B 54  ? 0.7977 0.6198 0.6951 0.0541  -0.0863 0.0557  46  LEU B CD2 
1796 N N   . ALA B 55  ? 0.7644 0.7130 0.6753 0.0229  -0.0910 0.0567  47  ALA B N   
1797 C CA  . ALA B 55  ? 0.7522 0.7493 0.6778 0.0281  -0.0890 0.0494  47  ALA B CA  
1798 C C   . ALA B 55  ? 0.7729 0.7993 0.6952 0.0100  -0.0867 0.0571  47  ALA B C   
1799 O O   . ALA B 55  ? 0.7085 0.7624 0.6335 0.0098  -0.0822 0.0558  47  ALA B O   
1800 C CB  . ALA B 55  ? 0.7581 0.7759 0.7005 0.0417  -0.0917 0.0405  47  ALA B CB  
1801 N N   . GLU B 56  ? 0.7987 0.8185 0.7138 -0.0062 -0.0892 0.0647  48  GLU B N   
1802 C CA  . GLU B 56  ? 0.8040 0.8501 0.7164 -0.0253 -0.0860 0.0716  48  GLU B CA  
1803 C C   . GLU B 56  ? 0.8047 0.8380 0.7026 -0.0329 -0.0783 0.0797  48  GLU B C   
1804 O O   . GLU B 56  ? 0.8334 0.8983 0.7342 -0.0378 -0.0731 0.0813  48  GLU B O   
1805 C CB  . GLU B 56  ? 0.7949 0.8290 0.6991 -0.0435 -0.0896 0.0774  48  GLU B CB  
1806 C CG  . GLU B 56  ? 0.8467 0.9020 0.7651 -0.0379 -0.0980 0.0715  48  GLU B CG  
1807 C CD  . GLU B 56  ? 0.8957 0.9307 0.8015 -0.0556 -0.1029 0.0763  48  GLU B CD  
1808 O OE1 . GLU B 56  ? 1.0174 1.0421 0.9087 -0.0779 -0.0986 0.0835  48  GLU B OE1 
1809 O OE2 . GLU B 56  ? 0.8006 0.8282 0.7092 -0.0473 -0.1103 0.0729  48  GLU B OE2 
1810 N N   . LYS B 57  ? 0.8329 0.8202 0.7152 -0.0329 -0.0766 0.0859  49  LYS B N   
1811 C CA  . LYS B 57  ? 0.7932 0.7670 0.6612 -0.0384 -0.0687 0.0962  49  LYS B CA  
1812 C C   . LYS B 57  ? 0.8218 0.8137 0.6962 -0.0231 -0.0677 0.0909  49  LYS B C   
1813 O O   . LYS B 57  ? 0.8796 0.8781 0.7454 -0.0268 -0.0615 0.0987  49  LYS B O   
1814 C CB  . LYS B 57  ? 0.8254 0.7442 0.6753 -0.0427 -0.0662 0.1060  49  LYS B CB  
1815 C CG  . LYS B 57  ? 0.8220 0.7205 0.6607 -0.0613 -0.0656 0.1110  49  LYS B CG  
1816 C CD  . LYS B 57  ? 0.9901 0.8422 0.8052 -0.0734 -0.0559 0.1255  49  LYS B CD  
1817 C CE  . LYS B 57  ? 1.1944 1.0379 0.9975 -0.0974 -0.0526 0.1293  49  LYS B CE  
1818 N NZ  . LYS B 57  ? 1.2470 1.0426 1.0249 -0.1106 -0.0400 0.1435  49  LYS B NZ  
1819 N N   . LEU B 58  ? 0.7779 0.7779 0.6661 -0.0062 -0.0729 0.0780  50  LEU B N   
1820 C CA  . LEU B 58  ? 0.8144 0.8368 0.7085 0.0059  -0.0716 0.0703  50  LEU B CA  
1821 C C   . LEU B 58  ? 0.7792 0.8497 0.6812 0.0032  -0.0684 0.0663  50  LEU B C   
1822 O O   . LEU B 58  ? 0.7506 0.8401 0.6484 0.0042  -0.0643 0.0670  50  LEU B O   
1823 C CB  . LEU B 58  ? 0.7593 0.7728 0.6648 0.0234  -0.0758 0.0567  50  LEU B CB  
1824 C CG  . LEU B 58  ? 0.7619 0.7296 0.6613 0.0290  -0.0779 0.0593  50  LEU B CG  
1825 C CD1 . LEU B 58  ? 0.8185 0.7823 0.7311 0.0461  -0.0802 0.0440  50  LEU B CD1 
1826 C CD2 . LEU B 58  ? 0.7570 0.7122 0.6449 0.0271  -0.0750 0.0684  50  LEU B CD2 
1827 N N   . ARG B 59  ? 0.7969 0.8889 0.7103 -0.0001 -0.0701 0.0629  51  ARG B N   
1828 C CA  . ARG B 59  ? 0.7588 0.8970 0.6812 -0.0029 -0.0660 0.0605  51  ARG B CA  
1829 C C   . ARG B 59  ? 0.8285 0.9732 0.7383 -0.0194 -0.0596 0.0729  51  ARG B C   
1830 O O   . ARG B 59  ? 0.8428 1.0128 0.7509 -0.0184 -0.0541 0.0728  51  ARG B O   
1831 C CB  . ARG B 59  ? 0.7808 0.9418 0.7193 -0.0038 -0.0693 0.0568  51  ARG B CB  
1832 C CG  . ARG B 59  ? 0.9940 1.2049 0.9451 -0.0062 -0.0645 0.0551  51  ARG B CG  
1833 C CD  . ARG B 59  ? 1.0842 1.3076 1.0292 -0.0278 -0.0605 0.0666  51  ARG B CD  
1834 N NE  . ARG B 59  ? 1.1268 1.3195 1.0616 -0.0431 -0.0643 0.0747  51  ARG B NE  
1835 C CZ  . ARG B 59  ? 1.0771 1.2701 1.0198 -0.0467 -0.0712 0.0734  51  ARG B CZ  
1836 N NH1 . ARG B 59  ? 1.0995 1.3234 1.0622 -0.0347 -0.0751 0.0658  51  ARG B NH1 
1837 N NH2 . ARG B 59  ? 1.0490 1.2102 0.9782 -0.0621 -0.0735 0.0802  51  ARG B NH2 
1838 N N   . SER B 60  ? 0.8421 0.9620 0.7413 -0.0350 -0.0591 0.0838  52  SER B N   
1839 C CA  . SER B 60  ? 0.8807 1.0014 0.7665 -0.0509 -0.0506 0.0963  52  SER B CA  
1840 C C   . SER B 60  ? 0.8604 0.9670 0.7318 -0.0449 -0.0458 0.1028  52  SER B C   
1841 O O   . SER B 60  ? 0.8898 1.0108 0.7529 -0.0513 -0.0376 0.1109  52  SER B O   
1842 C CB  . SER B 60  ? 0.8765 0.9663 0.7512 -0.0691 -0.0494 0.1057  52  SER B CB  
1843 O OG  . SER B 60  ? 0.8419 0.8838 0.7015 -0.0663 -0.0493 0.1120  52  SER B OG  
1844 N N   . LEU B 61  ? 0.8738 0.9539 0.7425 -0.0324 -0.0505 0.1001  53  LEU B N   
1845 C CA  . LEU B 61  ? 0.9184 0.9902 0.7755 -0.0259 -0.0474 0.1064  53  LEU B CA  
1846 C C   . LEU B 61  ? 0.8491 0.9612 0.7112 -0.0172 -0.0464 0.0982  53  LEU B C   
1847 O O   . LEU B 61  ? 0.8390 0.9609 0.6895 -0.0183 -0.0409 0.1066  53  LEU B O   
1848 C CB  . LEU B 61  ? 0.9149 0.9522 0.7711 -0.0151 -0.0530 0.1044  53  LEU B CB  
1849 C CG  . LEU B 61  ? 0.8576 0.8945 0.7076 -0.0051 -0.0529 0.1071  53  LEU B CG  
1850 C CD1 . LEU B 61  ? 0.9207 0.9483 0.7530 -0.0123 -0.0444 0.1266  53  LEU B CD1 
1851 C CD2 . LEU B 61  ? 0.9518 0.9577 0.8060 0.0054  -0.0589 0.1025  53  LEU B CD2 
1852 N N   . VAL B 62  ? 0.8506 0.9850 0.7283 -0.0079 -0.0508 0.0821  54  VAL B N   
1853 C CA  . VAL B 62  ? 0.8862 1.0563 0.7670 0.0001  -0.0487 0.0727  54  VAL B CA  
1854 C C   . VAL B 62  ? 0.8825 1.0834 0.7604 -0.0096 -0.0407 0.0792  54  VAL B C   
1855 O O   . VAL B 62  ? 0.9171 1.1376 0.7860 -0.0077 -0.0361 0.0809  54  VAL B O   
1856 C CB  . VAL B 62  ? 0.8988 1.0814 0.7965 0.0124  -0.0524 0.0546  54  VAL B CB  
1857 C CG1 . VAL B 62  ? 0.9799 1.2001 0.8802 0.0186  -0.0476 0.0446  54  VAL B CG1 
1858 C CG2 . VAL B 62  ? 0.8580 1.0115 0.7567 0.0231  -0.0583 0.0472  54  VAL B CG2 
1859 N N   . LEU B 63  ? 0.8714 1.0782 0.7566 -0.0206 -0.0389 0.0830  55  LEU B N   
1860 C CA  . LEU B 63  ? 0.8844 1.1214 0.7694 -0.0308 -0.0304 0.0888  55  LEU B CA  
1861 C C   . LEU B 63  ? 0.8878 1.1112 0.7530 -0.0409 -0.0225 0.1053  55  LEU B C   
1862 O O   . LEU B 63  ? 0.8963 1.1436 0.7553 -0.0428 -0.0145 0.1096  55  LEU B O   
1863 C CB  . LEU B 63  ? 0.9772 1.2253 0.8764 -0.0417 -0.0311 0.0888  55  LEU B CB  
1864 C CG  . LEU B 63  ? 1.0151 1.2855 0.9357 -0.0306 -0.0366 0.0749  55  LEU B CG  
1865 C CD1 . LEU B 63  ? 0.7896 1.0767 0.7240 -0.0428 -0.0377 0.0774  55  LEU B CD1 
1866 C CD2 . LEU B 63  ? 0.8247 1.1293 0.7510 -0.0187 -0.0316 0.0657  55  LEU B CD2 
1867 N N   . ASP B 64  ? 0.8598 1.0436 0.7139 -0.0467 -0.0232 0.1156  56  ASP B N   
1868 C CA  . ASP B 64  ? 0.8847 1.0522 0.7191 -0.0544 -0.0135 0.1330  56  ASP B CA  
1869 C C   . ASP B 64  ? 0.9369 1.1158 0.7611 -0.0419 -0.0125 0.1351  56  ASP B C   
1870 O O   . ASP B 64  ? 0.9348 1.1222 0.7456 -0.0451 -0.0029 0.1470  56  ASP B O   
1871 C CB  . ASP B 64  ? 0.8859 1.0055 0.7098 -0.0606 -0.0133 0.1433  56  ASP B CB  
1872 C CG  . ASP B 64  ? 0.9756 1.0831 0.8029 -0.0780 -0.0114 0.1446  56  ASP B CG  
1873 O OD1 . ASP B 64  ? 1.0031 1.1398 0.8381 -0.0881 -0.0075 0.1423  56  ASP B OD1 
1874 O OD2 . ASP B 64  ? 1.1000 1.1692 0.9218 -0.0820 -0.0139 0.1477  56  ASP B OD2 
1875 N N   . ILE B 65  ? 0.9099 1.0887 0.7395 -0.0278 -0.0220 0.1237  57  ILE B N   
1876 C CA  . ILE B 65  ? 0.9299 1.1244 0.7503 -0.0172 -0.0225 0.1234  57  ILE B CA  
1877 C C   . ILE B 65  ? 0.9408 1.1776 0.7634 -0.0149 -0.0188 0.1147  57  ILE B C   
1878 O O   . ILE B 65  ? 0.9813 1.2356 0.7907 -0.0111 -0.0151 0.1194  57  ILE B O   
1879 C CB  . ILE B 65  ? 0.8723 1.0542 0.6981 -0.0049 -0.0331 0.1125  57  ILE B CB  
1880 C CG1 . ILE B 65  ? 0.9031 1.0447 0.7213 -0.0057 -0.0340 0.1264  57  ILE B CG1 
1881 C CG2 . ILE B 65  ? 0.8701 1.0796 0.6905 0.0047  -0.0353 0.1049  57  ILE B CG2 
1882 C CD1 . ILE B 65  ? 0.8903 1.0165 0.7150 0.0051  -0.0435 0.1174  57  ILE B CD1 
1883 N N   . GLN B 66  ? 0.8632 1.1180 0.7018 -0.0164 -0.0192 0.1027  58  GLN B N   
1884 C CA  . GLN B 66  ? 0.9395 1.2333 0.7806 -0.0135 -0.0140 0.0947  58  GLN B CA  
1885 C C   . GLN B 66  ? 0.8805 1.1881 0.7126 -0.0243 -0.0023 0.1089  58  GLN B C   
1886 O O   . GLN B 66  ? 0.8297 1.1610 0.6514 -0.0211 0.0038  0.1100  58  GLN B O   
1887 C CB  . GLN B 66  ? 0.8707 1.1801 0.7330 -0.0101 -0.0166 0.0793  58  GLN B CB  
1888 C CG  . GLN B 66  ? 0.9105 1.2126 0.7796 0.0034  -0.0246 0.0628  58  GLN B CG  
1889 C CD  . GLN B 66  ? 1.0026 1.3137 0.8927 0.0084  -0.0263 0.0504  58  GLN B CD  
1890 O OE1 . GLN B 66  ? 1.0241 1.3499 0.9254 0.0015  -0.0229 0.0542  58  GLN B OE1 
1891 N NE2 . GLN B 66  ? 1.1503 1.4534 1.0462 0.0206  -0.0308 0.0358  58  GLN B NE2 
1892 N N   . SER B 67  ? 0.9125 1.2040 0.7468 -0.0379 0.0018  0.1197  59  SER B N   
1893 C CA  . SER B 67  ? 0.8892 1.1921 0.7166 -0.0500 0.0147  0.1323  59  SER B CA  
1894 C C   . SER B 67  ? 0.8796 1.1713 0.6833 -0.0491 0.0225  0.1487  59  SER B C   
1895 O O   . SER B 67  ? 0.9458 1.2521 0.7411 -0.0550 0.0347  0.1581  59  SER B O   
1896 C CB  . SER B 67  ? 0.8562 1.1429 0.6914 -0.0668 0.0172  0.1380  59  SER B CB  
1897 O OG  . SER B 67  ? 0.9421 1.1871 0.7638 -0.0724 0.0179  0.1501  59  SER B OG  
1898 N N   . THR B 68  ? 0.9789 1.2460 0.7723 -0.0414 0.0166  0.1533  60  THR B N   
1899 C CA  . THR B 68  ? 0.9770 1.2396 0.7489 -0.0372 0.0234  0.1695  60  THR B CA  
1900 C C   . THR B 68  ? 1.0396 1.3383 0.8046 -0.0263 0.0227  0.1629  60  THR B C   
1901 O O   . THR B 68  ? 1.0887 1.4012 0.8383 -0.0264 0.0331  0.1747  60  THR B O   
1902 C CB  . THR B 68  ? 1.0185 1.2487 0.7834 -0.0308 0.0170  0.1770  60  THR B CB  
1903 O OG1 . THR B 68  ? 0.9646 1.2021 0.7391 -0.0194 0.0028  0.1601  60  THR B OG1 
1904 C CG2 . THR B 68  ? 1.0337 1.2236 0.8013 -0.0417 0.0192  0.1844  60  THR B CG2 
1905 N N   . GLY B 69  ? 0.9841 1.2970 0.7587 -0.0170 0.0115  0.1439  61  GLY B N   
1906 C CA  . GLY B 69  ? 0.9944 1.3386 0.7604 -0.0076 0.0104  0.1352  61  GLY B CA  
1907 C C   . GLY B 69  ? 1.1281 1.4719 0.8763 0.0008  0.0061  0.1430  61  GLY B C   
1908 O O   . GLY B 69  ? 1.1592 1.5304 0.8961 0.0071  0.0057  0.1373  61  GLY B O   
1909 N N   . ASP B 70  ? 1.2933 1.6078 1.0383 0.0010  0.0033  0.1562  62  ASP B N   
1910 C CA  . ASP B 70  ? 1.1356 1.4511 0.8663 0.0097  -0.0014 0.1658  62  ASP B CA  
1911 C C   . ASP B 70  ? 1.1707 1.4740 0.9117 0.0158  -0.0155 0.1539  62  ASP B C   
1912 O O   . ASP B 70  ? 1.1924 1.4982 0.9248 0.0226  -0.0209 0.1614  62  ASP B O   
1913 C CB  . ASP B 70  ? 1.1459 1.4382 0.8637 0.0074  0.0086  0.1933  62  ASP B CB  
1914 C CG  . ASP B 70  ? 1.2416 1.5556 0.9389 0.0094  0.0202  0.2090  62  ASP B CG  
1915 O OD1 . ASP B 70  ? 1.2332 1.5810 0.9254 0.0122  0.0198  0.1985  62  ASP B OD1 
1916 O OD2 . ASP B 70  ? 1.2901 1.5856 0.9752 0.0087  0.0311  0.2326  62  ASP B OD2 
1917 N N   . GLU B 71  ? 1.0488 1.3398 0.8084 0.0138  -0.0212 0.1369  63  GLU B N   
1918 C CA  . GLU B 71  ? 1.0585 1.3384 0.8283 0.0199  -0.0332 0.1236  63  GLU B CA  
1919 C C   . GLU B 71  ? 0.9762 1.2666 0.7608 0.0212  -0.0370 0.0983  63  GLU B C   
1920 O O   . GLU B 71  ? 1.0411 1.3324 0.8350 0.0164  -0.0319 0.0942  63  GLU B O   
1921 C CB  . GLU B 71  ? 1.1103 1.3492 0.8874 0.0183  -0.0353 0.1336  63  GLU B CB  
1922 C CG  . GLU B 71  ? 1.2460 1.4738 1.0305 0.0257  -0.0465 0.1252  63  GLU B CG  
1923 C CD  . GLU B 71  ? 1.1473 1.3341 0.9354 0.0255  -0.0469 0.1388  63  GLU B CD  
1924 O OE1 . GLU B 71  ? 1.2714 1.4357 1.0563 0.0185  -0.0387 0.1524  63  GLU B OE1 
1925 O OE2 . GLU B 71  ? 1.0254 1.2020 0.8192 0.0316  -0.0546 0.1357  63  GLU B OE2 
1926 N N   . VAL B 72  ? 0.9523 1.2512 0.7391 0.0276  -0.0452 0.0818  64  VAL B N   
1927 C CA  . VAL B 72  ? 0.9085 1.2135 0.7079 0.0306  -0.0473 0.0573  64  VAL B CA  
1928 C C   . VAL B 72  ? 0.9549 1.2304 0.7685 0.0341  -0.0549 0.0497  64  VAL B C   
1929 O O   . VAL B 72  ? 1.0082 1.2734 0.8187 0.0364  -0.0612 0.0546  64  VAL B O   
1930 C CB  . VAL B 72  ? 0.9975 1.3337 0.7861 0.0341  -0.0480 0.0419  64  VAL B CB  
1931 C CG1 . VAL B 72  ? 1.0025 1.3326 0.8018 0.0387  -0.0530 0.0176  64  VAL B CG1 
