data_9AUD
# 
_entry.id   9AUD 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.401 
_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   9AUD         pdb_00009aud 10.2210/pdb9aud/pdb 
WWPDB D_1000280747 ?            ?                   
# 
_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       2025-02-05 
# 
_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                        9AUD 
_pdbx_database_status.recvd_initial_deposition_date   2024-02-29 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_database_related.db_name        PDB 
_pdbx_database_related.details        'TCR-MHCII peptide complex' 
_pdbx_database_related.db_id          8VQ8 
_pdbx_database_related.content_type   unspecified 
# 
_pdbx_contact_author.id                 3 
_pdbx_contact_author.email              jamie.rossjohn@monash.edu 
_pdbx_contact_author.name_first         Jamie 
_pdbx_contact_author.name_last          Rossjohn 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-2020-7522 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Chaurasia, P.' 1 0000-0003-4249-3678 
'Littler, D.R.' 2 0000-0001-5904-1905 
'La Gruta, N.'  3 0000-0001-5358-9363 
'Rossjohn, J.'  4 0000-0002-2020-7522 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To be published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'NP-LCK2-1TCR-MHC complex' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Zhang, J.B.'   1 0000-0002-8658-6342 
primary 'Chaurasia, P.' 2 0000-0001-5358-9363 
primary 'Littler, D.R.' 3 0000-0001-5904-1905 
primary 'La Gruta, N.'  4 0000-0001-5358-9363 
primary 'Rossjohn, J.'  5 0000-0002-2020-7522 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'H-2 class II histocompatibility antigen, A-B alpha chain'            21204.674 1  ? ? ? 
'Expression tag on C terminal residue 181-188' 
2 polymer     man 'Nucleoprotein,H-2 class II histocompatibility antigen, A beta chain' 26266.168 1  ? ? ? 
;Residue -25 to -11 (1-15 aligned sequence) QVYSLIRPNENPAHK- NP311-325, Flu peptide sequence. Residue GSGGSIEGRGGSGASGDS (16-34 aligned sequence) is unique peptide linker sequence from construct, not present in electron density.,Residue -25 to -11 (1-15 aligned sequence) QVYSLIRPNENPAHK- NP311-325, Flu peptide sequence. Residue GSGGSIEGRGGSGASGDS (16-34 aligned sequence) is unique peptide linker sequence from construct, not present in electron density.
;
3 polymer     man 'NPLCK1-2_TCR TRAV6-5 alpha chain'                                    23039.350 1  ? ? ? ? 
4 polymer     man 'NPLCK1-2 TCR TRBV1 Beta chain'                                       27811.383 1  ? ? ? ? 
5 non-polymer syn 1,2-ETHANEDIOL                                                        62.068    6  ? ? ? ? 
6 non-polymer syn 2-acetamido-2-deoxy-beta-D-glucopyranose                              221.208   2  ? ? ? ? 
7 water       nat water                                                                 18.015    42 ? ? ? ? 
# 
loop_
_entity_name_com.entity_id 
_entity_name_com.name 
1 IAalpha                          
2 'Nucleocapsid protein,Protein N' 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no 
;DIEADHVGTYGISVYQSPGDIGQYTFEFDGDELFYVDLDKKETVWMLPEFGQLASFDPQGGLQNIAVVKHNLGVLTKRSN
STPATNEAPQATVFPKSPVLLGQPNTLICFVDNIFPPVINITWLRNSKSVADGVYETSFFVNRDYSFHKLSYLTFIPSDD
DIYDCKVEHWGLEEPVLKHWTSGLEVLF
;
;DIEADHVGTYGISVYQSPGDIGQYTFEFDGDELFYVDLDKKETVWMLPEFGQLASFDPQGGLQNIAVVKHNLGVLTKRSN
STPATNEAPQATVFPKSPVLLGQPNTLICFVDNIFPPVINITWLRNSKSVADGVYETSFFVNRDYSFHKLSYLTFIPSDD
DIYDCKVEHWGLEEPVLKHWTSGLEVLF
;
C ? 
2 'polypeptide(L)' no no 
;QVYSLIRPNENPAHKGSGGSIEGRGGSGASGDSERHFVYQFMGECYFTNGTQRIRYVTRYIYNREEYVRYDSDVGEHRAV
TELGRPDAEYWNSQPEILERTRAELDTVCRHNYEGPETHTSLRRLEQPNVVISLSRTEALNHHNTLVCSVTDFYPAKIKV
RWFRNGQEETVGVSSTQLIRNGDWTFQVLVMLEMTPRRGEVYTCHVEHPSLKSPITVEWTGGLEVLFQ
;
;QVYSLIRPNENPAHKGSGGSIEGRGGSGASGDSERHFVYQFMGECYFTNGTQRIRYVTRYIYNREEYVRYDSDVGEHRAV
TELGRPDAEYWNSQPEILERTRAELDTVCRHNYEGPETHTSLRRLEQPNVVISLSRTEALNHHNTLVCSVTDFYPAKIKV
RWFRNGQEETVGVSSTQLIRNGDWTFQVLVMLEMTPRRGEVYTCHVEHPSLKSPITVEWTGGLEVLFQ
;
D ? 
3 'polypeptide(L)' no no 
;MGDSVTQTEGPVTLSEGTSLTVNCSYETKQYPTLFWYVQYPGEGPQLLFKVPKANEKGSSRGFEATYNKEATSFHLQKAS
VQESDSAVYYCALSLNSGGSNAKLTFGKGTKLSVKSHIQNPDPAVYQLRDSKSSDKSVCLFTDFDSQTNVSQSKDSDVYI
TDKCVLDMRSMDFKSNSAVAWSNKSDFACANAFNNSIIPEDTFFPSPESS
;
;MGDSVTQTEGPVTLSEGTSLTVNCSYETKQYPTLFWYVQYPGEGPQLLFKVPKANEKGSSRGFEATYNKEATSFHLQKAS
VQESDSAVYYCALSLNSGGSNAKLTFGKGTKLSVKSHIQNPDPAVYQLRDSKSSDKSVCLFTDFDSQTNVSQSKDSDVYI
TDKCVLDMRSMDFKSNSAVAWSNKSDFACANAFNNSIIPEDTFFPSPESS
;
A ? 
4 'polypeptide(L)' no no 
;MVTLLEQNPRWRLVPRGQAVNLRCILKNSQYPWMSWYQQDLQKQLQWLFTLRSPGDKEVKSLPGADYLATRVTDTELRLQ
VANMSQGRTLYCTCSPQTTEVFFGKGTRLTVVEDLNKVFPPEVAVFEPSEAEISHTQKATLVCLATGFYPDHVELSWWVN
GKEVHSGVCTDPQPLKEQPALNDSRYALSSRLRVSATFWQNPRNHFRCQVQFYGLSENDEWTQDRAKPVTQIVSAEAWGR
AD
;
;MVTLLEQNPRWRLVPRGQAVNLRCILKNSQYPWMSWYQQDLQKQLQWLFTLRSPGDKEVKSLPGADYLATRVTDTELRLQ
VANMSQGRTLYCTCSPQTTEVFFGKGTRLTVVEDLNKVFPPEVAVFEPSEAEISHTQKATLVCLATGFYPDHVELSWWVN
GKEVHSGVCTDPQPLKEQPALNDSRYALSSRLRVSATFWQNPRNHFRCQVQFYGLSENDEWTQDRAKPVTQIVSAEAWGR
AD
;
B ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
5 1,2-ETHANEDIOL                           EDO 
6 2-acetamido-2-deoxy-beta-D-glucopyranose NAG 
7 water                                    HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   ASP n 
1 2   ILE n 
1 3   GLU n 
1 4   ALA n 
1 5   ASP n 
1 6   HIS n 
1 7   VAL n 
1 8   GLY n 
1 9   THR n 
1 10  TYR n 
1 11  GLY n 
1 12  ILE n 
1 13  SER n 
1 14  VAL n 
1 15  TYR n 
1 16  GLN n 
1 17  SER n 
1 18  PRO n 
1 19  GLY n 
1 20  ASP n 
1 21  ILE n 
1 22  GLY n 
1 23  GLN n 
1 24  TYR n 
1 25  THR n 
1 26  PHE n 
1 27  GLU n 
1 28  PHE n 
1 29  ASP n 
1 30  GLY n 
1 31  ASP n 
1 32  GLU n 
1 33  LEU n 
1 34  PHE n 
1 35  TYR n 
1 36  VAL n 
1 37  ASP n 
1 38  LEU n 
1 39  ASP n 
1 40  LYS n 
1 41  LYS n 
1 42  GLU n 
1 43  THR n 
1 44  VAL n 
1 45  TRP n 
1 46  MET n 
1 47  LEU n 
1 48  PRO n 
1 49  GLU n 
1 50  PHE n 
1 51  GLY n 
1 52  GLN n 
1 53  LEU n 
1 54  ALA n 
1 55  SER n 
1 56  PHE n 
1 57  ASP n 
1 58  PRO n 
1 59  GLN n 
1 60  GLY n 
1 61  GLY n 
1 62  LEU n 
1 63  GLN n 
1 64  ASN n 
1 65  ILE n 
1 66  ALA n 
1 67  VAL n 
1 68  VAL n 
1 69  LYS n 
1 70  HIS n 
1 71  ASN n 
1 72  LEU n 
1 73  GLY n 
1 74  VAL n 
1 75  LEU n 
1 76  THR n 
1 77  LYS n 
1 78  ARG n 
1 79  SER n 
1 80  ASN n 
1 81  SER n 
1 82  THR n 
1 83  PRO n 
1 84  ALA n 
1 85  THR n 
1 86  ASN n 
1 87  GLU n 
1 88  ALA n 
1 89  PRO n 
1 90  GLN n 
1 91  ALA n 
1 92  THR n 
1 93  VAL n 
1 94  PHE n 
1 95  PRO n 
1 96  LYS n 
1 97  SER n 
1 98  PRO n 
1 99  VAL n 
1 100 LEU n 
1 101 LEU n 
1 102 GLY n 
1 103 GLN n 
1 104 PRO n 
1 105 ASN n 
1 106 THR n 
1 107 LEU n 
1 108 ILE n 
1 109 CYS n 
1 110 PHE n 
1 111 VAL n 
1 112 ASP n 
1 113 ASN n 
1 114 ILE n 
1 115 PHE n 
1 116 PRO n 
1 117 PRO n 
1 118 VAL n 
1 119 ILE n 
1 120 ASN n 
1 121 ILE n 
1 122 THR n 
1 123 TRP n 
1 124 LEU n 
1 125 ARG n 
1 126 ASN n 
1 127 SER n 
1 128 LYS n 
1 129 SER n 
1 130 VAL n 
1 131 ALA n 
1 132 ASP n 
1 133 GLY n 
1 134 VAL n 
1 135 TYR n 
1 136 GLU n 
1 137 THR n 
1 138 SER n 
1 139 PHE n 
1 140 PHE n 
1 141 VAL n 
1 142 ASN n 
1 143 ARG n 
1 144 ASP n 
1 145 TYR n 
1 146 SER n 
1 147 PHE n 
1 148 HIS n 
1 149 LYS n 
1 150 LEU n 
1 151 SER n 
1 152 TYR n 
1 153 LEU n 
1 154 THR n 
1 155 PHE n 
1 156 ILE n 
1 157 PRO n 
1 158 SER n 
1 159 ASP n 
1 160 ASP n 
1 161 ASP n 
1 162 ILE n 
1 163 TYR n 
1 164 ASP n 
1 165 CYS n 
1 166 LYS n 
1 167 VAL n 
1 168 GLU n 
1 169 HIS n 
1 170 TRP n 
1 171 GLY n 
1 172 LEU n 
1 173 GLU n 
1 174 GLU n 
1 175 PRO n 
1 176 VAL n 
1 177 LEU n 
1 178 LYS n 
1 179 HIS n 
1 180 TRP n 
1 181 THR n 
1 182 SER n 
1 183 GLY n 
1 184 LEU n 
1 185 GLU n 
1 186 VAL n 
1 187 LEU n 
1 188 PHE n 
2 1   GLN n 
2 2   VAL n 
2 3   TYR n 
2 4   SER n 
2 5   LEU n 
2 6   ILE n 
2 7   ARG n 
2 8   PRO n 
2 9   ASN n 
2 10  GLU n 
2 11  ASN n 
2 12  PRO n 
2 13  ALA n 
2 14  HIS n 
2 15  LYS n 
2 16  GLY n 
2 17  SER n 
2 18  GLY n 
2 19  GLY n 
2 20  SER n 
2 21  ILE n 
2 22  GLU n 
2 23  GLY n 
2 24  ARG n 
2 25  GLY n 
2 26  GLY n 
2 27  SER n 
2 28  GLY n 
2 29  ALA n 
2 30  SER n 
2 31  GLY n 
2 32  ASP n 
2 33  SER n 
2 34  GLU n 
2 35  ARG n 
2 36  HIS n 
2 37  PHE n 
2 38  VAL n 
2 39  TYR n 
2 40  GLN n 
2 41  PHE n 
2 42  MET n 
2 43  GLY n 
2 44  GLU n 
2 45  CYS n 
2 46  TYR n 
2 47  PHE n 
2 48  THR n 
2 49  ASN n 
2 50  GLY n 
2 51  THR n 
2 52  GLN n 
2 53  ARG n 
2 54  ILE n 
2 55  ARG n 
2 56  TYR n 
2 57  VAL n 
2 58  THR n 
2 59  ARG n 
2 60  TYR n 
2 61  ILE n 
2 62  TYR n 
2 63  ASN n 
2 64  ARG n 
2 65  GLU n 
2 66  GLU n 
2 67  TYR n 
2 68  VAL n 
2 69  ARG n 
2 70  TYR n 
2 71  ASP n 
2 72  SER n 
2 73  ASP n 
2 74  VAL n 
2 75  GLY n 
2 76  GLU n 
2 77  HIS n 
2 78  ARG n 
2 79  ALA n 
2 80  VAL n 
2 81  THR n 
2 82  GLU n 
2 83  LEU n 
2 84  GLY n 
2 85  ARG n 
2 86  PRO n 
2 87  ASP n 
2 88  ALA n 
2 89  GLU n 
2 90  TYR n 
2 91  TRP n 
2 92  ASN n 
2 93  SER n 
2 94  GLN n 
2 95  PRO n 
2 96  GLU n 
2 97  ILE n 
2 98  LEU n 
2 99  GLU n 
2 100 ARG n 
2 101 THR n 
2 102 ARG n 
2 103 ALA n 
2 104 GLU n 
2 105 LEU n 
2 106 ASP n 
2 107 THR n 
2 108 VAL n 
2 109 CYS n 
2 110 ARG n 
2 111 HIS n 
2 112 ASN n 
2 113 TYR n 
2 114 GLU n 
2 115 GLY n 
2 116 PRO n 
2 117 GLU n 
2 118 THR n 
2 119 HIS n 
2 120 THR n 
2 121 SER n 
2 122 LEU n 
2 123 ARG n 
2 124 ARG n 
2 125 LEU n 
2 126 GLU n 
2 127 GLN n 
2 128 PRO n 
2 129 ASN n 
2 130 VAL n 
2 131 VAL n 
2 132 ILE n 
2 133 SER n 
2 134 LEU n 
2 135 SER n 
2 136 ARG n 
2 137 THR n 
2 138 GLU n 
2 139 ALA n 
2 140 LEU n 
2 141 ASN n 
2 142 HIS n 
2 143 HIS n 
2 144 ASN n 
2 145 THR n 
2 146 LEU n 
2 147 VAL n 
2 148 CYS n 
2 149 SER n 
2 150 VAL n 
2 151 THR n 
2 152 ASP n 
2 153 PHE n 
2 154 TYR n 
2 155 PRO n 
2 156 ALA n 
2 157 LYS n 
2 158 ILE n 
2 159 LYS n 
2 160 VAL n 
2 161 ARG n 
2 162 TRP n 
2 163 PHE n 
2 164 ARG n 
2 165 ASN n 
2 166 GLY n 
2 167 GLN n 
2 168 GLU n 
2 169 GLU n 
2 170 THR n 
2 171 VAL n 
2 172 GLY n 
2 173 VAL n 
2 174 SER n 
2 175 SER n 
2 176 THR n 
2 177 GLN n 
2 178 LEU n 
2 179 ILE n 
2 180 ARG n 
2 181 ASN n 
2 182 GLY n 
2 183 ASP n 
2 184 TRP n 
2 185 THR n 
2 186 PHE n 
2 187 GLN n 
2 188 VAL n 
2 189 LEU n 
2 190 VAL n 
2 191 MET n 
2 192 LEU n 
2 193 GLU n 
2 194 MET n 
2 195 THR n 
2 196 PRO n 
2 197 ARG n 
2 198 ARG n 
2 199 GLY n 
2 200 GLU n 
2 201 VAL n 
2 202 TYR n 
2 203 THR n 
2 204 CYS n 
2 205 HIS n 
2 206 VAL n 
2 207 GLU n 
2 208 HIS n 
2 209 PRO n 
2 210 SER n 
2 211 LEU n 
2 212 LYS n 
2 213 SER n 
2 214 PRO n 
2 215 ILE n 
2 216 THR n 
2 217 VAL n 
2 218 GLU n 
2 219 TRP n 
2 220 THR n 
2 221 GLY n 
2 222 GLY n 
2 223 LEU n 
2 224 GLU n 
2 225 VAL n 
2 226 LEU n 
2 227 PHE n 
2 228 GLN n 
3 1   MET n 
3 2   GLY n 
3 3   ASP n 
3 4   SER n 
3 5   VAL n 
3 6   THR n 
3 7   GLN n 
3 8   THR n 
3 9   GLU n 
3 10  GLY n 
3 11  PRO n 
3 12  VAL n 
3 13  THR n 
3 14  LEU n 
3 15  SER n 
3 16  GLU n 
3 17  GLY n 
3 18  THR n 
3 19  SER n 
3 20  LEU n 
3 21  THR n 
3 22  VAL n 
3 23  ASN n 
3 24  CYS n 
3 25  SER n 
3 26  TYR n 
3 27  GLU n 
3 28  THR n 
3 29  LYS n 
3 30  GLN n 
3 31  TYR n 
3 32  PRO n 
3 33  THR n 
3 34  LEU n 
3 35  PHE n 
3 36  TRP n 
3 37  TYR n 
3 38  VAL n 
3 39  GLN n 
3 40  TYR n 
3 41  PRO n 
3 42  GLY n 
3 43  GLU n 
3 44  GLY n 
3 45  PRO n 
3 46  GLN n 
3 47  LEU n 
3 48  LEU n 
3 49  PHE n 
3 50  LYS n 
3 51  VAL n 
3 52  PRO n 
3 53  LYS n 
3 54  ALA n 
3 55  ASN n 
3 56  GLU n 
3 57  LYS n 
3 58  GLY n 
3 59  SER n 
3 60  SER n 
3 61  ARG n 
3 62  GLY n 
3 63  PHE n 
3 64  GLU n 
3 65  ALA n 
3 66  THR n 
3 67  TYR n 
3 68  ASN n 
3 69  LYS n 
3 70  GLU n 
3 71  ALA n 
3 72  THR n 
3 73  SER n 
3 74  PHE n 
3 75  HIS n 
3 76  LEU n 
3 77  GLN n 
3 78  LYS n 
3 79  ALA n 
3 80  SER n 
3 81  VAL n 
3 82  GLN n 
3 83  GLU n 
3 84  SER n 
3 85  ASP n 
3 86  SER n 
3 87  ALA n 
3 88  VAL n 
3 89  TYR n 
3 90  TYR n 
3 91  CYS n 
3 92  ALA n 
3 93  LEU n 
3 94  SER n 
3 95  LEU n 
3 96  ASN n 
3 97  SER n 
3 98  GLY n 
3 99  GLY n 
3 100 SER n 
3 101 ASN n 
3 102 ALA n 
3 103 LYS n 
3 104 LEU n 
3 105 THR n 
3 106 PHE n 
3 107 GLY n 
3 108 LYS n 
3 109 GLY n 
3 110 THR n 
3 111 LYS n 
3 112 LEU n 
3 113 SER n 
3 114 VAL n 
3 115 LYS n 
3 116 SER n 
3 117 HIS n 
3 118 ILE n 
3 119 GLN n 
3 120 ASN n 
3 121 PRO n 
3 122 ASP n 
3 123 PRO n 
3 124 ALA n 
3 125 VAL n 
3 126 TYR n 
3 127 GLN n 
3 128 LEU n 
3 129 ARG n 
3 130 ASP n 
3 131 SER n 
3 132 LYS n 
3 133 SER n 
3 134 SER n 
3 135 ASP n 
3 136 LYS n 
3 137 SER n 
3 138 VAL n 
3 139 CYS n 
3 140 LEU n 
3 141 PHE n 
3 142 THR n 
3 143 ASP n 
3 144 PHE n 
3 145 ASP n 
3 146 SER n 
3 147 GLN n 
3 148 THR n 
3 149 ASN n 
3 150 VAL n 
3 151 SER n 
3 152 GLN n 
3 153 SER n 
3 154 LYS n 
3 155 ASP n 
3 156 SER n 
3 157 ASP n 
3 158 VAL n 
3 159 TYR n 
3 160 ILE n 
3 161 THR n 
3 162 ASP n 
3 163 LYS n 
3 164 CYS n 
3 165 VAL n 
3 166 LEU n 
3 167 ASP n 
3 168 MET n 
3 169 ARG n 
3 170 SER n 
3 171 MET n 
3 172 ASP n 
3 173 PHE n 
3 174 LYS n 
3 175 SER n 
3 176 ASN n 
3 177 SER n 
3 178 ALA n 
3 179 VAL n 
3 180 ALA n 
3 181 TRP n 
3 182 SER n 
3 183 ASN n 
3 184 LYS n 
3 185 SER n 
3 186 ASP n 
3 187 PHE n 
3 188 ALA n 
3 189 CYS n 
3 190 ALA n 
3 191 ASN n 
3 192 ALA n 
3 193 PHE n 
3 194 ASN n 
3 195 ASN n 
3 196 SER n 
3 197 ILE n 
3 198 ILE n 
3 199 PRO n 
3 200 GLU n 
3 201 ASP n 
3 202 THR n 
3 203 PHE n 
3 204 PHE n 
3 205 PRO n 
3 206 SER n 
3 207 PRO n 
3 208 GLU n 
3 209 SER n 
3 210 SER n 
4 1   MET n 
4 2   VAL n 
4 3   THR n 
4 4   LEU n 
4 5   LEU n 
4 6   GLU n 
4 7   GLN n 
4 8   ASN n 
4 9   PRO n 
4 10  ARG n 
4 11  TRP n 
4 12  ARG n 
4 13  LEU n 
4 14  VAL n 
4 15  PRO n 
4 16  ARG n 
4 17  GLY n 
4 18  GLN n 
4 19  ALA n 
4 20  VAL n 
4 21  ASN n 
4 22  LEU n 
4 23  ARG n 
4 24  CYS n 
4 25  ILE n 
4 26  LEU n 
4 27  LYS n 
4 28  ASN n 
4 29  SER n 
4 30  GLN n 
4 31  TYR n 
4 32  PRO n 
4 33  TRP n 
4 34  MET n 
4 35  SER n 
4 36  TRP n 
4 37  TYR n 
4 38  GLN n 
4 39  GLN n 
4 40  ASP n 
4 41  LEU n 
4 42  GLN n 
4 43  LYS n 
4 44  GLN n 
4 45  LEU n 
4 46  GLN n 
4 47  TRP n 
4 48  LEU n 
4 49  PHE n 
4 50  THR n 
4 51  LEU n 
4 52  ARG n 
4 53  SER n 
4 54  PRO n 
4 55  GLY n 
4 56  ASP n 
4 57  LYS n 
4 58  GLU n 
4 59  VAL n 
4 60  LYS n 
4 61  SER n 
4 62  LEU n 
4 63  PRO n 
4 64  GLY n 
4 65  ALA n 
4 66  ASP n 
4 67  TYR n 
4 68  LEU n 
4 69  ALA n 
4 70  THR n 
4 71  ARG n 
4 72  VAL n 
4 73  THR n 
4 74  ASP n 
4 75  THR n 
4 76  GLU n 
4 77  LEU n 
4 78  ARG n 
4 79  LEU n 
4 80  GLN n 
4 81  VAL n 
4 82  ALA n 
4 83  ASN n 
4 84  MET n 
4 85  SER n 
4 86  GLN n 
4 87  GLY n 
4 88  ARG n 
4 89  THR n 
4 90  LEU n 
4 91  TYR n 
4 92  CYS n 
4 93  THR n 
4 94  CYS n 
4 95  SER n 
4 96  PRO n 
4 97  GLN n 
4 98  THR n 
4 99  THR n 
4 100 GLU n 
4 101 VAL n 
4 102 PHE n 
4 103 PHE n 
4 104 GLY n 
4 105 LYS n 
4 106 GLY n 
4 107 THR n 
4 108 ARG n 
4 109 LEU n 
4 110 THR n 
4 111 VAL n 
4 112 VAL n 
4 113 GLU n 
4 114 ASP n 
4 115 LEU n 
4 116 ASN n 
4 117 LYS n 
4 118 VAL n 
4 119 PHE n 
4 120 PRO n 
4 121 PRO n 
4 122 GLU n 
4 123 VAL n 
4 124 ALA n 
4 125 VAL n 
4 126 PHE n 
4 127 GLU n 
4 128 PRO n 
4 129 SER n 
4 130 GLU n 
4 131 ALA n 
4 132 GLU n 
4 133 ILE n 
4 134 SER n 
4 135 HIS n 
4 136 THR n 
4 137 GLN n 
4 138 LYS n 
4 139 ALA n 
4 140 THR n 
4 141 LEU n 
4 142 VAL n 
4 143 CYS n 
4 144 LEU n 
4 145 ALA n 
4 146 THR n 
4 147 GLY n 
4 148 PHE n 
4 149 TYR n 
4 150 PRO n 
4 151 ASP n 
4 152 HIS n 
4 153 VAL n 
4 154 GLU n 
4 155 LEU n 
4 156 SER n 
4 157 TRP n 
4 158 TRP n 
4 159 VAL n 
4 160 ASN n 
4 161 GLY n 
4 162 LYS n 
4 163 GLU n 
4 164 VAL n 
4 165 HIS n 
4 166 SER n 
4 167 GLY n 
4 168 VAL n 
4 169 CYS n 
4 170 THR n 
4 171 ASP n 
4 172 PRO n 
4 173 GLN n 
4 174 PRO n 
4 175 LEU n 
4 176 LYS n 
4 177 GLU n 
4 178 GLN n 
4 179 PRO n 
4 180 ALA n 
4 181 LEU n 
4 182 ASN n 
4 183 ASP n 
4 184 SER n 
4 185 ARG n 
4 186 TYR n 
4 187 ALA n 
4 188 LEU n 
4 189 SER n 
4 190 SER n 
4 191 ARG n 
4 192 LEU n 
4 193 ARG n 
4 194 VAL n 
4 195 SER n 
4 196 ALA n 
4 197 THR n 
4 198 PHE n 
4 199 TRP n 
4 200 GLN n 
4 201 ASN n 
4 202 PRO n 
4 203 ARG n 
4 204 ASN n 
4 205 HIS n 
4 206 PHE n 
4 207 ARG n 
4 208 CYS n 
4 209 GLN n 
4 210 VAL n 
4 211 GLN n 
4 212 PHE n 
4 213 TYR n 
4 214 GLY n 
4 215 LEU n 
4 216 SER n 
4 217 GLU n 
4 218 ASN n 
4 219 ASP n 
4 220 GLU n 
4 221 TRP n 
4 222 THR n 
4 223 GLN n 
4 224 ASP n 
4 225 ARG n 
4 226 ALA n 
4 227 LYS n 
4 228 PRO n 
4 229 VAL n 
4 230 THR n 
4 231 GLN n 
4 232 ILE n 
4 233 VAL n 
4 234 SER n 
4 235 ALA n 
4 236 GLU n 
4 237 ALA n 
4 238 TRP n 
4 239 GLY n 
4 240 ARG n 
4 241 ALA n 
4 242 ASP n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_entity_src_gen.gene_src_tissue 
_entity_src_gen.gene_src_tissue_fraction 
_entity_src_gen.gene_src_details 
_entity_src_gen.pdbx_gene_src_fragment 
_entity_src_gen.pdbx_gene_src_scientific_name 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_entity_src_gen.pdbx_gene_src_variant 
_entity_src_gen.pdbx_gene_src_cell_line 
_entity_src_gen.pdbx_gene_src_atcc 
_entity_src_gen.pdbx_gene_src_organ 
_entity_src_gen.pdbx_gene_src_organelle 
_entity_src_gen.pdbx_gene_src_cell 
_entity_src_gen.pdbx_gene_src_cellular_location 
_entity_src_gen.host_org_common_name 
_entity_src_gen.pdbx_host_org_scientific_name 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_entity_src_gen.host_org_genus 
_entity_src_gen.pdbx_host_org_gene 
_entity_src_gen.pdbx_host_org_organ 
_entity_src_gen.host_org_species 
_entity_src_gen.pdbx_host_org_tissue 
_entity_src_gen.pdbx_host_org_tissue_fraction 
_entity_src_gen.pdbx_host_org_strain 
_entity_src_gen.pdbx_host_org_variant 
_entity_src_gen.pdbx_host_org_cell_line 
_entity_src_gen.pdbx_host_org_atcc 
_entity_src_gen.pdbx_host_org_culture_collection 
_entity_src_gen.pdbx_host_org_cell 
_entity_src_gen.pdbx_host_org_organelle 
_entity_src_gen.pdbx_host_org_cellular_location 
_entity_src_gen.pdbx_host_org_vector_type 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
1 1 sample 'Biological sequence' 1  188 'house mouse' ? H2-Aa               ? ? ? ? ? ? 'Mus musculus'           10090 ? ? ? ? ? ? 
? ? 'Trichoplusia ni'  7111 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1  15  ?             ? NP                  ? ? ? ? ? ? 'Influenza A virus H3N2' 41857 ? ? ? ? ? ? 
? ? 'Trichoplusia ni'  7111 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 2 sample 'Biological sequence' 16 228 'house mouse' ? 'H2-Ab1, H2-iabeta' ? ? ? ? ? ? 'Mus musculus'           10090 ? ? ? ? ? ? 
? ? 'Trichoplusia ni'  7111 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
3 1 sample 'Biological sequence' 1  210 ?             ? ?                   ? ? ? ? ? ? 'Mus musculus'           10090 ? ? ? ? ? ? 
? ? 'Escherichia coli' 562  ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
4 1 sample 'Biological sequence' 1  242 ?             ? ?                   ? ? ? ? ? ? 'Mus musculus'           10090 ? ? ? ? ? ? 
? ? 'Escherichia coli' 562  ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking'          y ALANINE                                  ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking'          y ARGININE                                 ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking'          y ASPARAGINE                               ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking'          y 'ASPARTIC ACID'                          ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking'          y CYSTEINE                                 ? 'C3 H7 N O2 S'   121.158 
EDO non-polymer                  . 1,2-ETHANEDIOL                           'ETHYLENE GLYCOL' 'C2 H6 O2'       62.068  
GLN 'L-peptide linking'          y GLUTAMINE                                ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking'          y 'GLUTAMIC ACID'                          ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'            y GLYCINE                                  ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking'          y HISTIDINE                                ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer                  . WATER                                    ? 'H2 O'           18.015  
ILE 'L-peptide linking'          y ISOLEUCINE                               ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking'          y LEUCINE                                  ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking'          y LYSINE                                   ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking'          y METHIONINE                               ? 'C5 H11 N O2 S'  149.211 
NAG 'D-saccharide, beta linking' . 2-acetamido-2-deoxy-beta-D-glucopyranose 
;N-acetyl-beta-D-glucosamine; 2-acetamido-2-deoxy-beta-D-glucose; 2-acetamido-2-deoxy-D-glucose; 2-acetamido-2-deoxy-glucose; N-ACETYL-D-GLUCOSAMINE
;
'C8 H15 N O6'    221.208 
PHE 'L-peptide linking'          y PHENYLALANINE                            ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking'          y PROLINE                                  ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking'          y SERINE                                   ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking'          y THREONINE                                ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking'          y TRYPTOPHAN                               ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking'          y TYROSINE                                 ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking'          y VALINE                                   ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_chem_comp_identifier.comp_id 
_pdbx_chem_comp_identifier.type 
_pdbx_chem_comp_identifier.program 
_pdbx_chem_comp_identifier.program_version 
_pdbx_chem_comp_identifier.identifier 
NAG 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DGlcpNAcb                      
NAG 'COMMON NAME'                         GMML     1.0 N-acetyl-b-D-glucopyranosamine 
NAG 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 b-D-GlcpNAc                    
NAG 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 GlcNAc                         
# 
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   ASP 1   1   1   ASP ASP C . n 
A 1 2   ILE 2   2   2   ILE ILE C . n 
A 1 3   GLU 3   3   3   GLU GLU C . n 
A 1 4   ALA 4   4   4   ALA ALA C . n 
A 1 5   ASP 5   5   5   ASP ASP C . n 
A 1 6   HIS 6   6   6   HIS HIS C . n 
A 1 7   VAL 7   7   7   VAL VAL C . n 
A 1 8   GLY 8   8   8   GLY GLY C . n 
A 1 9   THR 9   9   9   THR THR C . n 
A 1 10  TYR 10  10  10  TYR TYR C . n 
A 1 11  GLY 11  11  11  GLY GLY C . n 
A 1 12  ILE 12  12  12  ILE ILE C . n 
A 1 13  SER 13  13  13  SER SER C . n 
A 1 14  VAL 14  14  14  VAL VAL C . n 
A 1 15  TYR 15  15  15  TYR TYR C . n 
A 1 16  GLN 16  16  16  GLN GLN C . n 
A 1 17  SER 17  17  17  SER SER C . n 
A 1 18  PRO 18  18  18  PRO PRO C . n 
A 1 19  GLY 19  19  19  GLY GLY C . n 
A 1 20  ASP 20  20  20  ASP ASP C . n 
A 1 21  ILE 21  21  21  ILE ILE C . n 
A 1 22  GLY 22  22  22  GLY GLY C . n 
A 1 23  GLN 23  23  23  GLN GLN C . n 
A 1 24  TYR 24  24  24  TYR TYR C . n 
A 1 25  THR 25  25  25  THR THR C . n 
A 1 26  PHE 26  26  26  PHE PHE C . n 
A 1 27  GLU 27  27  27  GLU GLU C . n 
A 1 28  PHE 28  28  28  PHE PHE C . n 
A 1 29  ASP 29  29  29  ASP ASP C . n 
A 1 30  GLY 30  30  30  GLY GLY C . n 
A 1 31  ASP 31  31  31  ASP ASP C . n 
A 1 32  GLU 32  32  32  GLU GLU C . n 
A 1 33  LEU 33  33  33  LEU LEU C . n 
A 1 34  PHE 34  34  34  PHE PHE C . n 
A 1 35  TYR 35  35  35  TYR TYR C . n 
A 1 36  VAL 36  36  36  VAL VAL C . n 
A 1 37  ASP 37  37  37  ASP ASP C . n 
A 1 38  LEU 38  38  38  LEU LEU C . n 
A 1 39  ASP 39  39  39  ASP ASP C . n 
A 1 40  LYS 40  40  40  LYS LYS C . n 
A 1 41  LYS 41  41  41  LYS LYS C . n 
A 1 42  GLU 42  42  42  GLU GLU C . n 
A 1 43  THR 43  43  43  THR THR C . n 
A 1 44  VAL 44  44  44  VAL VAL C . n 
A 1 45  TRP 45  45  45  TRP TRP C . n 
A 1 46  MET 46  46  46  MET MET C . n 
A 1 47  LEU 47  47  47  LEU LEU C . n 
A 1 48  PRO 48  48  48  PRO PRO C . n 
A 1 49  GLU 49  49  49  GLU GLU C . n 
A 1 50  PHE 50  50  50  PHE PHE C . n 
A 1 51  GLY 51  51  51  GLY GLY C . n 
A 1 52  GLN 52  52  52  GLN GLN C . n 
A 1 53  LEU 53  53  53  LEU LEU C . n 
A 1 54  ALA 54  54  54  ALA ALA C . n 
A 1 55  SER 55  55  55  SER SER C . n 
A 1 56  PHE 56  56  56  PHE PHE C . n 
A 1 57  ASP 57  57  57  ASP ASP C . n 
A 1 58  PRO 58  58  58  PRO PRO C . n 
A 1 59  GLN 59  59  59  GLN GLN C . n 
A 1 60  GLY 60  60  60  GLY GLY C . n 
A 1 61  GLY 61  61  61  GLY GLY C . n 
A 1 62  LEU 62  62  62  LEU LEU C . n 
A 1 63  GLN 63  63  63  GLN GLN C . n 
A 1 64  ASN 64  64  64  ASN ASN C . n 
A 1 65  ILE 65  65  65  ILE ILE C . n 
A 1 66  ALA 66  66  66  ALA ALA C . n 
A 1 67  VAL 67  67  67  VAL VAL C . n 
A 1 68  VAL 68  68  68  VAL VAL C . n 
A 1 69  LYS 69  69  69  LYS LYS C . n 
A 1 70  HIS 70  70  70  HIS HIS C . n 
A 1 71  ASN 71  71  71  ASN ASN C . n 
A 1 72  LEU 72  72  72  LEU LEU C . n 
A 1 73  GLY 73  73  73  GLY GLY C . n 
A 1 74  VAL 74  74  74  VAL VAL C . n 
A 1 75  LEU 75  75  75  LEU LEU C . n 
A 1 76  THR 76  76  76  THR THR C . n 
A 1 77  LYS 77  77  77  LYS LYS C . n 
A 1 78  ARG 78  78  78  ARG ARG C . n 
A 1 79  SER 79  79  79  SER SER C . n 
A 1 80  ASN 80  80  80  ASN ASN C . n 
A 1 81  SER 81  81  81  SER SER C . n 
A 1 82  THR 82  82  82  THR THR C . n 
A 1 83  PRO 83  83  83  PRO PRO C . n 
A 1 84  ALA 84  84  84  ALA ALA C . n 
A 1 85  THR 85  85  85  THR THR C . n 
A 1 86  ASN 86  86  86  ASN ASN C . n 
A 1 87  GLU 87  87  87  GLU GLU C . n 
A 1 88  ALA 88  88  88  ALA ALA C . n 
A 1 89  PRO 89  89  89  PRO PRO C . n 
A 1 90  GLN 90  90  90  GLN GLN C . n 
A 1 91  ALA 91  91  91  ALA ALA C . n 
A 1 92  THR 92  92  92  THR THR C . n 
A 1 93  VAL 93  93  93  VAL VAL C . n 
A 1 94  PHE 94  94  94  PHE PHE C . n 
A 1 95  PRO 95  95  95  PRO PRO C . n 
A 1 96  LYS 96  96  96  LYS LYS C . n 
A 1 97  SER 97  97  97  SER SER C . n 
A 1 98  PRO 98  98  98  PRO PRO C . n 
A 1 99  VAL 99  99  99  VAL VAL C . n 
A 1 100 LEU 100 100 100 LEU LEU C . n 
A 1 101 LEU 101 101 101 LEU LEU C . n 
A 1 102 GLY 102 102 102 GLY GLY C . n 
A 1 103 GLN 103 103 103 GLN GLN C . n 
A 1 104 PRO 104 104 104 PRO PRO C . n 
A 1 105 ASN 105 105 105 ASN ASN C . n 
A 1 106 THR 106 106 106 THR THR C . n 
A 1 107 LEU 107 107 107 LEU LEU C . n 
A 1 108 ILE 108 108 108 ILE ILE C . n 
A 1 109 CYS 109 109 109 CYS CYS C . n 
A 1 110 PHE 110 110 110 PHE PHE C . n 
A 1 111 VAL 111 111 111 VAL VAL C . n 
A 1 112 ASP 112 112 112 ASP ASP C . n 
A 1 113 ASN 113 113 113 ASN ASN C . n 
A 1 114 ILE 114 114 114 ILE ILE C . n 
A 1 115 PHE 115 115 115 PHE PHE C . n 
A 1 116 PRO 116 116 116 PRO PRO C . n 
A 1 117 PRO 117 117 117 PRO PRO C . n 
A 1 118 VAL 118 118 118 VAL VAL C . n 
A 1 119 ILE 119 119 119 ILE ILE C . n 
A 1 120 ASN 120 120 120 ASN ASN C . n 
A 1 121 ILE 121 121 121 ILE ILE C . n 
A 1 122 THR 122 122 122 THR THR C . n 
A 1 123 TRP 123 123 123 TRP TRP C . n 
A 1 124 LEU 124 124 124 LEU LEU C . n 
A 1 125 ARG 125 125 125 ARG ARG C . n 
A 1 126 ASN 126 126 126 ASN ASN C . n 
A 1 127 SER 127 127 127 SER SER C . n 
A 1 128 LYS 128 128 128 LYS LYS C . n 
A 1 129 SER 129 129 129 SER SER C . n 
A 1 130 VAL 130 130 130 VAL VAL C . n 
A 1 131 ALA 131 131 131 ALA ALA C . n 
A 1 132 ASP 132 132 132 ASP ASP C . n 
A 1 133 GLY 133 133 133 GLY GLY C . n 
A 1 134 VAL 134 134 134 VAL VAL C . n 
A 1 135 TYR 135 135 135 TYR TYR C . n 
A 1 136 GLU 136 136 136 GLU GLU C . n 
A 1 137 THR 137 137 137 THR THR C . n 
A 1 138 SER 138 138 138 SER SER C . n 
A 1 139 PHE 139 139 139 PHE PHE C . n 
A 1 140 PHE 140 140 140 PHE PHE C . n 
A 1 141 VAL 141 141 141 VAL VAL C . n 
A 1 142 ASN 142 142 142 ASN ASN C . n 
A 1 143 ARG 143 143 143 ARG ARG C . n 
A 1 144 ASP 144 144 144 ASP ASP C . n 
A 1 145 TYR 145 145 145 TYR TYR C . n 
A 1 146 SER 146 146 146 SER SER C . n 
A 1 147 PHE 147 147 147 PHE PHE C . n 
A 1 148 HIS 148 148 148 HIS HIS C . n 
A 1 149 LYS 149 149 149 LYS LYS C . n 
A 1 150 LEU 150 150 150 LEU LEU C . n 
A 1 151 SER 151 151 151 SER SER C . n 
A 1 152 TYR 152 152 152 TYR TYR C . n 
A 1 153 LEU 153 153 153 LEU LEU C . n 
A 1 154 THR 154 154 154 THR THR C . n 
A 1 155 PHE 155 155 155 PHE PHE C . n 
A 1 156 ILE 156 156 156 ILE ILE C . n 
A 1 157 PRO 157 157 157 PRO PRO C . n 
A 1 158 SER 158 158 158 SER SER C . n 
A 1 159 ASP 159 159 159 ASP ASP C . n 
A 1 160 ASP 160 160 160 ASP ASP C . n 
A 1 161 ASP 161 161 161 ASP ASP C . n 
A 1 162 ILE 162 162 162 ILE ILE C . n 
A 1 163 TYR 163 163 163 TYR TYR C . n 
A 1 164 ASP 164 164 164 ASP ASP C . n 
A 1 165 CYS 165 165 165 CYS CYS C . n 
A 1 166 LYS 166 166 166 LYS LYS C . n 
A 1 167 VAL 167 167 167 VAL VAL C . n 
A 1 168 GLU 168 168 168 GLU GLU C . n 
A 1 169 HIS 169 169 169 HIS HIS C . n 
A 1 170 TRP 170 170 170 TRP TRP C . n 
A 1 171 GLY 171 171 171 GLY GLY C . n 
A 1 172 LEU 172 172 172 LEU LEU C . n 
A 1 173 GLU 173 173 173 GLU GLU C . n 
A 1 174 GLU 174 174 174 GLU GLU C . n 
A 1 175 PRO 175 175 175 PRO PRO C . n 
A 1 176 VAL 176 176 176 VAL VAL C . n 
A 1 177 LEU 177 177 177 LEU LEU C . n 
A 1 178 LYS 178 178 178 LYS LYS C . n 
A 1 179 HIS 179 179 179 HIS HIS C . n 
A 1 180 TRP 180 180 180 TRP TRP C . n 
A 1 181 THR 181 181 181 THR THR C . n 
A 1 182 SER 182 182 182 SER SER C . n 
A 1 183 GLY 183 183 183 GLY GLY C . n 
A 1 184 LEU 184 184 184 LEU LEU C . n 
A 1 185 GLU 185 185 185 GLU GLU C . n 
A 1 186 VAL 186 186 186 VAL VAL C . n 
A 1 187 LEU 187 187 ?   ?   ?   C . n 
A 1 188 PHE 188 188 ?   ?   ?   C . n 
B 2 1   GLN 1   -25 -25 GLN GLN D . n 
B 2 2   VAL 2   -24 -24 VAL VAL D . n 
B 2 3   TYR 3   -23 -23 TYR TYR D . n 
B 2 4   SER 4   -22 -22 SER SER D . n 
B 2 5   LEU 5   -21 -21 LEU LEU D . n 
B 2 6   ILE 6   -20 -20 ILE ILE D . n 
B 2 7   ARG 7   -19 -19 ARG ARG D . n 
B 2 8   PRO 8   -18 -18 PRO PRO D . n 
B 2 9   ASN 9   -17 -17 ASN ASN D . n 
B 2 10  GLU 10  -16 -16 GLU GLU D . n 
B 2 11  ASN 11  -15 -15 ASN ASN D . n 
B 2 12  PRO 12  -14 -14 PRO PRO D . n 
B 2 13  ALA 13  -13 -13 ALA ALA D . n 
B 2 14  HIS 14  -13 ?   ?   ?   D A n 
B 2 15  LYS 15  -13 ?   ?   ?   D B n 
B 2 16  GLY 16  -13 ?   ?   ?   D C n 
B 2 17  SER 17  -13 ?   ?   ?   D D n 
B 2 18  GLY 18  -13 ?   ?   ?   D E n 
B 2 19  GLY 19  -13 ?   ?   ?   D F n 
B 2 20  SER 20  -13 ?   ?   ?   D G n 
B 2 21  ILE 21  -13 ?   ?   ?   D H n 
B 2 22  GLU 22  -13 ?   ?   ?   D I n 
B 2 23  GLY 23  -13 ?   ?   ?   D J n 
B 2 24  ARG 24  -13 ?   ?   ?   D K n 
B 2 25  GLY 25  -13 ?   ?   ?   D L n 
B 2 26  GLY 26  -13 ?   ?   ?   D M n 
B 2 27  SER 27  -13 ?   ?   ?   D N n 
B 2 28  GLY 28  -13 ?   ?   ?   D O n 
B 2 29  ALA 29  -13 ?   ?   ?   D P n 
B 2 30  SER 30  -13 ?   ?   ?   D Q n 
B 2 31  GLY 31  -13 ?   ?   ?   D R n 
B 2 32  ASP 32  -13 ?   ?   ?   D S n 
B 2 33  SER 33  -13 ?   ?   ?   D T n 
B 2 34  GLU 34  -13 ?   ?   ?   D U n 
B 2 35  ARG 35  2   2   ARG ARG D . n 
B 2 36  HIS 36  3   3   HIS HIS D . n 
B 2 37  PHE 37  4   4   PHE PHE D . n 
B 2 38  VAL 38  5   5   VAL VAL D . n 
B 2 39  TYR 39  6   6   TYR TYR D . n 
B 2 40  GLN 40  7   7   GLN GLN D . n 
B 2 41  PHE 41  8   8   PHE PHE D . n 
B 2 42  MET 42  9   9   MET MET D . n 
B 2 43  GLY 43  10  10  GLY GLY D . n 
B 2 44  GLU 44  11  11  GLU GLU D . n 
B 2 45  CYS 45  12  12  CYS CYS D . n 
B 2 46  TYR 46  13  13  TYR TYR D . n 
B 2 47  PHE 47  14  14  PHE PHE D . n 
B 2 48  THR 48  15  15  THR THR D . n 
B 2 49  ASN 49  16  16  ASN ASN D . n 
B 2 50  GLY 50  17  17  GLY GLY D . n 
B 2 51  THR 51  18  18  THR THR D . n 
B 2 52  GLN 52  19  19  GLN GLN D . n 
B 2 53  ARG 53  20  20  ARG ARG D . n 
B 2 54  ILE 54  21  21  ILE ILE D . n 
B 2 55  ARG 55  22  22  ARG ARG D . n 
B 2 56  TYR 56  23  23  TYR TYR D . n 
B 2 57  VAL 57  24  24  VAL VAL D . n 
B 2 58  THR 58  25  25  THR THR D . n 
B 2 59  ARG 59  26  26  ARG ARG D . n 
B 2 60  TYR 60  27  27  TYR TYR D . n 
B 2 61  ILE 61  28  28  ILE ILE D . n 
B 2 62  TYR 62  29  29  TYR TYR D . n 
B 2 63  ASN 63  30  30  ASN ASN D . n 
B 2 64  ARG 64  31  31  ARG ARG D . n 
B 2 65  GLU 65  32  32  GLU GLU D . n 
B 2 66  GLU 66  33  33  GLU GLU D . n 
B 2 67  TYR 67  34  34  TYR TYR D . n 
B 2 68  VAL 68  35  35  VAL VAL D . n 
B 2 69  ARG 69  36  36  ARG ARG D . n 
B 2 70  TYR 70  37  37  TYR TYR D . n 
B 2 71  ASP 71  38  38  ASP ASP D . n 
B 2 72  SER 72  39  39  SER SER D . n 
B 2 73  ASP 73  40  40  ASP ASP D . n 
B 2 74  VAL 74  41  41  VAL VAL D . n 
B 2 75  GLY 75  42  42  GLY GLY D . n 
B 2 76  GLU 76  43  43  GLU GLU D . n 
B 2 77  HIS 77  44  44  HIS HIS D . n 
B 2 78  ARG 78  45  45  ARG ARG D . n 
B 2 79  ALA 79  46  46  ALA ALA D . n 
B 2 80  VAL 80  47  47  VAL VAL D . n 
B 2 81  THR 81  48  48  THR THR D . n 
B 2 82  GLU 82  49  49  GLU GLU D . n 
B 2 83  LEU 83  50  50  LEU LEU D . n 
B 2 84  GLY 84  51  51  GLY GLY D . n 
B 2 85  ARG 85  52  52  ARG ARG D . n 
B 2 86  PRO 86  53  53  PRO PRO D . n 
B 2 87  ASP 87  54  54  ASP ASP D . n 
B 2 88  ALA 88  55  55  ALA ALA D . n 
B 2 89  GLU 89  56  56  GLU GLU D . n 
B 2 90  TYR 90  57  57  TYR TYR D . n 
B 2 91  TRP 91  58  58  TRP TRP D . n 
B 2 92  ASN 92  59  59  ASN ASN D . n 
B 2 93  SER 93  60  60  SER SER D . n 
B 2 94  GLN 94  61  61  GLN GLN D . n 
B 2 95  PRO 95  62  62  PRO PRO D . n 
B 2 96  GLU 96  63  63  GLU GLU D . n 
B 2 97  ILE 97  64  64  ILE ILE D . n 
B 2 98  LEU 98  65  65  LEU LEU D . n 
B 2 99  GLU 99  66  66  GLU GLU D . n 
B 2 100 ARG 100 67  67  ARG ARG D . n 
B 2 101 THR 101 68  68  THR THR D . n 
B 2 102 ARG 102 69  69  ARG ARG D . n 
B 2 103 ALA 103 70  70  ALA ALA D . n 
B 2 104 GLU 104 71  71  GLU GLU D . n 
B 2 105 LEU 105 72  72  LEU LEU D . n 
B 2 106 ASP 106 73  73  ASP ASP D . n 
B 2 107 THR 107 74  74  THR THR D . n 
B 2 108 VAL 108 75  75  VAL VAL D . n 
B 2 109 CYS 109 76  76  CYS CYS D . n 
B 2 110 ARG 110 77  77  ARG ARG D . n 
B 2 111 HIS 111 78  78  HIS HIS D . n 
B 2 112 ASN 112 79  79  ASN ASN D . n 
B 2 113 TYR 113 80  80  TYR TYR D . n 
B 2 114 GLU 114 81  81  GLU GLU D . n 
B 2 115 GLY 115 82  82  GLY GLY D . n 
B 2 116 PRO 116 83  83  PRO PRO D . n 
B 2 117 GLU 117 84  84  GLU GLU D . n 
B 2 118 THR 118 85  85  THR THR D . n 
B 2 119 HIS 119 86  86  HIS HIS D . n 
B 2 120 THR 120 87  87  THR THR D . n 
B 2 121 SER 121 88  88  SER SER D . n 
B 2 122 LEU 122 89  89  LEU LEU D . n 
B 2 123 ARG 123 90  90  ARG ARG D . n 
B 2 124 ARG 124 91  91  ARG ARG D . n 
B 2 125 LEU 125 92  92  LEU LEU D . n 
B 2 126 GLU 126 93  93  GLU GLU D . n 
B 2 127 GLN 127 94  94  GLN GLN D . n 
B 2 128 PRO 128 95  95  PRO PRO D . n 
B 2 129 ASN 129 96  96  ASN ASN D . n 
B 2 130 VAL 130 97  97  VAL VAL D . n 
B 2 131 VAL 131 98  98  VAL VAL D . n 
B 2 132 ILE 132 99  99  ILE ILE D . n 
B 2 133 SER 133 100 100 SER SER D . n 
B 2 134 LEU 134 101 101 LEU LEU D . n 
B 2 135 SER 135 102 102 SER SER D . n 
B 2 136 ARG 136 103 103 ARG ARG D . n 
B 2 137 THR 137 104 104 THR THR D . n 
B 2 138 GLU 138 105 ?   ?   ?   D . n 
B 2 139 ALA 139 106 ?   ?   ?   D . n 
B 2 140 LEU 140 107 ?   ?   ?   D . n 
B 2 141 ASN 141 108 ?   ?   ?   D . n 
B 2 142 HIS 142 109 ?   ?   ?   D . n 
B 2 143 HIS 143 110 ?   ?   ?   D . n 
B 2 144 ASN 144 111 ?   ?   ?   D . n 
B 2 145 THR 145 112 112 THR THR D . n 
B 2 146 LEU 146 113 113 LEU LEU D . n 
B 2 147 VAL 147 114 114 VAL VAL D . n 
B 2 148 CYS 148 115 115 CYS CYS D . n 
B 2 149 SER 149 116 116 SER SER D . n 
B 2 150 VAL 150 117 117 VAL VAL D . n 
B 2 151 THR 151 118 118 THR THR D . n 
B 2 152 ASP 152 119 119 ASP ASP D . n 
B 2 153 PHE 153 120 120 PHE PHE D . n 
B 2 154 TYR 154 121 121 TYR TYR D . n 
B 2 155 PRO 155 122 122 PRO PRO D . n 
B 2 156 ALA 156 123 123 ALA ALA D . n 
B 2 157 LYS 157 124 124 LYS LYS D . n 
B 2 158 ILE 158 125 125 ILE ILE D . n 
B 2 159 LYS 159 126 126 LYS LYS D . n 
B 2 160 VAL 160 127 127 VAL VAL D . n 
B 2 161 ARG 161 128 128 ARG ARG D . n 
B 2 162 TRP 162 129 129 TRP TRP D . n 
B 2 163 PHE 163 130 130 PHE PHE D . n 
B 2 164 ARG 164 131 131 ARG ARG D . n 
B 2 165 ASN 165 132 132 ASN ASN D . n 
B 2 166 GLY 166 133 133 GLY GLY D . n 
B 2 167 GLN 167 134 134 GLN GLN D . n 
B 2 168 GLU 168 135 135 GLU GLU D . n 
B 2 169 GLU 169 136 136 GLU GLU D . n 
B 2 170 THR 170 137 137 THR THR D . n 
B 2 171 VAL 171 138 ?   ?   ?   D . n 
B 2 172 GLY 172 139 ?   ?   ?   D . n 
B 2 173 VAL 173 140 140 VAL VAL D . n 
B 2 174 SER 174 141 141 SER SER D . n 
B 2 175 SER 175 142 142 SER SER D . n 
B 2 176 THR 176 143 143 THR THR D . n 
B 2 177 GLN 177 144 144 GLN GLN D . n 
B 2 178 LEU 178 145 145 LEU LEU D . n 
B 2 179 ILE 179 146 146 ILE ILE D . n 
B 2 180 ARG 180 147 147 ARG ARG D . n 
B 2 181 ASN 181 148 148 ASN ASN D . n 
B 2 182 GLY 182 149 149 GLY GLY D . n 
B 2 183 ASP 183 150 150 ASP ASP D . n 
B 2 184 TRP 184 151 151 TRP TRP D . n 
B 2 185 THR 185 152 152 THR THR D . n 
B 2 186 PHE 186 153 153 PHE PHE D . n 
B 2 187 GLN 187 154 154 GLN GLN D . n 
B 2 188 VAL 188 155 155 VAL VAL D . n 
B 2 189 LEU 189 156 156 LEU LEU D . n 
B 2 190 VAL 190 157 157 VAL VAL D . n 
B 2 191 MET 191 158 158 MET MET D . n 
B 2 192 LEU 192 159 159 LEU LEU D . n 
B 2 193 GLU 193 160 160 GLU GLU D . n 
B 2 194 MET 194 161 161 MET MET D . n 
B 2 195 THR 195 162 162 THR THR D . n 
B 2 196 PRO 196 163 ?   ?   ?   D . n 
B 2 197 ARG 197 164 ?   ?   ?   D . n 
B 2 198 ARG 198 165 ?   ?   ?   D . n 
B 2 199 GLY 199 166 ?   ?   ?   D . n 
B 2 200 GLU 200 167 ?   ?   ?   D . n 
B 2 201 VAL 201 168 168 VAL VAL D . n 
B 2 202 TYR 202 169 169 TYR TYR D . n 
B 2 203 THR 203 170 170 THR THR D . n 
B 2 204 CYS 204 171 171 CYS CYS D . n 
B 2 205 HIS 205 172 172 HIS HIS D . n 
B 2 206 VAL 206 173 173 VAL VAL D . n 
B 2 207 GLU 207 174 174 GLU GLU D . n 
B 2 208 HIS 208 175 175 HIS HIS D . n 
B 2 209 PRO 209 176 176 PRO PRO D . n 
B 2 210 SER 210 177 177 SER SER D . n 
B 2 211 LEU 211 178 178 LEU LEU D . n 
B 2 212 LYS 212 179 179 LYS LYS D . n 
B 2 213 SER 213 180 180 SER SER D . n 
B 2 214 PRO 214 181 181 PRO PRO D . n 
B 2 215 ILE 215 182 182 ILE ILE D . n 
B 2 216 THR 216 183 183 THR THR D . n 
B 2 217 VAL 217 184 184 VAL VAL D . n 
B 2 218 GLU 218 185 185 GLU GLU D . n 
B 2 219 TRP 219 186 186 TRP TRP D . n 
B 2 220 THR 220 187 187 THR THR D . n 
B 2 221 GLY 221 188 188 GLY GLY D . n 
B 2 222 GLY 222 189 ?   ?   ?   D . n 
B 2 223 LEU 223 190 ?   ?   ?   D . n 
B 2 224 GLU 224 191 ?   ?   ?   D . n 
B 2 225 VAL 225 192 ?   ?   ?   D . n 
B 2 226 LEU 226 193 ?   ?   ?   D . n 
B 2 227 PHE 227 194 ?   ?   ?   D . n 
B 2 228 GLN 228 195 ?   ?   ?   D . n 
C 3 1   MET 1   0   ?   ?   ?   A . n 
C 3 2   GLY 2   1   1   GLY GLY A . n 
C 3 3   ASP 3   2   2   ASP ASP A . n 
C 3 4   SER 4   3   3   SER SER A . n 
C 3 5   VAL 5   4   4   VAL VAL A . n 
C 3 6   THR 6   5   5   THR THR A . n 
C 3 7   GLN 7   6   6   GLN GLN A . n 
C 3 8   THR 8   7   7   THR THR A . n 
C 3 9   GLU 9   8   8   GLU GLU A . n 
C 3 10  GLY 10  9   9   GLY GLY A . n 
C 3 11  PRO 11  10  10  PRO PRO A . n 
C 3 12  VAL 12  11  11  VAL VAL A . n 
C 3 13  THR 13  12  12  THR THR A . n 
C 3 14  LEU 14  13  13  LEU LEU A . n 
C 3 15  SER 15  14  14  SER SER A . n 
C 3 16  GLU 16  15  15  GLU GLU A . n 
C 3 17  GLY 17  16  16  GLY GLY A . n 
C 3 18  THR 18  17  17  THR THR A . n 
C 3 19  SER 19  18  18  SER SER A . n 
C 3 20  LEU 20  19  19  LEU LEU A . n 
C 3 21  THR 21  20  20  THR THR A . n 
C 3 22  VAL 22  21  21  VAL VAL A . n 
C 3 23  ASN 23  22  22  ASN ASN A . n 
C 3 24  CYS 24  23  23  CYS CYS A . n 
C 3 25  SER 25  24  24  SER SER A . n 
C 3 26  TYR 26  25  25  TYR TYR A . n 
C 3 27  GLU 27  26  26  GLU GLU A . n 
C 3 28  THR 28  27  27  THR THR A . n 
C 3 29  LYS 29  28  28  LYS LYS A . n 
C 3 30  GLN 30  29  29  GLN GLN A . n 
C 3 31  TYR 31  36  36  TYR TYR A . n 
C 3 32  PRO 32  37  37  PRO PRO A . n 
C 3 33  THR 33  38  38  THR THR A . n 
C 3 34  LEU 34  39  39  LEU LEU A . n 
C 3 35  PHE 35  40  40  PHE PHE A . n 
C 3 36  TRP 36  41  41  TRP TRP A . n 
C 3 37  TYR 37  42  42  TYR TYR A . n 
C 3 38  VAL 38  43  43  VAL VAL A . n 
C 3 39  GLN 39  44  44  GLN GLN A . n 
C 3 40  TYR 40  45  45  TYR TYR A . n 
C 3 41  PRO 41  46  46  PRO PRO A . n 
C 3 42  GLY 42  47  47  GLY GLY A . n 
C 3 43  GLU 43  48  48  GLU GLU A . n 
C 3 44  GLY 44  49  49  GLY GLY A . n 
C 3 45  PRO 45  50  50  PRO PRO A . n 
C 3 46  GLN 46  51  51  GLN GLN A . n 
C 3 47  LEU 47  52  52  LEU LEU A . n 
C 3 48  LEU 48  53  53  LEU LEU A . n 
C 3 49  PHE 49  54  54  PHE PHE A . n 
C 3 50  LYS 50  55  55  LYS LYS A . n 
C 3 51  VAL 51  56  56  VAL VAL A . n 
C 3 52  PRO 52  57  57  PRO PRO A . n 
C 3 53  LYS 53  58  58  LYS LYS A . n 
C 3 54  ALA 54  59  59  ALA ALA A . n 
C 3 55  ASN 55  63  63  ASN ASN A . n 
C 3 56  GLU 56  64  64  GLU GLU A . n 
C 3 57  LYS 57  65  65  LYS LYS A . n 
C 3 58  GLY 58  66  66  GLY GLY A . n 
C 3 59  SER 59  67  67  SER SER A . n 
C 3 60  SER 60  68  68  SER SER A . n 
C 3 61  ARG 61  74  74  ARG ARG A . n 
C 3 62  GLY 62  75  75  GLY GLY A . n 
C 3 63  PHE 63  76  76  PHE PHE A . n 
C 3 64  GLU 64  77  77  GLU GLU A . n 
C 3 65  ALA 65  78  78  ALA ALA A . n 
C 3 66  THR 66  79  79  THR THR A . n 
C 3 67  TYR 67  80  80  TYR TYR A . n 
C 3 68  ASN 68  81  81  ASN ASN A . n 
C 3 69  LYS 69  82  82  LYS LYS A . n 
C 3 70  GLU 70  83  83  GLU GLU A . n 
C 3 71  ALA 71  84  84  ALA ALA A . n 
C 3 72  THR 72  85  85  THR THR A . n 
C 3 73  SER 73  86  86  SER SER A . n 
C 3 74  PHE 74  87  87  PHE PHE A . n 
C 3 75  HIS 75  88  88  HIS HIS A . n 
C 3 76  LEU 76  89  89  LEU LEU A . n 
C 3 77  GLN 77  90  90  GLN GLN A . n 
C 3 78  LYS 78  91  91  LYS LYS A . n 
C 3 79  ALA 79  92  92  ALA ALA A . n 
C 3 80  SER 80  93  93  SER SER A . n 
C 3 81  VAL 81  94  94  VAL VAL A . n 
C 3 82  GLN 82  95  95  GLN GLN A . n 
C 3 83  GLU 83  96  96  GLU GLU A . n 
C 3 84  SER 84  97  97  SER SER A . n 
C 3 85  ASP 85  98  98  ASP ASP A . n 
C 3 86  SER 86  99  99  SER SER A . n 
C 3 87  ALA 87  100 100 ALA ALA A . n 
C 3 88  VAL 88  101 101 VAL VAL A . n 
C 3 89  TYR 89  102 102 TYR TYR A . n 
C 3 90  TYR 90  103 103 TYR TYR A . n 
C 3 91  CYS 91  104 104 CYS CYS A . n 
C 3 92  ALA 92  105 105 ALA ALA A . n 
C 3 93  LEU 93  106 106 LEU LEU A . n 
C 3 94  SER 94  107 107 SER SER A . n 
C 3 95  LEU 95  108 108 LEU LEU A . n 
C 3 96  ASN 96  109 109 ASN ASN A . n 
C 3 97  SER 97  110 110 SER SER A . n 
C 3 98  GLY 98  111 111 GLY GLY A . n 
C 3 99  GLY 99  112 112 GLY GLY A . n 
C 3 100 SER 100 113 113 SER SER A . n 
C 3 101 ASN 101 114 114 ASN ASN A . n 
C 3 102 ALA 102 115 115 ALA ALA A . n 
C 3 103 LYS 103 116 116 LYS LYS A . n 
C 3 104 LEU 104 117 117 LEU LEU A . n 
C 3 105 THR 105 118 118 THR THR A . n 
C 3 106 PHE 106 119 119 PHE PHE A . n 
C 3 107 GLY 107 120 120 GLY GLY A . n 
C 3 108 LYS 108 121 121 LYS LYS A . n 
C 3 109 GLY 109 122 122 GLY GLY A . n 
C 3 110 THR 110 123 123 THR THR A . n 
C 3 111 LYS 111 124 124 LYS LYS A . n 
C 3 112 LEU 112 125 125 LEU LEU A . n 
C 3 113 SER 113 126 126 SER SER A . n 
C 3 114 VAL 114 127 127 VAL VAL A . n 
C 3 115 LYS 115 128 128 LYS LYS A . n 
C 3 116 SER 116 129 129 SER SER A . n 
C 3 117 HIS 117 130 130 HIS HIS A . n 
C 3 118 ILE 118 131 131 ILE ILE A . n 
C 3 119 GLN 119 132 ?   ?   ?   A . n 
C 3 120 ASN 120 133 ?   ?   ?   A . n 
C 3 121 PRO 121 134 134 PRO PRO A . n 
C 3 122 ASP 122 135 135 ASP ASP A . n 
C 3 123 PRO 123 136 136 PRO PRO A . n 
C 3 124 ALA 124 137 137 ALA ALA A . n 
C 3 125 VAL 125 138 138 VAL VAL A . n 
C 3 126 TYR 126 139 139 TYR TYR A . n 
C 3 127 GLN 127 140 140 GLN GLN A . n 
C 3 128 LEU 128 141 141 LEU LEU A . n 
C 3 129 ARG 129 142 142 ARG ARG A . n 
C 3 130 ASP 130 143 143 ASP ASP A . n 
C 3 131 SER 131 144 144 SER SER A . n 
C 3 132 LYS 132 145 145 LYS LYS A . n 
C 3 133 SER 133 146 146 SER SER A . n 
C 3 134 SER 134 147 ?   ?   ?   A . n 
C 3 135 ASP 135 148 ?   ?   ?   A . n 
C 3 136 LYS 136 149 149 LYS LYS A . n 
C 3 137 SER 137 150 150 SER SER A . n 
C 3 138 VAL 138 151 151 VAL VAL A . n 
C 3 139 CYS 139 152 152 CYS CYS A . n 
C 3 140 LEU 140 153 153 LEU LEU A . n 
C 3 141 PHE 141 154 154 PHE PHE A . n 
C 3 142 THR 142 155 155 THR THR A . n 
C 3 143 ASP 143 156 156 ASP ASP A . n 
C 3 144 PHE 144 157 157 PHE PHE A . n 
C 3 145 ASP 145 158 158 ASP ASP A . n 
C 3 146 SER 146 159 ?   ?   ?   A . n 
C 3 147 GLN 147 160 ?   ?   ?   A . n 
C 3 148 THR 148 161 ?   ?   ?   A . n 
C 3 149 ASN 149 162 ?   ?   ?   A . n 
C 3 150 VAL 150 163 ?   ?   ?   A . n 
C 3 151 SER 151 164 ?   ?   ?   A . n 
C 3 152 GLN 152 165 ?   ?   ?   A . n 
C 3 153 SER 153 166 166 SER SER A . n 
C 3 154 LYS 154 167 167 LYS LYS A . n 
C 3 155 ASP 155 168 168 ASP ASP A . n 
C 3 156 SER 156 169 169 SER SER A . n 
C 3 157 ASP 157 170 170 ASP ASP A . n 
C 3 158 VAL 158 171 171 VAL VAL A . n 
C 3 159 TYR 159 172 172 TYR TYR A . n 
C 3 160 ILE 160 173 173 ILE ILE A . n 
C 3 161 THR 161 174 174 THR THR A . n 
C 3 162 ASP 162 175 175 ASP ASP A . n 
C 3 163 LYS 163 176 176 LYS LYS A . n 
C 3 164 CYS 164 177 177 CYS CYS A . n 
C 3 165 VAL 165 178 178 VAL VAL A . n 
C 3 166 LEU 166 179 179 LEU LEU A . n 
C 3 167 ASP 167 180 ?   ?   ?   A . n 
C 3 168 MET 168 181 ?   ?   ?   A . n 
C 3 169 ARG 169 182 ?   ?   ?   A . n 
C 3 170 SER 170 183 ?   ?   ?   A . n 
C 3 171 MET 171 184 ?   ?   ?   A . n 
C 3 172 ASP 172 185 ?   ?   ?   A . n 
C 3 173 PHE 173 186 ?   ?   ?   A . n 
C 3 174 LYS 174 187 187 LYS LYS A . n 
C 3 175 SER 175 188 188 SER SER A . n 
C 3 176 ASN 176 189 189 ASN ASN A . n 
C 3 177 SER 177 190 190 SER SER A . n 
C 3 178 ALA 178 191 191 ALA ALA A . n 
C 3 179 VAL 179 192 192 VAL VAL A . n 
