data_8YK6
# 
_entry.id   8YK6 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   8YK6         pdb_00008yk6 10.2210/pdb8yk6/pdb 
WWPDB D_1300045436 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-02-26 
_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                        8YK6 
_pdbx_database_status.recvd_initial_deposition_date   2024-03-04 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              makisyou@ifst.ous.ac.jp 
_pdbx_contact_author.name_first         Syou 
_pdbx_contact_author.name_last          Maki 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-9972-5946 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Nakabayashi, M.' 1 0000-0002-4751-6667 
'Inaka, K.'       2 ?                   
'Fujiwara, M.'    3 0009-0001-3042-5507 
'Hagiwara, M.'    4 0000-0002-1087-521X 
'Maki, S.'        5 0000-0002-9972-5946 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Plos One' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1932-6203 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            20 
_citation.language                  ? 
_citation.page_first                e0315335 
_citation.page_last                 e0315335 
_citation.title                     
'Magnetic effects of thaumatin crystals; observation of crystal growth by magneto-Archimedes levitation and magnetic orientation.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1371/journal.pone.0315335 
_citation.pdbx_database_id_PubMed   39946396 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Maki, S.'        1 0000-0002-9972-5946 
primary 'Fujiwara, M.'    2 ?                   
primary 'Fujiwara, Y.'    3 ?                   
primary 'Nakabayashi, M.' 4 ?                   
primary 'Morimoto, S.'    5 ?                   
primary 'Tanaka, S.'      6 ?                   
primary 'Fujiwara, S.'    7 ?                   
primary 'Hagiwara, M.'    8 ?                   
primary 'Inaka, K.'       9 ?                   
# 
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     nat 'Thaumatin I'        22228.043 1   ? ? ? ? 
2 non-polymer syn 'L(+)-TARTARIC ACID' 150.087   1   ? ? ? ? 
3 water       nat water                18.015    347 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        Thaumatin-1 
# 
_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       
;ATFEIVNRCSYTVWAAASKGDAALDAGGRQLNSGESWTINVEPGTNGGKIWARTDCYFDDSGSGICKTGDCGGLLRCKRF
GRPPTTLAEFSLNQYGKDYIDISNIKGFNVPMDFSPTTRGCRGVRCAADIVGQCPAKLKAPGGGCNDACTVFQTSEYCCT
TGKCGPTEYSRFFKRLCPDAFSYVLDKPTTVTCPGSSNYRVTFCPTA
;
_entity_poly.pdbx_seq_one_letter_code_can   
;ATFEIVNRCSYTVWAAASKGDAALDAGGRQLNSGESWTINVEPGTNGGKIWARTDCYFDDSGSGICKTGDCGGLLRCKRF
GRPPTTLAEFSLNQYGKDYIDISNIKGFNVPMDFSPTTRGCRGVRCAADIVGQCPAKLKAPGGGCNDACTVFQTSEYCCT
TGKCGPTEYSRFFKRLCPDAFSYVLDKPTTVTCPGSSNYRVTFCPTA
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'L(+)-TARTARIC ACID' TLA 
3 water                HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   ALA n 
1 2   THR n 
1 3   PHE n 
1 4   GLU n 
1 5   ILE n 
1 6   VAL n 
1 7   ASN n 
1 8   ARG n 
1 9   CYS n 
1 10  SER n 
1 11  TYR n 
1 12  THR n 
1 13  VAL n 
1 14  TRP n 
1 15  ALA n 
1 16  ALA n 
1 17  ALA n 
1 18  SER n 
1 19  LYS n 
1 20  GLY n 
1 21  ASP n 
1 22  ALA n 
1 23  ALA n 
1 24  LEU n 
1 25  ASP n 
1 26  ALA n 
1 27  GLY n 
1 28  GLY n 
1 29  ARG n 
1 30  GLN n 
1 31  LEU n 
1 32  ASN n 
1 33  SER n 
1 34  GLY n 
1 35  GLU n 
1 36  SER n 
1 37  TRP n 
1 38  THR n 
1 39  ILE n 
1 40  ASN n 
1 41  VAL n 
1 42  GLU n 
1 43  PRO n 
1 44  GLY n 
1 45  THR n 
1 46  ASN n 
1 47  GLY n 
1 48  GLY n 
1 49  LYS n 
1 50  ILE n 
1 51  TRP n 
1 52  ALA n 
1 53  ARG n 
1 54  THR n 
1 55  ASP n 
1 56  CYS n 
1 57  TYR n 
1 58  PHE n 
1 59  ASP n 
1 60  ASP n 
1 61  SER n 
1 62  GLY n 
1 63  SER n 
1 64  GLY n 
1 65  ILE n 
1 66  CYS n 
1 67  LYS n 
1 68  THR n 
1 69  GLY n 
1 70  ASP n 
1 71  CYS n 
1 72  GLY n 
1 73  GLY n 
1 74  LEU n 
1 75  LEU n 
1 76  ARG n 
1 77  CYS n 
1 78  LYS n 
1 79  ARG n 
1 80  PHE n 
1 81  GLY n 
1 82  ARG n 
1 83  PRO n 
1 84  PRO n 
1 85  THR n 
1 86  THR n 
1 87  LEU n 
1 88  ALA n 
1 89  GLU n 
1 90  PHE n 
1 91  SER n 
1 92  LEU n 
1 93  ASN n 
1 94  GLN n 
1 95  TYR n 
1 96  GLY n 
1 97  LYS n 
1 98  ASP n 
1 99  TYR n 
1 100 ILE n 
1 101 ASP n 
1 102 ILE n 
1 103 SER n 
1 104 ASN n 
1 105 ILE n 
1 106 LYS n 
1 107 GLY n 
1 108 PHE n 
1 109 ASN n 
1 110 VAL n 
1 111 PRO n 
1 112 MET n 
1 113 ASP n 
1 114 PHE n 
1 115 SER n 
1 116 PRO n 
1 117 THR n 
1 118 THR n 
1 119 ARG n 
1 120 GLY n 
1 121 CYS n 
1 122 ARG n 
1 123 GLY n 
1 124 VAL n 
1 125 ARG n 
1 126 CYS n 
1 127 ALA n 
1 128 ALA n 
1 129 ASP n 
1 130 ILE n 
1 131 VAL n 
1 132 GLY n 
1 133 GLN n 
1 134 CYS n 
1 135 PRO n 
1 136 ALA n 
1 137 LYS n 
1 138 LEU n 
1 139 LYS n 
1 140 ALA n 
1 141 PRO n 
1 142 GLY n 
1 143 GLY n 
1 144 GLY n 
1 145 CYS n 
1 146 ASN n 
1 147 ASP n 
1 148 ALA n 
1 149 CYS n 
1 150 THR n 
1 151 VAL n 
1 152 PHE n 
1 153 GLN n 
1 154 THR n 
1 155 SER n 
1 156 GLU n 
1 157 TYR n 
1 158 CYS n 
1 159 CYS n 
1 160 THR n 
1 161 THR n 
1 162 GLY n 
1 163 LYS n 
1 164 CYS n 
1 165 GLY n 
1 166 PRO n 
1 167 THR n 
1 168 GLU n 
1 169 TYR n 
1 170 SER n 
1 171 ARG n 
1 172 PHE n 
1 173 PHE n 
1 174 LYS n 
1 175 ARG n 
1 176 LEU n 
1 177 CYS n 
1 178 PRO n 
1 179 ASP n 
1 180 ALA n 
1 181 PHE n 
1 182 SER n 
1 183 TYR n 
1 184 VAL n 
1 185 LEU n 
1 186 ASP n 
1 187 LYS n 
1 188 PRO n 
1 189 THR n 
1 190 THR n 
1 191 VAL n 
1 192 THR n 
1 193 CYS n 
1 194 PRO n 
1 195 GLY n 
1 196 SER n 
1 197 SER n 
1 198 ASN n 
1 199 TYR n 
1 200 ARG n 
1 201 VAL n 
1 202 THR n 
1 203 PHE n 
1 204 CYS n 
1 205 PRO n 
1 206 THR n 
1 207 ALA n 
# 
_entity_src_nat.entity_id                  1 
_entity_src_nat.pdbx_src_id                1 
_entity_src_nat.pdbx_alt_source_flag       sample 
_entity_src_nat.pdbx_beg_seq_num           1 
_entity_src_nat.pdbx_end_seq_num           207 
_entity_src_nat.common_name                ? 
_entity_src_nat.pdbx_organism_scientific   'Thaumatococcus daniellii' 
_entity_src_nat.pdbx_ncbi_taxonomy_id      4621 
_entity_src_nat.genus                      ? 
_entity_src_nat.species                    ? 
_entity_src_nat.strain                     ? 
_entity_src_nat.tissue                     ? 
_entity_src_nat.tissue_fraction            ? 
_entity_src_nat.pdbx_secretion             ? 
_entity_src_nat.pdbx_fragment              ? 
_entity_src_nat.pdbx_variant               ? 
_entity_src_nat.pdbx_cell_line             ? 
_entity_src_nat.pdbx_atcc                  ? 
_entity_src_nat.pdbx_cellular_location     ? 
_entity_src_nat.pdbx_organ                 ? 
_entity_src_nat.pdbx_organelle             ? 
_entity_src_nat.pdbx_cell                  ? 
_entity_src_nat.pdbx_plasmid_name          ? 
_entity_src_nat.pdbx_plasmid_details       ? 
_entity_src_nat.details                    ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE              ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE             ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE           ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'      ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE             ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE            ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'      ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE              ? 'C2 H5 N O2'     75.067  
HOH non-polymer         . WATER                ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE           ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE              ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE               ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE           ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE        ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE              ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE               ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE            ? 'C4 H9 N O3'     119.119 
TLA non-polymer         . 'L(+)-TARTARIC ACID' ? 'C4 H6 O6'       150.087 
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   ALA 1   1   1   ALA ALA A . n 
A 1 2   THR 2   2   2   THR THR A . n 
A 1 3   PHE 3   3   3   PHE PHE A . n 
A 1 4   GLU 4   4   4   GLU GLU A . n 
A 1 5   ILE 5   5   5   ILE ILE A . n 
A 1 6   VAL 6   6   6   VAL VAL A . n 
A 1 7   ASN 7   7   7   ASN ASN A . n 
A 1 8   ARG 8   8   8   ARG ARG A . n 
A 1 9   CYS 9   9   9   CYS CYS A . n 
A 1 10  SER 10  10  10  SER SER A . n 
A 1 11  TYR 11  11  11  TYR TYR A . n 
A 1 12  THR 12  12  12  THR THR A . n 
A 1 13  VAL 13  13  13  VAL VAL A . n 
A 1 14  TRP 14  14  14  TRP TRP A . n 
A 1 15  ALA 15  15  15  ALA ALA A . n 
A 1 16  ALA 16  16  16  ALA ALA A . n 
A 1 17  ALA 17  17  17  ALA ALA A . n 
A 1 18  SER 18  18  18  SER SER A . n 
A 1 19  LYS 19  19  19  LYS LYS A . n 
A 1 20  GLY 20  20  20  GLY GLY A . n 
A 1 21  ASP 21  21  21  ASP ASP A . n 
A 1 22  ALA 22  22  22  ALA ALA A . n 
A 1 23  ALA 23  23  23  ALA ALA A . n 
A 1 24  LEU 24  24  24  LEU LEU A . n 
A 1 25  ASP 25  25  25  ASP ASP A . n 
A 1 26  ALA 26  26  26  ALA ALA A . n 
A 1 27  GLY 27  27  27  GLY GLY A . n 
A 1 28  GLY 28  28  28  GLY GLY A . n 
A 1 29  ARG 29  29  29  ARG ARG A . n 
A 1 30  GLN 30  30  30  GLN GLN A . n 
A 1 31  LEU 31  31  31  LEU LEU A . n 
A 1 32  ASN 32  32  32  ASN ASN A . n 
A 1 33  SER 33  33  33  SER SER A . n 
A 1 34  GLY 34  34  34  GLY GLY A . n 
A 1 35  GLU 35  35  35  GLU GLU A . n 
A 1 36  SER 36  36  36  SER SER A . n 
A 1 37  TRP 37  37  37  TRP TRP A . n 
A 1 38  THR 38  38  38  THR THR A . n 
A 1 39  ILE 39  39  39  ILE ILE A . n 
A 1 40  ASN 40  40  40  ASN ASN A . n 
A 1 41  VAL 41  41  41  VAL VAL A . n 
A 1 42  GLU 42  42  42  GLU GLU A . n 
A 1 43  PRO 43  43  43  PRO PRO A . n 
A 1 44  GLY 44  44  44  GLY GLY A . n 
A 1 45  THR 45  45  45  THR THR A . n 
A 1 46  ASN 46  46  46  ASN ASN A . n 
A 1 47  GLY 47  47  47  GLY GLY A . n 
A 1 48  GLY 48  48  48  GLY GLY A . n 
A 1 49  LYS 49  49  49  LYS LYS A . n 
A 1 50  ILE 50  50  50  ILE ILE A . n 
A 1 51  TRP 51  51  51  TRP TRP A . n 
A 1 52  ALA 52  52  52  ALA ALA A . n 
A 1 53  ARG 53  53  53  ARG ARG A . n 
A 1 54  THR 54  54  54  THR THR A . n 
A 1 55  ASP 55  55  55  ASP ASP A . n 
A 1 56  CYS 56  56  56  CYS CYS A . n 
A 1 57  TYR 57  57  57  TYR TYR A . n 
A 1 58  PHE 58  58  58  PHE PHE A . n 
A 1 59  ASP 59  59  59  ASP ASP A . n 
A 1 60  ASP 60  60  60  ASP ASP A . n 
A 1 61  SER 61  61  61  SER SER A . n 
A 1 62  GLY 62  62  62  GLY GLY A . n 
A 1 63  SER 63  63  63  SER SER A . n 
A 1 64  GLY 64  64  64  GLY GLY A . n 
A 1 65  ILE 65  65  65  ILE ILE A . n 
A 1 66  CYS 66  66  66  CYS CYS A . n 
A 1 67  LYS 67  67  67  LYS LYS A . n 
A 1 68  THR 68  68  68  THR THR A . n 
A 1 69  GLY 69  69  69  GLY GLY A . n 
A 1 70  ASP 70  70  70  ASP ASP A . n 
A 1 71  CYS 71  71  71  CYS CYS A . n 
A 1 72  GLY 72  72  72  GLY GLY A . n 
A 1 73  GLY 73  73  73  GLY GLY A . n 
A 1 74  LEU 74  74  74  LEU LEU A . n 
A 1 75  LEU 75  75  75  LEU LEU A . n 
A 1 76  ARG 76  76  76  ARG ARG A . n 
A 1 77  CYS 77  77  77  CYS CYS A . n 
A 1 78  LYS 78  78  78  LYS LYS A . n 
A 1 79  ARG 79  79  79  ARG ARG A . n 
A 1 80  PHE 80  80  80  PHE PHE A . n 
A 1 81  GLY 81  81  81  GLY GLY A . n 
A 1 82  ARG 82  82  82  ARG ARG A . n 
A 1 83  PRO 83  83  83  PRO PRO A . n 
A 1 84  PRO 84  84  84  PRO PRO A . n 
A 1 85  THR 85  85  85  THR THR A . n 
A 1 86  THR 86  86  86  THR THR A . n 
A 1 87  LEU 87  87  87  LEU LEU A . n 
A 1 88  ALA 88  88  88  ALA ALA A . n 
A 1 89  GLU 89  89  89  GLU GLU A . n 
A 1 90  PHE 90  90  90  PHE PHE A . n 
A 1 91  SER 91  91  91  SER SER A . n 
A 1 92  LEU 92  92  92  LEU LEU A . n 
A 1 93  ASN 93  93  93  ASN ASN A . n 
A 1 94  GLN 94  94  94  GLN GLN A . n 
A 1 95  TYR 95  95  95  TYR TYR A . n 
A 1 96  GLY 96  96  96  GLY GLY A . n 
A 1 97  LYS 97  97  97  LYS LYS A . n 
A 1 98  ASP 98  98  98  ASP ASP A . n 
A 1 99  TYR 99  99  99  TYR TYR A . n 
A 1 100 ILE 100 100 100 ILE ILE A . n 
A 1 101 ASP 101 101 101 ASP ASP A . n 
A 1 102 ILE 102 102 102 ILE ILE A . n 
A 1 103 SER 103 103 103 SER SER A . n 
A 1 104 ASN 104 104 104 ASN ASN A . n 
A 1 105 ILE 105 105 105 ILE ILE A . n 
A 1 106 LYS 106 106 106 LYS LYS A . n 
A 1 107 GLY 107 107 107 GLY GLY A . n 
A 1 108 PHE 108 108 108 PHE PHE A . n 
A 1 109 ASN 109 109 109 ASN ASN A . n 
A 1 110 VAL 110 110 110 VAL VAL A . n 
A 1 111 PRO 111 111 111 PRO PRO A . n 
A 1 112 MET 112 112 112 MET MET A . n 
A 1 113 ASP 113 113 113 ASP ASP A . n 
A 1 114 PHE 114 114 114 PHE PHE A . n 
A 1 115 SER 115 115 115 SER SER A . n 
A 1 116 PRO 116 116 116 PRO PRO A . n 
A 1 117 THR 117 117 117 THR THR A . n 
A 1 118 THR 118 118 118 THR THR A . n 
A 1 119 ARG 119 119 119 ARG ARG A . n 
A 1 120 GLY 120 120 120 GLY GLY A . n 
A 1 121 CYS 121 121 121 CYS CYS A . n 
A 1 122 ARG 122 122 122 ARG ARG A . n 
A 1 123 GLY 123 123 123 GLY GLY A . n 
A 1 124 VAL 124 124 124 VAL VAL A . n 
A 1 125 ARG 125 125 125 ARG ARG A . n 
A 1 126 CYS 126 126 126 CYS CYS A . n 
A 1 127 ALA 127 127 127 ALA ALA A . n 
A 1 128 ALA 128 128 128 ALA ALA A . n 
A 1 129 ASP 129 129 129 ASP ASP A . n 
A 1 130 ILE 130 130 130 ILE ILE A . n 
A 1 131 VAL 131 131 131 VAL VAL A . n 
A 1 132 GLY 132 132 132 GLY GLY A . n 
A 1 133 GLN 133 133 133 GLN GLN A . n 
A 1 134 CYS 134 134 134 CYS CYS A . n 
A 1 135 PRO 135 135 135 PRO PRO A . n 
A 1 136 ALA 136 136 136 ALA ALA A . n 
A 1 137 LYS 137 137 137 LYS LYS A . n 
A 1 138 LEU 138 138 138 LEU LEU A . n 
A 1 139 LYS 139 139 139 LYS LYS A . n 
A 1 140 ALA 140 140 140 ALA ALA A . n 
A 1 141 PRO 141 141 141 PRO PRO A . n 
A 1 142 GLY 142 142 142 GLY GLY A . n 
A 1 143 GLY 143 143 143 GLY GLY A . n 
A 1 144 GLY 144 144 144 GLY GLY A . n 
A 1 145 CYS 145 145 145 CYS CYS A . n 
A 1 146 ASN 146 146 146 ASN ASN A . n 
A 1 147 ASP 147 147 147 ASP ASP A . n 
A 1 148 ALA 148 148 148 ALA ALA A . n 
A 1 149 CYS 149 149 149 CYS CYS A . n 
A 1 150 THR 150 150 150 THR THR A . n 
A 1 151 VAL 151 151 151 VAL VAL A . n 
A 1 152 PHE 152 152 152 PHE PHE A . n 
A 1 153 GLN 153 153 153 GLN GLN A . n 
A 1 154 THR 154 154 154 THR THR A . n 
A 1 155 SER 155 155 155 SER SER A . n 
A 1 156 GLU 156 156 156 GLU GLU A . n 
A 1 157 TYR 157 157 157 TYR TYR A . n 
A 1 158 CYS 158 158 158 CYS CYS A . n 
A 1 159 CYS 159 159 159 CYS CYS A . n 
A 1 160 THR 160 160 160 THR THR A . n 
A 1 161 THR 161 161 161 THR THR A . n 
A 1 162 GLY 162 162 162 GLY GLY A . n 
A 1 163 LYS 163 163 163 LYS LYS A . n 
A 1 164 CYS 164 164 164 CYS CYS A . n 
A 1 165 GLY 165 165 165 GLY GLY A . n 
A 1 166 PRO 166 166 166 PRO PRO A . n 
A 1 167 THR 167 167 167 THR THR A . n 
A 1 168 GLU 168 168 168 GLU GLU A . n 
A 1 169 TYR 169 169 169 TYR TYR A . n 
A 1 170 SER 170 170 170 SER SER A . n 
A 1 171 ARG 171 171 171 ARG ARG A . n 
A 1 172 PHE 172 172 172 PHE PHE A . n 
A 1 173 PHE 173 173 173 PHE PHE A . n 
A 1 174 LYS 174 174 174 LYS LYS A . n 
A 1 175 ARG 175 175 175 ARG ARG A . n 
A 1 176 LEU 176 176 176 LEU LEU A . n 
A 1 177 CYS 177 177 177 CYS CYS A . n 
A 1 178 PRO 178 178 178 PRO PRO A . n 
A 1 179 ASP 179 179 179 ASP ASP A . n 
A 1 180 ALA 180 180 180 ALA ALA A . n 
A 1 181 PHE 181 181 181 PHE PHE A . n 
A 1 182 SER 182 182 182 SER SER A . n 
A 1 183 TYR 183 183 183 TYR TYR A . n 
A 1 184 VAL 184 184 184 VAL VAL A . n 
A 1 185 LEU 185 185 185 LEU LEU A . n 
A 1 186 ASP 186 186 186 ASP ASP A . n 
A 1 187 LYS 187 187 187 LYS LYS A . n 
A 1 188 PRO 188 188 188 PRO PRO A . n 
A 1 189 THR 189 189 189 THR THR A . n 
A 1 190 THR 190 190 190 THR THR A . n 
A 1 191 VAL 191 191 191 VAL VAL A . n 
A 1 192 THR 192 192 192 THR THR A . n 
A 1 193 CYS 193 193 193 CYS CYS A . n 
A 1 194 PRO 194 194 194 PRO PRO A . n 
A 1 195 GLY 195 195 195 GLY GLY A . n 
A 1 196 SER 196 196 196 SER SER A . n 
A 1 197 SER 197 197 197 SER SER A . n 
A 1 198 ASN 198 198 198 ASN ASN A . n 
A 1 199 TYR 199 199 199 TYR TYR A . n 
A 1 200 ARG 200 200 200 ARG ARG A . n 
A 1 201 VAL 201 201 201 VAL VAL A . n 
A 1 202 THR 202 202 202 THR THR A . n 
A 1 203 PHE 203 203 203 PHE PHE A . n 
A 1 204 CYS 204 204 204 CYS CYS A . n 
A 1 205 PRO 205 205 205 PRO PRO A . n 
A 1 206 THR 206 206 206 THR THR A . n 
A 1 207 ALA 207 207 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        TLA 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   TLA 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 TLA 1   301 1   TLA TLA A . 
C 3 HOH 1   401 338 HOH HOH A . 
C 3 HOH 2   402 264 HOH HOH A . 
C 3 HOH 3   403 290 HOH HOH A . 
C 3 HOH 4   404 339 HOH HOH A . 
C 3 HOH 5   405 281 HOH HOH A . 
C 3 HOH 6   406 236 HOH HOH A . 
C 3 HOH 7   407 192 HOH HOH A . 
C 3 HOH 8   408 220 HOH HOH A . 
C 3 HOH 9   409 269 HOH HOH A . 
C 3 HOH 10  410 308 HOH HOH A . 
C 3 HOH 11  411 76  HOH HOH A . 
C 3 HOH 12  412 50  HOH HOH A . 
C 3 HOH 13  413 268 HOH HOH A . 
C 3 HOH 14  414 161 HOH HOH A . 
C 3 HOH 15  415 135 HOH HOH A . 
C 3 HOH 16  416 69  HOH HOH A . 
C 3 HOH 17  417 86  HOH HOH A . 
C 3 HOH 18  418 147 HOH HOH A . 
C 3 HOH 19  419 90  HOH HOH A . 
C 3 HOH 20  420 4   HOH HOH A . 
C 3 HOH 21  421 149 HOH HOH A . 
C 3 HOH 22  422 55  HOH HOH A . 
C 3 HOH 23  423 115 HOH HOH A . 
C 3 HOH 24  424 341 HOH HOH A . 
C 3 HOH 25  425 222 HOH HOH A . 
C 3 HOH 26  426 267 HOH HOH A . 
C 3 HOH 27  427 169 HOH HOH A . 
C 3 HOH 28  428 225 HOH HOH A . 
C 3 HOH 29  429 81  HOH HOH A . 
C 3 HOH 30  430 230 HOH HOH A . 
C 3 HOH 31  431 232 HOH HOH A . 
C 3 HOH 32  432 37  HOH HOH A . 
C 3 HOH 33  433 223 HOH HOH A . 
C 3 HOH 34  434 54  HOH HOH A . 
C 3 HOH 35  435 165 HOH HOH A . 
C 3 HOH 36  436 209 HOH HOH A . 
C 3 HOH 37  437 80  HOH HOH A . 
C 3 HOH 38  438 70  HOH HOH A . 
C 3 HOH 39  439 313 HOH HOH A . 
C 3 HOH 40  440 314 HOH HOH A . 
C 3 HOH 41  441 347 HOH HOH A . 
C 3 HOH 42  442 49  HOH HOH A . 
C 3 HOH 43  443 87  HOH HOH A . 
C 3 HOH 44  444 216 HOH HOH A . 
C 3 HOH 45  445 189 HOH HOH A . 
C 3 HOH 46  446 228 HOH HOH A . 
C 3 HOH 47  447 327 HOH HOH A . 
C 3 HOH 48  448 245 HOH HOH A . 
C 3 HOH 49  449 101 HOH HOH A . 
C 3 HOH 50  450 155 HOH HOH A . 
C 3 HOH 51  451 214 HOH HOH A . 
C 3 HOH 52  452 211 HOH HOH A . 
C 3 HOH 53  453 162 HOH HOH A . 
C 3 HOH 54  454 136 HOH HOH A . 
C 3 HOH 55  455 26  HOH HOH A . 
C 3 HOH 56  456 120 HOH HOH A . 
C 3 HOH 57  457 61  HOH HOH A . 
C 3 HOH 58  458 35  HOH HOH A . 
C 3 HOH 59  459 95  HOH HOH A . 
C 3 HOH 60  460 213 HOH HOH A . 
C 3 HOH 61  461 203 HOH HOH A . 
C 3 HOH 62  462 67  HOH HOH A . 
C 3 HOH 63  463 100 HOH HOH A . 
C 3 HOH 64  464 39  HOH HOH A . 
C 3 HOH 65  465 78  HOH HOH A . 
C 3 HOH 66  466 13  HOH HOH A . 
C 3 HOH 67  467 200 HOH HOH A . 
C 3 HOH 68  468 172 HOH HOH A . 
C 3 HOH 69  469 128 HOH HOH A . 
C 3 HOH 70  470 71  HOH HOH A . 
C 3 HOH 71  471 33  HOH HOH A . 
C 3 HOH 72  472 11  HOH HOH A . 
C 3 HOH 73  473 27  HOH HOH A . 
C 3 HOH 74  474 125 HOH HOH A . 
C 3 HOH 75  475 224 HOH HOH A . 
C 3 HOH 76  476 156 HOH HOH A . 
C 3 HOH 77  477 7   HOH HOH A . 
C 3 HOH 78  478 337 HOH HOH A . 
C 3 HOH 79  479 96  HOH HOH A . 
C 3 HOH 80  480 133 HOH HOH A . 
C 3 HOH 81  481 126 HOH HOH A . 
C 3 HOH 82  482 293 HOH HOH A . 
C 3 HOH 83  483 38  HOH HOH A . 
C 3 HOH 84  484 130 HOH HOH A . 
C 3 HOH 85  485 152 HOH HOH A . 
C 3 HOH 86  486 343 HOH HOH A . 
C 3 HOH 87  487 117 HOH HOH A . 
C 3 HOH 88  488 113 HOH HOH A . 
C 3 HOH 89  489 53  HOH HOH A . 
C 3 HOH 90  490 91  HOH HOH A . 
C 3 HOH 91  491 1   HOH HOH A . 
C 3 HOH 92  492 306 HOH HOH A . 
C 3 HOH 93  493 8   HOH HOH A . 
C 3 HOH 94  494 14  HOH HOH A . 
C 3 HOH 95  495 16  HOH HOH A . 
C 3 HOH 96  496 322 HOH HOH A . 
C 3 HOH 97  497 325 HOH HOH A . 
C 3 HOH 98  498 330 HOH HOH A . 
C 3 HOH 99  499 102 HOH HOH A . 
C 3 HOH 100 500 329 HOH HOH A . 
C 3 HOH 101 501 132 HOH HOH A . 
C 3 HOH 102 502 65  HOH HOH A . 
C 3 HOH 103 503 2   HOH HOH A . 
C 3 HOH 104 504 227 HOH HOH A . 
C 3 HOH 105 505 22  HOH HOH A . 
C 3 HOH 106 506 75  HOH HOH A . 
C 3 HOH 107 507 92  HOH HOH A . 
C 3 HOH 108 508 82  HOH HOH A . 
C 3 HOH 109 509 25  HOH HOH A . 
C 3 HOH 110 510 274 HOH HOH A . 
C 3 HOH 111 511 234 HOH HOH A . 
C 3 HOH 112 512 206 HOH HOH A . 
C 3 HOH 113 513 184 HOH HOH A . 
C 3 HOH 114 514 110 HOH HOH A . 
C 3 HOH 115 515 226 HOH HOH A . 
C 3 HOH 116 516 42  HOH HOH A . 
C 3 HOH 117 517 85  HOH HOH A . 
C 3 HOH 118 518 73  HOH HOH A . 
C 3 HOH 119 519 276 HOH HOH A . 
C 3 HOH 120 520 98  HOH HOH A . 
C 3 HOH 121 521 127 HOH HOH A . 
C 3 HOH 122 522 242 HOH HOH A . 
C 3 HOH 123 523 124 HOH HOH A . 
C 3 HOH 124 524 36  HOH HOH A . 
C 3 HOH 125 525 190 HOH HOH A . 
C 3 HOH 126 526 46  HOH HOH A . 
C 3 HOH 127 527 57  HOH HOH A . 
C 3 HOH 128 528 43  HOH HOH A . 
C 3 HOH 129 529 217 HOH HOH A . 
C 3 HOH 130 530 51  HOH HOH A . 
C 3 HOH 131 531 210 HOH HOH A . 
C 3 HOH 132 532 183 HOH HOH A . 
C 3 HOH 133 533 23  HOH HOH A . 
C 3 HOH 134 534 175 HOH HOH A . 
C 3 HOH 135 535 109 HOH HOH A . 
C 3 HOH 136 536 103 HOH HOH A . 
C 3 HOH 137 537 150 HOH HOH A . 
C 3 HOH 138 538 15  HOH HOH A . 
C 3 HOH 139 539 291 HOH HOH A . 
C 3 HOH 140 540 66  HOH HOH A . 
C 3 HOH 141 541 29  HOH HOH A . 
C 3 HOH 142 542 10  HOH HOH A . 
C 3 HOH 143 543 316 HOH HOH A . 
C 3 HOH 144 544 202 HOH HOH A . 
C 3 HOH 145 545 59  HOH HOH A . 
C 3 HOH 146 546 12  HOH HOH A . 
C 3 HOH 147 547 201 HOH HOH A . 
C 3 HOH 148 548 219 HOH HOH A . 
C 3 HOH 149 549 68  HOH HOH A . 
C 3 HOH 150 550 167 HOH HOH A . 
C 3 HOH 151 551 18  HOH HOH A . 
C 3 HOH 152 552 118 HOH HOH A . 
C 3 HOH 153 553 44  HOH HOH A . 
C 3 HOH 154 554 215 HOH HOH A . 
C 3 HOH 155 555 28  HOH HOH A . 
C 3 HOH 156 556 311 HOH HOH A . 
C 3 HOH 157 557 62  HOH HOH A . 
C 3 HOH 158 558 122 HOH HOH A . 
C 3 HOH 159 559 24  HOH HOH A . 
C 3 HOH 160 560 205 HOH HOH A . 
C 3 HOH 161 561 19  HOH HOH A . 
C 3 HOH 162 562 177 HOH HOH A . 
C 3 HOH 163 563 111 HOH HOH A . 
C 3 HOH 164 564 5   HOH HOH A . 
C 3 HOH 165 565 138 HOH HOH A . 
C 3 HOH 166 566 256 HOH HOH A . 
C 3 HOH 167 567 204 HOH HOH A . 
C 3 HOH 168 568 309 HOH HOH A . 
C 3 HOH 169 569 123 HOH HOH A . 
C 3 HOH 170 570 168 HOH HOH A . 
C 3 HOH 171 571 262 HOH HOH A . 
C 3 HOH 172 572 131 HOH HOH A . 
C 3 HOH 173 573 148 HOH HOH A . 
C 3 HOH 174 574 9   HOH HOH A . 
C 3 HOH 175 575 83  HOH HOH A . 
C 3 HOH 176 576 186 HOH HOH A . 
C 3 HOH 177 577 324 HOH HOH A . 
C 3 HOH 178 578 207 HOH HOH A . 
C 3 HOH 179 579 20  HOH HOH A . 
C 3 HOH 180 580 238 HOH HOH A . 
C 3 HOH 181 581 104 HOH HOH A . 
C 3 HOH 182 582 77  HOH HOH A . 
C 3 HOH 183 583 34  HOH HOH A . 
C 3 HOH 184 584 89  HOH HOH A . 
C 3 HOH 185 585 108 HOH HOH A . 
C 3 HOH 186 586 218 HOH HOH A . 
C 3 HOH 187 587 52  HOH HOH A . 
C 3 HOH 188 588 328 HOH HOH A . 
C 3 HOH 189 589 79  HOH HOH A . 
C 3 HOH 190 590 84  HOH HOH A . 
C 3 HOH 191 591 164 HOH HOH A . 
C 3 HOH 192 592 326 HOH HOH A . 
C 3 HOH 193 593 259 HOH HOH A . 
C 3 HOH 194 594 119 HOH HOH A . 
C 3 HOH 195 595 17  HOH HOH A . 
C 3 HOH 196 596 64  HOH HOH A . 
C 3 HOH 197 597 32  HOH HOH A . 
C 3 HOH 198 598 21  HOH HOH A . 
C 3 HOH 199 599 31  HOH HOH A . 
C 3 HOH 200 600 56  HOH HOH A . 
C 3 HOH 201 601 332 HOH HOH A . 
C 3 HOH 202 602 40  HOH HOH A . 
C 3 HOH 203 603 58  HOH HOH A . 
C 3 HOH 204 604 231 HOH HOH A . 
C 3 HOH 205 605 45  HOH HOH A . 
C 3 HOH 206 606 208 HOH HOH A . 
C 3 HOH 207 607 323 HOH HOH A . 
C 3 HOH 208 608 3   HOH HOH A . 
C 3 HOH 209 609 141 HOH HOH A . 
C 3 HOH 210 610 251 HOH HOH A . 
C 3 HOH 211 611 261 HOH HOH A . 
C 3 HOH 212 612 310 HOH HOH A . 
C 3 HOH 213 613 72  HOH HOH A . 
C 3 HOH 214 614 247 HOH HOH A . 
C 3 HOH 215 615 199 HOH HOH A . 
C 3 HOH 216 616 212 HOH HOH A . 
C 3 HOH 217 617 170 HOH HOH A . 
C 3 HOH 218 618 180 HOH HOH A . 
C 3 HOH 219 619 107 HOH HOH A . 
C 3 HOH 220 620 142 HOH HOH A . 
C 3 HOH 221 621 304 HOH HOH A . 
C 3 HOH 222 622 188 HOH HOH A . 
C 3 HOH 223 623 157 HOH HOH A . 
C 3 HOH 224 624 6   HOH HOH A . 
C 3 HOH 225 625 99  HOH HOH A . 
C 3 HOH 226 626 197 HOH HOH A . 
C 3 HOH 227 627 334 HOH HOH A . 
C 3 HOH 228 628 140 HOH HOH A . 
C 3 HOH 229 629 129 HOH HOH A . 
C 3 HOH 230 630 346 HOH HOH A . 
C 3 HOH 231 631 233 HOH HOH A . 
C 3 HOH 232 632 272 HOH HOH A . 
C 3 HOH 233 633 237 HOH HOH A . 
C 3 HOH 234 634 241 HOH HOH A . 
C 3 HOH 235 635 221 HOH HOH A . 
C 3 HOH 236 636 114 HOH HOH A . 
C 3 HOH 237 637 181 HOH HOH A . 
C 3 HOH 238 638 137 HOH HOH A . 
C 3 HOH 239 639 270 HOH HOH A . 
C 3 HOH 240 640 258 HOH HOH A . 
C 3 HOH 241 641 285 HOH HOH A . 
C 3 HOH 242 642 154 HOH HOH A . 
C 3 HOH 243 643 60  HOH HOH A . 
C 3 HOH 244 644 195 HOH HOH A . 
C 3 HOH 245 645 146 HOH HOH A . 
C 3 HOH 246 646 239 HOH HOH A . 
C 3 HOH 247 647 106 HOH HOH A . 
C 3 HOH 248 648 249 HOH HOH A . 
C 3 HOH 249 649 252 HOH HOH A . 
C 3 HOH 250 650 254 HOH HOH A . 
C 3 HOH 251 651 173 HOH HOH A . 
C 3 HOH 252 652 153 HOH HOH A . 
C 3 HOH 253 653 196 HOH HOH A . 
C 3 HOH 254 654 263 HOH HOH A . 
C 3 HOH 255 655 187 HOH HOH A . 
C 3 HOH 256 656 121 HOH HOH A . 
C 3 HOH 257 657 296 HOH HOH A . 
C 3 HOH 258 658 253 HOH HOH A . 
C 3 HOH 259 659 336 HOH HOH A . 
C 3 HOH 260 660 88  HOH HOH A . 
C 3 HOH 261 661 166 HOH HOH A . 
C 3 HOH 262 662 139 HOH HOH A . 
C 3 HOH 263 663 94  HOH HOH A . 
C 3 HOH 264 664 282 HOH HOH A . 
C 3 HOH 265 665 303 HOH HOH A . 
C 3 HOH 266 666 178 HOH HOH A . 
C 3 HOH 267 667 289 HOH HOH A . 
C 3 HOH 268 668 134 HOH HOH A . 
C 3 HOH 269 669 344 HOH HOH A . 
C 3 HOH 270 670 299 HOH HOH A . 
C 3 HOH 271 671 255 HOH HOH A . 
C 3 HOH 272 672 260 HOH HOH A . 
C 3 HOH 273 673 47  HOH HOH A . 
C 3 HOH 274 674 342 HOH HOH A . 
C 3 HOH 275 675 317 HOH HOH A . 
C 3 HOH 276 676 143 HOH HOH A . 
C 3 HOH 277 677 116 HOH HOH A . 
C 3 HOH 278 678 280 HOH HOH A . 
C 3 HOH 279 679 63  HOH HOH A . 
C 3 HOH 280 680 257 HOH HOH A . 
C 3 HOH 281 681 240 HOH HOH A . 
C 3 HOH 282 682 97  HOH HOH A . 
C 3 HOH 283 683 198 HOH HOH A . 
C 3 HOH 284 684 48  HOH HOH A . 
C 3 HOH 285 685 179 HOH HOH A . 
C 3 HOH 286 686 112 HOH HOH A . 
C 3 HOH 287 687 331 HOH HOH A . 
C 3 HOH 288 688 176 HOH HOH A . 
C 3 HOH 289 689 300 HOH HOH A . 
C 3 HOH 290 690 286 HOH HOH A . 
C 3 HOH 291 691 277 HOH HOH A . 
C 3 HOH 292 692 182 HOH HOH A . 
C 3 HOH 293 693 194 HOH HOH A . 
C 3 HOH 294 694 151 HOH HOH A . 
C 3 HOH 295 695 160 HOH HOH A . 
C 3 HOH 296 696 312 HOH HOH A . 
C 3 HOH 297 697 273 HOH HOH A . 
C 3 HOH 298 698 248 HOH HOH A . 
C 3 HOH 299 699 297 HOH HOH A . 
C 3 HOH 300 700 321 HOH HOH A . 
C 3 HOH 301 701 271 HOH HOH A . 
C 3 HOH 302 702 266 HOH HOH A . 
C 3 HOH 303 703 93  HOH HOH A . 
C 3 HOH 304 704 243 HOH HOH A . 
C 3 HOH 305 705 246 HOH HOH A . 
C 3 HOH 306 706 333 HOH HOH A . 
C 3 HOH 307 707 301 HOH HOH A . 
C 3 HOH 308 708 288 HOH HOH A . 
C 3 HOH 309 709 244 HOH HOH A . 
C 3 HOH 310 710 275 HOH HOH A . 
C 3 HOH 311 711 335 HOH HOH A . 
C 3 HOH 312 712 163 HOH HOH A . 
C 3 HOH 313 713 193 HOH HOH A . 
C 3 HOH 314 714 105 HOH HOH A . 
C 3 HOH 315 715 174 HOH HOH A . 
C 3 HOH 316 716 315 HOH HOH A . 
C 3 HOH 317 717 185 HOH HOH A . 
C 3 HOH 318 718 235 HOH HOH A . 
C 3 HOH 319 719 159 HOH HOH A . 
C 3 HOH 320 720 279 HOH HOH A . 
C 3 HOH 321 721 340 HOH HOH A . 
C 3 HOH 322 722 265 HOH HOH A . 
C 3 HOH 323 723 191 HOH HOH A . 
C 3 HOH 324 724 171 HOH HOH A . 
C 3 HOH 325 725 307 HOH HOH A . 
C 3 HOH 326 726 278 HOH HOH A . 
C 3 HOH 327 727 319 HOH HOH A . 
C 3 HOH 328 728 74  HOH HOH A . 
C 3 HOH 329 729 320 HOH HOH A . 
C 3 HOH 330 730 158 HOH HOH A . 
C 3 HOH 331 731 283 HOH HOH A . 
C 3 HOH 332 732 30  HOH HOH A . 
C 3 HOH 333 733 284 HOH HOH A . 
C 3 HOH 334 734 287 HOH HOH A . 
C 3 HOH 335 735 229 HOH HOH A . 
C 3 HOH 336 736 305 HOH HOH A . 
C 3 HOH 337 737 294 HOH HOH A . 
C 3 HOH 338 738 298 HOH HOH A . 
C 3 HOH 339 739 145 HOH HOH A . 
C 3 HOH 340 740 41  HOH HOH A . 
C 3 HOH 341 741 144 HOH HOH A . 
C 3 HOH 342 742 345 HOH HOH A . 
C 3 HOH 343 743 302 HOH HOH A . 
C 3 HOH 344 744 295 HOH HOH A . 
C 3 HOH 345 745 250 HOH HOH A . 
C 3 HOH 346 746 318 HOH HOH A . 
C 3 HOH 347 747 292 HOH HOH A . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC  ? ? ? 5.8.0267 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .        2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? MOLREP  ? ? ? .        4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8YK6 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     58.083 
_cell.length_a_esd                 ? 
_cell.length_b                     58.083 
_cell.length_b_esd                 ? 
_cell.length_c                     150.470 
_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                         8YK6 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                92 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 41 21 2' 
_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                   8YK6 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.87 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          56.91 
_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          'BATCH MODE' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              6.5 
_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    '84 mM ADA pH 6.5, 42 mM GdCl3, 0.51 M NaK-tartrate, 0.017 % NaN3' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-05-16 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.775 
_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                        'SPRING-8 BEAMLINE BL45XU' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.775 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL45XU 
_diffrn_source.pdbx_synchrotron_site       SPring-8 
# 
_reflns.B_iso_Wilson_estimate                          8.176 
_reflns.entry_id                                       8YK6 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              0.99 
_reflns.d_resolution_low                               45.98 
_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                                     145471 
_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                           99.0 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                8.2 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          20.6 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                0.026 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_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                              ? 
_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                                    0.99 
_reflns_shell.d_res_low                                     1.00 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           3.5 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             7116 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               8.0 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               0.314 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.930 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          100.0 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            -0.17 
_refine.aniso_B[1][2]                            -0.00 
_refine.aniso_B[1][3]                            -0.00 
_refine.aniso_B[2][2]                            -0.17 
_refine.aniso_B[2][3]                            -0.00 
_refine.aniso_B[3][3]                            0.33 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               11.856 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.977 
_refine.correlation_coeff_Fo_to_Fc_free          0.975 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_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                                 8YK6 
_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                            0.99 
_refine.ls_d_res_low                             37.99 
_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                     138147 
_refine.ls_number_reflns_R_free                  7248 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.80 
_refine.ls_percent_reflns_R_free                 5.0 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.12639 
_refine.ls_R_factor_R_free                       0.13382 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.12598 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.017 
_refine.pdbx_overall_ESU_R_Free                  0.017 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             0.390 
_refine.overall_SU_ML                            0.010 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       0.99 
_refine_hist.d_res_low                        37.99 
_refine_hist.number_atoms_solvent             347 
_refine_hist.number_atoms_total               1902 
_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        1545 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         10 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.012  0.013  1922 ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.002  0.018  1708 ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.920  1.662  2631 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 1.596  1.589  3972 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 7.099  5.000  263  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 34.787 21.327 98   ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 11.706 15.000 299  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? 16.483 15.000 15   ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.088  0.200  254  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.009  0.020  2272 ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.002  0.020  466  ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 0.930  0.994  986  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 0.926  0.992  985  ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 1.354  1.507  1244 ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 1.354  1.508  1245 ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 1.239  1.187  936  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 1.239  1.187  935  ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 1.587  1.696  1378 ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 2.699  13.723 2196 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 2.115  12.387 2072 ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? 2.122  3.000  3630 ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       0.99 
_refine_ls_shell.d_res_low                        1.011 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             518 
_refine_ls_shell.number_reflns_R_work             10046 
_refine_ls_shell.percent_reflns_obs               99.96 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.193 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.pdbx_R_complete                  ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   ? 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
_refine_ls_shell.R_factor_R_free                  0.189 
# 
_struct.entry_id                     8YK6 
_struct.title                        
'Magnetic effects of thaumatin crystals; observation of the crystal growth of magneto-Archimedes levitation and magnetic orientation' 
_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        8YK6 
_struct_keywords.text            'Sweet-Tasting Protein Magneto-Archimedes Levitation, PLANT PROTEIN' 
_struct_keywords.pdbx_keywords   'PLANT PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    THM1_THADA 
_struct_ref.pdbx_db_accession          P02883 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;ATFEIVNRCSYTVWAAASKGDAALDAGGRQLNSGESWTINVEPGTNGGKIWARTDCYFDDSGSGICKTGDCGGLLRCKRF
GRPPTTLAEFSLNQYGKDYIDISNIKGFNVPMDFSPTTRGCRGVRCAADIVGQCPAKLKAPGGGCNDACTVFQTSEYCCT
TGKCGPTEYSRFFKRLCPDAFSYVLDKPTTVTCPGSSNYRVTFCPTA
;
_struct_ref.pdbx_align_begin           23 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              8YK6 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 207 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P02883 
_struct_ref_seq.db_align_beg                  23 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  229 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       207 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 ASP A 129 ? CYS A 134 ? ASP A 129 CYS A 134 1 ? 6  
HELX_P HELX_P2 AA2 PRO A 135 ? LYS A 139 ? PRO A 135 LYS A 139 5 ? 5  
HELX_P HELX_P3 AA3 ASP A 147 ? GLN A 153 ? ASP A 147 GLN A 153 1 ? 7  
HELX_P HELX_P4 AA4 THR A 154 ? CYS A 159 ? THR A 154 CYS A 159 1 ? 6  
HELX_P HELX_P5 AA5 THR A 167 ? CYS A 177 ? THR A 167 CYS A 177 1 ? 11 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1  disulf ? ? A CYS 9   SG ? ? ? 1_555 A CYS 204 SG ? ? A CYS 9   A CYS 204 1_555 ? ? ? ? ? ? ? 2.108 ? ? 
disulf2  disulf ? ? A CYS 56  SG A ? ? 1_555 A CYS 66  SG A ? A CYS 56  A CYS 66  1_555 ? ? ? ? ? ? ? 2.117 ? ? 
disulf3  disulf ? ? A CYS 56  SG B ? ? 1_555 A CYS 66  SG B ? A CYS 56  A CYS 66  1_555 ? ? ? ? ? ? ? 2.095 ? ? 
disulf4  disulf ? ? A CYS 71  SG A ? ? 1_555 A CYS 77  SG A ? A CYS 71  A CYS 77  1_555 ? ? ? ? ? ? ? 2.059 ? ? 
disulf5  disulf ? ? A CYS 71  SG B ? ? 1_555 A CYS 77  SG B ? A CYS 71  A CYS 77  1_555 ? ? ? ? ? ? ? 2.043 ? ? 
disulf6  disulf ? ? A CYS 121 SG ? ? ? 1_555 A CYS 193 SG ? ? A CYS 121 A CYS 193 1_555 ? ? ? ? ? ? ? 2.109 ? ? 
disulf7  disulf ? ? A CYS 126 SG ? ? ? 1_555 A CYS 177 SG ? ? A CYS 126 A CYS 177 1_555 ? ? ? ? ? ? ? 2.111 ? ? 
disulf8  disulf ? ? A CYS 134 SG ? ? ? 1_555 A CYS 145 SG ? ? A CYS 134 A CYS 145 1_555 ? ? ? ? ? ? ? 2.079 ? ? 
disulf9  disulf ? ? A CYS 149 SG ? ? ? 1_555 A CYS 158 SG ? ? A CYS 149 A CYS 158 1_555 ? ? ? ? ? ? ? 2.068 ? ? 
disulf10 disulf ? ? A CYS 159 SG A ? ? 1_555 A CYS 164 SG ? ? A CYS 159 A CYS 164 1_555 ? ? ? ? ? ? ? 2.018 ? ? 
disulf11 disulf ? ? A CYS 159 SG B ? ? 1_555 A CYS 164 SG ? ? A CYS 159 A CYS 164 1_555 ? ? ? ? ? ? ? 2.101 ? ? 
# 
_struct_conn_type.id          disulf 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1  CYS A 9   ? CYS A 204 ? CYS A 9   ? 1_555 CYS A 204 ? 1_555 SG SG . . . None 'Disulfide bridge' 
2  CYS A 56  A CYS A 66  A CYS A 56  ? 1_555 CYS A 66  ? 1_555 SG SG . . . None 'Disulfide bridge' 
3  CYS A 56  B CYS A 66  B CYS A 56  ? 1_555 CYS A 66  ? 1_555 SG SG . . . None 'Disulfide bridge' 
4  CYS A 71  A CYS A 77  A CYS A 71  ? 1_555 CYS A 77  ? 1_555 SG SG . . . None 'Disulfide bridge' 
5  CYS A 71  B CYS A 77  B CYS A 71  ? 1_555 CYS A 77  ? 1_555 SG SG . . . None 'Disulfide bridge' 
6  CYS A 121 ? CYS A 193 ? CYS A 121 ? 1_555 CYS A 193 ? 1_555 SG SG . . . None 'Disulfide bridge' 
7  CYS A 126 ? CYS A 177 ? CYS A 126 ? 1_555 CYS A 177 ? 1_555 SG SG . . . None 'Disulfide bridge' 
8  CYS A 134 ? CYS A 145 ? CYS A 134 ? 1_555 CYS A 145 ? 1_555 SG SG . . . None 'Disulfide bridge' 
9  CYS A 149 ? CYS A 158 ? CYS A 149 ? 1_555 CYS A 158 ? 1_555 SG SG . . . None 'Disulfide bridge' 
10 CYS A 159 A CYS A 164 ? CYS A 159 ? 1_555 CYS A 164 ? 1_555 SG SG . . . None 'Disulfide bridge' 
11 CYS A 159 B CYS A 164 ? CYS A 159 ? 1_555 CYS A 164 ? 1_555 SG SG . . . None 'Disulfide bridge' 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          PRO 
_struct_mon_prot_cis.label_seq_id           83 
_struct_mon_prot_cis.label_asym_id          A 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           PRO 
_struct_mon_prot_cis.auth_seq_id            83 
_struct_mon_prot_cis.auth_asym_id           A 
_struct_mon_prot_cis.pdbx_label_comp_id_2   PRO 
_struct_mon_prot_cis.pdbx_label_seq_id_2    84 
_struct_mon_prot_cis.pdbx_label_asym_id_2   A 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    PRO 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     84 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    A 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       4.72 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 6 ? 
AA3 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA3 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 SER A 36  ? ASN A 40  ? SER A 36  ASN A 40  
AA1 2 THR A 2   ? ASN A 7   ? THR A 2   ASN A 7   
AA1 3 TYR A 199 ? PHE A 203 ? TYR A 199 PHE A 203 
AA1 4 MET A 112 ? PRO A 116 ? MET A 112 PRO A 116 
AA1 5 VAL A 124 ? CYS A 126 ? VAL A 124 CYS A 126 
AA2 1 ALA A 23  ? LEU A 31  ? ALA A 23  LEU A 31  
AA2 2 VAL A 13  ? SER A 18  ? VAL A 13  SER A 18  
AA2 3 GLY A 48  ? ARG A 53  ? GLY A 48  ARG A 53  
AA2 4 LEU A 87  ? GLN A 94  ? LEU A 87  GLN A 94  
AA2 5 LYS A 97  ? SER A 103 ? LYS A 97  SER A 103 
AA2 6 VAL A 191 ? PRO A 194 ? VAL A 191 PRO A 194 
AA3 1 TYR A 57  ? PHE A 58  ? TYR A 57  PHE A 58  
AA3 2 GLY A 64  ? ILE A 65  ? GLY A 64  ILE A 65  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O TRP A 37  ? O TRP A 37  N ILE A 5   ? N ILE A 5   
AA1 2 3 N VAL A 6   ? N VAL A 6   O VAL A 201 ? O VAL A 201 
AA1 3 4 O ARG A 200 ? O ARG A 200 N SER A 115 ? N SER A 115 
AA1 4 5 N PHE A 114 ? N PHE A 114 O VAL A 124 ? O VAL A 124 
AA2 1 2 O LEU A 31  ? O LEU A 31  N VAL A 13  ? N VAL A 13  
AA2 2 3 N SER A 18  ? N SER A 18  O LYS A 49  ? O LYS A 49  
AA2 3 4 N ILE A 50  ? N ILE A 50  O ALA A 88  ? O ALA A 88  
AA2 4 5 N GLN A 94  ? N GLN A 94  O LYS A 97  ? O LYS A 97  
AA2 5 6 N ASP A 98  ? N ASP A 98  O CYS A 193 ? O CYS A 193 
AA3 1 2 N TYR A 57  ? N TYR A 57  O ILE A 65  ? O ILE A 65  
# 
_pdbx_entry_details.entry_id                   8YK6 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 NH2 A ARG 122 ? ? O   A HOH 402 ? ? 1.59 
2  1 OD2 A ASP 55  ? A O   A HOH 404 ? ? 1.69 
3  1 OD1 A ASP 179 ? B O   A HOH 405 ? ? 1.79 
4  1 OE1 A GLU 4   ? B NH2 A ARG 200 ? ? 2.00 
5  1 OE2 A GLU 35  ? B O   A HOH 406 ? ? 2.02 
6  1 NH2 A ARG 171 ? A O   A HOH 407 ? ? 2.10 
7  1 SG  A CYS 159 ? A O   A HOH 615 ? ? 2.15 
8  1 OH  A TYR 57  ? B O   A HOH 408 ? ? 2.16 
9  1 O   A SER 63  ? B O   A HOH 409 ? ? 2.18 
10 1 O   A HOH 610 ? ? O   A HOH 664 ? ? 2.19 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    NZ 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    LYS 
_pdbx_validate_symm_contact.auth_seq_id_1     67 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    B 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    O 
_pdbx_validate_symm_contact.auth_asym_id_2    A 
_pdbx_validate_symm_contact.auth_comp_id_2    HOH 
_pdbx_validate_symm_contact.auth_seq_id_2     698 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   6_554 
_pdbx_validate_symm_contact.dist              2.19 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 CB A ASP 70  ? B CG A ASP 70  ? B OD1 A ASP 70  ? B 125.75 118.30 7.45   0.90 N 
2 1 CB A ASP 70  ? B CG A ASP 70  ? B OD2 A ASP 70  ? B 111.10 118.30 -7.20  0.90 N 
3 1 CG A ARG 82  ? B CD A ARG 82  ? B NE  A ARG 82  ? B 86.36  111.80 -25.44 2.10 N 
4 1 NE A ARG 122 ? ? CZ A ARG 122 ? ? NH1 A ARG 122 ? ? 123.50 120.30 3.20   0.50 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 ASP A 25 ? ? 55.97   -138.28 
2 1 CYS A 71 ? A -112.59 75.65   
3 1 CYS A 71 ? B -117.41 74.50   
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 746 ? 6.26 . 
2 1 O ? A HOH 747 ? 6.26 . 
# 
_pdbx_unobs_or_zero_occ_residues.id               1 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num    1 
_pdbx_unobs_or_zero_occ_residues.polymer_flag     Y 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag   1 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id     A 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id     ALA 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id      207 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code     ? 
_pdbx_unobs_or_zero_occ_residues.label_asym_id    A 
_pdbx_unobs_or_zero_occ_residues.label_comp_id    ALA 
_pdbx_unobs_or_zero_occ_residues.label_seq_id     207 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
GLN N    N N N 88  
GLN CA   C N S 89  
GLN C    C N N 90  
GLN O    O N N 91  
GLN CB   C N N 92  
GLN CG   C N N 93  
GLN CD   C N N 94  
GLN OE1  O N N 95  
GLN NE2  N N N 96  
GLN OXT  O N N 97  
GLN H    H N N 98  
GLN H2   H N N 99  
GLN HA   H N N 100 
GLN HB2  H N N 101 
GLN HB3  H N N 102 
GLN HG2  H N N 103 
GLN HG3  H N N 104 
GLN HE21 H N N 105 
GLN HE22 H N N 106 
GLN HXT  H N N 107 
GLU N    N N N 108 
GLU CA   C N S 109 
GLU C    C N N 110 
GLU O    O N N 111 
GLU CB   C N N 112 
GLU CG   C N N 113 
GLU CD   C N N 114 
GLU OE1  O N N 115 
GLU OE2  O N N 116 
GLU OXT  O N N 117 
GLU H    H N N 118 
GLU H2   H N N 119 
GLU HA   H N N 120 
GLU HB2  H N N 121 
GLU HB3  H N N 122 
GLU HG2  H N N 123 
GLU HG3  H N N 124 
GLU HE2  H N N 125 
GLU HXT  H N N 126 
GLY N    N N N 127 
GLY CA   C N N 128 
GLY C    C N N 129 
GLY O    O N N 130 
GLY OXT  O N N 131 
GLY H    H N N 132 
GLY H2   H N N 133 
GLY HA2  H N N 134 
GLY HA3  H N N 135 
GLY HXT  H N N 136 
HOH O    O N N 137 
HOH H1   H N N 138 
HOH H2   H N N 139 
ILE N    N N N 140 
ILE CA   C N S 141 
ILE C    C N N 142 
ILE O    O N N 143 
ILE CB   C N S 144 
ILE CG1  C N N 145 
ILE CG2  C N N 146 
ILE CD1  C N N 147 
ILE OXT  O N N 148 
ILE H    H N N 149 
ILE H2   H N N 150 
ILE HA   H N N 151 
ILE HB   H N N 152 
ILE HG12 H N N 153 
ILE HG13 H N N 154 
ILE HG21 H N N 155 
ILE HG22 H N N 156 
ILE HG23 H N N 157 
ILE HD11 H N N 158 
ILE HD12 H N N 159 
ILE HD13 H N N 160 
ILE HXT  H N N 161 
LEU N    N N N 162 
LEU CA   C N S 163 
LEU C    C N N 164 
LEU O    O N N 165 
LEU CB   C N N 166 
LEU CG   C N N 167 
LEU CD1  C N N 168 
LEU CD2  C N N 169 
LEU OXT  O N N 170 
LEU H    H N N 171 
LEU H2   H N N 172 
LEU HA   H N N 173 
LEU HB2  H N N 174 
LEU HB3  H N N 175 
LEU HG   H N N 176 
LEU HD11 H N N 177 
LEU HD12 H N N 178 
LEU HD13 H N N 179 
LEU HD21 H N N 180 
LEU HD22 H N N 181 
LEU HD23 H N N 182 
LEU HXT  H N N 183 
LYS N    N N N 184 
LYS CA   C N S 185 
LYS C    C N N 186 
LYS O    O N N 187 
LYS CB   C N N 188 
LYS CG   C N N 189 
LYS CD   C N N 190 
LYS CE   C N N 191 
LYS NZ   N N N 192 
LYS OXT  O N N 193 
LYS H    H N N 194 
LYS H2   H N N 195 
LYS HA   H N N 196 
LYS HB2  H N N 197 
LYS HB3  H N N 198 
LYS HG2  H N N 199 
LYS HG3  H N N 200 
LYS HD2  H N N 201 
LYS HD3  H N N 202 
LYS HE2  H N N 203 
LYS HE3  H N N 204 
LYS HZ1  H N N 205 
LYS HZ2  H N N 206 
LYS HZ3  H N N 207 
LYS HXT  H N N 208 
MET N    N N N 209 
MET CA   C N S 210 
MET C    C N N 211 
MET O    O N N 212 
MET CB   C N N 213 
MET CG   C N N 214 
MET SD   S N N 215 
MET CE   C N N 216 
MET OXT  O N N 217 
MET H    H N N 218 
MET H2   H N N 219 
MET HA   H N N 220 
MET HB2  H N N 221 
MET HB3  H N N 222 
MET HG2  H N N 223 
MET HG3  H N N 224 
MET HE1  H N N 225 
MET HE2  H N N 226 
MET HE3  H N N 227 
MET HXT  H N N 228 
PHE N    N N N 229 
PHE CA   C N S 230 
PHE C    C N N 231 
PHE O    O N N 232 
PHE CB   C N N 233 
PHE CG   C Y N 234 
PHE CD1  C Y N 235 
PHE CD2  C Y N 236 
PHE CE1  C Y N 237 
PHE CE2  C Y N 238 
PHE CZ   C Y N 239 
PHE OXT  O N N 240 
PHE H    H N N 241 
PHE H2   H N N 242 
PHE HA   H N N 243 
PHE HB2  H N N 244 
PHE HB3  H N N 245 
PHE HD1  H N N 246 
PHE HD2  H N N 247 
PHE HE1  H N N 248 
PHE HE2  H N N 249 
PHE HZ   H N N 250 
PHE HXT  H N N 251 
PRO N    N N N 252 
PRO CA   C N S 253 
PRO C    C N N 254 
PRO O    O N N 255 
PRO CB   C N N 256 
PRO CG   C N N 257 
PRO CD   C N N 258 
PRO OXT  O N N 259 
PRO H    H N N 260 
PRO HA   H N N 261 
PRO HB2  H N N 262 
PRO HB3  H N N 263 
PRO HG2  H N N 264 
PRO HG3  H N N 265 
PRO HD2  H N N 266 
PRO HD3  H N N 267 
PRO HXT  H N N 268 
SER N    N N N 269 
SER CA   C N S 270 
SER C    C N N 271 
SER O    O N N 272 
SER CB   C N N 273 
SER OG   O N N 274 
SER OXT  O N N 275 
SER H    H N N 276 
SER H2   H N N 277 
SER HA   H N N 278 
SER HB2  H N N 279 
SER HB3  H N N 280 
SER HG   H N N 281 
SER HXT  H N N 282 
THR N    N N N 283 
THR CA   C N S 284 
THR C    C N N 285 
THR O    O N N 286 
THR CB   C N R 287 
THR OG1  O N N 288 
THR CG2  C N N 289 
THR OXT  O N N 290 
THR H    H N N 291 
THR H2   H N N 292 
THR HA   H N N 293 
THR HB   H N N 294 
THR HG1  H N N 295 
THR HG21 H N N 296 
THR HG22 H N N 297 
THR HG23 H N N 298 
THR HXT  H N N 299 
TLA O1   O N N 300 
TLA O11  O N N 301 
TLA C1   C N N 302 
TLA C2   C N R 303 
TLA O2   O N N 304 
TLA C3   C N R 305 
TLA O3   O N N 306 
TLA C4   C N N 307 
TLA O4   O N N 308 
TLA O41  O N N 309 
TLA H11  H N N 310 
TLA H2   H N N 311 
TLA HA   H N N 312 
TLA H3   H N N 313 
TLA HB   H N N 314 
TLA H41  H N N 315 
TRP N    N N N 316 
TRP CA   C N S 317 
TRP C    C N N 318 
TRP O    O N N 319 
TRP CB   C N N 320 
TRP CG   C Y N 321 
TRP CD1  C Y N 322 
TRP CD2  C Y N 323 
TRP NE1  N Y N 324 
TRP CE2  C Y N 325 
TRP CE3  C Y N 326 
TRP CZ2  C Y N 327 
TRP CZ3  C Y N 328 
TRP CH2  C Y N 329 
TRP OXT  O N N 330 
TRP H    H N N 331 
TRP H2   H N N 332 
TRP HA   H N N 333 
TRP HB2  H N N 334 
TRP HB3  H N N 335 
TRP HD1  H N N 336 
TRP HE1  H N N 337 
TRP HE3  H N N 338 
TRP HZ2  H N N 339 
TRP HZ3  H N N 340 
TRP HH2  H N N 341 
TRP HXT  H N N 342 
TYR N    N N N 343 
TYR CA   C N S 344 
TYR C    C N N 345 
TYR O    O N N 346 
TYR CB   C N N 347 
TYR CG   C Y N 348 
TYR CD1  C Y N 349 
TYR CD2  C Y N 350 
TYR CE1  C Y N 351 
TYR CE2  C Y N 352 
TYR CZ   C Y N 353 
TYR OH   O N N 354 
TYR OXT  O N N 355 
TYR H    H N N 356 
TYR H2   H N N 357 
TYR HA   H N N 358 
TYR HB2  H N N 359 
TYR HB3  H N N 360 
TYR HD1  H N N 361 
TYR HD2  H N N 362 
TYR HE1  H N N 363 
TYR HE2  H N N 364 
TYR HH   H N N 365 
TYR HXT  H N N 366 
VAL N    N N N 367 
VAL CA   C N S 368 
VAL C    C N N 369 
VAL O    O N N 370 
VAL CB   C N N 371 
VAL CG1  C N N 372 
VAL CG2  C N N 373 
VAL OXT  O N N 374 
VAL H    H N N 375 
VAL H2   H N N 376 
VAL HA   H N N 377 
VAL HB   H N N 378 
VAL HG11 H N N 379 
VAL HG12 H N N 380 
VAL HG13 H N N 381 
VAL HG21 H N N 382 
VAL HG22 H N N 383 
VAL HG23 H N N 384 
VAL HXT  H N N 385 
# 
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 
HOH O   H1   sing N N 129 
HOH O   H2   sing N N 130 
ILE N   CA   sing N N 131 
ILE N   H    sing N N 132 
ILE N   H2   sing N N 133 
ILE CA  C    sing N N 134 
ILE CA  CB   sing N N 135 
ILE CA  HA   sing N N 136 
ILE C   O    doub N N 137 
ILE C   OXT  sing N N 138 
ILE CB  CG1  sing N N 139 
ILE CB  CG2  sing N N 140 
ILE CB  HB   sing N N 141 
ILE CG1 CD1  sing N N 142 
ILE CG1 HG12 sing N N 143 
ILE CG1 HG13 sing N N 144 
ILE CG2 HG21 sing N N 145 
ILE CG2 HG22 sing N N 146 
ILE CG2 HG23 sing N N 147 
ILE CD1 HD11 sing N N 148 
ILE CD1 HD12 sing N N 149 
ILE CD1 HD13 sing N N 150 
ILE OXT HXT  sing N N 151 
LEU N   CA   sing N N 152 
LEU N   H    sing N N 153 
LEU N   H2   sing N N 154 
LEU CA  C    sing N N 155 
LEU CA  CB   sing N N 156 
LEU CA  HA   sing N N 157 
LEU C   O    doub N N 158 
LEU C   OXT  sing N N 159 
LEU CB  CG   sing N N 160 
LEU CB  HB2  sing N N 161 
LEU CB  HB3  sing N N 162 
LEU CG  CD1  sing N N 163 
LEU CG  CD2  sing N N 164 
LEU CG  HG   sing N N 165 
LEU CD1 HD11 sing N N 166 
LEU CD1 HD12 sing N N 167 
LEU CD1 HD13 sing N N 168 
LEU CD2 HD21 sing N N 169 
LEU CD2 HD22 sing N N 170 
LEU CD2 HD23 sing N N 171 
LEU OXT HXT  sing N N 172 
LYS N   CA   sing N N 173 
LYS N   H    sing N N 174 
LYS N   H2   sing N N 175 
LYS CA  C    sing N N 176 
LYS CA  CB   sing N N 177 
LYS CA  HA   sing N N 178 
LYS C   O    doub N N 179 
LYS C   OXT  sing N N 180 
LYS CB  CG   sing N N 181 
LYS CB  HB2  sing N N 182 
LYS CB  HB3  sing N N 183 
LYS CG  CD   sing N N 184 
LYS CG  HG2  sing N N 185 
LYS CG  HG3  sing N N 186 
LYS CD  CE   sing N N 187 
LYS CD  HD2  sing N N 188 
LYS CD  HD3  sing N N 189 
LYS CE  NZ   sing N N 190 
LYS CE  HE2  sing N N 191 
LYS CE  HE3  sing N N 192 
LYS NZ  HZ1  sing N N 193 
LYS NZ  HZ2  sing N N 194 
LYS NZ  HZ3  sing N N 195 
LYS OXT HXT  sing N N 196 
MET N   CA   sing N N 197 
MET N   H    sing N N 198 
MET N   H2   sing N N 199 
MET CA  C    sing N N 200 
MET CA  CB   sing N N 201 
MET CA  HA   sing N N 202 
MET C   O    doub N N 203 
MET C   OXT  sing N N 204 
MET CB  CG   sing N N 205 
MET CB  HB2  sing N N 206 
MET CB  HB3  sing N N 207 
MET CG  SD   sing N N 208 
MET CG  HG2  sing N N 209 
MET CG  HG3  sing N N 210 
MET SD  CE   sing N N 211 
MET CE  HE1  sing N N 212 
MET CE  HE2  sing N N 213 
MET CE  HE3  sing N N 214 
MET OXT HXT  sing N N 215 
PHE N   CA   sing N N 216 
PHE N   H    sing N N 217 
PHE N   H2   sing N N 218 
PHE CA  C    sing N N 219 
PHE CA  CB   sing N N 220 
PHE CA  HA   sing N N 221 
PHE C   O    doub N N 222 
PHE C   OXT  sing N N 223 
PHE CB  CG   sing N N 224 
PHE CB  HB2  sing N N 225 
PHE CB  HB3  sing N N 226 
PHE CG  CD1  doub Y N 227 
PHE CG  CD2  sing Y N 228 
PHE CD1 CE1  sing Y N 229 
PHE CD1 HD1  sing N N 230 
PHE CD2 CE2  doub Y N 231 
PHE CD2 HD2  sing N N 232 
PHE CE1 CZ   doub Y N 233 
PHE CE1 HE1  sing N N 234 
PHE CE2 CZ   sing Y N 235 
PHE CE2 HE2  sing N N 236 
PHE CZ  HZ   sing N N 237 
PHE OXT HXT  sing N N 238 
PRO N   CA   sing N N 239 
PRO N   CD   sing N N 240 
PRO N   H    sing N N 241 
PRO CA  C    sing N N 242 
PRO CA  CB   sing N N 243 
PRO CA  HA   sing N N 244 
PRO C   O    doub N N 245 
PRO C   OXT  sing N N 246 
PRO CB  CG   sing N N 247 
PRO CB  HB2  sing N N 248 
PRO CB  HB3  sing N N 249 
PRO CG  CD   sing N N 250 
PRO CG  HG2  sing N N 251 
PRO CG  HG3  sing N N 252 
PRO CD  HD2  sing N N 253 
PRO CD  HD3  sing N N 254 
PRO OXT HXT  sing N N 255 
SER N   CA   sing N N 256 
SER N   H    sing N N 257 
SER N   H2   sing N N 258 
SER CA  C    sing N N 259 
SER CA  CB   sing N N 260 
SER CA  HA   sing N N 261 
SER C   O    doub N N 262 
SER C   OXT  sing N N 263 
SER CB  OG   sing N N 264 
SER CB  HB2  sing N N 265 
SER CB  HB3  sing N N 266 
SER OG  HG   sing N N 267 
SER OXT HXT  sing N N 268 
THR N   CA   sing N N 269 
THR N   H    sing N N 270 
THR N   H2   sing N N 271 
THR CA  C    sing N N 272 
THR CA  CB   sing N N 273 
THR CA  HA   sing N N 274 
THR C   O    doub N N 275 
THR C   OXT  sing N N 276 
THR CB  OG1  sing N N 277 
THR CB  CG2  sing N N 278 
THR CB  HB   sing N N 279 
THR OG1 HG1  sing N N 280 
THR CG2 HG21 sing N N 281 
THR CG2 HG22 sing N N 282 
THR CG2 HG23 sing N N 283 
THR OXT HXT  sing N N 284 
TLA O1  C1   doub N N 285 
TLA O11 C1   sing N N 286 
TLA O11 H11  sing N N 287 
TLA C1  C2   sing N N 288 
TLA C2  O2   sing N N 289 
TLA C2  C3   sing N N 290 
TLA C2  H2   sing N N 291 
TLA O2  HA   sing N N 292 
TLA C3  O3   sing N N 293 
TLA C3  C4   sing N N 294 
TLA C3  H3   sing N N 295 
TLA O3  HB   sing N N 296 
TLA C4  O4   doub N N 297 
TLA C4  O41  sing N N 298 
TLA O41 H41  sing N N 299 
TRP N   CA   sing N N 300 
TRP N   H    sing N N 301 
TRP N   H2   sing N N 302 
TRP CA  C    sing N N 303 
TRP CA  CB   sing N N 304 
TRP CA  HA   sing N N 305 
TRP C   O    doub N N 306 
TRP C   OXT  sing N N 307 
TRP CB  CG   sing N N 308 
TRP CB  HB2  sing N N 309 
TRP CB  HB3  sing N N 310 