1932 C CG2 . VAL B 72  ? 1.2750 1.6372 1.0576 0.0321  -0.0382 0.0398  64  VAL B CG2 
1933 N N   . ILE B 73  ? 0.8716 1.1349 0.7011 0.0352  -0.0539 0.0386  65  ILE B N   
1934 C CA  . ILE B 73  ? 0.8157 1.0498 0.6586 0.0395  -0.0597 0.0303  65  ILE B CA  
1935 C C   . ILE B 73  ? 0.7602 1.0041 0.6077 0.0459  -0.0611 0.0062  65  ILE B C   
1936 O O   . ILE B 73  ? 0.7927 1.0524 0.6445 0.0482  -0.0554 -0.0071 65  ILE B O   
1937 C CB  . ILE B 73  ? 0.8083 1.0227 0.6646 0.0377  -0.0576 0.0330  65  ILE B CB  
1938 C CG1 . ILE B 73  ? 0.8519 1.0494 0.7015 0.0295  -0.0559 0.0559  65  ILE B CG1 
1939 C CG2 . ILE B 73  ? 0.7827 0.9701 0.6526 0.0444  -0.0623 0.0213  65  ILE B CG2 
1940 C CD1 . ILE B 73  ? 0.9685 1.1580 0.8271 0.0235  -0.0527 0.0596  65  ILE B CD1 
1941 N N   . ASN B 74  ? 0.7534 0.9877 0.6004 0.0485  -0.0675 0.0007  66  ASN B N   
1942 C CA  . ASN B 74  ? 0.7434 0.9827 0.5941 0.0528  -0.0679 -0.0234 66  ASN B CA  
1943 C C   . ASN B 74  ? 0.7052 0.9278 0.5718 0.0585  -0.0630 -0.0365 66  ASN B C   
1944 O O   . ASN B 74  ? 0.7004 0.8986 0.5775 0.0599  -0.0640 -0.0278 66  ASN B O   
1945 C CB  . ASN B 74  ? 0.7089 0.9357 0.5608 0.0534  -0.0758 -0.0257 66  ASN B CB  
1946 C CG  . ASN B 74  ? 0.7642 0.9997 0.6164 0.0548  -0.0755 -0.0513 66  ASN B CG  
1947 O OD1 . ASN B 74  ? 0.8546 1.1190 0.6930 0.0513  -0.0756 -0.0591 66  ASN B OD1 
1948 N ND2 . ASN B 74  ? 0.7769 0.9862 0.6433 0.0595  -0.0745 -0.0648 66  ASN B ND2 
1949 N N   . ASP B 75  ? 0.7493 0.9851 0.6166 0.0622  -0.0568 -0.0570 67  ASP B N   
1950 C CA  . ASP B 75  ? 0.7345 0.9573 0.6167 0.0699  -0.0502 -0.0682 67  ASP B CA  
1951 C C   . ASP B 75  ? 0.7443 0.9316 0.6389 0.0749  -0.0540 -0.0718 67  ASP B C   
1952 O O   . ASP B 75  ? 0.6827 0.8515 0.5892 0.0792  -0.0534 -0.0660 67  ASP B O   
1953 C CB  . ASP B 75  ? 0.7747 1.0145 0.6534 0.0739  -0.0406 -0.0898 67  ASP B CB  
1954 C CG  . ASP B 75  ? 0.9139 1.1574 0.7813 0.0708  -0.0424 -0.1060 67  ASP B CG  
1955 O OD1 . ASP B 75  ? 0.9538 1.1929 0.8168 0.0657  -0.0522 -0.0991 67  ASP B OD1 
1956 O OD2 . ASP B 75  ? 0.9900 1.2416 0.8529 0.0731  -0.0334 -0.1258 67  ASP B OD2 
1957 N N   . LYS B 76  ? 0.9313 1.1096 0.8232 0.0739  -0.0582 -0.0807 68  LYS B N   
1958 C CA  . LYS B 76  ? 0.7937 0.9374 0.6979 0.0790  -0.0602 -0.0852 68  LYS B CA  
1959 C C   . LYS B 76  ? 0.7559 0.8766 0.6649 0.0782  -0.0664 -0.0639 68  LYS B C   
1960 O O   . LYS B 76  ? 0.7825 0.8761 0.7027 0.0843  -0.0651 -0.0636 68  LYS B O   
1961 C CB  . LYS B 76  ? 0.7565 0.8988 0.6574 0.0760  -0.0638 -0.0976 68  LYS B CB  
1962 C CG  . LYS B 76  ? 0.9665 1.1238 0.8623 0.0761  -0.0559 -0.1227 68  LYS B CG  
1963 C CD  . LYS B 76  ? 1.0869 1.2378 0.9826 0.0722  -0.0584 -0.1387 68  LYS B CD  
1964 C CE  . LYS B 76  ? 1.3774 1.5318 1.2693 0.0732  -0.0467 -0.1662 68  LYS B CE  
1965 N NZ  . LYS B 76  ? 1.7016 1.8517 1.5924 0.0667  -0.0481 -0.1846 68  LYS B NZ  
1966 N N   . ALA B 77  ? 0.7204 0.8503 0.6196 0.0709  -0.0720 -0.0454 69  ALA B N   
1967 C CA  . ALA B 77  ? 0.7007 0.8062 0.6016 0.0691  -0.0756 -0.0249 69  ALA B CA  
1968 C C   . ALA B 77  ? 0.7241 0.8237 0.6308 0.0702  -0.0718 -0.0204 69  ALA B C   
1969 O O   . ALA B 77  ? 0.7256 0.7957 0.6389 0.0724  -0.0732 -0.0143 69  ALA B O   
1970 C CB  . ALA B 77  ? 0.7104 0.8290 0.5980 0.0617  -0.0788 -0.0050 69  ALA B CB  
1971 N N   . GLU B 78  ? 0.7869 0.9158 0.6913 0.0686  -0.0671 -0.0233 70  GLU B N   
1972 C CA  . GLU B 78  ? 0.7659 0.8956 0.6777 0.0688  -0.0641 -0.0186 70  GLU B CA  
1973 C C   . GLU B 78  ? 0.7669 0.8771 0.6929 0.0792  -0.0622 -0.0305 70  GLU B C   
1974 O O   . GLU B 78  ? 0.7125 0.8053 0.6447 0.0798  -0.0640 -0.0227 70  GLU B O   
1975 C CB  . GLU B 78  ? 0.6928 0.8600 0.6020 0.0664  -0.0581 -0.0209 70  GLU B CB  
1976 C CG  . GLU B 78  ? 0.8427 1.0172 0.7605 0.0645  -0.0557 -0.0135 70  GLU B CG  
1977 C CD  . GLU B 78  ? 0.9920 1.2033 0.9062 0.0593  -0.0499 -0.0104 70  GLU B CD  
1978 O OE1 . GLU B 78  ? 0.8772 1.1062 0.7797 0.0575  -0.0477 -0.0132 70  GLU B OE1 
1979 O OE2 . GLU B 78  ? 1.0122 1.2357 0.9352 0.0569  -0.0475 -0.0050 70  GLU B OE2 
1980 N N   . VAL B 79  ? 0.7808 0.8925 0.7107 0.0872  -0.0578 -0.0494 71  VAL B N   
1981 C CA  . VAL B 79  ? 0.7081 0.7997 0.6508 0.0989  -0.0537 -0.0604 71  VAL B CA  
1982 C C   . VAL B 79  ? 0.7374 0.7901 0.6835 0.1005  -0.0593 -0.0538 71  VAL B C   
1983 O O   . VAL B 79  ? 0.8366 0.8710 0.7910 0.1071  -0.0587 -0.0518 71  VAL B O   
1984 C CB  . VAL B 79  ? 0.6959 0.7921 0.6400 0.1060  -0.0457 -0.0825 71  VAL B CB  
1985 C CG1 . VAL B 79  ? 0.8606 0.9306 0.8171 0.1192  -0.0396 -0.0927 71  VAL B CG1 
1986 C CG2 . VAL B 79  ? 0.7004 0.8323 0.6406 0.1056  -0.0381 -0.0889 71  VAL B CG2 
1987 N N   . LEU B 80  ? 0.7008 0.7410 0.6404 0.0953  -0.0645 -0.0499 72  LEU B N   
1988 C CA  . LEU B 80  ? 0.7770 0.7795 0.7190 0.0965  -0.0689 -0.0411 72  LEU B CA  
1989 C C   . LEU B 80  ? 0.7702 0.7627 0.7091 0.0913  -0.0722 -0.0227 72  LEU B C   
1990 O O   . LEU B 80  ? 0.8004 0.7619 0.7430 0.0952  -0.0734 -0.0185 72  LEU B O   
1991 C CB  . LEU B 80  ? 0.7726 0.7693 0.7087 0.0914  -0.0736 -0.0370 72  LEU B CB  
1992 C CG  . LEU B 80  ? 0.7105 0.7090 0.6507 0.0948  -0.0717 -0.0558 72  LEU B CG  
1993 C CD1 . LEU B 80  ? 0.8146 0.8209 0.7485 0.0878  -0.0778 -0.0488 72  LEU B CD1 
1994 C CD2 . LEU B 80  ? 0.8665 0.8293 0.8184 0.1044  -0.0682 -0.0654 72  LEU B CD2 
1995 N N   . MET B 81  ? 0.7290 0.7465 0.6600 0.0818  -0.0729 -0.0120 73  MET B N   
1996 C CA  . MET B 81  ? 0.7279 0.7381 0.6556 0.0746  -0.0747 0.0034  73  MET B CA  
1997 C C   . MET B 81  ? 0.7279 0.7458 0.6659 0.0798  -0.0729 -0.0021 73  MET B C   
1998 O O   . MET B 81  ? 0.7391 0.7433 0.6765 0.0756  -0.0754 0.0076  73  MET B O   
1999 C CB  . MET B 81  ? 0.7270 0.7619 0.6438 0.0626  -0.0740 0.0158  73  MET B CB  
2000 C CG  . MET B 81  ? 0.7754 0.7985 0.6802 0.0569  -0.0757 0.0287  73  MET B CG  
2001 S SD  . MET B 81  ? 0.7539 0.8015 0.6449 0.0438  -0.0724 0.0455  73  MET B SD  
2002 C CE  . MET B 81  ? 0.7667 0.8597 0.6574 0.0473  -0.0702 0.0320  73  MET B CE  
2003 N N   . PHE B 82  ? 0.7692 0.8100 0.7160 0.0886  -0.0679 -0.0168 74  PHE B N   
2004 C CA  . PHE B 82  ? 0.7740 0.8227 0.7326 0.0971  -0.0651 -0.0215 74  PHE B CA  
2005 C C   . PHE B 82  ? 0.8230 0.8364 0.7878 0.1085  -0.0654 -0.0264 74  PHE B C   
2006 O O   . PHE B 82  ? 0.8817 0.8868 0.8508 0.1110  -0.0677 -0.0206 74  PHE B O   
2007 C CB  . PHE B 82  ? 0.7710 0.8527 0.7359 0.1042  -0.0571 -0.0348 74  PHE B CB  
2008 C CG  . PHE B 82  ? 0.8580 0.9457 0.8367 0.1178  -0.0517 -0.0413 74  PHE B CG  
2009 C CD1 . PHE B 82  ? 0.8730 0.9894 0.8593 0.1163  -0.0514 -0.0341 74  PHE B CD1 
2010 C CD2 . PHE B 82  ? 0.9350 1.0011 0.9199 0.1324  -0.0460 -0.0543 74  PHE B CD2 
2011 C CE1 . PHE B 82  ? 0.9229 1.0486 0.9231 0.1305  -0.0461 -0.0382 74  PHE B CE1 
2012 C CE2 . PHE B 82  ? 1.0083 1.0798 1.0055 0.1469  -0.0392 -0.0587 74  PHE B CE2 
2013 C CZ  . PHE B 82  ? 0.9519 1.0545 0.9570 0.1466  -0.0396 -0.0500 74  PHE B CZ  
2014 N N   . TYR B 83  ? 0.8372 0.8301 0.8022 0.1151  -0.0630 -0.0369 75  TYR B N   
2015 C CA  . TYR B 83  ? 0.9272 0.8834 0.8977 0.1261  -0.0619 -0.0413 75  TYR B CA  
2016 C C   . TYR B 83  ? 0.8348 0.7579 0.7982 0.1199  -0.0688 -0.0268 75  TYR B C   
2017 O O   . TYR B 83  ? 0.8661 0.7607 0.8326 0.1280  -0.0687 -0.0261 75  TYR B O   
2018 C CB  . TYR B 83  ? 0.9684 0.9119 0.9415 0.1328  -0.0565 -0.0570 75  TYR B CB  
2019 C CG  . TYR B 83  ? 1.1140 1.0608 1.0971 0.1476  -0.0459 -0.0730 75  TYR B CG  
2020 C CD1 . TYR B 83  ? 1.1931 1.1727 1.1776 0.1491  -0.0388 -0.0832 75  TYR B CD1 
2021 C CD2 . TYR B 83  ? 1.2807 1.1961 1.2708 0.1608  -0.0414 -0.0771 75  TYR B CD2 
2022 C CE1 . TYR B 83  ? 1.2201 1.2002 1.2127 0.1634  -0.0265 -0.0969 75  TYR B CE1 
2023 C CE2 . TYR B 83  ? 1.3791 1.2956 1.3777 0.1758  -0.0294 -0.0904 75  TYR B CE2 
2024 C CZ  . TYR B 83  ? 1.2276 1.1761 1.2275 0.1770  -0.0215 -0.1002 75  TYR B CZ  
2025 O OH  . TYR B 83  ? 1.2912 1.2384 1.2986 0.1926  -0.0071 -0.1127 75  TYR B OH  
2026 N N   . ALA B 84  ? 0.8102 0.7349 0.7630 0.1064  -0.0735 -0.0146 76  ALA B N   
2027 C CA  . ALA B 84  ? 0.8499 0.7415 0.7938 0.0998  -0.0779 0.0003  76  ALA B CA  
2028 C C   . ALA B 84  ? 0.8180 0.7096 0.7607 0.0966  -0.0804 0.0077  76  ALA B C   
2029 O O   . ALA B 84  ? 0.7791 0.6373 0.7179 0.0980  -0.0824 0.0134  76  ALA B O   
2030 C CB  . ALA B 84  ? 0.8021 0.6973 0.7343 0.0869  -0.0799 0.0129  76  ALA B CB  
2031 N N   . ALA B 85  ? 0.8673 0.7972 0.8131 0.0918  -0.0803 0.0079  77  ALA B N   
2032 C CA  . ALA B 85  ? 0.8447 0.7819 0.7918 0.0882  -0.0834 0.0139  77  ALA B CA  
2033 C C   . ALA B 85  ? 0.7664 0.6953 0.7242 0.1047  -0.0823 0.0058  77  ALA B C   
2034 O O   . ALA B 85  ? 0.7589 0.6686 0.7134 0.1046  -0.0862 0.0116  77  ALA B O   
2035 C CB  . ALA B 85  ? 0.8410 0.8248 0.7920 0.0799  -0.0826 0.0157  77  ALA B CB  
2036 N N   . ARG B 86  ? 0.8035 0.7455 0.7726 0.1190  -0.0760 -0.0076 78  ARG B N   
2037 C CA  . ARG B 86  ? 0.8794 0.8130 0.8586 0.1367  -0.0724 -0.0146 78  ARG B CA  
2038 C C   . ARG B 86  ? 0.8495 0.7337 0.8232 0.1426  -0.0735 -0.0132 78  ARG B C   
2039 O O   . ARG B 86  ? 0.8633 0.7340 0.8384 0.1508  -0.0748 -0.0105 78  ARG B O   
2040 C CB  . ARG B 86  ? 0.9634 0.9129 0.9532 0.1505  -0.0624 -0.0299 78  ARG B CB  
2041 C CG  . ARG B 86  ? 1.1162 1.0495 1.1153 0.1710  -0.0555 -0.0374 78  ARG B CG  
2042 C CD  . ARG B 86  ? 1.1720 1.1219 1.1806 0.1840  -0.0429 -0.0523 78  ARG B CD  
2043 N NE  . ARG B 86  ? 1.3071 1.3034 1.3226 0.1836  -0.0405 -0.0507 78  ARG B NE  
2044 C CZ  . ARG B 86  ? 1.5594 1.5749 1.5834 0.1960  -0.0282 -0.0611 78  ARG B CZ  
2045 N NH1 . ARG B 86  ? 1.6013 1.5934 1.6273 0.2092  -0.0165 -0.0751 78  ARG B NH1 
2046 N NH2 . ARG B 86  ? 1.5208 1.5789 1.5513 0.1948  -0.0262 -0.0574 78  ARG B NH2 
2047 N N   . VAL B 87  ? 0.8953 0.7535 0.8631 0.1390  -0.0729 -0.0146 79  VAL B N   
2048 C CA  . VAL B 87  ? 0.8964 0.7066 0.8597 0.1444  -0.0728 -0.0127 79  VAL B CA  
2049 C C   . VAL B 87  ? 0.8774 0.6673 0.8282 0.1346  -0.0796 0.0021  79  VAL B C   
2050 O O   . VAL B 87  ? 0.8407 0.6005 0.7887 0.1423  -0.0800 0.0042  79  VAL B O   
2051 C CB  . VAL B 87  ? 0.9017 0.6946 0.8630 0.1411  -0.0710 -0.0157 79  VAL B CB  
2052 C CG1 . VAL B 87  ? 0.9386 0.6822 0.8945 0.1440  -0.0712 -0.0101 79  VAL B CG1 
2053 C CG2 . VAL B 87  ? 1.0604 0.8668 1.0327 0.1510  -0.0635 -0.0331 79  VAL B CG2 
2054 N N   . GLN B 88  ? 0.8404 0.6448 0.7819 0.1171  -0.0841 0.0123  80  GLN B N   
2055 C CA  . GLN B 88  ? 0.8034 0.5897 0.7310 0.1049  -0.0892 0.0253  80  GLN B CA  
2056 C C   . GLN B 88  ? 0.8517 0.6510 0.7826 0.1092  -0.0928 0.0251  80  GLN B C   
2057 O O   . GLN B 88  ? 0.8041 0.5745 0.7248 0.1078  -0.0959 0.0311  80  GLN B O   
2058 C CB  . GLN B 88  ? 0.7977 0.6034 0.7164 0.0855  -0.0909 0.0347  80  GLN B CB  
2059 C CG  . GLN B 88  ? 0.8182 0.6040 0.7202 0.0695  -0.0941 0.0475  80  GLN B CG  
2060 C CD  . GLN B 88  ? 0.8967 0.6291 0.7849 0.0685  -0.0918 0.0551  80  GLN B CD  
2061 O OE1 . GLN B 88  ? 0.8809 0.5928 0.7745 0.0807  -0.0887 0.0507  80  GLN B OE1 
2062 N NE2 . GLN B 88  ? 0.9793 0.6883 0.8496 0.0534  -0.0923 0.0663  80  GLN B NE2 
2063 N N   . LEU B 89  ? 0.8479 0.6916 0.7925 0.1145  -0.0921 0.0190  81  LEU B N   
2064 C CA  . LEU B 89  ? 0.7708 0.6340 0.7208 0.1196  -0.0958 0.0203  81  LEU B CA  
2065 C C   . LEU B 89  ? 0.8124 0.6478 0.7658 0.1399  -0.0930 0.0157  81  LEU B C   
2066 O O   . LEU B 89  ? 0.8285 0.6561 0.7770 0.1419  -0.0978 0.0210  81  LEU B O   
2067 C CB  . LEU B 89  ? 0.7426 0.6603 0.7085 0.1231  -0.0937 0.0158  81  LEU B CB  
2068 C CG  . LEU B 89  ? 0.7561 0.7018 0.7301 0.1286  -0.0979 0.0191  81  LEU B CG  