C 3 180 ALA 180 193 193 ALA ALA A . n 
C 3 181 TRP 181 194 194 TRP TRP A . n 
C 3 182 SER 182 195 195 SER SER A . n 
C 3 183 ASN 183 196 196 ASN ASN A . n 
C 3 184 LYS 184 197 197 LYS LYS A . n 
C 3 185 SER 185 198 198 SER SER A . n 
C 3 186 ASP 186 199 199 ASP ASP A . n 
C 3 187 PHE 187 200 200 PHE PHE A . n 
C 3 188 ALA 188 201 201 ALA ALA A . n 
C 3 189 CYS 189 202 202 CYS CYS A . n 
C 3 190 ALA 190 203 203 ALA ALA A . n 
C 3 191 ASN 191 204 ?   ?   ?   A . n 
C 3 192 ALA 192 205 ?   ?   ?   A . n 
C 3 193 PHE 193 206 ?   ?   ?   A . n 
C 3 194 ASN 194 207 ?   ?   ?   A . n 
C 3 195 ASN 195 208 ?   ?   ?   A . n 
C 3 196 SER 196 209 ?   ?   ?   A . n 
C 3 197 ILE 197 210 ?   ?   ?   A . n 
C 3 198 ILE 198 211 ?   ?   ?   A . n 
C 3 199 PRO 199 212 ?   ?   ?   A . n 
C 3 200 GLU 200 213 ?   ?   ?   A . n 
C 3 201 ASP 201 214 ?   ?   ?   A . n 
C 3 202 THR 202 215 ?   ?   ?   A . n 
C 3 203 PHE 203 216 ?   ?   ?   A . n 
C 3 204 PHE 204 217 ?   ?   ?   A . n 
C 3 205 PRO 205 218 ?   ?   ?   A . n 
C 3 206 SER 206 219 ?   ?   ?   A . n 
C 3 207 PRO 207 220 ?   ?   ?   A . n 
C 3 208 GLU 208 221 ?   ?   ?   A . n 
C 3 209 SER 209 222 ?   ?   ?   A . n 
C 3 210 SER 210 223 ?   ?   ?   A . n 
D 4 1   MET 1   0   ?   ?   ?   B . n 
D 4 2   VAL 2   1   1   VAL VAL B . n 
D 4 3   THR 3   2   2   THR THR B . n 
D 4 4   LEU 4   3   3   LEU LEU B . n 
D 4 5   LEU 5   4   4   LEU LEU B . n 
D 4 6   GLU 6   5   5   GLU GLU B . n 
D 4 7   GLN 7   6   6   GLN GLN B . n 
D 4 8   ASN 8   7   7   ASN ASN B . n 
D 4 9   PRO 9   8   8   PRO PRO B . n 
D 4 10  ARG 10  9   9   ARG ARG B . n 
D 4 11  TRP 11  10  10  TRP TRP B . n 
D 4 12  ARG 12  11  11  ARG ARG B . n 
D 4 13  LEU 13  12  12  LEU LEU B . n 
D 4 14  VAL 14  13  13  VAL VAL B . n 
D 4 15  PRO 15  14  14  PRO PRO B . n 
D 4 16  ARG 16  15  15  ARG ARG B . n 
D 4 17  GLY 17  16  16  GLY GLY B . n 
D 4 18  GLN 18  17  17  GLN GLN B . n 
D 4 19  ALA 19  18  18  ALA ALA B . n 
D 4 20  VAL 20  19  19  VAL VAL B . n 
D 4 21  ASN 21  20  20  ASN ASN B . n 
D 4 22  LEU 22  21  21  LEU LEU B . n 
D 4 23  ARG 23  22  22  ARG ARG B . n 
D 4 24  CYS 24  23  23  CYS CYS B . n 
D 4 25  ILE 25  24  24  ILE ILE B . n 
D 4 26  LEU 26  25  25  LEU LEU B . n 
D 4 27  LYS 27  26  26  LYS LYS B . n 
D 4 28  ASN 28  27  27  ASN ASN B . n 
D 4 29  SER 29  28  28  SER SER B . n 
D 4 30  GLN 30  29  29  GLN GLN B . n 
D 4 31  TYR 31  36  36  TYR TYR B . n 
D 4 32  PRO 32  37  37  PRO PRO B . n 
D 4 33  TRP 33  38  38  TRP TRP B . n 
D 4 34  MET 34  39  39  MET MET B . n 
D 4 35  SER 35  40  40  SER SER B . n 
D 4 36  TRP 36  41  41  TRP TRP B . n 
D 4 37  TYR 37  42  42  TYR TYR B . n 
D 4 38  GLN 38  43  43  GLN GLN B . n 
D 4 39  GLN 39  44  44  GLN GLN B . n 
D 4 40  ASP 40  45  45  ASP ASP B . n 
D 4 41  LEU 41  46  46  LEU LEU B . n 
D 4 42  GLN 42  47  47  GLN GLN B . n 
D 4 43  LYS 43  48  48  LYS LYS B . n 
D 4 44  GLN 44  49  49  GLN GLN B . n 
D 4 45  LEU 45  50  50  LEU LEU B . n 
D 4 46  GLN 46  51  51  GLN GLN B . n 
D 4 47  TRP 47  52  52  TRP TRP B . n 
D 4 48  LEU 48  53  53  LEU LEU B . n 
D 4 49  PHE 49  54  54  PHE PHE B . n 
D 4 50  THR 50  55  55  THR THR B . n 
D 4 51  LEU 51  56  56  LEU LEU B . n 
D 4 52  ARG 52  57  57  ARG ARG B . n 
D 4 53  SER 53  58  58  SER SER B . n 
D 4 54  PRO 54  63  63  PRO PRO B . n 
D 4 55  GLY 55  64  64  GLY GLY B . n 
D 4 56  ASP 56  65  65  ASP ASP B . n 
D 4 57  LYS 57  66  66  LYS LYS B . n 
D 4 58  GLU 58  67  67  GLU GLU B . n 
D 4 59  VAL 59  68  68  VAL VAL B . n 
D 4 60  LYS 60  69  69  LYS LYS B . n 
D 4 61  SER 61  70  70  SER SER B . n 
D 4 62  LEU 62  71  71  LEU LEU B . n 
D 4 63  PRO 63  72  72  PRO PRO B . n 
D 4 64  GLY 64  73  73  GLY GLY B . n 
D 4 65  ALA 65  74  74  ALA ALA B . n 
D 4 66  ASP 66  75  75  ASP ASP B . n 
D 4 67  TYR 67  76  76  TYR TYR B . n 
D 4 68  LEU 68  77  77  LEU LEU B . n 
D 4 69  ALA 69  78  78  ALA ALA B . n 
D 4 70  THR 70  79  79  THR THR B . n 
D 4 71  ARG 71  80  80  ARG ARG B . n 
D 4 72  VAL 72  81  81  VAL VAL B . n 
D 4 73  THR 73  83  83  THR THR B . n 
D 4 74  ASP 74  84  84  ASP ASP B . n 
D 4 75  THR 75  85  85  THR THR B . n 
D 4 76  GLU 76  86  86  GLU GLU B . n 
D 4 77  LEU 77  87  87  LEU LEU B . n 
D 4 78  ARG 78  88  88  ARG ARG B . n 
D 4 79  LEU 79  89  89  LEU LEU B . n 
D 4 80  GLN 80  90  90  GLN GLN B . n 
D 4 81  VAL 81  91  91  VAL VAL B . n 
D 4 82  ALA 82  92  92  ALA ALA B . n 
D 4 83  ASN 83  93  93  ASN ASN B . n 
D 4 84  MET 84  94  94  MET MET B . n 
D 4 85  SER 85  95  95  SER SER B . n 
D 4 86  GLN 86  98  98  GLN GLN B . n 
D 4 87  GLY 87  99  99  GLY GLY B . n 
D 4 88  ARG 88  100 100 ARG ARG B . n 
D 4 89  THR 89  101 101 THR THR B . n 
D 4 90  LEU 90  102 102 LEU LEU B . n 
D 4 91  TYR 91  103 103 TYR TYR B . n 
D 4 92  CYS 92  104 104 CYS CYS B . n 
D 4 93  THR 93  105 105 THR THR B . n 
D 4 94  CYS 94  106 106 CYS CYS B . n 
D 4 95  SER 95  107 107 SER SER B . n 
D 4 96  PRO 96  108 108 PRO PRO B . n 
D 4 97  GLN 97  109 109 GLN GLN B . n 
D 4 98  THR 98  110 110 THR THR B . n 
D 4 99  THR 99  111 111 THR THR B . n 
D 4 100 GLU 100 112 112 GLU GLU B . n 
D 4 101 VAL 101 113 113 VAL VAL B . n 
D 4 102 PHE 102 114 114 PHE PHE B . n 
D 4 103 PHE 103 115 115 PHE PHE B . n 
D 4 104 GLY 104 116 116 GLY GLY B . n 
D 4 105 LYS 105 117 117 LYS LYS B . n 
D 4 106 GLY 106 118 118 GLY GLY B . n 
D 4 107 THR 107 119 119 THR THR B . n 
D 4 108 ARG 108 120 120 ARG ARG B . n 
D 4 109 LEU 109 121 121 LEU LEU B . n 
D 4 110 THR 110 122 122 THR THR B . n 
D 4 111 VAL 111 123 123 VAL VAL B . n 
D 4 112 VAL 112 124 124 VAL VAL B . n 
D 4 113 GLU 113 125 125 GLU GLU B . n 
D 4 114 ASP 114 126 126 ASP ASP B . n 
D 4 115 LEU 115 127 127 LEU LEU B . n 
D 4 116 ASN 116 128 128 ASN ASN B . n 
D 4 117 LYS 117 129 129 LYS LYS B . n 
D 4 118 VAL 118 130 130 VAL VAL B . n 
D 4 119 PHE 119 131 131 PHE PHE B . n 
D 4 120 PRO 120 132 132 PRO PRO B . n 
D 4 121 PRO 121 133 133 PRO PRO B . n 
D 4 122 GLU 122 134 134 GLU GLU B . n 
D 4 123 VAL 123 135 135 VAL VAL B . n 
D 4 124 ALA 124 136 136 ALA ALA B . n 
D 4 125 VAL 125 137 137 VAL VAL B . n 
D 4 126 PHE 126 138 138 PHE PHE B . n 
D 4 127 GLU 127 139 139 GLU GLU B . n 
D 4 128 PRO 128 140 140 PRO PRO B . n 
D 4 129 SER 129 141 141 SER SER B . n 
D 4 130 GLU 130 142 142 GLU GLU B . n 
D 4 131 ALA 131 143 143 ALA ALA B . n 
D 4 132 GLU 132 144 144 GLU GLU B . n 
D 4 133 ILE 133 145 145 ILE ILE B . n 
D 4 134 SER 134 146 146 SER SER B . n 
D 4 135 HIS 135 147 147 HIS HIS B . n 
D 4 136 THR 136 148 148 THR THR B . n 
D 4 137 GLN 137 149 149 GLN GLN B . n 
D 4 138 LYS 138 150 150 LYS LYS B . n 
D 4 139 ALA 139 151 151 ALA ALA B . n 
D 4 140 THR 140 152 152 THR THR B . n 
D 4 141 LEU 141 153 153 LEU LEU B . n 
D 4 142 VAL 142 154 154 VAL VAL B . n 
D 4 143 CYS 143 155 155 CYS CYS B . n 
D 4 144 LEU 144 156 156 LEU LEU B . n 
D 4 145 ALA 145 157 157 ALA ALA B . n 
D 4 146 THR 146 158 158 THR THR B . n 
D 4 147 GLY 147 159 159 GLY GLY B . n 
D 4 148 PHE 148 160 160 PHE PHE B . n 
D 4 149 TYR 149 161 161 TYR TYR B . n 
D 4 150 PRO 150 162 162 PRO PRO B . n 
D 4 151 ASP 151 163 163 ASP ASP B . n 
D 4 152 HIS 152 164 164 HIS HIS B . n 
D 4 153 VAL 153 165 165 VAL VAL B . n 
D 4 154 GLU 154 166 166 GLU GLU B . n 
D 4 155 LEU 155 167 167 LEU LEU B . n 
D 4 156 SER 156 168 168 SER SER B . n 
D 4 157 TRP 157 169 169 TRP TRP B . n 
D 4 158 TRP 158 170 170 TRP TRP B . n 
D 4 159 VAL 159 171 171 VAL VAL B . n 
D 4 160 ASN 160 172 172 ASN ASN B . n 
D 4 161 GLY 161 173 173 GLY GLY B . n 
D 4 162 LYS 162 174 174 LYS LYS B . n 
D 4 163 GLU 163 175 175 GLU GLU B . n 
D 4 164 VAL 164 176 176 VAL VAL B . n 
D 4 165 HIS 165 177 177 HIS HIS B . n 
D 4 166 SER 166 178 178 SER SER B . n 
D 4 167 GLY 167 179 179 GLY GLY B . n 
D 4 168 VAL 168 180 180 VAL VAL B . n 
D 4 169 CYS 169 181 181 CYS CYS B . n 
D 4 170 THR 170 182 182 THR THR B . n 
D 4 171 ASP 171 183 183 ASP ASP B . n 
D 4 172 PRO 172 184 184 PRO PRO B . n 
D 4 173 GLN 173 185 185 GLN GLN B . n 
D 4 174 PRO 174 186 186 PRO PRO B . n 
D 4 175 LEU 175 187 187 LEU LEU B . n 
D 4 176 LYS 176 188 188 LYS LYS B . n 
D 4 177 GLU 177 189 189 GLU GLU B . n 
D 4 178 GLN 178 190 190 GLN GLN B . n 
D 4 179 PRO 179 191 191 PRO PRO B . n 
D 4 180 ALA 180 192 192 ALA ALA B . n 
D 4 181 LEU 181 193 193 LEU LEU B . n 
D 4 182 ASN 182 194 194 ASN ASN B . n 
D 4 183 ASP 183 195 195 ASP ASP B . n 
D 4 184 SER 184 196 196 SER SER B . n 
D 4 185 ARG 185 197 197 ARG ARG B . n 
D 4 186 TYR 186 198 198 TYR TYR B . n 
D 4 187 ALA 187 199 199 ALA ALA B . n 
D 4 188 LEU 188 200 200 LEU LEU B . n 
D 4 189 SER 189 201 201 SER SER B . n 
D 4 190 SER 190 202 202 SER SER B . n 
D 4 191 ARG 191 203 203 ARG ARG B . n 
D 4 192 LEU 192 204 204 LEU LEU B . n 
D 4 193 ARG 193 205 205 ARG ARG B . n 
D 4 194 VAL 194 206 206 VAL VAL B . n 
D 4 195 SER 195 207 207 SER SER B . n 
D 4 196 ALA 196 208 208 ALA ALA B . n 
D 4 197 THR 197 209 209 THR THR B . n 
D 4 198 PHE 198 210 210 PHE PHE B . n 
D 4 199 TRP 199 211 211 TRP TRP B . n 
D 4 200 GLN 200 212 212 GLN GLN B . n 
D 4 201 ASN 201 213 213 ASN ASN B . n 
D 4 202 PRO 202 214 214 PRO PRO B . n 
D 4 203 ARG 203 215 215 ARG ARG B . n 
D 4 204 ASN 204 216 216 ASN ASN B . n 
D 4 205 HIS 205 217 217 HIS HIS B . n 
D 4 206 PHE 206 218 218 PHE PHE B . n 
D 4 207 ARG 207 219 219 ARG ARG B . n 
D 4 208 CYS 208 220 220 CYS CYS B . n 
D 4 209 GLN 209 221 221 GLN GLN B . n 
D 4 210 VAL 210 222 222 VAL VAL B . n 
D 4 211 GLN 211 223 223 GLN GLN B . n 
D 4 212 PHE 212 224 224 PHE PHE B . n 
D 4 213 TYR 213 225 225 TYR TYR B . n 
D 4 214 GLY 214 226 226 GLY GLY B . n 
D 4 215 LEU 215 227 227 LEU LEU B . n 
D 4 216 SER 216 228 228 SER SER B . n 
D 4 217 GLU 217 229 229 GLU GLU B . n 
D 4 218 ASN 218 230 230 ASN ASN B . n 
D 4 219 ASP 219 231 231 ASP ASP B . n 
D 4 220 GLU 220 232 232 GLU GLU B . n 
D 4 221 TRP 221 233 233 TRP TRP B . n 
D 4 222 THR 222 234 234 THR THR B . n 
D 4 223 GLN 223 235 235 GLN GLN B . n 
D 4 224 ASP 224 236 236 ASP ASP B . n 
D 4 225 ARG 225 237 237 ARG ARG B . n 
D 4 226 ALA 226 238 238 ALA ALA B . n 
D 4 227 LYS 227 239 239 LYS LYS B . n 
D 4 228 PRO 228 240 240 PRO PRO B . n 
D 4 229 VAL 229 241 241 VAL VAL B . n 
D 4 230 THR 230 242 242 THR THR B . n 
D 4 231 GLN 231 243 243 GLN GLN B . n 
D 4 232 ILE 232 244 244 ILE ILE B . n 
D 4 233 VAL 233 245 245 VAL VAL B . n 
D 4 234 SER 234 246 246 SER SER B . n 
D 4 235 ALA 235 247 247 ALA ALA B . n 
D 4 236 GLU 236 248 248 GLU GLU B . n 
D 4 237 ALA 237 249 249 ALA ALA B . n 
D 4 238 TRP 238 250 250 TRP TRP B . n 
D 4 239 GLY 239 251 251 GLY GLY B . n 
D 4 240 ARG 240 252 252 ARG ARG B . n 
D 4 241 ALA 241 253 253 ALA ALA B . n 
D 4 242 ASP 242 254 ?   ?   ?   B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
E 5 EDO 1  201 201 EDO EDO C . 
F 5 EDO 1  202 301 EDO EDO C . 
G 6 NAG 1  203 401 NAG NAG C . 
H 5 EDO 1  204 501 EDO EDO C . 
I 6 NAG 1  301 301 NAG NAG D . 
J 5 EDO 1  302 301 EDO EDO D . 
K 5 EDO 1  401 401 EDO EDO B . 
L 5 EDO 1  402 501 EDO EDO B . 
M 7 HOH 1  301 6   HOH HOH C . 
M 7 HOH 2  302 17  HOH HOH C . 
M 7 HOH 3  303 1   HOH HOH C . 
M 7 HOH 4  304 11  HOH HOH C . 
M 7 HOH 5  305 8   HOH HOH C . 
M 7 HOH 6  306 24  HOH HOH C . 
M 7 HOH 7  307 30  HOH HOH C . 
M 7 HOH 8  308 26  HOH HOH C . 
M 7 HOH 9  309 28  HOH HOH C . 
M 7 HOH 10 310 16  HOH HOH C . 
M 7 HOH 11 311 19  HOH HOH C . 
M 7 HOH 12 312 47  HOH HOH C . 
M 7 HOH 13 313 59  HOH HOH C . 
M 7 HOH 14 314 38  HOH HOH C . 
M 7 HOH 15 315 52  HOH HOH C . 
M 7 HOH 16 316 57  HOH HOH C . 
M 7 HOH 17 317 29  HOH HOH C . 
M 7 HOH 18 318 48  HOH HOH C . 
M 7 HOH 19 319 33  HOH HOH C . 
M 7 HOH 20 320 43  HOH HOH C . 
M 7 HOH 21 321 44  HOH HOH C . 
M 7 HOH 22 322 39  HOH HOH C . 
M 7 HOH 23 323 53  HOH HOH C . 
M 7 HOH 24 324 31  HOH HOH C . 
N 7 HOH 1  401 2   HOH HOH D . 
N 7 HOH 2  402 12  HOH HOH D . 
N 7 HOH 3  403 55  HOH HOH D . 
N 7 HOH 4  404 58  HOH HOH D . 
N 7 HOH 5  405 54  HOH HOH D . 
N 7 HOH 6  406 56  HOH HOH D . 
N 7 HOH 7  407 35  HOH HOH D . 
N 7 HOH 8  408 14  HOH HOH D . 
N 7 HOH 9  409 15  HOH HOH D . 
O 7 HOH 1  301 37  HOH HOH A . 
O 7 HOH 2  302 10  HOH HOH A . 
O 7 HOH 3  303 18  HOH HOH A . 
O 7 HOH 4  304 36  HOH HOH A . 
O 7 HOH 5  305 27  HOH HOH A . 
O 7 HOH 6  306 60  HOH HOH A . 
P 7 HOH 1  501 23  HOH HOH B . 
P 7 HOH 2  502 42  HOH HOH B . 
P 7 HOH 3  503 50  HOH HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1   1 Y 1 C GLU 3   ? CG  ? A GLU 3   CG  
2   1 Y 1 C GLU 3   ? CD  ? A GLU 3   CD  
3   1 Y 1 C GLU 3   ? OE1 ? A GLU 3   OE1 
4   1 Y 1 C GLU 3   ? OE2 ? A GLU 3   OE2 
5   1 Y 1 C GLN 103 ? CG  ? A GLN 103 CG  
6   1 Y 1 C GLN 103 ? CD  ? A GLN 103 CD  
7   1 Y 1 C GLN 103 ? OE1 ? A GLN 103 OE1 
8   1 Y 1 C GLN 103 ? NE2 ? A GLN 103 NE2 
9   1 Y 1 C LYS 128 ? CG  ? A LYS 128 CG  
10  1 Y 1 C LYS 128 ? CD  ? A LYS 128 CD  
11  1 Y 1 C LYS 128 ? CE  ? A LYS 128 CE  
12  1 Y 1 C LYS 128 ? NZ  ? A LYS 128 NZ  
13  1 Y 1 C GLU 173 ? CG  ? A GLU 173 CG  
14  1 Y 1 C GLU 173 ? CD  ? A GLU 173 CD  
15  1 Y 1 C GLU 173 ? OE1 ? A GLU 173 OE1 
16  1 Y 1 C GLU 173 ? OE2 ? A GLU 173 OE2 
17  1 Y 1 D ARG 2   ? CG  ? B ARG 35  CG  
18  1 Y 1 D ARG 2   ? CD  ? B ARG 35  CD  
19  1 Y 1 D ARG 2   ? NE  ? B ARG 35  NE  
20  1 Y 1 D ARG 2   ? CZ  ? B ARG 35  CZ  
21  1 Y 1 D ARG 2   ? NH1 ? B ARG 35  NH1 
22  1 Y 1 D ARG 2   ? NH2 ? B ARG 35  NH2 
23  1 Y 1 D LEU 101 ? CG  ? B LEU 134 CG  
24  1 Y 1 D LEU 101 ? CD1 ? B LEU 134 CD1 
25  1 Y 1 D LEU 101 ? CD2 ? B LEU 134 CD2 
26  1 Y 1 D ARG 103 ? CG  ? B ARG 136 CG  
27  1 Y 1 D ARG 103 ? CD  ? B ARG 136 CD  
28  1 Y 1 D ARG 103 ? NE  ? B ARG 136 NE  
29  1 Y 1 D ARG 103 ? CZ  ? B ARG 136 CZ  
30  1 Y 1 D ARG 103 ? NH1 ? B ARG 136 NH1 
31  1 Y 1 D ARG 103 ? NH2 ? B ARG 136 NH2 
32  1 Y 1 D LYS 124 ? CG  ? B LYS 157 CG  
33  1 Y 1 D LYS 124 ? CD  ? B LYS 157 CD  
34  1 Y 1 D LYS 124 ? CE  ? B LYS 157 CE  
35  1 Y 1 D LYS 124 ? NZ  ? B LYS 157 NZ  
36  1 Y 1 D LYS 126 ? CG  ? B LYS 159 CG  
37  1 Y 1 D LYS 126 ? CD  ? B LYS 159 CD  
38  1 Y 1 D LYS 126 ? CE  ? B LYS 159 CE  
39  1 Y 1 D LYS 126 ? NZ  ? B LYS 159 NZ  
40  1 Y 1 D ARG 128 ? CG  ? B ARG 161 CG  
41  1 Y 1 D ARG 128 ? CD  ? B ARG 161 CD  
42  1 Y 1 D ARG 128 ? NE  ? B ARG 161 NE  
43  1 Y 1 D ARG 128 ? CZ  ? B ARG 161 CZ  
44  1 Y 1 D ARG 128 ? NH1 ? B ARG 161 NH1 
45  1 Y 1 D ARG 128 ? NH2 ? B ARG 161 NH2 
46  1 Y 1 D PHE 130 ? CG  ? B PHE 163 CG  
47  1 Y 1 D PHE 130 ? CD1 ? B PHE 163 CD1 
48  1 Y 1 D PHE 130 ? CD2 ? B PHE 163 CD2 
49  1 Y 1 D PHE 130 ? CE1 ? B PHE 163 CE1 
50  1 Y 1 D PHE 130 ? CE2 ? B PHE 163 CE2 
51  1 Y 1 D PHE 130 ? CZ  ? B PHE 163 CZ  
52  1 Y 1 D ARG 131 ? CG  ? B ARG 164 CG  
53  1 Y 1 D ARG 131 ? CD  ? B ARG 164 CD  
54  1 Y 1 D ARG 131 ? NE  ? B ARG 164 NE  
55  1 Y 1 D ARG 131 ? CZ  ? B ARG 164 CZ  
56  1 Y 1 D ARG 131 ? NH1 ? B ARG 164 NH1 
57  1 Y 1 D ARG 131 ? NH2 ? B ARG 164 NH2 
58  1 Y 1 D ASN 132 ? CG  ? B ASN 165 CG  
59  1 Y 1 D ASN 132 ? OD1 ? B ASN 165 OD1 
60  1 Y 1 D ASN 132 ? ND2 ? B ASN 165 ND2 
61  1 Y 1 D GLN 134 ? CG  ? B GLN 167 CG  
62  1 Y 1 D GLN 134 ? CD  ? B GLN 167 CD  
63  1 Y 1 D GLN 134 ? OE1 ? B GLN 167 OE1 
64  1 Y 1 D GLN 134 ? NE2 ? B GLN 167 NE2 
65  1 Y 1 D GLU 135 ? CG  ? B GLU 168 CG  
66  1 Y 1 D GLU 135 ? CD  ? B GLU 168 CD  
67  1 Y 1 D GLU 135 ? OE1 ? B GLU 168 OE1 
68  1 Y 1 D GLU 135 ? OE2 ? B GLU 168 OE2 
69  1 Y 1 D GLU 136 ? CG  ? B GLU 169 CG  
70  1 Y 1 D GLU 136 ? CD  ? B GLU 169 CD  
71  1 Y 1 D GLU 136 ? OE1 ? B GLU 169 OE1 
72  1 Y 1 D GLU 136 ? OE2 ? B GLU 169 OE2 
73  1 Y 1 D GLN 144 ? CG  ? B GLN 177 CG  
74  1 Y 1 D GLN 144 ? CD  ? B GLN 177 CD  
75  1 Y 1 D GLN 144 ? OE1 ? B GLN 177 OE1 
76  1 Y 1 D GLN 144 ? NE2 ? B GLN 177 NE2 
77  1 Y 1 D MET 158 ? CG  ? B MET 191 CG  
78  1 Y 1 D MET 158 ? SD  ? B MET 191 SD  
79  1 Y 1 D MET 158 ? CE  ? B MET 191 CE  
80  1 Y 1 D MET 161 ? CG  ? B MET 194 CG  
81  1 Y 1 D MET 161 ? SD  ? B MET 194 SD  
82  1 Y 1 D MET 161 ? CE  ? B MET 194 CE  
83  1 Y 1 D THR 162 ? OG1 ? B THR 195 OG1 
84  1 Y 1 D THR 162 ? CG2 ? B THR 195 CG2 
85  1 Y 1 D VAL 168 ? CG1 ? B VAL 201 CG1 
86  1 Y 1 D VAL 168 ? CG2 ? B VAL 201 CG2 
87  1 Y 1 D GLU 174 ? CG  ? B GLU 207 CG  
88  1 Y 1 D GLU 174 ? CD  ? B GLU 207 CD  
89  1 Y 1 D GLU 174 ? OE1 ? B GLU 207 OE1 
90  1 Y 1 D GLU 174 ? OE2 ? B GLU 207 OE2 
91  1 Y 1 D LYS 179 ? CG  ? B LYS 212 CG  
92  1 Y 1 D LYS 179 ? CD  ? B LYS 212 CD  
93  1 Y 1 D LYS 179 ? CE  ? B LYS 212 CE  
94  1 Y 1 D LYS 179 ? NZ  ? B LYS 212 NZ  
95  1 Y 1 D TRP 186 ? CG  ? B TRP 219 CG  
96  1 Y 1 D TRP 186 ? CD1 ? B TRP 219 CD1 
97  1 Y 1 D TRP 186 ? CD2 ? B TRP 219 CD2 
98  1 Y 1 D TRP 186 ? NE1 ? B TRP 219 NE1 
99  1 Y 1 D TRP 186 ? CE2 ? B TRP 219 CE2 
100 1 Y 1 D TRP 186 ? CE3 ? B TRP 219 CE3 
101 1 Y 1 D TRP 186 ? CZ2 ? B TRP 219 CZ2 
102 1 Y 1 D TRP 186 ? CZ3 ? B TRP 219 CZ3 
103 1 Y 1 D TRP 186 ? CH2 ? B TRP 219 CH2 
104 1 Y 1 A LYS 128 ? CG  ? C LYS 115 CG  
105 1 Y 1 A LYS 128 ? CD  ? C LYS 115 CD  
106 1 Y 1 A LYS 128 ? CE  ? C LYS 115 CE  
107 1 Y 1 A LYS 128 ? NZ  ? C LYS 115 NZ  
108 1 Y 1 A ILE 131 ? CG1 ? C ILE 118 CG1 
109 1 Y 1 A ILE 131 ? CG2 ? C ILE 118 CG2 
110 1 Y 1 A ILE 131 ? CD1 ? C ILE 118 CD1 
111 1 Y 1 A PRO 134 ? CG  ? C PRO 121 CG  
112 1 Y 1 A PRO 134 ? CD  ? C PRO 121 CD  
113 1 Y 1 A ASP 135 ? CG  ? C ASP 122 CG  
114 1 Y 1 A ASP 135 ? OD1 ? C ASP 122 OD1 
115 1 Y 1 A ASP 135 ? OD2 ? C ASP 122 OD2 
116 1 Y 1 A GLN 140 ? CG  ? C GLN 127 CG  
117 1 Y 1 A GLN 140 ? CD  ? C GLN 127 CD  
118 1 Y 1 A GLN 140 ? OE1 ? C GLN 127 OE1 
119 1 Y 1 A GLN 140 ? NE2 ? C GLN 127 NE2 
120 1 Y 1 A ARG 142 ? CG  ? C ARG 129 CG  
121 1 Y 1 A ARG 142 ? CD  ? C ARG 129 CD  
122 1 Y 1 A ARG 142 ? NE  ? C ARG 129 NE  
123 1 Y 1 A ARG 142 ? CZ  ? C ARG 129 CZ  
124 1 Y 1 A ARG 142 ? NH1 ? C ARG 129 NH1 
125 1 Y 1 A ARG 142 ? NH2 ? C ARG 129 NH2 
126 1 Y 1 A LYS 145 ? CG  ? C LYS 132 CG  
127 1 Y 1 A LYS 145 ? CD  ? C LYS 132 CD  
128 1 Y 1 A LYS 145 ? CE  ? C LYS 132 CE  
129 1 Y 1 A LYS 145 ? NZ  ? C LYS 132 NZ  
130 1 Y 1 A SER 146 ? OG  ? C SER 133 OG  
131 1 Y 1 A PHE 157 ? CG  ? C PHE 144 CG  
132 1 Y 1 A PHE 157 ? CD1 ? C PHE 144 CD1 
133 1 Y 1 A PHE 157 ? CD2 ? C PHE 144 CD2 
134 1 Y 1 A PHE 157 ? CE1 ? C PHE 144 CE1 
135 1 Y 1 A PHE 157 ? CE2 ? C PHE 144 CE2 
136 1 Y 1 A PHE 157 ? CZ  ? C PHE 144 CZ  
137 1 Y 1 A LYS 167 ? CG  ? C LYS 154 CG  
138 1 Y 1 A LYS 167 ? CD  ? C LYS 154 CD  
139 1 Y 1 A LYS 167 ? CE  ? C LYS 154 CE  
140 1 Y 1 A LYS 167 ? NZ  ? C LYS 154 NZ  
141 1 Y 1 A LYS 176 ? CG  ? C LYS 163 CG  
142 1 Y 1 A LYS 176 ? CD  ? C LYS 163 CD  
143 1 Y 1 A LYS 176 ? CE  ? C LYS 163 CE  
144 1 Y 1 A LYS 176 ? NZ  ? C LYS 163 NZ  
145 1 Y 1 A VAL 178 ? CG1 ? C VAL 165 CG1 
146 1 Y 1 A VAL 178 ? CG2 ? C VAL 165 CG2 
147 1 Y 1 A LEU 179 ? CG  ? C LEU 166 CG  
148 1 Y 1 A LEU 179 ? CD1 ? C LEU 166 CD1 
149 1 Y 1 A LEU 179 ? CD2 ? C LEU 166 CD2 
150 1 Y 1 A LYS 187 ? CG  ? C LYS 174 CG  
151 1 Y 1 A LYS 187 ? CD  ? C LYS 174 CD  
152 1 Y 1 A LYS 187 ? CE  ? C LYS 174 CE  
153 1 Y 1 A LYS 187 ? NZ  ? C LYS 174 NZ  
154 1 Y 1 A SER 198 ? OG  ? C SER 185 OG  
155 1 Y 1 A ASP 199 ? CG  ? C ASP 186 CG  
156 1 Y 1 A ASP 199 ? OD1 ? C ASP 186 OD1 
157 1 Y 1 A ASP 199 ? OD2 ? C ASP 186 OD2 
158 1 Y 1 A CYS 202 ? SG  ? C CYS 189 SG  
159 1 Y 1 B GLU 5   ? CG  ? D GLU 6   CG  
160 1 Y 1 B GLU 5   ? CD  ? D GLU 6   CD  
161 1 Y 1 B GLU 5   ? OE1 ? D GLU 6   OE1 
162 1 Y 1 B GLU 5   ? OE2 ? D GLU 6   OE2 
163 1 Y 1 B GLU 125 ? CG  ? D GLU 113 CG  
164 1 Y 1 B GLU 125 ? CD  ? D GLU 113 CD  
165 1 Y 1 B GLU 125 ? OE1 ? D GLU 113 OE1 
166 1 Y 1 B GLU 125 ? OE2 ? D GLU 113 OE2 
167 1 Y 1 B ASP 126 ? CG  ? D ASP 114 CG  
168 1 Y 1 B ASP 126 ? OD1 ? D ASP 114 OD1 
169 1 Y 1 B ASP 126 ? OD2 ? D ASP 114 OD2 
170 1 Y 1 B GLU 134 ? CG  ? D GLU 122 CG  
171 1 Y 1 B GLU 134 ? CD  ? D GLU 122 CD  
172 1 Y 1 B GLU 134 ? OE1 ? D GLU 122 OE1 
173 1 Y 1 B GLU 134 ? OE2 ? D GLU 122 OE2 
174 1 Y 1 B GLU 142 ? CG  ? D GLU 130 CG  
175 1 Y 1 B GLU 142 ? CD  ? D GLU 130 CD  
176 1 Y 1 B GLU 142 ? OE1 ? D GLU 130 OE1 
177 1 Y 1 B GLU 142 ? OE2 ? D GLU 130 OE2 
178 1 Y 1 B GLN 149 ? CG  ? D GLN 137 CG  
179 1 Y 1 B GLN 149 ? CD  ? D GLN 137 CD  
180 1 Y 1 B GLN 149 ? OE1 ? D GLN 137 OE1 
181 1 Y 1 B GLN 149 ? NE2 ? D GLN 137 NE2 
182 1 Y 1 B LYS 150 ? CG  ? D LYS 138 CG  
183 1 Y 1 B LYS 150 ? CD  ? D LYS 138 CD  
184 1 Y 1 B LYS 150 ? CE  ? D LYS 138 CE  
185 1 Y 1 B LYS 150 ? NZ  ? D LYS 138 NZ  
186 1 Y 1 B LYS 174 ? CG  ? D LYS 162 CG  
187 1 Y 1 B LYS 174 ? CD  ? D LYS 162 CD  
188 1 Y 1 B LYS 174 ? CE  ? D LYS 162 CE  
189 1 Y 1 B LYS 174 ? NZ  ? D LYS 162 NZ  
190 1 Y 1 B ARG 215 ? CG  ? D ARG 203 CG  
191 1 Y 1 B ARG 215 ? CD  ? D ARG 203 CD  
192 1 Y 1 B ARG 215 ? NE  ? D ARG 203 NE  
193 1 Y 1 B ARG 215 ? CZ  ? D ARG 203 CZ  
194 1 Y 1 B ARG 215 ? NH1 ? D ARG 203 NH1 
195 1 Y 1 B ARG 215 ? NH2 ? D ARG 203 NH2 
196 1 Y 1 B ASN 216 ? CG  ? D ASN 204 CG  
197 1 Y 1 B ASN 216 ? OD1 ? D ASN 204 OD1 
198 1 Y 1 B ASN 216 ? ND2 ? D ASN 204 ND2 
199 1 Y 1 B ARG 219 ? CG  ? D ARG 207 CG  
200 1 Y 1 B ARG 219 ? CD  ? D ARG 207 CD  
201 1 Y 1 B ARG 219 ? NE  ? D ARG 207 NE  
202 1 Y 1 B ARG 219 ? CZ  ? D ARG 207 CZ  
203 1 Y 1 B ARG 219 ? NH1 ? D ARG 207 NH1 
204 1 Y 1 B ARG 219 ? NH2 ? D ARG 207 NH2 
205 1 Y 1 B SER 228 ? OG  ? D SER 216 OG  
206 1 Y 1 B GLU 229 ? CG  ? D GLU 217 CG  
207 1 Y 1 B GLU 229 ? CD  ? D GLU 217 CD  
208 1 Y 1 B GLU 229 ? OE1 ? D GLU 217 OE1 
209 1 Y 1 B GLU 229 ? OE2 ? D GLU 217 OE2 
210 1 Y 1 B GLU 232 ? CG  ? D GLU 220 CG  
211 1 Y 1 B GLU 232 ? CD  ? D GLU 220 CD  
212 1 Y 1 B GLU 232 ? OE1 ? D GLU 220 OE1 
213 1 Y 1 B GLU 232 ? OE2 ? D GLU 220 OE2 
214 1 Y 1 B ASP 236 ? CG  ? D ASP 224 CG  
215 1 Y 1 B ASP 236 ? OD1 ? D ASP 224 OD1 
216 1 Y 1 B ASP 236 ? OD2 ? D ASP 224 OD2 
217 1 Y 1 B GLU 248 ? CG  ? D GLU 236 CG  
218 1 Y 1 B GLU 248 ? CD  ? D GLU 236 CD  
219 1 Y 1 B GLU 248 ? OE1 ? D GLU 236 OE1 
220 1 Y 1 B GLU 248 ? OE2 ? D GLU 236 OE2 
221 1 Y 1 B ARG 252 ? CG  ? D ARG 240 CG  
222 1 Y 1 B ARG 252 ? CD  ? D ARG 240 CD  
223 1 Y 1 B ARG 252 ? NE  ? D ARG 240 NE  
224 1 Y 1 B ARG 252 ? CZ  ? D ARG 240 CZ  
225 1 Y 1 B ARG 252 ? NH1 ? D ARG 240 NH1 
226 1 Y 1 B ARG 252 ? NH2 ? D ARG 240 NH2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? 1.20.1_4487 1 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? 1.20.1_4487 2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .           3 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .           4 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .           5 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  120.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9AUD 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     196.344 
_cell.length_a_esd                 ? 
_cell.length_b                     196.344 
_cell.length_b_esd                 ? 
_cell.length_c                     77.104 
_cell.length_c_esd                 ? 
_cell.volume                       2574203.103 
_cell.volume_esd                   ? 
_cell.Z_PDB                        9 
_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                         9AUD 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                146 
_symmetry.space_group_name_Hall            'R 3' 
_symmetry.space_group_name_H-M             'H 3' 
_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                   9AUD 
_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             3.18 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          61.36 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              8.5 
_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    '0.2 M Sodium Acetate, 0.1 M BIS-TRIS prop pH 8.5, 20 %w/v PEG 3350' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293.15 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-11-24 
_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   0.95373 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'AUSTRALIAN SYNCHROTRON BEAMLINE MX2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.95373 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   MX2 
_diffrn_source.pdbx_synchrotron_site       'Australian Synchrotron' 
# 
_reflns.B_iso_Wilson_estimate                          67.46 
_reflns.entry_id                                       9AUD 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.90 
_reflns.d_resolution_low                               49.37 
_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                                     24545 
_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                           100.0 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                4.8 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          11.0 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.091 
_reflns.pdbx_Rpim_I_all                                0.042 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.976 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.081 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.90 
_reflns_shell.d_res_low                                     3.08 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           4.0 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             3973 
_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                               4.7 
_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                               0.366 
_reflns_shell.pdbx_Rpim_I_all                               0.169 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.775 
_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                                  0.323 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               81.81 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9AUD 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.90 
_refine.ls_d_res_low                             49.37 
_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                     24536 
_refine.ls_number_reflns_R_free                  1286 
_refine.ls_number_reflns_R_work                  23250 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.97 
_refine.ls_percent_reflns_R_free                 5.24 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1847 
_refine.ls_R_factor_R_free                       0.2165 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1829 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.97 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_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                 24.0546 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.3399 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.90 
_refine_hist.d_res_low                        49.37 
_refine_hist.number_atoms_solvent             42 
_refine_hist.number_atoms_total               6153 
_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        6059 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         52 
_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' ? 0.0019  ? 6306 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.4534  ? 8610 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0434  ? 970  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0035  ? 1112 ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 11.2809 ? 2197 ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.90 3.02  . . 135 2559 99.96  . . . . 0.2503 . . . . . . . . . . . 0.3229 
'X-RAY DIFFRACTION' 3.02 3.15  . . 131 2594 100.00 . . . . 0.2309 . . . . . . . . . . . 0.2506 
'X-RAY DIFFRACTION' 3.15 3.32  . . 132 2618 99.96  . . . . 0.2335 . . . . . . . . . . . 0.2821 
'X-RAY DIFFRACTION' 3.32 3.53  . . 148 2572 100.00 . . . . 0.1977 . . . . . . . . . . . 0.2470 
'X-RAY DIFFRACTION' 3.53 3.80  . . 166 2561 100.00 . . . . 0.1886 . . . . . . . . . . . 0.2052 
'X-RAY DIFFRACTION' 3.80 4.18  . . 147 2586 100.00 . . . . 0.1857 . . . . . . . . . . . 0.2228 
'X-RAY DIFFRACTION' 4.18 4.79  . . 145 2598 100.00 . . . . 0.1426 . . . . . . . . . . . 0.1737 
'X-RAY DIFFRACTION' 4.79 6.03  . . 147 2565 100.00 . . . . 0.1643 . . . . . . . . . . . 0.2080 
'X-RAY DIFFRACTION' 6.03 49.37 . . 135 2597 99.78  . . . . 0.1817 . . . . . . . . . . . 0.2002 
# 
_struct.entry_id                     9AUD 
_struct.title                        'Immune receptor complex' 
_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        9AUD 
_struct_keywords.text            'peptide HLA complex, IMMUNE SYSTEM-VIRAL peptide complex, IMMUNE SYSTEM' 
_struct_keywords.pdbx_keywords   'IMMUNE SYSTEM' 
# 
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 ? 
D N N 4 ? 
E N N 5 ? 
F N N 5 ? 
G N N 6 ? 
H N N 5 ? 
I N N 6 ? 
J N N 5 ? 
K N N 5 ? 
L N N 5 ? 
M N N 7 ? 
N N N 7 ? 
O N N 7 ? 
P N N 7 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP HA2B_MOUSE   P14434 ? 1 
;DIEADHVGTYGISVYQSPGDIGQYTFEFDGDELFYVDLDKKETVWMLPEFGQLASFDPQGGLQNIAVVKHNLGVLTKRSN
STPATNEAPQATVFPKSPVLLGQPNTLICFVDNIFPPVINITWLRNSKSVADGVYETSFFVNRDYSFHKLSYLTFIPSDD
DIYDCKVEHWGLEEPVLKHW
;
26  
2 UNP O92607_9INFA O92607 ? 2 QVYSLIRPNENPAHK 311 
3 UNP HB2A_MOUSE   P14483 ? 2 
;GDSERHFVYQFMGECYFTNGTQRIRYVTRYIYNREEYVRYDSDVGEHRAVTELGRPDAEYWNSQPEILERTRAELDTVCR
HNYEGPETHTSLRRLEQPNVVISLSRTEALNHHNTLVCSVTDFYPAKIKVRWFRNGQEETVGVSSTQLIRNGDWTFQVLV
MLEMTPRRGEVYTCHVEHPSLKSPITVEW
;
28  
4 PDB 9AUD         9AUD   ? 3 ? 1   
5 PDB 9AUD         9AUD   ? 4 ? 1   
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9AUD C 1  ? 180 ? P14434 26  ? 205 ? 1   180 
2 2 9AUD D 1  ? 15  B O92607 311 ? 325 ? -25 -13 
3 3 9AUD D 31 R 219 ? P14483 28  ? 216 ? -13 186 
4 4 9AUD A 1  ? 210 ? 9AUD   0   ? 223 ? 0   223 
5 5 9AUD B 1  ? 242 ? 9AUD   0   ? 254 ? 0   254 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9AUD THR C 181 ? UNP P14434 ? ? 'expression tag' 181 1  
1 9AUD SER C 182 ? UNP P14434 ? ? 'expression tag' 182 2  
1 9AUD GLY C 183 ? UNP P14434 ? ? 'expression tag' 183 3  
1 9AUD LEU C 184 ? UNP P14434 ? ? 'expression tag' 184 4  
1 9AUD GLU C 185 ? UNP P14434 ? ? 'expression tag' 185 5  
1 9AUD VAL C 186 ? UNP P14434 ? ? 'expression tag' 186 6  
1 9AUD LEU C 187 ? UNP P14434 ? ? 'expression tag' 187 7  
1 9AUD PHE C 188 ? UNP P14434 ? ? 'expression tag' 188 8  
2 9AUD GLY D 16  C UNP O92607 ? ? linker           -13 9  
2 9AUD SER D 17  D UNP O92607 ? ? linker           -13 10 
2 9AUD GLY D 18  E UNP O92607 ? ? linker           -13 11 
2 9AUD GLY D 19  F UNP O92607 ? ? linker           -13 12 
2 9AUD SER D 20  G UNP O92607 ? ? linker           -13 13 
2 9AUD ILE D 21  H UNP O92607 ? ? linker           -13 14 
2 9AUD GLU D 22  I UNP O92607 ? ? linker           -13 15 
2 9AUD GLY D 23  J UNP O92607 ? ? linker           -13 16 
2 9AUD ARG D 24  K UNP O92607 ? ? linker           -13 17 
2 9AUD GLY D 25  L UNP O92607 ? ? linker           -13 18 
2 9AUD GLY D 26  M UNP O92607 ? ? linker           -13 19 
2 9AUD SER D 27  N UNP O92607 ? ? linker           -13 20 
2 9AUD GLY D 28  O UNP O92607 ? ? linker           -13 21 
2 9AUD ALA D 29  P UNP O92607 ? ? linker           -13 22 
2 9AUD SER D 30  Q UNP O92607 ? ? linker           -13 23 
3 9AUD THR D 220 ? UNP P14483 ? ? 'expression tag' 187 24 
3 9AUD GLY D 221 ? UNP P14483 ? ? 'expression tag' 188 25 
3 9AUD GLY D 222 ? UNP P14483 ? ? 'expression tag' 189 26 
3 9AUD LEU D 223 ? UNP P14483 ? ? 'expression tag' 190 27 
3 9AUD GLU D 224 ? UNP P14483 ? ? 'expression tag' 191 28 
3 9AUD VAL D 225 ? UNP P14483 ? ? 'expression tag' 192 29 
3 9AUD LEU D 226 ? UNP P14483 ? ? 'expression tag' 193 30 
3 9AUD PHE D 227 ? UNP P14483 ? ? 'expression tag' 194 31 
3 9AUD GLN D 228 ? UNP P14483 ? ? 'expression tag' 195 32 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   tetrameric 
_pdbx_struct_assembly.oligomeric_count     4 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'surface plasmon resonance' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 LEU A 47  ? ALA A 54  ? LEU C 47  ALA C 54  1 ? 8  
HELX_P HELX_P2  AA2 ASP A 57  ? LYS A 77  ? ASP C 57  LYS C 77  1 ? 21 
HELX_P HELX_P3  AA3 THR B 81  ? LEU B 83  ? THR D 48  LEU D 50  5 ? 3  
HELX_P HELX_P4  AA4 GLY B 84  ? GLN B 94  ? GLY D 51  GLN D 61  1 ? 11 
HELX_P HELX_P5  AA5 GLN B 94  ? ALA B 103 ? GLN D 61  ALA D 70  1 ? 10 
HELX_P HELX_P6  AA6 ALA B 103 ? VAL B 108 ? ALA D 70  VAL D 75  1 ? 6  
HELX_P HELX_P7  AA7 VAL B 108 ? GLY B 115 ? VAL D 75  GLY D 82  1 ? 8  
HELX_P HELX_P8  AA8 GLY B 115 ? THR B 120 ? GLY D 82  THR D 87  1 ? 6  
HELX_P HELX_P9  AA9 SER B 121 ? ARG B 124 ? SER D 88  ARG D 91  5 ? 4  
HELX_P HELX_P10 AB1 GLN C 82  ? SER C 86  ? GLN A 95  SER A 99  5 ? 5  
HELX_P HELX_P11 AB2 ASP D 114 ? VAL D 118 ? ASP B 126 VAL B 130 5 ? 5  
HELX_P HELX_P12 AB3 SER D 129 ? GLN D 137 ? SER B 141 GLN B 149 1 ? 9  
HELX_P HELX_P13 AB4 ALA D 196 ? GLN D 200 ? ALA B 208 GLN B 212 1 ? 5  
# 
_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 109 SG  ? ? ? 1_555 A CYS 165 SG ? ? C CYS 109 C CYS 165 1_555 ? ? ? ? ? ? ? 2.031 ? ?               
disulf2 disulf ?   ? B CYS 45  SG  ? ? ? 1_555 B CYS 109 SG ? ? D CYS 12  D CYS 76  1_555 ? ? ? ? ? ? ? 2.030 ? ?               
disulf3 disulf ?   ? B CYS 148 SG  ? ? ? 1_555 B CYS 204 SG ? ? D CYS 115 D CYS 171 1_555 ? ? ? ? ? ? ? 2.035 ? ?               
disulf4 disulf ?   ? C CYS 24  SG  ? ? ? 1_555 C CYS 91  SG ? ? A CYS 23  A CYS 104 1_555 ? ? ? ? ? ? ? 2.032 ? ?               
disulf5 disulf ?   ? C CYS 164 SG  ? ? ? 1_555 D CYS 169 SG ? ? A CYS 177 B CYS 181 1_555 ? ? ? ? ? ? ? 2.029 ? ?               
disulf6 disulf ?   ? D CYS 24  SG  ? ? ? 1_555 D CYS 92  SG ? ? B CYS 23  B CYS 104 1_555 ? ? ? ? ? ? ? 2.029 ? ?               
disulf7 disulf ?   ? D CYS 143 SG  ? ? ? 1_555 D CYS 208 SG ? ? B CYS 155 B CYS 220 1_555 ? ? ? ? ? ? ? 2.031 ? ?               
covale1 covale one ? A ASN 120 ND2 ? ? ? 1_555 G NAG .   C1 ? ? C ASN 120 C NAG 203 1_555 ? ? ? ? ? ? ? 1.459 ? N-Glycosylation 
covale2 covale one ? B ASN 49  ND2 ? ? ? 1_555 I NAG .   C1 ? ? D ASN 16  D NAG 301 1_555 ? ? ? ? ? ? ? 1.450 ? N-Glycosylation 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
# 
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 NAG G .   ? ASN A 120 ? NAG C 203 ? 1_555 ASN C 120 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
2 NAG I .   ? ASN B 49  ? NAG D 301 ? 1_555 ASN D 16  ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
3 CYS A 109 ? CYS A 165 ? CYS C 109 ? 1_555 CYS C 165 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
4 CYS B 45  ? CYS B 109 ? CYS D 12  ? 1_555 CYS D 76  ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
5 CYS B 148 ? CYS B 204 ? CYS D 115 ? 1_555 CYS D 171 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
6 CYS C 24  ? CYS C 91  ? CYS A 23  ? 1_555 CYS A 104 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
7 CYS C 164 ? CYS D 169 ? CYS A 177 ? 1_555 CYS B 181 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
8 CYS D 24  ? CYS D 92  ? CYS B 23  ? 1_555 CYS B 104 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
9 CYS D 143 ? CYS D 208 ? CYS B 155 ? 1_555 CYS B 220 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 SER 17  A . ? SER 17  C PRO 18  A ? PRO 18  C 1 0.16  
2 SER 17  A . ? SER 17  C PRO 18  A ? PRO 18  C 1 0.46  
3 PHE 115 A . ? PHE 115 C PRO 116 A ? PRO 116 C 1 -0.25 
4 TYR 154 B . ? TYR 121 D PRO 155 B ? PRO 122 D 1 3.51  
5 GLY 10  C . ? GLY 9   A PRO 11  C ? PRO 10  A 1 -0.90 
6 ASN 8   D . ? ASN 7   B PRO 9   D ? PRO 8   B 1 -0.77 
7 TYR 149 D . ? TYR 161 B PRO 150 D ? PRO 162 B 1 -2.42 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 8 ? 
AA2 ? 4 ? 
AA3 ? 4 ? 
AA4 ? 4 ? 
AA5 ? 4 ? 
AA6 ? 4 ? 
AA7 ? 3 ? 
AA8 ? 2 ? 
AA9 ? 5 ? 
AB1 ? 4 ? 
AB2 ? 4 ? 
AB3 ? 4 ? 
AB4 ? 5 ? 
AB5 ? 5 ? 
AB6 ? 4 ? 
AB7 ? 4 ? 
AB8 ? 4 ? 
AB9 ? 4 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA1 7 8 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA7 2 3 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA9 1 2 ? parallel      
AA9 2 3 ? anti-parallel 
AA9 3 4 ? anti-parallel 
AA9 4 5 ? anti-parallel 
AB1 1 2 ? parallel      
AB1 2 3 ? anti-parallel 
AB1 3 4 ? anti-parallel 
AB2 1 2 ? anti-parallel 
AB2 2 3 ? anti-parallel 
AB2 3 4 ? anti-parallel 
AB3 1 2 ? anti-parallel 
AB3 2 3 ? anti-parallel 
AB3 3 4 ? anti-parallel 
AB4 1 2 ? anti-parallel 
AB4 2 3 ? anti-parallel 
AB4 3 4 ? anti-parallel 
AB4 4 5 ? anti-parallel 
AB5 1 2 ? parallel      
AB5 2 3 ? anti-parallel 
AB5 3 4 ? anti-parallel 
AB5 4 5 ? anti-parallel 
AB6 1 2 ? parallel      
AB6 2 3 ? anti-parallel 
AB6 3 4 ? anti-parallel 
AB7 1 2 ? anti-parallel 
AB7 2 3 ? anti-parallel 
AB7 3 4 ? anti-parallel 
AB8 1 2 ? anti-parallel 
AB8 2 3 ? anti-parallel 
AB8 3 4 ? anti-parallel 
AB9 1 2 ? anti-parallel 
AB9 2 3 ? anti-parallel 
AB9 3 4 ? 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 GLU A 42  ? TRP A 45  ? GLU C 42  TRP C 45  
AA1 2 ASP A 31  ? ASP A 37  ? ASP C 31  ASP C 37  
AA1 3 ILE A 21  ? PHE A 28  ? ILE C 21  PHE C 28  
AA1 4 HIS A 6   ? SER A 17  ? HIS C 6   SER C 17  
AA1 5 PHE B 37  ? PHE B 47  ? PHE D 4   PHE D 14  
AA1 6 ILE B 54  ? TYR B 62  ? ILE D 21  TYR D 29  
AA1 7 GLU B 66  ? ASP B 71  ? GLU D 33  ASP D 38  
AA1 8 HIS B 77  ? ALA B 79  ? HIS D 44  ALA D 46  
AA2 1 GLN A 90  ? PRO A 95  ? GLN C 90  PRO C 95  
AA2 2 ASN A 105 ? ILE A 114 ? ASN C 105 ILE C 114 
AA2 3 PHE A 147 ? PHE A 155 ? PHE C 147 PHE C 155 
AA2 4 VAL A 134 ? GLU A 136 ? VAL C 134 GLU C 136 
AA3 1 GLN A 90  ? PRO A 95  ? GLN C 90  PRO C 95  
AA3 2 ASN A 105 ? ILE A 114 ? ASN C 105 ILE C 114 
AA3 3 PHE A 147 ? PHE A 155 ? PHE C 147 PHE C 155 
AA3 4 PHE A 140 ? VAL A 141 ? PHE C 140 VAL C 141 
AA4 1 LYS A 128 ? VAL A 130 ? LYS C 128 VAL C 130 
AA4 2 ASN A 120 ? ARG A 125 ? ASN C 120 ARG C 125 
AA4 3 TYR A 163 ? GLU A 168 ? TYR C 163 GLU C 168 
AA4 4 VAL A 176 ? TRP A 180 ? VAL C 176 TRP C 180 
AA5 1 ASN B 129 ? VAL B 131 ? ASN D 96  VAL D 98  
AA5 2 VAL B 147 ? PHE B 153 ? VAL D 114 PHE D 120 
AA5 3 PHE B 186 ? MET B 191 ? PHE D 153 MET D 158 
AA5 4 SER B 174 ? SER B 175 ? SER D 141 SER D 142 
AA6 1 ASN B 129 ? VAL B 131 ? ASN D 96  VAL D 98  
AA6 2 VAL B 147 ? PHE B 153 ? VAL D 114 PHE D 120 
AA6 3 PHE B 186 ? MET B 191 ? PHE D 153 MET D 158 
AA6 4 ILE B 179 ? ARG B 180 ? ILE D 146 ARG D 147 
AA7 1 LYS B 159 ? PHE B 163 ? LYS D 126 PHE D 130 
AA7 2 TYR B 202 ? GLU B 207 ? TYR D 169 GLU D 174 
AA7 3 ILE B 215 ? TRP B 219 ? ILE D 182 TRP D 186 
AA8 1 SER C 4   ? GLN C 7   ? SER A 3   GLN A 6   
AA8 2 CYS C 24  ? GLU C 27  ? CYS A 23  GLU A 26  
AA9 1 VAL C 12  ? SER C 15  ? VAL A 11  SER A 14  
AA9 2 THR C 110 ? LYS C 115 ? THR A 123 LYS A 128 
AA9 3 VAL C 88  ? LEU C 95  ? VAL A 101 LEU A 108 
AA9 4 PRO C 32  ? GLN C 39  ? PRO A 37  GLN A 44  
AA9 5 GLN C 46  ? VAL C 51  ? GLN A 51  VAL A 56  
AB1 1 VAL C 12  ? SER C 15  ? VAL A 11  SER A 14  
AB1 2 THR C 110 ? LYS C 115 ? THR A 123 LYS A 128 
AB1 3 VAL C 88  ? LEU C 95  ? VAL A 101 LEU A 108 
AB1 4 THR C 105 ? PHE C 106 ? THR A 118 PHE A 119 
AB2 1 LEU C 20  ? VAL C 22  ? LEU A 19  VAL A 21  
AB2 2 LEU C 76  ? LYS C 78  ? LEU A 89  LYS A 91  
AB2 3 PHE C 63  ? THR C 66  ? PHE A 76  THR A 79  
AB2 4 LYS C 57  ? SER C 60  ? LYS A 65  SER A 68  
AB3 1 VAL C 125 ? LEU C 128 ? VAL A 138 LEU A 141 
AB3 2 SER C 137 ? PHE C 141 ? SER A 150 PHE A 154 
AB3 3 ALA C 178 ? SER C 182 ? ALA A 191 SER A 195 
AB3 4 VAL C 158 ? ILE C 160 ? VAL A 171 ILE A 173 
AB4 1 LEU D 5   ? ASN D 8   ? LEU B 4   ASN B 7   
AB4 2 VAL D 20  ? LEU D 26  ? VAL B 19  LEU B 25  
AB4 3 LEU D 77  ? ALA D 82  ? LEU B 87  ALA B 92  
AB4 4 ALA D 65  ? ARG D 71  ? ALA B 74  ARG B 80  
AB4 5 LYS D 57  ? LEU D 62  ? LYS B 66  LEU B 71  
AB5 1 TRP D 11  ? PRO D 15  ? TRP B 10  PRO B 14  
AB5 2 THR D 107 ? VAL D 112 ? THR B 119 VAL B 124 
AB5 3 ARG D 88  ? SER D 95  ? ARG B 100 SER B 107 
AB5 4 TRP D 33  ? GLN D 39  ? TRP B 38  GLN B 44  
AB5 5 LEU D 45  ? LEU D 51  ? LEU B 50  LEU B 56  
AB6 1 TRP D 11  ? PRO D 15  ? TRP B 10  PRO B 14  
AB6 2 THR D 107 ? VAL D 112 ? THR B 119 VAL B 124 
AB6 3 ARG D 88  ? SER D 95  ? ARG B 100 SER B 107 
AB6 4 PHE D 102 ? PHE D 103 ? PHE B 114 PHE B 115 
AB7 1 GLU D 122 ? PHE D 126 ? GLU B 134 PHE B 138 
AB7 2 LYS D 138 ? PHE D 148 ? LYS B 150 PHE B 160 
AB7 3 TYR D 186 ? SER D 195 ? TYR B 198 SER B 207 
AB7 4 VAL D 168 ? THR D 170 ? VAL B 180 THR B 182 
AB8 1 GLU D 122 ? PHE D 126 ? GLU B 134 PHE B 138 
AB8 2 LYS D 138 ? PHE D 148 ? LYS B 150 PHE B 160 
AB8 3 TYR D 186 ? SER D 195 ? TYR B 198 SER B 207 
AB8 4 LEU D 175 ? LYS D 176 ? LEU B 187 LYS B 188 
AB9 1 LYS D 162 ? GLU D 163 ? LYS B 174 GLU B 175 
AB9 2 VAL D 153 ? VAL D 159 ? VAL B 165 VAL B 171 
AB9 3 HIS D 205 ? PHE D 212 ? HIS B 217 PHE B 224 
AB9 4 GLN D 231 ? TRP D 238 ? GLN B 243 TRP B 250 
# 
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 VAL A 44  ? O VAL C 44  N TYR A 35  ? N TYR C 35  
AA1 2 3 O LEU A 33  ? O LEU C 33  N PHE A 26  ? N PHE C 26  
AA1 3 4 O ILE A 21  ? O ILE C 21  N GLN A 16  ? N GLN C 16  
AA1 4 5 N GLY A 8   ? N GLY C 8   O CYS B 45  ? O CYS D 12  
AA1 5 6 N GLU B 44  ? N GLU D 11  O VAL B 57  ? O VAL D 24  
AA1 6 7 N TYR B 60  ? N TYR D 27  O TYR B 67  ? O TYR D 34  
AA1 7 8 N ARG B 69  ? N ARG D 36  O ARG B 78  ? O ARG D 45  
AA2 1 2 N THR A 92  ? N THR C 92  O PHE A 110 ? O PHE C 110 
AA2 2 3 N ILE A 114 ? N ILE C 114 O PHE A 147 ? O PHE C 147 
AA2 3 4 O TYR A 152 ? O TYR C 152 N TYR A 135 ? N TYR C 135 
AA3 1 2 N THR A 92  ? N THR C 92  O PHE A 110 ? O PHE C 110 
AA3 2 3 N ILE A 114 ? N ILE C 114 O PHE A 147 ? O PHE C 147 
AA3 3 4 O HIS A 148 ? O HIS C 148 N PHE A 140 ? N PHE C 140 
AA4 1 2 O LYS A 128 ? O LYS C 128 N ARG A 125 ? N ARG C 125 
AA4 2 3 N THR A 122 ? N THR C 122 O LYS A 166 ? O LYS C 166 
AA4 3 4 N VAL A 167 ? N VAL C 167 O VAL A 176 ? O VAL C 176 
AA5 1 2 N ASN B 129 ? N ASN D 96  O THR B 151 ? O THR D 118 
AA5 2 3 N CYS B 148 ? N CYS D 115 O VAL B 190 ? O VAL D 157 
AA5 3 4 O MET B 191 ? O MET D 158 N SER B 174 ? N SER D 141 
AA6 1 2 N ASN B 129 ? N ASN D 96  O THR B 151 ? O THR D 118 
AA6 2 3 N CYS B 148 ? N CYS D 115 O VAL B 190 ? O VAL D 157 
AA6 3 4 O GLN B 187 ? O GLN D 154 N ILE B 179 ? N ILE D 146 
AA7 1 2 N ARG B 161 ? N ARG D 128 O HIS B 205 ? O HIS D 172 
AA7 2 3 N TYR B 202 ? N TYR D 169 O TRP B 219 ? O TRP D 186 
AA8 1 2 N THR C 6   ? N THR A 5   O SER C 25  ? O SER A 24  
AA9 1 2 N VAL C 12  ? N VAL A 11  O LYS C 111 ? O LYS A 124 
AA9 2 3 O THR C 110 ? O THR A 123 N TYR C 89  ? N TYR A 102 
AA9 3 4 O ALA C 92  ? O ALA A 105 N PHE C 35  ? N PHE A 40  
AA9 4 5 N TRP C 36  ? N TRP A 41  O LEU C 48  ? O LEU A 53  
AB1 1 2 N VAL C 12  ? N VAL A 11  O LYS C 111 ? O LYS A 124 
AB1 2 3 O THR C 110 ? O THR A 123 N TYR C 89  ? N TYR A 102 
AB1 3 4 N LEU C 93  ? N LEU A 106 O THR C 105 ? O THR A 118 
AB2 1 2 N VAL C 22  ? N VAL A 21  O LEU C 76  ? O LEU A 89  
AB2 2 3 O GLN C 77  ? O GLN A 90  N GLU C 64  ? N GLU A 77  
AB2 3 4 O PHE C 63  ? O PHE A 76  N SER C 60  ? N SER A 68  
AB3 1 2 N LEU C 128 ? N LEU A 141 O VAL C 138 ? O VAL A 151 
AB3 2 3 N CYS C 139 ? N CYS A 152 O ALA C 180 ? O ALA A 193 
AB3 3 4 O TRP C 181 ? O TRP A 194 N TYR C 159 ? N TYR A 172 
AB4 1 2 N GLU D 6   ? N GLU B 5   O ILE D 25  ? O ILE B 24  
AB4 2 3 N VAL D 20  ? N VAL B 19  O VAL D 81  ? O VAL B 91  
AB4 3 4 O ARG D 78  ? O ARG B 88  N THR D 70  ? N THR B 79  
AB4 4 5 O TYR D 67  ? O TYR B 76  N LYS D 60  ? N LYS B 69  
AB5 1 2 N VAL D 14  ? N VAL B 13  O THR D 110 ? O THR B 122 
AB5 2 3 O LEU D 109 ? O LEU B 121 N ARG D 88  ? N ARG B 100 
AB5 3 4 O THR D 93  ? O THR B 105 N SER D 35  ? N SER B 40  
AB5 4 5 N GLN D 38  ? N GLN B 43  O GLN D 46  ? O GLN B 51  
AB6 1 2 N VAL D 14  ? N VAL B 13  O THR D 110 ? O THR B 122 
AB6 2 3 O LEU D 109 ? O LEU B 121 N ARG D 88  ? N ARG B 100 
AB6 3 4 N CYS D 94  ? N CYS B 106 O PHE D 102 ? O PHE B 114 
AB7 1 2 N PHE D 126 ? N PHE B 138 O VAL D 142 ? O VAL B 154 
AB7 2 3 N PHE D 148 ? N PHE B 160 O TYR D 186 ? O TYR B 198 
AB7 3 4 O ARG D 191 ? O ARG B 203 N CYS D 169 ? N CYS B 181 
AB8 1 2 N PHE D 126 ? N PHE B 138 O VAL D 142 ? O VAL B 154 
AB8 2 3 N PHE D 148 ? N PHE B 160 O TYR D 186 ? O TYR B 198 
AB8 3 4 O ALA D 187 ? O ALA B 199 N LEU D 175 ? N LEU B 187 
AB9 1 2 O LYS D 162 ? O LYS B 174 N VAL D 159 ? N VAL B 171 
AB9 2 3 N TRP D 158 ? N TRP B 170 O ARG D 207 ? O ARG B 219 
AB9 3 4 N PHE D 212 ? N PHE B 224 O GLN D 231 ? O GLN B 243 
# 
_pdbx_entry_details.entry_id                   9AUD 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     N 
_pdbx_entry_details.has_protein_modification   Y 
# 
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 SER C 81  ? ? 56.20   73.48   
2  1 THR D 15  ? ? -115.89 -73.09  
3  1 ASN D 16  ? ? -97.84  57.82   
4  1 VAL D 75  ? ? -124.80 -62.73  
5  1 THR D 87  ? ? -115.10 -85.50  
6  1 SER D 102 ? ? -170.68 144.01  
7  1 LEU D 113 ? ? 46.40   75.02   
8  1 ASP D 119 ? ? 58.51   76.83   
9  1 PHE D 130 ? ? -160.97 106.22  
10 1 ASP A 2   ? ? -90.08  -65.37  
11 1 ARG A 74  ? ? 57.20   -119.46 
12 1 PHE A 87  ? ? -152.39 59.11   
13 1 LYS A 145 ? ? -130.48 -37.16  
14 1 LEU B 53  ? ? -110.16 -71.03  
15 1 ARG B 57  ? ? -126.41 -53.96  
16 1 ARG B 57  ? ? -126.41 -54.27  
17 1 THR B 83  ? ? -118.99 -167.39 
18 1 GLU B 112 ? ? -150.66 84.99   
19 1 ASP B 163 ? ? -78.88  37.73   
20 1 ASP B 195 ? ? -89.79  35.04   
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z                 
2 -y,x-y,z              
3 -x+y,-x,z             
4 x+1/3,y+2/3,z+2/3     
5 -y+1/3,x-y+2/3,z+2/3  
6 -x+y+1/3,-x+2/3,z+2/3 
7 x+2/3,y+1/3,z+1/3     
8 -y+2/3,x-y+1/3,z+1/3  
9 -x+y+2/3,-x+1/3,z+1/3 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1  'X-RAY DIFFRACTION' ? refined 67.302653127  43.5627519352 18.3644661951 0.257400825601 ? 0.0258057777438  ? 0.0353823469405  ? 