TRP CG  CD1  doub Y N 311 
TRP CG  CD2  sing Y N 312 
TRP CD1 NE1  sing Y N 313 
TRP CD1 HD1  sing N N 314 
TRP CD2 CE2  doub Y N 315 
TRP CD2 CE3  sing Y N 316 
TRP NE1 CE2  sing Y N 317 
TRP NE1 HE1  sing N N 318 
TRP CE2 CZ2  sing Y N 319 
TRP CE3 CZ3  doub Y N 320 
TRP CE3 HE3  sing N N 321 
TRP CZ2 CH2  doub Y N 322 
TRP CZ2 HZ2  sing N N 323 
TRP CZ3 CH2  sing Y N 324 
TRP CZ3 HZ3  sing N N 325 
TRP CH2 HH2  sing N N 326 
TRP OXT HXT  sing N N 327 
TYR N   CA   sing N N 328 
TYR N   H    sing N N 329 
TYR N   H2   sing N N 330 
TYR CA  C    sing N N 331 
TYR CA  CB   sing N N 332 
TYR CA  HA   sing N N 333 
TYR C   O    doub N N 334 
TYR C   OXT  sing N N 335 
TYR CB  CG   sing N N 336 
TYR CB  HB2  sing N N 337 
TYR CB  HB3  sing N N 338 
TYR CG  CD1  doub Y N 339 
TYR CG  CD2  sing Y N 340 
TYR CD1 CE1  sing Y N 341 
TYR CD1 HD1  sing N N 342 
TYR CD2 CE2  doub Y N 343 
TYR CD2 HD2  sing N N 344 
TYR CE1 CZ   doub Y N 345 
TYR CE1 HE1  sing N N 346 
TYR CE2 CZ   sing Y N 347 
TYR CE2 HE2  sing N N 348 
TYR CZ  OH   sing N N 349 
TYR OH  HH   sing N N 350 
TYR OXT HXT  sing N N 351 
VAL N   CA   sing N N 352 
VAL N   H    sing N N 353 
VAL N   H2   sing N N 354 
VAL CA  C    sing N N 355 
VAL CA  CB   sing N N 356 
VAL CA  HA   sing N N 357 
VAL C   O    doub N N 358 
VAL C   OXT  sing N N 359 
VAL CB  CG1  sing N N 360 
VAL CB  CG2  sing N N 361 
VAL CB  HB   sing N N 362 
VAL CG1 HG11 sing N N 363 
VAL CG1 HG12 sing N N 364 
VAL CG1 HG13 sing N N 365 
VAL CG2 HG21 sing N N 366 
VAL CG2 HG22 sing N N 367 
VAL CG2 HG23 sing N N 368 
VAL OXT HXT  sing N N 369 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   5X9L 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8YK6 
_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]   0.017217 
_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]   0.017217 
_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]   0.006646 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . ALA A 1 1   ? -21.825 10.553 -9.937  1.00 11.13 ? 1   ALA A N   1 
ATOM   2    C CA  . ALA A 1 1   ? -21.449 11.977 -10.069 1.00 10.31 ? 1   ALA A CA  1 
ATOM   3    C C   . ALA A 1 1   ? -20.410 12.113 -11.160 1.00 9.58  ? 1   ALA A C   1 
ATOM   4    O O   . ALA A 1 1   ? -19.516 11.259 -11.281 1.00 12.04 ? 1   ALA A O   1 
ATOM   5    C CB  . ALA A 1 1   ? -20.868 12.482 -8.800  1.00 11.92 ? 1   ALA A CB  1 
ATOM   6    N N   . THR A 1 2   ? -20.491 13.186 -11.918 1.00 9.10  ? 2   THR A N   1 
ATOM   7    C CA  A THR A 1 2   ? -19.476 13.419 -12.947 0.72 8.63  ? 2   THR A CA  1 
ATOM   8    C CA  B THR A 1 2   ? -19.520 13.471 -12.991 0.28 9.70  ? 2   THR A CA  1 
ATOM   9    C C   . THR A 1 2   ? -18.426 14.393 -12.433 1.00 7.96  ? 2   THR A C   1 
ATOM   10   O O   . THR A 1 2   ? -18.753 15.381 -11.744 1.00 8.89  ? 2   THR A O   1 
ATOM   11   C CB  A THR A 1 2   ? -20.089 13.932 -14.245 0.72 10.13 ? 2   THR A CB  1 
ATOM   12   C CB  B THR A 1 2   ? -20.261 13.987 -14.232 0.28 12.47 ? 2   THR A CB  1 
ATOM   13   O OG1 A THR A 1 2   ? -20.637 15.225 -14.025 0.72 9.55  ? 2   THR A OG1 1 
ATOM   14   O OG1 B THR A 1 2   ? -20.802 12.869 -14.938 0.28 12.96 ? 2   THR A OG1 1 
ATOM   15   C CG2 A THR A 1 2   ? -21.228 13.066 -14.734 0.72 14.19 ? 2   THR A CG2 1 
ATOM   16   C CG2 B THR A 1 2   ? -19.385 14.732 -15.205 0.28 13.96 ? 2   THR A CG2 1 
ATOM   17   N N   . PHE A 1 3   ? -17.206 14.096 -12.798 1.00 7.88  ? 3   PHE A N   1 
ATOM   18   C CA  . PHE A 1 3   ? -16.063 14.983 -12.567 1.00 7.68  ? 3   PHE A CA  1 
ATOM   19   C C   . PHE A 1 3   ? -15.403 15.211 -13.916 1.00 7.77  ? 3   PHE A C   1 
ATOM   20   O O   . PHE A 1 3   ? -14.835 14.271 -14.492 1.00 9.34  ? 3   PHE A O   1 
ATOM   21   C CB  . PHE A 1 3   ? -15.048 14.381 -11.603 1.00 8.13  ? 3   PHE A CB  1 
ATOM   22   C CG  . PHE A 1 3   ? -15.479 14.315 -10.159 1.00 7.77  ? 3   PHE A CG  1 
ATOM   23   C CD1 . PHE A 1 3   ? -16.482 13.460 -9.737  1.00 9.19  ? 3   PHE A CD1 1 
ATOM   24   C CD2 . PHE A 1 3   ? -14.833 15.066 -9.196  1.00 8.43  ? 3   PHE A CD2 1 
ATOM   25   C CE1 . PHE A 1 3   ? -16.853 13.389 -8.401  1.00 10.30 ? 3   PHE A CE1 1 
ATOM   26   C CE2 . PHE A 1 3   ? -15.198 14.984 -7.856  1.00 8.86  ? 3   PHE A CE2 1 
ATOM   27   C CZ  . PHE A 1 3   ? -16.202 14.146 -7.469  1.00 9.40  ? 3   PHE A CZ  1 
ATOM   28   N N   . GLU A 1 4   ? -15.460 16.440 -14.402 1.00 7.08  ? 4   GLU A N   1 
ATOM   29   C CA  A GLU A 1 4   ? -14.678 16.771 -15.613 0.60 7.10  ? 4   GLU A CA  1 
ATOM   30   C CA  B GLU A 1 4   ? -14.743 16.890 -15.600 0.40 7.41  ? 4   GLU A CA  1 
ATOM   31   C C   . GLU A 1 4   ? -13.315 17.244 -15.147 1.00 7.02  ? 4   GLU A C   1 
ATOM   32   O O   . GLU A 1 4   ? -13.207 18.183 -14.358 1.00 8.53  ? 4   GLU A O   1 
ATOM   33   C CB  A GLU A 1 4   ? -15.271 17.828 -16.534 0.60 7.11  ? 4   GLU A CB  1 
ATOM   34   C CB  B GLU A 1 4   ? -15.604 18.024 -16.169 0.40 7.37  ? 4   GLU A CB  1 
ATOM   35   C CG  A GLU A 1 4   ? -14.508 17.950 -17.852 0.60 7.05  ? 4   GLU A CG  1 
ATOM   36   C CG  B GLU A 1 4   ? -15.126 18.470 -17.530 0.40 7.87  ? 4   GLU A CG  1 
ATOM   37   C CD  A GLU A 1 4   ? -15.101 18.974 -18.809 0.60 7.55  ? 4   GLU A CD  1 
ATOM   38   C CD  B GLU A 1 4   ? -15.853 19.641 -18.165 0.40 9.13  ? 4   GLU A CD  1 
ATOM   39   O OE1 A GLU A 1 4   ? -15.124 20.164 -18.470 0.60 8.37  ? 4   GLU A OE1 1 
ATOM   40   O OE1 B GLU A 1 4   ? -16.624 20.314 -17.456 0.40 12.24 ? 4   GLU A OE1 1 
ATOM   41   O OE2 A GLU A 1 4   ? -15.494 18.589 -19.923 0.60 10.63 ? 4   GLU A OE2 1 
ATOM   42   O OE2 B GLU A 1 4   ? -15.611 19.896 -19.364 0.40 10.61 ? 4   GLU A OE2 1 
ATOM   43   N N   . ILE A 1 5   ? -12.300 16.556 -15.610 1.00 7.02  ? 5   ILE A N   1 
ATOM   44   C CA  . ILE A 1 5   ? -10.901 16.839 -15.237 1.00 7.16  ? 5   ILE A CA  1 
ATOM   45   C C   . ILE A 1 5   ? -10.254 17.520 -16.434 1.00 7.46  ? 5   ILE A C   1 
ATOM   46   O O   . ILE A 1 5   ? -10.215 16.932 -17.542 1.00 8.91  ? 5   ILE A O   1 
ATOM   47   C CB  . ILE A 1 5   ? -10.177 15.564 -14.804 1.00 7.33  ? 5   ILE A CB  1 
ATOM   48   C CG1 . ILE A 1 5   ? -10.936 14.852 -13.677 1.00 8.06  ? 5   ILE A CG1 1 
ATOM   49   C CG2 . ILE A 1 5   ? -8.774  15.934 -14.383 1.00 7.81  ? 5   ILE A CG2 1 
ATOM   50   C CD1 . ILE A 1 5   ? -10.385 13.483 -13.325 1.00 9.33  ? 5   ILE A CD1 1 
ATOM   51   N N   . VAL A 1 6   ? -9.796  18.737 -16.255 1.00 7.37  ? 6   VAL A N   1 
ATOM   52   C CA  . VAL A 1 6   ? -9.335  19.605 -17.355 1.00 7.28  ? 6   VAL A CA  1 
ATOM   53   C C   . VAL A 1 6   ? -7.897  19.979 -17.102 1.00 7.23  ? 6   VAL A C   1 
ATOM   54   O O   . VAL A 1 6   ? -7.575  20.505 -16.008 1.00 7.93  ? 6   VAL A O   1 
ATOM   55   C CB  . VAL A 1 6   ? -10.194 20.864 -17.463 1.00 7.14  ? 6   VAL A CB  1 
ATOM   56   C CG1 . VAL A 1 6   ? -9.704  21.758 -18.606 1.00 8.32  ? 6   VAL A CG1 1 
ATOM   57   C CG2 . VAL A 1 6   ? -11.662 20.502 -17.649 1.00 8.22  ? 6   VAL A CG2 1 
ATOM   58   N N   . ASN A 1 7   ? -7.028  19.754 -18.082 1.00 7.16  ? 7   ASN A N   1 
ATOM   59   C CA  . ASN A 1 7   ? -5.630  20.165 -17.955 1.00 6.86  ? 7   ASN A CA  1 
ATOM   60   C C   . ASN A 1 7   ? -5.413  21.492 -18.683 1.00 6.96  ? 7   ASN A C   1 
ATOM   61   O O   . ASN A 1 7   ? -5.304  21.480 -19.916 1.00 8.37  ? 7   ASN A O   1 
ATOM   62   C CB  . ASN A 1 7   ? -4.704  19.110 -18.516 1.00 7.18  ? 7   ASN A CB  1 
ATOM   63   C CG  . ASN A 1 7   ? -3.268  19.533 -18.358 1.00 7.02  ? 7   ASN A CG  1 
ATOM   64   O OD1 . ASN A 1 7   ? -2.963  20.397 -17.536 1.00 7.52  ? 7   ASN A OD1 1 
ATOM   65   N ND2 . ASN A 1 7   ? -2.377  18.918 -19.133 1.00 7.71  ? 7   ASN A ND2 1 
ATOM   66   N N   . ARG A 1 8   ? -5.362  22.606 -17.955 1.00 6.69  ? 8   ARG A N   1 
ATOM   67   C CA  . ARG A 1 8   ? -5.032  23.911 -18.562 1.00 6.94  ? 8   ARG A CA  1 
ATOM   68   C C   . ARG A 1 8   ? -3.531  24.178 -18.489 1.00 7.27  ? 8   ARG A C   1 
ATOM   69   O O   . ARG A 1 8   ? -3.069  25.224 -18.974 1.00 8.70  ? 8   ARG A O   1 
ATOM   70   C CB  . ARG A 1 8   ? -5.873  25.002 -17.913 1.00 7.37  ? 8   ARG A CB  1 
ATOM   71   C CG  . ARG A 1 8   ? -5.826  26.359 -18.584 1.00 8.91  ? 8   ARG A CG  1 
ATOM   72   C CD  . ARG A 1 8   ? -6.799  27.329 -17.957 1.00 9.77  ? 8   ARG A CD  1 
ATOM   73   N NE  . ARG A 1 8   ? -8.165  26.932 -18.186 1.00 9.74  ? 8   ARG A NE  1 
ATOM   74   C CZ  . ARG A 1 8   ? -9.194  27.126 -17.365 1.00 10.92 ? 8   ARG A CZ  1 
ATOM   75   N NH1 . ARG A 1 8   ? -9.054  27.788 -16.235 1.00 13.09 ? 8   ARG A NH1 1 
ATOM   76   N NH2 . ARG A 1 8   ? -10.379 26.635 -17.685 1.00 12.83 ? 8   ARG A NH2 1 
ATOM   77   N N   . CYS A 1 9   ? -2.751  23.264 -17.919 1.00 7.09  ? 9   CYS A N   1 
ATOM   78   C CA  . CYS A 1 9   ? -1.299  23.449 -17.897 1.00 7.37  ? 9   CYS A CA  1 
ATOM   79   C C   . CYS A 1 9   ? -0.732  23.413 -19.310 1.00 7.57  ? 9   CYS A C   1 
ATOM   80   O O   . CYS A 1 9   ? -1.299  22.777 -20.199 1.00 8.33  ? 9   CYS A O   1 
ATOM   81   C CB  . CYS A 1 9   ? -0.608  22.363 -17.083 1.00 7.81  ? 9   CYS A CB  1 
ATOM   82   S SG  . CYS A 1 9   ? -1.271  22.180 -15.398 1.00 8.86  ? 9   CYS A SG  1 
ATOM   83   N N   . SER A 1 10  ? 0.432   24.030 -19.469 1.00 8.48  ? 10  SER A N   1 
ATOM   84   C CA  . SER A 1 10  ? 1.149   24.006 -20.749 1.00 9.34  ? 10  SER A CA  1 
ATOM   85   C C   . SER A 1 10  ? 1.859   22.669 -20.974 1.00 9.55  ? 10  SER A C   1 
ATOM   86   O O   . SER A 1 10  ? 2.339   22.448 -22.081 1.00 13.36 ? 10  SER A O   1 
ATOM   87   C CB  . SER A 1 10  ? 2.097   25.162 -20.845 1.00 11.66 ? 10  SER A CB  1 
ATOM   88   O OG  . SER A 1 10  ? 3.062   25.085 -19.825 1.00 14.35 ? 10  SER A OG  1 
ATOM   89   N N   . TYR A 1 11  ? 1.903   21.793 -19.985 1.00 9.22  ? 11  TYR A N   1 
ATOM   90   C CA  . TYR A 1 11  ? 2.557   20.482 -20.007 1.00 9.61  ? 11  TYR A CA  1 
ATOM   91   C C   . TYR A 1 11  ? 1.501   19.405 -19.851 1.00 8.53  ? 11  TYR A C   1 
ATOM   92   O O   . TYR A 1 11  ? 0.444   19.621 -19.230 1.00 8.77  ? 11  TYR A O   1 
ATOM   93   C CB  . TYR A 1 11  ? 3.632   20.396 -18.912 1.00 10.29 ? 11  TYR A CB  1 
ATOM   94   C CG  . TYR A 1 11  ? 3.204   20.877 -17.540 1.00 9.60  ? 11  TYR A CG  1 
ATOM   95   C CD1 . TYR A 1 11  ? 2.562   20.031 -16.636 1.00 9.82  ? 11  TYR A CD1 1 
ATOM   96   C CD2 . TYR A 1 11  ? 3.394   22.192 -17.154 1.00 10.08 ? 11  TYR A CD2 1 
ATOM   97   C CE1 . TYR A 1 11  ? 2.174   20.471 -15.374 1.00 9.90  ? 11  TYR A CE1 1 
ATOM   98   C CE2 . TYR A 1 11  ? 3.012   22.647 -15.901 1.00 9.72  ? 11  TYR A CE2 1 
ATOM   99   C CZ  . TYR A 1 11  ? 2.400   21.785 -15.002 1.00 9.55  ? 11  TYR A CZ  1 
ATOM   100  O OH  . TYR A 1 11  ? 2.031   22.190 -13.747 1.00 11.09 ? 11  TYR A OH  1 
ATOM   101  N N   . THR A 1 12  ? 1.816   18.218 -20.343 1.00 9.10  ? 12  THR A N   1 
ATOM   102  C CA  . THR A 1 12  ? 0.982   17.031 -20.130 1.00 8.51  ? 12  THR A CA  1 
ATOM   103  C C   . THR A 1 12  ? 0.937   16.671 -18.641 1.00 8.22  ? 12  THR A C   1 
ATOM   104  O O   . THR A 1 12  ? 1.954   16.765 -17.951 1.00 9.20  ? 12  THR A O   1 
ATOM   105  C CB  . THR A 1 12  ? 1.538   15.860 -20.948 1.00 9.99  ? 12  THR A CB  1 
ATOM   106  O OG1 . THR A 1 12  ? 1.567   16.296 -22.304 1.00 12.34 ? 12  THR A OG1 1 
ATOM   107  C CG2 . THR A 1 12  ? 0.737   14.585 -20.808 1.00 9.86  ? 12  THR A CG2 1 
ATOM   108  N N   . VAL A 1 13  ? -0.218  16.228 -18.196 1.00 7.87  ? 13  VAL A N   1 
ATOM   109  C CA  . VAL A 1 13  ? -0.321  15.576 -16.881 1.00 8.53  ? 13  VAL A CA  1 
ATOM   110  C C   . VAL A 1 13  ? -1.023  14.252 -17.058 1.00 8.14  ? 13  VAL A C   1 
ATOM   111  O O   . VAL A 1 13  ? -1.699  14.026 -18.070 1.00 10.21 ? 13  VAL A O   1 
ATOM   112  C CB  . VAL A 1 13  ? -1.018  16.441 -15.828 1.00 9.36  ? 13  VAL A CB  1 
ATOM   113  C CG1 . VAL A 1 13  ? -0.358  17.788 -15.665 1.00 10.46 ? 13  VAL A CG1 1 
ATOM   114  C CG2 . VAL A 1 13  ? -2.464  16.580 -16.131 1.00 9.95  ? 13  VAL A CG2 1 
ATOM   115  N N   . TRP A 1 14  ? -0.857  13.373 -16.094 1.00 7.75  ? 14  TRP A N   1 
ATOM   116  C CA  . TRP A 1 14  ? -1.579  12.101 -16.055 1.00 8.16  ? 14  TRP A CA  1 
ATOM   117  C C   . TRP A 1 14  ? -2.499  12.185 -14.861 1.00 7.59  ? 14  TRP A C   1 
ATOM   118  O O   . TRP A 1 14  ? -2.039  12.122 -13.697 1.00 8.33  ? 14  TRP A O   1 
ATOM   119  C CB  . TRP A 1 14  ? -0.627  10.912 -16.001 1.00 9.24  ? 14  TRP A CB  1 
ATOM   120  C CG  . TRP A 1 14  ? 0.081   10.672 -17.294 1.00 9.98  ? 14  TRP A CG  1 
ATOM   121  C CD1 . TRP A 1 14  ? -0.206  9.682  -18.184 1.00 11.15 ? 14  TRP A CD1 1 
ATOM   122  C CD2 . TRP A 1 14  ? 1.168   11.427 -17.860 1.00 10.31 ? 14  TRP A CD2 1 
ATOM   123  N NE1 . TRP A 1 14  ? 0.632   9.749  -19.270 1.00 12.01 ? 14  TRP A NE1 1 
ATOM   124  C CE2 . TRP A 1 14  ? 1.486   10.809 -19.098 1.00 11.28 ? 14  TRP A CE2 1 
ATOM   125  C CE3 . TRP A 1 14  ? 1.939   12.519 -17.452 1.00 10.56 ? 14  TRP A CE3 1 
ATOM   126  C CZ2 . TRP A 1 14  ? 2.515   11.264 -19.928 1.00 12.53 ? 14  TRP A CZ2 1 
ATOM   127  C CZ3 . TRP A 1 14  ? 2.970   12.955 -18.260 1.00 11.72 ? 14  TRP A CZ3 1 
ATOM   128  C CH2 . TRP A 1 14  ? 3.246   12.343 -19.490 1.00 13.14 ? 14  TRP A CH2 1 
ATOM   129  N N   . ALA A 1 15  ? -3.764  12.440 -15.110 1.00 7.33  ? 15  ALA A N   1 
ATOM   130  C CA  . ALA A 1 15  ? -4.746  12.525 -14.023 1.00 7.50  ? 15  ALA A CA  1 
ATOM   131  C C   . ALA A 1 15  ? -4.870  11.167 -13.352 1.00 7.34  ? 15  ALA A C   1 
ATOM   132  O O   . ALA A 1 15  ? -4.699  10.123 -13.994 1.00 8.28  ? 15  ALA A O   1 
ATOM   133  C CB  . ALA A 1 15  ? -6.066  12.991 -14.571 1.00 8.83  ? 15  ALA A CB  1 
ATOM   134  N N   . ALA A 1 16  ? -5.225  11.210 -12.077 1.00 7.60  ? 16  ALA A N   1 
ATOM   135  C CA  . ALA A 1 16  ? -5.422  10.009 -11.257 1.00 8.21  ? 16  ALA A CA  1 
ATOM   136  C C   . ALA A 1 16  ? -6.644  10.213 -10.383 1.00 7.89  ? 16  ALA A C   1 
ATOM   137  O O   . ALA A 1 16  ? -6.898  11.338 -9.933  1.00 8.15  ? 16  ALA A O   1 
ATOM   138  C CB  . ALA A 1 16  ? -4.195  9.767  -10.399 1.00 9.60  ? 16  ALA A CB  1 
ATOM   139  N N   . ALA A 1 17  ? -7.361  9.127  -10.122 1.00 8.61  ? 17  ALA A N   1 
ATOM   140  C CA  . ALA A 1 17  ? -8.586  9.186  -9.294  1.00 8.84  ? 17  ALA A CA  1 
ATOM   141  C C   . ALA A 1 17  ? -8.706  7.868  -8.540  1.00 9.36  ? 17  ALA A C   1 
ATOM   142  O O   . ALA A 1 17  ? -8.778  6.798  -9.165  1.00 10.69 ? 17  ALA A O   1 
ATOM   143  C CB  . ALA A 1 17  ? -9.791  9.431  -10.162 1.00 9.59  ? 17  ALA A CB  1 
ATOM   144  N N   . SER A 1 18  ? -8.745  7.942  -7.219  1.00 9.21  ? 18  SER A N   1 
ATOM   145  C CA  . SER A 1 18  ? -8.742  6.732  -6.372  1.00 10.25 ? 18  SER A CA  1 
ATOM   146  C C   . SER A 1 18  ? -9.449  7.044  -5.064  1.00 9.98  ? 18  SER A C   1 
ATOM   147  O O   . SER A 1 18  ? -9.488  8.196  -4.635  1.00 10.43 ? 18  SER A O   1 
ATOM   148  C CB  . SER A 1 18  ? -7.307  6.295  -6.113  1.00 11.48 ? 18  SER A CB  1 
ATOM   149  O OG  . SER A 1 18  ? -7.206  5.214  -5.185  1.00 12.94 ? 18  SER A OG  1 
ATOM   150  N N   . LYS A 1 19  ? -9.942  6.009  -4.395  1.00 11.06 ? 19  LYS A N   1 
ATOM   151  C CA  . LYS A 1 19  ? -10.386 6.134  -2.983  1.00 11.83 ? 19  LYS A CA  1 
ATOM   152  C C   . LYS A 1 19  ? -9.444  5.357  -2.061  1.00 13.26 ? 19  LYS A C   1 
ATOM   153  O O   . LYS A 1 19  ? -9.807  5.129  -0.889  1.00 14.68 ? 19  LYS A O   1 
ATOM   154  C CB  . LYS A 1 19  ? -11.862 5.768  -2.799  1.00 13.29 ? 19  LYS A CB  1 
ATOM   155  C CG  . LYS A 1 19  ? -12.236 4.337  -3.113  1.00 15.73 ? 19  LYS A CG  1 
ATOM   156  C CD  . LYS A 1 19  ? -13.707 4.102  -2.886  1.00 17.29 ? 19  LYS A CD  1 
ATOM   157  C CE  . LYS A 1 19  ? -14.104 2.646  -2.967  1.00 20.80 ? 19  LYS A CE  1 
ATOM   158  N NZ  . LYS A 1 19  ? -13.648 1.871  -1.790  1.00 25.27 ? 19  LYS A NZ  1 
ATOM   159  N N   . GLY A 1 20  ? -8.255  5.002  -2.534  1.00 13.35 ? 20  GLY A N   1 
ATOM   160  C CA  . GLY A 1 20  ? -7.167  4.499  -1.669  1.00 14.78 ? 20  GLY A CA  1 
ATOM   161  C C   . GLY A 1 20  ? -7.041  2.993  -1.713  1.00 15.50 ? 20  GLY A C   1 
ATOM   162  O O   . GLY A 1 20  ? -5.922  2.483  -1.646  1.00 17.75 ? 20  GLY A O   1 
ATOM   163  N N   A ASP A 1 21  ? -8.170  2.294  -1.828  0.50 16.95 ? 21  ASP A N   1 
ATOM   164  N N   B ASP A 1 21  ? -8.176  2.306  -1.827  0.50 16.33 ? 21  ASP A N   1 
ATOM   165  C CA  A ASP A 1 21  ? -8.217  0.819  -1.961  0.50 18.54 ? 21  ASP A CA  1 
ATOM   166  C CA  B ASP A 1 21  ? -8.238  0.831  -1.947  0.50 17.94 ? 21  ASP A CA  1 
ATOM   167  C C   A ASP A 1 21  ? -8.875  0.421  -3.282  0.50 18.07 ? 21  ASP A C   1 
ATOM   168  C C   B ASP A 1 21  ? -8.840  0.422  -3.291  0.50 17.58 ? 21  ASP A C   1 
ATOM   169  O O   A ASP A 1 21  ? -9.147  -0.770 -3.456  0.50 20.46 ? 21  ASP A O   1 
ATOM   170  O O   B ASP A 1 21  ? -9.023  -0.778 -3.495  0.50 22.85 ? 21  ASP A O   1 
ATOM   171  C CB  A ASP A 1 21  ? -8.943  0.190  -0.768  0.50 20.89 ? 21  ASP A CB  1 
ATOM   172  C CB  B ASP A 1 21  ? -9.028  0.219  -0.786  0.50 20.26 ? 21  ASP A CB  1 
ATOM   173  C CG  A ASP A 1 21  ? -10.334 0.749  -0.510  0.50 22.76 ? 21  ASP A CG  1 
ATOM   174  C CG  B ASP A 1 21  ? -10.491 0.632  -0.738  0.50 21.57 ? 21  ASP A CG  1 
ATOM   175  O OD1 A ASP A 1 21  ? -10.847 1.482  -1.379  0.50 22.32 ? 21  ASP A OD1 1 
ATOM   176  O OD1 B ASP A 1 21  ? -11.291 -0.110 -0.130  0.50 23.86 ? 21  ASP A OD1 1 
ATOM   177  O OD2 A ASP A 1 21  ? -10.901 0.436  0.560   0.50 26.59 ? 21  ASP A OD2 1 
ATOM   178  O OD2 B ASP A 1 21  ? -10.821 1.690  -1.302  0.50 21.36 ? 21  ASP A OD2 1 
ATOM   179  N N   . ALA A 1 22  ? -9.127  1.371  -4.176  1.00 15.87 ? 22  ALA A N   1 
ATOM   180  C CA  . ALA A 1 22  ? -9.727  1.080  -5.489  1.00 16.20 ? 22  ALA A CA  1 
ATOM   181  C C   . ALA A 1 22  ? -9.591  2.308  -6.370  1.00 14.48 ? 22  ALA A C   1 
ATOM   182  O O   . ALA A 1 22  ? -9.560  3.435  -5.876  1.00 14.66 ? 22  ALA A O   1 
ATOM   183  C CB  . ALA A 1 22  ? -11.184 0.696  -5.368  1.00 18.09 ? 22  ALA A CB  1 
ATOM   184  N N   . ALA A 1 23  ? -9.561  2.067  -7.669  1.00 14.36 ? 23  ALA A N   1 
ATOM   185  C CA  . ALA A 1 23  ? -9.687  3.120  -8.683  1.00 13.46 ? 23  ALA A CA  1 
ATOM   186  C C   . ALA A 1 23  ? -11.077 3.743  -8.590  1.00 12.90 ? 23  ALA A C   1 
ATOM   187  O O   . ALA A 1 23  ? -12.057 3.058  -8.275  1.00 15.41 ? 23  ALA A O   1 
ATOM   188  C CB  . ALA A 1 23  ? -9.492  2.535  -10.064 1.00 14.26 ? 23  ALA A CB  1 
ATOM   189  N N   . LEU A 1 24  ? -11.159 5.010  -8.956  1.00 11.57 ? 24  LEU A N   1 
ATOM   190  C CA  . LEU A 1 24  ? -12.440 5.635  -9.328  1.00 11.71 ? 24  LEU A CA  1 
ATOM   191  C C   . LEU A 1 24  ? -12.477 5.678  -10.852 1.00 11.57 ? 24  LEU A C   1 
ATOM   192  O O   . LEU A 1 24  ? -11.528 6.174  -11.470 1.00 11.96 ? 24  LEU A O   1 
ATOM   193  C CB  . LEU A 1 24  ? -12.566 7.037  -8.746  1.00 11.30 ? 24  LEU A CB  1 
ATOM   194  C CG  . LEU A 1 24  ? -12.456 7.103  -7.229  1.00 11.77 ? 24  LEU A CG  1 
ATOM   195  C CD1 . LEU A 1 24  ? -12.543 8.546  -6.777  1.00 12.80 ? 24  LEU A CD1 1 
ATOM   196  C CD2 . LEU A 1 24  ? -13.507 6.261  -6.530  1.00 13.75 ? 24  LEU A CD2 1 
ATOM   197  N N   . ASP A 1 25  ? -13.546 5.171  -11.450 1.00 12.11 ? 25  ASP A N   1 
ATOM   198  C CA  . ASP A 1 25  ? -13.616 5.084  -12.932 1.00 12.51 ? 25  ASP A CA  1 
ATOM   199  C C   . ASP A 1 25  ? -12.385 4.286  -13.387 1.00 12.24 ? 25  ASP A C   1 
ATOM   200  O O   . ASP A 1 25  ? -12.008 3.307  -12.711 1.00 13.79 ? 25  ASP A O   1 
ATOM   201  C CB  . ASP A 1 25  ? -13.791 6.490  -13.531 1.00 12.16 ? 25  ASP A CB  1 
ATOM   202  C CG  . ASP A 1 25  ? -14.243 6.552  -14.982 1.00 13.41 ? 25  ASP A CG  1 
ATOM   203  O OD1 . ASP A 1 25  ? -13.428 6.233  -15.905 1.00 16.37 ? 25  ASP A OD1 1 
ATOM   204  O OD2 . ASP A 1 25  ? -15.395 7.002  -15.205 1.00 12.47 ? 25  ASP A OD2 1 
ATOM   205  N N   . ALA A 1 26  ? -11.722 4.694  -14.459 1.00 12.01 ? 26  ALA A N   1 
ATOM   206  C CA  . ALA A 1 26  ? -10.540 3.971  -14.954 1.00 12.72 ? 26  ALA A CA  1 
ATOM   207  C C   . ALA A 1 26  ? -9.326  4.179  -14.058 1.00 12.90 ? 26  ALA A C   1 
ATOM   208  O O   . ALA A 1 26  ? -8.362  3.448  -14.208 1.00 18.22 ? 26  ALA A O   1 
ATOM   209  C CB  . ALA A 1 26  ? -10.228 4.411  -16.354 1.00 13.75 ? 26  ALA A CB  1 
ATOM   210  N N   . GLY A 1 27  ? -9.363  5.166  -13.166 1.00 11.11 ? 27  GLY A N   1 
ATOM   211  C CA  . GLY A 1 27  ? -8.267  5.401  -12.222 1.00 11.36 ? 27  GLY A CA  1 
ATOM   212  C C   . GLY A 1 27  ? -7.191  6.332  -12.725 1.00 10.05 ? 27  GLY A C   1 
ATOM   213  O O   . GLY A 1 27  ? -6.503  6.954  -11.908 1.00 10.27 ? 27  GLY A O   1 
ATOM   214  N N   . GLY A 1 28  ? -7.020  6.479  -14.036 1.00 9.98  ? 28  GLY A N   1 
ATOM   215  C CA  . GLY A 1 28  ? -6.031  7.423  -14.546 1.00 9.63  ? 28  GLY A CA  1 
ATOM   216  C C   . GLY A 1 28  ? -6.065  7.505  -16.051 1.00 9.09  ? 28  GLY A C   1 
ATOM   217  O O   . GLY A 1 28  ? -6.560  6.581  -16.712 1.00 10.55 ? 28  GLY A O   1 
ATOM   218  N N   . ARG A 1 29  ? -5.524  8.593  -16.566 1.00 8.50  ? 29  ARG A N   1 
ATOM   219  C CA  . ARG A 1 29  ? -5.480  8.825  -18.014 1.00 8.60  ? 29  ARG A CA  1 
ATOM   220  C C   . ARG A 1 29  ? -4.513  9.958  -18.299 1.00 8.24  ? 29  ARG A C   1 
ATOM   221  O O   . ARG A 1 29  ? -4.412  10.911 -17.506 1.00 8.52  ? 29  ARG A O   1 
ATOM   222  C CB  . ARG A 1 29  ? -6.855  9.220  -18.577 1.00 8.75  ? 29  ARG A CB  1 
ATOM   223  C CG  . ARG A 1 29  ? -7.070  8.742  -20.013 1.00 9.52  ? 29  ARG A CG  1 
ATOM   224  C CD  . ARG A 1 29  ? -8.148  9.505  -20.755 1.00 9.55  ? 29  ARG A CD  1 
ATOM   225  N NE  . ARG A 1 29  ? -7.651  10.815 -21.135 1.00 8.92  ? 29  ARG A NE  1 
ATOM   226  C CZ  . ARG A 1 29  ? -8.326  11.664 -21.895 1.00 8.77  ? 29  ARG A CZ  1 
ATOM   227  N NH1 . ARG A 1 29  ? -9.590  11.429 -22.207 1.00 9.59  ? 29  ARG A NH1 1 
ATOM   228  N NH2 . ARG A 1 29  ? -7.731  12.761 -22.329 1.00 9.48  ? 29  ARG A NH2 1 
ATOM   229  N N   . GLN A 1 30  ? -3.878  9.915  -19.455 1.00 8.66  ? 30  GLN A N   1 
ATOM   230  C CA  . GLN A 1 30  ? -3.089  11.046 -19.953 1.00 8.68  ? 30  GLN A CA  1 
ATOM   231  C C   . GLN A 1 30  ? -4.000  12.200 -20.367 1.00 7.99  ? 30  GLN A C   1 
ATOM   232  O O   . GLN A 1 30  ? -5.005  11.971 -21.074 1.00 9.41  ? 30  GLN A O   1 
ATOM   233  C CB  . GLN A 1 30  ? -2.271  10.579 -21.150 1.00 9.77  ? 30  GLN A CB  1 
ATOM   234  C CG  . GLN A 1 30  ? -1.304  11.640 -21.633 1.00 10.50 ? 30  GLN A CG  1 
ATOM   235  C CD  . GLN A 1 30  ? -0.397  11.107 -22.706 1.00 12.35 ? 30  GLN A CD  1 
ATOM   236  O OE1 . GLN A 1 30  ? 0.027   9.953  -22.661 1.00 16.59 ? 30  GLN A OE1 1 
ATOM   237  N NE2 . GLN A 1 30  ? -0.035  11.943 -23.664 1.00 14.63 ? 30  GLN A NE2 1 
ATOM   238  N N   . LEU A 1 31  ? -3.622  13.416 -19.983 1.00 7.88  ? 31  LEU A N   1 
ATOM   239  C CA  A LEU A 1 31  ? -4.263  14.676 -20.441 0.49 8.44  ? 31  LEU A CA  1 
ATOM   240  C CA  B LEU A 1 31  ? -4.280  14.651 -20.446 0.51 8.29  ? 31  LEU A CA  1 
ATOM   241  C C   . LEU A 1 31  ? -3.198  15.578 -21.020 1.00 8.04  ? 31  LEU A C   1 
ATOM   242  O O   . LEU A 1 31  ? -2.436  16.200 -20.269 1.00 8.54  ? 31  LEU A O   1 
ATOM   243  C CB  A LEU A 1 31  ? -4.892  15.528 -19.349 0.49 8.41  ? 31  LEU A CB  1 
ATOM   244  C CB  B LEU A 1 31  ? -5.066  15.315 -19.312 0.51 10.03 ? 31  LEU A CB  1 
ATOM   245  C CG  A LEU A 1 31  ? -6.063  14.925 -18.606 0.49 10.92 ? 31  LEU A CG  1 
ATOM   246  C CG  B LEU A 1 31  ? -6.483  14.804 -19.028 0.51 9.28  ? 31  LEU A CG  1 
ATOM   247  C CD1 A LEU A 1 31  ? -6.448  15.778 -17.406 0.49 9.40  ? 31  LEU A CD1 1 
ATOM   248  C CD1 B LEU A 1 31  ? -6.423  13.462 -18.297 0.51 10.32 ? 31  LEU A CD1 1 
ATOM   249  C CD2 A LEU A 1 31  ? -7.247  14.827 -19.542 0.49 11.75 ? 31  LEU A CD2 1 
ATOM   250  C CD2 B LEU A 1 31  ? -7.225  15.815 -18.146 0.51 9.25  ? 31  LEU A CD2 1 
ATOM   251  N N   . ASN A 1 32  ? -3.166  15.681 -22.329 1.00 8.56  ? 32  ASN A N   1 
ATOM   252  C CA  . ASN A 1 32  ? -2.303  16.694 -22.940 1.00 8.91  ? 32  ASN A CA  1 
ATOM   253  C C   . ASN A 1 32  ? -2.845  18.077 -22.594 1.00 8.18  ? 32  ASN A C   1 
ATOM   254  O O   . ASN A 1 32  ? -3.990  18.218 -22.132 1.00 8.10  ? 32  ASN A O   1 
ATOM   255  C CB  . ASN A 1 32  ? -2.213  16.489 -24.446 1.00 10.39 ? 32  ASN A CB  1 
ATOM   256  C CG  . ASN A 1 32  ? -1.505  15.199 -24.786 1.00 13.36 ? 32  ASN A CG  1 
ATOM   257  O OD1 . ASN A 1 32  ? -0.614  14.743 -24.082 1.00 18.55 ? 32  ASN A OD1 1 
ATOM   258  N ND2 . ASN A 1 32  ? -1.901  14.575 -25.869 1.00 20.44 ? 32  ASN A ND2 1 
ATOM   259  N N   . SER A 1 33  ? -2.025  19.091 -22.804 1.00 8.24  ? 33  SER A N   1 
ATOM   260  C CA  . SER A 1 33  ? -2.417  20.480 -22.548 1.00 8.03  ? 33  SER A CA  1 
ATOM   261  C C   . SER A 1 33  ? -3.720  20.811 -23.276 1.00 7.64  ? 33  SER A C   1 
ATOM   262  O O   . SER A 1 33  ? -3.770  20.741 -24.539 1.00 8.14  ? 33  SER A O   1 
ATOM   263  C CB  . SER A 1 33  ? -1.318  21.400 -22.994 1.00 8.58  ? 33  SER A CB  1 
ATOM   264  O OG  . SER A 1 33  ? -1.706  22.749 -22.883 1.00 9.21  ? 33  SER A OG  1 
ATOM   265  N N   . GLY A 1 34  ? -4.726  21.196 -22.519 1.00 7.41  ? 34  GLY A N   1 
ATOM   266  C CA  . GLY A 1 34  ? -6.039  21.564 -23.027 1.00 7.38  ? 34  GLY A CA  1 
ATOM   267  C C   . GLY A 1 34  ? -7.072  20.467 -22.988 1.00 7.57  ? 34  GLY A C   1 
ATOM   268  O O   . GLY A 1 34  ? -8.252  20.785 -23.178 1.00 8.25  ? 34  GLY A O   1 
ATOM   269  N N   . GLU A 1 35  ? -6.674  19.220 -22.794 1.00 7.16  ? 35  GLU A N   1 
ATOM   270  C CA  A GLU A 1 35  ? -7.621  18.092 -22.839 0.52 7.84  ? 35  GLU A CA  1 
ATOM   271  C CA  B GLU A 1 35  ? -7.619  18.096 -22.842 0.48 7.83  ? 35  GLU A CA  1 
ATOM   272  C C   . GLU A 1 35  ? -8.494  18.042 -21.587 1.00 7.35  ? 35  GLU A C   1 
ATOM   273  O O   . GLU A 1 35  ? -8.071  18.432 -20.470 1.00 8.15  ? 35  GLU A O   1 
ATOM   274  C CB  A GLU A 1 35  ? -6.928  16.738 -22.982 0.52 7.33  ? 35  GLU A CB  1 
ATOM   275  C CB  B GLU A 1 35  ? -6.858  16.796 -23.075 0.48 7.64  ? 35  GLU A CB  1 
ATOM   276  C CG  A GLU A 1 35  ? -6.416  16.452 -24.386 0.52 7.38  ? 35  GLU A CG  1 
ATOM   277  C CG  B GLU A 1 35  ? -6.128  16.776 -24.411 0.48 7.92  ? 35  GLU A CG  1 
ATOM   278  C CD  A GLU A 1 35  ? -5.955  15.024 -24.631 0.52 7.32  ? 35  GLU A CD  1 
ATOM   279  C CD  B GLU A 1 35  ? -5.518  15.441 -24.798 0.48 8.83  ? 35  GLU A CD  1 
ATOM   280  O OE1 A GLU A 1 35  ? -5.470  14.360 -23.695 0.52 8.29  ? 35  GLU A OE1 1 
ATOM   281  O OE1 B GLU A 1 35  ? -5.122  14.660 -23.911 0.48 8.34  ? 35  GLU A OE1 1 
ATOM   282  O OE2 A GLU A 1 35  ? -6.123  14.557 -25.785 0.52 8.88  ? 35  GLU A OE2 1 
ATOM   283  O OE2 B GLU A 1 35  ? -5.376  15.216 -26.028 0.48 11.29 ? 35  GLU A OE2 1 
ATOM   284  N N   . SER A 1 36  ? -9.673  17.478 -21.783 1.00 7.37  ? 36  SER A N   1 
ATOM   285  C CA  . SER A 1 36  ? -10.688 17.242 -20.751 1.00 7.37  ? 36  SER A CA  1 
ATOM   286  C C   . SER A 1 36  ? -11.048 15.765 -20.739 1.00 7.17  ? 36  SER A C   1 
ATOM   287  O O   . SER A 1 36  ? -11.261 15.180 -21.820 1.00 8.60  ? 36  SER A O   1 
ATOM   288  C CB  . SER A 1 36  ? -11.915 18.093 -21.001 1.00 7.67  ? 36  SER A CB  1 
ATOM   289  O OG  . SER A 1 36  ? -11.625 19.477 -21.078 1.00 8.09  ? 36  SER A OG  1 
ATOM   290  N N   . TRP A 1 37  ? -11.177 15.204 -19.552 1.00 7.25  ? 37  TRP A N   1 
ATOM   291  C CA  . TRP A 1 37  ? -11.536 13.799 -19.340 1.00 7.77  ? 37  TRP A CA  1 
ATOM   292  C C   . TRP A 1 37  ? -12.644 13.767 -18.302 1.00 7.43  ? 37  TRP A C   1 
ATOM   293  O O   . TRP A 1 37  ? -12.421 14.254 -17.183 1.00 8.19  ? 37  TRP A O   1 
ATOM   294  C CB  . TRP A 1 37  ? -10.321 13.041 -18.830 1.00 8.89  ? 37  TRP A CB  1 
ATOM   295  C CG  . TRP A 1 37  ? -10.574 11.610 -18.477 1.00 9.14  ? 37  TRP A CG  1 
ATOM   296  C CD1 . TRP A 1 37  ? -11.378 10.716 -19.111 1.00 10.17 ? 37  TRP A CD1 1 
ATOM   297  C CD2 . TRP A 1 37  ? -9.970  10.889 -17.393 1.00 9.41  ? 37  TRP A CD2 1 
ATOM   298  N NE1 . TRP A 1 37  ? -11.297 9.488  -18.506 1.00 11.03 ? 37  TRP A NE1 1 
ATOM   299  C CE2 . TRP A 1 37  ? -10.442 9.561  -17.450 1.00 10.13 ? 37  TRP A CE2 1 
ATOM   300  C CE3 . TRP A 1 37  ? -9.105  11.237 -16.358 1.00 10.08 ? 37  TRP A CE3 1 
ATOM   301  C CZ2 . TRP A 1 37  ? -10.079 8.596  -16.507 1.00 11.50 ? 37  TRP A CZ2 1 
ATOM   302  C CZ3 . TRP A 1 37  ? -8.730  10.282 -15.438 1.00 11.71 ? 37  TRP A CZ3 1 
ATOM   303  C CH2 . TRP A 1 37  ? -9.226  8.983  -15.501 1.00 11.67 ? 37  TRP A CH2 1 
ATOM   304  N N   . THR A 1 38  ? -13.795 13.226 -18.644 1.00 8.19  ? 38  THR A N   1 
ATOM   305  C CA  . THR A 1 38  ? -14.905 13.160 -17.693 1.00 8.93  ? 38  THR A CA  1 
ATOM   306  C C   . THR A 1 38  ? -15.016 11.758 -17.134 1.00 9.03  ? 38  THR A C   1 
ATOM   307  O O   . THR A 1 38  ? -15.145 10.785 -17.884 1.00 10.82 ? 38  THR A O   1 
ATOM   308  C CB  . THR A 1 38  ? -16.211 13.623 -18.310 1.00 11.09 ? 38  THR A CB  1 
ATOM   309  O OG1 . THR A 1 38  ? -15.988 14.941 -18.796 1.00 13.11 ? 38  THR A OG1 1 
ATOM   310  C CG2 . THR A 1 38  ? -17.338 13.623 -17.306 1.00 12.69 ? 38  THR A CG2 1 
ATOM   311  N N   . ILE A 1 39  ? -14.984 11.680 -15.814 1.00 9.13  ? 39  ILE A N   1 
ATOM   312  C CA  . ILE A 1 39  ? -15.153 10.401 -15.115 1.00 9.09  ? 39  ILE A CA  1 
ATOM   313  C C   . ILE A 1 39  ? -16.473 10.401 -14.357 1.00 8.79  ? 39  ILE A C   1 
ATOM   314  O O   . ILE A 1 39  ? -17.056 11.441 -14.044 1.00 9.56  ? 39  ILE A O   1 
ATOM   315  C CB  . ILE A 1 39  ? -13.970 10.085 -14.186 1.00 9.64  ? 39  ILE A CB  1 
ATOM   316  C CG1 . ILE A 1 39  ? -13.834 11.068 -13.018 1.00 9.66  ? 39  ILE A CG1 1 
ATOM   317  C CG2 . ILE A 1 39  ? -12.695 9.989  -14.995 1.00 11.88 ? 39  ILE A CG2 1 
ATOM   318  C CD1 . ILE A 1 39  ? -12.879 10.601 -11.942 1.00 10.66 ? 39  ILE A CD1 1 
ATOM   319  N N   . ASN A 1 40  ? -16.898 9.185  -14.042 1.00 9.10  ? 40  ASN A N   1 
ATOM   320  C CA  . ASN A 1 40  ? -18.084 8.936  -13.214 1.00 9.80  ? 40  ASN A CA  1 
ATOM   321  C C   . ASN A 1 40  ? -17.620 8.309  -11.917 1.00 9.91  ? 40  ASN A C   1 
ATOM   322  O O   . ASN A 1 40  ? -16.898 7.301  -11.935 1.00 12.76 ? 40  ASN A O   1 
ATOM   323  C CB  . ASN A 1 40  ? -19.064 8.064  -13.968 1.00 11.85 ? 40  ASN A CB  1 
ATOM   324  C CG  . ASN A 1 40  ? -19.678 8.889  -15.077 1.00 13.75 ? 40  ASN A CG  1 
ATOM   325  O OD1 . ASN A 1 40  ? -20.624 9.626  -14.834 1.00 15.33 ? 40  ASN A OD1 1 
ATOM   326  N ND2 . ASN A 1 40  ? -19.093 8.874  -16.263 1.00 16.01 ? 40  ASN A ND2 1 
ATOM   327  N N   . VAL A 1 41  ? -18.031 8.922  -10.824 1.00 9.79  ? 41  VAL A N   1 
ATOM   328  C CA  . VAL A 1 41  ? -17.697 8.462  -9.461  1.00 10.09 ? 41  VAL A CA  1 
ATOM   329  C C   . VAL A 1 41  ? -18.992 7.977  -8.807  1.00 10.37 ? 41  VAL A C   1 
ATOM   330  O O   . VAL A 1 41  ? -20.006 8.683  -8.834  1.00 11.29 ? 41  VAL A O   1 
ATOM   331  C CB  . VAL A 1 41  ? -17.027 9.588  -8.667  1.00 10.60 ? 41  VAL A CB  1 
ATOM   332  C CG1 . VAL A 1 41  ? -16.828 9.188  -7.216  1.00 11.32 ? 41  VAL A CG1 1 
ATOM   333  C CG2 . VAL A 1 41  ? -15.709 10.007 -9.300  1.00 11.52 ? 41  VAL A CG2 1 
ATOM   334  N N   . GLU A 1 42  ? -18.969 6.798  -8.217  1.00 10.30 ? 42  GLU A N   1 
ATOM   335  C CA  . GLU A 1 42  ? -20.197 6.224  -7.639  1.00 10.94 ? 42  GLU A CA  1 
ATOM   336  C C   . GLU A 1 42  ? -20.701 7.096  -6.502  1.00 10.25 ? 42  GLU A C   1 
ATOM   337  O O   . GLU A 1 42  ? -19.918 7.539  -5.636  1.00 10.31 ? 42  GLU A O   1 
ATOM   338  C CB  . GLU A 1 42  ? -19.970 4.806  -7.126  1.00 12.69 ? 42  GLU A CB  1 
ATOM   339  C CG  . GLU A 1 42  ? -21.298 4.138  -6.754  1.00 15.88 ? 42  GLU A CG  1 
ATOM   340  C CD  . GLU A 1 42  ? -21.331 2.719  -6.228  1.00 18.88 ? 42  GLU A CD  1 
ATOM   341  O OE1 . GLU A 1 42  ? -20.414 2.355  -5.468  1.00 25.13 ? 42  GLU A OE1 1 
ATOM   342  O OE2 . GLU A 1 42  ? -22.334 2.013  -6.502  1.00 20.36 ? 42  GLU A OE2 1 
ATOM   343  N N   A PRO A 1 43  ? -22.021 7.432  -6.432  0.49 10.47 ? 43  PRO A N   1 
ATOM   344  N N   B PRO A 1 43  ? -22.031 7.208  -6.388  0.51 10.57 ? 43  PRO A N   1 
ATOM   345  C CA  A PRO A 1 43  ? -22.560 8.160  -5.283  0.49 10.03 ? 43  PRO A CA  1 
ATOM   346  C CA  B PRO A 1 43  ? -22.593 7.796  -5.190  0.51 9.60  ? 43  PRO A CA  1 
ATOM   347  C C   A PRO A 1 43  ? -22.226 7.478  -3.958  0.49 9.40  ? 43  PRO A C   1 
ATOM   348  C C   B PRO A 1 43  ? -22.036 7.044  -3.973  0.51 9.01  ? 43  PRO A C   1 
ATOM   349  O O   A PRO A 1 43  ? -22.118 6.268  -3.908  0.49 9.70  ? 43  PRO A O   1 
ATOM   350  O O   B PRO A 1 43  ? -21.782 5.834  -3.992  0.51 8.98  ? 43  PRO A O   1 
ATOM   351  C CB  A PRO A 1 43  ? -24.078 8.114  -5.486  0.49 10.41 ? 43  PRO A CB  1 
ATOM   352  C CB  B PRO A 1 43  ? -24.105 7.645  -5.402  0.51 10.54 ? 43  PRO A CB  1 
ATOM   353  C CG  A PRO A 1 43  ? -24.229 8.057  -6.973  0.49 10.70 ? 43  PRO A CG  1 
ATOM   354  C CG  B PRO A 1 43  ? -24.272 7.536  -6.893  0.51 12.06 ? 43  PRO A CG  1 
ATOM   355  C CD  A PRO A 1 43  ? -23.072 7.186  -7.432  0.49 10.48 ? 43  PRO A CD  1 
ATOM   356  C CD  B PRO A 1 43  ? -23.047 6.783  -7.361  0.51 11.01 ? 43  PRO A CD  1 
ATOM   357  N N   A GLY A 1 44  ? -22.101 8.277  -2.905  0.49 8.75  ? 44  GLY A N   1 
ATOM   358  N N   B GLY A 1 44  ? -21.811 7.808  -2.918  0.51 8.36  ? 44  GLY A N   1 
ATOM   359  C CA  A GLY A 1 44  ? -21.748 7.754  -1.583  0.49 9.46  ? 44  GLY A CA  1 
ATOM   360  C CA  B GLY A 1 44  ? -21.391 7.248  -1.629  0.51 8.31  ? 44  GLY A CA  1 
ATOM   361  C C   A GLY A 1 44  ? -20.252 7.548  -1.418  0.49 9.35  ? 44  GLY A C   1 
ATOM   362  C C   B GLY A 1 44  ? -19.890 7.090  -1.512  0.51 8.58  ? 44  GLY A C   1 
ATOM   363  O O   A GLY A 1 44  ? -19.831 7.130  -0.337  0.49 10.30 ? 44  GLY A O   1 
ATOM   364  O O   B GLY A 1 44  ? -19.446 6.612  -0.462  0.51 10.11 ? 44  GLY A O   1 
ATOM   365  N N   A THR A 1 45  ? -19.439 7.845  -2.427  0.49 9.71  ? 45  THR A N   1 
ATOM   366  N N   B THR A 1 45  ? -19.109 7.479  -2.515  0.51 7.95  ? 45  THR A N   1 
ATOM   367  C CA  A THR A 1 45  ? -17.975 7.646  -2.321  0.49 9.73  ? 45  THR A CA  1 
ATOM   368  C CA  B THR A 1 45  ? -17.643 7.327  -2.445  0.51 8.73  ? 45  THR A CA  1 
ATOM   369  C C   A THR A 1 45  ? -17.436 8.492  -1.165  0.49 9.23  ? 45  THR A C   1 
ATOM   370  C C   B THR A 1 45  ? -17.122 8.183  -1.298  0.51 8.62  ? 45  THR A C   1 
ATOM   371  O O   A THR A 1 45  ? -17.689 9.704  -1.138  0.49 10.35 ? 45  THR A O   1 
ATOM   372  O O   B THR A 1 45  ? -17.318 9.401  -1.306  0.51 8.77  ? 45  THR A O   1 
ATOM   373  C CB  A THR A 1 45  ? -17.279 7.981  -3.645  0.49 10.31 ? 45  THR A CB  1 
ATOM   374  C CB  B THR A 1 45  ? -16.969 7.755  -3.750  0.51 9.59  ? 45  THR A CB  1 
ATOM   375  O OG1 A THR A 1 45  ? -17.511 6.912  -4.564  0.49 11.10 ? 45  THR A OG1 1 
ATOM   376  O OG1 B THR A 1 45  ? -17.392 6.898  -4.810  0.51 11.88 ? 45  THR A OG1 1 
ATOM   377  C CG2 A THR A 1 45  ? -15.784 8.168  -3.500  0.49 9.96  ? 45  THR A CG2 1 
ATOM   378  C CG2 B THR A 1 45  ? -15.461 7.714  -3.653  0.51 10.01 ? 45  THR A CG2 1 
ATOM   379  N N   A ASN A 1 46  ? -16.720 7.843  -0.254  0.49 10.69 ? 46  ASN A N   1 
ATOM   380  N N   B ASN A 1 46  ? -16.446 7.544  -0.365  0.51 9.11  ? 46  ASN A N   1 
ATOM   381  C CA  A ASN A 1 46  ? -16.086 8.478  0.921   0.49 12.69 ? 46  ASN A CA  1 
ATOM   382  C CA  B ASN A 1 46  ? -15.927 8.245  0.818   0.51 11.20 ? 46  ASN A CA  1 
ATOM   383  C C   A ASN A 1 46  ? -14.564 8.399  0.761   0.49 11.57 ? 46  ASN A C   1 
ATOM   384  C C   B ASN A 1 46  ? -14.426 8.364  0.627   0.51 11.08 ? 46  ASN A C   1 
ATOM   385  O O   A ASN A 1 46  ? -14.035 7.288  0.591   0.49 14.10 ? 46  ASN A O   1 
ATOM   386  O O   B ASN A 1 46  ? -13.760 7.370  0.249   0.51 11.65 ? 46  ASN A O   1 
ATOM   387  C CB  A ASN A 1 46  ? -16.556 7.804  2.209   0.49 16.42 ? 46  ASN A CB  1 
ATOM   388  C CB  B ASN A 1 46  ? -16.346 7.514  2.086   0.51 13.94 ? 46  ASN A CB  1 
ATOM   389  C CG  A ASN A 1 46  ? -15.965 8.419  3.459   0.49 19.51 ? 46  ASN A CG  1 
ATOM   390  C CG  B ASN A 1 46  ? -16.202 8.333  3.353   0.51 17.01 ? 46  ASN A CG  1 
ATOM   391  O OD1 A ASN A 1 46  ? -16.657 9.116  4.193   0.49 25.74 ? 46  ASN A OD1 1 
ATOM   392  O OD1 B ASN A 1 46  ? -16.449 9.544  3.400   0.51 19.11 ? 46  ASN A OD1 1 
ATOM   393  N ND2 A ASN A 1 46  ? -14.690 8.173  3.710   0.49 20.71 ? 46  ASN A ND2 1 
ATOM   394  N ND2 B ASN A 1 46  ? -15.804 7.665  4.418   0.51 21.57 ? 46  ASN A ND2 1 
ATOM   395  N N   . GLY A 1 47  ? -13.887 9.535  0.893   1.00 10.99 ? 47  GLY A N   1 
ATOM   396  C CA  . GLY A 1 47  ? -12.426 9.623  0.874   1.00 11.09 ? 47  GLY A CA  1 
ATOM   397  C C   . GLY A 1 47  ? -11.844 9.455  -0.520  1.00 10.07 ? 47  GLY A C   1 
ATOM   398  O O   . GLY A 1 47  ? -10.745 8.901  -0.672  1.00 11.90 ? 47  GLY A O   1 
ATOM   399  N N   . GLY A 1 48  ? -12.531 9.975  -1.529  1.00 9.27  ? 48  GLY A N   1 
ATOM   400  C CA  . GLY A 1 48  ? -11.963 10.003 -2.878  1.00 8.79  ? 48  GLY A CA  1 
ATOM   401  C C   . GLY A 1 48  ? -10.958 11.117 -3.034  1.00 8.05  ? 48  GLY A C   1 
ATOM   402  O O   . GLY A 1 48  ? -11.057 12.177 -2.373  1.00 8.33  ? 48  GLY A O   1 
ATOM   403  N N   . LYS A 1 49  ? -10.027 10.929 -3.963  1.00 7.75  ? 49  LYS A N   1 
ATOM   404  C CA  . LYS A 1 49  ? -9.026  11.948 -4.303  1.00 7.82  ? 49  LYS A CA  1 
ATOM   405  C C   . LYS A 1 49  ? -8.772  11.927 -5.798  1.00 7.55  ? 49  LYS A C   1 
ATOM   406  O O   . LYS A 1 49  ? -8.755  10.862 -6.419  1.00 8.53  ? 49  LYS A O   1 
ATOM   407  C CB  . LYS A 1 49  ? -7.710  11.741 -3.561  1.00 8.74  ? 49  LYS A CB  1 
ATOM   408  C CG  . LYS A 1 49  ? -7.856  11.674 -2.044  1.00 9.44  ? 49  LYS A CG  1 
ATOM   409  C CD  . LYS A 1 49  ? -6.525  11.628 -1.335  1.00 11.41 ? 49  LYS A CD  1 
ATOM   410  C CE  . LYS A 1 49  ? -6.605  11.195 0.099   1.00 13.53 ? 49  LYS A CE  1 
ATOM   411  N NZ  . LYS A 1 49  ? -7.487  12.061 0.912   1.00 14.07 ? 49  LYS A NZ  1 
ATOM   412  N N   . ILE A 1 50  ? -8.547  13.124 -6.332  1.00 6.90  ? 50  ILE A N   1 
ATOM   413  C CA  . ILE A 1 50  ? -8.051  13.343 -7.702  1.00 6.79  ? 50  ILE A CA  1 
ATOM   414  C C   . ILE A 1 50  ? -6.771  14.146 -7.608  1.00 6.51  ? 50  ILE A C   1 
ATOM   415  O O   . ILE A 1 50  ? -6.672  15.100 -6.814  1.00 6.81  ? 50  ILE A O   1 
ATOM   416  C CB  . ILE A 1 50  ? -9.120  14.039 -8.565  1.00 7.12  ? 50  ILE A CB  1 
ATOM   417  C CG1 . ILE A 1 50  ? -10.276 13.086 -8.844  1.00 8.09  ? 50  ILE A CG1 1 
ATOM   418  C CG2 . ILE A 1 50  ? -8.526  14.584 -9.863  1.00 7.73  ? 50  ILE A CG2 1 
ATOM   419  C CD1 . ILE A 1 50  ? -11.550 13.756 -9.309  1.00 8.77  ? 50  ILE A CD1 1 
ATOM   420  N N   . TRP A 1 51  ? -5.794  13.782 -8.435  1.00 6.53  ? 51  TRP A N   1 
ATOM   421  C CA  . TRP A 1 51  ? -4.524  14.506 -8.474  1.00 6.46  ? 51  TRP A CA  1 
ATOM   422  C C   . TRP A 1 51  ? -3.933  14.404 -9.878  1.00 6.38  ? 51  TRP A C   1 
ATOM   423  O O   . TRP A 1 51  ? -4.380  13.606 -10.703 1.00 7.28  ? 51  TRP A O   1 
ATOM   424  C CB  . TRP A 1 51  ? -3.533  14.016 -7.392  1.00 6.92  ? 51  TRP A CB  1 
ATOM   425  C CG  . TRP A 1 51  ? -3.030  12.609 -7.539  1.00 7.63  ? 51  TRP A CG  1 
ATOM   426  C CD1 . TRP A 1 51  ? -1.800  12.248 -7.988  1.00 8.11  ? 51  TRP A CD1 1 
ATOM   427  C CD2 . TRP A 1 51  ? -3.708  11.379 -7.178  1.00 8.22  ? 51  TRP A CD2 1 
ATOM   428  N NE1 . TRP A 1 51  ? -1.646  10.887 -7.923  1.00 9.14  ? 51  TRP A NE1 1 
ATOM   429  C CE2 . TRP A 1 51  ? -2.803  10.327 -7.425  1.00 9.15  ? 51  TRP A CE2 1 
ATOM   430  C CE3 . TRP A 1 51  ? -4.983  11.050 -6.677  1.00 8.86  ? 51  TRP A CE3 1 
ATOM   431  C CZ2 . TRP A 1 51  ? -3.133  8.984  -7.220  1.00 10.50 ? 51  TRP A CZ2 1 
ATOM   432  C CZ3 . TRP A 1 51  ? -5.308  9.725  -6.487  1.00 9.96  ? 51  TRP A CZ3 1 
ATOM   433  C CH2 . TRP A 1 51  ? -4.396  8.702  -6.749  1.00 10.99 ? 51  TRP A CH2 1 
ATOM   434  N N   . ALA A 1 52  ? -2.950  15.246 -10.108 1.00 6.69  ? 52  ALA A N   1 
ATOM   435  C CA  . ALA A 1 52  ? -2.122  15.199 -11.314 1.00 6.99  ? 52  ALA A CA  1 
ATOM   436  C C   . ALA A 1 52  ? -0.815  14.487 -11.017 1.00 7.24  ? 52  ALA A C   1 
ATOM   437  O O   . ALA A 1 52  ? -0.250  14.605 -9.926  1.00 8.48  ? 52  ALA A O   1 
ATOM   438  C CB  . ALA A 1 52  ? -1.836  16.587 -11.842 1.00 8.20  ? 52  ALA A CB  1 
ATOM   439  N N   . ARG A 1 53  ? -0.311  13.807 -12.030 1.00 7.56  ? 53  ARG A N   1 
ATOM   440  C CA  . ARG A 1 53  ? 1.016   13.203 -12.029 1.00 8.10  ? 53  ARG A CA  1 
ATOM   441  C C   . ARG A 1 53  ? 1.810   13.832 -13.161 1.00 8.11  ? 53  ARG A C   1 
ATOM   442  O O   . ARG A 1 53  ? 1.258   14.109 -14.247 1.00 8.43  ? 53  ARG A O   1 
ATOM   443  C CB  . ARG A 1 53  ? 0.939   11.696 -12.226 1.00 8.75  ? 53  ARG A CB  1 
ATOM   444  C CG  . ARG A 1 53  ? 0.106   11.026 -11.152 1.00 9.37  ? 53  ARG A CG  1 
ATOM   445  C CD  . ARG A 1 53  ? -0.136  9.579  -11.466 1.00 9.92  ? 53  ARG A CD  1 
ATOM   446  N NE  . ARG A 1 53  ? -1.099  9.465  -12.568 1.00 9.89  ? 53  ARG A NE  1 
ATOM   447  C CZ  . ARG A 1 53  ? -1.427  8.326  -13.142 1.00 10.95 ? 53  ARG A CZ  1 
ATOM   448  N NH1 . ARG A 1 53  ? -0.737  7.229  -12.895 1.00 12.87 ? 53  ARG A NH1 1 
ATOM   449  N NH2 . ARG A 1 53  ? -2.404  8.299  -14.037 1.00 11.27 ? 53  ARG A NH2 1 
ATOM   450  N N   . THR A 1 54  ? 3.076   14.047 -12.915 1.00 8.87  ? 54  THR A N   1 
ATOM   451  C CA  . THR A 1 54  ? 3.940   14.685 -13.899 1.00 9.36  ? 54  THR A CA  1 
ATOM   452  C C   . THR A 1 54  ? 5.109   13.788 -14.288 1.00 9.85  ? 54  THR A C   1 
ATOM   453  O O   . THR A 1 54  ? 5.550   12.928 -13.496 1.00 11.01 ? 54  THR A O   1 
ATOM   454  C CB  . THR A 1 54  ? 4.427   16.032 -13.396 1.00 10.17 ? 54  THR A CB  1 
ATOM   455  O OG1 . THR A 1 54  ? 5.222   15.817 -12.230 1.00 11.44 ? 54  THR A OG1 1 
ATOM   456  C CG2 . THR A 1 54  ? 3.277   16.975 -13.102 1.00 11.16 ? 54  THR A CG2 1 
ATOM   457  N N   A ASP A 1 55  ? 5.504   13.855 -15.540 0.54 7.96  ? 55  ASP A N   1 
ATOM   458  N N   B ASP A 1 55  ? 5.658   14.188 -15.466 0.46 10.01 ? 55  ASP A N   1 
ATOM   459  C CA  A ASP A 1 55  ? 6.781   13.220 -15.935 0.54 7.60  ? 55  ASP A CA  1 
ATOM   460  C CA  B ASP A 1 55  ? 6.846   13.666 -16.212 0.46 10.99 ? 55  ASP A CA  1 
ATOM   461  C C   A ASP A 1 55  ? 6.626   11.707 -15.838 0.54 6.85  ? 55  ASP A C   1 
ATOM   462  C C   B ASP A 1 55  ? 6.817   12.147 -16.160 0.46 9.73  ? 55  ASP A C   1 
ATOM   463  O O   A ASP A 1 55  ? 7.490   11.027 -15.255 0.54 7.69  ? 55  ASP A O   1 
ATOM   464  O O   B ASP A 1 55  ? 7.705   11.517 -15.561 0.46 10.74 ? 55  ASP A O   1 
ATOM   465  C CB  A ASP A 1 55  ? 7.943   13.794 -15.132 0.54 7.28  ? 55  ASP A CB  1 
ATOM   466  C CB  B ASP A 1 55  ? 8.189   14.213 -15.726 0.46 11.98 ? 55  ASP A CB  1 
ATOM   467  C CG  A ASP A 1 55  ? 8.110   15.301 -15.303 0.54 8.08  ? 55  ASP A CG  1 
ATOM   468  C CG  B ASP A 1 55  ? 8.513   15.589 -16.275 0.46 14.21 ? 55  ASP A CG  1 
ATOM   469  O OD1 A ASP A 1 55  ? 7.713   15.841 -16.368 0.54 9.96  ? 55  ASP A OD1 1 
ATOM   470  O OD1 B ASP A 1 55  ? 8.628   15.719 -17.504 0.46 18.73 ? 55  ASP A OD1 1 
ATOM   471  O OD2 A ASP A 1 55  ? 8.666   15.935 -14.385 0.54 11.55 ? 55  ASP A OD2 1 
ATOM   472  O OD2 B ASP A 1 55  ? 8.598   16.527 -15.476 0.46 18.52 ? 55  ASP A OD2 1 
ATOM   473  N N   A CYS A 1 56  ? 5.553   11.189 -16.437 0.54 6.60  ? 56  CYS A N   1 
ATOM   474  N N   B CYS A 1 56  ? 5.818   11.582 -16.810 0.46 9.02  ? 56  CYS A N   1 
ATOM   475  C CA  A CYS A 1 56  ? 5.224   9.746  -16.432 0.54 6.86  ? 56  CYS A CA  1 
ATOM   476  C CA  B CYS A 1 56  ? 5.526   10.137 -16.732 0.46 8.67  ? 56  CYS A CA  1 
ATOM   477  C C   A CYS A 1 56  ? 5.651   9.075  -17.732 0.54 6.93  ? 56  CYS A C   1 
ATOM   478  C C   B CYS A 1 56  ? 6.043   9.452  -17.996 0.46 8.85  ? 56  CYS A C   1 
ATOM   479  O O   A CYS A 1 56  ? 5.632   9.694  -18.809 0.54 7.44  ? 56  CYS A O   1 
ATOM   480  O O   B CYS A 1 56  ? 6.057   10.075 -19.086 0.46 10.15 ? 56  CYS A O   1 
ATOM   481  C CB  A CYS A 1 56  ? 3.729   9.488  -16.332 0.54 7.65  ? 56  CYS A CB  1 
ATOM   482  C CB  B CYS A 1 56  ? 4.029   9.886  -16.600 0.46 9.31  ? 56  CYS A CB  1 
ATOM   483  S SG  A CYS A 1 56  ? 2.901   10.260 -14.921 0.54 8.40  ? 56  CYS A SG  1 
ATOM   484  S SG  B CYS A 1 56  ? 3.250   10.624 -15.133 0.46 10.45 ? 56  CYS A SG  1 
ATOM   485  N N   A TYR A 1 57  ? 5.940   7.791  -17.610 0.54 7.12  ? 57  TYR A N   1 
ATOM   486  N N   B TYR A 1 57  ? 6.428   8.193  -17.826 0.46 9.53  ? 57  TYR A N   1 
ATOM   487  C CA  A TYR A 1 57  ? 6.216   6.865  -18.728 0.54 7.40  ? 57  TYR A CA  1 
ATOM   488  C CA  B TYR A 1 57  ? 6.775   7.232  -18.897 0.46 9.71  ? 57  TYR A CA  1 
ATOM   489  C C   A TYR A 1 57  ? 5.481   5.571  -18.432 0.54 8.14  ? 57  TYR A C   1 
ATOM   490  C C   B TYR A 1 57  ? 5.969   5.969  -18.651 0.46 10.40 ? 57  TYR A C   1 
ATOM   491  O O   A TYR A 1 57  ? 5.745   4.955  -17.406 0.54 10.15 ? 57  TYR A O   1 
ATOM   492  O O   B TYR A 1 57  ? 6.012   5.466  -17.538 0.46 11.76 ? 57  TYR A O   1 
ATOM   493  C CB  A TYR A 1 57  ? 7.719   6.614  -18.891 0.54 7.74  ? 57  TYR A CB  1 
ATOM   494  C CB  B TYR A 1 57  ? 8.278   6.975  -18.896 0.46 10.19 ? 57  TYR A CB  1 
ATOM   495  C CG  A TYR A 1 57  ? 8.466   7.831  -19.362 0.54 8.64  ? 57  TYR A CG  1 
ATOM   496  C CG  B TYR A 1 57  ? 8.976   8.267  -19.166 0.46 14.15 ? 57  TYR A CG  1 
ATOM   497  C CD1 A TYR A 1 57  ? 8.329   8.266  -20.672 0.54 9.96  ? 57  TYR A CD1 1 
ATOM   498  C CD1 B TYR A 1 57  ? 9.299   8.618  -20.463 0.46 15.30 ? 57  TYR A CD1 1 
ATOM   499  C CD2 A TYR A 1 57  ? 9.249   8.584  -18.509 0.54 9.16  ? 57  TYR A CD2 1 
ATOM   500  C CD2 B TYR A 1 57  ? 9.153   9.196  -18.157 0.46 15.87 ? 57  TYR A CD2 1 
ATOM   501  C CE1 A TYR A 1 57  ? 8.976   9.401  -21.140 0.54 10.20 ? 57  TYR A CE1 1 
ATOM   502  C CE1 B TYR A 1 57  ? 9.883   9.837  -20.754 0.46 15.14 ? 57  TYR A CE1 1 
ATOM   503  C CE2 A TYR A 1 57  ? 9.899   9.722  -18.958 0.54 10.27 ? 57  TYR A CE2 1 
ATOM   504  C CE2 B TYR A 1 57  ? 9.722   10.424 -18.424 0.46 17.42 ? 57  TYR A CE2 1 
ATOM   505  C CZ  A TYR A 1 57  ? 9.734   10.152 -20.257 0.54 9.82  ? 57  TYR A CZ  1 
ATOM   506  C CZ  B TYR A 1 57  ? 10.098  10.734 -19.720 0.46 17.11 ? 57  TYR A CZ  1 
ATOM   507  O OH  A TYR A 1 57  ? 10.378  11.264 -20.709 0.54 10.53 ? 57  TYR A OH  1 
ATOM   508  O OH  B TYR A 1 57  ? 10.661  11.952 -19.949 0.46 22.53 ? 57  TYR A OH  1 
ATOM   509  N N   A PHE A 1 58  ? 4.610   5.153  -19.342 0.54 9.21  ? 58  PHE A N   1 
ATOM   510  N N   B PHE A 1 58  ? 5.259   5.498  -19.676 0.46 11.12 ? 58  PHE A N   1 
ATOM   511  C CA  A PHE A 1 58  ? 3.858   3.893  -19.208 0.54 10.07 ? 58  PHE A CA  1 
ATOM   512  C CA  B PHE A 1 58  ? 4.501   4.227  -19.621 0.46 11.91 ? 58  PHE A CA  1 
ATOM   513  C C   A PHE A 1 58  ? 4.108   3.053  -20.447 0.54 12.26 ? 58  PHE A C   1 
ATOM   514  C C   B PHE A 1 58  ? 4.744   3.430  -20.898 0.46 13.98 ? 58  PHE A C   1 
ATOM   515  O O   A PHE A 1 58  ? 4.127   3.585  -21.575 0.54 14.13 ? 58  PHE A O   1 
ATOM   516  O O   B PHE A 1 58  ? 4.793   4.016  -21.991 0.46 15.52 ? 58  PHE A O   1 
ATOM   517  C CB  A PHE A 1 58  ? 2.372   4.154  -19.006 0.54 10.38 ? 58  PHE A CB  1 
ATOM   518  C CB  B PHE A 1 58  ? 3.006   4.473  -19.431 0.46 12.55 ? 58  PHE A CB  1 
ATOM   519  C CG  A PHE A 1 58  ? 2.072   4.839  -17.706 0.54 9.56  ? 58  PHE A CG  1 
ATOM   520  C CG  B PHE A 1 58  ? 2.675   5.150  -18.130 0.46 11.30 ? 58  PHE A CG  1 
ATOM   521  C CD1 A PHE A 1 58  ? 2.191   4.154  -16.513 0.54 9.72  ? 58  PHE A CD1 1 
ATOM   522  C CD1 B PHE A 1 58  ? 2.860   4.489  -16.928 0.46 11.27 ? 58  PHE A CD1 1 
ATOM   523  C CD2 A PHE A 1 58  ? 1.698   6.171  -17.667 0.54 10.38 ? 58  PHE A CD2 1 
ATOM   524  C CD2 B PHE A 1 58  ? 2.199   6.448  -18.109 0.46 11.14 ? 58  PHE A CD2 1 
ATOM   525  C CE1 A PHE A 1 58  ? 1.940   4.778  -15.303 0.54 10.15 ? 58  PHE A CE1 1 
ATOM   526  C CE1 B PHE A 1 58  ? 2.570   5.112  -15.723 0.46 11.91 ? 58  PHE A CE1 1 
ATOM   527  C CE2 A PHE A 1 58  ? 1.459   6.795  -16.454 0.54 10.65 ? 58  PHE A CE2 1 
ATOM   528  C CE2 B PHE A 1 58  ? 1.903   7.066  -16.905 0.46 11.66 ? 58  PHE A CE2 1 
ATOM   529  C CZ  A PHE A 1 58  ? 1.569   6.097  -15.275 0.54 10.78 ? 58  PHE A CZ  1 
ATOM   530  C CZ  B PHE A 1 58  ? 2.082   6.398  -15.718 0.46 11.98 ? 58  PHE A CZ  1 
ATOM   531  N N   A ASP A 1 59  ? 4.266   1.755  -20.222 0.54 13.53 ? 59  ASP A N   1 
ATOM   532  N N   B ASP A 1 59  ? 4.867   2.115  -20.743 0.46 15.86 ? 59  ASP A N   1 
ATOM   533  C CA  A ASP A 1 59  ? 4.388   0.775  -21.319 0.54 15.98 ? 59  ASP A CA  1 
ATOM   534  C CA  B ASP A 1 59  ? 4.984   1.165  -21.879 0.46 17.70 ? 59  ASP A CA  1 
ATOM   535  C C   A ASP A 1 59  ? 2.968   0.508  -21.819 0.54 17.81 ? 59  ASP A C   1 
ATOM   536  C C   B ASP A 1 59  ? 3.579   0.751  -22.359 0.46 19.73 ? 59  ASP A C   1 
ATOM   537  O O   A ASP A 1 59  ? 2.001   1.078  -21.299 0.54 18.62 ? 59  ASP A O   1 
ATOM   538  O O   B ASP A 1 59  ? 2.588   1.299  -21.847 0.46 20.98 ? 59  ASP A O   1 
ATOM   539  C CB  A ASP A 1 59  ? 5.164   -0.468 -20.874 0.54 16.75 ? 59  ASP A CB  1 
ATOM   540  C CB  B ASP A 1 59  ? 5.889   -0.004 -21.488 0.46 19.17 ? 59  ASP A CB  1 
ATOM   541  C CG  A ASP A 1 59  ? 4.444   -1.344 -19.862 0.54 17.08 ? 59  ASP A CG  1 
ATOM   542  C CG  B ASP A 1 59  ? 5.294   -0.929 -20.443 0.46 19.14 ? 59  ASP A CG  1 
ATOM   543  O OD1 A ASP A 1 59  ? 3.216   -1.194 -19.711 0.54 16.67 ? 59  ASP A OD1 1 
ATOM   544  O OD1 B ASP A 1 59  ? 4.092   -0.785 -20.156 0.46 19.59 ? 59  ASP A OD1 1 
ATOM   545  O OD2 A ASP A 1 59  ? 5.117   -2.182 -19.238 0.54 20.28 ? 59  ASP A OD2 1 
ATOM   546  O OD2 B ASP A 1 59  ? 6.040   -1.794 -19.931 0.46 22.68 ? 59  ASP A OD2 1 
ATOM   547  N N   A ASP A 1 60  ? 2.846   -0.385 -22.793 0.50 19.74 ? 60  ASP A N   1 
ATOM   548  N N   B ASP A 1 60  ? 3.490   -0.154 -23.347 0.50 21.87 ? 60  ASP A N   1 
ATOM   549  C CA  A ASP A 1 60  ? 1.575   -0.662 -23.504 0.50 21.65 ? 60  ASP A CA  1 
ATOM   550  C CA  B ASP A 1 60  ? 2.213   -0.613 -23.968 0.50 27.24 ? 60  ASP A CA  1 
ATOM   551  C C   A ASP A 1 60  ? 0.595   -1.450 -22.621 0.50 22.55 ? 60  ASP A C   1 
ATOM   552  C C   B ASP A 1 60  ? 1.242   -1.146 -22.902 0.50 26.64 ? 60  ASP A C   1 
ATOM   553  O O   A ASP A 1 60  ? -0.549  -1.634 -23.065 0.50 27.49 ? 60  ASP A O   1 
ATOM   554  O O   B ASP A 1 60  ? 0.020   -0.918 -23.054 0.50 29.94 ? 60  ASP A O   1 
ATOM   555  C CB  A ASP A 1 60  ? 1.880   -1.391 -24.810 0.50 23.76 ? 60  ASP A CB  1 
ATOM   556  C CB  B ASP A 1 60  ? 2.455   -1.704 -25.014 0.50 31.43 ? 60  ASP A CB  1 
ATOM   557  C CG  A ASP A 1 60  ? 3.016   -0.741 -25.582 0.50 27.99 ? 60  ASP A CG  1 
ATOM   558  C CG  B ASP A 1 60  ? 3.200   -1.229 -26.249 0.50 35.22 ? 60  ASP A CG  1 
ATOM   559  O OD1 A ASP A 1 60  ? 2.892   0.463  -25.902 0.50 32.59 ? 60  ASP A OD1 1 
ATOM   560  O OD1 B ASP A 1 60  ? 3.120   -0.021 -26.558 0.50 39.28 ? 60  ASP A OD1 1 
ATOM   561  O OD2 A ASP A 1 60  ? 4.035   -1.428 -25.814 0.50 32.97 ? 60  ASP A OD2 1 
ATOM   562  O OD2 B ASP A 1 60  ? 3.858   -2.072 -26.890 0.50 35.43 ? 60  ASP A OD2 1 
ATOM   563  N N   A SER A 1 61  ? 1.011   -1.902 -21.434 0.50 19.14 ? 61  SER A N   1 
ATOM   564  N N   B SER A 1 61  ? 1.764   -1.837 -21.880 0.50 23.07 ? 61  SER A N   1 
ATOM   565  C CA  A SER A 1 61  ? 0.130   -2.578 -20.445 0.50 19.89 ? 61  SER A CA  1 
ATOM   566  C CA  B SER A 1 61  ? 0.994   -2.558 -20.830 0.50 24.01 ? 61  SER A CA  1 
ATOM   567  C C   A SER A 1 61  ? -0.350  -1.597 -19.366 0.50 18.32 ? 61  SER A C   1 
ATOM   568  C C   B SER A 1 61  ? 0.487   -1.606 -19.734 0.50 20.58 ? 61  SER A C   1 
ATOM   569  O O   A SER A 1 61  ? -1.120  -2.046 -18.494 0.50 21.15 ? 61  SER A O   1 
ATOM   570  O O   B SER A 1 61  ? -0.316  -2.070 -18.901 0.50 22.61 ? 61  SER A O   1 
ATOM   571  C CB  A SER A 1 61  ? 0.832   -3.751 -19.819 0.50 21.72 ? 61  SER A CB  1 
ATOM   572  C CB  B SER A 1 61  ? 1.821   -3.663 -20.223 0.50 24.70 ? 61  SER A CB  1 
ATOM   573  O OG  A SER A 1 61  ? 1.696   -3.325 -18.778 0.50 25.64 ? 61  SER A OG  1 
ATOM   574  O OG  B SER A 1 61  ? 2.559   -3.206 -19.098 0.50 26.58 ? 61  SER A OG  1 
ATOM   575  N N   A GLY A 1 62  ? 0.060   -0.322 -19.417 0.55 16.19 ? 62  GLY A N   1 
ATOM   576  N N   B GLY A 1 62  ? 0.926   -0.331 -19.726 0.45 16.70 ? 62  GLY A N   1 
ATOM   577  C CA  A GLY A 1 62  ? -0.284  0.661  -18.376 0.55 14.56 ? 62  GLY A CA  1 
ATOM   578  C CA  B GLY A 1 62  ? 0.503   0.716  -18.762 0.45 15.08 ? 62  GLY A CA  1 
ATOM   579  C C   A GLY A 1 62  ? 0.551   0.497  -17.120 0.55 12.67 ? 62  GLY A C   1 
ATOM   580  C C   B GLY A 1 62  ? 1.391   0.786  -17.527 0.45 13.34 ? 62  GLY A C   1 
ATOM   581  O O   A GLY A 1 62  ? 0.069   0.896  -16.068 0.55 12.82 ? 62  GLY A O   1 
ATOM   582  O O   B GLY A 1 62  ? 0.912   1.238  -16.467 0.45 13.18 ? 62  GLY A O   1 
ATOM   583  N N   A SER A 1 63  ? 1.773   -0.032 -17.219 0.55 11.69 ? 63  SER A N   1 
ATOM   584  N N   B SER A 1 63  ? 2.651   0.376  -17.644 0.45 13.68 ? 63  SER A N   1 
ATOM   585  C CA  A SER A 1 63  ? 2.732   -0.084 -16.087 0.55 11.40 ? 63  SER A CA  1 
ATOM   586  C CA  B SER A 1 63  ? 3.610   0.276  -16.517 0.45 14.36 ? 63  SER A CA  1 
ATOM   587  C C   A SER A 1 63  ? 3.890   0.867  -16.368 0.55 9.66  ? 63  SER A C   1 
ATOM   588  C C   B SER A 1 63  ? 4.767   1.242  -16.763 0.45 12.73 ? 63  SER A C   1 
ATOM   589  O O   A SER A 1 63  ? 4.344   0.951  -17.515 0.55 11.41 ? 63  SER A O   1 
ATOM   590  O O   B SER A 1 63  ? 5.234   1.340  -17.910 0.45 13.72 ? 63  SER A O   1 
ATOM   591  C CB  A SER A 1 63  ? 3.234   -1.472 -15.843 0.55 14.21 ? 63  SER A CB  1 
ATOM   592  C CB  B SER A 1 63  ? 4.094   -1.141 -16.353 0.45 17.08 ? 63  SER A CB  1 
ATOM   593  O OG  A SER A 1 63  ? 2.186   -2.303 -15.369 0.55 18.66 ? 63  SER A OG  1 
ATOM   594  O OG  B SER A 1 63  ? 3.026   -2.010 -16.012 0.45 21.18 ? 63  SER A OG  1 
ATOM   595  N N   A GLY A 1 64  ? 4.360   1.576  -15.351 0.55 8.58  ? 64  GLY A N   1 
ATOM   596  N N   B GLY A 1 64  ? 5.217   1.932  -15.725 0.45 11.75 ? 64  GLY A N   1 
ATOM   597  C CA  A GLY A 1 64  ? 5.458   2.518  -15.579 0.55 8.50  ? 64  GLY A CA  1 
ATOM   598  C CA  B GLY A 1 64  ? 6.309   2.903  -15.882 0.45 11.86 ? 64  GLY A CA  1 
ATOM   599  C C   A GLY A 1 64  ? 5.816   3.280  -14.329 0.55 7.57  ? 64  GLY A C   1 
ATOM   600  C C   B GLY A 1 64  ? 6.569   3.667  -14.606 0.45 10.66 ? 64  GLY A C   1 
ATOM   601  O O   A GLY A 1 64  ? 5.881   2.681  -13.249 0.55 8.58  ? 64  GLY A O   1 
ATOM   602  O O   B GLY A 1 64  ? 6.584   3.065  -13.518 0.45 11.17 ? 64  GLY A O   1 
ATOM   603  N N   A ILE A 1 65  ? 6.067   4.570  -14.492 0.55 7.27  ? 65  ILE A N   1 
ATOM   604  N N   B ILE A 1 65  ? 6.751   4.969  -14.740 0.45 9.36  ? 65  ILE A N   1 