2069 C CD1 . LEU B 89  ? 0.7177 0.6718 0.6808 0.1063  -0.1072 0.0299  81  LEU B CD1 
2070 C CD2 . LEU B 89  ? 0.7896 0.7841 0.7824 0.1389  -0.0924 0.0136  81  LEU B CD2 
2071 N N   . VAL B 90  ? 0.8354 0.6571 0.7969 0.1550  -0.0847 0.0055  82  VAL B N   
2072 C CA  . VAL B 90  ? 0.8656 0.6597 0.8310 0.1755  -0.0795 0.0005  82  VAL B CA  
2073 C C   . VAL B 90  ? 0.9053 0.6475 0.8558 0.1730  -0.0821 0.0070  82  VAL B C   
2074 O O   . VAL B 90  ? 0.8451 0.5666 0.7928 0.1848  -0.0818 0.0088  82  VAL B O   
2075 C CB  . VAL B 90  ? 0.9294 0.7207 0.9067 0.1898  -0.0682 -0.0134 82  VAL B CB  
2076 C CG1 . VAL B 90  ? 1.0434 0.7930 1.0218 0.2081  -0.0610 -0.0181 82  VAL B CG1 
2077 C CG2 . VAL B 90  ? 1.0149 0.8528 1.0062 0.1977  -0.0630 -0.0198 82  VAL B CG2 
2078 N N   . GLU B 91  ? 0.9465 0.6666 0.8868 0.1587  -0.0837 0.0114  83  GLU B N   
2079 C CA  . GLU B 91  ? 0.8667 0.5336 0.7942 0.1587  -0.0831 0.0167  83  GLU B CA  
2080 C C   . GLU B 91  ? 0.8603 0.5120 0.7689 0.1437  -0.0903 0.0293  83  GLU B C   
2081 O O   . GLU B 91  ? 0.9532 0.5868 0.8594 0.1383  -0.0829 0.0325  83  GLU B O   
2082 C CB  . GLU B 91  ? 0.8946 0.5490 0.8240 0.1508  -0.0775 0.0158  83  GLU B CB  
2083 C CG  . GLU B 91  ? 0.9639 0.6225 0.9120 0.1411  -0.0579 0.0146  83  GLU B CG  
2084 C CD  . GLU B 91  ? 1.0057 0.6793 0.9743 0.1514  -0.0468 0.0037  83  GLU B CD  
2085 O OE1 . GLU B 91  ? 0.8729 0.5545 0.8442 0.1632  -0.0491 -0.0065 83  GLU B OE1 
2086 O OE2 . GLU B 91  ? 1.0314 0.7093 1.0144 0.1472  -0.0352 0.0053  83  GLU B OE2 
2087 N N   . THR B 92  ? 0.8337 0.5180 0.7381 0.1263  -0.0962 0.0347  84  THR B N   
2088 C CA  . THR B 92  ? 0.9004 0.5710 0.7857 0.1093  -0.1021 0.0452  84  THR B CA  
2089 C C   . THR B 92  ? 0.7510 0.4547 0.6378 0.1076  -0.1094 0.0460  84  THR B C   
2090 O O   . THR B 92  ? 0.7582 0.4456 0.6279 0.0961  -0.1146 0.0526  84  THR B O   
2091 C CB  . THR B 92  ? 0.9491 0.6270 0.8251 0.0870  -0.1025 0.0525  84  THR B CB  
2092 O OG1 . THR B 92  ? 0.9470 0.6794 0.8328 0.0788  -0.1061 0.0508  84  THR B OG1 
2093 C CG2 . THR B 92  ? 0.9028 0.5659 0.7822 0.0896  -0.0961 0.0519  84  THR B CG2 
2094 N N   . VAL B 93  ? 0.6616 0.6149 0.6408 0.1785  0.0260  -0.0687 85  VAL B N   
2095 C CA  . VAL B 93  ? 0.7581 0.6698 0.7139 0.1671  0.0199  -0.0467 85  VAL B CA  
2096 C C   . VAL B 93  ? 0.7422 0.6502 0.7137 0.1381  0.0211  -0.0301 85  VAL B C   
2097 O O   . VAL B 93  ? 0.7051 0.5990 0.6554 0.1203  0.0252  -0.0149 85  VAL B O   
2098 C CB  . VAL B 93  ? 0.7908 0.6735 0.7430 0.1835  0.0063  -0.0441 85  VAL B CB  
2099 C CG1 . VAL B 93  ? 0.8314 0.6745 0.7664 0.1706  -0.0002 -0.0208 85  VAL B CG1 
2100 C CG2 . VAL B 93  ? 0.8114 0.6970 0.7456 0.2031  0.0042  -0.0559 85  VAL B CG2 
2101 N N   . ILE B 94  ? 0.7522 0.6697 0.7587 0.1329  0.0163  -0.0326 86  ILE B N   
2102 C CA  . ILE B 94  ? 0.7013 0.6075 0.7229 0.1069  0.0140  -0.0154 86  ILE B CA  
2103 C C   . ILE B 94  ? 0.7117 0.6428 0.7373 0.0845  0.0271  -0.0125 86  ILE B C   
2104 O O   . ILE B 94  ? 0.6900 0.6037 0.6954 0.0647  0.0299  0.0056  86  ILE B O   
2105 C CB  . ILE B 94  ? 0.7081 0.6156 0.7651 0.1088  0.0048  -0.0207 86  ILE B CB  
2106 C CG1 . ILE B 94  ? 0.7215 0.5989 0.7702 0.1277  -0.0062 -0.0192 86  ILE B CG1 
2107 C CG2 . ILE B 94  ? 0.7393 0.6392 0.8156 0.0813  0.0028  -0.0052 86  ILE B CG2 
2108 C CD1 . ILE B 94  ? 0.8032 0.6808 0.8804 0.1348  -0.0143 -0.0283 86  ILE B CD1 
2109 N N   . LYS B 95  ? 0.7333 0.7054 0.7848 0.0867  0.0351  -0.0297 87  LYS B N   
2110 C CA  . LYS B 95  ? 0.6846 0.6837 0.7449 0.0637  0.0493  -0.0265 87  LYS B CA  
2111 C C   . LYS B 95  ? 0.6733 0.6672 0.6933 0.0586  0.0617  -0.0195 87  LYS B C   
2112 O O   . LYS B 95  ? 0.7173 0.7047 0.7265 0.0329  0.0684  -0.0032 87  LYS B O   
2113 C CB  . LYS B 95  ? 0.6934 0.7412 0.7900 0.0703  0.0562  -0.0480 87  LYS B CB  
2114 C CG  . LYS B 95  ? 0.7537 0.8103 0.8931 0.0622  0.0464  -0.0512 87  LYS B CG  
2115 C CD  . LYS B 95  ? 0.7561 0.8625 0.9333 0.0676  0.0516  -0.0724 87  LYS B CD  
2116 C CE  . LYS B 95  ? 0.8104 0.9226 1.0285 0.0577  0.0401  -0.0754 87  LYS B CE  
2117 N NZ  . LYS B 95  ? 0.8387 0.9980 1.0959 0.0642  0.0414  -0.0966 87  LYS B NZ  
2118 N N   . PRO B 96  ? 0.6181 0.6124 0.6127 0.0811  0.0648  -0.0309 88  PRO B N   
2119 C CA  . PRO B 96  ? 0.6727 0.6555 0.6240 0.0757  0.0753  -0.0239 88  PRO B CA  
2120 C C   . PRO B 96  ? 0.7386 0.6750 0.6595 0.0590  0.0661  0.0011  88  PRO B C   
2121 O O   . PRO B 96  ? 0.8353 0.7642 0.7293 0.0397  0.0749  0.0132  88  PRO B O   
2122 C CB  . PRO B 96  ? 0.6054 0.5887 0.5380 0.1065  0.0744  -0.0410 88  PRO B CB  
2123 C CG  . PRO B 96  ? 0.6475 0.6645 0.6206 0.1240  0.0720  -0.0614 88  PRO B CG  
2124 C CD  . PRO B 96  ? 0.6920 0.7014 0.6966 0.1115  0.0604  -0.0525 88  PRO B CD  
2125 N N   . ALA B 97  ? 0.7920 0.6972 0.7168 0.0657  0.0485  0.0093  89  ALA B N   
2126 C CA  . ALA B 97  ? 0.7174 0.5793 0.6185 0.0508  0.0377  0.0333  89  ALA B CA  
2127 C C   . ALA B 97  ? 0.7343 0.5945 0.6463 0.0198  0.0395  0.0504  89  ALA B C   
2128 O O   . ALA B 97  ? 0.8139 0.6564 0.6948 0.0011  0.0423  0.0662  89  ALA B O   
2129 C CB  . ALA B 97  ? 0.8386 0.6735 0.7511 0.0644  0.0203  0.0375  89  ALA B CB  
2130 N N   . LEU B 98  ? 0.7777 0.6551 0.7320 0.0136  0.0375  0.0473  90  LEU B N   
2131 C CA  . LEU B 98  ? 0.7594 0.6357 0.7265 -0.0162 0.0389  0.0631  90  LEU B CA  
2132 C C   . LEU B 98  ? 0.7574 0.6553 0.7046 -0.0334 0.0579  0.0643  90  LEU B C   
2133 O O   . LEU B 98  ? 0.8631 0.7450 0.7944 -0.0597 0.0592  0.0840  90  LEU B O   
2134 C CB  . LEU B 98  ? 0.7677 0.6652 0.7843 -0.0181 0.0357  0.0544  90  LEU B CB  
2135 C CG  . LEU B 98  ? 0.7186 0.5986 0.7582 -0.0016 0.0192  0.0505  90  LEU B CG  
2136 C CD1 . LEU B 98  ? 0.6396 0.5472 0.7238 -0.0024 0.0188  0.0368  90  LEU B CD1 
2137 C CD2 . LEU B 98  ? 0.7142 0.5508 0.7483 -0.0134 0.0046  0.0735  90  LEU B CD2 
2138 N N   . ALA B 99  ? 0.7478 0.6824 0.6960 -0.0189 0.0731  0.0435  91  ALA B N   
2139 C CA  . ALA B 99  ? 0.7703 0.7301 0.7022 -0.0333 0.0945  0.0424  91  ALA B CA  
2140 C C   . ALA B 99  ? 0.7846 0.7124 0.6592 -0.0401 0.0971  0.0558  91  ALA B C   
2141 O O   . ALA B 99  ? 0.7769 0.7080 0.6298 -0.0627 0.1106  0.0660  91  ALA B O   
2142 C CB  . ALA B 99  ? 0.8426 0.8491 0.7919 -0.0126 0.1092  0.0155  91  ALA B CB  
2143 N N   . ARG B 100 ? 0.8737 0.7696 0.7221 -0.0220 0.0840  0.0564  92  ARG B N   
2144 C CA  . ARG B 100 ? 0.8244 0.6838 0.6181 -0.0284 0.0816  0.0700  92  ARG B CA  
2145 C C   . ARG B 100 ? 0.8495 0.6682 0.6321 -0.0527 0.0660  0.0982  92  ARG B C   
2146 O O   . ARG B 100 ? 0.9212 0.7054 0.6582 -0.0604 0.0603  0.1120  92  ARG B O   
2147 C CB  . ARG B 100 ? 0.8434 0.6829 0.6161 -0.0007 0.0715  0.0609  92  ARG B CB  
2148 C CG  . ARG B 100 ? 0.9300 0.8033 0.7067 0.0251  0.0847  0.0339  92  ARG B CG  
2149 C CD  . ARG B 100 ? 0.9354 0.7817 0.6789 0.0479  0.0754  0.0282  92  ARG B CD  
2150 N NE  . ARG B 100 ? 0.8354 0.6609 0.5978 0.0617  0.0556  0.0314  92  ARG B NE  
2151 C CZ  . ARG B 100 ? 0.8105 0.6538 0.5999 0.0857  0.0529  0.0141  92  ARG B CZ  
2152 N NH1 . ARG B 100 ? 0.6630 0.5464 0.4683 0.0992  0.0665  -0.0077 92  ARG B NH1 
2153 N NH2 . ARG B 100 ? 0.9935 0.8142 0.7943 0.0963  0.0361  0.0191  92  ARG B NH2 
2154 N N   . GLY B 101 ? 0.8096 0.6297 0.6321 -0.0645 0.0575  0.1067  93  GLY B N   
2155 C CA  . GLY B 101 ? 0.8538 0.6341 0.6717 -0.0842 0.0399  0.1325  93  GLY B CA  
2156 C C   . GLY B 101 ? 0.9056 0.6532 0.7296 -0.0689 0.0180  0.1382  93  GLY B C   
2157 O O   . GLY B 101 ? 0.8725 0.5852 0.6936 -0.0832 0.0016  0.1600  93  GLY B O   
2158 N N   . GLN B 102 ? 0.8984 0.6555 0.7302 -0.0405 0.0172  0.1201  94  GLN B N   
2159 C CA  . GLN B 102 ? 0.8944 0.6263 0.7394 -0.0251 -0.0011 0.1239  94  GLN B CA  
2160 C C   . GLN B 102 ? 0.7870 0.5270 0.6822 -0.0248 -0.0075 0.1225  94  GLN B C   
2161 O O   . GLN B 102 ? 0.7235 0.4974 0.6466 -0.0219 0.0025  0.1070  94  GLN B O   
2162 C CB  . GLN B 102 ? 0.9048 0.6445 0.7403 0.0044  0.0013  0.1050  94  GLN B CB  
2163 C CG  . GLN B 102 ? 0.9686 0.6951 0.7538 0.0084  0.0050  0.1043  94  GLN B CG  
2164 C CD  . GLN B 102 ? 0.9209 0.6582 0.7012 0.0382  0.0079  0.0836  94  GLN B CD  
2165 O OE1 . GLN B 102 ? 0.9446 0.7131 0.7537 0.0533  0.0150  0.0650  94  GLN B OE1 
2166 N NE2 . GLN B 102 ? 0.9544 0.6638 0.6981 0.0463  0.0005  0.0872  94  GLN B NE2 
2167 N N   . TRP B 103 ? 0.8058 0.5143 0.7133 -0.0276 -0.0249 0.1383  95  TRP B N   
2168 C CA  . TRP B 103 ? 0.8402 0.5521 0.7926 -0.0204 -0.0318 0.1338  95  TRP B CA  
2169 C C   . TRP B 103 ? 0.7978 0.5188 0.7590 0.0097  -0.0315 0.1153  95  TRP B C   
2170 O O   . TRP B 103 ? 0.8110 0.5253 0.7450 0.0236  -0.0311 0.1119  95  TRP B O   
2171 C CB  . TRP B 103 ? 0.8183 0.4952 0.7831 -0.0314 -0.0491 0.1554  95  TRP B CB  
2172 C CG  . TRP B 103 ? 0.7713 0.4463 0.7366 -0.0583 -0.0490 0.1684  95  TRP B CG  
2173 C CD1 . TRP B 103 ? 0.8140 0.4816 0.7462 -0.0807 -0.0446 0.1822  95  TRP B CD1 
2174 C CD2 . TRP B 103 ? 0.7262 0.4064 0.7211 -0.0652 -0.0528 0.1675  95  TRP B CD2 
2175 N NE1 . TRP B 103 ? 0.8021 0.4720 0.7462 -0.1000 -0.0453 0.1898  95  TRP B NE1 
2176 C CE2 . TRP B 103 ? 0.7280 0.4037 0.7101 -0.0904 -0.0516 0.1812  95  TRP B CE2 
2177 C CE3 . TRP B 103 ? 0.7726 0.4604 0.7987 -0.0525 -0.0569 0.1560  95  TRP B CE3 
2178 C CZ2 . TRP B 103 ? 0.7661 0.4427 0.7682 -0.1014 -0.0561 0.1838  95  TRP B CZ2 
2179 C CZ3 . TRP B 103 ? 0.7784 0.4663 0.8221 -0.0644 -0.0615 0.1591  95  TRP B CZ3 
2180 C CH2 . TRP B 103 ? 0.8145 0.4962 0.8473 -0.0878 -0.0618 0.1729  95  TRP B CH2 
2181 N N   . VAL B 104 ? 0.7209 0.4552 0.7186 0.0194  -0.0325 0.1035  96  VAL B N   
2182 C CA  . VAL B 104 ? 0.8333 0.5742 0.8388 0.0471  -0.0327 0.0867  96  VAL B CA  
2183 C C   . VAL B 104 ? 0.7393 0.4624 0.7751 0.0522  -0.0433 0.0910  96  VAL B C   
2184 O O   . VAL B 104 ? 0.6997 0.4248 0.7631 0.0406  -0.0460 0.0927  96  VAL B O   
2185 C CB  . VAL B 104 ? 0.8166 0.5962 0.8324 0.0587  -0.0213 0.0622  96  VAL B CB  
2186 C CG1 . VAL B 104 ? 0.8183 0.6007 0.8345 0.0874  -0.0229 0.0463  96  VAL B CG1 
2187 C CG2 . VAL B 104 ? 0.7844 0.5838 0.7745 0.0519  -0.0089 0.0583  96  VAL B CG2 
2188 N N   . ILE B 105 ? 0.7756 0.5015 0.7954 0.0660  -0.0393 0.0856  97  ILE B N   
2189 C CA  . ILE B 105 ? 0.8150 0.5513 0.8425 0.0708  -0.0354 0.0777  97  ILE B CA  
2190 C C   . ILE B 105 ? 0.7673 0.5198 0.7930 0.0921  -0.0270 0.0622  97  ILE B C   
2191 O O   . ILE B 105 ? 0.7710 0.5377 0.7917 0.0985  -0.0188 0.0624  97  ILE B O   
2192 C CB  . ILE B 105 ? 0.8410 0.5758 0.8520 0.0652  -0.0316 0.0848  97  ILE B CB  
2193 C CG1 . ILE B 105 ? 0.7821 0.5053 0.7853 0.0473  -0.0365 0.1000  97  ILE B CG1 
2194 C CG2 . ILE B 105 ? 0.8499 0.5891 0.8737 0.0641  -0.0324 0.0804  97  ILE B CG2 
2195 C CD1 . ILE B 105 ? 0.8353 0.5517 0.8564 0.0292  -0.0444 0.1079  97  ILE B CD1 
2196 N N   . GLY B 106 ? 0.8149 0.5760 0.8583 0.0978  -0.0278 0.0505  98  GLY B N   
2197 C CA  . GLY B 106 ? 0.9411 0.7218 0.9854 0.1139  -0.0175 0.0379  98  GLY B CA  
2198 C C   . GLY B 106 ? 0.9140 0.7011 0.9541 0.1144  -0.0111 0.0357  98  GLY B C   
2199 O O   . GLY B 106 ? 0.7410 0.5141 0.7827 0.1078  -0.0176 0.0389  98  GLY B O   
2200 N N   . ASP B 107 ? 1.0754 0.8874 1.1249 0.1171  0.0006  0.0317  99  ASP B N   
2201 C CA  . ASP B 107 ? 1.1434 0.9545 1.1946 0.1202  0.0012  0.0288  99  ASP B CA  
2202 C C   . ASP B 107 ? 1.1200 0.9428 1.1867 0.1264  0.0021  0.0157  99  ASP B C   
2203 O O   . ASP B 107 ? 1.1183 0.9536 1.1920 0.1295  -0.0008 0.0071  99  ASP B O   
2204 C CB  . ASP B 107 ? 1.1282 0.9479 1.1878 0.1161  0.0023  0.0347  99  ASP B CB  
2205 C CG  . ASP B 107 ? 1.2177 1.0319 1.2724 0.1198  0.0054  0.0347  99  ASP B CG  
2206 O OD1 . ASP B 107 ? 1.3097 1.1226 1.3682 0.1250  0.0064  0.0270  99  ASP B OD1 