0.453250884021 ? 0.0627616363375 ? 0.287179579015 ? 6.43660707927  ? 3.17370559013   ? 1.23893815625   ? 8.27129934354 ? 
1.22018748172   ? 2.09664885621  ? -0.17332318971   ? 0.464040598583  ? 0.14823003302      ? -0.0885775918047 ? 0.165396790075   ? 
0.170713745327   ? -0.148092399776  ? 0.187386745939    ? 0.0233515436533  ? 
2  'X-RAY DIFFRACTION' ? refined 84.5358241597 31.0388564596 16.8840218391 0.368309963405 ? 0.0745106033929  ? -0.0419218656017 ? 
0.555964698883 ? 0.0841817723972 ? 0.401179488351 ? 4.81014799652  ? -2.89254452166  ? -2.19794242575  ? 9.33372829699 ? 
4.35942062836   ? 4.71035713129  ? -0.125189745104  ? 0.145799329407  ? -0.357510381558    ? 0.164275404814   ? 0.0609271257903  ? 
-0.408271216443  ? 0.339801011691   ? 0.371363937209    ? 0.0626732958253  ? 
3  'X-RAY DIFFRACTION' ? refined 64.1078670274 44.278066992  31.4775270285 0.47184801657  ? 0.106137111097   ? 0.0438162872567  ? 
0.510396819562 ? 0.114085216726  ? 0.363171453993 ? 4.30540045457  ? 1.08909605993   ? 0.29357921742   ? 4.1511114755  ? 
1.10776393102   ? 3.80274508709  ? -0.144103277305  ? -0.724191700997 ? -0.000683067612867 ? 0.708015978268   ? 0.04175356515    ? 
0.287841458633   ? -0.0232822617097 ? 0.136423178826    ? 0.0833101242027  ? 
4  'X-RAY DIFFRACTION' ? refined 64.6115273717 55.6642633627 39.7043463281 0.804755029312 ? 0.0394815112121  ? 0.0627495950139  ? 
0.556789685783 ? 0.0929960467521 ? 0.534149223528 ? 2.65369474088  ? -3.06667093844  ? -3.01833188263  ? 9.07494192447 ? 
6.84510078036   ? 5.48868191841  ? 0.0753182976179  ? -0.938514509366 ? 0.495628711147     ? 0.679159596814   ? -0.259407626537  ? 
0.263249582573   ? -0.507381877597  ? -0.0777595071242  ? 0.0950111265233  ? 
5  'X-RAY DIFFRACTION' ? refined 53.1329877888 49.8119646236 31.513152416  0.541406036728 ? 0.181082536016   ? 0.201353976008   ? 
0.684941785827 ? 0.0999631758111 ? 0.684418997563 ? 1.73565203963  ? 2.86902423314   ? 3.47445849785   ? 6.94432420654 ? 
3.71165311981   ? 8.86968672593  ? -0.200299706208  ? -0.317098833666 ? -0.0240380419233   ? 0.257413614836   ? 0.0866577265619  ? 
1.09882750069    ? -0.641527991761  ? -1.20641621312    ? 0.0649231908791  ? 
6  'X-RAY DIFFRACTION' ? refined 64.048230754  19.3943087606 18.2018759486 0.538892900684 ? -0.0212356310241 ? 0.132372402525   ? 
0.568449282832 ? 0.0174005568776 ? 1.23138871298  ? 1.4759429923   ? 0.589926782072  ? -0.291129201022 ? 2.76197648396 ? 
1.26538987602   ? 3.42009780775  ? -0.221499428293  ? 0.273495511042  ? -1.92125072851     ? 0.0354749600877  ? -0.0781175844585 ? 
0.545092931122   ? 0.750165284474   ? 0.206373072394    ? 0.208129123643   ? 
7  'X-RAY DIFFRACTION' ? refined 70.8082044626 1.98672631299 28.9342773317 1.3330213706   ? 0.136265431838   ? 0.150182941387   ? 
1.34280319274  ? 0.416804766754  ? 1.26495302201  ? 1.71905650305  ? -0.291052381038 ? 0.392048798954  ? 2.53320440702 ? 
0.779383327051  ? 0.382606400468 ? -0.727905921393  ? 0.638312650621  ? 0.485124166233     ? -0.660530179319  ? 0.852462040277   ? 
0.419962541708   ? 0.725644186375   ? 0.213197926571    ? 0.00447956526988 ? 
8  'X-RAY DIFFRACTION' ? refined 68.9332184961 10.9037487573 19.1083866528 0.847869177122 ? 0.113496895821   ? 0.172426129507   ? 
0.647787284167 ? 0.173283983476  ? 1.50698142741  ? 0.946497053999 ? -1.58735755133  ? 0.896721378586  ? 4.45238266044 ? 
-0.32699697385  ? 5.8917105965   ? -0.149920709578  ? -0.432952540347 ? -1.75403998131     ? 0.696774037555   ? -0.225523393789  ? 
0.721814388264   ? 1.27418175818    ? 0.207487802288    ? 0.34317743203    ? 
9  'X-RAY DIFFRACTION' ? refined 38.1764521369 61.0091382698 18.6830444802 0.468162556459 ? 0.0675972873961  ? 0.126248948476   ? 
0.733873342277 ? 0.242271405478  ? 1.36322103416  ? 6.40699994225  ? -3.05115630955  ? 1.34980275951   ? 1.49833095305 ? 
-0.924155167694 ? 2.52914317863  ? 0.155122697178   ? 0.0578453576146 ? -0.123758513141    ? 0.35655196094    ? 0.344830846595   ? 
1.24546028203    ? -0.29720370785   ? -0.699542539727   ? -0.423179287922  ? 
10 'X-RAY DIFFRACTION' ? refined 20.5483496497 91.3216750499 15.1026321138 1.19789166493  ? 0.283301528593   ? 0.265726211753   ? 
1.52106106037  ? 0.0367970919614 ? 1.18646612264  ? 1.61401581362  ? 2.3386775042    ? -3.32391902739  ? 4.13666224399 ? 
-5.76657604626  ? 8.20671010329  ? 0.322722076633   ? 0.431766652595  ? -0.038465402073    ? 1.68574085895    ? 0.455002978266   ? 
1.53352951424    ? -1.17467213617   ? -0.709925046967   ? -0.688736015995  ? 
11 'X-RAY DIFFRACTION' ? refined 30.4152014344 101.038721898 6.22673746848 1.2117714663   ? 0.259404479045   ? -0.0186382954251 ? 
1.22517681613  ? 0.225071570829  ? 0.685939869359 ? 9.25383330954  ? 6.28892829212   ? 3.16769632295   ? 7.87687018558 ? 
6.81758713619   ? 7.1756911425   ? -0.74839641377   ? 0.753451278683  ? 1.62598485914      ? -1.66229363086   ? 0.547930814171   ? 
0.960311191763   ? -0.0539520273774 ? 0.054408894577    ? 0.389789997063   ? 
12 'X-RAY DIFFRACTION' ? refined 26.783299931  91.5019524392 5.18717266857 0.900359253352 ? 0.329310159566   ? -0.113834348672  ? 
0.984137771494 ? 0.0165057147096 ? 0.528961995303 ? 5.19286714079  ? 3.59986976813   ? -6.19453304527  ? 8.29147003584 ? 
-3.71596529981  ? 8.95949926914  ? 0.417016449792   ? 0.460645285605  ? 0.169240967795     ? 0.353417319288   ? 0.226431265662   ? 
0.411058308599   ? -0.990572560575  ? -0.822141092454   ? -0.655371225471  ? 
13 'X-RAY DIFFRACTION' ? refined 57.332638352  70.9062413129 9.92239730692 0.332421991538 ? -0.0663202029131 ? -0.0439211910003 ? 
0.430635597859 ? 0.0288652205111 ? 0.503665603416 ? 4.37150173481  ? -1.57629824812  ? 1.25166908527   ? 6.45415466178 ? 
-3.2089932593   ? 5.15471189164  ? -0.0973071855672 ? 0.360294071689  ? -0.336357742283    ? -0.191761450976  ? 0.318787682631   ? 
0.571791609034   ? -0.147252436578  ? -0.00896426208077 ? -0.20904681931   ? 
14 'X-RAY DIFFRACTION' ? refined 41.5454903348 95.3610856638 9.76473758698 1.02893499234  ? -0.0415552144607 ? -0.132358630818  ? 
0.984418511293 ? 0.0229969855716 ? 0.533364126011 ? 5.41999049282  ? -0.451775183847 ? -2.45967520432  ? 1.67799280299 ? 
0.509357595556  ? 7.43008388336  ? 0.233319986948   ? -1.34575924744  ? 0.588958931324     ? 0.53246199033    ? 0.123376197589   ? 
-0.0287475465263 ? -0.811572428189  ? 1.16964725237     ? -0.351610664421  ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1  'X-RAY DIFFRACTION' 1  A 1   C 1   ? A 76  C 76  ? ? 
;chain 'C' and (resid 1 through 76 )
;
2  'X-RAY DIFFRACTION' 2  A 77  C 77  ? A 186 C 186 ? ? 
;chain 'C' and (resid 77 through 186 )
;
3  'X-RAY DIFFRACTION' 3  F 1   D -25 ? F 60  D 48  ? ? 
;chain 'D' and (resid -25 through 48 )
;
4  'X-RAY DIFFRACTION' 4  F 61  D 49  ? F 73  D 61  ? ? 
;chain 'D' and (resid 49 through 61 )
;
5  'X-RAY DIFFRACTION' 5  F 74  D 62  ? F 86  D 74  ? ? 
;chain 'D' and (resid 62 through 74 )
;
6  'X-RAY DIFFRACTION' 6  F 87  D 75  ? F 135 D 130 ? ? 
;chain 'D' and (resid 75 through 130 )
;
7  'X-RAY DIFFRACTION' 7  F 136 D 131 ? F 145 D 142 ? ? 
;chain 'D' and (resid 131 through 142 )
;
8  'X-RAY DIFFRACTION' 8  F 146 D 143 ? F 186 D 188 ? ? 
;chain 'D' and (resid 143 through 188 )
;
9  'X-RAY DIFFRACTION' 9  H 1   A 1   ? H 114 A 128 ? ? 
;chain 'A' and (resid 1 through 128 )
;
10 'X-RAY DIFFRACTION' 10 H 115 A 129 ? H 125 A 141 ? ? 
;chain 'A' and (resid 129 through 141 )
;
11 'X-RAY DIFFRACTION' 11 H 126 A 142 ? H 136 A 154 ? ? 
;chain 'A' and (resid 142 through 154 )
;
12 'X-RAY DIFFRACTION' 12 H 137 A 155 ? H 171 A 203 ? ? 
;chain 'A' and (resid 155 through 204 )
;
13 'X-RAY DIFFRACTION' 13 I 1   B 1   ? I 120 B 133 ? ? 
;chain 'B' and (resid 1 through 133 )
;
14 'X-RAY DIFFRACTION' 14 I 121 B 134 ? I 240 B 253 ? ? 
;chain 'B' and (resid 134 through 253 )
;
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      A 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       306 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   7.76 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 C LEU 187 ? A LEU 187 
2  1 Y 1 C PHE 188 ? A PHE 188 
3  1 Y 1 D HIS -13 A B HIS 14  
4  1 Y 1 D LYS -13 B B LYS 15  
5  1 Y 1 D GLY -13 C B GLY 16  
6  1 Y 1 D SER -13 D B SER 17  
7  1 Y 1 D GLY -13 E B GLY 18  
8  1 Y 1 D GLY -13 F B GLY 19  
9  1 Y 1 D SER -13 G B SER 20  
10 1 Y 1 D ILE -13 H B ILE 21  
11 1 Y 1 D GLU -13 I B GLU 22  
12 1 Y 1 D GLY -13 J B GLY 23  
13 1 Y 1 D ARG -13 K B ARG 24  
14 1 Y 1 D GLY -13 L B GLY 25  
15 1 Y 1 D GLY -13 M B GLY 26  
16 1 Y 1 D SER -13 N B SER 27  
17 1 Y 1 D GLY -13 O B GLY 28  
18 1 Y 1 D ALA -13 P B ALA 29  
19 1 Y 1 D SER -13 Q B SER 30  
20 1 Y 1 D GLY -13 R B GLY 31  
21 1 Y 1 D ASP -13 S B ASP 32  
22 1 Y 1 D SER -13 T B SER 33  
23 1 Y 1 D GLU -13 U B GLU 34  
24 1 Y 1 D GLU 105 ? B GLU 138 
25 1 Y 1 D ALA 106 ? B ALA 139 
26 1 Y 1 D LEU 107 ? B LEU 140 
27 1 Y 1 D ASN 108 ? B ASN 141 
28 1 Y 1 D HIS 109 ? B HIS 142 
29 1 Y 1 D HIS 110 ? B HIS 143 
30 1 Y 1 D ASN 111 ? B ASN 144 
31 1 Y 1 D VAL 138 ? B VAL 171 
32 1 Y 1 D GLY 139 ? B GLY 172 
33 1 Y 1 D PRO 163 ? B PRO 196 
34 1 Y 1 D ARG 164 ? B ARG 197 
35 1 Y 1 D ARG 165 ? B ARG 198 
36 1 Y 1 D GLY 166 ? B GLY 199 
37 1 Y 1 D GLU 167 ? B GLU 200 
38 1 Y 1 D GLY 189 ? B GLY 222 
39 1 Y 1 D LEU 190 ? B LEU 223 
40 1 Y 1 D GLU 191 ? B GLU 224 
41 1 Y 1 D VAL 192 ? B VAL 225 
42 1 Y 1 D LEU 193 ? B LEU 226 
43 1 Y 1 D PHE 194 ? B PHE 227 
44 1 Y 1 D GLN 195 ? B GLN 228 
45 1 Y 1 A MET 0   ? C MET 1   
46 1 Y 1 A GLN 132 ? C GLN 119 
47 1 Y 1 A ASN 133 ? C ASN 120 
48 1 Y 1 A SER 147 ? C SER 134 
49 1 Y 1 A ASP 148 ? C ASP 135 
50 1 Y 1 A SER 159 ? C SER 146 
51 1 Y 1 A GLN 160 ? C GLN 147 
52 1 Y 1 A THR 161 ? C THR 148 
53 1 Y 1 A ASN 162 ? C ASN 149 
54 1 Y 1 A VAL 163 ? C VAL 150 
55 1 Y 1 A SER 164 ? C SER 151 
56 1 Y 1 A GLN 165 ? C GLN 152 
57 1 Y 1 A ASP 180 ? C ASP 167 
58 1 Y 1 A MET 181 ? C MET 168 
59 1 Y 1 A ARG 182 ? C ARG 169 
60 1 Y 1 A SER 183 ? C SER 170 
61 1 Y 1 A MET 184 ? C MET 171 
62 1 Y 1 A ASP 185 ? C ASP 172 
63 1 Y 1 A PHE 186 ? C PHE 173 
64 1 Y 1 A ASN 204 ? C ASN 191 
65 1 Y 1 A ALA 205 ? C ALA 192 
66 1 Y 1 A PHE 206 ? C PHE 193 
67 1 Y 1 A ASN 207 ? C ASN 194 
68 1 Y 1 A ASN 208 ? C ASN 195 
69 1 Y 1 A SER 209 ? C SER 196 
70 1 Y 1 A ILE 210 ? C ILE 197 
71 1 Y 1 A ILE 211 ? C ILE 198 
72 1 Y 1 A PRO 212 ? C PRO 199 
73 1 Y 1 A GLU 213 ? C GLU 200 
74 1 Y 1 A ASP 214 ? C ASP 201 
75 1 Y 1 A THR 215 ? C THR 202 
76 1 Y 1 A PHE 216 ? C PHE 203 
77 1 Y 1 A PHE 217 ? C PHE 204 
78 1 Y 1 A PRO 218 ? C PRO 205 
79 1 Y 1 A SER 219 ? C SER 206 
80 1 Y 1 A PRO 220 ? C PRO 207 
81 1 Y 1 A GLU 221 ? C GLU 208 
82 1 Y 1 A SER 222 ? C SER 209 
83 1 Y 1 A SER 223 ? C SER 210 
84 1 Y 1 B MET 0   ? D MET 1   
85 1 Y 1 B ASP 254 ? D ASP 242 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
EDO C1   C N N 88  
EDO O1   O N N 89  
EDO C2   C N N 90  
EDO O2   O N N 91  
EDO H11  H N N 92  
EDO H12  H N N 93  
EDO HO1  H N N 94  
EDO H21  H N N 95  
EDO H22  H N N 96  
EDO HO2  H N N 97  
GLN N    N N N 98  
GLN CA   C N S 99  
GLN C    C N N 100 
GLN O    O N N 101 
GLN CB   C N N 102 
GLN CG   C N N 103 
GLN CD   C N N 104 
GLN OE1  O N N 105 
GLN NE2  N N N 106 
GLN OXT  O N N 107 
GLN H    H N N 108 
GLN H2   H N N 109 
GLN HA   H N N 110 
GLN HB2  H N N 111 
GLN HB3  H N N 112 
GLN HG2  H N N 113 
GLN HG3  H N N 114 
GLN HE21 H N N 115 
GLN HE22 H N N 116 
GLN HXT  H N N 117 
GLU N    N N N 118 
GLU CA   C N S 119 
GLU C    C N N 120 
GLU O    O N N 121 
GLU CB   C N N 122 
GLU CG   C N N 123 
GLU CD   C N N 124 
GLU OE1  O N N 125 
GLU OE2  O N N 126 
GLU OXT  O N N 127 
GLU H    H N N 128 
GLU H2   H N N 129 
GLU HA   H N N 130 
GLU HB2  H N N 131 
GLU HB3  H N N 132 
GLU HG2  H N N 133 
GLU HG3  H N N 134 
GLU HE2  H N N 135 
GLU HXT  H N N 136 
GLY N    N N N 137 
GLY CA   C N N 138 
GLY C    C N N 139 
GLY O    O N N 140 
GLY OXT  O N N 141 
GLY H    H N N 142 
GLY H2   H N N 143 
GLY HA2  H N N 144 
GLY HA3  H N N 145 
GLY HXT  H N N 146 
HIS N    N N N 147 
HIS CA   C N S 148 
HIS C    C N N 149 
HIS O    O N N 150 
HIS CB   C N N 151 
HIS CG   C Y N 152 
HIS ND1  N Y N 153 
HIS CD2  C Y N 154 
HIS CE1  C Y N 155 
HIS NE2  N Y N 156 
HIS OXT  O N N 157 
HIS H    H N N 158 
HIS H2   H N N 159 
HIS HA   H N N 160 
HIS HB2  H N N 161 
HIS HB3  H N N 162 
HIS HD1  H N N 163 
HIS HD2  H N N 164 
HIS HE1  H N N 165 
HIS HE2  H N N 166 
HIS HXT  H N N 167 
HOH O    O N N 168 
HOH H1   H N N 169 
HOH H2   H N N 170 
ILE N    N N N 171 
ILE CA   C N S 172 
ILE C    C N N 173 
ILE O    O N N 174 
ILE CB   C N S 175 
ILE CG1  C N N 176 
ILE CG2  C N N 177 
ILE CD1  C N N 178 
ILE OXT  O N N 179 
ILE H    H N N 180 
ILE H2   H N N 181 
ILE HA   H N N 182 
ILE HB   H N N 183 
ILE HG12 H N N 184 
ILE HG13 H N N 185 
ILE HG21 H N N 186 
ILE HG22 H N N 187 
ILE HG23 H N N 188 
ILE HD11 H N N 189 
ILE HD12 H N N 190 
ILE HD13 H N N 191 
ILE HXT  H N N 192 
LEU N    N N N 193 
LEU CA   C N S 194 
LEU C    C N N 195 
LEU O    O N N 196 
LEU CB   C N N 197 
LEU CG   C N N 198 
LEU CD1  C N N 199 
LEU CD2  C N N 200 
LEU OXT  O N N 201 
LEU H    H N N 202 
LEU H2   H N N 203 
LEU HA   H N N 204 
LEU HB2  H N N 205 
LEU HB3  H N N 206 
LEU HG   H N N 207 
LEU HD11 H N N 208 
LEU HD12 H N N 209 
LEU HD13 H N N 210 
LEU HD21 H N N 211 
LEU HD22 H N N 212 
LEU HD23 H N N 213 
LEU HXT  H N N 214 
LYS N    N N N 215 
LYS CA   C N S 216 
LYS C    C N N 217 
LYS O    O N N 218 
LYS CB   C N N 219 
LYS CG   C N N 220 
LYS CD   C N N 221 
LYS CE   C N N 222 
LYS NZ   N N N 223 
LYS OXT  O N N 224 
LYS H    H N N 225 
LYS H2   H N N 226 
LYS HA   H N N 227 
LYS HB2  H N N 228 
LYS HB3  H N N 229 
LYS HG2  H N N 230 
LYS HG3  H N N 231 
LYS HD2  H N N 232 
LYS HD3  H N N 233 
LYS HE2  H N N 234 
LYS HE3  H N N 235 
LYS HZ1  H N N 236 
LYS HZ2  H N N 237 
LYS HZ3  H N N 238 
LYS HXT  H N N 239 
MET N    N N N 240 
MET CA   C N S 241 
MET C    C N N 242 
MET O    O N N 243 
MET CB   C N N 244 
MET CG   C N N 245 
MET SD   S N N 246 
MET CE   C N N 247 
MET OXT  O N N 248 
MET H    H N N 249 
MET H2   H N N 250 
MET HA   H N N 251 
MET HB2  H N N 252 
MET HB3  H N N 253 
MET HG2  H N N 254 
MET HG3  H N N 255 
MET HE1  H N N 256 
MET HE2  H N N 257 
MET HE3  H N N 258 
MET HXT  H N N 259 
NAG C1   C N R 260 
NAG C2   C N R 261 
NAG C3   C N R 262 
NAG C4   C N S 263 
NAG C5   C N R 264 
NAG C6   C N N 265 
NAG C7   C N N 266 
NAG C8   C N N 267 
NAG N2   N N N 268 
NAG O1   O N N 269 
NAG O3   O N N 270 
NAG O4   O N N 271 
NAG O5   O N N 272 
NAG O6   O N N 273 
NAG O7   O N N 274 
NAG H1   H N N 275 
NAG H2   H N N 276 
NAG H3   H N N 277 
NAG H4   H N N 278 
NAG H5   H N N 279 
NAG H61  H N N 280 
NAG H62  H N N 281 
NAG H81  H N N 282 
NAG H82  H N N 283 
NAG H83  H N N 284 
NAG HN2  H N N 285 
NAG HO1  H N N 286 
NAG HO3  H N N 287 
NAG HO4  H N N 288 
NAG HO6  H N N 289 
PHE N    N N N 290 
PHE CA   C N S 291 
PHE C    C N N 292 
PHE O    O N N 293 
PHE CB   C N N 294 
PHE CG   C Y N 295 
PHE CD1  C Y N 296 
PHE CD2  C Y N 297 
PHE CE1  C Y N 298 
PHE CE2  C Y N 299 
PHE CZ   C Y N 300 
PHE OXT  O N N 301 
PHE H    H N N 302 
PHE H2   H N N 303 
PHE HA   H N N 304 
PHE HB2  H N N 305 
PHE HB3  H N N 306 
PHE HD1  H N N 307 
PHE HD2  H N N 308 
PHE HE1  H N N 309 
PHE HE2  H N N 310 
PHE HZ   H N N 311 
PHE HXT  H N N 312 
PRO N    N N N 313 
PRO CA   C N S 314 
PRO C    C N N 315 
PRO O    O N N 316 
PRO CB   C N N 317 
PRO CG   C N N 318 
PRO CD   C N N 319 
PRO OXT  O N N 320 
PRO H    H N N 321 
PRO HA   H N N 322 
PRO HB2  H N N 323 
PRO HB3  H N N 324 
PRO HG2  H N N 325 
PRO HG3  H N N 326 
PRO HD2  H N N 327 
PRO HD3  H N N 328 
PRO HXT  H N N 329 
SER N    N N N 330 
SER CA   C N S 331 
SER C    C N N 332 
SER O    O N N 333 
SER CB   C N N 334 
SER OG   O N N 335 
SER OXT  O N N 336 
SER H    H N N 337 
SER H2   H N N 338 
SER HA   H N N 339 
SER HB2  H N N 340 
SER HB3  H N N 341 
SER HG   H N N 342 
SER HXT  H N N 343 
THR N    N N N 344 
THR CA   C N S 345 
THR C    C N N 346 
THR O    O N N 347 
THR CB   C N R 348 
THR OG1  O N N 349 
THR CG2  C N N 350 
THR OXT  O N N 351 
THR H    H N N 352 
THR H2   H N N 353 
THR HA   H N N 354 
THR HB   H N N 355 
THR HG1  H N N 356 
THR HG21 H N N 357 
THR HG22 H N N 358 
THR HG23 H N N 359 
THR HXT  H N N 360 
TRP N    N N N 361 
TRP CA   C N S 362 
TRP C    C N N 363 
TRP O    O N N 364 
TRP CB   C N N 365 
TRP CG   C Y N 366 
TRP CD1  C Y N 367 
TRP CD2  C Y N 368 
TRP NE1  N Y N 369 
TRP CE2  C Y N 370 
TRP CE3  C Y N 371 
TRP CZ2  C Y N 372 
TRP CZ3  C Y N 373 
TRP CH2  C Y N 374 
TRP OXT  O N N 375 
TRP H    H N N 376 
TRP H2   H N N 377 
TRP HA   H N N 378 
TRP HB2  H N N 379 
TRP HB3  H N N 380 
TRP HD1  H N N 381 
TRP HE1  H N N 382 
TRP HE3  H N N 383 
TRP HZ2  H N N 384 
TRP HZ3  H N N 385 
TRP HH2  H N N 386 
TRP HXT  H N N 387 
TYR N    N N N 388 
TYR CA   C N S 389 
TYR C    C N N 390 
TYR O    O N N 391 
TYR CB   C N N 392 
TYR CG   C Y N 393 
TYR CD1  C Y N 394 
TYR CD2  C Y N 395 
TYR CE1  C Y N 396 
TYR CE2  C Y N 397 
TYR CZ   C Y N 398 
TYR OH   O N N 399 
TYR OXT  O N N 400 
TYR H    H N N 401 
TYR H2   H N N 402 
TYR HA   H N N 403 
TYR HB2  H N N 404 
TYR HB3  H N N 405 
TYR HD1  H N N 406 
TYR HD2  H N N 407 
TYR HE1  H N N 408 
TYR HE2  H N N 409 
TYR HH   H N N 410 
TYR HXT  H N N 411 
VAL N    N N N 412 
VAL CA   C N S 413 
VAL C    C N N 414 
VAL O    O N N 415 
VAL CB   C N N 416 
VAL CG1  C N N 417 
VAL CG2  C N N 418 
VAL OXT  O N N 419 
VAL H    H N N 420 
VAL H2   H N N 421 
VAL HA   H N N 422 
VAL HB   H N N 423 
VAL HG11 H N N 424 
VAL HG12 H N N 425 
VAL HG13 H N N 426 
VAL HG21 H N N 427 
VAL HG22 H N N 428 
VAL HG23 H N N 429 
VAL HXT  H N N 430 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
EDO C1  O1   sing N N 83  
EDO C1  C2   sing N N 84  
EDO C1  H11  sing N N 85  
EDO C1  H12  sing N N 86  
EDO O1  HO1  sing N N 87  
EDO C2  O2   sing N N 88  
EDO C2  H21  sing N N 89  
EDO C2  H22  sing N N 90  
EDO O2  HO2  sing N N 91  
GLN N   CA   sing N N 92  
GLN N   H    sing N N 93  
GLN N   H2   sing N N 94  
GLN CA  C    sing N N 95  
GLN CA  CB   sing N N 96  
GLN CA  HA   sing N N 97  
GLN C   O    doub N N 98  
GLN C   OXT  sing N N 99  
GLN CB  CG   sing N N 100 
GLN CB  HB2  sing N N 101 
GLN CB  HB3  sing N N 102 
GLN CG  CD   sing N N 103 
GLN CG  HG2  sing N N 104 
GLN CG  HG3  sing N N 105 
GLN CD  OE1  doub N N 106 
GLN CD  NE2  sing N N 107 
GLN NE2 HE21 sing N N 108 
GLN NE2 HE22 sing N N 109 
GLN OXT HXT  sing N N 110 
GLU N   CA   sing N N 111 
GLU N   H    sing N N 112 
GLU N   H2   sing N N 113 
GLU CA  C    sing N N 114 
GLU CA  CB   sing N N 115 
GLU CA  HA   sing N N 116 
GLU C   O    doub N N 117 
GLU C   OXT  sing N N 118 
GLU CB  CG   sing N N 119 
GLU CB  HB2  sing N N 120 
GLU CB  HB3  sing N N 121 
GLU CG  CD   sing N N 122 
GLU CG  HG2  sing N N 123 
GLU CG  HG3  sing N N 124 
GLU CD  OE1  doub N N 125 
GLU CD  OE2  sing N N 126 
GLU OE2 HE2  sing N N 127 
GLU OXT HXT  sing N N 128 
GLY N   CA   sing N N 129 
GLY N   H    sing N N 130 
GLY N   H2   sing N N 131 
GLY CA  C    sing N N 132 
GLY CA  HA2  sing N N 133 
GLY CA  HA3  sing N N 134 
GLY C   O    doub N N 135 
GLY C   OXT  sing N N 136 
GLY OXT HXT  sing N N 137 
HIS N   CA   sing N N 138 
HIS N   H    sing N N 139 
HIS N   H2   sing N N 140 
HIS CA  C    sing N N 141 
HIS CA  CB   sing N N 142 
HIS CA  HA   sing N N 143 
HIS C   O    doub N N 144 
HIS C   OXT  sing N N 145 
HIS CB  CG   sing N N 146 
HIS CB  HB2  sing N N 147 
HIS CB  HB3  sing N N 148 
HIS CG  ND1  sing Y N 149 
HIS CG  CD2  doub Y N 150 
HIS ND1 CE1  doub Y N 151 
HIS ND1 HD1  sing N N 152 
HIS CD2 NE2  sing Y N 153 
HIS CD2 HD2  sing N N 154 
HIS CE1 NE2  sing Y N 155 
HIS CE1 HE1  sing N N 156 
HIS NE2 HE2  sing N N 157 
HIS OXT HXT  sing N N 158 
HOH O   H1   sing N N 159 
HOH O   H2   sing N N 160 
ILE N   CA   sing N N 161 
ILE N   H    sing N N 162 
ILE N   H2   sing N N 163 
ILE CA  C    sing N N 164 
ILE CA  CB   sing N N 165 
ILE CA  HA   sing N N 166 
ILE C   O    doub N N 167 
ILE C   OXT  sing N N 168 
ILE CB  CG1  sing N N 169 
ILE CB  CG2  sing N N 170 
ILE CB  HB   sing N N 171 
ILE CG1 CD1  sing N N 172 
ILE CG1 HG12 sing N N 173 
ILE CG1 HG13 sing N N 174 
ILE CG2 HG21 sing N N 175 
ILE CG2 HG22 sing N N 176 
ILE CG2 HG23 sing N N 177 
ILE CD1 HD11 sing N N 178 
ILE CD1 HD12 sing N N 179 
ILE CD1 HD13 sing N N 180 
ILE OXT HXT  sing N N 181 
LEU N   CA   sing N N 182 
LEU N   H    sing N N 183 
LEU N   H2   sing N N 184 
LEU CA  C    sing N N 185 
LEU CA  CB   sing N N 186 
LEU CA  HA   sing N N 187 
LEU C   O    doub N N 188 
LEU C   OXT  sing N N 189 
LEU CB  CG   sing N N 190 
LEU CB  HB2  sing N N 191 
LEU CB  HB3  sing N N 192 
LEU CG  CD1  sing N N 193 
LEU CG  CD2  sing N N 194 
LEU CG  HG   sing N N 195 
LEU CD1 HD11 sing N N 196 
LEU CD1 HD12 sing N N 197 
LEU CD1 HD13 sing N N 198 
LEU CD2 HD21 sing N N 199 
LEU CD2 HD22 sing N N 200 
LEU CD2 HD23 sing N N 201 
LEU OXT HXT  sing N N 202 
LYS N   CA   sing N N 203 
LYS N   H    sing N N 204 
LYS N   H2   sing N N 205 
LYS CA  C    sing N N 206 
LYS CA  CB   sing N N 207 
LYS CA  HA   sing N N 208 
LYS C   O    doub N N 209 
LYS C   OXT  sing N N 210 
LYS CB  CG   sing N N 211 
LYS CB  HB2  sing N N 212 
LYS CB  HB3  sing N N 213 
LYS CG  CD   sing N N 214 
LYS CG  HG2  sing N N 215 
LYS CG  HG3  sing N N 216 
LYS CD  CE   sing N N 217 
LYS CD  HD2  sing N N 218 
LYS CD  HD3  sing N N 219 
LYS CE  NZ   sing N N 220 
LYS CE  HE2  sing N N 221 
LYS CE  HE3  sing N N 222 
LYS NZ  HZ1  sing N N 223 
LYS NZ  HZ2  sing N N 224 
LYS NZ  HZ3  sing N N 225 
LYS OXT HXT  sing N N 226 
MET N   CA   sing N N 227 
MET N   H    sing N N 228 
MET N   H2   sing N N 229 
MET CA  C    sing N N 230 
MET CA  CB   sing N N 231 
MET CA  HA   sing N N 232 
MET C   O    doub N N 233 
MET C   OXT  sing N N 234 
MET CB  CG   sing N N 235 
MET CB  HB2  sing N N 236 
MET CB  HB3  sing N N 237 
MET CG  SD   sing N N 238 
MET CG  HG2  sing N N 239 
MET CG  HG3  sing N N 240 
MET SD  CE   sing N N 241 
MET CE  HE1  sing N N 242 
MET CE  HE2  sing N N 243 
MET CE  HE3  sing N N 244 
MET OXT HXT  sing N N 245 
NAG C1  C2   sing N N 246 
NAG C1  O1   sing N N 247 
NAG C1  O5   sing N N 248 
NAG C1  H1   sing N N 249 
NAG C2  C3   sing N N 250 
NAG C2  N2   sing N N 251 
NAG C2  H2   sing N N 252 
NAG C3  C4   sing N N 253 
NAG C3  O3   sing N N 254 
NAG C3  H3   sing N N 255 
NAG C4  C5   sing N N 256 
NAG C4  O4   sing N N 257 
NAG C4  H4   sing N N 258 
NAG C5  C6   sing N N 259 
NAG C5  O5   sing N N 260 
NAG C5  H5   sing N N 261 
NAG C6  O6   sing N N 262 
NAG C6  H61  sing N N 263 
NAG C6  H62  sing N N 264 
NAG C7  C8   sing N N 265 
NAG C7  N2   sing N N 266 
NAG C7  O7   doub N N 267 
NAG C8  H81  sing N N 268 
NAG C8  H82  sing N N 269 
NAG C8  H83  sing N N 270 
NAG N2  HN2  sing N N 271 
NAG O1  HO1  sing N N 272 
NAG O3  HO3  sing N N 273 
NAG O4  HO4  sing N N 274 
NAG O6  HO6  sing N N 275 
PHE N   CA   sing N N 276 
PHE N   H    sing N N 277 
PHE N   H2   sing N N 278 
PHE CA  C    sing N N 279 
PHE CA  CB   sing N N 280 
PHE CA  HA   sing N N 281 
PHE C   O    doub N N 282 
PHE C   OXT  sing N N 283 
PHE CB  CG   sing N N 284 
PHE CB  HB2  sing N N 285 
PHE CB  HB3  sing N N 286 
PHE CG  CD1  doub Y N 287 
PHE CG  CD2  sing Y N 288 
PHE CD1 CE1  sing Y N 289 
PHE CD1 HD1  sing N N 290 
PHE CD2 CE2  doub Y N 291 
PHE CD2 HD2  sing N N 292 
PHE CE1 CZ   doub Y N 293 
PHE CE1 HE1  sing N N 294 
PHE CE2 CZ   sing Y N 295 
PHE CE2 HE2  sing N N 296 
PHE CZ  HZ   sing N N 297 
PHE OXT HXT  sing N N 298 
PRO N   CA   sing N N 299 
PRO N   CD   sing N N 300 
PRO N   H    sing N N 301 
PRO CA  C    sing N N 302 
PRO CA  CB   sing N N 303 
PRO CA  HA   sing N N 304 
PRO C   O    doub N N 305 
PRO C   OXT  sing N N 306 
PRO CB  CG   sing N N 307 
PRO CB  HB2  sing N N 308 
PRO CB  HB3  sing N N 309 
PRO CG  CD   sing N N 310 
PRO CG  HG2  sing N N 311 
PRO CG  HG3  sing N N 312 
PRO CD  HD2  sing N N 313 
PRO CD  HD3  sing N N 314 
PRO OXT HXT  sing N N 315 
SER N   CA   sing N N 316 
SER N   H    sing N N 317 
SER N   H2   sing N N 318 
SER CA  C    sing N N 319 
SER CA  CB   sing N N 320 
SER CA  HA   sing N N 321 
SER C   O    doub N N 322 
SER C   OXT  sing N N 323 
SER CB  OG   sing N N 324 
SER CB  HB2  sing N N 325 
SER CB  HB3  sing N N 326 
SER OG  HG   sing N N 327 
SER OXT HXT  sing N N 328 
THR N   CA   sing N N 329 
THR N   H    sing N N 330 
THR N   H2   sing N N 331 
THR CA  C    sing N N 332 
THR CA  CB   sing N N 333 
THR CA  HA   sing N N 334 
THR C   O    doub N N 335 
THR C   OXT  sing N N 336 
THR CB  OG1  sing N N 337 
THR CB  CG2  sing N N 338 
THR CB  HB   sing N N 339 
THR OG1 HG1  sing N N 340 
THR CG2 HG21 sing N N 341 
THR CG2 HG22 sing N N 342 
THR CG2 HG23 sing N N 343 
THR OXT HXT  sing N N 344 
TRP N   CA   sing N N 345 
TRP N   H    sing N N 346 
TRP N   H2   sing N N 347 
TRP CA  C    sing N N 348 
TRP CA  CB   sing N N 349 
TRP CA  HA   sing N N 350 
TRP C   O    doub N N 351 
TRP C   OXT  sing N N 352 
TRP CB  CG   sing N N 353 
TRP CB  HB2  sing N N 354 
TRP CB  HB3  sing N N 355 
TRP CG  CD1  doub Y N 356 
TRP CG  CD2  sing Y N 357 
TRP CD1 NE1  sing Y N 358 
TRP CD1 HD1  sing N N 359 
TRP CD2 CE2  doub Y N 360 
TRP CD2 CE3  sing Y N 361 
TRP NE1 CE2  sing Y N 362 
TRP NE1 HE1  sing N N 363 
TRP CE2 CZ2  sing Y N 364 
TRP CE3 CZ3  doub Y N 365 
TRP CE3 HE3  sing N N 366 
TRP CZ2 CH2  doub Y N 367 
TRP CZ2 HZ2  sing N N 368 
TRP CZ3 CH2  sing Y N 369 
TRP CZ3 HZ3  sing N N 370 
TRP CH2 HH2  sing N N 371 
TRP OXT HXT  sing N N 372 
TYR N   CA   sing N N 373 
TYR N   H    sing N N 374 
TYR N   H2   sing N N 375 
TYR CA  C    sing N N 376 
TYR CA  CB   sing N N 377 
TYR CA  HA   sing N N 378 
TYR C   O    doub N N 379 
TYR C   OXT  sing N N 380 
TYR CB  CG   sing N N 381 
TYR CB  HB2  sing N N 382 
TYR CB  HB3  sing N N 383 
TYR CG  CD1  doub Y N 384 
TYR CG  CD2  sing Y N 385 
TYR CD1 CE1  sing Y N 386 
TYR CD1 HD1  sing N N 387 
TYR CD2 CE2  doub Y N 388 
TYR CD2 HD2  sing N N 389 
TYR CE1 CZ   doub Y N 390 
TYR CE1 HE1  sing N N 391 
TYR CE2 CZ   sing Y N 392 
TYR CE2 HE2  sing N N 393 
TYR CZ  OH   sing N N 394 
TYR OH  HH   sing N N 395 
TYR OXT HXT  sing N N 396 
VAL N   CA   sing N N 397 
VAL N   H    sing N N 398 
VAL N   H2   sing N N 399 
VAL CA  C    sing N N 400 
VAL CA  CB   sing N N 401 
VAL CA  HA   sing N N 402 
VAL C   O    doub N N 403 
VAL C   OXT  sing N N 404 
VAL CB  CG1  sing N N 405 
VAL CB  CG2  sing N N 406 
VAL CB  HB   sing N N 407 
VAL CG1 HG11 sing N N 408 
VAL CG1 HG12 sing N N 409 
VAL CG1 HG13 sing N N 410 
VAL CG2 HG21 sing N N 411 
VAL CG2 HG22 sing N N 412 
VAL CG2 HG23 sing N N 413 
VAL OXT HXT  sing N N 414 
# 
_pdbx_audit_support.funding_organization   'National Health and Medical Research Council (NHMRC, Australia)' 
_pdbx_audit_support.country                Australia 
_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   4P23 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'R 3 :H' 
_space_group.name_Hall        'R 3' 
_space_group.IT_number        146 
_space_group.crystal_system   trigonal 
_space_group.id               1 
# 
_atom_sites.entry_id                    9AUD 
_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]   0.005093 
_atom_sites.fract_transf_matrix[1][2]   0.002941 
_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]   0.005881 
_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]   0.012969 
_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 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C   ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N   ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O   ? ? 7.96527 ?       ? ? 9.05267  ?        ? ? 0.0 
;1-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O1- ? ? 5.12366 3.84317 ? ? 3.49406  27.47979 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S   ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
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   . ASP A 1 1   ? 67.59171  31.58958  38.88899  1.000 88.07410  ?  1   ASP C N   1 
ATOM   2    C CA  . ASP A 1 1   ? 67.09885  31.27902  37.55229  1.000 111.13640 ?  1   ASP C CA  1 
ATOM   3    C C   . ASP A 1 1   ? 65.57526  31.18350  37.55443  1.000 111.62390 ?  1   ASP C C   1 
ATOM   4    O O   . ASP A 1 1   ? 64.96142  30.96270  38.59844  1.000 112.74551 ?  1   ASP C O   1 
ATOM   5    C CB  . ASP A 1 1   ? 67.71734  29.97518  37.04218  1.000 122.54927 ?  1   ASP C CB  1 
ATOM   6    C CG  . ASP A 1 1   ? 67.51863  29.77867  35.55200  1.000 131.16251 ?  1   ASP C CG  1 
ATOM   7    O OD1 . ASP A 1 1   ? 68.10331  30.55420  34.76636  1.000 134.74845 ?  1   ASP C OD1 1 
ATOM   8    O OD2 . ASP A 1 1   ? 66.77962  28.84878  35.16621  1.000 141.12182 ?  1   ASP C OD2 1 
ATOM   9    N N   . ILE A 1 2   ? 64.96922  31.35149  36.38173  1.000 94.24026  ?  2   ILE C N   1 
ATOM   10   C CA  . ILE A 1 2   ? 63.51909  31.34913  36.22582  1.000 96.74431  ?  2   ILE C CA  1 
ATOM   11   C C   . ILE A 1 2   ? 63.11791  30.11304  35.43300  1.000 87.58726  ?  2   ILE C C   1 
ATOM   12   O O   . ILE A 1 2   ? 63.66626  29.85310  34.35495  1.000 97.03837  ?  2   ILE C O   1 
ATOM   13   C CB  . ILE A 1 2   ? 63.02759  32.63335  35.53577  1.000 84.23202  ?  2   ILE C CB  1 
ATOM   14   C CG1 . ILE A 1 2   ? 63.46591  33.86359  36.33393  1.000 66.48203  ?  2   ILE C CG1 1 
ATOM   15   C CG2 . ILE A 1 2   ? 61.51559  32.60804  35.37327  1.000 85.84105  ?  2   ILE C CG2 1 
ATOM   16   C CD1 . ILE A 1 2   ? 63.01393  35.17660  35.73593  1.000 71.47690  ?  2   ILE C CD1 1 
ATOM   17   N N   . GLU A 1 3   ? 62.16253  29.35541  35.96503  1.000 82.17517  ?  3   GLU C N   1 
ATOM   18   C CA  . GLU A 1 3   ? 61.67935  28.13449  35.33379  1.000 80.23041  ?  3   GLU C CA  1 
ATOM   19   C C   . GLU A 1 3   ? 60.43043  28.43809  34.51700  1.000 83.13949  ?  3   GLU C C   1 
ATOM   20   O O   . GLU A 1 3   ? 59.48896  29.05983  35.02103  1.000 94.67007  ?  3   GLU C O   1 
ATOM   21   C CB  . GLU A 1 3   ? 61.37751  27.06178  36.38163  1.000 75.78523  ?  3   GLU C CB  1 
ATOM   22   N N   . ALA A 1 4   ? 60.42532  27.99428  33.26250  1.000 74.63952  ?  4   ALA C N   1 
ATOM   23   C CA  . ALA A 1 4   ? 59.30316  28.23000  32.36457  1.000 60.02277  ?  4   ALA C CA  1 
ATOM   24   C C   . ALA A 1 4   ? 59.40833  27.26653  31.19121  1.000 62.54295  ?  4   ALA C C   1 
ATOM   25   O O   . ALA A 1 4   ? 60.40329  26.55560  31.03144  1.000 89.29074  ?  4   ALA C O   1 
ATOM   26   C CB  . ALA A 1 4   ? 59.26995  29.68308  31.88045  1.000 56.20368  ?  4   ALA C CB  1 
ATOM   27   N N   . ASP A 1 5   ? 58.35947  27.25110  30.36866  1.000 61.16453  ?  5   ASP C N   1 
ATOM   28   C CA  . ASP A 1 5   ? 58.34811  26.42747  29.16619  1.000 54.68874  ?  5   ASP C CA  1 
ATOM   29   C C   . ASP A 1 5   ? 58.96385  27.13248  27.96753  1.000 50.08165  ?  5   ASP C C   1 
ATOM   30   O O   . ASP A 1 5   ? 59.56482  26.47286  27.11210  1.000 65.61662  ?  5   ASP C O   1 
ATOM   31   C CB  . ASP A 1 5   ? 56.91676  26.00412  28.82267  1.000 55.90653  ?  5   ASP C CB  1 
ATOM   32   C CG  . ASP A 1 5   ? 56.32704  25.05724  29.84696  1.000 72.18283  ?  5   ASP C CG  1 
ATOM   33   O OD1 . ASP A 1 5   ? 56.96302  24.84736  30.90114  1.000 94.02997  ?  5   ASP C OD1 1 
ATOM   34   O OD2 . ASP A 1 5   ? 55.22846  24.51869  29.59511  1.000 75.49054  -1 5   ASP C OD2 1 
ATOM   35   N N   . HIS A 1 6   ? 58.82446  28.45342  27.88332  1.000 53.47094  ?  6   HIS C N   1 
ATOM   36   C CA  . HIS A 1 6   ? 59.38115  29.22972  26.78682  1.000 46.44885  ?  6   HIS C CA  1 
ATOM   37   C C   . HIS A 1 6   ? 59.84610  30.57871  27.31340  1.000 46.99217  ?  6   HIS C C   1 
ATOM   38   O O   . HIS A 1 6   ? 59.25263  31.14079  28.23752  1.000 58.80459  ?  6   HIS C O   1 
ATOM   39   C CB  . HIS A 1 6   ? 58.36150  29.43349  25.65761  1.000 54.62317  ?  6   HIS C CB  1 
ATOM   40   C CG  . HIS A 1 6   ? 57.87482  28.15807  25.04392  1.000 56.60996  ?  6   HIS C CG  1 
ATOM   41   N ND1 . HIS A 1 6   ? 58.53213  27.53331  24.00620  1.000 53.54408  ?  6   HIS C ND1 1 
ATOM   42   C CD2 . HIS A 1 6   ? 56.79384  27.39105  25.32053  1.000 60.05023  ?  6   HIS C CD2 1 
ATOM   43   C CE1 . HIS A 1 6   ? 57.87811  26.43561  23.67087  1.000 50.92522  ?  6   HIS C CE1 1 
ATOM   44   N NE2 . HIS A 1 6   ? 56.81958  26.32607  24.45322  1.000 75.71478  ?  6   HIS C NE2 1 
ATOM   45   N N   . VAL A 1 7   ? 60.91850  31.09133  26.71648  1.000 40.29586  ?  7   VAL C N   1 
ATOM   46   C CA  . VAL A 1 7   ? 61.48113  32.38981  27.06892  1.000 45.40576  ?  7   VAL C CA  1 
ATOM   47   C C   . VAL A 1 7   ? 61.57962  33.20613  25.78879  1.000 53.89254  ?  7   VAL C C   1 
ATOM   48   O O   . VAL A 1 7   ? 62.38359  32.88631  24.90399  1.000 57.22611  ?  7   VAL C O   1 
ATOM   49   C CB  . VAL A 1 7   ? 62.85411  32.27083  27.74411  1.000 44.88149  ?  7   VAL C CB  1 
ATOM   50   C CG1 . VAL A 1 7   ? 63.39370  33.65162  28.08459  1.000 54.14602  ?  7   VAL C CG1 1 
ATOM   51   C CG2 . VAL A 1 7   ? 62.76242  31.40648  28.99137  1.000 64.11938  ?  7   VAL C CG2 1 
ATOM   52   N N   . GLY A 1 8   ? 60.76639  34.25308  25.68601  1.000 43.52613  ?  8   GLY C N   1 
ATOM   53   C CA  . GLY A 1 8   ? 60.81294  35.13175  24.53591  1.000 42.22557  ?  8   GLY C CA  1 
ATOM   54   C C   . GLY A 1 8   ? 61.48896  36.45043  24.84502  1.000 40.04418  ?  8   GLY C C   1 
ATOM   55   O O   . GLY A 1 8   ? 60.91445  37.30440  25.52650  1.000 59.93881  ?  8   GLY C O   1 
ATOM   56   N N   . THR A 1 9   ? 62.71604  36.62642  24.35888  1.000 41.57871  ?  9   THR C N   1 
ATOM   57   C CA  . THR A 1 9   ? 63.46100  37.86659  24.56954  1.000 48.66499  ?  9   THR C CA  1 
ATOM   58   C C   . THR A 1 9   ? 63.11641  38.80420  23.42141  1.000 40.45757  ?  9   THR C C   1 
ATOM   59   O O   . THR A 1 9   ? 63.78919  38.83981  22.39039  1.000 50.21545  ?  9   THR C O   1 
ATOM   60   C CB  . THR A 1 9   ? 64.95790  37.60090  24.65525  1.000 50.11767  ?  9   THR C CB  1 
ATOM   61   O OG1 . THR A 1 9   ? 65.18249  36.30906  25.23304  1.000 55.01427  ?  9   THR C OG1 1 
ATOM   62   C CG2 . THR A 1 9   ? 65.62057  38.65009  25.52960  1.000 39.99898  ?  9   THR C CG2 1 
ATOM   63   N N   . TYR A 1 10  ? 62.04605  39.57386  23.60630  1.000 56.59846  ?  10  TYR C N   1 
ATOM   64   C CA  . TYR A 1 10  ? 61.51299  40.43561  22.55213  1.000 54.55448  ?  10  TYR C CA  1 
ATOM   65   C C   . TYR A 1 10  ? 62.11910  41.83280  22.68064  1.000 54.54161  ?  10  TYR C C   1 
ATOM   66   O O   . TYR A 1 10  ? 61.46525  42.81553  23.03692  1.000 43.25639  ?  10  TYR C O   1 
ATOM   67   C CB  . TYR A 1 10  ? 59.99244  40.45546  22.61517  1.000 40.67352  ?  10  TYR C CB  1 
ATOM   68   C CG  . TYR A 1 10  ? 59.39784  39.07442  22.47602  1.000 48.89264  ?  10  TYR C CG  1 
ATOM   69   C CD1 . TYR A 1 10  ? 59.86192  38.19783  21.50307  1.000 45.42240  ?  10  TYR C CD1 1 
ATOM   70   C CD2 . TYR A 1 10  ? 58.39797  38.63404  23.33169  1.000 43.28510  ?  10  TYR C CD2 1 
ATOM   71   C CE1 . TYR A 1 10  ? 59.33306  36.93037  21.37162  1.000 40.93068  ?  10  TYR C CE1 1 
ATOM   72   C CE2 . TYR A 1 10  ? 57.86188  37.36497  23.20813  1.000 50.76190  ?  10  TYR C CE2 1 
ATOM   73   C CZ  . TYR A 1 10  ? 58.33392  36.51854  22.22605  1.000 42.78080  ?  10  TYR C CZ  1 
ATOM   74   O OH  . TYR A 1 10  ? 57.80663  35.25527  22.09608  1.000 52.29577  ?  10  TYR C OH  1 
ATOM   75   N N   . GLY A 1 11  ? 63.41143  41.89676  22.37322  1.000 60.67617  ?  11  GLY C N   1 
ATOM   76   C CA  . GLY A 1 11  ? 64.15799  43.13300  22.45780  1.000 40.73693  ?  11  GLY C CA  1 
ATOM   77   C C   . GLY A 1 11  ? 65.45636  42.98097  23.22069  1.000 33.20007  ?  11  GLY C C   1 
ATOM   78   O O   . GLY A 1 11  ? 65.44976  42.83092  24.44510  1.000 34.64303  ?  11  GLY C O   1 
ATOM   79   N N   . ILE A 1 12  ? 66.57746  43.00307  22.50553  1.000 36.90000  ?  12  ILE C N   1 
ATOM   80   C CA  . ILE A 1 12  ? 67.90640  43.01429  23.10694  1.000 46.32983  ?  12  ILE C CA  1 
ATOM   81   C C   . ILE A 1 12  ? 68.67032  44.16931  22.47819  1.000 44.10411  ?  12  ILE C C   1 
ATOM   82   O O   . ILE A 1 12  ? 69.06178  44.09464  21.30709  1.000 49.84582  ?  12  ILE C O   1 
ATOM   83   C CB  . ILE A 1 12  ? 68.65839  41.69193  22.90577  1.000 44.14424  ?  12  ILE C CB  1 
ATOM   84   C CG1 . ILE A 1 12  ? 67.93822  40.55100  23.62178  1.000 50.48388  ?  12  ILE C CG1 1 
ATOM   85   C CG2 . ILE A 1 12  ? 70.08432  41.81238  23.41450  1.000 28.16892  ?  12  ILE C CG2 1 
ATOM   86   C CD1 . ILE A 1 12  ? 68.64212  39.21713  23.50285  1.000 46.22264  ?  12  ILE C CD1 1 
ATOM   87   N N   . SER A 1 13  ? 68.87670  45.23497  23.24423  1.000 48.52393  ?  13  SER C N   1 
ATOM   88   C CA  . SER A 1 13  ? 69.61408  46.40539  22.78796  1.000 42.57677  ?  13  SER C CA  1 
ATOM   89   C C   . SER A 1 13  ? 70.98790  46.40490  23.44265  1.000 48.36455  ?  13  SER C C   1 
ATOM   90   O O   . SER A 1 13  ? 71.09253  46.35968  24.67349  1.000 49.99758  ?  13  SER C O   1 
ATOM   91   C CB  . SER A 1 13  ? 68.86094  47.69360  23.11918  1.000 44.99505  ?  13  SER C CB  1 
ATOM   92   O OG  . SER A 1 13  ? 67.62041  47.74804  22.43805  1.000 63.73926  ?  13  SER C OG  1 
ATOM   93   N N   . VAL A 1 14  ? 72.03455  46.44265  22.62130  1.000 38.83953  ?  14  VAL C N   1 
ATOM   94   C CA  . VAL A 1 14  ? 73.41031  46.53536  23.09351  1.000 39.75243  ?  14  VAL C CA  1 
ATOM   95   C C   . VAL A 1 14  ? 74.08486  47.68244  22.35696  1.000 35.97932  ?  14  VAL C C   1 
ATOM   96   O O   . VAL A 1 14  ? 74.03121  47.75035  21.12391  1.000 39.22333  ?  14  VAL C O   1 
ATOM   97   C CB  . VAL A 1 14  ? 74.18834  45.22258  22.87837  1.000 37.99648  ?  14  VAL C CB  1 
ATOM   98   C CG1 . VAL A 1 14  ? 75.58901  45.34180  23.45407  1.000 33.75076  ?  14  VAL C CG1 1 
ATOM   99   C CG2 . VAL A 1 14  ? 73.44984  44.05192  23.50887  1.000 42.12146  ?  14  VAL C CG2 1 
ATOM   100  N N   . TYR A 1 15  ? 74.71292  48.58273  23.10906  1.000 41.88982  ?  15  TYR C N   1 
ATOM   101  C CA  . TYR A 1 15  ? 75.39352  49.73217  22.53251  1.000 36.27435  ?  15  TYR C CA  1 
ATOM   102  C C   . TYR A 1 15  ? 76.74819  49.90203  23.20107  1.000 39.02399  ?  15  TYR C C   1 
ATOM   103  O O   . TYR A 1 15  ? 76.88279  49.69516  24.41039  1.000 44.89671  ?  15  TYR C O   1 
ATOM   104  C CB  . TYR A 1 15  ? 74.56139  51.01305  22.68759  1.000 37.67882  ?  15  TYR C CB  1 
ATOM   105  C CG  . TYR A 1 15  ? 75.18422  52.22991  22.04152  1.000 38.59579  ?  15  TYR C CG  1 
ATOM   106  C CD1 . TYR A 1 15  ? 75.12317  52.41779  20.66690  1.000 34.88374  ?  15  TYR C CD1 1 
ATOM   107  C CD2 . TYR A 1 15  ? 75.82962  53.19265  22.80605  1.000 36.17325  ?  15  TYR C CD2 1 
ATOM   108  C CE1 . TYR A 1 15  ? 75.69137  53.52808  20.07145  1.000 40.41624  ?  15  TYR C CE1 1 
ATOM   109  C CE2 . TYR A 1 15  ? 76.40006  54.30580  22.21993  1.000 37.88349  ?  15  TYR C CE2 1 
ATOM   110  C CZ  . TYR A 1 15  ? 76.32762  54.46872  20.85280  1.000 43.11002  ?  15  TYR C CZ  1 
ATOM   111  O OH  . TYR A 1 15  ? 76.89423  55.57633  20.26547  1.000 65.15626  ?  15  TYR C OH  1 
ATOM   112  N N   . GLN A 1 16  ? 77.74842  50.27641  22.40669  1.000 44.63919  ?  16  GLN C N   1 
ATOM   113  C CA  . GLN A 1 16  ? 79.10333  50.47899  22.89446  1.000 50.89302  ?  16  GLN C CA  1 
ATOM   114  C C   . GLN A 1 16  ? 79.60261  51.85373  22.47688  1.000 53.06206  ?  16  GLN C C   1 
ATOM   115  O O   . GLN A 1 16  ? 79.22415  52.37875  21.42600  1.000 47.72854  ?  16  GLN C O   1 
ATOM   116  C CB  . GLN A 1 16  ? 80.06536  49.40479  22.36675  1.000 49.99946  ?  16  GLN C CB  1 
ATOM   117  C CG  . GLN A 1 16  ? 79.72381  47.98770  22.78883  1.000 46.35371  ?  16  GLN C CG  1 
ATOM   118  C CD  . GLN A 1 16  ? 80.76708  46.98597  22.33504  1.000 50.85195  ?  16  GLN C CD  1 
ATOM   119  O OE1 . GLN A 1 16  ? 81.78501  46.78973  22.99831  1.000 57.49215  ?  16  GLN C OE1 1 
ATOM   120  N NE2 . GLN A 1 16  ? 80.52208  46.35085  21.19541  1.000 48.08633  ?  16  GLN C NE2 1 
ATOM   121  N N   A SER A 1 17  ? 80.46013  52.43336  23.31730  0.500 59.17576  ?  17  SER C N   1 
ATOM   122  N N   B SER A 1 17  ? 80.46523  52.42989  23.31428  0.500 56.29147  ?  17  SER C N   1 
ATOM   123  C CA  A SER A 1 17  ? 81.07226  53.72501  23.05637  0.500 54.53752  ?  17  SER C CA  1 
ATOM   124  C CA  B SER A 1 17  ? 81.07114  53.72530  23.06005  0.500 53.82392  ?  17  SER C CA  1 
ATOM   125  C C   A SER A 1 17  ? 82.50104  53.70212  23.58168  0.500 64.17537  ?  17  SER C C   1 
ATOM   126  C C   B SER A 1 17  ? 82.50049  53.70505  23.58448  0.500 64.18955  ?  17  SER C C   1 
ATOM   127  O O   A SER A 1 17  ? 82.75352  53.15808  24.66736  0.500 66.65751  ?  17  SER C O   1 
ATOM   128  O O   B SER A 1 17  ? 82.75335  53.16572  24.67241  0.500 66.66353  ?  17  SER C O   1 
ATOM   129  C CB  A SER A 1 17  ? 80.29377  54.87308  23.71405  0.500 50.57058  ?  17  SER C CB  1 
ATOM   130  C CB  B SER A 1 17  ? 80.28536  54.86289  23.72696  0.500 53.29495  ?  17  SER C CB  1 
ATOM   131  O OG  A SER A 1 17  ? 80.28182  54.74138  25.12465  0.500 56.33629  ?  17  SER C OG  1 
ATOM   132  O OG  B SER A 1 17  ? 80.83029  56.12666  23.39091  0.500 53.78876  ?  17  SER C OG  1 
ATOM   133  N N   . PRO A 1 18  ? 83.45617  54.27686  22.83939  1.000 67.70605  ?  18  PRO C N   1 
ATOM   134  C CA  . PRO A 1 18  ? 83.30568  54.95279  21.54280  1.000 59.48495  ?  18  PRO C CA  1 
ATOM   135  C C   . PRO A 1 18  ? 83.17437  53.97152  20.38323  1.000 64.05843  ?  18  PRO C C   1 
ATOM   136  O O   . PRO A 1 18  ? 83.20939  52.75923  20.57749  1.000 72.09352  ?  18  PRO C O   1 
ATOM   137  C CB  . PRO A 1 18  ? 84.59152  55.78020  21.44755  1.000 61.63202  ?  18  PRO C CB  1 
ATOM   138  C CG  . PRO A 1 18  ? 85.60753  54.92995  22.15130  1.000 66.10968  ?  18  PRO C CG  1 
ATOM   139  C CD  . PRO A 1 18  ? 84.85787  54.28775  23.29686  1.000 59.93367  ?  18  PRO C CD  1 
ATOM   140  N N   . GLY A 1 19  ? 83.02222  54.47732  19.16161  1.000 56.00876  ?  19  GLY C N   1 
ATOM   141  C CA  . GLY A 1 19  ? 82.81133  53.65557  17.99499  1.000 52.16022  ?  19  GLY C CA  1 
ATOM   142  C C   . GLY A 1 19  ? 81.38742  53.65307  17.47918  1.000 49.15597  ?  19  GLY C C   1 
ATOM   143  O O   . GLY A 1 19  ? 81.17196  53.33514  16.30328  1.000 70.54834  ?  19  GLY C O   1 
ATOM   144  N N   . ASP A 1 20  ? 80.41573  54.00009  18.32710  1.000 44.58936  ?  20  ASP C N   1 
ATOM   145  C CA  . ASP A 1 20  ? 79.00526  54.05982  17.94202  1.000 52.32801  ?  20  ASP C CA  1 
ATOM   146  C C   . ASP A 1 20  ? 78.53778  52.71603  17.38234  1.000 46.75132  ?  20  ASP C C   1 
ATOM   147  O O   . ASP A 1 20  ? 78.01112  52.62369  16.27168  1.000 75.20123  ?  20  ASP C O   1 
ATOM   148  C CB  . ASP A 1 20  ? 78.76050  55.19617  16.94444  1.000 63.61058  ?  20  ASP C CB  1 
ATOM   149  C CG  . ASP A 1 20  ? 77.28993  55.51801  16.77166  1.000 75.47918  ?  20  ASP C CG  1 
ATOM   150  O OD1 . ASP A 1 20  ? 76.66296  55.98184  17.74724  1.000 84.18102  ?  20  ASP C OD1 1 
ATOM   151  O OD2 . ASP A 1 20  ? 76.76380  55.31361  15.65747  1.000 90.86496  -1 20  ASP C OD2 1 
ATOM   152  N N   . ILE A 1 21  ? 78.74376  51.66210  18.16794  1.000 49.02484  ?  21  ILE C N   1 
ATOM   153  C CA  . ILE A 1 21  ? 78.43579  50.29606  17.76061  1.000 47.36274  ?  21  ILE C CA  1 
ATOM   154  C C   . ILE A 1 21  ? 77.16129  49.85522  18.46280  1.000 46.32699  ?  21  ILE C C   1 