ATOM   605  C CA  A ILE A 1 65  ? 6.621   5.437  -13.425 0.55 6.91  ? 65  ILE A CA  1 
ATOM   606  C CA  B ILE A 1 65  ? 7.056   5.821  -13.570 0.45 9.20  ? 65  ILE A CA  1 
ATOM   607  C C   A ILE A 1 65  ? 6.135   6.865  -13.647 0.55 6.37  ? 65  ILE A C   1 
ATOM   608  C C   B ILE A 1 65  ? 6.735   7.269  -13.904 0.45 8.77  ? 65  ILE A C   1 
ATOM   609  O O   A ILE A 1 65  ? 5.991   7.283  -14.792 0.55 7.44  ? 65  ILE A O   1 
ATOM   610  O O   B ILE A 1 65  ? 6.900   7.696  -15.053 0.45 9.74  ? 65  ILE A O   1 
ATOM   611  C CB  A ILE A 1 65  ? 8.158   5.354  -13.395 0.55 7.92  ? 65  ILE A CB  1 
ATOM   612  C CB  B ILE A 1 65  ? 8.517   5.670  -13.132 0.45 9.53  ? 65  ILE A CB  1 
ATOM   613  C CG1 A ILE A 1 65  ? 8.733   6.109  -12.197 0.55 9.21  ? 65  ILE A CG1 1 
ATOM   614  C CG1 B ILE A 1 65  ? 8.703   6.335  -11.771 0.45 12.18 ? 65  ILE A CG1 1 
ATOM   615  C CG2 A ILE A 1 65  ? 8.776   5.807  -14.711 0.55 8.54  ? 65  ILE A CG2 1 
ATOM   616  C CG2 B ILE A 1 65  ? 9.468   6.212  -14.187 0.45 10.34 ? 65  ILE A CG2 1 
ATOM   617  C CD1 A ILE A 1 65  ? 10.195  5.898  -11.971 0.55 10.80 ? 65  ILE A CD1 1 
ATOM   618  C CD1 B ILE A 1 65  ? 9.869   5.821  -11.007 0.45 13.83 ? 65  ILE A CD1 1 
ATOM   619  N N   A CYS A 1 66  ? 5.952   7.597  -12.557 0.55 7.20  ? 66  CYS A N   1 
ATOM   620  N N   B CYS A 1 66  ? 6.312   7.998  -12.879 0.45 9.11  ? 66  CYS A N   1 
ATOM   621  C CA  A CYS A 1 66  ? 5.759   9.065  -12.584 0.55 7.46  ? 66  CYS A CA  1 
ATOM   622  C CA  B CYS A 1 66  ? 6.116   9.460  -12.924 0.45 9.12  ? 66  CYS A CA  1 
ATOM   623  C C   A CYS A 1 66  ? 6.689   9.710  -11.568 0.55 6.77  ? 66  CYS A C   1 
ATOM   624  C C   B CYS A 1 66  ? 7.058   10.136 -11.943 0.45 8.69  ? 66  CYS A C   1 
ATOM   625  O O   A CYS A 1 66  ? 6.978   9.083  -10.533 0.55 7.64  ? 66  CYS A O   1 
ATOM   626  O O   B CYS A 1 66  ? 7.217   9.629  -10.824 0.45 9.37  ? 66  CYS A O   1 
ATOM   627  C CB  A CYS A 1 66  ? 4.342   9.467  -12.222 0.55 9.11  ? 66  CYS A CB  1 
ATOM   628  C CB  B CYS A 1 66  ? 4.693   9.836  -12.551 0.45 9.87  ? 66  CYS A CB  1 
ATOM   629  S SG  A CYS A 1 66  ? 3.150   8.803  -13.405 0.55 10.08 ? 66  CYS A SG  1 
ATOM   630  S SG  B CYS A 1 66  ? 3.502   9.118  -13.698 0.45 13.15 ? 66  CYS A SG  1 
ATOM   631  N N   A LYS A 1 67  ? 7.071   10.959 -11.809 0.55 6.40  ? 67  LYS A N   1 
ATOM   632  N N   B LYS A 1 67  ? 7.605   11.270 -12.347 0.45 9.63  ? 67  LYS A N   1 
ATOM   633  C CA  A LYS A 1 67  ? 7.950   11.688 -10.847 0.55 6.58  ? 67  LYS A CA  1 
ATOM   634  C CA  B LYS A 1 67  ? 8.493   12.057 -11.470 0.45 10.78 ? 67  LYS A CA  1 
ATOM   635  C C   A LYS A 1 67  ? 7.158   12.293 -9.697  0.55 5.86  ? 67  LYS A C   1 
ATOM   636  C C   B LYS A 1 67  ? 7.756   12.560 -10.230 0.45 10.36 ? 67  LYS A C   1 
ATOM   637  O O   A LYS A 1 67  ? 7.750   12.488 -8.623  0.55 6.30  ? 67  LYS A O   1 
ATOM   638  O O   B LYS A 1 67  ? 8.402   12.654 -9.181  0.45 12.14 ? 67  LYS A O   1 
ATOM   639  C CB  A LYS A 1 67  ? 8.803   12.768 -11.511 0.55 6.89  ? 67  LYS A CB  1 
ATOM   640  C CB  B LYS A 1 67  ? 9.089   13.221 -12.242 0.45 14.73 ? 67  LYS A CB  1 
ATOM   641  C CG  A LYS A 1 67  ? 9.818   12.213 -12.487 0.55 7.49  ? 67  LYS A CG  1 
ATOM   642  C CG  B LYS A 1 67  ? 10.471  12.907 -12.754 0.45 15.18 ? 67  LYS A CG  1 
ATOM   643  C CD  A LYS A 1 67  ? 10.859  13.225 -12.913 0.55 8.29  ? 67  LYS A CD  1 
ATOM   644  C CD  B LYS A 1 67  ? 11.210  14.111 -13.191 0.45 14.59 ? 67  LYS A CD  1 
ATOM   645  C CE  A LYS A 1 67  ? 11.878  12.631 -13.853 0.55 9.13  ? 67  LYS A CE  1 
ATOM   646  C CE  B LYS A 1 67  ? 12.260  13.672 -14.176 0.45 15.00 ? 67  LYS A CE  1 
ATOM   647  N NZ  A LYS A 1 67  ? 12.950  13.585 -14.230 0.55 9.66  ? 67  LYS A NZ  1 
ATOM   648  N NZ  B LYS A 1 67  ? 13.097  14.801 -14.630 0.45 13.84 ? 67  LYS A NZ  1 
ATOM   649  N N   A THR A 1 68  ? 5.892   12.618 -9.899  0.55 5.77  ? 68  THR A N   1 
ATOM   650  N N   B THR A 1 68  ? 6.478   12.939 -10.348 0.45 9.43  ? 68  THR A N   1 
ATOM   651  C CA  A THR A 1 68  ? 4.995   13.026 -8.812  0.55 5.72  ? 68  THR A CA  1 
ATOM   652  C CA  B THR A 1 68  ? 5.632   13.291 -9.170  0.45 8.87  ? 68  THR A CA  1 
ATOM   653  C C   A THR A 1 68  ? 3.705   12.216 -8.914  0.55 5.58  ? 68  THR A C   1 
ATOM   654  C C   B THR A 1 68  ? 4.331   12.494 -9.196  0.45 7.62  ? 68  THR A C   1 
ATOM   655  O O   A THR A 1 68  ? 3.201   11.997 -10.028 0.55 6.15  ? 68  THR A O   1 
ATOM   656  O O   B THR A 1 68  ? 3.784   12.275 -10.283 0.45 8.10  ? 68  THR A O   1 
ATOM   657  C CB  A THR A 1 68  ? 4.714   14.533 -8.770  0.55 6.02  ? 68  THR A CB  1 
ATOM   658  C CB  B THR A 1 68  ? 5.356   14.798 -9.043  0.45 9.59  ? 68  THR A CB  1 
ATOM   659  O OG1 A THR A 1 68  ? 3.909   14.925 -9.892  0.55 6.17  ? 68  THR A OG1 1 
ATOM   660  O OG1 B THR A 1 68  ? 4.484   15.227 -10.096 0.45 9.25  ? 68  THR A OG1 1 
ATOM   661  C CG2 A THR A 1 68  ? 5.973   15.366 -8.700  0.55 6.55  ? 68  THR A CG2 1 
ATOM   662  C CG2 B THR A 1 68  ? 6.629   15.617 -9.054  0.45 10.61 ? 68  THR A CG2 1 
ATOM   663  N N   A GLY A 1 69  ? 3.170   11.801 -7.776  0.55 5.93  ? 69  GLY A N   1 
ATOM   664  N N   B GLY A 1 69  ? 3.867   12.074 -8.026  0.45 7.71  ? 69  GLY A N   1 
ATOM   665  C CA  A GLY A 1 69  ? 1.845   11.168 -7.691  0.55 6.42  ? 69  GLY A CA  1 
ATOM   666  C CA  B GLY A 1 69  ? 2.528   11.481 -7.850  0.45 6.84  ? 69  GLY A CA  1 
ATOM   667  C C   A GLY A 1 69  ? 1.778   9.729  -8.198  0.55 6.27  ? 69  GLY A C   1 
ATOM   668  C C   B GLY A 1 69  ? 2.428   10.060 -8.366  0.45 6.43  ? 69  GLY A C   1 
ATOM   669  O O   A GLY A 1 69  ? 0.653   9.225  -8.335  0.55 6.61  ? 69  GLY A O   1 
ATOM   670  O O   B GLY A 1 69  ? 1.290   9.575  -8.489  0.45 6.90  ? 69  GLY A O   1 
ATOM   671  N N   A ASP A 1 70  ? 2.905   9.052  -8.370  0.55 6.64  ? 70  ASP A N   1 
ATOM   672  N N   B ASP A 1 70  ? 3.542   9.368  -8.583  0.45 7.49  ? 70  ASP A N   1 
ATOM   673  C CA  A ASP A 1 70  ? 2.909   7.650  -8.852  0.55 7.41  ? 70  ASP A CA  1 
ATOM   674  C CA  B ASP A 1 70  ? 3.467   7.993  -9.116  0.45 7.87  ? 70  ASP A CA  1 
ATOM   675  C C   A ASP A 1 70  ? 2.055   6.802  -7.908  0.55 7.65  ? 70  ASP A C   1 
ATOM   676  C C   B ASP A 1 70  ? 2.657   7.108  -8.178  0.45 7.42  ? 70  ASP A C   1 
ATOM   677  O O   A ASP A 1 70  ? 2.257   6.875  -6.684  0.55 8.31  ? 70  ASP A O   1 
ATOM   678  O O   B ASP A 1 70  ? 2.833   7.201  -6.944  0.45 8.34  ? 70  ASP A O   1 
ATOM   679  C CB  A ASP A 1 70  ? 4.359   7.178  -8.935  0.55 8.68  ? 70  ASP A CB  1 
ATOM   680  C CB  B ASP A 1 70  ? 4.822   7.355  -9.285  0.45 9.09  ? 70  ASP A CB  1 
ATOM   681  C CG  A ASP A 1 70  ? 4.727   6.005  -9.841  0.55 11.68 ? 70  ASP A CG  1 
ATOM   682  C CG  B ASP A 1 70  ? 4.721   5.973  -9.911  0.45 10.06 ? 70  ASP A CG  1 
ATOM   683  O OD1 A ASP A 1 70  ? 4.636   6.091  -11.129 0.55 11.83 ? 70  ASP A OD1 1 
ATOM   684  O OD1 B ASP A 1 70  ? 3.617   5.375  -10.263 0.45 11.33 ? 70  ASP A OD1 1 
ATOM   685  O OD2 A ASP A 1 70  ? 5.230   5.055  -9.263  0.55 13.34 ? 70  ASP A OD2 1 
ATOM   686  O OD2 B ASP A 1 70  ? 5.742   5.540  -10.104 0.45 8.12  ? 70  ASP A OD2 1 
ATOM   687  N N   A CYS A 1 71  ? 1.159   5.987  -8.455  0.55 8.45  ? 71  CYS A N   1 
ATOM   688  N N   B CYS A 1 71  ? 1.844   6.226  -8.753  0.45 8.27  ? 71  CYS A N   1 
ATOM   689  C CA  A CYS A 1 71  ? 0.284   5.075  -7.683  0.55 9.62  ? 71  CYS A CA  1 
ATOM   690  C CA  B CYS A 1 71  ? 0.982   5.292  -7.990  0.45 9.21  ? 71  CYS A CA  1 
ATOM   691  C C   A CYS A 1 71  ? 0.692   3.634  -7.988  0.55 10.12 ? 71  CYS A C   1 
ATOM   692  C C   B CYS A 1 71  ? 1.415   3.859  -8.313  0.45 10.06 ? 71  CYS A C   1 
ATOM   693  O O   A CYS A 1 71  ? 0.027   2.941  -8.784  0.55 11.87 ? 71  CYS A O   1 
ATOM   694  O O   B CYS A 1 71  ? 0.747   3.178  -9.109  0.45 11.10 ? 71  CYS A O   1 
ATOM   695  C CB  A CYS A 1 71  ? -1.181  5.312  -8.015  0.55 10.15 ? 71  CYS A CB  1 
ATOM   696  C CB  B CYS A 1 71  ? -0.483  5.516  -8.336  0.45 9.90  ? 71  CYS A CB  1 
ATOM   697  S SG  A CYS A 1 71  ? -1.554  5.028  -9.761  0.55 10.47 ? 71  CYS A SG  1 
ATOM   698  S SG  B CYS A 1 71  ? -0.851  5.237  -10.087 0.45 10.29 ? 71  CYS A SG  1 
ATOM   699  N N   A GLY A 1 72  ? 1.804   3.200  -7.413  0.55 10.59 ? 72  GLY A N   1 
ATOM   700  N N   B GLY A 1 72  ? 2.546   3.441  -7.764  0.45 10.91 ? 72  GLY A N   1 
ATOM   701  C CA  A GLY A 1 72  ? 2.273   1.815  -7.585  0.55 11.44 ? 72  GLY A CA  1 
ATOM   702  C CA  B GLY A 1 72  ? 3.032   2.066  -7.951  0.45 11.34 ? 72  GLY A CA  1 
ATOM   703  C C   A GLY A 1 72  ? 2.618   1.493  -9.023  0.55 10.26 ? 72  GLY A C   1 
ATOM   704  C C   B GLY A 1 72  ? 3.310   1.773  -9.413  0.45 10.77 ? 72  GLY A C   1 
ATOM   705  O O   A GLY A 1 72  ? 2.531   0.317  -9.418  0.55 12.34 ? 72  GLY A O   1 
ATOM   706  O O   B GLY A 1 72  ? 3.136   0.613  -9.826  0.45 11.97 ? 72  GLY A O   1 
ATOM   707  N N   A GLY A 1 73  ? 2.989   2.499  -9.806  0.55 9.38  ? 73  GLY A N   1 
ATOM   708  N N   B GLY A 1 73  ? 3.737   2.786  -10.169 0.45 10.23 ? 73  GLY A N   1 
ATOM   709  C CA  A GLY A 1 73  ? 3.462   2.295  -11.183 0.55 9.53  ? 73  GLY A CA  1 
ATOM   710  C CA  B GLY A 1 73  ? 4.213   2.645  -11.555 0.45 10.88 ? 73  GLY A CA  1 
ATOM   711  C C   A GLY A 1 73  ? 2.333   2.006  -12.158 0.55 9.47  ? 73  GLY A C   1 
ATOM   712  C C   B GLY A 1 73  ? 3.097   2.355  -12.545 0.45 11.04 ? 73  GLY A C   1 
ATOM   713  O O   A GLY A 1 73  ? 2.636   1.563  -13.263 0.55 12.17 ? 73  GLY A O   1 
ATOM   714  O O   B GLY A 1 73  ? 3.426   1.899  -13.654 0.45 14.32 ? 73  GLY A O   1 
ATOM   715  N N   A LEU A 1 74  ? 1.075   2.276  -11.810 0.55 9.27  ? 74  LEU A N   1 
ATOM   716  N N   B LEU A 1 74  ? 1.828   2.606  -12.202 0.45 10.11 ? 74  LEU A N   1 
ATOM   717  C CA  A LEU A 1 74  ? -0.057  1.978  -12.726 0.55 9.53  ? 74  LEU A CA  1 
ATOM   718  C CA  B LEU A 1 74  ? 0.687   2.290  -13.105 0.45 10.78 ? 74  LEU A CA  1 
ATOM   719  C C   A LEU A 1 74  ? -0.553  3.250  -13.412 0.55 9.25  ? 74  LEU A C   1 
ATOM   720  C C   B LEU A 1 74  ? 0.155   3.561  -13.770 0.45 9.49  ? 74  LEU A C   1 
ATOM   721  O O   A LEU A 1 74  ? -0.702  4.283  -12.755 0.55 9.91  ? 74  LEU A O   1 
ATOM   722  O O   B LEU A 1 74  ? 0.004   4.587  -13.092 0.45 9.62  ? 74  LEU A O   1 
ATOM   723  C CB  A LEU A 1 74  ? -1.211  1.334  -11.968 0.55 11.09 ? 74  LEU A CB  1 
ATOM   724  C CB  B LEU A 1 74  ? -0.451  1.620  -12.331 0.45 11.35 ? 74  LEU A CB  1 
ATOM   725  C CG  A LEU A 1 74  ? -0.886  0.025  -11.260 0.55 13.37 ? 74  LEU A CG  1 
ATOM   726  C CG  B LEU A 1 74  ? -0.112  0.288  -11.674 0.45 13.45 ? 74  LEU A CG  1 
ATOM   727  C CD1 A LEU A 1 74  ? -2.144  -0.555 -10.646 0.55 15.23 ? 74  LEU A CD1 1 
ATOM   728  C CD1 B LEU A 1 74  ? -1.346  -0.325 -11.030 0.45 14.46 ? 74  LEU A CD1 1 
ATOM   729  C CD2 A LEU A 1 74  ? -0.242  -0.975 -12.211 0.55 15.22 ? 74  LEU A CD2 1 
ATOM   730  C CD2 B LEU A 1 74  ? 0.501   -0.675 -12.678 0.45 14.02 ? 74  LEU A CD2 1 
ATOM   731  N N   A LEU A 1 75  ? -0.883  3.162  -14.699 0.55 9.45  ? 75  LEU A N   1 
ATOM   732  N N   B LEU A 1 75  ? -0.204  3.473  -15.043 0.45 9.59  ? 75  LEU A N   1 
ATOM   733  C CA  A LEU A 1 75  ? -1.623  4.266  -15.370 0.55 9.31  ? 75  LEU A CA  1 
ATOM   734  C CA  B LEU A 1 75  ? -1.001  4.531  -15.697 0.45 9.66  ? 75  LEU A CA  1 
ATOM   735  C C   A LEU A 1 75  ? -3.002  4.422  -14.709 0.55 10.15 ? 75  LEU A C   1 
ATOM   736  C C   B LEU A 1 75  ? -2.365  4.599  -15.002 0.45 9.48  ? 75  LEU A C   1 
ATOM   737  O O   A LEU A 1 75  ? -3.424  5.553  -14.448 0.55 10.47 ? 75  LEU A O   1 
ATOM   738  O O   B LEU A 1 75  ? -2.773  5.719  -14.646 0.45 10.17 ? 75  LEU A O   1 
ATOM   739  C CB  A LEU A 1 75  ? -1.764  3.958  -16.863 0.55 10.54 ? 75  LEU A CB  1 
ATOM   740  C CB  B LEU A 1 75  ? -1.129  4.208  -17.185 0.45 10.62 ? 75  LEU A CB  1 
ATOM   741  C CG  A LEU A 1 75  ? -2.691  4.891  -17.638 0.55 11.86 ? 75  LEU A CG  1 
ATOM   742  C CG  B LEU A 1 75  ? -2.074  5.105  -17.984 0.45 11.79 ? 75  LEU A CG  1 
ATOM   743  C CD1 A LEU A 1 75  ? -2.184  6.322  -17.651 0.55 10.77 ? 75  LEU A CD1 1 
ATOM   744  C CD1 B LEU A 1 75  ? -1.635  6.559  -17.928 0.45 12.25 ? 75  LEU A CD1 1 
ATOM   745  C CD2 A LEU A 1 75  ? -2.892  4.382  -19.058 0.55 13.86 ? 75  LEU A CD2 1 
ATOM   746  C CD2 B LEU A 1 75  ? -2.167  4.626  -19.434 0.45 13.27 ? 75  LEU A CD2 1 
ATOM   747  N N   A ARG A 1 76  ? -3.701  3.299  -14.470 0.52 10.64 ? 76  ARG A N   1 
ATOM   748  N N   B ARG A 1 76  ? -3.044  3.453  -14.796 0.48 10.55 ? 76  ARG A N   1 
ATOM   749  C CA  A ARG A 1 76  ? -5.080  3.269  -13.918 0.52 11.99 ? 76  ARG A CA  1 
ATOM   750  C CA  B ARG A 1 76  ? -4.405  3.389  -14.210 0.48 10.81 ? 76  ARG A CA  1 
ATOM   751  C C   A ARG A 1 76  ? -4.975  3.077  -12.409 0.52 11.48 ? 76  ARG A C   1 
ATOM   752  C C   B ARG A 1 76  ? -4.253  3.165  -12.713 0.48 10.63 ? 76  ARG A C   1 
ATOM   753  O O   A ARG A 1 76  ? -4.871  1.932  -11.965 0.52 13.53 ? 76  ARG A O   1 
ATOM   754  O O   B ARG A 1 76  ? -4.131  2.021  -12.281 0.48 12.79 ? 76  ARG A O   1 
ATOM   755  C CB  A ARG A 1 76  ? -5.864  2.193  -14.661 0.52 13.96 ? 76  ARG A CB  1 
ATOM   756  C CB  B ARG A 1 76  ? -5.207  2.298  -14.909 0.48 12.59 ? 76  ARG A CB  1 
ATOM   757  C CG  A ARG A 1 76  ? -6.123  2.620  -16.094 0.52 15.91 ? 76  ARG A CG  1 
ATOM   758  C CG  B ARG A 1 76  ? -5.386  2.561  -16.394 0.48 16.06 ? 76  ARG A CG  1 
ATOM   759  C CD  A ARG A 1 76  ? -6.813  1.522  -16.850 0.52 19.39 ? 76  ARG A CD  1 
ATOM   760  C CD  B ARG A 1 76  ? -6.781  3.003  -16.782 0.48 20.89 ? 76  ARG A CD  1 
ATOM   761  N NE  A ARG A 1 76  ? -5.910  0.424  -17.174 0.52 24.93 ? 76  ARG A NE  1 
ATOM   762  N NE  B ARG A 1 76  ? -7.697  1.879  -16.910 0.48 25.68 ? 76  ARG A NE  1 
ATOM   763  C CZ  A ARG A 1 76  ? -6.285  -0.830 -17.426 0.52 28.94 ? 76  ARG A CZ  1 
ATOM   764  C CZ  B ARG A 1 76  ? -8.489  1.665  -17.958 0.48 28.63 ? 76  ARG A CZ  1 
ATOM   765  N NH1 A ARG A 1 76  ? -7.561  -1.177 -17.379 0.52 32.66 ? 76  ARG A NH1 1 
ATOM   766  N NH1 B ARG A 1 76  ? -8.497  2.518  -18.970 0.48 30.65 ? 76  ARG A NH1 1 
ATOM   767  N NH2 A ARG A 1 76  ? -5.372  -1.742 -17.719 0.52 30.88 ? 76  ARG A NH2 1 
ATOM   768  N NH2 B ARG A 1 76  ? -9.283  0.609  -17.985 0.48 30.82 ? 76  ARG A NH2 1 
ATOM   769  N N   A CYS A 1 77  ? -4.949  4.170  -11.647 0.55 11.73 ? 77  CYS A N   1 
ATOM   770  N N   B CYS A 1 77  ? -4.255  4.247  -11.939 0.45 9.57  ? 77  CYS A N   1 
ATOM   771  C CA  A CYS A 1 77  ? -4.654  4.103  -10.199 0.55 11.47 ? 77  CYS A CA  1 
ATOM   772  C CA  B CYS A 1 77  ? -3.962  4.192  -10.485 0.45 9.99  ? 77  CYS A CA  1 
ATOM   773  C C   A CYS A 1 77  ? -5.752  3.357  -9.457  0.55 13.45 ? 77  CYS A C   1 
ATOM   774  C C   B CYS A 1 77  ? -5.073  3.452  -9.727  0.45 11.18 ? 77  CYS A C   1 
ATOM   775  O O   A CYS A 1 77  ? -6.932  3.635  -9.702  0.55 14.24 ? 77  CYS A O   1 
ATOM   776  O O   B CYS A 1 77  ? -6.251  3.683  -10.013 0.45 13.65 ? 77  CYS A O   1 
ATOM   777  C CB  A CYS A 1 77  ? -4.519  5.493  -9.599  0.55 11.25 ? 77  CYS A CB  1 
ATOM   778  C CB  B CYS A 1 77  ? -3.837  5.582  -9.880  0.45 9.21  ? 77  CYS A CB  1 
ATOM   779  S SG  A CYS A 1 77  ? -3.054  6.373  -10.187 0.55 10.38 ? 77  CYS A SG  1 
ATOM   780  S SG  B CYS A 1 77  ? -2.398  6.518  -10.460 0.45 9.90  ? 77  CYS A SG  1 
ATOM   781  N N   A LYS A 1 78  ? -5.340  2.432  -8.589  0.55 13.09 ? 78  LYS A N   1 
ATOM   782  N N   B LYS A 1 78  ? -4.699  2.603  -8.761  0.45 11.30 ? 78  LYS A N   1 
ATOM   783  C CA  A LYS A 1 78  ? -6.191  1.867  -7.530  0.55 15.50 ? 78  LYS A CA  1 
ATOM   784  C CA  B LYS A 1 78  ? -5.654  1.844  -7.882  0.45 13.67 ? 78  LYS A CA  1 
ATOM   785  C C   A LYS A 1 78  ? -5.757  2.475  -6.198  0.55 16.83 ? 78  LYS A C   1 
ATOM   786  C C   B LYS A 1 78  ? -5.538  2.226  -6.388  0.45 15.30 ? 78  LYS A C   1 
ATOM   787  O O   A LYS A 1 78  ? -6.591  2.439  -5.280  0.55 22.49 ? 78  LYS A O   1 
ATOM   788  O O   B LYS A 1 78  ? -6.285  1.696  -5.526  0.45 16.16 ? 78  LYS A O   1 
ATOM   789  C CB  A LYS A 1 78  ? -6.081  0.341  -7.497  0.55 19.54 ? 78  LYS A CB  1 
ATOM   790  C CB  B LYS A 1 78  ? -5.376  0.334  -7.927  0.45 16.22 ? 78  LYS A CB  1 
ATOM   791  C CG  A LYS A 1 78  ? -6.029  -0.362 -8.847  0.55 22.85 ? 78  LYS A CG  1 
ATOM   792  C CG  B LYS A 1 78  ? -5.345  -0.359 -9.285  0.45 20.10 ? 78  LYS A CG  1 
ATOM   793  C CD  A LYS A 1 78  ? -6.115  -1.871 -8.763  0.55 25.85 ? 78  LYS A CD  1 
ATOM   794  C CD  B LYS A 1 78  ? -4.886  -1.801 -9.135  0.45 23.70 ? 78  LYS A CD  1 
ATOM   795  C CE  A LYS A 1 78  ? -5.131  -2.508 -7.801  0.55 28.93 ? 78  LYS A CE  1 
ATOM   796  C CE  B LYS A 1 78  ? -5.257  -2.714 -10.284 0.45 26.58 ? 78  LYS A CE  1 
ATOM   797  N NZ  A LYS A 1 78  ? -3.741  -2.457 -8.311  0.55 29.18 ? 78  LYS A NZ  1 
ATOM   798  N NZ  B LYS A 1 78  ? -5.088  -4.138 -9.913  0.45 29.85 ? 78  LYS A NZ  1 
ATOM   799  N N   . ARG A 1 79  ? -4.531  3.021  -6.078  1.00 15.62 ? 79  ARG A N   1 
ATOM   800  C CA  . ARG A 1 79  ? -4.070  3.460  -4.746  1.00 15.87 ? 79  ARG A CA  1 
ATOM   801  C C   . ARG A 1 79  ? -3.692  4.932  -4.839  1.00 13.77 ? 79  ARG A C   1 
ATOM   802  O O   . ARG A 1 79  ? -3.554  5.465  -5.946  1.00 14.10 ? 79  ARG A O   1 
ATOM   803  C CB  . ARG A 1 79  ? -2.854  2.638  -4.292  1.00 19.36 ? 79  ARG A CB  1 
ATOM   804  C CG  . ARG A 1 79  ? -3.045  1.129  -4.301  1.00 25.01 ? 79  ARG A CG  1 
ATOM   805  C CD  . ARG A 1 79  ? -3.920  0.659  -3.164  1.00 29.34 ? 79  ARG A CD  1 
ATOM   806  N NE  . ARG A 1 79  ? -4.102  -0.787 -3.175  1.00 34.13 ? 79  ARG A NE  1 
ATOM   807  C CZ  . ARG A 1 79  ? -5.088  -1.438 -3.795  1.00 34.48 ? 79  ARG A CZ  1 
ATOM   808  N NH1 . ARG A 1 79  ? -6.015  -0.779 -4.473  1.00 31.18 ? 79  ARG A NH1 1 
ATOM   809  N NH2 . ARG A 1 79  ? -5.147  -2.756 -3.729  1.00 37.42 ? 79  ARG A NH2 1 
ATOM   810  N N   . PHE A 1 80  ? -3.468  5.547  -3.687  1.00 13.01 ? 80  PHE A N   1 
ATOM   811  C CA  . PHE A 1 80  ? -3.046  6.958  -3.637  1.00 11.83 ? 80  PHE A CA  1 
ATOM   812  C C   . PHE A 1 80  ? -1.603  7.105  -4.131  1.00 11.88 ? 80  PHE A C   1 
ATOM   813  O O   . PHE A 1 80  ? -0.781  6.167  -4.177  1.00 15.68 ? 80  PHE A O   1 
ATOM   814  C CB  . PHE A 1 80  ? -3.248  7.538  -2.241  1.00 12.41 ? 80  PHE A CB  1 
ATOM   815  C CG  . PHE A 1 80  ? -4.689  7.653  -1.812  1.00 12.10 ? 80  PHE A CG  1 
ATOM   816  C CD1 . PHE A 1 80  ? -5.689  8.035  -2.689  1.00 12.43 ? 80  PHE A CD1 1 
ATOM   817  C CD2 . PHE A 1 80  ? -5.051  7.403  -0.501  1.00 13.97 ? 80  PHE A CD2 1 
ATOM   818  C CE1 . PHE A 1 80  ? -7.003  8.158  -2.271  1.00 13.07 ? 80  PHE A CE1 1 
ATOM   819  C CE2 . PHE A 1 80  ? -6.370  7.510  -0.091  1.00 15.14 ? 80  PHE A CE2 1 
ATOM   820  C CZ  . PHE A 1 80  ? -7.339  7.897  -0.975  1.00 14.04 ? 80  PHE A CZ  1 
ATOM   821  N N   . GLY A 1 81  ? -1.294  8.328  -4.523  1.00 11.27 ? 81  GLY A N   1 
ATOM   822  C CA  . GLY A 1 81  ? -0.031  8.667  -5.179  1.00 11.75 ? 81  GLY A CA  1 
ATOM   823  C C   . GLY A 1 81  ? 1.078   9.105  -4.249  1.00 10.31 ? 81  GLY A C   1 
ATOM   824  O O   . GLY A 1 81  ? 0.852   9.586  -3.140  1.00 10.57 ? 81  GLY A O   1 
ATOM   825  N N   . ARG A 1 82  ? 2.290   8.938  -4.741  1.00 10.53 ? 82  ARG A N   1 
ATOM   826  C CA  A ARG A 1 82  ? 3.495   9.300  -3.986  0.67 9.55  ? 82  ARG A CA  1 
ATOM   827  C CA  B ARG A 1 82  ? 3.561   9.315  -4.052  0.33 10.50 ? 82  ARG A CA  1 
ATOM   828  C C   . ARG A 1 82  ? 3.624   10.823 -3.927  1.00 8.80  ? 82  ARG A C   1 
ATOM   829  O O   . ARG A 1 82  ? 3.617   11.510 -4.961  1.00 9.94  ? 82  ARG A O   1 
ATOM   830  C CB  A ARG A 1 82  ? 4.651   8.634  -4.713  0.67 8.79  ? 82  ARG A CB  1 
ATOM   831  C CB  B ARG A 1 82  ? 4.816   9.070  -4.899  0.33 12.15 ? 82  ARG A CB  1 
ATOM   832  C CG  A ARG A 1 82  ? 5.955   8.811  -3.977  0.67 9.04  ? 82  ARG A CG  1 
ATOM   833  C CG  B ARG A 1 82  ? 5.764   7.991  -4.421  0.33 14.45 ? 82  ARG A CG  1 
ATOM   834  C CD  A ARG A 1 82  ? 6.942   8.009  -4.741  0.67 9.50  ? 82  ARG A CD  1 
ATOM   835  C CD  B ARG A 1 82  ? 6.425   8.068  -3.063  0.33 12.44 ? 82  ARG A CD  1 
ATOM   836  N NE  A ARG A 1 82  ? 8.175   7.894  -4.004  0.67 9.98  ? 82  ARG A NE  1 
ATOM   837  N NE  B ARG A 1 82  ? 6.527   6.639  -3.133  0.33 11.28 ? 82  ARG A NE  1 
ATOM   838  C CZ  A ARG A 1 82  ? 9.165   8.798  -3.985  0.67 9.22  ? 82  ARG A CZ  1 
ATOM   839  C CZ  B ARG A 1 82  ? 7.567   5.979  -3.623  0.33 11.70 ? 82  ARG A CZ  1 
ATOM   840  N NH1 A ARG A 1 82  ? 9.046   9.930  -4.661  0.67 8.92  ? 82  ARG A NH1 1 
ATOM   841  N NH1 B ARG A 1 82  ? 8.664   6.616  -3.990  0.33 11.72 ? 82  ARG A NH1 1 
ATOM   842  N NH2 A ARG A 1 82  ? 10.221  8.561  -3.234  0.67 11.03 ? 82  ARG A NH2 1 
ATOM   843  N NH2 B ARG A 1 82  ? 7.519   4.667  -3.718  0.33 13.58 ? 82  ARG A NH2 1 
ATOM   844  N N   . PRO A 1 83  ? 3.809   11.398 -2.730  1.00 8.05  ? 83  PRO A N   1 
ATOM   845  C CA  . PRO A 1 83  ? 4.001   12.841 -2.619  1.00 7.78  ? 83  PRO A CA  1 
ATOM   846  C C   . PRO A 1 83  ? 5.224   13.266 -3.402  1.00 8.06  ? 83  PRO A C   1 
ATOM   847  O O   . PRO A 1 83  ? 6.146   12.474 -3.618  1.00 9.49  ? 83  PRO A O   1 
ATOM   848  C CB  . PRO A 1 83  ? 4.153   13.074 -1.108  1.00 9.34  ? 83  PRO A CB  1 
ATOM   849  C CG  . PRO A 1 83  ? 3.355   11.919 -0.527  1.00 11.48 ? 83  PRO A CG  1 
ATOM   850  C CD  . PRO A 1 83  ? 3.713   10.750 -1.416  1.00 9.81  ? 83  PRO A CD  1 
ATOM   851  N N   . PRO A 1 84  ? 5.286   14.536 -3.840  1.00 7.57  ? 84  PRO A N   1 
ATOM   852  C CA  . PRO A 1 84  ? 4.315   15.595 -3.549  1.00 7.47  ? 84  PRO A CA  1 
ATOM   853  C C   . PRO A 1 84  ? 3.146   15.581 -4.530  1.00 6.85  ? 84  PRO A C   1 
ATOM   854  O O   . PRO A 1 84  ? 3.333   15.462 -5.744  1.00 7.98  ? 84  PRO A O   1 
ATOM   855  C CB  . PRO A 1 84  ? 5.137   16.871 -3.719  1.00 8.68  ? 84  PRO A CB  1 
ATOM   856  C CG  . PRO A 1 84  ? 6.178   16.500 -4.760  1.00 10.03 ? 84  PRO A CG  1 
ATOM   857  C CD  . PRO A 1 84  ? 6.493   15.041 -4.510  1.00 8.92  ? 84  PRO A CD  1 
ATOM   858  N N   . THR A 1 85  ? 1.951   15.771 -3.985  1.00 6.81  ? 85  THR A N   1 
ATOM   859  C CA  . THR A 1 85  ? 0.718   15.782 -4.778  1.00 7.07  ? 85  THR A CA  1 
ATOM   860  C C   . THR A 1 85  ? -0.258  16.793 -4.233  1.00 6.47  ? 85  THR A C   1 
ATOM   861  O O   . THR A 1 85  ? -0.770  16.567 -3.116  1.00 7.42  ? 85  THR A O   1 
ATOM   862  C CB  . THR A 1 85  ? 0.006   14.424 -4.755  1.00 8.05  ? 85  THR A CB  1 
ATOM   863  O OG1 . THR A 1 85  ? -0.169  13.994 -3.400  1.00 8.69  ? 85  THR A OG1 1 
ATOM   864  C CG2 . THR A 1 85  ? 0.748   13.342 -5.505  1.00 9.04  ? 85  THR A CG2 1 
ATOM   865  N N   . THR A 1 86  ? -0.637  17.801 -4.987  1.00 6.20  ? 86  THR A N   1 
ATOM   866  C CA  . THR A 1 86  ? -1.786  18.629 -4.627  1.00 6.05  ? 86  THR A CA  1 
ATOM   867  C C   . THR A 1 86  ? -3.034  17.743 -4.717  1.00 6.22  ? 86  THR A C   1 
ATOM   868  O O   . THR A 1 86  ? -3.181  17.024 -5.718  1.00 7.30  ? 86  THR A O   1 
ATOM   869  C CB  . THR A 1 86  ? -1.937  19.815 -5.582  1.00 6.08  ? 86  THR A CB  1 
ATOM   870  O OG1 . THR A 1 86  ? -0.643  20.310 -5.892  1.00 6.34  ? 86  THR A OG1 1 
ATOM   871  C CG2 . THR A 1 86  ? -2.793  20.903 -4.983  1.00 7.69  ? 86  THR A CG2 1 
ATOM   872  N N   . LEU A 1 87  ? -3.928  17.764 -3.726  1.00 6.11  ? 87  LEU A N   1 
ATOM   873  C CA  . LEU A 1 87  ? -5.044  16.813 -3.707  1.00 6.21  ? 87  LEU A CA  1 
ATOM   874  C C   . LEU A 1 87  ? -6.391  17.516 -3.738  1.00 6.27  ? 87  LEU A C   1 
ATOM   875  O O   . LEU A 1 87  ? -6.684  18.363 -2.883  1.00 6.90  ? 87  LEU A O   1 
ATOM   876  C CB  . LEU A 1 87  ? -4.983  15.950 -2.447  1.00 6.86  ? 87  LEU A CB  1 
ATOM   877  C CG  . LEU A 1 87  ? -3.759  15.055 -2.328  1.00 7.67  ? 87  LEU A CG  1 
ATOM   878  C CD1 . LEU A 1 87  ? -3.675  14.455 -0.925  1.00 8.93  ? 87  LEU A CD1 1 
ATOM   879  C CD2 . LEU A 1 87  ? -3.758  13.967 -3.387  1.00 8.88  ? 87  LEU A CD2 1 
ATOM   880  N N   . ALA A 1 88  ? -7.240  17.096 -4.679  1.00 5.88  ? 88  ALA A N   1 
ATOM   881  C CA  . ALA A 1 88  ? -8.686  17.384 -4.653  1.00 6.25  ? 88  ALA A CA  1 
ATOM   882  C C   . ALA A 1 88  ? -9.348  16.242 -3.901  1.00 6.61  ? 88  ALA A C   1 
ATOM   883  O O   . ALA A 1 88  ? -9.233  15.103 -4.322  1.00 8.81  ? 88  ALA A O   1 
ATOM   884  C CB  . ALA A 1 88  ? -9.234  17.494 -6.062  1.00 7.01  ? 88  ALA A CB  1 
ATOM   885  N N   . GLU A 1 89  ? -10.012 16.541 -2.792  1.00 6.49  ? 89  GLU A N   1 
ATOM   886  C CA  . GLU A 1 89  ? -10.532 15.507 -1.883  1.00 6.90  ? 89  GLU A CA  1 
ATOM   887  C C   . GLU A 1 89  ? -12.035 15.648 -1.754  1.00 6.93  ? 89  GLU A C   1 
ATOM   888  O O   . GLU A 1 89  ? -12.556 16.762 -1.649  1.00 7.28  ? 89  GLU A O   1 
ATOM   889  C CB  . GLU A 1 89  ? -9.897  15.666 -0.499  1.00 7.47  ? 89  GLU A CB  1 
ATOM   890  C CG  . GLU A 1 89  ? -8.386  15.621 -0.543  1.00 7.95  ? 89  GLU A CG  1 
ATOM   891  C CD  . GLU A 1 89  ? -7.757  15.633 0.832   1.00 8.41  ? 89  GLU A CD  1 
ATOM   892  O OE1 . GLU A 1 89  ? -8.172  16.489 1.660   1.00 9.30  ? 89  GLU A OE1 1 
ATOM   893  O OE2 . GLU A 1 89  ? -6.878  14.795 1.096   1.00 10.31 ? 89  GLU A OE2 1 
ATOM   894  N N   . PHE A 1 90  ? -12.739 14.526 -1.715  1.00 7.35  ? 90  PHE A N   1 
ATOM   895  C CA  . PHE A 1 90  ? -14.208 14.590 -1.685  1.00 8.02  ? 90  PHE A CA  1 
ATOM   896  C C   . PHE A 1 90  ? -14.788 13.339 -1.040  1.00 8.15  ? 90  PHE A C   1 
ATOM   897  O O   . PHE A 1 90  ? -14.283 12.228 -1.177  1.00 9.24  ? 90  PHE A O   1 
ATOM   898  C CB  . PHE A 1 90  ? -14.773 14.771 -3.103  1.00 7.95  ? 90  PHE A CB  1 
ATOM   899  C CG  . PHE A 1 90  ? -14.177 13.842 -4.134  1.00 8.14  ? 90  PHE A CG  1 
ATOM   900  C CD1 . PHE A 1 90  ? -13.012 14.208 -4.793  1.00 8.34  ? 90  PHE A CD1 1 
ATOM   901  C CD2 . PHE A 1 90  ? -14.730 12.608 -4.430  1.00 9.11  ? 90  PHE A CD2 1 
ATOM   902  C CE1 . PHE A 1 90  ? -12.402 13.359 -5.703  1.00 9.18  ? 90  PHE A CE1 1 
ATOM   903  C CE2 . PHE A 1 90  ? -14.136 11.767 -5.362  1.00 9.83  ? 90  PHE A CE2 1 
ATOM   904  C CZ  . PHE A 1 90  ? -12.972 12.148 -5.981  1.00 10.00 ? 90  PHE A CZ  1 
ATOM   905  N N   . SER A 1 91  ? -15.912 13.568 -0.371  1.00 8.21  ? 91  SER A N   1 
ATOM   906  C CA  . SER A 1 91  ? -16.785 12.498 0.120   1.00 9.10  ? 91  SER A CA  1 
ATOM   907  C C   . SER A 1 91  ? -18.195 12.861 -0.293  1.00 9.00  ? 91  SER A C   1 
ATOM   908  O O   . SER A 1 91  ? -18.644 13.982 -0.025  1.00 10.26 ? 91  SER A O   1 
ATOM   909  C CB  . SER A 1 91  ? -16.669 12.324 1.617   1.00 10.95 ? 91  SER A CB  1 
ATOM   910  O OG  . SER A 1 91  ? -15.354 11.923 1.959   1.00 12.38 ? 91  SER A OG  1 
ATOM   911  N N   A LEU A 1 92  ? -18.938 11.979 -0.955  0.51 8.85  ? 92  LEU A N   1 
ATOM   912  N N   B LEU A 1 92  ? -18.798 11.899 -0.986  0.49 8.72  ? 92  LEU A N   1 
ATOM   913  C CA  A LEU A 1 92  ? -20.225 12.381 -1.586  0.51 8.23  ? 92  LEU A CA  1 
ATOM   914  C CA  B LEU A 1 92  ? -20.084 12.062 -1.691  0.49 7.97  ? 92  LEU A CA  1 
ATOM   915  C C   A LEU A 1 92  ? -21.409 11.732 -0.880  0.51 8.16  ? 92  LEU A C   1 
ATOM   916  C C   B LEU A 1 92  ? -21.179 11.319 -0.940  0.49 7.67  ? 92  LEU A C   1 
ATOM   917  O O   A LEU A 1 92  ? -21.263 10.612 -0.375  0.51 8.48  ? 92  LEU A O   1 
ATOM   918  O O   B LEU A 1 92  ? -20.970 10.176 -0.492  0.49 8.19  ? 92  LEU A O   1 
ATOM   919  C CB  A LEU A 1 92  ? -20.213 11.958 -3.055  0.51 7.98  ? 92  LEU A CB  1 
ATOM   920  C CB  B LEU A 1 92  ? -19.984 11.523 -3.118  0.49 7.60  ? 92  LEU A CB  1 
ATOM   921  C CG  A LEU A 1 92  ? -18.985 12.408 -3.845  0.51 8.22  ? 92  LEU A CG  1 
ATOM   922  C CG  B LEU A 1 92  ? -18.766 11.977 -3.918  0.49 7.65  ? 92  LEU A CG  1 
ATOM   923  C CD1 A LEU A 1 92  ? -19.062 11.881 -5.266  0.51 8.87  ? 92  LEU A CD1 1 
ATOM   924  C CD1 B LEU A 1 92  ? -18.864 11.454 -5.342  0.49 8.77  ? 92  LEU A CD1 1 
ATOM   925  C CD2 A LEU A 1 92  ? -18.845 13.929 -3.849  0.51 8.32  ? 92  LEU A CD2 1 
ATOM   926  C CD2 B LEU A 1 92  ? -18.620 13.494 -3.923  0.49 7.51  ? 92  LEU A CD2 1 
ATOM   927  N N   A ASN A 1 93  ? -22.563 12.386 -0.856  0.51 8.54  ? 93  ASN A N   1 
ATOM   928  N N   B ASN A 1 93  ? -22.335 11.960 -0.869  0.49 7.77  ? 93  ASN A N   1 
ATOM   929  C CA  A ASN A 1 93  ? -23.773 11.688 -0.357  0.51 10.23 ? 93  ASN A CA  1 
ATOM   930  C CA  B ASN A 1 93  ? -23.566 11.404 -0.251  0.49 8.37  ? 93  ASN A CA  1 
ATOM   931  C C   A ASN A 1 93  ? -23.580 11.299 1.113   0.51 9.91  ? 93  ASN A C   1 
ATOM   932  C C   B ASN A 1 93  ? -23.216 10.833 1.129   0.49 7.51  ? 93  ASN A C   1 
ATOM   933  O O   A ASN A 1 93  ? -23.919 10.167 1.494   0.51 11.47 ? 93  ASN A O   1 
ATOM   934  O O   B ASN A 1 93  ? -23.421 9.648  1.440   0.49 7.77  ? 93  ASN A O   1 
ATOM   935  C CB  A ASN A 1 93  ? -24.061 10.397 -1.145  0.51 9.94  ? 93  ASN A CB  1 
ATOM   936  C CB  B ASN A 1 93  ? -24.347 10.478 -1.196  0.49 9.29  ? 93  ASN A CB  1 
ATOM   937  C CG  A ASN A 1 93  ? -24.115 10.668 -2.632  0.51 8.19  ? 93  ASN A CG  1 
ATOM   938  C CG  B ASN A 1 93  ? -24.434 11.046 -2.602  0.49 8.90  ? 93  ASN A CG  1 
ATOM   939  O OD1 A ASN A 1 93  ? -23.225 10.292 -3.392  0.51 7.98  ? 93  ASN A OD1 1 
ATOM   940  O OD1 B ASN A 1 93  ? -23.559 10.776 -3.414  0.49 9.15  ? 93  ASN A OD1 1 
ATOM   941  N ND2 A ASN A 1 93  ? -25.127 11.408 -3.033  0.51 8.42  ? 93  ASN A ND2 1 
ATOM   942  N ND2 B ASN A 1 93  ? -25.446 11.847 -2.902  0.49 9.57  ? 93  ASN A ND2 1 
ATOM   943  N N   A GLN A 1 94  ? -23.053 12.207 1.927   0.51 9.26  ? 94  GLN A N   1 
ATOM   944  N N   B GLN A 1 94  ? -22.755 11.740 1.970   0.49 7.97  ? 94  GLN A N   1 
ATOM   945  C CA  A GLN A 1 94  ? -22.782 11.965 3.358   0.51 9.81  ? 94  GLN A CA  1 
ATOM   946  C CA  B GLN A 1 94  ? -22.506 11.501 3.398   0.49 8.29  ? 94  GLN A CA  1 
ATOM   947  C C   A GLN A 1 94  ? -23.913 12.612 4.144   0.51 10.01 ? 94  GLN A C   1 
ATOM   948  C C   B GLN A 1 94  ? -23.654 12.164 4.147   0.49 8.64  ? 94  GLN A C   1 
ATOM   949  O O   A GLN A 1 94  ? -23.957 13.857 4.269   0.51 10.01 ? 94  GLN A O   1 
ATOM   950  O O   B GLN A 1 94  ? -23.647 13.389 4.315   0.49 9.07  ? 94  GLN A O   1 
ATOM   951  C CB  A GLN A 1 94  ? -21.427 12.531 3.760   0.51 10.12 ? 94  GLN A CB  1 
ATOM   952  C CB  B GLN A 1 94  ? -21.146 12.071 3.764   0.49 9.73  ? 94  GLN A CB  1 
ATOM   953  C CG  A GLN A 1 94  ? -20.263 11.946 2.979   0.51 10.99 ? 94  GLN A CG  1 
ATOM   954  C CG  B GLN A 1 94  ? -20.010 11.484 2.947   0.49 11.66 ? 94  GLN A CG  1 
ATOM   955  C CD  A GLN A 1 94  ? -20.017 10.469 3.182   0.51 12.96 ? 94  GLN A CD  1 
ATOM   956  C CD  B GLN A 1 94  ? -19.865 9.990  3.094   0.49 13.18 ? 94  GLN A CD  1 
ATOM   957  O OE1 A GLN A 1 94  ? -19.661 10.022 4.273   0.51 17.01 ? 94  GLN A OE1 1 
ATOM   958  O OE1 B GLN A 1 94  ? -19.881 9.446  4.199   0.49 17.31 ? 94  GLN A OE1 1 
ATOM   959  N NE2 A GLN A 1 94  ? -20.147 9.697  2.109   0.51 14.60 ? 94  GLN A NE2 1 
ATOM   960  N NE2 B GLN A 1 94  ? -19.692 9.320  1.965   0.49 13.65 ? 94  GLN A NE2 1 
ATOM   961  N N   A TYR A 1 95  ? -24.852 11.781 4.586   0.51 11.19 ? 95  TYR A N   1 
ATOM   962  N N   B TYR A 1 95  ? -24.676 11.387 4.480   0.49 9.15  ? 95  TYR A N   1 
ATOM   963  C CA  A TYR A 1 95  ? -26.082 12.247 5.256   0.51 12.00 ? 95  TYR A CA  1 
ATOM   964  C CA  B TYR A 1 95  ? -25.896 11.910 5.148   0.49 10.42 ? 95  TYR A CA  1 
ATOM   965  C C   A TYR A 1 95  ? -26.663 13.325 4.367   0.51 12.65 ? 95  TYR A C   1 
ATOM   966  C C   B TYR A 1 95  ? -26.508 13.120 4.404   0.49 11.26 ? 95  TYR A C   1 
ATOM   967  O O   A TYR A 1 95  ? -27.079 14.416 4.821   0.51 12.75 ? 95  TYR A O   1 
ATOM   968  O O   B TYR A 1 95  ? -26.886 14.083 5.058   0.49 12.38 ? 95  TYR A O   1 
ATOM   969  C CB  A TYR A 1 95  ? -25.804 12.681 6.693   0.51 11.79 ? 95  TYR A CB  1 
ATOM   970  C CB  B TYR A 1 95  ? -25.582 12.218 6.617   0.49 10.84 ? 95  TYR A CB  1 
ATOM   971  C CG  A TYR A 1 95  ? -25.333 11.541 7.555   0.51 12.80 ? 95  TYR A CG  1 
ATOM   972  C CG  B TYR A 1 95  ? -25.066 11.033 7.396   0.49 11.29 ? 95  TYR A CG  1 
ATOM   973  C CD1 A TYR A 1 95  ? -26.220 10.597 8.042   0.51 15.17 ? 95  TYR A CD1 1 
ATOM   974  C CD1 B TYR A 1 95  ? -25.925 10.043 7.838   0.49 11.96 ? 95  TYR A CD1 1 
ATOM   975  C CD2 A TYR A 1 95  ? -23.995 11.400 7.885   0.51 16.36 ? 95  TYR A CD2 1 
ATOM   976  C CD2 B TYR A 1 95  ? -23.710 10.852 7.618   0.49 13.44 ? 95  TYR A CD2 1 
ATOM   977  C CE1 A TYR A 1 95  ? -25.794 9.544  8.838   0.51 17.52 ? 95  TYR A CE1 1 
ATOM   978  C CE1 B TYR A 1 95  ? -25.462 8.936  8.528   0.49 13.93 ? 95  TYR A CE1 1 
ATOM   979  C CE2 A TYR A 1 95  ? -23.553 10.359 8.689   0.51 18.17 ? 95  TYR A CE2 1 
ATOM   980  C CE2 B TYR A 1 95  ? -23.231 9.760  8.324   0.49 15.42 ? 95  TYR A CE2 1 
ATOM   981  C CZ  A TYR A 1 95  ? -24.453 9.418  9.162   0.51 17.43 ? 95  TYR A CZ  1 
ATOM   982  C CZ  B TYR A 1 95  ? -24.110 8.804  8.801   0.49 15.16 ? 95  TYR A CZ  1 
ATOM   983  O OH  A TYR A 1 95  ? -24.024 8.390  9.956   0.51 19.98 ? 95  TYR A OH  1 
ATOM   984  O OH  B TYR A 1 95  ? -23.631 7.720  9.477   0.49 18.60 ? 95  TYR A OH  1 
ATOM   985  N N   . GLY A 1 96  ? -26.645 13.023 3.073   1.00 12.68 ? 96  GLY A N   1 
ATOM   986  C CA  . GLY A 1 96  ? -27.377 13.918 2.174   1.00 13.93 ? 96  GLY A CA  1 
ATOM   987  C C   . GLY A 1 96  ? -26.562 15.065 1.621   1.00 13.00 ? 96  GLY A C   1 
ATOM   988  O O   . GLY A 1 96  ? -27.139 15.857 0.857   1.00 15.21 ? 96  GLY A O   1 
ATOM   989  N N   . LYS A 1 97  ? -25.284 15.176 1.943   1.00 12.40 ? 97  LYS A N   1 
ATOM   990  C CA  . LYS A 1 97  ? -24.440 16.287 1.473   1.00 12.16 ? 97  LYS A CA  1 
ATOM   991  C C   . LYS A 1 97  ? -23.156 15.716 0.883   1.00 10.22 ? 97  LYS A C   1 
ATOM   992  O O   . LYS A 1 97  ? -22.739 14.590 1.191   1.00 11.96 ? 97  LYS A O   1 
ATOM   993  C CB  . LYS A 1 97  ? -24.101 17.257 2.607   1.00 15.27 ? 97  LYS A CB  1 
ATOM   994  C CG  . LYS A 1 97  ? -25.300 17.987 3.212   1.00 18.92 ? 97  LYS A CG  1 
ATOM   995  C CD  . LYS A 1 97  ? -25.949 18.980 2.254   1.00 22.69 ? 97  LYS A CD  1 
ATOM   996  C CE  . LYS A 1 97  ? -27.138 19.713 2.836   1.00 27.44 ? 97  LYS A CE  1 
ATOM   997  N NZ  . LYS A 1 97  ? -27.733 20.646 1.850   1.00 31.36 ? 97  LYS A NZ  1 
ATOM   998  N N   . ASP A 1 98  ? -22.511 16.557 0.068   1.00 9.78  ? 98  ASP A N   1 
ATOM   999  C CA  . ASP A 1 98  ? -21.157 16.272 -0.410  1.00 9.12  ? 98  ASP A CA  1 
ATOM   1000 C C   . ASP A 1 98  ? -20.179 17.225 0.280   1.00 9.04  ? 98  ASP A C   1 
ATOM   1001 O O   . ASP A 1 98  ? -20.554 18.357 0.623   1.00 9.95  ? 98  ASP A O   1 
ATOM   1002 C CB  . ASP A 1 98  ? -21.052 16.508 -1.914  1.00 9.30  ? 98  ASP A CB  1 
ATOM   1003 C CG  . ASP A 1 98  ? -21.839 15.602 -2.846  1.00 9.31  ? 98  ASP A CG  1 
ATOM   1004 O OD1 . ASP A 1 98  ? -22.495 14.633 -2.408  1.00 10.06 ? 98  ASP A OD1 1 
ATOM   1005 O OD2 . ASP A 1 98  ? -21.764 15.912 -4.070  1.00 9.38  ? 98  ASP A OD2 1 
ATOM   1006 N N   . TYR A 1 99  ? -18.943 16.807 0.428   1.00 8.94  ? 99  TYR A N   1 
ATOM   1007 C CA  . TYR A 1 99  ? -17.910 17.619 1.087   1.00 8.90  ? 99  TYR A CA  1 
ATOM   1008 C C   . TYR A 1 99  ? -16.671 17.629 0.207   1.00 8.56  ? 99  TYR A C   1 
ATOM   1009 O O   . TYR A 1 99  ? -16.156 16.556 -0.114  1.00 10.48 ? 99  TYR A O   1 
ATOM   1010 C CB  . TYR A 1 99  ? -17.597 17.034 2.461   1.00 10.28 ? 99  TYR A CB  1 
ATOM   1011 C CG  . TYR A 1 99  ? -18.774 17.116 3.398   1.00 10.87 ? 99  TYR A CG  1 
ATOM   1012 C CD1 . TYR A 1 99  ? -19.030 18.276 4.096   1.00 12.00 ? 99  TYR A CD1 1 
ATOM   1013 C CD2 . TYR A 1 99  ? -19.711 16.093 3.489   1.00 12.85 ? 99  TYR A CD2 1 
ATOM   1014 C CE1 . TYR A 1 99  ? -20.135 18.392 4.923   1.00 12.88 ? 99  TYR A CE1 1 
ATOM   1015 C CE2 . TYR A 1 99  ? -20.832 16.198 4.301   1.00 14.17 ? 99  TYR A CE2 1 
ATOM   1016 C CZ  . TYR A 1 99  ? -21.033 17.354 5.032   1.00 14.31 ? 99  TYR A CZ  1 
ATOM   1017 O OH  . TYR A 1 99  ? -22.125 17.506 5.836   1.00 17.48 ? 99  TYR A OH  1 
ATOM   1018 N N   . ILE A 1 100 ? -16.165 18.818 -0.112  1.00 7.97  ? 100 ILE A N   1 
ATOM   1019 C CA  . ILE A 1 100 ? -14.980 18.961 -0.988  1.00 7.67  ? 100 ILE A CA  1 
ATOM   1020 C C   . ILE A 1 100 ? -13.928 19.842 -0.332  1.00 7.35  ? 100 ILE A C   1 
ATOM   1021 O O   . ILE A 1 100 ? -14.239 20.778 0.422   1.00 8.29  ? 100 ILE A O   1 
ATOM   1022 C CB  . ILE A 1 100 ? -15.356 19.500 -2.389  1.00 8.32  ? 100 ILE A CB  1 
ATOM   1023 C CG1 . ILE A 1 100 ? -15.852 20.950 -2.369  1.00 9.07  ? 100 ILE A CG1 1 
ATOM   1024 C CG2 . ILE A 1 100 ? -16.368 18.565 -3.048  1.00 9.19  ? 100 ILE A CG2 1 
ATOM   1025 C CD1 . ILE A 1 100 ? -16.004 21.570 -3.751  1.00 10.17 ? 100 ILE A CD1 1 
ATOM   1026 N N   . ASP A 1 101 ? -12.680 19.568 -0.657  1.00 7.14  ? 101 ASP A N   1 
ATOM   1027 C CA  . ASP A 1 101 ? -11.572 20.422 -0.212  1.00 6.89  ? 101 ASP A CA  1 
ATOM   1028 C C   . ASP A 1 101 ? -10.371 20.221 -1.135  1.00 6.25  ? 101 ASP A C   1 
ATOM   1029 O O   . ASP A 1 101 ? -10.337 19.270 -1.923  1.00 6.73  ? 101 ASP A O   1 
ATOM   1030 C CB  . ASP A 1 101 ? -11.190 20.161 1.257   1.00 7.80  ? 101 ASP A CB  1 
ATOM   1031 C CG  . ASP A 1 101 ? -10.574 18.797 1.472   1.00 8.47  ? 101 ASP A CG  1 
ATOM   1032 O OD1 . ASP A 1 101 ? -9.342  18.691 1.196   1.00 8.80  ? 101 ASP A OD1 1 
ATOM   1033 O OD2 . ASP A 1 101 ? -11.287 17.847 1.861   1.00 11.15 ? 101 ASP A OD2 1 
ATOM   1034 N N   . ILE A 1 102 ? -9.414  21.125 -1.013  1.00 6.10  ? 102 ILE A N   1 
ATOM   1035 C CA  . ILE A 1 102 ? -8.056  20.899 -1.530  1.00 5.99  ? 102 ILE A CA  1 
ATOM   1036 C C   . ILE A 1 102 ? -7.116  20.785 -0.340  1.00 5.87  ? 102 ILE A C   1 
ATOM   1037 O O   . ILE A 1 102 ? -7.267  21.513 0.656   1.00 6.66  ? 102 ILE A O   1 
ATOM   1038 C CB  . ILE A 1 102 ? -7.614  21.993 -2.520  1.00 6.52  ? 102 ILE A CB  1 
ATOM   1039 C CG1 . ILE A 1 102 ? -8.472  21.901 -3.788  1.00 7.37  ? 102 ILE A CG1 1 
ATOM   1040 C CG2 . ILE A 1 102 ? -6.136  21.875 -2.875  1.00 7.07  ? 102 ILE A CG2 1 
ATOM   1041 C CD1 . ILE A 1 102 ? -8.290  23.074 -4.729  1.00 8.32  ? 102 ILE A CD1 1 
ATOM   1042 N N   . SER A 1 103 ? -6.147  19.897 -0.473  1.00 6.30  ? 103 SER A N   1 
ATOM   1043 C CA  . SER A 1 103 ? -5.150  19.662 0.580   1.00 6.59  ? 103 SER A CA  1 
ATOM   1044 C C   . SER A 1 103 ? -3.744  19.742 0.021   1.00 6.15  ? 103 SER A C   1 
ATOM   1045 O O   . SER A 1 103 ? -3.442  19.151 -1.035  1.00 6.73  ? 103 SER A O   1 
ATOM   1046 C CB  . SER A 1 103 ? -5.393  18.319 1.185   1.00 7.24  ? 103 SER A CB  1 
ATOM   1047 O OG  . SER A 1 103 ? -4.388  18.036 2.145   1.00 8.04  ? 103 SER A OG  1 
ATOM   1048 N N   . ASN A 1 104 ? -2.877  20.378 0.814   1.00 6.36  ? 104 ASN A N   1 
ATOM   1049 C CA  . ASN A 1 104 ? -1.411  20.391 0.668   1.00 6.31  ? 104 ASN A CA  1 
ATOM   1050 C C   . ASN A 1 104 ? -0.737  19.530 1.744   1.00 6.16  ? 104 ASN A C   1 
ATOM   1051 O O   . ASN A 1 104 ? 0.489   19.611 1.916   1.00 6.81  ? 104 ASN A O   1 
ATOM   1052 C CB  . ASN A 1 104 ? -0.864  21.808 0.738   1.00 6.94  ? 104 ASN A CB  1 
ATOM   1053 C CG  . ASN A 1 104 ? -1.200  22.611 -0.496  1.00 7.33  ? 104 ASN A CG  1 
ATOM   1054 O OD1 . ASN A 1 104 ? -1.081  22.109 -1.613  1.00 9.25  ? 104 ASN A OD1 1 
ATOM   1055 N ND2 . ASN A 1 104 ? -1.570  23.864 -0.304  1.00 8.50  ? 104 ASN A ND2 1 
ATOM   1056 N N   . ILE A 1 105 ? -1.492  18.692 2.453   1.00 6.34  ? 105 ILE A N   1 
ATOM   1057 C CA  . ILE A 1 105 ? -0.908  17.844 3.513   1.00 6.96  ? 105 ILE A CA  1 
ATOM   1058 C C   . ILE A 1 105 ? 0.115   16.852 2.960   1.00 6.73  ? 105 ILE A C   1 
ATOM   1059 O O   . ILE A 1 105 ? 1.035   16.452 3.684   1.00 7.60  ? 105 ILE A O   1 
ATOM   1060 C CB  . ILE A 1 105 ? -2.051  17.166 4.300   1.00 7.73  ? 105 ILE A CB  1 
ATOM   1061 C CG1 . ILE A 1 105 ? -2.818  18.217 5.094   1.00 8.64  ? 105 ILE A CG1 1 
ATOM   1062 C CG2 . ILE A 1 105 ? -1.556  16.038 5.187   1.00 9.15  ? 105 ILE A CG2 1 
ATOM   1063 C CD1 . ILE A 1 105 ? -4.137  17.725 5.671   1.00 10.28 ? 105 ILE A CD1 1 
ATOM   1064 N N   . LYS A 1 106 ? -0.064  16.443 1.693   1.00 6.29  ? 106 LYS A N   1 
ATOM   1065 C CA  . LYS A 1 106 ? 0.865   15.557 0.982   1.00 6.77  ? 106 LYS A CA  1 
ATOM   1066 C C   . LYS A 1 106 ? 1.675   16.348 -0.041  1.00 6.69  ? 106 LYS A C   1 
ATOM   1067 O O   . LYS A 1 106 ? 2.149   15.765 -1.032  1.00 7.85  ? 106 LYS A O   1 
ATOM   1068 C CB  . LYS A 1 106 ? 0.084   14.413 0.339   1.00 7.96  ? 106 LYS A CB  1 
ATOM   1069 C CG  . LYS A 1 106 ? -0.551  13.492 1.353   1.00 9.97  ? 106 LYS A CG  1 
ATOM   1070 C CD  . LYS A 1 106 ? 0.489   12.627 2.029   1.00 14.48 ? 106 LYS A CD  1 
ATOM   1071 C CE  . LYS A 1 106 ? -0.030  11.696 3.078   1.00 17.25 ? 106 LYS A CE  1 
ATOM   1072 N NZ  . LYS A 1 106 ? 1.084   10.849 3.545   1.00 21.72 ? 106 LYS A NZ  1 
ATOM   1073 N N   . GLY A 1 107 ? 1.890   17.623 0.219   1.00 6.81  ? 107 GLY A N   1 
ATOM   1074 C CA  . GLY A 1 107 ? 2.702   18.476 -0.635  1.00 7.10  ? 107 GLY A CA  1 
ATOM   1075 C C   . GLY A 1 107 ? 1.929   19.015 -1.814  1.00 6.65  ? 107 GLY A C   1 
ATOM   1076 O O   . GLY A 1 107 ? 0.704   18.886 -1.907  1.00 8.22  ? 107 GLY A O   1 
ATOM   1077 N N   . PHE A 1 108 ? 2.682   19.622 -2.724  1.00 6.38  ? 108 PHE A N   1 
ATOM   1078 C CA  . PHE A 1 108 ? 2.111   20.341 -3.866  1.00 6.47  ? 108 PHE A CA  1 
ATOM   1079 C C   . PHE A 1 108 ? 2.959   20.026 -5.082  1.00 6.70  ? 108 PHE A C   1 
ATOM   1080 O O   . PHE A 1 108 ? 4.193   20.101 -5.034  1.00 7.04  ? 108 PHE A O   1 
ATOM   1081 C CB  . PHE A 1 108 ? 2.109   21.844 -3.586  1.00 6.68  ? 108 PHE A CB  1 
ATOM   1082 C CG  . PHE A 1 108 ? 1.599   22.711 -4.710  1.00 6.72  ? 108 PHE A CG  1 
ATOM   1083 C CD1 . PHE A 1 108 ? 2.416   23.002 -5.802  1.00 6.96  ? 108 PHE A CD1 1 
ATOM   1084 C CD2 . PHE A 1 108 ? 0.326   23.248 -4.679  1.00 7.00  ? 108 PHE A CD2 1 
ATOM   1085 C CE1 . PHE A 1 108 ? 1.965   23.825 -6.824  1.00 7.61  ? 108 PHE A CE1 1 
ATOM   1086 C CE2 . PHE A 1 108 ? -0.119  24.078 -5.696  1.00 7.74  ? 108 PHE A CE2 1 
ATOM   1087 C CZ  . PHE A 1 108 ? 0.709   24.371 -6.758  1.00 7.68  ? 108 PHE A CZ  1 
ATOM   1088 N N   . ASN A 1 109 ? 2.293   19.703 -6.191  1.00 6.72  ? 109 ASN A N   1 
ATOM   1089 C CA  . ASN A 1 109 ? 3.001   19.515 -7.469  1.00 7.16  ? 109 ASN A CA  1 
ATOM   1090 C C   . ASN A 1 109 ? 2.449   20.429 -8.564  1.00 7.24  ? 109 ASN A C   1 
ATOM   1091 O O   . ASN A 1 109 ? 3.250   21.051 -9.281  1.00 9.49  ? 109 ASN A O   1 
ATOM   1092 C CB  . ASN A 1 109 ? 3.062   18.047 -7.904  1.00 7.36  ? 109 ASN A CB  1 
ATOM   1093 C CG  . ASN A 1 109 ? 1.728   17.379 -8.172  1.00 7.30  ? 109 ASN A CG  1 
ATOM   1094 O OD1 . ASN A 1 109 ? 0.673   17.812 -7.681  1.00 6.91  ? 109 ASN A OD1 1 
ATOM   1095 N ND2 . ASN A 1 109 ? 1.773   16.305 -8.955  1.00 8.31  ? 109 ASN A ND2 1 
ATOM   1096 N N   . VAL A 1 110 ? 1.133   20.498 -8.701  1.00 6.50  ? 110 VAL A N   1 
ATOM   1097 C CA  . VAL A 1 110 ? 0.455   21.206 -9.795  1.00 6.98  ? 110 VAL A CA  1 
ATOM   1098 C C   . VAL A 1 110 ? -0.638  22.049 -9.177  1.00 6.42  ? 110 VAL A C   1 
ATOM   1099 O O   . VAL A 1 110 ? -1.375  21.567 -8.299  1.00 6.75  ? 110 VAL A O   1 
ATOM   1100 C CB  . VAL A 1 110 ? -0.102  20.162 -10.800 1.00 7.55  ? 110 VAL A CB  1 
ATOM   1101 C CG1 . VAL A 1 110 ? -0.943  20.775 -11.899 1.00 7.80  ? 110 VAL A CG1 1 
ATOM   1102 C CG2 . VAL A 1 110 ? 1.010   19.327 -11.411 1.00 7.86  ? 110 VAL A CG2 1 
ATOM   1103 N N   . PRO A 1 111 ? -0.825  23.303 -9.636  1.00 6.34  ? 111 PRO A N   1 
ATOM   1104 C CA  . PRO A 1 111 ? -1.917  24.124 -9.127  1.00 6.76  ? 111 PRO A CA  1 
ATOM   1105 C C   . PRO A 1 111 ? -3.268  23.576 -9.586  1.00 6.35  ? 111 PRO A C   1 
ATOM   1106 O O   . PRO A 1 111 ? -3.373  22.958 -10.657 1.00 6.54  ? 111 PRO A O   1 
ATOM   1107 C CB  . PRO A 1 111 ? -1.617  25.495 -9.736  1.00 7.64  ? 111 PRO A CB  1 
ATOM   1108 C CG  . PRO A 1 111 ? -0.840  25.180 -11.010 1.00 8.27  ? 111 PRO A CG  1 
ATOM   1109 C CD  . PRO A 1 111 ? 0.020   24.014 -10.620 1.00 7.00  ? 111 PRO A CD  1 
ATOM   1110 N N   . MET A 1 112 ? -4.314  23.836 -8.804  1.00 6.61  ? 112 MET A N   1 
ATOM   1111 C CA  A MET A 1 112 ? -5.637  23.273 -9.172  0.54 6.33  ? 112 MET A CA  1 
ATOM   1112 C CA  B MET A 1 112 ? -5.612  23.191 -8.968  0.46 6.74  ? 112 MET A CA  1 
ATOM   1113 C C   . MET A 1 112 ? -6.768  24.119 -8.598  1.00 6.29  ? 112 MET A C   1 
ATOM   1114 O O   . MET A 1 112 ? -6.667  24.775 -7.554  1.00 7.51  ? 112 MET A O   1 
ATOM   1115 C CB  A MET A 1 112 ? -5.851  21.790 -8.780  0.54 6.70  ? 112 MET A CB  1 
ATOM   1116 C CB  B MET A 1 112 ? -5.568  22.038 -7.975  0.46 7.36  ? 112 MET A CB  1 
ATOM   1117 C CG  A MET A 1 112 ? -5.517  21.506 -7.315  0.54 7.74  ? 112 MET A CG  1 
ATOM   1118 C CG  B MET A 1 112 ? -6.865  21.305 -7.897  0.46 8.31  ? 112 MET A CG  1 
ATOM   1119 S SD  A MET A 1 112 ? -6.218  19.998 -6.594  0.54 8.73  ? 112 MET A SD  1 
ATOM   1120 S SD  B MET A 1 112 ? -6.807  19.982 -6.709  0.46 7.81  ? 112 MET A SD  1 
ATOM   1121 C CE  A MET A 1 112 ? -5.478  18.754 -7.646  0.54 8.36  ? 112 MET A CE  1 
ATOM   1122 C CE  B MET A 1 112 ? -5.996  18.722 -7.690  0.46 7.90  ? 112 MET A CE  1 
ATOM   1123 N N   . ASP A 1 113 ? -7.860  24.054 -9.343  1.00 6.47  ? 113 ASP A N   1 
ATOM   1124 C CA  . ASP A 1 113 ? -9.183  24.540 -8.937  1.00 6.60  ? 113 ASP A CA  1 
ATOM   1125 C C   . ASP A 1 113 ? -10.110 23.339 -8.850  1.00 6.34  ? 113 ASP A C   1 
ATOM   1126 O O   . ASP A 1 113 ? -10.082 22.476 -9.744  1.00 7.42  ? 113 ASP A O   1 
ATOM   1127 C CB  . ASP A 1 113 ? -9.710  25.563 -9.937  1.00 7.45  ? 113 ASP A CB  1 
ATOM   1128 C CG  . ASP A 1 113 ? -11.063 26.117 -9.554  1.00 7.86  ? 113 ASP A CG  1 
ATOM   1129 O OD1 . ASP A 1 113 ? -12.077 25.449 -9.833  1.00 8.89  ? 113 ASP A OD1 1 
ATOM   1130 O OD2 . ASP A 1 113 ? -11.087 27.196 -8.931  1.00 10.25 ? 113 ASP A OD2 1 
ATOM   1131 N N   . PHE A 1 114 ? -10.926 23.278 -7.816  1.00 6.33  ? 114 PHE A N   1 
ATOM   1132 C CA  . PHE A 1 114 ? -11.903 22.198 -7.647  1.00 6.52  ? 114 PHE A CA  1 
ATOM   1133 C C   . PHE A 1 114 ? -13.242 22.845 -7.348  1.00 6.62  ? 114 PHE A C   1 
ATOM   1134 O O   . PHE A 1 114 ? -13.436 23.401 -6.263  1.00 7.61  ? 114 PHE A O   1 
ATOM   1135 C CB  . PHE A 1 114 ? -11.439 21.285 -6.518  1.00 7.05  ? 114 PHE A CB  1 
ATOM   1136 C CG  . PHE A 1 114 ? -12.303 20.089 -6.195  1.00 6.93  ? 114 PHE A CG  1 
ATOM   1137 C CD1 . PHE A 1 114 ? -13.242 19.577 -7.077  1.00 7.84  ? 114 PHE A CD1 1 
ATOM   1138 C CD2 . PHE A 1 114 ? -12.130 19.435 -4.977  1.00 7.27  ? 114 PHE A CD2 1 
ATOM   1139 C CE1 . PHE A 1 114 ? -13.983 18.456 -6.750  1.00 8.45  ? 114 PHE A CE1 1 
ATOM   1140 C CE2 . PHE A 1 114 ? -12.855 18.305 -4.669  1.00 7.92  ? 114 PHE A CE2 1 
ATOM   1141 C CZ  . PHE A 1 114 ? -13.784 17.810 -5.549  1.00 8.49  ? 114 PHE A CZ  1 
ATOM   1142 N N   . SER A 1 115 ? -14.138 22.833 -8.331  1.00 7.10  ? 115 SER A N   1 
ATOM   1143 C CA  . SER A 1 115 ? -15.394 23.593 -8.250  1.00 8.00  ? 115 SER A CA  1 
ATOM   1144 C C   . SER A 1 115 ? -16.572 22.718 -8.619  1.00 7.80  ? 115 SER A C   1 
ATOM   1145 O O   . SER A 1 115 ? -16.481 21.868 -9.504  1.00 8.48  ? 115 SER A O   1 
ATOM   1146 C CB  . SER A 1 115 ? -15.364 24.797 -9.178  1.00 9.12  ? 115 SER A CB  1 
ATOM   1147 O OG  . SER A 1 115 ? -14.480 25.813 -8.719  1.00 10.04 ? 115 SER A OG  1 
ATOM   1148 N N   . PRO A 1 116 ? -17.744 22.979 -8.032  1.00 8.29  ? 116 PRO A N   1 
ATOM   1149 C CA  . PRO A 1 116 ? -18.964 22.348 -8.521  1.00 8.34  ? 116 PRO A CA  1 
ATOM   1150 C C   . PRO A 1 116 ? -19.310 22.890 -9.907  1.00 8.76  ? 116 PRO A C   1 
ATOM   1151 O O   . PRO A 1 116 ? -19.015 24.043 -10.221 1.00 10.37 ? 116 PRO A O   1 
ATOM   1152 C CB  . PRO A 1 116 ? -20.007 22.793 -7.493  1.00 9.71  ? 116 PRO A CB  1 
ATOM   1153 C CG  . PRO A 1 116 ? -19.507 24.148 -7.037  1.00 11.06 ? 116 PRO A CG  1 
ATOM   1154 C CD  . PRO A 1 116 ? -18.002 23.966 -6.963  1.00 10.06 ? 116 PRO A CD  1 
ATOM   1155 N N   . THR A 1 117 ? -19.962 22.052 -10.698 1.00 8.90  ? 117 THR A N   1 
ATOM   1156 C CA  . THR A 1 117 ? -20.565 22.470 -11.988 1.00 9.69  ? 117 THR A CA  1 
ATOM   1157 C C   . THR A 1 117 ? -22.081 22.619 -11.847 1.00 10.73 ? 117 THR A C   1 
ATOM   1158 O O   . THR A 1 117 ? -22.743 22.950 -12.837 1.00 14.64 ? 117 THR A O   1 
ATOM   1159 C CB  . THR A 1 117 ? -20.193 21.501 -13.103 1.00 9.71  ? 117 THR A CB  1 
ATOM   1160 O OG1 . THR A 1 117 ? -20.651 20.218 -12.717 1.00 11.09 ? 117 THR A OG1 1 
ATOM   1161 C CG2 . THR A 1 117 ? -18.715 21.490 -13.385 1.00 10.27 ? 117 THR A CG2 1 
ATOM   1162 N N   . THR A 1 118 ? -22.606 22.349 -10.671 1.00 10.81 ? 118 THR A N   1 
ATOM   1163 C CA  . THR A 1 118 ? -24.038 22.411 -10.330 1.00 11.61 ? 118 THR A CA  1 
ATOM   1164 C C   . THR A 1 118 ? -24.203 23.433 -9.200  1.00 13.55 ? 118 THR A C   1 
ATOM   1165 O O   . THR A 1 118 ? -23.193 23.901 -8.619  1.00 16.41 ? 118 THR A O   1 
ATOM   1166 C CB  . THR A 1 118 ? -24.530 21.000 -9.985  1.00 12.31 ? 118 THR A CB  1 
ATOM   1167 O OG1 . THR A 1 118 ? -23.692 20.457 -8.961  1.00 12.13 ? 118 THR A OG1 1 
ATOM   1168 C CG2 . THR A 1 118 ? -24.497 20.067 -11.171 1.00 14.02 ? 118 THR A CG2 1 
ATOM   1169 N N   . ARG A 1 119 ? -25.443 23.747 -8.853  1.00 15.03 ? 119 ARG A N   1 
ATOM   1170 C CA  . ARG A 1 119 ? -25.727 24.884 -7.936  1.00 17.34 ? 119 ARG A CA  1 
ATOM   1171 C C   . ARG A 1 119 ? -25.488 24.544 -6.462  1.00 16.11 ? 119 ARG A C   1 
ATOM   1172 O O   . ARG A 1 119 ? -25.514 23.365 -6.071  1.00 20.33 ? 119 ARG A O   1 
ATOM   1173 C CB  . ARG A 1 119 ? -27.189 25.318 -8.063  1.00 21.79 ? 119 ARG A CB  1 
ATOM   1174 C CG  . ARG A 1 119 ? -27.610 25.749 -9.460  1.00 28.22 ? 119 ARG A CG  1 
ATOM   1175 C CD  . ARG A 1 119 ? -29.124 25.762 -9.587  1.00 34.52 ? 119 ARG A CD  1 
ATOM   1176 N NE  . ARG A 1 119 ? -29.572 26.037 -10.945 1.00 41.36 ? 119 ARG A NE  1 
ATOM   1177 C CZ  . ARG A 1 119 ? -29.602 27.242 -11.515 1.00 43.90 ? 119 ARG A CZ  1 
ATOM   1178 N NH1 . ARG A 1 119 ? -29.199 28.311 -10.848 1.00 44.65 ? 119 ARG A NH1 1 
ATOM   1179 N NH2 . ARG A 1 119 ? -30.030 27.372 -12.760 1.00 46.31 ? 119 ARG A NH2 1 
ATOM   1180 N N   . GLY A 1 120 ? -25.302 25.583 -5.655  1.00 16.70 ? 120 GLY A N   1 
ATOM   1181 C CA  . GLY A 1 120 ? -25.515 25.497 -4.206  1.00 16.99 ? 120 GLY A CA  1 
ATOM   1182 C C   . GLY A 1 120 ? -24.259 25.542 -3.365  1.00 15.28 ? 120 GLY A C   1 
ATOM   1183 O O   . GLY A 1 120 ? -24.401 25.397 -2.172  1.00 17.29 ? 120 GLY A O   1 
ATOM   1184 N N   . CYS A 1 121 ? -23.083 25.784 -3.915  1.00 13.86 ? 121 CYS A N   1 
ATOM   1185 C CA  . CYS A 1 121 ? -21.842 25.902 -3.118  1.00 13.05 ? 121 CYS A CA  1 
ATOM   1186 C C   . CYS A 1 121 ? -20.749 26.534 -3.980  1.00 13.66 ? 121 CYS A C   1 
ATOM   1187 O O   . CYS A 1 121 ? -20.821 26.571 -5.216  1.00 16.58 ? 121 CYS A O   1 
ATOM   1188 C CB  . CYS A 1 121 ? -21.397 24.544 -2.587  1.00 13.45 ? 121 CYS A CB  1 
ATOM   1189 S SG  . CYS A 1 121 ? -21.216 23.320 -3.910  1.00 13.58 ? 121 CYS A SG  1 
ATOM   1190 N N   . ARG A 1 122 ? -19.665 26.903 -3.357  1.00 15.10 ? 122 ARG A N   1 
ATOM   1191 C CA  . ARG A 1 122 ? -18.508 27.527 -4.010  1.00 13.67 ? 122 ARG A CA  1 
ATOM   1192 C C   . ARG A 1 122 ? -17.457 26.464 -4.300  1.00 11.04 ? 122 ARG A C   1 
ATOM   1193 O O   . ARG A 1 122 ? -17.509 25.331 -3.783  1.00 12.61 ? 122 ARG A O   1 
ATOM   1194 C CB  . ARG A 1 122 ? -17.957 28.605 -3.070  1.00 16.40 ? 122 ARG A CB  1 
ATOM   1195 C CG  . ARG A 1 122 ? -17.207 28.059 -1.856  1.00 17.38 ? 122 ARG A CG  1 
ATOM   1196 C CD  . ARG A 1 122 ? -16.505 29.153 -1.050  1.00 21.65 ? 122 ARG A CD  1 
ATOM   1197 N NE  . ARG A 1 122 ? -15.657 28.722 0.073   1.00 22.63 ? 122 ARG A NE  1 
ATOM   1198 C CZ  . ARG A 1 122 ? -14.341 28.408 0.019   1.00 24.14 ? 122 ARG A CZ  1 
ATOM   1199 N NH1 . ARG A 1 122 ? -13.629 28.420 -1.104  1.00 19.45 ? 122 ARG A NH1 1 
ATOM   1200 N NH2 . ARG A 1 122 ? -13.726 28.060 1.134   1.00 27.90 ? 122 ARG A NH2 1 
ATOM   1201 N N   . GLY A 1 123 ? -16.514 26.841 -5.138  1.00 9.81  ? 123 GLY A N   1 
ATOM   1202 C CA  . GLY A 1 123 ? -15.307 26.054 -5.332  1.00 9.31  ? 123 GLY A CA  1 
ATOM   1203 C C   . GLY A 1 123 ? -14.166 26.475 -4.425  1.00 8.78  ? 123 GLY A C   1 
ATOM   1204 O O   . GLY A 1 123 ? -14.244 27.466 -3.677  1.00 10.89 ? 123 GLY A O   1 
ATOM   1205 N N   . VAL A 1 124 ? -13.109 25.698 -4.508  1.00 8.82  ? 124 VAL A N   1 
ATOM   1206 C CA  . VAL A 1 124 ? -11.853 25.912 -3.773  1.00 9.70  ? 124 VAL A CA  1 
ATOM   1207 C C   . VAL A 1 124 ? -10.712 25.950 -4.777  1.00 8.42  ? 124 VAL A C   1 
ATOM   1208 O O   . VAL A 1 124 ? -10.784 25.320 -5.829  1.00 8.51  ? 124 VAL A O   1 
ATOM   1209 C CB  . VAL A 1 124 ? -11.666 24.840 -2.672  1.00 13.06 ? 124 VAL A CB  1 
ATOM   1210 C CG1 . VAL A 1 124 ? -12.649 25.036 -1.515  1.00 16.81 ? 124 VAL A CG1 1 
ATOM   1211 C CG2 . VAL A 1 124 ? -11.754 23.412 -3.165  1.00 14.73 ? 124 VAL A CG2 1 
ATOM   1212 N N   . ARG A 1 125 ? -9.646  26.642 -4.434  1.00 9.56  ? 125 ARG A N   1 
ATOM   1213 C CA  . ARG A 1 125 ? -8.530  26.806 -5.373  1.00 9.33  ? 125 ARG A CA  1 
ATOM   1214 C C   . ARG A 1 125 ? -7.215  26.905 -4.615  1.00 9.15  ? 125 ARG A C   1 
ATOM   1215 O O   . ARG A 1 125 ? -7.144  27.589 -3.581  1.00 10.82 ? 125 ARG A O   1 
ATOM   1216 C CB  . ARG A 1 125 ? -8.757  28.035 -6.264  1.00 11.02 ? 125 ARG A CB  1 
ATOM   1217 C CG  . ARG A 1 125 ? -7.674  28.231 -7.313  1.00 11.43 ? 125 ARG A CG  1 
ATOM   1218 C CD  . ARG A 1 125 ? -7.917  29.423 -8.198  1.00 13.65 ? 125 ARG A CD  1 
ATOM   1219 N NE  . ARG A 1 125 ? -9.040  29.175 -9.076  1.00 13.39 ? 125 ARG A NE  1 
ATOM   1220 C CZ  . ARG A 1 125 ? -9.287  29.902 -10.151 1.00 15.66 ? 125 ARG A CZ  1 
ATOM   1221 N NH1 . ARG A 1 125 ? -8.519  30.934 -10.464 1.00 20.95 ? 125 ARG A NH1 1 
ATOM   1222 N NH2 . ARG A 1 125 ? -10.319 29.597 -10.914 1.00 18.08 ? 125 ARG A NH2 1 
ATOM   1223 N N   . CYS A 1 126 ? -6.188  26.280 -5.170  1.00 8.46  ? 126 CYS A N   1 
ATOM   1224 C CA  . CYS A 1 126 ? -4.794  26.469 -4.736  1.00 8.36  ? 126 CYS A CA  1 
ATOM   1225 C C   . CYS A 1 126 ? -3.962  26.614 -5.990  1.00 8.44  ? 126 CYS A C   1 
ATOM   1226 O O   . CYS A 1 126 ? -3.549  25.615 -6.596  1.00 9.22  ? 126 CYS A O   1 
ATOM   1227 C CB  . CYS A 1 126 ? -4.240  25.360 -3.877  1.00 11.29 ? 126 CYS A CB  1 
ATOM   1228 S SG  . CYS A 1 126 ? -2.497  25.635 -3.384  1.00 11.40 ? 126 CYS A SG  1 
ATOM   1229 N N   . ALA A 1 127 ? -3.729  27.855 -6.372  1.00 9.52  ? 127 ALA A N   1 
ATOM   1230 C CA  . ALA A 1 127 ? -3.094  28.142 -7.668  1.00 11.55 ? 127 ALA A CA  1 