2207 O OD2 . ASP B 107 ? 1.2471 1.0559 1.2903 0.1189  0.0062  0.0415  99  ASP B OD2 
2208 N N   . ARG B 108 ? 1.1492 0.9622 1.2136 0.1304  0.0009  0.0108  100 ARG B N   
2209 C CA  . ARG B 108 ? 1.2624 1.0818 1.3363 0.1372  0.0012  -0.0020 100 ARG B CA  
2210 C C   . ARG B 108 ? 1.3061 1.1374 1.3841 0.1398  -0.0022 -0.0134 100 ARG B C   
2211 O O   . ARG B 108 ? 1.4055 1.2495 1.4816 0.1442  -0.0053 -0.0246 100 ARG B O   
2212 C CB  . ARG B 108 ? 1.2469 1.0746 1.3233 0.1389  0.0016  -0.0052 100 ARG B CB  
2213 C CG  . ARG B 108 ? 1.2305 1.0600 1.3043 0.1451  -0.0010 -0.0182 100 ARG B CG  
2214 C CD  . ARG B 108 ? 1.2169 1.0452 1.2878 0.1468  -0.0001 -0.0175 100 ARG B CD  
2215 N NE  . ARG B 108 ? 1.1189 0.9535 1.1758 0.1464  -0.0046 -0.0165 100 ARG B NE  
2216 C CZ  . ARG B 108 ? 1.0366 0.8698 1.0987 0.1407  -0.0040 -0.0057 100 ARG B CZ  
2217 N NH1 . ARG B 108 ? 1.0892 0.9184 1.1704 0.1334  0.0008  0.0060  100 ARG B NH1 
2218 N NH2 . ARG B 108 ? 0.9840 0.8198 1.0243 0.1422  -0.0084 -0.0063 100 ARG B NH2 
2219 N N   . HIS B 109 ? 1.4189 1.2434 1.5035 0.1388  -0.0120 -0.0166 101 HIS B N   
2220 C CA  . HIS B 109 ? 1.5316 1.3679 1.6309 0.1435  -0.0227 -0.0336 101 HIS B CA  
2221 C C   . HIS B 109 ? 1.5348 1.3741 1.6437 0.1461  -0.0282 -0.0471 101 HIS B C   
2222 O O   . HIS B 109 ? 1.5184 1.3495 1.6487 0.1408  -0.0374 -0.0512 101 HIS B O   
2223 C CB  . HIS B 109 ? 1.6246 1.4542 1.7469 0.1371  -0.0334 -0.0329 101 HIS B CB  
2224 C CG  . HIS B 109 ? 1.7601 1.6085 1.9037 0.1430  -0.0396 -0.0495 101 HIS B CG  
2225 N ND1 . HIS B 109 ? 1.7784 1.6408 1.9085 0.1517  -0.0351 -0.0531 101 HIS B ND1 
2226 C CD2 . HIS B 109 ? 1.8265 1.6855 2.0086 0.1411  -0.0487 -0.0645 101 HIS B CD2 
2227 C CE1 . HIS B 109 ? 1.7360 1.6210 1.8932 0.1569  -0.0397 -0.0709 101 HIS B CE1 
2228 N NE2 . HIS B 109 ? 1.8006 1.6880 1.9876 0.1460  -0.0458 -0.0756 101 HIS B NE2 
2229 N N   . GLN B 125 ? 1.8084 1.6616 1.9225 0.2153  -0.1717 -0.2418 117 GLN B N   
2230 C CA  . GLN B 125 ? 2.2580 2.1124 2.3773 0.2060  -0.1515 -0.2221 117 GLN B CA  
2231 C C   . GLN B 125 ? 2.1445 2.0102 2.3104 0.1965  -0.1582 -0.2279 117 GLN B C   
2232 O O   . GLN B 125 ? 1.6853 1.5601 1.8608 0.1909  -0.1468 -0.2159 117 GLN B O   
2233 C CB  . GLN B 125 ? 1.7358 1.5650 1.8368 0.2015  -0.1333 -0.2064 117 GLN B CB  
2234 N N   . THR B 126 ? 1.8027 1.6663 1.9993 0.1939  -0.1771 -0.2464 118 THR B N   
2235 C CA  . THR B 126 ? 1.8294 1.7064 2.0788 0.1839  -0.1860 -0.2552 118 THR B CA  
2236 C C   . THR B 126 ? 1.7228 1.6337 1.9887 0.1891  -0.1882 -0.2622 118 THR B C   
2237 O O   . THR B 126 ? 1.6287 1.5552 1.9341 0.1815  -0.1854 -0.2627 118 THR B O   
2238 C CB  . THR B 126 ? 1.8902 1.7592 2.1713 0.1792  -0.2082 -0.2758 118 THR B CB  
2239 O OG1 . THR B 126 ? 1.8490 1.6867 2.1138 0.1747  -0.2044 -0.2685 118 THR B OG1 
2240 C CG2 . THR B 126 ? 1.8476 1.7291 2.1905 0.1652  -0.2168 -0.2854 118 THR B CG2 
2241 N N   . MET B 127 ? 1.6663 1.5890 1.9038 0.2021  -0.1925 -0.2672 119 MET B N   
2242 C CA  . MET B 127 ? 1.5829 1.5386 1.8325 0.2085  -0.1943 -0.2735 119 MET B CA  
2243 C C   . MET B 127 ? 1.5572 1.5185 1.7893 0.2059  -0.1719 -0.2521 119 MET B C   
2244 O O   . MET B 127 ? 1.4870 1.4768 1.7394 0.2076  -0.1693 -0.2554 119 MET B O   
2245 C CB  . MET B 127 ? 1.6081 1.5694 1.8291 0.2226  -0.2074 -0.2834 119 MET B CB  
2246 C CG  . MET B 127 ? 1.6029 1.5610 1.8414 0.2271  -0.2334 -0.3071 119 MET B CG  
2247 S SD  . MET B 127 ? 1.6862 1.6028 1.9001 0.2234  -0.2349 -0.3035 119 MET B SD  
2248 C CE  . MET B 127 ? 1.5928 1.4967 1.7459 0.2392  -0.2369 -0.2997 119 MET B CE  
2249 N N   . LEU B 128 ? 1.6561 1.5921 1.8532 0.2021  -0.1553 -0.2307 120 LEU B N   
2250 C CA  . LEU B 128 ? 1.4996 1.4373 1.6841 0.1980  -0.1358 -0.2107 120 LEU B CA  
2251 C C   . LEU B 128 ? 1.5351 1.4849 1.7639 0.1893  -0.1333 -0.2117 120 LEU B C   
2252 O O   . LEU B 128 ? 1.4997 1.4683 1.7341 0.1898  -0.1245 -0.2067 120 LEU B O   
2253 C CB  . LEU B 128 ? 1.6268 1.5361 1.7772 0.1940  -0.1201 -0.1899 120 LEU B CB  
2254 C CG  . LEU B 128 ? 1.5000 1.4020 1.6066 0.1998  -0.1112 -0.1790 120 LEU B CG  
2255 C CD1 . LEU B 128 ? 1.4289 1.3392 1.5238 0.1979  -0.0974 -0.1638 120 LEU B CD1 
2256 C CD2 . LEU B 128 ? 1.3838 1.2942 1.4789 0.2108  -0.1272 -0.1949 120 LEU B CD2 
2257 N N   . ALA B 129 ? 1.4625 1.4003 1.7243 0.1805  -0.1410 -0.2179 121 ALA B N   
2258 C CA  . ALA B 129 ? 1.3501 1.2953 1.6597 0.1698  -0.1388 -0.2172 121 ALA B CA  
2259 C C   . ALA B 129 ? 1.4832 1.4710 1.8367 0.1671  -0.1452 -0.2323 121 ALA B C   
2260 O O   . ALA B 129 ? 1.3230 1.3349 1.6941 0.1494  -0.1332 -0.2190 121 ALA B O   
2261 C CB  . ALA B 129 ? 1.3553 1.2714 1.6875 0.1570  -0.1458 -0.2166 121 ALA B CB  
2262 N N   . THR B 130 ? 1.6854 1.6877 2.0482 0.1767  -0.1612 -0.2533 122 THR B N   
2263 C CA  . THR B 130 ? 1.7677 1.8186 2.1681 0.1663  -0.1651 -0.2611 122 THR B CA  
2264 C C   . THR B 130 ? 1.5766 1.6592 1.9707 0.1761  -0.1516 -0.2572 122 THR B C   
2265 O O   . THR B 130 ? 1.6018 1.7250 2.0277 0.1611  -0.1443 -0.2544 122 THR B O   
2266 C CB  . THR B 130 ? 1.9705 2.0278 2.3807 0.1768  -0.1879 -0.2849 122 THR B CB  
2267 O OG1 . THR B 130 ? 1.4481 1.4901 1.8136 0.2031  -0.1921 -0.2920 122 THR B OG1 
2268 C CG2 . THR B 130 ? 1.6082 1.6342 2.0264 0.1652  -0.2018 -0.2899 122 THR B CG2 
2269 N N   . LEU B 131 ? 1.5382 1.6023 1.8861 0.1966  -0.1467 -0.2541 123 LEU B N   
2270 C CA  . LEU B 131 ? 1.5256 1.6111 1.8573 0.2007  -0.1320 -0.2451 123 LEU B CA  
2271 C C   . LEU B 131 ? 1.4604 1.5503 1.8076 0.1891  -0.1147 -0.2302 123 LEU B C   
2272 O O   . LEU B 131 ? 1.4253 1.5502 1.7880 0.1818  -0.1034 -0.2268 123 LEU B O   
2273 C CB  . LEU B 131 ? 1.3777 1.4356 1.6418 0.2079  -0.1271 -0.2309 123 LEU B CB  
2274 C CG  . LEU B 131 ? 1.2980 1.3561 1.5387 0.2184  -0.1413 -0.2413 123 LEU B CG  
2275 C CD1 . LEU B 131 ? 1.4295 1.4603 1.6118 0.2212  -0.1330 -0.2228 123 LEU B CD1 
2276 C CD2 . LEU B 131 ? 1.0387 1.1370 1.3051 0.2252  -0.1468 -0.2560 123 LEU B CD2 
2277 N N   . ARG B 132 ? 1.2096 1.2619 1.5420 0.1801  -0.1106 -0.2154 124 ARG B N   
2278 C CA  . ARG B 132 ? 1.1907 1.2400 1.5234 0.1600  -0.0947 -0.1936 124 ARG B CA  
2279 C C   . ARG B 132 ? 1.1358 1.2205 1.5088 0.1329  -0.0904 -0.1905 124 ARG B C   
2280 O O   . ARG B 132 ? 1.1657 1.2744 1.5417 0.1233  -0.0756 -0.1813 124 ARG B O   
2281 C CB  . ARG B 132 ? 1.1894 1.1931 1.5080 0.1539  -0.0954 -0.1802 124 ARG B CB  
2282 C CG  . ARG B 132 ? 1.1935 1.1881 1.5100 0.1331  -0.0823 -0.1563 124 ARG B CG  
2283 C CD  . ARG B 132 ? 1.3352 1.2842 1.6393 0.1308  -0.0846 -0.1437 124 ARG B CD  
2284 N NE  . ARG B 132 ? 1.4802 1.4183 1.7777 0.1138  -0.0739 -0.1201 124 ARG B NE  
2285 C CZ  . ARG B 132 ? 1.5481 1.4715 1.8166 0.1231  -0.0658 -0.1083 124 ARG B CZ  
2286 N NH1 . ARG B 132 ? 1.5030 1.4192 1.7461 0.1489  -0.0661 -0.1166 124 ARG B NH1 
2287 N NH2 . ARG B 132 ? 1.3820 1.2962 1.6456 0.1053  -0.0584 -0.0871 124 ARG B NH2 
2288 N N   . ASP B 133 ? 1.2914 1.3800 1.6950 0.1202  -0.1031 -0.1987 125 ASP B N   
2289 C CA  . ASP B 133 ? 1.2031 1.3246 1.6478 0.0922  -0.0994 -0.1948 125 ASP B CA  
2290 C C   . ASP B 133 ? 1.1258 1.3005 1.5923 0.0959  -0.0936 -0.2054 125 ASP B C   
2291 O O   . ASP B 133 ? 1.0873 1.2947 1.5838 0.0731  -0.0835 -0.1990 125 ASP B O   
2292 C CB  . ASP B 133 ? 1.1960 1.3084 1.6691 0.0795  -0.1171 -0.2033 125 ASP B CB  
2293 C CG  . ASP B 133 ? 1.1403 1.2008 1.5962 0.0754  -0.1224 -0.1935 125 ASP B CG  
2294 O OD1 . ASP B 133 ? 1.1581 1.1969 1.5934 0.0703  -0.1104 -0.1743 125 ASP B OD1 
2295 O OD2 . ASP B 133 ? 1.2317 1.2725 1.6951 0.0778  -0.1393 -0.2055 125 ASP B OD2 
2296 N N   . ALA B 134 ? 1.3759 1.5597 1.8285 0.1240  -0.0994 -0.2213 126 ALA B N   
2297 C CA  . ALA B 134 ? 1.4639 1.6976 1.9383 0.1315  -0.0951 -0.2330 126 ALA B CA  
2298 C C   . ALA B 134 ? 1.4448 1.6887 1.8965 0.1372  -0.0742 -0.2230 126 ALA B C   
2299 O O   . ALA B 134 ? 1.8556 2.1400 2.3311 0.1257  -0.0602 -0.2214 126 ALA B O   
2300 C CB  . ALA B 134 ? 1.1670 1.4040 1.6370 0.1598  -0.1139 -0.2551 126 ALA B CB  
2301 N N   . VAL B 135 ? 1.1862 1.3933 1.5920 0.1543  -0.0716 -0.2163 127 VAL B N   
2302 C CA  . VAL B 135 ? 1.1411 1.3534 1.5207 0.1640  -0.0553 -0.2096 127 VAL B CA  
2303 C C   . VAL B 135 ? 1.0840 1.2798 1.4492 0.1417  -0.0389 -0.1865 127 VAL B C   
2304 O O   . VAL B 135 ? 0.9576 1.1771 1.3235 0.1335  -0.0221 -0.1806 127 VAL B O   
2305 C CB  . VAL B 135 ? 1.1404 1.3227 1.4785 0.1948  -0.0626 -0.2150 127 VAL B CB  
2306 C CG1 . VAL B 135 ? 1.1099 1.3009 1.4468 0.2082  -0.0788 -0.2307 127 VAL B CG1 
2307 C CG2 . VAL B 135 ? 1.2197 1.3502 1.5288 0.1942  -0.0674 -0.2031 127 VAL B CG2 
2308 N N   . LEU B 136 ? 1.0563 1.4914 1.4070 -0.0923 -0.1805 0.0492  128 LEU B N   
2309 C CA  . LEU B 136 ? 1.0588 1.4855 1.4055 -0.0822 -0.1508 0.0560  128 LEU B CA  
2310 C C   . LEU B 136 ? 0.8863 1.3363 1.2726 -0.0958 -0.1293 0.0632  128 LEU B C   
2311 O O   . LEU B 136 ? 0.8581 1.3107 1.2486 -0.0833 -0.1056 0.0710  128 LEU B O   
2312 C CB  . LEU B 136 ? 1.0878 1.4602 1.3858 -0.0890 -0.1440 0.0495  128 LEU B CB  
2313 C CG  . LEU B 136 ? 1.0250 1.3679 1.2782 -0.0785 -0.1604 0.0432  128 LEU B CG  
2314 C CD1 . LEU B 136 ? 1.0954 1.3914 1.3096 -0.0872 -0.1489 0.0368  128 LEU B CD1 
2315 C CD2 . LEU B 136 ? 1.2243 1.5829 1.4768 -0.0474 -0.1622 0.0497  128 LEU B CD2 
2316 N N   . GLY B 137 ? 0.8651 1.3277 1.2771 -0.1219 -0.1380 0.0609  129 GLY B N   
2317 C CA  . GLY B 137 ? 0.7854 1.2677 1.2336 -0.1380 -0.1183 0.0683  129 GLY B CA  
2318 C C   . GLY B 137 ? 0.8448 1.2824 1.2628 -0.1464 -0.0973 0.0682  129 GLY B C   
2319 O O   . GLY B 137 ? 0.9354 1.3285 1.3143 -0.1554 -0.1032 0.0590  129 GLY B O   
2320 N N   . ASP B 138 ? 0.7865 1.2350 1.2215 -0.1425 -0.0719 0.0782  130 ASP B N   
2321 C CA  . ASP B 138 ? 0.8134 1.2198 1.2228 -0.1500 -0.0530 0.0785  130 ASP B CA  
2322 C C   . ASP B 138 ? 0.7736 1.1460 1.1430 -0.1256 -0.0452 0.0763  130 ASP B C   
2323 O O   . ASP B 138 ? 0.8123 1.1488 1.1601 -0.1275 -0.0311 0.0756  130 ASP B O   
2324 C CB  . ASP B 138 ? 0.7355 1.1609 1.1742 -0.1573 -0.0299 0.0906  130 ASP B CB  
2325 C CG  . ASP B 138 ? 0.7001 1.1587 1.1555 -0.1307 -0.0151 0.1010  130 ASP B CG  
2326 O OD1 . ASP B 138 ? 0.7609 1.2256 1.2041 -0.1056 -0.0245 0.0986  130 ASP B OD1 
2327 O OD2 . ASP B 138 ? 0.7585 1.2342 1.2360 -0.1351 0.0063  0.1117  130 ASP B OD2 
2328 N N   . PHE B 139 ? 0.7336 1.1153 1.0930 -0.1028 -0.0557 0.0751  131 PHE B N   
2329 C CA  . PHE B 139 ? 0.7639 1.1146 1.0876 -0.0808 -0.0508 0.0733  131 PHE B CA  
2330 C C   . PHE B 139 ? 0.7178 1.0236 1.0079 -0.0928 -0.0547 0.0618  131 PHE B C   
2331 O O   . PHE B 139 ? 0.8067 1.1050 1.0862 -0.1064 -0.0709 0.0530  131 PHE B O   
2332 C CB  . PHE B 139 ? 0.8486 1.2155 1.1659 -0.0574 -0.0655 0.0736  131 PHE B CB  
2333 C CG  . PHE B 139 ? 0.8042 1.1398 1.0860 -0.0360 -0.0636 0.0723  131 PHE B CG  
2334 C CD1 . PHE B 139 ? 0.8406 1.1776 1.1202 -0.0117 -0.0506 0.0810  131 PHE B CD1 
2335 C CD2 . PHE B 139 ? 0.8466 1.1504 1.0968 -0.0408 -0.0748 0.0623  131 PHE B CD2 
2336 C CE1 . PHE B 139 ? 0.7998 1.1066 1.0478 0.0073  -0.0519 0.0797  131 PHE B CE1 
2337 C CE2 . PHE B 139 ? 0.9096 1.1876 1.1322 -0.0232 -0.0737 0.0613  131 PHE B CE2 
2338 C CZ  . PHE B 139 ? 0.8278 1.1071 1.0502 0.0009  -0.0639 0.0699  131 PHE B CZ  
2339 N N   . ARG B 140 ? 0.7030 0.9779 0.9755 -0.0865 -0.0396 0.0614  132 ARG B N   
2340 C CA  . ARG B 140 ? 0.7107 0.9452 0.9550 -0.0936 -0.0394 0.0500  132 ARG B CA  
2341 C C   . ARG B 140 ? 0.7338 0.9464 0.9606 -0.0711 -0.0303 0.0507  132 ARG B C   
2342 O O   . ARG B 140 ? 0.7237 0.9416 0.9574 -0.0557 -0.0199 0.0604  132 ARG B O   
2343 C CB  . ARG B 140 ? 0.7213 0.9358 0.9672 -0.1161 -0.0312 0.0463  132 ARG B CB  