ATOM   155  O O   . ILE A 1 21  ? 77.06810  49.91822  19.69528  1.000 53.25605  ?  21  ILE C O   1 
ATOM   156  C CB  . ILE A 1 21  ? 79.59792  49.34317  18.08660  1.000 61.79739  ?  21  ILE C CB  1 
ATOM   157  C CG1 . ILE A 1 21  ? 80.93528  49.98941  17.72306  1.000 58.37672  ?  21  ILE C CG1 1 
ATOM   158  C CG2 . ILE A 1 21  ? 79.43020  48.02908  17.34348  1.000 68.07888  ?  21  ILE C CG2 1 
ATOM   159  C CD1 . ILE A 1 21  ? 82.13853  49.16989  18.13268  1.000 64.25559  ?  21  ILE C CD1 1 
ATOM   160  N N   . GLY A 1 22  ? 76.17761  49.39955  17.68206  1.000 45.31252  ?  22  GLY C N   1 
ATOM   161  C CA  . GLY A 1 22  ? 74.91256  48.96797  18.22891  1.000 40.48605  ?  22  GLY C CA  1 
ATOM   162  C C   . GLY A 1 22  ? 74.47074  47.64457  17.62845  1.000 42.02749  ?  22  GLY C C   1 
ATOM   163  O O   . GLY A 1 22  ? 74.98996  47.19317  16.60498  1.000 51.04380  ?  22  GLY C O   1 
ATOM   164  N N   . GLN A 1 23  ? 73.49020  47.03421  18.28936  1.000 40.84220  ?  23  GLN C N   1 
ATOM   165  C CA  . GLN A 1 23  ? 72.92897  45.76679  17.84579  1.000 40.80032  ?  23  GLN C CA  1 
ATOM   166  C C   . GLN A 1 23  ? 71.56850  45.57992  18.49994  1.000 36.04822  ?  23  GLN C C   1 
ATOM   167  O O   . GLN A 1 23  ? 71.41470  45.82224  19.69966  1.000 36.16948  ?  23  GLN C O   1 
ATOM   168  C CB  . GLN A 1 23  ? 73.85433  44.59201  18.19155  1.000 34.38385  ?  23  GLN C CB  1 
ATOM   169  C CG  . GLN A 1 23  ? 73.24155  43.22069  17.94437  1.000 32.62659  ?  23  GLN C CG  1 
ATOM   170  C CD  . GLN A 1 23  ? 74.20371  42.08666  18.24077  1.000 46.68084  ?  23  GLN C CD  1 
ATOM   171  O OE1 . GLN A 1 23  ? 75.29542  42.01906  17.67580  1.000 43.87256  ?  23  GLN C OE1 1 
ATOM   172  N NE2 . GLN A 1 23  ? 73.80333  41.18944  19.13429  1.000 36.32152  ?  23  GLN C NE2 1 
ATOM   173  N N   . TYR A 1 24  ? 70.58814  45.15643  17.70412  1.000 28.64951  ?  24  TYR C N   1 
ATOM   174  C CA  . TYR A 1 24  ? 69.24537  44.87364  18.19295  1.000 31.93896  ?  24  TYR C CA  1 
ATOM   175  C C   . TYR A 1 24  ? 68.79233  43.53177  17.63864  1.000 34.14378  ?  24  TYR C C   1 
ATOM   176  O O   . TYR A 1 24  ? 68.81837  43.31947  16.42217  1.000 39.75552  ?  24  TYR C O   1 
ATOM   177  C CB  . TYR A 1 24  ? 68.25962  45.97673  17.79306  1.000 33.36269  ?  24  TYR C CB  1 
ATOM   178  C CG  . TYR A 1 24  ? 66.91743  45.85215  18.47378  1.000 38.35335  ?  24  TYR C CG  1 
ATOM   179  C CD1 . TYR A 1 24  ? 66.75081  46.25089  19.79290  1.000 47.08151  ?  24  TYR C CD1 1 
ATOM   180  C CD2 . TYR A 1 24  ? 65.81917  45.33087  17.80270  1.000 41.80524  ?  24  TYR C CD2 1 
ATOM   181  C CE1 . TYR A 1 24  ? 65.52986  46.13651  20.42504  1.000 45.25740  ?  24  TYR C CE1 1 
ATOM   182  C CE2 . TYR A 1 24  ? 64.59163  45.21304  18.42766  1.000 36.26079  ?  24  TYR C CE2 1 
ATOM   183  C CZ  . TYR A 1 24  ? 64.45427  45.61749  19.73867  1.000 38.18165  ?  24  TYR C CZ  1 
ATOM   184  O OH  . TYR A 1 24  ? 63.23734  45.50372  20.36831  1.000 55.55109  ?  24  TYR C OH  1 
ATOM   185  N N   . THR A 1 25  ? 68.37916  42.62986  18.52718  1.000 35.79015  ?  25  THR C N   1 
ATOM   186  C CA  . THR A 1 25  ? 68.00401  41.28000  18.13294  1.000 35.57315  ?  25  THR C CA  1 
ATOM   187  C C   . THR A 1 25  ? 66.71950  40.86656  18.83663  1.000 37.57040  ?  25  THR C C   1 
ATOM   188  O O   . THR A 1 25  ? 66.31946  41.44903  19.84774  1.000 41.28620  ?  25  THR C O   1 
ATOM   189  C CB  . THR A 1 25  ? 69.10941  40.26250  18.45317  1.000 36.54302  ?  25  THR C CB  1 
ATOM   190  O OG1 . THR A 1 25  ? 69.47726  40.37318  19.83371  1.000 43.49660  ?  25  THR C OG1 1 
ATOM   191  C CG2 . THR A 1 25  ? 70.33276  40.49783  17.58053  1.000 39.31655  ?  25  THR C CG2 1 
ATOM   192  N N   . PHE A 1 26  ? 66.07799  39.84409  18.27595  1.000 49.92791  ?  26  PHE C N   1 
ATOM   193  C CA  . PHE A 1 26  ? 64.92379  39.18528  18.87199  1.000 45.20473  ?  26  PHE C CA  1 
ATOM   194  C C   . PHE A 1 26  ? 65.26184  37.71584  19.07322  1.000 45.88245  ?  26  PHE C C   1 
ATOM   195  O O   . PHE A 1 26  ? 65.82186  37.07780  18.17534  1.000 49.56193  ?  26  PHE C O   1 
ATOM   196  C CB  . PHE A 1 26  ? 63.68439  39.32685  17.98418  1.000 50.05655  ?  26  PHE C CB  1 
ATOM   197  C CG  . PHE A 1 26  ? 62.70065  40.35423  18.46658  1.000 46.51182  ?  26  PHE C CG  1 
ATOM   198  C CD1 . PHE A 1 26  ? 63.09398  41.66359  18.68807  1.000 60.11335  ?  26  PHE C CD1 1 
ATOM   199  C CD2 . PHE A 1 26  ? 61.37505  40.01286  18.67876  1.000 41.63095  ?  26  PHE C CD2 1 
ATOM   200  C CE1 . PHE A 1 26  ? 62.18539  42.61022  19.12660  1.000 49.61550  ?  26  PHE C CE1 1 
ATOM   201  C CE2 . PHE A 1 26  ? 60.46225  40.95360  19.11484  1.000 48.50419  ?  26  PHE C CE2 1 
ATOM   202  C CZ  . PHE A 1 26  ? 60.86766  42.25432  19.33934  1.000 48.38255  ?  26  PHE C CZ  1 
ATOM   203  N N   . GLU A 1 27  ? 64.92755  37.18149  20.24524  1.000 48.82180  ?  27  GLU C N   1 
ATOM   204  C CA  . GLU A 1 27  ? 65.24112  35.80041  20.57836  1.000 56.33778  ?  27  GLU C CA  1 
ATOM   205  C C   . GLU A 1 27  ? 63.98559  35.05780  21.00926  1.000 46.46557  ?  27  GLU C C   1 
ATOM   206  O O   . GLU A 1 27  ? 63.03592  35.65133  21.52695  1.000 50.78227  ?  27  GLU C O   1 
ATOM   207  C CB  . GLU A 1 27  ? 66.29347  35.70633  21.69386  1.000 56.93809  ?  27  GLU C CB  1 
ATOM   208  C CG  . GLU A 1 27  ? 67.70245  36.08142  21.26851  1.000 58.69555  ?  27  GLU C CG  1 
ATOM   209  C CD  . GLU A 1 27  ? 68.73437  35.74872  22.32987  1.000 73.53865  ?  27  GLU C CD  1 
ATOM   210  O OE1 . GLU A 1 27  ? 68.38551  35.04048  23.29817  1.000 75.78365  ?  27  GLU C OE1 1 
ATOM   211  O OE2 . GLU A 1 27  ? 69.89356  36.19485  22.19750  1.000 79.55940  -1 27  GLU C OE2 1 
ATOM   212  N N   . PHE A 1 28  ? 63.99670  33.74556  20.78573  1.000 54.77156  ?  28  PHE C N   1 
ATOM   213  C CA  . PHE A 1 28  ? 62.95040  32.86047  21.28598  1.000 47.81779  ?  28  PHE C CA  1 
ATOM   214  C C   . PHE A 1 28  ? 63.58975  31.52153  21.61520  1.000 56.04402  ?  28  PHE C C   1 
ATOM   215  O O   . PHE A 1 28  ? 64.12177  30.85532  20.72166  1.000 68.42888  ?  28  PHE C O   1 
ATOM   216  C CB  . PHE A 1 28  ? 61.82307  32.68769  20.26603  1.000 53.31450  ?  28  PHE C CB  1 
ATOM   217  C CG  . PHE A 1 28  ? 60.62905  31.95127  20.80558  1.000 58.20209  ?  28  PHE C CG  1 
ATOM   218  C CD1 . PHE A 1 28  ? 59.60121  32.63746  21.43215  1.000 52.52943  ?  28  PHE C CD1 1 
ATOM   219  C CD2 . PHE A 1 28  ? 60.53780  30.57334  20.69451  1.000 50.23662  ?  28  PHE C CD2 1 
ATOM   220  C CE1 . PHE A 1 28  ? 58.50239  31.96366  21.93387  1.000 49.90275  ?  28  PHE C CE1 1 
ATOM   221  C CE2 . PHE A 1 28  ? 59.44175  29.89391  21.19360  1.000 54.65472  ?  28  PHE C CE2 1 
ATOM   222  C CZ  . PHE A 1 28  ? 58.42298  30.59024  21.81421  1.000 54.26016  ?  28  PHE C CZ  1 
ATOM   223  N N   . ASP A 1 29  ? 63.53954  31.13768  22.89254  1.000 54.54150  ?  29  ASP C N   1 
ATOM   224  C CA  . ASP A 1 29  ? 64.16631  29.90871  23.38303  1.000 63.79635  ?  29  ASP C CA  1 
ATOM   225  C C   . ASP A 1 29  ? 65.66323  29.87537  23.08497  1.000 66.37355  ?  29  ASP C C   1 
ATOM   226  O O   . ASP A 1 29  ? 66.23491  28.81013  22.84014  1.000 85.33094  ?  29  ASP C O   1 
ATOM   227  C CB  . ASP A 1 29  ? 63.48012  28.66226  22.81450  1.000 75.93480  ?  29  ASP C CB  1 
ATOM   228  C CG  . ASP A 1 29  ? 62.10576  28.42962  23.41202  1.000 75.86920  ?  29  ASP C CG  1 
ATOM   229  O OD1 . ASP A 1 29  ? 61.88658  28.83063  24.57449  1.000 69.83577  ?  29  ASP C OD1 1 
ATOM   230  O OD2 . ASP A 1 29  ? 61.24611  27.84241  22.72151  1.000 76.28102  -1 29  ASP C OD2 1 
ATOM   231  N N   . GLY A 1 30  ? 66.30932  31.04152  23.10305  1.000 57.22057  ?  30  GLY C N   1 
ATOM   232  C CA  . GLY A 1 30  ? 67.73974  31.13389  22.91404  1.000 62.69212  ?  30  GLY C CA  1 
ATOM   233  C C   . GLY A 1 30  ? 68.19862  31.29870  21.48156  1.000 55.44705  ?  30  GLY C C   1 
ATOM   234  O O   . GLY A 1 30  ? 69.37538  31.61281  21.25970  1.000 53.07814  ?  30  GLY C O   1 
ATOM   235  N N   . ASP A 1 31  ? 67.32037  31.09571  20.50561  1.000 47.78065  ?  31  ASP C N   1 
ATOM   236  C CA  . ASP A 1 31  ? 67.66847  31.23592  19.10046  1.000 44.71005  ?  31  ASP C CA  1 
ATOM   237  C C   . ASP A 1 31  ? 67.25787  32.61137  18.59017  1.000 56.56603  ?  31  ASP C C   1 
ATOM   238  O O   . ASP A 1 31  ? 66.28209  33.20287  19.05813  1.000 56.55499  ?  31  ASP C O   1 
ATOM   239  C CB  . ASP A 1 31  ? 67.00350  30.14297  18.26164  1.000 51.00844  ?  31  ASP C CB  1 
ATOM   240  C CG  . ASP A 1 31  ? 67.53980  28.75920  18.57788  1.000 63.75688  ?  31  ASP C CG  1 
ATOM   241  O OD1 . ASP A 1 31  ? 68.76547  28.62585  18.78006  1.000 60.75239  ?  31  ASP C OD1 1 
ATOM   242  O OD2 . ASP A 1 31  ? 66.73544  27.80541  18.62884  1.000 71.64586  -1 31  ASP C OD2 1 
ATOM   243  N N   . GLU A 1 32  ? 68.01558  33.11465  17.61958  1.000 53.33647  ?  32  GLU C N   1 
ATOM   244  C CA  . GLU A 1 32  ? 67.80464  34.46185  17.10582  1.000 50.04559  ?  32  GLU C CA  1 
ATOM   245  C C   . GLU A 1 32  ? 66.67860  34.45964  16.07902  1.000 48.67533  ?  32  GLU C C   1 
ATOM   246  O O   . GLU A 1 32  ? 66.78117  33.80209  15.03754  1.000 47.37634  ?  32  GLU C O   1 
ATOM   247  C CB  . GLU A 1 32  ? 69.08996  35.00129  16.48276  1.000 50.77616  ?  32  GLU C CB  1 
ATOM   248  C CG  . GLU A 1 32  ? 69.04545  36.48722  16.16399  1.000 44.98496  ?  32  GLU C CG  1 
ATOM   249  C CD  . GLU A 1 32  ? 70.03571  36.88421  15.08761  1.000 59.75752  ?  32  GLU C CD  1 
ATOM   250  O OE1 . GLU A 1 32  ? 69.79963  36.54361  13.90883  1.000 65.71729  ?  32  GLU C OE1 1 
ATOM   251  O OE2 . GLU A 1 32  ? 71.05240  37.53000  15.41985  1.000 72.27138  -1 32  GLU C OE2 1 
ATOM   252  N N   . LEU A 1 33  ? 65.60494  35.19631  16.37199  1.000 48.69117  ?  33  LEU C N   1 
ATOM   253  C CA  . LEU A 1 33  ? 64.55774  35.40318  15.37719  1.000 44.36416  ?  33  LEU C CA  1 
ATOM   254  C C   . LEU A 1 33  ? 65.06459  36.26602  14.22906  1.000 45.94930  ?  33  LEU C C   1 
ATOM   255  O O   . LEU A 1 33  ? 64.97563  35.87796  13.05799  1.000 48.57571  ?  33  LEU C O   1 
ATOM   256  C CB  . LEU A 1 33  ? 63.33084  36.04286  16.02807  1.000 43.18761  ?  33  LEU C CB  1 
ATOM   257  C CG  . LEU A 1 33  ? 62.39768  35.12553  16.81829  1.000 51.23650  ?  33  LEU C CG  1 
ATOM   258  C CD1 . LEU A 1 33  ? 61.36856  35.94326  17.57974  1.000 41.39343  ?  33  LEU C CD1 1 
ATOM   259  C CD2 . LEU A 1 33  ? 61.71288  34.13996  15.88594  1.000 39.76073  ?  33  LEU C CD2 1 
ATOM   260  N N   . PHE A 1 34  ? 65.60506  37.43849  14.54851  1.000 54.40646  ?  34  PHE C N   1 
ATOM   261  C CA  . PHE A 1 34  ? 66.13564  38.34639  13.54218  1.000 51.53655  ?  34  PHE C CA  1 
ATOM   262  C C   . PHE A 1 34  ? 67.04529  39.35487  14.22723  1.000 42.83266  ?  34  PHE C C   1 
ATOM   263  O O   . PHE A 1 34  ? 67.13709  39.40835  15.45586  1.000 52.55196  ?  34  PHE C O   1 
ATOM   264  C CB  . PHE A 1 34  ? 65.01198  39.05953  12.77979  1.000 56.53347  ?  34  PHE C CB  1 
ATOM   265  C CG  . PHE A 1 34  ? 64.07896  39.84662  13.66150  1.000 51.80046  ?  34  PHE C CG  1 
ATOM   266  C CD1 . PHE A 1 34  ? 64.39900  41.13467  14.06490  1.000 46.31478  ?  34  PHE C CD1 1 
ATOM   267  C CD2 . PHE A 1 34  ? 62.87536  39.30179  14.07606  1.000 49.60719  ?  34  PHE C CD2 1 
ATOM   268  C CE1 . PHE A 1 34  ? 63.54260  41.85739  14.87262  1.000 50.77539  ?  34  PHE C CE1 1 
ATOM   269  C CE2 . PHE A 1 34  ? 62.01278  40.02152  14.88191  1.000 51.17879  ?  34  PHE C CE2 1 
ATOM   270  C CZ  . PHE A 1 34  ? 62.34684  41.30077  15.27995  1.000 48.12727  ?  34  PHE C CZ  1 
ATOM   271  N N   . TYR A 1 35  ? 67.71833  40.15767  13.40824  1.000 43.29610  ?  35  TYR C N   1 
ATOM   272  C CA  . TYR A 1 35  ? 68.44094  41.32959  13.87497  1.000 46.49502  ?  35  TYR C CA  1 
ATOM   273  C C   . TYR A 1 35  ? 68.12683  42.49248  12.94647  1.000 48.73417  ?  35  TYR C C   1 
ATOM   274  O O   . TYR A 1 35  ? 67.87302  42.30286  11.75364  1.000 53.89458  ?  35  TYR C O   1 
ATOM   275  C CB  . TYR A 1 35  ? 69.96253  41.08984  13.93912  1.000 35.50557  ?  35  TYR C CB  1 
ATOM   276  C CG  . TYR A 1 35  ? 70.64182  40.97762  12.59167  1.000 38.31058  ?  35  TYR C CG  1 
ATOM   277  C CD1 . TYR A 1 35  ? 70.73997  39.75491  11.94203  1.000 46.01988  ?  35  TYR C CD1 1 
ATOM   278  C CD2 . TYR A 1 35  ? 71.19543  42.09299  11.97413  1.000 38.95149  ?  35  TYR C CD2 1 
ATOM   279  C CE1 . TYR A 1 35  ? 71.36161  39.64639  10.71338  1.000 39.77118  ?  35  TYR C CE1 1 
ATOM   280  C CE2 . TYR A 1 35  ? 71.81615  41.99396  10.74384  1.000 39.75996  ?  35  TYR C CE2 1 
ATOM   281  C CZ  . TYR A 1 35  ? 71.89673  40.76831  10.11864  1.000 41.48679  ?  35  TYR C CZ  1 
ATOM   282  O OH  . TYR A 1 35  ? 72.51668  40.66377  8.89457   1.000 47.64480  ?  35  TYR C OH  1 
ATOM   283  N N   . VAL A 1 36  ? 68.13448  43.69697  13.50381  1.000 47.08524  ?  36  VAL C N   1 
ATOM   284  C CA  . VAL A 1 36  ? 67.85698  44.91258  12.74887  1.000 43.53652  ?  36  VAL C CA  1 
ATOM   285  C C   . VAL A 1 36  ? 69.19208  45.52032  12.34239  1.000 39.27728  ?  36  VAL C C   1 
ATOM   286  O O   . VAL A 1 36  ? 69.97423  45.95304  13.19556  1.000 56.29298  ?  36  VAL C O   1 
ATOM   287  C CB  . VAL A 1 36  ? 67.01545  45.90592  13.56041  1.000 46.78476  ?  36  VAL C CB  1 
ATOM   288  C CG1 . VAL A 1 36  ? 66.80101  47.18635  12.76836  1.000 41.76908  ?  36  VAL C CG1 1 
ATOM   289  C CG2 . VAL A 1 36  ? 65.68255  45.28236  13.94470  1.000 53.68027  ?  36  VAL C CG2 1 
ATOM   290  N N   . ASP A 1 37  ? 69.46056  45.54673  11.03992  1.000 42.94755  ?  37  ASP C N   1 
ATOM   291  C CA  . ASP A 1 37  ? 70.65864  46.19560  10.51317  1.000 49.34098  ?  37  ASP C CA  1 
ATOM   292  C C   . ASP A 1 37  ? 70.52449  47.69528  10.74026  1.000 61.73710  ?  37  ASP C C   1 
ATOM   293  O O   . ASP A 1 37  ? 69.77256  48.37746  10.04231  1.000 60.42318  ?  37  ASP C O   1 
ATOM   294  C CB  . ASP A 1 37  ? 70.83664  45.86909  9.03464   1.000 44.64183  ?  37  ASP C CB  1 
ATOM   295  C CG  . ASP A 1 37  ? 72.13044  46.42209  8.46327   1.000 65.04167  ?  37  ASP C CG  1 
ATOM   296  O OD1 . ASP A 1 37  ? 72.95865  46.94334  9.23952   1.000 81.52031  ?  37  ASP C OD1 1 
ATOM   297  O OD2 . ASP A 1 37  ? 72.32006  46.33382  7.23212   1.000 65.64365  -1 37  ASP C OD2 1 
ATOM   298  N N   . LEU A 1 38  ? 71.25804  48.21670  11.72579  1.000 53.22451  ?  38  LEU C N   1 
ATOM   299  C CA  . LEU A 1 38  ? 71.12048  49.61940  12.09810  1.000 51.68734  ?  38  LEU C CA  1 
ATOM   300  C C   . LEU A 1 38  ? 71.60852  50.56614  11.00855  1.000 59.70664  ?  38  LEU C C   1 
ATOM   301  O O   . LEU A 1 38  ? 71.20014  51.73270  10.99283  1.000 56.96822  ?  38  LEU C O   1 
ATOM   302  C CB  . LEU A 1 38  ? 71.87397  49.88755  13.40013  1.000 44.13350  ?  38  LEU C CB  1 
ATOM   303  C CG  . LEU A 1 38  ? 71.48582  48.99562  14.58199  1.000 37.07337  ?  38  LEU C CG  1 
ATOM   304  C CD1 . LEU A 1 38  ? 72.17235  49.46852  15.84863  1.000 38.39775  ?  38  LEU C CD1 1 
ATOM   305  C CD2 . LEU A 1 38  ? 69.97576  48.96304  14.76728  1.000 42.74259  ?  38  LEU C CD2 1 
ATOM   306  N N   . ASP A 1 39  ? 72.46445  50.09495  10.10021  1.000 50.89733  ?  39  ASP C N   1 
ATOM   307  C CA  . ASP A 1 39  ? 72.95279  50.92406  9.00535   1.000 59.45768  ?  39  ASP C CA  1 
ATOM   308  C C   . ASP A 1 39  ? 71.98565  50.94354  7.82803   1.000 65.71234  ?  39  ASP C C   1 
ATOM   309  O O   . ASP A 1 39  ? 71.74482  52.00466  7.24201   1.000 72.05484  ?  39  ASP C O   1 
ATOM   310  C CB  . ASP A 1 39  ? 74.32834  50.43381  8.54433   1.000 65.51850  ?  39  ASP C CB  1 
ATOM   311  C CG  . ASP A 1 39  ? 75.36883  50.49964  9.64683   1.000 90.07596  ?  39  ASP C CG  1 
ATOM   312  O OD1 . ASP A 1 39  ? 75.29471  49.68084  10.58634  1.000 106.22430 ?  39  ASP C OD1 1 
ATOM   313  O OD2 . ASP A 1 39  ? 76.26082  51.36989  9.57134   1.000 94.36061  -1 39  ASP C OD2 1 
ATOM   314  N N   . LYS A 1 40  ? 71.42821  49.78913  7.46285   1.000 60.43829  ?  40  LYS C N   1 
ATOM   315  C CA  . LYS A 1 40  ? 70.45698  49.71806  6.38001   1.000 60.40175  ?  40  LYS C CA  1 
ATOM   316  C C   . LYS A 1 40  ? 69.02337  49.91433  6.85233   1.000 71.33417  ?  40  LYS C C   1 
ATOM   317  O O   . LYS A 1 40  ? 68.13303  50.08266  6.01199   1.000 59.79363  ?  40  LYS C O   1 
ATOM   318  C CB  . LYS A 1 40  ? 70.57063  48.37535  5.65096   1.000 65.92184  ?  40  LYS C CB  1 
ATOM   319  C CG  . LYS A 1 40  ? 71.87694  48.17934  4.90014   1.000 64.82582  ?  40  LYS C CG  1 
ATOM   320  C CD  . LYS A 1 40  ? 71.90777  46.83557  4.18854   1.000 63.66991  ?  40  LYS C CD  1 
ATOM   321  C CE  . LYS A 1 40  ? 73.20564  46.64943  3.41988   1.000 95.80098  ?  40  LYS C CE  1 
ATOM   322  N NZ  . LYS A 1 40  ? 73.24826  45.34042  2.71269   1.000 98.00550  ?  40  LYS C NZ  1 
ATOM   323  N N   . LYS A 1 41  ? 68.78393  49.89081  8.16613   1.000 68.94569  ?  41  LYS C N   1 
ATOM   324  C CA  . LYS A 1 41  ? 67.45374  50.10042  8.74094   1.000 59.06872  ?  41  LYS C CA  1 
ATOM   325  C C   . LYS A 1 41  ? 66.45905  49.06533  8.21516   1.000 58.77450  ?  41  LYS C C   1 
ATOM   326  O O   . LYS A 1 41  ? 65.33804  49.38782  7.81669   1.000 65.96008  ?  41  LYS C O   1 
ATOM   327  C CB  . LYS A 1 41  ? 66.96478  51.52717  8.47876   1.000 51.39528  ?  41  LYS C CB  1 
ATOM   328  C CG  . LYS A 1 41  ? 67.95416  52.59756  8.91122   1.000 57.89961  ?  41  LYS C CG  1 
ATOM   329  C CD  . LYS A 1 41  ? 67.46877  53.99084  8.55028   1.000 83.56276  ?  41  LYS C CD  1 
ATOM   330  C CE  . LYS A 1 41  ? 68.47765  55.04685  8.97432   1.000 78.29228  ?  41  LYS C CE  1 
ATOM   331  N NZ  . LYS A 1 41  ? 68.04567  56.41937  8.59090   1.000 102.15846 ?  41  LYS C NZ  1 
ATOM   332  N N   . GLU A 1 42  ? 66.88451  47.80315  8.21820   1.000 51.21416  ?  42  GLU C N   1 
ATOM   333  C CA  . GLU A 1 42  ? 66.07857  46.70756  7.70257   1.000 48.47201  ?  42  GLU C CA  1 
ATOM   334  C C   . GLU A 1 42  ? 66.16068  45.52080  8.65087   1.000 56.80079  ?  42  GLU C C   1 
ATOM   335  O O   . GLU A 1 42  ? 67.15899  45.33077  9.35050   1.000 59.62593  ?  42  GLU C O   1 
ATOM   336  C CB  . GLU A 1 42  ? 66.53238  46.28540  6.29788   1.000 56.85498  ?  42  GLU C CB  1 
ATOM   337  C CG  . GLU A 1 42  ? 66.36489  47.36410  5.23981   1.000 97.81903  ?  42  GLU C CG  1 
ATOM   338  C CD  . GLU A 1 42  ? 66.89306  46.93887  3.88463   1.000 118.34571 ?  42  GLU C CD  1 
ATOM   339  O OE1 . GLU A 1 42  ? 67.46030  45.83011  3.78808   1.000 117.16814 ?  42  GLU C OE1 1 
ATOM   340  O OE2 . GLU A 1 42  ? 66.74102  47.71358  2.91635   1.000 114.08642 -1 42  GLU C OE2 1 
ATOM   341  N N   . THR A 1 43  ? 65.09633  44.72255  8.66286   1.000 53.31225  ?  43  THR C N   1 
ATOM   342  C CA  . THR A 1 43  ? 65.02723  43.52379  9.48676   1.000 44.97456  ?  43  THR C CA  1 
ATOM   343  C C   . THR A 1 43  ? 65.58093  42.33624  8.70903   1.000 42.50284  ?  43  THR C C   1 
ATOM   344  O O   . THR A 1 43  ? 65.18012  42.09365  7.56631   1.000 50.34569  ?  43  THR C O   1 
ATOM   345  C CB  . THR A 1 43  ? 63.58546  43.25052  9.91923   1.000 53.79452  ?  43  THR C CB  1 
ATOM   346  O OG1 . THR A 1 43  ? 63.10752  44.34378  10.71375  1.000 49.75343  ?  43  THR C OG1 1 
ATOM   347  C CG2 . THR A 1 43  ? 63.50129  41.96488  10.72843  1.000 47.07798  ?  43  THR C CG2 1 
ATOM   348  N N   . VAL A 1 44  ? 66.50188  41.60225  9.32825   1.000 55.06828  ?  44  VAL C N   1 
ATOM   349  C CA  . VAL A 1 44  ? 67.16386  40.46271  8.70124   1.000 54.41759  ?  44  VAL C CA  1 
ATOM   350  C C   . VAL A 1 44  ? 66.85581  39.22827  9.53651   1.000 51.70182  ?  44  VAL C C   1 
ATOM   351  O O   . VAL A 1 44  ? 67.38201  39.07424  10.64608  1.000 64.41188  ?  44  VAL C O   1 
ATOM   352  C CB  . VAL A 1 44  ? 68.67805  40.67408  8.57385   1.000 45.51479  ?  44  VAL C CB  1 
ATOM   353  C CG1 . VAL A 1 44  ? 69.30989  39.52002  7.81003   1.000 45.60570  ?  44  VAL C CG1 1 
ATOM   354  C CG2 . VAL A 1 44  ? 68.97517  42.00269  7.89579   1.000 51.52004  ?  44  VAL C CG2 1 
ATOM   355  N N   . TRP A 1 45  ? 66.01529  38.34553  9.00403   1.000 51.48917  ?  45  TRP C N   1 
ATOM   356  C CA  . TRP A 1 45  ? 65.64801  37.12298  9.70393   1.000 51.88318  ?  45  TRP C CA  1 
ATOM   357  C C   . TRP A 1 45  ? 66.70048  36.04499  9.48506   1.000 46.07244  ?  45  TRP C C   1 
ATOM   358  O O   . TRP A 1 45  ? 67.20832  35.86986  8.37390   1.000 50.73995  ?  45  TRP C O   1 
ATOM   359  C CB  . TRP A 1 45  ? 64.28694  36.62019  9.22214   1.000 58.76913  ?  45  TRP C CB  1 
ATOM   360  C CG  . TRP A 1 45  ? 63.18007  37.61122  9.39556   1.000 53.55051  ?  45  TRP C CG  1 
ATOM   361  C CD1 . TRP A 1 45  ? 62.91402  38.68999  8.60370   1.000 41.88114  ?  45  TRP C CD1 1 
ATOM   362  C CD2 . TRP A 1 45  ? 62.18127  37.61055  10.42187  1.000 47.44420  ?  45  TRP C CD2 1 
ATOM   363  N NE1 . TRP A 1 45  ? 61.81532  39.36439  9.07672   1.000 57.09802  ?  45  TRP C NE1 1 
ATOM   364  C CE2 . TRP A 1 45  ? 61.34625  38.72153  10.19197  1.000 49.46526  ?  45  TRP C CE2 1 
ATOM   365  C CE3 . TRP A 1 45  ? 61.91382  36.78012  11.51428  1.000 45.27014  ?  45  TRP C CE3 1 
ATOM   366  C CZ2 . TRP A 1 45  ? 60.26282  39.02336  11.01354  1.000 51.61370  ?  45  TRP C CZ2 1 
ATOM   367  C CZ3 . TRP A 1 45  ? 60.83826  37.08096  12.32831  1.000 46.29892  ?  45  TRP C CZ3 1 
ATOM   368  C CH2 . TRP A 1 45  ? 60.02596  38.19302  12.07406  1.000 57.08835  ?  45  TRP C CH2 1 
ATOM   369  N N   . MET A 1 46  ? 67.02618  35.31772  10.55637  1.000 56.12255  ?  46  MET C N   1 
ATOM   370  C CA  . MET A 1 46  ? 67.96453  34.20669  10.43169  1.000 52.21835  ?  46  MET C CA  1 
ATOM   371  C C   . MET A 1 46  ? 67.35212  33.06752  9.62706   1.000 49.49133  ?  46  MET C C   1 
ATOM   372  O O   . MET A 1 46  ? 67.99439  32.51250  8.72817   1.000 65.94894  ?  46  MET C O   1 
ATOM   373  C CB  . MET A 1 46  ? 68.39996  33.72242  11.81478  1.000 52.53086  ?  46  MET C CB  1 
ATOM   374  C CG  . MET A 1 46  ? 69.31044  32.50527  11.77875  1.000 47.62050  ?  46  MET C CG  1 
ATOM   375  S SD  . MET A 1 46  ? 70.04753  32.12763  13.37908  1.000 86.57110  ?  46  MET C SD  1 
ATOM   376  C CE  . MET A 1 46  ? 71.12264  33.54293  13.59959  1.000 66.53674  ?  46  MET C CE  1 
ATOM   377  N N   . LEU A 1 47  ? 66.10740  32.70445  9.93730   1.000 65.43146  ?  47  LEU C N   1 
ATOM   378  C CA  . LEU A 1 47  ? 65.37011  31.73789  9.13621   1.000 67.34051  ?  47  LEU C CA  1 
ATOM   379  C C   . LEU A 1 47  ? 64.57822  32.49309  8.07871   1.000 68.77468  ?  47  LEU C C   1 
ATOM   380  O O   . LEU A 1 47  ? 63.66036  33.24954  8.43292   1.000 79.12011  ?  47  LEU C O   1 
ATOM   381  C CB  . LEU A 1 47  ? 64.43765  30.90864  10.00815  1.000 66.15615  ?  47  LEU C CB  1 
ATOM   382  C CG  . LEU A 1 47  ? 65.08271  29.93076  10.99138  1.000 68.68244  ?  47  LEU C CG  1 
ATOM   383  C CD1 . LEU A 1 47  ? 64.01363  29.19580  11.78405  1.000 67.06759  ?  47  LEU C CD1 1 
ATOM   384  C CD2 . LEU A 1 47  ? 65.98146  28.94711  10.25964  1.000 49.71373  ?  47  LEU C CD2 1 
ATOM   385  N N   . PRO A 1 48  ? 64.89085  32.33869  6.78937   1.000 70.50885  ?  48  PRO C N   1 
ATOM   386  C CA  . PRO A 1 48  ? 64.13294  33.07297  5.76277   1.000 71.87104  ?  48  PRO C CA  1 
ATOM   387  C C   . PRO A 1 48  ? 62.65639  32.72415  5.73829   1.000 72.86192  ?  48  PRO C C   1 
ATOM   388  O O   . PRO A 1 48  ? 61.84252  33.54517  5.29724   1.000 80.36104  ?  48  PRO C O   1 
ATOM   389  C CB  . PRO A 1 48  ? 64.83079  32.66750  4.45621   1.000 67.32663  ?  48  PRO C CB  1 
ATOM   390  C CG  . PRO A 1 48  ? 66.19141  32.20887  4.87400   1.000 72.12031  ?  48  PRO C CG  1 
ATOM   391  C CD  . PRO A 1 48  ? 66.00130  31.56488  6.21174   1.000 75.61582  ?  48  PRO C CD  1 
ATOM   392  N N   . GLU A 1 49  ? 62.28333  31.52926  6.20174   1.000 80.43590  ?  49  GLU C N   1 
ATOM   393  C CA  . GLU A 1 49  ? 60.87456  31.15413  6.22052   1.000 73.79452  ?  49  GLU C CA  1 
ATOM   394  C C   . GLU A 1 49  ? 60.08942  31.97078  7.23894   1.000 70.01961  ?  49  GLU C C   1 
ATOM   395  O O   . GLU A 1 49  ? 58.89425  32.21749  7.04205   1.000 75.27567  ?  49  GLU C O   1 
ATOM   396  C CB  . GLU A 1 49  ? 60.72812  29.65980  6.51338   1.000 80.98701  ?  49  GLU C CB  1 
ATOM   397  C CG  . GLU A 1 49  ? 61.58086  28.75616  5.63327   1.000 98.50269  ?  49  GLU C CG  1 
ATOM   398  C CD  . GLU A 1 49  ? 62.96502  28.51348  6.20701   1.000 98.71379  ?  49  GLU C CD  1 
ATOM   399  O OE1 . GLU A 1 49  ? 63.10785  28.53217  7.44769   1.000 94.57068  ?  49  GLU C OE1 1 
ATOM   400  O OE2 . GLU A 1 49  ? 63.91040  28.30710  5.41733   1.000 114.07188 -1 49  GLU C OE2 1 
ATOM   401  N N   . PHE A 1 50  ? 60.73593  32.39856  8.32656   1.000 61.61775  ?  50  PHE C N   1 
ATOM   402  C CA  . PHE A 1 50  ? 60.03490  33.19170  9.33129   1.000 64.11134  ?  50  PHE C CA  1 
ATOM   403  C C   . PHE A 1 50  ? 59.70174  34.58003  8.79967   1.000 70.61573  ?  50  PHE C C   1 
ATOM   404  O O   . PHE A 1 50  ? 58.63773  35.13017  9.10548   1.000 71.13588  ?  50  PHE C O   1 
ATOM   405  C CB  . PHE A 1 50  ? 60.87039  33.28730  10.60858  1.000 57.12423  ?  50  PHE C CB  1 
ATOM   406  C CG  . PHE A 1 50  ? 60.78443  32.06548  11.48674  1.000 58.31905  ?  50  PHE C CG  1 
ATOM   407  C CD1 . PHE A 1 50  ? 60.15928  30.91050  11.03977  1.000 65.64223  ?  50  PHE C CD1 1 
ATOM   408  C CD2 . PHE A 1 50  ? 61.31345  32.07892  12.76646  1.000 60.17078  ?  50  PHE C CD2 1 
ATOM   409  C CE1 . PHE A 1 50  ? 60.07705  29.79129  11.84785  1.000 48.81405  ?  50  PHE C CE1 1 
ATOM   410  C CE2 . PHE A 1 50  ? 61.23209  30.96359  13.57916  1.000 63.30291  ?  50  PHE C CE2 1 
ATOM   411  C CZ  . PHE A 1 50  ? 60.61323  29.81933  13.11946  1.000 55.25708  ?  50  PHE C CZ  1 
ATOM   412  N N   . GLY A 1 51  ? 60.59804  35.16162  7.99934   1.000 68.73927  ?  51  GLY C N   1 
ATOM   413  C CA  . GLY A 1 51  ? 60.32093  36.44352  7.37435   1.000 49.90280  ?  51  GLY C CA  1 
ATOM   414  C C   . GLY A 1 51  ? 59.16296  36.40753  6.40000   1.000 63.26081  ?  51  GLY C C   1 
ATOM   415  O O   . GLY A 1 51  ? 58.52469  37.44055  6.16775   1.000 67.65943  ?  51  GLY C O   1 
ATOM   416  N N   . GLN A 1 52  ? 58.88107  35.23989  5.82014   1.000 69.88247  ?  52  GLN C N   1 
ATOM   417  C CA  . GLN A 1 52  ? 57.74932  35.09777  4.91491   1.000 62.44986  ?  52  GLN C CA  1 
ATOM   418  C C   . GLN A 1 52  ? 56.41910  35.01272  5.64694   1.000 68.60894  ?  52  GLN C C   1 
ATOM   419  O O   . GLN A 1 52  ? 55.37045  35.21960  5.02567   1.000 72.90582  ?  52  GLN C O   1 
ATOM   420  C CB  . GLN A 1 52  ? 57.92324  33.85581  4.03919   1.000 63.71063  ?  52  GLN C CB  1 
ATOM   421  C CG  . GLN A 1 52  ? 58.95418  34.01326  2.94244   1.000 85.97784  ?  52  GLN C CG  1 
ATOM   422  C CD  . GLN A 1 52  ? 58.62033  35.15184  2.00120   1.000 106.37675 ?  52  GLN C CD  1 
ATOM   423  O OE1 . GLN A 1 52  ? 59.26861  36.19744  2.02258   1.000 106.45009 ?  52  GLN C OE1 1 
ATOM   424  N NE2 . GLN A 1 52  ? 57.60351  34.95524  1.16784   1.000 91.18243  ?  52  GLN C NE2 1 
ATOM   425  N N   . LEU A 1 53  ? 56.43698  34.71004  6.94359   1.000 59.21716  ?  53  LEU C N   1 
ATOM   426  C CA  . LEU A 1 53  ? 55.22055  34.55880  7.73160   1.000 55.28616  ?  53  LEU C CA  1 
ATOM   427  C C   . LEU A 1 53  ? 54.96585  35.74865  8.64836   1.000 55.30119  ?  53  LEU C C   1 
ATOM   428  O O   . LEU A 1 53  ? 53.86384  36.30437  8.65156   1.000 75.49160  ?  53  LEU C O   1 
ATOM   429  C CB  . LEU A 1 53  ? 55.29050  33.26738  8.55527   1.000 65.64351  ?  53  LEU C CB  1 
ATOM   430  C CG  . LEU A 1 53  ? 55.56382  31.99865  7.74520   1.000 60.88849  ?  53  LEU C CG  1 
ATOM   431  C CD1 . LEU A 1 53  ? 55.74676  30.79695  8.65748   1.000 63.72175  ?  53  LEU C CD1 1 
ATOM   432  C CD2 . LEU A 1 53  ? 54.44592  31.75197  6.74327   1.000 55.04439  ?  53  LEU C CD2 1 
ATOM   433  N N   . ALA A 1 54  ? 55.96434  36.15309  9.42604   1.000 60.74113  ?  54  ALA C N   1 
ATOM   434  C CA  . ALA A 1 54  ? 55.83478  37.27063  10.34425  1.000 56.66420  ?  54  ALA C CA  1 
ATOM   435  C C   . ALA A 1 54  ? 56.53124  38.50346  9.77334   1.000 57.36170  ?  54  ALA C C   1 
ATOM   436  O O   . ALA A 1 54  ? 57.11456  38.47784  8.68697   1.000 71.05251  ?  54  ALA C O   1 
ATOM   437  C CB  . ALA A 1 54  ? 56.40068  36.90220  11.71646  1.000 57.46918  ?  54  ALA C CB  1 
ATOM   438  N N   . SER A 1 55  ? 56.46305  39.60087  10.52204  1.000 61.72320  ?  55  SER C N   1 
ATOM   439  C CA  . SER A 1 55  ? 57.11187  40.84370  10.12755  1.000 58.01798  ?  55  SER C CA  1 
ATOM   440  C C   . SER A 1 55  ? 57.37571  41.66916  11.37838  1.000 49.12890  ?  55  SER C C   1 
ATOM   441  O O   . SER A 1 55  ? 56.86865  41.37197  12.46259  1.000 45.97404  ?  55  SER C O   1 
ATOM   442  C CB  . SER A 1 55  ? 56.26490  41.62459  9.11800   1.000 47.72597  ?  55  SER C CB  1 
ATOM   443  O OG  . SER A 1 55  ? 54.99497  41.94280  9.65637   1.000 72.21477  ?  55  SER C OG  1 
ATOM   444  N N   . PHE A 1 56  ? 58.18082  42.71687  11.21054  1.000 60.03599  ?  56  PHE C N   1 
ATOM   445  C CA  . PHE A 1 56  ? 58.56482  43.57566  12.32385  1.000 44.10648  ?  56  PHE C CA  1 
ATOM   446  C C   . PHE A 1 56  ? 59.04035  44.90868  11.77052  1.000 47.41695  ?  56  PHE C C   1 
ATOM   447  O O   . PHE A 1 56  ? 59.86335  44.93856  10.85090  1.000 59.41520  ?  56  PHE C O   1 
ATOM   448  C CB  . PHE A 1 56  ? 59.66381  42.91960  13.16854  1.000 44.05519  ?  56  PHE C CB  1 
ATOM   449  C CG  . PHE A 1 56  ? 60.20893  43.80357  14.25372  1.000 40.85613  ?  56  PHE C CG  1 
ATOM   450  C CD1 . PHE A 1 56  ? 59.52971  43.95300  15.45124  1.000 47.23436  ?  56  PHE C CD1 1 
ATOM   451  C CD2 . PHE A 1 56  ? 61.40836  44.47451  14.08144  1.000 42.51684  ?  56  PHE C CD2 1 
ATOM   452  C CE1 . PHE A 1 56  ? 60.03241  44.76187  16.45346  1.000 43.32693  ?  56  PHE C CE1 1 
ATOM   453  C CE2 . PHE A 1 56  ? 61.91652  45.28327  15.07978  1.000 42.22070  ?  56  PHE C CE2 1 
ATOM   454  C CZ  . PHE A 1 56  ? 61.22733  45.42750  16.26715  1.000 38.82638  ?  56  PHE C CZ  1 
ATOM   455  N N   . ASP A 1 57  ? 58.52202  46.00155  12.32762  1.000 51.66281  ?  57  ASP C N   1 
ATOM   456  C CA  . ASP A 1 57  ? 58.92773  47.33823  11.91227  1.000 51.13765  ?  57  ASP C CA  1 
ATOM   457  C C   . ASP A 1 57  ? 60.30879  47.64185  12.47962  1.000 54.47420  ?  57  ASP C C   1 
ATOM   458  O O   . ASP A 1 57  ? 60.46552  47.76135  13.70166  1.000 56.35510  ?  57  ASP C O   1 
ATOM   459  C CB  . ASP A 1 57  ? 57.90868  48.38192  12.37521  1.000 52.38687  ?  57  ASP C CB  1 
ATOM   460  C CG  . ASP A 1 57  ? 58.05872  49.71120  11.65520  1.000 63.25480  ?  57  ASP C CG  1 
ATOM   461  O OD1 . ASP A 1 57  ? 59.18362  50.04505  11.22760  1.000 64.23549  ?  57  ASP C OD1 1 
ATOM   462  O OD2 . ASP A 1 57  ? 57.04434  50.42696  11.51758  1.000 88.33169  -1 57  ASP C OD2 1 
ATOM   463  N N   . PRO A 1 58  ? 61.33134  47.77694  11.62987  1.000 51.95569  ?  58  PRO C N   1 
ATOM   464  C CA  . PRO A 1 58  ? 62.68776  48.00993  12.14955  1.000 45.24809  ?  58  PRO C CA  1 
ATOM   465  C C   . PRO A 1 58  ? 62.86678  49.36587  12.80731  1.000 50.61159  ?  58  PRO C C   1 
ATOM   466  O O   . PRO A 1 58  ? 63.79915  49.52355  13.60549  1.000 52.84914  ?  58  PRO C O   1 
ATOM   467  C CB  . PRO A 1 58  ? 63.56935  47.87492  10.90132  1.000 45.70710  ?  58  PRO C CB  1 
ATOM   468  C CG  . PRO A 1 58  ? 62.66405  48.22373  9.76922   1.000 45.36945  ?  58  PRO C CG  1 
ATOM   469  C CD  . PRO A 1 58  ? 61.30169  47.72126  10.15821  1.000 45.01263  ?  58  PRO C CD  1 
ATOM   470  N N   . GLN A 1 59  ? 62.01042  50.34657  12.50402  1.000 63.21851  ?  59  GLN C N   1 
ATOM   471  C CA  . GLN A 1 59  ? 62.13756  51.65665  13.13520  1.000 55.12035  ?  59  GLN C CA  1 
ATOM   472  C C   . GLN A 1 59  ? 61.93941  51.57420  14.64232  1.000 52.10457  ?  59  GLN C C   1 
ATOM   473  O O   . GLN A 1 59  ? 62.46582  52.41197  15.38351  1.000 70.04366  ?  59  GLN C O   1 
ATOM   474  C CB  . GLN A 1 59  ? 61.14183  52.64074  12.52151  1.000 48.06033  ?  59  GLN C CB  1 
ATOM   475  C CG  . GLN A 1 59  ? 61.43993  53.00560  11.07684  1.000 72.50457  ?  59  GLN C CG  1 
ATOM   476  C CD  . GLN A 1 59  ? 60.52198  54.09049  10.55014  1.000 85.36824  ?  59  GLN C CD  1 
ATOM   477  O OE1 . GLN A 1 59  ? 59.60972  54.53814  11.24435  1.000 89.08084  ?  59  GLN C OE1 1 
ATOM   478  N NE2 . GLN A 1 59  ? 60.76132  54.52179  9.31725   1.000 101.30570 ?  59  GLN C NE2 1 
ATOM   479  N N   . GLY A 1 60  ? 61.18635  50.57950  15.11411  1.000 52.60127  ?  60  GLY C N   1 
ATOM   480  C CA  . GLY A 1 60  ? 61.06965  50.37640  16.54762  1.000 48.41723  ?  60  GLY C CA  1 
ATOM   481  C C   . GLY A 1 60  ? 62.38643  49.97076  17.17986  1.000 53.55029  ?  60  GLY C C   1 
ATOM   482  O O   . GLY A 1 60  ? 62.73355  50.43837  18.26821  1.000 53.18408  ?  60  GLY C O   1 
ATOM   483  N N   . GLY A 1 61  ? 63.13760  49.09482  16.50879  1.000 45.88597  ?  61  GLY C N   1 
ATOM   484  C CA  . GLY A 1 61  ? 64.44799  48.72167  17.00948  1.000 40.86326  ?  61  GLY C CA  1 
ATOM   485  C C   . GLY A 1 61  ? 65.45614  49.84814  16.92392  1.000 38.43457  ?  61  GLY C C   1 
ATOM   486  O O   . GLY A 1 61  ? 66.32299  49.97596  17.79324  1.000 42.18464  ?  61  GLY C O   1 
ATOM   487  N N   . LEU A 1 62  ? 65.36119  50.67711  15.88216  1.000 55.41553  ?  62  LEU C N   1 
ATOM   488  C CA  . LEU A 1 62  ? 66.25147  51.82704  15.76402  1.000 44.98648  ?  62  LEU C CA  1 
ATOM   489  C C   . LEU A 1 62  ? 66.04910  52.79354  16.92351  1.000 52.05982  ?  62  LEU C C   1 
ATOM   490  O O   . LEU A 1 62  ? 67.01543  53.23858  17.55399  1.000 47.47479  ?  62  LEU C O   1 
ATOM   491  C CB  . LEU A 1 62  ? 66.02101  52.53000  14.42693  1.000 46.89738  ?  62  LEU C CB  1 
ATOM   492  C CG  . LEU A 1 62  ? 66.45132  51.76102  13.17849  1.000 44.66179  ?  62  LEU C CG  1 
ATOM   493  C CD1 . LEU A 1 62  ? 65.93883  52.45220  11.92855  1.000 63.14082  ?  62  LEU C CD1 1 
ATOM   494  C CD2 . LEU A 1 62  ? 67.96370  51.63190  13.13595  1.000 46.29948  ?  62  LEU C CD2 1 
ATOM   495  N N   . GLN A 1 63  ? 64.79234  53.12716  17.22329  1.000 45.31205  ?  63  GLN C N   1 
ATOM   496  C CA  . GLN A 1 63  ? 64.50157  53.98773  18.36198  1.000 49.16028  ?  63  GLN C CA  1 
ATOM   497  C C   . GLN A 1 63  ? 64.75199  53.29602  19.69424  1.000 46.22588  ?  63  GLN C C   1 
ATOM   498  O O   . GLN A 1 63  ? 64.80685  53.97527  20.72480  1.000 54.55256  ?  63  GLN C O   1 
ATOM   499  C CB  . GLN A 1 63  ? 63.05802  54.48442  18.28659  1.000 41.70542  ?  63  GLN C CB  1 
ATOM   500  C CG  . GLN A 1 63  ? 62.76970  55.30714  17.04192  1.000 52.09174  ?  63  GLN C CG  1 
ATOM   501  C CD  . GLN A 1 63  ? 61.38187  55.90942  17.04490  1.000 51.78168  ?  63  GLN C CD  1 
ATOM   502  O OE1 . GLN A 1 63  ? 60.57564  55.63726  17.93396  1.000 53.52235  ?  63  GLN C OE1 1 
ATOM   503  N NE2 . GLN A 1 63  ? 61.09636  56.73880  16.04808  1.000 59.25511  ?  63  GLN C NE2 1 
ATOM   504  N N   . ASN A 1 64  ? 64.90266  51.97007  19.69914  1.000 51.19905  ?  64  ASN C N   1 
ATOM   505  C CA  . ASN A 1 64  ? 65.31830  51.28080  20.91510  1.000 47.35467  ?  64  ASN C CA  1 
ATOM   506  C C   . ASN A 1 64  ? 66.78512  51.55739  21.21825  1.000 46.53947  ?  64  ASN C C   1 
ATOM   507  O O   . ASN A 1 64  ? 67.16769  51.71196  22.38405  1.000 44.83951  ?  64  ASN C O   1 
ATOM   508  C CB  . ASN A 1 64  ? 65.06931  49.77905  20.77565  1.000 45.74316  ?  64  ASN C CB  1 
ATOM   509  C CG  . ASN A 1 64  ? 64.60150  49.14289  22.06700  1.000 45.37998  ?  64  ASN C CG  1 
ATOM   510  O OD1 . ASN A 1 64  ? 65.40378  48.82920  22.94510  1.000 59.91339  ?  64  ASN C OD1 1 
ATOM   511  N ND2 . ASN A 1 64  ? 63.29441  48.94257  22.18656  1.000 61.70574  ?  64  ASN C ND2 1 
ATOM   512  N N   . ILE A 1 65  ? 67.61878  51.62708  20.17661  1.000 51.91279  ?  65  ILE C N   1 
ATOM   513  C CA  . ILE A 1 65  ? 69.02758  51.96095  20.35822  1.000 43.19454  ?  65  ILE C CA  1 
ATOM   514  C C   . ILE A 1 65  ? 69.18808  53.42564  20.74703  1.000 52.65894  ?  65  ILE C C   1 
ATOM   515  O O   . ILE A 1 65  ? 70.09268  53.77711  21.51573  1.000 42.10430  ?  65  ILE C O   1 
ATOM   516  C CB  . ILE A 1 65  ? 69.81837  51.61853  19.08005  1.000 43.21243  ?  65  ILE C CB  1 
ATOM   517  C CG1 . ILE A 1 65  ? 69.82187  50.10742  18.84216  1.000 34.98531  ?  65  ILE C CG1 1 
ATOM   518  C CG2 . ILE A 1 65  ? 71.24716  52.14167  19.16080  1.000 36.46572  ?  65  ILE C CG2 1 
ATOM   519  C CD1 . ILE A 1 65  ? 70.55997  49.32480  19.90818  1.000 37.00730  ?  65  ILE C CD1 1 
ATOM   520  N N   . ALA A 1 66  ? 68.31594  54.30106  20.23891  1.000 44.98457  ?  66  ALA C N   1 
ATOM   521  C CA  . ALA A 1 66  ? 68.39541  55.71356  20.59574  1.000 45.76087  ?  66  ALA C CA  1 
ATOM   522  C C   . ALA A 1 66  ? 68.20954  55.92709  22.09210  1.000 50.20362  ?  66  ALA C C   1 
ATOM   523  O O   . ALA A 1 66  ? 68.76294  56.87755  22.65664  1.000 44.91741  ?  66  ALA C O   1 
ATOM   524  C CB  . ALA A 1 66  ? 67.35508  56.51334  19.81196  1.000 55.01954  ?  66  ALA C CB  1 
ATOM   525  N N   . VAL A 1 67  ? 67.44743  55.05466  22.75101  1.000 46.72797  ?  67  VAL C N   1 
ATOM   526  C CA  . VAL A 1 67  ? 67.22447  55.19368  24.18593  1.000 46.62617  ?  67  VAL C CA  1 
ATOM   527  C C   . VAL A 1 67  ? 68.45012  54.74221  24.97064  1.000 51.04382  ?  67  VAL C C   1 
ATOM   528  O O   . VAL A 1 67  ? 68.88517  55.41848  25.90991  1.000 45.85996  ?  67  VAL C O   1 
ATOM   529  C CB  . VAL A 1 67  ? 65.96418  54.41636  24.60801  1.000 46.13138  ?  67  VAL C CB  1 
ATOM   530  C CG1 . VAL A 1 67  ? 65.79457  54.46021  26.11893  1.000 44.42386  ?  67  VAL C CG1 1 
ATOM   531  C CG2 . VAL A 1 67  ? 64.73768  54.98577  23.91460  1.000 40.62181  ?  67  VAL C CG2 1 
ATOM   532  N N   . VAL A 1 68  ? 69.02846  53.59568  24.60064  1.000 50.72832  ?  68  VAL C N   1 
ATOM   533  C CA  . VAL A 1 68  ? 70.18326  53.09397  25.34021  1.000 50.21875  ?  68  VAL C CA  1 
ATOM   534  C C   . VAL A 1 68  ? 71.41179  53.95688  25.07753  1.000 42.94481  ?  68  VAL C C   1 
ATOM   535  O O   . VAL A 1 68  ? 72.25567  54.13087  25.96555  1.000 42.84111  ?  68  VAL C O   1 
ATOM   536  C CB  . VAL A 1 68  ? 70.44323  51.61079  25.00831  1.000 36.35550  ?  68  VAL C CB  1 
ATOM   537  C CG1 . VAL A 1 68  ? 69.23932  50.76439  25.39053  1.000 50.62268  ?  68  VAL C CG1 1 
ATOM   538  C CG2 . VAL A 1 68  ? 70.78132  51.42701  23.53899  1.000 46.02824  ?  68  VAL C CG2 1 
ATOM   539  N N   . LYS A 1 69  ? 71.53564  54.51639  23.87053  1.000 43.99022  ?  69  LYS C N   1 
ATOM   540  C CA  . LYS A 1 69  ? 72.61331  55.46445  23.60902  1.000 40.81492  ?  69  LYS C CA  1 
ATOM   541  C C   . LYS A 1 69  ? 72.46691  56.71148  24.46975  1.000 40.07614  ?  69  LYS C C   1 
ATOM   542  O O   . LYS A 1 69  ? 73.46911  57.31233  24.87396  1.000 49.43871  ?  69  LYS C O   1 
ATOM   543  C CB  . LYS A 1 69  ? 72.63819  55.83492  22.12464  1.000 37.94669  ?  69  LYS C CB  1 
ATOM   544  C CG  . LYS A 1 69  ? 73.74880  56.79914  21.73656  1.000 55.74062  ?  69  LYS C CG  1 
ATOM   545  C CD  . LYS A 1 69  ? 73.71122  57.12298  20.25111  1.000 68.31901  ?  69  LYS C CD  1 
ATOM   546  C CE  . LYS A 1 69  ? 74.81582  58.09763  19.87188  1.000 88.11083  ?  69  LYS C CE  1 
ATOM   547  N NZ  . LYS A 1 69  ? 74.79260  58.43232  18.42085  1.000 108.99948 ?  69  LYS C NZ  1 
ATOM   548  N N   . HIS A 1 70  ? 71.22818  57.10572  24.76824  1.000 45.69304  ?  70  HIS C N   1 
ATOM   549  C CA  . HIS A 1 70  ? 70.99483  58.24364  25.65019  1.000 53.98071  ?  70  HIS C CA  1 
ATOM   550  C C   . HIS A 1 70  ? 71.29502  57.88465  27.10093  1.000 55.58684  ?  70  HIS C C   1 
ATOM   551  O O   . HIS A 1 70  ? 71.94731  58.65164  27.81873  1.000 58.86020  ?  70  HIS C O   1 
ATOM   552  C CB  . HIS A 1 70  ? 69.55205  58.72667  25.49778  1.000 52.84036  ?  70  HIS C CB  1 
ATOM   553  C CG  . HIS A 1 70  ? 69.13114  59.71845  26.53621  1.000 51.73420  ?  70  HIS C CG  1 
ATOM   554  N ND1 . HIS A 1 70  ? 69.49747  61.04626  26.49020  1.000 66.76343  ?  70  HIS C ND1 1 
ATOM   555  C CD2 . HIS A 1 70  ? 68.37181  59.57578  27.64818  1.000 50.27237  ?  70  HIS C CD2 1 
ATOM   556  C CE1 . HIS A 1 70  ? 68.98241  61.67886  27.52937  1.000 71.63261  ?  70  HIS C CE1 1 
ATOM   557  N NE2 . HIS A 1 70  ? 68.29509  60.80925  28.24778  1.000 68.58951  ?  70  HIS C NE2 1 
ATOM   558  N N   . ASN A 1 71  ? 70.82774  56.71596  27.54970  1.000 58.18186  ?  71  ASN C N   1 
ATOM   559  C CA  . ASN A 1 71  ? 71.04024  56.31493  28.93688  1.000 51.12297  ?  71  ASN C CA  1 
ATOM   560  C C   . ASN A 1 71  ? 72.51143  56.05554  29.23563  1.000 58.44954  ?  71  ASN C C   1 
ATOM   561  O O   . ASN A 1 71  ? 72.96583  56.30869  30.35711  1.000 62.13114  ?  71  ASN C O   1 
ATOM   562  C CB  . ASN A 1 71  ? 70.21018  55.07183  29.26007  1.000 55.73720  ?  71  ASN C CB  1 
ATOM   563  C CG  . ASN A 1 71  ? 68.71808  55.33265  29.19392  1.000 55.06939  ?  71  ASN C CG  1 
ATOM   564  O OD1 . ASN A 1 71  ? 68.27086  56.47370  29.30540  1.000 59.52898  ?  71  ASN C OD1 1 
ATOM   565  N ND2 . ASN A 1 71  ? 67.93816  54.27163  29.02069  1.000 45.70897  ?  71  ASN C ND2 1 
ATOM   566  N N   . LEU A 1 72  ? 73.26742  55.55222  28.25620  1.000 49.20927  ?  72  LEU C N   1 
ATOM   567  C CA  . LEU A 1 72  ? 74.68308  55.27953  28.48435  1.000 42.68610  ?  72  LEU C CA  1 
ATOM   568  C C   . LEU A 1 72  ? 75.46326  56.56601  28.72400  1.000 55.40051  ?  72  LEU C C   1 
ATOM   569  O O   . LEU A 1 72  ? 76.36648  56.60243  29.56791  1.000 63.95209  ?  72  LEU C O   1 
ATOM   570  C CB  . LEU A 1 72  ? 75.26773  54.50815  27.30143  1.000 44.13284  ?  72  LEU C CB  1 
ATOM   571  C CG  . LEU A 1 72  ? 76.76661  54.20270  27.36477  1.000 46.44364  ?  72  LEU C CG  1 
ATOM   572  C CD1 . LEU A 1 72  ? 77.11243  53.43827  28.63339  1.000 42.54509  ?  72  LEU C CD1 1 
ATOM   573  C CD2 . LEU A 1 72  ? 77.20796  53.42688  26.13450  1.000 50.96678  ?  72  LEU C CD2 1 
ATOM   574  N N   . GLY A 1 73  ? 75.13114  57.63099  27.99295  1.000 49.97270  ?  73  GLY C N   1 
ATOM   575  C CA  . GLY A 1 73  ? 75.80530  58.89936  28.21161  1.000 51.37244  ?  73  GLY C CA  1 
ATOM   576  C C   . GLY A 1 73  ? 75.52019  59.48076  29.58274  1.000 63.24014  ?  73  GLY C C   1 
ATOM   577  O O   . GLY A 1 73  ? 76.39427  60.09462  30.20060  1.000 89.18147  ?  73  GLY C O   1 
ATOM   578  N N   . VAL A 1 74  ? 74.29584  59.29402  30.07896  1.000 53.49504  ?  74  VAL C N   1 
ATOM   579  C CA  . VAL A 1 74  ? 73.95125  59.78421  31.40944  1.000 58.99411  ?  74  VAL C CA  1 
ATOM   580  C C   . VAL A 1 74  ? 74.63489  58.94419  32.48113  1.000 71.71998  ?  74  VAL C C   1 
ATOM   581  O O   . VAL A 1 74  ? 75.07824  59.46617  33.51133  1.000 81.04293  ?  74  VAL C O   1 
ATOM   582  C CB  . VAL A 1 74  ? 72.42233  59.80206  31.58883  1.000 55.68141  ?  74  VAL C CB  1 
ATOM   583  C CG1 . VAL A 1 74  ? 72.05107  60.29007  32.98116  1.000 65.35303  ?  74  VAL C CG1 1 
ATOM   584  C CG2 . VAL A 1 74  ? 71.77555  60.67282  30.52249  1.000 55.35996  ?  74  VAL C CG2 1 
ATOM   585  N N   . LEU A 1 75  ? 74.74066  57.63324  32.25470  1.000 61.72425  ?  75  LEU C N   1 
ATOM   586  C CA  . LEU A 1 75  ? 75.38218  56.76564  33.23628  1.000 66.68082  ?  75  LEU C CA  1 