ATOM   1231 C C   . ALA A 1 127 ? -1.879  29.038 -7.574  1.00 11.11 ? 127 ALA A C   1 
ATOM   1232 O O   . ALA A 1 127 ? -1.365  29.415 -8.616  1.00 14.72 ? 127 ALA A O   1 
ATOM   1233 C CB  . ALA A 1 127 ? -4.093  28.689 -8.653  1.00 15.65 ? 127 ALA A CB  1 
ATOM   1234 N N   . ALA A 1 128 ? -1.365  29.287 -6.401  1.00 10.28 ? 128 ALA A N   1 
ATOM   1235 C CA  . ALA A 1 128 ? -0.123  30.053 -6.240  1.00 10.57 ? 128 ALA A CA  1 
ATOM   1236 C C   . ALA A 1 128 ? 1.076   29.219 -6.686  1.00 9.95  ? 128 ALA A C   1 
ATOM   1237 O O   . ALA A 1 128 ? 0.990   27.995 -6.806  1.00 10.52 ? 128 ALA A O   1 
ATOM   1238 C CB  . ALA A 1 128 ? -0.006  30.464 -4.797  1.00 12.30 ? 128 ALA A CB  1 
ATOM   1239 N N   . ASP A 1 129 ? 2.209   29.896 -6.870  1.00 10.32 ? 129 ASP A N   1 
ATOM   1240 C CA  . ASP A 1 129 ? 3.447   29.244 -7.352  1.00 10.28 ? 129 ASP A CA  1 
ATOM   1241 C C   . ASP A 1 129 ? 4.201   28.613 -6.179  1.00 8.86  ? 129 ASP A C   1 
ATOM   1242 O O   . ASP A 1 129 ? 5.312   29.040 -5.829  1.00 9.81  ? 129 ASP A O   1 
ATOM   1243 C CB  . ASP A 1 129 ? 4.328   30.207 -8.126  1.00 12.38 ? 129 ASP A CB  1 
ATOM   1244 C CG  . ASP A 1 129 ? 5.526   29.529 -8.770  1.00 12.83 ? 129 ASP A CG  1 
ATOM   1245 O OD1 . ASP A 1 129 ? 5.577   28.269 -8.852  1.00 12.29 ? 129 ASP A OD1 1 
ATOM   1246 O OD2 . ASP A 1 129 ? 6.397   30.270 -9.238  1.00 16.45 ? 129 ASP A OD2 1 
ATOM   1247 N N   . ILE A 1 130 ? 3.593   27.592 -5.605  1.00 8.02  ? 130 ILE A N   1 
ATOM   1248 C CA  . ILE A 1 130 ? 4.200   26.925 -4.446  1.00 7.48  ? 130 ILE A CA  1 
ATOM   1249 C C   . ILE A 1 130 ? 5.520   26.269 -4.837  1.00 7.60  ? 130 ILE A C   1 
ATOM   1250 O O   . ILE A 1 130 ? 6.451   26.283 -4.027  1.00 8.60  ? 130 ILE A O   1 
ATOM   1251 C CB  . ILE A 1 130 ? 3.195   25.969 -3.798  1.00 7.52  ? 130 ILE A CB  1 
ATOM   1252 C CG1 . ILE A 1 130 ? 2.202   26.787 -2.973  1.00 8.94  ? 130 ILE A CG1 1 
ATOM   1253 C CG2 . ILE A 1 130 ? 3.881   24.922 -2.935  1.00 8.54  ? 130 ILE A CG2 1 
ATOM   1254 C CD1 . ILE A 1 130 ? 1.055   26.030 -2.358  1.00 10.01 ? 130 ILE A CD1 1 
ATOM   1255 N N   . VAL A 1 131 ? 5.622   25.668 -6.017  1.00 7.73  ? 131 VAL A N   1 
ATOM   1256 C CA  . VAL A 1 131 ? 6.914   25.039 -6.363  1.00 8.16  ? 131 VAL A CA  1 
ATOM   1257 C C   . VAL A 1 131 ? 7.999   26.104 -6.470  1.00 8.58  ? 131 VAL A C   1 
ATOM   1258 O O   . VAL A 1 131 ? 9.093   25.925 -5.938  1.00 9.50  ? 131 VAL A O   1 
ATOM   1259 C CB  . VAL A 1 131 ? 6.818   24.177 -7.623  1.00 9.34  ? 131 VAL A CB  1 
ATOM   1260 C CG1 . VAL A 1 131 ? 8.168   23.571 -7.949  1.00 12.01 ? 131 VAL A CG1 1 
ATOM   1261 C CG2 . VAL A 1 131 ? 5.772   23.088 -7.462  1.00 9.57  ? 131 VAL A CG2 1 
ATOM   1262 N N   . GLY A 1 132 ? 7.726   27.216 -7.139  1.00 8.71  ? 132 GLY A N   1 
ATOM   1263 C CA  . GLY A 1 132 ? 8.749   28.255 -7.297  1.00 9.73  ? 132 GLY A CA  1 
ATOM   1264 C C   . GLY A 1 132 ? 9.192   28.851 -5.973  1.00 9.06  ? 132 GLY A C   1 
ATOM   1265 O O   . GLY A 1 132 ? 10.355  29.205 -5.819  1.00 9.91  ? 132 GLY A O   1 
ATOM   1266 N N   . GLN A 1 133 ? 8.264   28.966 -5.034  1.00 8.32  ? 133 GLN A N   1 
ATOM   1267 C CA  . GLN A 1 133 ? 8.531   29.650 -3.744  1.00 8.29  ? 133 GLN A CA  1 
ATOM   1268 C C   . GLN A 1 133 ? 8.929   28.659 -2.644  1.00 7.95  ? 133 GLN A C   1 
ATOM   1269 O O   . GLN A 1 133 ? 9.224   29.100 -1.524  1.00 8.92  ? 133 GLN A O   1 
ATOM   1270 C CB  . GLN A 1 133 ? 7.309   30.450 -3.319  1.00 9.12  ? 133 GLN A CB  1 
ATOM   1271 C CG  . GLN A 1 133 ? 6.889   31.515 -4.306  1.00 10.26 ? 133 GLN A CG  1 
ATOM   1272 C CD  . GLN A 1 133 ? 7.894   32.601 -4.559  1.00 11.06 ? 133 GLN A CD  1 
ATOM   1273 O OE1 . GLN A 1 133 ? 8.925   32.707 -3.922  1.00 11.64 ? 133 GLN A OE1 1 
ATOM   1274 N NE2 . GLN A 1 133 ? 7.579   33.436 -5.530  1.00 16.32 ? 133 GLN A NE2 1 
ATOM   1275 N N   . CYS A 1 134 ? 8.954   27.372 -2.941  1.00 8.20  ? 134 CYS A N   1 
ATOM   1276 C CA  . CYS A 1 134 ? 9.150   26.282 -1.960  1.00 8.48  ? 134 CYS A CA  1 
ATOM   1277 C C   . CYS A 1 134 ? 10.404  26.530 -1.132  1.00 8.44  ? 134 CYS A C   1 
ATOM   1278 O O   . CYS A 1 134 ? 11.470  26.770 -1.693  1.00 9.83  ? 134 CYS A O   1 
ATOM   1279 C CB  . CYS A 1 134 ? 9.276   24.961 -2.725  1.00 8.54  ? 134 CYS A CB  1 
ATOM   1280 S SG  . CYS A 1 134 ? 9.250   23.490 -1.676  1.00 8.51  ? 134 CYS A SG  1 
ATOM   1281 N N   . PRO A 1 135 ? 10.331  26.412 0.203   1.00 8.64  ? 135 PRO A N   1 
ATOM   1282 C CA  . PRO A 1 135 ? 11.534  26.469 1.019   1.00 9.88  ? 135 PRO A CA  1 
ATOM   1283 C C   . PRO A 1 135 ? 12.543  25.404 0.582   1.00 8.96  ? 135 PRO A C   1 
ATOM   1284 O O   . PRO A 1 135 ? 12.177  24.274 0.250   1.00 8.66  ? 135 PRO A O   1 
ATOM   1285 C CB  . PRO A 1 135 ? 11.010  26.172 2.424   1.00 12.71 ? 135 PRO A CB  1 
ATOM   1286 C CG  . PRO A 1 135 ? 9.551   26.553 2.412   1.00 12.81 ? 135 PRO A CG  1 
ATOM   1287 C CD  . PRO A 1 135 ? 9.110   26.223 1.019   1.00 9.28  ? 135 PRO A CD  1 
ATOM   1288 N N   . ALA A 1 136 ? 13.816  25.739 0.691   1.00 10.22 ? 136 ALA A N   1 
ATOM   1289 C CA  . ALA A 1 136 ? 14.881  24.844 0.219   1.00 10.48 ? 136 ALA A CA  1 
ATOM   1290 C C   . ALA A 1 136 ? 14.718  23.428 0.773   1.00 9.42  ? 136 ALA A C   1 
ATOM   1291 O O   . ALA A 1 136 ? 14.884  22.465 0.019   1.00 10.68 ? 136 ALA A O   1 
ATOM   1292 C CB  . ALA A 1 136 ? 16.224  25.432 0.572   1.00 13.80 ? 136 ALA A CB  1 
ATOM   1293 N N   . LYS A 1 137 ? 14.455  23.268 2.061   1.00 8.96  ? 137 LYS A N   1 
ATOM   1294 C CA  . LYS A 1 137 ? 14.461  21.919 2.673   1.00 9.72  ? 137 LYS A CA  1 
ATOM   1295 C C   . LYS A 1 137 ? 13.271  21.080 2.207   1.00 9.12  ? 137 LYS A C   1 
ATOM   1296 O O   . LYS A 1 137 ? 13.307  19.862 2.394   1.00 11.17 ? 137 LYS A O   1 
ATOM   1297 C CB  . LYS A 1 137 ? 14.520  22.010 4.195   1.00 11.32 ? 137 LYS A CB  1 
ATOM   1298 C CG  . LYS A 1 137 ? 15.896  22.445 4.689   1.00 12.81 ? 137 LYS A CG  1 
ATOM   1299 C CD  . LYS A 1 137 ? 16.013  22.546 6.169   1.00 15.75 ? 137 LYS A CD  1 
ATOM   1300 C CE  . LYS A 1 137 ? 17.438  22.736 6.623   1.00 19.19 ? 137 LYS A CE  1 
ATOM   1301 N NZ  . LYS A 1 137 ? 17.510  22.822 8.087   1.00 22.50 ? 137 LYS A NZ  1 
ATOM   1302 N N   . LEU A 1 138 ? 12.240  21.710 1.660   1.00 7.67  ? 138 LEU A N   1 
ATOM   1303 C CA  . LEU A 1 138 ? 11.045  20.976 1.192   1.00 7.61  ? 138 LEU A CA  1 
ATOM   1304 C C   . LEU A 1 138 ? 11.098  20.697 -0.310  1.00 7.38  ? 138 LEU A C   1 
ATOM   1305 O O   . LEU A 1 138 ? 10.247  19.960 -0.804  1.00 8.57  ? 138 LEU A O   1 
ATOM   1306 C CB  . LEU A 1 138 ? 9.772   21.756 1.508   1.00 7.41  ? 138 LEU A CB  1 
ATOM   1307 C CG  . LEU A 1 138 ? 9.493   22.018 2.988   1.00 8.17  ? 138 LEU A CG  1 
ATOM   1308 C CD1 . LEU A 1 138 ? 8.143   22.699 3.104   1.00 9.08  ? 138 LEU A CD1 1 
ATOM   1309 C CD2 . LEU A 1 138 ? 9.523   20.745 3.826   1.00 9.09  ? 138 LEU A CD2 1 
ATOM   1310 N N   . LYS A 1 139 ? 12.042  21.247 -1.048  1.00 8.00  ? 139 LYS A N   1 
ATOM   1311 C CA  . LYS A 1 139 ? 12.042  21.036 -2.495  1.00 8.75  ? 139 LYS A CA  1 
ATOM   1312 C C   . LYS A 1 139 ? 12.261  19.550 -2.766  1.00 9.57  ? 139 LYS A C   1 
ATOM   1313 O O   . LYS A 1 139 ? 13.145  18.918 -2.189  1.00 11.01 ? 139 LYS A O   1 
ATOM   1314 C CB  . LYS A 1 139 ? 13.174  21.823 -3.146  1.00 10.65 ? 139 LYS A CB  1 
ATOM   1315 C CG  . LYS A 1 139 ? 12.990  23.322 -3.143  1.00 12.33 ? 139 LYS A CG  1 
ATOM   1316 C CD  . LYS A 1 139 ? 14.193  24.077 -3.676  1.00 15.21 ? 139 LYS A CD  1 
ATOM   1317 C CE  . LYS A 1 139 ? 14.046  25.576 -3.610  1.00 19.76 ? 139 LYS A CE  1 
ATOM   1318 N NZ  . LYS A 1 139 ? 13.536  26.137 -4.877  1.00 22.52 ? 139 LYS A NZ  1 
ATOM   1319 N N   . ALA A 1 140 ? 11.475  18.957 -3.638  1.00 11.02 ? 140 ALA A N   1 
ATOM   1320 C CA  . ALA A 1 140 ? 11.652  17.510 -3.931  1.00 12.83 ? 140 ALA A CA  1 
ATOM   1321 C C   . ALA A 1 140 ? 12.597  17.429 -5.092  1.00 11.92 ? 140 ALA A C   1 
ATOM   1322 O O   . ALA A 1 140 ? 12.206  17.987 -6.093  1.00 11.44 ? 140 ALA A O   1 
ATOM   1323 C CB  . ALA A 1 140 ? 10.324  16.868 -4.261  1.00 13.63 ? 140 ALA A CB  1 
ATOM   1324 N N   . PRO A 1 141 ? 13.766  16.732 -5.063  1.00 13.18 ? 141 PRO A N   1 
ATOM   1325 C CA  . PRO A 1 141 ? 14.619  16.669 -6.251  1.00 13.65 ? 141 PRO A CA  1 
ATOM   1326 C C   . PRO A 1 141 ? 13.911  16.048 -7.452  1.00 13.53 ? 141 PRO A C   1 
ATOM   1327 O O   . PRO A 1 141 ? 14.290  16.356 -8.557  1.00 15.76 ? 141 PRO A O   1 
ATOM   1328 C CB  . PRO A 1 141 ? 15.804  15.827 -5.787  1.00 15.57 ? 141 PRO A CB  1 
ATOM   1329 C CG  . PRO A 1 141 ? 15.905  16.153 -4.323  1.00 15.87 ? 141 PRO A CG  1 
ATOM   1330 C CD  . PRO A 1 141 ? 14.465  16.220 -3.872  1.00 14.41 ? 141 PRO A CD  1 
ATOM   1331 N N   . GLY A 1 142 ? 12.926  15.183 -7.218  1.00 13.07 ? 142 GLY A N   1 
ATOM   1332 C CA  . GLY A 1 142 ? 12.146  14.564 -8.304  1.00 13.16 ? 142 GLY A CA  1 
ATOM   1333 C C   . GLY A 1 142 ? 11.086  15.483 -8.897  1.00 12.27 ? 142 GLY A C   1 
ATOM   1334 O O   . GLY A 1 142 ? 10.452  15.099 -9.883  1.00 14.85 ? 142 GLY A O   1 
ATOM   1335 N N   . GLY A 1 143 ? 10.878  16.645 -8.294  1.00 11.96 ? 143 GLY A N   1 
ATOM   1336 C CA  . GLY A 1 143 ? 9.900   17.666 -8.724  1.00 12.48 ? 143 GLY A CA  1 
ATOM   1337 C C   . GLY A 1 143 ? 8.855   17.946 -7.641  1.00 11.86 ? 143 GLY A C   1 
ATOM   1338 O O   . GLY A 1 143 ? 8.454   16.993 -6.921  1.00 12.65 ? 143 GLY A O   1 
ATOM   1339 N N   . GLY A 1 144 ? 8.406   19.222 -7.499  1.00 12.20 ? 144 GLY A N   1 
ATOM   1340 C CA  . GLY A 1 144 ? 7.361   19.611 -6.527  1.00 9.07  ? 144 GLY A CA  1 
ATOM   1341 C C   . GLY A 1 144 ? 7.890   20.122 -5.203  1.00 8.48  ? 144 GLY A C   1 
ATOM   1342 O O   . GLY A 1 144 ? 9.082   20.277 -5.016  1.00 11.85 ? 144 GLY A O   1 
ATOM   1343 N N   . CYS A 1 145 ? 6.966   20.341 -4.278  1.00 7.21  ? 145 CYS A N   1 
ATOM   1344 C CA  . CYS A 1 145 ? 7.263   20.887 -2.936  1.00 6.97  ? 145 CYS A CA  1 
ATOM   1345 C C   . CYS A 1 145 ? 6.680   19.916 -1.915  1.00 6.49  ? 145 CYS A C   1 
ATOM   1346 O O   . CYS A 1 145 ? 5.465   19.783 -1.813  1.00 7.22  ? 145 CYS A O   1 
ATOM   1347 C CB  . CYS A 1 145 ? 6.682   22.281 -2.774  1.00 7.84  ? 145 CYS A CB  1 
ATOM   1348 S SG  . CYS A 1 145 ? 7.237   23.151 -1.283  1.00 8.98  ? 145 CYS A SG  1 
ATOM   1349 N N   . ASN A 1 146 ? 7.557   19.202 -1.226  1.00 6.92  ? 146 ASN A N   1 
ATOM   1350 C CA  . ASN A 1 146 ? 7.109   18.212 -0.242  1.00 7.24  ? 146 ASN A CA  1 
ATOM   1351 C C   . ASN A 1 146 ? 6.493   18.878 0.983   1.00 6.94  ? 146 ASN A C   1 
ATOM   1352 O O   . ASN A 1 146 ? 6.911   19.951 1.401   1.00 7.94  ? 146 ASN A O   1 
ATOM   1353 C CB  . ASN A 1 146 ? 8.298   17.412 0.244   1.00 8.43  ? 146 ASN A CB  1 
ATOM   1354 C CG  . ASN A 1 146 ? 8.899   16.445 -0.717  1.00 9.91  ? 146 ASN A CG  1 
ATOM   1355 O OD1 . ASN A 1 146 ? 8.150   15.687 -1.302  1.00 11.69 ? 146 ASN A OD1 1 
ATOM   1356 N ND2 . ASN A 1 146 ? 10.216  16.415 -0.825  1.00 12.25 ? 146 ASN A ND2 1 
ATOM   1357 N N   . ASP A 1 147 ? 5.555   18.160 1.585   1.00 7.46  ? 147 ASP A N   1 
ATOM   1358 C CA  . ASP A 1 147 ? 5.137   18.488 2.950   1.00 7.38  ? 147 ASP A CA  1 
ATOM   1359 C C   . ASP A 1 147 ? 6.227   18.094 3.943   1.00 6.94  ? 147 ASP A C   1 
ATOM   1360 O O   . ASP A 1 147 ? 7.050   17.201 3.696   1.00 7.58  ? 147 ASP A O   1 
ATOM   1361 C CB  . ASP A 1 147 ? 3.827   17.790 3.280   1.00 7.93  ? 147 ASP A CB  1 
ATOM   1362 C CG  . ASP A 1 147 ? 4.037   16.286 3.285   1.00 8.34  ? 147 ASP A CG  1 
ATOM   1363 O OD1 . ASP A 1 147 ? 4.130   15.698 2.182   1.00 8.99  ? 147 ASP A OD1 1 
ATOM   1364 O OD2 . ASP A 1 147 ? 4.178   15.744 4.397   1.00 9.56  ? 147 ASP A OD2 1 
ATOM   1365 N N   . ALA A 1 148 ? 6.174   18.711 5.124   1.00 7.00  ? 148 ALA A N   1 
ATOM   1366 C CA  . ALA A 1 148 ? 7.204   18.466 6.146   1.00 7.23  ? 148 ALA A CA  1 
ATOM   1367 C C   . ALA A 1 148 ? 7.136   17.044 6.708   1.00 7.22  ? 148 ALA A C   1 
ATOM   1368 O O   . ALA A 1 148 ? 8.174   16.524 7.147   1.00 8.61  ? 148 ALA A O   1 
ATOM   1369 C CB  . ALA A 1 148 ? 7.066   19.483 7.256   1.00 7.99  ? 148 ALA A CB  1 
ATOM   1370 N N   . CYS A 1 149 ? 5.970   16.430 6.771   1.00 7.11  ? 149 CYS A N   1 
ATOM   1371 C CA  . CYS A 1 149 ? 5.873   15.038 7.248   1.00 7.89  ? 149 CYS A CA  1 
ATOM   1372 C C   . CYS A 1 149 ? 6.691   14.106 6.358   1.00 7.82  ? 149 CYS A C   1 
ATOM   1373 O O   . CYS A 1 149 ? 7.504   13.319 6.832   1.00 8.64  ? 149 CYS A O   1 
ATOM   1374 C CB  . CYS A 1 149 ? 4.405   14.650 7.367   1.00 9.02  ? 149 CYS A CB  1 
ATOM   1375 S SG  . CYS A 1 149 ? 4.131   12.911 7.737   1.00 10.87 ? 149 CYS A SG  1 
ATOM   1376 N N   . THR A 1 150 ? 6.495   14.233 5.046   1.00 8.05  ? 150 THR A N   1 
ATOM   1377 C CA  . THR A 1 150 ? 7.241   13.435 4.066   1.00 8.42  ? 150 THR A CA  1 
ATOM   1378 C C   . THR A 1 150 ? 8.745   13.604 4.280   1.00 8.32  ? 150 THR A C   1 
ATOM   1379 O O   . THR A 1 150 ? 9.497   12.638 4.194   1.00 10.03 ? 150 THR A O   1 
ATOM   1380 C CB  . THR A 1 150 ? 6.827   13.863 2.653   1.00 9.04  ? 150 THR A CB  1 
ATOM   1381 O OG1 . THR A 1 150 ? 5.463   13.475 2.453   1.00 10.01 ? 150 THR A OG1 1 
ATOM   1382 C CG2 . THR A 1 150 ? 7.696   13.255 1.577   1.00 12.21 ? 150 THR A CG2 1 
ATOM   1383 N N   . VAL A 1 151 ? 9.185   14.835 4.504   1.00 7.81  ? 151 VAL A N   1 
ATOM   1384 C CA  . VAL A 1 151 ? 10.633  15.103 4.588   1.00 8.19  ? 151 VAL A CA  1 
ATOM   1385 C C   . VAL A 1 151 ? 11.211  14.597 5.917   1.00 8.18  ? 151 VAL A C   1 
ATOM   1386 O O   . VAL A 1 151 ? 12.287  14.007 5.914   1.00 9.72  ? 151 VAL A O   1 
ATOM   1387 C CB  . VAL A 1 151 ? 10.937  16.582 4.349   1.00 8.30  ? 151 VAL A CB  1 
ATOM   1388 C CG1 . VAL A 1 151 ? 12.408  16.870 4.490   1.00 8.98  ? 151 VAL A CG1 1 
ATOM   1389 C CG2 . VAL A 1 151 ? 10.437  16.994 2.968   1.00 9.06  ? 151 VAL A CG2 1 
ATOM   1390 N N   . PHE A 1 152 ? 10.557  14.897 7.030   1.00 8.15  ? 152 PHE A N   1 
ATOM   1391 C CA  . PHE A 1 152 ? 11.208  14.761 8.351   1.00 8.18  ? 152 PHE A CA  1 
ATOM   1392 C C   . PHE A 1 152 ? 10.636  13.657 9.232   1.00 8.43  ? 152 PHE A C   1 
ATOM   1393 O O   . PHE A 1 152 ? 11.301  13.287 10.204  1.00 9.48  ? 152 PHE A O   1 
ATOM   1394 C CB  . PHE A 1 152 ? 11.134  16.094 9.092   1.00 8.42  ? 152 PHE A CB  1 
ATOM   1395 C CG  . PHE A 1 152 ? 11.927  17.177 8.420   1.00 8.72  ? 152 PHE A CG  1 
ATOM   1396 C CD1 . PHE A 1 152 ? 13.315  17.133 8.439   1.00 9.11  ? 152 PHE A CD1 1 
ATOM   1397 C CD2 . PHE A 1 152 ? 11.296  18.218 7.746   1.00 8.63  ? 152 PHE A CD2 1 
ATOM   1398 C CE1 . PHE A 1 152 ? 14.060  18.129 7.830   1.00 10.19 ? 152 PHE A CE1 1 
ATOM   1399 C CE2 . PHE A 1 152 ? 12.044  19.203 7.123   1.00 9.54  ? 152 PHE A CE2 1 
ATOM   1400 C CZ  . PHE A 1 152 ? 13.421  19.158 7.174   1.00 10.14 ? 152 PHE A CZ  1 
ATOM   1401 N N   . GLN A 1 153 ? 9.426   13.165 8.970   1.00 8.00  ? 153 GLN A N   1 
ATOM   1402 C CA  . GLN A 1 153 ? 8.888   11.958 9.648   1.00 7.98  ? 153 GLN A CA  1 
ATOM   1403 C C   . GLN A 1 153 ? 8.863   12.148 11.175  1.00 7.47  ? 153 GLN A C   1 
ATOM   1404 O O   . GLN A 1 153 ? 9.256   11.244 11.914  1.00 8.48  ? 153 GLN A O   1 
ATOM   1405 C CB  . GLN A 1 153 ? 9.680   10.713 9.259   1.00 9.46  ? 153 GLN A CB  1 
ATOM   1406 C CG  . GLN A 1 153 ? 9.617   10.371 7.771   1.00 11.28 ? 153 GLN A CG  1 
ATOM   1407 C CD  . GLN A 1 153 ? 8.323   9.686  7.422   1.00 11.69 ? 153 GLN A CD  1 
ATOM   1408 O OE1 . GLN A 1 153 ? 8.195   8.474  7.592   1.00 13.62 ? 153 GLN A OE1 1 
ATOM   1409 N NE2 . GLN A 1 153 ? 7.343   10.431 6.920   1.00 13.36 ? 153 GLN A NE2 1 
ATOM   1410 N N   . THR A 1 154 ? 8.337   13.272 11.629  1.00 8.14  ? 154 THR A N   1 
ATOM   1411 C CA  . THR A 1 154 ? 8.156   13.535 13.057  1.00 7.68  ? 154 THR A CA  1 
ATOM   1412 C C   . THR A 1 154 ? 6.693   13.455 13.426  1.00 7.08  ? 154 THR A C   1 
ATOM   1413 O O   . THR A 1 154 ? 5.793   13.727 12.631  1.00 7.39  ? 154 THR A O   1 
ATOM   1414 C CB  . THR A 1 154 ? 8.718   14.889 13.502  1.00 7.91  ? 154 THR A CB  1 
ATOM   1415 O OG1 . THR A 1 154 ? 7.890   15.901 12.936  1.00 8.10  ? 154 THR A OG1 1 
ATOM   1416 C CG2 . THR A 1 154 ? 10.162  15.094 13.112  1.00 9.16  ? 154 THR A CG2 1 
ATOM   1417 N N   . SER A 1 155 ? 6.460   13.182 14.716  1.00 7.10  ? 155 SER A N   1 
ATOM   1418 C CA  . SER A 1 155 ? 5.091   13.183 15.233  1.00 7.76  ? 155 SER A CA  1 
ATOM   1419 C C   . SER A 1 155 ? 4.446   14.555 15.032  1.00 7.29  ? 155 SER A C   1 
ATOM   1420 O O   . SER A 1 155 ? 3.242   14.634 14.769  1.00 8.56  ? 155 SER A O   1 
ATOM   1421 C CB  . SER A 1 155 ? 5.119   12.835 16.707  1.00 8.93  ? 155 SER A CB  1 
ATOM   1422 O OG  . SER A 1 155 ? 5.545   11.509 16.948  1.00 13.52 ? 155 SER A OG  1 
ATOM   1423 N N   . GLU A 1 156 ? 5.213   15.631 15.179  1.00 6.89  ? 156 GLU A N   1 
ATOM   1424 C CA  . GLU A 1 156 ? 4.649   16.983 15.071  1.00 7.13  ? 156 GLU A CA  1 
ATOM   1425 C C   . GLU A 1 156 ? 4.169   17.265 13.647  1.00 7.20  ? 156 GLU A C   1 
ATOM   1426 O O   . GLU A 1 156 ? 3.091   17.817 13.461  1.00 9.04  ? 156 GLU A O   1 
ATOM   1427 C CB  . GLU A 1 156 ? 5.675   18.024 15.501  1.00 7.69  ? 156 GLU A CB  1 
ATOM   1428 C CG  . GLU A 1 156 ? 5.056   19.387 15.678  1.00 8.72  ? 156 GLU A CG  1 
ATOM   1429 C CD  . GLU A 1 156 ? 4.033   19.471 16.804  1.00 8.79  ? 156 GLU A CD  1 
ATOM   1430 O OE1 . GLU A 1 156 ? 4.003   18.553 17.651  1.00 9.50  ? 156 GLU A OE1 1 
ATOM   1431 O OE2 . GLU A 1 156 ? 3.292   20.481 16.851  1.00 10.29 ? 156 GLU A OE2 1 
ATOM   1432 N N   . TYR A 1 157 ? 4.957   16.905 12.646  1.00 7.06  ? 157 TYR A N   1 
ATOM   1433 C CA  . TYR A 1 157 ? 4.548   17.213 11.264  1.00 7.23  ? 157 TYR A CA  1 
ATOM   1434 C C   . TYR A 1 157 ? 3.484   16.252 10.769  1.00 7.79  ? 157 TYR A C   1 
ATOM   1435 O O   . TYR A 1 157 ? 2.667   16.634 9.928   1.00 9.49  ? 157 TYR A O   1 
ATOM   1436 C CB  . TYR A 1 157 ? 5.739   17.143 10.312  1.00 7.41  ? 157 TYR A CB  1 
ATOM   1437 C CG  . TYR A 1 157 ? 6.789   18.188 10.565  1.00 7.63  ? 157 TYR A CG  1 
ATOM   1438 C CD1 . TYR A 1 157 ? 6.477   19.522 10.800  1.00 8.03  ? 157 TYR A CD1 1 
ATOM   1439 C CD2 . TYR A 1 157 ? 8.124   17.855 10.494  1.00 7.74  ? 157 TYR A CD2 1 
ATOM   1440 C CE1 . TYR A 1 157 ? 7.468   20.464 11.028  1.00 8.32  ? 157 TYR A CE1 1 
ATOM   1441 C CE2 . TYR A 1 157 ? 9.122   18.786 10.693  1.00 7.67  ? 157 TYR A CE2 1 
ATOM   1442 C CZ  . TYR A 1 157 ? 8.793   20.097 10.997  1.00 7.93  ? 157 TYR A CZ  1 
ATOM   1443 O OH  . TYR A 1 157 ? 9.738   21.048 11.264  1.00 8.24  ? 157 TYR A OH  1 
ATOM   1444 N N   . CYS A 1 158 ? 3.544   15.011 11.223  1.00 8.26  ? 158 CYS A N   1 
ATOM   1445 C CA  . CYS A 1 158 ? 2.659   13.958 10.728  1.00 9.08  ? 158 CYS A CA  1 
ATOM   1446 C C   . CYS A 1 158 ? 1.361   13.924 11.546  1.00 10.23 ? 158 CYS A C   1 
ATOM   1447 O O   . CYS A 1 158 ? 0.451   13.229 11.178  1.00 12.19 ? 158 CYS A O   1 
ATOM   1448 C CB  . CYS A 1 158 ? 3.419   12.644 10.704  1.00 9.94  ? 158 CYS A CB  1 
ATOM   1449 S SG  . CYS A 1 158 ? 4.908   12.675 9.639   1.00 10.20 ? 158 CYS A SG  1 
ATOM   1450 N N   . CYS A 1 159 ? 1.331   14.621 12.688  1.00 11.28 ? 159 CYS A N   1 
ATOM   1451 C CA  A CYS A 1 159 ? 0.159   14.716 13.601  0.40 11.95 ? 159 CYS A CA  1 
ATOM   1452 C CA  B CYS A 1 159 ? 0.174   14.696 13.605  0.60 12.24 ? 159 CYS A CA  1 
ATOM   1453 C C   . CYS A 1 159 ? -0.215  13.311 14.103  1.00 12.15 ? 159 CYS A C   1 
ATOM   1454 O O   . CYS A 1 159 ? -1.381  13.039 14.300  1.00 15.44 ? 159 CYS A O   1 
ATOM   1455 C CB  A CYS A 1 159 ? -0.982  15.484 12.940  0.40 12.34 ? 159 CYS A CB  1 
ATOM   1456 C CB  B CYS A 1 159 ? -1.007  15.415 12.995  0.60 14.81 ? 159 CYS A CB  1 
ATOM   1457 S SG  A CYS A 1 159 ? -0.559  17.207 12.539  0.40 14.34 ? 159 CYS A SG  1 
ATOM   1458 S SG  B CYS A 1 159 ? -1.838  16.337 14.303  0.60 18.99 ? 159 CYS A SG  1 
ATOM   1459 N N   . THR A 1 160 ? 0.779   12.500 14.375  1.00 11.93 ? 160 THR A N   1 
ATOM   1460 C CA  . THR A 1 160 ? 0.639   11.065 14.635  1.00 13.09 ? 160 THR A CA  1 
ATOM   1461 C C   . THR A 1 160 ? -0.309  10.798 15.779  1.00 15.37 ? 160 THR A C   1 
ATOM   1462 O O   . THR A 1 160 ? -1.102  9.863  15.668  1.00 21.11 ? 160 THR A O   1 
ATOM   1463 C CB  . THR A 1 160 ? 2.031   10.532 14.939  1.00 14.11 ? 160 THR A CB  1 
ATOM   1464 O OG1 . THR A 1 160 ? 2.878   10.860 13.853  1.00 13.68 ? 160 THR A OG1 1 
ATOM   1465 C CG2 . THR A 1 160 ? 2.021   9.048  15.163  1.00 15.37 ? 160 THR A CG2 1 
ATOM   1466 N N   A THR A 1 161 ? -0.297  11.601 16.824  0.50 15.16 ? 161 THR A N   1 
ATOM   1467 N N   B THR A 1 161 ? -0.075  11.579 16.858  0.50 17.26 ? 161 THR A N   1 
ATOM   1468 C CA  A THR A 1 161 ? -1.202  11.319 17.961  0.50 15.46 ? 161 THR A CA  1 
ATOM   1469 C CA  B THR A 1 161 ? -0.682  11.502 18.221  0.50 21.46 ? 161 THR A CA  1 
ATOM   1470 C C   A THR A 1 161 ? -2.417  12.247 17.940  0.50 16.74 ? 161 THR A C   1 
ATOM   1471 C C   B THR A 1 161 ? -1.983  12.307 18.313  0.50 23.27 ? 161 THR A C   1 
ATOM   1472 O O   A THR A 1 161 ? -3.239  12.124 18.844  0.50 17.49 ? 161 THR A O   1 
ATOM   1473 O O   B THR A 1 161 ? -2.613  12.280 19.389  0.50 28.65 ? 161 THR A O   1 
ATOM   1474 C CB  A THR A 1 161 ? -0.426  11.407 19.272  0.50 15.68 ? 161 THR A CB  1 
ATOM   1475 C CB  B THR A 1 161 ? 0.150   12.158 19.340  0.50 24.56 ? 161 THR A CB  1 
ATOM   1476 O OG1 A THR A 1 161 ? 0.066   12.744 19.347  0.50 18.55 ? 161 THR A OG1 1 
ATOM   1477 O OG1 B THR A 1 161 ? 0.002   13.577 19.250  0.50 27.00 ? 161 THR A OG1 1 
ATOM   1478 C CG2 A THR A 1 161 ? 0.711   10.411 19.337  0.50 18.05 ? 161 THR A CG2 1 
ATOM   1479 C CG2 B THR A 1 161 ? 1.622   11.808 19.344  0.50 23.53 ? 161 THR A CG2 1 
ATOM   1480 N N   A GLY A 1 162 ? -2.511  13.149 16.965  0.50 18.07 ? 162 GLY A N   1 
ATOM   1481 N N   B GLY A 1 162 ? -2.314  13.067 17.266  0.50 26.20 ? 162 GLY A N   1 
ATOM   1482 C CA  A GLY A 1 162 ? -3.636  14.090 16.833  0.50 21.57 ? 162 GLY A CA  1 
ATOM   1483 C CA  B GLY A 1 162 ? -3.560  13.852 17.152  0.50 26.53 ? 162 GLY A CA  1 
ATOM   1484 C C   A GLY A 1 162 ? -3.532  15.312 17.737  0.50 23.29 ? 162 GLY A C   1 
ATOM   1485 C C   B GLY A 1 162 ? -3.525  15.160 17.930  0.50 26.93 ? 162 GLY A C   1 
ATOM   1486 O O   A GLY A 1 162 ? -4.580  15.929 17.938  0.50 26.50 ? 162 GLY A O   1 
ATOM   1487 O O   B GLY A 1 162 ? -4.620  15.647 18.268  0.50 30.17 ? 162 GLY A O   1 
ATOM   1488 N N   . LYS A 1 163 ? -2.341  15.734 18.192  1.00 28.34 ? 163 LYS A N   1 
ATOM   1489 C CA  . LYS A 1 163 ? -2.205  16.962 19.050  1.00 29.28 ? 163 LYS A CA  1 
ATOM   1490 C C   . LYS A 1 163 ? -1.368  18.123 18.477  1.00 24.80 ? 163 LYS A C   1 
ATOM   1491 O O   . LYS A 1 163 ? -1.131  19.123 19.165  1.00 29.60 ? 163 LYS A O   1 
ATOM   1492 C CB  . LYS A 1 163 ? -1.565  16.550 20.374  1.00 34.06 ? 163 LYS A CB  1 
ATOM   1493 C CG  . LYS A 1 163 ? -2.322  15.487 21.158  1.00 35.23 ? 163 LYS A CG  1 
ATOM   1494 C CD  . LYS A 1 163 ? -1.493  14.841 22.244  1.00 40.66 ? 163 LYS A CD  1 
ATOM   1495 C CE  . LYS A 1 163 ? -0.910  15.834 23.231  1.00 42.09 ? 163 LYS A CE  1 
ATOM   1496 N NZ  . LYS A 1 163 ? 0.332   16.475 22.731  1.00 43.14 ? 163 LYS A NZ  1 
ATOM   1497 N N   . CYS A 1 164 ? -0.931  18.017 17.254  1.00 19.07 ? 164 CYS A N   1 
ATOM   1498 C CA  . CYS A 1 164 ? 0.118   18.869 16.677  1.00 13.90 ? 164 CYS A CA  1 
ATOM   1499 C C   . CYS A 1 164 ? -0.389  20.294 16.529  1.00 13.08 ? 164 CYS A C   1 
ATOM   1500 O O   . CYS A 1 164 ? -1.625  20.539 16.570  1.00 19.42 ? 164 CYS A O   1 
ATOM   1501 C CB  . CYS A 1 164 ? 0.440   18.279 15.314  1.00 12.95 ? 164 CYS A CB  1 
ATOM   1502 S SG  . CYS A 1 164 ? -0.998  18.260 14.204  1.00 16.79 ? 164 CYS A SG  1 
ATOM   1503 N N   . GLY A 1 165 ? 0.528   21.197 16.254  1.00 10.94 ? 165 GLY A N   1 
ATOM   1504 C CA  . GLY A 1 165 ? 0.185   22.571 15.897  1.00 10.46 ? 165 GLY A CA  1 
ATOM   1505 C C   . GLY A 1 165 ? 0.682   22.923 14.506  1.00 8.62  ? 165 GLY A C   1 
ATOM   1506 O O   . GLY A 1 165 ? 1.380   22.150 13.852  1.00 9.40  ? 165 GLY A O   1 
ATOM   1507 N N   . PRO A 1 166 ? 0.375   24.154 14.072  1.00 7.97  ? 166 PRO A N   1 
ATOM   1508 C CA  . PRO A 1 166 ? 0.988   24.690 12.866  1.00 7.80  ? 166 PRO A CA  1 
ATOM   1509 C C   . PRO A 1 166 ? 2.498   24.815 13.062  1.00 7.26  ? 166 PRO A C   1 
ATOM   1510 O O   . PRO A 1 166 ? 2.989   24.897 14.200  1.00 8.08  ? 166 PRO A O   1 
ATOM   1511 C CB  . PRO A 1 166 ? 0.315   26.050 12.699  1.00 9.48  ? 166 PRO A CB  1 
ATOM   1512 C CG  . PRO A 1 166 ? -0.121  26.436 14.072  1.00 12.09 ? 166 PRO A CG  1 
ATOM   1513 C CD  . PRO A 1 166 ? -0.421  25.155 14.794  1.00 9.22  ? 166 PRO A CD  1 
ATOM   1514 N N   . THR A 1 167 ? 3.207   24.859 11.950  1.00 7.25  ? 167 THR A N   1 
ATOM   1515 C CA  . THR A 1 167 ? 4.663   24.858 11.945  1.00 7.26  ? 167 THR A CA  1 
ATOM   1516 C C   . THR A 1 167 ? 5.160   25.917 10.963  1.00 7.27  ? 167 THR A C   1 
ATOM   1517 O O   . THR A 1 167 ? 4.393   26.432 10.127  1.00 7.27  ? 167 THR A O   1 
ATOM   1518 C CB  . THR A 1 167 ? 5.209   23.475 11.581  1.00 7.25  ? 167 THR A CB  1 
ATOM   1519 O OG1 . THR A 1 167 ? 4.879   23.184 10.219  1.00 7.87  ? 167 THR A OG1 1 
ATOM   1520 C CG2 . THR A 1 167 ? 4.665   22.400 12.506  1.00 7.61  ? 167 THR A CG2 1 
ATOM   1521 N N   . GLU A 1 168 ? 6.455   26.190 10.965  1.00 7.28  ? 168 GLU A N   1 
ATOM   1522 C CA  . GLU A 1 168 ? 6.982   27.125 9.963   1.00 7.68  ? 168 GLU A CA  1 
ATOM   1523 C C   . GLU A 1 168 ? 6.670   26.593 8.558   1.00 7.30  ? 168 GLU A C   1 
ATOM   1524 O O   . GLU A 1 168 ? 6.319   27.364 7.651   1.00 8.30  ? 168 GLU A O   1 
ATOM   1525 C CB  . GLU A 1 168 ? 8.474   27.321 10.176  1.00 10.14 ? 168 GLU A CB  1 
ATOM   1526 C CG  . GLU A 1 168 ? 9.014   28.562 9.502   1.00 14.15 ? 168 GLU A CG  1 
ATOM   1527 C CD  . GLU A 1 168 ? 10.390  29.075 9.950   1.00 21.26 ? 168 GLU A CD  1 
ATOM   1528 O OE1 . GLU A 1 168 ? 11.194  29.476 9.073   1.00 27.29 ? 168 GLU A OE1 1 
ATOM   1529 O OE2 . GLU A 1 168 ? 10.655  29.158 11.170  1.00 31.34 ? 168 GLU A OE2 1 
ATOM   1530 N N   . TYR A 1 169 ? 6.794   25.290 8.362   1.00 6.97  ? 169 TYR A N   1 
ATOM   1531 C CA  . TYR A 1 169 ? 6.516   24.690 7.037   1.00 7.05  ? 169 TYR A CA  1 
ATOM   1532 C C   . TYR A 1 169 ? 5.030   24.755 6.700   1.00 6.95  ? 169 TYR A C   1 
ATOM   1533 O O   . TYR A 1 169 ? 4.679   25.135 5.565   1.00 7.37  ? 169 TYR A O   1 
ATOM   1534 C CB  . TYR A 1 169 ? 7.039   23.264 6.989   1.00 7.29  ? 169 TYR A CB  1 
ATOM   1535 C CG  . TYR A 1 169 ? 8.540   23.153 7.112   1.00 7.35  ? 169 TYR A CG  1 
ATOM   1536 C CD1 . TYR A 1 169 ? 9.399   23.848 6.274   1.00 8.16  ? 169 TYR A CD1 1 
ATOM   1537 C CD2 . TYR A 1 169 ? 9.116   22.331 8.072   1.00 7.39  ? 169 TYR A CD2 1 
ATOM   1538 C CE1 . TYR A 1 169 ? 10.771  23.724 6.382   1.00 8.52  ? 169 TYR A CE1 1 
ATOM   1539 C CE2 . TYR A 1 169 ? 10.486  22.195 8.199   1.00 7.80  ? 169 TYR A CE2 1 
ATOM   1540 C CZ  . TYR A 1 169 ? 11.318  22.890 7.345   1.00 8.07  ? 169 TYR A CZ  1 
ATOM   1541 O OH  . TYR A 1 169 ? 12.680  22.790 7.422   1.00 9.10  ? 169 TYR A OH  1 
ATOM   1542 N N   . SER A 1 170 ? 4.141   24.382 7.619   1.00 6.79  ? 170 SER A N   1 
ATOM   1543 C CA  . SER A 1 170 ? 2.710   24.433 7.273   1.00 6.83  ? 170 SER A CA  1 
ATOM   1544 C C   . SER A 1 170 ? 2.302   25.867 6.961   1.00 6.62  ? 170 SER A C   1 
ATOM   1545 O O   . SER A 1 170 ? 1.480   26.093 6.053   1.00 7.12  ? 170 SER A O   1 
ATOM   1546 C CB  . SER A 1 170 ? 1.831   23.824 8.344   1.00 6.92  ? 170 SER A CB  1 
ATOM   1547 O OG  . SER A 1 170 ? 1.743   24.629 9.523   1.00 7.31  ? 170 SER A OG  1 
ATOM   1548 N N   . ARG A 1 171 ? 2.861   26.833 7.685   1.00 6.72  ? 171 ARG A N   1 
ATOM   1549 C CA  A ARG A 1 171 ? 2.507   28.248 7.489   0.58 6.95  ? 171 ARG A CA  1 
ATOM   1550 C CA  B ARG A 1 171 ? 2.437   28.231 7.470   0.42 7.03  ? 171 ARG A CA  1 
ATOM   1551 C C   . ARG A 1 171 ? 2.913   28.724 6.094   1.00 6.70  ? 171 ARG A C   1 
ATOM   1552 O O   . ARG A 1 171 ? 2.258   29.624 5.565   1.00 7.42  ? 171 ARG A O   1 
ATOM   1553 C CB  A ARG A 1 171 ? 3.175   29.130 8.539   0.58 7.11  ? 171 ARG A CB  1 
ATOM   1554 C CB  B ARG A 1 171 ? 2.885   29.139 8.617   0.42 7.28  ? 171 ARG A CB  1 
ATOM   1555 C CG  A ARG A 1 171 ? 2.516   29.003 9.906   0.58 7.90  ? 171 ARG A CG  1 
ATOM   1556 C CG  B ARG A 1 171 ? 2.057   28.963 9.887   0.42 7.75  ? 171 ARG A CG  1 
ATOM   1557 C CD  A ARG A 1 171 ? 3.087   30.011 10.888  0.58 8.89  ? 171 ARG A CD  1 
ATOM   1558 C CD  B ARG A 1 171 ? 2.344   30.046 10.927  0.42 8.23  ? 171 ARG A CD  1 
ATOM   1559 N NE  A ARG A 1 171 ? 2.575   29.791 12.234  0.58 10.03 ? 171 ARG A NE  1 
ATOM   1560 N NE  B ARG A 1 171 ? 3.718   29.964 11.399  0.42 8.08  ? 171 ARG A NE  1 
ATOM   1561 C CZ  A ARG A 1 171 ? 3.163   29.059 13.177  0.58 9.46  ? 171 ARG A CZ  1 
ATOM   1562 C CZ  B ARG A 1 171 ? 4.112   29.241 12.439  0.42 8.08  ? 171 ARG A CZ  1 
ATOM   1563 N NH1 A ARG A 1 171 ? 4.344   28.496 12.969  0.58 10.20 ? 171 ARG A NH1 1 
ATOM   1564 N NH1 B ARG A 1 171 ? 3.238   28.629 13.223  0.42 9.72  ? 171 ARG A NH1 1 
ATOM   1565 N NH2 A ARG A 1 171 ? 2.552   28.874 14.334  0.58 10.40 ? 171 ARG A NH2 1 
ATOM   1566 N NH2 B ARG A 1 171 ? 5.401   29.134 12.683  0.42 8.64  ? 171 ARG A NH2 1 
ATOM   1567 N N   . PHE A 1 172 ? 3.972   28.166 5.520   1.00 6.90  ? 172 PHE A N   1 
ATOM   1568 C CA  . PHE A 1 172 ? 4.345   28.492 4.132   1.00 6.90  ? 172 PHE A CA  1 
ATOM   1569 C C   . PHE A 1 172 ? 3.198   28.090 3.184   1.00 6.54  ? 172 PHE A C   1 
ATOM   1570 O O   . PHE A 1 172 ? 2.733   28.900 2.375   1.00 7.04  ? 172 PHE A O   1 
ATOM   1571 C CB  . PHE A 1 172 ? 5.652   27.796 3.756   1.00 7.42  ? 172 PHE A CB  1 
ATOM   1572 C CG  . PHE A 1 172 ? 5.821   27.683 2.263   1.00 7.39  ? 172 PHE A CG  1 
ATOM   1573 C CD1 . PHE A 1 172 ? 6.161   28.777 1.492   1.00 7.88  ? 172 PHE A CD1 1 
ATOM   1574 C CD2 . PHE A 1 172 ? 5.562   26.482 1.626   1.00 8.17  ? 172 PHE A CD2 1 
ATOM   1575 C CE1 . PHE A 1 172 ? 6.221   28.670 0.109   1.00 8.84  ? 172 PHE A CE1 1 
ATOM   1576 C CE2 . PHE A 1 172 ? 5.629   26.370 0.254   1.00 9.19  ? 172 PHE A CE2 1 
ATOM   1577 C CZ  . PHE A 1 172 ? 5.958   27.467 -0.506  1.00 9.22  ? 172 PHE A CZ  1 
ATOM   1578 N N   . PHE A 1 173 ? 2.749   26.845 3.285   1.00 6.54  ? 173 PHE A N   1 
ATOM   1579 C CA  . PHE A 1 173 ? 1.646   26.388 2.415   1.00 6.66  ? 173 PHE A CA  1 
ATOM   1580 C C   . PHE A 1 173 ? 0.408   27.247 2.655   1.00 6.49  ? 173 PHE A C   1 
ATOM   1581 O O   . PHE A 1 173 ? -0.302  27.574 1.694   1.00 7.30  ? 173 PHE A O   1 
ATOM   1582 C CB  . PHE A 1 173 ? 1.338   24.904 2.639   1.00 6.98  ? 173 PHE A CB  1 
ATOM   1583 C CG  . PHE A 1 173 ? 2.387   23.974 2.087   1.00 6.60  ? 173 PHE A CG  1 
ATOM   1584 C CD1 . PHE A 1 173 ? 2.375   23.601 0.758   1.00 7.19  ? 173 PHE A CD1 1 
ATOM   1585 C CD2 . PHE A 1 173 ? 3.401   23.470 2.891   1.00 7.70  ? 173 PHE A CD2 1 
ATOM   1586 C CE1 . PHE A 1 173 ? 3.342   22.743 0.253   1.00 8.30  ? 173 PHE A CE1 1 
ATOM   1587 C CE2 . PHE A 1 173 ? 4.363   22.616 2.395   1.00 8.51  ? 173 PHE A CE2 1 
ATOM   1588 C CZ  . PHE A 1 173 ? 4.332   22.252 1.070   1.00 8.56  ? 173 PHE A CZ  1 
ATOM   1589 N N   . LYS A 1 174 ? 0.124   27.579 3.915   1.00 6.51  ? 174 LYS A N   1 
ATOM   1590 C CA  . LYS A 1 174 ? -1.101  28.315 4.234   1.00 6.97  ? 174 LYS A CA  1 
ATOM   1591 C C   . LYS A 1 174 ? -1.027  29.760 3.739   1.00 6.98  ? 174 LYS A C   1 
ATOM   1592 O O   . LYS A 1 174 ? -2.057  30.342 3.372   1.00 8.24  ? 174 LYS A O   1 
ATOM   1593 C CB  . LYS A 1 174 ? -1.337  28.282 5.740   1.00 7.46  ? 174 LYS A CB  1 
ATOM   1594 C CG  . LYS A 1 174 ? -2.755  28.642 6.134   1.00 8.82  ? 174 LYS A CG  1 
ATOM   1595 C CD  . LYS A 1 174 ? -3.769  27.614 5.540   1.00 9.83  ? 174 LYS A CD  1 
ATOM   1596 C CE  . LYS A 1 174 ? -5.132  27.756 6.170   1.00 10.48 ? 174 LYS A CE  1 
ATOM   1597 N NZ  . LYS A 1 174 ? -6.013  26.713 5.640   1.00 10.77 ? 174 LYS A NZ  1 
ATOM   1598 N N   . ARG A 1 175 ? 0.162   30.355 3.769   1.00 7.05  ? 175 ARG A N   1 
ATOM   1599 C CA  . ARG A 1 175 ? 0.346   31.720 3.260   1.00 7.50  ? 175 ARG A CA  1 
ATOM   1600 C C   . ARG A 1 175 ? 0.101   31.732 1.750   1.00 7.56  ? 175 ARG A C   1 
ATOM   1601 O O   . ARG A 1 175 ? -0.594  32.609 1.220   1.00 9.31  ? 175 ARG A O   1 
ATOM   1602 C CB  . ARG A 1 175 ? 1.751   32.210 3.592   1.00 7.84  ? 175 ARG A CB  1 
ATOM   1603 C CG  . ARG A 1 175 ? 2.050   33.595 3.042   1.00 9.13  ? 175 ARG A CG  1 
ATOM   1604 C CD  . ARG A 1 175 ? 3.364   34.144 3.525   1.00 9.47  ? 175 ARG A CD  1 
ATOM   1605 N NE  . ARG A 1 175 ? 4.513   33.345 3.153   1.00 10.15 ? 175 ARG A NE  1 
ATOM   1606 C CZ  . ARG A 1 175 ? 5.155   33.480 1.977   1.00 10.15 ? 175 ARG A CZ  1 
ATOM   1607 N NH1 . ARG A 1 175 ? 4.714   34.291 1.025   1.00 11.13 ? 175 ARG A NH1 1 
ATOM   1608 N NH2 . ARG A 1 175 ? 6.280   32.815 1.763   1.00 11.68 ? 175 ARG A NH2 1 
ATOM   1609 N N   . LEU A 1 176 ? 0.684   30.783 1.042   1.00 7.50  ? 176 LEU A N   1 
ATOM   1610 C CA  . LEU A 1 176 ? 0.526   30.727 -0.428  1.00 8.37  ? 176 LEU A CA  1 
ATOM   1611 C C   . LEU A 1 176 ? -0.889  30.325 -0.810  1.00 8.05  ? 176 LEU A C   1 
ATOM   1612 O O   . LEU A 1 176 ? -1.392  30.827 -1.836  1.00 9.82  ? 176 LEU A O   1 
ATOM   1613 C CB  . LEU A 1 176 ? 1.580   29.797 -1.028  1.00 9.88  ? 176 LEU A CB  1 
ATOM   1614 C CG  . LEU A 1 176 ? 2.738   30.707 -1.362  1.00 15.07 ? 176 LEU A CG  1 
ATOM   1615 C CD1 . LEU A 1 176 ? 3.638   31.100 -0.242  1.00 12.36 ? 176 LEU A CD1 1 
ATOM   1616 C CD2 . LEU A 1 176 ? 3.359   30.498 -2.657  1.00 16.08 ? 176 LEU A CD2 1 
ATOM   1617 N N   . CYS A 1 177 ? -1.500  29.425 -0.064  1.00 7.89  ? 177 CYS A N   1 
ATOM   1618 C CA  . CYS A 1 177 ? -2.832  28.884 -0.380  1.00 8.32  ? 177 CYS A CA  1 
ATOM   1619 C C   . CYS A 1 177 ? -3.687  28.826 0.872   1.00 8.13  ? 177 CYS A C   1 
ATOM   1620 O O   . CYS A 1 177 ? -3.814  27.785 1.525   1.00 8.98  ? 177 CYS A O   1 
ATOM   1621 C CB  . CYS A 1 177 ? -2.773  27.522 -1.034  1.00 9.79  ? 177 CYS A CB  1 
ATOM   1622 S SG  . CYS A 1 177 ? -2.270  27.642 -2.769  1.00 11.56 ? 177 CYS A SG  1 
ATOM   1623 N N   . PRO A 1 178 ? -4.339  29.939 1.218   1.00 8.48  ? 178 PRO A N   1 
ATOM   1624 C CA  . PRO A 1 178 ? -5.172  29.954 2.414   1.00 9.24  ? 178 PRO A CA  1 
ATOM   1625 C C   . PRO A 1 178 ? -6.338  28.970 2.358   1.00 8.61  ? 178 PRO A C   1 
ATOM   1626 O O   . PRO A 1 178 ? -6.831  28.567 3.400   1.00 9.93  ? 178 PRO A O   1 
ATOM   1627 C CB  . PRO A 1 178 ? -5.661  31.407 2.493   1.00 11.66 ? 178 PRO A CB  1 
ATOM   1628 C CG  . PRO A 1 178 ? -4.618  32.200 1.726   1.00 13.94 ? 178 PRO A CG  1 
ATOM   1629 C CD  . PRO A 1 178 ? -4.156  31.275 0.631   1.00 9.88  ? 178 PRO A CD  1 
ATOM   1630 N N   . ASP A 1 179 ? -6.783  28.618 1.153   1.00 8.61  ? 179 ASP A N   1 
ATOM   1631 C CA  A ASP A 1 179 ? -8.014  27.845 0.924   0.53 9.22  ? 179 ASP A CA  1 
ATOM   1632 C CA  B ASP A 1 179 ? -8.033  27.834 1.032   0.47 9.40  ? 179 ASP A CA  1 
ATOM   1633 C C   . ASP A 1 179 ? -7.745  26.346 0.862   1.00 9.19  ? 179 ASP A C   1 
ATOM   1634 O O   . ASP A 1 179 ? -8.637  25.646 0.387   1.00 13.53 ? 179 ASP A O   1 
ATOM   1635 C CB  A ASP A 1 179 ? -8.654  28.301 -0.382  0.53 11.33 ? 179 ASP A CB  1 
ATOM   1636 C CB  B ASP A 1 179 ? -8.896  28.375 -0.100  0.47 10.39 ? 179 ASP A CB  1 
ATOM   1637 C CG  A ASP A 1 179 ? -10.135 27.999 -0.437  0.53 11.12 ? 179 ASP A CG  1 
ATOM   1638 C CG  B ASP A 1 179 ? -9.456  29.755 0.168   0.47 14.00 ? 179 ASP A CG  1 
ATOM   1639 O OD1 A ASP A 1 179 ? -10.743 27.967 0.648   0.53 12.55 ? 179 ASP A OD1 1 
ATOM   1640 O OD1 B ASP A 1 179 ? -9.540  30.131 1.349   0.47 17.92 ? 179 ASP A OD1 1 
ATOM   1641 O OD2 A ASP A 1 179 ? -10.667 27.852 -1.559  0.53 12.58 ? 179 ASP A OD2 1 
ATOM   1642 O OD2 B ASP A 1 179 ? -9.774  30.449 -0.796  0.47 17.95 ? 179 ASP A OD2 1 
ATOM   1643 N N   . ALA A 1 180 ? -6.577  25.883 1.251   1.00 8.05  ? 180 ALA A N   1 
ATOM   1644 C CA  . ALA A 1 180 ? -6.219  24.457 1.248   1.00 7.85  ? 180 ALA A CA  1 
ATOM   1645 C C   . ALA A 1 180 ? -5.718  24.066 2.631   1.00 7.27  ? 180 ALA A C   1 
ATOM   1646 O O   . ALA A 1 180 ? -5.076  24.865 3.326   1.00 8.06  ? 180 ALA A O   1 
ATOM   1647 C CB  . ALA A 1 180 ? -5.175  24.175 0.198   1.00 8.34  ? 180 ALA A CB  1 
ATOM   1648 N N   . PHE A 1 181 ? -5.935  22.818 3.003   1.00 6.79  ? 181 PHE A N   1 
ATOM   1649 C CA  . PHE A 1 181 ? -5.361  22.269 4.249   1.00 6.90  ? 181 PHE A CA  1 
ATOM   1650 C C   . PHE A 1 181 ? -3.841  22.302 4.172   1.00 6.66  ? 181 PHE A C   1 
ATOM   1651 O O   . PHE A 1 181 ? -3.237  21.798 3.223   1.00 7.19  ? 181 PHE A O   1 
ATOM   1652 C CB  . PHE A 1 181 ? -5.808  20.835 4.485   1.00 7.29  ? 181 PHE A CB  1 
ATOM   1653 C CG  . PHE A 1 181 ? -7.227  20.684 4.985   1.00 7.95  ? 181 PHE A CG  1 
ATOM   1654 C CD1 . PHE A 1 181 ? -8.305  20.681 4.116   1.00 8.98  ? 181 PHE A CD1 1 
ATOM   1655 C CD2 . PHE A 1 181 ? -7.478  20.539 6.341   1.00 9.37  ? 181 PHE A CD2 1 
ATOM   1656 C CE1 . PHE A 1 181 ? -9.597  20.559 4.595   1.00 10.46 ? 181 PHE A CE1 1 
ATOM   1657 C CE2 . PHE A 1 181 ? -8.769  20.401 6.817   1.00 10.79 ? 181 PHE A CE2 1 
ATOM   1658 C CZ  . PHE A 1 181 ? -9.828  20.409 5.943   1.00 11.08 ? 181 PHE A CZ  1 
ATOM   1659 N N   . SER A 1 182 ? -3.225  22.816 5.242   1.00 7.06  ? 182 SER A N   1 
ATOM   1660 C CA  . SER A 1 182 ? -1.758  22.925 5.300   1.00 7.05  ? 182 SER A CA  1 
ATOM   1661 C C   . SER A 1 182 ? -1.121  21.925 6.271   1.00 7.29  ? 182 SER A C   1 
ATOM   1662 O O   . SER A 1 182 ? 0.096   21.710 6.202   1.00 8.08  ? 182 SER A O   1 
ATOM   1663 C CB  . SER A 1 182 ? -1.323  24.342 5.638   1.00 7.29  ? 182 SER A CB  1 
ATOM   1664 O OG  . SER A 1 182 ? -1.711  24.732 6.955   1.00 7.91  ? 182 SER A OG  1 
ATOM   1665 N N   . TYR A 1 183 ? -1.908  21.382 7.182   1.00 8.00  ? 183 TYR A N   1 
ATOM   1666 C CA  . TYR A 1 183 ? -1.460  20.340 8.125   1.00 9.35  ? 183 TYR A CA  1 
ATOM   1667 C C   . TYR A 1 183 ? -2.717  19.641 8.594   1.00 10.06 ? 183 TYR A C   1 
ATOM   1668 O O   . TYR A 1 183 ? -3.840  20.082 8.323   1.00 9.43  ? 183 TYR A O   1 
ATOM   1669 C CB  . TYR A 1 183 ? -0.597  20.909 9.266   1.00 10.35 ? 183 TYR A CB  1 
ATOM   1670 C CG  . TYR A 1 183 ? -1.321  21.722 10.301  1.00 10.24 ? 183 TYR A CG  1 
ATOM   1671 C CD1 . TYR A 1 183 ? -1.739  23.012 10.040  1.00 10.32 ? 183 TYR A CD1 1 
ATOM   1672 C CD2 . TYR A 1 183 ? -1.528  21.197 11.570  1.00 11.76 ? 183 TYR A CD2 1 
ATOM   1673 C CE1 . TYR A 1 183 ? -2.372  23.759 11.011  1.00 11.42 ? 183 TYR A CE1 1 
ATOM   1674 C CE2 . TYR A 1 183 ? -2.166  21.925 12.556  1.00 12.97 ? 183 TYR A CE2 1 
ATOM   1675 C CZ  . TYR A 1 183 ? -2.611  23.205 12.264  1.00 12.58 ? 183 TYR A CZ  1 
ATOM   1676 O OH  . TYR A 1 183 ? -3.226  23.959 13.223  1.00 16.14 ? 183 TYR A OH  1 
ATOM   1677 N N   . VAL A 1 184 ? -2.554  18.540 9.303   1.00 12.56 ? 184 VAL A N   1 
ATOM   1678 C CA  . VAL A 1 184 ? -3.697  17.635 9.563   1.00 13.24 ? 184 VAL A CA  1 
ATOM   1679 C C   . VAL A 1 184 ? -4.778  18.360 10.368  1.00 12.91 ? 184 VAL A C   1 
ATOM   1680 O O   . VAL A 1 184 ? -5.958  18.156 10.093  1.00 13.67 ? 184 VAL A O   1 
ATOM   1681 C CB  . VAL A 1 184 ? -3.207  16.358 10.260  1.00 15.63 ? 184 VAL A CB  1 
ATOM   1682 C CG1 . VAL A 1 184 ? -4.351  15.543 10.836  1.00 17.65 ? 184 VAL A CG1 1 
ATOM   1683 C CG2 . VAL A 1 184 ? -2.388  15.530 9.291   1.00 17.76 ? 184 VAL A CG2 1 
ATOM   1684 N N   . LEU A 1 185 ? -4.395  19.142 11.368  1.00 13.64 ? 185 LEU A N   1 
ATOM   1685 C CA  . LEU A 1 185 ? -5.366  19.818 12.262  1.00 14.35 ? 185 LEU A CA  1 
ATOM   1686 C C   . LEU A 1 185 ? -5.595  21.271 11.877  1.00 13.18 ? 185 LEU A C   1 
ATOM   1687 O O   . LEU A 1 185 ? -6.081  22.039 12.690  1.00 15.73 ? 185 LEU A O   1 
ATOM   1688 C CB  . LEU A 1 185 ? -4.911  19.682 13.716  1.00 17.24 ? 185 LEU A CB  1 
ATOM   1689 C CG  . LEU A 1 185 ? -4.969  18.263 14.266  1.00 20.38 ? 185 LEU A CG  1 
ATOM   1690 C CD1 . LEU A 1 185 ? -4.535  18.256 15.715  1.00 22.74 ? 185 LEU A CD1 1 
ATOM   1691 C CD2 . LEU A 1 185 ? -6.356  17.668 14.094  1.00 22.46 ? 185 LEU A CD2 1 
ATOM   1692 N N   . ASP A 1 186 ? -5.385  21.611 10.618  1.00 11.72 ? 186 ASP A N   1 
ATOM   1693 C CA  . ASP A 1 186 ? -5.668  22.977 10.149  1.00 10.90 ? 186 ASP A CA  1 
ATOM   1694 C C   . ASP A 1 186 ? -7.147  23.280 10.362  1.00 11.42 ? 186 ASP A C   1 
ATOM   1695 O O   . ASP A 1 186 ? -8.008  22.366 10.266  1.00 13.94 ? 186 ASP A O   1 
ATOM   1696 C CB  . ASP A 1 186 ? -5.245  23.109 8.693   1.00 9.82  ? 186 ASP A CB  1 
ATOM   1697 C CG  . ASP A 1 186 ? -4.937  24.509 8.229   1.00 9.71  ? 186 ASP A CG  1 
ATOM   1698 O OD1 . ASP A 1 186 ? -5.159  25.467 8.998   1.00 11.74 ? 186 ASP A OD1 1 
ATOM   1699 O OD2 . ASP A 1 186 ? -4.411  24.604 7.103   1.00 9.66  ? 186 ASP A OD2 1 
ATOM   1700 N N   . LYS A 1 187 ? -7.452  24.554 10.570  1.00 12.50 ? 187 LYS A N   1 
ATOM   1701 C CA  . LYS A 1 187 ? -8.853  25.014 10.554  1.00 13.78 ? 187 LYS A CA  1 
ATOM   1702 C C   . LYS A 1 187 ? -9.454  24.594 9.217   1.00 13.04 ? 187 LYS A C   1 
ATOM   1703 O O   . LYS A 1 187 ? -8.918  24.926 8.161   1.00 12.58 ? 187 LYS A O   1 
ATOM   1704 C CB  . LYS A 1 187 ? -8.926  26.525 10.761  1.00 16.87 ? 187 LYS A CB  1 
ATOM   1705 C CG  . LYS A 1 187 ? -10.330 27.098 10.635  1.00 21.02 ? 187 LYS A CG  1 
ATOM   1706 C CD  . LYS A 1 187 ? -10.400 28.585 10.853  1.00 26.07 ? 187 LYS A CD  1 
ATOM   1707 C CE  . LYS A 1 187 ? -11.798 29.139 10.671  1.00 32.01 ? 187 LYS A CE  1 
ATOM   1708 N NZ  . LYS A 1 187 ? -12.019 30.335 11.516  1.00 37.04 ? 187 LYS A NZ  1 
ATOM   1709 N N   . PRO A 1 188 ? -10.550 23.811 9.199   1.00 13.77 ? 188 PRO A N   1 
ATOM   1710 C CA  . PRO A 1 188 ? -10.997 23.261 7.925   1.00 12.97 ? 188 PRO A CA  1 
ATOM   1711 C C   . PRO A 1 188 ? -11.428 24.309 6.898   1.00 12.15 ? 188 PRO A C   1 
ATOM   1712 O O   . PRO A 1 188 ? -12.034 25.317 7.215   1.00 14.47 ? 188 PRO A O   1 
ATOM   1713 C CB  . PRO A 1 188 ? -12.166 22.351 8.287   1.00 16.02 ? 188 PRO A CB  1 
ATOM   1714 C CG  . PRO A 1 188 ? -11.999 22.047 9.741   1.00 20.39 ? 188 PRO A CG  1 
ATOM   1715 C CD  . PRO A 1 188 ? -11.283 23.241 10.340  1.00 16.69 ? 188 PRO A CD  1 
ATOM   1716 N N   . THR A 1 189 ? -11.124 23.976 5.649   1.00 10.90 ? 189 THR A N   1 
ATOM   1717 C CA  . THR A 1 189 ? -11.531 24.736 4.451   1.00 11.02 ? 189 THR A CA  1 
ATOM   1718 C C   . THR A 1 189 ? -12.405 23.862 3.561   1.00 10.06 ? 189 THR A C   1 
ATOM   1719 O O   . THR A 1 189 ? -12.510 24.105 2.356   1.00 12.77 ? 189 THR A O   1 
ATOM   1720 C CB  . THR A 1 189 ? -10.307 25.252 3.708   1.00 11.54 ? 189 THR A CB  1 
ATOM   1721 O OG1 . THR A 1 189 ? -9.379  24.188 3.589   1.00 11.93 ? 189 THR A OG1 1 
ATOM   1722 C CG2 . THR A 1 189 ? -9.665  26.404 4.443   1.00 12.87 ? 189 THR A CG2 1 
ATOM   1723 N N   . THR A 1 190 ? -13.075 22.898 4.165   1.00 10.25 ? 190 THR A N   1 
ATOM   1724 C CA  . THR A 1 190 ? -14.022 22.014 3.478   1.00 9.69  ? 190 THR A CA  1 
ATOM   1725 C C   . THR A 1 190 ? -15.295 22.778 3.164   1.00 9.82  ? 190 THR A C   1 
ATOM   1726 O O   . THR A 1 190 ? -15.842 23.465 4.020   1.00 13.55 ? 190 THR A O   1 
ATOM   1727 C CB  . THR A 1 190 ? -14.280 20.792 4.341   1.00 10.99 ? 190 THR A CB  1 
ATOM   1728 O OG1 . THR A 1 190 ? -12.996 20.243 4.636   1.00 13.90 ? 190 THR A OG1 1 
ATOM   1729 C CG2 . THR A 1 190 ? -15.164 19.773 3.683   1.00 11.58 ? 190 THR A CG2 1 
ATOM   1730 N N   . VAL A 1 191 ? -15.798 22.570 1.961   1.00 9.15  ? 191 VAL A N   1 
ATOM   1731 C CA  . VAL A 1 191 ? -17.058 23.171 1.495   1.00 9.06  ? 191 VAL A CA  1 
ATOM   1732 C C   . VAL A 1 191 ? -18.128 22.095 1.482   1.00 9.13  ? 191 VAL A C   1 
ATOM   1733 O O   . VAL A 1 191 ? -17.909 20.995 0.960   1.00 9.92  ? 191 VAL A O   1 
ATOM   1734 C CB  . VAL A 1 191 ? -16.862 23.800 0.108   1.00 10.18 ? 191 VAL A CB  1 
ATOM   1735 C CG1 . VAL A 1 191 ? -18.169 24.293 -0.492  1.00 11.63 ? 191 VAL A CG1 1 
ATOM   1736 C CG2 . VAL A 1 191 ? -15.847 24.931 0.177   1.00 12.24 ? 191 VAL A CG2 1 
ATOM   1737 N N   . THR A 1 192 ? -19.305 22.461 1.992   1.00 9.81  ? 192 THR A N   1 
ATOM   1738 C CA  . THR A 1 192 ? -20.485 21.596 1.946   1.00 10.56 ? 192 THR A CA  1 
ATOM   1739 C C   . THR A 1 192 ? -21.264 21.905 0.676   1.00 10.31 ? 192 THR A C   1 
ATOM   1740 O O   . THR A 1 192 ? -21.679 23.045 0.485   1.00 11.81 ? 192 THR A O   1 
ATOM   1741 C CB  . THR A 1 192 ? -21.384 21.824 3.154   1.00 12.31 ? 192 THR A CB  1 
ATOM   1742 O OG1 . THR A 1 192 ? -20.586 21.677 4.324   1.00 13.41 ? 192 THR A OG1 1 
ATOM   1743 C CG2 . THR A 1 192 ? -22.539 20.851 3.169   1.00 13.73 ? 192 THR A CG2 1 
ATOM   1744 N N   . CYS A 1 193 ? -21.494 20.892 -0.135  1.00 10.29 ? 193 CYS A N   1 
ATOM   1745 C CA  . CYS A 1 193 ? -22.286 21.003 -1.369  1.00 10.35 ? 193 CYS A CA  1 
ATOM   1746 C C   . CYS A 1 193 ? -23.524 20.124 -1.235  1.00 10.60 ? 193 CYS A C   1 
ATOM   1747 O O   . CYS A 1 193 ? -23.560 19.158 -0.476  1.00 11.06 ? 193 CYS A O   1 
ATOM   1748 C CB  . CYS A 1 193 ? -21.437 20.589 -2.569  1.00 10.82 ? 193 CYS A CB  1 
ATOM   1749 S SG  . CYS A 1 193 ? -20.123 21.757 -3.011  1.00 13.09 ? 193 CYS A SG  1 
ATOM   1750 N N   . PRO A 1 194 ? -24.560 20.382 -2.050  1.00 11.16 ? 194 PRO A N   1 
ATOM   1751 C CA  . PRO A 1 194 ? -25.704 19.482 -2.098  1.00 12.04 ? 194 PRO A CA  1 
ATOM   1752 C C   . PRO A 1 194 ? -25.253 18.058 -2.399  1.00 10.80 ? 194 PRO A C   1 
ATOM   1753 O O   . PRO A 1 194 ? -24.345 17.854 -3.203  1.00 10.67 ? 194 PRO A O   1 
ATOM   1754 C CB  . PRO A 1 194 ? -26.570 20.041 -3.228  1.00 13.65 ? 194 PRO A CB  1 
ATOM   1755 C CG  . PRO A 1 194 ? -26.243 21.512 -3.202  1.00 13.64 ? 194 PRO A CG  1 
ATOM   1756 C CD  . PRO A 1 194 ? -24.758 21.564 -2.893  1.00 12.36 ? 194 PRO A CD  1 
ATOM   1757 N N   . GLY A 1 195 ? -25.938 17.076 -1.825  1.00 12.08 ? 195 GLY A N   1 
ATOM   1758 C CA  . GLY A 1 195 ? -25.660 15.689 -2.193  1.00 11.70 ? 195 GLY A CA  1 
ATOM   1759 C C   . GLY A 1 195 ? -25.826 15.532 -3.685  1.00 11.38 ? 195 GLY A C   1 
ATOM   1760 O O   . GLY A 1 195 ? -26.748 16.118 -4.284  1.00 12.86 ? 195 GLY A O   1 
ATOM   1761 N N   . SER A 1 196 ? -24.969 14.740 -4.291  1.00 10.43 ? 196 SER A N   1 
ATOM   1762 C CA  . SER A 1 196 ? -25.052 14.407 -5.728  1.00 10.38 ? 196 SER A CA  1 
ATOM   1763 C C   . SER A 1 196 ? -24.759 15.627 -6.609  1.00 9.89  ? 196 SER A C   1 
ATOM   1764 O O   . SER A 1 196 ? -25.244 15.680 -7.750  1.00 10.85 ? 196 SER A O   1 
ATOM   1765 C CB  . SER A 1 196 ? -26.379 13.756 -6.111  1.00 11.44 ? 196 SER A CB  1 
ATOM   1766 O OG  . SER A 1 196 ? -26.539 12.537 -5.424  1.00 13.20 ? 196 SER A OG  1 
ATOM   1767 N N   . SER A 1 197 ? -23.923 16.543 -6.150  1.00 9.28  ? 197 SER A N   1 
ATOM   1768 C CA  . SER A 1 197 ? -23.387 17.594 -7.033  1.00 9.20  ? 197 SER A CA  1 
ATOM   1769 C C   . SER A 1 197 ? -22.444 16.962 -8.064  1.00 8.55  ? 197 SER A C   1 
ATOM   1770 O O   . SER A 1 197 ? -21.975 15.832 -7.902  1.00 9.34  ? 197 SER A O   1 
ATOM   1771 C CB  . SER A 1 197 ? -22.670 18.651 -6.223  1.00 9.21  ? 197 SER A CB  1 
ATOM   1772 O OG  . SER A 1 197 ? -23.548 19.339 -5.335  1.00 10.32 ? 197 SER A OG  1 
ATOM   1773 N N   . ASN A 1 198 ? -22.169 17.723 -9.129  1.00 8.36  ? 198 ASN A N   1 
ATOM   1774 C CA  . ASN A 1 198 ? -21.126 17.360 -10.100 1.00 8.02  ? 198 ASN A CA  1 
ATOM   1775 C C   . ASN A 1 198 ? -20.027 18.414 -10.045 1.00 7.47  ? 198 ASN A C   1 
ATOM   1776 O O   . ASN A 1 198 ? -20.266 19.520 -9.536  1.00 8.09  ? 198 ASN A O   1 
ATOM   1777 C CB  . ASN A 1 198 ? -21.703 17.237 -11.508 1.00 8.86  ? 198 ASN A CB  1 
ATOM   1778 C CG  . ASN A 1 198 ? -22.741 16.145 -11.594 1.00 9.36  ? 198 ASN A CG  1 
ATOM   1779 O OD1 . ASN A 1 198 ? -22.575 15.042 -11.091 1.00 10.01 ? 198 ASN A OD1 1 
ATOM   1780 N ND2 . ASN A 1 198 ? -23.804 16.442 -12.310 1.00 13.35 ? 198 ASN A ND2 1 
ATOM   1781 N N   . TYR A 1 199 ? -18.857 18.086 -10.585 1.00 7.30  ? 199 TYR A N   1 
ATOM   1782 C CA  . TYR A 1 199 ? -17.658 18.894 -10.333 1.00 7.07  ? 199 TYR A CA  1 
ATOM   1783 C C   . TYR A 1 199 ? -16.759 18.992 -11.548 1.00 6.75  ? 199 TYR A C   1 
ATOM   1784 O O   . TYR A 1 199 ? -16.840 18.186 -12.492 1.00 7.28  ? 199 TYR A O   1 
ATOM   1785 C CB  . TYR A 1 199 ? -16.852 18.293 -9.166  1.00 7.48  ? 199 TYR A CB  1 
ATOM   1786 C CG  . TYR A 1 199 ? -17.654 18.155 -7.896  1.00 7.64  ? 199 TYR A CG  1 
ATOM   1787 C CD1 . TYR A 1 199 ? -17.756 19.214 -7.014  1.00 7.68  ? 199 TYR A CD1 1 
ATOM   1788 C CD2 . TYR A 1 199 ? -18.337 16.995 -7.589  1.00 8.18  ? 199 TYR A CD2 1 
ATOM   1789 C CE1 . TYR A 1 199 ? -18.530 19.128 -5.872  1.00 8.30  ? 199 TYR A CE1 1 
ATOM   1790 C CE2 . TYR A 1 199 ? -19.106 16.879 -6.437  1.00 8.85  ? 199 TYR A CE2 1 
ATOM   1791 C CZ  . TYR A 1 199 ? -19.199 17.953 -5.577  1.00 8.37  ? 199 TYR A CZ  1 
ATOM   1792 O OH  . TYR A 1 199 ? -19.933 17.909 -4.418  1.00 9.79  ? 199 TYR A OH  1 
ATOM   1793 N N   . ARG A 1 200 ? -15.843 19.955 -11.462 1.00 6.92  ? 200 ARG A N   1 
ATOM   1794 C CA  . ARG A 1 200 ? -14.731 20.105 -12.411 1.00 6.90  ? 200 ARG A CA  1 
ATOM   1795 C C   . ARG A 1 200 ? -13.456 20.308 -11.608 1.00 6.54  ? 200 ARG A C   1 
ATOM   1796 O O   . ARG A 1 200 ? -13.416 21.174 -10.713 1.00 7.33  ? 200 ARG A O   1 
ATOM   1797 C CB  . ARG A 1 200 ? -14.958 21.275 -13.369 1.00 8.42  ? 200 ARG A CB  1 
ATOM   1798 C CG  . ARG A 1 200 ? -13.809 21.464 -14.356 1.00 9.37  ? 200 ARG A CG  1 
ATOM   1799 C CD  . ARG A 1 200 ? -13.976 22.521 -15.402 1.00 11.84 ? 200 ARG A CD  1 
ATOM   1800 N NE  . ARG A 1 200 ? -14.979 22.128 -16.356 1.00 12.89 ? 200 ARG A NE  1 
ATOM   1801 C CZ  . ARG A 1 200 ? -16.144 22.678 -16.419 1.00 14.61 ? 200 ARG A CZ  1 
ATOM   1802 N NH1 . ARG A 1 200 ? -16.487 23.598 -15.535 1.00 15.09 ? 200 ARG A NH1 1 
ATOM   1803 N NH2 . ARG A 1 200 ? -17.016 22.269 -17.329 1.00 16.87 ? 200 ARG A NH2 1 
ATOM   1804 N N   . VAL A 1 201 ? -12.430 19.557 -11.944 1.00 6.45  ? 201 VAL A N   1 
ATOM   1805 C CA  . VAL A 1 201 ? -11.067 19.754 -11.414 1.00 6.55  ? 201 VAL A CA  1 
ATOM   1806 C C   . VAL A 1 201 ? -10.249 20.321 -12.561 1.00 6.22  ? 201 VAL A C   1 
ATOM   1807 O O   . VAL A 1 201 ? -10.131 19.646 -13.600 1.00 7.39  ? 201 VAL A O   1 
ATOM   1808 C CB  . VAL A 1 201 ? -10.458 18.451 -10.879 1.00 7.41  ? 201 VAL A CB  1 
ATOM   1809 C CG1 . VAL A 1 201 ? -9.028  18.686 -10.438 1.00 8.85  ? 201 VAL A CG1 1 
ATOM   1810 C CG2 . VAL A 1 201 ? -11.287 17.892 -9.734  1.00 9.18  ? 201 VAL A CG2 1 
ATOM   1811 N N   . THR A 1 202 ? -9.706  21.512 -12.386 1.00 6.40  ? 202 THR A N   1 
ATOM   1812 C CA  . THR A 1 202 ? -8.903  22.172 -13.426 1.00 6.42  ? 202 THR A CA  1 
ATOM   1813 C C   . THR A 1 202 ? -7.469  22.291 -12.925 1.00 6.43  ? 202 THR A C   1 
ATOM   1814 O O   . THR A 1 202 ? -7.224  22.962 -11.915 1.00 7.65  ? 202 THR A O   1 
ATOM   1815 C CB  . THR A 1 202 ? -9.440  23.557 -13.777 1.00 7.31  ? 202 THR A CB  1 
ATOM   1816 O OG1 . THR A 1 202 ? -10.827 23.492 -14.105 1.00 8.13  ? 202 THR A OG1 1 
ATOM   1817 C CG2 . THR A 1 202 ? -8.694  24.159 -14.947 1.00 8.39  ? 202 THR A CG2 1 
ATOM   1818 N N   . PHE A 1 203 ? -6.539  21.682 -13.643 1.00 6.33  ? 203 PHE A N   1 
ATOM   1819 C CA  . PHE A 1 203 ? -5.108  21.864 -13.370 1.00 6.41  ? 203 PHE A CA  1 
ATOM   1820 C C   . PHE A 1 203 ? -4.653  23.155 -14.043 1.00 6.37  ? 203 PHE A C   1 
ATOM   1821 O O   . PHE A 1 203 ? -5.039  23.447 -15.184 1.00 6.99  ? 203 PHE A O   1 
ATOM   1822 C CB  . PHE A 1 203 ? -4.303  20.665 -13.865 1.00 6.62  ? 203 PHE A CB  1 
ATOM   1823 C CG  . PHE A 1 203 ? -4.757  19.354 -13.267 1.00 6.91  ? 203 PHE A CG  1 
ATOM   1824 C CD1 . PHE A 1 203 ? -4.708  19.119 -11.906 1.00 8.37  ? 203 PHE A CD1 1 
ATOM   1825 C CD2 . PHE A 1 203 ? -5.201  18.326 -14.089 1.00 8.19  ? 203 PHE A CD2 1 
ATOM   1826 C CE1 . PHE A 1 203 ? -5.142  17.894 -11.389 1.00 9.25  ? 203 PHE A CE1 1 
ATOM   1827 C CE2 . PHE A 1 203 ? -5.610  17.104 -13.589 1.00 9.32  ? 203 PHE A CE2 1 
ATOM   1828 C CZ  . PHE A 1 203 ? -5.585  16.896 -12.233 1.00 9.75  ? 203 PHE A CZ  1 
ATOM   1829 N N   . CYS A 1 204 ? -3.830  23.922 -13.338 1.00 6.81  ? 204 CYS A N   1 
ATOM   1830 C CA  . CYS A 1 204 ? -3.318  25.227 -13.819 1.00 7.43  ? 204 CYS A CA  1 
ATOM   1831 C C   . CYS A 1 204 ? -4.455  26.158 -14.214 1.00 7.50  ? 204 CYS A C   1 
ATOM   1832 O O   . CYS A 1 204 ? -4.524  26.664 -15.336 1.00 8.56  ? 204 CYS A O   1 
ATOM   1833 C CB  . CYS A 1 204 ? -2.312  25.088 -14.959 1.00 8.30  ? 204 CYS A CB  1 
ATOM   1834 S SG  . CYS A 1 204 ? -0.859  24.070 -14.560 1.00 10.05 ? 204 CYS A SG  1 
ATOM   1835 N N   . PRO A 1 205 ? -5.366  26.458 -13.273 1.00 7.54  ? 205 PRO A N   1 
ATOM   1836 C CA  . PRO A 1 205 ? -6.527  27.263 -13.621 1.00 8.81  ? 205 PRO A CA  1 
ATOM   1837 C C   . PRO A 1 205 ? -6.190  28.675 -14.089 1.00 10.34 ? 205 PRO A C   1 
ATOM   1838 O O   . PRO A 1 205 ? -6.986  29.219 -14.840 1.00 13.03 ? 205 PRO A O   1 
ATOM   1839 C CB  . PRO A 1 205 ? -7.369  27.231 -12.342 1.00 9.30  ? 205 PRO A CB  1 
ATOM   1840 C CG  . PRO A 1 205 ? -6.342  27.032 -11.252 1.00 8.51  ? 205 PRO A CG  1 
ATOM   1841 C CD  . PRO A 1 205 ? -5.356  26.048 -11.855 1.00 7.53  ? 205 PRO A CD  1 
ATOM   1842 N N   . THR A 1 206 ? -5.075  29.249 -13.657 1.00 10.97 ? 206 THR A N   1 
ATOM   1843 C CA  . THR A 1 206 ? -4.719  30.628 -14.049 1.00 15.31 ? 206 THR A CA  1 
ATOM   1844 C C   . THR A 1 206 ? -3.799  30.598 -15.277 1.00 21.86 ? 206 THR A C   1 
ATOM   1845 O O   . THR A 1 206 ? -3.659  29.598 -15.992 1.00 24.93 ? 206 THR A O   1 
ATOM   1846 C CB  . THR A 1 206 ? -4.094  31.398 -12.897 1.00 19.16 ? 206 THR A CB  1 
ATOM   1847 O OG1 . THR A 1 206 ? -2.758  30.945 -12.699 1.00 28.66 ? 206 THR A OG1 1 
ATOM   1848 C CG2 . THR A 1 206 ? -4.835  31.213 -11.597 1.00 22.87 ? 206 THR A CG2 1 
HETATM 1849 O O1  . TLA B 2 .   ? 12.131  19.939 11.297  1.00 8.53  ? 301 TLA A O1  1 
HETATM 1850 O O11 . TLA B 2 .   ? 11.628  18.528 12.957  1.00 8.59  ? 301 TLA A O11 1 
HETATM 1851 C C1  . TLA B 2 .   ? 12.371  18.983 12.047  1.00 8.15  ? 301 TLA A C1  1 
HETATM 1852 C C2  . TLA B 2 .   ? 13.706  18.276 11.868  1.00 8.26  ? 301 TLA A C2  1 
HETATM 1853 O O2  . TLA B 2 .   ? 13.689  17.033 12.554  1.00 9.68  ? 301 TLA A O2  1 
HETATM 1854 C C3  . TLA B 2 .   ? 14.839  19.163 12.389  1.00 8.02  ? 301 TLA A C3  1 
HETATM 1855 O O3  . TLA B 2 .   ? 14.631  19.518 13.737  1.00 8.12  ? 301 TLA A O3  1 
HETATM 1856 C C4  . TLA B 2 .   ? 16.153  18.425 12.125  1.00 9.26  ? 301 TLA A C4  1 