2344 C CG  . ARG B 140 ? 0.7786 1.0108 1.0430 -0.1410 -0.0409 0.0462  132 ARG B CG  
2345 C CD  . ARG B 140 ? 0.8833 1.1015 1.1277 -0.1538 -0.0579 0.0341  132 ARG B CD  
2346 N NE  . ARG B 140 ? 0.9272 1.1551 1.1863 -0.1786 -0.0696 0.0332  132 ARG B NE  
2347 C CZ  . ARG B 140 ? 1.0383 1.3023 1.3224 -0.1822 -0.0848 0.0376  132 ARG B CZ  
2348 N NH1 . ARG B 140 ? 1.0276 1.3206 1.3220 -0.1617 -0.0899 0.0428  132 ARG B NH1 
2349 N NH2 . ARG B 140 ? 1.0257 1.2961 1.3251 -0.2064 -0.0966 0.0363  132 ARG B NH2 
2350 N N   . PRO B 141 ? 0.7282 0.9147 0.9323 -0.0693 -0.0336 0.0405  133 PRO B N   
2351 C CA  . PRO B 141 ? 0.6324 0.7966 0.8246 -0.0502 -0.0261 0.0400  133 PRO B CA  
2352 C C   . PRO B 141 ? 0.5468 0.6920 0.7428 -0.0521 -0.0118 0.0416  133 PRO B C   
2353 O O   . PRO B 141 ? 0.5891 0.7274 0.7893 -0.0718 -0.0079 0.0382  133 PRO B O   
2354 C CB  . PRO B 141 ? 0.6585 0.8022 0.8323 -0.0553 -0.0307 0.0269  133 PRO B CB  
2355 C CG  . PRO B 141 ? 0.7450 0.9002 0.9139 -0.0723 -0.0425 0.0228  133 PRO B CG  
2356 C CD  . PRO B 141 ? 0.7095 0.8829 0.8976 -0.0860 -0.0426 0.0284  133 PRO B CD  
2357 N N   . HIS B 142 ? 0.5954 0.7280 0.7863 -0.0311 -0.0058 0.0471  134 HIS B N   
2358 C CA  . HIS B 142 ? 0.6056 0.7126 0.7935 -0.0309 0.0060  0.0486  134 HIS B CA  
2359 C C   . HIS B 142 ? 0.5691 0.6454 0.7474 -0.0372 0.0068  0.0343  134 HIS B C   
2360 O O   . HIS B 142 ? 0.5577 0.6144 0.7340 -0.0491 0.0134  0.0314  134 HIS B O   
2361 C CB  . HIS B 142 ? 0.6118 0.7077 0.7909 -0.0053 0.0099  0.0577  134 HIS B CB  
2362 C CG  . HIS B 142 ? 0.5608 0.6850 0.7483 0.0020  0.0134  0.0716  134 HIS B CG  
2363 N ND1 . HIS B 142 ? 0.6206 0.7745 0.8139 0.0091  0.0036  0.0741  134 HIS B ND1 
2364 C CD2 . HIS B 142 ? 0.7130 0.8412 0.9045 0.0025  0.0265  0.0832  134 HIS B CD2 
2365 C CE1 . HIS B 142 ? 0.8058 0.9830 1.0089 0.0162  0.0105  0.0860  134 HIS B CE1 
2366 N NE2 . HIS B 142 ? 0.8970 1.0605 1.0999 0.0116  0.0259  0.0920  134 HIS B NE2 
2367 N N   . LEU B 143 ? 0.6023 0.6742 0.7750 -0.0295 0.0005  0.0253  135 LEU B N   
2368 C CA  . LEU B 143 ? 0.6131 0.6624 0.7808 -0.0342 0.0026  0.0102  135 LEU B CA  
2369 C C   . LEU B 143 ? 0.6005 0.6624 0.7648 -0.0433 -0.0034 0.0019  135 LEU B C   
2370 O O   . LEU B 143 ? 0.5842 0.6608 0.7469 -0.0343 -0.0110 0.0063  135 LEU B O   
2371 C CB  . LEU B 143 ? 0.6587 0.6858 0.8242 -0.0125 0.0030  0.0070  135 LEU B CB  
2372 C CG  . LEU B 143 ? 0.6573 0.6676 0.8243 -0.0141 0.0053  -0.0101 135 LEU B CG  
2373 C CD1 . LEU B 143 ? 0.6843 0.6740 0.8471 -0.0277 0.0125  -0.0178 135 LEU B CD1 
2374 C CD2 . LEU B 143 ? 0.7364 0.7312 0.9073 0.0092  0.0016  -0.0127 135 LEU B CD2 
2375 N N   . THR B 144 ? 0.6924 0.7446 0.8512 -0.0611 -0.0001 -0.0098 136 THR B N   
2376 C CA  . THR B 144 ? 0.6986 0.7525 0.8479 -0.0699 -0.0020 -0.0202 136 THR B CA  
2377 C C   . THR B 144 ? 0.6774 0.7113 0.8274 -0.0648 0.0070  -0.0345 136 THR B C   
2378 O O   . THR B 144 ? 0.6411 0.6556 0.7919 -0.0662 0.0137  -0.0407 136 THR B O   
2379 C CB  . THR B 144 ? 0.7293 0.7844 0.8676 -0.0934 -0.0051 -0.0238 136 THR B CB  
2380 O OG1 . THR B 144 ? 0.7365 0.8100 0.8836 -0.0982 -0.0120 -0.0111 136 THR B OG1 
2381 C CG2 . THR B 144 ? 0.8301 0.8894 0.9524 -0.1008 -0.0105 -0.0293 136 THR B CG2 
2382 N N   . LEU B 145 ? 0.7575 0.7961 0.9084 -0.0584 0.0068  -0.0397 137 LEU B N   
2383 C CA  . LEU B 145 ? 0.7730 0.8001 0.9318 -0.0525 0.0159  -0.0540 137 LEU B CA  
2384 C C   . LEU B 145 ? 0.8056 0.8327 0.9508 -0.0698 0.0226  -0.0654 137 LEU B C   
2385 O O   . LEU B 145 ? 0.7757 0.8136 0.9145 -0.0731 0.0192  -0.0636 137 LEU B O   
2386 C CB  . LEU B 145 ? 0.8018 0.8347 0.9755 -0.0327 0.0109  -0.0509 137 LEU B CB  
2387 C CG  . LEU B 145 ? 0.9113 0.9401 1.1010 -0.0268 0.0188  -0.0660 137 LEU B CG  
2388 C CD1 . LEU B 145 ? 0.9996 1.0090 1.1972 -0.0206 0.0258  -0.0760 137 LEU B CD1 
2389 C CD2 . LEU B 145 ? 0.9477 0.9832 1.1526 -0.0092 0.0096  -0.0614 137 LEU B CD2 
2390 N N   . TYR B 146 ? 0.8519 0.8628 0.9881 -0.0809 0.0320  -0.0770 138 TYR B N   
2391 C CA  . TYR B 146 ? 0.9075 0.9120 1.0239 -0.0976 0.0405  -0.0887 138 TYR B CA  
2392 C C   . TYR B 146 ? 0.9121 0.9165 1.0423 -0.0902 0.0549  -0.1032 138 TYR B C   
2393 O O   . TYR B 146 ? 0.8538 0.8496 1.0007 -0.0782 0.0614  -0.1120 138 TYR B O   
2394 C CB  . TYR B 146 ? 0.8715 0.8551 0.9678 -0.1126 0.0429  -0.0946 138 TYR B CB  
2395 C CG  . TYR B 146 ? 0.9967 0.9659 1.0665 -0.1281 0.0534  -0.1082 138 TYR B CG  
2396 C CD1 . TYR B 146 ? 1.0433 1.0188 1.0949 -0.1383 0.0519  -0.1067 138 TYR B CD1 
2397 C CD2 . TYR B 146 ? 1.0088 0.9535 1.0666 -0.1322 0.0646  -0.1228 138 TYR B CD2 
2398 C CE1 . TYR B 146 ? 1.1402 1.0977 1.1614 -0.1530 0.0629  -0.1188 138 TYR B CE1 
2399 C CE2 . TYR B 146 ? 1.1077 1.0358 1.1363 -0.1454 0.0759  -0.1356 138 TYR B CE2 
2400 C CZ  . TYR B 146 ? 1.1754 1.1097 1.1851 -0.1563 0.0758  -0.1333 138 TYR B CZ  
2401 O OH  . TYR B 146 ? 1.1660 1.0791 1.1407 -0.1700 0.0885  -0.1456 138 TYR B OH  
2402 N N   . LEU B 147 ? 0.9925 1.0061 1.1163 -0.0973 0.0595  -0.1060 139 LEU B N   
2403 C CA  . LEU B 147 ? 0.9898 1.0082 1.1285 -0.0945 0.0759  -0.1202 139 LEU B CA  
2404 C C   . LEU B 147 ? 1.0049 1.0073 1.1146 -0.1125 0.0918  -0.1334 139 LEU B C   
2405 O O   . LEU B 147 ? 1.0955 1.0932 1.1747 -0.1293 0.0911  -0.1304 139 LEU B O   
2406 C CB  . LEU B 147 ? 1.0297 1.0666 1.1787 -0.0930 0.0721  -0.1141 139 LEU B CB  
2407 C CG  . LEU B 147 ? 0.8874 0.9360 1.0609 -0.0738 0.0557  -0.1018 139 LEU B CG  
2408 C CD1 . LEU B 147 ? 0.8525 0.9142 1.0295 -0.0749 0.0498  -0.0957 139 LEU B CD1 
2409 C CD2 . LEU B 147 ? 0.9868 1.0349 1.1941 -0.0544 0.0590  -0.1100 139 LEU B CD2 
2410 N N   . ASP B 148 ? 1.0922 1.0820 1.2070 -0.1080 0.1052  -0.1483 140 ASP B N   
2411 C CA  . ASP B 148 ? 1.0390 1.0073 1.1213 -0.1228 0.1204  -0.1616 140 ASP B CA  
2412 C C   . ASP B 148 ? 1.1507 1.1289 1.2407 -0.1249 0.1436  -0.1756 140 ASP B C   
2413 O O   . ASP B 148 ? 1.1932 1.1859 1.3211 -0.1094 0.1540  -0.1859 140 ASP B O   
2414 C CB  . ASP B 148 ? 1.1423 1.0874 1.2210 -0.1165 0.1226  -0.1710 140 ASP B CB  
2415 C CG  . ASP B 148 ? 1.2948 1.2131 1.3369 -0.1292 0.1384  -0.1862 140 ASP B CG  
2416 O OD1 . ASP B 148 ? 1.3016 1.1994 1.3042 -0.1465 0.1301  -0.1814 140 ASP B OD1 
2417 O OD2 . ASP B 148 ? 1.3877 1.3051 1.4405 -0.1210 0.1585  -0.2035 140 ASP B OD2 
2418 N N   . VAL B 149 ? 1.3154 1.2853 1.3699 -0.1443 0.1515  -0.1763 141 VAL B N   
2419 C CA  . VAL B 149 ? 1.4070 1.3798 1.4580 -0.1513 0.1785  -0.1908 141 VAL B CA  
2420 C C   . VAL B 149 ? 1.5358 1.4731 1.5299 -0.1689 0.1892  -0.1990 141 VAL B C   
2421 O O   . VAL B 149 ? 1.4923 1.4082 1.4470 -0.1815 0.1718  -0.1892 141 VAL B O   
2422 C CB  . VAL B 149 ? 1.5335 1.5270 1.5914 -0.1599 0.1804  -0.1832 141 VAL B CB  
2423 C CG1 . VAL B 149 ? 1.4218 1.4488 1.5388 -0.1417 0.1756  -0.1805 141 VAL B CG1 
2424 C CG2 . VAL B 149 ? 1.4785 1.4604 1.4997 -0.1728 0.1578  -0.1657 141 VAL B CG2 
2425 N N   . THR B 150 ? 1.6600 1.5899 1.6499 -0.1685 0.2168  -0.2177 142 THR B N   
2426 C CA  . THR B 150 ? 1.5995 1.4919 1.5291 -0.1855 0.2299  -0.2265 142 THR B CA  
2427 C C   . THR B 150 ? 1.6773 1.5646 1.5714 -0.2066 0.2322  -0.2184 142 THR B C   
2428 O O   . THR B 150 ? 1.7559 1.6716 1.6776 -0.2076 0.2413  -0.2157 142 THR B O   
2429 C CB  . THR B 150 ? 1.5128 1.4010 1.4470 -0.1784 0.2625  -0.2490 142 THR B CB  
2430 O OG1 . THR B 150 ? 1.6188 1.5277 1.5625 -0.1863 0.2885  -0.2544 142 THR B OG1 
2431 C CG2 . THR B 150 ? 1.2648 1.1729 1.2547 -0.1526 0.2619  -0.2573 142 THR B CG2 
2432 N N   . PRO B 151 ? 1.5748 1.4236 1.4062 -0.2241 0.2226  -0.2147 143 PRO B N   
2433 C CA  . PRO B 151 ? 1.6326 1.4711 1.4252 -0.2436 0.2208  -0.2060 143 PRO B CA  
2434 C C   . PRO B 151 ? 1.6552 1.5035 1.4491 -0.2513 0.2551  -0.2158 143 PRO B C   
2435 O O   . PRO B 151 ? 1.6774 1.5305 1.4601 -0.2640 0.2541  -0.2067 143 PRO B O   
2436 C CB  . PRO B 151 ? 1.6532 1.4403 1.3740 -0.2591 0.2096  -0.2067 143 PRO B CB  
2437 C CG  . PRO B 151 ? 1.6280 1.4092 1.3624 -0.2479 0.1921  -0.2073 143 PRO B CG  
2438 C CD  . PRO B 151 ? 1.5909 1.4005 1.3817 -0.2277 0.2108  -0.2181 143 PRO B CD  
2439 N N   . GLU B 152 ? 1.7233 1.5745 1.5307 -0.2441 0.2857  -0.2342 144 GLU B N   
2440 C CA  . GLU B 152 ? 1.7207 1.5912 1.5429 -0.2500 0.3214  -0.2443 144 GLU B CA  
2441 C C   . GLU B 152 ? 1.6648 1.5879 1.5591 -0.2405 0.3179  -0.2372 144 GLU B C   
2442 O O   . GLU B 152 ? 1.7540 1.6884 1.6472 -0.2549 0.3238  -0.2301 144 GLU B O   
2443 C CB  . GLU B 152 ? 1.8002 1.6664 1.6282 -0.2397 0.3539  -0.2669 144 GLU B CB  
2444 C CG  . GLU B 152 ? 1.9641 1.8377 1.7861 -0.2509 0.3972  -0.2799 144 GLU B CG  
2445 C CD  . GLU B 152 ? 1.9748 1.9084 1.8819 -0.2380 0.4154  -0.2865 144 GLU B CD  
2446 O OE1 . GLU B 152 ? 1.9238 1.8886 1.8913 -0.2181 0.3939  -0.2823 144 GLU B OE1 
2447 O OE2 . GLU B 152 ? 2.0102 1.9588 1.9234 -0.2483 0.4514  -0.2959 144 GLU B OE2 
2448 N N   . VAL B 153 ? 2.2181 2.1691 2.1715 -0.2170 0.3054  -0.2382 145 VAL B N   
2449 C CA  . VAL B 153 ? 2.2095 2.2071 2.2318 -0.2056 0.3007  -0.2333 145 VAL B CA  
2450 C C   . VAL B 153 ? 2.0700 2.0699 2.0831 -0.2143 0.2724  -0.2118 145 VAL B C   
2451 O O   . VAL B 153 ? 1.9203 1.9450 1.9601 -0.2195 0.2750  -0.2063 145 VAL B O   
2452 C CB  . VAL B 153 ? 1.8164 1.8330 1.8933 -0.1776 0.2897  -0.2387 145 VAL B CB  
2453 C CG1 . VAL B 153 ? 1.5890 1.6454 1.7289 -0.1651 0.2754  -0.2304 145 VAL B CG1 
2454 C CG2 . VAL B 153 ? 1.4140 1.4332 1.5076 -0.1665 0.3195  -0.2620 145 VAL B CG2 
2455 N N   . GLY B 154 ? 2.0525 2.0270 2.0292 -0.2157 0.2443  -0.1995 146 GLY B N   
2456 C CA  . GLY B 154 ? 2.0868 2.0634 2.0549 -0.2203 0.2161  -0.1800 146 GLY B CA  
2457 C C   . GLY B 154 ? 1.8475 1.8093 1.7731 -0.2441 0.2235  -0.1751 146 GLY B C   
2458 O O   . GLY B 154 ? 1.7400 1.7163 1.6787 -0.2469 0.2119  -0.1636 146 GLY B O   
2459 N N   . LEU B 155 ? 1.9263 1.8539 1.7952 -0.2617 0.2418  -0.1835 147 LEU B N   
2460 C CA  . LEU B 155 ? 1.8739 1.7795 1.6931 -0.2860 0.2497  -0.1789 147 LEU B CA  
2461 C C   . LEU B 155 ? 1.4570 1.3932 1.3139 -0.2926 0.2773  -0.1839 147 LEU B C   
2462 O O   . LEU B 155 ? 1.6231 1.5572 1.4656 -0.3076 0.2730  -0.1737 147 LEU B O   
2463 C CB  . LEU B 155 ? 2.1681 2.0246 1.9132 -0.3026 0.2637  -0.1877 147 LEU B CB  
2464 C CG  . LEU B 155 ? 2.1955 2.0108 1.8792 -0.3103 0.2305  -0.1764 147 LEU B CG  
2465 C CD1 . LEU B 155 ? 1.8085 1.6356 1.5219 -0.2908 0.2015  -0.1712 147 LEU B CD1 
2466 C CD2 . LEU B 155 ? 1.7756 1.5366 1.3806 -0.3282 0.2442  -0.1856 147 LEU B CD2 
2467 N N   . LYS B 156 ? 1.6396 1.6043 1.5460 -0.2817 0.3049  -0.1998 148 LYS B N   
2468 C CA  . LYS B 156 ? 1.4216 1.4230 1.3757 -0.2870 0.3306  -0.2054 148 LYS B CA  
2469 C C   . LYS B 156 ? 1.5969 1.6290 1.5990 -0.2800 0.3048  -0.1910 148 LYS B C   
2470 O O   . LYS B 156 ? 1.7213 1.7630 1.7276 -0.2965 0.3111  -0.1852 148 LYS B O   
2471 C CB  . LYS B 156 ? 1.4697 1.5010 1.4783 -0.2705 0.3591  -0.2257 148 LYS B CB  
2472 C CG  . LYS B 156 ? 1.6685 1.6701 1.6297 -0.2781 0.3913  -0.2422 148 LYS B CG  
2473 C CD  . LYS B 156 ? 1.6073 1.6445 1.6227 -0.2686 0.4302  -0.2633 148 LYS B CD  
2474 C CE  . LYS B 156 ? 2.6676 2.6792 2.6290 -0.2893 0.4721  -0.2754 148 LYS B CE  
2475 N NZ  . LYS B 156 ? 2.2067 2.2365 2.2002 -0.2740 0.5079  -0.2993 148 LYS B NZ  
2476 N N   . ARG B 157 ? 1.6415 1.6858 1.6764 -0.2564 0.2754  -0.1848 149 ARG B N   
2477 C CA  . ARG B 157 ? 1.5204 1.5888 1.5963 -0.2469 0.2494  -0.1714 149 ARG B CA  
2478 C C   . ARG B 157 ? 1.5253 1.5677 1.5502 -0.2617 0.2252  -0.1531 149 ARG B C   
2479 O O   . ARG B 157 ? 1.4831 1.5389 1.5270 -0.2655 0.2144  -0.1436 149 ARG B O   
2480 C CB  . ARG B 157 ? 1.4906 1.5718 1.6051 -0.2179 0.2263  -0.1697 149 ARG B CB  