ATOM   587  C C   . LEU A 1 75  ? 76.89283  56.95463  33.25854  1.000 73.28493  ?  75  LEU C C   1 
ATOM   588  O O   . LEU A 1 75  ? 77.51445  56.82338  34.31918  1.000 89.31968  ?  75  LEU C O   1 
ATOM   589  C CB  . LEU A 1 75  ? 75.03569  55.30583  32.95389  1.000 65.99127  ?  75  LEU C CB  1 
ATOM   590  C CG  . LEU A 1 75  ? 73.85470  54.71883  33.72779  1.000 52.90941  ?  75  LEU C CG  1 
ATOM   591  C CD1 . LEU A 1 75  ? 72.59335  55.54848  33.54522  1.000 66.56905  ?  75  LEU C CD1 1 
ATOM   592  C CD2 . LEU A 1 75  ? 73.62376  53.29609  33.28068  1.000 62.31298  ?  75  LEU C CD2 1 
ATOM   593  N N   . THR A 1 76  ? 77.50036  57.25086  32.10690  1.000 74.40357  ?  76  THR C N   1 
ATOM   594  C CA  . THR A 1 76  ? 78.93311  57.52763  32.08171  1.000 86.25379  ?  76  THR C CA  1 
ATOM   595  C C   . THR A 1 76  ? 79.26204  58.76661  32.90524  1.000 83.66887  ?  76  THR C C   1 
ATOM   596  O O   . THR A 1 76  ? 80.27739  58.80422  33.61065  1.000 89.47622  ?  76  THR C O   1 
ATOM   597  C CB  . THR A 1 76  ? 79.41151  57.69593  30.63847  1.000 72.69479  ?  76  THR C CB  1 
ATOM   598  O OG1 . THR A 1 76  ? 79.14250  56.49691  29.90186  1.000 60.91840  ?  76  THR C OG1 1 
ATOM   599  C CG2 . THR A 1 76  ? 80.90574  57.98056  30.59672  1.000 91.30858  ?  76  THR C CG2 1 
ATOM   600  N N   . LYS A 1 77  ? 78.40484  59.78310  32.84088  1.000 72.58544  ?  77  LYS C N   1 
ATOM   601  C CA  . LYS A 1 77  ? 78.56462  61.00371  33.61920  1.000 78.81936  ?  77  LYS C CA  1 
ATOM   602  C C   . LYS A 1 77  ? 78.12007  60.84485  35.06854  1.000 93.38602  ?  77  LYS C C   1 
ATOM   603  O O   . LYS A 1 77  ? 78.12827  61.83019  35.81427  1.000 99.47626  ?  77  LYS C O   1 
ATOM   604  C CB  . LYS A 1 77  ? 77.78639  62.14741  32.96300  1.000 83.08809  ?  77  LYS C CB  1 
ATOM   605  C CG  . LYS A 1 77  ? 78.20063  62.43908  31.52917  1.000 103.78697 ?  77  LYS C CG  1 
ATOM   606  C CD  . LYS A 1 77  ? 77.35916  63.55365  30.92686  1.000 114.70449 ?  77  LYS C CD  1 
ATOM   607  C CE  . LYS A 1 77  ? 77.73832  63.81634  29.47736  1.000 118.73016 ?  77  LYS C CE  1 
ATOM   608  N NZ  . LYS A 1 77  ? 76.92643  64.91751  28.88762  1.000 136.44485 ?  77  LYS C NZ  1 
ATOM   609  N N   . ARG A 1 78  ? 77.73063  59.64040  35.47997  1.000 90.86467  ?  78  ARG C N   1 
ATOM   610  C CA  . ARG A 1 78  ? 77.29795  59.37191  36.84624  1.000 90.55705  ?  78  ARG C CA  1 
ATOM   611  C C   . ARG A 1 78  ? 78.25803  58.48192  37.61741  1.000 87.45461  ?  78  ARG C C   1 
ATOM   612  O O   . ARG A 1 78  ? 78.48395  58.71310  38.80728  1.000 113.19300 ?  78  ARG C O   1 
ATOM   613  C CB  . ARG A 1 78  ? 75.90662  58.72638  36.84288  1.000 92.29772  ?  78  ARG C CB  1 
ATOM   614  C CG  . ARG A 1 78  ? 75.31152  58.52410  38.22793  1.000 90.63053  ?  78  ARG C CG  1 
ATOM   615  C CD  . ARG A 1 78  ? 73.99120  57.77270  38.16342  1.000 78.66037  ?  78  ARG C CD  1 
ATOM   616  N NE  . ARG A 1 78  ? 72.97955  58.49685  37.40349  1.000 86.31573  ?  78  ARG C NE  1 
ATOM   617  C CZ  . ARG A 1 78  ? 71.75498  58.04529  37.16904  1.000 85.98192  ?  78  ARG C CZ  1 
ATOM   618  N NH1 . ARG A 1 78  ? 71.35345  56.86901  37.62256  1.000 69.53479  ?  78  ARG C NH1 1 
ATOM   619  N NH2 . ARG A 1 78  ? 70.91237  58.79197  36.46088  1.000 90.42948  ?  78  ARG C NH2 1 
ATOM   620  N N   . SER A 1 79  ? 78.83459  57.46956  36.97042  1.000 83.15456  ?  79  SER C N   1 
ATOM   621  C CA  . SER A 1 79  ? 79.75710  56.55062  37.62053  1.000 94.15469  ?  79  SER C CA  1 
ATOM   622  C C   . SER A 1 79  ? 81.20286  57.02928  37.56369  1.000 100.52468 ?  79  SER C C   1 
ATOM   623  O O   . SER A 1 79  ? 82.11789  56.22588  37.78173  1.000 104.95631 ?  79  SER C O   1 
ATOM   624  C CB  . SER A 1 79  ? 79.64175  55.15752  36.99636  1.000 87.34596  ?  79  SER C CB  1 
ATOM   625  O OG  . SER A 1 79  ? 80.01606  55.17614  35.62996  1.000 79.91165  ?  79  SER C OG  1 
ATOM   626  N N   . ASN A 1 80  ? 81.42509  58.31379  37.27494  1.000 99.30446  ?  80  ASN C N   1 
ATOM   627  C CA  . ASN A 1 80  ? 82.77060  58.88285  37.18097  1.000 114.86436 ?  80  ASN C CA  1 
ATOM   628  C C   . ASN A 1 80  ? 83.60858  58.15456  36.13233  1.000 124.94029 ?  80  ASN C C   1 
ATOM   629  O O   . ASN A 1 80  ? 84.82319  58.00276  36.27948  1.000 116.97175 ?  80  ASN C O   1 
ATOM   630  C CB  . ASN A 1 80  ? 83.46846  58.87855  38.54403  1.000 106.60974 ?  80  ASN C CB  1 
ATOM   631  C CG  . ASN A 1 80  ? 82.82921  59.84087  39.52537  1.000 133.30436 ?  80  ASN C CG  1 
ATOM   632  O OD1 . ASN A 1 80  ? 82.32023  60.89096  39.13479  1.000 134.96128 ?  80  ASN C OD1 1 
ATOM   633  N ND2 . ASN A 1 80  ? 82.85419  59.48996  40.80577  1.000 142.62542 ?  80  ASN C ND2 1 
ATOM   634  N N   . SER A 1 81  ? 82.94639  57.70216  35.06432  1.000 116.29258 ?  81  SER C N   1 
ATOM   635  C CA  . SER A 1 81  ? 83.57731  56.98581  33.95489  1.000 110.10164 ?  81  SER C CA  1 
ATOM   636  C C   . SER A 1 81  ? 84.32636  55.74807  34.46117  1.000 110.83868 ?  81  SER C C   1 
ATOM   637  O O   . SER A 1 81  ? 85.55661  55.69598  34.51786  1.000 110.86720 ?  81  SER C O   1 
ATOM   638  C CB  . SER A 1 81  ? 84.50497  57.91480  33.16148  1.000 121.98464 ?  81  SER C CB  1 
ATOM   639  O OG  . SER A 1 81  ? 83.77923  58.98438  32.57908  1.000 114.01222 ?  81  SER C OG  1 
ATOM   640  N N   . THR A 1 82  ? 83.53357  54.74194  34.82968  1.000 109.26025 ?  82  THR C N   1 
ATOM   641  C CA  . THR A 1 82  ? 84.07705  53.48393  35.31646  1.000 98.68619  ?  82  THR C CA  1 
ATOM   642  C C   . THR A 1 82  ? 83.94398  52.43174  34.22755  1.000 97.08629  ?  82  THR C C   1 
ATOM   643  O O   . THR A 1 82  ? 82.82393  51.96737  33.96443  1.000 106.09789 ?  82  THR C O   1 
ATOM   644  C CB  . THR A 1 82  ? 83.35276  53.03302  36.58387  1.000 93.57208  ?  82  THR C CB  1 
ATOM   645  O OG1 . THR A 1 82  ? 83.44495  54.05855  37.58100  1.000 82.17156  ?  82  THR C OG1 1 
ATOM   646  C CG2 . THR A 1 82  ? 83.97576  51.75278  37.12470  1.000 89.51463  ?  82  THR C CG2 1 
ATOM   647  N N   . PRO A 1 83  ? 85.02801  52.02746  33.57215  1.000 90.36754  ?  83  PRO C N   1 
ATOM   648  C CA  . PRO A 1 83  ? 84.92880  51.02998  32.50641  1.000 76.53399  ?  83  PRO C CA  1 
ATOM   649  C C   . PRO A 1 83  ? 85.10904  49.60939  33.02479  1.000 76.21775  ?  83  PRO C C   1 
ATOM   650  O O   . PRO A 1 83  ? 85.66374  49.36723  34.09870  1.000 90.57866  ?  83  PRO C O   1 
ATOM   651  C CB  . PRO A 1 83  ? 86.07774  51.41884  31.56413  1.000 68.52670  ?  83  PRO C CB  1 
ATOM   652  C CG  . PRO A 1 83  ? 87.06538  52.18176  32.43645  1.000 67.93234  ?  83  PRO C CG  1 
ATOM   653  C CD  . PRO A 1 83  ? 86.41694  52.46960  33.77308  1.000 68.74525  ?  83  PRO C CD  1 
ATOM   654  N N   . ALA A 1 84  ? 84.61933  48.66440  32.22922  1.000 78.96863  ?  84  ALA C N   1 
ATOM   655  C CA  . ALA A 1 84  ? 84.70690  47.24783  32.54988  1.000 95.34154  ?  84  ALA C CA  1 
ATOM   656  C C   . ALA A 1 84  ? 85.89773  46.62561  31.83398  1.000 86.51333  ?  84  ALA C C   1 
ATOM   657  O O   . ALA A 1 84  ? 86.16833  46.93613  30.67006  1.000 87.08001  ?  84  ALA C O   1 
ATOM   658  C CB  . ALA A 1 84  ? 83.42025  46.51786  32.16221  1.000 93.31633  ?  84  ALA C CB  1 
ATOM   659  N N   . THR A 1 85  ? 86.60442  45.74485  32.53693  1.000 79.32043  ?  85  THR C N   1 
ATOM   660  C CA  . THR A 1 85  ? 87.80624  45.13618  31.98995  1.000 89.74903  ?  85  THR C CA  1 
ATOM   661  C C   . THR A 1 85  ? 87.45908  44.14217  30.88418  1.000 80.00895  ?  85  THR C C   1 
ATOM   662  O O   . THR A 1 85  ? 86.33096  43.65248  30.77645  1.000 70.05132  ?  85  THR C O   1 
ATOM   663  C CB  . THR A 1 85  ? 88.60207  44.43234  33.08982  1.000 91.46025  ?  85  THR C CB  1 
ATOM   664  O OG1 . THR A 1 85  ? 87.79766  43.40465  33.68174  1.000 97.42632  ?  85  THR C OG1 1 
ATOM   665  C CG2 . THR A 1 85  ? 89.01792  45.42593  34.16511  1.000 102.75084 ?  85  THR C CG2 1 
ATOM   666  N N   . ASN A 1 86  ? 88.45562  43.84794  30.05426  1.000 69.60790  ?  86  ASN C N   1 
ATOM   667  C CA  . ASN A 1 86  ? 88.28167  42.90201  28.96403  1.000 62.63745  ?  86  ASN C CA  1 
ATOM   668  C C   . ASN A 1 86  ? 88.39043  41.47069  29.47446  1.000 60.04706  ?  86  ASN C C   1 
ATOM   669  O O   . ASN A 1 86  ? 89.07329  41.18875  30.46302  1.000 60.77659  ?  86  ASN C O   1 
ATOM   670  C CB  . ASN A 1 86  ? 89.32188  43.14352  27.86936  1.000 53.90435  ?  86  ASN C CB  1 
ATOM   671  C CG  . ASN A 1 86  ? 89.25004  44.54470  27.29499  1.000 60.67184  ?  86  ASN C CG  1 
ATOM   672  O OD1 . ASN A 1 86  ? 88.19057  45.17024  27.28417  1.000 77.72869  ?  86  ASN C OD1 1 
ATOM   673  N ND2 . ASN A 1 86  ? 90.38124  45.04519  26.81314  1.000 66.07204  ?  86  ASN C ND2 1 
ATOM   674  N N   . GLU A 1 87  ? 87.70377  40.56460  28.78809  1.000 63.48545  ?  87  GLU C N   1 
ATOM   675  C CA  . GLU A 1 87  ? 87.72276  39.14850  29.11398  1.000 51.48752  ?  87  GLU C CA  1 
ATOM   676  C C   . GLU A 1 87  ? 88.39959  38.36174  27.99971  1.000 66.73736  ?  87  GLU C C   1 
ATOM   677  O O   . GLU A 1 87  ? 88.46331  38.79821  26.84695  1.000 57.58919  ?  87  GLU C O   1 
ATOM   678  C CB  . GLU A 1 87  ? 86.30313  38.61643  29.34280  1.000 65.12682  ?  87  GLU C CB  1 
ATOM   679  C CG  . GLU A 1 87  ? 85.66192  39.07484  30.64336  1.000 61.86268  ?  87  GLU C CG  1 
ATOM   680  C CD  . GLU A 1 87  ? 86.18275  38.32167  31.85248  1.000 70.97348  ?  87  GLU C CD  1 
ATOM   681  O OE1 . GLU A 1 87  ? 86.94295  37.34690  31.67026  1.000 87.01235  ?  87  GLU C OE1 1 
ATOM   682  O OE2 . GLU A 1 87  ? 85.82822  38.70269  32.98774  1.000 90.56351  -1 87  GLU C OE2 1 
ATOM   683  N N   . ALA A 1 88  ? 88.91128  37.18793  28.36394  1.000 75.74419  ?  88  ALA C N   1 
ATOM   684  C CA  . ALA A 1 88  ? 89.53716  36.29454  27.39967  1.000 56.06060  ?  88  ALA C CA  1 
ATOM   685  C C   . ALA A 1 88  ? 88.50864  35.29231  26.89489  1.000 55.05255  ?  88  ALA C C   1 
ATOM   686  O O   . ALA A 1 88  ? 88.01050  34.48252  27.68871  1.000 61.92976  ?  88  ALA C O   1 
ATOM   687  C CB  . ALA A 1 88  ? 90.71321  35.56553  28.02561  1.000 57.47760  ?  88  ALA C CB  1 
ATOM   688  N N   . PRO A 1 89  ? 88.15906  35.30860  25.61156  1.000 57.53195  ?  89  PRO C N   1 
ATOM   689  C CA  . PRO A 1 89  ? 87.14496  34.37638  25.10615  1.000 48.37252  ?  89  PRO C CA  1 
ATOM   690  C C   . PRO A 1 89  ? 87.69102  32.96062  24.98908  1.000 56.21062  ?  89  PRO C C   1 
ATOM   691  O O   . PRO A 1 89  ? 88.89542  32.70912  25.06078  1.000 55.63261  ?  89  PRO C O   1 
ATOM   692  C CB  . PRO A 1 89  ? 86.78695  34.95265  23.73418  1.000 52.47727  ?  89  PRO C CB  1 
ATOM   693  C CG  . PRO A 1 89  ? 88.01711  35.68569  23.31146  1.000 61.21929  ?  89  PRO C CG  1 
ATOM   694  C CD  . PRO A 1 89  ? 88.62453  36.24270  24.57176  1.000 45.34453  ?  89  PRO C CD  1 
ATOM   695  N N   . GLN A 1 90  ? 86.76534  32.02122  24.80534  1.000 61.93868  ?  90  GLN C N   1 
ATOM   696  C CA  . GLN A 1 90  ? 87.08694  30.60976  24.64109  1.000 52.22071  ?  90  GLN C CA  1 
ATOM   697  C C   . GLN A 1 90  ? 86.34457  30.08289  23.42323  1.000 51.15378  ?  90  GLN C C   1 
ATOM   698  O O   . GLN A 1 90  ? 85.13573  30.29929  23.29225  1.000 65.91188  ?  90  GLN C O   1 
ATOM   699  C CB  . GLN A 1 90  ? 86.69985  29.80125  25.88530  1.000 70.92607  ?  90  GLN C CB  1 
ATOM   700  C CG  . GLN A 1 90  ? 87.27362  30.33035  27.19152  1.000 91.94111  ?  90  GLN C CG  1 
ATOM   701  C CD  . GLN A 1 90  ? 86.48924  29.85959  28.40394  1.000 115.43035 ?  90  GLN C CD  1 
ATOM   702  O OE1 . GLN A 1 90  ? 85.39356  29.31124  28.27482  1.000 114.57113 ?  90  GLN C OE1 1 
ATOM   703  N NE2 . GLN A 1 90  ? 87.04620  30.07530  29.59002  1.000 127.07086 ?  90  GLN C NE2 1 
ATOM   704  N N   . ALA A 1 91  ? 87.06111  29.39248  22.54037  1.000 53.42597  ?  91  ALA C N   1 
ATOM   705  C CA  . ALA A 1 91  ? 86.49556  28.87755  21.30263  1.000 56.12135  ?  91  ALA C CA  1 
ATOM   706  C C   . ALA A 1 91  ? 86.37350  27.35939  21.35431  1.000 51.94733  ?  91  ALA C C   1 
ATOM   707  O O   . ALA A 1 91  ? 87.11914  26.68060  22.06567  1.000 55.02818  ?  91  ALA C O   1 
ATOM   708  C CB  . ALA A 1 91  ? 87.34677  29.28513  20.09592  1.000 72.37272  ?  91  ALA C CB  1 
ATOM   709  N N   . THR A 1 92  ? 85.42037  26.83455  20.58656  1.000 63.98713  ?  92  THR C N   1 
ATOM   710  C CA  . THR A 1 92  ? 85.19271  25.39847  20.49231  1.000 51.14445  ?  92  THR C CA  1 
ATOM   711  C C   . THR A 1 92  ? 84.68791  25.08787  19.09263  1.000 57.78725  ?  92  THR C C   1 
ATOM   712  O O   . THR A 1 92  ? 83.71411  25.69418  18.63689  1.000 59.55247  ?  92  THR C O   1 
ATOM   713  C CB  . THR A 1 92  ? 84.18200  24.91912  21.54205  1.000 57.05195  ?  92  THR C CB  1 
ATOM   714  O OG1 . THR A 1 92  ? 84.65513  25.25104  22.85329  1.000 87.61373  ?  92  THR C OG1 1 
ATOM   715  C CG2 . THR A 1 92  ? 83.98592  23.41226  21.44858  1.000 58.41179  ?  92  THR C CG2 1 
ATOM   716  N N   . VAL A 1 93  ? 85.35152  24.15503  18.41545  1.000 58.94363  ?  93  VAL C N   1 
ATOM   717  C CA  . VAL A 1 93  ? 85.01519  23.77678  17.04803  1.000 53.56994  ?  93  VAL C CA  1 
ATOM   718  C C   . VAL A 1 93  ? 84.40783  22.38225  17.06777  1.000 64.44648  ?  93  VAL C C   1 
ATOM   719  O O   . VAL A 1 93  ? 84.96724  21.46224  17.67710  1.000 69.17824  ?  93  VAL C O   1 
ATOM   720  C CB  . VAL A 1 93  ? 86.24672  23.82916  16.12790  1.000 56.96435  ?  93  VAL C CB  1 
ATOM   721  C CG1 . VAL A 1 93  ? 85.86816  23.42837  14.71053  1.000 58.86489  ?  93  VAL C CG1 1 
ATOM   722  C CG2 . VAL A 1 93  ? 86.85762  25.21931  16.14636  1.000 61.16239  ?  93  VAL C CG2 1 
ATOM   723  N N   . PHE A 1 94  ? 83.26282  22.22856  16.40516  1.000 53.96765  ?  94  PHE C N   1 
ATOM   724  C CA  . PHE A 1 94  ? 82.58850  20.94194  16.30873  1.000 61.36940  ?  94  PHE C CA  1 
ATOM   725  C C   . PHE A 1 94  ? 81.73076  20.94742  15.05471  1.000 62.02541  ?  94  PHE C C   1 
ATOM   726  O O   . PHE A 1 94  ? 81.31075  22.01935  14.60416  1.000 59.34283  ?  94  PHE C O   1 
ATOM   727  C CB  . PHE A 1 94  ? 81.72996  20.66708  17.55386  1.000 58.46548  ?  94  PHE C CB  1 
ATOM   728  C CG  . PHE A 1 94  ? 80.56480  21.60353  17.71276  1.000 60.53134  ?  94  PHE C CG  1 
ATOM   729  C CD1 . PHE A 1 94  ? 80.73011  22.84325  18.30784  1.000 55.14815  ?  94  PHE C CD1 1 
ATOM   730  C CD2 . PHE A 1 94  ? 79.29994  21.23704  17.28016  1.000 59.21084  ?  94  PHE C CD2 1 
ATOM   731  C CE1 . PHE A 1 94  ? 79.65841  23.70387  18.45875  1.000 49.81979  ?  94  PHE C CE1 1 
ATOM   732  C CE2 . PHE A 1 94  ? 78.22509  22.09315  17.42826  1.000 54.11601  ?  94  PHE C CE2 1 
ATOM   733  C CZ  . PHE A 1 94  ? 78.40449  23.32765  18.01868  1.000 47.39672  ?  94  PHE C CZ  1 
ATOM   734  N N   . PRO A 1 95  ? 81.46131  19.78574  14.46546  1.000 62.06156  ?  95  PRO C N   1 
ATOM   735  C CA  . PRO A 1 95  ? 80.63257  19.74667  13.25840  1.000 65.97063  ?  95  PRO C CA  1 
ATOM   736  C C   . PRO A 1 95  ? 79.14745  19.76427  13.58370  1.000 69.05997  ?  95  PRO C C   1 
ATOM   737  O O   . PRO A 1 95  ? 78.70797  19.32721  14.65029  1.000 67.40335  ?  95  PRO C O   1 
ATOM   738  C CB  . PRO A 1 95  ? 81.03375  18.42216  12.59079  1.000 58.91600  ?  95  PRO C CB  1 
ATOM   739  C CG  . PRO A 1 95  ? 82.06061  17.77582  13.51179  1.000 56.11528  ?  95  PRO C CG  1 
ATOM   740  C CD  . PRO A 1 95  ? 81.94375  18.44760  14.83472  1.000 54.81526  ?  95  PRO C CD  1 
ATOM   741  N N   . LYS A 1 96  ? 78.37110  20.28575  12.63083  1.000 66.71999  ?  96  LYS C N   1 
ATOM   742  C CA  . LYS A 1 96  ? 76.92401  20.36235  12.79883  1.000 60.83461  ?  96  LYS C CA  1 
ATOM   743  C C   . LYS A 1 96  ? 76.26701  18.99639  12.63400  1.000 76.72395  ?  96  LYS C C   1 
ATOM   744  O O   . LYS A 1 96  ? 75.39428  18.62352  13.42650  1.000 84.53631  ?  96  LYS C O   1 
ATOM   745  C CB  . LYS A 1 96  ? 76.33632  21.36272  11.80098  1.000 63.93089  ?  96  LYS C CB  1 
ATOM   746  C CG  . LYS A 1 96  ? 74.81762  21.35642  11.72358  1.000 73.81370  ?  96  LYS C CG  1 
ATOM   747  C CD  . LYS A 1 96  ? 74.31386  22.37151  10.70720  1.000 67.31357  ?  96  LYS C CD  1 
ATOM   748  C CE  . LYS A 1 96  ? 72.82849  22.19151  10.43079  1.000 72.97233  ?  96  LYS C CE  1 
ATOM   749  N NZ  . LYS A 1 96  ? 72.00448  22.32762  11.66356  1.000 89.19952  ?  96  LYS C NZ  1 
ATOM   750  N N   . SER A 1 97  ? 76.66946  18.24385  11.61828  1.000 72.76244  ?  97  SER C N   1 
ATOM   751  C CA  . SER A 1 97  ? 76.12802  16.93128  11.31401  1.000 71.59451  ?  97  SER C CA  1 
ATOM   752  C C   . SER A 1 97  ? 77.21079  15.87276  11.48205  1.000 80.86336  ?  97  SER C C   1 
ATOM   753  O O   . SER A 1 97  ? 78.40467  16.19594  11.50393  1.000 69.34997  ?  97  SER C O   1 
ATOM   754  C CB  . SER A 1 97  ? 75.57662  16.89601  9.88023   1.000 93.00479  ?  97  SER C CB  1 
ATOM   755  O OG  . SER A 1 97  ? 74.52651  17.83303  9.71217   1.000 98.50338  ?  97  SER C OG  1 
ATOM   756  N N   . PRO A 1 98  ? 76.83360  14.60055  11.62251  1.000 92.77596  ?  98  PRO C N   1 
ATOM   757  C CA  . PRO A 1 98  ? 77.84885  13.54029  11.69032  1.000 82.37454  ?  98  PRO C CA  1 
ATOM   758  C C   . PRO A 1 98  ? 78.71394  13.53058  10.43814  1.000 87.57915  ?  98  PRO C C   1 
ATOM   759  O O   . PRO A 1 98  ? 78.21070  13.52885  9.31232   1.000 98.28748  ?  98  PRO C O   1 
ATOM   760  C CB  . PRO A 1 98  ? 77.01847  12.25685  11.82392  1.000 83.46455  ?  98  PRO C CB  1 
ATOM   761  C CG  . PRO A 1 98  ? 75.63220  12.63545  11.40028  1.000 93.14725  ?  98  PRO C CG  1 
ATOM   762  C CD  . PRO A 1 98  ? 75.47503  14.06394  11.80674  1.000 94.46804  ?  98  PRO C CD  1 
ATOM   763  N N   . VAL A 1 99  ? 80.02902  13.52583  10.64775  1.000 80.83815  ?  99  VAL C N   1 
ATOM   764  C CA  . VAL A 1 99  ? 80.97558  13.71404  9.55377   1.000 82.49008  ?  99  VAL C CA  1 
ATOM   765  C C   . VAL A 1 99  ? 80.96439  12.48870  8.64964   1.000 88.27747  ?  99  VAL C C   1 
ATOM   766  O O   . VAL A 1 99  ? 81.20323  11.36143  9.09868   1.000 76.96809  ?  99  VAL C O   1 
ATOM   767  C CB  . VAL A 1 99  ? 82.38503  13.99170  10.09046  1.000 77.44305  ?  99  VAL C CB  1 
ATOM   768  C CG1 . VAL A 1 99  ? 83.37162  14.12810  8.94029   1.000 79.27428  ?  99  VAL C CG1 1 
ATOM   769  C CG2 . VAL A 1 99  ? 82.38496  15.24454  10.94688  1.000 69.78828  ?  99  VAL C CG2 1 
ATOM   770  N N   . LEU A 1 100 ? 80.68528  12.70885  7.36709   1.000 94.26251  ?  100 LEU C N   1 
ATOM   771  C CA  . LEU A 1 100 ? 80.80521  11.68410  6.33799   1.000 92.06135  ?  100 LEU C CA  1 
ATOM   772  C C   . LEU A 1 100 ? 81.67633  12.24160  5.22478   1.000 94.47019  ?  100 LEU C C   1 
ATOM   773  O O   . LEU A 1 100 ? 81.38196  13.31246  4.68308   1.000 83.67836  ?  100 LEU C O   1 
ATOM   774  C CB  . LEU A 1 100 ? 79.43508  11.26700  5.79580   1.000 91.02127  ?  100 LEU C CB  1 
ATOM   775  C CG  . LEU A 1 100 ? 78.51126  10.52835  6.76485   1.000 97.05420  ?  100 LEU C CG  1 
ATOM   776  C CD1 . LEU A 1 100 ? 77.22368  10.11790  6.06696   1.000 94.56681  ?  100 LEU C CD1 1 
ATOM   777  C CD2 . LEU A 1 100 ? 79.21487  9.31778   7.35637   1.000 87.46884  ?  100 LEU C CD2 1 
ATOM   778  N N   . LEU A 1 101 ? 82.74820  11.52530  4.89471   1.000 99.21266  ?  101 LEU C N   1 
ATOM   779  C CA  . LEU A 1 101 ? 83.66702  11.98903  3.86420   1.000 92.20396  ?  101 LEU C CA  1 
ATOM   780  C C   . LEU A 1 101 ? 82.95048  12.09208  2.52414   1.000 97.89678  ?  101 LEU C C   1 
ATOM   781  O O   . LEU A 1 101 ? 82.22643  11.17794  2.12053   1.000 113.65845 ?  101 LEU C O   1 
ATOM   782  C CB  . LEU A 1 101 ? 84.86757  11.04660  3.75918   1.000 82.39963  ?  101 LEU C CB  1 
ATOM   783  C CG  . LEU A 1 101 ? 86.04444  11.27766  4.71546   1.000 97.61751  ?  101 LEU C CG  1 
ATOM   784  C CD1 . LEU A 1 101 ? 85.64433  11.09303  6.17396   1.000 88.75721  ?  101 LEU C CD1 1 
ATOM   785  C CD2 . LEU A 1 101 ? 87.20823  10.36204  4.36171   1.000 106.21361 ?  101 LEU C CD2 1 
ATOM   786  N N   . GLY A 1 102 ? 83.14156  13.22121  1.84259   1.000 92.00464  ?  102 GLY C N   1 
ATOM   787  C CA  . GLY A 1 102 ? 82.51616  13.48239  0.56725   1.000 98.57926  ?  102 GLY C CA  1 
ATOM   788  C C   . GLY A 1 102 ? 81.15534  14.14613  0.65203   1.000 104.01825 ?  102 GLY C C   1 
ATOM   789  O O   . GLY A 1 102 ? 80.76019  14.84899  -0.28407  1.000 104.85254 ?  102 GLY C O   1 
ATOM   790  N N   . GLN A 1 103 ? 80.42675  13.93900  1.75110   1.000 94.09201  ?  103 GLN C N   1 
ATOM   791  C CA  . GLN A 1 103 ? 79.10786  14.54213  1.91804   1.000 110.16599 ?  103 GLN C CA  1 
ATOM   792  C C   . GLN A 1 103 ? 79.24337  15.91855  2.55747   1.000 92.77440  ?  103 GLN C C   1 
ATOM   793  O O   . GLN A 1 103 ? 79.88967  16.04365  3.60371   1.000 72.77249  ?  103 GLN C O   1 
ATOM   794  C CB  . GLN A 1 103 ? 78.21375  13.66021  2.77821   1.000 110.30741 ?  103 GLN C CB  1 
ATOM   795  N N   . PRO A 1 104 ? 78.64937  16.95766  1.96889   1.000 88.22613  ?  104 PRO C N   1 
ATOM   796  C CA  . PRO A 1 104 ? 78.84287  18.31690  2.49167   1.000 74.10436  ?  104 PRO C CA  1 
ATOM   797  C C   . PRO A 1 104 ? 78.39196  18.44246  3.94011   1.000 77.67963  ?  104 PRO C C   1 
ATOM   798  O O   . PRO A 1 104 ? 77.41535  17.82217  4.36574   1.000 89.33688  ?  104 PRO C O   1 
ATOM   799  C CB  . PRO A 1 104 ? 77.98395  19.17933  1.55939   1.000 78.15183  ?  104 PRO C CB  1 
ATOM   800  C CG  . PRO A 1 104 ? 77.86173  18.37593  0.30526   1.000 95.53035  ?  104 PRO C CG  1 
ATOM   801  C CD  . PRO A 1 104 ? 77.82535  16.94438  0.74885   1.000 94.23173  ?  104 PRO C CD  1 
ATOM   802  N N   . ASN A 1 105 ? 79.12237  19.25842  4.69686   1.000 70.77918  ?  105 ASN C N   1 
ATOM   803  C CA  . ASN A 1 105 ? 78.84837  19.46059  6.11131   1.000 69.00065  ?  105 ASN C CA  1 
ATOM   804  C C   . ASN A 1 105 ? 79.22921  20.88929  6.47628   1.000 74.87012  ?  105 ASN C C   1 
ATOM   805  O O   . ASN A 1 105 ? 79.84524  21.61088  5.68792   1.000 81.36358  ?  105 ASN C O   1 
ATOM   806  C CB  . ASN A 1 105 ? 79.60643  18.44112  6.97203   1.000 61.58766  ?  105 ASN C CB  1 
ATOM   807  C CG  . ASN A 1 105 ? 79.02644  18.30237  8.36685   1.000 66.77007  ?  105 ASN C CG  1 
ATOM   808  O OD1 . ASN A 1 105 ? 78.61394  19.28472  8.98318   1.000 76.23935  ?  105 ASN C OD1 1 
ATOM   809  N ND2 . ASN A 1 105 ? 78.99072  17.07441  8.87122   1.000 74.30273  ?  105 ASN C ND2 1 
ATOM   810  N N   . THR A 1 106 ? 78.85252  21.29472  7.68652   1.000 62.71072  ?  106 THR C N   1 
ATOM   811  C CA  . THR A 1 106 ? 79.12370  22.63379  8.19167   1.000 58.20244  ?  106 THR C CA  1 
ATOM   812  C C   . THR A 1 106 ? 79.92249  22.53620  9.48301   1.000 61.89222  ?  106 THR C C   1 
ATOM   813  O O   . THR A 1 106 ? 79.56655  21.76650  10.38183  1.000 55.81945  ?  106 THR C O   1 
ATOM   814  C CB  . THR A 1 106 ? 77.82399  23.40942  8.43262   1.000 63.83086  ?  106 THR C CB  1 
ATOM   815  O OG1 . THR A 1 106 ? 77.11679  23.55815  7.19519   1.000 86.33526  ?  106 THR C OG1 1 
ATOM   816  C CG2 . THR A 1 106 ? 78.12045  24.78700  9.00840   1.000 55.48505  ?  106 THR C CG2 1 
ATOM   817  N N   . LEU A 1 107 ? 80.99912  23.31167  9.56889   1.000 56.20876  ?  107 LEU C N   1 
ATOM   818  C CA  . LEU A 1 107 ? 81.82069  23.38700  10.76729  1.000 55.62221  ?  107 LEU C CA  1 
ATOM   819  C C   . LEU A 1 107 ? 81.40411  24.59851  11.59079  1.000 55.02587  ?  107 LEU C C   1 
ATOM   820  O O   . LEU A 1 107 ? 81.16728  25.68045  11.04569  1.000 59.71277  ?  107 LEU C O   1 
ATOM   821  C CB  . LEU A 1 107 ? 83.30474  23.47578  10.40617  1.000 45.91459  ?  107 LEU C CB  1 
ATOM   822  C CG  . LEU A 1 107 ? 84.27428  22.72154  11.31762  1.000 66.57411  ?  107 LEU C CG  1 
ATOM   823  C CD1 . LEU A 1 107 ? 83.92192  21.24277  11.36138  1.000 65.19901  ?  107 LEU C CD1 1 
ATOM   824  C CD2 . LEU A 1 107 ? 85.70776  22.91463  10.85139  1.000 64.39865  ?  107 LEU C CD2 1 
ATOM   825  N N   . ILE A 1 108 ? 81.31102  24.41112  12.90460  1.000 51.15954  ?  108 ILE C N   1 
ATOM   826  C CA  . ILE A 1 108 ? 80.82576  25.43717  13.81990  1.000 43.94395  ?  108 ILE C CA  1 
ATOM   827  C C   . ILE A 1 108 ? 81.93735  25.78445  14.79826  1.000 53.15322  ?  108 ILE C C   1 
ATOM   828  O O   . ILE A 1 108 ? 82.54044  24.88985  15.40145  1.000 66.49372  ?  108 ILE C O   1 
ATOM   829  C CB  . ILE A 1 108 ? 79.56839  24.97235  14.57680  1.000 52.85849  ?  108 ILE C CB  1 
ATOM   830  C CG1 . ILE A 1 108 ? 78.48016  24.53848  13.59360  1.000 51.00965  ?  108 ILE C CG1 1 
ATOM   831  C CG2 . ILE A 1 108 ? 79.06074  26.07525  15.49330  1.000 41.10829  ?  108 ILE C CG2 1 
ATOM   832  C CD1 . ILE A 1 108 ? 77.24341  23.98578  14.26397  1.000 51.67147  ?  108 ILE C CD1 1 
ATOM   833  N N   . CYS A 1 109 ? 82.20255  27.07943  14.95785  1.000 56.79694  ?  109 CYS C N   1 
ATOM   834  C CA  . CYS A 1 109 ? 83.14302  27.57987  15.95535  1.000 58.14435  ?  109 CYS C CA  1 
ATOM   835  C C   . CYS A 1 109 ? 82.35028  28.36645  16.99178  1.000 61.44296  ?  109 CYS C C   1 
ATOM   836  O O   . CYS A 1 109 ? 81.79037  29.42389  16.68286  1.000 50.47289  ?  109 CYS C O   1 
ATOM   837  C CB  . CYS A 1 109 ? 84.22753  28.44358  15.31569  1.000 56.84950  ?  109 CYS C CB  1 
ATOM   838  S SG  . CYS A 1 109 ? 85.50026  29.00249  16.47396  1.000 63.28857  ?  109 CYS C SG  1 
ATOM   839  N N   . PHE A 1 110 ? 82.30283  27.84737  18.21572  1.000 51.99895  ?  110 PHE C N   1 
ATOM   840  C CA  . PHE A 1 110 ? 81.52690  28.43841  19.29991  1.000 41.33062  ?  110 PHE C CA  1 
ATOM   841  C C   . PHE A 1 110 ? 82.47279  29.20455  20.21793  1.000 51.56707  ?  110 PHE C C   1 
ATOM   842  O O   . PHE A 1 110 ? 83.23499  28.60049  20.97950  1.000 57.10737  ?  110 PHE C O   1 
ATOM   843  C CB  . PHE A 1 110 ? 80.76608  27.35613  20.06281  1.000 46.86669  ?  110 PHE C CB  1 
ATOM   844  C CG  . PHE A 1 110 ? 80.06146  27.85667  21.28911  1.000 50.15229  ?  110 PHE C CG  1 
ATOM   845  C CD1 . PHE A 1 110 ? 78.90530  28.61041  21.18145  1.000 52.00141  ?  110 PHE C CD1 1 
ATOM   846  C CD2 . PHE A 1 110 ? 80.54822  27.56156  22.55131  1.000 60.77093  ?  110 PHE C CD2 1 
ATOM   847  C CE1 . PHE A 1 110 ? 78.25326  29.06885  22.30978  1.000 47.50313  ?  110 PHE C CE1 1 
ATOM   848  C CE2 . PHE A 1 110 ? 79.90015  28.01645  23.68331  1.000 60.62537  ?  110 PHE C CE2 1 
ATOM   849  C CZ  . PHE A 1 110 ? 78.75158  28.77116  23.56222  1.000 48.50465  ?  110 PHE C CZ  1 
ATOM   850  N N   . VAL A 1 111 ? 82.42137  30.53121  20.14503  1.000 50.13882  ?  111 VAL C N   1 
ATOM   851  C CA  . VAL A 1 111 ? 83.26810  31.40223  20.95170  1.000 48.89702  ?  111 VAL C CA  1 
ATOM   852  C C   . VAL A 1 111 ? 82.42373  31.96931  22.08394  1.000 44.99742  ?  111 VAL C C   1 
ATOM   853  O O   . VAL A 1 111 ? 81.42719  32.65924  21.83908  1.000 49.48931  ?  111 VAL C O   1 
ATOM   854  C CB  . VAL A 1 111 ? 83.88564  32.52566  20.10523  1.000 42.96858  ?  111 VAL C CB  1 
ATOM   855  C CG1 . VAL A 1 111 ? 84.93763  33.27401  20.90807  1.000 46.88805  ?  111 VAL C CG1 1 
ATOM   856  C CG2 . VAL A 1 111 ? 84.48213  31.95689  18.82768  1.000 48.99986  ?  111 VAL C CG2 1 
ATOM   857  N N   . ASP A 1 112 ? 82.81990  31.68453  23.32063  1.000 45.62194  ?  112 ASP C N   1 
ATOM   858  C CA  . ASP A 1 112 ? 82.08332  32.10269  24.50358  1.000 44.98174  ?  112 ASP C CA  1 
ATOM   859  C C   . ASP A 1 112 ? 82.94375  33.03641  25.34735  1.000 47.65437  ?  112 ASP C C   1 
ATOM   860  O O   . ASP A 1 112 ? 84.13126  33.23672  25.08049  1.000 61.42647  ?  112 ASP C O   1 
ATOM   861  C CB  . ASP A 1 112 ? 81.63816  30.88789  25.33010  1.000 43.50467  ?  112 ASP C CB  1 
ATOM   862  C CG  . ASP A 1 112 ? 80.41606  31.17560  26.18434  1.000 68.49565  ?  112 ASP C CG  1 
ATOM   863  O OD1 . ASP A 1 112 ? 80.17478  32.35827  26.50624  1.000 75.47537  ?  112 ASP C OD1 1 
ATOM   864  O OD2 . ASP A 1 112 ? 79.69603  30.21698  26.53509  1.000 68.58192  -1 112 ASP C OD2 1 
ATOM   865  N N   . ASN A 1 113 ? 82.31631  33.61213  26.37666  1.000 59.90665  ?  113 ASN C N   1 
ATOM   866  C CA  . ASN A 1 113 ? 82.97278  34.53557  27.30615  1.000 42.31997  ?  113 ASN C CA  1 
ATOM   867  C C   . ASN A 1 113 ? 83.56492  35.73578  26.56579  1.000 46.02210  ?  113 ASN C C   1 
ATOM   868  O O   . ASN A 1 113 ? 84.72226  36.11187  26.76317  1.000 51.26078  ?  113 ASN C O   1 
ATOM   869  C CB  . ASN A 1 113 ? 84.04055  33.81631  28.13530  1.000 45.93589  ?  113 ASN C CB  1 
ATOM   870  C CG  . ASN A 1 113 ? 84.46228  34.60827  29.35879  1.000 48.68724  ?  113 ASN C CG  1 
ATOM   871  O OD1 . ASN A 1 113 ? 83.65700  35.31574  29.96211  1.000 61.62052  ?  113 ASN C OD1 1 
ATOM   872  N ND2 . ASN A 1 113 ? 85.73225  34.49496  29.72836  1.000 71.34338  ?  113 ASN C ND2 1 
ATOM   873  N N   . ILE A 1 114 ? 82.75270  36.34241  25.70641  1.000 51.68721  ?  114 ILE C N   1 
ATOM   874  C CA  . ILE A 1 114 ? 83.16687  37.47976  24.89308  1.000 43.40018  ?  114 ILE C CA  1 
ATOM   875  C C   . ILE A 1 114 ? 82.69740  38.75170  25.58499  1.000 42.67711  ?  114 ILE C C   1 
ATOM   876  O O   . ILE A 1 114 ? 81.49234  39.00412  25.69029  1.000 49.88853  ?  114 ILE C O   1 
ATOM   877  C CB  . ILE A 1 114 ? 82.60562  37.39508  23.46782  1.000 46.93177  ?  114 ILE C CB  1 
ATOM   878  C CG1 . ILE A 1 114 ? 83.04354  36.09851  22.78670  1.000 50.51464  ?  114 ILE C CG1 1 
ATOM   879  C CG2 . ILE A 1 114 ? 83.04278  38.60399  22.65379  1.000 40.10295  ?  114 ILE C CG2 1 
ATOM   880  C CD1 . ILE A 1 114 ? 82.41989  35.89925  21.42274  1.000 38.55853  ?  114 ILE C CD1 1 
ATOM   881  N N   . PHE A 1 115 ? 83.64468  39.55683  26.05715  1.000 55.80546  ?  115 PHE C N   1 
ATOM   882  C CA  . PHE A 1 115 ? 83.32085  40.89023  26.54616  1.000 51.68926  ?  115 PHE C CA  1 
ATOM   883  C C   . PHE A 1 115 ? 84.55009  41.78770  26.47463  1.000 62.33192  ?  115 PHE C C   1 
ATOM   884  O O   . PHE A 1 115 ? 85.62908  41.40323  26.94482  1.000 57.84891  ?  115 PHE C O   1 
ATOM   885  C CB  . PHE A 1 115 ? 82.78202  40.85048  27.97579  1.000 43.01276  ?  115 PHE C CB  1 
ATOM   886  C CG  . PHE A 1 115 ? 82.26744  42.17649  28.45281  1.000 61.09943  ?  115 PHE C CG  1 
ATOM   887  C CD1 . PHE A 1 115 ? 80.99302  42.60090  28.11268  1.000 63.25576  ?  115 PHE C CD1 1 
ATOM   888  C CD2 . PHE A 1 115 ? 83.06313  43.00890  29.22086  1.000 50.96178  ?  115 PHE C CD2 1 
ATOM   889  C CE1 . PHE A 1 115 ? 80.51763  43.82590  28.53948  1.000 49.70830  ?  115 PHE C CE1 1 
ATOM   890  C CE2 . PHE A 1 115 ? 82.59350  44.23337  29.65093  1.000 44.08328  ?  115 PHE C CE2 1 
ATOM   891  C CZ  . PHE A 1 115 ? 81.31938  44.64337  29.30946  1.000 52.25406  ?  115 PHE C CZ  1 
ATOM   892  N N   . PRO A 1 116 ? 84.43091  42.99163  25.89851  1.000 47.40291  ?  116 PRO C N   1 
ATOM   893  C CA  . PRO A 1 116 ? 83.22884  43.58954  25.29622  1.000 49.47371  ?  116 PRO C CA  1 
ATOM   894  C C   . PRO A 1 116 ? 82.87002  42.92698  23.96807  1.000 53.58754  ?  116 PRO C C   1 
ATOM   895  O O   . PRO A 1 116 ? 83.70846  42.26278  23.36472  1.000 58.53694  ?  116 PRO C O   1 
ATOM   896  C CB  . PRO A 1 116 ? 83.63307  45.06076  25.12604  1.000 40.77612  ?  116 PRO C CB  1 
ATOM   897  C CG  . PRO A 1 116 ? 85.11062  45.00620  24.90853  1.000 41.88235  ?  116 PRO C CG  1 
ATOM   898  C CD  . PRO A 1 116 ? 85.59121  43.89538  25.80772  1.000 50.20098  ?  116 PRO C CD  1 
ATOM   899  N N   . PRO A 1 117 ? 81.62914  43.07581  23.49186  1.000 47.35986  ?  117 PRO C N   1 
ATOM   900  C CA  . PRO A 1 117 ? 81.22954  42.38883  22.25500  1.000 46.67738  ?  117 PRO C CA  1 
ATOM   901  C C   . PRO A 1 117 ? 81.86973  42.97129  21.00260  1.000 39.90943  ?  117 PRO C C   1 
ATOM   902  O O   . PRO A 1 117 ? 81.18041  43.52977  20.14339  1.000 47.39259  ?  117 PRO C O   1 
ATOM   903  C CB  . PRO A 1 117 ? 79.70465  42.55958  22.23890  1.000 47.49299  ?  117 PRO C CB  1 
ATOM   904  C CG  . PRO A 1 117 ? 79.45422  43.78273  23.05033  1.000 45.02620  ?  117 PRO C CG  1 
ATOM   905  C CD  . PRO A 1 117 ? 80.50069  43.78126  24.12433  1.000 44.32803  ?  117 PRO C CD  1 
ATOM   906  N N   . VAL A 1 118 ? 83.19231  42.84856  20.89526  1.000 38.28257  ?  118 VAL C N   1 
ATOM   907  C CA  . VAL A 1 118 ? 83.93623  43.18777  19.68491  1.000 45.98035  ?  118 VAL C CA  1 
ATOM   908  C C   . VAL A 1 118 ? 84.95776  42.08166  19.46265  1.000 39.14408  ?  118 VAL C C   1 
ATOM   909  O O   . VAL A 1 118 ? 85.80347  41.83706  20.32981  1.000 53.95849  ?  118 VAL C O   1 
ATOM   910  C CB  . VAL A 1 118 ? 84.64235  44.55261  19.78171  1.000 39.05357  ?  118 VAL C CB  1 
ATOM   911  C CG1 . VAL A 1 118 ? 85.40949  44.83894  18.50155  1.000 41.13228  ?  118 VAL C CG1 1 
ATOM   912  C CG2 . VAL A 1 118 ? 83.64310  45.66449  20.06357  1.000 54.36569  ?  118 VAL C CG2 1 
ATOM   913  N N   . ILE A 1 119 ? 84.88680  41.41014  18.31072  1.000 42.46374  ?  119 ILE C N   1 
ATOM   914  C CA  . ILE A 1 119 ? 85.71504  40.23670  18.05837  1.000 41.45900  ?  119 ILE C CA  1 
ATOM   915  C C   . ILE A 1 119 ? 85.99196  40.11372  16.56485  1.000 48.81704  ?  119 ILE C C   1 
ATOM   916  O O   . ILE A 1 119 ? 85.28208  40.67519  15.72745  1.000 61.59594  ?  119 ILE C O   1 
ATOM   917  C CB  . ILE A 1 119 ? 85.04902  38.95182  18.60929  1.000 45.96501  ?  119 ILE C CB  1 
ATOM   918  C CG1 . ILE A 1 119 ? 86.10803  37.90900  18.97216  1.000 44.62354  ?  119 ILE C CG1 1 
ATOM   919  C CG2 . ILE A 1 119 ? 84.04474  38.39095  17.61035  1.000 40.02611  ?  119 ILE C CG2 1 
ATOM   920  C CD1 . ILE A 1 119 ? 85.56206  36.74452  19.75847  1.000 40.96391  ?  119 ILE C CD1 1 
ATOM   921  N N   . ASN A 1 120 ? 87.04688  39.36352  16.23796  1.000 57.39549  ?  120 ASN C N   1 
ATOM   922  C CA  . ASN A 1 120 ? 87.53252  39.16308  14.87013  1.000 55.22346  ?  120 ASN C CA  1 
ATOM   923  C C   . ASN A 1 120 ? 87.75281  37.66115  14.69992  1.000 42.36379  ?  120 ASN C C   1 
ATOM   924  O O   . ASN A 1 120 ? 88.81977  37.13940  15.03333  1.000 66.40499  ?  120 ASN C O   1 
ATOM   925  C CB  . ASN A 1 120 ? 88.81043  39.98093  14.63407  1.000 60.88971  ?  120 ASN C CB  1 
ATOM   926  C CG  . ASN A 1 120 ? 89.48307  39.69077  13.29408  1.000 95.16530  ?  120 ASN C CG  1 
ATOM   927  O OD1 . ASN A 1 120 ? 88.86639  39.17126  12.36269  1.000 85.18257  ?  120 ASN C OD1 1 
ATOM   928  N ND2 . ASN A 1 120 ? 90.77493  40.04725  13.21040  1.000 111.62335 ?  120 ASN C ND2 1 
ATOM   929  N N   . ILE A 1 121 ? 86.73475  36.96722  14.19357  1.000 43.69949  ?  121 ILE C N   1 
ATOM   930  C CA  . ILE A 1 121 ? 86.76517  35.51780  14.02159  1.000 38.18552  ?  121 ILE C CA  1 
ATOM   931  C C   . ILE A 1 121 ? 87.01350  35.20300  12.55332  1.000 42.73198  ?  121 ILE C C   1 
ATOM   932  O O   . ILE A 1 121 ? 86.35653  35.76731  11.66920  1.000 71.04193  ?  121 ILE C O   1 
ATOM   933  C CB  . ILE A 1 121 ? 85.45592  34.87224  14.50703  1.000 53.01738  ?  121 ILE C CB  1 
ATOM   934  C CG1 . ILE A 1 121 ? 85.20745  35.20721  15.97844  1.000 51.08946  ?  121 ILE C CG1 1 
ATOM   935  C CG2 . ILE A 1 121 ? 85.49225  33.36488  14.30229  1.000 47.06654  ?  121 ILE C CG2 1 
ATOM   936  C CD1 . ILE A 1 121 ? 83.88949  34.68743  16.50333  1.000 35.49304  ?  121 ILE C CD1 1 
ATOM   937  N N   . THR A 1 122 ? 87.95806  34.30034  12.29175  1.000 51.07678  ?  122 THR C N   1 
ATOM   938  C CA  . THR A 1 122 ? 88.31426  33.91212  10.93497  1.000 54.63163  ?  122 THR C CA  1 
ATOM   939  C C   . THR A 1 122 ? 88.65879  32.43027  10.90047  1.000 52.94918  ?  122 THR C C   1 
ATOM   940  O O   . THR A 1 122 ? 89.09797  31.85467  11.89964  1.000 48.20641  ?  122 THR C O   1 
ATOM   941  C CB  . THR A 1 122 ? 89.49865  34.73104  10.40016  1.000 50.60644  ?  122 THR C CB  1 
ATOM   942  O OG1 . THR A 1 122 ? 90.46095  34.92010  11.44475  1.000 65.75586  ?  122 THR C OG1 1 
ATOM   943  C CG2 . THR A 1 122 ? 89.03167  36.08662  9.88791   1.000 67.98874  ?  122 THR C CG2 1 
ATOM   944  N N   . TRP A 1 123 ? 88.45655  31.82071  9.73677   1.000 55.24733  ?  123 TRP C N   1 
ATOM   945  C CA  . TRP A 1 123 ? 88.75722  30.41458  9.51585   1.000 48.74527  ?  123 TRP C CA  1 
ATOM   946  C C   . TRP A 1 123 ? 90.04096  30.25776  8.70910   1.000 55.55351  ?  123 TRP C C   1 
ATOM   947  O O   . TRP A 1 123 ? 90.46339  31.15916  7.98072   1.000 66.91697  ?  123 TRP C O   1 
ATOM   948  C CB  . TRP A 1 123 ? 87.60525  29.71696  8.78817   1.000 52.26831  ?  123 TRP C CB  1 
ATOM   949  C CG  . TRP A 1 123 ? 86.36239  29.56904  9.60527   1.000 52.38324  ?  123 TRP C CG  1 
ATOM   950  C CD1 . TRP A 1 123 ? 85.32885  30.45395  9.69150   1.000 58.80474  ?  123 TRP C CD1 1 
ATOM   951  C CD2 . TRP A 1 123 ? 86.01410  28.46155  10.44489  1.000 61.80967  ?  123 TRP C CD2 1 
ATOM   952  N NE1 . TRP A 1 123 ? 84.35985  29.96921  10.53601  1.000 61.70568  ?  123 TRP C NE1 1 
ATOM   953  C CE2 . TRP A 1 123 ? 84.75654  28.74738  11.01178  1.000 50.69642  ?  123 TRP C CE2 1 
ATOM   954  C CE3 . TRP A 1 123 ? 86.64483  27.25774  10.77460  1.000 49.83268  ?  123 TRP C CE3 1 
ATOM   955  C CZ2 . TRP A 1 123 ? 84.11678  27.87391  11.88818  1.000 56.27980  ?  123 TRP C CZ2 1 
ATOM   956  C CZ3 . TRP A 1 123 ? 86.00801  26.39200  11.64602  1.000 56.93185  ?  123 TRP C CZ3 1 
ATOM   957  C CH2 . TRP A 1 123 ? 84.75738  26.70449  12.19276  1.000 54.48766  ?  123 TRP C CH2 1 
ATOM   958  N N   . LEU A 1 124 ? 90.65669  29.08510  8.84621   1.000 56.17217  ?  124 LEU C N   1 
ATOM   959  C CA  . LEU A 1 124 ? 91.86815  28.74483  8.11274   1.000 60.39701  ?  124 LEU C CA  1 
ATOM   960  C C   . LEU A 1 124 ? 91.76738  27.30610  7.63207   1.000 62.40632  ?  124 LEU C C   1 
ATOM   961  O O   . LEU A 1 124 ? 91.43941  26.41112  8.41634   1.000 62.13152  ?  124 LEU C O   1 
ATOM   962  C CB  . LEU A 1 124 ? 93.11893  28.91934  8.98474   1.000 71.45638  ?  124 LEU C CB  1 
ATOM   963  C CG  . LEU A 1 124 ? 93.41879  30.30427  9.56344   1.000 64.79569  ?  124 LEU C CG  1 
ATOM   964  C CD1 . LEU A 1 124 ? 94.59788  30.23481  10.52002  1.000 68.16864  ?  124 LEU C CD1 1 
ATOM   965  C CD2 . LEU A 1 124 ? 93.69180  31.30770  8.45765   1.000 58.15426  ?  124 LEU C CD2 1 
ATOM   966  N N   . ARG A 1 125 ? 92.04045  27.08773  6.34770   1.000 65.67916  ?  125 ARG C N   1 
ATOM   967  C CA  . ARG A 1 125 ? 92.13022  25.74910  5.77263   1.000 67.00185  ?  125 ARG C CA  1 
ATOM   968  C C   . ARG A 1 125 ? 93.58717  25.49732  5.40642   1.000 68.20644  ?  125 ARG C C   1 
ATOM   969  O O   . ARG A 1 125 ? 94.11514  26.12325  4.48032   1.000 64.14094  ?  125 ARG C O   1 
ATOM   970  C CB  . ARG A 1 125 ? 91.22389  25.59779  4.55194   1.000 81.92545  ?  125 ARG C CB  1 
ATOM   971  C CG  . ARG A 1 125 ? 91.41834  24.27557  3.81748   1.000 69.80098  ?  125 ARG C CG  1 
ATOM   972  C CD  . ARG A 1 125 ? 90.57434  24.17858  2.55398   1.000 69.69138  ?  125 ARG C CD  1 
ATOM   973  N NE  . ARG A 1 125 ? 89.15881  23.97972  2.84214   1.000 91.21115  ?  125 ARG C NE  1 
ATOM   974  C CZ  . ARG A 1 125 ? 88.23257  24.92349  2.74325   1.000 93.18405  ?  125 ARG C CZ  1 
ATOM   975  N NH1 . ARG A 1 125 ? 88.53585  26.15207  2.35713   1.000 98.51279  ?  125 ARG C NH1 1 
ATOM   976  N NH2 . ARG A 1 125 ? 86.96923  24.62573  3.03415   1.000 61.72007  ?  125 ARG C NH2 1 
ATOM   977  N N   . ASN A 1 126 ? 94.23021  24.58369  6.13698   1.000 61.68458  ?  126 ASN C N   1 
ATOM   978  C CA  . ASN A 1 126 ? 95.64058  24.24981  5.93273   1.000 65.49209  ?  126 ASN C CA  1 
ATOM   979  C C   . ASN A 1 126 ? 96.51889  25.49612  6.03819   1.000 67.29058  ?  126 ASN C C   1 
ATOM   980  O O   . ASN A 1 126 ? 97.31169  25.80552  5.14610   1.000 71.06827  ?  126 ASN C O   1 
ATOM   981  C CB  . ASN A 1 126 ? 95.85047  23.53728  4.59414   1.000 68.60880  ?  126 ASN C CB  1 
ATOM   982  C CG  . ASN A 1 126 ? 95.07774  22.23734  4.50013   1.000 67.62396  ?  126 ASN C CG  1 
ATOM   983  O OD1 . ASN A 1 126 ? 94.88669  21.54224  5.49798   1.000 66.03352  ?  126 ASN C OD1 1 
ATOM   984  N ND2 . ASN A 1 126 ? 94.62610  21.90267  3.29699   1.000 85.21130  ?  126 ASN C ND2 1 
ATOM   985  N N   . SER A 1 127 ? 96.35469  26.22317  7.14450   1.000 71.68380  ?  127 SER C N   1 
ATOM   986  C CA  . SER A 1 127 ? 97.11447  27.43499  7.45023   1.000 69.42044  ?  127 SER C CA  1 
ATOM   987  C C   . SER A 1 127 ? 96.92461  28.52810  6.40119   1.000 76.67479  ?  127 SER C C   1 
ATOM   988  O O   . SER A 1 127 ? 97.71263  29.47756  6.34061   1.000 83.03503  ?  127 SER C O   1 
ATOM   989  C CB  . SER A 1 127 ? 98.60579  27.12469  7.62754   1.000 94.98998  ?  127 SER C CB  1 
ATOM   990  O OG  . SER A 1 127 ? 98.80433  26.14169  8.62897   1.000 83.67626  ?  127 SER C OG  1 
ATOM   991  N N   . LYS A 1 128 ? 95.88940  28.41660  5.57296   1.000 71.44821  ?  128 LYS C N   1 
ATOM   992  C CA  . LYS A 1 128 ? 95.56510  29.41681  4.56683   1.000 73.40056  ?  128 LYS C CA  1 
ATOM   993  C C   . LYS A 1 128 ? 94.15365  29.93103  4.80958   1.000 77.32511  ?  128 LYS C C   1 
ATOM   994  O O   . LYS A 1 128 ? 93.24224  29.15222  5.10690   1.000 72.26568  ?  128 LYS C O   1 
ATOM   995  C CB  . LYS A 1 128 ? 95.68343  28.84240  3.15089   1.000 71.61770  ?  128 LYS C CB  1 
ATOM   996  N N   . SER A 1 129 ? 93.97818  31.24323  4.68041   1.000 85.98750  ?  129 SER C N   1 
ATOM   997  C CA  . SER A 1 129 ? 92.70041  31.86174  5.00449   1.000 83.35609  ?  129 SER C CA  1 
ATOM   998  C C   . SER A 1 129 ? 91.63781  31.49483  3.97657   1.000 84.80139  ?  129 SER C C   1 
ATOM   999  O O   . SER A 1 129 ? 91.92168  31.35554  2.78362   1.000 91.97740  ?  129 SER C O   1 
ATOM   1000 C CB  . SER A 1 129 ? 92.84956  33.38077  5.08062   1.000 78.38615  ?  129 SER C CB  1 
ATOM   1001 O OG  . SER A 1 129 ? 93.19799  33.92219  3.81865   1.000 116.42006 ?  129 SER C OG  1 
ATOM   1002 N N   . VAL A 1 130 ? 90.40508  31.33582  4.45200   1.000 83.22147  ?  130 VAL C N   1 
ATOM   1003 C CA  . VAL A 1 130 ? 89.24737  31.08554  3.60189   1.000 97.77186  ?  130 VAL C CA  1 
ATOM   1004 C C   . VAL A 1 130 ? 88.14709  32.05086  4.02214   1.000 114.25824 ?  130 VAL C C   1 
ATOM   1005 O O   . VAL A 1 130 ? 87.71619  32.04200  5.18185   1.000 100.93834 ?  130 VAL C O   1 
ATOM   1006 C CB  . VAL A 1 130 ? 88.76556  29.62567  3.68675   1.000 87.24462  ?  130 VAL C CB  1 
ATOM   1007 C CG1 . VAL A 1 130 ? 88.78083  29.12890  5.12836   1.000 66.87297  ?  130 VAL C CG1 1 
ATOM   1008 C CG2 . VAL A 1 130 ? 87.37590  29.48728  3.08114   1.000 97.17654  ?  130 VAL C CG2 1 
ATOM   1009 N N   . ALA A 1 131 ? 87.70521  32.89392  3.08661   1.000 120.78858 ?  131 ALA C N   1 
ATOM   1010 C CA  . ALA A 1 131 ? 86.69756  33.90409  3.37249   1.000 119.70269 ?  131 ALA C CA  1 
ATOM   1011 C C   . ALA A 1 131 ? 85.35902  33.64591  2.69897   1.000 122.74958 ?  131 ALA C C   1 
ATOM   1012 O O   . ALA A 1 131 ? 84.35927  34.24749  3.10334   1.000 118.94982 ?  131 ALA C O   1 
ATOM   1013 C CB  . ALA A 1 131 ? 87.20138  35.29370  2.95450   1.000 101.04554 ?  131 ALA C CB  1 
ATOM   1014 N N   A ASP A 1 132 ? 85.31167  32.77779  1.69264   0.500 115.84779 ?  132 ASP C N   1 
ATOM   1015 N N   B ASP A 1 132 ? 85.31304  32.77629  1.69412   0.500 115.84838 ?  132 ASP C N   1 
ATOM   1016 C CA  A ASP A 1 132 ? 84.07295  32.47707  0.99048   0.500 111.16133 ?  132 ASP C CA  1 
ATOM   1017 C CA  B ASP A 1 132 ? 84.07759  32.46933  0.98913   0.500 111.16922 ?  132 ASP C CA  1 
ATOM   1018 C C   A ASP A 1 132 ? 83.31720  31.36295  1.70202   0.500 109.83118 ?  132 ASP C C   1 
ATOM   1019 C C   B ASP A 1 132 ? 83.31744  31.36119  1.70597   0.500 109.83245 ?  132 ASP C C   1 