HETATM 1857 O O4  . TLA B 2 .   ? 16.528  18.357 10.937  1.00 11.24 ? 301 TLA A O4  1 
HETATM 1858 O O41 . TLA B 2 .   ? 16.734  17.913 13.101  1.00 10.72 ? 301 TLA A O41 1 
HETATM 1859 O O   . HOH C 3 .   ? -15.702 18.007 -21.353 0.90 22.32 ? 401 HOH A O   1 
HETATM 1860 O O   . HOH C 3 .   ? -13.017 26.955 2.022   1.00 24.06 ? 402 HOH A O   1 
HETATM 1861 O O   . HOH C 3 .   ? 8.167   15.738 -19.024 0.90 15.60 ? 403 HOH A O   1 
HETATM 1862 O O   . HOH C 3 .   ? 7.916   16.366 -12.937 1.00 25.06 ? 404 HOH A O   1 
HETATM 1863 O O   . HOH C 3 .   ? -10.885 29.889 2.508   1.00 32.61 ? 405 HOH A O   1 
HETATM 1864 O O   . HOH C 3 .   ? -3.897  15.075 -27.400 1.00 24.39 ? 406 HOH A O   1 
HETATM 1865 O O   . HOH C 3 .   ? 0.655   29.749 14.132  1.00 22.73 ? 407 HOH A O   1 
HETATM 1866 O O   . HOH C 3 .   ? 9.159   13.164 -18.982 1.00 18.59 ? 408 HOH A O   1 
HETATM 1867 O O   . HOH C 3 .   ? 7.236   0.490  -17.893 1.00 25.26 ? 409 HOH A O   1 
HETATM 1868 O O   . HOH C 3 .   ? -2.819  27.962 -17.191 1.00 29.13 ? 410 HOH A O   1 
HETATM 1869 O O   . HOH C 3 .   ? -10.250 29.487 -3.142  1.00 21.77 ? 411 HOH A O   1 
HETATM 1870 O O   . HOH C 3 .   ? 6.706   12.277 -19.407 1.00 15.04 ? 412 HOH A O   1 
HETATM 1871 O O   . HOH C 3 .   ? 9.148   18.632 -14.569 0.90 20.51 ? 413 HOH A O   1 
HETATM 1872 O O   . HOH C 3 .   ? 2.537   -4.646 -16.880 1.00 36.30 ? 414 HOH A O   1 
HETATM 1873 O O   . HOH C 3 .   ? 6.948   5.189  -22.204 1.00 27.00 ? 415 HOH A O   1 
HETATM 1874 O O   . HOH C 3 .   ? -17.039 20.638 -21.234 1.00 14.88 ? 416 HOH A O   1 
HETATM 1875 O O   . HOH C 3 .   ? -2.210  2.083  -8.090  1.00 19.91 ? 417 HOH A O   1 
HETATM 1876 O O   . HOH C 3 .   ? -20.517 6.454  1.977   1.00 29.36 ? 418 HOH A O   1 
HETATM 1877 O O   . HOH C 3 .   ? -20.118 4.117  -3.228  1.00 17.47 ? 419 HOH A O   1 
HETATM 1878 O O   . HOH C 3 .   ? 1.558   6.048  -11.546 1.00 17.89 ? 420 HOH A O   1 
HETATM 1879 O O   . HOH C 3 .   ? 0.988   -1.395 -8.395  1.00 28.35 ? 421 HOH A O   1 
HETATM 1880 O O   . HOH C 3 .   ? -26.420 10.522 1.730   1.00 13.68 ? 422 HOH A O   1 
HETATM 1881 O O   . HOH C 3 .   ? 10.677  31.326 7.415   1.00 17.06 ? 423 HOH A O   1 
HETATM 1882 O O   . HOH C 3 .   ? -3.723  0.638  -18.445 1.00 34.40 ? 424 HOH A O   1 
HETATM 1883 O O   . HOH C 3 .   ? -22.471 26.088 -7.097  1.00 28.63 ? 425 HOH A O   1 
HETATM 1884 O O   . HOH C 3 .   ? -19.178 10.977 6.589   1.00 34.44 ? 426 HOH A O   1 
HETATM 1885 O O   . HOH C 3 .   ? -5.289  -0.557 -12.343 1.00 32.48 ? 427 HOH A O   1 
HETATM 1886 O O   . HOH C 3 .   ? 2.964   -3.102 -13.061 1.00 31.24 ? 428 HOH A O   1 
HETATM 1887 O O   . HOH C 3 .   ? -23.695 15.468 6.247   1.00 24.07 ? 429 HOH A O   1 
HETATM 1888 O O   . HOH C 3 .   ? 6.660   17.858 -11.628 0.74 13.33 ? 430 HOH A O   1 
HETATM 1889 O O   . HOH C 3 .   ? 0.037   2.737  -21.462 1.00 31.01 ? 431 HOH A O   1 
HETATM 1890 O O   . HOH C 3 .   ? -25.177 20.900 -6.758  1.00 14.84 ? 432 HOH A O   1 
HETATM 1891 O O   . HOH C 3 .   ? -22.568 19.478 7.444   1.00 31.06 ? 433 HOH A O   1 
HETATM 1892 O O   . HOH C 3 .   ? -4.249  27.634 10.103  1.00 18.66 ? 434 HOH A O   1 
HETATM 1893 O O   . HOH C 3 .   ? -15.059 11.526 4.514   1.00 30.51 ? 435 HOH A O   1 
HETATM 1894 O O   . HOH C 3 .   ? 4.133   -1.185 -11.437 1.00 23.65 ? 436 HOH A O   1 
HETATM 1895 O O   . HOH C 3 .   ? -2.492  0.655  -15.607 1.00 22.97 ? 437 HOH A O   1 
HETATM 1896 O O   . HOH C 3 .   ? 2.888   24.498 -12.861 1.00 17.19 ? 438 HOH A O   1 
HETATM 1897 O O   . HOH C 3 .   ? -14.880 8.409  -18.956 1.00 32.36 ? 439 HOH A O   1 
HETATM 1898 O O   . HOH C 3 .   ? -17.339 4.327  -4.149  0.90 22.85 ? 440 HOH A O   1 
HETATM 1899 O O   . HOH C 3 .   ? -21.765 8.341  5.655   1.00 29.90 ? 441 HOH A O   1 
HETATM 1900 O O   . HOH C 3 .   ? -1.942  34.773 1.861   1.00 23.12 ? 442 HOH A O   1 
HETATM 1901 O O   . HOH C 3 .   ? -11.890 5.627  0.865   1.00 23.91 ? 443 HOH A O   1 
HETATM 1902 O O   . HOH C 3 .   ? -22.421 16.449 -15.541 0.90 18.55 ? 444 HOH A O   1 
HETATM 1903 O O   . HOH C 3 .   ? -17.086 7.108  -17.240 1.00 27.74 ? 445 HOH A O   1 
HETATM 1904 O O   . HOH C 3 .   ? -17.410 4.742  -12.414 1.00 30.41 ? 446 HOH A O   1 
HETATM 1905 O O   . HOH C 3 .   ? -28.754 16.425 4.366   1.00 35.17 ? 447 HOH A O   1 
HETATM 1906 O O   . HOH C 3 .   ? 9.096   16.515 -11.829 0.90 15.96 ? 448 HOH A O   1 
HETATM 1907 O O   . HOH C 3 .   ? 6.816   3.161  -10.636 1.00 14.19 ? 449 HOH A O   1 
HETATM 1908 O O   . HOH C 3 .   ? -4.333  26.334 12.738  1.00 30.47 ? 450 HOH A O   1 
HETATM 1909 O O   . HOH C 3 .   ? 17.771  16.609 9.355   1.00 23.36 ? 451 HOH A O   1 
HETATM 1910 O O   . HOH C 3 .   ? -17.976 15.623 -20.444 1.00 26.32 ? 452 HOH A O   1 
HETATM 1911 O O   . HOH C 3 .   ? -15.324 28.349 -8.808  1.00 31.42 ? 453 HOH A O   1 
HETATM 1912 O O   . HOH C 3 .   ? 5.327   23.740 -20.308 1.00 28.56 ? 454 HOH A O   1 
HETATM 1913 O O   . HOH C 3 .   ? -22.961 11.518 -5.923  1.00 11.75 ? 455 HOH A O   1 
HETATM 1914 O O   . HOH C 3 .   ? 5.790   32.856 -9.629  1.00 25.03 ? 456 HOH A O   1 
HETATM 1915 O O   . HOH C 3 .   ? -8.343  19.702 10.334  1.00 15.89 ? 457 HOH A O   1 
HETATM 1916 O O   . HOH C 3 .   ? -18.060 22.019 5.177   1.00 22.90 ? 458 HOH A O   1 
HETATM 1917 O O   . HOH C 3 .   ? -24.865 7.473  0.798   1.00 20.76 ? 459 HOH A O   1 
HETATM 1918 O O   . HOH C 3 .   ? -14.652 30.063 -4.246  1.00 27.38 ? 460 HOH A O   1 
HETATM 1919 O O   . HOH C 3 .   ? 11.315  24.411 -6.052  1.00 19.96 ? 461 HOH A O   1 
HETATM 1920 O O   . HOH C 3 .   ? -5.064  15.523 2.951   1.00 15.79 ? 462 HOH A O   1 
HETATM 1921 O O   . HOH C 3 .   ? 0.149   11.812 8.904   1.00 20.69 ? 463 HOH A O   1 
HETATM 1922 O O   . HOH C 3 .   ? 3.299   26.928 16.049  1.00 13.25 ? 464 HOH A O   1 
HETATM 1923 O O   . HOH C 3 .   ? -28.871 12.189 -4.107  1.00 18.14 ? 465 HOH A O   1 
HETATM 1924 O O   . HOH C 3 .   ? -21.745 13.922 -5.900  1.00 10.18 ? 466 HOH A O   1 
HETATM 1925 O O   . HOH C 3 .   ? 7.535   5.999  -8.131  0.90 16.49 ? 467 HOH A O   1 
HETATM 1926 O O   . HOH C 3 .   ? -13.304 1.550  -11.113 1.00 34.17 ? 468 HOH A O   1 
HETATM 1927 O O   . HOH C 3 .   ? -22.019 21.912 6.607   1.00 29.30 ? 469 HOH A O   1 
HETATM 1928 O O   . HOH C 3 .   ? -8.060  27.396 7.457   1.00 17.06 ? 470 HOH A O   1 
HETATM 1929 O O   . HOH C 3 .   ? 4.481   16.097 -17.243 1.00 12.39 ? 471 HOH A O   1 
HETATM 1930 O O   . HOH C 3 .   ? -0.248  26.336 8.847   1.00 8.92  ? 472 HOH A O   1 
HETATM 1931 O O   . HOH C 3 .   ? -10.794 19.983 -23.659 1.00 8.09  ? 473 HOH A O   1 
HETATM 1932 O O   . HOH C 3 .   ? -21.427 25.654 1.179   1.00 19.82 ? 474 HOH A O   1 
HETATM 1933 O O   . HOH C 3 .   ? 8.470   29.786 -10.921 1.00 35.19 ? 475 HOH A O   1 
HETATM 1934 O O   . HOH C 3 .   ? -12.720 6.910  -18.440 1.00 22.10 ? 476 HOH A O   1 
HETATM 1935 O O   . HOH C 3 .   ? -12.481 23.664 -11.846 1.00 8.50  ? 477 HOH A O   1 
HETATM 1936 O O   . HOH C 3 .   ? -16.260 4.515  -5.480  0.90 23.45 ? 478 HOH A O   1 
HETATM 1937 O O   . HOH C 3 .   ? -22.706 9.394  -16.573 1.00 20.11 ? 479 HOH A O   1 
HETATM 1938 O O   . HOH C 3 .   ? 16.905  22.242 -1.794  1.00 32.53 ? 480 HOH A O   1 
HETATM 1939 O O   . HOH C 3 .   ? -12.791 28.400 -7.177  1.00 26.94 ? 481 HOH A O   1 
HETATM 1940 O O   . HOH C 3 .   ? 19.366  17.242 12.868  1.00 28.01 ? 482 HOH A O   1 
HETATM 1941 O O   . HOH C 3 .   ? 3.348   20.944 9.947   1.00 9.38  ? 483 HOH A O   1 
HETATM 1942 O O   . HOH C 3 .   ? 6.189   -0.011 -12.935 1.00 19.56 ? 484 HOH A O   1 
HETATM 1943 O O   . HOH C 3 .   ? -28.101 17.423 -6.264  1.00 26.31 ? 485 HOH A O   1 
HETATM 1944 O O   . HOH C 3 .   ? -11.775 24.632 -16.456 1.00 28.49 ? 486 HOH A O   1 
HETATM 1945 O O   . HOH C 3 .   ? 0.759   7.710  -21.280 1.00 17.30 ? 487 HOH A O   1 
HETATM 1946 O O   . HOH C 3 .   ? 1.509   26.785 -9.208  1.00 13.68 ? 488 HOH A O   1 
HETATM 1947 O O   . HOH C 3 .   ? 2.292   20.563 -24.068 1.00 15.35 ? 489 HOH A O   1 
HETATM 1948 O O   . HOH C 3 .   ? -7.379  5.154  -18.903 1.00 21.22 ? 490 HOH A O   1 
HETATM 1949 O O   . HOH C 3 .   ? -2.048  17.189 -8.209  1.00 7.58  ? 491 HOH A O   1 
HETATM 1950 O O   . HOH C 3 .   ? 15.872  19.156 -2.371  1.00 30.02 ? 492 HOH A O   1 
HETATM 1951 O O   . HOH C 3 .   ? 13.647  21.550 9.673   1.00 8.83  ? 493 HOH A O   1 
HETATM 1952 O O   . HOH C 3 .   ? -1.496  17.286 -0.509  1.00 7.78  ? 494 HOH A O   1 
HETATM 1953 O O   . HOH C 3 .   ? 4.053   25.991 -8.616  1.00 10.41 ? 495 HOH A O   1 
HETATM 1954 O O   . HOH C 3 .   ? -1.247  7.138  15.304  1.00 30.34 ? 496 HOH A O   1 
HETATM 1955 O O   . HOH C 3 .   ? -4.683  12.887 -27.435 1.00 35.69 ? 497 HOH A O   1 
HETATM 1956 O O   . HOH C 3 .   ? 13.723  16.168 -11.246 0.90 18.55 ? 498 HOH A O   1 
HETATM 1957 O O   . HOH C 3 .   ? 1.593   18.154 24.514  1.00 23.37 ? 499 HOH A O   1 
HETATM 1958 O O   . HOH C 3 .   ? 5.435   15.692 -0.244  0.90 21.50 ? 500 HOH A O   1 
HETATM 1959 O O   . HOH C 3 .   ? 3.258   23.931 -24.214 1.00 28.25 ? 501 HOH A O   1 
HETATM 1960 O O   . HOH C 3 .   ? -24.558 13.737 -9.588  1.00 13.37 ? 502 HOH A O   1 
HETATM 1961 O O   . HOH C 3 .   ? -10.148 23.377 0.838   1.00 10.99 ? 503 HOH A O   1 
HETATM 1962 O O   . HOH C 3 .   ? -3.717  31.353 -3.234  1.00 25.51 ? 504 HOH A O   1 
HETATM 1963 O O   . HOH C 3 .   ? 0.622   18.474 -23.719 1.00 12.80 ? 505 HOH A O   1 
HETATM 1964 O O   . HOH C 3 .   ? -1.056  11.521 -2.539  1.00 11.76 ? 506 HOH A O   1 
HETATM 1965 O O   . HOH C 3 .   ? -3.503  22.654 15.650  1.00 23.67 ? 507 HOH A O   1 
HETATM 1966 O O   . HOH C 3 .   ? 6.136   18.117 -16.448 1.00 13.90 ? 508 HOH A O   1 
HETATM 1967 O O   . HOH C 3 .   ? 6.910   11.503 -6.100  1.00 12.17 ? 509 HOH A O   1 
HETATM 1968 O O   . HOH C 3 .   ? 6.775   5.498  -7.003  0.90 19.55 ? 510 HOH A O   1 
HETATM 1969 O O   . HOH C 3 .   ? 5.671   10.751 1.962   1.00 29.52 ? 511 HOH A O   1 
HETATM 1970 O O   . HOH C 3 .   ? -8.836  30.129 4.516   1.00 26.60 ? 512 HOH A O   1 
HETATM 1971 O O   . HOH C 3 .   ? 0.397   8.422  -0.661  1.00 30.40 ? 513 HOH A O   1 
HETATM 1972 O O   . HOH C 3 .   ? -16.514 4.770  -0.273  1.00 20.63 ? 514 HOH A O   1 
HETATM 1973 O O   . HOH C 3 .   ? 2.227   9.534  11.502  0.90 19.32 ? 515 HOH A O   1 
HETATM 1974 O O   . HOH C 3 .   ? 5.206   16.244 18.616  1.00 11.01 ? 516 HOH A O   1 
HETATM 1975 O O   . HOH C 3 .   ? -22.305 9.843  -12.633 1.00 17.29 ? 517 HOH A O   1 
HETATM 1976 O O   . HOH C 3 .   ? -3.136  32.386 4.917   1.00 18.41 ? 518 HOH A O   1 
HETATM 1977 O O   . HOH C 3 .   ? -12.410 28.027 6.718   1.00 30.83 ? 519 HOH A O   1 
HETATM 1978 O O   . HOH C 3 .   ? 13.745  25.273 6.763   1.00 19.24 ? 520 HOH A O   1 
HETATM 1979 O O   . HOH C 3 .   ? -0.753  33.396 -2.688  1.00 21.87 ? 521 HOH A O   1 
HETATM 1980 O O   . HOH C 3 .   ? -18.023 28.222 1.450   1.00 32.54 ? 522 HOH A O   1 
HETATM 1981 O O   . HOH C 3 .   ? -4.011  12.010 -24.052 1.00 22.66 ? 523 HOH A O   1 
HETATM 1982 O O   . HOH C 3 .   ? 16.209  20.510 9.193   1.00 13.01 ? 524 HOH A O   1 
HETATM 1983 O O   . HOH C 3 .   ? -22.671 18.939 -14.156 1.00 18.68 ? 525 HOH A O   1 
HETATM 1984 O O   . HOH C 3 .   ? 12.344  28.548 -7.664  1.00 23.55 ? 526 HOH A O   1 
HETATM 1985 O O   . HOH C 3 .   ? -3.674  4.059  -1.129  1.00 19.33 ? 527 HOH A O   1 
HETATM 1986 O O   . HOH C 3 .   ? 6.396   30.117 7.181   1.00 9.54  ? 528 HOH A O   1 
HETATM 1987 O O   . HOH C 3 .   ? -17.289 10.300 -19.614 1.00 27.41 ? 529 HOH A O   1 
HETATM 1988 O O   . HOH C 3 .   ? -10.452 12.298 0.356   1.00 16.75 ? 530 HOH A O   1 
HETATM 1989 O O   . HOH C 3 .   ? -6.928  16.144 8.407   1.00 27.49 ? 531 HOH A O   1 
HETATM 1990 O O   . HOH C 3 .   ? 15.713  18.661 3.190   1.00 29.47 ? 532 HOH A O   1 
HETATM 1991 O O   . HOH C 3 .   ? 1.800   20.641 4.246   1.00 13.00 ? 533 HOH A O   1 
HETATM 1992 O O   . HOH C 3 .   ? 3.895   4.684  -5.640  1.00 25.65 ? 534 HOH A O   1 
HETATM 1993 O O   . HOH C 3 .   ? -13.985 2.435  -6.331  1.00 28.23 ? 535 HOH A O   1 
HETATM 1994 O O   . HOH C 3 .   ? -13.544 26.123 9.444   1.00 29.49 ? 536 HOH A O   1 
HETATM 1995 O O   . HOH C 3 .   ? -14.925 23.663 6.670   1.00 22.31 ? 537 HOH A O   1 
HETATM 1996 O O   . HOH C 3 .   ? 0.764   31.442 7.105   1.00 10.51 ? 538 HOH A O   1 
HETATM 1997 O O   . HOH C 3 .   ? -13.326 13.657 -22.975 1.00 20.60 ? 539 HOH A O   1 
HETATM 1998 O O   . HOH C 3 .   ? 9.036   14.219 -6.811  1.00 12.61 ? 540 HOH A O   1 
HETATM 1999 O O   . HOH C 3 .   ? 12.684  17.847 0.376   1.00 12.77 ? 541 HOH A O   1 
HETATM 2000 O O   . HOH C 3 .   ? -13.556 21.460 -20.538 1.00 8.13  ? 542 HOH A O   1 
HETATM 2001 O O   . HOH C 3 .   ? -22.339 7.596  3.049   1.00 31.39 ? 543 HOH A O   1 
HETATM 2002 O O   . HOH C 3 .   ? 1.684   14.067 5.050   1.00 16.23 ? 544 HOH A O   1 
HETATM 2003 O O   . HOH C 3 .   ? -14.624 16.003 -21.030 1.00 14.38 ? 545 HOH A O   1 
HETATM 2004 O O   . HOH C 3 .   ? -7.475  24.199 5.840   1.00 12.07 ? 546 HOH A O   1 
HETATM 2005 O O   . HOH C 3 .   ? -3.174  19.548 -9.135  0.55 12.06 ? 547 HOH A O   1 
HETATM 2006 O O   . HOH C 3 .   ? -26.510 17.662 -9.325  1.00 32.33 ? 548 HOH A O   1 
HETATM 2007 O O   . HOH C 3 .   ? 4.832   9.268  -21.509 0.90 14.61 ? 549 HOH A O   1 
HETATM 2008 O O   . HOH C 3 .   ? -11.968 25.844 -15.197 0.90 17.77 ? 550 HOH A O   1 
HETATM 2009 O O   . HOH C 3 .   ? -3.153  10.391 -3.956  1.00 11.90 ? 551 HOH A O   1 
HETATM 2010 O O   . HOH C 3 .   ? 8.936   13.095 -2.138  1.00 14.95 ? 552 HOH A O   1 
HETATM 2011 O O   . HOH C 3 .   ? -5.789  29.072 -1.579  1.00 12.15 ? 553 HOH A O   1 
HETATM 2012 O O   . HOH C 3 .   ? -17.404 25.151 -12.280 1.00 24.18 ? 554 HOH A O   1 
HETATM 2013 O O   . HOH C 3 .   ? 1.789   19.962 12.079  1.00 9.08  ? 555 HOH A O   1 
HETATM 2014 O O   . HOH C 3 .   ? 18.006  15.426 12.548  0.90 24.57 ? 556 HOH A O   1 
HETATM 2015 O O   . HOH C 3 .   ? 4.384   22.950 15.940  1.00 10.25 ? 557 HOH A O   1 
HETATM 2016 O O   . HOH C 3 .   ? 7.221   26.843 -10.692 1.00 27.55 ? 558 HOH A O   1 
HETATM 2017 O O   . HOH C 3 .   ? 4.823   31.849 5.561   1.00 12.36 ? 559 HOH A O   1 
HETATM 2018 O O   . HOH C 3 .   ? 1.180   14.583 16.740  1.00 27.14 ? 560 HOH A O   1 
HETATM 2019 O O   . HOH C 3 .   ? -2.535  28.137 -12.241 1.00 12.53 ? 561 HOH A O   1 
HETATM 2020 O O   . HOH C 3 .   ? -15.816 3.795  -10.401 1.00 22.85 ? 562 HOH A O   1 
HETATM 2021 O O   . HOH C 3 .   ? 3.574   12.376 4.294   1.00 18.95 ? 563 HOH A O   1 
HETATM 2022 O O   . HOH C 3 .   ? 9.945   11.395 -23.534 1.00 18.85 ? 564 HOH A O   1 
HETATM 2023 O O   . HOH C 3 .   ? 11.081  21.628 -6.554  1.00 28.41 ? 565 HOH A O   1 
HETATM 2024 O O   . HOH C 3 .   ? -4.345  29.941 -18.754 1.00 30.50 ? 566 HOH A O   1 
HETATM 2025 O O   . HOH C 3 .   ? 3.382   18.067 7.550   1.00 25.33 ? 567 HOH A O   1 
HETATM 2026 O O   . HOH C 3 .   ? -9.524  7.804  1.679   0.50 22.31 ? 568 HOH A O   1 
HETATM 2027 O O   . HOH C 3 .   ? 0.797   15.706 7.962   1.00 26.88 ? 569 HOH A O   1 
HETATM 2028 O O   . HOH C 3 .   ? -13.726 16.356 1.629   1.00 17.73 ? 570 HOH A O   1 
HETATM 2029 O O   . HOH C 3 .   ? -6.480  11.610 3.561   1.00 28.49 ? 571 HOH A O   1 
HETATM 2030 O O   . HOH C 3 .   ? 7.358   11.115 -1.397  1.00 18.60 ? 572 HOH A O   1 
HETATM 2031 O O   . HOH C 3 .   ? -9.102  9.170  1.671   0.50 20.58 ? 573 HOH A O   1 
HETATM 2032 O O   . HOH C 3 .   ? -27.639 12.510 -1.165  1.00 10.11 ? 574 HOH A O   1 
HETATM 2033 O O   . HOH C 3 .   ? -14.332 11.988 -21.189 1.00 14.55 ? 575 HOH A O   1 
HETATM 2034 O O   . HOH C 3 .   ? -27.596 22.709 -10.462 1.00 30.82 ? 576 HOH A O   1 
HETATM 2035 O O   . HOH C 3 .   ? 3.434   6.984  -21.339 0.90 19.27 ? 577 HOH A O   1 
HETATM 2036 O O   . HOH C 3 .   ? 1.587   17.903 6.117   1.00 18.72 ? 578 HOH A O   1 
HETATM 2037 O O   . HOH C 3 .   ? 9.169   23.856 10.907  1.00 12.38 ? 579 HOH A O   1 
HETATM 2038 O O   . HOH C 3 .   ? 11.553  26.945 7.729   1.00 20.70 ? 580 HOH A O   1 
HETATM 2039 O O   . HOH C 3 .   ? 2.325   35.837 0.512   1.00 24.88 ? 581 HOH A O   1 
HETATM 2040 O O   . HOH C 3 .   ? -5.124  30.096 -5.187  1.00 15.65 ? 582 HOH A O   1 
HETATM 2041 O O   . HOH C 3 .   ? 14.358  25.389 4.027   1.00 18.05 ? 583 HOH A O   1 
HETATM 2042 O O   . HOH C 3 .   ? 9.949   12.683 -4.698  0.90 13.22 ? 584 HOH A O   1 
HETATM 2043 O O   . HOH C 3 .   ? 5.802   19.701 -9.604  1.00 17.24 ? 585 HOH A O   1 
HETATM 2044 O O   . HOH C 3 .   ? -16.716 29.402 -6.496  1.00 31.36 ? 586 HOH A O   1 
HETATM 2045 O O   . HOH C 3 .   ? -16.450 5.357  -8.366  1.00 18.30 ? 587 HOH A O   1 
HETATM 2046 O O   . HOH C 3 .   ? 0.172   17.340 8.614   0.90 20.22 ? 588 HOH A O   1 
HETATM 2047 O O   . HOH C 3 .   ? 3.893   23.690 -10.317 1.00 13.25 ? 589 HOH A O   1 
HETATM 2048 O O   . HOH C 3 .   ? 2.337   32.767 -6.402  1.00 20.93 ? 590 HOH A O   1 
HETATM 2049 O O   . HOH C 3 .   ? -14.378 3.763  -17.126 1.00 36.12 ? 591 HOH A O   1 
HETATM 2050 O O   . HOH C 3 .   ? 9.668   20.879 -9.539  1.00 27.26 ? 592 HOH A O   1 
HETATM 2051 O O   . HOH C 3 .   ? -25.417 28.316 -6.668  1.00 33.38 ? 593 HOH A O   1 
HETATM 2052 O O   . HOH C 3 .   ? 14.383  13.560 -11.688 1.00 13.36 ? 594 HOH A O   1 
HETATM 2053 O O   . HOH C 3 .   ? 4.305   20.925 5.481   1.00 9.43  ? 595 HOH A O   1 
HETATM 2054 O O   . HOH C 3 .   ? -24.138 11.222 -8.279  1.00 13.72 ? 596 HOH A O   1 
HETATM 2055 O O   . HOH C 3 .   ? -12.957 13.581 1.680   1.00 17.88 ? 597 HOH A O   1 
HETATM 2056 O O   . HOH C 3 .   ? -3.941  7.598  -21.246 1.00 14.41 ? 598 HOH A O   1 
HETATM 2057 O O   . HOH C 3 .   ? 1.250   25.706 -17.208 1.00 16.23 ? 599 HOH A O   1 
HETATM 2058 O O   . HOH C 3 .   ? 4.496   17.922 -21.493 1.00 16.07 ? 600 HOH A O   1 
HETATM 2059 O O   . HOH C 3 .   ? 3.616   27.954 -19.590 1.00 35.94 ? 601 HOH A O   1 
HETATM 2060 O O   . HOH C 3 .   ? -9.613  -0.733 -8.569  1.00 24.92 ? 602 HOH A O   1 
HETATM 2061 O O   . HOH C 3 .   ? 2.405   20.359 7.426   0.90 11.68 ? 603 HOH A O   1 
HETATM 2062 O O   . HOH C 3 .   ? -26.407 16.472 6.818   1.00 33.36 ? 604 HOH A O   1 
HETATM 2063 O O   . HOH C 3 .   ? -19.574 25.100 3.275   1.00 18.06 ? 605 HOH A O   1 
HETATM 2064 O O   . HOH C 3 .   ? 4.744   10.158 5.557   0.90 19.23 ? 606 HOH A O   1 
HETATM 2065 O O   . HOH C 3 .   ? 5.294   6.938  -22.250 0.90 27.80 ? 607 HOH A O   1 
HETATM 2066 O O   . HOH C 3 .   ? -2.341  25.300 2.302   1.00 8.56  ? 608 HOH A O   1 
HETATM 2067 O O   . HOH C 3 .   ? -6.732  32.576 -8.759  1.00 29.58 ? 609 HOH A O   1 
HETATM 2068 O O   . HOH C 3 .   ? 12.028  14.357 -1.968  1.00 21.69 ? 610 HOH A O   1 
HETATM 2069 O O   . HOH C 3 .   ? 2.175   5.643  -3.974  1.00 27.59 ? 611 HOH A O   1 
HETATM 2070 O O   . HOH C 3 .   ? -20.878 17.557 8.544   1.00 39.38 ? 612 HOH A O   1 
HETATM 2071 O O   . HOH C 3 .   ? -11.325 9.004  -22.151 1.00 16.47 ? 613 HOH A O   1 
HETATM 2072 O O   . HOH C 3 .   ? 12.401  13.800 -4.628  0.90 13.95 ? 614 HOH A O   1 
HETATM 2073 O O   . HOH C 3 .   ? 0.087   18.000 10.646  1.00 16.54 ? 615 HOH A O   1 
HETATM 2074 O O   . HOH C 3 .   ? 0.805   28.422 16.743  1.00 24.60 ? 616 HOH A O   1 
HETATM 2075 O O   . HOH C 3 .   ? 5.013   33.662 -7.096  1.00 26.94 ? 617 HOH A O   1 
HETATM 2076 O O   . HOH C 3 .   ? -30.066 14.773 5.044   1.00 33.82 ? 618 HOH A O   1 
HETATM 2077 O O   . HOH C 3 .   ? 14.601  28.640 1.000   1.00 20.37 ? 619 HOH A O   1 
HETATM 2078 O O   . HOH C 3 .   ? -29.804 16.880 1.853   1.00 29.57 ? 620 HOH A O   1 
HETATM 2079 O O   . HOH C 3 .   ? -15.056 26.393 3.889   1.00 40.62 ? 621 HOH A O   1 
HETATM 2080 O O   . HOH C 3 .   ? -19.885 3.605  -0.504  1.00 32.07 ? 622 HOH A O   1 
HETATM 2081 O O   . HOH C 3 .   ? 9.503   10.029 14.690  1.00 13.07 ? 623 HOH A O   1 
HETATM 2082 O O   . HOH C 3 .   ? 9.875   5.965  8.042   1.00 14.06 ? 624 HOH A O   1 
HETATM 2083 O O   . HOH C 3 .   ? -20.249 27.448 -0.410  1.00 20.47 ? 625 HOH A O   1 
HETATM 2084 O O   . HOH C 3 .   ? -28.756 14.949 7.327   1.00 33.85 ? 626 HOH A O   1 
HETATM 2085 O O   . HOH C 3 .   ? 7.803   2.967  -18.514 0.90 21.61 ? 627 HOH A O   1 
HETATM 2086 O O   . HOH C 3 .   ? 5.468   34.482 -1.944  1.00 25.47 ? 628 HOH A O   1 
HETATM 2087 O O   . HOH C 3 .   ? 9.296   18.241 -19.154 1.00 18.03 ? 629 HOH A O   1 
HETATM 2088 O O   . HOH C 3 .   ? 13.580  20.625 -6.968  1.00 30.75 ? 630 HOH A O   1 
HETATM 2089 O O   . HOH C 3 .   ? -13.297 27.849 -11.388 1.00 32.88 ? 631 HOH A O   1 
HETATM 2090 O O   . HOH C 3 .   ? 3.114   13.850 -23.447 1.00 34.72 ? 632 HOH A O   1 
HETATM 2091 O O   . HOH C 3 .   ? -3.858  17.478 -27.538 1.00 15.70 ? 633 HOH A O   1 
HETATM 2092 O O   . HOH C 3 .   ? 2.675   9.113  1.491   1.00 32.33 ? 634 HOH A O   1 
HETATM 2093 O O   . HOH C 3 .   ? 2.022   14.290 -25.772 1.00 27.03 ? 635 HOH A O   1 
HETATM 2094 O O   . HOH C 3 .   ? -28.618 18.343 -0.634  1.00 28.37 ? 636 HOH A O   1 
HETATM 2095 O O   . HOH C 3 .   ? -14.114 3.713  0.779   1.00 33.25 ? 637 HOH A O   1 
HETATM 2096 O O   . HOH C 3 .   ? 2.949   14.729 18.789  1.00 28.98 ? 638 HOH A O   1 
HETATM 2097 O O   . HOH C 3 .   ? 0.738   28.636 -10.950 1.00 32.43 ? 639 HOH A O   1 
HETATM 2098 O O   . HOH C 3 .   ? -17.307 26.349 3.868   1.00 33.67 ? 640 HOH A O   1 
HETATM 2099 O O   . HOH C 3 .   ? 11.506  12.846 1.656   1.00 34.24 ? 641 HOH A O   1 
HETATM 2100 O O   . HOH C 3 .   ? 3.993   26.054 -16.863 1.00 27.29 ? 642 HOH A O   1 
HETATM 2101 O O   . HOH C 3 .   ? -14.794 24.894 -13.046 1.00 17.21 ? 643 HOH A O   1 
HETATM 2102 O O   . HOH C 3 .   ? -29.766 12.217 3.887   1.00 13.44 ? 644 HOH A O   1 
HETATM 2103 O O   . HOH C 3 .   ? -10.066 5.399  -19.611 1.00 28.38 ? 645 HOH A O   1 
HETATM 2104 O O   . HOH C 3 .   ? -25.015 22.717 0.681   1.00 35.91 ? 646 HOH A O   1 
HETATM 2105 O O   . HOH C 3 .   ? -7.768  30.864 -4.137  1.00 23.47 ? 647 HOH A O   1 
HETATM 2106 O O   . HOH C 3 .   ? -6.779  31.757 -1.717  1.00 27.73 ? 648 HOH A O   1 
HETATM 2107 O O   . HOH C 3 .   ? 5.692   21.916 -22.232 1.00 33.27 ? 649 HOH A O   1 
HETATM 2108 O O   . HOH C 3 .   ? 4.192   9.545  8.010   1.00 30.25 ? 650 HOH A O   1 
HETATM 2109 O O   . HOH C 3 .   ? -5.076  9.429  -23.421 1.00 28.43 ? 651 HOH A O   1 
HETATM 2110 O O   . HOH C 3 .   ? 17.178  22.298 11.502  1.00 31.35 ? 652 HOH A O   1 
HETATM 2111 O O   . HOH C 3 .   ? 4.672   14.535 -22.051 1.00 28.33 ? 653 HOH A O   1 
HETATM 2112 O O   . HOH C 3 .   ? 0.384   1.235  -4.745  1.00 32.18 ? 654 HOH A O   1 
HETATM 2113 O O   . HOH C 3 .   ? 3.446   10.878 -23.350 1.00 30.18 ? 655 HOH A O   1 
HETATM 2114 O O   . HOH C 3 .   ? -12.033 29.914 -5.196  1.00 26.88 ? 656 HOH A O   1 
HETATM 2115 O O   . HOH C 3 .   ? -2.491  1.550  -21.271 1.00 33.53 ? 657 HOH A O   1 
HETATM 2116 O O   . HOH C 3 .   ? -3.817  -1.600 -14.395 1.00 40.64 ? 658 HOH A O   1 
HETATM 2117 O O   . HOH C 3 .   ? 6.708   1.014  -8.927  1.00 30.47 ? 659 HOH A O   1 
HETATM 2118 O O   . HOH C 3 .   ? 6.456   31.522 9.478   1.00 23.99 ? 660 HOH A O   1 
HETATM 2119 O O   . HOH C 3 .   ? 1.124   28.085 -18.827 1.00 31.16 ? 661 HOH A O   1 
HETATM 2120 O O   . HOH C 3 .   ? -1.060  -0.158 -6.955  1.00 30.13 ? 662 HOH A O   1 
HETATM 2121 O O   . HOH C 3 .   ? -26.876 8.084  -3.235  1.00 14.79 ? 663 HOH A O   1 
HETATM 2122 O O   . HOH C 3 .   ? 13.406  13.361 -3.348  1.00 28.76 ? 664 HOH A O   1 
HETATM 2123 O O   . HOH C 3 .   ? -2.079  10.024 5.526   1.00 35.15 ? 665 HOH A O   1 
HETATM 2124 O O   . HOH C 3 .   ? -13.872 9.262  -21.332 1.00 29.65 ? 666 HOH A O   1 
HETATM 2125 O O   . HOH C 3 .   ? 5.551   15.606 -19.791 1.00 23.06 ? 667 HOH A O   1 
HETATM 2126 O O   . HOH C 3 .   ? 4.597   17.746 -24.176 1.00 27.21 ? 668 HOH A O   1 
HETATM 2127 O O   . HOH C 3 .   ? 7.799   21.314 -10.691 1.00 28.55 ? 669 HOH A O   1 
HETATM 2128 O O   . HOH C 3 .   ? 11.692  25.756 -8.794  1.00 39.65 ? 670 HOH A O   1 
HETATM 2129 O O   . HOH C 3 .   ? -6.456  29.109 9.146   1.00 30.17 ? 671 HOH A O   1 
HETATM 2130 O O   . HOH C 3 .   ? 16.934  19.367 6.439   1.00 26.28 ? 672 HOH A O   1 
HETATM 2131 O O   . HOH C 3 .   ? -28.115 9.554  -1.176  1.00 15.61 ? 673 HOH A O   1 
HETATM 2132 O O   . HOH C 3 .   ? -0.337  32.185 11.159  1.00 36.62 ? 674 HOH A O   1 
HETATM 2133 O O   . HOH C 3 .   ? -17.392 13.612 4.894   1.00 36.79 ? 675 HOH A O   1 
HETATM 2134 O O   . HOH C 3 .   ? 4.174   33.513 9.647   1.00 22.82 ? 676 HOH A O   1 
HETATM 2135 O O   . HOH C 3 .   ? -17.702 3.501  -2.270  1.00 34.52 ? 677 HOH A O   1 
HETATM 2136 O O   . HOH C 3 .   ? 9.792   26.430 -10.474 1.00 35.78 ? 678 HOH A O   1 
HETATM 2137 O O   . HOH C 3 .   ? 2.932   33.189 7.265   1.00 15.62 ? 679 HOH A O   1 
HETATM 2138 O O   . HOH C 3 .   ? 13.872  15.428 0.495   1.00 35.95 ? 680 HOH A O   1 
HETATM 2139 O O   . HOH C 3 .   ? 15.884  20.107 -5.590  1.00 30.72 ? 681 HOH A O   1 
HETATM 2140 O O   . HOH C 3 .   ? -0.917  33.374 6.196   1.00 21.31 ? 682 HOH A O   1 
HETATM 2141 O O   . HOH C 3 .   ? 10.168  27.794 5.543   1.00 18.39 ? 683 HOH A O   1 
HETATM 2142 O O   . HOH C 3 .   ? -21.619 29.626 -1.095  1.00 38.57 ? 684 HOH A O   1 
HETATM 2143 O O   . HOH C 3 .   ? 1.843   33.668 11.228  1.00 29.97 ? 685 HOH A O   1 
HETATM 2144 O O   . HOH C 3 .   ? -27.452 19.762 -7.520  1.00 31.17 ? 686 HOH A O   1 
HETATM 2145 O O   . HOH C 3 .   ? -0.066  -3.763 -9.618  1.00 38.79 ? 687 HOH A O   1 
HETATM 2146 O O   . HOH C 3 .   ? -3.551  11.193 1.735   1.00 26.32 ? 688 HOH A O   1 
HETATM 2147 O O   . HOH C 3 .   ? 3.790   34.079 -4.055  1.00 32.69 ? 689 HOH A O   1 
HETATM 2148 O O   . HOH C 3 .   ? 6.860   9.104  0.152   1.00 32.53 ? 690 HOH A O   1 
HETATM 2149 O O   . HOH C 3 .   ? -9.576  19.627 12.918  1.00 36.29 ? 691 HOH A O   1 
HETATM 2150 O O   . HOH C 3 .   ? -4.341  4.586  1.534   1.00 33.95 ? 692 HOH A O   1 
HETATM 2151 O O   . HOH C 3 .   ? 8.767   30.242 5.817   1.00 13.57 ? 693 HOH A O   1 
HETATM 2152 O O   . HOH C 3 .   ? -1.583  29.362 12.696  1.00 26.63 ? 694 HOH A O   1 
HETATM 2153 O O   . HOH C 3 .   ? 0.022   13.636 7.013   1.00 27.72 ? 695 HOH A O   1 
HETATM 2154 O O   . HOH C 3 .   ? 19.980  15.964 10.696  1.00 31.90 ? 696 HOH A O   1 
HETATM 2155 O O   . HOH C 3 .   ? -16.374 3.191  -6.553  1.00 26.48 ? 697 HOH A O   1 
HETATM 2156 O O   . HOH C 3 .   ? -17.304 12.733 -22.154 1.00 30.99 ? 698 HOH A O   1 
HETATM 2157 O O   . HOH C 3 .   ? 0.258   5.275  -22.125 1.00 29.52 ? 699 HOH A O   1 
HETATM 2158 O O   . HOH C 3 .   ? -0.270  8.718  11.652  1.00 28.06 ? 700 HOH A O   1 
HETATM 2159 O O   . HOH C 3 .   ? -17.293 7.358  -19.820 1.00 38.74 ? 701 HOH A O   1 
HETATM 2160 O O   . HOH C 3 .   ? 14.305  28.171 4.183   1.00 34.00 ? 702 HOH A O   1 
HETATM 2161 O O   . HOH C 3 .   ? -3.639  13.265 3.461   1.00 21.81 ? 703 HOH A O   1 
HETATM 2162 O O   . HOH C 3 .   ? -2.132  10.534 -0.151  1.00 26.54 ? 704 HOH A O   1 
HETATM 2163 O O   . HOH C 3 .   ? 17.325  25.785 4.103   1.00 28.90 ? 705 HOH A O   1 
HETATM 2164 O O   . HOH C 3 .   ? -3.698  35.218 -0.325  1.00 35.41 ? 706 HOH A O   1 
HETATM 2165 O O   . HOH C 3 .   ? -19.786 19.962 8.573   1.00 34.50 ? 707 HOH A O   1 
HETATM 2166 O O   . HOH C 3 .   ? -2.984  24.853 17.487  1.00 38.47 ? 708 HOH A O   1 
HETATM 2167 O O   . HOH C 3 .   ? -21.383 0.106  -1.833  1.00 31.61 ? 709 HOH A O   1 
HETATM 2168 O O   . HOH C 3 .   ? 17.707  18.729 -7.141  1.00 25.49 ? 710 HOH A O   1 
HETATM 2169 O O   . HOH C 3 .   ? -10.555 10.664 3.747   1.00 38.76 ? 711 HOH A O   1 
HETATM 2170 O O   . HOH C 3 .   ? 5.185   25.227 -14.257 1.00 31.39 ? 712 HOH A O   1 
HETATM 2171 O O   . HOH C 3 .   ? -0.140  27.569 -13.803 1.00 30.06 ? 713 HOH A O   1 
HETATM 2172 O O   . HOH C 3 .   ? 7.094   19.769 -18.426 1.00 16.13 ? 714 HOH A O   1 
HETATM 2173 O O   . HOH C 3 .   ? -15.391 21.162 8.249   1.00 27.20 ? 715 HOH A O   1 
HETATM 2174 O O   . HOH C 3 .   ? -3.451  28.138 14.711  1.00 31.81 ? 716 HOH A O   1 
HETATM 2175 O O   . HOH C 3 .   ? -14.478 15.835 4.221   1.00 29.04 ? 717 HOH A O   1 
HETATM 2176 O O   . HOH C 3 .   ? -9.919  29.245 6.883   1.00 26.86 ? 718 HOH A O   1 
HETATM 2177 O O   . HOH C 3 .   ? -17.386 19.930 6.941   1.00 26.46 ? 719 HOH A O   1 
HETATM 2178 O O   . HOH C 3 .   ? 6.511   23.468 -11.201 1.00 28.81 ? 720 HOH A O   1 
HETATM 2179 O O   . HOH C 3 .   ? 11.092  29.119 -10.254 1.00 38.29 ? 721 HOH A O   1 
HETATM 2180 O O   . HOH C 3 .   ? -4.987  33.561 -2.163  1.00 29.13 ? 722 HOH A O   1 
HETATM 2181 O O   . HOH C 3 .   ? -1.614  8.418  0.837   1.00 37.84 ? 723 HOH A O   1 
HETATM 2182 O O   . HOH C 3 .   ? -5.361  31.678 6.429   1.00 36.21 ? 724 HOH A O   1 
HETATM 2183 O O   . HOH C 3 .   ? 18.882  24.135 3.036   1.00 33.49 ? 725 HOH A O   1 
HETATM 2184 O O   . HOH C 3 .   ? -8.106  32.734 4.921   1.00 36.15 ? 726 HOH A O   1 
HETATM 2185 O O   . HOH C 3 .   ? 8.784   33.265 10.199  1.00 29.25 ? 727 HOH A O   1 
HETATM 2186 O O   . HOH C 3 .   ? -5.716  5.519  -21.197 1.00 18.36 ? 728 HOH A O   1 
HETATM 2187 O O   . HOH C 3 .   ? 1.534   9.626  8.040   1.00 29.94 ? 729 HOH A O   1 
HETATM 2188 O O   . HOH C 3 .   ? 10.352  4.242  -18.854 0.90 18.11 ? 730 HOH A O   1 
HETATM 2189 O O   . HOH C 3 .   ? 16.501  28.933 2.852   1.00 20.47 ? 731 HOH A O   1 
HETATM 2190 O O   . HOH C 3 .   ? -1.608  28.329 10.161  1.00 13.40 ? 732 HOH A O   1 
HETATM 2191 O O   . HOH C 3 .   ? -10.721 18.599 9.353   1.00 32.28 ? 733 HOH A O   1 
HETATM 2192 O O   . HOH C 3 .   ? -1.320  30.777 16.289  0.90 13.00 ? 734 HOH A O   1 
HETATM 2193 O O   . HOH C 3 .   ? -0.254  33.866 -5.314  1.00 32.93 ? 735 HOH A O   1 
HETATM 2194 O O   . HOH C 3 .   ? -3.923  34.801 3.823   1.00 31.64 ? 736 HOH A O   1 
HETATM 2195 O O   . HOH C 3 .   ? -10.143 6.533  -22.064 1.00 24.21 ? 737 HOH A O   1 
HETATM 2196 O O   . HOH C 3 .   ? 6.964   22.630 -18.504 1.00 36.62 ? 738 HOH A O   1 
HETATM 2197 O O   . HOH C 3 .   ? -2.543  12.790 6.062   1.00 26.50 ? 739 HOH A O   1 
HETATM 2198 O O   . HOH C 3 .   ? -1.055  30.764 9.058   1.00 17.89 ? 740 HOH A O   1 
HETATM 2199 O O   . HOH C 3 .   ? -7.651  6.250  -22.978 1.00 29.13 ? 741 HOH A O   1 
HETATM 2200 O O   . HOH C 3 .   ? -1.891  27.491 16.902  1.00 31.87 ? 742 HOH A O   1 
HETATM 2201 O O   . HOH C 3 .   ? -5.382  14.005 7.364   1.00 38.63 ? 743 HOH A O   1 
HETATM 2202 O O   . HOH C 3 .   ? -4.506  3.198  -22.032 1.00 31.13 ? 744 HOH A O   1 
HETATM 2203 O O   . HOH C 3 .   ? 18.565  27.867 3.138   1.00 33.79 ? 745 HOH A O   1 
HETATM 2204 O O   . HOH C 3 .   ? 5.436   35.909 10.432  1.00 30.50 ? 746 HOH A O   1 
HETATM 2205 O O   . HOH C 3 .   ? -15.149 9.127  -23.953 1.00 37.00 ? 747 HOH A O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . ALA A 1   ? 0.1624 0.1615 0.0989 -0.0381 -0.0110 0.0046  1   ALA A N   
2    C CA  . ALA A 1   ? 0.1473 0.1566 0.0876 -0.0278 0.0019  0.0132  1   ALA A CA  
3    C C   . ALA A 1   ? 0.1512 0.1503 0.0624 -0.0142 -0.0082 0.0095  1   ALA A C   
4    O O   . ALA A 1   ? 0.1915 0.1779 0.0879 0.0125  0.0143  0.0356  1   ALA A O   
5    C CB  . ALA A 1   ? 0.1829 0.1811 0.0888 -0.0526 0.0294  -0.0173 1   ALA A CB  
6    N N   . THR A 2   ? 0.1257 0.1334 0.0864 -0.0239 -0.0127 0.0076  2   THR A N   
7    C CA  A THR A 2   ? 0.1401 0.1276 0.0601 -0.0171 -0.0113 0.0025  2   THR A CA  
8    C CA  B THR A 2   ? 0.1544 0.1467 0.0674 -0.0289 -0.0067 -0.0003 2   THR A CA  
9    C C   . THR A 2   ? 0.1394 0.1167 0.0460 -0.0146 -0.0071 0.0123  2   THR A C   
10   O O   . THR A 2   ? 0.1404 0.1326 0.0645 -0.0222 0.0076  -0.0048 2   THR A O   
11   C CB  A THR A 2   ? 0.1610 0.1590 0.0648 -0.0076 -0.0278 -0.0060 2   THR A CB  
12   C CB  B THR A 2   ? 0.1943 0.1974 0.0818 -0.0108 -0.0168 0.0150  2   THR A CB  
13   O OG1 A THR A 2   ? 0.1415 0.1728 0.0485 0.0102  -0.0161 0.0063  2   THR A OG1 
14   O OG1 B THR A 2   ? 0.1989 0.2143 0.0791 -0.0117 0.0001  -0.0002 2   THR A OG1 
15   C CG2 A THR A 2   ? 0.1977 0.1980 0.1432 -0.0210 -0.0730 -0.0246 2   THR A CG2 
16   C CG2 B THR A 2   ? 0.2275 0.2213 0.0813 -0.0027 0.0092  0.0160  2   THR A CG2 
17   N N   . PHE A 3   ? 0.1362 0.1146 0.0486 -0.0094 -0.0077 0.0076  3   PHE A N   
18   C CA  . PHE A 3   ? 0.1362 0.1081 0.0474 -0.0119 -0.0043 0.0050  3   PHE A CA  
19   C C   . PHE A 3   ? 0.1427 0.1103 0.0420 -0.0133 -0.0079 0.0013  3   PHE A C   
20   O O   . PHE A 3   ? 0.1796 0.1165 0.0586 -0.0051 0.0160  0.0110  3   PHE A O   
21   C CB  . PHE A 3   ? 0.1339 0.1251 0.0496 -0.0122 -0.0028 0.0089  3   PHE A CB  
22   C CG  . PHE A 3   ? 0.1270 0.1223 0.0459 -0.0088 -0.0117 0.0046  3   PHE A CG  
23   C CD1 . PHE A 3   ? 0.1631 0.1386 0.0473 -0.0324 -0.0218 0.0137  3   PHE A CD1 
24   C CD2 . PHE A 3   ? 0.1229 0.1368 0.0606 -0.0168 -0.0203 0.0059  3   PHE A CD2 
25   C CE1 . PHE A 3   ? 0.1569 0.1764 0.0578 -0.0355 -0.0085 0.0317  3   PHE A CE1 
26   C CE2 . PHE A 3   ? 0.1493 0.1401 0.0469 -0.0060 -0.0358 -0.0002 3   PHE A CE2 
27   C CZ  . PHE A 3   ? 0.1541 0.1572 0.0456 -0.0024 -0.0091 0.0196  3   PHE A CZ  
28   N N   . GLU A 4   ? 0.1254 0.1098 0.0337 -0.0114 -0.0098 0.0043  4   GLU A N   
29   C CA  A GLU A 4   ? 0.1323 0.1095 0.0280 -0.0215 -0.0163 0.0074  4   GLU A CA  
30   C CA  B GLU A 4   ? 0.1323 0.1215 0.0277 -0.0195 -0.0161 0.0034  4   GLU A CA  
31   C C   . GLU A 4   ? 0.1295 0.1104 0.0267 -0.0199 -0.0119 0.0024  4   GLU A C   
32   O O   . GLU A 4   ? 0.1231 0.1459 0.0550 -0.0155 -0.0081 -0.0357 4   GLU A O   
33   C CB  A GLU A 4   ? 0.1223 0.1120 0.0357 -0.0119 -0.0196 0.0017  4   GLU A CB  
34   C CB  B GLU A 4   ? 0.1266 0.1270 0.0263 -0.0136 -0.0098 -0.0005 4   GLU A CB  
35   C CG  A GLU A 4   ? 0.1190 0.1137 0.0349 -0.0072 -0.0147 0.0080  4   GLU A CG  
36   C CG  B GLU A 4   ? 0.1290 0.1387 0.0313 -0.0123 -0.0004 0.0070  4   GLU A CG  
37   C CD  A GLU A 4   ? 0.1216 0.1215 0.0436 -0.0078 -0.0142 0.0147  4   GLU A CD  
38   C CD  B GLU A 4   ? 0.1266 0.1635 0.0568 -0.0132 -0.0211 0.0218  4   GLU A CD  
39   O OE1 A GLU A 4   ? 0.1383 0.1274 0.0522 0.0020  -0.0264 0.0077  4   GLU A OE1 
40   O OE1 B GLU A 4   ? 0.2005 0.1678 0.0966 0.0348  -0.0226 0.0167  4   GLU A OE1 
41   O OE2 A GLU A 4   ? 0.2054 0.1487 0.0495 0.0068  -0.0472 0.0129  4   GLU A OE2 
42   O OE2 B GLU A 4   ? 0.1508 0.1932 0.0591 -0.0143 -0.0282 0.0389  4   GLU A OE2 
43   N N   . ILE A 5   ? 0.1314 0.1075 0.0278 -0.0176 -0.0162 0.0012  5   ILE A N   
44   C CA  . ILE A 5   ? 0.1343 0.1110 0.0267 -0.0164 -0.0109 -0.0032 5   ILE A CA  
45   C C   . ILE A 5   ? 0.1395 0.1179 0.0260 -0.0091 -0.0060 -0.0052 5   ILE A C   
46   O O   . ILE A 5   ? 0.1798 0.1326 0.0259 -0.0319 -0.0011 -0.0077 5   ILE A O   
47   C CB  . ILE A 5   ? 0.1396 0.1116 0.0270 -0.0081 -0.0081 -0.0009 5   ILE A CB  
48   C CG1 . ILE A 5   ? 0.1444 0.1228 0.0388 -0.0130 -0.0114 0.0107  5   ILE A CG1 
49   C CG2 . ILE A 5   ? 0.1309 0.1227 0.0429 0.0039  -0.0043 -0.0001 5   ILE A CG2 
50   C CD1 . ILE A 5   ? 0.1792 0.1219 0.0532 -0.0080 -0.0120 0.0115  5   ILE A CD1 
51   N N   . VAL A 6   ? 0.1362 0.1182 0.0255 -0.0174 -0.0045 0.0034  6   VAL A N   
52   C CA  . VAL A 6   ? 0.1332 0.1177 0.0256 -0.0159 -0.0042 0.0046  6   VAL A CA  
53   C C   . VAL A 6   ? 0.1315 0.1176 0.0255 -0.0074 -0.0039 -0.0030 6   VAL A C   
54   O O   . VAL A 6   ? 0.1305 0.1440 0.0267 -0.0164 -0.0034 -0.0117 6   VAL A O   
55   C CB  . VAL A 6   ? 0.1203 0.1244 0.0266 -0.0095 -0.0086 0.0031  6   VAL A CB  
56   C CG1 . VAL A 6   ? 0.1372 0.1298 0.0488 -0.0065 -0.0109 0.0234  6   VAL A CG1 
57   C CG2 . VAL A 6   ? 0.1254 0.1431 0.0438 -0.0099 -0.0159 0.0099  6   VAL A CG2 
58   N N   . ASN A 7   ? 0.1282 0.1182 0.0255 0.0015  -0.0017 -0.0045 7   ASN A N   
59   C CA  . ASN A 7   ? 0.1229 0.1117 0.0257 0.0025  -0.0063 0.0009  7   ASN A CA  
60   C C   . ASN A 7   ? 0.1231 0.1155 0.0256 0.0046  -0.0046 0.0024  7   ASN A C   
61   O O   . ASN A 7   ? 0.1618 0.1307 0.0253 -0.0001 -0.0001 0.0026  7   ASN A O   
62   C CB  . ASN A 7   ? 0.1326 0.1145 0.0255 0.0083  -0.0036 0.0031  7   ASN A CB  
63   C CG  . ASN A 7   ? 0.1245 0.1159 0.0262 0.0101  -0.0066 0.0057  7   ASN A CG  
64   O OD1 . ASN A 7   ? 0.1194 0.1264 0.0399 0.0057  -0.0108 -0.0031 7   ASN A OD1 
65   N ND2 . ASN A 7   ? 0.1227 0.1329 0.0372 0.0116  -0.0016 -0.0028 7   ASN A ND2 
66   N N   . ARG A 8   ? 0.1179 0.1102 0.0257 0.0022  -0.0054 0.0033  8   ARG A N   
67   C CA  . ARG A 8   ? 0.1235 0.1125 0.0276 0.0036  -0.0088 0.0111  8   ARG A CA  
68   C C   . ARG A 8   ? 0.1240 0.1188 0.0333 0.0018  0.0001  0.0065  8   ARG A C   
69   O O   . ARG A 8   ? 0.1323 0.1271 0.0708 -0.0042 0.0018  0.0188  8   ARG A O   
70   C CB  . ARG A 8   ? 0.1166 0.1208 0.0427 0.0048  -0.0063 0.0042  8   ARG A CB  
71   C CG  . ARG A 8   ? 0.1422 0.1311 0.0650 -0.0068 -0.0144 0.0041  8   ARG A CG  
72   C CD  . ARG A 8   ? 0.1559 0.1397 0.0756 -0.0048 -0.0187 -0.0132 8   ARG A CD  
73   N NE  . ARG A 8   ? 0.1515 0.1538 0.0645 0.0104  -0.0126 -0.0192 8   ARG A NE  
74   C CZ  . ARG A 8   ? 0.1644 0.1818 0.0685 -0.0018 -0.0066 -0.0170 8   ARG A CZ  
75   N NH1 . ARG A 8   ? 0.1839 0.2231 0.0901 0.0101  -0.0096 -0.0488 8   ARG A NH1 
76   N NH2 . ARG A 8   ? 0.1598 0.2431 0.0845 -0.0097 0.0091  -0.0461 8   ARG A NH2 
77   N N   . CYS A 9   ? 0.1177 0.1254 0.0259 0.0005  -0.0028 0.0066  9   CYS A N   
78   C CA  . CYS A 9   ? 0.1175 0.1303 0.0321 -0.0021 -0.0002 0.0038  9   CYS A CA  
79   C C   . CYS A 9   ? 0.1210 0.1322 0.0342 0.0034  -0.0004 0.0106  9   CYS A C   
80   O O   . CYS A 9   ? 0.1304 0.1553 0.0307 -0.0014 0.0016  0.0073  9   CYS A O   
81   C CB  . CYS A 9   ? 0.1170 0.1449 0.0347 -0.0006 -0.0030 0.0057  9   CYS A CB  
82   S SG  . CYS A 9   ? 0.1315 0.1736 0.0315 -0.0066 -0.0051 0.0144  9   CYS A SG  
83   N N   . SER A 10  ? 0.1267 0.1535 0.0418 -0.0032 0.0051  0.0123  10  SER A N   
84   C CA  . SER A 10  ? 0.1335 0.1748 0.0464 -0.0033 0.0099  0.0227  10  SER A CA  
85   C C   . SER A 10  ? 0.1257 0.1917 0.0453 0.0010  0.0110  0.0117  10  SER A C   
86   O O   . SER A 10  ? 0.2003 0.2482 0.0590 0.0309  0.0441  0.0215  10  SER A O   
87   C CB  . SER A 10  ? 0.1579 0.1912 0.0939 -0.0189 0.0246  0.0300  10  SER A CB  
88   O OG  . SER A 10  ? 0.1683 0.2410 0.1359 -0.0537 -0.0072 0.0204  10  SER A OG  
89   N N   . TYR A 11  ? 0.1359 0.1662 0.0482 0.0032  0.0149  0.0043  11  TYR A N   
90   C CA  . TYR A 11  ? 0.1311 0.1746 0.0594 0.0078  0.0111  -0.0029 11  TYR A CA  
91   C C   . TYR A 11  ? 0.1195 0.1567 0.0479 0.0175  0.0032  0.0016  11  TYR A C   
92   O O   . TYR A 11  ? 0.1245 0.1529 0.0557 0.0151  0.0072  -0.0022 11  TYR A O   
93   C CB  . TYR A 11  ? 0.1251 0.1711 0.0944 0.0100  0.0006  -0.0037 11  TYR A CB  
94   C CG  . TYR A 11  ? 0.1208 0.1677 0.0761 0.0034  -0.0148 0.0035  11  TYR A CG  
95   C CD1 . TYR A 11  ? 0.1421 0.1551 0.0757 0.0030  -0.0251 0.0098  11  TYR A CD1 
96   C CD2 . TYR A 11  ? 0.1333 0.1713 0.0782 -0.0108 -0.0086 0.0089  11  TYR A CD2 
97   C CE1 . TYR A 11  ? 0.1500 0.1647 0.0613 -0.0092 -0.0242 0.0202  11  TYR A CE1 
98   C CE2 . TYR A 11  ? 0.1490 0.1557 0.0646 -0.0137 -0.0141 0.0071  11  TYR A CE2 
99   C CZ  . TYR A 11  ? 0.1392 0.1740 0.0495 -0.0085 -0.0199 0.0171  11  TYR A CZ  
100  O OH  . TYR A 11  ? 0.1728 0.1975 0.0511 -0.0187 -0.0142 0.0074  11  TYR A OH  
101  N N   . THR A 12  ? 0.1315 0.1668 0.0472 0.0225  0.0092  -0.0063 12  THR A N   
102  C CA  . THR A 12  ? 0.1219 0.1573 0.0439 0.0265  -0.0049 -0.0081 12  THR A CA  
103  C C   . THR A 12  ? 0.1266 0.1421 0.0436 0.0289  -0.0138 -0.0075 12  THR A C   
104  O O   . THR A 12  ? 0.1321 0.1527 0.0647 0.0238  -0.0228 -0.0047 12  THR A O   
105  C CB  . THR A 12  ? 0.1515 0.1774 0.0506 0.0400  -0.0014 -0.0139 12  THR A CB  
106  O OG1 . THR A 12  ? 0.2174 0.1980 0.0534 0.0448  0.0205  -0.0064 12  THR A OG1 
107  C CG2 . THR A 12  ? 0.1510 0.1656 0.0578 0.0411  -0.0158 -0.0285 12  THR A CG2 
108  N N   . VAL A 13  ? 0.1289 0.1363 0.0338 0.0250  -0.0156 -0.0024 13  VAL A N   
109  C CA  . VAL A 13  ? 0.1531 0.1387 0.0320 0.0149  -0.0182 -0.0033 13  VAL A CA  
110  C C   . VAL A 13  ? 0.1425 0.1371 0.0296 0.0216  -0.0206 -0.0088 13  VAL A C   
111  O O   . VAL A 13  ? 0.1887 0.1509 0.0481 -0.0011 -0.0489 0.0056  13  VAL A O   
112  C CB  . VAL A 13  ? 0.1801 0.1418 0.0337 0.0057  0.0006  -0.0084 13  VAL A CB  
113  C CG1 . VAL A 13  ? 0.1944 0.1461 0.0567 -0.0045 0.0078  -0.0169 13  VAL A CG1 
114  C CG2 . VAL A 13  ? 0.1900 0.1402 0.0478 0.0348  0.0004  0.0058  13  VAL A CG2 
115  N N   . TRP A 14  ? 0.1351 0.1269 0.0323 0.0265  -0.0259 -0.0097 14  TRP A N   
116  C CA  . TRP A 14  ? 0.1450 0.1282 0.0369 0.0287  -0.0301 -0.0150 14  TRP A CA  
117  C C   . TRP A 14  ? 0.1505 0.1048 0.0329 0.0243  -0.0257 -0.0073 14  TRP A C   
118  O O   . TRP A 14  ? 0.1588 0.1234 0.0344 0.0254  -0.0310 -0.0057 14  TRP A O   
119  C CB  . TRP A 14  ? 0.1586 0.1342 0.0581 0.0390  -0.0323 -0.0198 14  TRP A CB  
120  C CG  . TRP A 14  ? 0.1586 0.1547 0.0656 0.0537  -0.0356 -0.0333 14  TRP A CG  
121  C CD1 . TRP A 14  ? 0.1765 0.1548 0.0923 0.0482  -0.0416 -0.0420 14  TRP A CD1 
122  C CD2 . TRP A 14  ? 0.1605 0.1641 0.0671 0.0606  -0.0413 -0.0363 14  TRP A CD2 
123  N NE1 . TRP A 14  ? 0.1892 0.1921 0.0749 0.0690  -0.0385 -0.0571 14  TRP A NE1 
124  C CE2 . TRP A 14  ? 0.1668 0.1918 0.0698 0.0695  -0.0296 -0.0370 14  TRP A CE2 
125  C CE3 . TRP A 14  ? 0.1432 0.1778 0.0800 0.0575  -0.0217 -0.0323 14  TRP A CE3 
126  C CZ2 . TRP A 14  ? 0.1729 0.2356 0.0673 0.0797  -0.0162 -0.0434 14  TRP A CZ2 
127  C CZ3 . TRP A 14  ? 0.1499 0.2026 0.0926 0.0585  -0.0145 -0.0237 14  TRP A CZ3 
128  C CH2 . TRP A 14  ? 0.1580 0.2394 0.1018 0.0622  -0.0001 -0.0289 14  TRP A CH2 
129  N N   . ALA A 15  ? 0.1407 0.1069 0.0306 0.0180  -0.0241 0.0011  15  ALA A N   
130  C CA  . ALA A 15  ? 0.1484 0.1017 0.0346 0.0167  -0.0189 -0.0058 15  ALA A CA  
131  C C   . ALA A 15  ? 0.1423 0.0978 0.0386 0.0149  -0.0257 -0.0094 15  ALA A C   
132  O O   . ALA A 15  ? 0.1769 0.0988 0.0389 0.0175  -0.0265 -0.0083 15  ALA A O   
133  C CB  . ALA A 15  ? 0.1494 0.1170 0.0690 0.0245  -0.0113 0.0123  15  ALA A CB  
134  N N   . ALA A 16  ? 0.1551 0.0915 0.0419 0.0082  -0.0203 -0.0050 16  ALA A N   
135  C CA  . ALA A 16  ? 0.1713 0.0935 0.0470 0.0095  -0.0257 -0.0026 16  ALA A CA  
136  C C   . ALA A 16  ? 0.1664 0.0953 0.0380 0.0001  -0.0244 -0.0046 16  ALA A C   
137  O O   . ALA A 16  ? 0.1627 0.0985 0.0483 -0.0012 -0.0149 -0.0038 16  ALA A O   
138  C CB  . ALA A 16  ? 0.1723 0.1305 0.0616 0.0229  -0.0252 0.0072  16  ALA A CB  
139  N N   . ALA A 17  ? 0.1841 0.0923 0.0508 -0.0051 -0.0195 -0.0034 17  ALA A N   
140  C CA  . ALA A 17  ? 0.1809 0.1016 0.0533 -0.0081 -0.0182 -0.0041 17  ALA A CA  
141  C C   . ALA A 17  ? 0.1877 0.1048 0.0630 -0.0162 -0.0222 0.0001  17  ALA A C   
142  O O   . ALA A 17  ? 0.2331 0.1032 0.0698 -0.0241 -0.0214 0.0026  17  ALA A O   
143  C CB  . ALA A 17  ? 0.1765 0.1128 0.0748 -0.0105 -0.0197 0.0071  17  ALA A CB  
144  N N   . SER A 18  ? 0.1932 0.0959 0.0609 -0.0168 -0.0225 0.0073  18  SER A N   
145  C CA  . SER A 18  ? 0.2145 0.0995 0.0752 -0.0172 -0.0310 0.0137  18  SER A CA  
146  C C   . SER A 18  ? 0.2070 0.1063 0.0657 -0.0159 -0.0390 0.0224  18  SER A C   
147  O O   . SER A 18  ? 0.2232 0.1098 0.0631 -0.0185 -0.0132 0.0167  18  SER A O   
148  C CB  . SER A 18  ? 0.2229 0.1136 0.0993 0.0010  -0.0232 0.0187  18  SER A CB  
149  O OG  . SER A 18  ? 0.2412 0.1266 0.1237 0.0036  -0.0351 0.0322  18  SER A OG  
150  N N   . LYS A 19  ? 0.2234 0.1151 0.0816 -0.0246 -0.0283 0.0278  19  LYS A N   
151  C CA  . LYS A 19  ? 0.2332 0.1318 0.0842 -0.0260 -0.0220 0.0334  19  LYS A CA  
152  C C   . LYS A 19  ? 0.2657 0.1439 0.0941 -0.0252 -0.0442 0.0408  19  LYS A C   
153  O O   . LYS A 19  ? 0.2768 0.1779 0.1028 -0.0190 -0.0297 0.0597  19  LYS A O   
154  C CB  . LYS A 19  ? 0.2332 0.1660 0.1057 -0.0366 -0.0178 0.0498  19  LYS A CB  
155  C CG  . LYS A 19  ? 0.2603 0.1761 0.1612 -0.0479 -0.0250 0.0531  19  LYS A CG  
156  C CD  . LYS A 19  ? 0.2621 0.2265 0.1683 -0.0654 -0.0185 0.0716  19  LYS A CD  
157  C CE  . LYS A 19  ? 0.2844 0.2407 0.2652 -0.0858 -0.0032 0.0597  19  LYS A CE  
158  N NZ  . LYS A 19  ? 0.3890 0.2614 0.3098 -0.0698 0.0040  0.1039  19  LYS A NZ  
159  N N   . GLY A 20  ? 0.2580 0.1355 0.1135 -0.0174 -0.0509 0.0433  20  GLY A N   
160  C CA  . GLY A 20  ? 0.2819 0.1482 0.1313 -0.0080 -0.0633 0.0489  20  GLY A CA  
161  C C   . GLY A 20  ? 0.3065 0.1492 0.1330 -0.0035 -0.0684 0.0518  20  GLY A C   
162  O O   . GLY A 20  ? 0.3140 0.1679 0.1922 0.0128  -0.0540 0.0512  20  GLY A O   
163  N N   A ASP A 21  ? 0.3349 0.1736 0.1355 -0.0285 -0.0799 0.0472  21  ASP A N   
164  N N   B ASP A 21  ? 0.3274 0.1332 0.1596 -0.0155 -0.0592 0.0633  21  ASP A N   
165  C CA  A ASP A 21  ? 0.3765 0.1723 0.1555 -0.0273 -0.0797 0.0670  21  ASP A CA  
166  C CA  B ASP A 21  ? 0.3688 0.1343 0.1784 -0.0198 -0.0702 0.0711  21  ASP A CA  
167  C C   A ASP A 21  ? 0.3705 0.1604 0.1555 -0.0327 -0.0716 0.0603  21  ASP A C   
168  C C   B ASP A 21  ? 0.3662 0.1224 0.1792 -0.0330 -0.0560 0.0557  21  ASP A C   
169  O O   A ASP A 21  ? 0.4340 0.1532 0.1899 -0.0281 -0.1065 0.0738  21  ASP A O   
170  O O   B ASP A 21  ? 0.4362 0.1273 0.3045 -0.0493 -0.0597 0.0368  21  ASP A O   
171  C CB  A ASP A 21  ? 0.4185 0.2062 0.1687 -0.0465 -0.0693 0.0874  21  ASP A CB  
172  C CB  B ASP A 21  ? 0.4095 0.1647 0.1954 -0.0326 -0.0577 0.0979  21  ASP A CB  
173  C CG  A ASP A 21  ? 0.4184 0.2391 0.2071 -0.0710 -0.0290 0.0834  21  ASP A CG  
174  C CG  B ASP A 21  ? 0.4063 0.1958 0.2172 -0.0505 -0.0299 0.1062  21  ASP A CG  
175  O OD1 A ASP A 21  ? 0.3953 0.2336 0.2191 -0.0950 -0.0281 0.0961  21  ASP A OD1 
176  O OD1 B ASP A 21  ? 0.4111 0.2153 0.2802 -0.0706 -0.0164 0.0992  21  ASP A OD1 
177  O OD2 A ASP A 21  ? 0.4530 0.3374 0.2196 -0.0877 -0.0138 0.0907  21  ASP A OD2 
178  O OD2 B ASP A 21  ? 0.3807 0.2038 0.2268 -0.0301 -0.0496 0.0965  21  ASP A OD2 
179  N N   . ALA A 22  ? 0.3327 0.1262 0.1441 -0.0293 -0.0592 0.0381  22  ALA A N   
180  C CA  . ALA A 22  ? 0.3464 0.1140 0.1552 -0.0400 -0.0697 0.0331  22  ALA A CA  
181  C C   . ALA A 22  ? 0.3075 0.1128 0.1297 -0.0288 -0.0521 0.0246  22  ALA A C   
182  O O   . ALA A 22  ? 0.3258 0.1176 0.1134 -0.0323 -0.0423 0.0214  22  ALA A O   
183  C CB  . ALA A 22  ? 0.3551 0.1548 0.1771 -0.0524 -0.0672 0.0518  22  ALA A CB  
184  N N   . ALA A 23  ? 0.3077 0.1054 0.1323 -0.0179 -0.0513 0.0167  23  ALA A N   
185  C CA  . ALA A 23  ? 0.2876 0.0967 0.1268 -0.0193 -0.0530 0.0080  23  ALA A CA  
186  C C   . ALA A 23  ? 0.2799 0.1060 0.1042 -0.0301 -0.0402 0.0118  23  ALA A C   
187  O O   . ALA A 23  ? 0.2955 0.1232 0.1668 -0.0424 -0.0320 0.0344  23  ALA A O   
188  C CB  . ALA A 23  ? 0.2915 0.1182 0.1320 -0.0168 -0.0449 -0.0023 23  ALA A CB  
189  N N   . LEU A 24  ? 0.2474 0.1059 0.0859 -0.0222 -0.0322 0.0108  24  LEU A N   
190  C CA  . LEU A 24  ? 0.2416 0.1202 0.0830 -0.0379 -0.0346 0.0123  24  LEU A CA  
191  C C   . LEU A 24  ? 0.2371 0.1123 0.0902 -0.0315 -0.0378 0.0041  24  LEU A C   
192  O O   . LEU A 24  ? 0.2511 0.1265 0.0768 -0.0378 -0.0305 -0.0020 24  LEU A O   
193  C CB  . LEU A 24  ? 0.2102 0.1310 0.0879 -0.0216 -0.0319 0.0035  24  LEU A CB  
194  C CG  . LEU A 24  ? 0.1943 0.1622 0.0905 -0.0067 -0.0354 -0.0069 24  LEU A CG  
195  C CD1 . LEU A 24  ? 0.1978 0.1799 0.1083 -0.0083 -0.0270 -0.0323 24  LEU A CD1 
196  C CD2 . LEU A 24  ? 0.2430 0.1819 0.0974 -0.0106 -0.0126 0.0142  24  LEU A CD2 
197  N N   . ASP A 25  ? 0.2322 0.1365 0.0913 -0.0380 -0.0308 0.0078  25  ASP A N   
198  C CA  . ASP A 25  ? 0.2462 0.1329 0.0960 -0.0180 -0.0453 -0.0050 25  ASP A CA  
199  C C   . ASP A 25  ? 0.2493 0.1144 0.1012 -0.0205 -0.0561 -0.0057 25  ASP A C   
200  O O   . ASP A 25  ? 0.2802 0.1161 0.1275 -0.0245 -0.0545 0.0090  25  ASP A O   
201  C CB  . ASP A 25  ? 0.2379 0.1398 0.0843 0.0111  -0.0258 -0.0090 25  ASP A CB  
202  C CG  . ASP A 25  ? 0.2552 0.1629 0.0913 0.0248  -0.0352 -0.0095 25  ASP A CG  
203  O OD1 . ASP A 25  ? 0.2807 0.2380 0.1030 0.0615  -0.0340 -0.0071 25  ASP A OD1 
204  O OD2 . ASP A 25  ? 0.2272 0.1528 0.0938 0.0039  -0.0325 -0.0166 25  ASP A OD2 
205  N N   . ALA A 26  ? 0.2454 0.1175 0.0931 -0.0075 -0.0576 -0.0078 26  ALA A N   
206  C CA  . ALA A 26  ? 0.2525 0.1202 0.1106 0.0013  -0.0525 -0.0254 26  ALA A CA  
207  C C   . ALA A 26  ? 0.2570 0.1110 0.1218 0.0068  -0.0593 -0.0296 26  ALA A C   
208  O O   . ALA A 26  ? 0.2839 0.1678 0.2403 0.0372  -0.1001 -0.1012 26  ALA A O   
209  C CB  . ALA A 26  ? 0.2679 0.1435 0.1110 0.0094  -0.0314 -0.0313 26  ALA A CB  
210  N N   . GLY A 27  ? 0.2366 0.1025 0.0829 -0.0098 -0.0402 -0.0087 27  GLY A N   
211  C CA  . GLY A 27  ? 0.2483 0.1040 0.0793 -0.0126 -0.0547 0.0022  27  GLY A CA  
212  C C   . GLY A 27  ? 0.2249 0.0931 0.0636 0.0062  -0.0420 -0.0020 27  GLY A C   
213  O O   . GLY A 27  ? 0.2189 0.1114 0.0596 -0.0049 -0.0348 -0.0045 27  GLY A O   
214  N N   . GLY A 28  ? 0.2199 0.0995 0.0599 -0.0003 -0.0452 -0.0021 28  GLY A N   
215  C CA  . GLY A 28  ? 0.2017 0.1037 0.0605 0.0077  -0.0438 -0.0056 28  GLY A CA  
216  C C   . GLY A 28  ? 0.1813 0.1017 0.0622 0.0146  -0.0384 -0.0086 28  GLY A C   
217  O O   . GLY A 28  ? 0.2207 0.1137 0.0661 0.0000  -0.0437 -0.0111 28  GLY A O   
218  N N   . ARG A 29  ? 0.1740 0.1081 0.0410 0.0185  -0.0324 -0.0095 29  ARG A N   
219  C CA  . ARG A 29  ? 0.1647 0.1231 0.0388 0.0170  -0.0297 -0.0144 29  ARG A CA  
220  C C   . ARG A 29  ? 0.1507 0.1262 0.0360 0.0205  -0.0299 -0.0118 29  ARG A C   
221  O O   . ARG A 29  ? 0.1616 0.1253 0.0366 0.0069  -0.0186 -0.0131 29  ARG A O   
222  C CB  . ARG A 29  ? 0.1585 0.1200 0.0538 0.0122  -0.0243 -0.0105 29  ARG A CB  
223  C CG  . ARG A 29  ? 0.1776 0.1243 0.0597 0.0084  -0.0401 -0.0123 29  ARG A CG  
224  C CD  . ARG A 29  ? 0.1701 0.1291 0.0634 0.0054  -0.0379 -0.0119 29  ARG A CD  
225  N NE  . ARG A 29  ? 0.1486 0.1276 0.0627 0.0087  -0.0400 -0.0048 29  ARG A NE  
226  C CZ  . ARG A 29  ? 0.1557 0.1277 0.0496 0.0112  -0.0342 -0.0063 29  ARG A CZ  
227  N NH1 . ARG A 29  ? 0.1559 0.1402 0.0682 0.0102  -0.0371 0.0011  29  ARG A NH1 
228  N NH2 . ARG A 29  ? 0.1493 0.1416 0.0690 0.0074  -0.0381 0.0083  29  ARG A NH2 
229  N N   . GLN A 30  ? 0.1545 0.1322 0.0421 0.0153  -0.0229 -0.0220 30  GLN A N   
230  C CA  . GLN A 30  ? 0.1515 0.1365 0.0414 0.0185  -0.0240 -0.0200 30  GLN A CA  
231  C C   . GLN A 30  ? 0.1334 0.1392 0.0309 0.0141  -0.0147 -0.0114 30  GLN A C   
232  O O   . GLN A 30  ? 0.1532 0.1447 0.0594 0.0127  -0.0362 -0.0143 30  GLN A O   
233  C CB  . GLN A 30  ? 0.1612 0.1552 0.0546 0.0305  -0.0146 -0.0183 30  GLN A CB  
234  C CG  . GLN A 30  ? 0.1656 0.1717 0.0616 0.0271  -0.0009 -0.0193 30  GLN A CG  
235  C CD  . GLN A 30  ? 0.1864 0.1956 0.0871 0.0466  0.0200  -0.0143 30  GLN A CD  
236  O OE1 . GLN A 30  ? 0.2663 0.2101 0.1536 0.0799  0.0729  0.0030  30  GLN A OE1 
237  N NE2 . GLN A 30  ? 0.2429 0.1961 0.1167 0.0602  0.0592  -0.0015 30  GLN A NE2 
238  N N   . LEU A 31  ? 0.1343 0.1369 0.0281 0.0116  -0.0164 -0.0076 31  LEU A N   
239  C CA  A LEU A 31  ? 0.1384 0.1415 0.0408 0.0245  -0.0160 -0.0108 31  LEU A CA  
240  C CA  B LEU A 31  ? 0.1296 0.1400 0.0450 0.0261  -0.0172 -0.0214 31  LEU A CA  
241  C C   . LEU A 31  ? 0.1332 0.1302 0.0421 0.0274  -0.0203 -0.0099 31  LEU A C   
242  O O   . LEU A 31  ? 0.1387 0.1374 0.0481 0.0228  -0.0310 -0.0067 31  LEU A O   
243  C CB  A LEU A 31  ? 0.1517 0.1182 0.0493 0.0176  0.0073  0.0074  31  LEU A CB  
244  C CB  B LEU A 31  ? 0.1355 0.1564 0.0892 0.0166  -0.0008 -0.0491 31  LEU A CB  
245  C CG  A LEU A 31  ? 0.1602 0.1834 0.0712 -0.0137 0.0223  -0.0239 31  LEU A CG  
246  C CG  B LEU A 31  ? 0.1356 0.1705 0.0465 0.0227  -0.0095 -0.0011 31  LEU A CG  
247  C CD1 A LEU A 31  ? 0.1377 0.1697 0.0495 -0.0048 0.0184  -0.0016 31  LEU A CD1 
248  C CD1 B LEU A 31  ? 0.1513 0.1496 0.0909 0.0183  0.0033  -0.0011 31  LEU A CD1 
249  C CD2 A LEU A 31  ? 0.1461 0.2113 0.0891 -0.0154 0.0236  -0.0365 31  LEU A CD2 
250  C CD2 B LEU A 31  ? 0.1262 0.1570 0.0681 0.0067  0.0080  -0.0018 31  LEU A CD2 
251  N N   . ASN A 32  ? 0.1483 0.1356 0.0413 0.0226  -0.0290 -0.0069 32  ASN A N   
252  C CA  . ASN A 32  ? 0.1437 0.1524 0.0423 0.0210  -0.0197 -0.0022 32  ASN A CA  
253  C C   . ASN A 32  ? 0.1342 0.1457 0.0307 0.0200  -0.0176 0.0054  32  ASN A C   
254  O O   . ASN A 32  ? 0.1339 0.1309 0.0426 0.0130  -0.0164 0.0079  32  ASN A O   
255  C CB  . ASN A 32  ? 0.1693 0.1801 0.0452 0.0281  -0.0058 -0.0122 32  ASN A CB  
256  C CG  . ASN A 32  ? 0.2260 0.1954 0.0861 0.0303  0.0357  -0.0352 32  ASN A CG  
257  O OD1 . ASN A 32  ? 0.3068 0.2292 0.1688 0.1168  0.0156  -0.0248 32  ASN A OD1 
258  N ND2 . ASN A 32  ? 0.3420 0.2831 0.1514 0.0489  -0.0065 -0.1045 32  ASN A ND2 
259  N N   . SER A 33  ? 0.1363 0.1461 0.0304 0.0154  -0.0031 0.0087  33  SER A N   
260  C CA  . SER A 33  ? 0.1374 0.1410 0.0263 0.0035  -0.0055 0.0093  33  SER A CA  
261  C C   . SER A 33  ? 0.1435 0.1207 0.0261 0.0048  0.0013  0.0085  33  SER A C   
262  O O   . SER A 33  ? 0.1451 0.1383 0.0257 0.0029  0.0010  0.0070  33  SER A O   
263  C CB  . SER A 33  ? 0.1355 0.1603 0.0299 -0.0033 -0.0040 0.0081  33  SER A CB  
264  O OG  . SER A 33  ? 0.1560 0.1568 0.0371 -0.0119 0.0018  0.0107  33  SER A OG  
265  N N   . GLY A 34  ? 0.1342 0.1215 0.0257 0.0110  0.0022  0.0065  34  GLY A N   
266  C CA  . GLY A 34  ? 0.1343 0.1183 0.0277 0.0154  0.0075  0.0094  34  GLY A CA  
267  C C   . GLY A 34  ? 0.1372 0.1245 0.0258 0.0200  -0.0037 0.0053  34  GLY A C   
268  O O   . GLY A 34  ? 0.1392 0.1288 0.0453 0.0198  -0.0029 0.0034  34  GLY A O   
269  N N   . GLU A 35  ? 0.1240 0.1216 0.0263 0.0156  -0.0028 0.0087  35  GLU A N   
270  C CA  A GLU A 35  ? 0.1409 0.1304 0.0262 0.0096  -0.0102 0.0012  35  GLU A CA  
271  C CA  B GLU A 35  ? 0.1388 0.1320 0.0264 0.0117  -0.0112 -0.0008 35  GLU A CA  
272  C C   . GLU A 35  ? 0.1367 0.1164 0.0259 0.0082  -0.0078 -0.0016 35  GLU A C   
273  O O   . GLU A 35  ? 0.1468 0.1363 0.0263 -0.0064 -0.0104 -0.0025 35  GLU A O   
274  C CB  A GLU A 35  ? 0.1283 0.1217 0.0285 0.0053  -0.0110 0.0049  35  GLU A CB  
275  C CB  B GLU A 35  ? 0.1278 0.1343 0.0279 0.0160  -0.0162 -0.0044 35  GLU A CB  
276  C CG  A GLU A 35  ? 0.1277 0.1238 0.0288 0.0113  -0.0160 0.0001  35  GLU A CG  
277  C CG  B GLU A 35  ? 0.1310 0.1417 0.0282 0.0082  -0.0153 -0.0101 35  GLU A CG  
278  C CD  A GLU A 35  ? 0.1159 0.1233 0.0387 0.0029  -0.0101 -0.0097 35  GLU A CD  
279  C CD  B GLU A 35  ? 0.1365 0.1411 0.0579 0.0098  -0.0227 -0.0093 35  GLU A CD  
280  O OE1 A GLU A 35  ? 0.1422 0.1257 0.0468 -0.0038 -0.0150 -0.0019 35  GLU A OE1 
281  O OE1 B GLU A 35  ? 0.1408 0.1225 0.0536 0.0025  -0.0039 -0.0080 35  GLU A OE1 
282  O OE2 A GLU A 35  ? 0.1650 0.1267 0.0456 0.0114  -0.0220 -0.0156 35  GLU A OE2 
283  O OE2 B GLU A 35  ? 0.1927 0.1702 0.0658 0.0379  -0.0205 -0.0238 35  GLU A OE2 