2481 C CG  . ARG B 157 ? 1.3633 1.4715 1.5353 -0.2001 0.2454  -0.1874 149 ARG B CG  
2482 C CD  . ARG B 157 ? 1.3466 1.4451 1.5230 -0.1781 0.2292  -0.1887 149 ARG B CD  
2483 N NE  . ARG B 157 ? 1.2527 1.3769 1.4901 -0.1559 0.2368  -0.2023 149 ARG B NE  
2484 C CZ  . ARG B 157 ? 1.1915 1.3168 1.4535 -0.1326 0.2157  -0.1998 149 ARG B CZ  
2485 N NH1 . ARG B 157 ? 1.2688 1.3759 1.5047 -0.1288 0.1884  -0.1838 149 ARG B NH1 
2486 N NH2 . ARG B 157 ? 1.2722 1.4168 1.5861 -0.1125 0.2225  -0.2138 149 ARG B NH2 
2487 N N   . ALA B 158 ? 1.7097 1.7134 1.6699 -0.2696 0.2145  -0.1485 150 ALA B N   
2488 C CA  . ALA B 158 ? 1.8039 1.7797 1.7119 -0.2826 0.1907  -0.1327 150 ALA B CA  
2489 C C   . ALA B 158 ? 1.3850 1.3496 1.2654 -0.3096 0.2099  -0.1323 150 ALA B C   
2490 O O   . ALA B 158 ? 1.4686 1.4270 1.3367 -0.3172 0.1918  -0.1193 150 ALA B O   
2491 C CB  . ALA B 158 ? 1.5470 1.4837 1.3933 -0.2861 0.1763  -0.1303 150 ALA B CB  
2492 N N   . ARG B 159 ? 1.5736 1.5329 1.4413 -0.3246 0.2474  -0.1465 151 ARG B N   
2493 C CA  . ARG B 159 ? 1.6828 1.6333 1.5267 -0.3523 0.2718  -0.1470 151 ARG B CA  
2494 C C   . ARG B 159 ? 1.5862 1.5803 1.4980 -0.3515 0.2748  -0.1441 151 ARG B C   
2495 O O   . ARG B 159 ? 1.5322 1.5171 1.4249 -0.3724 0.2743  -0.1352 151 ARG B O   
2496 C CB  . ARG B 159 ? 1.7249 1.6667 1.5498 -0.3649 0.3155  -0.1646 151 ARG B CB  
2497 C CG  . ARG B 159 ? 1.7959 1.6856 1.5426 -0.3705 0.3141  -0.1680 151 ARG B CG  
2498 C CD  . ARG B 159 ? 1.7902 1.6810 1.5388 -0.3694 0.3534  -0.1882 151 ARG B CD  
2499 N NE  . ARG B 159 ? 1.9380 1.7699 1.5955 -0.3881 0.3650  -0.1921 151 ARG B NE  
2500 C CZ  . ARG B 159 ? 1.8799 1.6845 1.4859 -0.4154 0.3918  -0.1932 151 ARG B CZ  
2501 N NH1 . ARG B 159 ? 1.7221 1.5554 1.3609 -0.4293 0.4108  -0.1904 151 ARG B NH1 
2502 N NH2 . ARG B 159 ? 1.8748 1.6193 1.3921 -0.4299 0.3991  -0.1970 151 ARG B NH2 
2503 N N   . ALA B 160 ? 1.4631 1.5019 1.4525 -0.3284 0.2769  -0.1519 152 ALA B N   
2504 C CA  . ALA B 160 ? 1.3454 1.4265 1.4054 -0.3243 0.2749  -0.1500 152 ALA B CA  
2505 C C   . ALA B 160 ? 1.3163 1.3923 1.3780 -0.3127 0.2309  -0.1317 152 ALA B C   
2506 O O   . ALA B 160 ? 1.2315 1.3275 1.3297 -0.3154 0.2217  -0.1254 152 ALA B O   
2507 C CB  . ALA B 160 ? 1.1734 1.2988 1.3119 -0.3012 0.2892  -0.1656 152 ALA B CB  
2508 N N   . LEU B 172 ? 2.0931 1.7045 1.5361 -0.3324 0.2285  -0.2170 164 LEU B N   
2509 C CA  . LEU B 172 ? 2.1646 1.7336 1.5496 -0.3443 0.1926  -0.2077 164 LEU B CA  
2510 C C   . LEU B 172 ? 2.3888 1.9514 1.7852 -0.3355 0.1650  -0.2074 164 LEU B C   
2511 O O   . LEU B 172 ? 2.3462 1.9496 1.8083 -0.3189 0.1629  -0.2065 164 LEU B O   
2512 C CB  . LEU B 172 ? 2.1076 1.6979 1.5069 -0.3470 0.1671  -0.1900 164 LEU B CB  
2513 C CG  . LEU B 172 ? 2.6038 2.1510 1.9425 -0.3588 0.1294  -0.1809 164 LEU B CG  
2514 C CD1 . LEU B 172 ? 2.6506 2.1529 1.9153 -0.3789 0.1383  -0.1804 164 LEU B CD1 
2515 C CD2 . LEU B 172 ? 2.0948 1.6801 1.4816 -0.3479 0.0928  -0.1646 164 LEU B CD2 
2516 N N   . ASP B 173 ? 2.1255 1.6341 1.4558 -0.3476 0.1430  -0.2080 165 ASP B N   
2517 C CA  . ASP B 173 ? 2.0928 1.5914 1.4302 -0.3431 0.1157  -0.2078 165 ASP B CA  
2518 C C   . ASP B 173 ? 2.1199 1.6636 1.5165 -0.3346 0.0817  -0.1913 165 ASP B C   
2519 O O   . ASP B 173 ? 2.0783 1.6456 1.5216 -0.3242 0.0724  -0.1900 165 ASP B O   
2520 C CB  . ASP B 173 ? 2.2017 1.6300 1.4533 -0.3592 0.0969  -0.2121 165 ASP B CB  
2521 C CG  . ASP B 173 ? 2.2428 1.6208 1.4339 -0.3646 0.1298  -0.2302 165 ASP B CG  
2522 O OD1 . ASP B 173 ? 2.3880 1.7848 1.6123 -0.3525 0.1585  -0.2411 165 ASP B OD1 
2523 O OD2 . ASP B 173 ? 2.2832 1.6109 1.4059 -0.3749 0.1258  -0.2276 165 ASP B OD2 
2524 N N   . PHE B 174 ? 2.2996 1.8532 1.6921 -0.3390 0.0630  -0.1788 166 PHE B N   
2525 C CA  . PHE B 174 ? 2.1410 1.7391 1.5894 -0.3289 0.0333  -0.1635 166 PHE B CA  
2526 C C   . PHE B 174 ? 2.0872 1.7423 1.6141 -0.3108 0.0499  -0.1613 166 PHE B C   
2527 O O   . PHE B 174 ? 2.0238 1.7098 1.5998 -0.3004 0.0329  -0.1538 166 PHE B O   
2528 C CB  . PHE B 174 ? 2.1326 1.7294 1.5598 -0.3341 0.0149  -0.1523 166 PHE B CB  
2529 C CG  . PHE B 174 ? 2.1149 1.7412 1.5776 -0.3263 -0.0231 -0.1381 166 PHE B CG  
2530 C CD1 . PHE B 174 ? 1.9972 1.6800 1.5287 -0.3098 -0.0239 -0.1281 166 PHE B CD1 
2531 C CD2 . PHE B 174 ? 2.0860 1.6827 1.5123 -0.3348 -0.0581 -0.1351 166 PHE B CD2 
2532 C CE1 . PHE B 174 ? 1.9208 1.6313 1.4839 -0.3015 -0.0556 -0.1155 166 PHE B CE1 
2533 C CE2 . PHE B 174 ? 2.0108 1.6393 1.4745 -0.3266 -0.0914 -0.1230 166 PHE B CE2 
2534 C CZ  . PHE B 174 ? 1.9435 1.6296 1.4753 -0.3097 -0.0884 -0.1132 166 PHE B CZ  
2535 N N   . PHE B 175 ? 2.2991 1.9674 1.8384 -0.3072 0.0833  -0.1679 167 PHE B N   
2536 C CA  . PHE B 175 ? 2.2958 2.0143 1.9074 -0.2891 0.0976  -0.1670 167 PHE B CA  
2537 C C   . PHE B 175 ? 2.1538 1.8722 1.7883 -0.2798 0.1061  -0.1768 167 PHE B C   
2538 O O   . PHE B 175 ? 2.0086 1.7608 1.6986 -0.2651 0.0993  -0.1714 167 PHE B O   
2539 C CB  . PHE B 175 ? 1.9771 1.7098 1.5974 -0.2891 0.1295  -0.1726 167 PHE B CB  
2540 N N   . ASN B 176 ? 2.2007 1.8769 1.7886 -0.2878 0.1207  -0.1912 168 ASN B N   
2541 C CA  . ASN B 176 ? 2.2314 1.9006 1.8344 -0.2787 0.1273  -0.2013 168 ASN B CA  
2542 C C   . ASN B 176 ? 2.1394 1.8056 1.7522 -0.2797 0.0939  -0.1920 168 ASN B C   
2543 O O   . ASN B 176 ? 1.9967 1.6766 1.6471 -0.2686 0.0930  -0.1931 168 ASN B O   
2544 C CB  . ASN B 176 ? 2.3854 2.0044 1.9289 -0.2866 0.1493  -0.2192 168 ASN B CB  
2545 C CG  . ASN B 176 ? 2.1823 1.8122 1.7307 -0.2823 0.1895  -0.2313 168 ASN B CG  
2546 O OD1 . ASN B 176 ? 2.3413 2.0070 1.9452 -0.2657 0.2071  -0.2369 168 ASN B OD1 
2547 N ND2 . ASN B 176 ? 2.0506 1.6486 1.5406 -0.2976 0.2041  -0.2358 168 ASN B ND2 
2548 N N   . ARG B 177 ? 2.1932 1.8401 1.7721 -0.2935 0.0661  -0.1833 169 ARG B N   
2549 C CA  . ARG B 177 ? 2.1842 1.8341 1.7787 -0.2961 0.0342  -0.1740 169 ARG B CA  
2550 C C   . ARG B 177 ? 1.9385 1.6442 1.6015 -0.2831 0.0237  -0.1592 169 ARG B C   
2551 O O   . ARG B 177 ? 1.7113 1.4318 1.4099 -0.2776 0.0152  -0.1552 169 ARG B O   
2552 C CB  . ARG B 177 ? 2.2718 1.8887 1.8157 -0.3131 0.0056  -0.1696 169 ARG B CB  
2553 N N   . THR B 178 ? 1.9145 1.6483 1.5930 -0.2782 0.0246  -0.1509 170 THR B N   
2554 C CA  . THR B 178 ? 1.6370 1.4195 1.3737 -0.2646 0.0139  -0.1367 170 THR B CA  
2555 C C   . THR B 178 ? 1.5449 1.3523 1.3300 -0.2480 0.0334  -0.1398 170 THR B C   
2556 O O   . THR B 178 ? 1.6436 1.4785 1.4716 -0.2381 0.0234  -0.1302 170 THR B O   
2557 C CB  . THR B 178 ? 2.1087 1.9083 1.8439 -0.2625 0.0102  -0.1283 170 THR B CB  
2558 O OG1 . THR B 178 ? 1.9241 1.7109 1.6370 -0.2651 0.0369  -0.1382 170 THR B OG1 
2559 C CG2 . THR B 178 ? 2.1158 1.8967 1.8132 -0.2748 -0.0185 -0.1218 170 THR B CG2 
2560 N N   . ARG B 179 ? 1.6639 1.4616 1.4427 -0.2440 0.0613  -0.1534 171 ARG B N   
2561 C CA  . ARG B 179 ? 1.4361 1.2535 1.2594 -0.2268 0.0772  -0.1584 171 ARG B CA  
2562 C C   . ARG B 179 ? 1.5003 1.3023 1.3284 -0.2260 0.0686  -0.1603 171 ARG B C   
2563 O O   . ARG B 179 ? 1.4940 1.3168 1.3634 -0.2132 0.0656  -0.1548 171 ARG B O   
2564 C CB  . ARG B 179 ? 1.3713 1.1813 1.1879 -0.2229 0.1085  -0.1748 171 ARG B CB  
2565 C CG  . ARG B 179 ? 1.5111 1.3414 1.3759 -0.2027 0.1226  -0.1816 171 ARG B CG  
2566 C CD  . ARG B 179 ? 1.6290 1.4651 1.5013 -0.1965 0.1535  -0.1972 171 ARG B CD  
2567 N NE  . ARG B 179 ? 1.5567 1.4100 1.4758 -0.1755 0.1625  -0.2046 171 ARG B NE  
2568 C CZ  . ARG B 179 ? 1.6242 1.4620 1.5414 -0.1671 0.1815  -0.2227 171 ARG B CZ  
2569 N NH1 . ARG B 179 ? 1.8258 1.6324 1.6972 -0.1776 0.1982  -0.2361 171 ARG B NH1 
2570 N NH2 . ARG B 179 ? 1.6833 1.5343 1.6428 -0.1465 0.1831  -0.2279 171 ARG B NH2 
2571 N N   . ALA B 180 ? 1.7464 1.5079 1.5289 -0.2404 0.0637  -0.1678 172 ALA B N   
2572 C CA  . ALA B 180 ? 1.9230 1.6649 1.7056 -0.2426 0.0535  -0.1693 172 ALA B CA  
2573 C C   . ALA B 180 ? 1.7953 1.5628 1.6108 -0.2445 0.0286  -0.1516 172 ALA B C   
2574 O O   . ALA B 180 ? 1.7719 1.5447 1.6146 -0.2385 0.0258  -0.1483 172 ALA B O   
2575 C CB  . ALA B 180 ? 2.4189 2.1092 2.1415 -0.2595 0.0483  -0.1794 172 ALA B CB  
2576 N N   . ARG B 181 ? 1.7673 1.5500 1.5799 -0.2525 0.0108  -0.1402 173 ARG B N   
2577 C CA  . ARG B 181 ? 1.6865 1.4987 1.5335 -0.2534 -0.0110 -0.1238 173 ARG B CA  
2578 C C   . ARG B 181 ? 1.4998 1.3502 1.3976 -0.2343 -0.0025 -0.1153 173 ARG B C   
2579 O O   . ARG B 181 ? 1.4546 1.3183 1.3814 -0.2322 -0.0097 -0.1066 173 ARG B O   
2580 C CB  . ARG B 181 ? 1.7211 1.5429 1.5549 -0.2617 -0.0308 -0.1154 173 ARG B CB  
2581 C CG  . ARG B 181 ? 1.7152 1.5685 1.5834 -0.2634 -0.0542 -0.0999 173 ARG B CG  
2582 C CD  . ARG B 181 ? 1.7289 1.5911 1.5833 -0.2675 -0.0739 -0.0936 173 ARG B CD  
2583 N NE  . ARG B 181 ? 1.7261 1.5975 1.5744 -0.2563 -0.0617 -0.0937 173 ARG B NE  
2584 C CZ  . ARG B 181 ? 1.8021 1.7109 1.6859 -0.2406 -0.0607 -0.0833 173 ARG B CZ  
2585 N NH1 . ARG B 181 ? 1.8150 1.7572 1.7419 -0.2330 -0.0696 -0.0717 173 ARG B NH1 
2586 N NH2 . ARG B 181 ? 1.7751 1.6864 1.6496 -0.2328 -0.0499 -0.0846 173 ARG B NH2 
2587 N N   . TYR B 182 ? 1.5149 1.3810 1.4223 -0.2212 0.0126  -0.1175 174 TYR B N   
2588 C CA  . TYR B 182 ? 1.3980 1.2947 1.3494 -0.2020 0.0190  -0.1105 174 TYR B CA  
2589 C C   . TYR B 182 ? 1.3718 1.2557 1.3372 -0.1933 0.0302  -0.1177 174 TYR B C   
2590 O O   . TYR B 182 ? 1.3426 1.2411 1.3381 -0.1834 0.0267  -0.1087 174 TYR B O   
2591 C CB  . TYR B 182 ? 1.3890 1.3009 1.3461 -0.1916 0.0315  -0.1130 174 TYR B CB  
2592 C CG  . TYR B 182 ? 1.4627 1.3938 1.4171 -0.1932 0.0178  -0.1014 174 TYR B CG  
2593 C CD1 . TYR B 182 ? 1.6631 1.6153 1.6350 -0.1912 -0.0017 -0.0865 174 TYR B CD1 
2594 C CD2 . TYR B 182 ? 1.4714 1.3988 1.4051 -0.1964 0.0250  -0.1057 174 TYR B CD2 
2595 C CE1 . TYR B 182 ? 1.7214 1.6892 1.6892 -0.1900 -0.0154 -0.0771 174 TYR B CE1 
2596 C CE2 . TYR B 182 ? 1.4579 1.3973 1.3842 -0.1974 0.0106  -0.0954 174 TYR B CE2 
2597 C CZ  . TYR B 182 ? 1.6919 1.6510 1.6350 -0.1929 -0.0105 -0.0815 174 TYR B CZ  
2598 O OH  . TYR B 182 ? 1.5992 1.5684 1.5333 -0.1914 -0.0261 -0.0723 174 TYR B OH  
2599 N N   . LEU B 183 ? 1.3843 1.2379 1.3251 -0.1959 0.0441  -0.1343 175 LEU B N   
2600 C CA  . LEU B 183 ? 1.3948 1.2330 1.3466 -0.1849 0.0540  -0.1431 175 LEU B CA  
2601 C C   . LEU B 183 ? 1.3839 1.2037 1.3314 -0.1944 0.0398  -0.1372 175 LEU B C   
2602 O O   . LEU B 183 ? 1.4187 1.2354 1.3855 -0.1841 0.0409  -0.1355 175 LEU B O   
2603 C CB  . LEU B 183 ? 1.5985 1.4094 1.5243 -0.1835 0.0734  -0.1635 175 LEU B CB  
2604 C CG  . LEU B 183 ? 1.5231 1.3550 1.4665 -0.1702 0.0930  -0.1715 175 LEU B CG  
2605 C CD1 . LEU B 183 ? 1.7251 1.5314 1.6396 -0.1718 0.1142  -0.1918 175 LEU B CD1 
2606 C CD2 . LEU B 183 ? 1.3801 1.2334 1.3692 -0.1479 0.0962  -0.1700 175 LEU B CD2 
2607 N N   . GLU B 184 ? 1.3470 1.1522 1.2684 -0.2148 0.0252  -0.1342 176 GLU B N   
2608 C CA  . GLU B 184 ? 1.2800 1.0710 1.2014 -0.2272 0.0101  -0.1272 176 GLU B CA  
2609 C C   . GLU B 184 ? 1.2719 1.0993 1.2343 -0.2230 0.0015  -0.1087 176 GLU B C   
2610 O O   . GLU B 184 ? 1.2136 1.0346 1.1902 -0.2207 0.0011  -0.1040 176 GLU B O   
2611 C CB  . GLU B 184 ? 1.4357 1.2062 1.3239 -0.2502 -0.0068 -0.1277 176 GLU B CB  
2612 C CG  . GLU B 184 ? 1.5254 1.2814 1.4152 -0.2667 -0.0243 -0.1207 176 GLU B CG  
2613 C CD  . GLU B 184 ? 1.5614 1.3154 1.4364 -0.2882 -0.0473 -0.1155 176 GLU B CD  
2614 O OE1 . GLU B 184 ? 1.6439 1.3942 1.4941 -0.2905 -0.0493 -0.1203 176 GLU B OE1 
2615 O OE2 . GLU B 184 ? 1.6265 1.3819 1.5148 -0.3032 -0.0641 -0.1065 176 GLU B OE2 
2616 N N   . LEU B 185 ? 1.3032 1.1657 1.2814 -0.2217 -0.0051 -0.0981 177 LEU B N   
2617 C CA  . LEU B 185 ? 1.1680 1.0661 1.1837 -0.2146 -0.0104 -0.0812 177 LEU B CA  