ATOM   1020 O O   A ASP A 1 132 ? 83.91854  30.41468  2.21484   0.500 104.80063 ?  132 ASP C O   1 
ATOM   1021 O O   B ASP A 1 132 ? 83.91595  30.41541  2.22668   0.500 104.79693 ?  132 ASP C O   1 
ATOM   1022 C CB  A ASP A 1 132 ? 84.35757  32.07649  -0.45791  0.500 114.04475 ?  132 ASP C CB  1 
ATOM   1023 C CB  B ASP A 1 132 ? 84.37340  32.05631  -0.45350  0.500 114.05739 ?  132 ASP C CB  1 
ATOM   1024 C CG  A ASP A 1 132 ? 84.96639  33.20586  -1.26526  0.500 113.42396 ?  132 ASP C CG  1 
ATOM   1025 C CG  B ASP A 1 132 ? 85.48959  31.03431  -0.54893  0.500 111.54403 ?  132 ASP C CG  1 
ATOM   1026 O OD1 A ASP A 1 132 ? 85.10500  34.32065  -0.71915  0.500 104.84463 ?  132 ASP C OD1 1 
ATOM   1027 O OD1 B ASP A 1 132 ? 86.42088  31.09124  0.28168   0.500 97.58422  ?  132 ASP C OD1 1 
ATOM   1028 O OD2 A ASP A 1 132 ? 85.30652  32.97907  -2.44555  0.500 107.66780 -1 132 ASP C OD2 1 
ATOM   1029 O OD2 B ASP A 1 132 ? 85.43681  30.17501  -1.45371  0.500 116.92116 -1 132 ASP C OD2 1 
ATOM   1030 N N   . GLY A 1 133 ? 81.99456  31.48602  1.72916   1.000 106.89683 ?  133 GLY C N   1 
ATOM   1031 C CA  . GLY A 1 133 ? 81.15845  30.49188  2.38017   1.000 107.68860 ?  133 GLY C CA  1 
ATOM   1032 C C   . GLY A 1 133 ? 81.26813  30.48212  3.88938   1.000 97.82583  ?  133 GLY C C   1 
ATOM   1033 O O   . GLY A 1 133 ? 81.32474  29.40403  4.49562   1.000 78.95139  ?  133 GLY C O   1 
ATOM   1034 N N   . VAL A 1 134 ? 81.30348  31.65819  4.51299   1.000 85.26490  ?  134 VAL C N   1 
ATOM   1035 C CA  . VAL A 1 134 ? 81.42341  31.78798  5.96011   1.000 79.28972  ?  134 VAL C CA  1 
ATOM   1036 C C   . VAL A 1 134 ? 80.29096  32.67266  6.45973   1.000 62.33068  ?  134 VAL C C   1 
ATOM   1037 O O   . VAL A 1 134 ? 80.09976  33.78572  5.95712   1.000 79.51867  ?  134 VAL C O   1 
ATOM   1038 C CB  . VAL A 1 134 ? 82.78840  32.37239  6.37408   1.000 61.87948  ?  134 VAL C CB  1 
ATOM   1039 C CG1 . VAL A 1 134 ? 82.86693  32.52389  7.88661   1.000 48.12905  ?  134 VAL C CG1 1 
ATOM   1040 C CG2 . VAL A 1 134 ? 83.92037  31.49445  5.86451   1.000 82.59655  ?  134 VAL C CG2 1 
ATOM   1041 N N   . TYR A 1 135 ? 79.54322  32.17781  7.44378   1.000 61.86920  ?  135 TYR C N   1 
ATOM   1042 C CA  . TYR A 1 135 ? 78.45506  32.91928  8.06380   1.000 47.91330  ?  135 TYR C CA  1 
ATOM   1043 C C   . TYR A 1 135 ? 78.76018  33.13331  9.54016   1.000 42.66355  ?  135 TYR C C   1 
ATOM   1044 O O   . TYR A 1 135 ? 79.35096  32.26875  10.19567  1.000 50.32450  ?  135 TYR C O   1 
ATOM   1045 C CB  . TYR A 1 135 ? 77.11584  32.18522  7.90143   1.000 55.04349  ?  135 TYR C CB  1 
ATOM   1046 C CG  . TYR A 1 135 ? 75.96559  32.84124  8.63282   1.000 72.38076  ?  135 TYR C CG  1 
ATOM   1047 C CD1 . TYR A 1 135 ? 75.31981  33.95016  8.10111   1.000 67.33949  ?  135 TYR C CD1 1 
ATOM   1048 C CD2 . TYR A 1 135 ? 75.52595  32.35148  9.85579   1.000 76.71836  ?  135 TYR C CD2 1 
ATOM   1049 C CE1 . TYR A 1 135 ? 74.26937  34.55329  8.76905   1.000 85.95698  ?  135 TYR C CE1 1 
ATOM   1050 C CE2 . TYR A 1 135 ? 74.47779  32.94740  10.52998  1.000 66.31707  ?  135 TYR C CE2 1 
ATOM   1051 C CZ  . TYR A 1 135 ? 73.85292  34.04736  9.98245   1.000 77.78879  ?  135 TYR C CZ  1 
ATOM   1052 O OH  . TYR A 1 135 ? 72.80788  34.64389  10.65010  1.000 74.19650  ?  135 TYR C OH  1 
ATOM   1053 N N   . GLU A 1 136 ? 78.35120  34.28844  10.05938  1.000 56.67659  ?  136 GLU C N   1 
ATOM   1054 C CA  . GLU A 1 136 ? 78.60837  34.65624  11.44479  1.000 53.55502  ?  136 GLU C CA  1 
ATOM   1055 C C   . GLU A 1 136 ? 77.34252  35.24360  12.04813  1.000 59.92685  ?  136 GLU C C   1 
ATOM   1056 O O   . GLU A 1 136 ? 76.69515  36.09247  11.42877  1.000 64.08077  ?  136 GLU C O   1 
ATOM   1057 C CB  . GLU A 1 136 ? 79.76543  35.65822  11.53681  1.000 66.12812  ?  136 GLU C CB  1 
ATOM   1058 C CG  . GLU A 1 136 ? 80.04334  36.17594  12.93358  1.000 70.65065  ?  136 GLU C CG  1 
ATOM   1059 C CD  . GLU A 1 136 ? 81.24867  37.09696  12.97976  1.000 86.63205  ?  136 GLU C CD  1 
ATOM   1060 O OE1 . GLU A 1 136 ? 82.13220  36.96515  12.10653  1.000 87.25215  ?  136 GLU C OE1 1 
ATOM   1061 O OE2 . GLU A 1 136 ? 81.31170  37.95560  13.88480  1.000 90.41251  -1 136 GLU C OE2 1 
ATOM   1062 N N   . THR A 1 137 ? 76.99228  34.78998  13.24973  1.000 50.81400  ?  137 THR C N   1 
ATOM   1063 C CA  . THR A 1 137 ? 75.79038  35.25187  13.92357  1.000 54.15975  ?  137 THR C CA  1 
ATOM   1064 C C   . THR A 1 137 ? 76.07967  36.51958  14.72543  1.000 55.30912  ?  137 THR C C   1 
ATOM   1065 O O   . THR A 1 137 ? 77.20707  37.01721  14.77511  1.000 61.83479  ?  137 THR C O   1 
ATOM   1066 C CB  . THR A 1 137 ? 75.22799  34.16098  14.83484  1.000 55.02515  ?  137 THR C CB  1 
ATOM   1067 O OG1 . THR A 1 137 ? 76.14724  33.90533  15.90472  1.000 45.04426  ?  137 THR C OG1 1 
ATOM   1068 C CG2 . THR A 1 137 ? 74.99839  32.87998  14.05399  1.000 63.51292  ?  137 THR C CG2 1 
ATOM   1069 N N   . SER A 1 138 ? 75.04023  37.04852  15.36583  1.000 59.14366  ?  138 SER C N   1 
ATOM   1070 C CA  . SER A 1 138 ? 75.17902  38.21234  16.22477  1.000 41.92854  ?  138 SER C CA  1 
ATOM   1071 C C   . SER A 1 138 ? 75.68317  37.78652  17.60248  1.000 50.96981  ?  138 SER C C   1 
ATOM   1072 O O   . SER A 1 138 ? 75.86892  36.60034  17.88913  1.000 51.58811  ?  138 SER C O   1 
ATOM   1073 C CB  . SER A 1 138 ? 73.84880  38.95396  16.33089  1.000 40.97418  ?  138 SER C CB  1 
ATOM   1074 O OG  . SER A 1 138 ? 73.34157  39.27838  15.04910  1.000 53.71328  ?  138 SER C OG  1 
ATOM   1075 N N   . PHE A 1 139 ? 75.90875  38.76936  18.47134  1.000 40.14276  ?  139 PHE C N   1 
ATOM   1076 C CA  . PHE A 1 139 ? 76.35637  38.50236  19.83458  1.000 44.81881  ?  139 PHE C CA  1 
ATOM   1077 C C   . PHE A 1 139 ? 75.15716  38.09056  20.68038  1.000 42.25646  ?  139 PHE C C   1 
ATOM   1078 O O   . PHE A 1 139 ? 74.26904  38.90620  20.94849  1.000 53.48131  ?  139 PHE C O   1 
ATOM   1079 C CB  . PHE A 1 139 ? 77.03828  39.73090  20.43037  1.000 50.84720  ?  139 PHE C CB  1 
ATOM   1080 C CG  . PHE A 1 139 ? 78.35401  40.07483  19.79069  1.000 38.47770  ?  139 PHE C CG  1 
ATOM   1081 C CD1 . PHE A 1 139 ? 78.41020  40.94028  18.71121  1.000 47.63250  ?  139 PHE C CD1 1 
ATOM   1082 C CD2 . PHE A 1 139 ? 79.53668  39.54714  20.28149  1.000 48.15546  ?  139 PHE C CD2 1 
ATOM   1083 C CE1 . PHE A 1 139 ? 79.62005  41.26591  18.12633  1.000 32.83533  ?  139 PHE C CE1 1 
ATOM   1084 C CE2 . PHE A 1 139 ? 80.75000  39.86844  19.70127  1.000 46.64382  ?  139 PHE C CE2 1 
ATOM   1085 C CZ  . PHE A 1 139 ? 80.79142  40.73058  18.62332  1.000 38.91646  ?  139 PHE C CZ  1 
ATOM   1086 N N   . PHE A 1 140 ? 75.12496  36.82851  21.09954  1.000 40.06223  ?  140 PHE C N   1 
ATOM   1087 C CA  . PHE A 1 140 ? 74.10194  36.36743  22.02674  1.000 43.03992  ?  140 PHE C CA  1 
ATOM   1088 C C   . PHE A 1 140 ? 74.51100  36.69853  23.45607  1.000 43.67226  ?  140 PHE C C   1 
ATOM   1089 O O   . PHE A 1 140 ? 75.68279  36.58376  23.82379  1.000 59.58754  ?  140 PHE C O   1 
ATOM   1090 C CB  . PHE A 1 140 ? 73.87829  34.86235  21.88247  1.000 47.49477  ?  140 PHE C CB  1 
ATOM   1091 C CG  . PHE A 1 140 ? 73.30272  34.45331  20.55611  1.000 47.50931  ?  140 PHE C CG  1 
ATOM   1092 C CD1 . PHE A 1 140 ? 71.93242  34.44417  20.35399  1.000 55.89934  ?  140 PHE C CD1 1 
ATOM   1093 C CD2 . PHE A 1 140 ? 74.13043  34.06337  19.51661  1.000 54.01557  ?  140 PHE C CD2 1 
ATOM   1094 C CE1 . PHE A 1 140 ? 71.39864  34.06287  19.13732  1.000 48.17816  ?  140 PHE C CE1 1 
ATOM   1095 C CE2 . PHE A 1 140 ? 73.60227  33.68081  18.29689  1.000 64.18984  ?  140 PHE C CE2 1 
ATOM   1096 C CZ  . PHE A 1 140 ? 72.23463  33.68065  18.10771  1.000 45.20946  ?  140 PHE C CZ  1 
ATOM   1097 N N   A VAL A 1 141 ? 73.53783  37.12128  24.25390  0.500 51.54562  ?  141 VAL C N   1 
ATOM   1098 N N   B VAL A 1 141 ? 73.53559  37.09408  24.26880  0.500 48.00218  ?  141 VAL C N   1 
ATOM   1099 C CA  A VAL A 1 141 ? 73.79613  37.49932  25.63685  0.500 51.58667  ?  141 VAL C CA  1 
ATOM   1100 C CA  B VAL A 1 141 ? 73.78568  37.51940  25.64261  0.500 50.78116  ?  141 VAL C CA  1 
ATOM   1101 C C   A VAL A 1 141 ? 73.85463  36.25053  26.50492  0.500 53.34105  ?  141 VAL C C   1 
ATOM   1102 C C   B VAL A 1 141 ? 73.78186  36.30494  26.56146  0.500 53.87118  ?  141 VAL C C   1 
ATOM   1103 O O   A VAL A 1 141 ? 73.17556  35.24935  26.24863  0.500 61.76349  ?  141 VAL C O   1 
ATOM   1104 O O   B VAL A 1 141 ? 72.97705  35.38089  26.39351  0.500 62.03308  ?  141 VAL C O   1 
ATOM   1105 C CB  A VAL A 1 141 ? 72.72447  38.48640  26.14220  0.500 54.53382  ?  141 VAL C CB  1 
ATOM   1106 C CB  B VAL A 1 141 ? 72.73995  38.55942  26.08855  0.500 55.90406  ?  141 VAL C CB  1 
ATOM   1107 C CG1 A VAL A 1 141 ? 72.76332  39.77227  25.33301  0.500 60.05606  ?  141 VAL C CG1 1 
ATOM   1108 C CG1 B VAL A 1 141 ? 73.08047  39.10913  27.46711  0.500 49.30677  ?  141 VAL C CG1 1 
ATOM   1109 C CG2 A VAL A 1 141 ? 71.34157  37.85436  26.07686  0.500 50.65591  ?  141 VAL C CG2 1 
ATOM   1110 C CG2 B VAL A 1 141 ? 72.64497  39.68402  25.06977  0.500 60.21558  ?  141 VAL C CG2 1 
ATOM   1111 N N   . ASN A 1 142 ? 74.68480  36.30651  27.53855  1.000 50.52545  ?  142 ASN C N   1 
ATOM   1112 C CA  . ASN A 1 142 ? 74.78363  35.24918  28.53238  1.000 58.30061  ?  142 ASN C CA  1 
ATOM   1113 C C   . ASN A 1 142 ? 74.18898  35.72694  29.85226  1.000 57.13750  ?  142 ASN C C   1 
ATOM   1114 O O   . ASN A 1 142 ? 73.86491  36.90380  30.02902  1.000 68.69195  ?  142 ASN C O   1 
ATOM   1115 C CB  . ASN A 1 142 ? 76.24079  34.81353  28.72389  1.000 59.42073  ?  142 ASN C CB  1 
ATOM   1116 C CG  . ASN A 1 142 ? 76.82347  34.16325  27.48483  1.000 59.85685  ?  142 ASN C CG  1 
ATOM   1117 O OD1 . ASN A 1 142 ? 76.10774  33.53764  26.70356  1.000 68.12021  ?  142 ASN C OD1 1 
ATOM   1118 N ND2 . ASN A 1 142 ? 78.13094  34.30620  27.30032  1.000 60.84499  ?  142 ASN C ND2 1 
ATOM   1119 N N   . ARG A 1 143 ? 74.04633  34.78952  30.79156  1.000 57.33456  ?  143 ARG C N   1 
ATOM   1120 C CA  . ARG A 1 143 ? 73.44983  35.12699  32.07853  1.000 67.93710  ?  143 ARG C CA  1 
ATOM   1121 C C   . ARG A 1 143 ? 74.37679  35.96373  32.95003  1.000 68.42454  ?  143 ARG C C   1 
ATOM   1122 O O   . ARG A 1 143 ? 73.89318  36.68504  33.82896  1.000 79.18275  ?  143 ARG C O   1 
ATOM   1123 C CB  . ARG A 1 143 ? 73.02812  33.85420  32.81396  1.000 73.10546  ?  143 ARG C CB  1 
ATOM   1124 C CG  . ARG A 1 143 ? 71.68361  33.31056  32.35302  1.000 92.25905  ?  143 ARG C CG  1 
ATOM   1125 C CD  . ARG A 1 143 ? 71.32312  32.01261  33.05516  1.000 116.50454 ?  143 ARG C CD  1 
ATOM   1126 N NE  . ARG A 1 143 ? 72.15871  30.90237  32.61462  1.000 128.02457 ?  143 ARG C NE  1 
ATOM   1127 C CZ  . ARG A 1 143 ? 72.00235  29.64595  33.00830  1.000 133.88607 ?  143 ARG C CZ  1 
ATOM   1128 N NH1 . ARG A 1 143 ? 71.04777  29.30139  33.85715  1.000 130.01619 ?  143 ARG C NH1 1 
ATOM   1129 N NH2 . ARG A 1 143 ? 72.82342  28.71147  32.53744  1.000 137.68549 ?  143 ARG C NH2 1 
ATOM   1130 N N   . ASP A 1 144 ? 75.68876  35.88959  32.72983  1.000 67.56789  ?  144 ASP C N   1 
ATOM   1131 C CA  . ASP A 1 144 ? 76.63867  36.76186  33.40455  1.000 60.52141  ?  144 ASP C CA  1 
ATOM   1132 C C   . ASP A 1 144 ? 76.88269  38.05345  32.63342  1.000 64.17467  ?  144 ASP C C   1 
ATOM   1133 O O   . ASP A 1 144 ? 77.86384  38.75496  32.90767  1.000 75.02395  ?  144 ASP C O   1 
ATOM   1134 C CB  . ASP A 1 144 ? 77.96119  36.02821  33.64341  1.000 61.08803  ?  144 ASP C CB  1 
ATOM   1135 C CG  . ASP A 1 144 ? 78.70497  35.72638  32.35753  1.000 68.43923  ?  144 ASP C CG  1 
ATOM   1136 O OD1 . ASP A 1 144 ? 78.04630  35.53169  31.31492  1.000 80.09390  ?  144 ASP C OD1 1 
ATOM   1137 O OD2 . ASP A 1 144 ? 79.95287  35.68116  32.39143  1.000 76.19665  -1 144 ASP C OD2 1 
ATOM   1138 N N   . TYR A 1 145 ? 76.01838  38.36495  31.66629  1.000 72.59676  ?  145 TYR C N   1 
ATOM   1139 C CA  . TYR A 1 145 ? 76.06759  39.58984  30.86980  1.000 73.03496  ?  145 TYR C CA  1 
ATOM   1140 C C   . TYR A 1 145 ? 77.32820  39.68151  30.01716  1.000 65.03023  ?  145 TYR C C   1 
ATOM   1141 O O   . TYR A 1 145 ? 77.68253  40.76356  29.53709  1.000 69.98530  ?  145 TYR C O   1 
ATOM   1142 C CB  . TYR A 1 145 ? 75.91039  40.82988  31.75649  1.000 56.78668  ?  145 TYR C CB  1 
ATOM   1143 C CG  . TYR A 1 145 ? 74.63015  40.79492  32.56022  1.000 63.28768  ?  145 TYR C CG  1 
ATOM   1144 C CD1 . TYR A 1 145 ? 73.45121  40.32011  31.99726  1.000 53.46011  ?  145 TYR C CD1 1 
ATOM   1145 C CD2 . TYR A 1 145 ? 74.60339  41.20518  33.88547  1.000 68.63638  ?  145 TYR C CD2 1 
ATOM   1146 C CE1 . TYR A 1 145 ? 72.27886  40.27099  32.72585  1.000 51.71304  ?  145 TYR C CE1 1 
ATOM   1147 C CE2 . TYR A 1 145 ? 73.43383  41.15979  34.62323  1.000 72.88834  ?  145 TYR C CE2 1 
ATOM   1148 C CZ  . TYR A 1 145 ? 72.27506  40.69173  34.03781  1.000 60.49146  ?  145 TYR C CZ  1 
ATOM   1149 O OH  . TYR A 1 145 ? 71.10778  40.64395  34.76558  1.000 67.81067  ?  145 TYR C OH  1 
ATOM   1150 N N   . SER A 1 146 ? 78.01138  38.55866  29.81877  1.000 66.51020  ?  146 SER C N   1 
ATOM   1151 C CA  . SER A 1 146 ? 79.00792  38.43976  28.76859  1.000 58.52579  ?  146 SER C CA  1 
ATOM   1152 C C   . SER A 1 146 ? 78.29614  38.00949  27.48706  1.000 57.29683  ?  146 SER C C   1 
ATOM   1153 O O   . SER A 1 146 ? 77.06653  37.91706  27.43732  1.000 57.92840  ?  146 SER C O   1 
ATOM   1154 C CB  . SER A 1 146 ? 80.10766  37.46351  29.17857  1.000 59.45424  ?  146 SER C CB  1 
ATOM   1155 O OG  . SER A 1 146 ? 79.59122  36.15495  29.34124  1.000 66.80143  ?  146 SER C OG  1 
ATOM   1156 N N   . PHE A 1 147 ? 79.05703  37.73155  26.43450  1.000 51.61741  ?  147 PHE C N   1 
ATOM   1157 C CA  . PHE A 1 147 ? 78.47591  37.39767  25.14502  1.000 49.77034  ?  147 PHE C CA  1 
ATOM   1158 C C   . PHE A 1 147 ? 79.13666  36.15237  24.57307  1.000 57.26049  ?  147 PHE C C   1 
ATOM   1159 O O   . PHE A 1 147 ? 80.24512  35.77368  24.95998  1.000 58.95805  ?  147 PHE C O   1 
ATOM   1160 C CB  . PHE A 1 147 ? 78.60933  38.56081  24.15265  1.000 47.44204  ?  147 PHE C CB  1 
ATOM   1161 C CG  . PHE A 1 147 ? 77.88808  39.80701  24.57909  1.000 43.68105  ?  147 PHE C CG  1 
ATOM   1162 C CD1 . PHE A 1 147 ? 78.51603  40.74807  25.37827  1.000 60.54773  ?  147 PHE C CD1 1 
ATOM   1163 C CD2 . PHE A 1 147 ? 76.58298  40.03907  24.17879  1.000 42.05942  ?  147 PHE C CD2 1 
ATOM   1164 C CE1 . PHE A 1 147 ? 77.85530  41.89555  25.77188  1.000 62.94541  ?  147 PHE C CE1 1 
ATOM   1165 C CE2 . PHE A 1 147 ? 75.91764  41.18613  24.56815  1.000 49.40816  ?  147 PHE C CE2 1 
ATOM   1166 C CZ  . PHE A 1 147 ? 76.55452  42.11441  25.36484  1.000 62.03412  ?  147 PHE C CZ  1 
ATOM   1167 N N   . HIS A 1 148 ? 78.42663  35.51010  23.64755  1.000 48.17603  ?  148 HIS C N   1 
ATOM   1168 C CA  . HIS A 1 148 ? 78.98170  34.41601  22.86706  1.000 52.65803  ?  148 HIS C CA  1 
ATOM   1169 C C   . HIS A 1 148 ? 78.49948  34.54861  21.42977  1.000 46.32260  ?  148 HIS C C   1 
ATOM   1170 O O   . HIS A 1 148 ? 77.45702  35.14777  21.15412  1.000 44.48098  ?  148 HIS C O   1 
ATOM   1171 C CB  . HIS A 1 148 ? 78.61525  33.03909  23.45032  1.000 50.52505  ?  148 HIS C CB  1 
ATOM   1172 C CG  . HIS A 1 148 ? 77.18746  32.63881  23.23918  1.000 50.43839  ?  148 HIS C CG  1 
ATOM   1173 N ND1 . HIS A 1 148 ? 76.22663  32.76540  24.21919  1.000 64.68673  ?  148 HIS C ND1 1 
ATOM   1174 C CD2 . HIS A 1 148 ? 76.56345  32.08835  22.17054  1.000 48.86969  ?  148 HIS C CD2 1 
ATOM   1175 C CE1 . HIS A 1 148 ? 75.07017  32.32163  23.75979  1.000 43.23710  ?  148 HIS C CE1 1 
ATOM   1176 N NE2 . HIS A 1 148 ? 75.24676  31.90702  22.51822  1.000 41.93577  ?  148 HIS C NE2 1 
ATOM   1177 N N   . LYS A 1 149 ? 79.28297  33.98831  20.51141  1.000 38.71551  ?  149 LYS C N   1 
ATOM   1178 C CA  . LYS A 1 149 ? 79.02006  34.12046  19.08664  1.000 44.90197  ?  149 LYS C CA  1 
ATOM   1179 C C   . LYS A 1 149 ? 79.45266  32.84208  18.38446  1.000 45.69610  ?  149 LYS C C   1 
ATOM   1180 O O   . LYS A 1 149 ? 80.42947  32.20097  18.78089  1.000 60.48754  ?  149 LYS C O   1 
ATOM   1181 C CB  . LYS A 1 149 ? 79.75242  35.33444  18.49776  1.000 34.97020  ?  149 LYS C CB  1 
ATOM   1182 C CG  . LYS A 1 149 ? 79.61876  35.48668  16.99157  1.000 59.78305  ?  149 LYS C CG  1 
ATOM   1183 C CD  . LYS A 1 149 ? 80.67435  36.42656  16.43703  1.000 57.21768  ?  149 LYS C CD  1 
ATOM   1184 C CE  . LYS A 1 149 ? 80.36747  37.87084  16.77332  1.000 54.04966  ?  149 LYS C CE  1 
ATOM   1185 N NZ  . LYS A 1 149 ? 79.15489  38.36361  16.06345  1.000 56.05334  ?  149 LYS C NZ  1 
ATOM   1186 N N   . LEU A 1 150 ? 78.71435  32.47560  17.33958  1.000 39.27591  ?  150 LEU C N   1 
ATOM   1187 C CA  . LEU A 1 150 ? 78.99343  31.27972  16.55873  1.000 46.55675  ?  150 LEU C CA  1 
ATOM   1188 C C   . LEU A 1 150 ? 79.33489  31.66144  15.12537  1.000 47.74893  ?  150 LEU C C   1 
ATOM   1189 O O   . LEU A 1 150 ? 78.69865  32.54213  14.53746  1.000 49.44241  ?  150 LEU C O   1 
ATOM   1190 C CB  . LEU A 1 150 ? 77.80136  30.31301  16.56748  1.000 44.62829  ?  150 LEU C CB  1 
ATOM   1191 C CG  . LEU A 1 150 ? 77.45306  29.61335  17.88442  1.000 45.91062  ?  150 LEU C CG  1 
ATOM   1192 C CD1 . LEU A 1 150 ? 76.61743  30.50624  18.79214  1.000 49.17862  ?  150 LEU C CD1 1 
ATOM   1193 C CD2 . LEU A 1 150 ? 76.73857  28.29793  17.61480  1.000 55.83819  ?  150 LEU C CD2 1 
ATOM   1194 N N   . SER A 1 151 ? 80.34355  30.99437  14.57002  1.000 44.76393  ?  151 SER C N   1 
ATOM   1195 C CA  . SER A 1 151 ? 80.73884  31.16588  13.18096  1.000 50.74362  ?  151 SER C CA  1 
ATOM   1196 C C   . SER A 1 151 ? 80.63001  29.83035  12.45773  1.000 47.06657  ?  151 SER C C   1 
ATOM   1197 O O   . SER A 1 151 ? 80.86855  28.76923  13.04194  1.000 56.90302  ?  151 SER C O   1 
ATOM   1198 C CB  . SER A 1 151 ? 82.16735  31.71282  13.06733  1.000 46.82935  ?  151 SER C CB  1 
ATOM   1199 O OG  . SER A 1 151 ? 82.51446  31.95346  11.71446  1.000 48.88001  ?  151 SER C OG  1 
ATOM   1200 N N   . TYR A 1 152 ? 80.26786  29.88903  11.17929  1.000 48.08027  ?  152 TYR C N   1 
ATOM   1201 C CA  . TYR A 1 152 ? 79.99531  28.69714  10.39168  1.000 59.32327  ?  152 TYR C CA  1 
ATOM   1202 C C   . TYR A 1 152 ? 80.87377  28.66638  9.14886   1.000 68.64513  ?  152 TYR C C   1 
ATOM   1203 O O   . TYR A 1 152 ? 81.18614  29.70606  8.56037   1.000 63.00812  ?  152 TYR C O   1 
ATOM   1204 C CB  . TYR A 1 152 ? 78.51728  28.62968  9.98717   1.000 44.78555  ?  152 TYR C CB  1 
ATOM   1205 C CG  . TYR A 1 152 ? 77.57003  28.63574  11.16428  1.000 42.63911  ?  152 TYR C CG  1 
ATOM   1206 C CD1 . TYR A 1 152 ? 77.12022  29.82949  11.71120  1.000 41.39595  ?  152 TYR C CD1 1 
ATOM   1207 C CD2 . TYR A 1 152 ? 77.12979  27.44793  11.73246  1.000 53.77508  ?  152 TYR C CD2 1 
ATOM   1208 C CE1 . TYR A 1 152 ? 76.25802  29.84073  12.78872  1.000 48.79778  ?  152 TYR C CE1 1 
ATOM   1209 C CE2 . TYR A 1 152 ? 76.26563  27.44954  12.81096  1.000 63.85491  ?  152 TYR C CE2 1 
ATOM   1210 C CZ  . TYR A 1 152 ? 75.83350  28.64941  13.33459  1.000 48.60526  ?  152 TYR C CZ  1 
ATOM   1211 O OH  . TYR A 1 152 ? 74.97350  28.65906  14.40770  1.000 66.33244  ?  152 TYR C OH  1 
ATOM   1212 N N   . LEU A 1 153 ? 81.26531  27.45552  8.75453   1.000 63.28089  ?  153 LEU C N   1 
ATOM   1213 C CA  . LEU A 1 153 ? 82.10601  27.24148  7.57935   1.000 64.42772  ?  153 LEU C CA  1 
ATOM   1214 C C   . LEU A 1 153 ? 81.64298  25.96804  6.88678   1.000 63.69060  ?  153 LEU C C   1 
ATOM   1215 O O   . LEU A 1 153 ? 81.77277  24.87405  7.44530   1.000 67.04471  ?  153 LEU C O   1 
ATOM   1216 C CB  . LEU A 1 153 ? 83.58360  27.14293  7.96172   1.000 58.47251  ?  153 LEU C CB  1 
ATOM   1217 C CG  . LEU A 1 153 ? 84.53469  26.70645  6.84300   1.000 49.47035  ?  153 LEU C CG  1 
ATOM   1218 C CD1 . LEU A 1 153 ? 84.62646  27.77087  5.75949   1.000 58.01794  ?  153 LEU C CD1 1 
ATOM   1219 C CD2 . LEU A 1 153 ? 85.91252  26.37403  7.39462   1.000 54.63493  ?  153 LEU C CD2 1 
ATOM   1220 N N   . THR A 1 154 ? 81.10436  26.10775  5.67888   1.000 57.91667  ?  154 THR C N   1 
ATOM   1221 C CA  . THR A 1 154 ? 80.72446  24.95007  4.88323   1.000 69.34461  ?  154 THR C CA  1 
ATOM   1222 C C   . THR A 1 154 ? 81.95106  24.37243  4.18969   1.000 72.26351  ?  154 THR C C   1 
ATOM   1223 O O   . THR A 1 154 ? 82.76778  25.10698  3.62644   1.000 79.55337  ?  154 THR C O   1 
ATOM   1224 C CB  . THR A 1 154 ? 79.66479  25.32986  3.84904   1.000 67.25526  ?  154 THR C CB  1 
ATOM   1225 O OG1 . THR A 1 154 ? 80.18994  26.33190  2.96947   1.000 87.60221  ?  154 THR C OG1 1 
ATOM   1226 C CG2 . THR A 1 154 ? 78.42083  25.86968  4.53916   1.000 57.27093  ?  154 THR C CG2 1 
ATOM   1227 N N   . PHE A 1 155 ? 82.07862  23.04846  4.23440   1.000 66.52833  ?  155 PHE C N   1 
ATOM   1228 C CA  . PHE A 1 155 ? 83.26628  22.38560  3.71879   1.000 78.78950  ?  155 PHE C CA  1 
ATOM   1229 C C   . PHE A 1 155 ? 82.90219  20.98207  3.25659   1.000 76.52980  ?  155 PHE C C   1 
ATOM   1230 O O   . PHE A 1 155 ? 81.80876  20.47778  3.52455   1.000 70.92789  ?  155 PHE C O   1 
ATOM   1231 C CB  . PHE A 1 155 ? 84.37462  22.33281  4.77616   1.000 73.08099  ?  155 PHE C CB  1 
ATOM   1232 C CG  . PHE A 1 155 ? 84.10678  21.35525  5.88705   1.000 73.01853  ?  155 PHE C CG  1 
ATOM   1233 C CD1 . PHE A 1 155 ? 83.14385  21.62105  6.84762   1.000 69.19430  ?  155 PHE C CD1 1 
ATOM   1234 C CD2 . PHE A 1 155 ? 84.82324  20.17281  5.97405   1.000 64.37233  ?  155 PHE C CD2 1 
ATOM   1235 C CE1 . PHE A 1 155 ? 82.89639  20.72369  7.86991   1.000 60.70645  ?  155 PHE C CE1 1 
ATOM   1236 C CE2 . PHE A 1 155 ? 84.58140  19.27263  6.99499   1.000 69.04935  ?  155 PHE C CE2 1 
ATOM   1237 C CZ  . PHE A 1 155 ? 83.61650  19.54839  7.94357   1.000 66.71461  ?  155 PHE C CZ  1 
ATOM   1238 N N   . ILE A 1 156 ? 83.84034  20.35657  2.55562   1.000 65.10319  ?  156 ILE C N   1 
ATOM   1239 C CA  . ILE A 1 156 ? 83.73020  18.97096  2.11232   1.000 73.35130  ?  156 ILE C CA  1 
ATOM   1240 C C   . ILE A 1 156 ? 84.67829  18.13905  2.97058   1.000 70.18275  ?  156 ILE C C   1 
ATOM   1241 O O   . ILE A 1 156 ? 85.90544  18.26559  2.83755   1.000 78.29638  ?  156 ILE C O   1 
ATOM   1242 C CB  . ILE A 1 156 ? 84.05369  18.82474  0.61995   1.000 95.88475  ?  156 ILE C CB  1 
ATOM   1243 C CG1 . ILE A 1 156 ? 83.09020  19.66620  -0.21879  1.000 72.62597  ?  156 ILE C CG1 1 
ATOM   1244 C CG2 . ILE A 1 156 ? 83.99191  17.36230  0.20303   1.000 77.65051  ?  156 ILE C CG2 1 
ATOM   1245 C CD1 . ILE A 1 156 ? 81.63945  19.27155  -0.05895  1.000 86.24547  ?  156 ILE C CD1 1 
ATOM   1246 N N   . PRO A 1 157 ? 84.16970  17.28871  3.86273   1.000 65.23653  ?  157 PRO C N   1 
ATOM   1247 C CA  . PRO A 1 157 ? 85.05332  16.53230  4.76088   1.000 77.17023  ?  157 PRO C CA  1 
ATOM   1248 C C   . PRO A 1 157 ? 86.00744  15.60121  4.02967   1.000 76.26960  ?  157 PRO C C   1 
ATOM   1249 O O   . PRO A 1 157 ? 85.60903  14.53011  3.56264   1.000 86.05452  ?  157 PRO C O   1 
ATOM   1250 C CB  . PRO A 1 157 ? 84.06901  15.74354  5.63517   1.000 65.34479  ?  157 PRO C CB  1 
ATOM   1251 C CG  . PRO A 1 157 ? 82.78861  16.51309  5.55940   1.000 73.81001  ?  157 PRO C CG  1 
ATOM   1252 C CD  . PRO A 1 157 ? 82.74761  17.07672  4.17376   1.000 76.50882  ?  157 PRO C CD  1 
ATOM   1253 N N   . SER A 1 158 ? 87.26908  16.00408  3.92254   1.000 86.16176  ?  158 SER C N   1 
ATOM   1254 C CA  . SER A 1 158 ? 88.32060  15.15752  3.38382   1.000 89.65713  ?  158 SER C CA  1 
ATOM   1255 C C   . SER A 1 158 ? 89.22506  14.69171  4.51728   1.000 90.04205  ?  158 SER C C   1 
ATOM   1256 O O   . SER A 1 158 ? 89.30102  15.31617  5.57878   1.000 94.29538  ?  158 SER C O   1 
ATOM   1257 C CB  . SER A 1 158 ? 89.14119  15.89395  2.31642   1.000 90.09118  ?  158 SER C CB  1 
ATOM   1258 O OG  . SER A 1 158 ? 90.00202  16.85511  2.90057   1.000 92.27016  ?  158 SER C OG  1 
ATOM   1259 N N   . ASP A 1 159 ? 89.91380  13.57473  4.28000   1.000 99.49840  ?  159 ASP C N   1 
ATOM   1260 C CA  . ASP A 1 159 ? 90.78515  13.00726  5.30130   1.000 104.87591 ?  159 ASP C CA  1 
ATOM   1261 C C   . ASP A 1 159 ? 92.05176  13.82874  5.51750   1.000 103.25305 ?  159 ASP C C   1 
ATOM   1262 O O   . ASP A 1 159 ? 92.74230  13.62285  6.52194   1.000 93.31826  ?  159 ASP C O   1 
ATOM   1263 C CB  . ASP A 1 159 ? 91.15308  11.57009  4.92777   1.000 112.51434 ?  159 ASP C CB  1 
ATOM   1264 C CG  . ASP A 1 159 ? 91.57620  11.43362  3.47498   1.000 130.91155 ?  159 ASP C CG  1 
ATOM   1265 O OD1 . ASP A 1 159 ? 91.65652  12.46273  2.77254   1.000 123.52410 ?  159 ASP C OD1 1 
ATOM   1266 O OD2 . ASP A 1 159 ? 91.82393  10.29040  3.03363   1.000 133.70787 ?  159 ASP C OD2 1 
ATOM   1267 N N   . ASP A 1 160 ? 92.36381  14.76104  4.61697   1.000 105.50254 ?  160 ASP C N   1 
ATOM   1268 C CA  . ASP A 1 160 ? 93.63979  15.46547  4.63622   1.000 98.99539  ?  160 ASP C CA  1 
ATOM   1269 C C   . ASP A 1 160 ? 93.55474  16.85780  5.25219   1.000 95.02228  ?  160 ASP C C   1 
ATOM   1270 O O   . ASP A 1 160 ? 94.49938  17.29011  5.92168   1.000 95.64037  ?  160 ASP C O   1 
ATOM   1271 C CB  . ASP A 1 160 ? 94.19710  15.56853  3.21247   1.000 101.60404 ?  160 ASP C CB  1 
ATOM   1272 C CG  . ASP A 1 160 ? 95.69166  15.82700  3.18721   1.000 102.63387 ?  160 ASP C CG  1 
ATOM   1273 O OD1 . ASP A 1 160 ? 96.44321  15.03213  3.78275   1.000 113.18115 ?  160 ASP C OD1 1 
ATOM   1274 O OD2 . ASP A 1 160 ? 96.11240  16.81895  2.55323   1.000 116.16392 -1 160 ASP C OD2 1 
ATOM   1275 N N   . ASP A 1 161 ? 92.44532  17.56802  5.05848   1.000 96.06618  ?  161 ASP C N   1 
ATOM   1276 C CA  . ASP A 1 161 ? 92.38853  18.97934  5.41629   1.000 69.41896  ?  161 ASP C CA  1 
ATOM   1277 C C   . ASP A 1 161 ? 92.41702  19.18197  6.93067   1.000 73.87705  ?  161 ASP C C   1 
ATOM   1278 O O   . ASP A 1 161 ? 91.93075  18.35507  7.70814   1.000 75.97971  ?  161 ASP C O   1 
ATOM   1279 C CB  . ASP A 1 161 ? 91.13672  19.62523  4.82417   1.000 82.56861  ?  161 ASP C CB  1 
ATOM   1280 C CG  . ASP A 1 161 ? 91.15938  19.66203  3.30260   1.000 100.43094 ?  161 ASP C CG  1 
ATOM   1281 O OD1 . ASP A 1 161 ? 92.26231  19.70055  2.71394   1.000 103.98475 ?  161 ASP C OD1 1 
ATOM   1282 O OD2 . ASP A 1 161 ? 90.06802  19.65501  2.69458   1.000 94.12924  -1 161 ASP C OD2 1 
ATOM   1283 N N   . ILE A 1 162 ? 93.00419  20.30483  7.34060   1.000 73.60680  ?  162 ILE C N   1 
ATOM   1284 C CA  . ILE A 1 162 ? 93.10984  20.70115  8.74070   1.000 59.47564  ?  162 ILE C CA  1 
ATOM   1285 C C   . ILE A 1 162 ? 92.53352  22.10417  8.86440   1.000 56.67311  ?  162 ILE C C   1 
ATOM   1286 O O   . ILE A 1 162 ? 92.99766  23.02918  8.18697   1.000 67.01282  ?  162 ILE C O   1 
ATOM   1287 C CB  . ILE A 1 162 ? 94.56339  20.66970  9.24195   1.000 62.13609  ?  162 ILE C CB  1 
ATOM   1288 C CG1 . ILE A 1 162 ? 95.19352  19.30226  8.97140   1.000 69.71839  ?  162 ILE C CG1 1 
ATOM   1289 C CG2 . ILE A 1 162 ? 94.62524  21.01111  10.72279  1.000 61.13783  ?  162 ILE C CG2 1 
ATOM   1290 C CD1 . ILE A 1 162 ? 96.68526  19.26801  9.20457   1.000 69.10789  ?  162 ILE C CD1 1 
ATOM   1291 N N   . TYR A 1 163 ? 91.52829  22.26410  9.71993   1.000 57.64680  ?  163 TYR C N   1 
ATOM   1292 C CA  . TYR A 1 163 ? 90.82627  23.52952  9.87899   1.000 57.84108  ?  163 TYR C CA  1 
ATOM   1293 C C   . TYR A 1 163 ? 91.15957  24.15836  11.22504  1.000 51.02626  ?  163 TYR C C   1 
ATOM   1294 O O   . TYR A 1 163 ? 91.33425  23.45521  12.22548  1.000 51.07863  ?  163 TYR C O   1 
ATOM   1295 C CB  . TYR A 1 163 ? 89.31219  23.33597  9.75476   1.000 49.82919  ?  163 TYR C CB  1 
ATOM   1296 C CG  . TYR A 1 163 ? 88.86336  22.91679  8.37320   1.000 59.49596  ?  163 TYR C CG  1 
ATOM   1297 C CD1 . TYR A 1 163 ? 88.78229  21.57464  8.02452   1.000 61.88522  ?  163 TYR C CD1 1 
ATOM   1298 C CD2 . TYR A 1 163 ? 88.52366  23.86381  7.41602   1.000 53.19702  ?  163 TYR C CD2 1 
ATOM   1299 C CE1 . TYR A 1 163 ? 88.37369  21.18769  6.76118   1.000 65.95682  ?  163 TYR C CE1 1 
ATOM   1300 C CE2 . TYR A 1 163 ? 88.11395  23.48666  6.15068   1.000 59.96266  ?  163 TYR C CE2 1 
ATOM   1301 C CZ  . TYR A 1 163 ? 88.04086  22.14807  5.82863   1.000 65.75989  ?  163 TYR C CZ  1 
ATOM   1302 O OH  . TYR A 1 163 ? 87.63399  21.77002  4.56949   1.000 72.08201  ?  163 TYR C OH  1 
ATOM   1303 N N   . ASP A 1 164 ? 91.24198  25.48788  11.24063  1.000 52.10664  ?  164 ASP C N   1 
ATOM   1304 C CA  . ASP A 1 164 ? 91.51459  26.25607  12.44674  1.000 48.67905  ?  164 ASP C CA  1 
ATOM   1305 C C   . ASP A 1 164 ? 90.51974  27.40141  12.55516  1.000 50.40571  ?  164 ASP C C   1 
ATOM   1306 O O   . ASP A 1 164 ? 90.12109  27.98621  11.54343  1.000 59.30597  ?  164 ASP C O   1 
ATOM   1307 C CB  . ASP A 1 164 ? 92.94550  26.81599  12.44902  1.000 51.28960  ?  164 ASP C CB  1 
ATOM   1308 C CG  . ASP A 1 164 ? 93.99866  25.73119  12.54322  1.000 61.15187  ?  164 ASP C CG  1 
ATOM   1309 O OD1 . ASP A 1 164 ? 93.77004  24.73919  13.26643  1.000 80.35129  ?  164 ASP C OD1 1 
ATOM   1310 O OD2 . ASP A 1 164 ? 95.05711  25.87182  11.89433  1.000 74.54807  -1 164 ASP C OD2 1 
ATOM   1311 N N   . CYS A 1 165 ? 90.12109  27.71776  13.78493  1.000 54.78666  ?  165 CYS C N   1 
ATOM   1312 C CA  . CYS A 1 165 ? 89.26101  28.86171  14.07125  1.000 54.00241  ?  165 CYS C CA  1 
ATOM   1313 C C   . CYS A 1 165 ? 90.08466  29.88414  14.84407  1.000 56.23797  ?  165 CYS C C   1 
ATOM   1314 O O   . CYS A 1 165 ? 90.37669  29.68711  16.02858  1.000 68.02312  ?  165 CYS C O   1 
ATOM   1315 C CB  . CYS A 1 165 ? 88.02135  28.44415  14.85971  1.000 41.27932  ?  165 CYS C CB  1 
ATOM   1316 S SG  . CYS A 1 165 ? 86.93406  29.82548  15.29333  1.000 70.53227  ?  165 CYS C SG  1 
ATOM   1317 N N   . LYS A 1 166 ? 90.45982  30.96985  14.17423  1.000 50.03950  ?  166 LYS C N   1 
ATOM   1318 C CA  . LYS A 1 166 ? 91.28405  32.00556  14.78044  1.000 57.64254  ?  166 LYS C CA  1 
ATOM   1319 C C   . LYS A 1 166 ? 90.39603  33.04550  15.45128  1.000 65.39882  ?  166 LYS C C   1 
ATOM   1320 O O   . LYS A 1 166 ? 89.46915  33.57557  14.82973  1.000 58.53750  ?  166 LYS C O   1 
ATOM   1321 C CB  . LYS A 1 166 ? 92.17934  32.66297  13.72989  1.000 57.32254  ?  166 LYS C CB  1 
ATOM   1322 C CG  . LYS A 1 166 ? 93.24160  33.58274  14.30592  1.000 70.70566  ?  166 LYS C CG  1 
ATOM   1323 C CD  . LYS A 1 166 ? 94.25257  33.97907  13.24387  1.000 63.90932  ?  166 LYS C CD  1 
ATOM   1324 C CE  . LYS A 1 166 ? 95.31994  34.89994  13.80987  1.000 75.56539  ?  166 LYS C CE  1 
ATOM   1325 N NZ  . LYS A 1 166 ? 96.32855  35.27524  12.78056  1.000 96.81211  ?  166 LYS C NZ  1 
ATOM   1326 N N   . VAL A 1 167 ? 90.68188  33.33155  16.71858  1.000 56.82698  ?  167 VAL C N   1 
ATOM   1327 C CA  . VAL A 1 167 ? 89.90689  34.27424  17.51724  1.000 50.54973  ?  167 VAL C CA  1 
ATOM   1328 C C   . VAL A 1 167 ? 90.84141  35.38255  17.97961  1.000 58.07451  ?  167 VAL C C   1 
ATOM   1329 O O   . VAL A 1 167 ? 91.84847  35.11441  18.64771  1.000 53.53904  ?  167 VAL C O   1 
ATOM   1330 C CB  . VAL A 1 167 ? 89.23526  33.58879  18.71748  1.000 47.16234  ?  167 VAL C CB  1 
ATOM   1331 C CG1 . VAL A 1 167 ? 88.49904  34.61023  19.56643  1.000 39.86813  ?  167 VAL C CG1 1 
ATOM   1332 C CG2 . VAL A 1 167 ? 88.28745  32.49733  18.24375  1.000 40.47681  ?  167 VAL C CG2 1 
ATOM   1333 N N   . GLU A 1 168 ? 90.51069  36.62199  17.62398  1.000 57.27396  ?  168 GLU C N   1 
ATOM   1334 C CA  . GLU A 1 168 ? 91.27078  37.79506  18.03372  1.000 51.21423  ?  168 GLU C CA  1 
ATOM   1335 C C   . GLU A 1 168 ? 90.38595  38.68542  18.89222  1.000 44.86707  ?  168 GLU C C   1 
ATOM   1336 O O   . GLU A 1 168 ? 89.26820  39.02717  18.49215  1.000 55.11263  ?  168 GLU C O   1 
ATOM   1337 C CB  . GLU A 1 168 ? 91.79186  38.57335  16.82286  1.000 53.88020  ?  168 GLU C CB  1 
ATOM   1338 C CG  . GLU A 1 168 ? 92.80091  37.81142  15.98159  1.000 77.65274  ?  168 GLU C CG  1 
ATOM   1339 C CD  . GLU A 1 168 ? 93.49784  38.69796  14.96951  1.000 105.89556 ?  168 GLU C CD  1 
ATOM   1340 O OE1 . GLU A 1 168 ? 93.30317  39.93077  15.02568  1.000 106.38285 ?  168 GLU C OE1 1 
ATOM   1341 O OE2 . GLU A 1 168 ? 94.24089  38.16340  14.11949  1.000 111.40932 -1 168 GLU C OE2 1 
ATOM   1342 N N   . HIS A 1 169 ? 90.88813  39.05927  20.06655  1.000 51.62762  ?  169 HIS C N   1 
ATOM   1343 C CA  . HIS A 1 169 ? 90.12046  39.85824  21.00839  1.000 45.70340  ?  169 HIS C CA  1 
ATOM   1344 C C   . HIS A 1 169 ? 91.07648  40.73094  21.80750  1.000 49.38675  ?  169 HIS C C   1 
ATOM   1345 O O   . HIS A 1 169 ? 92.27056  40.44027  21.91634  1.000 76.11194  ?  169 HIS C O   1 
ATOM   1346 C CB  . HIS A 1 169 ? 89.28473  38.97043  21.93980  1.000 47.45795  ?  169 HIS C CB  1 
ATOM   1347 C CG  . HIS A 1 169 ? 88.25650  39.71797  22.72993  1.000 52.72395  ?  169 HIS C CG  1 
ATOM   1348 N ND1 . HIS A 1 169 ? 88.51820  40.25923  23.97007  1.000 54.33443  ?  169 HIS C ND1 1 
ATOM   1349 C CD2 . HIS A 1 169 ? 86.96280  40.00966  22.45808  1.000 49.90898  ?  169 HIS C CD2 1 
ATOM   1350 C CE1 . HIS A 1 169 ? 87.43184  40.85656  24.42590  1.000 52.58518  ?  169 HIS C CE1 1 
ATOM   1351 N NE2 . HIS A 1 169 ? 86.47327  40.71902  23.52779  1.000 54.85425  ?  169 HIS C NE2 1 
ATOM   1352 N N   . TRP A 1 170 ? 90.53181  41.81451  22.36647  1.000 49.42580  ?  170 TRP C N   1 
ATOM   1353 C CA  . TRP A 1 170 ? 91.34569  42.73087  23.15891  1.000 53.03731  ?  170 TRP C CA  1 
ATOM   1354 C C   . TRP A 1 170 ? 91.89462  42.06170  24.41198  1.000 55.40089  ?  170 TRP C C   1 
ATOM   1355 O O   . TRP A 1 170 ? 92.97418  42.42935  24.88895  1.000 67.53982  ?  170 TRP C O   1 
ATOM   1356 C CB  . TRP A 1 170 ? 90.52759  43.96712  23.53278  1.000 61.10286  ?  170 TRP C CB  1 
ATOM   1357 C CG  . TRP A 1 170 ? 90.23320  44.86814  22.37190  1.000 60.95063  ?  170 TRP C CG  1 
ATOM   1358 C CD1 . TRP A 1 170 ? 90.96445  44.99599  21.22690  1.000 56.22608  ?  170 TRP C CD1 1 
ATOM   1359 C CD2 . TRP A 1 170 ? 89.12145  45.76253  22.23994  1.000 58.66417  ?  170 TRP C CD2 1 
ATOM   1360 N NE1 . TRP A 1 170 ? 90.38047  45.91925  20.39291  1.000 62.46225  ?  170 TRP C NE1 1 
ATOM   1361 C CE2 . TRP A 1 170 ? 89.24698  46.40348  20.99117  1.000 59.33176  ?  170 TRP C CE2 1 
ATOM   1362 C CE3 . TRP A 1 170 ? 88.03352  46.08489  23.05727  1.000 60.04771  ?  170 TRP C CE3 1 
ATOM   1363 C CZ2 . TRP A 1 170 ? 88.32560  47.34695  20.54003  1.000 56.17333  ?  170 TRP C CZ2 1 
ATOM   1364 C CZ3 . TRP A 1 170 ? 87.12009  47.02221  22.60778  1.000 51.65329  ?  170 TRP C CZ3 1 
ATOM   1365 C CH2 . TRP A 1 170 ? 87.27199  47.64179  21.36086  1.000 52.61824  ?  170 TRP C CH2 1 
ATOM   1366 N N   . GLY A 1 171 ? 91.17465  41.08639  24.95791  1.000 56.55386  ?  171 GLY C N   1 
ATOM   1367 C CA  . GLY A 1 171 ? 91.61579  40.36847  26.13319  1.000 68.91199  ?  171 GLY C CA  1 
ATOM   1368 C C   . GLY A 1 171 ? 92.53889  39.20138  25.87334  1.000 66.93713  ?  171 GLY C C   1 
ATOM   1369 O O   . GLY A 1 171 ? 92.75084  38.37987  26.76952  1.000 60.08098  ?  171 GLY C O   1 
ATOM   1370 N N   . LEU A 1 172 ? 93.09907  39.10020  24.66940  1.000 66.60955  ?  172 LEU C N   1 
ATOM   1371 C CA  . LEU A 1 172 ? 93.99814  38.01486  24.29844  1.000 65.02333  ?  172 LEU C CA  1 
ATOM   1372 C C   . LEU A 1 172 ? 95.35171  38.60193  23.92931  1.000 64.29480  ?  172 LEU C C   1 
ATOM   1373 O O   . LEU A 1 172 ? 95.44620  39.41655  23.00488  1.000 81.41228  ?  172 LEU C O   1 
ATOM   1374 C CB  . LEU A 1 172 ? 93.43058  37.20600  23.13056  1.000 55.92370  ?  172 LEU C CB  1 
ATOM   1375 C CG  . LEU A 1 172 ? 92.11632  36.46263  23.36851  1.000 52.08180  ?  172 LEU C CG  1 
ATOM   1376 C CD1 . LEU A 1 172 ? 91.61374  35.84510  22.07315  1.000 49.01705  ?  172 LEU C CD1 1 
ATOM   1377 C CD2 . LEU A 1 172 ? 92.28931  35.39923  24.44096  1.000 54.26606  ?  172 LEU C CD2 1 
ATOM   1378 N N   . GLU A 1 173 ? 96.39546  38.19120  24.65239  1.000 69.27824  ?  173 GLU C N   1 
ATOM   1379 C CA  . GLU A 1 173 ? 97.74600  38.60214  24.28439  1.000 74.48648  ?  173 GLU C CA  1 
ATOM   1380 C C   . GLU A 1 173 ? 98.15513  37.99040  22.95124  1.000 74.78623  ?  173 GLU C C   1 
ATOM   1381 O O   . GLU A 1 173 ? 98.84810  38.63093  22.15264  1.000 86.53554  ?  173 GLU C O   1 
ATOM   1382 C CB  . GLU A 1 173 ? 98.73358  38.21246  25.38403  1.000 80.60191  ?  173 GLU C CB  1 
ATOM   1383 N N   . GLU A 1 174 ? 97.73168  36.75731  22.69461  1.000 95.58820  ?  174 GLU C N   1 
ATOM   1384 C CA  . GLU A 1 174 ? 97.95549  36.06246  21.43922  1.000 90.11915  ?  174 GLU C CA  1 
ATOM   1385 C C   . GLU A 1 174 ? 96.63708  35.49926  20.93297  1.000 85.33573  ?  174 GLU C C   1 
ATOM   1386 O O   . GLU A 1 174 ? 95.76031  35.15071  21.73042  1.000 81.06764  ?  174 GLU C O   1 
ATOM   1387 C CB  . GLU A 1 174 ? 98.97346  34.92342  21.60293  1.000 89.84387  ?  174 GLU C CB  1 
ATOM   1388 C CG  . GLU A 1 174 ? 100.38096 35.38166  21.96012  1.000 106.04992 ?  174 GLU C CG  1 
ATOM   1389 C CD  . GLU A 1 174 ? 101.11869 35.99523  20.78338  1.000 115.96881 ?  174 GLU C CD  1 
ATOM   1390 O OE1 . GLU A 1 174 ? 100.62625 35.88016  19.64093  1.000 114.59792 ?  174 GLU C OE1 1 
ATOM   1391 O OE2 . GLU A 1 174 ? 102.19517 36.59093  21.00106  1.000 103.07211 -1 174 GLU C OE2 1 
ATOM   1392 N N   . PRO A 1 175 ? 96.46336  35.41164  19.61475  1.000 83.93523  ?  175 PRO C N   1 
ATOM   1393 C CA  . PRO A 1 175 ? 95.21194  34.86643  19.07446  1.000 70.07482  ?  175 PRO C CA  1 
ATOM   1394 C C   . PRO A 1 175 ? 95.01343  33.41322  19.48117  1.000 71.47492  ?  175 PRO C C   1 
ATOM   1395 O O   . PRO A 1 175 ? 95.96770  32.63986  19.58627  1.000 89.94638  ?  175 PRO C O   1 
ATOM   1396 C CB  . PRO A 1 175 ? 95.38879  35.00766  17.55807  1.000 69.48810  ?  175 PRO C CB  1 
ATOM   1397 C CG  . PRO A 1 175 ? 96.41447  36.08284  17.39191  1.000 63.37456  ?  175 PRO C CG  1 
ATOM   1398 C CD  . PRO A 1 175 ? 97.34549  35.92820  18.55495  1.000 78.87190  ?  175 PRO C CD  1 
ATOM   1399 N N   . VAL A 1 176 ? 93.75594  33.05047  19.71313  1.000 70.69686  ?  176 VAL C N   1 
ATOM   1400 C CA  . VAL A 1 176 ? 93.38821  31.69258  20.09739  1.000 69.75808  ?  176 VAL C CA  1 
ATOM   1401 C C   . VAL A 1 176 ? 93.10548  30.88586  18.83757  1.000 66.45584  ?  176 VAL C C   1 
ATOM   1402 O O   . VAL A 1 176 ? 92.41722  31.35902  17.92516  1.000 68.40956  ?  176 VAL C O   1 
ATOM   1403 C CB  . VAL A 1 176 ? 92.17209  31.69946  21.03966  1.000 76.81750  ?  176 VAL C CB  1 
ATOM   1404 C CG1 . VAL A 1 176 ? 91.63309  30.29062  21.23634  1.000 82.67432  ?  176 VAL C CG1 1 
ATOM   1405 C CG2 . VAL A 1 176 ? 92.54790  32.31363  22.37801  1.000 84.78249  ?  176 VAL C CG2 1 
ATOM   1406 N N   . LEU A 1 177 ? 93.63851  29.66685  18.78501  1.000 57.59150  ?  177 LEU C N   1 
ATOM   1407 C CA  . LEU A 1 177 ? 93.49971  28.79395  17.62579  1.000 60.38139  ?  177 LEU C CA  1 
ATOM   1408 C C   . LEU A 1 177 ? 92.98092  27.43968  18.08190  1.000 55.17788  ?  177 LEU C C   1 
ATOM   1409 O O   . LEU A 1 177 ? 93.66364  26.73119  18.82884  1.000 62.83198  ?  177 LEU C O   1 
ATOM   1410 C CB  . LEU A 1 177 ? 94.83633  28.63942  16.89442  1.000 56.19491  ?  177 LEU C CB  1 
ATOM   1411 C CG  . LEU A 1 177 ? 95.37458  29.90531  16.22672  1.000 57.49403  ?  177 LEU C CG  1 
ATOM   1412 C CD1 . LEU A 1 177 ? 96.84793  29.76054  15.89705  1.000 61.02984  ?  177 LEU C CD1 1 
ATOM   1413 C CD2 . LEU A 1 177 ? 94.57648  30.21263  14.97246  1.000 62.61187  ?  177 LEU C CD2 1 
ATOM   1414 N N   . LYS A 1 178 ? 91.77888  27.08501  17.63733  1.000 53.22074  ?  178 LYS C N   1 
ATOM   1415 C CA  . LYS A 1 178 ? 91.19363  25.77553  17.89084  1.000 51.97707  ?  178 LYS C CA  1 
ATOM   1416 C C   . LYS A 1 178 ? 91.24857  24.95393  16.61131  1.000 59.03500  ?  178 LYS C C   1 
ATOM   1417 O O   . LYS A 1 178 ? 90.87519  25.44172  15.53930  1.000 48.27637  ?  178 LYS C O   1 
ATOM   1418 C CB  . LYS A 1 178 ? 89.75162  25.89929  18.38741  1.000 50.75370  ?  178 LYS C CB  1 
ATOM   1419 C CG  . LYS A 1 178 ? 89.63210  26.44539  19.79981  1.000 54.16492  ?  178 LYS C CG  1 
ATOM   1420 C CD  . LYS A 1 178 ? 90.33683  25.54222  20.79896  1.000 51.75382  ?  178 LYS C CD  1 
ATOM   1421 C CE  . LYS A 1 178 ? 90.31425  26.13841  22.19708  1.000 69.40207  ?  178 LYS C CE  1 
ATOM   1422 N NZ  . LYS A 1 178 ? 91.03894  25.28380  23.17754  1.000 93.45754  ?  178 LYS C NZ  1 
ATOM   1423 N N   . HIS A 1 179 ? 91.71278  23.71519  16.72634  1.000 70.08964  ?  179 HIS C N   1 
ATOM   1424 C CA  . HIS A 1 179 ? 91.94008  22.85296  15.57756  1.000 57.72180  ?  179 HIS C CA  1 
ATOM   1425 C C   . HIS A 1 179 ? 90.81730  21.83220  15.43278  1.000 59.74760  ?  179 HIS C C   1 
ATOM   1426 O O   . HIS A 1 179 ? 90.07379  21.54860  16.37538  1.000 77.99019  ?  179 HIS C O   1 
ATOM   1427 C CB  . HIS A 1 179 ? 93.28562  22.13475  15.70598  1.000 59.22861  ?  179 HIS C CB  1 
ATOM   1428 C CG  . HIS A 1 179 ? 94.36224  22.97698  16.31608  1.000 62.30886  ?  179 HIS C CG  1 
ATOM   1429 N ND1 . HIS A 1 179 ? 94.76452  24.17882  15.77463  1.000 65.24413  ?  179 HIS C ND1 1 
ATOM   1430 C CD2 . HIS A 1 179 ? 95.12033  22.79060  17.42247  1.000 78.00749  ?  179 HIS C CD2 1 
ATOM   1431 C CE1 . HIS A 1 179 ? 95.72379  24.69665  16.52101  1.000 70.33624  ?  179 HIS C CE1 1 
ATOM   1432 N NE2 . HIS A 1 179 ? 95.95876  23.87384  17.52717  1.000 71.06486  ?  179 HIS C NE2 1 
ATOM   1433 N N   . TRP A 1 180 ? 90.70493  21.27930  14.22659  1.000 60.38153  ?  180 TRP C N   1 
ATOM   1434 C CA  . TRP A 1 180 ? 89.72376  20.24037  13.95083  1.000 64.36538  ?  180 TRP C CA  1 
ATOM   1435 C C   . TRP A 1 180 ? 90.15457  19.46471  12.71544  1.000 62.72661  ?  180 TRP C C   1 
ATOM   1436 O O   . TRP A 1 180 ? 90.61186  20.05475  11.73363  1.000 60.63203  ?  180 TRP C O   1 
ATOM   1437 C CB  . TRP A 1 180 ? 88.32165  20.82440  13.74157  1.000 61.75285  ?  180 TRP C CB  1 
ATOM   1438 C CG  . TRP A 1 180 ? 87.26592  19.77302  13.57184  1.000 69.51445  ?  180 TRP C CG  1 
ATOM   1439 C CD1 . TRP A 1 180 ? 86.49317  19.22277  14.55279  1.000 72.34241  ?  180 TRP C CD1 1 
ATOM   1440 C CD2 . TRP A 1 180 ? 86.87311  19.13741  12.34835  1.000 67.53882  ?  180 TRP C CD2 1 
ATOM   1441 N NE1 . TRP A 1 180 ? 85.64177  18.28731  14.01644  1.000 64.54964  ?  180 TRP C NE1 1 
ATOM   1442 C CE2 . TRP A 1 180 ? 85.85522  18.21587  12.66502  1.000 56.69623  ?  180 TRP C CE2 1 
ATOM   1443 C CE3 . TRP A 1 180 ? 87.28196  19.25937  11.01642  1.000 65.75452  ?  180 TRP C CE3 1 
ATOM   1444 C CZ2 . TRP A 1 180 ? 85.24080  17.42163  11.69966  1.000 62.51455  ?  180 TRP C CZ2 1 
ATOM   1445 C CZ3 . TRP A 1 180 ? 86.67103  18.46915  10.05954  1.000 63.43157  ?  180 TRP C CZ3 1 
ATOM   1446 C CH2 . TRP A 1 180 ? 85.66152  17.56267  10.40589  1.000 75.18984  ?  180 TRP C CH2 1 
ATOM   1447 N N   . THR A 1 181 ? 89.99936  18.14449  12.77427  1.000 71.04615  ?  181 THR C N   1 
ATOM   1448 C CA  . THR A 1 181 ? 90.27540  17.25867  11.65379  1.000 75.43231  ?  181 THR C CA  1 
ATOM   1449 C C   . THR A 1 181 ? 89.11460  16.28082  11.51179  1.000 78.39113  ?  181 THR C C   1 
ATOM   1450 O O   . THR A 1 181 ? 88.25080  16.17735  12.38677  1.000 73.95098  ?  181 THR C O   1 
ATOM   1451 C CB  . THR A 1 181 ? 91.60541  16.51069  11.84192  1.000 73.26833  ?  181 THR C CB  1 
ATOM   1452 O OG1 . THR A 1 181 ? 92.53188  17.35337  12.53761  1.000 77.72279  ?  181 THR C OG1 1 