284  N N   . SER A 36  ? 0.1354 0.1186 0.0260 -0.0020 -0.0078 0.0034  36  SER A N   
285  C CA  . SER A 36  ? 0.1344 0.1196 0.0257 -0.0033 -0.0061 -0.0018 36  SER A CA  
286  C C   . SER A 36  ? 0.1254 0.1196 0.0273 -0.0048 -0.0128 -0.0053 36  SER A C   
287  O O   . SER A 36  ? 0.1579 0.1376 0.0312 -0.0175 -0.0140 -0.0129 36  SER A O   
288  C CB  . SER A 36  ? 0.1341 0.1304 0.0270 0.0005  -0.0024 0.0035  36  SER A CB  
289  O OG  . SER A 36  ? 0.1458 0.1253 0.0361 0.0101  -0.0005 0.0009  36  SER A OG  
290  N N   . TRP A 37  ? 0.1409 0.1065 0.0279 -0.0078 -0.0094 -0.0067 37  TRP A N   
291  C CA  . TRP A 37  ? 0.1516 0.1070 0.0366 -0.0062 -0.0092 -0.0075 37  TRP A CA  
292  C C   . TRP A 37  ? 0.1455 0.0996 0.0372 -0.0129 -0.0114 -0.0039 37  TRP A C   
293  O O   . TRP A 37  ? 0.1549 0.1180 0.0382 -0.0157 -0.0061 -0.0114 37  TRP A O   
294  C CB  . TRP A 37  ? 0.1510 0.1127 0.0741 -0.0072 -0.0071 0.0011  37  TRP A CB  
295  C CG  . TRP A 37  ? 0.1542 0.1123 0.0805 0.0038  -0.0054 0.0003  37  TRP A CG  
296  C CD1 . TRP A 37  ? 0.1631 0.1143 0.1087 0.0019  -0.0082 -0.0056 37  TRP A CD1 
297  C CD2 . TRP A 37  ? 0.1560 0.1161 0.0852 0.0106  0.0002  -0.0006 37  TRP A CD2 
298  N NE1 . TRP A 37  ? 0.1879 0.1137 0.1172 -0.0001 -0.0034 -0.0044 37  TRP A NE1 
299  C CE2 . TRP A 37  ? 0.1644 0.1215 0.0988 0.0066  0.0093  0.0072  37  TRP A CE2 
300  C CE3 . TRP A 37  ? 0.1672 0.1289 0.0869 0.0145  -0.0071 0.0144  37  TRP A CE3 
301  C CZ2 . TRP A 37  ? 0.1869 0.1258 0.1242 0.0189  0.0120  0.0193  37  TRP A CZ2 
302  C CZ3 . TRP A 37  ? 0.1901 0.1529 0.1019 0.0279  -0.0075 0.0246  37  TRP A CZ3 
303  C CH2 . TRP A 37  ? 0.1819 0.1454 0.1160 0.0314  0.0034  0.0378  37  TRP A CH2 
304  N N   . THR A 38  ? 0.1475 0.1188 0.0447 -0.0177 -0.0119 -0.0011 38  THR A N   
305  C CA  . THR A 38  ? 0.1501 0.1254 0.0637 -0.0188 -0.0097 0.0052  38  THR A CA  
306  C C   . THR A 38  ? 0.1575 0.1219 0.0635 -0.0205 -0.0123 0.0021  38  THR A C   
307  O O   . THR A 38  ? 0.2120 0.1292 0.0696 -0.0383 -0.0199 -0.0031 38  THR A O   
308  C CB  . THR A 38  ? 0.1542 0.1585 0.1083 -0.0156 -0.0147 0.0288  38  THR A CB  
309  O OG1 . THR A 38  ? 0.1769 0.1617 0.1596 -0.0099 -0.0258 0.0415  38  THR A OG1 
310  C CG2 . THR A 38  ? 0.1549 0.1794 0.1475 -0.0090 0.0002  0.0363  38  THR A CG2 
311  N N   . ILE A 39  ? 0.1708 0.1125 0.0634 -0.0137 0.0049  0.0019  39  ILE A N   
312  C CA  . ILE A 39  ? 0.1696 0.1149 0.0608 -0.0173 0.0006  0.0006  39  ILE A CA  
313  C C   . ILE A 39  ? 0.1544 0.1161 0.0633 -0.0172 -0.0141 0.0011  39  ILE A C   
314  O O   . ILE A 39  ? 0.1524 0.1173 0.0935 -0.0204 -0.0030 -0.0015 39  ILE A O   
315  C CB  . ILE A 39  ? 0.1611 0.1267 0.0784 -0.0098 0.0036  0.0083  39  ILE A CB  
316  C CG1 . ILE A 39  ? 0.1523 0.1317 0.0828 -0.0129 -0.0036 0.0069  39  ILE A CG1 
317  C CG2 . ILE A 39  ? 0.1754 0.1679 0.1078 -0.0041 0.0167  -0.0048 39  ILE A CG2 
318  C CD1 . ILE A 39  ? 0.1610 0.1520 0.0919 -0.0142 -0.0105 0.0137  39  ILE A CD1 
319  N N   . ASN A 40  ? 0.1631 0.1195 0.0628 -0.0174 -0.0080 0.0028  40  ASN A N   
320  C CA  . ASN A 40  ? 0.1662 0.1310 0.0748 -0.0284 -0.0069 0.0098  40  ASN A CA  
321  C C   . ASN A 40  ? 0.1689 0.1354 0.0720 -0.0248 0.0001  0.0123  40  ASN A C   
322  O O   . ASN A 40  ? 0.2441 0.1523 0.0883 0.0140  0.0050  0.0175  40  ASN A O   
323  C CB  . ASN A 40  ? 0.1597 0.1861 0.1043 -0.0419 -0.0053 -0.0023 40  ASN A CB  
324  C CG  . ASN A 40  ? 0.1736 0.2392 0.1095 -0.0271 -0.0163 -0.0033 40  ASN A CG  
325  O OD1 . ASN A 40  ? 0.1791 0.2848 0.1185 -0.0014 -0.0350 -0.0057 40  ASN A OD1 
326  N ND2 . ASN A 40  ? 0.2073 0.2934 0.1076 -0.0036 -0.0146 0.0015  40  ASN A ND2 
327  N N   . VAL A 41  ? 0.1617 0.1456 0.0644 -0.0080 -0.0021 0.0210  41  VAL A N   
328  C CA  . VAL A 41  ? 0.1550 0.1568 0.0715 -0.0084 -0.0040 0.0228  41  VAL A CA  
329  C C   . VAL A 41  ? 0.1646 0.1649 0.0643 -0.0256 -0.0085 0.0209  41  VAL A C   
330  O O   . VAL A 41  ? 0.1595 0.1820 0.0872 -0.0228 -0.0054 0.0392  41  VAL A O   
331  C CB  . VAL A 41  ? 0.1564 0.1701 0.0763 -0.0207 -0.0044 0.0101  41  VAL A CB  
332  C CG1 . VAL A 41  ? 0.1591 0.1962 0.0747 -0.0269 -0.0162 0.0021  41  VAL A CG1 
333  C CG2 . VAL A 41  ? 0.1607 0.1779 0.0991 -0.0213 0.0007  0.0210  41  VAL A CG2 
334  N N   . GLU A 42  ? 0.1667 0.1528 0.0717 -0.0230 -0.0024 0.0135  42  GLU A N   
335  C CA  . GLU A 42  ? 0.1741 0.1618 0.0797 -0.0481 -0.0099 0.0073  42  GLU A CA  
336  C C   . GLU A 42  ? 0.1673 0.1579 0.0642 -0.0517 -0.0048 0.0161  42  GLU A C   
337  O O   . GLU A 42  ? 0.1527 0.1616 0.0773 -0.0460 -0.0054 0.0102  42  GLU A O   
338  C CB  . GLU A 42  ? 0.2192 0.1550 0.1078 -0.0445 -0.0053 0.0017  42  GLU A CB  
339  C CG  . GLU A 42  ? 0.2465 0.2009 0.1558 -0.0585 0.0008  0.0036  42  GLU A CG  
340  C CD  . GLU A 42  ? 0.2578 0.2119 0.2477 -0.0408 -0.0330 0.0140  42  GLU A CD  
341  O OE1 . GLU A 42  ? 0.3161 0.2917 0.3468 -0.0022 -0.0968 0.0253  42  GLU A OE1 
342  O OE2 . GLU A 42  ? 0.2205 0.2592 0.2937 -0.0346 0.0064  -0.0287 42  GLU A OE2 
343  N N   A PRO A 43  ? 0.1589 0.1724 0.0662 -0.0730 0.0003  0.0081  43  PRO A N   
344  N N   B PRO A 43  ? 0.1656 0.1696 0.0663 -0.0638 -0.0179 0.0118  43  PRO A N   
345  C CA  A PRO A 43  ? 0.1561 0.1529 0.0717 -0.0771 0.0088  0.0120  43  PRO A CA  
346  C CA  B PRO A 43  ? 0.1568 0.1430 0.0650 -0.0600 -0.0162 0.0231  43  PRO A CA  
347  C C   A PRO A 43  ? 0.1491 0.1368 0.0711 -0.0546 0.0107  -0.0021 43  PRO A C   
348  C C   B PRO A 43  ? 0.1496 0.1210 0.0718 -0.0372 -0.0138 0.0123  43  PRO A C   
349  O O   A PRO A 43  ? 0.1510 0.1392 0.0783 -0.0374 0.0124  -0.0108 43  PRO A O   
350  O O   B PRO A 43  ? 0.1420 0.1263 0.0729 -0.0285 -0.0090 0.0145  43  PRO A O   
351  C CB  A PRO A 43  ? 0.1575 0.1404 0.0977 -0.0694 -0.0062 0.0141  43  PRO A CB  
352  C CB  B PRO A 43  ? 0.1567 0.1468 0.0970 -0.0608 -0.0197 0.0258  43  PRO A CB  
353  C CG  A PRO A 43  ? 0.1605 0.1455 0.1002 -0.0676 -0.0118 0.0031  43  PRO A CG  
354  C CG  B PRO A 43  ? 0.1748 0.1817 0.1015 -0.0671 -0.0212 0.0149  43  PRO A CG  
355  C CD  A PRO A 43  ? 0.1543 0.1556 0.0881 -0.0735 -0.0042 0.0102  43  PRO A CD  
356  C CD  B PRO A 43  ? 0.1766 0.1718 0.0696 -0.0771 -0.0181 0.0153  43  PRO A CD  
357  N N   A GLY A 44  ? 0.1288 0.1318 0.0718 -0.0445 0.0136  -0.0034 44  GLY A N   
358  N N   B GLY A 44  ? 0.1392 0.1194 0.0590 -0.0230 -0.0008 0.0159  44  GLY A N   
359  C CA  A GLY A 44  ? 0.1263 0.1439 0.0890 -0.0431 -0.0020 0.0013  44  GLY A CA  
360  C CA  B GLY A 44  ? 0.1390 0.1145 0.0621 -0.0163 -0.0039 0.0119  44  GLY A CA  
361  C C   A GLY A 44  ? 0.1270 0.1452 0.0830 -0.0408 -0.0013 0.0011  44  GLY A C   
362  C C   B GLY A 44  ? 0.1359 0.1212 0.0685 -0.0179 -0.0011 0.0193  44  GLY A C   
363  O O   A GLY A 44  ? 0.1356 0.1614 0.0941 -0.0246 0.0079  0.0231  44  GLY A O   
364  O O   B GLY A 44  ? 0.1353 0.1687 0.0799 -0.0050 -0.0031 0.0344  44  GLY A O   
365  N N   A THR A 45  ? 0.1322 0.1455 0.0913 -0.0314 0.0109  0.0018  45  THR A N   
366  N N   B THR A 45  ? 0.1285 0.1170 0.0563 -0.0173 -0.0089 0.0185  45  THR A N   
367  C CA  A THR A 45  ? 0.1291 0.1497 0.0907 -0.0344 0.0135  -0.0121 45  THR A CA  
368  C CA  B THR A 45  ? 0.1303 0.1260 0.0754 -0.0148 -0.0163 0.0157  45  THR A CA  
369  C C   A THR A 45  ? 0.1165 0.1434 0.0904 -0.0348 0.0181  -0.0112 45  THR A C   
370  C C   B THR A 45  ? 0.1340 0.1241 0.0692 -0.0166 -0.0054 0.0155  45  THR A C   
371  O O   A THR A 45  ? 0.1212 0.1513 0.1208 -0.0183 0.0108  -0.0237 45  THR A O   
372  O O   B THR A 45  ? 0.1250 0.1264 0.0818 -0.0048 -0.0071 0.0023  45  THR A O   
373  C CB  A THR A 45  ? 0.1261 0.1726 0.0928 -0.0231 0.0131  -0.0028 45  THR A CB  
374  C CB  B THR A 45  ? 0.1478 0.1438 0.0725 -0.0176 -0.0105 0.0110  45  THR A CB  
375  O OG1 A THR A 45  ? 0.1587 0.1837 0.0793 -0.0131 0.0060  -0.0019 45  THR A OG1 
376  O OG1 B THR A 45  ? 0.1965 0.1914 0.0635 -0.0437 0.0020  -0.0032 45  THR A OG1 
377  C CG2 A THR A 45  ? 0.1269 0.1617 0.0899 -0.0204 0.0142  -0.0007 45  THR A CG2 
378  C CG2 B THR A 45  ? 0.1465 0.1528 0.0807 -0.0052 -0.0059 0.0000  45  THR A CG2 
379  N N   A ASN A 46  ? 0.1574 0.1481 0.1005 -0.0441 0.0045  0.0044  46  ASN A N   
380  N N   B ASN A 46  ? 0.1446 0.1279 0.0733 -0.0318 -0.0196 0.0192  46  ASN A N   
381  C CA  A ASN A 46  ? 0.1843 0.1971 0.1007 -0.0709 -0.0100 0.0134  46  ASN A CA  
382  C CA  B ASN A 46  ? 0.1939 0.1800 0.0514 -0.0561 -0.0152 0.0210  46  ASN A CA  
383  C C   A ASN A 46  ? 0.1816 0.1861 0.0717 -0.0633 -0.0187 0.0339  46  ASN A C   
384  C C   B ASN A 46  ? 0.1860 0.1648 0.0699 -0.0451 -0.0278 0.0322  46  ASN A C   
385  O O   A ASN A 46  ? 0.1783 0.2018 0.1555 -0.0541 -0.0004 0.0276  46  ASN A O   
386  O O   B ASN A 46  ? 0.1800 0.1547 0.1080 -0.0477 -0.0118 0.0446  46  ASN A O   
387  C CB  A ASN A 46  ? 0.2449 0.2514 0.1273 -0.0657 0.0204  0.0346  46  ASN A CB  
388  C CB  B ASN A 46  ? 0.2512 0.2123 0.0660 -0.0842 0.0080  0.0219  46  ASN A CB  
389  C CG  A ASN A 46  ? 0.2933 0.3092 0.1387 -0.0489 -0.0028 0.0210  46  ASN A CG  
390  C CG  B ASN A 46  ? 0.3369 0.2326 0.0764 -0.1026 0.0116  0.0134  46  ASN A CG  
391  O OD1 A ASN A 46  ? 0.3827 0.4182 0.1769 0.0210  0.0050  -0.0186 46  ASN A OD1 
392  O OD1 B ASN A 46  ? 0.3964 0.2502 0.0793 -0.0704 0.0227  -0.0038 46  ASN A OD1 
393  N ND2 A ASN A 46  ? 0.3035 0.3734 0.1097 -0.0388 -0.0236 0.0014  46  ASN A ND2 
394  N ND2 B ASN A 46  ? 0.4273 0.2647 0.1275 -0.0547 -0.0107 0.0395  46  ASN A ND2 
395  N N   . GLY A 47  ? 0.1831 0.1644 0.0700 -0.0484 -0.0185 0.0336  47  GLY A N   
396  C CA  . GLY A 47  ? 0.1792 0.1749 0.0671 -0.0489 -0.0278 0.0373  47  GLY A CA  
397  C C   . GLY A 47  ? 0.1695 0.1423 0.0706 -0.0392 -0.0272 0.0318  47  GLY A C   
398  O O   . GLY A 47  ? 0.1923 0.1758 0.0838 -0.0102 -0.0381 0.0264  47  GLY A O   
399  N N   . GLY A 48  ? 0.1476 0.1379 0.0666 -0.0346 -0.0139 0.0291  48  GLY A N   
400  C CA  . GLY A 48  ? 0.1551 0.1201 0.0588 -0.0289 -0.0217 0.0197  48  GLY A CA  
401  C C   . GLY A 48  ? 0.1410 0.1199 0.0448 -0.0217 -0.0208 0.0211  48  GLY A C   
402  O O   . GLY A 48  ? 0.1414 0.1162 0.0586 -0.0218 -0.0056 0.0119  48  GLY A O   
403  N N   . LYS A 49  ? 0.1445 0.1014 0.0484 -0.0207 -0.0212 0.0086  49  LYS A N   
404  C CA  . LYS A 49  ? 0.1461 0.1046 0.0464 -0.0181 -0.0109 0.0114  49  LYS A CA  
405  C C   . LYS A 49  ? 0.1388 0.1021 0.0460 -0.0116 -0.0129 0.0053  49  LYS A C   
406  O O   . LYS A 49  ? 0.1749 0.1001 0.0491 -0.0161 -0.0129 0.0089  49  LYS A O   
407  C CB  . LYS A 49  ? 0.1498 0.1277 0.0545 -0.0250 -0.0170 0.0140  49  LYS A CB  
408  C CG  . LYS A 49  ? 0.1764 0.1301 0.0522 -0.0311 -0.0272 0.0149  49  LYS A CG  
409  C CD  . LYS A 49  ? 0.1931 0.1541 0.0861 -0.0390 -0.0478 0.0169  49  LYS A CD  
410  C CE  . LYS A 49  ? 0.2599 0.1690 0.0851 -0.0239 -0.0695 0.0210  49  LYS A CE  
411  N NZ  . LYS A 49  ? 0.2493 0.1780 0.1071 -0.0352 -0.0477 0.0407  49  LYS A NZ  
412  N N   . ILE A 50  ? 0.1288 0.0962 0.0370 -0.0120 -0.0104 0.0023  50  ILE A N   
413  C CA  . ILE A 50  ? 0.1324 0.0927 0.0329 -0.0055 -0.0137 0.0000  50  ILE A CA  
414  C C   . ILE A 50  ? 0.1257 0.0935 0.0279 -0.0006 -0.0141 0.0042  50  ILE A C   
415  O O   . ILE A 50  ? 0.1233 0.0977 0.0374 -0.0046 -0.0029 -0.0037 50  ILE A O   
416  C CB  . ILE A 50  ? 0.1264 0.0998 0.0440 -0.0024 -0.0145 0.0006  50  ILE A CB  
417  C CG1 . ILE A 50  ? 0.1365 0.1170 0.0539 -0.0091 -0.0172 -0.0072 50  ILE A CG1 
418  C CG2 . ILE A 50  ? 0.1364 0.1120 0.0450 0.0033  -0.0163 0.0065  50  ILE A CG2 
419  C CD1 . ILE A 50  ? 0.1347 0.1384 0.0599 -0.0137 -0.0229 -0.0015 50  ILE A CD1 
420  N N   . TRP A 51  ? 0.1284 0.0912 0.0281 0.0000  -0.0164 0.0004  51  TRP A N   
421  C CA  . TRP A 51  ? 0.1269 0.0894 0.0292 0.0011  -0.0142 -0.0034 51  TRP A CA  
422  C C   . TRP A 51  ? 0.1233 0.0893 0.0295 0.0097  -0.0192 -0.0040 51  TRP A C   
423  O O   . TRP A 51  ? 0.1378 0.1030 0.0355 -0.0014 -0.0130 -0.0085 51  TRP A O   
424  C CB  . TRP A 51  ? 0.1303 0.1038 0.0285 0.0019  -0.0152 -0.0010 51  TRP A CB  
425  C CG  . TRP A 51  ? 0.1496 0.1091 0.0309 0.0136  -0.0260 0.0012  51  TRP A CG  
426  C CD1 . TRP A 51  ? 0.1545 0.1138 0.0396 0.0195  -0.0312 -0.0019 51  TRP A CD1 
427  C CD2 . TRP A 51  ? 0.1651 0.1045 0.0425 0.0103  -0.0378 0.0055  51  TRP A CD2 
428  N NE1 . TRP A 51  ? 0.1785 0.1182 0.0504 0.0315  -0.0403 -0.0018 51  TRP A NE1 
429  C CE2 . TRP A 51  ? 0.1796 0.1177 0.0501 0.0167  -0.0390 0.0078  51  TRP A CE2 
430  C CE3 . TRP A 51  ? 0.1644 0.1113 0.0609 -0.0002 -0.0324 0.0211  51  TRP A CE3 
431  C CZ2 . TRP A 51  ? 0.2215 0.1053 0.0719 0.0265  -0.0611 0.0054  51  TRP A CZ2 
432  C CZ3 . TRP A 51  ? 0.1846 0.1154 0.0783 -0.0052 -0.0425 0.0278  51  TRP A CZ3 
433  C CH2 . TRP A 51  ? 0.2204 0.1092 0.0880 -0.0001 -0.0516 0.0187  51  TRP A CH2 
434  N N   . ALA A 52  ? 0.1259 0.1010 0.0271 0.0052  -0.0105 -0.0076 52  ALA A N   
435  C CA  . ALA A 52  ? 0.1268 0.1068 0.0318 0.0131  -0.0038 -0.0038 52  ALA A CA  
436  C C   . ALA A 52  ? 0.1336 0.1112 0.0302 0.0140  -0.0169 -0.0115 52  ALA A C   
437  O O   . ALA A 52  ? 0.1426 0.1419 0.0376 0.0230  -0.0250 -0.0237 52  ALA A O   
438  C CB  . ALA A 52  ? 0.1328 0.1155 0.0630 0.0155  0.0145  0.0073  52  ALA A CB  
439  N N   . ARG A 53  ? 0.1308 0.1266 0.0298 0.0283  -0.0209 -0.0114 53  ARG A N   
440  C CA  . ARG A 53  ? 0.1410 0.1356 0.0312 0.0384  -0.0245 -0.0161 53  ARG A CA  
441  C C   . ARG A 53  ? 0.1352 0.1339 0.0391 0.0356  -0.0239 -0.0182 53  ARG A C   
442  O O   . ARG A 53  ? 0.1367 0.1445 0.0390 0.0263  -0.0220 -0.0096 53  ARG A O   
443  C CB  . ARG A 53  ? 0.1543 0.1337 0.0444 0.0433  -0.0331 -0.0113 53  ARG A CB  
444  C CG  . ARG A 53  ? 0.1777 0.1368 0.0415 0.0387  -0.0315 -0.0070 53  ARG A CG  
445  C CD  . ARG A 53  ? 0.1908 0.1307 0.0551 0.0448  -0.0383 0.0011  53  ARG A CD  
446  N NE  . ARG A 53  ? 0.1880 0.1239 0.0637 0.0493  -0.0418 -0.0134 53  ARG A NE  
447  C CZ  . ARG A 53  ? 0.2165 0.1201 0.0792 0.0485  -0.0437 -0.0112 53  ARG A CZ  
448  N NH1 . ARG A 53  ? 0.2545 0.1247 0.1098 0.0595  -0.0587 -0.0220 53  ARG A NH1 
449  N NH2 . ARG A 53  ? 0.2142 0.1227 0.0913 0.0453  -0.0496 -0.0267 53  ARG A NH2 
450  N N   . THR A 54  ? 0.1307 0.1614 0.0447 0.0427  -0.0216 -0.0140 54  THR A N   
451  C CA  . THR A 54  ? 0.1301 0.1668 0.0587 0.0401  -0.0253 -0.0276 54  THR A CA  
452  C C   . THR A 54  ? 0.1374 0.1798 0.0567 0.0425  -0.0238 -0.0375 54  THR A C   
453  O O   . THR A 54  ? 0.1399 0.1960 0.0823 0.0613  -0.0351 -0.0345 54  THR A O   
454  C CB  . THR A 54  ? 0.1415 0.1689 0.0759 0.0276  -0.0054 -0.0210 54  THR A CB  
455  O OG1 . THR A 54  ? 0.1488 0.2168 0.0690 0.0264  -0.0132 -0.0380 54  THR A OG1 
456  C CG2 . THR A 54  ? 0.1506 0.1571 0.1162 0.0242  0.0057  -0.0266 54  THR A CG2 
457  N N   A ASP A 55  ? 0.1188 0.1265 0.0571 0.0234  -0.0284 -0.0227 55  ASP A N   
458  N N   B ASP A 55  ? 0.1343 0.1585 0.0875 0.0298  -0.0117 -0.0475 55  ASP A N   
459  C CA  A ASP A 55  ? 0.1147 0.1158 0.0581 0.0168  -0.0135 -0.0034 55  ASP A CA  
460  C CA  B ASP A 55  ? 0.1285 0.1397 0.1490 0.0324  0.0120  -0.0106 55  ASP A CA  
461  C C   A ASP A 55  ? 0.1080 0.1159 0.0361 0.0100  0.0007  -0.0043 55  ASP A C   
462  C C   B ASP A 55  ? 0.1154 0.1352 0.1190 0.0149  0.0128  -0.0025 55  ASP A C   
463  O O   A ASP A 55  ? 0.1064 0.1221 0.0635 0.0047  -0.0084 0.0088  55  ASP A O   
464  O O   B ASP A 55  ? 0.1255 0.1408 0.1417 0.0103  0.0130  0.0275  55  ASP A O   
465  C CB  A ASP A 55  ? 0.1085 0.1256 0.0422 0.0068  -0.0010 0.0036  55  ASP A CB  
466  C CB  B ASP A 55  ? 0.1369 0.1754 0.1426 0.0137  0.0173  -0.0056 55  ASP A CB  
467  C CG  A ASP A 55  ? 0.1274 0.1299 0.0495 -0.0027 0.0080  0.0025  55  ASP A CG  
468  C CG  B ASP A 55  ? 0.1722 0.1956 0.1719 -0.0043 0.0216  0.0121  55  ASP A CG  
469  O OD1 A ASP A 55  ? 0.1534 0.1520 0.0728 0.0114  -0.0061 0.0145  55  ASP A OD1 
470  O OD1 B ASP A 55  ? 0.2939 0.2349 0.1827 -0.0421 0.0750  -0.0024 55  ASP A OD1 
471  O OD2 A ASP A 55  ? 0.2112 0.1506 0.0770 -0.0114 -0.0409 0.0025  55  ASP A OD2 
472  O OD2 B ASP A 55  ? 0.2700 0.2177 0.2156 -0.0124 0.0549  -0.0191 55  ASP A OD2 
473  N N   A CYS A 56  ? 0.1112 0.1052 0.0340 0.0052  -0.0028 0.0070  56  CYS A N   
474  N N   B CYS A 56  ? 0.1278 0.1427 0.0722 0.0136  0.0112  0.0030  56  CYS A N   
475  C CA  A CYS A 56  ? 0.1206 0.1025 0.0372 0.0091  -0.0042 0.0000  56  CYS A CA  
476  C CA  B CYS A 56  ? 0.1171 0.1436 0.0688 0.0091  0.0049  -0.0085 56  CYS A CA  
477  C C   A CYS A 56  ? 0.1083 0.1151 0.0397 0.0036  0.0012  0.0000  56  CYS A C   
478  C C   B CYS A 56  ? 0.1169 0.1489 0.0705 0.0179  0.0048  -0.0072 56  CYS A C   
479  O O   A CYS A 56  ? 0.1198 0.1143 0.0486 0.0128  0.0105  0.0066  56  CYS A O   
480  O O   B CYS A 56  ? 0.1530 0.1658 0.0667 0.0206  0.0162  -0.0068 56  CYS A O   
481  C CB  A CYS A 56  ? 0.1215 0.1145 0.0544 0.0026  -0.0031 -0.0006 56  CYS A CB  
482  C CB  B CYS A 56  ? 0.1153 0.1424 0.0957 0.0101  -0.0024 -0.0171 56  CYS A CB  
483  S SG  A CYS A 56  ? 0.1101 0.1449 0.0642 0.0138  -0.0058 -0.0119 56  CYS A SG  
484  S SG  B CYS A 56  ? 0.1098 0.1842 0.1028 0.0272  0.0037  -0.0141 56  CYS A SG  
485  N N   A TYR A 57  ? 0.1123 0.1128 0.0451 0.0066  0.0004  -0.0087 57  TYR A N   
486  N N   B TYR A 57  ? 0.1354 0.1455 0.0812 0.0157  0.0116  -0.0112 57  TYR A N   
487  C CA  A TYR A 57  ? 0.1230 0.1162 0.0420 0.0047  -0.0017 -0.0087 57  TYR A CA  
488  C CA  B TYR A 57  ? 0.1325 0.1609 0.0755 0.0109  0.0161  -0.0140 57  TYR A CA  
489  C C   A TYR A 57  ? 0.1392 0.1186 0.0515 0.0012  0.0005  0.0001  57  TYR A C   
490  C C   B TYR A 57  ? 0.1563 0.1583 0.0803 0.0004  0.0164  -0.0210 57  TYR A C   
491  O O   A TYR A 57  ? 0.1942 0.1256 0.0655 -0.0263 -0.0262 0.0090  57  TYR A O   
492  O O   B TYR A 57  ? 0.1772 0.1826 0.0869 -0.0332 0.0278  -0.0051 57  TYR A O   
493  C CB  A TYR A 57  ? 0.1285 0.1229 0.0427 0.0182  0.0072  -0.0080 57  TYR A CB  
494  C CB  B TYR A 57  ? 0.1293 0.1844 0.0732 0.0071  0.0231  -0.0306 57  TYR A CB  
495  C CG  A TYR A 57  ? 0.1224 0.1397 0.0662 0.0038  0.0150  -0.0044 57  TYR A CG  
496  C CG  B TYR A 57  ? 0.1643 0.2036 0.1698 -0.0084 0.0208  -0.0178 57  TYR A CG  
497  C CD1 A TYR A 57  ? 0.1626 0.1574 0.0582 -0.0022 0.0207  -0.0131 57  TYR A CD1 
498  C CD1 B TYR A 57  ? 0.1697 0.2372 0.1741 -0.0080 0.0264  -0.0195 57  TYR A CD1 
499  C CD2 A TYR A 57  ? 0.1309 0.1408 0.0761 0.0161  -0.0092 0.0029  57  TYR A CD2 
500  C CD2 B TYR A 57  ? 0.1884 0.2327 0.1816 0.0103  0.0295  -0.0396 57  TYR A CD2 
501  C CE1 A TYR A 57  ? 0.1842 0.1579 0.0455 0.0087  0.0092  0.0067  57  TYR A CE1 
502  C CE1 B TYR A 57  ? 0.0940 0.2246 0.2563 -0.0058 -0.0034 -0.0411 57  TYR A CE1 
503  C CE2 A TYR A 57  ? 0.1485 0.1575 0.0840 0.0016  -0.0062 0.0017  57  TYR A CE2 
504  C CE2 B TYR A 57  ? 0.1909 0.2410 0.2298 -0.0118 0.0425  -0.0722 57  TYR A CE2 
505  C CZ  A TYR A 57  ? 0.1480 0.1488 0.0763 0.0051  0.0205  0.0031  57  TYR A CZ  
506  C CZ  B TYR A 57  ? 0.1704 0.2384 0.2413 -0.0081 0.0395  -0.0486 57  TYR A CZ  
507  O OH  A TYR A 57  ? 0.1323 0.1675 0.0999 -0.0038 0.0259  0.0138  57  TYR A OH  
508  O OH  B TYR A 57  ? 0.2749 0.2257 0.3552 -0.0202 0.0177  -0.0298 57  TYR A OH  
509  N N   A PHE A 58  ? 0.1656 0.1345 0.0498 -0.0176 -0.0058 -0.0014 58  PHE A N   
510  N N   B PHE A 58  ? 0.1515 0.1759 0.0948 -0.0006 0.0107  -0.0207 58  PHE A N   
511  C CA  A PHE A 58  ? 0.1785 0.1371 0.0670 -0.0231 -0.0102 -0.0083 58  PHE A CA  
512  C CA  B PHE A 58  ? 0.1724 0.1629 0.1172 0.0052  0.0166  -0.0215 58  PHE A CA  
513  C C   A PHE A 58  ? 0.2309 0.1613 0.0733 -0.0248 -0.0115 -0.0205 58  PHE A C   
514  C C   B PHE A 58  ? 0.1956 0.2041 0.1315 0.0024  0.0167  -0.0474 58  PHE A C   
515  O O   A PHE A 58  ? 0.2974 0.1697 0.0698 -0.0228 -0.0228 -0.0189 58  PHE A O   
516  O O   B PHE A 58  ? 0.2357 0.2245 0.1293 -0.0105 0.0275  -0.0500 58  PHE A O   
517  C CB  A PHE A 58  ? 0.1729 0.1391 0.0823 -0.0243 -0.0190 -0.0029 58  PHE A CB  
518  C CB  B PHE A 58  ? 0.1689 0.1700 0.1377 0.0051  0.0199  -0.0127 58  PHE A CB  
519  C CG  A PHE A 58  ? 0.1505 0.1209 0.0917 -0.0165 -0.0183 -0.0052 58  PHE A CG  
520  C CG  B PHE A 58  ? 0.1391 0.1485 0.1416 -0.0003 0.0155  -0.0102 58  PHE A CG  
521  C CD1 A PHE A 58  ? 0.1438 0.1203 0.1052 -0.0033 -0.0120 0.0047  58  PHE A CD1 
522  C CD1 B PHE A 58  ? 0.1331 0.1376 0.1575 0.0033  0.0138  -0.0004 58  PHE A CD1 
523  C CD2 A PHE A 58  ? 0.1447 0.1258 0.1239 -0.0014 -0.0317 0.0133  58  PHE A CD2 
524  C CD2 B PHE A 58  ? 0.1253 0.1497 0.1482 0.0021  0.0022  0.0144  58  PHE A CD2 
525  C CE1 A PHE A 58  ? 0.1388 0.1409 0.1059 -0.0076 -0.0125 -0.0024 58  PHE A CE1 
526  C CE1 B PHE A 58  ? 0.1395 0.1487 0.1643 -0.0060 0.0287  -0.0085 58  PHE A CE1 
527  C CE2 A PHE A 58  ? 0.1377 0.1126 0.1542 0.0002  -0.0159 -0.0083 58  PHE A CE2 
528  C CE2 B PHE A 58  ? 0.1224 0.1392 0.1811 -0.0034 0.0253  -0.0073 58  PHE A CE2 
529  C CZ  A PHE A 58  ? 0.1355 0.1430 0.1310 -0.0059 -0.0084 -0.0169 58  PHE A CZ  
530  C CZ  B PHE A 58  ? 0.1345 0.1488 0.1717 -0.0056 0.0263  -0.0154 58  PHE A CZ  
531  N N   A ASP A 59  ? 0.2801 0.1618 0.0718 -0.0066 -0.0134 -0.0384 59  ASP A N   
532  N N   B ASP A 59  ? 0.2590 0.2124 0.1309 0.0341  0.0280  -0.0451 59  ASP A N   
533  C CA  A ASP A 59  ? 0.3155 0.1737 0.1180 0.0061  -0.0105 -0.0667 59  ASP A CA  
534  C CA  B ASP A 59  ? 0.3081 0.2354 0.1287 0.0539  0.0115  -0.0543 59  ASP A CA  
535  C C   A ASP A 59  ? 0.3419 0.2169 0.1176 0.0025  -0.0371 -0.0869 59  ASP A C   
536  C C   B ASP A 59  ? 0.3261 0.2656 0.1577 0.0686  -0.0314 -0.0633 59  ASP A C   
537  O O   A ASP A 59  ? 0.3574 0.2116 0.1384 0.0368  -0.0517 -0.0668 59  ASP A O   
538  O O   B ASP A 59  ? 0.3595 0.2656 0.1720 0.0861  -0.0366 -0.1059 59  ASP A O   
539  C CB  A ASP A 59  ? 0.3047 0.1813 0.1503 0.0273  0.0037  -0.0864 59  ASP A CB  
540  C CB  B ASP A 59  ? 0.3028 0.2467 0.1787 0.0587  -0.0024 -0.0532 59  ASP A CB  
541  C CG  A ASP A 59  ? 0.3064 0.1762 0.1662 0.0178  -0.0115 -0.0784 59  ASP A CG  
542  C CG  B ASP A 59  ? 0.2980 0.2354 0.1936 0.0553  -0.0059 -0.0543 59  ASP A CG  
543  O OD1 A ASP A 59  ? 0.2970 0.1588 0.1776 -0.0080 -0.0310 -0.0523 59  ASP A OD1 
544  O OD1 B ASP A 59  ? 0.2887 0.2545 0.2008 0.0344  -0.0139 -0.0912 59  ASP A OD1 
545  O OD2 A ASP A 59  ? 0.3324 0.1873 0.2508 0.0317  -0.0107 -0.0404 59  ASP A OD2 
546  O OD2 B ASP A 59  ? 0.3366 0.2713 0.2537 0.0678  -0.0358 -0.0279 59  ASP A OD2 
547  N N   A ASP A 60  ? 0.3813 0.2329 0.1356 0.0025  -0.0466 -0.1045 60  ASP A N   
548  N N   B ASP A 60  ? 0.3861 0.2939 0.1508 0.0696  -0.0199 -0.0741 60  ASP A N   
549  C CA  A ASP A 60  ? 0.4029 0.2890 0.1305 -0.0136 -0.0657 -0.1027 60  ASP A CA  
550  C CA  B ASP A 60  ? 0.4167 0.3608 0.2572 0.0399  -0.0639 -0.0769 60  ASP A CA  
551  C C   A ASP A 60  ? 0.3680 0.3040 0.1845 -0.0134 -0.0729 -0.0837 60  ASP A C   
552  C C   B ASP A 60  ? 0.4128 0.3464 0.2528 0.0292  -0.0700 -0.0901 60  ASP A C   
553  O O   A ASP A 60  ? 0.4084 0.3770 0.2591 -0.0536 -0.1356 -0.0725 60  ASP A O   
554  O O   B ASP A 60  ? 0.4172 0.3818 0.3384 0.0161  -0.1018 -0.0757 60  ASP A O   
555  C CB  A ASP A 60  ? 0.4328 0.3192 0.1506 -0.0028 -0.0444 -0.1193 60  ASP A CB  
556  C CB  B ASP A 60  ? 0.4879 0.4054 0.3008 0.0386  -0.0497 -0.1143 60  ASP A CB  
557  C CG  A ASP A 60  ? 0.4899 0.3883 0.1851 0.0081  0.0175  -0.1013 60  ASP A CG  
558  C CG  B ASP A 60  ? 0.5249 0.4772 0.3361 0.0435  -0.0336 -0.0758 60  ASP A CG  
559  O OD1 A ASP A 60  ? 0.5490 0.4357 0.2532 0.0565  0.0214  -0.0348 60  ASP A OD1 
560  O OD1 B ASP A 60  ? 0.6060 0.4835 0.4030 0.0522  -0.0068 -0.0615 60  ASP A OD1 
561  O OD2 A ASP A 60  ? 0.5170 0.4656 0.2699 0.0521  -0.0101 -0.1397 60  ASP A OD2 
562  O OD2 B ASP A 60  ? 0.5860 0.5409 0.2190 0.0363  -0.0383 -0.1273 60  ASP A OD2 
563  N N   A SER A 61  ? 0.3416 0.2089 0.1766 -0.0116 -0.0450 -0.0908 61  SER A N   
564  N N   B SER A 61  ? 0.3784 0.2666 0.2315 0.0453  -0.0434 -0.1274 61  SER A N   
565  C CA  A SER A 61  ? 0.3129 0.2369 0.2060 -0.0147 -0.0255 -0.1061 61  SER A CA  
566  C CA  B SER A 61  ? 0.3645 0.2846 0.2629 0.0398  -0.0371 -0.1066 61  SER A CA  
567  C C   A SER A 61  ? 0.2724 0.2187 0.2048 -0.0045 0.0004  -0.0749 61  SER A C   
568  C C   B SER A 61  ? 0.3069 0.2592 0.2159 0.0196  -0.0548 -0.0822 61  SER A C   
569  O O   A SER A 61  ? 0.2970 0.2787 0.2276 -0.0206 0.0386  -0.1042 61  SER A O   
570  O O   B SER A 61  ? 0.3491 0.2968 0.2131 0.0589  -0.0068 -0.0792 61  SER A O   
571  C CB  A SER A 61  ? 0.3601 0.1971 0.2679 -0.0022 0.0315  -0.0937 61  SER A CB  
572  C CB  B SER A 61  ? 0.3877 0.2644 0.2864 0.0564  -0.0205 -0.1170 61  SER A CB  
573  O OG  A SER A 61  ? 0.3545 0.2964 0.3234 -0.0424 0.0137  -0.0707 61  SER A OG  
574  O OG  B SER A 61  ? 0.3682 0.3245 0.3170 0.0763  -0.0733 -0.0665 61  SER A OG  
575  N N   A GLY A 62  ? 0.2014 0.2215 0.1919 0.0042  -0.0352 -0.0681 62  GLY A N   
576  N N   B GLY A 62  ? 0.2257 0.2338 0.1748 0.0648  -0.0268 -0.0833 62  GLY A N   
577  C CA  A GLY A 62  ? 0.1721 0.2171 0.1639 0.0153  -0.0369 -0.0503 62  GLY A CA  
578  C CA  B GLY A 62  ? 0.2028 0.2003 0.1699 0.0427  -0.0227 -0.0700 62  GLY A CA  
579  C C   A GLY A 62  ? 0.1643 0.1633 0.1539 0.0004  -0.0259 -0.0464 62  GLY A C   
580  C C   B GLY A 62  ? 0.1877 0.1449 0.1742 0.0213  -0.0194 -0.0649 62  GLY A C   
581  O O   A GLY A 62  ? 0.1712 0.1664 0.1495 0.0176  -0.0145 -0.0285 62  GLY A O   
582  O O   B GLY A 62  ? 0.1742 0.1487 0.1778 0.0206  -0.0105 -0.0598 62  GLY A O   
583  N N   A SER A 63  ? 0.1647 0.1381 0.1413 -0.0044 -0.0350 -0.0409 63  SER A N   
584  N N   B SER A 63  ? 0.1806 0.1545 0.1844 0.0074  -0.0141 -0.0699 63  SER A N   
585  C CA  A SER A 63  ? 0.1631 0.1368 0.1332 -0.0236 -0.0272 -0.0216 63  SER A CA  
586  C CA  B SER A 63  ? 0.1742 0.1658 0.2053 -0.0158 -0.0233 -0.0618 63  SER A CA  
587  C C   A SER A 63  ? 0.1498 0.1104 0.1065 -0.0050 -0.0236 -0.0180 63  SER A C   
588  C C   B SER A 63  ? 0.1432 0.1533 0.1868 0.0076  -0.0110 -0.0526 63  SER A C   
589  O O   A SER A 63  ? 0.1757 0.1474 0.1103 -0.0288 -0.0152 -0.0270 63  SER A O   
590  O O   B SER A 63  ? 0.1623 0.1698 0.1890 0.0128  0.0043  -0.0733 63  SER A O   
591  C CB  A SER A 63  ? 0.2190 0.1404 0.1803 -0.0237 -0.0351 -0.0076 63  SER A CB  
592  C CB  B SER A 63  ? 0.2069 0.1858 0.2562 0.0069  -0.0319 -0.0470 63  SER A CB  
593  O OG  A SER A 63  ? 0.2505 0.1957 0.2625 -0.0458 -0.0105 0.0130  63  SER A OG  
594  O OG  B SER A 63  ? 0.2789 0.2270 0.2989 -0.0339 0.0016  -0.0418 63  SER A OG  
595  N N   A GLY A 64  ? 0.1350 0.1021 0.0887 -0.0021 -0.0159 -0.0078 64  GLY A N   
596  N N   B GLY A 64  ? 0.1367 0.1405 0.1693 0.0016  -0.0006 -0.0405 64  GLY A N   
597  C CA  A GLY A 64  ? 0.1315 0.1137 0.0774 -0.0083 -0.0171 -0.0084 64  GLY A CA  
598  C CA  B GLY A 64  ? 0.1406 0.1381 0.1718 0.0044  0.0089  -0.0436 64  GLY A CA  
599  C C   A GLY A 64  ? 0.1181 0.1042 0.0651 -0.0014 -0.0045 -0.0035 64  GLY A C   
600  C C   B GLY A 64  ? 0.1184 0.1349 0.1515 0.0080  -0.0007 -0.0241 64  GLY A C   
601  O O   A GLY A 64  ? 0.1460 0.1051 0.0746 -0.0054 -0.0188 0.0023  64  GLY A O   
602  O O   B GLY A 64  ? 0.1267 0.1292 0.1683 -0.0067 -0.0118 -0.0143 64  GLY A O   
603  N N   A ILE A 65  ? 0.1169 0.1036 0.0554 0.0016  -0.0134 -0.0043 65  ILE A N   
604  N N   B ILE A 65  ? 0.0964 0.1389 0.1200 0.0002  0.0032  -0.0191 65  ILE A N   
605  C CA  A ILE A 65  ? 0.1193 0.0971 0.0459 0.0061  -0.0081 -0.0019 65  ILE A CA  
606  C CA  B ILE A 65  ? 0.1130 0.1279 0.1086 0.0021  0.0137  -0.0140 65  ILE A CA  
607  C C   A ILE A 65  ? 0.1021 0.1001 0.0398 0.0056  -0.0119 0.0000  65  ILE A C   
608  C C   B ILE A 65  ? 0.1036 0.1332 0.0963 0.0089  0.0132  -0.0054 65  ILE A C   
609  O O   A ILE A 65  ? 0.1386 0.1033 0.0406 0.0079  -0.0119 0.0016  65  ILE A O   
610  O O   B ILE A 65  ? 0.1444 0.1398 0.0856 0.0126  -0.0012 -0.0091 65  ILE A O   
611  C CB  A ILE A 65  ? 0.1241 0.1144 0.0624 0.0098  -0.0082 0.0019  65  ILE A CB  
612  C CB  B ILE A 65  ? 0.1168 0.1232 0.1217 0.0083  0.0061  -0.0047 65  ILE A CB  
613  C CG1 A ILE A 65  ? 0.1386 0.1306 0.0806 0.0152  -0.0154 -0.0176 65  ILE A CG1 
614  C CG1 B ILE A 65  ? 0.1917 0.1482 0.1227 0.0028  -0.0189 -0.0013 65  ILE A CG1 
615  C CG2 A ILE A 65  ? 0.1267 0.1279 0.0696 -0.0036 -0.0020 -0.0042 65  ILE A CG2 
616  C CG2 B ILE A 65  ? 0.1155 0.1493 0.1280 0.0081  0.0141  -0.0089 65  ILE A CG2 
617  C CD1 A ILE A 65  ? 0.1397 0.1512 0.1191 0.0060  -0.0264 -0.0203 65  ILE A CD1 
618  C CD1 B ILE A 65  ? 0.1951 0.1823 0.1478 0.0006  -0.0184 0.0310  65  ILE A CD1 
619  N N   A CYS A 66  ? 0.1230 0.1020 0.0484 0.0130  -0.0105 -0.0068 66  CYS A N   
620  N N   B CYS A 66  ? 0.1190 0.1353 0.0918 0.0168  0.0168  -0.0008 66  CYS A N   
621  C CA  A CYS A 66  ? 0.1314 0.0998 0.0523 0.0119  -0.0209 -0.0023 66  CYS A CA  
622  C CA  B CYS A 66  ? 0.1221 0.1368 0.0876 0.0264  0.0131  -0.0044 66  CYS A CA  
623  C C   A CYS A 66  ? 0.1159 0.1009 0.0403 0.0069  -0.0031 -0.0018 66  CYS A C   
624  C C   B CYS A 66  ? 0.1125 0.1202 0.0974 0.0268  0.0028  0.0123  66  CYS A C   
625  O O   A CYS A 66  ? 0.1341 0.1129 0.0431 0.0040  -0.0180 -0.0001 66  CYS A O   
626  O O   B CYS A 66  ? 0.1287 0.1379 0.0893 0.0223  0.0101  0.0110  66  CYS A O   
627  C CB  A CYS A 66  ? 0.1359 0.1195 0.0906 0.0207  -0.0206 -0.0307 66  CYS A CB  
628  C CB  B CYS A 66  ? 0.1203 0.1497 0.1049 0.0196  0.0204  -0.0028 66  CYS A CB  
629  S SG  A CYS A 66  ? 0.1264 0.1458 0.1107 0.0043  -0.0098 -0.0432 66  CYS A SG  
630  S SG  B CYS A 66  ? 0.1545 0.1868 0.1580 0.0158  -0.0061 -0.0152 66  CYS A SG  
631  N N   A LYS A 67  ? 0.1068 0.1036 0.0327 0.0073  -0.0042 0.0099  67  LYS A N   
632  N N   B LYS A 67  ? 0.1030 0.1404 0.1225 0.0208  0.0069  0.0345  67  LYS A N   
633  C CA  A LYS A 67  ? 0.1054 0.1139 0.0306 0.0137  -0.0051 0.0007  67  LYS A CA  
634  C CA  B LYS A 67  ? 0.0950 0.1541 0.1605 0.0036  -0.0062 0.0461  67  LYS A CA  
635  C C   A LYS A 67  ? 0.0951 0.0970 0.0303 0.0061  -0.0046 0.0034  67  LYS A C   
636  C C   B LYS A 67  ? 0.0878 0.1474 0.1582 -0.0051 -0.0145 0.0397  67  LYS A C   
637  O O   A LYS A 67  ? 0.0897 0.1158 0.0336 0.0036  -0.0075 0.0037  67  LYS A O   
638  O O   B LYS A 67  ? 0.0905 0.1920 0.1785 -0.0111 -0.0351 0.0479  67  LYS A O   
639  C CB  A LYS A 67  ? 0.1173 0.1139 0.0305 0.0127  -0.0009 -0.0056 67  LYS A CB  
640  C CB  B LYS A 67  ? 0.1598 0.1837 0.2160 -0.0174 0.0191  0.0652  67  LYS A CB  
641  C CG  A LYS A 67  ? 0.1176 0.1204 0.0465 0.0090  0.0055  -0.0097 67  LYS A CG  
642  C CG  B LYS A 67  ? 0.1731 0.1982 0.2053 -0.0129 0.0287  0.0575  67  LYS A CG  
643  C CD  A LYS A 67  ? 0.1388 0.1374 0.0384 -0.0012 0.0147  -0.0051 67  LYS A CD  
644  C CD  B LYS A 67  ? 0.1715 0.2128 0.1699 -0.0302 0.0172  0.0484  67  LYS A CD  
645  C CE  A LYS A 67  ? 0.1315 0.1539 0.0615 0.0043  0.0182  -0.0023 67  LYS A CE  
646  C CE  B LYS A 67  ? 0.1690 0.2133 0.1876 -0.0262 0.0131  0.0225  67  LYS A CE  
647  N NZ  A LYS A 67  ? 0.1459 0.1562 0.0649 -0.0018 0.0144  -0.0050 67  LYS A NZ  
648  N NZ  B LYS A 67  ? 0.1776 0.2117 0.1362 -0.0173 0.0295  0.0204  67  LYS A NZ  
649  N N   A THR A 68  ? 0.0880 0.1054 0.0258 -0.0007 -0.0040 0.0045  68  THR A N   
650  N N   B THR A 68  ? 0.0912 0.1323 0.1348 -0.0025 -0.0183 0.0253  68  THR A N   
651  C CA  A THR A 68  ? 0.0871 0.1042 0.0258 -0.0012 -0.0058 0.0001  68  THR A CA  
652  C CA  B THR A 68  ? 0.0887 0.1269 0.1211 -0.0063 -0.0279 0.0141  68  THR A CA  
653  C C   A THR A 68  ? 0.0847 0.0996 0.0276 0.0015  -0.0087 0.0039  68  THR A C   
654  C C   B THR A 68  ? 0.0926 0.1064 0.0903 -0.0038 -0.0306 0.0047  68  THR A C   
655  O O   A THR A 68  ? 0.0911 0.1087 0.0337 -0.0005 -0.0165 0.0023  68  THR A O   
656  O O   B THR A 68  ? 0.0903 0.1340 0.0832 0.0011  -0.0195 -0.0078 68  THR A O   
657  C CB  A THR A 68  ? 0.0959 0.1072 0.0256 0.0042  -0.0038 0.0028  68  THR A CB  
658  C CB  B THR A 68  ? 0.1094 0.1303 0.1245 -0.0083 -0.0168 0.0025  68  THR A CB  
659  O OG1 A THR A 68  ? 0.0947 0.1139 0.0259 0.0039  -0.0059 0.0022  68  THR A OG1 
660  O OG1 B THR A 68  ? 0.1049 0.1284 0.1181 -0.0035 -0.0008 0.0131  68  THR A OG1 
661  C CG2 A THR A 68  ? 0.0980 0.1105 0.0403 0.0028  -0.0010 0.0020  68  THR A CG2 
662  C CG2 B THR A 68  ? 0.1273 0.1369 0.1390 -0.0221 -0.0193 0.0061  68  THR A CG2 
663  N N   A GLY A 69  ? 0.0816 0.1073 0.0362 -0.0001 -0.0035 0.0079  69  GLY A N   
664  N N   B GLY A 69  ? 0.1043 0.1129 0.0757 0.0037  -0.0370 0.0031  69  GLY A N   
665  C CA  A GLY A 69  ? 0.0883 0.1060 0.0496 -0.0037 -0.0082 0.0054  69  GLY A CA  
666  C CA  B GLY A 69  ? 0.0972 0.1109 0.0515 0.0095  -0.0231 -0.0024 69  GLY A CA  
667  C C   A GLY A 69  ? 0.0906 0.1025 0.0447 -0.0075 -0.0044 0.0131  69  GLY A C   
668  C C   B GLY A 69  ? 0.0927 0.1047 0.0469 0.0072  -0.0216 0.0081  69  GLY A C   
669  O O   A GLY A 69  ? 0.0916 0.1061 0.0532 -0.0078 -0.0020 0.0131  69  GLY A O   
670  O O   B GLY A 69  ? 0.0885 0.1066 0.0667 0.0042  -0.0099 0.0065  69  GLY A O   
671  N N   A ASP A 70  ? 0.0996 0.1013 0.0513 -0.0013 -0.0052 0.0049  70  ASP A N   
672  N N   B ASP A 70  ? 0.0991 0.1125 0.0730 0.0075  -0.0153 0.0048  70  ASP A N   
673  C CA  A ASP A 70  ? 0.1156 0.0966 0.0692 -0.0021 0.0008  0.0049  70  ASP A CA  
674  C CA  B ASP A 70  ? 0.1081 0.1088 0.0818 0.0038  -0.0092 0.0119  70  ASP A CA  
675  C C   A ASP A 70  ? 0.1113 0.1052 0.0742 -0.0010 -0.0013 0.0106  70  ASP A C   
676  C C   B ASP A 70  ? 0.0916 0.1079 0.0822 0.0040  -0.0065 0.0055  70  ASP A C   
677  O O   A ASP A 70  ? 0.1236 0.1175 0.0744 -0.0019 -0.0084 0.0157  70  ASP A O   
678  O O   B ASP A 70  ? 0.1104 0.1256 0.0806 0.0024  -0.0029 0.0101  70  ASP A O   
679  C CB  A ASP A 70  ? 0.1304 0.1159 0.0835 0.0133  0.0046  0.0066  70  ASP A CB  
680  C CB  B ASP A 70  ? 0.1224 0.1247 0.0981 0.0223  -0.0103 0.0102  70  ASP A CB  
681  C CG  A ASP A 70  ? 0.2046 0.1250 0.1138 -0.0010 -0.0337 -0.0297 70  ASP A CG  
682  C CG  B ASP A 70  ? 0.1400 0.1255 0.1166 0.0269  -0.0253 0.0068  70  ASP A CG  
683  O OD1 A ASP A 70  ? 0.1690 0.1685 0.1120 0.0246  0.0002  -0.0222 70  ASP A OD1 
684  O OD1 B ASP A 70  ? 0.1377 0.1494 0.1431 0.0226  -0.0143 -0.0101 70  ASP A OD1 
685  O OD2 A ASP A 70  ? 0.1913 0.1550 0.1603 0.0005  -0.0391 0.0016  70  ASP A OD2 
686  O OD2 B ASP A 70  ? 0.1289 0.1041 0.0752 0.0068  0.0003  -0.0044 70  ASP A OD2 
687  N N   A CYS A 71  ? 0.1108 0.1121 0.0979 -0.0115 0.0038  0.0100  71  CYS A N   
688  N N   B CYS A 71  ? 0.1022 0.1062 0.1058 0.0021  -0.0143 0.0012  71  CYS A N   
689  C CA  A CYS A 71  ? 0.1256 0.1261 0.1136 -0.0085 0.0178  0.0183  71  CYS A CA  
690  C CA  B CYS A 71  ? 0.1230 0.1156 0.1113 -0.0023 -0.0097 0.0051  71  CYS A CA  
691  C C   A CYS A 71  ? 0.1296 0.1332 0.1217 -0.0012 0.0066  0.0175  71  CYS A C   
692  C C   B CYS A 71  ? 0.1330 0.1171 0.1318 0.0009  -0.0153 0.0134  71  CYS A C   
693  O O   A CYS A 71  ? 0.1496 0.1348 0.1666 -0.0067 -0.0018 0.0021  71  CYS A O   
694  O O   B CYS A 71  ? 0.1368 0.1275 0.1572 0.0090  -0.0212 -0.0081 71  CYS A O   
695  C CB  A CYS A 71  ? 0.1296 0.1248 0.1311 -0.0081 0.0082  0.0051  71  CYS A CB  
696  C CB  B CYS A 71  ? 0.1244 0.1249 0.1269 0.0088  -0.0044 0.0111  71  CYS A CB  
697  S SG  A CYS A 71  ? 0.1282 0.1340 0.1356 -0.0088 -0.0099 -0.0019 71  CYS A SG  
698  S SG  B CYS A 71  ? 0.1126 0.1439 0.1343 -0.0074 -0.0086 -0.0034 71  CYS A SG  
699  N N   A GLY A 72  ? 0.1458 0.1482 0.1083 0.0098  -0.0007 0.0167  72  GLY A N   
700  N N   B GLY A 72  ? 0.1442 0.1286 0.1415 0.0104  -0.0218 0.0140  72  GLY A N   
701  C CA  A GLY A 72  ? 0.1613 0.1447 0.1286 0.0185  0.0074  0.0385  72  GLY A CA  
702  C CA  B GLY A 72  ? 0.1396 0.1347 0.1565 0.0198  -0.0041 0.0258  72  GLY A CA  
703  C C   A GLY A 72  ? 0.1368 0.1222 0.1307 0.0112  -0.0066 0.0240  72  GLY A C   
704  C C   B GLY A 72  ? 0.1279 0.1203 0.1610 0.0186  -0.0059 0.0032  72  GLY A C   
705  O O   A GLY A 72  ? 0.1776 0.1307 0.1604 -0.0049 0.0030  0.0121  72  GLY A O   
706  O O   B GLY A 72  ? 0.1496 0.1065 0.1985 0.0158  -0.0087 0.0185  72  GLY A O   
707  N N   A GLY A 73  ? 0.1344 0.1179 0.1038 0.0084  -0.0031 0.0101  73  GLY A N   
708  N N   B GLY A 73  ? 0.1310 0.1169 0.1408 0.0193  -0.0073 -0.0070 73  GLY A N   
709  C CA  A GLY A 73  ? 0.1410 0.1188 0.1023 0.0093  -0.0107 0.0032  73  GLY A CA  
710  C CA  B GLY A 73  ? 0.1418 0.1295 0.1420 0.0039  0.0038  0.0044  73  GLY A CA  
711  C C   A GLY A 73  ? 0.1426 0.1187 0.0984 0.0055  -0.0067 0.0034  73  GLY A C   
712  C C   B GLY A 73  ? 0.1508 0.1174 0.1512 -0.0024 0.0042  -0.0113 73  GLY A C   
713  O O   A GLY A 73  ? 0.1551 0.1878 0.1194 -0.0032 0.0003  -0.0332 73  GLY A O   
714  O O   B GLY A 73  ? 0.1817 0.2038 0.1583 -0.0393 0.0381  -0.0297 73  GLY A O   
715  N N   A LEU A 74  ? 0.1358 0.1082 0.1080 0.0029  -0.0155 -0.0009 74  LEU A N   
716  N N   B LEU A 74  ? 0.1501 0.1054 0.1286 0.0197  -0.0153 0.0022  74  LEU A N   
717  C CA  A LEU A 74  ? 0.1363 0.1073 0.1184 0.0028  -0.0175 -0.0071 74  LEU A CA  
718  C CA  B LEU A 74  ? 0.1544 0.1074 0.1476 0.0101  -0.0161 -0.0079 74  LEU A CA  
719  C C   A LEU A 74  ? 0.1338 0.1052 0.1123 -0.0082 -0.0175 -0.0042 74  LEU A C   
720  C C   B LEU A 74  ? 0.1328 0.1114 0.1163 0.0039  -0.0133 -0.0100 74  LEU A C   
721  O O   A LEU A 74  ? 0.1508 0.1036 0.1221 -0.0024 -0.0197 -0.0065 74  LEU A O   
722  O O   B LEU A 74  ? 0.1424 0.1072 0.1159 0.0105  -0.0197 -0.0074 74  LEU A O   
723  C CB  A LEU A 74  ? 0.1521 0.1222 0.1469 -0.0055 -0.0100 0.0050  74  LEU A CB  
724  C CB  B LEU A 74  ? 0.1620 0.1183 0.1508 0.0059  -0.0141 -0.0026 74  LEU A CB  
725  C CG  A LEU A 74  ? 0.1818 0.1307 0.1954 -0.0070 -0.0061 0.0263  74  LEU A CG  
726  C CG  B LEU A 74  ? 0.1916 0.1273 0.1918 0.0013  -0.0118 0.0166  74  LEU A CG  
727  C CD1 A LEU A 74  ? 0.2023 0.1521 0.2241 -0.0195 0.0087  0.0249  74  LEU A CD1 
728  C CD1 B LEU A 74  ? 0.1964 0.1501 0.2029 -0.0115 -0.0078 0.0107  74  LEU A CD1 
729  C CD2 A LEU A 74  ? 0.2104 0.1362 0.2315 -0.0064 0.0209  0.0238  74  LEU A CD2 
730  C CD2 B LEU A 74  ? 0.1885 0.1328 0.2111 0.0042  0.0087  0.0206  74  LEU A CD2 
731  N N   A LEU A 75  ? 0.1321 0.1061 0.1208 0.0036  -0.0301 -0.0178 75  LEU A N   
732  N N   B LEU A 75  ? 0.1279 0.1187 0.1176 0.0031  -0.0129 -0.0172 75  LEU A N   
733  C CA  A LEU A 75  ? 0.1277 0.1099 0.1159 -0.0066 -0.0352 -0.0083 75  LEU A CA  
734  C CA  B LEU A 75  ? 0.1265 0.1190 0.1214 -0.0024 -0.0111 -0.0105 75  LEU A CA  
735  C C   A LEU A 75  ? 0.1246 0.1092 0.1515 -0.0025 -0.0263 -0.0163 75  LEU A C   
736  C C   B LEU A 75  ? 0.1161 0.1232 0.1208 0.0002  -0.0224 -0.0137 75  LEU A C   
737  O O   A LEU A 75  ? 0.1141 0.1109 0.1726 0.0056  -0.0363 -0.0192 75  LEU A O   
738  O O   B LEU A 75  ? 0.1057 0.1314 0.1491 0.0014  -0.0154 -0.0233 75  LEU A O   
739  C CB  A LEU A 75  ? 0.1557 0.1271 0.1173 -0.0053 -0.0387 -0.0070 75  LEU A CB  
740  C CB  B LEU A 75  ? 0.1454 0.1364 0.1217 -0.0058 -0.0106 -0.0088 75  LEU A CB  
741  C CG  A LEU A 75  ? 0.1512 0.1443 0.1549 -0.0044 -0.0476 0.0025  75  LEU A CG  
742  C CG  B LEU A 75  ? 0.1565 0.1594 0.1318 -0.0045 -0.0154 0.0057  75  LEU A CG  
743  C CD1 A LEU A 75  ? 0.1404 0.1424 0.1262 0.0026  -0.0462 -0.0008 75  LEU A CD1 
744  C CD1 B LEU A 75  ? 0.1555 0.1678 0.1420 -0.0173 -0.0144 0.0075  75  LEU A CD1 
745  C CD2 A LEU A 75  ? 0.1906 0.1709 0.1651 -0.0166 -0.0629 -0.0003 75  LEU A CD2 
746  C CD2 B LEU A 75  ? 0.1806 0.1851 0.1385 -0.0138 -0.0233 -0.0046 75  LEU A CD2 
747  N N   A ARG A 76  ? 0.1265 0.1074 0.1703 -0.0012 -0.0234 -0.0096 76  ARG A N   
748  N N   B ARG A 76  ? 0.1328 0.1161 0.1518 0.0023  -0.0175 -0.0139 76  ARG A N   
749  C CA  A ARG A 76  ? 0.1391 0.1222 0.1942 0.0027  -0.0081 0.0027  76  ARG A CA  
750  C CA  B ARG A 76  ? 0.1368 0.1195 0.1543 -0.0012 -0.0172 -0.0132 76  ARG A CA  
751  C C   A ARG A 76  ? 0.1181 0.1183 0.1995 0.0041  0.0014  0.0171  76  ARG A C   
752  C C   B ARG A 76  ? 0.1268 0.1169 0.1598 0.0020  -0.0081 0.0004  76  ARG A C   
753  O O   A ARG A 76  ? 0.1815 0.1305 0.2020 0.0114  0.0002  0.0287  76  ARG A O   
754  O O   B ARG A 76  ? 0.1818 0.1246 0.1795 0.0000  -0.0072 0.0113  76  ARG A O   
755  C CB  A ARG A 76  ? 0.1487 0.1464 0.2353 -0.0028 -0.0216 -0.0111 76  ARG A CB  
756  C CB  B ARG A 76  ? 0.1701 0.1363 0.1719 -0.0090 -0.0174 -0.0320 76  ARG A CB  
757  C CG  A ARG A 76  ? 0.1889 0.1960 0.2196 0.0069  -0.0671 -0.0464 76  ARG A CG  
758  C CG  B ARG A 76  ? 0.2382 0.2057 0.1663 -0.0411 -0.0453 -0.0594 76  ARG A CG  
759  C CD  A ARG A 76  ? 0.2902 0.2306 0.2156 -0.0114 -0.1052 -0.0589 76  ARG A CD  
760  C CD  B ARG A 76  ? 0.2733 0.2703 0.2501 0.0090  -0.0455 -0.0426 76  ARG A CD  
761  N NE  A ARG A 76  ? 0.3258 0.2880 0.3333 0.0144  -0.0686 -0.0737 76  ARG A NE  
762  N NE  B ARG A 76  ? 0.3625 0.2874 0.3257 -0.0248 -0.0588 -0.0977 76  ARG A NE  
763  C CZ  A ARG A 76  ? 0.3981 0.3101 0.3911 -0.0362 -0.0737 -0.0572 76  ARG A CZ  
764  C CZ  B ARG A 76  ? 0.3933 0.3706 0.3239 -0.0284 -0.0737 -0.0738 76  ARG A CZ  
765  N NH1 A ARG A 76  ? 0.4022 0.4093 0.4294 -0.0413 -0.0442 -0.0803 76  ARG A NH1 
766  N NH1 B ARG A 76  ? 0.4346 0.3951 0.3346 -0.0339 -0.0716 -0.0606 76  ARG A NH1 
767  N NH2 A ARG A 76  ? 0.3816 0.3644 0.4274 -0.0256 -0.0671 -0.0678 76  ARG A NH2 
768  N NH2 B ARG A 76  ? 0.4457 0.4295 0.2958 -0.0884 -0.0934 -0.0783 76  ARG A NH2 
769  N N   A CYS A 77  ? 0.1343 0.1179 0.1934 -0.0061 -0.0240 0.0182  77  CYS A N   
770  N N   B CYS A 77  ? 0.1253 0.1127 0.1252 -0.0037 -0.0202 0.0129  77  CYS A N   
771  C CA  A CYS A 77  ? 0.1240 0.1192 0.1926 0.0021  -0.0188 0.0225  77  CYS A CA  
772  C CA  B CYS A 77  ? 0.1224 0.1335 0.1235 0.0020  -0.0135 0.0214  77  CYS A CA  
773  C C   A CYS A 77  ? 0.1333 0.1548 0.2227 -0.0125 -0.0122 0.0294  77  CYS A C   
774  C C   B CYS A 77  ? 0.1390 0.1384 0.1473 -0.0103 -0.0134 0.0351  77  CYS A C   
775  O O   A CYS A 77  ? 0.1384 0.1891 0.2135 -0.0084 -0.0060 0.0657  77  CYS A O   
776  O O   B CYS A 77  ? 0.1257 0.2146 0.1780 -0.0161 0.0090  0.0551  77  CYS A O   
777  C CB  A CYS A 77  ? 0.1352 0.1171 0.1749 -0.0113 -0.0071 0.0280  77  CYS A CB  
778  C CB  B CYS A 77  ? 0.1058 0.1327 0.1113 0.0039  -0.0107 0.0190  77  CYS A CB  
779  S SG  A CYS A 77  ? 0.1306 0.1136 0.1501 -0.0073 -0.0025 0.0038  77  CYS A SG  
780  S SG  B CYS A 77  ? 0.1172 0.1325 0.1263 -0.0073 0.0000  0.0022  77  CYS A SG  
781  N N   A LYS A 78  ? 0.1430 0.1472 0.2070 -0.0059 -0.0442 -0.0026 78  LYS A N   
782  N N   B LYS A 78  ? 0.1642 0.1401 0.1250 -0.0164 -0.0481 0.0136  78  LYS A N   
783  C CA  A LYS A 78  ? 0.2167 0.1680 0.2041 -0.0129 -0.0141 -0.0106 78  LYS A CA  
784  C CA  B LYS A 78  ? 0.2179 0.1617 0.1398 -0.0183 -0.0233 0.0269  78  LYS A CA  
785  C C   A LYS A 78  ? 0.3092 0.1163 0.2137 -0.0150 -0.0451 -0.0041 78  LYS A C   
786  C C   B LYS A 78  ? 0.2967 0.1360 0.1486 0.0043  -0.0525 0.0235  78  LYS A C   
787  O O   A LYS A 78  ? 0.3318 0.2410 0.2818 -0.0226 0.0002  -0.0494 78  LYS A O   
788  O O   B LYS A 78  ? 0.3212 0.1404 0.1523 0.0080  -0.0329 0.0026  78  LYS A O   
789  C CB  A LYS A 78  ? 0.2691 0.1708 0.3025 -0.0524 0.0024  -0.0047 78  LYS A CB  
790  C CB  B LYS A 78  ? 0.2645 0.1603 0.1916 -0.0544 0.0001  0.0123  78  LYS A CB  
791  C CG  A LYS A 78  ? 0.3052 0.2413 0.3213 -0.0260 0.0249  -0.0249 78  LYS A CG  
792  C CG  B LYS A 78  ? 0.3115 0.2204 0.2316 -0.0390 0.0146  -0.0257 78  LYS A CG  
793  C CD  A LYS A 78  ? 0.3548 0.2452 0.3820 -0.0267 0.0326  -0.0254 78  LYS A CD  
794  C CD  B LYS A 78  ? 0.3406 0.2344 0.3251 -0.0311 0.0133  0.0164  78  LYS A CD  
795  C CE  A LYS A 78  ? 0.3816 0.3219 0.3955 -0.0337 0.0031  -0.0199 78  LYS A CE  
796  C CE  B LYS A 78  ? 0.3889 0.2602 0.3607 -0.0299 0.0100  -0.0091 78  LYS A CE  
797  N NZ  A LYS A 78  ? 0.4004 0.2906 0.4174 -0.0498 0.0251  -0.0182 78  LYS A NZ  
798  N NZ  B LYS A 78  ? 0.4267 0.2896 0.4180 -0.0054 0.0174  0.0383  78  LYS A NZ  
799  N N   . ARG A 79  ? 0.2975 0.1453 0.1507 -0.0019 -0.0403 0.0178  79  ARG A N   
800  C CA  . ARG A 79  ? 0.3299 0.1375 0.1353 0.0108  -0.0430 0.0268  79  ARG A CA  
801  C C   . ARG A 79  ? 0.2608 0.1389 0.1232 0.0151  -0.0535 0.0277  79  ARG A C   
802  O O   . ARG A 79  ? 0.2869 0.1295 0.1192 0.0107  -0.0449 0.0208  79  ARG A O   
803  C CB  . ARG A 79  ? 0.4084 0.1621 0.1648 0.0395  -0.0990 0.0373  79  ARG A CB  
804  C CG  . ARG A 79  ? 0.4823 0.1724 0.2954 0.0242  -0.0820 0.0272  79  ARG A CG  
805  C CD  . ARG A 79  ? 0.5213 0.2562 0.3370 0.0173  -0.0447 0.0376  79  ARG A CD  
806  N NE  . ARG A 79  ? 0.5980 0.2717 0.4268 -0.0343 -0.0449 0.0780  79  ARG A NE  
807  C CZ  . ARG A 79  ? 0.5814 0.2974 0.4312 0.0231  -0.0612 0.0142  79  ARG A CZ  
808  N NH1 . ARG A 79  ? 0.5509 0.2492 0.3843 0.0043  -0.0234 0.0348  79  ARG A NH1 
809  N NH2 . ARG A 79  ? 0.6209 0.3017 0.4989 0.0304  -0.0387 0.0393  79  ARG A NH2 
810  N N   . PHE A 80  ? 0.2475 0.1380 0.1089 -0.0014 -0.0443 0.0382  80  PHE A N   
811  C CA  . PHE A 80  ? 0.2098 0.1383 0.1013 0.0046  -0.0469 0.0270  80  PHE A CA  
812  C C   . PHE A 80  ? 0.2114 0.1352 0.1046 0.0145  -0.0557 0.0260  80  PHE A C   
813  O O   . PHE A 80  ? 0.2493 0.1545 0.1917 0.0401  -0.0411 0.0377  80  PHE A O   
814  C CB  . PHE A 80  ? 0.2213 0.1497 0.1002 0.0037  -0.0561 0.0230  80  PHE A CB  
815  C CG  . PHE A 80  ? 0.2141 0.1419 0.1037 -0.0089 -0.0375 0.0231  80  PHE A CG  
816  C CD1 . PHE A 80  ? 0.2160 0.1418 0.1143 -0.0040 -0.0443 0.0118  80  PHE A CD1 
817  C CD2 . PHE A 80  ? 0.2528 0.1707 0.1073 0.0045  -0.0319 0.0319  80  PHE A CD2 
818  C CE1 . PHE A 80  ? 0.2054 0.1456 0.1455 -0.0149 -0.0420 0.0037  80  PHE A CE1 
819  C CE2 . PHE A 80  ? 0.2510 0.1836 0.1406 -0.0072 -0.0190 0.0208  80  PHE A CE2 
820  C CZ  . PHE A 80  ? 0.2185 0.1607 0.1542 -0.0082 -0.0146 -0.0047 80  PHE A CZ  
821  N N   . GLY A 81  ? 0.1987 0.1329 0.0966 0.0055  -0.0444 0.0149  81  GLY A N   
822  C CA  . GLY A 81  ? 0.2100 0.1479 0.0883 0.0163  -0.0507 0.0055  81  GLY A CA  
823  C C   . GLY A 81  ? 0.1934 0.1269 0.0713 0.0153  -0.0356 0.0133  81  GLY A C   
824  O O   . GLY A 81  ? 0.1807 0.1526 0.0683 0.0052  -0.0232 0.0134  81  GLY A O   
825  N N   . ARG A 82  ? 0.1980 0.1322 0.0696 0.0189  -0.0345 0.0069  82  ARG A N   
826  C CA  A ARG A 82  ? 0.1770 0.1348 0.0509 0.0249  -0.0221 0.0176  82  ARG A CA  
827  C CA  B ARG A 82  ? 0.1960 0.1384 0.0646 0.0139  -0.0301 0.0169  82  ARG A CA  
828  C C   . ARG A 82  ? 0.1531 0.1336 0.0473 0.0191  -0.0193 0.0160  82  ARG A C   
829  O O   . ARG A 82  ? 0.1994 0.1398 0.0385 0.0267  -0.0220 0.0161  82  ARG A O   
830  C CB  A ARG A 82  ? 0.1725 0.1058 0.0556 0.0250  -0.0238 0.0222  82  ARG A CB  
831  C CB  B ARG A 82  ? 0.2220 0.1572 0.0823 0.0020  -0.0026 0.0229  82  ARG A CB  
832  C CG  A ARG A 82  ? 0.1709 0.1256 0.0468 0.0385  -0.0348 -0.0012 82  ARG A CG  
833  C CG  B ARG A 82  ? 0.2133 0.2019 0.1337 0.0110  -0.0064 0.0412  82  ARG A CG  
834  C CD  A ARG A 82  ? 0.1236 0.1424 0.0949 0.0081  0.0035  0.0153  82  ARG A CD  
835  C CD  B ARG A 82  ? 0.1714 0.1836 0.1174 0.0123  0.0154  0.0394  82  ARG A CD  
836  N NE  A ARG A 82  ? 0.1292 0.1429 0.1068 0.0157  0.0034  0.0339  82  ARG A NE  
837  N NE  B ARG A 82  ? 0.1428 0.1836 0.1019 0.0091  -0.0031 0.0407  82  ARG A NE  
838  C CZ  A ARG A 82  ? 0.1442 0.1384 0.0676 0.0269  0.0091  0.0187  82  ARG A CZ  
839  C CZ  B ARG A 82  ? 0.1466 0.1806 0.1172 0.0213  -0.0155 0.0301  82  ARG A CZ  
840  N NH1 A ARG A 82  ? 0.1337 0.1336 0.0714 0.0003  0.0043  0.0196  82  ARG A NH1 
841  N NH1 B ARG A 82  ? 0.1344 0.1855 0.1251 0.0312  -0.0039 0.0192  82  ARG A NH1 
842  N NH2 A ARG A 82  ? 0.1319 0.1803 0.1067 -0.0131 -0.0027 0.0422  82  ARG A NH2 
843  N NH2 B ARG A 82  ? 0.1908 0.1734 0.1514 0.0311  -0.0331 0.0534  82  ARG A NH2 
844  N N   . PRO A 83  ? 0.1264 0.1389 0.0403 0.0088  -0.0113 0.0188  83  PRO A N   
845  C CA  . PRO A 83  ? 0.1176 0.1399 0.0380 0.0190  -0.0088 0.0182  83  PRO A CA  
846  C C   . PRO A 83  ? 0.1182 0.1375 0.0505 0.0212  -0.0019 0.0117  83  PRO A C   
847  O O   . PRO A 83  ? 0.1368 0.1449 0.0788 0.0297  0.0140  0.0180  83  PRO A O   
848  C CB  . PRO A 83  ? 0.1549 0.1578 0.0421 0.0352  -0.0058 0.0040  83  PRO A CB  
849  C CG  . PRO A 83  ? 0.1927 0.1862 0.0572 0.0313  0.0130  0.0270  83  PRO A CG  
850  C CD  . PRO A 83  ? 0.1657 0.1620 0.0448 0.0102  -0.0057 0.0271  83  PRO A CD  
851  N N   . PRO A 84  ? 0.1108 0.1281 0.0486 0.0094  -0.0026 0.0001  84  PRO A N   
852  C CA  . PRO A 84  ? 0.1165 0.1259 0.0413 0.0088  -0.0091 -0.0078 84  PRO A CA  
853  C C   . PRO A 84  ? 0.1196 0.1095 0.0311 0.0093  -0.0034 -0.0034 84  PRO A C   
854  O O   . PRO A 84  ? 0.1305 0.1422 0.0302 0.0112  -0.0015 -0.0047 84  PRO A O   
855  C CB  . PRO A 84  ? 0.1193 0.1305 0.0798 0.0053  -0.0176 -0.0143 84  PRO A CB  
856  C CG  . PRO A 84  ? 0.1359 0.1399 0.1050 -0.0009 0.0009  -0.0092 84  PRO A CG  
857  C CD  . PRO A 84  ? 0.1270 0.1406 0.0713 0.0029  0.0043  -0.0074 84  PRO A CD  
858  N N   . THR A 85  ? 0.1136 0.1186 0.0265 0.0117  -0.0101 0.0006  85  THR A N   
859  C CA  . THR A 85  ? 0.1201 0.1201 0.0284 0.0093  -0.0169 0.0004  85  THR A CA  
860  C C   . THR A 85  ? 0.1132 0.1056 0.0268 -0.0036 -0.0113 0.0005  85  THR A C   
861  O O   . THR A 85  ? 0.1260 0.1199 0.0357 0.0063  -0.0010 0.0102  85  THR A O   
862  C CB  . THR A 85  ? 0.1340 0.1196 0.0520 0.0091  -0.0272 0.0007  85  THR A CB  
863  O OG1 . THR A 85  ? 0.1447 0.1232 0.0621 -0.0005 -0.0112 0.0138  85  THR A OG1 
864  C CG2 . THR A 85  ? 0.1608 0.1165 0.0662 0.0095  -0.0307 -0.0069 85  THR A CG2 
865  N N   . THR A 86  ? 0.1033 0.1059 0.0261 -0.0013 -0.0079 0.0022  86  THR A N   
866  C CA  . THR A 86  ? 0.1030 0.1013 0.0256 -0.0059 -0.0037 -0.0026 86  THR A CA  
867  C C   . THR A 86  ? 0.1085 0.1012 0.0265 -0.0063 -0.0097 -0.0011 86  THR A C   
868  O O   . THR A 86  ? 0.1287 0.1159 0.0327 -0.0224 0.0017  -0.0137 86  THR A O   
869  C CB  . THR A 86  ? 0.1053 0.0991 0.0266 -0.0071 -0.0092 -0.0033 86  THR A CB  
870  O OG1 . THR A 86  ? 0.1000 0.1062 0.0345 -0.0067 -0.0076 -0.0005 86  THR A OG1 
871  C CG2 . THR A 86  ? 0.1222 0.1054 0.0644 0.0004  0.0166  0.0105  86  THR A CG2 
872  N N   . LEU A 87  ? 0.1052 0.1005 0.0262 -0.0064 -0.0079 -0.0019 87  LEU A N   
873  C CA  . LEU A 87  ? 0.1065 0.1036 0.0257 -0.0063 -0.0054 -0.0014 87  LEU A CA  
874  C C   . LEU A 87  ? 0.1086 0.1039 0.0255 -0.0089 -0.0044 0.0002  87  LEU A C   
875  O O   . LEU A 87  ? 0.1059 0.1193 0.0367 -0.0018 -0.0100 -0.0128 87  LEU A O   
876  C CB  . LEU A 87  ? 0.1100 0.1154 0.0350 -0.0114 -0.0096 0.0086  87  LEU A CB  
877  C CG  . LEU A 87  ? 0.1152 0.1166 0.0595 -0.0084 -0.0111 0.0203  87  LEU A CG  
878  C CD1 . LEU A 87  ? 0.1346 0.1356 0.0688 -0.0208 -0.0349 0.0304  87  LEU A CD1 
879  C CD2 . LEU A 87  ? 0.1446 0.1158 0.0768 0.0106  -0.0026 0.0187  87  LEU A CD2 
880  N N   . ALA A 88  ? 0.1014 0.0957 0.0263 -0.0057 -0.0067 -0.0012 88  ALA A N   
881  C CA  . ALA A 88  ? 0.1034 0.0985 0.0355 -0.0035 -0.0070 -0.0054 88  ALA A CA  
882  C C   . ALA A 88  ? 0.1067 0.1053 0.0388 -0.0124 -0.0053 -0.0064 88  ALA A C   
883  O O   . ALA A 88  ? 0.1623 0.1056 0.0666 -0.0240 0.0249  -0.0049 88  ALA A O   
884  C CB  . ALA A 88  ? 0.1142 0.1146 0.0376 0.0030  -0.0078 -0.0016 88  ALA A CB  
885  N N   . GLU A 89  ? 0.1071 0.1054 0.0340 -0.0163 -0.0054 -0.0011 89  GLU A N   
886  C CA  . GLU A 89  ? 0.1140 0.1108 0.0372 -0.0187 -0.0084 0.0050  89  GLU A CA  
887  C C   . GLU A 89  ? 0.1130 0.1171 0.0330 -0.0230 -0.0081 0.0015  89  GLU A C   
888  O O   . GLU A 89  ? 0.1067 0.1250 0.0446 -0.0222 -0.0024 -0.0004 89  GLU A O   
889  C CB  . GLU A 89  ? 0.1135 0.1255 0.0445 -0.0254 -0.0120 0.0072  89  GLU A CB  
890  C CG  . GLU A 89  ? 0.1117 0.1373 0.0529 -0.0146 -0.0122 0.0130  89  GLU A CG  
891  C CD  . GLU A 89  ? 0.1226 0.1368 0.0601 -0.0168 -0.0182 0.0111  89  GLU A CD  
892  O OE1 . GLU A 89  ? 0.1409 0.1561 0.0563 -0.0115 -0.0243 0.0015  89  GLU A OE1 
893  O OE2 . GLU A 89  ? 0.1494 0.1513 0.0908 -0.0014 -0.0367 0.0032  89  GLU A OE2 
894  N N   . PHE A 90  ? 0.1139 0.1196 0.0455 -0.0246 -0.0105 0.0079  90  PHE A N   
895  C CA  . PHE A 90  ? 0.1139 0.1337 0.0570 -0.0292 -0.0055 0.0067  90  PHE A CA  
896  C C   . PHE A 90  ? 0.1149 0.1425 0.0520 -0.0322 -0.0115 0.0105  90  PHE A C   
897  O O   . PHE A 90  ? 0.1307 0.1370 0.0833 -0.0319 -0.0036 0.0195  90  PHE A O   
898  C CB  . PHE A 90  ? 0.1095 0.1303 0.0622 -0.0237 -0.0100 0.0101  90  PHE A CB  
899  C CG  . PHE A 90  ? 0.1212 0.1314 0.0565 -0.0204 -0.0235 0.0156  90  PHE A CG  
900  C CD1 . PHE A 90  ? 0.1324 0.1383 0.0462 -0.0198 -0.0175 0.0102  90  PHE A CD1 
901  C CD2 . PHE A 90  ? 0.1373 0.1391 0.0696 -0.0280 -0.0288 0.0182  90  PHE A CD2 
902  C CE1 . PHE A 90  ? 0.1515 0.1441 0.0529 -0.0066 -0.0170 0.0099  90  PHE A CE1 
903  C CE2 . PHE A 90  ? 0.1631 0.1280 0.0821 -0.0236 -0.0397 0.0057  90  PHE A CE2 
904  C CZ  . PHE A 90  ? 0.1685 0.1473 0.0641 -0.0108 -0.0245 0.0058  90  PHE A CZ  
905  N N   . SER A 91  ? 0.1222 0.1380 0.0515 -0.0387 -0.0033 0.0059  91  SER A N   
906  C CA  . SER A 91  ? 0.1326 0.1542 0.0587 -0.0490 -0.0038 0.0102  91  SER A CA  
907  C C   . SER A 91  ? 0.1335 0.1496 0.0589 -0.0474 0.0013  0.0069  91  SER A C   
908  O O   . SER A 91  ? 0.1297 0.1619 0.0981 -0.0439 -0.0074 -0.0032 91  SER A O   
909  C CB  . SER A 91  ? 0.1593 0.1951 0.0615 -0.0541 0.0000  0.0235  91  SER A CB  
910  O OG  . SER A 91  ? 0.1815 0.2274 0.0614 -0.0328 -0.0176 0.0267  91  SER A OG  
911  N N   A LEU A 92  ? 0.1239 0.1594 0.0527 -0.0468 0.0093  0.0002  92  LEU A N   
912  N N   B LEU A 92  ? 0.1261 0.1506 0.0546 -0.0412 -0.0108 0.0114  92  LEU A N   
913  C CA  A LEU A 92  ? 0.1242 0.1405 0.0479 -0.0386 0.0144  0.0018  92  LEU A CA  
914  C CA  B LEU A 92  ? 0.1193 0.1245 0.0589 -0.0204 -0.0015 0.0055  92  LEU A CA  
915  C C   A LEU A 92  ? 0.1194 0.1438 0.0466 -0.0412 0.0049  0.0009  92  LEU A C   
916  C C   B LEU A 92  ? 0.1216 0.1102 0.0595 -0.0220 -0.0071 -0.0002 92  LEU A C   
917  O O   A LEU A 92  ? 0.1147 0.1366 0.0710 -0.0365 0.0232  0.0023  92  LEU A O   
918  O O   B LEU A 92  ? 0.1218 0.1118 0.0774 -0.0089 -0.0041 0.0000  92  LEU A O   
919  C CB  A LEU A 92  ? 0.1183 0.1362 0.0486 -0.0157 0.0095  0.0029  92  LEU A CB  
920  C CB  B LEU A 92  ? 0.1124 0.1192 0.0569 -0.0150 -0.0054 0.0064  92  LEU A CB  
921  C CG  A LEU A 92  ? 0.1220 0.1340 0.0562 -0.0128 0.0127  0.0069  92  LEU A CG  
922  C CG  B LEU A 92  ? 0.1151 0.1207 0.0545 -0.0019 0.0012  0.0162  92  LEU A CG  
923  C CD1 A LEU A 92  ? 0.1339 0.1422 0.0609 -0.0060 0.0186  0.0012  92  LEU A CD1 
924  C CD1 B LEU A 92  ? 0.1417 0.1315 0.0598 -0.0014 0.0080  0.0081  92  LEU A CD1 