2618 C C   . LEU B 185 ? 1.1302 1.0325 1.1664 -0.1931 0.0035  -0.0809 177 LEU B C   
2619 O O   . LEU B 185 ? 1.0755 0.9876 1.1332 -0.1887 0.0020  -0.0697 177 LEU B O   
2620 C CB  . LEU B 185 ? 1.1548 1.0861 1.1793 -0.2126 -0.0191 -0.0725 177 LEU B CB  
2621 C CG  . LEU B 185 ? 1.3936 1.3234 1.4013 -0.2322 -0.0380 -0.0709 177 LEU B CG  
2622 C CD1 . LEU B 185 ? 1.5444 1.4983 1.5520 -0.2266 -0.0457 -0.0658 177 LEU B CD1 
2623 C CD2 . LEU B 185 ? 1.3200 1.2624 1.3501 -0.2449 -0.0516 -0.0597 177 LEU B CD2 
2624 N N   . ALA B 186 ? 1.1647 1.0586 1.1944 -0.1797 0.0169  -0.0934 178 ALA B N   
2625 C CA  . ALA B 186 ? 1.1282 1.0234 1.1780 -0.1583 0.0271  -0.0951 178 ALA B CA  
2626 C C   . ALA B 186 ? 1.1224 0.9869 1.1676 -0.1583 0.0282  -0.0983 178 ALA B C   
2627 O O   . ALA B 186 ? 1.1138 0.9798 1.1757 -0.1473 0.0279  -0.0901 178 ALA B O   
2628 C CB  . ALA B 186 ? 1.2312 1.1250 1.2785 -0.1464 0.0408  -0.1098 178 ALA B CB  
2629 N N   . ALA B 187 ? 1.1884 1.0198 1.2059 -0.1708 0.0286  -0.1102 179 ALA B N   
2630 C CA  . ALA B 187 ? 1.2354 1.0311 1.2424 -0.1721 0.0275  -0.1138 179 ALA B CA  
2631 C C   . ALA B 187 ? 1.1663 0.9648 1.1805 -0.1874 0.0154  -0.0968 179 ALA B C   
2632 O O   . ALA B 187 ? 1.1453 0.9246 1.1615 -0.1836 0.0153  -0.0929 179 ALA B O   
2633 C CB  . ALA B 187 ? 1.3412 1.0977 1.3121 -0.1817 0.0297  -0.1310 179 ALA B CB  
2634 N N   . GLN B 188 ? 1.1611 0.9829 1.1797 -0.2047 0.0050  -0.0867 180 GLN B N   
2635 C CA  . GLN B 188 ? 1.0891 0.9177 1.1185 -0.2226 -0.0060 -0.0716 180 GLN B CA  
2636 C C   . GLN B 188 ? 0.9373 0.8061 1.0007 -0.2142 -0.0048 -0.0539 180 GLN B C   
2637 O O   . GLN B 188 ? 0.9754 0.8508 1.0518 -0.2267 -0.0092 -0.0409 180 GLN B O   
2638 C CB  . GLN B 188 ? 1.0792 0.9120 1.0983 -0.2461 -0.0206 -0.0710 180 GLN B CB  
2639 C CG  . GLN B 188 ? 1.1613 0.9465 1.1426 -0.2609 -0.0260 -0.0846 180 GLN B CG  
2640 C CD  . GLN B 188 ? 1.2768 1.0627 1.2432 -0.2812 -0.0422 -0.0856 180 GLN B CD  
2641 O OE1 . GLN B 188 ? 1.1990 1.0226 1.1844 -0.2829 -0.0495 -0.0769 180 GLN B OE1 
2642 N NE2 . GLN B 188 ? 1.4794 1.2202 1.4087 -0.2954 -0.0495 -0.0967 180 GLN B NE2 
2643 N N   . ASP B 189 ? 0.9533 0.8477 1.0301 -0.1942 0.0013  -0.0527 181 ASP B N   
2644 C CA  . ASP B 189 ? 0.8961 0.8281 1.0004 -0.1854 0.0011  -0.0363 181 ASP B CA  
2645 C C   . ASP B 189 ? 0.8882 0.8129 0.9992 -0.1622 0.0109  -0.0339 181 ASP B C   
2646 O O   . ASP B 189 ? 0.8263 0.7482 0.9353 -0.1441 0.0160  -0.0431 181 ASP B O   
2647 C CB  . ASP B 189 ? 0.8730 0.8381 0.9841 -0.1811 -0.0039 -0.0350 181 ASP B CB  
2648 C CG  . ASP B 189 ? 0.8157 0.8205 0.9530 -0.1754 -0.0075 -0.0182 181 ASP B CG  
2649 O OD1 . ASP B 189 ? 0.8078 0.8153 0.9581 -0.1694 -0.0015 -0.0078 181 ASP B OD1 
2650 O OD2 . ASP B 189 ? 0.7446 0.7754 0.8866 -0.1761 -0.0161 -0.0156 181 ASP B OD2 
2651 N N   . PRO B 190 ? 0.8465 0.7665 0.9647 -0.1622 0.0136  -0.0219 182 PRO B N   
2652 C CA  . PRO B 190 ? 0.8169 0.7214 0.9345 -0.1392 0.0207  -0.0202 182 PRO B CA  
2653 C C   . PRO B 190 ? 0.7941 0.7273 0.9260 -0.1177 0.0219  -0.0149 182 PRO B C   
2654 O O   . PRO B 190 ? 0.8140 0.7324 0.9438 -0.0963 0.0248  -0.0185 182 PRO B O   
2655 C CB  . PRO B 190 ? 0.9052 0.7989 1.0229 -0.1488 0.0234  -0.0059 182 PRO B CB  
2656 C CG  . PRO B 190 ? 0.8598 0.7876 0.9942 -0.1710 0.0190  0.0044  182 PRO B CG  
2657 C CD  . PRO B 190 ? 0.8739 0.8050 1.0023 -0.1831 0.0102  -0.0083 182 PRO B CD  
2658 N N   . THR B 191 ? 0.8071 0.7786 0.9528 -0.1221 0.0176  -0.0068 183 THR B N   
2659 C CA  . THR B 191 ? 0.7313 0.7272 0.8866 -0.1022 0.0165  -0.0018 183 THR B CA  
2660 C C   . THR B 191 ? 0.6775 0.6760 0.8281 -0.0966 0.0139  -0.0149 183 THR B C   
2661 O O   . THR B 191 ? 0.6228 0.6410 0.7792 -0.0835 0.0107  -0.0114 183 THR B O   
2662 C CB  . THR B 191 ? 0.6615 0.6962 0.8324 -0.1070 0.0123  0.0123  183 THR B CB  
2663 O OG1 . THR B 191 ? 0.7486 0.7987 0.9206 -0.1259 0.0037  0.0078  183 THR B OG1 
2664 C CG2 . THR B 191 ? 0.6584 0.6953 0.8376 -0.1140 0.0184  0.0259  183 THR B CG2 
2665 N N   . ILE B 192 ? 0.7101 0.6879 0.8483 -0.1069 0.0157  -0.0296 184 ILE B N   
2666 C CA  . ILE B 192 ? 0.7365 0.7139 0.8691 -0.1027 0.0176  -0.0430 184 ILE B CA  
2667 C C   . ILE B 192 ? 0.7278 0.6779 0.8585 -0.0900 0.0253  -0.0563 184 ILE B C   
2668 O O   . ILE B 192 ? 0.7853 0.7077 0.9060 -0.0958 0.0279  -0.0623 184 ILE B O   
2669 C CB  . ILE B 192 ? 0.8349 0.8107 0.9515 -0.1241 0.0147  -0.0509 184 ILE B CB  
2670 C CG1 . ILE B 192 ? 0.8780 0.8808 0.9984 -0.1352 0.0035  -0.0390 184 ILE B CG1 
2671 C CG2 . ILE B 192 ? 0.8025 0.7754 0.9107 -0.1198 0.0207  -0.0647 184 ILE B CG2 
2672 C CD1 . ILE B 192 ? 0.8666 0.8625 0.9674 -0.1567 -0.0033 -0.0461 184 ILE B CD1 
2673 N N   . ARG B 193 ? 0.6957 0.6531 0.8366 -0.0727 0.0275  -0.0612 185 ARG B N   
2674 C CA  . ARG B 193 ? 0.7110 0.6495 0.8569 -0.0590 0.0338  -0.0761 185 ARG B CA  
2675 C C   . ARG B 193 ? 0.7084 0.6598 0.8574 -0.0607 0.0400  -0.0885 185 ARG B C   
2676 O O   . ARG B 193 ? 0.6627 0.6371 0.8141 -0.0631 0.0368  -0.0824 185 ARG B O   
2677 C CB  . ARG B 193 ? 0.7806 0.7151 0.9405 -0.0354 0.0297  -0.0708 185 ARG B CB  
2678 C CG  . ARG B 193 ? 0.8406 0.7594 0.9929 -0.0335 0.0258  -0.0574 185 ARG B CG  
2679 C CD  . ARG B 193 ? 0.9825 0.8669 1.1208 -0.0404 0.0288  -0.0650 185 ARG B CD  
2680 N NE  . ARG B 193 ? 0.9811 0.8516 1.1090 -0.0459 0.0268  -0.0503 185 ARG B NE  
2681 C CZ  . ARG B 193 ? 1.0254 0.8788 1.1505 -0.0297 0.0243  -0.0421 185 ARG B CZ  
2682 N NH1 . ARG B 193 ? 1.0585 0.9056 1.1914 -0.0060 0.0204  -0.0474 185 ARG B NH1 
2683 N NH2 . ARG B 193 ? 0.9611 0.8020 1.0744 -0.0383 0.0256  -0.0282 185 ARG B NH2 
2684 N N   . THR B 194 ? 0.7759 0.7110 0.9232 -0.0594 0.0496  -0.1061 186 THR B N   
2685 C CA  . THR B 194 ? 0.8548 0.7998 1.0024 -0.0640 0.0601  -0.1194 186 THR B CA  
2686 C C   . THR B 194 ? 0.8751 0.8262 1.0504 -0.0440 0.0659  -0.1306 186 THR B C   
2687 O O   . THR B 194 ? 0.8760 0.8101 1.0618 -0.0284 0.0645  -0.1367 186 THR B O   
2688 C CB  . THR B 194 ? 0.8133 0.7362 0.9360 -0.0790 0.0692  -0.1327 186 THR B CB  
2689 O OG1 . THR B 194 ? 0.9318 0.8480 1.0314 -0.0981 0.0605  -0.1225 186 THR B OG1 
2690 C CG2 . THR B 194 ? 0.9171 0.8493 1.0351 -0.0853 0.0830  -0.1454 186 THR B CG2 
2691 N N   . VAL B 195 ? 0.9033 0.8774 1.0901 -0.0451 0.0710  -0.1332 187 VAL B N   
2692 C CA  . VAL B 195 ? 0.9889 0.9750 1.2066 -0.0305 0.0782  -0.1458 187 VAL B CA  
2693 C C   . VAL B 195 ? 1.0935 1.0873 1.3049 -0.0442 0.0969  -0.1598 187 VAL B C   
2694 O O   . VAL B 195 ? 1.0768 1.0795 1.2695 -0.0612 0.0987  -0.1536 187 VAL B O   
2695 C CB  . VAL B 195 ? 1.0405 1.0474 1.2801 -0.0198 0.0669  -0.1346 187 VAL B CB  
2696 C CG1 . VAL B 195 ? 1.1273 1.1536 1.3994 -0.0130 0.0758  -0.1477 187 VAL B CG1 
2697 C CG2 . VAL B 195 ? 1.1478 1.1418 1.3946 -0.0011 0.0513  -0.1248 187 VAL B CG2 
2698 N N   . ASP B 196 ? 1.1182 1.1062 1.3424 -0.0365 0.1110  -0.1789 188 ASP B N   
2699 C CA  . ASP B 196 ? 1.1879 1.1847 1.4082 -0.0476 0.1327  -0.1933 188 ASP B CA  
2700 C C   . ASP B 196 ? 1.1407 1.1700 1.3905 -0.0473 0.1361  -0.1914 188 ASP B C   
2701 O O   . ASP B 196 ? 1.0577 1.1029 1.3492 -0.0293 0.1318  -0.1950 188 ASP B O   
2702 C CB  . ASP B 196 ? 1.2867 1.2723 1.5176 -0.0360 0.1481  -0.2153 188 ASP B CB  
2703 C CG  . ASP B 196 ? 1.3640 1.3583 1.5887 -0.0473 0.1744  -0.2308 188 ASP B CG  
2704 O OD1 . ASP B 196 ? 1.3192 1.2955 1.4993 -0.0670 0.1815  -0.2299 188 ASP B OD1 
2705 O OD2 . ASP B 196 ? 1.3271 1.3457 1.5913 -0.0366 0.1880  -0.2438 188 ASP B OD2 
2706 N N   . ALA B 197 ? 1.1750 1.2109 1.4013 -0.0676 0.1415  -0.1852 189 ALA B N   
2707 C CA  . ALA B 197 ? 1.2705 1.3327 1.5176 -0.0718 0.1443  -0.1819 189 ALA B CA  
2708 C C   . ALA B 197 ? 1.3338 1.4093 1.5916 -0.0804 0.1722  -0.1991 189 ALA B C   
2709 O O   . ALA B 197 ? 1.2744 1.3739 1.5559 -0.0848 0.1770  -0.1981 189 ALA B O   
2710 C CB  . ALA B 197 ? 1.3068 1.3658 1.5195 -0.0885 0.1316  -0.1639 189 ALA B CB  
2711 N N   . THR B 198 ? 1.3282 1.3881 1.5691 -0.0829 0.1913  -0.2148 190 THR B N   
2712 C CA  . THR B 198 ? 1.3351 1.4074 1.5837 -0.0907 0.2218  -0.2318 190 THR B CA  
2713 C C   . THR B 198 ? 1.2344 1.3399 1.5488 -0.0721 0.2305  -0.2450 190 THR B C   
2714 O O   . THR B 198 ? 1.3323 1.4586 1.6654 -0.0787 0.2566  -0.2579 190 THR B O   
2715 C CB  . THR B 198 ? 1.4457 1.4891 1.6569 -0.0949 0.2399  -0.2467 190 THR B CB  
2716 O OG1 . THR B 198 ? 1.3742 1.4114 1.6099 -0.0716 0.2375  -0.2589 190 THR B OG1 
2717 C CG2 . THR B 198 ? 1.4140 1.4223 1.5634 -0.1116 0.2268  -0.2347 190 THR B CG2 
2718 N N   . GLN B 199 ? 1.2412 1.3509 1.5903 -0.0493 0.2095  -0.2426 191 GLN B N   
2719 C CA  . GLN B 199 ? 1.2464 1.3845 1.6594 -0.0288 0.2119  -0.2555 191 GLN B CA  
2720 C C   . GLN B 199 ? 1.2377 1.4065 1.6855 -0.0329 0.2026  -0.2452 191 GLN B C   
2721 O O   . GLN B 199 ? 1.1826 1.3470 1.6011 -0.0500 0.1936  -0.2279 191 GLN B O   
2722 C CB  . GLN B 199 ? 1.1913 1.3113 1.6173 -0.0026 0.1906  -0.2571 191 GLN B CB  
2723 C CG  . GLN B 199 ? 1.1572 1.2618 1.5668 0.0005  0.1600  -0.2349 191 GLN B CG  
2724 C CD  . GLN B 199 ? 1.1213 1.1965 1.5248 0.0207  0.1428  -0.2353 191 GLN B CD  
2725 O OE1 . GLN B 199 ? 0.9646 1.0317 1.3827 0.0360  0.1498  -0.2529 191 GLN B OE1 
2726 N NE2 . GLN B 199 ? 1.1479 1.2054 1.5279 0.0210  0.1208  -0.2159 191 GLN B NE2 
2727 N N   . PRO B 200 ? 1.2386 1.4380 1.7493 -0.0175 0.2034  -0.2562 192 PRO B N   
2728 C CA  . PRO B 200 ? 1.2416 1.4689 1.7869 -0.0228 0.1931  -0.2468 192 PRO B CA  
2729 C C   . PRO B 200 ? 1.1840 1.3935 1.7128 -0.0161 0.1580  -0.2252 192 PRO B C   
2730 O O   . PRO B 200 ? 1.1472 1.3303 1.6578 -0.0005 0.1403  -0.2202 192 PRO B O   
2731 C CB  . PRO B 200 ? 1.3311 1.5916 1.9510 -0.0029 0.1968  -0.2652 192 PRO B CB  
2732 C CG  . PRO B 200 ? 1.1576 1.4153 1.7781 0.0046  0.2225  -0.2869 192 PRO B CG  
2733 C CD  . PRO B 200 ? 1.1508 1.3622 1.7048 0.0037  0.2156  -0.2794 192 PRO B CD  
2734 N N   . LEU B 201 ? 1.1341 1.3574 1.6687 -0.0284 0.1489  -0.2125 193 LEU B N   
2735 C CA  . LEU B 201 ? 1.0809 1.2861 1.5923 -0.0239 0.1180  -0.1913 193 LEU B CA  
2736 C C   . LEU B 201 ? 1.1027 1.2994 1.6419 0.0057  0.0925  -0.1910 193 LEU B C   
2737 O O   . LEU B 201 ? 1.1492 1.3184 1.6562 0.0152  0.0731  -0.1778 193 LEU B O   
2738 C CB  . LEU B 201 ? 1.1472 1.3679 1.6643 -0.0404 0.1124  -0.1806 193 LEU B CB  
2739 C CG  . LEU B 201 ? 1.0298 1.2306 1.5126 -0.0403 0.0839  -0.1581 193 LEU B CG  
2740 C CD1 . LEU B 201 ? 1.2026 1.3762 1.6232 -0.0486 0.0836  -0.1476 193 LEU B CD1 
2741 C CD2 . LEU B 201 ? 0.9222 1.1370 1.4107 -0.0589 0.0816  -0.1507 193 LEU B CD2 
2742 N N   . GLU B 202 ? 1.1074 1.3265 1.7060 0.0206  0.0919  -0.2055 194 GLU B N   
2743 C CA  . GLU B 202 ? 1.1359 1.3414 1.7577 0.0498  0.0652  -0.2061 194 GLU B CA  
2744 C C   . GLU B 202 ? 1.1423 1.3150 1.7331 0.0637  0.0640  -0.2091 194 GLU B C   
2745 O O   . GLU B 202 ? 1.1361 1.2807 1.7125 0.0815  0.0401  -0.2000 194 GLU B O   
2746 C CB  . GLU B 202 ? 1.2440 1.4805 1.9381 0.0637  0.0652  -0.2244 194 GLU B CB  
2747 C CG  . GLU B 202 ? 1.3330 1.5527 2.0517 0.0943  0.0327  -0.2250 194 GLU B CG  
2748 C CD  . GLU B 202 ? 1.3687 1.5861 2.0935 0.0959  0.0040  -0.2091 194 GLU B CD  
2749 O OE1 . GLU B 202 ? 1.4116 1.6584 2.1601 0.0778  0.0095  -0.2070 194 GLU B OE1 
2750 O OE2 . GLU B 202 ? 1.3718 1.5549 2.0743 0.1147  -0.0238 -0.1984 194 GLU B OE2 
2751 N N   . ALA B 203 ? 1.1133 1.2858 1.6910 0.0554  0.0897  -0.2217 195 ALA B N   
2752 C CA  . ALA B 203 ? 1.0246 1.1627 1.5681 0.0648  0.0885  -0.2238 195 ALA B CA  
2753 C C   . ALA B 203 ? 1.0431 1.1545 1.5285 0.0527  0.0792  -0.2025 195 ALA B C   
2754 O O   . ALA B 203 ? 1.0778 1.1591 1.5407 0.0648  0.0640  -0.1953 195 ALA B O   