ATOM   1453 C CG2 . THR A 1 181 ? 92.20986  16.13584  10.49512  1.000 87.32702  ?  181 THR C CG2 1 
ATOM   1454 N N   . SER A 1 182 ? 89.09739  15.55646  10.39036  1.000 84.48908  ?  182 SER C N   1 
ATOM   1455 C CA  . SER A 1 182 ? 87.98480  14.66147  10.09274  1.000 85.00690  ?  182 SER C CA  1 
ATOM   1456 C C   . SER A 1 182 ? 87.93487  13.44763  11.01335  1.000 98.05358  ?  182 SER C C   1 
ATOM   1457 O O   . SER A 1 182 ? 86.88611  12.80040  11.10196  1.000 119.68850 ?  182 SER C O   1 
ATOM   1458 C CB  . SER A 1 182 ? 88.06005  14.19982  8.63642   1.000 99.29747  ?  182 SER C CB  1 
ATOM   1459 O OG  . SER A 1 182 ? 89.26250  13.49250  8.38690   1.000 107.96017 ?  182 SER C OG  1 
ATOM   1460 N N   . GLY A 1 183 ? 89.02952  13.12309  11.69697  1.000 87.46233  ?  183 GLY C N   1 
ATOM   1461 C CA  . GLY A 1 183 ? 89.06061  11.93684  12.53084  1.000 91.22896  ?  183 GLY C CA  1 
ATOM   1462 C C   . GLY A 1 183 ? 89.10916  12.21616  14.01913  1.000 108.06896 ?  183 GLY C C   1 
ATOM   1463 O O   . GLY A 1 183 ? 89.74818  11.47515  14.77217  1.000 102.84944 ?  183 GLY C O   1 
ATOM   1464 N N   . LEU A 1 184 ? 88.43466  13.27306  14.45844  1.000 105.81810 ?  184 LEU C N   1 
ATOM   1465 C CA  . LEU A 1 184 ? 88.41009  13.66706  15.85927  1.000 106.12533 ?  184 LEU C CA  1 
ATOM   1466 C C   . LEU A 1 184 ? 87.05591  13.34717  16.48048  1.000 120.08808 ?  184 LEU C C   1 
ATOM   1467 O O   . LEU A 1 184 ? 86.08527  13.01884  15.79313  1.000 129.79701 ?  184 LEU C O   1 
ATOM   1468 C CB  . LEU A 1 184 ? 88.72315  15.16074  16.01141  1.000 95.45320  ?  184 LEU C CB  1 
ATOM   1469 C CG  . LEU A 1 184 ? 90.17473  15.55640  16.29305  1.000 90.94912  ?  184 LEU C CG  1 
ATOM   1470 C CD1 . LEU A 1 184 ? 91.10876  15.05800  15.20047  1.000 102.53462 ?  184 LEU C CD1 1 
ATOM   1471 C CD2 . LEU A 1 184 ? 90.28849  17.06491  16.45354  1.000 80.58129  ?  184 LEU C CD2 1 
ATOM   1472 N N   . GLU A 1 185 ? 87.00554  13.44564  17.80759  1.000 134.88232 ?  185 GLU C N   1 
ATOM   1473 C CA  . GLU A 1 185 ? 85.77637  13.26358  18.56358  1.000 128.31427 ?  185 GLU C CA  1 
ATOM   1474 C C   . GLU A 1 185 ? 85.62296  14.40901  19.55360  1.000 134.48373 ?  185 GLU C C   1 
ATOM   1475 O O   . GLU A 1 185 ? 86.60988  14.95537  20.05482  1.000 138.67677 ?  185 GLU C O   1 
ATOM   1476 C CB  . GLU A 1 185 ? 85.75197  11.91405  19.30598  1.000 127.45237 ?  185 GLU C CB  1 
ATOM   1477 C CG  . GLU A 1 185 ? 86.61267  11.85443  20.56258  1.000 151.63566 ?  185 GLU C CG  1 
ATOM   1478 C CD  . GLU A 1 185 ? 88.09954  11.88423  20.26532  1.000 160.85094 ?  185 GLU C CD  1 
ATOM   1479 O OE1 . GLU A 1 185 ? 88.49198  11.51530  19.13838  1.000 146.74136 ?  185 GLU C OE1 1 
ATOM   1480 O OE2 . GLU A 1 185 ? 88.87653  12.27860  21.16021  1.000 171.97388 ?  185 GLU C OE2 1 
ATOM   1481 N N   . VAL A 1 186 ? 84.37377  14.77365  19.82293  1.000 140.32357 ?  186 VAL C N   1 
ATOM   1482 C CA  . VAL A 1 186 ? 84.07857  15.87609  20.72929  1.000 129.61354 ?  186 VAL C CA  1 
ATOM   1483 C C   . VAL A 1 186 ? 82.66730  15.74020  21.28698  1.000 122.21291 ?  186 VAL C C   1 
ATOM   1484 O O   . VAL A 1 186 ? 82.46770  15.73635  22.50164  1.000 122.88041 ?  186 VAL C O   1 
ATOM   1485 C CB  . VAL A 1 186 ? 84.25842  17.23562  20.02886  1.000 114.73703 ?  186 VAL C CB  1 
ATOM   1486 C CG1 . VAL A 1 186 ? 83.35835  17.32572  18.80662  1.000 102.85319 ?  186 VAL C CG1 1 
ATOM   1487 C CG2 . VAL A 1 186 ? 83.97116  18.37433  20.99607  1.000 96.49187  ?  186 VAL C CG2 1 
ATOM   1488 N N   . GLN B 2 1   ? 53.03558  37.14687  12.35748  1.000 93.14876  ?  -25 GLN D N   1 
ATOM   1489 C CA  . GLN B 2 1   ? 52.31821  38.17075  11.60939  1.000 68.68170  ?  -25 GLN D CA  1 
ATOM   1490 C C   . GLN B 2 1   ? 52.96667  39.53658  11.79531  1.000 61.45942  ?  -25 GLN D C   1 
ATOM   1491 O O   . GLN B 2 1   ? 53.47146  40.12372  10.83979  1.000 80.28542  ?  -25 GLN D O   1 
ATOM   1492 C CB  . GLN B 2 1   ? 50.85083  38.20781  12.02940  1.000 53.54515  ?  -25 GLN D CB  1 
ATOM   1493 C CG  . GLN B 2 1   ? 49.99843  37.19032  11.29812  1.000 92.66485  ?  -25 GLN D CG  1 
ATOM   1494 C CD  . GLN B 2 1   ? 50.00911  37.41438  9.79906   1.000 94.09195  ?  -25 GLN D CD  1 
ATOM   1495 O OE1 . GLN B 2 1   ? 50.06930  38.55219  9.33195   1.000 82.63346  ?  -25 GLN D OE1 1 
ATOM   1496 N NE2 . GLN B 2 1   ? 49.96062  36.32906  9.03625   1.000 107.53219 ?  -25 GLN D NE2 1 
ATOM   1497 N N   . VAL B 2 2   ? 52.95292  40.03659  13.02965  1.000 44.46333  ?  -24 VAL D N   1 
ATOM   1498 C CA  . VAL B 2 2   ? 53.63492  41.27965  13.37759  1.000 59.58063  ?  -24 VAL D CA  1 
ATOM   1499 C C   . VAL B 2 2   ? 54.15970  41.15670  14.80208  1.000 55.81288  ?  -24 VAL D C   1 
ATOM   1500 O O   . VAL B 2 2   ? 53.40350  40.83670  15.72551  1.000 50.90809  ?  -24 VAL D O   1 
ATOM   1501 C CB  . VAL B 2 2   ? 52.70675  42.50082  13.22396  1.000 63.35664  ?  -24 VAL D CB  1 
ATOM   1502 C CG1 . VAL B 2 2   ? 53.13685  43.61549  14.15324  1.000 66.34773  ?  -24 VAL D CG1 1 
ATOM   1503 C CG2 . VAL B 2 2   ? 52.70887  43.00279  11.78618  1.000 61.21103  ?  -24 VAL D CG2 1 
ATOM   1504 N N   . TYR B 2 3   ? 55.45672  41.39444  14.98980  1.000 54.69127  ?  -23 TYR D N   1 
ATOM   1505 C CA  . TYR B 2 3   ? 56.07316  41.29214  16.30553  1.000 53.13064  ?  -23 TYR D CA  1 
ATOM   1506 C C   . TYR B 2 3   ? 56.02393  42.63055  17.03000  1.000 53.23847  ?  -23 TYR D C   1 
ATOM   1507 O O   . TYR B 2 3   ? 56.20443  43.68943  16.42259  1.000 46.98133  ?  -23 TYR D O   1 
ATOM   1508 C CB  . TYR B 2 3   ? 57.52402  40.81677  16.19644  1.000 47.40358  ?  -23 TYR D CB  1 
ATOM   1509 C CG  . TYR B 2 3   ? 57.67760  39.31284  16.13792  1.000 42.09797  ?  -23 TYR D CG  1 
ATOM   1510 C CD1 . TYR B 2 3   ? 57.73156  38.55310  17.30077  1.000 44.33235  ?  -23 TYR D CD1 1 
ATOM   1511 C CD2 . TYR B 2 3   ? 57.77138  38.65288  14.92113  1.000 48.50416  ?  -23 TYR D CD2 1 
ATOM   1512 C CE1 . TYR B 2 3   ? 57.86993  37.17606  17.25060  1.000 43.49645  ?  -23 TYR D CE1 1 
ATOM   1513 C CE2 . TYR B 2 3   ? 57.91165  37.27942  14.86185  1.000 35.77426  ?  -23 TYR D CE2 1 
ATOM   1514 C CZ  . TYR B 2 3   ? 57.95880  36.54613  16.02767  1.000 43.07129  ?  -23 TYR D CZ  1 
ATOM   1515 O OH  . TYR B 2 3   ? 58.09714  35.17831  15.96639  1.000 54.16604  ?  -23 TYR D OH  1 
ATOM   1516 N N   . SER B 2 4   ? 55.77713  42.57227  18.33474  1.000 51.23498  ?  -22 SER D N   1 
ATOM   1517 C CA  . SER B 2 4   ? 55.79736  43.74012  19.19990  1.000 40.60876  ?  -22 SER D CA  1 
ATOM   1518 C C   . SER B 2 4   ? 57.05823  43.72232  20.05362  1.000 51.58982  ?  -22 SER D C   1 
ATOM   1519 O O   . SER B 2 4   ? 57.55566  42.65790  20.43231  1.000 54.45645  ?  -22 SER D O   1 
ATOM   1520 C CB  . SER B 2 4   ? 54.55673  43.78680  20.09668  1.000 58.28644  ?  -22 SER D CB  1 
ATOM   1521 O OG  . SER B 2 4   ? 53.37600  43.93629  19.32740  1.000 56.41884  ?  -22 SER D OG  1 
ATOM   1522 N N   . LEU B 2 5   ? 57.57181  44.91179  20.35612  1.000 52.83044  ?  -21 LEU D N   1 
ATOM   1523 C CA  . LEU B 2 5   ? 58.83184  45.05461  21.06787  1.000 52.02029  ?  -21 LEU D CA  1 
ATOM   1524 C C   . LEU B 2 5   ? 58.62879  45.80513  22.37663  1.000 50.56949  ?  -21 LEU D C   1 
ATOM   1525 O O   . LEU B 2 5   ? 57.68883  46.59175  22.52724  1.000 51.25252  ?  -21 LEU D O   1 
ATOM   1526 C CB  . LEU B 2 5   ? 59.87827  45.78758  20.21500  1.000 42.51504  ?  -21 LEU D CB  1 
ATOM   1527 C CG  . LEU B 2 5   ? 59.86278  47.31883  20.21003  1.000 44.18540  ?  -21 LEU D CG  1 
ATOM   1528 C CD1 . LEU B 2 5   ? 61.11487  47.84772  19.53712  1.000 53.36457  ?  -21 LEU D CD1 1 
ATOM   1529 C CD2 . LEU B 2 5   ? 58.61851  47.86894  19.52659  1.000 40.97190  ?  -21 LEU D CD2 1 
ATOM   1530 N N   . ILE B 2 6   ? 59.52870  45.55243  23.31921  1.000 57.95673  ?  -20 ILE D N   1 
ATOM   1531 C CA  . ILE B 2 6   ? 59.54458  46.24763  24.59946  1.000 49.63798  ?  -20 ILE D CA  1 
ATOM   1532 C C   . ILE B 2 6   ? 60.39753  47.50015  24.45965  1.000 54.80639  ?  -20 ILE D C   1 
ATOM   1533 O O   . ILE B 2 6   ? 61.51650  47.44624  23.93530  1.000 56.57566  ?  -20 ILE D O   1 
ATOM   1534 C CB  . ILE B 2 6   ? 60.08228  45.33231  25.71057  1.000 46.66440  ?  -20 ILE D CB  1 
ATOM   1535 C CG1 . ILE B 2 6   ? 59.10557  44.18419  25.96292  1.000 56.36494  ?  -20 ILE D CG1 1 
ATOM   1536 C CG2 . ILE B 2 6   ? 60.33590  46.12514  26.98228  1.000 45.57485  ?  -20 ILE D CG2 1 
ATOM   1537 C CD1 . ILE B 2 6   ? 59.77203  42.89033  26.35737  1.000 53.20904  ?  -20 ILE D CD1 1 
ATOM   1538 N N   . ARG B 2 7   ? 59.86987  48.63202  24.92398  1.000 52.22937  ?  -19 ARG D N   1 
ATOM   1539 C CA  . ARG B 2 7   ? 60.58083  49.89697  24.82979  1.000 44.78249  ?  -19 ARG D CA  1 
ATOM   1540 C C   . ARG B 2 7   ? 61.20271  50.23831  26.17294  1.000 51.73359  ?  -19 ARG D C   1 
ATOM   1541 O O   . ARG B 2 7   ? 60.48124  50.29417  27.18155  1.000 46.45535  ?  -19 ARG D O   1 
ATOM   1542 C CB  . ARG B 2 7   ? 59.63801  51.00809  24.38409  1.000 40.61785  ?  -19 ARG D CB  1 
ATOM   1543 C CG  . ARG B 2 7   ? 59.10503  50.82412  22.97099  1.000 42.95963  ?  -19 ARG D CG  1 
ATOM   1544 C CD  . ARG B 2 7   ? 58.31661  52.03626  22.51080  1.000 39.29158  ?  -19 ARG D CD  1 
ATOM   1545 N NE  . ARG B 2 7   ? 58.24711  52.11925  21.05648  1.000 42.55993  ?  -19 ARG D NE  1 
ATOM   1546 C CZ  . ARG B 2 7   ? 57.18674  51.78854  20.33276  1.000 52.00280  ?  -19 ARG D CZ  1 
ATOM   1547 N NH1 . ARG B 2 7   ? 56.07216  51.35728  20.89758  1.000 71.72286  ?  -19 ARG D NH1 1 
ATOM   1548 N NH2 . ARG B 2 7   ? 57.24391  51.90169  19.00877  1.000 57.72571  ?  -19 ARG D NH2 1 
ATOM   1549 N N   . PRO B 2 8   ? 62.51160  50.46466  26.24324  1.000 56.85673  ?  -18 PRO D N   1 
ATOM   1550 C CA  . PRO B 2 8   ? 63.13413  50.82614  27.51870  1.000 38.95572  ?  -18 PRO D CA  1 
ATOM   1551 C C   . PRO B 2 8   ? 62.86033  52.27286  27.89282  1.000 53.51515  ?  -18 PRO D C   1 
ATOM   1552 O O   . PRO B 2 8   ? 62.71251  53.14971  27.03820  1.000 43.76704  ?  -18 PRO D O   1 
ATOM   1553 C CB  . PRO B 2 8   ? 64.62729  50.60368  27.25288  1.000 45.44821  ?  -18 PRO D CB  1 
ATOM   1554 C CG  . PRO B 2 8   ? 64.77327  50.85164  25.79103  1.000 40.06538  ?  -18 PRO D CG  1 
ATOM   1555 C CD  . PRO B 2 8   ? 63.49907  50.35816  25.15491  1.000 44.30610  ?  -18 PRO D CD  1 
ATOM   1556 N N   . ASN B 2 9   ? 62.79757  52.51315  29.19836  1.000 41.13644  ?  -17 ASN D N   1 
ATOM   1557 C CA  . ASN B 2 9   ? 62.58516  53.86119  29.69590  1.000 53.96078  ?  -17 ASN D CA  1 
ATOM   1558 C C   . ASN B 2 9   ? 63.87132  54.67682  29.59190  1.000 47.33993  ?  -17 ASN D C   1 
ATOM   1559 O O   . ASN B 2 9   ? 64.98123  54.13888  29.55215  1.000 57.78938  ?  -17 ASN D O   1 
ATOM   1560 C CB  . ASN B 2 9   ? 62.08598  53.82875  31.13984  1.000 47.77134  ?  -17 ASN D CB  1 
ATOM   1561 C CG  . ASN B 2 9   ? 60.70049  53.22613  31.26187  1.000 58.22365  ?  -17 ASN D CG  1 
ATOM   1562 O OD1 . ASN B 2 9   ? 59.86085  53.38785  30.37583  1.000 54.04183  ?  -17 ASN D OD1 1 
ATOM   1563 N ND2 . ASN B 2 9   ? 60.45453  52.52452  32.36195  1.000 56.22041  ?  -17 ASN D ND2 1 
ATOM   1564 N N   . GLU B 2 10  ? 63.70694  55.99437  29.54552  1.000 53.91454  ?  -16 GLU D N   1 
ATOM   1565 C CA  . GLU B 2 10  ? 64.81229  56.91477  29.33125  1.000 45.78243  ?  -16 GLU D CA  1 
ATOM   1566 C C   . GLU B 2 10  ? 65.25039  57.55016  30.64506  1.000 50.10932  ?  -16 GLU D C   1 
ATOM   1567 O O   . GLU B 2 10  ? 64.44702  57.75273  31.55907  1.000 53.73740  ?  -16 GLU D O   1 
ATOM   1568 C CB  . GLU B 2 10  ? 64.41990  58.00989  28.33704  1.000 48.80935  ?  -16 GLU D CB  1 
ATOM   1569 C CG  . GLU B 2 10  ? 63.60939  57.51428  27.15083  1.000 48.14638  ?  -16 GLU D CG  1 
ATOM   1570 C CD  . GLU B 2 10  ? 63.22907  58.63205  26.19898  1.000 63.32289  ?  -16 GLU D CD  1 
ATOM   1571 O OE1 . GLU B 2 10  ? 64.11210  59.44211  25.84727  1.000 57.87968  ?  -16 GLU D OE1 1 
ATOM   1572 O OE2 . GLU B 2 10  ? 62.04479  58.70665  25.80899  1.000 77.60864  -1 -16 GLU D OE2 1 
ATOM   1573 N N   . ASN B 2 11  ? 66.54360  57.86348  30.72781  1.000 64.13201  ?  -15 ASN D N   1 
ATOM   1574 C CA  . ASN B 2 11  ? 67.07801  58.58448  31.87465  1.000 71.19826  ?  -15 ASN D CA  1 
ATOM   1575 C C   . ASN B 2 11  ? 66.74227  60.07065  31.76148  1.000 72.07351  ?  -15 ASN D C   1 
ATOM   1576 O O   . ASN B 2 11  ? 66.87589  60.65691  30.68426  1.000 81.61913  ?  -15 ASN D O   1 
ATOM   1577 C CB  . ASN B 2 11  ? 68.59217  58.40273  31.96954  1.000 69.80230  ?  -15 ASN D CB  1 
ATOM   1578 C CG  . ASN B 2 11  ? 68.98428  57.11657  32.66929  1.000 62.44811  ?  -15 ASN D CG  1 
ATOM   1579 O OD1 . ASN B 2 11  ? 68.76966  56.02164  32.15082  1.000 67.86784  ?  -15 ASN D OD1 1 
ATOM   1580 N ND2 . ASN B 2 11  ? 69.57441  57.24500  33.85129  1.000 73.84440  ?  -15 ASN D ND2 1 
ATOM   1581 N N   . PRO B 2 12  ? 66.30433  60.69876  32.84800  1.000 65.80692  ?  -14 PRO D N   1 
ATOM   1582 C CA  . PRO B 2 12  ? 65.97244  62.12460  32.79391  1.000 73.42388  ?  -14 PRO D CA  1 
ATOM   1583 C C   . PRO B 2 12  ? 67.21313  63.00330  32.78810  1.000 73.85699  ?  -14 PRO D C   1 
ATOM   1584 O O   . PRO B 2 12  ? 68.26009  62.65242  33.33815  1.000 77.84685  ?  -14 PRO D O   1 
ATOM   1585 C CB  . PRO B 2 12  ? 65.15240  62.34003  34.07117  1.000 68.56387  ?  -14 PRO D CB  1 
ATOM   1586 C CG  . PRO B 2 12  ? 65.67527  61.31081  35.01423  1.000 63.55514  ?  -14 PRO D CG  1 
ATOM   1587 C CD  . PRO B 2 12  ? 66.02126  60.11149  34.16951  1.000 63.65673  ?  -14 PRO D CD  1 
ATOM   1588 N N   . ALA B 2 13  ? 67.07183  64.16307  32.14846  1.000 86.28413  ?  -13 ALA D N   1 
ATOM   1589 C CA  . ALA B 2 13  ? 68.12967  65.17081  32.07071  1.000 92.41475  ?  -13 ALA D CA  1 
ATOM   1590 C C   . ALA B 2 13  ? 69.44201  64.59093  31.54784  1.000 102.94648 ?  -13 ALA D C   1 
ATOM   1591 O O   . ALA B 2 13  ? 70.50895  64.83853  32.11066  1.000 96.81944  ?  -13 ALA D O   1 
ATOM   1592 C CB  . ALA B 2 13  ? 68.34340  65.81985  33.43449  1.000 67.49850  ?  -13 ALA D CB  1 
ATOM   1593 N N   . ARG B 2 35  ? 88.77895  53.93102  27.69775  1.000 97.92035  ?  2   ARG D N   1 
ATOM   1594 C CA  . ARG B 2 35  ? 87.45597  54.35315  28.14266  1.000 90.50158  ?  2   ARG D CA  1 
ATOM   1595 C C   . ARG B 2 35  ? 86.36233  53.74075  27.27328  1.000 84.03822  ?  2   ARG D C   1 
ATOM   1596 O O   . ARG B 2 35  ? 85.68985  54.44329  26.51946  1.000 99.64943  ?  2   ARG D O   1 
ATOM   1597 C CB  . ARG B 2 35  ? 87.34730  55.87930  28.12821  1.000 72.28056  ?  2   ARG D CB  1 
ATOM   1598 N N   . HIS B 2 36  ? 86.19072  52.42681  27.38379  1.000 73.70865  ?  3   HIS D N   1 
ATOM   1599 C CA  . HIS B 2 36  ? 85.18207  51.69131  26.63366  1.000 58.60055  ?  3   HIS D CA  1 
ATOM   1600 C C   . HIS B 2 36  ? 84.04264  51.31242  27.56861  1.000 58.35642  ?  3   HIS D C   1 
ATOM   1601 O O   . HIS B 2 36  ? 84.28193  50.83716  28.68393  1.000 57.09051  ?  3   HIS D O   1 
ATOM   1602 C CB  . HIS B 2 36  ? 85.78254  50.43911  25.99066  1.000 59.81307  ?  3   HIS D CB  1 
ATOM   1603 C CG  . HIS B 2 36  ? 84.85591  49.73981  25.04544  1.000 57.99310  ?  3   HIS D CG  1 
ATOM   1604 N ND1 . HIS B 2 36  ? 84.79989  50.03850  23.70106  1.000 69.26714  ?  3   HIS D ND1 1 
ATOM   1605 C CD2 . HIS B 2 36  ? 83.94791  48.75635  25.25015  1.000 54.29187  ?  3   HIS D CD2 1 
ATOM   1606 C CE1 . HIS B 2 36  ? 83.89869  49.26840  23.11791  1.000 57.29703  ?  3   HIS D CE1 1 
ATOM   1607 N NE2 . HIS B 2 36  ? 83.36677  48.48159  24.03587  1.000 60.32489  ?  3   HIS D NE2 1 
ATOM   1608 N N   . PHE B 2 37  ? 82.80957  51.52236  27.11358  1.000 53.26999  ?  4   PHE D N   1 
ATOM   1609 C CA  . PHE B 2 37  ? 81.62382  51.25809  27.91481  1.000 51.09083  ?  4   PHE D CA  1 
ATOM   1610 C C   . PHE B 2 37  ? 80.62256  50.45513  27.09920  1.000 54.37134  ?  4   PHE D C   1 
ATOM   1611 O O   . PHE B 2 37  ? 80.49808  50.64932  25.88625  1.000 53.23502  ?  4   PHE D O   1 
ATOM   1612 C CB  . PHE B 2 37  ? 80.97708  52.56160  28.39808  1.000 62.35121  ?  4   PHE D CB  1 
ATOM   1613 C CG  . PHE B 2 37  ? 81.90743  53.44885  29.17281  1.000 58.66422  ?  4   PHE D CG  1 
ATOM   1614 C CD1 . PHE B 2 37  ? 82.68897  54.39099  28.52341  1.000 76.56438  ?  4   PHE D CD1 1 
ATOM   1615 C CD2 . PHE B 2 37  ? 82.00023  53.34259  30.55033  1.000 67.63475  ?  4   PHE D CD2 1 
ATOM   1616 C CE1 . PHE B 2 37  ? 83.54733  55.20928  29.23299  1.000 65.62645  ?  4   PHE D CE1 1 
ATOM   1617 C CE2 . PHE B 2 37  ? 82.85611  54.15860  31.26627  1.000 78.17734  ?  4   PHE D CE2 1 
ATOM   1618 C CZ  . PHE B 2 37  ? 83.63050  55.09322  30.60637  1.000 80.86309  ?  4   PHE D CZ  1 
ATOM   1619 N N   . VAL B 2 38  ? 79.91137  49.55286  27.77182  1.000 46.74583  ?  5   VAL D N   1 
ATOM   1620 C CA  . VAL B 2 38  ? 78.89934  48.71136  27.14548  1.000 44.21131  ?  5   VAL D CA  1 
ATOM   1621 C C   . VAL B 2 38  ? 77.59639  48.87869  27.91352  1.000 47.24080  ?  5   VAL D C   1 
ATOM   1622 O O   . VAL B 2 38  ? 77.58319  48.79508  29.14673  1.000 54.03213  ?  5   VAL D O   1 
ATOM   1623 C CB  . VAL B 2 38  ? 79.32036  47.22872  27.11557  1.000 47.03275  ?  5   VAL D CB  1 
ATOM   1624 C CG1 . VAL B 2 38  ? 78.27314  46.39308  26.39250  1.000 47.32371  ?  5   VAL D CG1 1 
ATOM   1625 C CG2 . VAL B 2 38  ? 80.68276  47.07069  26.45889  1.000 46.59208  ?  5   VAL D CG2 1 
ATOM   1626 N N   . TYR B 2 39  ? 76.50674  49.11714  27.18792  1.000 44.58702  ?  6   TYR D N   1 
ATOM   1627 C CA  . TYR B 2 39  ? 75.17656  49.23412  27.76949  1.000 48.74464  ?  6   TYR D CA  1 
ATOM   1628 C C   . TYR B 2 39  ? 74.27817  48.17285  27.15272  1.000 47.23446  ?  6   TYR D C   1 
ATOM   1629 O O   . TYR B 2 39  ? 74.26172  48.00451  25.92873  1.000 49.89277  ?  6   TYR D O   1 
ATOM   1630 C CB  . TYR B 2 39  ? 74.58907  50.63066  27.53833  1.000 46.34278  ?  6   TYR D CB  1 
ATOM   1631 C CG  . TYR B 2 39  ? 73.34358  50.91991  28.34986  1.000 46.17371  ?  6   TYR D CG  1 
ATOM   1632 C CD1 . TYR B 2 39  ? 72.09791  50.45902  27.94025  1.000 46.22204  ?  6   TYR D CD1 1 
ATOM   1633 C CD2 . TYR B 2 39  ? 73.41319  51.66008  29.52275  1.000 47.10209  ?  6   TYR D CD2 1 
ATOM   1634 C CE1 . TYR B 2 39  ? 70.95894  50.72181  28.67870  1.000 42.01830  ?  6   TYR D CE1 1 
ATOM   1635 C CE2 . TYR B 2 39  ? 72.27932  51.92921  30.26694  1.000 41.15939  ?  6   TYR D CE2 1 
ATOM   1636 C CZ  . TYR B 2 39  ? 71.05570  51.45777  29.84034  1.000 42.77986  ?  6   TYR D CZ  1 
ATOM   1637 O OH  . TYR B 2 39  ? 69.92549  51.72343  30.57845  1.000 44.49708  ?  6   TYR D OH  1 
ATOM   1638 N N   . GLN B 2 40  ? 73.53289  47.46301  27.99708  1.000 50.27690  ?  7   GLN D N   1 
ATOM   1639 C CA  . GLN B 2 40  ? 72.64070  46.40447  27.54821  1.000 46.04192  ?  7   GLN D CA  1 
ATOM   1640 C C   . GLN B 2 40  ? 71.24586  46.62355  28.11149  1.000 42.04188  ?  7   GLN D C   1 
ATOM   1641 O O   . GLN B 2 40  ? 71.08707  46.98069  29.28266  1.000 48.71557  ?  7   GLN D O   1 
ATOM   1642 C CB  . GLN B 2 40  ? 73.14127  45.02014  27.97842  1.000 50.80839  ?  7   GLN D CB  1 
ATOM   1643 C CG  . GLN B 2 40  ? 74.59326  44.73418  27.65491  1.000 60.63638  ?  7   GLN D CG  1 
ATOM   1644 C CD  . GLN B 2 40  ? 75.00104  43.33283  28.06147  1.000 69.75024  ?  7   GLN D CD  1 
ATOM   1645 O OE1 . GLN B 2 40  ? 74.18076  42.41434  28.06461  1.000 62.76224  ?  7   GLN D OE1 1 
ATOM   1646 N NE2 . GLN B 2 40  ? 76.27107  43.16155  28.41366  1.000 55.39152  ?  7   GLN D NE2 1 
ATOM   1647 N N   . PHE B 2 41  ? 70.23879  46.40338  27.27136  1.000 39.29041  ?  8   PHE D N   1 
ATOM   1648 C CA  . PHE B 2 41  ? 68.85166  46.33917  27.70533  1.000 39.60013  ?  8   PHE D CA  1 
ATOM   1649 C C   . PHE B 2 41  ? 68.19866  45.11920  27.07737  1.000 34.09385  ?  8   PHE D C   1 
ATOM   1650 O O   . PHE B 2 41  ? 68.46723  44.78903  25.91841  1.000 45.45076  ?  8   PHE D O   1 
ATOM   1651 C CB  . PHE B 2 41  ? 68.06448  47.60079  27.32908  1.000 37.22452  ?  8   PHE D CB  1 
ATOM   1652 C CG  . PHE B 2 41  ? 66.59391  47.50019  27.62628  1.000 51.00106  ?  8   PHE D CG  1 
ATOM   1653 C CD1 . PHE B 2 41  ? 66.11912  47.69859  28.91273  1.000 55.89734  ?  8   PHE D CD1 1 
ATOM   1654 C CD2 . PHE B 2 41  ? 65.68798  47.19343  26.62315  1.000 41.58724  ?  8   PHE D CD2 1 
ATOM   1655 C CE1 . PHE B 2 41  ? 64.76860  47.59881  29.19302  1.000 34.34244  ?  8   PHE D CE1 1 
ATOM   1656 C CE2 . PHE B 2 41  ? 64.33735  47.09145  26.89703  1.000 46.70407  ?  8   PHE D CE2 1 
ATOM   1657 C CZ  . PHE B 2 41  ? 63.87718  47.29472  28.18404  1.000 45.95235  ?  8   PHE D CZ  1 
ATOM   1658 N N   . MET B 2 42  ? 67.33842  44.45418  27.84353  1.000 38.54681  ?  9   MET D N   1 
ATOM   1659 C CA  . MET B 2 42  ? 66.66459  43.26031  27.35423  1.000 54.42598  ?  9   MET D CA  1 
ATOM   1660 C C   . MET B 2 42  ? 65.33792  43.08929  28.07652  1.000 49.60890  ?  9   MET D C   1 
ATOM   1661 O O   . MET B 2 42  ? 65.26661  43.24007  29.29997  1.000 51.46804  ?  9   MET D O   1 
ATOM   1662 C CB  . MET B 2 42  ? 67.54437  42.01815  27.53782  1.000 50.25277  ?  9   MET D CB  1 
ATOM   1663 C CG  . MET B 2 42  ? 68.17054  41.89099  28.91673  1.000 64.08957  ?  9   MET D CG  1 
ATOM   1664 S SD  . MET B 2 42  ? 69.52405  40.69952  28.95288  1.000 74.26405  ?  9   MET D SD  1 
ATOM   1665 C CE  . MET B 2 42  ? 68.68983  39.22244  28.37996  1.000 67.51531  ?  9   MET D CE  1 
ATOM   1666 N N   . GLY B 2 43  ? 64.29324  42.78725  27.31017  1.000 41.83696  ?  10  GLY D N   1 
ATOM   1667 C CA  . GLY B 2 43  ? 62.99231  42.48196  27.86987  1.000 45.45295  ?  10  GLY D CA  1 
ATOM   1668 C C   . GLY B 2 43  ? 62.63025  41.02760  27.65785  1.000 51.11703  ?  10  GLY D C   1 
ATOM   1669 O O   . GLY B 2 43  ? 62.59925  40.55025  26.51937  1.000 47.29285  ?  10  GLY D O   1 
ATOM   1670 N N   . GLU B 2 44  ? 62.34845  40.31437  28.74382  1.000 55.47344  ?  11  GLU D N   1 
ATOM   1671 C CA  . GLU B 2 44  ? 62.17206  38.86907  28.71634  1.000 46.07604  ?  11  GLU D CA  1 
ATOM   1672 C C   . GLU B 2 44  ? 60.73324  38.50517  29.05856  1.000 51.57855  ?  11  GLU D C   1 
ATOM   1673 O O   . GLU B 2 44  ? 60.15840  39.04610  30.00966  1.000 58.81498  ?  11  GLU D O   1 
ATOM   1674 C CB  . GLU B 2 44  ? 63.13601  38.19690  29.69425  1.000 52.55059  ?  11  GLU D CB  1 
ATOM   1675 C CG  . GLU B 2 44  ? 64.59547  38.57276  29.47225  1.000 52.34625  ?  11  GLU D CG  1 
ATOM   1676 C CD  . GLU B 2 44  ? 65.50440  38.07228  30.57777  1.000 71.31003  ?  11  GLU D CD  1 
ATOM   1677 O OE1 . GLU B 2 44  ? 64.98463  37.69237  31.64746  1.000 65.84775  ?  11  GLU D OE1 1 
ATOM   1678 O OE2 . GLU B 2 44  ? 66.73727  38.05666  30.37810  1.000 81.34687  -1 11  GLU D OE2 1 
ATOM   1679 N N   . CYS B 2 45  ? 60.15968  37.58635  28.28435  1.000 53.79666  ?  12  CYS D N   1 
ATOM   1680 C CA  . CYS B 2 45  ? 58.80888  37.08369  28.50644  1.000 42.60632  ?  12  CYS D CA  1 
ATOM   1681 C C   . CYS B 2 45  ? 58.88891  35.59695  28.81561  1.000 43.29052  ?  12  CYS D C   1 
ATOM   1682 O O   . CYS B 2 45  ? 59.31587  34.80708  27.96675  1.000 58.35414  ?  12  CYS D O   1 
ATOM   1683 C CB  . CYS B 2 45  ? 57.91980  37.32214  27.28459  1.000 44.50250  ?  12  CYS D CB  1 
ATOM   1684 S SG  . CYS B 2 45  ? 57.67146  39.04930  26.82705  1.000 61.22687  ?  12  CYS D SG  1 
ATOM   1685 N N   . TYR B 2 46  ? 58.47300  35.21748  30.01959  1.000 53.74102  ?  13  TYR D N   1 
ATOM   1686 C CA  . TYR B 2 46  ? 58.51197  33.82956  30.46135  1.000 49.12608  ?  13  TYR D CA  1 
ATOM   1687 C C   . TYR B 2 46  ? 57.10641  33.24448  30.40257  1.000 56.18626  ?  13  TYR D C   1 
ATOM   1688 O O   . TYR B 2 46  ? 56.17622  33.79243  31.00307  1.000 59.05839  ?  13  TYR D O   1 
ATOM   1689 C CB  . TYR B 2 46  ? 59.08650  33.72683  31.87331  1.000 57.78931  ?  13  TYR D CB  1 
ATOM   1690 C CG  . TYR B 2 46  ? 60.51562  34.20812  31.97485  1.000 59.00308  ?  13  TYR D CG  1 
ATOM   1691 C CD1 . TYR B 2 46  ? 60.80317  35.53862  32.24859  1.000 55.39328  ?  13  TYR D CD1 1 
ATOM   1692 C CD2 . TYR B 2 46  ? 61.57748  33.33334  31.78952  1.000 46.84325  ?  13  TYR D CD2 1 
ATOM   1693 C CE1 . TYR B 2 46  ? 62.10763  35.98316  32.33830  1.000 60.02782  ?  13  TYR D CE1 1 
ATOM   1694 C CE2 . TYR B 2 46  ? 62.88562  33.76877  31.87773  1.000 60.25335  ?  13  TYR D CE2 1 
ATOM   1695 C CZ  . TYR B 2 46  ? 63.14484  35.09423  32.15211  1.000 65.61789  ?  13  TYR D CZ  1 
ATOM   1696 O OH  . TYR B 2 46  ? 64.44571  35.53206  32.24076  1.000 67.48172  ?  13  TYR D OH  1 
ATOM   1697 N N   . PHE B 2 47  ? 56.95795  32.13517  29.68236  1.000 49.25488  ?  14  PHE D N   1 
ATOM   1698 C CA  . PHE B 2 47  ? 55.67291  31.48157  29.48318  1.000 53.89813  ?  14  PHE D CA  1 
ATOM   1699 C C   . PHE B 2 47  ? 55.70018  30.09078  30.10052  1.000 59.88331  ?  14  PHE D C   1 
ATOM   1700 O O   . PHE B 2 47  ? 56.68626  29.36024  29.96286  1.000 65.59872  ?  14  PHE D O   1 
ATOM   1701 C CB  . PHE B 2 47  ? 55.33123  31.38099  27.99309  1.000 65.14023  ?  14  PHE D CB  1 
ATOM   1702 C CG  . PHE B 2 47  ? 55.37575  32.69618  27.26871  1.000 56.76765  ?  14  PHE D CG  1 
ATOM   1703 C CD1 . PHE B 2 47  ? 54.29924  33.56718  27.31772  1.000 55.06949  ?  14  PHE D CD1 1 
ATOM   1704 C CD2 . PHE B 2 47  ? 56.49188  33.05808  26.53176  1.000 54.19629  ?  14  PHE D CD2 1 
ATOM   1705 C CE1 . PHE B 2 47  ? 54.33730  34.77719  26.64992  1.000 52.21495  ?  14  PHE D CE1 1 
ATOM   1706 C CE2 . PHE B 2 47  ? 56.53628  34.26591  25.86095  1.000 49.22126  ?  14  PHE D CE2 1 
ATOM   1707 C CZ  . PHE B 2 47  ? 55.45741  35.12645  25.91996  1.000 55.07756  ?  14  PHE D CZ  1 
ATOM   1708 N N   . THR B 2 48  ? 54.60685  29.72260  30.77294  1.000 67.21583  ?  15  THR D N   1 
ATOM   1709 C CA  . THR B 2 48  ? 54.51137  28.42210  31.43302  1.000 76.47923  ?  15  THR D CA  1 
ATOM   1710 C C   . THR B 2 48  ? 53.41557  27.57060  30.80366  1.000 89.07639  ?  15  THR D C   1 
ATOM   1711 O O   . THR B 2 48  ? 53.72890  26.61177  30.09499  1.000 114.25548 ?  15  THR D O   1 
ATOM   1712 C CB  . THR B 2 48  ? 54.28922  28.60858  32.93481  1.000 71.76841  ?  15  THR D CB  1 
ATOM   1713 O OG1 . THR B 2 48  ? 55.20556  29.59117  33.43380  1.000 99.28950  ?  15  THR D OG1 1 
ATOM   1714 C CG2 . THR B 2 48  ? 54.52084  27.29999  33.67078  1.000 65.03327  ?  15  THR D CG2 1 
ATOM   1715 N N   . ASN B 2 49  ? 52.14369  27.87815  31.03834  1.000 60.74175  ?  16  ASN D N   1 
ATOM   1716 C CA  . ASN B 2 49  ? 51.04171  27.16071  30.39397  1.000 91.54889  ?  16  ASN D CA  1 
ATOM   1717 C C   . ASN B 2 49  ? 50.54458  27.94525  29.18122  1.000 96.28234  ?  16  ASN D C   1 
ATOM   1718 O O   . ASN B 2 49  ? 49.37584  28.31678  29.07280  1.000 113.36915 ?  16  ASN D O   1 
ATOM   1719 C CB  . ASN B 2 49  ? 49.91457  26.90744  31.39358  1.000 109.53976 ?  16  ASN D CB  1 
ATOM   1720 C CG  . ASN B 2 49  ? 49.43455  25.46398  31.38325  1.000 113.66982 ?  16  ASN D CG  1 
ATOM   1721 O OD1 . ASN B 2 49  ? 50.00950  24.61613  30.70031  1.000 105.57930 ?  16  ASN D OD1 1 
ATOM   1722 N ND2 . ASN B 2 49  ? 48.37526  25.18079  32.14798  1.000 132.36188 ?  16  ASN D ND2 1 
ATOM   1723 N N   . GLY B 2 50  ? 51.46712  28.19619  28.25618  1.000 72.91672  ?  17  GLY D N   1 
ATOM   1724 C CA  . GLY B 2 50  ? 51.17727  29.05147  27.12367  1.000 73.50832  ?  17  GLY D CA  1 
ATOM   1725 C C   . GLY B 2 50  ? 51.13360  30.50807  27.53375  1.000 67.78142  ?  17  GLY D C   1 
ATOM   1726 O O   . GLY B 2 50  ? 52.17568  31.15998  27.64279  1.000 90.21308  ?  17  GLY D O   1 
ATOM   1727 N N   . THR B 2 51  ? 49.93095  31.03017  27.77248  1.000 65.46621  ?  18  THR D N   1 
ATOM   1728 C CA  . THR B 2 51  ? 49.75858  32.38754  28.27544  1.000 65.60091  ?  18  THR D CA  1 
ATOM   1729 C C   . THR B 2 51  ? 49.05157  32.41880  29.62389  1.000 72.94136  ?  18  THR D C   1 
ATOM   1730 O O   . THR B 2 51  ? 48.74574  33.50643  30.12738  1.000 75.27755  ?  18  THR D O   1 
ATOM   1731 C CB  . THR B 2 51  ? 48.99158  33.24476  27.26433  1.000 59.03525  ?  18  THR D CB  1 
ATOM   1732 O OG1 . THR B 2 51  ? 47.76567  32.59184  26.91152  1.000 87.11352  ?  18  THR D OG1 1 
ATOM   1733 C CG2 . THR B 2 51  ? 49.82744  33.46241  26.01442  1.000 51.06062  ?  18  THR D CG2 1 
ATOM   1734 N N   . GLN B 2 52  ? 48.78440  31.25580  30.22203  1.000 65.14082  ?  19  GLN D N   1 
ATOM   1735 C CA  . GLN B 2 52  ? 48.13627  31.21677  31.52647  1.000 71.59583  ?  19  GLN D CA  1 
ATOM   1736 C C   . GLN B 2 52  ? 49.05650  31.69195  32.64119  1.000 61.16632  ?  19  GLN D C   1 
ATOM   1737 O O   . GLN B 2 52  ? 48.56750  32.10942  33.69604  1.000 81.00583  ?  19  GLN D O   1 
ATOM   1738 C CB  . GLN B 2 52  ? 47.64331  29.80049  31.82063  1.000 84.82945  ?  19  GLN D CB  1 
ATOM   1739 C CG  . GLN B 2 52  ? 46.71304  29.24872  30.75554  1.000 99.42323  ?  19  GLN D CG  1 
ATOM   1740 C CD  . GLN B 2 52  ? 46.42959  27.77216  30.93406  1.000 119.98814 ?  19  GLN D CD  1 
ATOM   1741 O OE1 . GLN B 2 52  ? 46.70260  27.19737  31.98821  1.000 108.19921 ?  19  GLN D OE1 1 
ATOM   1742 N NE2 . GLN B 2 52  ? 45.88306  27.14710  29.89748  1.000 112.44126 ?  19  GLN D NE2 1 
ATOM   1743 N N   . ARG B 2 53  ? 50.37105  31.63638  32.43354  1.000 67.06974  ?  20  ARG D N   1 
ATOM   1744 C CA  . ARG B 2 53  ? 51.34483  32.13120  33.40664  1.000 58.05414  ?  20  ARG D CA  1 
ATOM   1745 C C   . ARG B 2 53  ? 52.44462  32.84842  32.63157  1.000 54.00779  ?  20  ARG D C   1 
ATOM   1746 O O   . ARG B 2 53  ? 53.33561  32.20605  32.06800  1.000 77.87059  ?  20  ARG D O   1 
ATOM   1747 C CB  . ARG B 2 53  ? 51.90972  31.00150  34.25879  1.000 60.41690  ?  20  ARG D CB  1 
ATOM   1748 C CG  . ARG B 2 53  ? 51.34361  30.95555  35.66508  1.000 95.68481  ?  20  ARG D CG  1 
ATOM   1749 C CD  . ARG B 2 53  ? 51.56559  32.28123  36.37221  1.000 113.26106 ?  20  ARG D CD  1 
ATOM   1750 N NE  . ARG B 2 53  ? 50.92010  32.32661  37.67822  1.000 110.45629 ?  20  ARG D NE  1 
ATOM   1751 C CZ  . ARG B 2 53  ? 50.85693  33.40848  38.44200  1.000 100.75762 ?  20  ARG D CZ  1 
ATOM   1752 N NH1 . ARG B 2 53  ? 51.38977  34.55725  38.05863  1.000 104.44375 ?  20  ARG D NH1 1 
ATOM   1753 N NH2 . ARG B 2 53  ? 50.24151  33.33708  39.61828  1.000 99.58095  ?  20  ARG D NH2 1 
ATOM   1754 N N   . ILE B 2 54  ? 52.37669  34.17594  32.60416  1.000 54.68743  ?  21  ILE D N   1 
ATOM   1755 C CA  . ILE B 2 54  ? 53.35223  35.00755  31.91084  1.000 61.35179  ?  21  ILE D CA  1 
ATOM   1756 C C   . ILE B 2 54  ? 54.09464  35.84060  32.94397  1.000 51.54131  ?  21  ILE D C   1 
ATOM   1757 O O   . ILE B 2 54  ? 53.47077  36.52522  33.76412  1.000 53.89718  ?  21  ILE D O   1 
ATOM   1758 C CB  . ILE B 2 54  ? 52.68416  35.90923  30.85880  1.000 51.81037  ?  21  ILE D CB  1 
ATOM   1759 C CG1 . ILE B 2 54  ? 51.95009  35.06314  29.81750  1.000 62.46770  ?  21  ILE D CG1 1 
ATOM   1760 C CG2 . ILE B 2 54  ? 53.71890  36.79893  30.19058  1.000 44.51451  ?  21  ILE D CG2 1 
ATOM   1761 C CD1 . ILE B 2 54  ? 51.25002  35.88018  28.75432  1.000 58.70782  ?  21  ILE D CD1 1 
ATOM   1762 N N   . ARG B 2 55  ? 55.42266  35.77707  32.90886  1.000 49.07930  ?  22  ARG D N   1 
ATOM   1763 C CA  . ARG B 2 55  ? 56.27364  36.60993  33.74601  1.000 59.80838  ?  22  ARG D CA  1 
ATOM   1764 C C   . ARG B 2 55  ? 57.09929  37.51659  32.84635  1.000 56.04217  ?  22  ARG D C   1 
ATOM   1765 O O   . ARG B 2 55  ? 57.69306  37.05274  31.86718  1.000 61.53959  ?  22  ARG D O   1 
ATOM   1766 C CB  . ARG B 2 55  ? 57.18119  35.76409  34.64083  1.000 48.82836  ?  22  ARG D CB  1 
ATOM   1767 C CG  . ARG B 2 55  ? 57.97540  36.58145  35.64332  1.000 49.34321  ?  22  ARG D CG  1 
ATOM   1768 C CD  . ARG B 2 55  ? 58.73894  35.69165  36.60533  1.000 63.31821  ?  22  ARG D CD  1 
ATOM   1769 N NE  . ARG B 2 55  ? 59.60422  36.46769  37.48478  1.000 57.87254  ?  22  ARG D NE  1 
ATOM   1770 C CZ  . ARG B 2 55  ? 60.37835  35.94549  38.42556  1.000 56.32406  ?  22  ARG D CZ  1 
ATOM   1771 N NH1 . ARG B 2 55  ? 60.41273  34.64164  38.64739  1.000 79.27015  ?  22  ARG D NH1 1 
ATOM   1772 N NH2 . ARG B 2 55  ? 61.13719  36.75165  39.16218  1.000 55.23913  ?  22  ARG D NH2 1 
ATOM   1773 N N   . TYR B 2 56  ? 57.13336  38.80361  33.18057  1.000 58.41345  ?  23  TYR D N   1 
ATOM   1774 C CA  . TYR B 2 56  ? 57.72075  39.83275  32.33192  1.000 60.70875  ?  23  TYR D CA  1 
ATOM   1775 C C   . TYR B 2 56  ? 58.80241  40.56396  33.11399  1.000 47.89101  ?  23  TYR D C   1 
ATOM   1776 O O   . TYR B 2 56  ? 58.53374  41.11036  34.18949  1.000 47.15087  ?  23  TYR D O   1 
ATOM   1777 C CB  . TYR B 2 56  ? 56.63576  40.79523  31.84393  1.000 60.15674  ?  23  TYR D CB  1 
ATOM   1778 C CG  . TYR B 2 56  ? 57.14130  42.07504  31.22842  1.000 51.56071  ?  23  TYR D CG  1 
ATOM   1779 C CD1 . TYR B 2 56  ? 57.98762  42.05699  30.12869  1.000 62.80264  ?  23  TYR D CD1 1 
ATOM   1780 C CD2 . TYR B 2 56  ? 56.74783  43.30600  31.73339  1.000 58.07607  ?  23  TYR D CD2 1 
ATOM   1781 C CE1 . TYR B 2 56  ? 58.44243  43.23175  29.56241  1.000 52.78885  ?  23  TYR D CE1 1 
ATOM   1782 C CE2 . TYR B 2 56  ? 57.19501  44.48280  31.17404  1.000 59.46666  ?  23  TYR D CE2 1 
ATOM   1783 C CZ  . TYR B 2 56  ? 58.04022  44.44062  30.08902  1.000 54.47556  ?  23  TYR D CZ  1 
ATOM   1784 O OH  . TYR B 2 56  ? 58.48362  45.61496  29.53238  1.000 69.52545  ?  23  TYR D OH  1 
ATOM   1785 N N   . VAL B 2 57  ? 60.02188  40.56656  32.57733  1.000 47.16879  ?  24  VAL D N   1 
ATOM   1786 C CA  . VAL B 2 57  ? 61.18482  41.13321  33.25383  1.000 53.74991  ?  24  VAL D CA  1 
ATOM   1787 C C   . VAL B 2 57  ? 61.98329  41.96017  32.25490  1.000 55.80794  ?  24  VAL D C   1 
ATOM   1788 O O   . VAL B 2 57  ? 62.26182  41.49967  31.14268  1.000 52.11167  ?  24  VAL D O   1 
ATOM   1789 C CB  . VAL B 2 57  ? 62.07864  40.03768  33.87219  1.000 58.15828  ?  24  VAL D CB  1 
ATOM   1790 C CG1 . VAL B 2 57  ? 63.33411  40.64780  34.47800  1.000 52.43959  ?  24  VAL D CG1 1 
ATOM   1791 C CG2 . VAL B 2 57  ? 61.31334  39.24107  34.91911  1.000 49.87801  ?  24  VAL D CG2 1 
ATOM   1792 N N   . THR B 2 58  ? 62.35055  43.17864  32.64925  1.000 49.80252  ?  25  THR D N   1 
ATOM   1793 C CA  . THR B 2 58  ? 63.27516  44.00886  31.89107  1.000 55.10171  ?  25  THR D CA  1 
ATOM   1794 C C   . THR B 2 58  ? 64.53907  44.23045  32.70939  1.000 48.54101  ?  25  THR D C   1 
ATOM   1795 O O   . THR B 2 58  ? 64.49487  44.30184  33.94087  1.000 45.51985  ?  25  THR D O   1 
ATOM   1796 C CB  . THR B 2 58  ? 62.66357  45.36578  31.52134  1.000 46.71583  ?  25  THR D CB  1 
ATOM   1797 O OG1 . THR B 2 58  ? 62.42476  46.12704  32.71147  1.000 48.96612  ?  25  THR D OG1 1 
ATOM   1798 C CG2 . THR B 2 58  ? 61.35971  45.17367  30.77618  1.000 49.82133  ?  25  THR D CG2 1 
ATOM   1799 N N   . ARG B 2 59  ? 65.67013  44.33893  32.01614  1.000 43.51062  ?  26  ARG D N   1 
ATOM   1800 C CA  . ARG B 2 59  ? 66.96766  44.47209  32.66431  1.000 49.67204  ?  26  ARG D CA  1 
ATOM   1801 C C   . ARG B 2 59  ? 67.75325  45.60252  32.01757  1.000 48.04520  ?  26  ARG D C   1 
ATOM   1802 O O   . ARG B 2 59  ? 67.85341  45.67228  30.78814  1.000 42.53603  ?  26  ARG D O   1 
ATOM   1803 C CB  . ARG B 2 59  ? 67.76020  43.16250  32.58480  1.000 56.03842  ?  26  ARG D CB  1 
ATOM   1804 C CG  . ARG B 2 59  ? 67.01406  41.95754  33.12903  1.000 61.27131  ?  26  ARG D CG  1 
ATOM   1805 C CD  . ARG B 2 59  ? 67.83228  40.68488  33.01279  1.000 57.02963  ?  26  ARG D CD  1 
ATOM   1806 N NE  . ARG B 2 59  ? 67.01804  39.50587  33.28078  1.000 56.57680  ?  26  ARG D NE  1 
ATOM   1807 C CZ  . ARG B 2 59  ? 66.74544  39.04357  34.49289  1.000 46.55991  ?  26  ARG D CZ  1 
ATOM   1808 N NH1 . ARG B 2 59  ? 67.21753  39.63235  35.57950  1.000 52.01901  ?  26  ARG D NH1 1 
ATOM   1809 N NH2 . ARG B 2 59  ? 65.97736  37.96517  34.61812  1.000 64.34113  ?  26  ARG D NH2 1 
ATOM   1810 N N   . TYR B 2 60  ? 68.30405  46.48246  32.84907  1.000 45.16631  ?  27  TYR D N   1 
ATOM   1811 C CA  . TYR B 2 60  ? 69.17938  47.56274  32.41306  1.000 38.50437  ?  27  TYR D CA  1 
ATOM   1812 C C   . TYR B 2 60  ? 70.58573  47.25447  32.91072  1.000 46.84192  ?  27  TYR D C   1 
ATOM   1813 O O   . TYR B 2 60  ? 70.82283  47.21817  34.12341  1.000 48.25262  ?  27  TYR D O   1 
ATOM   1814 C CB  . TYR B 2 60  ? 68.69833  48.91206  32.94884  1.000 41.77048  ?  27  TYR D CB  1 
ATOM   1815 C CG  . TYR B 2 60  ? 67.31775  49.32524  32.48334  1.000 49.81864  ?  27  TYR D CG  1 
ATOM   1816 C CD1 . TYR B 2 60  ? 66.17548  48.80476  33.07890  1.000 40.39238  ?  27  TYR D CD1 1 
ATOM   1817 C CD2 . TYR B 2 60  ? 67.15769  50.25133  31.46127  1.000 46.09124  ?  27  TYR D CD2 1 
ATOM   1818 C CE1 . TYR B 2 60  ? 64.91428  49.18500  32.66086  1.000 41.35591  ?  27  TYR D CE1 1 
ATOM   1819 C CE2 . TYR B 2 60  ? 65.90068  50.63875  31.03749  1.000 45.08515  ?  27  TYR D CE2 1 
ATOM   1820 C CZ  . TYR B 2 60  ? 64.78299  50.10305  31.64020  1.000 49.88307  ?  27  TYR D CZ  1 
ATOM   1821 O OH  . TYR B 2 60  ? 63.53044  50.48821  31.21920  1.000 50.58657  ?  27  TYR D OH  1 
ATOM   1822 N N   . ILE B 2 61  ? 71.51141  47.02756  31.98199  1.000 40.81898  ?  28  ILE D N   1 
ATOM   1823 C CA  . ILE B 2 61  ? 72.86696  46.59896  32.30767  1.000 46.60693  ?  28  ILE D CA  1 
ATOM   1824 C C   . ILE B 2 61  ? 73.84368  47.68183  31.87205  1.000 41.30051  ?  28  ILE D C   1 
ATOM   1825 O O   . ILE B 2 61  ? 73.75987  48.18679  30.74644  1.000 46.44024  ?  28  ILE D O   1 
ATOM   1826 C CB  . ILE B 2 61  ? 73.21557  45.25155  31.64628  1.000 52.74847  ?  28  ILE D CB  1 
ATOM   1827 C CG1 . ILE B 2 61  ? 72.33460  44.12943  32.20159  1.000 52.32159  ?  28  ILE D CG1 1 
ATOM   1828 C CG2 . ILE B 2 61  ? 74.68480  44.91322  31.85349  1.000 65.44941  ?  28  ILE D CG2 1 
ATOM   1829 C CD1 . ILE B 2 61  ? 71.07669  43.87999  31.40289  1.000 44.06132  ?  28  ILE D CD1 1 
ATOM   1830 N N   . TYR B 2 62  ? 74.76743  48.03336  32.76475  1.000 45.82700  ?  29  TYR D N   1 
ATOM   1831 C CA  . TYR B 2 62  ? 75.83637  48.98507  32.47745  1.000 47.18569  ?  29  TYR D CA  1 
ATOM   1832 C C   . TYR B 2 62  ? 77.15672  48.35020  32.89145  1.000 46.96179  ?  29  TYR D C   1 
ATOM   1833 O O   . TYR B 2 62  ? 77.44232  48.23492  34.08803  1.000 59.53841  ?  29  TYR D O   1 
ATOM   1834 C CB  . TYR B 2 62  ? 75.60979  50.30875  33.20905  1.000 46.39599  ?  29  TYR D CB  1 
ATOM   1835 C CG  . TYR B 2 62  ? 76.79503  51.24868  33.17091  1.000 55.31457  ?  29  TYR D CG  1 
ATOM   1836 C CD1 . TYR B 2 62  ? 77.08989  51.98144  32.02878  1.000 59.27189  ?  29  TYR D CD1 1 
ATOM   1837 C CD2 . TYR B 2 62  ? 77.61418  51.40948  34.28126  1.000 52.40975  ?  29  TYR D CD2 1 
ATOM   1838 C CE1 . TYR B 2 62  ? 78.17162  52.84175  31.99134  1.000 56.24507  ?  29  TYR D CE1 1 
ATOM   1839 C CE2 . TYR B 2 62  ? 78.69717  52.26705  34.25278  1.000 53.65180  ?  29  TYR D CE2 1 
ATOM   1840 C CZ  . TYR B 2 62  ? 78.97099  52.98065  33.10585  1.000 60.18944  ?  29  TYR D CZ  1 
ATOM   1841 O OH  . TYR B 2 62  ? 80.04795  53.83650  33.07331  1.000 72.09996  ?  29  TYR D OH  1 
ATOM   1842 N N   . ASN B 2 63  ? 77.95180  47.93305  31.90386  1.000 49.83845  ?  30  ASN D N   1 
ATOM   1843 C CA  . ASN B 2 63  ? 79.25756  47.31052  32.13135  1.000 73.65111  ?  30  ASN D CA  1 
ATOM   1844 C C   . ASN B 2 63  ? 79.12888  46.05159  32.99341  1.000 75.43686  ?  30  ASN D C   1 
ATOM   1845 O O   . ASN B 2 63  ? 79.68749  45.95100  34.08845  1.000 79.97231  ?  30  ASN D O   1 
ATOM   1846 C CB  . ASN B 2 63  ? 80.24083  48.30974  32.75213  1.000 70.52054  ?  30  ASN D CB  1 
ATOM   1847 C CG  . ASN B 2 63  ? 80.85757  49.23540  31.72377  1.000 75.41154  ?  30  ASN D CG  1 
ATOM   1848 O OD1 . ASN B 2 63  ? 80.55998  49.14650  30.53232  1.000 72.67538  ?  30  ASN D OD1 1 
ATOM   1849 N ND2 . ASN B 2 63  ? 81.72007  50.13463  32.18084  1.000 82.07377  ?  30  ASN D ND2 1 
ATOM   1850 N N   . ARG B 2 64  ? 78.37187  45.08479  32.46831  1.000 65.48967  ?  31  ARG D N   1 
ATOM   1851 C CA  . ARG B 2 64  ? 78.16576  43.78494  33.11293  1.000 66.93766  ?  31  ARG D CA  1 
ATOM   1852 C C   . ARG B 2 64  ? 77.58851  43.92276  34.51851  1.000 53.42854  ?  31  ARG D C   1 
ATOM   1853 O O   . ARG B 2 64  ? 77.79345  43.05545  35.37114  1.000 76.13034  ?  31  ARG D O   1 
ATOM   1854 C CB  . ARG B 2 64  ? 79.46153  42.96868  33.15764  1.000 56.49923  ?  31  ARG D CB  1 
ATOM   1855 C CG  . ARG B 2 64  ? 80.02036  42.60679  31.79719  1.000 52.39224  ?  31  ARG D CG  1 
ATOM   1856 C CD  . ARG B 2 64  ? 81.16107  41.61042  31.91850  1.000 54.94302  ?  31  ARG D CD  1 
ATOM   1857 N NE  . ARG B 2 64  ? 80.69946  40.31271  32.39632  1.000 54.47159  ?  31  ARG D NE  1 
ATOM   1858 C CZ  . ARG B 2 64  ? 81.47757  39.25007  32.54800  1.000 62.35994  ?  31  ARG D CZ  1 
ATOM   1859 N NH1 . ARG B 2 64  ? 82.77146  39.29653  32.27692  1.000 69.82614  ?  31  ARG D NH1 1 
ATOM   1860 N NH2 . ARG B 2 64  ? 80.94378  38.11159  32.98108  1.000 84.30978  ?  31  ARG D NH2 1 
ATOM   1861 N N   . GLU B 2 65  ? 76.86181  45.00786  34.77738  1.000 56.50204  ?  32  GLU D N   1 
ATOM   1862 C CA  . GLU B 2 65  ? 76.28239  45.25189  36.09787  1.000 60.97607  ?  32  GLU D CA  1 
ATOM   1863 C C   . GLU B 2 65  ? 74.84234  45.71621  35.90822  1.000 63.21297  ?  32  GLU D C   1 
ATOM   1864 O O   . GLU B 2 65  ? 74.59650  46.87276  35.55275  1.000 65.95353  ?  32  GLU D O   1 
ATOM   1865 C CB  . GLU B 2 65  ? 77.09770  46.27254  36.88274  1.000 70.23048  ?  32  GLU D CB  1 
ATOM   1866 C CG  . GLU B 2 65  ? 76.49942  46.63183  38.23351  1.000 80.77981  ?  32  GLU D CG  1 
ATOM   1867 C CD  . GLU B 2 65  ? 77.44000  47.45803  39.08703  1.000 102.33953 ?  32  GLU D CD  1 
ATOM   1868 O OE1 . GLU B 2 65  ? 78.65257  47.15736  39.09948  1.000 106.75590 ?  32  GLU D OE1 1 
ATOM   1869 O OE2 . GLU B 2 65  ? 76.96741  48.41118  39.74152  1.000 103.75044 -1 32  GLU D OE2 1 
ATOM   1870 N N   . GLU B 2 66  ? 73.89960  44.80705  36.13710  1.000 62.18135  ?  33  GLU D N   1 
ATOM   1871 C CA  . GLU B 2 66  ? 72.48901  45.16568  36.13792  1.000 55.53529  ?  33  GLU D CA  1 
ATOM   1872 C C   . GLU B 2 66  ? 72.20879  46.12520  37.28602  1.000 62.23457  ?  33  GLU D C   1 
ATOM   1873 O O   . GLU B 2 66  ? 72.50017  45.81740  38.44575  1.000 67.59104  ?  33  GLU D O   1 
ATOM   1874 C CB  . GLU B 2 66  ? 71.63609  43.90442  36.26464  1.000 55.19751  ?  33  GLU D CB  1 
ATOM   1875 C CG  . GLU B 2 66  ? 70.13816  44.14221  36.24972  1.000 65.01516  ?  33  GLU D CG  1 
ATOM   1876 C CD  . GLU B 2 66  ? 69.35237  42.86518  36.47896  1.000 74.41895  ?  33  GLU D CD  1 
ATOM   1877 O OE1 . GLU B 2 66  ? 69.95474  41.87134  36.93817  1.000 75.73896  ?  33  GLU D OE1 1 
ATOM   1878 O OE2 . GLU B 2 66  ? 68.13515  42.85213  36.19873  1.000 63.35124  -1 33  GLU D OE2 1 
ATOM   1879 N N   . TYR B 2 67  ? 71.65802  47.29812  36.96448  1.000 57.52871  ?  34  TYR D N   1 
ATOM   1880 C CA  . TYR B 2 67  ? 71.41024  48.32311  37.96785  1.000 64.88359  ?  34  TYR D CA  1 
ATOM   1881 C C   . TYR B 2 67  ? 69.94114  48.67605  38.15149  1.000 54.40876  ?  34  TYR D C   1 
ATOM   1882 O O   . TYR B 2 67  ? 69.58273  49.19004  39.21662  1.000 62.18832  ?  34  TYR D O   1 
ATOM   1883 C CB  . TYR B 2 67  ? 72.19650  49.60434  37.63652  1.000 54.11326  ?  34  TYR D CB  1 
ATOM   1884 C CG  . TYR B 2 67  ? 71.68507  50.36822  36.43673  1.000 48.28798  ?  34  TYR D CG  1 
ATOM   1885 C CD1 . TYR B 2 67  ? 71.96915  49.94676  35.14537  1.000 45.38645  ?  34  TYR D CD1 1 