925  C CD2 A LEU A 92  ? 0.1196 0.1329 0.0635 -0.0163 0.0152  0.0147  92  LEU A CD2 
926  C CD2 B LEU A 92  ? 0.1106 0.1223 0.0525 -0.0011 0.0026  0.0130  92  LEU A CD2 
927  N N   A ASN A 93  ? 0.1179 0.1587 0.0478 -0.0402 0.0157  -0.0030 93  ASN A N   
928  N N   B ASN A 93  ? 0.1170 0.1180 0.0600 -0.0257 -0.0070 0.0072  93  ASN A N   
929  C CA  A ASN A 93  ? 0.1307 0.2034 0.0546 -0.0607 0.0147  0.0012  93  ASN A CA  
930  C CA  B ASN A 93  ? 0.1133 0.1538 0.0506 -0.0328 -0.0104 0.0014  93  ASN A CA  
931  C C   A ASN A 93  ? 0.1280 0.1938 0.0545 -0.0475 0.0143  -0.0072 93  ASN A C   
932  C C   B ASN A 93  ? 0.1040 0.1286 0.0525 -0.0235 0.0039  0.0050  93  ASN A C   
933  O O   A ASN A 93  ? 0.1699 0.2003 0.0654 -0.0689 0.0281  -0.0146 93  ASN A O   
934  O O   B ASN A 93  ? 0.1158 0.1313 0.0480 -0.0304 0.0025  0.0068  93  ASN A O   
935  C CB  A ASN A 93  ? 0.1164 0.1931 0.0680 -0.0489 0.0027  0.0082  93  ASN A CB  
936  C CB  B ASN A 93  ? 0.1055 0.1979 0.0494 -0.0542 0.0058  -0.0116 93  ASN A CB  
937  C CG  A ASN A 93  ? 0.0995 0.1399 0.0717 -0.0322 -0.0044 0.0009  93  ASN A CG  
938  C CG  B ASN A 93  ? 0.1035 0.1776 0.0570 -0.0377 0.0084  -0.0121 93  ASN A CG  
939  O OD1 A ASN A 93  ? 0.1170 0.1303 0.0558 -0.0157 -0.0043 0.0160  93  ASN A OD1 
940  O OD1 B ASN A 93  ? 0.1202 0.1563 0.0710 -0.0229 0.0182  -0.0095 93  ASN A OD1 
941  N ND2 A ASN A 93  ? 0.1125 0.1425 0.0648 -0.0148 0.0060  -0.0058 93  ASN A ND2 
942  N ND2 B ASN A 93  ? 0.1199 0.1812 0.0622 -0.0218 0.0214  -0.0164 93  ASN A ND2 
943  N N   A GLN A 94  ? 0.1273 0.1734 0.0511 -0.0295 0.0099  -0.0052 94  GLN A N   
944  N N   B GLN A 94  ? 0.1271 0.1233 0.0523 -0.0218 -0.0030 0.0082  94  GLN A N   
945  C CA  A GLN A 94  ? 0.1439 0.1774 0.0513 -0.0310 0.0089  -0.0053 94  GLN A CA  
946  C CA  B GLN A 94  ? 0.1349 0.1262 0.0536 -0.0189 -0.0074 0.0044  94  GLN A CA  
947  C C   A GLN A 94  ? 0.1458 0.1781 0.0563 -0.0476 0.0198  -0.0189 94  GLN A C   
948  C C   B GLN A 94  ? 0.1317 0.1351 0.0613 -0.0173 -0.0058 0.0050  94  GLN A C   
949  O O   A GLN A 94  ? 0.1362 0.1757 0.0683 -0.0409 0.0170  -0.0237 94  GLN A O   
950  O O   B GLN A 94  ? 0.1303 0.1399 0.0742 -0.0157 0.0060  -0.0081 94  GLN A O   
951  C CB  A GLN A 94  ? 0.1473 0.1806 0.0566 -0.0347 0.0046  0.0022  94  GLN A CB  
952  C CB  B GLN A 94  ? 0.1492 0.1535 0.0668 -0.0235 -0.0315 -0.0056 94  GLN A CB  
953  C CG  A GLN A 94  ? 0.1567 0.1873 0.0734 -0.0186 0.0047  0.0056  94  GLN A CG  
954  C CG  B GLN A 94  ? 0.1658 0.1798 0.0971 -0.0142 -0.0168 -0.0069 94  GLN A CG  
955  C CD  A GLN A 94  ? 0.2256 0.1961 0.0705 0.0002  -0.0099 0.0131  94  GLN A CD  
956  C CD  B GLN A 94  ? 0.2036 0.1893 0.1078 0.0077  -0.0243 0.0050  94  GLN A CD  
957  O OE1 A GLN A 94  ? 0.3311 0.2348 0.0802 0.0021  -0.0563 0.0102  94  GLN A OE1 
958  O OE1 B GLN A 94  ? 0.3033 0.2244 0.1300 -0.0136 -0.0242 0.0349  94  GLN A OE1 
959  N NE2 A GLN A 94  ? 0.2866 0.1809 0.0873 0.0091  -0.0272 0.0097  94  GLN A NE2 
960  N NE2 B GLN A 94  ? 0.2253 0.1643 0.1288 0.0375  -0.0344 -0.0027 94  GLN A NE2 
961  N N   A TYR A 95  ? 0.1582 0.1871 0.0797 -0.0631 0.0234  -0.0341 95  TYR A N   
962  N N   B TYR A 95  ? 0.1420 0.1617 0.0438 -0.0342 0.0002  -0.0109 95  TYR A N   
963  C CA  A TYR A 95  ? 0.1589 0.2265 0.0703 -0.0636 0.0314  -0.0307 95  TYR A CA  
964  C CA  B TYR A 95  ? 0.1442 0.1970 0.0544 -0.0415 0.0175  -0.0086 95  TYR A CA  
965  C C   A TYR A 95  ? 0.1406 0.2559 0.0842 -0.0736 0.0255  -0.0141 95  TYR A C   
966  C C   B TYR A 95  ? 0.1302 0.2177 0.0800 -0.0441 -0.0014 -0.0043 95  TYR A C   
967  O O   A TYR A 95  ? 0.1544 0.2575 0.0722 -0.0435 -0.0022 0.0203  95  TYR A O   
968  O O   B TYR A 95  ? 0.1706 0.2061 0.0935 -0.0232 0.0033  0.0099  95  TYR A O   
969  C CB  A TYR A 95  ? 0.1663 0.2143 0.0673 -0.0467 0.0383  -0.0318 95  TYR A CB  
970  C CB  B TYR A 95  ? 0.1533 0.1926 0.0660 -0.0353 0.0025  -0.0204 95  TYR A CB  
971  C CG  A TYR A 95  ? 0.1865 0.2070 0.0927 -0.0425 -0.0014 -0.0435 95  TYR A CG  
972  C CG  B TYR A 95  ? 0.1731 0.1983 0.0573 -0.0389 -0.0069 -0.0200 95  TYR A CG  
973  C CD1 A TYR A 95  ? 0.2183 0.2168 0.1412 -0.0538 -0.0220 -0.0061 95  TYR A CD1 
974  C CD1 B TYR A 95  ? 0.1544 0.1967 0.1030 -0.0306 -0.0138 -0.0103 95  TYR A CD1 
975  C CD2 A TYR A 95  ? 0.1933 0.2284 0.1996 -0.0410 -0.0229 -0.0186 95  TYR A CD2 
976  C CD2 B TYR A 95  ? 0.1765 0.2182 0.1159 -0.0397 -0.0181 -0.0125 95  TYR A CD2 
977  C CE1 A TYR A 95  ? 0.2548 0.2119 0.1987 -0.0462 -0.0201 0.0123  95  TYR A CE1 
978  C CE1 B TYR A 95  ? 0.1777 0.2020 0.1492 -0.0226 -0.0346 0.0004  95  TYR A CE1 
979  C CE2 A TYR A 95  ? 0.2426 0.2506 0.1972 -0.0321 -0.0335 -0.0061 95  TYR A CE2 
980  C CE2 B TYR A 95  ? 0.1935 0.2258 0.1665 -0.0186 -0.0450 -0.0124 95  TYR A CE2 
981  C CZ  A TYR A 95  ? 0.2690 0.2288 0.1643 -0.0371 -0.0416 -0.0165 95  TYR A CZ  
982  C CZ  B TYR A 95  ? 0.1916 0.2312 0.1532 -0.0127 -0.0555 0.0049  95  TYR A CZ  
983  O OH  A TYR A 95  ? 0.3251 0.2439 0.1899 -0.0229 -0.0629 -0.0070 95  TYR A OH  
984  O OH  B TYR A 95  ? 0.2187 0.2387 0.2490 0.0041  -0.0923 0.0182  95  TYR A OH  
985  N N   . GLY A 96  ? 0.1409 0.2680 0.0728 -0.0732 0.0083  0.0017  96  GLY A N   
986  C CA  . GLY A 96  ? 0.1333 0.2982 0.0977 -0.0603 0.0062  0.0135  96  GLY A CA  
987  C C   . GLY A 96  ? 0.1364 0.2870 0.0703 -0.0451 0.0147  0.0052  96  GLY A C   
988  O O   . GLY A 96  ? 0.1439 0.3291 0.1049 -0.0351 0.0139  0.0325  96  GLY A O   
989  N N   . LYS A 97  ? 0.1378 0.2485 0.0846 -0.0530 0.0182  -0.0073 97  LYS A N   
990  C CA  . LYS A 97  ? 0.1366 0.2444 0.0810 -0.0511 0.0318  -0.0181 97  LYS A CA  
991  C C   . LYS A 97  ? 0.1281 0.2020 0.0580 -0.0463 0.0083  -0.0058 97  LYS A C   
992  O O   . LYS A 97  ? 0.1597 0.2058 0.0887 -0.0516 0.0308  0.0096  97  LYS A O   
993  C CB  . LYS A 97  ? 0.1667 0.2965 0.1170 -0.0669 0.0446  -0.0599 97  LYS A CB  
994  C CG  . LYS A 97  ? 0.1864 0.3607 0.1716 -0.0590 0.0589  -0.0972 97  LYS A CG  
995  C CD  . LYS A 97  ? 0.2151 0.3849 0.2619 -0.0279 0.0530  -0.0792 97  LYS A CD  
996  C CE  . LYS A 97  ? 0.2407 0.4326 0.3692 0.0078  0.0570  -0.0918 97  LYS A CE  
997  N NZ  . LYS A 97  ? 0.3042 0.4632 0.4242 0.0192  0.0448  -0.0711 97  LYS A NZ  
998  N N   . ASP A 98  ? 0.1217 0.1910 0.0589 -0.0394 0.0070  -0.0032 98  ASP A N   
999  C CA  . ASP A 98  ? 0.1208 0.1740 0.0516 -0.0399 0.0049  -0.0040 98  ASP A CA  
1000 C C   . ASP A 98  ? 0.1199 0.1759 0.0477 -0.0304 0.0063  -0.0090 98  ASP A C   
1001 O O   . ASP A 98  ? 0.1257 0.1789 0.0734 -0.0280 -0.0065 -0.0091 98  ASP A O   
1002 C CB  . ASP A 98  ? 0.1241 0.1773 0.0519 -0.0362 0.0027  0.0001  98  ASP A CB  
1003 C CG  . ASP A 98  ? 0.1209 0.1807 0.0522 -0.0369 0.0011  -0.0008 98  ASP A CG  
1004 O OD1 . ASP A 98  ? 0.1353 0.1921 0.0548 -0.0538 -0.0011 -0.0006 98  ASP A OD1 
1005 O OD2 . ASP A 98  ? 0.1293 0.1804 0.0466 -0.0370 -0.0020 -0.0022 98  ASP A OD2 
1006 N N   . TYR A 99  ? 0.1142 0.1642 0.0611 -0.0391 0.0098  -0.0151 99  TYR A N   
1007 C CA  . TYR A 99  ? 0.1156 0.1649 0.0574 -0.0362 0.0075  -0.0149 99  TYR A CA  
1008 C C   . TYR A 99  ? 0.1085 0.1561 0.0604 -0.0314 0.0013  -0.0156 99  TYR A C   
1009 O O   . TYR A 99  ? 0.1298 0.1488 0.1192 -0.0307 0.0295  -0.0089 99  TYR A O   
1010 C CB  . TYR A 99  ? 0.1402 0.1875 0.0627 -0.0463 -0.0090 -0.0119 99  TYR A CB  
1011 C CG  . TYR A 99  ? 0.1555 0.1985 0.0589 -0.0550 -0.0003 -0.0073 99  TYR A CG  
1012 C CD1 . TYR A 99  ? 0.1654 0.2135 0.0770 -0.0662 0.0089  -0.0266 99  TYR A CD1 
1013 C CD2 . TYR A 99  ? 0.1920 0.2041 0.0919 -0.0648 0.0347  -0.0207 99  TYR A CD2 
1014 C CE1 . TYR A 99  ? 0.1868 0.2157 0.0868 -0.0598 0.0253  -0.0339 99  TYR A CE1 
1015 C CE2 . TYR A 99  ? 0.2006 0.2223 0.1153 -0.0749 0.0476  -0.0241 99  TYR A CE2 
1016 C CZ  . TYR A 99  ? 0.2032 0.2417 0.0986 -0.0795 0.0521  -0.0407 99  TYR A CZ  
1017 O OH  . TYR A 99  ? 0.2283 0.2844 0.1513 -0.0925 0.0848  -0.0797 99  TYR A OH  
1018 N N   . ILE A 100 ? 0.0995 0.1484 0.0549 -0.0210 -0.0010 -0.0150 100 ILE A N   
1019 C CA  . ILE A 100 ? 0.0987 0.1440 0.0485 -0.0175 0.0013  -0.0140 100 ILE A CA  
1020 C C   . ILE A 100 ? 0.1021 0.1357 0.0413 -0.0184 -0.0008 -0.0081 100 ILE A C   
1021 O O   . ILE A 100 ? 0.1025 0.1481 0.0644 -0.0208 0.0001  -0.0232 100 ILE A O   
1022 C CB  . ILE A 100 ? 0.1081 0.1545 0.0534 -0.0178 -0.0066 -0.0130 100 ILE A CB  
1023 C CG1 . ILE A 100 ? 0.1290 0.1521 0.0635 -0.0206 -0.0129 -0.0035 100 ILE A CG1 
1024 C CG2 . ILE A 100 ? 0.1133 0.1685 0.0670 -0.0172 -0.0167 -0.0201 100 ILE A CG2 
1025 C CD1 . ILE A 100 ? 0.1464 0.1702 0.0696 -0.0274 -0.0126 0.0054  100 ILE A CD1 
1026 N N   . ASP A 101 ? 0.1002 0.1268 0.0440 -0.0197 -0.0009 -0.0071 101 ASP A N   
1027 C CA  . ASP A 101 ? 0.1018 0.1235 0.0364 -0.0135 -0.0070 -0.0089 101 ASP A CA  
1028 C C   . ASP A 101 ? 0.0987 0.1107 0.0278 -0.0098 -0.0125 -0.0010 101 ASP A C   
1029 O O   . ASP A 101 ? 0.1034 0.1141 0.0381 -0.0156 -0.0089 -0.0071 101 ASP A O   
1030 C CB  . ASP A 101 ? 0.1160 0.1452 0.0349 -0.0230 -0.0040 -0.0063 101 ASP A CB  
1031 C CG  . ASP A 101 ? 0.1334 0.1526 0.0356 -0.0232 -0.0074 0.0047  101 ASP A CG  
1032 O OD1 . ASP A 101 ? 0.1218 0.1407 0.0718 -0.0167 -0.0213 0.0009  101 ASP A OD1 
1033 O OD2 . ASP A 101 ? 0.1580 0.1604 0.1052 -0.0191 0.0181  0.0217  101 ASP A OD2 
1034 N N   . ILE A 102 ? 0.0950 0.1030 0.0336 -0.0076 -0.0103 -0.0055 102 ILE A N   
1035 C CA  . ILE A 102 ? 0.0943 0.1039 0.0292 -0.0064 -0.0092 -0.0060 102 ILE A CA  
1036 C C   . ILE A 102 ? 0.0927 0.0987 0.0315 -0.0133 -0.0101 -0.0062 102 ILE A C   
1037 O O   . ILE A 102 ? 0.1008 0.1173 0.0349 -0.0042 -0.0116 -0.0149 102 ILE A O   
1038 C CB  . ILE A 102 ? 0.1036 0.1087 0.0350 -0.0098 -0.0053 -0.0014 102 ILE A CB  
1039 C CG1 . ILE A 102 ? 0.1053 0.1280 0.0465 -0.0056 -0.0126 0.0066  102 ILE A CG1 
1040 C CG2 . ILE A 102 ? 0.1046 0.1194 0.0446 -0.0084 -0.0068 0.0060  102 ILE A CG2 
1041 C CD1 . ILE A 102 ? 0.1188 0.1455 0.0514 -0.0020 -0.0066 0.0147  102 ILE A CD1 
1042 N N   . SER A 103 ? 0.0979 0.1127 0.0288 -0.0011 -0.0133 -0.0052 103 SER A N   
1043 C CA  . SER A 103 ? 0.0993 0.1228 0.0282 -0.0054 -0.0143 -0.0026 103 SER A CA  
1044 C C   . SER A 103 ? 0.1009 0.1051 0.0275 -0.0018 -0.0129 0.0002  103 SER A C   
1045 O O   . SER A 103 ? 0.1028 0.1246 0.0282 -0.0003 -0.0134 -0.0074 103 SER A O   
1046 C CB  . SER A 103 ? 0.1067 0.1294 0.0388 -0.0068 -0.0138 0.0051  103 SER A CB  
1047 O OG  . SER A 103 ? 0.1085 0.1466 0.0503 -0.0157 -0.0186 0.0208  103 SER A OG  
1048 N N   . ASN A 104 ? 0.1025 0.1122 0.0268 -0.0041 -0.0107 -0.0010 104 ASN A N   
1049 C CA  . ASN A 104 ? 0.0995 0.1141 0.0261 -0.0073 -0.0075 0.0026  104 ASN A CA  
1050 C C   . ASN A 104 ? 0.0984 0.1094 0.0262 -0.0088 -0.0078 -0.0006 104 ASN A C   
1051 O O   . ASN A 104 ? 0.1020 0.1222 0.0344 -0.0090 -0.0137 0.0053  104 ASN A O   
1052 C CB  . ASN A 104 ? 0.1065 0.1208 0.0362 -0.0067 -0.0108 0.0019  104 ASN A CB  
1053 C CG  . ASN A 104 ? 0.1153 0.1204 0.0426 -0.0047 -0.0082 0.0077  104 ASN A CG  
1054 O OD1 . ASN A 104 ? 0.1793 0.1333 0.0385 0.0048  0.0032  0.0102  104 ASN A OD1 
1055 N ND2 . ASN A 104 ? 0.1427 0.1229 0.0573 0.0086  -0.0120 0.0123  104 ASN A ND2 
1056 N N   . ILE A 105 ? 0.0968 0.1173 0.0268 -0.0013 -0.0095 0.0044  105 ILE A N   
1057 C CA  . ILE A 105 ? 0.1127 0.1242 0.0273 -0.0001 -0.0109 0.0080  105 ILE A CA  
1058 C C   . ILE A 105 ? 0.0999 0.1284 0.0274 -0.0038 -0.0055 0.0137  105 ILE A C   
1059 O O   . ILE A 105 ? 0.1090 0.1482 0.0314 0.0118  -0.0086 0.0156  105 ILE A O   
1060 C CB  . ILE A 105 ? 0.1170 0.1481 0.0285 0.0103  0.0048  0.0191  105 ILE A CB  
1061 C CG1 . ILE A 105 ? 0.1349 0.1590 0.0342 0.0193  0.0090  0.0156  105 ILE A CG1 
1062 C CG2 . ILE A 105 ? 0.1303 0.1649 0.0523 0.0099  0.0092  0.0405  105 ILE A CG2 
1063 C CD1 . ILE A 105 ? 0.1422 0.1806 0.0676 0.0291  0.0283  0.0291  105 ILE A CD1 
1064 N N   . LYS A 106 ? 0.0989 0.1130 0.0269 -0.0002 -0.0071 0.0090  106 LYS A N   
1065 C CA  . LYS A 106 ? 0.1053 0.1227 0.0290 0.0062  -0.0061 0.0077  106 LYS A CA  
1066 C C   . LYS A 106 ? 0.0992 0.1284 0.0266 0.0069  -0.0063 0.0084  106 LYS A C   
1067 O O   . LYS A 106 ? 0.1203 0.1471 0.0306 0.0151  -0.0021 0.0019  106 LYS A O   
1068 C CB  . LYS A 106 ? 0.1226 0.1251 0.0546 0.0001  -0.0076 -0.0003 106 LYS A CB  
1069 C CG  . LYS A 106 ? 0.1799 0.1306 0.0681 -0.0197 -0.0034 0.0085  106 LYS A CG  
1070 C CD  . LYS A 106 ? 0.2361 0.1837 0.1304 -0.0439 -0.0616 0.0482  106 LYS A CD  
1071 C CE  . LYS A 106 ? 0.3148 0.2057 0.1347 -0.0460 -0.0377 0.0601  106 LYS A CE  
1072 N NZ  . LYS A 106 ? 0.3736 0.2323 0.2194 -0.0317 -0.0883 0.0738  106 LYS A NZ  
1073 N N   . GLY A 107 ? 0.0997 0.1315 0.0273 -0.0036 -0.0049 0.0134  107 GLY A N   
1074 C CA  . GLY A 107 ? 0.1011 0.1403 0.0280 -0.0122 -0.0072 0.0164  107 GLY A CA  
1075 C C   . GLY A 107 ? 0.0975 0.1286 0.0265 -0.0092 -0.0058 0.0097  107 GLY A C   
1076 O O   . GLY A 107 ? 0.1065 0.1674 0.0383 -0.0138 -0.0121 0.0325  107 GLY A O   
1077 N N   . PHE A 108 ? 0.0939 0.1220 0.0265 -0.0051 -0.0074 0.0064  108 PHE A N   
1078 C CA  . PHE A 108 ? 0.1030 0.1162 0.0264 -0.0097 -0.0092 0.0027  108 PHE A CA  
1079 C C   . PHE A 108 ? 0.1072 0.1208 0.0266 -0.0096 -0.0102 0.0031  108 PHE A C   
1080 O O   . PHE A 108 ? 0.1053 0.1359 0.0263 -0.0085 -0.0089 0.0005  108 PHE A O   
1081 C CB  . PHE A 108 ? 0.1112 0.1157 0.0266 -0.0059 -0.0094 -0.0044 108 PHE A CB  
1082 C CG  . PHE A 108 ? 0.1185 0.1074 0.0291 -0.0116 -0.0171 -0.0050 108 PHE A CG  
1083 C CD1 . PHE A 108 ? 0.1165 0.1131 0.0346 -0.0119 -0.0121 0.0049  108 PHE A CD1 
1084 C CD2 . PHE A 108 ? 0.1185 0.1121 0.0354 -0.0112 -0.0183 -0.0051 108 PHE A CD2 
1085 C CE1 . PHE A 108 ? 0.1341 0.1189 0.0358 -0.0172 -0.0177 0.0091  108 PHE A CE1 
1086 C CE2 . PHE A 108 ? 0.1222 0.1214 0.0503 -0.0062 -0.0249 0.0006  108 PHE A CE2 
1087 C CZ  . PHE A 108 ? 0.1392 0.1119 0.0406 -0.0119 -0.0269 0.0066  108 PHE A CZ  
1088 N N   . ASN A 109 ? 0.1066 0.1223 0.0262 -0.0079 -0.0073 -0.0042 109 ASN A N   
1089 C CA  . ASN A 109 ? 0.1078 0.1385 0.0257 0.0054  -0.0056 -0.0007 109 ASN A CA  
1090 C C   . ASN A 109 ? 0.1064 0.1431 0.0255 -0.0013 -0.0038 0.0003  109 ASN A C   
1091 O O   . ASN A 109 ? 0.1056 0.2068 0.0480 -0.0139 -0.0036 0.0402  109 ASN A O   
1092 C CB  . ASN A 109 ? 0.1225 0.1311 0.0258 0.0183  -0.0065 -0.0037 109 ASN A CB  
1093 C CG  . ASN A 109 ? 0.1363 0.1131 0.0280 0.0123  -0.0168 -0.0052 109 ASN A CG  
1094 O OD1 . ASN A 109 ? 0.1230 0.1080 0.0314 -0.0013 -0.0141 -0.0074 109 ASN A OD1 
1095 N ND2 . ASN A 109 ? 0.1603 0.1160 0.0394 0.0172  -0.0235 -0.0147 109 ASN A ND2 
1096 N N   . VAL A 110 ? 0.1031 0.1175 0.0261 -0.0017 -0.0076 0.0027  110 VAL A N   
1097 C CA  . VAL A 110 ? 0.1088 0.1291 0.0274 -0.0037 -0.0128 0.0046  110 VAL A CA  
1098 C C   . VAL A 110 ? 0.0958 0.1209 0.0272 -0.0032 -0.0113 0.0035  110 VAL A C   
1099 O O   . VAL A 110 ? 0.1035 0.1242 0.0286 -0.0016 -0.0015 0.0080  110 VAL A O   
1100 C CB  . VAL A 110 ? 0.1210 0.1387 0.0270 0.0004  -0.0113 -0.0067 110 VAL A CB  
1101 C CG1 . VAL A 110 ? 0.1269 0.1375 0.0319 0.0043  -0.0199 -0.0023 110 VAL A CG1 
1102 C CG2 . VAL A 110 ? 0.1296 0.1416 0.0274 0.0053  -0.0101 -0.0120 110 VAL A CG2 
1103 N N   . PRO A 111 ? 0.0978 0.1150 0.0279 -0.0025 -0.0100 0.0039  111 PRO A N   
1104 C CA  . PRO A 111 ? 0.1048 0.1147 0.0371 -0.0003 -0.0141 -0.0017 111 PRO A CA  
1105 C C   . PRO A 111 ? 0.1056 0.1087 0.0269 0.0007  -0.0104 0.0042  111 PRO A C   
1106 O O   . PRO A 111 ? 0.1042 0.1170 0.0271 -0.0009 -0.0088 -0.0016 111 PRO A O   
1107 C CB  . PRO A 111 ? 0.1097 0.1169 0.0637 -0.0063 -0.0164 -0.0020 111 PRO A CB  
1108 C CG  . PRO A 111 ? 0.1259 0.1250 0.0632 -0.0071 -0.0085 0.0077  111 PRO A CG  
1109 C CD  . PRO A 111 ? 0.1113 0.1191 0.0355 -0.0070 -0.0069 0.0089  111 PRO A CD  
1110 N N   . MET A 112 ? 0.1043 0.1196 0.0271 -0.0033 -0.0119 -0.0006 112 MET A N   
1111 C CA  A MET A 112 ? 0.1030 0.1077 0.0298 -0.0074 -0.0024 0.0075  112 MET A CA  
1112 C CA  B MET A 112 ? 0.1076 0.1095 0.0387 -0.0031 -0.0069 0.0027  112 MET A CA  
1113 C C   . MET A 112 ? 0.1056 0.1055 0.0276 -0.0086 -0.0057 -0.0019 112 MET A C   
1114 O O   . MET A 112 ? 0.1080 0.1377 0.0394 0.0005  -0.0124 -0.0208 112 MET A O   
1115 C CB  A MET A 112 ? 0.1138 0.1053 0.0353 -0.0071 -0.0122 -0.0049 112 MET A CB  
1116 C CB  B MET A 112 ? 0.1188 0.1192 0.0414 -0.0029 -0.0105 0.0087  112 MET A CB  
1117 C CG  A MET A 112 ? 0.1382 0.1196 0.0361 -0.0136 -0.0112 0.0027  112 MET A CG  
1118 C CG  B MET A 112 ? 0.1258 0.1244 0.0652 -0.0098 -0.0012 0.0072  112 MET A CG  
1119 S SD  A MET A 112 ? 0.1496 0.1289 0.0532 -0.0182 0.0125  -0.0001 112 MET A SD  
1120 S SD  B MET A 112 ? 0.1185 0.1271 0.0511 -0.0084 0.0056  0.0036  112 MET A SD  
1121 C CE  A MET A 112 ? 0.1369 0.1257 0.0549 0.0088  -0.0065 0.0149  112 MET A CE  
1122 C CE  B MET A 112 ? 0.1156 0.1294 0.0551 -0.0014 0.0112  0.0143  112 MET A CE  
1123 N N   . ASP A 113 ? 0.1042 0.1103 0.0313 -0.0042 -0.0071 -0.0102 113 ASP A N   
1124 C CA  . ASP A 113 ? 0.1035 0.1099 0.0372 -0.0035 -0.0082 -0.0145 113 ASP A CA  
1125 C C   . ASP A 113 ? 0.0986 0.1138 0.0285 -0.0013 -0.0090 -0.0131 113 ASP A C   
1126 O O   . ASP A 113 ? 0.1196 0.1219 0.0403 -0.0170 0.0040  -0.0223 113 ASP A O   
1127 C CB  . ASP A 113 ? 0.1126 0.1154 0.0548 -0.0055 -0.0132 -0.0043 113 ASP A CB  
1128 C CG  . ASP A 113 ? 0.1215 0.1159 0.0610 0.0014  -0.0186 -0.0054 113 ASP A CG  
1129 O OD1 . ASP A 113 ? 0.1149 0.1399 0.0830 -0.0029 -0.0113 -0.0172 113 ASP A OD1 
1130 O OD2 . ASP A 113 ? 0.1351 0.1376 0.1165 0.0082  -0.0187 -0.0335 113 ASP A OD2 
1131 N N   . PHE A 114 ? 0.1012 0.1110 0.0280 -0.0045 -0.0080 -0.0114 114 PHE A N   
1132 C CA  . PHE A 114 ? 0.1048 0.1128 0.0299 -0.0040 -0.0090 -0.0071 114 PHE A CA  
1133 C C   . PHE A 114 ? 0.1048 0.1125 0.0341 -0.0064 -0.0039 -0.0072 114 PHE A C   
1134 O O   . PHE A 114 ? 0.1111 0.1362 0.0416 -0.0009 -0.0023 -0.0192 114 PHE A O   
1135 C CB  . PHE A 114 ? 0.1041 0.1292 0.0343 0.0003  -0.0107 0.0007  114 PHE A CB  
1136 C CG  . PHE A 114 ? 0.1083 0.1217 0.0330 0.0039  -0.0053 -0.0012 114 PHE A CG  
1137 C CD1 . PHE A 114 ? 0.1259 0.1285 0.0434 -0.0105 -0.0186 0.0132  114 PHE A CD1 
1138 C CD2 . PHE A 114 ? 0.1175 0.1282 0.0302 0.0008  -0.0087 -0.0029 114 PHE A CD2 
1139 C CE1 . PHE A 114 ? 0.1340 0.1307 0.0564 -0.0145 -0.0262 0.0117  114 PHE A CE1 
1140 C CE2 . PHE A 114 ? 0.1351 0.1298 0.0357 0.0031  -0.0032 0.0072  114 PHE A CE2 
1141 C CZ  . PHE A 114 ? 0.1366 0.1338 0.0521 -0.0085 -0.0082 0.0133  114 PHE A CZ  
1142 N N   . SER A 115 ? 0.1001 0.1227 0.0468 0.0000  -0.0106 -0.0160 115 SER A N   
1143 C CA  . SER A 115 ? 0.1074 0.1280 0.0683 0.0008  -0.0131 -0.0190 115 SER A CA  
1144 C C   . SER A 115 ? 0.1061 0.1349 0.0550 0.0013  -0.0161 -0.0158 115 SER A C   
1145 O O   . SER A 115 ? 0.1138 0.1411 0.0669 -0.0063 -0.0098 -0.0278 115 SER A O   
1146 C CB  . SER A 115 ? 0.1077 0.1404 0.0983 0.0057  -0.0144 -0.0026 115 SER A CB  
1147 O OG  . SER A 115 ? 0.1297 0.1306 0.1211 0.0010  -0.0007 -0.0178 115 SER A OG  
1148 N N   . PRO A 116 ? 0.1056 0.1423 0.0669 -0.0025 -0.0096 -0.0254 116 PRO A N   
1149 C CA  . PRO A 116 ? 0.1049 0.1398 0.0720 -0.0027 -0.0114 -0.0130 116 PRO A CA  
1150 C C   . PRO A 116 ? 0.1106 0.1356 0.0864 -0.0020 -0.0213 -0.0031 116 PRO A C   
1151 O O   . PRO A 116 ? 0.1399 0.1447 0.1092 -0.0126 -0.0244 -0.0035 116 PRO A O   
1152 C CB  . PRO A 116 ? 0.1105 0.1789 0.0795 -0.0035 -0.0033 -0.0155 116 PRO A CB  
1153 C CG  . PRO A 116 ? 0.1342 0.1844 0.1013 0.0055  -0.0012 -0.0303 116 PRO A CG  
1154 C CD  . PRO A 116 ? 0.1235 0.1626 0.0959 -0.0033 0.0047  -0.0463 116 PRO A CD  
1155 N N   . THR A 117 ? 0.1177 0.1439 0.0763 -0.0110 -0.0289 0.0050  117 THR A N   
1156 C CA  . THR A 117 ? 0.1264 0.1610 0.0808 -0.0015 -0.0273 0.0118  117 THR A CA  
1157 C C   . THR A 117 ? 0.1288 0.1834 0.0954 0.0068  -0.0285 0.0140  117 THR A C   
1158 O O   . THR A 117 ? 0.1466 0.3018 0.1079 0.0399  -0.0361 0.0202  117 THR A O   
1159 C CB  . THR A 117 ? 0.1355 0.1683 0.0651 -0.0066 -0.0260 0.0054  117 THR A CB  
1160 O OG1 . THR A 117 ? 0.1640 0.1788 0.0784 -0.0319 -0.0327 0.0060  117 THR A OG1 
1161 C CG2 . THR A 117 ? 0.1411 0.1745 0.0746 -0.0054 -0.0171 0.0057  117 THR A CG2 
1162 N N   . THR A 118 ? 0.1174 0.1948 0.0984 -0.0007 -0.0265 0.0008  118 THR A N   
1163 C CA  . THR A 118 ? 0.1173 0.2024 0.1211 0.0025  -0.0274 0.0030  118 THR A CA  
1164 C C   . THR A 118 ? 0.1323 0.2189 0.1634 0.0115  -0.0172 -0.0111 118 THR A C   
1165 O O   . THR A 118 ? 0.1544 0.2480 0.2209 -0.0104 -0.0126 -0.0744 118 THR A O   
1166 C CB  . THR A 118 ? 0.1206 0.2081 0.1388 -0.0077 -0.0161 -0.0037 118 THR A CB  
1167 O OG1 . THR A 118 ? 0.1395 0.1942 0.1271 -0.0008 -0.0107 0.0042  118 THR A OG1 
1168 C CG2 . THR A 118 ? 0.1573 0.2153 0.1598 -0.0084 -0.0424 -0.0180 118 THR A CG2 
1169 N N   . ARG A 119 ? 0.1363 0.2486 0.1858 0.0255  -0.0137 -0.0213 119 ARG A N   
1170 C CA  . ARG A 119 ? 0.1812 0.2743 0.2031 0.0302  -0.0236 -0.0429 119 ARG A CA  
1171 C C   . ARG A 119 ? 0.1723 0.2436 0.1962 0.0175  -0.0084 -0.0505 119 ARG A C   
1172 O O   . ARG A 119 ? 0.3046 0.2454 0.2223 -0.0025 0.0413  -0.0498 119 ARG A O   
1173 C CB  . ARG A 119 ? 0.2173 0.3393 0.2709 0.0861  -0.0561 -0.0833 119 ARG A CB  
1174 C CG  . ARG A 119 ? 0.3620 0.4010 0.3092 0.0893  -0.0692 -0.0315 119 ARG A CG  
1175 C CD  . ARG A 119 ? 0.3712 0.4817 0.4585 0.0837  -0.0849 -0.0297 119 ARG A CD  
1176 N NE  . ARG A 119 ? 0.5372 0.5806 0.4534 0.0317  -0.0983 -0.0251 119 ARG A NE  
1177 C CZ  . ARG A 119 ? 0.5946 0.5329 0.5402 -0.0341 -0.0598 -0.0568 119 ARG A CZ  
1178 N NH1 . ARG A 119 ? 0.6145 0.5597 0.5221 -0.0371 -0.0456 -0.0903 119 ARG A NH1 
1179 N NH2 . ARG A 119 ? 0.6099 0.6118 0.5379 -0.0223 -0.0471 -0.0452 119 ARG A NH2 
1180 N N   . GLY A 120 ? 0.1855 0.2412 0.2078 0.0273  -0.0226 -0.0495 120 GLY A N   
1181 C CA  . GLY A 120 ? 0.1723 0.2704 0.2026 0.0155  -0.0232 -0.0571 120 GLY A CA  
1182 C C   . GLY A 120 ? 0.1637 0.2529 0.1639 0.0018  -0.0070 -0.0427 120 GLY A C   
1183 O O   . GLY A 120 ? 0.1820 0.3113 0.1636 -0.0039 0.0073  -0.0474 120 GLY A O   
1184 N N   . CYS A 121 ? 0.1674 0.2189 0.1400 0.0113  -0.0069 -0.0322 121 CYS A N   
1185 C CA  . CYS A 121 ? 0.1612 0.2065 0.1280 0.0184  -0.0034 -0.0257 121 CYS A CA  
1186 C C   . CYS A 121 ? 0.1850 0.1892 0.1445 0.0115  -0.0065 -0.0007 121 CYS A C   
1187 O O   . CYS A 121 ? 0.2323 0.2527 0.1448 0.0056  -0.0084 -0.0299 121 CYS A O   
1188 C CB  . CYS A 121 ? 0.1623 0.2036 0.1449 0.0136  0.0100  -0.0188 121 CYS A CB  
1189 S SG  . CYS A 121 ? 0.1950 0.2022 0.1188 0.0075  0.0106  -0.0146 121 CYS A SG  
1190 N N   . ARG A 122 ? 0.1373 0.2877 0.1485 0.0288  0.0104  0.0428  122 ARG A N   
1191 C CA  . ARG A 122 ? 0.1417 0.2116 0.1661 0.0387  0.0205  0.0214  122 ARG A CA  
1192 C C   . ARG A 122 ? 0.1311 0.1923 0.0959 0.0230  -0.0098 -0.0039 122 ARG A C   
1193 O O   . ARG A 122 ? 0.1555 0.1959 0.1275 0.0246  0.0009  0.0048  122 ARG A O   
1194 C CB  . ARG A 122 ? 0.2202 0.2058 0.1970 0.0492  0.0445  -0.0192 122 ARG A CB  
1195 C CG  . ARG A 122 ? 0.2701 0.2233 0.1667 0.0448  0.0312  -0.0441 122 ARG A CG  
1196 C CD  . ARG A 122 ? 0.3216 0.2652 0.2357 0.0247  0.0033  -0.0719 122 ARG A CD  
1197 N NE  . ARG A 122 ? 0.3133 0.3492 0.1973 0.0130  0.0104  -0.0992 122 ARG A NE  
1198 C CZ  . ARG A 122 ? 0.3039 0.3687 0.2445 0.0289  -0.0073 -0.0914 122 ARG A CZ  
1199 N NH1 . ARG A 122 ? 0.2534 0.2978 0.1876 0.0372  -0.0621 -0.1188 122 ARG A NH1 
1200 N NH2 . ARG A 122 ? 0.3579 0.4445 0.2574 -0.0006 -0.0310 -0.0733 122 ARG A NH2 
1201 N N   . GLY A 123 ? 0.1164 0.1577 0.0986 0.0169  -0.0160 -0.0150 123 GLY A N   
1202 C CA  . GLY A 123 ? 0.1122 0.1550 0.0863 0.0097  -0.0093 -0.0324 123 GLY A CA  
1203 C C   . GLY A 123 ? 0.1191 0.1489 0.0655 0.0115  -0.0117 -0.0240 123 GLY A C   
1204 O O   . GLY A 123 ? 0.1286 0.1743 0.1108 0.0223  -0.0231 -0.0584 123 GLY A O   
1205 N N   . VAL A 124 ? 0.1127 0.1538 0.0684 0.0105  -0.0116 -0.0314 124 VAL A N   
1206 C CA  . VAL A 124 ? 0.1191 0.1850 0.0644 0.0232  -0.0192 -0.0369 124 VAL A CA  
1207 C C   . VAL A 124 ? 0.1173 0.1416 0.0609 0.0181  -0.0212 -0.0365 124 VAL A C   
1208 O O   . VAL A 124 ? 0.1234 0.1421 0.0576 -0.0019 -0.0107 -0.0331 124 VAL A O   
1209 C CB  . VAL A 124 ? 0.1332 0.2815 0.0815 0.0338  -0.0120 0.0135  124 VAL A CB  
1210 C CG1 . VAL A 124 ? 0.1973 0.3422 0.0990 0.0774  0.0187  0.0337  124 VAL A CG1 
1211 C CG2 . VAL A 124 ? 0.1836 0.2797 0.0962 0.0538  0.0019  0.0214  124 VAL A CG2 
1212 N N   . ARG A 125 ? 0.1244 0.1677 0.0710 0.0061  -0.0145 -0.0566 125 ARG A N   
1213 C CA  . ARG A 125 ? 0.1260 0.1486 0.0797 -0.0037 -0.0204 -0.0405 125 ARG A CA  
1214 C C   . ARG A 125 ? 0.1263 0.1489 0.0722 -0.0074 -0.0157 -0.0385 125 ARG A C   
1215 O O   . ARG A 125 ? 0.1355 0.1836 0.0920 -0.0044 -0.0174 -0.0657 125 ARG A O   
1216 C CB  . ARG A 125 ? 0.1470 0.1603 0.1114 0.0060  -0.0388 -0.0320 125 ARG A CB  
1217 C CG  . ARG A 125 ? 0.1641 0.1585 0.1113 -0.0058 -0.0338 -0.0190 125 ARG A CG  
1218 C CD  . ARG A 125 ? 0.2029 0.1692 0.1464 -0.0170 -0.0581 -0.0018 125 ARG A CD  
1219 N NE  . ARG A 125 ? 0.2046 0.1500 0.1541 -0.0157 -0.0602 0.0052  125 ARG A NE  
1220 C CZ  . ARG A 125 ? 0.2361 0.1830 0.1756 -0.0108 -0.0647 0.0321  125 ARG A CZ  
1221 N NH1 . ARG A 125 ? 0.2993 0.2309 0.2655 -0.0557 -0.1073 0.0940  125 ARG A NH1 
1222 N NH2 . ARG A 125 ? 0.2680 0.2093 0.2094 -0.0194 -0.1017 0.0391  125 ARG A NH2 
1223 N N   . CYS A 126 ? 0.1226 0.1404 0.0583 -0.0108 -0.0088 -0.0301 126 CYS A N   
1224 C CA  . CYS A 126 ? 0.1251 0.1458 0.0464 -0.0005 -0.0174 -0.0194 126 CYS A CA  
1225 C C   . CYS A 126 ? 0.1210 0.1440 0.0556 -0.0113 -0.0155 -0.0249 126 CYS A C   
1226 O O   . CYS A 126 ? 0.1273 0.1588 0.0642 -0.0051 -0.0126 -0.0343 126 CYS A O   
1227 C CB  . CYS A 126 ? 0.1616 0.1847 0.0825 0.0420  0.0042  0.0175  126 CYS A CB  
1228 S SG  . CYS A 126 ? 0.1735 0.1857 0.0739 0.0212  -0.0186 -0.0040 126 CYS A SG  
1229 N N   . ALA A 127 ? 0.1576 0.1502 0.0538 -0.0223 -0.0038 -0.0224 127 ALA A N   
1230 C CA  . ALA A 127 ? 0.1859 0.1998 0.0529 -0.0331 0.0001  -0.0211 127 ALA A CA  
1231 C C   . ALA A 127 ? 0.1710 0.1654 0.0854 -0.0094 -0.0107 0.0200  127 ALA A C   
1232 O O   . ALA A 127 ? 0.2227 0.2450 0.0914 -0.0032 0.0092  0.0464  127 ALA A O   
1233 C CB  . ALA A 127 ? 0.2044 0.3200 0.0702 -0.0765 -0.0370 0.0183  127 ALA A CB  
1234 N N   . ALA A 128 ? 0.1512 0.1551 0.0844 -0.0051 -0.0139 0.0206  128 ALA A N   
1235 C CA  . ALA A 128 ? 0.1549 0.1477 0.0989 -0.0116 -0.0150 0.0246  128 ALA A CA  
1236 C C   . ALA A 128 ? 0.1550 0.1392 0.0839 -0.0084 -0.0187 0.0329  128 ALA A C   
1237 O O   . ALA A 128 ? 0.1525 0.1517 0.0954 -0.0127 -0.0186 0.0246  128 ALA A O   
1238 C CB  . ALA A 128 ? 0.1701 0.1889 0.1083 -0.0109 -0.0111 0.0015  128 ALA A CB  
1239 N N   . ASP A 129 ? 0.1514 0.1377 0.1030 -0.0053 -0.0105 0.0334  129 ASP A N   
1240 C CA  . ASP A 129 ? 0.1526 0.1566 0.0813 -0.0074 -0.0055 0.0345  129 ASP A CA  
1241 C C   . ASP A 129 ? 0.1400 0.1257 0.0709 -0.0073 0.0033  0.0150  129 ASP A C   
1242 O O   . ASP A 129 ? 0.1489 0.1343 0.0893 -0.0177 -0.0002 0.0168  129 ASP A O   
1243 C CB  . ASP A 129 ? 0.1726 0.1810 0.1164 -0.0114 -0.0009 0.0643  129 ASP A CB  
1244 C CG  . ASP A 129 ? 0.1676 0.2150 0.1049 -0.0173 0.0054  0.0691  129 ASP A CG  
1245 O OD1 . ASP A 129 ? 0.1678 0.2209 0.0783 -0.0197 -0.0053 0.0390  129 ASP A OD1 
1246 O OD2 . ASP A 129 ? 0.1993 0.2462 0.1792 -0.0340 0.0363  0.0782  129 ASP A OD2 
1247 N N   . ILE A 130 ? 0.1285 0.1179 0.0583 -0.0084 -0.0093 0.0097  130 ILE A N   
1248 C CA  . ILE A 130 ? 0.1275 0.1122 0.0442 -0.0112 -0.0113 -0.0013 130 ILE A CA  
1249 C C   . ILE A 130 ? 0.1265 0.1219 0.0401 -0.0147 -0.0080 -0.0011 130 ILE A C   
1250 O O   . ILE A 130 ? 0.1271 0.1484 0.0511 -0.0113 -0.0139 -0.0072 130 ILE A O   
1251 C CB  . ILE A 130 ? 0.1270 0.1132 0.0451 -0.0129 -0.0106 -0.0062 130 ILE A CB  
1252 C CG1 . ILE A 130 ? 0.1409 0.1293 0.0695 -0.0065 0.0061  -0.0071 130 ILE A CG1 
1253 C CG2 . ILE A 130 ? 0.1443 0.1250 0.0549 -0.0204 -0.0196 0.0073  130 ILE A CG2 
1254 C CD1 . ILE A 130 ? 0.1421 0.1448 0.0932 -0.0159 0.0043  -0.0074 130 ILE A CD1 
1255 N N   . VAL A 131 ? 0.1217 0.1288 0.0430 -0.0056 -0.0111 -0.0060 131 VAL A N   
1256 C CA  . VAL A 131 ? 0.1305 0.1366 0.0427 -0.0027 -0.0108 -0.0009 131 VAL A CA  
1257 C C   . VAL A 131 ? 0.1355 0.1475 0.0429 -0.0079 -0.0078 -0.0104 131 VAL A C   
1258 O O   . VAL A 131 ? 0.1359 0.1574 0.0674 -0.0118 -0.0092 -0.0043 131 VAL A O   
1259 C CB  . VAL A 131 ? 0.1371 0.1574 0.0603 -0.0106 -0.0039 -0.0212 131 VAL A CB  
1260 C CG1 . VAL A 131 ? 0.1505 0.1828 0.1229 -0.0004 -0.0073 -0.0599 131 VAL A CG1 
1261 C CG2 . VAL A 131 ? 0.1410 0.1445 0.0779 -0.0056 -0.0108 -0.0129 131 VAL A CG2 
1262 N N   . GLY A 132 ? 0.1388 0.1499 0.0422 -0.0193 -0.0055 -0.0003 132 GLY A N   
1263 C CA  . GLY A 132 ? 0.1595 0.1670 0.0430 -0.0311 0.0043  0.0064  132 GLY A CA  
1264 C C   . GLY A 132 ? 0.1471 0.1429 0.0541 -0.0326 0.0000  0.0119  132 GLY A C   
1265 O O   . GLY A 132 ? 0.1490 0.1621 0.0651 -0.0356 0.0087  0.0009  132 GLY A O   
1266 N N   . GLN A 133 ? 0.1437 0.1279 0.0443 -0.0283 -0.0035 0.0060  133 GLN A N   
1267 C CA  . GLN A 133 ? 0.1465 0.1206 0.0475 -0.0272 -0.0037 0.0032  133 GLN A CA  
1268 C C   . GLN A 133 ? 0.1270 0.1294 0.0455 -0.0255 -0.0069 0.0041  133 GLN A C   
1269 O O   . GLN A 133 ? 0.1597 0.1330 0.0459 -0.0274 -0.0111 0.0004  133 GLN A O   
1270 C CB  . GLN A 133 ? 0.1519 0.1288 0.0657 -0.0221 -0.0054 0.0024  133 GLN A CB  
1271 C CG  . GLN A 133 ? 0.1741 0.1335 0.0820 -0.0094 -0.0159 0.0054  133 GLN A CG  
1272 C CD  . GLN A 133 ? 0.2040 0.1371 0.0790 -0.0214 -0.0107 0.0133  133 GLN A CD  
1273 O OE1 . GLN A 133 ? 0.2260 0.1463 0.0698 -0.0592 -0.0250 0.0115  133 GLN A OE1 
1274 N NE2 . GLN A 133 ? 0.2425 0.2107 0.1668 -0.0463 -0.0430 0.0858  133 GLN A NE2 
1275 N N   . CYS A 134 ? 0.1346 0.1292 0.0476 -0.0204 -0.0137 0.0040  134 CYS A N   
1276 C CA  . CYS A 134 ? 0.1294 0.1311 0.0615 -0.0195 -0.0163 0.0080  134 CYS A CA  
1277 C C   . CYS A 134 ? 0.1322 0.1262 0.0621 -0.0184 -0.0168 0.0080  134 CYS A C   
1278 O O   . CYS A 134 ? 0.1290 0.1611 0.0831 -0.0254 -0.0148 0.0073  134 CYS A O   
1279 C CB  . CYS A 134 ? 0.1340 0.1462 0.0442 -0.0189 -0.0067 -0.0010 134 CYS A CB  
1280 S SG  . CYS A 134 ? 0.1333 0.1319 0.0579 -0.0056 -0.0160 -0.0021 134 CYS A SG  
1281 N N   . PRO A 135 ? 0.1421 0.1308 0.0553 -0.0124 -0.0231 -0.0034 135 PRO A N   
1282 C CA  . PRO A 135 ? 0.1531 0.1435 0.0786 -0.0088 -0.0401 -0.0162 135 PRO A CA  
1283 C C   . PRO A 135 ? 0.1358 0.1466 0.0578 -0.0215 -0.0271 -0.0028 135 PRO A C   
1284 O O   . PRO A 135 ? 0.1268 0.1386 0.0637 -0.0104 -0.0162 -0.0023 135 PRO A O   
1285 C CB  . PRO A 135 ? 0.2145 0.2086 0.0598 0.0551  -0.0281 -0.0293 135 PRO A CB  
1286 C CG  . PRO A 135 ? 0.1900 0.2274 0.0693 -0.0073 -0.0231 -0.0176 135 PRO A CG  
1287 C CD  . PRO A 135 ? 0.1499 0.1456 0.0569 -0.0113 -0.0077 -0.0021 135 PRO A CD  
1288 N N   . ALA A 136 ? 0.1392 0.1599 0.0892 -0.0257 -0.0274 -0.0045 136 ALA A N   
1289 C CA  . ALA A 136 ? 0.1450 0.1762 0.0767 -0.0260 -0.0117 0.0069  136 ALA A CA  
1290 C C   . ALA A 136 ? 0.1173 0.1711 0.0695 -0.0181 -0.0045 -0.0041 136 ALA A C   
1291 O O   . ALA A 136 ? 0.1336 0.1876 0.0842 -0.0103 0.0064  -0.0138 136 ALA A O   
1292 C CB  . ALA A 136 ? 0.1394 0.2122 0.1726 -0.0347 -0.0043 0.0209  136 ALA A CB  
1293 N N   . LYS A 137 ? 0.1143 0.1658 0.0604 -0.0097 -0.0146 -0.0068 137 LYS A N   
1294 C CA  . LYS A 137 ? 0.1147 0.1737 0.0809 -0.0117 -0.0221 0.0059  137 LYS A CA  
1295 C C   . LYS A 137 ? 0.1161 0.1569 0.0733 -0.0019 -0.0214 0.0023  137 LYS A C   
1296 O O   . LYS A 137 ? 0.1298 0.1587 0.1358 0.0040  -0.0312 0.0152  137 LYS A O   
1297 C CB  . LYS A 137 ? 0.1378 0.2142 0.0780 -0.0168 -0.0342 0.0218  137 LYS A CB  
1298 C CG  . LYS A 137 ? 0.1477 0.2425 0.0962 -0.0285 -0.0412 0.0149  137 LYS A CG  
1299 C CD  . LYS A 137 ? 0.2006 0.2960 0.1018 -0.0754 -0.0544 0.0185  137 LYS A CD  
1300 C CE  . LYS A 137 ? 0.2096 0.3700 0.1492 -0.0822 -0.0716 0.0244  137 LYS A CE  
1301 N NZ  . LYS A 137 ? 0.2843 0.4119 0.1585 -0.1009 -0.0732 0.0038  137 LYS A NZ  
1302 N N   . LEU A 138 ? 0.1055 0.1349 0.0510 -0.0072 -0.0128 -0.0099 138 LEU A N   
1303 C CA  . LEU A 138 ? 0.1047 0.1356 0.0487 -0.0112 -0.0062 -0.0074 138 LEU A CA  
1304 C C   . LEU A 138 ? 0.1003 0.1249 0.0549 0.0042  -0.0077 -0.0133 138 LEU A C   
1305 O O   . LEU A 138 ? 0.1097 0.1523 0.0633 -0.0091 0.0054  -0.0331 138 LEU A O   
1306 C CB  . LEU A 138 ? 0.1096 0.1342 0.0377 -0.0054 -0.0075 -0.0080 138 LEU A CB  
1307 C CG  . LEU A 138 ? 0.1252 0.1463 0.0385 -0.0121 -0.0048 -0.0125 138 LEU A CG  
1308 C CD1 . LEU A 138 ? 0.1365 0.1630 0.0454 -0.0021 0.0048  -0.0195 138 LEU A CD1 
1309 C CD2 . LEU A 138 ? 0.1461 0.1583 0.0407 -0.0124 -0.0035 -0.0035 138 LEU A CD2 
1310 N N   . LYS A 139 ? 0.1126 0.1449 0.0463 -0.0100 -0.0049 -0.0153 139 LYS A N   
1311 C CA  . LYS A 139 ? 0.1319 0.1563 0.0440 0.0007  -0.0030 -0.0134 139 LYS A CA  
1312 C C   . LYS A 139 ? 0.1121 0.1702 0.0814 -0.0003 0.0066  -0.0316 139 LYS A C   
1313 O O   . LYS A 139 ? 0.1377 0.1699 0.1106 0.0156  0.0055  -0.0190 139 LYS A O   
1314 C CB  . LYS A 139 ? 0.1697 0.1777 0.0570 -0.0243 0.0031  -0.0064 139 LYS A CB  
1315 C CG  . LYS A 139 ? 0.1937 0.1876 0.0872 0.0031  0.0145  -0.0118 139 LYS A CG  
1316 C CD  . LYS A 139 ? 0.2465 0.2133 0.1181 -0.0137 0.0472  0.0167  139 LYS A CD  
1317 C CE  . LYS A 139 ? 0.3267 0.2251 0.1989 -0.0053 0.0478  0.0336  139 LYS A CE  
1318 N NZ  . LYS A 139 ? 0.3626 0.2827 0.2103 0.0334  0.0511  0.0574  139 LYS A NZ  
1319 N N   . ALA A 140 ? 0.1261 0.1935 0.0992 0.0010  0.0136  -0.0722 140 ALA A N   
1320 C CA  . ALA A 140 ? 0.1671 0.1864 0.1339 -0.0159 0.0270  -0.0480 140 ALA A CA  
1321 C C   . ALA A 140 ? 0.1693 0.1903 0.0929 0.0151  0.0137  -0.0089 140 ALA A C   
1322 O O   . ALA A 140 ? 0.1760 0.1723 0.0862 0.0102  0.0178  -0.0103 140 ALA A O   
1323 C CB  . ALA A 140 ? 0.1846 0.2164 0.1166 -0.0427 0.0291  -0.0479 140 ALA A CB  
1324 N N   . PRO A 141 ? 0.1648 0.2012 0.1346 0.0172  0.0155  -0.0065 141 PRO A N   
1325 C CA  . PRO A 141 ? 0.1746 0.2127 0.1312 -0.0031 0.0225  -0.0104 141 PRO A CA  
1326 C C   . PRO A 141 ? 0.1708 0.2089 0.1342 -0.0131 0.0294  -0.0102 141 PRO A C   
1327 O O   . PRO A 141 ? 0.2345 0.2272 0.1371 -0.0228 0.0570  -0.0280 141 PRO A O   
1328 C CB  . PRO A 141 ? 0.1740 0.2143 0.2032 0.0057  0.0128  -0.0341 141 PRO A CB  
1329 C CG  . PRO A 141 ? 0.1950 0.2072 0.2007 0.0263  0.0027  -0.0267 141 PRO A CG  
1330 C CD  . PRO A 141 ? 0.1893 0.2122 0.1458 0.0296  -0.0075 -0.0118 141 PRO A CD  
1331 N N   . GLY A 142 ? 0.1771 0.1946 0.1249 -0.0068 0.0148  -0.0043 142 GLY A N   
1332 C CA  . GLY A 142 ? 0.1722 0.1829 0.1450 -0.0024 0.0188  -0.0186 142 GLY A CA  
1333 C C   . GLY A 142 ? 0.1721 0.1739 0.1202 -0.0085 0.0126  -0.0206 142 GLY A C   
1334 O O   . GLY A 142 ? 0.2089 0.2336 0.1213 0.0012  -0.0059 -0.0237 142 GLY A O   
1335 N N   . GLY A 143 ? 0.1726 0.1914 0.0903 0.0126  -0.0051 -0.0260 143 GLY A N   
1336 C CA  . GLY A 143 ? 0.1942 0.1861 0.0936 0.0143  -0.0016 -0.0234 143 GLY A CA  
1337 C C   . GLY A 143 ? 0.1695 0.1993 0.0818 0.0061  -0.0036 -0.0225 143 GLY A C   
1338 O O   . GLY A 143 ? 0.1712 0.1909 0.1185 0.0029  0.0075  -0.0186 143 GLY A O   
1339 N N   . GLY A 144 ? 0.1717 0.2378 0.0538 0.0161  0.0056  -0.0019 144 GLY A N   
1340 C CA  . GLY A 144 ? 0.1392 0.1722 0.0331 -0.0112 0.0014  0.0074  144 GLY A CA  
1341 C C   . GLY A 144 ? 0.1056 0.1781 0.0383 -0.0103 -0.0005 0.0067  144 GLY A C   
1342 O O   . GLY A 144 ? 0.1100 0.2812 0.0588 -0.0074 0.0019  -0.0138 144 GLY A O   
1343 N N   . CYS A 145 ? 0.0972 0.1473 0.0293 -0.0074 -0.0108 0.0138  145 CYS A N   
1344 C CA  . CYS A 145 ? 0.0972 0.1343 0.0332 -0.0021 -0.0072 0.0087  145 CYS A CA  
1345 C C   . CYS A 145 ? 0.0949 0.1257 0.0259 -0.0020 -0.0060 0.0032  145 CYS A C   
1346 O O   . CYS A 145 ? 0.0984 0.1411 0.0345 -0.0071 -0.0094 0.0136  145 CYS A O   
1347 C CB  . CYS A 145 ? 0.1080 0.1368 0.0530 -0.0041 0.0005  0.0136  145 CYS A CB  
1348 S SG  . CYS A 145 ? 0.1398 0.1428 0.0584 0.0056  0.0015  0.0006  145 CYS A SG  
1349 N N   . ASN A 146 ? 0.0999 0.1331 0.0300 0.0020  -0.0058 0.0097  146 ASN A N   
1350 C CA  . ASN A 146 ? 0.1179 0.1310 0.0259 -0.0022 -0.0059 0.0050  146 ASN A CA  
1351 C C   . ASN A 146 ? 0.1060 0.1278 0.0297 -0.0018 -0.0092 0.0049  146 ASN A C   
1352 O O   . ASN A 146 ? 0.1200 0.1313 0.0504 -0.0067 0.0005  -0.0040 146 ASN A O   
1353 C CB  . ASN A 146 ? 0.1323 0.1492 0.0388 0.0155  0.0001  0.0146  146 ASN A CB  
1354 C CG  . ASN A 146 ? 0.1510 0.1547 0.0707 0.0066  0.0060  -0.0021 146 ASN A CG  
1355 O OD1 . ASN A 146 ? 0.1634 0.1631 0.1178 -0.0130 0.0085  -0.0206 146 ASN A OD1 
1356 N ND2 . ASN A 146 ? 0.1533 0.2046 0.1073 0.0125  0.0165  -0.0301 146 ASN A ND2 
1357 N N   . ASP A 147 ? 0.1175 0.1388 0.0269 -0.0103 -0.0121 0.0030  147 ASP A N   
1358 C CA  . ASP A 147 ? 0.1154 0.1384 0.0263 0.0017  -0.0095 0.0018  147 ASP A CA  
1359 C C   . ASP A 147 ? 0.1091 0.1283 0.0262 -0.0012 -0.0088 0.0015  147 ASP A C   
1360 O O   . ASP A 147 ? 0.1239 0.1361 0.0277 0.0085  -0.0149 -0.0051 147 ASP A O   
1361 C CB  . ASP A 147 ? 0.1152 0.1566 0.0292 -0.0025 -0.0124 0.0043  147 ASP A CB  
1362 C CG  . ASP A 147 ? 0.1193 0.1619 0.0354 -0.0023 -0.0124 0.0078  147 ASP A CG  
1363 O OD1 . ASP A 147 ? 0.1339 0.1597 0.0480 0.0004  -0.0163 -0.0008 147 ASP A OD1 
1364 O OD2 . ASP A 147 ? 0.1438 0.1722 0.0469 0.0007  -0.0121 0.0203  147 ASP A OD2 
1365 N N   . ALA A 148 ? 0.1113 0.1279 0.0265 0.0038  -0.0101 0.0010  148 ALA A N   
1366 C CA  . ALA A 148 ? 0.1139 0.1322 0.0286 0.0026  -0.0166 0.0035  148 ALA A CA  
1367 C C   . ALA A 148 ? 0.1192 0.1257 0.0291 0.0060  -0.0180 -0.0072 148 ALA A C   
1368 O O   . ALA A 148 ? 0.1283 0.1364 0.0621 0.0131  -0.0327 -0.0019 148 ALA A O   
1369 C CB  . ALA A 148 ? 0.1435 0.1281 0.0318 0.0000  -0.0276 0.0004  148 ALA A CB  
1370 N N   . CYS A 149 ? 0.1216 0.1213 0.0272 0.0071  -0.0124 0.0047  149 CYS A N   
1371 C CA  . CYS A 149 ? 0.1474 0.1251 0.0272 -0.0033 -0.0151 0.0022  149 CYS A CA  
1372 C C   . CYS A 149 ? 0.1464 0.1208 0.0296 0.0062  -0.0185 0.0023  149 CYS A C   
1373 O O   . CYS A 149 ? 0.1642 0.1267 0.0373 0.0135  -0.0252 0.0035  149 CYS A O   
1374 C CB  . CYS A 149 ? 0.1523 0.1398 0.0505 -0.0133 -0.0100 0.0006  149 CYS A CB  
1375 S SG  . CYS A 149 ? 0.1884 0.1501 0.0743 -0.0257 -0.0088 0.0050  149 CYS A SG  
1376 N N   . THR A 150 ? 0.1524 0.1248 0.0287 0.0151  -0.0200 -0.0019 150 THR A N   
1377 C CA  . THR A 150 ? 0.1548 0.1281 0.0370 0.0141  -0.0195 -0.0109 150 THR A CA  
1378 C C   . THR A 150 ? 0.1541 0.1341 0.0276 0.0193  -0.0140 -0.0053 150 THR A C   
1379 O O   . THR A 150 ? 0.1621 0.1377 0.0811 0.0211  -0.0349 -0.0225 150 THR A O   
1380 C CB  . THR A 150 ? 0.1534 0.1548 0.0351 0.0128  -0.0236 -0.0126 150 THR A CB  
1381 O OG1 . THR A 150 ? 0.1665 0.1648 0.0489 0.0024  -0.0353 -0.0124 150 THR A OG1 
1382 C CG2 . THR A 150 ? 0.1831 0.2371 0.0435 0.0454  -0.0199 -0.0242 150 THR A CG2 
1383 N N   . VAL A 151 ? 0.1437 0.1271 0.0257 0.0130  -0.0043 -0.0055 151 VAL A N   
1384 C CA  . VAL A 151 ? 0.1409 0.1447 0.0256 0.0183  0.0042  -0.0033 151 VAL A CA  
1385 C C   . VAL A 151 ? 0.1355 0.1452 0.0297 0.0228  0.0011  -0.0011 151 VAL A C   
1386 O O   . VAL A 151 ? 0.1514 0.1780 0.0397 0.0435  0.0092  0.0076  151 VAL A O   
1387 C CB  . VAL A 151 ? 0.1453 0.1429 0.0271 0.0070  -0.0016 -0.0015 151 VAL A CB  
1388 C CG1 . VAL A 151 ? 0.1440 0.1582 0.0390 0.0051  0.0009  -0.0034 151 VAL A CG1 
1389 C CG2 . VAL A 151 ? 0.1505 0.1511 0.0424 -0.0049 -0.0089 0.0172  151 VAL A CG2 
1390 N N   . PHE A 152 ? 0.1308 0.1530 0.0258 0.0198  -0.0043 0.0058  152 PHE A N   
1391 C CA  . PHE A 152 ? 0.1208 0.1642 0.0257 0.0243  -0.0040 0.0050  152 PHE A CA  
1392 C C   . PHE A 152 ? 0.1297 0.1616 0.0287 0.0305  -0.0026 0.0132  152 PHE A C   
1393 O O   . PHE A 152 ? 0.1406 0.1874 0.0322 0.0254  -0.0096 0.0207  152 PHE A O   
1394 C CB  . PHE A 152 ? 0.1241 0.1684 0.0272 0.0244  -0.0035 0.0004  152 PHE A CB  
1395 C CG  . PHE A 152 ? 0.1296 0.1755 0.0262 0.0169  0.0003  -0.0112 152 PHE A CG  
1396 C CD1 . PHE A 152 ? 0.1338 0.1782 0.0340 0.0252  -0.0031 -0.0179 152 PHE A CD1 
1397 C CD2 . PHE A 152 ? 0.1329 0.1623 0.0325 0.0178  0.0016  -0.0100 152 PHE A CD2 
1398 C CE1 . PHE A 152 ? 0.1313 0.2023 0.0532 0.0036  0.0083  -0.0359 152 PHE A CE1 
1399 C CE2 . PHE A 152 ? 0.1651 0.1536 0.0438 0.0108  0.0080  -0.0176 152 PHE A CE2 
1400 C CZ  . PHE A 152 ? 0.1599 0.1750 0.0502 -0.0086 0.0130  -0.0255 152 PHE A CZ  
1401 N N   . GLN A 153 ? 0.1367 0.1405 0.0268 0.0276  -0.0055 0.0099  153 GLN A N   
1402 C CA  . GLN A 153 ? 0.1428 0.1328 0.0275 0.0277  -0.0093 0.0028  153 GLN A CA  
1403 C C   . GLN A 153 ? 0.1196 0.1363 0.0278 0.0118  -0.0127 0.0075  153 GLN A C   
1404 O O   . GLN A 153 ? 0.1497 0.1351 0.0372 0.0139  -0.0077 0.0106  153 GLN A O   
1405 C CB  . GLN A 153 ? 0.1746 0.1523 0.0323 0.0512  0.0059  0.0179  153 GLN A CB  
1406 C CG  . GLN A 153 ? 0.2314 0.1555 0.0416 0.0729  0.0115  0.0080  153 GLN A CG  
1407 C CD  . GLN A 153 ? 0.2606 0.1484 0.0348 0.0842  -0.0008 0.0002  153 GLN A CD  
1408 O OE1 . GLN A 153 ? 0.2801 0.1588 0.0786 0.0814  0.0296  0.0301  153 GLN A OE1 
1409 N NE2 . GLN A 153 ? 0.2774 0.1410 0.0890 0.0652  -0.0685 -0.0229 153 GLN A NE2 
1410 N N   . THR A 154 ? 0.1371 0.1457 0.0262 0.0257  -0.0064 0.0062  154 THR A N   
1411 C CA  . THR A 154 ? 0.1263 0.1390 0.0264 0.0159  -0.0105 -0.0018 154 THR A CA  
1412 C C   . THR A 154 ? 0.1285 0.1136 0.0268 0.0073  -0.0120 -0.0041 154 THR A C   
1413 O O   . THR A 154 ? 0.1243 0.1262 0.0300 0.0037  -0.0109 -0.0052 154 THR A O   
1414 C CB  . THR A 154 ? 0.1240 0.1481 0.0284 0.0013  -0.0098 -0.0021 154 THR A CB  
1415 O OG1 . THR A 154 ? 0.1256 0.1353 0.0465 0.0023  -0.0188 -0.0065 154 THR A OG1 
1416 C CG2 . THR A 154 ? 0.1283 0.1728 0.0466 0.0021  -0.0068 0.0013  154 THR A CG2 
1417 N N   . SER A 155 ? 0.1309 0.1118 0.0267 0.0032  -0.0073 -0.0027 155 SER A N   
1418 C CA  . SER A 155 ? 0.1397 0.1131 0.0420 -0.0079 0.0047  -0.0038 155 SER A CA  
1419 C C   . SER A 155 ? 0.1223 0.1217 0.0329 -0.0054 0.0028  -0.0029 155 SER A C   
1420 O O   . SER A 155 ? 0.1229 0.1272 0.0751 -0.0056 0.0047  -0.0039 155 SER A O   
1421 C CB  . SER A 155 ? 0.1661 0.1211 0.0521 -0.0071 0.0134  0.0081  155 SER A CB  
1422 O OG  . SER A 155 ? 0.3015 0.1405 0.0714 0.0148  0.0107  0.0083  155 SER A OG  
1423 N N   . GLU A 156 ? 0.1198 0.1124 0.0295 -0.0001 -0.0044 -0.0036 156 GLU A N   
1424 C CA  . GLU A 156 ? 0.1284 0.1115 0.0309 0.0042  -0.0010 -0.0071 156 GLU A CA  
1425 C C   . GLU A 156 ? 0.1282 0.1103 0.0350 0.0081  -0.0044 -0.0061 156 GLU A C   
1426 O O   . GLU A 156 ? 0.1354 0.1629 0.0450 0.0275  0.0004  -0.0004 156 GLU A O   
1427 C CB  . GLU A 156 ? 0.1422 0.1176 0.0322 0.0003  -0.0056 -0.0045 156 GLU A CB  
1428 C CG  . GLU A 156 ? 0.1635 0.1205 0.0472 0.0084  -0.0047 -0.0010 156 GLU A CG  
1429 C CD  . GLU A 156 ? 0.1702 0.1171 0.0466 0.0054  -0.0034 -0.0086 156 GLU A CD  
1430 O OE1 . GLU A 156 ? 0.1747 0.1361 0.0500 0.0117  0.0051  0.0003  156 GLU A OE1 
1431 O OE2 . GLU A 156 ? 0.1798 0.1382 0.0730 0.0224  0.0162  0.0007  156 GLU A OE2 
1432 N N   . TYR A 157 ? 0.1179 0.1236 0.0266 0.0068  -0.0070 -0.0023 157 TYR A N   
1433 C CA  . TYR A 157 ? 0.1200 0.1264 0.0280 0.0087  -0.0072 0.0040  157 TYR A CA  
1434 C C   . TYR A 157 ? 0.1233 0.1341 0.0386 0.0027  -0.0055 0.0090  157 TYR A C   
1435 O O   . TYR A 157 ? 0.1462 0.1537 0.0606 0.0026  -0.0345 0.0122  157 TYR A O   
1436 C CB  . TYR A 157 ? 0.1294 0.1256 0.0265 0.0044  -0.0022 -0.0015 157 TYR A CB  
1437 C CG  . TYR A 157 ? 0.1294 0.1345 0.0257 0.0040  -0.0065 -0.0020 157 TYR A CG  
1438 C CD1 . TYR A 157 ? 0.1219 0.1317 0.0512 0.0069  0.0000  -0.0091 157 TYR A CD1 
1439 C CD2 . TYR A 157 ? 0.1317 0.1361 0.0261 0.0096  -0.0003 -0.0095 157 TYR A CD2 
1440 C CE1 . TYR A 157 ? 0.1361 0.1242 0.0556 0.0020  0.0006  -0.0098 157 TYR A CE1 
1441 C CE2 . TYR A 157 ? 0.1170 0.1482 0.0262 0.0073  -0.0025 -0.0089 157 TYR A CE2 
1442 C CZ  . TYR A 157 ? 0.1322 0.1434 0.0258 0.0005  0.0006  -0.0075 157 TYR A CZ  
1443 O OH  . TYR A 157 ? 0.1353 0.1415 0.0364 -0.0097 0.0004  -0.0114 157 TYR A OH  
1444 N N   . CYS A 158 ? 0.1298 0.1363 0.0478 -0.0048 -0.0134 0.0053  158 CYS A N   
1445 C CA  . CYS A 158 ? 0.1328 0.1499 0.0623 -0.0093 -0.0174 0.0095  158 CYS A CA  
1446 C C   . CYS A 158 ? 0.1376 0.1635 0.0875 -0.0142 -0.0156 0.0203  158 CYS A C   
1447 O O   . CYS A 158 ? 0.1593 0.1716 0.1319 -0.0304 -0.0062 -0.0121 158 CYS A O   
1448 C CB  . CYS A 158 ? 0.1556 0.1429 0.0791 -0.0126 -0.0216 0.0047  158 CYS A CB  
1449 S SG  . CYS A 158 ? 0.1611 0.1516 0.0746 -0.0065 -0.0064 0.0042  158 CYS A SG  
1450 N N   . CYS A 159 ? 0.1534 0.1958 0.0791 -0.0082 -0.0006 0.0190  159 CYS A N   
1451 C CA  A CYS A 159 ? 0.1564 0.1859 0.1116 -0.0071 0.0067  0.0135  159 CYS A CA  
1452 C CA  B CYS A 159 ? 0.1668 0.1961 0.1019 0.0119  0.0067  0.0366  159 CYS A CA  
1453 C C   . CYS A 159 ? 0.1514 0.1837 0.1262 0.0063  0.0098  0.0217  159 CYS A C   
1454 O O   . CYS A 159 ? 0.1551 0.2201 0.2113 0.0059  0.0236  0.0554  159 CYS A O   
1455 C CB  A CYS A 159 ? 0.1793 0.1707 0.1187 -0.0015 0.0042  0.0150  159 CYS A CB  
1456 C CB  B CYS A 159 ? 0.2125 0.2124 0.1379 0.0415  -0.0109 0.0360  159 CYS A CB  
1457 S SG  A CYS A 159 ? 0.1904 0.1824 0.1720 -0.0169 -0.0221 0.0465  159 CYS A SG  
1458 S SG  B CYS A 159 ? 0.2743 0.2813 0.1658 0.0658  0.0076  0.0231  159 CYS A SG  
1459 N N   . THR A 160 ? 0.1541 0.1731 0.1260 0.0047  0.0136  0.0189  160 THR A N   
1460 C CA  . THR A 160 ? 0.1776 0.1752 0.1442 0.0182  0.0270  0.0199  160 THR A CA  
1461 C C   . THR A 160 ? 0.2244 0.1769 0.1827 0.0115  0.0679  0.0361  160 THR A C   
1462 O O   . THR A 160 ? 0.2306 0.2466 0.3248 -0.0296 0.1052  0.0027  160 THR A O   
1463 C CB  . THR A 160 ? 0.1838 0.1894 0.1629 0.0208  0.0245  0.0348  160 THR A CB  
1464 O OG1 . THR A 160 ? 0.1761 0.1636 0.1797 0.0043  0.0425  0.0009  160 THR A OG1 
1465 C CG2 . THR A 160 ? 0.2088 0.1969 0.1782 0.0006  0.0287  0.0433  160 THR A CG2 
1466 N N   A THR A 161 ? 0.2016 0.2250 0.1493 0.0488  0.0469  0.0394  161 THR A N   
1467 N N   B THR A 161 ? 0.2833 0.2123 0.1599 -0.0103 0.0817  0.0501  161 THR A N   
1468 C CA  A THR A 161 ? 0.1874 0.2307 0.1692 0.0338  0.0411  0.0535  161 THR A CA  
1469 C CA  B THR A 161 ? 0.3682 0.2592 0.1880 0.0316  0.1205  0.0871  161 THR A CA  
1470 C C   A THR A 161 ? 0.1771 0.2791 0.1795 0.0463  0.0819  0.0230  161 THR A C   
1471 C C   B THR A 161 ? 0.3942 0.2737 0.2162 0.0581  0.1452  0.0966  161 THR A C   
1472 O O   A THR A 161 ? 0.1767 0.3244 0.1631 0.0337  0.0657  0.0496  161 THR A O   
1473 O O   B THR A 161 ? 0.4370 0.4035 0.2480 0.0395  0.1796  0.0972  161 THR A O   
1474 C CB  A THR A 161 ? 0.2297 0.2326 0.1333 0.0360  0.0553  0.0312  161 THR A CB  
1475 C CB  B THR A 161 ? 0.4502 0.2835 0.1994 0.0574  0.0770  0.0688  161 THR A CB  
1476 O OG1 A THR A 161 ? 0.3058 0.2251 0.1736 0.0297  0.0640  0.0508  161 THR A OG1 
1477 O OG1 B THR A 161 ? 0.5518 0.2949 0.1790 0.0820  0.0520  0.0990  161 THR A OG1 
1478 C CG2 A THR A 161 ? 0.2713 0.2468 0.1675 0.0586  0.0414  0.0546  161 THR A CG2 
1479 C CG2 B THR A 161 ? 0.4598 0.2804 0.1536 0.0833  0.0475  0.0766  161 THR A CG2 
1480 N N   A GLY A 162 ? 0.1915 0.2872 0.2077 0.0598  0.0880  0.0370  162 GLY A N   
1481 N N   B GLY A 162 ? 0.4370 0.3042 0.2543 0.0443  0.1334  0.1383  162 GLY A N   
1482 C CA  A GLY A 162 ? 0.2390 0.3134 0.2670 0.0869  0.0945  0.0868  162 GLY A CA  
1483 C CA  B GLY A 162 ? 0.4097 0.3711 0.2270 0.0470  0.1473  0.1223  162 GLY A CA  
1484 C C   A GLY A 162 ? 0.3450 0.3077 0.2322 0.0422  0.1858  0.1106  162 GLY A C   
1485 C C   B GLY A 162 ? 0.4255 0.3855 0.2121 0.0285  0.1324  0.1089  162 GLY A C   
1486 O O   A GLY A 162 ? 0.3933 0.3015 0.3120 0.1106  0.1585  0.1448  162 GLY A O   
1487 O O   B GLY A 162 ? 0.4709 0.4586 0.2164 0.1314  0.0850  0.0902  162 GLY A O   
1488 N N   . LYS A 163 ? 0.3794 0.4282 0.2689 0.0295  0.1966  0.0671  163 LYS A N   
1489 C CA  . LYS A 163 ? 0.4579 0.4325 0.2220 -0.0334 0.2021  0.0717  163 LYS A CA  
1490 C C   . LYS A 163 ? 0.3692 0.3223 0.2505 0.0073  0.1262  0.0280  163 LYS A C   
1491 O O   . LYS A 163 ? 0.4743 0.3381 0.3122 0.0333  0.1044  -0.0220 163 LYS A O   
1492 C CB  . LYS A 163 ? 0.5746 0.4865 0.2331 -0.0269 0.1528  0.0846  163 LYS A CB  
1493 C CG  . LYS A 163 ? 0.5659 0.4858 0.2866 -0.0390 0.1527  0.0900  163 LYS A CG  
1494 C CD  . LYS A 163 ? 0.5905 0.5731 0.3812 -0.0181 0.1026  0.0605  163 LYS A CD  
1495 C CE  . LYS A 163 ? 0.5779 0.5809 0.4405 -0.0414 0.0988  0.0554  163 LYS A CE  
1496 N NZ  . LYS A 163 ? 0.5585 0.6217 0.4586 -0.0292 0.1142  0.0447  163 LYS A NZ  
1497 N N   . CYS A 164 ? 0.3179 0.1780 0.2285 -0.0096 0.1086  0.0659  164 CYS A N   
1498 C CA  . CYS A 164 ? 0.2368 0.1645 0.1267 0.0060  0.0588  0.0347  164 CYS A CA  
1499 C C   . CYS A 164 ? 0.2032 0.1620 0.1315 0.0010  0.0699  0.0196  164 CYS A C   
1500 O O   . CYS A 164 ? 0.2154 0.1946 0.3279 0.0017  0.1047  0.0479  164 CYS A O   
1501 C CB  . CYS A 164 ? 0.1949 0.1471 0.1498 0.0010  0.0343  0.0089  164 CYS A CB  
1502 S SG  . CYS A 164 ? 0.2298 0.2373 0.1707 0.0253  0.0184  0.0125  164 CYS A SG  
1503 N N   . GLY A 165 ? 0.1597 0.1543 0.1017 0.0096  0.0267  0.0139  165 GLY A N   
1504 C CA  . GLY A 165 ? 0.1648 0.1467 0.0856 0.0087  0.0288  0.0113  165 GLY A CA  
1505 C C   . GLY A 165 ? 0.1369 0.1281 0.0624 0.0007  0.0083  -0.0112 165 GLY A C   
1506 O O   . GLY A 165 ? 0.1482 0.1331 0.0758 0.0082  0.0204  -0.0062 165 GLY A O   
1507 N N   . PRO A 166 ? 0.1314 0.1291 0.0423 0.0004  0.0044  -0.0067 166 PRO A N   
1508 C CA  . PRO A 166 ? 0.1268 0.1385 0.0310 -0.0017 -0.0056 -0.0080 166 PRO A CA  
1509 C C   . PRO A 166 ? 0.1278 0.1206 0.0275 -0.0026 -0.0083 -0.0053 166 PRO A C   
1510 O O   . PRO A 166 ? 0.1363 0.1442 0.0264 -0.0031 -0.0099 -0.0047 166 PRO A O   
1511 C CB  . PRO A 166 ? 0.1334 0.1499 0.0770 0.0073  -0.0063 0.0119  166 PRO A CB  
1512 C CG  . PRO A 166 ? 0.1931 0.1538 0.1123 0.0202  0.0333  0.0028  166 PRO A CG  
1513 C CD  . PRO A 166 ? 0.1480 0.1383 0.0640 0.0096  0.0087  -0.0134 166 PRO A CD  
1514 N N   . THR A 167 ? 0.1174 0.1305 0.0273 -0.0047 -0.0132 -0.0029 167 THR A N   
1515 C CA  . THR A 167 ? 0.1166 0.1318 0.0272 -0.0078 -0.0130 0.0005  167 THR A CA  
1516 C C   . THR A 167 ? 0.1221 0.1252 0.0287 -0.0116 -0.0172 -0.0039 167 THR A C   
1517 O O   . THR A 167 ? 0.1217 0.1247 0.0299 -0.0074 -0.0210 0.0020  167 THR A O   
1518 C CB  . THR A 167 ? 0.1168 0.1317 0.0268 -0.0074 -0.0102 0.0011  167 THR A CB  
1519 O OG1 . THR A 167 ? 0.1398 0.1320 0.0271 -0.0060 -0.0142 -0.0003 167 THR A OG1 
1520 C CG2 . THR A 167 ? 0.1188 0.1328 0.0375 -0.0057 -0.0081 0.0061  167 THR A CG2 
1521 N N   . GLU A 168 ? 0.1239 0.1233 0.0292 -0.0109 -0.0193 -0.0010 168 GLU A N   
1522 C CA  . GLU A 168 ? 0.1269 0.1251 0.0396 -0.0163 -0.0199 0.0035  168 GLU A CA  
1523 C C   . GLU A 168 ? 0.1210 0.1211 0.0351 -0.0117 -0.0127 0.0032  168 GLU A C   
1524 O O   . GLU A 168 ? 0.1532 0.1202 0.0419 -0.0210 -0.0185 0.0083  168 GLU A O   
1525 C CB  . GLU A 168 ? 0.1405 0.1622 0.0823 -0.0437 -0.0386 0.0196  168 GLU A CB  
1526 C CG  . GLU A 168 ? 0.2148 0.2185 0.1041 -0.0544 -0.0362 0.0665  168 GLU A CG  
1527 C CD  . GLU A 168 ? 0.2719 0.2653 0.2704 -0.0719 -0.0922 0.0799  168 GLU A CD  
1528 O OE1 . GLU A 168 ? 0.3921 0.3221 0.3224 -0.0553 -0.0364 0.1361  168 GLU A OE1 
1529 O OE2 . GLU A 168 ? 0.4371 0.5074 0.2460 -0.0250 -0.0398 0.1309  168 GLU A OE2 
1530 N N   . TYR A 169 ? 0.1162 0.1221 0.0265 -0.0085 -0.0099 0.0039  169 TYR A N   
1531 C CA  . TYR A 169 ? 0.1178 0.1229 0.0269 -0.0070 -0.0079 -0.0017 169 TYR A CA  
1532 C C   . TYR A 169 ? 0.1186 0.1191 0.0264 -0.0066 -0.0082 -0.0054 169 TYR A C   
1533 O O   . TYR A 169 ? 0.1254 0.1283 0.0260 -0.0049 -0.0086 0.0009  169 TYR A O   
1534 C CB  . TYR A 169 ? 0.1203 0.1283 0.0282 -0.0009 -0.0078 -0.0058 169 TYR A CB  
1535 C CG  . TYR A 169 ? 0.1181 0.1350 0.0261 -0.0002 -0.0034 -0.0084 169 TYR A CG  
1536 C CD1 . TYR A 169 ? 0.1230 0.1535 0.0332 -0.0053 -0.0051 0.0049  169 TYR A CD1 
1537 C CD2 . TYR A 169 ? 0.1194 0.1338 0.0274 -0.0032 -0.0065 -0.0080 169 TYR A CD2 
1538 C CE1 . TYR A 169 ? 0.1260 0.1614 0.0360 -0.0018 0.0075  0.0020  169 TYR A CE1 
1539 C CE2 . TYR A 169 ? 0.1231 0.1449 0.0281 0.0027  -0.0049 -0.0037 169 TYR A CE2 
1540 C CZ  . TYR A 169 ? 0.1185 0.1549 0.0330 -0.0027 -0.0014 -0.0089 169 TYR A CZ  
1541 O OH  . TYR A 169 ? 0.1208 0.1740 0.0507 0.0000  0.0015  0.0069  169 TYR A OH  
1542 N N   . SER A 170 ? 0.1134 0.1177 0.0269 -0.0063 -0.0118 0.0015  170 SER A N   
1543 C CA  . SER A 170 ? 0.1103 0.1204 0.0286 -0.0109 -0.0160 -0.0031 170 SER A CA  
1544 C C   . SER A 170 ? 0.1051 0.1192 0.0271 -0.0101 -0.0121 0.0009  170 SER A C   
1545 O O   . SER A 170 ? 0.1132 0.1222 0.0350 -0.0126 -0.0211 0.0056  170 SER A O   
1546 C CB  . SER A 170 ? 0.1130 0.1165 0.0334 -0.0117 -0.0137 0.0009  170 SER A CB  
1547 O OG  . SER A 170 ? 0.1143 0.1365 0.0268 -0.0134 -0.0115 -0.0001 170 SER A OG  
1548 N N   . ARG A 171 ? 0.1093 0.1180 0.0279 -0.0072 -0.0145 -0.0023 171 ARG A N   
1549 C CA  A ARG A 171 ? 0.1118 0.1195 0.0325 -0.0071 -0.0137 -0.0033 171 ARG A CA  
1550 C CA  B ARG A 171 ? 0.1167 0.1185 0.0317 -0.0079 -0.0103 -0.0077 171 ARG A CA  
1551 C C   . ARG A 171 ? 0.1077 0.1112 0.0355 -0.0121 -0.0137 -0.0073 171 ARG A C   
1552 O O   . ARG A 171 ? 0.1266 0.1187 0.0365 -0.0002 -0.0103 -0.0013 171 ARG A O   
1553 C CB  A ARG A 171 ? 0.1141 0.1217 0.0344 -0.0019 -0.0171 -0.0072 171 ARG A CB  
1554 C CB  B ARG A 171 ? 0.1125 0.1280 0.0360 -0.0115 -0.0140 -0.0102 171 ARG A CB  
1555 C CG  A ARG A 171 ? 0.1238 0.1348 0.0416 0.0053  -0.0089 -0.0052 171 ARG A CG  
1556 C CG  B ARG A 171 ? 0.1212 0.1437 0.0296 -0.0012 -0.0134 -0.0168 171 ARG A CG  
1557 C CD  A ARG A 171 ? 0.1372 0.1505 0.0499 0.0035  -0.0242 -0.0063 171 ARG A CD  
1558 C CD  B ARG A 171 ? 0.1295 0.1439 0.0393 -0.0035 -0.0147 -0.0204 171 ARG A CD  
1559 N NE  A ARG A 171 ? 0.1830 0.1553 0.0427 0.0221  -0.0183 -0.0163 171 ARG A NE  
1560 N NE  B ARG A 171 ? 0.1298 0.1288 0.0484 0.0040  -0.0174 -0.0068 171 ARG A NE  
1561 C CZ  A ARG A 171 ? 0.1826 0.1403 0.0365 0.0019  -0.0168 -0.0157 171 ARG A CZ  
1562 C CZ  B ARG A 171 ? 0.1452 0.1226 0.0389 0.0025  -0.0129 -0.0114 171 ARG A CZ  
1563 N NH1 A ARG A 171 ? 0.1891 0.1602 0.0383 0.0170  -0.0242 0.0036  171 ARG A NH1 
1564 N NH1 B ARG A 171 ? 0.1570 0.1558 0.0562 -0.0086 -0.0116 0.0013  171 ARG A NH1 