2755 C CB  . ALA B 203 ? 0.9287 1.0710 1.4698 0.0584  0.1176  -0.2430 195 ALA B CB  
2756 N N   . VAL B 204 ? 1.0477 1.1694 1.5085 0.0288  0.0882  -0.1926 196 VAL B N   
2757 C CA  . VAL B 204 ? 1.0547 1.1561 1.4659 0.0182  0.0782  -0.1732 196 VAL B CA  
2758 C C   . VAL B 204 ? 1.0574 1.1480 1.4691 0.0341  0.0508  -0.1573 196 VAL B C   
2759 O O   . VAL B 204 ? 0.9484 1.0161 1.3288 0.0377  0.0401  -0.1449 196 VAL B O   
2760 C CB  . VAL B 204 ? 1.0349 1.1483 1.4215 -0.0081 0.0892  -0.1664 196 VAL B CB  
2761 C CG1 . VAL B 204 ? 0.9705 1.0648 1.3090 -0.0173 0.0778  -0.1482 196 VAL B CG1 
2762 C CG2 . VAL B 204 ? 1.0548 1.1747 1.4367 -0.0233 0.1179  -0.1828 196 VAL B CG2 
2763 N N   . GLU B 205 ? 1.0738 1.1802 1.5207 0.0434  0.0395  -0.1573 197 GLU B N   
2764 C CA  . GLU B 205 ? 1.0477 1.1390 1.4918 0.0604  0.0125  -0.1431 197 GLU B CA  
2765 C C   . GLU B 205 ? 0.9415 1.0043 1.3838 0.0832  0.0013  -0.1457 197 GLU B C   
2766 O O   . GLU B 205 ? 0.9861 1.0241 1.3989 0.0917  -0.0135 -0.1309 197 GLU B O   
2767 C CB  . GLU B 205 ? 1.2414 1.3529 1.7260 0.0656  0.0012  -0.1451 197 GLU B CB  
2768 C CG  . GLU B 205 ? 1.0594 1.1513 1.5434 0.0864  -0.0286 -0.1333 197 GLU B CG  
2769 C CD  . GLU B 205 ? 1.0064 1.1173 1.5375 0.0922  -0.0413 -0.1388 197 GLU B CD  
2770 O OE1 . GLU B 205 ? 1.1933 1.3365 1.7617 0.0796  -0.0243 -0.1522 197 GLU B OE1 
2771 O OE2 . GLU B 205 ? 0.8940 0.9871 1.4248 0.1088  -0.0678 -0.1299 197 GLU B OE2 
2772 N N   . ARG B 206 ? 0.9303 0.9946 1.4020 0.0939  0.0084  -0.1647 198 ARG B N   
2773 C CA  . ARG B 206 ? 0.8966 0.9277 1.3617 0.1156  -0.0038 -0.1679 198 ARG B CA  
2774 C C   . ARG B 206 ? 0.9302 0.9341 1.3459 0.1070  0.0017  -0.1582 198 ARG B C   
2775 O O   . ARG B 206 ? 0.8453 0.8173 1.2371 0.1191  -0.0125 -0.1482 198 ARG B O   
2776 C CB  . ARG B 206 ? 0.9115 0.9484 1.4148 0.1286  0.0036  -0.1918 198 ARG B CB  
2777 C CG  . ARG B 206 ? 0.9534 0.9492 1.4382 0.1469  -0.0050 -0.1969 198 ARG B CG  
2778 C CD  . ARG B 206 ? 1.0419 1.0051 1.5131 0.1669  -0.0336 -0.1843 198 ARG B CD  
2779 N NE  . ARG B 206 ? 1.1686 1.1435 1.6621 0.1764  -0.0497 -0.1857 198 ARG B NE  
2780 C CZ  . ARG B 206 ? 0.9868 0.9359 1.4540 0.1868  -0.0729 -0.1727 198 ARG B CZ  
2781 N NH1 . ARG B 206 ? 1.0081 0.9192 1.4241 0.1896  -0.0811 -0.1558 198 ARG B NH1 
2782 N NH2 . ARG B 206 ? 0.9035 0.8653 1.3967 0.1936  -0.0865 -0.1774 198 ARG B NH2 
2783 N N   . ASP B 207 ? 1.0130 1.0274 1.4121 0.0855  0.0223  -0.1613 199 ASP B N   
2784 C CA  . ASP B 207 ? 1.0452 1.0352 1.4033 0.0759  0.0274  -0.1552 199 ASP B CA  
2785 C C   . ASP B 207 ? 0.9576 0.9442 1.2841 0.0662  0.0192  -0.1327 199 ASP B C   
2786 O O   . ASP B 207 ? 0.8861 0.8475 1.1876 0.0700  0.0122  -0.1224 199 ASP B O   
2787 C CB  . ASP B 207 ? 1.0840 1.0825 1.4336 0.0572  0.0499  -0.1674 199 ASP B CB  
2788 C CG  . ASP B 207 ? 1.1283 1.1188 1.4975 0.0696  0.0588  -0.1897 199 ASP B CG  
2789 O OD1 . ASP B 207 ? 1.1027 1.0687 1.4772 0.0901  0.0458  -0.1933 199 ASP B OD1 
2790 O OD2 . ASP B 207 ? 1.2367 1.2428 1.6132 0.0596  0.0787  -0.2039 199 ASP B OD2 
2791 N N   . ILE B 208 ? 0.9569 0.9679 1.2832 0.0534  0.0208  -0.1251 200 ILE B N   
2792 C CA  . ILE B 208 ? 0.9781 0.9876 1.2783 0.0489  0.0105  -0.1047 200 ILE B CA  
2793 C C   . ILE B 208 ? 0.9561 0.9441 1.2535 0.0710  -0.0074 -0.0945 200 ILE B C   
2794 O O   . ILE B 208 ? 0.9623 0.9331 1.2337 0.0721  -0.0111 -0.0820 200 ILE B O   
2795 C CB  . ILE B 208 ? 0.9839 1.0181 1.2876 0.0384  0.0093  -0.0994 200 ILE B CB  
2796 C CG1 . ILE B 208 ? 1.0039 1.0510 1.2948 0.0138  0.0267  -0.1055 200 ILE B CG1 
2797 C CG2 . ILE B 208 ? 0.9685 0.9987 1.2502 0.0425  -0.0061 -0.0793 200 ILE B CG2 
2798 C CD1 . ILE B 208 ? 0.9877 1.0536 1.2771 0.0013  0.0265  -0.1014 200 ILE B CD1 
2799 N N   . ARG B 209 ? 0.9844 0.9723 1.3085 0.0885  -0.0187 -0.1001 201 ARG B N   
2800 C CA  . ARG B 209 ? 0.8997 0.8612 1.2169 0.1110  -0.0379 -0.0912 201 ARG B CA  
2801 C C   . ARG B 209 ? 0.8864 0.8142 1.1846 0.1191  -0.0374 -0.0919 201 ARG B C   
2802 O O   . ARG B 209 ? 0.9426 0.8455 1.2135 0.1277  -0.0458 -0.0778 201 ARG B O   
2803 C CB  . ARG B 209 ? 0.8952 0.8611 1.2488 0.1275  -0.0514 -0.1009 201 ARG B CB  
2804 C CG  . ARG B 209 ? 0.9654 0.8986 1.3106 0.1526  -0.0745 -0.0936 201 ARG B CG  
2805 C CD  . ARG B 209 ? 0.8862 0.8315 1.2548 0.1605  -0.0916 -0.0924 201 ARG B CD  
2806 N NE  . ARG B 209 ? 1.0584 0.9756 1.3830 0.1692  -0.1078 -0.0762 201 ARG B NE  
2807 C CZ  . ARG B 209 ? 1.0161 0.9366 1.3369 0.1698  -0.1215 -0.0700 201 ARG B CZ  
2808 N NH1 . ARG B 209 ? 1.0805 1.0303 1.4411 0.1630  -0.1243 -0.0772 201 ARG B NH1 
2809 N NH2 . ARG B 209 ? 1.1445 1.0380 1.4220 0.1764  -0.1312 -0.0571 201 ARG B NH2 
2810 N N   . ALA B 210 ? 0.9310 0.8550 1.2400 0.1161  -0.0268 -0.1080 202 ALA B N   
2811 C CA  . ALA B 210 ? 0.9192 0.8062 1.2066 0.1225  -0.0274 -0.1093 202 ALA B CA  
2812 C C   . ALA B 210 ? 0.9502 0.8314 1.2030 0.1037  -0.0179 -0.0957 202 ALA B C   
2813 O O   . ALA B 210 ? 1.0054 0.8555 1.2321 0.1083  -0.0221 -0.0861 202 ALA B O   
2814 C CB  . ALA B 210 ? 0.9159 0.7991 1.2225 0.1255  -0.0196 -0.1313 202 ALA B CB  
2815 N N   . VAL B 211 ? 0.9235 0.8332 1.1757 0.0817  -0.0051 -0.0952 203 VAL B N   
2816 C CA  . VAL B 211 ? 0.8957 0.8027 1.1208 0.0626  0.0025  -0.0846 203 VAL B CA  
2817 C C   . VAL B 211 ? 0.9609 0.8663 1.1687 0.0659  -0.0050 -0.0637 203 VAL B C   
2818 O O   . VAL B 211 ? 1.0128 0.8982 1.1996 0.0631  -0.0039 -0.0539 203 VAL B O   
2819 C CB  . VAL B 211 ? 0.9556 0.8909 1.1820 0.0400  0.0143  -0.0890 203 VAL B CB  
2820 C CG1 . VAL B 211 ? 0.9299 0.8684 1.1327 0.0215  0.0168  -0.0751 203 VAL B CG1 
2821 C CG2 . VAL B 211 ? 0.9239 0.8540 1.1580 0.0351  0.0256  -0.1092 203 VAL B CG2 
2822 N N   . VAL B 212 ? 0.9771 0.9029 1.1925 0.0714  -0.0118 -0.0567 204 VAL B N   
2823 C CA  . VAL B 212 ? 0.9328 0.8573 1.1307 0.0775  -0.0184 -0.0379 204 VAL B CA  
2824 C C   . VAL B 212 ? 0.9086 0.7958 1.0925 0.0973  -0.0262 -0.0326 204 VAL B C   
2825 O O   . VAL B 212 ? 0.9750 0.8493 1.1366 0.0969  -0.0236 -0.0189 204 VAL B O   
2826 C CB  . VAL B 212 ? 0.9890 0.9355 1.1948 0.0827  -0.0271 -0.0332 204 VAL B CB  
2827 C CG1 . VAL B 212 ? 1.0979 1.0364 1.2837 0.0958  -0.0356 -0.0154 204 VAL B CG1 
2828 C CG2 . VAL B 212 ? 0.9892 0.9665 1.1981 0.0610  -0.0195 -0.0352 204 VAL B CG2 
2829 N N   . ASN B 213 ? 0.9839 0.8523 1.1805 0.1147  -0.0357 -0.0438 205 ASN B N   
2830 C CA  . ASN B 213 ? 1.0328 0.8581 1.2110 0.1346  -0.0457 -0.0400 205 ASN B CA  
2831 C C   . ASN B 213 ? 1.0144 0.8127 1.1701 0.1256  -0.0364 -0.0382 205 ASN B C   
2832 O O   . ASN B 213 ? 0.9864 0.7561 1.1131 0.1312  -0.0372 -0.0250 205 ASN B O   
2833 C CB  . ASN B 213 ? 0.9971 0.8084 1.1978 0.1539  -0.0594 -0.0555 205 ASN B CB  
2834 C CG  . ASN B 213 ? 1.1402 0.9008 1.3181 0.1763  -0.0738 -0.0525 205 ASN B CG  
2835 O OD1 . ASN B 213 ? 1.2199 0.9572 1.3634 0.1798  -0.0739 -0.0363 205 ASN B OD1 
2836 N ND2 . ASN B 213 ? 1.1586 0.9116 1.3441 0.1841  -0.0801 -0.0643 205 ASN B ND2 
2837 N N   . ARG B 214 ? 1.0010 0.8052 1.1668 0.1111  -0.0271 -0.0510 206 ARG B N   
2838 C CA  . ARG B 214 ? 1.0523 0.8275 1.1952 0.1007  -0.0201 -0.0499 206 ARG B CA  
2839 C C   . ARG B 214 ? 1.0515 0.8386 1.1766 0.0821  -0.0101 -0.0317 206 ARG B C   
2840 O O   . ARG B 214 ? 1.0459 0.8033 1.1454 0.0800  -0.0075 -0.0215 206 ARG B O   
2841 C CB  . ARG B 214 ? 1.0074 0.7867 1.1626 0.0891  -0.0128 -0.0679 206 ARG B CB  
2842 C CG  . ARG B 214 ? 1.0991 0.8468 1.2287 0.0753  -0.0069 -0.0673 206 ARG B CG  
2843 C CD  . ARG B 214 ? 1.1736 0.8668 1.2798 0.0928  -0.0169 -0.0673 206 ARG B CD  
2844 N NE  . ARG B 214 ? 1.2196 0.8844 1.2925 0.0780  -0.0116 -0.0533 206 ARG B NE  
2845 C CZ  . ARG B 214 ? 1.4492 1.0661 1.4915 0.0884  -0.0177 -0.0455 206 ARG B CZ  
2846 N NH1 . ARG B 214 ? 1.4829 1.0716 1.5215 0.1156  -0.0321 -0.0504 206 ARG B NH1 
2847 N NH2 . ARG B 214 ? 1.4244 1.0196 1.4383 0.0704  -0.0099 -0.0322 206 ARG B NH2 
2848 N N   . TRP B 215 ? 0.9767 0.8067 1.1154 0.0680  -0.0045 -0.0278 207 TRP B N   
2849 C CA  . TRP B 215 ? 0.9537 0.8013 1.0826 0.0509  0.0036  -0.0121 207 TRP B CA  
2850 C C   . TRP B 215 ? 0.9408 0.7778 1.0529 0.0647  0.0018  0.0051  207 TRP B C   
2851 O O   . TRP B 215 ? 0.9556 0.7825 1.0516 0.0562  0.0097  0.0172  207 TRP B O   
2852 C CB  . TRP B 215 ? 0.9266 0.8191 1.0721 0.0372  0.0060  -0.0126 207 TRP B CB  
2853 C CG  . TRP B 215 ? 0.9012 0.8160 1.0426 0.0210  0.0118  0.0017  207 TRP B CG  
2854 C CD1 . TRP B 215 ? 0.8314 0.7475 0.9696 -0.0014 0.0187  0.0035  207 TRP B CD1 
2855 C CD2 . TRP B 215 ? 0.8099 0.7499 0.9522 0.0267  0.0101  0.0158  207 TRP B CD2 
2856 N NE1 . TRP B 215 ? 0.7428 0.6874 0.8849 -0.0106 0.0216  0.0175  207 TRP B NE1 
2857 C CE2 . TRP B 215 ? 0.7554 0.7153 0.8995 0.0075  0.0170  0.0249  207 TRP B CE2 
2858 C CE3 . TRP B 215 ? 0.8024 0.7491 0.9439 0.0467  0.0023  0.0211  207 TRP B CE3 
2859 C CZ2 . TRP B 215 ? 0.7860 0.7753 0.9341 0.0093  0.0175  0.0383  207 TRP B CZ2 
2860 C CZ3 . TRP B 215 ? 0.7874 0.7585 0.9271 0.0487  0.0026  0.0346  207 TRP B CZ3 
2861 C CH2 . TRP B 215 ? 0.7720 0.7657 0.9163 0.0310  0.0107  0.0427  207 TRP B CH2 
2862 N N   . VAL B 216 ? 0.9597 0.7975 1.0744 0.0858  -0.0084 0.0063  208 VAL B N   
2863 C CA  . VAL B 216 ? 0.9902 0.8153 1.0843 0.1013  -0.0105 0.0222  208 VAL B CA  
2864 C C   . VAL B 216 ? 0.9747 0.7503 1.0399 0.1081  -0.0085 0.0270  208 VAL B C   
2865 O O   . VAL B 216 ? 0.9621 0.7277 1.0052 0.1087  -0.0004 0.0424  208 VAL B O   
2866 C CB  . VAL B 216 ? 0.9763 0.8017 1.0749 0.1238  -0.0256 0.0204  208 VAL B CB  
2867 C CG1 . VAL B 216 ? 0.9166 0.7130 0.9852 0.1442  -0.0298 0.0346  208 VAL B CG1 
2868 C CG2 . VAL B 216 ? 0.9318 0.8028 1.0498 0.1157  -0.0266 0.0204  208 VAL B CG2 
2869 N N   . ALA B 217 ? 0.9996 0.7418 1.0630 0.1140  -0.0156 0.0136  209 ALA B N   
2870 C CA  . ALA B 217 ? 1.0555 0.7435 1.0863 0.1195  -0.0156 0.0171  209 ALA B CA  
2871 C C   . ALA B 217 ? 1.0463 0.7344 1.0653 0.0940  0.0009  0.0260  209 ALA B C   
2872 O O   . ALA B 217 ? 1.0133 0.6685 1.0010 0.0936  0.0073  0.0385  209 ALA B O   
2873 C CB  . ALA B 217 ? 1.1658 0.8209 1.2004 0.1309  -0.0283 -0.0014 209 ALA B CB  
2874 N N   . GLU B 218 ? 1.0107 0.7340 1.0531 0.0714  0.0077  0.0199  210 GLU B N   
2875 C CA  . GLU B 218 ? 1.0331 0.7597 1.0693 0.0446  0.0207  0.0274  210 GLU B CA  
2876 C C   . GLU B 218 ? 0.9317 0.6880 0.9681 0.0359  0.0327  0.0465  210 GLU B C   
2877 O O   . GLU B 218 ? 0.8624 0.6228 0.8961 0.0133  0.0439  0.0549  210 GLU B O   
2878 C CB  . GLU B 218 ? 1.0286 0.7835 1.0881 0.0241  0.0221  0.0151  210 GLU B CB  
2879 C CG  . GLU B 218 ? 1.0763 0.8048 1.1366 0.0301  0.0143  -0.0049 210 GLU B CG  
2880 C CD  . GLU B 218 ? 1.0992 0.8556 1.1780 0.0107  0.0175  -0.0164 210 GLU B CD  
2881 O OE1 . GLU B 218 ? 1.0415 0.8284 1.1272 -0.0104 0.0241  -0.0076 210 GLU B OE1 
2882 O OE2 . GLU B 218 ? 1.0871 0.8344 1.1730 0.0172  0.0134  -0.0344 210 GLU B OE2 
2883 N N   . GLN B 219 ? 0.9576 0.7360 0.9991 0.0528  0.0302  0.0530  211 GLN B N   
2884 C CA  . GLN B 219 ? 1.1008 0.9074 1.1425 0.0490  0.0419  0.0702  211 GLN B CA  
2885 C C   . GLN B 219 ? 1.1631 0.9280 1.1687 0.0645  0.0476  0.0830  211 GLN B C   
2886 O O   . GLN B 219 ? 1.2499 1.0115 1.2440 0.0874  0.0435  0.0885  211 GLN B O   
2887 C CB  . GLN B 219 ? 1.0292 0.8795 1.0908 0.0595  0.0360  0.0709  211 GLN B CB  
2888 C CG  . GLN B 219 ? 0.9363 0.8215 1.0267 0.0468  0.0292  0.0580  211 GLN B CG  
2889 C CD  . GLN B 219 ? 0.9543 0.8621 1.0594 0.0170  0.0374  0.0579  211 GLN B CD  
2890 O OE1 . GLN B 219 ? 0.8943 0.8339 1.0099 0.0058  0.0452  0.0689  211 GLN B OE1 
2891 N NE2 . GLN B 219 ? 0.9489 0.8401 1.0557 0.0046  0.0347  0.0447  211 GLN B NE2 
# 