1565 N NH2 A ARG A 171 ? 0.1967 0.1529 0.0455 0.0083  -0.0039 -0.0033 171 ARG A NH2 
1566 N NH2 B ARG A 171 ? 0.1453 0.1399 0.0431 -0.0051 -0.0105 0.0043  171 ARG A NH2 
1567 N N   . PHE A 172 ? 0.1101 0.1199 0.0319 -0.0094 -0.0121 0.0027  172 PHE A N   
1568 C CA  . PHE A 172 ? 0.1139 0.1170 0.0313 -0.0146 -0.0082 -0.0009 172 PHE A CA  
1569 C C   . PHE A 172 ? 0.1065 0.1109 0.0311 -0.0120 -0.0038 -0.0011 172 PHE A C   
1570 O O   . PHE A 172 ? 0.1165 0.1118 0.0391 -0.0071 -0.0106 -0.0004 172 PHE A O   
1571 C CB  . PHE A 172 ? 0.1093 0.1308 0.0418 -0.0160 -0.0095 0.0039  172 PHE A CB  
1572 C CG  . PHE A 172 ? 0.1065 0.1283 0.0460 -0.0143 -0.0088 -0.0020 172 PHE A CG  
1573 C CD1 . PHE A 172 ? 0.1240 0.1276 0.0476 -0.0181 0.0051  -0.0044 172 PHE A CD1 
1574 C CD2 . PHE A 172 ? 0.1203 0.1279 0.0620 -0.0138 0.0002  -0.0043 172 PHE A CD2 
1575 C CE1 . PHE A 172 ? 0.1351 0.1530 0.0478 -0.0016 0.0029  0.0086  172 PHE A CE1 
1576 C CE2 . PHE A 172 ? 0.1341 0.1504 0.0644 -0.0080 -0.0122 -0.0265 172 PHE A CE2 
1577 C CZ  . PHE A 172 ? 0.1378 0.1721 0.0401 0.0008  -0.0045 -0.0135 172 PHE A CZ  
1578 N N   . PHE A 173 ? 0.1065 0.1071 0.0349 -0.0071 -0.0111 0.0010  173 PHE A N   
1579 C CA  . PHE A 173 ? 0.1120 0.1100 0.0310 -0.0067 -0.0091 -0.0056 173 PHE A CA  
1580 C C   . PHE A 173 ? 0.1094 0.1019 0.0352 -0.0115 -0.0127 -0.0007 173 PHE A C   
1581 O O   . PHE A 173 ? 0.1209 0.1150 0.0414 0.0004  -0.0186 -0.0059 173 PHE A O   
1582 C CB  . PHE A 173 ? 0.1131 0.1080 0.0438 -0.0088 -0.0113 -0.0059 173 PHE A CB  
1583 C CG  . PHE A 173 ? 0.1088 0.1029 0.0391 -0.0082 -0.0110 -0.0027 173 PHE A CG  
1584 C CD1 . PHE A 173 ? 0.1218 0.1132 0.0381 -0.0005 -0.0207 -0.0003 173 PHE A CD1 
1585 C CD2 . PHE A 173 ? 0.1250 0.1257 0.0416 0.0021  -0.0196 -0.0054 173 PHE A CD2 
1586 C CE1 . PHE A 173 ? 0.1466 0.1309 0.0378 0.0011  0.0001  -0.0067 173 PHE A CE1 
1587 C CE2 . PHE A 173 ? 0.1261 0.1327 0.0644 0.0117  -0.0176 0.0038  173 PHE A CE2 
1588 C CZ  . PHE A 173 ? 0.1323 0.1254 0.0674 0.0134  0.0085  -0.0009 173 PHE A CZ  
1589 N N   . LYS A 174 ? 0.1086 0.1028 0.0356 -0.0059 -0.0142 -0.0023 174 LYS A N   
1590 C CA  . LYS A 174 ? 0.1113 0.1107 0.0427 -0.0070 -0.0163 -0.0072 174 LYS A CA  
1591 C C   . LYS A 174 ? 0.1144 0.1070 0.0438 -0.0028 -0.0098 -0.0110 174 LYS A C   
1592 O O   . LYS A 174 ? 0.1196 0.1161 0.0773 0.0019  -0.0159 0.0000  174 LYS A O   
1593 C CB  . LYS A 174 ? 0.1189 0.1202 0.0441 -0.0076 -0.0091 -0.0088 174 LYS A CB  
1594 C CG  . LYS A 174 ? 0.1290 0.1537 0.0522 0.0028  -0.0052 -0.0068 174 LYS A CG  
1595 C CD  . LYS A 174 ? 0.1383 0.1647 0.0705 0.0016  -0.0056 -0.0126 174 LYS A CD  
1596 C CE  . LYS A 174 ? 0.1339 0.1730 0.0912 -0.0130 -0.0054 -0.0178 174 LYS A CE  
1597 N NZ  . LYS A 174 ? 0.1437 0.1773 0.0881 -0.0203 -0.0095 -0.0164 174 LYS A NZ  
1598 N N   . ARG A 175 ? 0.1176 0.1033 0.0469 -0.0049 -0.0163 -0.0032 175 ARG A N   
1599 C CA  . ARG A 175 ? 0.1288 0.1007 0.0551 -0.0033 -0.0139 -0.0039 175 ARG A CA  
1600 C C   . ARG A 175 ? 0.1237 0.1039 0.0596 -0.0055 -0.0144 -0.0007 175 ARG A C   
1601 O O   . ARG A 175 ? 0.1536 0.1221 0.0778 0.0060  -0.0218 0.0072  175 ARG A O   
1602 C CB  . ARG A 175 ? 0.1328 0.1116 0.0534 -0.0118 -0.0169 -0.0065 175 ARG A CB  
1603 C CG  . ARG A 175 ? 0.1525 0.1169 0.0772 -0.0145 -0.0158 0.0009  175 ARG A CG  
1604 C CD  . ARG A 175 ? 0.1600 0.1167 0.0829 -0.0260 -0.0155 0.0000  175 ARG A CD  
1605 N NE  . ARG A 175 ? 0.1642 0.1307 0.0905 -0.0351 -0.0181 -0.0006 175 ARG A NE  
1606 C CZ  . ARG A 175 ? 0.1621 0.1327 0.0907 -0.0340 -0.0208 -0.0087 175 ARG A CZ  
1607 N NH1 . ARG A 175 ? 0.1808 0.1554 0.0867 -0.0333 -0.0114 0.0095  175 ARG A NH1 
1608 N NH2 . ARG A 175 ? 0.1768 0.1634 0.1035 -0.0274 -0.0153 -0.0074 175 ARG A NH2 
1609 N N   . LEU A 176 ? 0.1349 0.1076 0.0424 -0.0070 -0.0111 0.0004  176 LEU A N   
1610 C CA  . LEU A 176 ? 0.1460 0.1294 0.0426 -0.0231 -0.0117 0.0009  176 LEU A CA  
1611 C C   . LEU A 176 ? 0.1409 0.1182 0.0464 -0.0094 -0.0150 0.0026  176 LEU A C   
1612 O O   . LEU A 176 ? 0.1555 0.1615 0.0560 -0.0061 -0.0217 0.0178  176 LEU A O   
1613 C CB  . LEU A 176 ? 0.1310 0.1948 0.0493 -0.0288 -0.0035 -0.0270 176 LEU A CB  
1614 C CG  . LEU A 176 ? 0.1955 0.2927 0.0844 -0.0962 0.0020  -0.0140 176 LEU A CG  
1615 C CD1 . LEU A 176 ? 0.1889 0.1994 0.0813 -0.0718 0.0132  -0.0379 176 LEU A CD1 
1616 C CD2 . LEU A 176 ? 0.2349 0.2817 0.0943 -0.1106 0.0207  0.0076  176 LEU A CD2 
1617 N N   . CYS A 177 ? 0.1219 0.1214 0.0566 -0.0057 -0.0190 0.0116  177 CYS A N   
1618 C CA  . CYS A 177 ? 0.1242 0.1310 0.0606 -0.0091 -0.0211 0.0032  177 CYS A CA  
1619 C C   . CYS A 177 ? 0.1198 0.1208 0.0681 -0.0041 -0.0181 0.0047  177 CYS A C   
1620 O O   . CYS A 177 ? 0.1322 0.1293 0.0797 0.0011  -0.0065 0.0093  177 CYS A O   
1621 C CB  . CYS A 177 ? 0.1470 0.1331 0.0916 -0.0249 -0.0363 -0.0097 177 CYS A CB  
1622 S SG  . CYS A 177 ? 0.1871 0.1714 0.0804 0.0000  -0.0261 -0.0115 177 CYS A SG  
1623 N N   . PRO A 178 ? 0.1227 0.1208 0.0787 -0.0085 -0.0151 -0.0059 178 PRO A N   
1624 C CA  . PRO A 178 ? 0.1334 0.1342 0.0833 -0.0079 -0.0084 -0.0208 178 PRO A CA  
1625 C C   . PRO A 178 ? 0.1139 0.1318 0.0811 0.0035  -0.0049 -0.0142 178 PRO A C   
1626 O O   . PRO A 178 ? 0.1339 0.1610 0.0823 -0.0133 -0.0027 -0.0112 178 PRO A O   
1627 C CB  . PRO A 178 ? 0.1580 0.1410 0.1439 -0.0011 -0.0019 -0.0329 178 PRO A CB  
1628 C CG  . PRO A 178 ? 0.1994 0.1519 0.1782 0.0068  0.0188  -0.0184 178 PRO A CG  
1629 C CD  . PRO A 178 ? 0.1381 0.1254 0.1119 -0.0068 -0.0180 0.0006  178 PRO A CD  
1630 N N   . ASP A 179 ? 0.1166 0.1252 0.0852 0.0005  -0.0172 -0.0104 179 ASP A N   
1631 C CA  A ASP A 179 ? 0.1154 0.1357 0.0990 -0.0027 -0.0121 -0.0072 179 ASP A CA  
1632 C CA  B ASP A 179 ? 0.1169 0.1356 0.1046 0.0003  -0.0349 -0.0044 179 ASP A CA  
1633 C C   . ASP A 179 ? 0.1224 0.1293 0.0972 -0.0142 -0.0220 -0.0105 179 ASP A C   
1634 O O   . ASP A 179 ? 0.1522 0.1408 0.2211 -0.0156 -0.0753 -0.0103 179 ASP A O   
1635 C CB  A ASP A 179 ? 0.1470 0.1615 0.1216 -0.0029 -0.0371 -0.0043 179 ASP A CB  
1636 C CB  B ASP A 179 ? 0.1316 0.1407 0.1224 -0.0012 -0.0536 -0.0085 179 ASP A CB  
1637 C CG  A ASP A 179 ? 0.1481 0.1595 0.1146 0.0044  -0.0408 -0.0292 179 ASP A CG  
1638 C CG  B ASP A 179 ? 0.1931 0.1708 0.1680 0.0321  -0.0438 -0.0284 179 ASP A CG  
1639 O OD1 A ASP A 179 ? 0.1315 0.2097 0.1357 0.0272  -0.0297 -0.0427 179 ASP A OD1 
1640 O OD1 B ASP A 179 ? 0.2638 0.2401 0.1769 0.0453  -0.0397 -0.0450 179 ASP A OD1 
1641 O OD2 A ASP A 179 ? 0.1723 0.1856 0.1201 0.0024  -0.0528 -0.0257 179 ASP A OD2 
1642 O OD2 B ASP A 179 ? 0.2844 0.2322 0.1652 0.0746  -0.0592 -0.0279 179 ASP A OD2 
1643 N N   . ALA A 180 ? 0.1254 0.1192 0.0610 -0.0093 -0.0254 -0.0043 180 ALA A N   
1644 C CA  . ALA A 180 ? 0.1260 0.1222 0.0500 -0.0103 -0.0214 -0.0095 180 ALA A CA  
1645 C C   . ALA A 180 ? 0.1111 0.1204 0.0446 -0.0111 -0.0143 -0.0133 180 ALA A C   
1646 O O   . ALA A 180 ? 0.1352 0.1219 0.0488 -0.0152 -0.0221 -0.0141 180 ALA A O   
1647 C CB  . ALA A 180 ? 0.1459 0.1263 0.0444 -0.0084 -0.0156 -0.0090 180 ALA A CB  
1648 N N   . PHE A 181 ? 0.1029 0.1212 0.0337 -0.0112 -0.0143 -0.0105 181 PHE A N   
1649 C CA  . PHE A 181 ? 0.1077 0.1227 0.0314 -0.0084 -0.0115 -0.0067 181 PHE A CA  
1650 C C   . PHE A 181 ? 0.1064 0.1198 0.0268 -0.0094 -0.0087 -0.0063 181 PHE A C   
1651 O O   . PHE A 181 ? 0.1039 0.1326 0.0365 -0.0117 -0.0065 -0.0195 181 PHE A O   
1652 C CB  . PHE A 181 ? 0.1137 0.1254 0.0379 -0.0107 -0.0072 -0.0040 181 PHE A CB  
1653 C CG  . PHE A 181 ? 0.1167 0.1420 0.0432 -0.0237 -0.0078 -0.0049 181 PHE A CG  
1654 C CD1 . PHE A 181 ? 0.1217 0.1786 0.0408 -0.0283 -0.0101 -0.0007 181 PHE A CD1 
1655 C CD2 . PHE A 181 ? 0.1303 0.1831 0.0423 -0.0241 -0.0111 0.0004  181 PHE A CD2 
1656 C CE1 . PHE A 181 ? 0.1194 0.2271 0.0507 -0.0331 -0.0161 -0.0039 181 PHE A CE1 
1657 C CE2 . PHE A 181 ? 0.1430 0.2214 0.0454 -0.0308 0.0019  -0.0006 181 PHE A CE2 
1658 C CZ  . PHE A 181 ? 0.1313 0.2315 0.0580 -0.0404 0.0066  -0.0085 181 PHE A CZ  
1659 N N   . SER A 182 ? 0.1068 0.1338 0.0274 -0.0090 -0.0049 -0.0135 182 SER A N   
1660 C CA  . SER A 182 ? 0.1024 0.1378 0.0275 -0.0114 -0.0054 -0.0132 182 SER A CA  
1661 C C   . SER A 182 ? 0.1117 0.1372 0.0280 -0.0103 -0.0077 -0.0140 182 SER A C   
1662 O O   . SER A 182 ? 0.1124 0.1562 0.0384 -0.0032 -0.0079 -0.0074 182 SER A O   
1663 C CB  . SER A 182 ? 0.1149 0.1340 0.0281 -0.0191 -0.0100 -0.0031 182 SER A CB  
1664 O OG  . SER A 182 ? 0.1333 0.1353 0.0317 -0.0142 -0.0133 -0.0147 182 SER A OG  
1665 N N   . TYR A 183 ? 0.1099 0.1478 0.0462 -0.0104 -0.0092 0.0054  183 TYR A N   
1666 C CA  . TYR A 183 ? 0.1306 0.1673 0.0570 -0.0154 -0.0170 0.0241  183 TYR A CA  
1667 C C   . TYR A 183 ? 0.1321 0.1776 0.0726 -0.0138 -0.0155 0.0258  183 TYR A C   
1668 O O   . TYR A 183 ? 0.1274 0.1680 0.0628 -0.0230 -0.0117 0.0178  183 TYR A O   
1669 C CB  . TYR A 183 ? 0.1257 0.2114 0.0559 -0.0210 -0.0173 0.0294  183 TYR A CB  
1670 C CG  . TYR A 183 ? 0.1202 0.2158 0.0529 -0.0296 -0.0191 0.0223  183 TYR A CG  
1671 C CD1 . TYR A 183 ? 0.1256 0.2154 0.0512 -0.0309 -0.0225 -0.0019 183 TYR A CD1 
1672 C CD2 . TYR A 183 ? 0.1566 0.2375 0.0526 -0.0304 -0.0147 0.0249  183 TYR A CD2 
1673 C CE1 . TYR A 183 ? 0.1465 0.2127 0.0744 -0.0360 -0.0230 -0.0171 183 TYR A CE1 
1674 C CE2 . TYR A 183 ? 0.1697 0.2633 0.0598 -0.0476 -0.0006 0.0069  183 TYR A CE2 
1675 C CZ  . TYR A 183 ? 0.1605 0.2530 0.0643 -0.0412 -0.0041 -0.0301 183 TYR A CZ  
1676 O OH  . TYR A 183 ? 0.1985 0.3170 0.0974 -0.0542 0.0201  -0.0631 183 TYR A OH  
1677 N N   . VAL A 184 ? 0.1402 0.2123 0.1246 -0.0153 -0.0082 0.0760  184 VAL A N   
1678 C CA  . VAL A 184 ? 0.1683 0.1977 0.1368 -0.0289 -0.0056 0.0729  184 VAL A CA  
1679 C C   . VAL A 184 ? 0.1471 0.2148 0.1286 -0.0364 -0.0124 0.0710  184 VAL A C   
1680 O O   . VAL A 184 ? 0.1538 0.2264 0.1389 -0.0452 -0.0077 0.0438  184 VAL A O   
1681 C CB  . VAL A 184 ? 0.1979 0.2283 0.1675 -0.0032 0.0127  0.0972  184 VAL A CB  
1682 C CG1 . VAL A 184 ? 0.2416 0.2348 0.1939 -0.0310 0.0241  0.1012  184 VAL A CG1 
1683 C CG2 . VAL A 184 ? 0.2335 0.2314 0.2097 0.0169  0.0393  0.1035  184 VAL A CG2 
1684 N N   . LEU A 185 ? 0.1463 0.2750 0.0969 -0.0492 -0.0131 0.0652  185 LEU A N   
1685 C CA  . LEU A 185 ? 0.1597 0.2978 0.0875 -0.0589 0.0037  0.0496  185 LEU A CA  
1686 C C   . LEU A 185 ? 0.1576 0.2845 0.0584 -0.0487 -0.0044 0.0198  185 LEU A C   
1687 O O   . LEU A 185 ? 0.2134 0.3276 0.0567 -0.0437 0.0150  0.0054  185 LEU A O   
1688 C CB  . LEU A 185 ? 0.2107 0.3632 0.0810 -0.0318 0.0068  0.0753  185 LEU A CB  
1689 C CG  . LEU A 185 ? 0.2415 0.3925 0.1403 -0.0206 0.0165  0.1211  185 LEU A CG  
1690 C CD1 . LEU A 185 ? 0.2743 0.4599 0.1296 0.0062  0.0194  0.1366  185 LEU A CD1 
1691 C CD2 . LEU A 185 ? 0.2884 0.3675 0.1974 -0.0654 -0.0039 0.1157  185 LEU A CD2 
1692 N N   . ASP A 186 ? 0.1510 0.2426 0.0514 -0.0298 -0.0005 0.0035  186 ASP A N   
1693 C CA  . ASP A 186 ? 0.1371 0.2226 0.0541 -0.0227 -0.0023 -0.0098 186 ASP A CA  
1694 C C   . ASP A 186 ? 0.1412 0.2443 0.0481 -0.0231 -0.0014 -0.0182 186 ASP A C   
1695 O O   . ASP A 186 ? 0.1421 0.2677 0.1196 -0.0317 -0.0003 -0.0066 186 ASP A O   
1696 C CB  . ASP A 186 ? 0.1333 0.1890 0.0507 -0.0150 0.0003  -0.0268 186 ASP A CB  
1697 C CG  . ASP A 186 ? 0.1351 0.1845 0.0491 -0.0140 -0.0006 -0.0301 186 ASP A CG  
1698 O OD1 . ASP A 186 ? 0.1790 0.1959 0.0711 -0.0192 0.0198  -0.0447 186 ASP A OD1 
1699 O OD2 . ASP A 186 ? 0.1402 0.1704 0.0563 -0.0113 0.0068  -0.0241 186 ASP A OD2 
1700 N N   . LYS A 187 ? 0.1565 0.2580 0.0604 0.0016  -0.0093 -0.0434 187 LYS A N   
1701 C CA  . LYS A 187 ? 0.1596 0.2959 0.0681 0.0095  -0.0016 -0.0406 187 LYS A CA  
1702 C C   . LYS A 187 ? 0.1531 0.2755 0.0667 0.0008  -0.0004 -0.0342 187 LYS A C   
1703 O O   . LYS A 187 ? 0.1705 0.2391 0.0681 -0.0091 -0.0064 -0.0316 187 LYS A O   
1704 C CB  . LYS A 187 ? 0.2274 0.3082 0.1053 0.0390  -0.0184 -0.0853 187 LYS A CB  
1705 C CG  . LYS A 187 ? 0.2589 0.3613 0.1784 0.0859  -0.0221 -0.0916 187 LYS A CG  
1706 C CD  . LYS A 187 ? 0.3673 0.3718 0.2511 0.1025  -0.0139 -0.1011 187 LYS A CD  
1707 C CE  . LYS A 187 ? 0.3909 0.4332 0.3919 0.1282  -0.0273 -0.0823 187 LYS A CE  
1708 N NZ  . LYS A 187 ? 0.5157 0.4548 0.4366 0.1030  -0.0205 -0.1123 187 LYS A NZ  
1709 N N   . PRO A 188 ? 0.1517 0.3062 0.0650 -0.0082 0.0012  -0.0273 188 PRO A N   
1710 C CA  . PRO A 188 ? 0.1512 0.2597 0.0817 -0.0151 -0.0099 -0.0211 188 PRO A CA  
1711 C C   . PRO A 188 ? 0.1454 0.2304 0.0857 -0.0113 -0.0133 -0.0315 188 PRO A C   
1712 O O   . PRO A 188 ? 0.1799 0.2616 0.1080 0.0137  -0.0125 -0.0466 188 PRO A O   
1713 C CB  . PRO A 188 ? 0.1928 0.2930 0.1229 -0.0439 0.0116  -0.0087 188 PRO A CB  
1714 C CG  . PRO A 188 ? 0.2431 0.3881 0.1434 -0.0745 0.0077  0.0189  188 PRO A CG  
1715 C CD  . PRO A 188 ? 0.1516 0.3957 0.0868 -0.0337 0.0014  -0.0124 188 PRO A CD  
1716 N N   . THR A 189 ? 0.1468 0.1893 0.0779 -0.0237 -0.0190 -0.0219 189 THR A N   
1717 C CA  . THR A 189 ? 0.1473 0.1746 0.0968 -0.0200 -0.0237 -0.0181 189 THR A CA  
1718 C C   . THR A 189 ? 0.1284 0.1696 0.0841 -0.0128 -0.0203 -0.0121 189 THR A C   
1719 O O   . THR A 189 ? 0.1713 0.2286 0.0853 -0.0562 -0.0309 -0.0034 189 THR A O   
1720 C CB  . THR A 189 ? 0.1426 0.1859 0.1097 -0.0220 -0.0296 -0.0109 189 THR A CB  
1721 O OG1 . THR A 189 ? 0.1503 0.1935 0.1092 -0.0155 -0.0147 -0.0134 189 THR A OG1 
1722 C CG2 . THR A 189 ? 0.1736 0.1820 0.1333 -0.0213 -0.0206 -0.0212 189 THR A CG2 
1723 N N   . THR A 190 ? 0.1387 0.1814 0.0692 -0.0262 -0.0153 -0.0208 190 THR A N   
1724 C CA  . THR A 190 ? 0.1242 0.1744 0.0694 -0.0190 -0.0083 -0.0213 190 THR A CA  
1725 C C   . THR A 190 ? 0.1300 0.1764 0.0668 -0.0060 -0.0039 -0.0313 190 THR A C   
1726 O O   . THR A 190 ? 0.1788 0.2484 0.0877 0.0341  -0.0219 -0.0732 190 THR A O   
1727 C CB  . THR A 190 ? 0.1427 0.1959 0.0791 -0.0283 -0.0208 -0.0041 190 THR A CB  
1728 O OG1 . THR A 190 ? 0.1620 0.2106 0.1554 -0.0195 -0.0490 0.0172  190 THR A OG1 
1729 C CG2 . THR A 190 ? 0.1493 0.1954 0.0950 -0.0342 -0.0195 0.0008  190 THR A CG2 
1730 N N   . VAL A 191 ? 0.1159 0.1671 0.0644 -0.0062 -0.0018 -0.0242 191 VAL A N   
1731 C CA  . VAL A 191 ? 0.1203 0.1546 0.0692 -0.0032 -0.0034 -0.0233 191 VAL A CA  
1732 C C   . VAL A 191 ? 0.1186 0.1643 0.0639 -0.0088 -0.0007 -0.0199 191 VAL A C   
1733 O O   . VAL A 191 ? 0.1263 0.1626 0.0878 -0.0140 0.0081  -0.0250 191 VAL A O   
1734 C CB  . VAL A 191 ? 0.1319 0.1788 0.0761 -0.0012 0.0022  -0.0124 191 VAL A CB  
1735 C CG1 . VAL A 191 ? 0.1415 0.2002 0.1000 0.0011  -0.0020 0.0120  191 VAL A CG1 
1736 C CG2 . VAL A 191 ? 0.1426 0.2005 0.1219 -0.0132 -0.0004 0.0067  191 VAL A CG2 
1737 N N   . THR A 192 ? 0.1213 0.1756 0.0757 -0.0067 0.0020  -0.0272 192 THR A N   
1738 C CA  . THR A 192 ? 0.1257 0.1932 0.0823 -0.0133 0.0031  -0.0258 192 THR A CA  
1739 C C   . THR A 192 ? 0.1125 0.1905 0.0888 -0.0012 0.0002  -0.0312 192 THR A C   
1740 O O   . THR A 192 ? 0.1486 0.1931 0.1070 0.0090  -0.0133 -0.0386 192 THR A O   
1741 C CB  . THR A 192 ? 0.1359 0.2392 0.0925 -0.0239 0.0126  -0.0292 192 THR A CB  
1742 O OG1 . THR A 192 ? 0.1745 0.2493 0.0857 -0.0398 0.0080  -0.0278 192 THR A OG1 
1743 C CG2 . THR A 192 ? 0.1567 0.2631 0.1016 -0.0434 0.0145  -0.0171 192 THR A CG2 
1744 N N   . CYS A 193 ? 0.1221 0.1836 0.0849 -0.0044 -0.0042 -0.0262 193 CYS A N   
1745 C CA  . CYS A 193 ? 0.1237 0.1852 0.0841 0.0004  -0.0041 -0.0231 193 CYS A CA  
1746 C C   . CYS A 193 ? 0.1207 0.1869 0.0951 0.0034  -0.0070 -0.0340 193 CYS A C   
1747 O O   . CYS A 193 ? 0.1217 0.2083 0.0900 -0.0142 -0.0032 -0.0217 193 CYS A O   
1748 C CB  . CYS A 193 ? 0.1306 0.1823 0.0982 -0.0037 0.0008  -0.0324 193 CYS A CB  
1749 S SG  . CYS A 193 ? 0.1549 0.2107 0.1315 -0.0164 0.0256  -0.0369 193 CYS A SG  
1750 N N   . PRO A 194 ? 0.1221 0.2043 0.0977 0.0042  -0.0046 -0.0249 194 PRO A N   
1751 C CA  . PRO A 194 ? 0.1255 0.2204 0.1115 -0.0098 -0.0086 -0.0223 194 PRO A CA  
1752 C C   . PRO A 194 ? 0.1233 0.2067 0.0802 -0.0202 -0.0031 -0.0185 194 PRO A C   
1753 O O   . PRO A 194 ? 0.1223 0.2100 0.0730 -0.0267 0.0034  -0.0242 194 PRO A O   
1754 C CB  . PRO A 194 ? 0.1360 0.2454 0.1371 0.0002  -0.0259 -0.0316 194 PRO A CB  
1755 C CG  . PRO A 194 ? 0.1467 0.2358 0.1356 0.0228  -0.0238 -0.0165 194 PRO A CG  
1756 C CD  . PRO A 194 ? 0.1412 0.1953 0.1330 0.0073  -0.0027 -0.0304 194 PRO A CD  
1757 N N   . GLY A 195 ? 0.1184 0.2426 0.0977 -0.0398 0.0146  -0.0090 195 GLY A N   
1758 C CA  . GLY A 195 ? 0.1364 0.2297 0.0781 -0.0587 0.0107  -0.0069 195 GLY A CA  
1759 C C   . GLY A 195 ? 0.1228 0.2320 0.0775 -0.0560 -0.0011 -0.0092 195 GLY A C   
1760 O O   . GLY A 195 ? 0.1284 0.2519 0.1083 -0.0344 -0.0049 -0.0182 195 GLY A O   
1761 N N   . SER A 196 ? 0.1223 0.2069 0.0670 -0.0574 -0.0023 -0.0039 196 SER A N   
1762 C CA  . SER A 196 ? 0.1326 0.2001 0.0614 -0.0513 -0.0067 0.0029  196 SER A CA  
1763 C C   . SER A 196 ? 0.1256 0.1881 0.0620 -0.0409 -0.0055 -0.0046 196 SER A C   
1764 O O   . SER A 196 ? 0.1414 0.1996 0.0711 -0.0433 -0.0217 0.0027  196 SER A O   
1765 C CB  . SER A 196 ? 0.1514 0.2115 0.0716 -0.0654 -0.0128 -0.0070 196 SER A CB  
1766 O OG  . SER A 196 ? 0.1791 0.2443 0.0781 -0.0972 -0.0160 0.0172  196 SER A OG  
1767 N N   . SER A 197 ? 0.1182 0.1775 0.0569 -0.0339 -0.0027 -0.0067 197 SER A N   
1768 C CA  . SER A 197 ? 0.1099 0.1711 0.0685 -0.0294 -0.0094 -0.0050 197 SER A CA  
1769 C C   . SER A 197 ? 0.1160 0.1567 0.0520 -0.0302 -0.0072 -0.0035 197 SER A C   
1770 O O   . SER A 197 ? 0.1379 0.1591 0.0576 -0.0266 0.0016  0.0022  197 SER A O   
1771 C CB  . SER A 197 ? 0.1167 0.1661 0.0670 -0.0182 -0.0013 -0.0141 197 SER A CB  
1772 O OG  . SER A 197 ? 0.1314 0.1817 0.0787 -0.0125 0.0016  -0.0144 197 SER A OG  
1773 N N   . ASN A 198 ? 0.1123 0.1499 0.0551 -0.0175 -0.0137 0.0038  198 ASN A N   
1774 C CA  . ASN A 198 ? 0.1110 0.1397 0.0538 -0.0143 -0.0109 0.0024  198 ASN A CA  
1775 C C   . ASN A 198 ? 0.1124 0.1307 0.0405 -0.0137 -0.0101 0.0028  198 ASN A C   
1776 O O   . ASN A 198 ? 0.1110 0.1362 0.0601 -0.0127 -0.0088 -0.0031 198 ASN A O   
1777 C CB  . ASN A 198 ? 0.1271 0.1524 0.0570 -0.0131 -0.0175 -0.0082 198 ASN A CB  
1778 C CG  . ASN A 198 ? 0.1207 0.1644 0.0705 -0.0169 -0.0173 -0.0154 198 ASN A CG  
1779 O OD1 . ASN A 198 ? 0.1350 0.1605 0.0846 -0.0342 -0.0035 -0.0081 198 ASN A OD1 
1780 N ND2 . ASN A 198 ? 0.1568 0.1971 0.1533 -0.0227 -0.0663 -0.0148 198 ASN A ND2 
1781 N N   . TYR A 199 ? 0.1114 0.1306 0.0352 -0.0132 -0.0116 -0.0010 199 TYR A N   
1782 C CA  . TYR A 199 ? 0.1086 0.1201 0.0398 -0.0121 -0.0113 0.0018  199 TYR A CA  
1783 C C   . TYR A 199 ? 0.1058 0.1130 0.0374 -0.0053 -0.0147 -0.0008 199 TYR A C   
1784 O O   . TYR A 199 ? 0.1183 0.1158 0.0424 -0.0168 -0.0076 -0.0042 199 TYR A O   
1785 C CB  . TYR A 199 ? 0.1070 0.1340 0.0432 -0.0089 -0.0095 0.0034  199 TYR A CB  
1786 C CG  . TYR A 199 ? 0.1071 0.1443 0.0386 -0.0125 -0.0154 0.0033  199 TYR A CG  
1787 C CD1 . TYR A 199 ? 0.1032 0.1476 0.0408 -0.0144 -0.0130 0.0052  199 TYR A CD1 
1788 C CD2 . TYR A 199 ? 0.1209 0.1443 0.0456 -0.0143 -0.0161 0.0064  199 TYR A CD2 
1789 C CE1 . TYR A 199 ? 0.1154 0.1576 0.0423 -0.0166 -0.0105 -0.0054 199 TYR A CE1 
1790 C CE2 . TYR A 199 ? 0.1290 0.1538 0.0534 -0.0272 -0.0121 0.0126  199 TYR A CE2 
1791 C CZ  . TYR A 199 ? 0.1080 0.1665 0.0432 -0.0198 -0.0073 0.0057  199 TYR A CZ  
1792 O OH  . TYR A 199 ? 0.1306 0.1938 0.0474 -0.0337 0.0021  0.0016  199 TYR A OH  
1793 N N   . ARG A 200 ? 0.1076 0.1173 0.0377 -0.0104 -0.0081 -0.0099 200 ARG A N   
1794 C CA  . ARG A 200 ? 0.1082 0.1169 0.0368 -0.0132 -0.0071 -0.0084 200 ARG A CA  
1795 C C   . ARG A 200 ? 0.1117 0.1104 0.0261 -0.0157 -0.0064 -0.0039 200 ARG A C   
1796 O O   . ARG A 200 ? 0.1109 0.1218 0.0456 -0.0043 -0.0083 -0.0196 200 ARG A O   
1797 C CB  . ARG A 200 ? 0.1358 0.1344 0.0497 -0.0221 -0.0239 0.0044  200 ARG A CB  
1798 C CG  . ARG A 200 ? 0.1671 0.1473 0.0414 -0.0400 -0.0120 0.0050  200 ARG A CG  
1799 C CD  . ARG A 200 ? 0.1971 0.1777 0.0750 -0.0446 -0.0307 0.0312  200 ARG A CD  
1800 N NE  . ARG A 200 ? 0.1980 0.1997 0.0918 -0.0464 -0.0318 0.0353  200 ARG A NE  
1801 C CZ  . ARG A 200 ? 0.1728 0.2509 0.1315 -0.0311 0.0154  -0.0092 200 ARG A CZ  
1802 N NH1 . ARG A 200 ? 0.1834 0.2310 0.1589 0.0045  0.0009  0.0079  200 ARG A NH1 
1803 N NH2 . ARG A 200 ? 0.1649 0.3112 0.1648 0.0023  -0.0309 -0.0264 200 ARG A NH2 
1804 N N   . VAL A 201 ? 0.1103 0.1076 0.0269 -0.0147 -0.0045 -0.0097 201 VAL A N   
1805 C CA  . VAL A 201 ? 0.1125 0.1093 0.0269 -0.0118 -0.0076 -0.0079 201 VAL A CA  
1806 C C   . VAL A 201 ? 0.1003 0.1086 0.0274 -0.0050 -0.0099 -0.0072 201 VAL A C   
1807 O O   . VAL A 201 ? 0.1284 0.1242 0.0279 -0.0191 0.0005  -0.0158 201 VAL A O   
1808 C CB  . VAL A 201 ? 0.1325 0.1104 0.0385 -0.0042 -0.0088 -0.0015 201 VAL A CB  
1809 C CG1 . VAL A 201 ? 0.1384 0.1283 0.0696 0.0089  -0.0272 0.0001  201 VAL A CG1 
1810 C CG2 . VAL A 201 ? 0.1649 0.1333 0.0505 -0.0066 -0.0068 0.0165  201 VAL A CG2 
1811 N N   . THR A 202 ? 0.1044 0.1123 0.0263 -0.0107 -0.0025 -0.0086 202 THR A N   
1812 C CA  . THR A 202 ? 0.1065 0.1081 0.0290 -0.0129 -0.0035 -0.0077 202 THR A CA  
1813 C C   . THR A 202 ? 0.1085 0.1084 0.0273 -0.0047 -0.0075 -0.0102 202 THR A C   
1814 O O   . THR A 202 ? 0.1067 0.1416 0.0420 -0.0101 -0.0047 -0.0313 202 THR A O   
1815 C CB  . THR A 202 ? 0.1139 0.1161 0.0477 -0.0108 -0.0104 -0.0029 202 THR A CB  
1816 O OG1 . THR A 202 ? 0.1140 0.1368 0.0578 -0.0050 -0.0117 0.0085  202 THR A OG1 
1817 C CG2 . THR A 202 ? 0.1255 0.1277 0.0654 -0.0076 -0.0012 0.0147  202 THR A CG2 
1818 N N   . PHE A 203 ? 0.1080 0.1065 0.0257 -0.0042 -0.0056 -0.0023 203 PHE A N   
1819 C CA  . PHE A 203 ? 0.1062 0.1113 0.0259 -0.0038 -0.0054 -0.0047 203 PHE A CA  
1820 C C   . PHE A 203 ? 0.1080 0.1084 0.0256 -0.0005 -0.0043 -0.0030 203 PHE A C   
1821 O O   . PHE A 203 ? 0.1248 0.1149 0.0259 -0.0070 -0.0067 0.0038  203 PHE A O   
1822 C CB  . PHE A 203 ? 0.1075 0.1175 0.0264 0.0007  -0.0095 -0.0006 203 PHE A CB  
1823 C CG  . PHE A 203 ? 0.1083 0.1157 0.0383 0.0120  -0.0040 0.0030  203 PHE A CG  
1824 C CD1 . PHE A 203 ? 0.1562 0.1255 0.0362 0.0274  0.0070  0.0074  203 PHE A CD1 
1825 C CD2 . PHE A 203 ? 0.1337 0.1229 0.0546 -0.0004 -0.0261 0.0077  203 PHE A CD2 
1826 C CE1 . PHE A 203 ? 0.1567 0.1444 0.0503 0.0341  0.0222  0.0252  203 PHE A CE1 
1827 C CE2 . PHE A 203 ? 0.1394 0.1210 0.0935 -0.0019 -0.0258 0.0127  203 PHE A CE2 
1828 C CZ  . PHE A 203 ? 0.1396 0.1286 0.1020 0.0060  0.0108  0.0239  203 PHE A CZ  
1829 N N   . CYS A 204 ? 0.1201 0.1122 0.0264 -0.0084 -0.0102 0.0006  204 CYS A N   
1830 C CA  . CYS A 204 ? 0.1266 0.1214 0.0340 -0.0160 -0.0072 0.0016  204 CYS A CA  
1831 C C   . CYS A 204 ? 0.1342 0.1105 0.0401 -0.0126 -0.0098 -0.0002 204 CYS A C   
1832 O O   . CYS A 204 ? 0.1536 0.1303 0.0413 -0.0113 -0.0085 0.0129  204 CYS A O   
1833 C CB  . CYS A 204 ? 0.1396 0.1357 0.0401 -0.0174 0.0002  -0.0002 204 CYS A CB  
1834 S SG  . CYS A 204 ? 0.1396 0.1893 0.0526 0.0002  -0.0016 0.0000  204 CYS A SG  
1835 N N   . PRO A 205 ? 0.1314 0.1125 0.0425 -0.0051 -0.0087 0.0041  205 PRO A N   
1836 C CA  . PRO A 205 ? 0.1384 0.1297 0.0665 -0.0015 -0.0176 0.0035  205 PRO A CA  
1837 C C   . PRO A 205 ? 0.1619 0.1313 0.0994 0.0028  -0.0152 0.0106  205 PRO A C   
1838 O O   . PRO A 205 ? 0.2121 0.1527 0.1301 0.0141  -0.0502 0.0188  205 PRO A O   
1839 C CB  . PRO A 205 ? 0.1406 0.1414 0.0711 -0.0023 -0.0111 -0.0049 205 PRO A CB  
1840 C CG  . PRO A 205 ? 0.1362 0.1274 0.0596 -0.0093 -0.0021 -0.0094 205 PRO A CG  
1841 C CD  . PRO A 205 ? 0.1267 0.1213 0.0381 -0.0079 -0.0072 0.0015  205 PRO A CD  
1842 N N   . THR A 206 ? 0.1823 0.1224 0.1120 -0.0111 -0.0261 0.0117  206 THR A N   
1843 C CA  . THR A 206 ? 0.2574 0.1409 0.1832 -0.0342 -0.0453 0.0328  206 THR A CA  
1844 C C   . THR A 206 ? 0.3378 0.1943 0.2984 -0.1080 0.0516  0.0466  206 THR A C   
1845 O O   . THR A 206 ? 0.3584 0.2896 0.2990 -0.0666 0.0426  0.0101  206 THR A O   
1846 C CB  . THR A 206 ? 0.3441 0.1521 0.2317 -0.0609 -0.0913 0.0293  206 THR A CB  
1847 O OG1 . THR A 206 ? 0.3843 0.2533 0.4512 -0.0054 -0.2109 -0.0311 206 THR A OG1 
1848 C CG2 . THR A 206 ? 0.5043 0.1905 0.1738 -0.0763 -0.0694 -0.0091 206 THR A CG2 
1849 O O1  . TLA B .   ? 0.1273 0.1619 0.0346 -0.0090 0.0005  -0.0124 301 TLA A O1  
1850 O O11 . TLA B .   ? 0.1286 0.1638 0.0336 -0.0202 0.0036  -0.0177 301 TLA A O11 
1851 C C1  . TLA B .   ? 0.1247 0.1542 0.0306 -0.0178 0.0013  -0.0259 301 TLA A C1  
1852 C C2  . TLA B .   ? 0.1374 0.1424 0.0341 -0.0097 0.0050  -0.0166 301 TLA A C2  
1853 O O2  . TLA B .   ? 0.1662 0.1352 0.0664 -0.0089 0.0050  -0.0240 301 TLA A O2  
1854 C C3  . TLA B .   ? 0.1347 0.1371 0.0329 -0.0025 0.0001  -0.0127 301 TLA A C3  
1855 O O3  . TLA B .   ? 0.1306 0.1423 0.0356 -0.0070 -0.0004 -0.0200 301 TLA A O3  
1856 C C4  . TLA B .   ? 0.1457 0.1517 0.0542 0.0044  0.0014  -0.0115 301 TLA A C4  
1857 O O4  . TLA B .   ? 0.1574 0.2074 0.0620 0.0223  0.0159  -0.0154 301 TLA A O4  
1858 O O41 . TLA B .   ? 0.1741 0.1667 0.0665 0.0227  -0.0079 -0.0140 301 TLA A O41 
1859 O O   . HOH C .   ? 0.3929 0.2743 0.1806 0.0419  -0.0614 0.0293  401 HOH A O   
1860 O O   . HOH C .   ? 0.3217 0.2810 0.3113 0.0132  -0.0701 0.0010  402 HOH A O   
1861 O O   . HOH C .   ? 0.2223 0.2531 0.1171 0.0249  0.0217  -0.0032 403 HOH A O   
1862 O O   . HOH C .   ? 0.2250 0.3688 0.3582 -0.0320 0.0202  0.0167  404 HOH A O   
1863 O O   . HOH C .   ? 0.4894 0.3792 0.3703 0.1283  -0.0785 -0.1049 405 HOH A O   
1864 O O   . HOH C .   ? 0.3846 0.3822 0.1597 -0.0236 -0.0421 -0.0120 406 HOH A O   
1865 O O   . HOH C .   ? 0.4344 0.2706 0.1584 -0.0400 -0.0255 -0.0118 407 HOH A O   
1866 O O   . HOH C .   ? 0.2219 0.2412 0.2431 -0.0058 -0.0020 0.0208  408 HOH A O   
1867 O O   . HOH C .   ? 0.3196 0.3418 0.2983 0.0594  -0.0494 -0.1228 409 HOH A O   
1868 O O   . HOH C .   ? 0.4766 0.4107 0.2194 -0.1389 -0.1012 0.0959  410 HOH A O   
1869 O O   . HOH C .   ? 0.2790 0.3708 0.1772 0.0625  -0.0743 -0.1400 411 HOH A O   
1870 O O   . HOH C .   ? 0.2257 0.2008 0.1447 -0.0038 -0.0221 -0.0032 412 HOH A O   
1871 O O   . HOH C .   ? 0.2866 0.2597 0.2329 0.0017  0.0108  -0.0049 413 HOH A O   
1872 O O   . HOH C .   ? 0.5694 0.3452 0.4645 -0.0120 -0.0946 -0.1077 414 HOH A O   
1873 O O   . HOH C .   ? 0.5670 0.3236 0.1352 -0.1402 -0.0237 0.0283  415 HOH A O   
1874 O O   . HOH C .   ? 0.1911 0.2781 0.0962 -0.0865 -0.0523 0.0983  416 HOH A O   
1875 O O   . HOH C .   ? 0.3614 0.1715 0.2234 0.0601  -0.0934 -0.0090 417 HOH A O   
1876 O O   . HOH C .   ? 0.5937 0.3653 0.1563 -0.0197 0.0787  0.0417  418 HOH A O   
1877 O O   . HOH C .   ? 0.2064 0.2542 0.2031 -0.0620 -0.0232 0.0335  419 HOH A O   
1878 O O   . HOH C .   ? 0.3656 0.1832 0.1309 0.0911  -0.0917 -0.0430 420 HOH A O   
1879 O O   . HOH C .   ? 0.4601 0.2665 0.3504 0.1007  -0.0489 0.0747  421 HOH A O   
1880 O O   . HOH C .   ? 0.1876 0.2607 0.0712 -0.0931 0.0088  -0.0046 422 HOH A O   
1881 O O   . HOH C .   ? 0.2583 0.2097 0.1800 -0.0761 -0.0371 0.0246  423 HOH A O   
1882 O O   . HOH C .   ? 0.4992 0.4004 0.4072 0.1076  -0.0491 -0.1349 424 HOH A O   
1883 O O   . HOH C .   ? 0.2209 0.3645 0.5021 0.0088  -0.0459 -0.1829 425 HOH A O   
1884 O O   . HOH C .   ? 0.5806 0.4904 0.2372 0.0056  -0.1395 -0.0451 426 HOH A O   
1885 O O   . HOH C .   ? 0.5004 0.2079 0.5255 -0.0401 -0.1191 -0.0174 427 HOH A O   
1886 O O   . HOH C .   ? 0.4682 0.2511 0.4677 0.0669  -0.1428 -0.0639 428 HOH A O   
1887 O O   . HOH C .   ? 0.4001 0.3507 0.1636 -0.1983 0.1293  -0.1026 429 HOH A O   
1888 O O   . HOH C .   ? 0.1983 0.2003 0.1079 -0.0141 0.0003  -0.0104 430 HOH A O   
1889 O O   . HOH C .   ? 0.4065 0.3302 0.4415 0.0780  -0.1312 -0.0121 431 HOH A O   
1890 O O   . HOH C .   ? 0.1841 0.2525 0.1271 0.0234  -0.0209 -0.0160 432 HOH A O   
1891 O O   . HOH C .   ? 0.4782 0.3702 0.3318 -0.0460 0.1874  -0.0807 433 HOH A O   
1892 O O   . HOH C .   ? 0.2068 0.2658 0.2363 -0.0339 0.0062  -0.1135 434 HOH A O   
1893 O O   . HOH C .   ? 0.4933 0.5292 0.1364 -0.0799 -0.0320 0.0474  435 HOH A O   
1894 O O   . HOH C .   ? 0.3620 0.2081 0.3284 0.0490  -0.0057 -0.0432 436 HOH A O   
1895 O O   . HOH C .   ? 0.4087 0.1674 0.2963 0.0831  -0.1460 -0.0776 437 HOH A O   
1896 O O   . HOH C .   ? 0.2863 0.2636 0.1031 -0.0716 0.0168  -0.0197 438 HOH A O   
1897 O O   . HOH C .   ? 0.4695 0.2501 0.5099 -0.0750 0.0798  -0.1349 439 HOH A O   
1898 O O   . HOH C .   ? 0.3326 0.2770 0.2584 -0.0659 0.0083  0.0333  440 HOH A O   
1899 O O   . HOH C .   ? 0.3343 0.5448 0.2570 -0.0963 -0.0763 0.0662  441 HOH A O   
1900 O O   . HOH C .   ? 0.2799 0.1851 0.4132 0.0390  0.0440  -0.0438 442 HOH A O   
1901 O O   . HOH C .   ? 0.3625 0.3662 0.1796 0.0968  0.0210  0.1079  443 HOH A O   
1902 O O   . HOH C .   ? 0.3007 0.2697 0.1343 0.0731  -0.0145 0.0231  444 HOH A O   
1903 O O   . HOH C .   ? 0.3884 0.4694 0.1962 0.1408  -0.1253 -0.0976 445 HOH A O   
1904 O O   . HOH C .   ? 0.3862 0.2091 0.5599 -0.0151 -0.1328 -0.0362 446 HOH A O   
1905 O O   . HOH C .   ? 0.4146 0.6050 0.3165 0.0416  0.0119  0.0778  447 HOH A O   
1906 O O   . HOH C .   ? 0.2555 0.2149 0.1359 0.0345  -0.0331 -0.0214 448 HOH A O   
1907 O O   . HOH C .   ? 0.2042 0.1750 0.1598 0.0168  -0.0320 0.0010  449 HOH A O   
1908 O O   . HOH C .   ? 0.5813 0.4088 0.1675 0.0653  0.0285  -0.0493 450 HOH A O   
1909 O O   . HOH C .   ? 0.3117 0.2599 0.3156 -0.0315 0.1437  -0.1095 451 HOH A O   
1910 O O   . HOH C .   ? 0.2195 0.5592 0.2211 0.0671  -0.0132 0.1632  452 HOH A O   
1911 O O   . HOH C .   ? 0.4995 0.2336 0.4604 0.0918  0.1023  0.0255  453 HOH A O   
1912 O O   . HOH C .   ? 0.2264 0.4498 0.4088 0.0388  0.0384  0.1380  454 HOH A O   
1913 O O   . HOH C .   ? 0.1829 0.2027 0.0607 -0.0601 -0.0003 0.0040  455 HOH A O   
1914 O O   . HOH C .   ? 0.3040 0.2879 0.3590 -0.0338 0.0065  0.1514  456 HOH A O   
1915 O O   . HOH C .   ? 0.1877 0.2811 0.1350 -0.0488 -0.0236 0.0119  457 HOH A O   
1916 O O   . HOH C .   ? 0.2034 0.5400 0.1264 -0.0828 -0.0266 0.0407  458 HOH A O   
1917 O O   . HOH C .   ? 0.3879 0.2885 0.1123 -0.1586 0.0840  -0.0558 459 HOH A O   
1918 O O   . HOH C .   ? 0.3394 0.2822 0.4186 0.0337  0.0791  0.0113  460 HOH A O   
1919 O O   . HOH C .   ? 0.2393 0.3166 0.2024 0.0468  -0.0313 -0.0166 461 HOH A O   
1920 O O   . HOH C .   ? 0.2345 0.1875 0.1778 -0.0696 -0.1210 0.0852  462 HOH A O   
1921 O O   . HOH C .   ? 0.3542 0.2792 0.1526 -0.0525 -0.0580 -0.0126 463 HOH A O   
1922 O O   . HOH C .   ? 0.2559 0.1642 0.0832 0.0126  -0.0641 -0.0213 464 HOH A O   
1923 O O   . HOH C .   ? 0.2379 0.2904 0.1607 -0.0811 0.0307  -0.0169 465 HOH A O   
1924 O O   . HOH C .   ? 0.1477 0.1763 0.0625 -0.0385 -0.0099 0.0011  466 HOH A O   
1925 O O   . HOH C .   ? 0.2105 0.2160 0.1999 0.0118  -0.0503 -0.0104 467 HOH A O   
1926 O O   . HOH C .   ? 0.4788 0.3334 0.4859 -0.0904 0.0040  0.1929  468 HOH A O   
1927 O O   . HOH C .   ? 0.3560 0.5594 0.1978 -0.0702 0.1127  -0.1190 469 HOH A O   
1928 O O   . HOH C .   ? 0.2352 0.2633 0.1494 -0.0104 0.0344  -0.0828 470 HOH A O   
1929 O O   . HOH C .   ? 0.1512 0.2075 0.1118 0.0512  -0.0310 -0.0143 471 HOH A O   
1930 O O   . HOH C .   ? 0.1348 0.1493 0.0549 -0.0042 -0.0305 -0.0159 472 HOH A O   
1931 O O   . HOH C .   ? 0.1483 0.1327 0.0262 0.0237  -0.0084 0.0041  473 HOH A O   
1932 O O   . HOH C .   ? 0.2675 0.2396 0.2458 -0.0086 0.0390  -0.0721 474 HOH A O   
1933 O O   . HOH C .   ? 0.3802 0.6114 0.3452 -0.0089 0.1574  -0.0582 475 HOH A O   
1934 O O   . HOH C .   ? 0.4469 0.2508 0.1417 -0.1212 -0.0614 0.0048  476 HOH A O   
1935 O O   . HOH C .   ? 0.1272 0.1280 0.0675 -0.0075 -0.0062 -0.0076 477 HOH A O   
1936 O O   . HOH C .   ? 0.3307 0.2744 0.2858 -0.0567 -0.0231 0.0679  478 HOH A O   
1937 O O   . HOH C .   ? 0.2125 0.3947 0.1568 0.0202  -0.0520 -0.0522 479 HOH A O   
1938 O O   . HOH C .   ? 0.2486 0.6083 0.3790 0.0058  0.1380  -0.0733 480 HOH A O   
1939 O O   . HOH C .   ? 0.2575 0.4623 0.3038 0.0600  0.0031  -0.2082 481 HOH A O   
1940 O O   . HOH C .   ? 0.2787 0.5683 0.2171 0.0871  -0.0087 -0.1323 482 HOH A O   
1941 O O   . HOH C .   ? 0.1550 0.1419 0.0593 -0.0151 -0.0172 0.0000  483 HOH A O   
1942 O O   . HOH C .   ? 0.2892 0.1753 0.2785 0.0634  -0.0306 -0.0024 484 HOH A O   
1943 O O   . HOH C .   ? 0.2742 0.4025 0.3229 -0.0316 -0.0607 0.1123  485 HOH A O   
1944 O O   . HOH C .   ? 0.5103 0.3968 0.1751 -0.0500 -0.0577 0.0758  486 HOH A O   
1945 O O   . HOH C .   ? 0.2429 0.2573 0.1570 0.0206  0.0008  -0.0851 487 HOH A O   
1946 O O   . HOH C .   ? 0.1883 0.2021 0.1294 -0.0333 -0.0291 -0.0091 488 HOH A O   
1947 O O   . HOH C .   ? 0.2058 0.2904 0.0870 0.0080  -0.0121 0.0148  489 HOH A O   
1948 O O   . HOH C .   ? 0.4798 0.2162 0.1101 -0.0816 -0.0720 -0.0417 490 HOH A O   
1949 O O   . HOH C .   ? 0.1360 0.1172 0.0345 -0.0094 -0.0024 -0.0147 491 HOH A O   
1950 O O   . HOH C .   ? 0.2029 0.3687 0.5688 0.0395  0.0021  -0.1298 492 HOH A O   
1951 O O   . HOH C .   ? 0.1277 0.1638 0.0439 -0.0039 -0.0030 -0.0091 493 HOH A O   
1952 O O   . HOH C .   ? 0.1330 0.1359 0.0267 0.0145  -0.0123 -0.0024 494 HOH A O   
1953 O O   . HOH C .   ? 0.1629 0.1662 0.0662 -0.0035 -0.0162 -0.0010 495 HOH A O   
1954 O O   . HOH C .   ? 0.2824 0.4543 0.4159 0.0224  0.1352  -0.0423 496 HOH A O   
1955 O O   . HOH C .   ? 0.4627 0.4343 0.4588 0.0907  0.0108  -0.1674 497 HOH A O   
1956 O O   . HOH C .   ? 0.2646 0.2356 0.2045 0.0269  0.0378  -0.0368 498 HOH A O   
1957 O O   . HOH C .   ? 0.4570 0.2311 0.1999 -0.0474 0.1105  -0.0267 499 HOH A O   
1958 O O   . HOH C .   ? 0.2834 0.2843 0.2491 -0.0380 -0.0017 -0.0367 500 HOH A O   
1959 O O   . HOH C .   ? 0.4145 0.5179 0.1410 -0.0445 0.0280  0.1034  501 HOH A O   
1960 O O   . HOH C .   ? 0.1715 0.2151 0.1212 -0.0486 0.0060  -0.0158 502 HOH A O   
1961 O O   . HOH C .   ? 0.1463 0.1452 0.1259 -0.0087 0.0125  -0.0383 503 HOH A O   
1962 O O   . HOH C .   ? 0.3656 0.3083 0.2952 0.1261  -0.1937 -0.1287 504 HOH A O   
1963 O O   . HOH C .   ? 0.1685 0.2328 0.0850 0.0417  0.0169  0.0117  505 HOH A O   
1964 O O   . HOH C .   ? 0.1962 0.1416 0.1088 -0.0124 -0.0285 0.0176  506 HOH A O   
1965 O O   . HOH C .   ? 0.3140 0.4503 0.1350 -0.0096 0.0390  0.0082  507 HOH A O   
1966 O O   . HOH C .   ? 0.1845 0.2167 0.1266 0.0002  -0.0028 -0.0100 508 HOH A O   
1967 O O   . HOH C .   ? 0.1629 0.2338 0.0656 -0.0265 0.0145  -0.0180 509 HOH A O   
1968 O O   . HOH C .   ? 0.2292 0.2920 0.2214 -0.0283 -0.0268 0.0779  510 HOH A O   
1969 O O   . HOH C .   ? 0.4701 0.2303 0.4211 0.0348  -0.1839 -0.0033 511 HOH A O   
1970 O O   . HOH C .   ? 0.3510 0.3141 0.3455 0.0674  0.1380  -0.0216 512 HOH A O   
1971 O O   . HOH C .   ? 0.5212 0.4444 0.1893 -0.0093 0.0405  0.1370  513 HOH A O   
1972 O O   . HOH C .   ? 0.3208 0.1982 0.2645 -0.0526 -0.0315 0.0401  514 HOH A O   
1973 O O   . HOH C .   ? 0.2950 0.2212 0.2179 -0.0256 -0.0645 0.0184  515 HOH A O   
1974 O O   . HOH C .   ? 0.1791 0.1686 0.0707 0.0111  0.0103  0.0033  516 HOH A O   
1975 O O   . HOH C .   ? 0.2044 0.3389 0.1136 -0.0615 -0.0038 -0.0246 517 HOH A O   
1976 O O   . HOH C .   ? 0.2466 0.2225 0.2303 0.0645  -0.0325 -0.0891 518 HOH A O   
1977 O O   . HOH C .   ? 0.3324 0.4033 0.4355 0.0308  0.0385  -0.1238 519 HOH A O   
1978 O O   . HOH C .   ? 0.3057 0.2717 0.1534 -0.0651 0.0135  0.0232  520 HOH A O   
1979 O O   . HOH C .   ? 0.3833 0.2031 0.2446 -0.0398 -0.0661 0.0774  521 HOH A O   
1980 O O   . HOH C .   ? 0.4080 0.4446 0.3838 0.0691  -0.0875 -0.1629 522 HOH A O   
1981 O O   . HOH C .   ? 0.4513 0.2611 0.1485 0.1377  -0.0076 -0.0137 523 HOH A O   
1982 O O   . HOH C .   ? 0.1490 0.2268 0.1183 0.0068  0.0194  0.0319  524 HOH A O   
1983 O O   . HOH C .   ? 0.3294 0.2477 0.1323 -0.0489 -0.0596 0.0294  525 HOH A O   
1984 O O   . HOH C .   ? 0.2504 0.3684 0.2759 -0.0634 0.1245  -0.1211 526 HOH A O   
1985 O O   . HOH C .   ? 0.3802 0.2093 0.1447 -0.0024 -0.0641 0.0618  527 HOH A O   
1986 O O   . HOH C .   ? 0.1591 0.1302 0.0729 -0.0210 -0.0189 0.0057  528 HOH A O   
1987 O O   . HOH C .   ? 0.3006 0.3746 0.3661 -0.0101 -0.1445 -0.0935 529 HOH A O   
1988 O O   . HOH C .   ? 0.3614 0.1998 0.0751 -0.1219 -0.0296 0.0220  530 HOH A O   
1989 O O   . HOH C .   ? 0.3834 0.3658 0.2953 -0.0744 -0.1200 0.0143  531 HOH A O   
1990 O O   . HOH C .   ? 0.2209 0.3011 0.5974 0.0771  -0.1200 0.0387  532 HOH A O   
1991 O O   . HOH C .   ? 0.1271 0.2748 0.0921 0.0063  -0.0311 -0.0640 533 HOH A O   
1992 O O   . HOH C .   ? 0.5251 0.2606 0.1888 -0.0452 -0.1309 0.0425  534 HOH A O   
1993 O O   . HOH C .   ? 0.3520 0.4133 0.3073 -0.0926 -0.0041 0.1580  535 HOH A O   
1994 O O   . HOH C .   ? 0.2955 0.5677 0.2572 0.0839  0.0059  -0.1309 536 HOH A O   
1995 O O   . HOH C .   ? 0.2217 0.5029 0.1228 -0.0229 -0.0177 -0.0975 537 HOH A O   
1996 O O   . HOH C .   ? 0.1658 0.1508 0.0824 0.0039  0.0018  -0.0226 538 HOH A O   
1997 O O   . HOH C .   ? 0.2384 0.4358 0.1082 -0.1406 0.0352  -0.0724 539 HOH A O   
1998 O O   . HOH C .   ? 0.1933 0.1975 0.0882 -0.0008 -0.0125 -0.0136 540 HOH A O   
1999 O O   . HOH C .   ? 0.1781 0.1847 0.1222 0.0162  0.0144  0.0078  541 HOH A O   
2000 O O   . HOH C .   ? 0.1290 0.1303 0.0496 0.0063  -0.0064 0.0162  542 HOH A O   
2001 O O   . HOH C .   ? 0.3492 0.3364 0.5068 -0.0439 -0.0501 0.0826  543 HOH A O   
2002 O O   . HOH C .   ? 0.2181 0.2184 0.1799 -0.0004 -0.0171 0.0259  544 HOH A O   
2003 O O   . HOH C .   ? 0.1738 0.2788 0.0936 -0.0358 -0.0136 -0.0058 545 HOH A O   
2004 O O   . HOH C .   ? 0.1507 0.2051 0.1025 -0.0001 -0.0026 -0.0402 546 HOH A O   
2005 O O   . HOH C .   ? 0.1727 0.1877 0.0975 -0.0102 -0.0225 -0.0041 547 HOH A O   
2006 O O   . HOH C .   ? 0.4620 0.3906 0.3756 0.0378  -0.2097 0.0343  548 HOH A O   
2007 O O   . HOH C .   ? 0.2259 0.2361 0.0928 0.0142  0.0027  -0.0061 549 HOH A O   
2008 O O   . HOH C .   ? 0.2478 0.2579 0.1694 0.0511  0.0398  0.0553  550 HOH A O   
2009 O O   . HOH C .   ? 0.2175 0.1374 0.0971 0.0078  -0.0540 0.0120  551 HOH A O   
2010 O O   . HOH C .   ? 0.2687 0.1871 0.1120 0.0343  0.0518  0.0180  552 HOH A O   
2011 O O   . HOH C .   ? 0.1883 0.1932 0.0800 -0.0291 -0.0281 -0.0210 553 HOH A O   
2012 O O   . HOH C .   ? 0.2187 0.4488 0.2509 -0.0285 0.0037  0.1531  554 HOH A O   
2013 O O   . HOH C .   ? 0.1450 0.1334 0.0665 0.0070  -0.0076 -0.0007 555 HOH A O   
2014 O O   . HOH C .   ? 0.2869 0.4059 0.2408 0.0210  -0.0297 -0.0436 556 HOH A O   
2015 O O   . HOH C .   ? 0.1733 0.1630 0.0529 -0.0018 -0.0128 -0.0022 557 HOH A O   
2016 O O   . HOH C .   ? 0.3854 0.5164 0.1447 0.0153  0.0407  -0.0328 558 HOH A O   
2017 O O   . HOH C .   ? 0.1788 0.1797 0.1109 -0.0019 -0.0255 0.0119  559 HOH A O   
2018 O O   . HOH C .   ? 0.2657 0.6018 0.1634 -0.0685 0.0266  -0.0882 560 HOH A O   
2019 O O   . HOH C .   ? 0.1618 0.1135 0.2008 -0.0149 -0.0714 0.0179  561 HOH A O   
2020 O O   . HOH C .   ? 0.3614 0.2529 0.2536 -0.0459 0.0299  -0.0510 562 HOH A O   
2021 O O   . HOH C .   ? 0.2690 0.2802 0.1705 -0.0714 -0.0600 0.0786  563 HOH A O   
2022 O O   . HOH C .   ? 0.1959 0.4016 0.1185 0.1119  0.0751  0.0997  564 HOH A O   
2023 O O   . HOH C .   ? 0.2096 0.3189 0.5506 0.0209  0.1095  0.1249  565 HOH A O   
2024 O O   . HOH C .   ? 0.5000 0.3683 0.2904 -0.1010 -0.1010 0.1472  566 HOH A O   
2025 O O   . HOH C .   ? 0.1959 0.4766 0.2899 0.0019  -0.0187 0.2316  567 HOH A O   
2026 O O   . HOH C .   ? 0.3139 0.4173 0.1164 -0.0073 -0.0033 0.0870  568 HOH A O   
2027 O O   . HOH C .   ? 0.2568 0.5984 0.1659 -0.0413 -0.0487 0.1127  569 HOH A O   
2028 O O   . HOH C .   ? 0.2011 0.3378 0.1345 -0.0777 -0.0192 -0.0341 570 HOH A O   
2029 O O   . HOH C .   ? 0.4685 0.4672 0.1468 -0.0335 -0.0615 0.0780  571 HOH A O   
2030 O O   . HOH C .   ? 0.2500 0.2333 0.2232 0.0496  -0.0435 -0.0078 572 HOH A O   
2031 O O   . HOH C .   ? 0.2096 0.4632 0.1092 0.0034  -0.0427 0.0697  573 HOH A O   
2032 O O   . HOH C .   ? 0.1469 0.1549 0.0820 -0.0354 0.0335  0.0081  574 HOH A O   
2033 O O   . HOH C .   ? 0.2589 0.1989 0.0947 -0.0362 -0.0380 -0.0383 575 HOH A O   
2034 O O   . HOH C .   ? 0.2257 0.3840 0.5611 0.0258  -0.1351 -0.0736 576 HOH A O   
2035 O O   . HOH C .   ? 0.3026 0.2743 0.1552 0.0109  -0.0047 0.0359  577 HOH A O   
2036 O O   . HOH C .   ? 0.3033 0.3018 0.1061 -0.0895 0.0471  -0.0455 578 HOH A O   
2037 O O   . HOH C .   ? 0.2562 0.1587 0.0552 -0.0139 0.0434  -0.0207 579 HOH A O   
2038 O O   . HOH C .   ? 0.3354 0.2250 0.2259 -0.0221 0.0604  -0.0069 580 HOH A O   
2039 O O   . HOH C .   ? 0.3220 0.3107 0.3127 0.0181  0.0070  0.1691  581 HOH A O   
2040 O O   . HOH C .   ? 0.2588 0.1945 0.1412 0.0151  -0.0543 -0.0506 582 HOH A O   
2041 O O   . HOH C .   ? 0.3378 0.2503 0.0977 -0.0309 -0.0320 -0.0176 583 HOH A O   
2042 O O   . HOH C .   ? 0.2080 0.1884 0.1058 -0.0107 -0.0010 0.0114  584 HOH A O   
2043 O O   . HOH C .   ? 0.2009 0.3244 0.1297 0.0436  -0.0286 -0.0301 585 HOH A O   
2044 O O   . HOH C .   ? 0.5164 0.2827 0.3921 0.1098  0.0918  0.1178  586 HOH A O   
2045 O O   . HOH C .   ? 0.2346 0.2105 0.2501 -0.0347 -0.0668 0.0802  587 HOH A O   
2046 O O   . HOH C .   ? 0.2341 0.3317 0.2024 0.0107  -0.0199 0.0122  588 HOH A O   
2047 O O   . HOH C .   ? 0.2157 0.2019 0.0857 -0.0302 -0.0009 0.0009  589 HOH A O   
2048 O O   . HOH C .   ? 0.3012 0.1661 0.3279 -0.0157 0.0736  0.0425  590 HOH A O   
2049 O O   . HOH C .   ? 0.5490 0.3724 0.4508 -0.1388 -0.0210 -0.1099 591 HOH A O   
2050 O O   . HOH C .   ? 0.4567 0.3387 0.2401 0.1335  0.1682  0.0849  592 HOH A O   
2051 O O   . HOH C .   ? 0.5591 0.3029 0.4060 0.0679  -0.0249 0.0317  593 HOH A O   
2052 O O   . HOH C .   ? 0.1984 0.1573 0.1516 -0.0050 0.0028  0.0259  594 HOH A O   
2053 O O   . HOH C .   ? 0.1275 0.1598 0.0711 0.0170  -0.0135 -0.0165 595 HOH A O   
2054 O O   . HOH C .   ? 0.1906 0.2322 0.0985 -0.0735 -0.0028 -0.0017 596 HOH A O   
2055 O O   . HOH C .   ? 0.2609 0.2755 0.1429 -0.0688 -0.0230 0.0127  597 HOH A O   
2056 O O   . HOH C .   ? 0.2243 0.1972 0.1257 0.0199  0.0067  -0.0794 598 HOH A O   
2057 O O   . HOH C .   ? 0.2320 0.2457 0.1390 -0.0457 -0.0166 -0.0433 599 HOH A O   
2058 O O   . HOH C .   ? 0.1635 0.2829 0.1641 0.0090  0.0519  -0.0486 600 HOH A O   
2059 O O   . HOH C .   ? 0.4337 0.4721 0.4595 -0.0537 -0.0367 -0.1336 601 HOH A O   
2060 O O   . HOH C .   ? 0.5315 0.1492 0.2659 -0.0395 -0.0305 -0.0362 602 HOH A O   
2061 O O   . HOH C .   ? 0.1816 0.2001 0.0619 0.0312  -0.0072 0.0087  603 HOH A O   
2062 O O   . HOH C .   ? 0.3766 0.5746 0.3160 -0.0050 0.0751  -0.1299 604 HOH A O   
2063 O O   . HOH C .   ? 0.2289 0.2491 0.2079 0.0104  0.0174  -0.0794 605 HOH A O   
2064 O O   . HOH C .   ? 0.3042 0.2706 0.1556 0.0381  -0.0163 0.0154  606 HOH A O   
2065 O O   . HOH C .   ? 0.4978 0.3638 0.1944 0.1632  -0.0576 -0.1036 607 HOH A O   
2066 O O   . HOH C .   ? 0.1352 0.1270 0.0629 -0.0106 -0.0198 -0.0013 608 HOH A O   
2067 O O   . HOH C .   ? 0.4578 0.2681 0.3979 -0.1238 -0.1516 0.0629  609 HOH A O   
2068 O O   . HOH C .   ? 0.3181 0.3285 0.1774 0.0342  0.0313  -0.0014 610 HOH A O   
2069 O O   . HOH C .   ? 0.3793 0.3455 0.3232 0.0503  -0.0563 0.0710  611 HOH A O   
2070 O O   . HOH C .   ? 0.5343 0.5806 0.3814 -0.0505 0.0696  -0.0381 612 HOH A O   
2071 O O   . HOH C .   ? 0.2559 0.1986 0.1712 -0.0466 -0.0588 -0.0069 613 HOH A O   
2072 O O   . HOH C .   ? 0.1963 0.1959 0.1379 -0.0028 0.0244  -0.0163 614 HOH A O   
2073 O O   . HOH C .   ? 0.2219 0.2121 0.1945 -0.0053 -0.0201 0.0006  615 HOH A O   
2074 O O   . HOH C .   ? 0.3897 0.3621 0.1826 0.0730  -0.0798 -0.0551 616 HOH A O   
2075 O O   . HOH C .   ? 0.3518 0.2693 0.4022 -0.0633 -0.1233 0.1161  617 HOH A O   
2076 O O   . HOH C .   ? 0.4884 0.3017 0.4946 0.0195  0.1306  -0.1002 618 HOH A O   
2077 O O   . HOH C .   ? 0.2463 0.2126 0.3150 -0.0566 -0.0672 -0.0614 619 HOH A O   
2078 O O   . HOH C .   ? 0.2343 0.6172 0.2718 0.0618  0.0085  0.0467  620 HOH A O   
2079 O O   . HOH C .   ? 0.5357 0.5191 0.4883 -0.0038 -0.0143 -0.0718 621 HOH A O   
2080 O O   . HOH C .   ? 0.5379 0.3413 0.3390 -0.0499 -0.1402 0.0792  622 HOH A O   
2081 O O   . HOH C .   ? 0.2230 0.1904 0.0829 0.0359  0.0065  0.0011  623 HOH A O   
2082 O O   . HOH C .   ? 0.1398 0.3280 0.0662 0.0316  0.0002  0.0301  624 HOH A O   
2083 O O   . HOH C .   ? 0.2793 0.3354 0.1627 -0.0327 -0.0031 -0.0393 625 HOH A O   
2084 O O   . HOH C .   ? 0.4556 0.2799 0.5505 -0.0117 0.1069  -0.0731 626 HOH A O   
2085 O O   . HOH C .   ? 0.2446 0.2566 0.3198 0.0265  -0.0198 0.0034  627 HOH A O   
2086 O O   . HOH C .   ? 0.3655 0.3643 0.2379 -0.0683 0.0744  0.0085  628 HOH A O   
2087 O O   . HOH C .   ? 0.2434 0.2460 0.1954 0.0299  0.0511  0.0132  629 HOH A O   
2088 O O   . HOH C .   ? 0.3575 0.4715 0.3391 0.1279  0.0383  -0.0255 630 HOH A O   
2089 O O   . HOH C .   ? 0.5294 0.3192 0.4005 0.0260  -0.1509 0.1016  631 HOH A O   
2090 O O   . HOH C .   ? 0.3794 0.5246 0.4149 0.0786  0.2034  -0.1312 632 HOH A O   
2091 O O   . HOH C .   ? 0.2355 0.2462 0.1146 0.0484  -0.0516 -0.0289 633 HOH A O   
2092 O O   . HOH C .   ? 0.6168 0.3132 0.2983 0.0320  0.0468  0.1337  634 HOH A O   
2093 O O   . HOH C .   ? 0.3048 0.4791 0.2429 0.0617  0.0552  -0.0125 635 HOH A O   
2094 O O   . HOH C .   ? 0.2229 0.5972 0.2576 0.0455  0.0933  0.0864  636 HOH A O   
2095 O O   . HOH C .   ? 0.3950 0.4879 0.3805 0.0524  0.0132  0.1806  637 HOH A O   
2096 O O   . HOH C .   ? 0.5189 0.2998 0.2824 -0.1468 0.0385  -0.0603 638 HOH A O   
2097 O O   . HOH C .   ? 0.5823 0.3042 0.3457 -0.0171 -0.1026 0.1265  639 HOH A O   
2098 O O   . HOH C .   ? 0.4286 0.4208 0.4298 -0.0523 0.1525  -0.0946 640 HOH A O   
2099 O O   . HOH C .   ? 0.4520 0.5922 0.2565 0.0729  0.0542  -0.0866 641 HOH A O   
2100 O O   . HOH C .   ? 0.3211 0.3434 0.3723 -0.1153 -0.0690 0.0583  642 HOH A O   
2101 O O   . HOH C .   ? 0.1983 0.2456 0.2099 0.0284  0.0117  0.0527  643 HOH A O   
2102 O O   . HOH C .   ? 0.2009 0.1703 0.1393 -0.0269 -0.0273 -0.0093 644 HOH A O   
2103 O O   . HOH C .   ? 0.5061 0.3638 0.2082 -0.0947 -0.0959 0.0537  645 HOH A O   
2104 O O   . HOH C .   ? 0.5377 0.4450 0.3817 0.1339  0.0202  -0.0178 646 HOH A O   
2105 O O   . HOH C .   ? 0.2868 0.2391 0.3657 0.0085  -0.1052 -0.0981 647 HOH A O   
2106 O O   . HOH C .   ? 0.3942 0.3137 0.3455 0.0264  -0.1810 -0.0622 648 HOH A O   
2107 O O   . HOH C .   ? 0.3560 0.5384 0.3697 0.1483  0.0390  0.0423  649 HOH A O   
2108 O O   . HOH C .   ? 0.3220 0.2360 0.5912 0.0607  0.0236  0.1199  650 HOH A O   
2109 O O   . HOH C .   ? 0.4314 0.4812 0.1676 -0.0144 -0.0592 -0.0381 651 HOH A O   
2110 O O   . HOH C .   ? 0.3052 0.4944 0.3915 -0.0507 0.0348  -0.1711 652 HOH A O   
2111 O O   . HOH C .   ? 0.3182 0.4558 0.3024 0.0892  0.0314  0.0143  653 HOH A O   
2112 O O   . HOH C .   ? 0.5547 0.3338 0.3340 0.1374  0.0400  0.0581  654 HOH A O   
2113 O O   . HOH C .   ? 0.3786 0.5390 0.2291 0.1075  0.0075  0.1333  655 HOH A O   
2114 O O   . HOH C .   ? 0.3673 0.3323 0.3216 0.1414  -0.1334 -0.1396 656 HOH A O   
2115 O O   . HOH C .   ? 0.4440 0.3302 0.4998 0.0394  -0.0849 -0.1498 657 HOH A O   
2116 O O   . HOH C .   ? 0.6268 0.3001 0.6172 -0.0363 -0.0090 -0.0715 658 HOH A O   
2117 O O   . HOH C .   ? 0.5624 0.2899 0.3051 -0.0168 -0.1399 0.0992  659 HOH A O   
2118 O O   . HOH C .   ? 0.6130 0.2141 0.0842 -0.0857 -0.0270 -0.0058 660 HOH A O   
2119 O O   . HOH C .   ? 0.5022 0.3442 0.3374 -0.0519 -0.1160 0.0090  661 HOH A O   
2120 O O   . HOH C .   ? 0.5666 0.2782 0.2998 0.1520  -0.0324 0.0671  662 HOH A O   
2121 O O   . HOH C .   ? 0.2120 0.2242 0.1255 0.0170  0.0414  0.0400  663 HOH A O   
2122 O O   . HOH C .   ? 0.4808 0.4403 0.1716 0.1317  0.0139  -0.0517 664 HOH A O   
2123 O O   . HOH C .   ? 0.6145 0.4159 0.3049 -0.0380 -0.0129 0.0905  665 HOH A O   
2124 O O   . HOH C .   ? 0.3189 0.2516 0.5557 -0.0055 -0.1286 -0.0995 666 HOH A O   
2125 O O   . HOH C .   ? 0.2622 0.4148 0.1989 -0.0202 0.0484  -0.1408 667 HOH A O   
2126 O O   . HOH C .   ? 0.2593 0.6069 0.1676 -0.0856 0.0275  -0.0492 668 HOH A O   
2127 O O   . HOH C .   ? 0.3508 0.4237 0.3102 -0.1086 0.0892  -0.1879 669 HOH A O   
2128 O O   . HOH C .   ? 0.4208 0.6181 0.4674 -0.0283 0.1846  0.0168  670 HOH A O   
2129 O O   . HOH C .   ? 0.3534 0.4236 0.3692 -0.0108 -0.0382 -0.2341 671 HOH A O   
2130 O O   . HOH C .   ? 0.3264 0.4290 0.2431 0.0485  0.0497  0.0237  672 HOH A O   
2131 O O   . HOH C .   ? 0.2609 0.2333 0.0987 -0.1030 0.0556  -0.0187 673 HOH A O   
2132 O O   . HOH C .   ? 0.5683 0.5237 0.2992 -0.0050 0.0711  -0.1616 674 HOH A O   
2133 O O   . HOH C .   ? 0.5431 0.5858 0.2686 0.0243  -0.0772 -0.0895 675 HOH A O   
2134 O O   . HOH C .   ? 0.4077 0.2963 0.1627 -0.0909 -0.0589 0.0239  676 HOH A O   
2135 O O   . HOH C .   ? 0.3449 0.4176 0.5489 -0.0189 -0.1430 -0.0628 677 HOH A O   
2136 O O   . HOH C .   ? 0.3741 0.5427 0.4427 -0.0081 0.0448  -0.0529 678 HOH A O   
2137 O O   . HOH C .   ? 0.2199 0.2183 0.1552 -0.0406 0.0059  -0.0346 679 HOH A O   
2138 O O   . HOH C .   ? 0.5319 0.2872 0.5468 0.1491  0.0509  0.0127  680 HOH A O   
2139 O O   . HOH C .   ? 0.3314 0.4020 0.4337 0.0466  0.0214  -0.2139 681 HOH A O   
2140 O O   . HOH C .   ? 0.3580 0.2738 0.1777 0.0994  -0.0707 -0.0519 682 HOH A O   
2141 O O   . HOH C .   ? 0.3344 0.2337 0.1307 -0.0089 -0.0081 -0.0203 683 HOH A O   
2142 O O   . HOH C .   ? 0.4934 0.4133 0.5586 0.1024  0.0322  0.0749  684 HOH A O   
2143 O O   . HOH C .   ? 0.4847 0.3657 0.2883 0.0625  -0.0551 -0.0317 685 HOH A O   
2144 O O   . HOH C .   ? 0.3035 0.4019 0.4790 -0.0845 -0.1546 0.0912  686 HOH A O   
2145 O O   . HOH C .   ? 0.6313 0.2706 0.5718 0.0202  -0.0096 0.0643  687 HOH A O   
2146 O O   . HOH C .   ? 0.3017 0.4715 0.2269 -0.1177 -0.0367 0.0146  688 HOH A O   
2147 O O   . HOH C .   ? 0.4997 0.3275 0.4149 -0.0874 -0.1419 0.0365  689 HOH A O   
2148 O O   . HOH C .   ? 0.4104 0.4114 0.4140 0.0234  -0.1539 0.1734  690 HOH A O   
2149 O O   . HOH C .   ? 0.4524 0.6127 0.3136 -0.0227 0.1683  0.0748  691 HOH A O   
2150 O O   . HOH C .   ? 0.6182 0.4315 0.2401 0.0379  0.0159  0.1052  692 HOH A O   
2151 O O   . HOH C .   ? 0.1953 0.1861 0.1341 -0.0287 0.0008  0.0025  693 HOH A O   
2152 O O   . HOH C .   ? 0.5315 0.2874 0.1927 0.1212  -0.1376 -0.0527 694 HOH A O   
2153 O O   . HOH C .   ? 0.3292 0.3747 0.3494 0.0385  -0.0377 0.1703  695 HOH A O   
2154 O O   . HOH C .   ? 0.3323 0.4341 0.4455 -0.0040 0.0160  -0.1926 696 HOH A O   
2155 O O   . HOH C .   ? 0.4218 0.2858 0.2983 -0.0780 -0.0367 0.0791  697 HOH A O   
2156 O O   . HOH C .   ? 0.3039 0.6284 0.2450 -0.0074 -0.0637 -0.0430 698 HOH A O   
2157 O O   . HOH C .   ? 0.4650 0.3440 0.3125 0.1249  -0.0667 -0.1104 699 HOH A O   
2158 O O   . HOH C .   ? 0.4254 0.3851 0.2554 0.1229  0.0048  0.0475  700 HOH A O   
2159 O O   . HOH C .   ? 0.6177 0.4098 0.4442 0.0461  0.0383  -0.0235 701 HOH A O   
2160 O O   . HOH C .   ? 0.5295 0.3433 0.4189 -0.1517 -0.0704 0.0033  702 HOH A O   
2161 O O   . HOH C .   ? 0.3253 0.3004 0.2027 0.0806  -0.0048 0.0345  703 HOH A O   
2162 O O   . HOH C .   ? 0.5557 0.2881 0.1646 -0.1593 0.0466  0.0084  704 HOH A O   
2163 O O   . HOH C .   ? 0.3956 0.4482 0.2543 -0.1937 0.0525  -0.0567 705 HOH A O   
2164 O O   . HOH C .   ? 0.4845 0.3881 0.4728 -0.0100 -0.1308 0.0964  706 HOH A O   
2165 O O   . HOH C .   ? 0.4505 0.5947 0.2654 -0.0824 0.0369  -0.0050 707 HOH A O   
2166 O O   . HOH C .   ? 0.5104 0.5706 0.3805 0.0574  0.1242  -0.1254 708 HOH A O   
2167 O O   . HOH C .   ? 0.2162 0.3587 0.6261 0.0006  0.0300  0.0367  709 HOH A O   
2168 O O   . HOH C .   ? 0.3773 0.3455 0.2455 0.0688  0.0442  -0.0714 710 HOH A O   
2169 O O   . HOH C .   ? 0.6047 0.5915 0.2764 -0.0344 -0.1007 -0.1219 711 HOH A O   
2170 O O   . HOH C .   ? 0.4280 0.4283 0.3363 -0.0992 0.0711  -0.0194 712 HOH A O   
2171 O O   . HOH C .   ? 0.4101 0.3223 0.4098 -0.1220 -0.1318 0.1162  713 HOH A O   
2172 O O   . HOH C .   ? 0.2139 0.2620 0.1369 0.0334  0.0096  0.0229  714 HOH A O   
2173 O O   . HOH C .   ? 0.2886 0.5540 0.1908 -0.1589 -0.0373 0.0334  715 HOH A O   
2174 O O   . HOH C .   ? 0.3438 0.4388 0.4258 0.0876  -0.0642 -0.1606 716 HOH A O   
2175 O O   . HOH C .   ? 0.4337 0.4762 0.1932 -0.0209 0.0116  0.0523  717 HOH A O   
2176 O O   . HOH C .   ? 0.3694 0.3506 0.3006 0.0987  0.0830  -0.0343 718 HOH A O   
2177 O O   . HOH C .   ? 0.3409 0.4772 0.1871 -0.1489 -0.0549 0.0435  719 HOH A O   
2178 O O   . HOH C .   ? 0.2927 0.6325 0.1693 -0.0054 0.0073  -0.0170 720 HOH A O   
2179 O O   . HOH C .   ? 0.6091 0.6329 0.2128 0.0028  0.1006  -0.0117 721 HOH A O   
2180 O O   . HOH C .   ? 0.4660 0.2816 0.3590 0.0717  -0.1500 -0.0177 722 HOH A O   
2181 O O   . HOH C .   ? 0.6053 0.4936 0.3388 0.0219  -0.0870 0.1220  723 HOH A O   
2182 O O   . HOH C .   ? 0.4724 0.4987 0.4044 0.0389  0.1056  -0.1623 724 HOH A O   
2183 O O   . HOH C .   ? 0.3200 0.5605 0.3920 -0.1104 -0.0143 0.0851  725 HOH A O   
2184 O O   . HOH C .   ? 0.4556 0.4096 0.5080 0.0535  0.1277  -0.1215 726 HOH A O   
2185 O O   . HOH C .   ? 0.3682 0.4887 0.2545 -0.1508 0.0294  -0.0040 727 HOH A O   
2186 O O   . HOH C .   ? 0.3244 0.1909 0.1823 0.0197  -0.0630 -0.0583 728 HOH A O   
2187 O O   . HOH C .   ? 0.4652 0.3703 0.3020 0.0552  -0.1475 -0.0649 729 HOH A O   
2188 O O   . HOH C .   ? 0.2406 0.2660 0.1813 0.0352  -0.0497 -0.0672 730 HOH A O   
2189 O O   . HOH C .   ? 0.3015 0.1893 0.2868 -0.0070 -0.0775 -0.0256 731 HOH A O   
2190 O O   . HOH C .   ? 0.1856 0.1921 0.1315 0.0077  -0.0029 -0.0545 732 HOH A O   
2191 O O   . HOH C .   ? 0.3048 0.5332 0.3882 -0.1697 -0.0167 0.0461  733 HOH A O   
2192 O O   . HOH C .   ? 0.2083 0.1857 0.0997 0.0492  -0.0095 -0.0238 734 HOH A O   
2193 O O   . HOH C .   ? 0.6160 0.3480 0.2869 0.0396  0.0485  0.0902  735 HOH A O   
2194 O O   . HOH C .   ? 0.4943 0.2888 0.4191 0.0900  -0.1259 -0.0873 736 HOH A O   
2195 O O   . HOH C .   ? 0.4553 0.2448 0.2197 -0.0152 -0.0859 -0.0174 737 HOH A O   
2196 O O   . HOH C .   ? 0.3666 0.4265 0.5981 -0.0712 -0.0551 0.0519  738 HOH A O   
2197 O O   . HOH C .   ? 0.4783 0.2800 0.2483 -0.0815 -0.0632 0.0837  739 HOH A O   
2198 O O   . HOH C .   ? 0.2776 0.2189 0.1830 0.0231  0.0658  0.0071  740 HOH A O   
2199 O O   . HOH C .   ? 0.4692 0.4204 0.2172 0.0831  -0.1135 -0.0403 741 HOH A O   
2200 O O   . HOH C .   ? 0.4215 0.4933 0.2960 0.0550  0.0863  -0.0616 742 HOH A O   
2201 O O   . HOH C .   ? 0.5980 0.6313 0.2385 0.0079  -0.1178 0.0266  743 HOH A O   
2202 O O   . HOH C .   ? 0.4643 0.3561 0.3623 0.0831  -0.1063 -0.1672 744 HOH A O   
2203 O O   . HOH C .   ? 0.4401 0.2244 0.6193 -0.0371 -0.0038 -0.0754 745 HOH A O   
2204 O O   . HOH C .   ? 0.5544 0.3754 0.2289 -0.1366 0.0587  0.0156  746 HOH A O   
2205 O O   . HOH C .   ? 0.5956 0.5491 0.2611 -0.0272 -0.1170 -0.0620 747 HOH A O   
# 