ATOM   1886 C CD2 . TYR B 2 67  ? 70.93271  51.52340  36.59749  1.000 53.93519  ?  34  TYR D CD2 1 
ATOM   1887 C CE1 . TYR B 2 67  ? 71.50454  50.64704  34.04814  1.000 48.40496  ?  34  TYR D CE1 1 
ATOM   1888 C CE2 . TYR B 2 67  ? 70.46332  52.23019  35.50866  1.000 46.67831  ?  34  TYR D CE2 1 
ATOM   1889 C CZ  . TYR B 2 67  ? 70.75048  51.78821  34.23643  1.000 53.67388  ?  34  TYR D CZ  1 
ATOM   1890 O OH  . TYR B 2 67  ? 70.28516  52.49345  33.14997  1.000 51.88599  ?  34  TYR D OH  1 
ATOM   1891 N N   . VAL B 2 68  ? 69.08795  48.42022  37.16185  1.000 54.67824  ?  35  VAL D N   1 
ATOM   1892 C CA  . VAL B 2 68  ? 67.64707  48.62267  37.28479  1.000 61.42880  ?  35  VAL D CA  1 
ATOM   1893 C C   . VAL B 2 68  ? 66.94331  47.44079  36.63397  1.000 53.80061  ?  35  VAL D C   1 
ATOM   1894 O O   . VAL B 2 68  ? 67.29752  47.03723  35.52126  1.000 46.95727  ?  35  VAL D O   1 
ATOM   1895 C CB  . VAL B 2 68  ? 67.18353  49.94623  36.64198  1.000 53.23122  ?  35  VAL D CB  1 
ATOM   1896 C CG1 . VAL B 2 68  ? 65.67347  49.95256  36.46523  1.000 48.58381  ?  35  VAL D CG1 1 
ATOM   1897 C CG2 . VAL B 2 68  ? 67.60540  51.12715  37.49279  1.000 54.98647  ?  35  VAL D CG2 1 
ATOM   1898 N N   . ARG B 2 69  ? 65.95267  46.88241  37.32661  1.000 52.68297  ?  36  ARG D N   1 
ATOM   1899 C CA  . ARG B 2 69  ? 65.16982  45.77544  36.79617  1.000 50.95263  ?  36  ARG D CA  1 
ATOM   1900 C C   . ARG B 2 69  ? 63.70356  45.97967  37.13804  1.000 50.43863  ?  36  ARG D C   1 
ATOM   1901 O O   . ARG B 2 69  ? 63.36945  46.30113  38.28220  1.000 61.19844  ?  36  ARG D O   1 
ATOM   1902 C CB  . ARG B 2 69  ? 65.65281  44.42818  37.35191  1.000 51.91003  ?  36  ARG D CB  1 
ATOM   1903 C CG  . ARG B 2 69  ? 64.74852  43.25921  36.98178  1.000 58.82574  ?  36  ARG D CG  1 
ATOM   1904 C CD  . ARG B 2 69  ? 65.34743  41.90743  37.35110  1.000 82.82417  ?  36  ARG D CD  1 
ATOM   1905 N NE  . ARG B 2 69  ? 65.41733  41.69375  38.79172  1.000 77.23437  ?  36  ARG D NE  1 
ATOM   1906 C CZ  . ARG B 2 69  ? 66.54550  41.59517  39.48129  1.000 80.56232  ?  36  ARG D CZ  1 
ATOM   1907 N NH1 . ARG B 2 69  ? 67.72628  41.67450  38.89002  1.000 64.15853  ?  36  ARG D NH1 1 
ATOM   1908 N NH2 . ARG B 2 69  ? 66.48755  41.40431  40.79625  1.000 92.41257  ?  36  ARG D NH2 1 
ATOM   1909 N N   . TYR B 2 70  ? 62.83673  45.80339  36.14528  1.000 48.62519  ?  37  TYR D N   1 
ATOM   1910 C CA  . TYR B 2 70  ? 61.40264  45.69937  36.37172  1.000 57.18214  ?  37  TYR D CA  1 
ATOM   1911 C C   . TYR B 2 70  ? 61.00740  44.23069  36.33129  1.000 63.44279  ?  37  TYR D C   1 
ATOM   1912 O O   . TYR B 2 70  ? 61.43300  43.49315  35.43619  1.000 59.36690  ?  37  TYR D O   1 
ATOM   1913 C CB  . TYR B 2 70  ? 60.60342  46.48590  35.33155  1.000 52.90749  ?  37  TYR D CB  1 
ATOM   1914 C CG  . TYR B 2 70  ? 59.11378  46.22828  35.41566  1.000 55.89512  ?  37  TYR D CG  1 
ATOM   1915 C CD1 . TYR B 2 70  ? 58.32412  46.90120  36.33919  1.000 65.10064  ?  37  TYR D CD1 1 
ATOM   1916 C CD2 . TYR B 2 70  ? 58.49945  45.30290  34.58071  1.000 51.07595  ?  37  TYR D CD2 1 
ATOM   1917 C CE1 . TYR B 2 70  ? 56.96430  46.66315  36.42547  1.000 63.44765  ?  37  TYR D CE1 1 
ATOM   1918 C CE2 . TYR B 2 70  ? 57.14275  45.05762  34.66116  1.000 52.85483  ?  37  TYR D CE2 1 
ATOM   1919 C CZ  . TYR B 2 70  ? 56.37992  45.74048  35.58342  1.000 66.02173  ?  37  TYR D CZ  1 
ATOM   1920 O OH  . TYR B 2 70  ? 55.02829  45.49698  35.66282  1.000 59.02497  ?  37  TYR D OH  1 
ATOM   1921 N N   . ASP B 2 71  ? 60.19548  43.81243  37.29762  1.000 51.74694  ?  38  ASP D N   1 
ATOM   1922 C CA  . ASP B 2 71  ? 59.72834  42.43713  37.38931  1.000 56.69892  ?  38  ASP D CA  1 
ATOM   1923 C C   . ASP B 2 71  ? 58.22720  42.45045  37.62749  1.000 67.49005  ?  38  ASP D C   1 
ATOM   1924 O O   . ASP B 2 71  ? 57.75211  43.09534  38.56803  1.000 68.82324  ?  38  ASP D O   1 
ATOM   1925 C CB  . ASP B 2 71  ? 60.44969  41.68450  38.51390  1.000 64.40814  ?  38  ASP D CB  1 
ATOM   1926 C CG  . ASP B 2 71  ? 60.24435  40.18289  38.44212  1.000 65.56215  ?  38  ASP D CG  1 
ATOM   1927 O OD1 . ASP B 2 71  ? 59.45359  39.72178  37.59252  1.000 79.41967  ?  38  ASP D OD1 1 
ATOM   1928 O OD2 . ASP B 2 71  ? 60.88224  39.46096  39.23649  1.000 61.16162  -1 38  ASP D OD2 1 
ATOM   1929 N N   . SER B 2 72  ? 57.48446  41.74164  36.77218  1.000 61.89210  ?  39  SER D N   1 
ATOM   1930 C CA  . SER B 2 72  ? 56.03202  41.70196  36.90151  1.000 54.10802  ?  39  SER D CA  1 
ATOM   1931 C C   . SER B 2 72  ? 55.58738  41.09838  38.22634  1.000 54.43026  ?  39  SER D C   1 
ATOM   1932 O O   . SER B 2 72  ? 54.47243  41.37931  38.67897  1.000 74.23635  ?  39  SER D O   1 
ATOM   1933 C CB  . SER B 2 72  ? 55.41946  40.92083  35.73765  1.000 49.31777  ?  39  SER D CB  1 
ATOM   1934 O OG  . SER B 2 72  ? 55.86323  39.57620  35.73365  1.000 70.58184  ?  39  SER D OG  1 
ATOM   1935 N N   . ASP B 2 73  ? 56.42936  40.27645  38.85690  1.000 64.60031  ?  40  ASP D N   1 
ATOM   1936 C CA  . ASP B 2 73  ? 56.11416  39.76644  40.18518  1.000 71.10948  ?  40  ASP D CA  1 
ATOM   1937 C C   . ASP B 2 73  ? 56.20384  40.84889  41.25192  1.000 67.60453  ?  40  ASP D C   1 
ATOM   1938 O O   . ASP B 2 73  ? 55.56838  40.72002  42.30339  1.000 67.32753  ?  40  ASP D O   1 
ATOM   1939 C CB  . ASP B 2 73  ? 57.04409  38.60577  40.54065  1.000 71.48750  ?  40  ASP D CB  1 
ATOM   1940 C CG  . ASP B 2 73  ? 56.78003  37.36935  39.70346  1.000 85.69552  ?  40  ASP D CG  1 
ATOM   1941 O OD1 . ASP B 2 73  ? 55.94157  37.44229  38.78044  1.000 94.33585  ?  40  ASP D OD1 1 
ATOM   1942 O OD2 . ASP B 2 73  ? 57.40778  36.32297  39.97156  1.000 91.87025  -1 40  ASP D OD2 1 
ATOM   1943 N N   . VAL B 2 74  ? 56.97502  41.90459  41.00790  1.000 72.72130  ?  41  VAL D N   1 
ATOM   1944 C CA  . VAL B 2 74  ? 57.05994  43.01948  41.94547  1.000 71.51171  ?  41  VAL D CA  1 
ATOM   1945 C C   . VAL B 2 74  ? 56.07886  44.12490  41.57653  1.000 70.89820  ?  41  VAL D C   1 
ATOM   1946 O O   . VAL B 2 74  ? 55.46528  44.73693  42.45425  1.000 70.45114  ?  41  VAL D O   1 
ATOM   1947 C CB  . VAL B 2 74  ? 58.50840  43.54489  42.00499  1.000 62.50454  ?  41  VAL D CB  1 
ATOM   1948 C CG1 . VAL B 2 74  ? 58.63126  44.66161  43.03057  1.000 69.23653  ?  41  VAL D CG1 1 
ATOM   1949 C CG2 . VAL B 2 74  ? 59.46914  42.41114  42.32588  1.000 65.95319  ?  41  VAL D CG2 1 
ATOM   1950 N N   . GLY B 2 75  ? 55.90860  44.38772  40.28221  1.000 64.46155  ?  42  GLY D N   1 
ATOM   1951 C CA  . GLY B 2 75  ? 54.97900  45.39263  39.81594  1.000 66.00220  ?  42  GLY D CA  1 
ATOM   1952 C C   . GLY B 2 75  ? 55.55784  46.77844  39.64079  1.000 68.14248  ?  42  GLY D C   1 
ATOM   1953 O O   . GLY B 2 75  ? 54.82005  47.69400  39.25416  1.000 72.50965  ?  42  GLY D O   1 
ATOM   1954 N N   . GLU B 2 76  ? 56.84736  46.96563  39.90832  1.000 69.70013  ?  43  GLU D N   1 
ATOM   1955 C CA  . GLU B 2 76  ? 57.47048  48.27478  39.78281  1.000 71.78285  ?  43  GLU D CA  1 
ATOM   1956 C C   . GLU B 2 76  ? 58.96357  48.08621  39.56841  1.000 59.79238  ?  43  GLU D C   1 
ATOM   1957 O O   . GLU B 2 76  ? 59.51355  47.00914  39.81244  1.000 71.23054  ?  43  GLU D O   1 
ATOM   1958 C CB  . GLU B 2 76  ? 57.20692  49.14250  41.01810  1.000 65.79775  ?  43  GLU D CB  1 
ATOM   1959 C CG  . GLU B 2 76  ? 57.74035  48.54967  42.31162  1.000 69.73139  ?  43  GLU D CG  1 
ATOM   1960 C CD  . GLU B 2 76  ? 57.37828  49.37936  43.52680  1.000 93.58914  ?  43  GLU D CD  1 
ATOM   1961 O OE1 . GLU B 2 76  ? 56.59817  50.34386  43.37891  1.000 87.00440  ?  43  GLU D OE1 1 
ATOM   1962 O OE2 . GLU B 2 76  ? 57.87402  49.06681  44.63012  1.000 106.76973 -1 43  GLU D OE2 1 
ATOM   1963 N N   . HIS B 2 77  ? 59.61151  49.15111  39.10524  1.000 64.62497  ?  44  HIS D N   1 
ATOM   1964 C CA  . HIS B 2 77  ? 61.05262  49.11495  38.90674  1.000 54.15854  ?  44  HIS D CA  1 
ATOM   1965 C C   . HIS B 2 77  ? 61.77019  49.07690  40.24916  1.000 54.45073  ?  44  HIS D C   1 
ATOM   1966 O O   . HIS B 2 77  ? 61.33619  49.69647  41.22399  1.000 57.49005  ?  44  HIS D O   1 
ATOM   1967 C CB  . HIS B 2 77  ? 61.51258  50.32681  38.09699  1.000 50.78277  ?  44  HIS D CB  1 
ATOM   1968 C CG  . HIS B 2 77  ? 60.94901  50.37581  36.71114  1.000 55.77292  ?  44  HIS D CG  1 
ATOM   1969 N ND1 . HIS B 2 77  ? 59.66495  50.79963  36.44404  1.000 49.18709  ?  44  HIS D ND1 1 
ATOM   1970 C CD2 . HIS B 2 77  ? 61.49358  50.04892  35.51524  1.000 47.52014  ?  44  HIS D CD2 1 
ATOM   1971 C CE1 . HIS B 2 77  ? 59.44353  50.73397  35.14323  1.000 54.73681  ?  44  HIS D CE1 1 
ATOM   1972 N NE2 . HIS B 2 77  ? 60.53714  50.28128  34.55684  1.000 53.96346  ?  44  HIS D NE2 1 
ATOM   1973 N N   . ARG B 2 78  ? 62.87273  48.33660  40.29651  1.000 59.72496  ?  45  ARG D N   1 
ATOM   1974 C CA  . ARG B 2 78  ? 63.67582  48.19930  41.50130  1.000 63.55561  ?  45  ARG D CA  1 
ATOM   1975 C C   . ARG B 2 78  ? 65.14296  48.39467  41.15427  1.000 68.10092  ?  45  ARG D C   1 
ATOM   1976 O O   . ARG B 2 78  ? 65.59978  47.97048  40.08837  1.000 62.24583  ?  45  ARG D O   1 
ATOM   1977 C CB  . ARG B 2 78  ? 63.46938  46.82992  42.15569  1.000 65.73901  ?  45  ARG D CB  1 
ATOM   1978 C CG  . ARG B 2 78  ? 62.10542  46.63526  42.79538  1.000 60.11358  ?  45  ARG D CG  1 
ATOM   1979 C CD  . ARG B 2 78  ? 61.93394  47.53184  44.00844  1.000 73.79550  ?  45  ARG D CD  1 
ATOM   1980 N NE  . ARG B 2 78  ? 60.77200  47.15308  44.80280  1.000 72.20365  ?  45  ARG D NE  1 
ATOM   1981 C CZ  . ARG B 2 78  ? 60.78861  46.23342  45.75779  1.000 96.03952  ?  45  ARG D CZ  1 
ATOM   1982 N NH1 . ARG B 2 78  ? 61.89460  45.57476  46.06364  1.000 89.78977  ?  45  ARG D NH1 1 
ATOM   1983 N NH2 . ARG B 2 78  ? 59.66746  45.96669  46.42164  1.000 117.13366 ?  45  ARG D NH2 1 
ATOM   1984 N N   . ALA B 2 79  ? 65.87605  49.03970  42.05813  1.000 63.24919  ?  46  ALA D N   1 
ATOM   1985 C CA  . ALA B 2 79  ? 67.29700  49.29978  41.85539  1.000 57.42178  ?  46  ALA D CA  1 
ATOM   1986 C C   . ALA B 2 79  ? 68.08923  48.05911  42.24680  1.000 58.18745  ?  46  ALA D C   1 
ATOM   1987 O O   . ALA B 2 79  ? 68.12662  47.68326  43.42233  1.000 73.31779  ?  46  ALA D O   1 
ATOM   1988 C CB  . ALA B 2 79  ? 67.73847  50.51309  42.66773  1.000 60.25738  ?  46  ALA D CB  1 
ATOM   1989 N N   . VAL B 2 80  ? 68.72303  47.41767  41.26366  1.000 55.65774  ?  47  VAL D N   1 
ATOM   1990 C CA  . VAL B 2 80  ? 69.53665  46.24307  41.55978  1.000 56.65558  ?  47  VAL D CA  1 
ATOM   1991 C C   . VAL B 2 80  ? 70.78968  46.64448  42.32743  1.000 61.83924  ?  47  VAL D C   1 
ATOM   1992 O O   . VAL B 2 80  ? 71.18200  45.98097  43.29468  1.000 72.92922  ?  47  VAL D O   1 
ATOM   1993 C CB  . VAL B 2 80  ? 69.87927  45.48933  40.26296  1.000 56.08517  ?  47  VAL D CB  1 
ATOM   1994 C CG1 . VAL B 2 80  ? 70.60122  44.18984  40.58047  1.000 55.00322  ?  47  VAL D CG1 1 
ATOM   1995 C CG2 . VAL B 2 80  ? 68.61806  45.22411  39.45667  1.000 65.09739  ?  47  VAL D CG2 1 
ATOM   1996 N N   . THR B 2 81  ? 71.43318  47.73127  41.91464  1.000 68.61944  ?  48  THR D N   1 
ATOM   1997 C CA  . THR B 2 81  ? 72.57618  48.29610  42.61405  1.000 69.72539  ?  48  THR D CA  1 
ATOM   1998 C C   . THR B 2 81  ? 72.28320  49.74777  42.97304  1.000 69.77982  ?  48  THR D C   1 
ATOM   1999 O O   . THR B 2 81  ? 71.26091  50.31623  42.58060  1.000 68.67906  ?  48  THR D O   1 
ATOM   2000 C CB  . THR B 2 81  ? 73.85136  48.20340  41.76588  1.000 64.21972  ?  48  THR D CB  1 
ATOM   2001 O OG1 . THR B 2 81  ? 73.67189  48.93624  40.54785  1.000 76.77459  ?  48  THR D OG1 1 
ATOM   2002 C CG2 . THR B 2 81  ? 74.16921  46.75186  41.43732  1.000 65.27783  ?  48  THR D CG2 1 
ATOM   2003 N N   . GLU B 2 82  ? 73.20352  50.35029  43.73039  1.000 72.31746  ?  49  GLU D N   1 
ATOM   2004 C CA  . GLU B 2 82  ? 73.02621  51.73348  44.15917  1.000 79.08836  ?  49  GLU D CA  1 
ATOM   2005 C C   . GLU B 2 82  ? 72.99215  52.70420  42.98673  1.000 78.96299  ?  49  GLU D C   1 
ATOM   2006 O O   . GLU B 2 82  ? 72.41977  53.79233  43.11310  1.000 77.65743  ?  49  GLU D O   1 
ATOM   2007 C CB  . GLU B 2 82  ? 74.14176  52.13223  45.12647  1.000 83.92466  ?  49  GLU D CB  1 
ATOM   2008 C CG  . GLU B 2 82  ? 74.24130  51.25247  46.36029  1.000 124.18310 ?  49  GLU D CG  1 
ATOM   2009 C CD  . GLU B 2 82  ? 75.30249  51.73187  47.33062  1.000 142.38977 ?  49  GLU D CD  1 
ATOM   2010 O OE1 . GLU B 2 82  ? 75.96589  52.74766  47.03303  1.000 145.69183 ?  49  GLU D OE1 1 
ATOM   2011 O OE2 . GLU B 2 82  ? 75.47276  51.09419  48.39101  1.000 153.06018 -1 49  GLU D OE2 1 
ATOM   2012 N N   . LEU B 2 83  ? 73.58810  52.33518  41.85113  1.000 78.62872  ?  50  LEU D N   1 
ATOM   2013 C CA  . LEU B 2 83  ? 73.61567  53.21729  40.69137  1.000 62.04235  ?  50  LEU D CA  1 
ATOM   2014 C C   . LEU B 2 83  ? 72.22920  53.45219  40.10535  1.000 67.70522  ?  50  LEU D C   1 
ATOM   2015 O O   . LEU B 2 83  ? 72.01819  54.46724  39.43324  1.000 74.05117  ?  50  LEU D O   1 
ATOM   2016 C CB  . LEU B 2 83  ? 74.54232  52.63552  39.62120  1.000 61.29460  ?  50  LEU D CB  1 
ATOM   2017 C CG  . LEU B 2 83  ? 74.94141  53.53827  38.45269  1.000 74.26814  ?  50  LEU D CG  1 
ATOM   2018 C CD1 . LEU B 2 83  ? 75.82842  54.67635  38.93435  1.000 71.06224  ?  50  LEU D CD1 1 
ATOM   2019 C CD2 . LEU B 2 83  ? 75.63514  52.73299  37.36439  1.000 70.80634  ?  50  LEU D CD2 1 
ATOM   2020 N N   . GLY B 2 84  ? 71.28292  52.55065  40.34956  1.000 68.34664  ?  51  GLY D N   1 
ATOM   2021 C CA  . GLY B 2 84  ? 69.96180  52.62836  39.76558  1.000 62.54900  ?  51  GLY D CA  1 
ATOM   2022 C C   . GLY B 2 84  ? 68.86862  53.18091  40.65320  1.000 67.30790  ?  51  GLY D C   1 
ATOM   2023 O O   . GLY B 2 84  ? 67.69989  53.15598  40.24917  1.000 68.03726  ?  51  GLY D O   1 
ATOM   2024 N N   . ARG B 2 85  ? 69.19911  53.67602  41.84580  1.000 66.75586  ?  52  ARG D N   1 
ATOM   2025 C CA  . ARG B 2 85  ? 68.16951  54.23534  42.72052  1.000 74.86663  ?  52  ARG D CA  1 
ATOM   2026 C C   . ARG B 2 85  ? 67.45607  55.43646  42.10947  1.000 75.54735  ?  52  ARG D C   1 
ATOM   2027 O O   . ARG B 2 85  ? 66.21510  55.48254  42.17412  1.000 73.06034  ?  52  ARG D O   1 
ATOM   2028 C CB  . ARG B 2 85  ? 68.77654  54.58314  44.08450  1.000 79.99431  ?  52  ARG D CB  1 
ATOM   2029 C CG  . ARG B 2 85  ? 69.00139  53.39083  44.99942  1.000 68.66312  ?  52  ARG D CG  1 
ATOM   2030 C CD  . ARG B 2 85  ? 69.15699  53.84655  46.44260  1.000 93.25967  ?  52  ARG D CD  1 
ATOM   2031 N NE  . ARG B 2 85  ? 69.27538  52.72804  47.36998  1.000 103.57604 ?  52  ARG D NE  1 
ATOM   2032 C CZ  . ARG B 2 85  ? 70.42272  52.28155  47.86177  1.000 107.93091 ?  52  ARG D CZ  1 
ATOM   2033 N NH1 . ARG B 2 85  ? 71.57725  52.83939  47.53696  1.000 105.80363 ?  52  ARG D NH1 1 
ATOM   2034 N NH2 . ARG B 2 85  ? 70.41099  51.25207  48.70372  1.000 123.32787 ?  52  ARG D NH2 1 
ATOM   2035 N N   . PRO B 2 86  ? 68.13962  56.43000  41.52339  1.000 62.30772  ?  53  PRO D N   1 
ATOM   2036 C CA  . PRO B 2 86  ? 67.38917  57.55036  40.92854  1.000 60.24227  ?  53  PRO D CA  1 
ATOM   2037 C C   . PRO B 2 86  ? 66.51848  57.14050  39.75391  1.000 61.02734  ?  53  PRO D C   1 
ATOM   2038 O O   . PRO B 2 86  ? 65.40933  57.66663  39.59887  1.000 72.12492  ?  53  PRO D O   1 
ATOM   2039 C CB  . PRO B 2 86  ? 68.49669  58.52505  40.50069  1.000 60.63057  ?  53  PRO D CB  1 
ATOM   2040 C CG  . PRO B 2 86  ? 69.66612  58.16845  41.34312  1.000 57.73780  ?  53  PRO D CG  1 
ATOM   2041 C CD  . PRO B 2 86  ? 69.59139  56.68550  41.49767  1.000 63.26326  ?  53  PRO D CD  1 
ATOM   2042 N N   . ASP B 2 87  ? 66.98834  56.21014  38.91960  1.000 71.43204  ?  54  ASP D N   1 
ATOM   2043 C CA  . ASP B 2 87  ? 66.22411  55.82845  37.73580  1.000 72.39727  ?  54  ASP D CA  1 
ATOM   2044 C C   . ASP B 2 87  ? 64.97932  55.03192  38.10768  1.000 70.96004  ?  54  ASP D C   1 
ATOM   2045 O O   . ASP B 2 87  ? 63.91710  55.21163  37.50033  1.000 68.03882  ?  54  ASP D O   1 
ATOM   2046 C CB  . ASP B 2 87  ? 67.10674  55.03069  36.77707  1.000 66.27863  ?  54  ASP D CB  1 
ATOM   2047 C CG  . ASP B 2 87  ? 68.30749  55.82134  36.29898  1.000 90.77410  ?  54  ASP D CG  1 
ATOM   2048 O OD1 . ASP B 2 87  ? 68.23808  57.06896  36.30247  1.000 84.19568  ?  54  ASP D OD1 1 
ATOM   2049 O OD2 . ASP B 2 87  ? 69.31972  55.19714  35.91606  1.000 84.74391  -1 54  ASP D OD2 1 
ATOM   2050 N N   . ALA B 2 88  ? 65.08884  54.14593  39.09980  1.000 61.83133  ?  55  ALA D N   1 
ATOM   2051 C CA  . ALA B 2 88  ? 63.93265  53.35581  39.50991  1.000 65.48946  ?  55  ALA D CA  1 
ATOM   2052 C C   . ALA B 2 88  ? 62.88248  54.22462  40.19068  1.000 73.80149  ?  55  ALA D C   1 
ATOM   2053 O O   . ALA B 2 88  ? 61.67862  54.02626  39.98819  1.000 65.35372  ?  55  ALA D O   1 
ATOM   2054 C CB  . ALA B 2 88  ? 64.37253  52.21917  40.43241  1.000 57.19806  ?  55  ALA D CB  1 
ATOM   2055 N N   . GLU B 2 89  ? 63.31814  55.19432  40.99881  1.000 79.39697  ?  56  GLU D N   1 
ATOM   2056 C CA  . GLU B 2 89  ? 62.36993  56.07143  41.67779  1.000 77.51191  ?  56  GLU D CA  1 
ATOM   2057 C C   . GLU B 2 89  ? 61.68459  57.01356  40.69640  1.000 70.01458  ?  56  GLU D C   1 
ATOM   2058 O O   . GLU B 2 89  ? 60.49022  57.30086  40.83583  1.000 73.96230  ?  56  GLU D O   1 
ATOM   2059 C CB  . GLU B 2 89  ? 63.07964  56.86486  42.77532  1.000 84.97637  ?  56  GLU D CB  1 
ATOM   2060 C CG  . GLU B 2 89  ? 63.53121  56.02822  43.96336  1.000 115.00272 ?  56  GLU D CG  1 
ATOM   2061 C CD  . GLU B 2 89  ? 62.37536  55.57172  44.83483  1.000 129.02430 ?  56  GLU D CD  1 
ATOM   2062 O OE1 . GLU B 2 89  ? 61.26549  56.12907  44.69839  1.000 134.61220 ?  56  GLU D OE1 1 
ATOM   2063 O OE2 . GLU B 2 89  ? 62.57779  54.65512  45.65906  1.000 129.37465 -1 56  GLU D OE2 1 
ATOM   2064 N N   . TYR B 2 90  ? 62.42157  57.50249  39.69647  1.000 66.27451  ?  57  TYR D N   1 
ATOM   2065 C CA  . TYR B 2 90  ? 61.83804  58.43602  38.73819  1.000 65.99409  ?  57  TYR D CA  1 
ATOM   2066 C C   . TYR B 2 90  ? 60.82570  57.74478  37.83302  1.000 67.85083  ?  57  TYR D C   1 
ATOM   2067 O O   . TYR B 2 90  ? 59.75246  58.29490  37.55986  1.000 67.92378  ?  57  TYR D O   1 
ATOM   2068 C CB  . TYR B 2 90  ? 62.94152  59.09316  37.90896  1.000 54.77134  ?  57  TYR D CB  1 
ATOM   2069 C CG  . TYR B 2 90  ? 62.43044  60.00172  36.81282  1.000 69.53157  ?  57  TYR D CG  1 
ATOM   2070 C CD1 . TYR B 2 90  ? 61.92014  61.25929  37.10794  1.000 67.87012  ?  57  TYR D CD1 1 
ATOM   2071 C CD2 . TYR B 2 90  ? 62.46574  59.60492  35.48184  1.000 72.12660  ?  57  TYR D CD2 1 
ATOM   2072 C CE1 . TYR B 2 90  ? 61.45348  62.09382  36.10929  1.000 78.05749  ?  57  TYR D CE1 1 
ATOM   2073 C CE2 . TYR B 2 90  ? 62.00214  60.43288  34.47620  1.000 77.10933  ?  57  TYR D CE2 1 
ATOM   2074 C CZ  . TYR B 2 90  ? 61.49718  61.67581  34.79555  1.000 84.34355  ?  57  TYR D CZ  1 
ATOM   2075 O OH  . TYR B 2 90  ? 61.03442  62.50350  33.79790  1.000 95.34193  ?  57  TYR D OH  1 
ATOM   2076 N N   . TRP B 2 91  ? 61.14622  56.53810  37.36135  1.000 63.81568  ?  58  TRP D N   1 
ATOM   2077 C CA  . TRP B 2 91  ? 60.24573  55.83824  36.45085  1.000 63.01334  ?  58  TRP D CA  1 
ATOM   2078 C C   . TRP B 2 91  ? 58.98001  55.37754  37.16330  1.000 70.83699  ?  58  TRP D C   1 
ATOM   2079 O O   . TRP B 2 91  ? 57.89449  55.37572  36.57097  1.000 73.75969  ?  58  TRP D O   1 
ATOM   2080 C CB  . TRP B 2 91  ? 60.97016  54.65559  35.80967  1.000 60.08344  ?  58  TRP D CB  1 
ATOM   2081 C CG  . TRP B 2 91  ? 62.06640  55.07486  34.88189  1.000 53.19695  ?  58  TRP D CG  1 
ATOM   2082 C CD1 . TRP B 2 91  ? 62.17287  56.26772  34.22890  1.000 62.47370  ?  58  TRP D CD1 1 
ATOM   2083 C CD2 . TRP B 2 91  ? 63.22028  54.31099  34.51232  1.000 53.04556  ?  58  TRP D CD2 1 
ATOM   2084 N NE1 . TRP B 2 91  ? 63.31664  56.29147  33.46918  1.000 53.81718  ?  58  TRP D NE1 1 
ATOM   2085 C CE2 . TRP B 2 91  ? 63.97919  55.10313  33.62789  1.000 47.34264  ?  58  TRP D CE2 1 
ATOM   2086 C CE3 . TRP B 2 91  ? 63.68452  53.03403  34.84130  1.000 61.78305  ?  58  TRP D CE3 1 
ATOM   2087 C CZ2 . TRP B 2 91  ? 65.17454  54.65970  33.06676  1.000 55.43845  ?  58  TRP D CZ2 1 
ATOM   2088 C CZ3 . TRP B 2 91  ? 64.87255  52.59622  34.28343  1.000 55.46722  ?  58  TRP D CZ3 1 
ATOM   2089 C CH2 . TRP B 2 91  ? 65.60391  53.40693  33.40697  1.000 52.05040  ?  58  TRP D CH2 1 
ATOM   2090 N N   . ASN B 2 92  ? 59.09516  54.98547  38.43300  1.000 64.88459  ?  59  ASN D N   1 
ATOM   2091 C CA  . ASN B 2 92  ? 57.92304  54.57138  39.19303  1.000 59.69327  ?  59  ASN D CA  1 
ATOM   2092 C C   . ASN B 2 92  ? 57.09845  55.75087  39.68963  1.000 68.97111  ?  59  ASN D C   1 
ATOM   2093 O O   . ASN B 2 92  ? 55.91439  55.57479  39.99601  1.000 75.39207  ?  59  ASN D O   1 
ATOM   2094 C CB  . ASN B 2 92  ? 58.34061  53.69918  40.37911  1.000 67.79917  ?  59  ASN D CB  1 
ATOM   2095 C CG  . ASN B 2 92  ? 58.90676  52.35982  39.94710  1.000 74.38745  ?  59  ASN D CG  1 
ATOM   2096 O OD1 . ASN B 2 92  ? 58.65249  51.89420  38.83595  1.000 74.00323  ?  59  ASN D OD1 1 
ATOM   2097 N ND2 . ASN B 2 92  ? 59.67355  51.72942  40.82888  1.000 66.09215  ?  59  ASN D ND2 1 
ATOM   2098 N N   . SER B 2 93  ? 57.69075  56.94379  39.77525  1.000 75.89362  ?  60  SER D N   1 
ATOM   2099 C CA  . SER B 2 93  ? 56.94988  58.12058  40.21145  1.000 74.80442  ?  60  SER D CA  1 
ATOM   2100 C C   . SER B 2 93  ? 56.06917  58.69876  39.11313  1.000 77.94278  ?  60  SER D C   1 
ATOM   2101 O O   . SER B 2 93  ? 55.13052  59.44236  39.41767  1.000 77.06827  ?  60  SER D O   1 
ATOM   2102 C CB  . SER B 2 93  ? 57.91284  59.19859  40.71256  1.000 61.94863  ?  60  SER D CB  1 
ATOM   2103 O OG  . SER B 2 93  ? 58.75131  59.65642  39.66653  1.000 82.92158  ?  60  SER D OG  1 
ATOM   2104 N N   . GLN B 2 94  ? 56.35085  58.38144  37.84976  1.000 75.20953  ?  61  GLN D N   1 
ATOM   2105 C CA  . GLN B 2 94  ? 55.53307  58.85129  36.74105  1.000 70.62665  ?  61  GLN D CA  1 
ATOM   2106 C C   . GLN B 2 94  ? 54.46649  57.80626  36.44291  1.000 77.75033  ?  61  GLN D C   1 
ATOM   2107 O O   . GLN B 2 94  ? 54.80978  56.69692  36.00468  1.000 72.47068  ?  61  GLN D O   1 
ATOM   2108 C CB  . GLN B 2 94  ? 56.39141  59.10381  35.51017  1.000 85.35805  ?  61  GLN D CB  1 
ATOM   2109 C CG  . GLN B 2 94  ? 57.54780  60.06642  35.73949  1.000 76.87617  ?  61  GLN D CG  1 
ATOM   2110 C CD  . GLN B 2 94  ? 57.08941  61.49552  35.95659  1.000 106.38289 ?  61  GLN D CD  1 
ATOM   2111 O OE1 . GLN B 2 94  ? 55.97763  61.86833  35.58106  1.000 123.80422 ?  61  GLN D OE1 1 
ATOM   2112 N NE2 . GLN B 2 94  ? 57.94784  62.30522  36.56599  1.000 109.16367 ?  61  GLN D NE2 1 
ATOM   2113 N N   . PRO B 2 95  ? 53.18165  58.09706  36.66781  1.000 75.27453  ?  62  PRO D N   1 
ATOM   2114 C CA  . PRO B 2 95  ? 52.15012  57.07625  36.41174  1.000 65.05610  ?  62  PRO D CA  1 
ATOM   2115 C C   . PRO B 2 95  ? 52.08098  56.63373  34.96101  1.000 62.73165  ?  62  PRO D C   1 
ATOM   2116 O O   . PRO B 2 95  ? 51.93724  55.43477  34.69233  1.000 71.12747  ?  62  PRO D O   1 
ATOM   2117 C CB  . PRO B 2 95  ? 50.85567  57.77261  36.85715  1.000 69.92997  ?  62  PRO D CB  1 
ATOM   2118 C CG  . PRO B 2 95  ? 51.30114  58.83326  37.81116  1.000 71.20552  ?  62  PRO D CG  1 
ATOM   2119 C CD  . PRO B 2 95  ? 52.62131  59.30902  37.28692  1.000 76.52240  ?  62  PRO D CD  1 
ATOM   2120 N N   . GLU B 2 96  ? 52.18159  57.56845  34.01271  1.000 69.83033  ?  63  GLU D N   1 
ATOM   2121 C CA  . GLU B 2 96  ? 52.11656  57.20073  32.60273  1.000 72.90742  ?  63  GLU D CA  1 
ATOM   2122 C C   . GLU B 2 96  ? 53.29736  56.33875  32.17738  1.000 72.86553  ?  63  GLU D C   1 
ATOM   2123 O O   . GLU B 2 96  ? 53.19260  55.60968  31.18516  1.000 73.24533  ?  63  GLU D O   1 
ATOM   2124 C CB  . GLU B 2 96  ? 52.04297  58.45553  31.72763  1.000 70.64443  ?  63  GLU D CB  1 
ATOM   2125 C CG  . GLU B 2 96  ? 53.33290  59.26448  31.65760  1.000 83.90007  ?  63  GLU D CG  1 
ATOM   2126 C CD  . GLU B 2 96  ? 53.59257  60.08147  32.91028  1.000 102.07196 ?  63  GLU D CD  1 
ATOM   2127 O OE1 . GLU B 2 96  ? 52.69313  60.15896  33.77431  1.000 99.85750  ?  63  GLU D OE1 1 
ATOM   2128 O OE2 . GLU B 2 96  ? 54.69911  60.64873  33.02934  1.000 106.63364 -1 63  GLU D OE2 1 
ATOM   2129 N N   . ILE B 2 97  ? 54.41363  56.40288  32.90234  1.000 67.23976  ?  64  ILE D N   1 
ATOM   2130 C CA  . ILE B 2 97  ? 55.55992  55.55921  32.58457  1.000 66.15211  ?  64  ILE D CA  1 
ATOM   2131 C C   . ILE B 2 97  ? 55.40350  54.18303  33.21755  1.000 63.00510  ?  64  ILE D C   1 
ATOM   2132 O O   . ILE B 2 97  ? 55.63275  53.15513  32.56983  1.000 59.06530  ?  64  ILE D O   1 
ATOM   2133 C CB  . ILE B 2 97  ? 56.86570  56.24329  33.03117  1.000 58.48668  ?  64  ILE D CB  1 
ATOM   2134 C CG1 . ILE B 2 97  ? 57.09006  57.53207  32.23855  1.000 52.32995  ?  64  ILE D CG1 1 
ATOM   2135 C CG2 . ILE B 2 97  ? 58.04941  55.30069  32.86858  1.000 56.06841  ?  64  ILE D CG2 1 
ATOM   2136 C CD1 . ILE B 2 97  ? 58.38978  58.23281  32.56657  1.000 63.05782  ?  64  ILE D CD1 1 
ATOM   2137 N N   . LEU B 2 98  ? 55.00457  54.14288  34.49128  1.000 66.86772  ?  65  LEU D N   1 
ATOM   2138 C CA  . LEU B 2 98  ? 54.84367  52.86476  35.17729  1.000 64.21273  ?  65  LEU D CA  1 
ATOM   2139 C C   . LEU B 2 98  ? 53.72744  52.03637  34.55253  1.000 73.87417  ?  65  LEU D C   1 
ATOM   2140 O O   . LEU B 2 98  ? 53.83850  50.80861  34.45602  1.000 72.37343  ?  65  LEU D O   1 
ATOM   2141 C CB  . LEU B 2 98  ? 54.57431  53.09859  36.66429  1.000 57.26027  ?  65  LEU D CB  1 
ATOM   2142 C CG  . LEU B 2 98  ? 54.39614  51.85272  37.53516  1.000 61.70325  ?  65  LEU D CG  1 
ATOM   2143 C CD1 . LEU B 2 98  ? 55.63151  50.96832  37.46915  1.000 66.02247  ?  65  LEU D CD1 1 
ATOM   2144 C CD2 . LEU B 2 98  ? 54.08733  52.24030  38.97322  1.000 56.95937  ?  65  LEU D CD2 1 
ATOM   2145 N N   . GLU B 2 99  ? 52.64658  52.68831  34.11612  1.000 72.46522  ?  66  GLU D N   1 
ATOM   2146 C CA  . GLU B 2 99  ? 51.54506  51.95320  33.50362  1.000 62.11183  ?  66  GLU D CA  1 
ATOM   2147 C C   . GLU B 2 99  ? 51.90718  51.44317  32.11502  1.000 63.38897  ?  66  GLU D C   1 
ATOM   2148 O O   . GLU B 2 99  ? 51.39128  50.40479  31.68654  1.000 71.19209  ?  66  GLU D O   1 
ATOM   2149 C CB  . GLU B 2 99  ? 50.29470  52.82980  33.43844  1.000 63.73180  ?  66  GLU D CB  1 
ATOM   2150 C CG  . GLU B 2 99  ? 49.68373  53.13658  34.79691  1.000 103.52742 ?  66  GLU D CG  1 
ATOM   2151 C CD  . GLU B 2 99  ? 49.21730  51.88942  35.52390  1.000 102.09169 ?  66  GLU D CD  1 
ATOM   2152 O OE1 . GLU B 2 99  ? 48.78259  50.93126  34.85030  1.000 106.17809 ?  66  GLU D OE1 1 
ATOM   2153 O OE2 . GLU B 2 99  ? 49.29000  51.86580  36.77044  1.000 111.08360 -1 66  GLU D OE2 1 
ATOM   2154 N N   . ARG B 2 100 ? 52.78280  52.15131  31.39754  1.000 66.26465  ?  67  ARG D N   1 
ATOM   2155 C CA  . ARG B 2 100 ? 53.20331  51.67345  30.08454  1.000 55.86339  ?  67  ARG D CA  1 
ATOM   2156 C C   . ARG B 2 100 ? 54.09673  50.44666  30.21064  1.000 64.15360  ?  67  ARG D C   1 
ATOM   2157 O O   . ARG B 2 100 ? 54.01049  49.52128  29.39513  1.000 63.92328  ?  67  ARG D O   1 
ATOM   2158 C CB  . ARG B 2 100 ? 53.92517  52.78271  29.31972  1.000 57.23382  ?  67  ARG D CB  1 
ATOM   2159 C CG  . ARG B 2 100 ? 53.84819  52.63052  27.80706  1.000 66.83429  ?  67  ARG D CG  1 
ATOM   2160 C CD  . ARG B 2 100 ? 54.97581  53.36547  27.09839  1.000 64.21587  ?  67  ARG D CD  1 
ATOM   2161 N NE  . ARG B 2 100 ? 56.19954  52.57334  27.05660  1.000 66.39693  ?  67  ARG D NE  1 
ATOM   2162 C CZ  . ARG B 2 100 ? 57.21581  52.71477  27.89635  1.000 75.01082  ?  67  ARG D CZ  1 
ATOM   2163 N NH1 . ARG B 2 100 ? 57.19823  53.62539  28.85614  1.000 86.89711  ?  67  ARG D NH1 1 
ATOM   2164 N NH2 . ARG B 2 100 ? 58.27817  51.92479  27.76768  1.000 53.21177  ?  67  ARG D NH2 1 
ATOM   2165 N N   . THR B 2 101 ? 54.96177  50.42313  31.22717  1.000 61.58887  ?  68  THR D N   1 
ATOM   2166 C CA  . THR B 2 101 ? 55.81726  49.26226  31.44703  1.000 48.02143  ?  68  THR D CA  1 
ATOM   2167 C C   . THR B 2 101 ? 55.00401  48.05814  31.90617  1.000 59.26669  ?  68  THR D C   1 
ATOM   2168 O O   . THR B 2 101 ? 55.24167  46.93214  31.45342  1.000 67.96718  ?  68  THR D O   1 
ATOM   2169 C CB  . THR B 2 101 ? 56.90328  49.59872  32.46994  1.000 56.87291  ?  68  THR D CB  1 
ATOM   2170 O OG1 . THR B 2 101 ? 57.68861  50.69802  31.99179  1.000 60.43149  ?  68  THR D OG1 1 
ATOM   2171 C CG2 . THR B 2 101 ? 57.81063  48.39943  32.70458  1.000 70.00365  ?  68  THR D CG2 1 
ATOM   2172 N N   . ARG B 2 102 ? 54.03715  48.27717  32.80108  1.000 58.90378  ?  69  ARG D N   1 
ATOM   2173 C CA  . ARG B 2 102 ? 53.20827  47.17698  33.28338  1.000 51.12572  ?  69  ARG D CA  1 
ATOM   2174 C C   . ARG B 2 102 ? 52.39627  46.55655  32.15393  1.000 57.07576  ?  69  ARG D C   1 
ATOM   2175 O O   . ARG B 2 102 ? 52.26996  45.32910  32.07170  1.000 58.01679  ?  69  ARG D O   1 
ATOM   2176 C CB  . ARG B 2 102 ? 52.28178  47.66651  34.39629  1.000 55.10439  ?  69  ARG D CB  1 
ATOM   2177 C CG  . ARG B 2 102 ? 52.97806  47.95755  35.71281  1.000 59.12047  ?  69  ARG D CG  1 
ATOM   2178 C CD  . ARG B 2 102 ? 52.01065  48.55209  36.72228  1.000 71.96240  ?  69  ARG D CD  1 
ATOM   2179 N NE  . ARG B 2 102 ? 52.58921  48.62279  38.05843  1.000 75.15578  ?  69  ARG D NE  1 
ATOM   2180 C CZ  . ARG B 2 102 ? 52.01674  49.22610  39.09095  1.000 73.88674  ?  69  ARG D CZ  1 
ATOM   2181 N NH1 . ARG B 2 102 ? 50.85216  49.84247  38.97234  1.000 70.65071  ?  69  ARG D NH1 1 
ATOM   2182 N NH2 . ARG B 2 102 ? 52.62921  49.21273  40.27154  1.000 76.58372  ?  69  ARG D NH2 1 
ATOM   2183 N N   . ALA B 2 103 ? 51.84202  47.38843  31.26985  1.000 52.75761  ?  70  ALA D N   1 
ATOM   2184 C CA  . ALA B 2 103 ? 50.98837  46.89511  30.19631  1.000 57.88569  ?  70  ALA D CA  1 
ATOM   2185 C C   . ALA B 2 103 ? 51.75504  46.12882  29.12747  1.000 53.61754  ?  70  ALA D C   1 
ATOM   2186 O O   . ALA B 2 103 ? 51.12304  45.50312  28.26958  1.000 52.22806  ?  70  ALA D O   1 
ATOM   2187 C CB  . ALA B 2 103 ? 50.23236  48.05790  29.55173  1.000 58.39111  ?  70  ALA D CB  1 
ATOM   2188 N N   . GLU B 2 104 ? 53.08919  46.15732  29.15449  1.000 49.60830  ?  71  GLU D N   1 
ATOM   2189 C CA  . GLU B 2 104 ? 53.86415  45.44440  28.14670  1.000 59.20435  ?  71  GLU D CA  1 
ATOM   2190 C C   . GLU B 2 104 ? 53.75793  43.93186  28.29406  1.000 54.00189  ?  71  GLU D C   1 
ATOM   2191 O O   . GLU B 2 104 ? 54.08719  43.20699  27.34974  1.000 53.84770  ?  71  GLU D O   1 
ATOM   2192 C CB  . GLU B 2 104 ? 55.32797  45.88580  28.20099  1.000 48.70569  ?  71  GLU D CB  1 
ATOM   2193 C CG  . GLU B 2 104 ? 55.56988  47.26128  27.59381  1.000 49.49714  ?  71  GLU D CG  1 
ATOM   2194 C CD  . GLU B 2 104 ? 57.00619  47.72747  27.73632  1.000 61.22215  ?  71  GLU D CD  1 
ATOM   2195 O OE1 . GLU B 2 104 ? 57.59502  47.52414  28.81845  1.000 70.40337  ?  71  GLU D OE1 1 
ATOM   2196 O OE2 . GLU B 2 104 ? 57.54771  48.29562  26.76396  1.000 57.05724  -1 71  GLU D OE2 1 
ATOM   2197 N N   . LEU B 2 105 ? 53.30333  43.43830  29.44853  1.000 50.90315  ?  72  LEU D N   1 
ATOM   2198 C CA  . LEU B 2 105 ? 53.05544  42.00696  29.58323  1.000 49.98194  ?  72  LEU D CA  1 
ATOM   2199 C C   . LEU B 2 105 ? 51.94266  41.55120  28.64905  1.000 59.38298  ?  72  LEU D C   1 
ATOM   2200 O O   . LEU B 2 105 ? 51.95588  40.40860  28.17770  1.000 58.55220  ?  72  LEU D O   1 
ATOM   2201 C CB  . LEU B 2 105 ? 52.71557  41.66637  31.03664  1.000 52.04964  ?  72  LEU D CB  1 
ATOM   2202 C CG  . LEU B 2 105 ? 52.64158  40.19024  31.44052  1.000 53.94255  ?  72  LEU D CG  1 
ATOM   2203 C CD1 . LEU B 2 105 ? 53.13867  40.00944  32.86548  1.000 54.98637  ?  72  LEU D CD1 1 
ATOM   2204 C CD2 . LEU B 2 105 ? 51.22684  39.64490  31.30685  1.000 57.13184  ?  72  LEU D CD2 1 
ATOM   2205 N N   . ASP B 2 106 ? 50.97682  42.42638  28.36841  1.000 66.98189  ?  73  ASP D N   1 
ATOM   2206 C CA  . ASP B 2 106 ? 49.89882  42.11541  27.43817  1.000 58.86649  ?  73  ASP D CA  1 
ATOM   2207 C C   . ASP B 2 106 ? 50.21316  42.56608  26.01708  1.000 58.47784  ?  73  ASP D C   1 
ATOM   2208 O O   . ASP B 2 106 ? 49.96629  41.82100  25.06270  1.000 63.48964  ?  73  ASP D O   1 
ATOM   2209 C CB  . ASP B 2 106 ? 48.59235  42.76366  27.90632  1.000 60.60412  ?  73  ASP D CB  1 
ATOM   2210 C CG  . ASP B 2 106 ? 48.04571  42.13065  29.17103  1.000 84.64072  ?  73  ASP D CG  1 
ATOM   2211 O OD1 . ASP B 2 106 ? 48.19971  40.90228  29.33730  1.000 86.76993  ?  73  ASP D OD1 1 
ATOM   2212 O OD2 . ASP B 2 106 ? 47.45950  42.86114  29.99807  1.000 70.35929  -1 73  ASP D OD2 1 
ATOM   2213 N N   . THR B 2 107 ? 50.75947  43.77108  25.85640  1.000 51.97377  ?  74  THR D N   1 
ATOM   2214 C CA  . THR B 2 107 ? 51.00281  44.32384  24.53083  1.000 57.10813  ?  74  THR D CA  1 
ATOM   2215 C C   . THR B 2 107 ? 52.23699  43.74302  23.85241  1.000 59.24808  ?  74  THR D C   1 
ATOM   2216 O O   . THR B 2 107 ? 52.41640  43.95960  22.64904  1.000 52.97678  ?  74  THR D O   1 
ATOM   2217 C CB  . THR B 2 107 ? 51.13785  45.84706  24.61142  1.000 51.48698  ?  74  THR D CB  1 
ATOM   2218 O OG1 . THR B 2 107 ? 52.31960  46.18727  25.34666  1.000 55.82995  ?  74  THR D OG1 1 
ATOM   2219 C CG2 . THR B 2 107 ? 49.92938  46.44829  25.30805  1.000 54.45586  ?  74  THR D CG2 1 
ATOM   2220 N N   . VAL B 2 108 ? 53.08967  43.02188  24.58022  1.000 43.25134  ?  75  VAL D N   1 
ATOM   2221 C CA  . VAL B 2 108 ? 54.28840  42.44069  23.98504  1.000 51.06355  ?  75  VAL D CA  1 
ATOM   2222 C C   . VAL B 2 108 ? 54.31818  40.93882  24.23540  1.000 48.04443  ?  75  VAL D C   1 
ATOM   2223 O O   . VAL B 2 108 ? 54.28943  40.14222  23.29052  1.000 44.34718  ?  75  VAL D O   1 
ATOM   2224 C CB  . VAL B 2 108 ? 55.56923  43.10323  24.52543  1.000 50.47213  ?  75  VAL D CB  1 
ATOM   2225 C CG1 . VAL B 2 108 ? 56.77385  42.63983  23.72447  1.000 50.22882  ?  75  VAL D CG1 1 
ATOM   2226 C CG2 . VAL B 2 108 ? 55.44998  44.61779  24.49513  1.000 41.27679  ?  75  VAL D CG2 1 
ATOM   2227 N N   . CYS B 2 109 ? 54.38371  40.54390  25.50927  1.000 48.92132  ?  76  CYS D N   1 
ATOM   2228 C CA  . CYS B 2 109 ? 54.51984  39.13015  25.84860  1.000 43.40840  ?  76  CYS D CA  1 
ATOM   2229 C C   . CYS B 2 109 ? 53.32400  38.32556  25.35232  1.000 55.34940  ?  76  CYS D C   1 
ATOM   2230 O O   . CYS B 2 109 ? 53.47754  37.35563  24.60119  1.000 53.79670  ?  76  CYS D O   1 
ATOM   2231 C CB  . CYS B 2 109 ? 54.68890  38.96369  27.36071  1.000 47.33763  ?  76  CYS D CB  1 
ATOM   2232 S SG  . CYS B 2 109 ? 56.19153  39.69014  28.06035  1.000 58.21113  ?  76  CYS D SG  1 
ATOM   2233 N N   . ARG B 2 110 ? 52.11701  38.71758  25.76593  1.000 63.07371  ?  77  ARG D N   1 
ATOM   2234 C CA  . ARG B 2 110 ? 50.92607  37.96834  25.37911  1.000 47.06642  ?  77  ARG D CA  1 
ATOM   2235 C C   . ARG B 2 110 ? 50.65408  38.09181  23.88532  1.000 47.86806  ?  77  ARG D C   1 
ATOM   2236 O O   . ARG B 2 110 ? 50.19042  37.13655  23.25175  1.000 54.98712  ?  77  ARG D O   1 
ATOM   2237 C CB  . ARG B 2 110 ? 49.72006  38.44914  26.18483  1.000 47.89379  ?  77  ARG D CB  1 
ATOM   2238 C CG  . ARG B 2 110 ? 48.48235  37.58421  26.02002  1.000 65.74051  ?  77  ARG D CG  1 
ATOM   2239 C CD  . ARG B 2 110 ? 47.29591  38.16953  26.76612  1.000 74.29457  ?  77  ARG D CD  1 
ATOM   2240 N NE  . ARG B 2 110 ? 47.61583  38.46521  28.15747  1.000 74.59279  ?  77  ARG D NE  1 
ATOM   2241 C CZ  . ARG B 2 110 ? 47.54581  37.58474  29.14618  1.000 70.44574  ?  77  ARG D CZ  1 
ATOM   2242 N NH1 . ARG B 2 110 ? 47.17978  36.33184  28.93116  1.000 64.57173  ?  77  ARG D NH1 1 
ATOM   2243 N NH2 . ARG B 2 110 ? 47.85256  37.97069  30.38145  1.000 78.40882  ?  77  ARG D NH2 1 
ATOM   2244 N N   . HIS B 2 111 ? 50.93972  39.25771  23.30462  1.000 41.38356  ?  78  HIS D N   1 
ATOM   2245 C CA  . HIS B 2 111 ? 50.67335  39.46223  21.88496  1.000 42.07009  ?  78  HIS D CA  1 
ATOM   2246 C C   . HIS B 2 111 ? 51.59378  38.60812  21.02044  1.000 51.41146  ?  78  HIS D C   1 
ATOM   2247 O O   . HIS B 2 111 ? 51.14249  37.96378  20.06634  1.000 47.86539  ?  78  HIS D O   1 
ATOM   2248 C CB  . HIS B 2 111 ? 50.82064  40.94286  21.53511  1.000 40.83176  ?  78  HIS D CB  1 
ATOM   2249 C CG  . HIS B 2 111 ? 50.79443  41.22134  20.06497  1.000 41.48996  ?  78  HIS D CG  1 
ATOM   2250 N ND1 . HIS B 2 111 ? 51.92743  41.18512  19.28121  1.000 52.03435  ?  78  HIS D ND1 1 
ATOM   2251 C CD2 . HIS B 2 111 ? 49.77381  41.54421  19.23598  1.000 47.36758  ?  78  HIS D CD2 1 
ATOM   2252 C CE1 . HIS B 2 111 ? 51.60574  41.47160  18.03262  1.000 49.64249  ?  78  HIS D CE1 1 
ATOM   2253 N NE2 . HIS B 2 111 ? 50.30495  41.69329  17.97791  1.000 45.28807  ?  78  HIS D NE2 1 
ATOM   2254 N N   . ASN B 2 112 ? 52.89056  38.58791  21.34055  1.000 47.54496  ?  79  ASN D N   1 
ATOM   2255 C CA  . ASN B 2 112 ? 53.84146  37.85159  20.51265  1.000 45.08059  ?  79  ASN D CA  1 
ATOM   2256 C C   . ASN B 2 112 ? 53.59000  36.34981  20.56984  1.000 51.92909  ?  79  ASN D C   1 
ATOM   2257 O O   . ASN B 2 112 ? 53.64938  35.66907  19.53978  1.000 55.10615  ?  79  ASN D O   1 
ATOM   2258 C CB  . ASN B 2 112 ? 55.27410  38.17329  20.93763  1.000 50.49193  ?  79  ASN D CB  1 
ATOM   2259 C CG  . ASN B 2 112 ? 55.75798  39.50348  20.39377  1.000 49.64888  ?  79  ASN D CG  1 
ATOM   2260 O OD1 . ASN B 2 112 ? 55.32364  39.94692  19.33070  1.000 52.84600  ?  79  ASN D OD1 1 
ATOM   2261 N ND2 . ASN B 2 112 ? 56.66494  40.14555  21.11933  1.000 43.62700  ?  79  ASN D ND2 1 
ATOM   2262 N N   . TYR B 2 113 ? 53.30376  35.81451  21.75897  1.000 50.82680  ?  80  TYR D N   1 
ATOM   2263 C CA  . TYR B 2 113 ? 53.07245  34.37816  21.88411  1.000 47.30996  ?  80  TYR D CA  1 
ATOM   2264 C C   . TYR B 2 113 ? 51.81823  33.95595  21.12787  1.000 56.89568  ?  80  TYR D C   1 
ATOM   2265 O O   . TYR B 2 113 ? 51.85644  33.03024  20.30907  1.000 61.16034  ?  80  TYR D O   1 
ATOM   2266 C CB  . TYR B 2 113 ? 52.97083  33.98727  23.35965  1.000 52.38731  ?  80  TYR D CB  1 
ATOM   2267 C CG  . TYR B 2 113 ? 52.98589  32.49257  23.60509  1.000 61.01062  ?  80  TYR D CG  1 
ATOM   2268 C CD1 . TYR B 2 113 ? 51.81067  31.75124  23.58293  1.000 69.51018  ?  80  TYR D CD1 1 
ATOM   2269 C CD2 . TYR B 2 113 ? 54.17598  31.82379  23.86283  1.000 54.34615  ?  80  TYR D CD2 1 
ATOM   2270 C CE1 . TYR B 2 113 ? 51.82069  30.38675  23.80694  1.000 58.36592  ?  80  TYR D CE1 1 
ATOM   2271 C CE2 . TYR B 2 113 ? 54.19570  30.45904  24.08879  1.000 61.48569  ?  80  TYR D CE2 1 
ATOM   2272 C CZ  . TYR B 2 113 ? 53.01501  29.74618  24.05981  1.000 73.17564  ?  80  TYR D CZ  1 
ATOM   2273 O OH  . TYR B 2 113 ? 53.02674  28.38816  24.28364  1.000 78.65140  ?  80  TYR D OH  1 
ATOM   2274 N N   . GLU B 2 114 ? 50.69626  34.62842  21.38483  1.000 48.56700  ?  81  GLU D N   1 
ATOM   2275 C CA  . GLU B 2 114 ? 49.43461  34.28415  20.74252  1.000 51.88998  ?  81  GLU D CA  1 
ATOM   2276 C C   . GLU B 2 114 ? 49.35174  34.74632  19.29402  1.000 58.88041  ?  81  GLU D C   1 
ATOM   2277 O O   . GLU B 2 114 ? 48.36822  34.42618  18.61764  1.000 55.09764  ?  81  GLU D O   1 
ATOM   2278 C CB  . GLU B 2 114 ? 48.26396  34.88069  21.52924  1.000 51.35746  ?  81  GLU D CB  1 
ATOM   2279 C CG  . GLU B 2 114 ? 48.17186  34.40199  22.96629  1.000 51.64172  ?  81  GLU D CG  1 
ATOM   2280 C CD  . GLU B 2 114 ? 47.04584  35.06791  23.73269  1.000 79.27010  ?  81  GLU D CD  1 
ATOM   2281 O OE1 . GLU B 2 114 ? 46.35584  35.93014  23.14889  1.000 91.09487  ?  81  GLU D OE1 1 
ATOM   2282 O OE2 . GLU B 2 114 ? 46.85103  34.72940  24.91942  1.000 81.79980  -1 81  GLU D OE2 1 
ATOM   2283 N N   . GLY B 2 115 ? 50.34550  35.48109  18.80148  1.000 52.87007  ?  82  GLY D N   1 
ATOM   2284 C CA  . GLY B 2 115 ? 50.28524  36.03478  17.47078  1.000 51.51903  ?  82  GLY D CA  1 
ATOM   2285 C C   . GLY B 2 115 ? 51.34059  35.47945  16.53737  1.000 56.66944  ?  82  GLY D C   1 
ATOM   2286 O O   . GLY B 2 115 ? 51.18244  34.40550  15.94796  1.000 58.11346  ?  82  GLY D O   1 
ATOM   2287 N N   . PRO B 2 116 ? 52.44601  36.21426  16.38245  1.000 60.61242  ?  83  PRO D N   1 
ATOM   2288 C CA  . PRO B 2 116 ? 53.46174  35.79418  15.40209  1.000 51.75083  ?  83  PRO D CA  1 
ATOM   2289 C C   . PRO B 2 116 ? 54.14006  34.48049  15.74721  1.000 53.96188  ?  83  PRO D C   1 
ATOM   2290 O O   . PRO B 2 116 ? 54.41731  33.68404  14.84161  1.000 56.68940  ?  83  PRO D O   1 
ATOM   2291 C CB  . PRO B 2 116 ? 54.45129  36.96819  15.40468  1.000 49.93421  ?  83  PRO D CB  1 
ATOM   2292 C CG  . PRO B 2 116 ? 54.25208  37.63158  16.72957  1.000 55.81426  ?  83  PRO D CG  1 
ATOM   2293 C CD  . PRO B 2 116 ? 52.79243  37.48833  17.03302  1.000 49.29033  ?  83  PRO D CD  1 
ATOM   2294 N N   . GLU B 2 117 ? 54.42017  34.22556  17.02869  1.000 52.54280  ?  84  GLU D N   1 
ATOM   2295 C CA  . GLU B 2 117 ? 55.08919  32.98308  17.40036  1.000 51.51573  ?  84  GLU D CA  1 
ATOM   2296 C C   . GLU B 2 117 ? 54.24093  31.75714  17.09130  1.000 50.64340  ?  84  GLU D C   1 
ATOM   2297 O O   . GLU B 2 117 ? 54.79250  30.66637  16.90913  1.000 68.80006  ?  84  GLU D O   1 
ATOM   2298 C CB  . GLU B 2 117 ? 55.46083  32.99710  18.88581  1.000 44.21313  ?  84  GLU D CB  1 
ATOM   2299 C CG  . GLU B 2 117 ? 56.35526  34.15808  19.31294  1.000 54.28797  ?  84  GLU D CG  1 
ATOM   2300 C CD  . GLU B 2 117 ? 57.79036  34.03120  18.83053  1.000 64.65579  ?  84  GLU D CD  1 
ATOM   2301 O OE1 . GLU B 2 117 ? 58.11254  33.04912  18.13110  1.000 62.91563  ?  84  GLU D OE1 1 
ATOM   2302 O OE2 . GLU B 2 117 ? 58.60354  34.92112  19.15806  1.000 62.62118  -1 84  GLU D OE2 1 
ATOM   2303 N N   . THR B 2 118 ? 52.91590  31.90997  17.02568  1.000 54.92907  ?  85  THR D N   1 
ATOM   2304 C CA  . THR B 2 118 ? 52.05982  30.78964  16.65017  1.000 60.92165  ?  85  THR D CA  1 
ATOM   2305 C C   . THR B 2 118 ? 52.28142  30.38141  15.19851  1.000 68.66924  ?  85  THR D C   1 
ATOM   2306 O O   . THR B 2 118 ? 52.07243  29.21551  14.84331  1.000 73.28346  ?  85  THR D O   1 
ATOM   2307 C CB  . THR B 2 118 ? 50.59138  31.14947  16.88687  1.000 54.03213  ?  85  THR D CB  1 
ATOM   2308 O OG1 . THR B 2 118 ? 50.43740  31.68428  18.20726  1.000 64.33155  ?  85  THR D OG1 1 
ATOM   2309 C CG2 . THR B 2 118 ? 49.70467  29.92119  16.74754  1.000 83.70592  ?  85  THR D CG2 1 
ATOM   2310 N N   . HIS B 2 119 ? 52.71366  31.31683  14.35215  1.000 72.37512  ?  86  HIS D N   1 
ATOM   2311 C CA  . HIS B 2 119 ? 52.98282  31.01870  12.95226  1.000 70.13672  ?  86  HIS D CA  1 
ATOM   2312 C C   . HIS B 2 119 ? 54.43470  30.64546  12.68688  1.000 71.76655  ?  86  HIS D C   1 
ATOM   2313 O O   . HIS B 2 119 ? 54.72420  30.05319  11.64100  1.000 67.75008  ?  86  HIS D O   1 
ATOM   2314 C CB  . HIS B 2 119 ? 52.61115  32.21673  12.07077  1.000 69.05752  ?  86  HIS D CB  1 
ATOM   2315 C CG  . HIS B 2 119 ? 51.17494  32.62674  12.17511  1.000 72.64601  ?  86  HIS D CG  1 
ATOM   2316 N ND1 . HIS B 2 119 ? 50.68975  33.38022  13.22232  1.000 69.90858  ?  86  HIS D ND1 1 
ATOM   2317 C CD2 . HIS B 2 119 ? 50.11966  32.39315  11.35935  1.000 61.09333  ?  86  HIS D CD2 1 
ATOM   2318 C CE1 . HIS B 2 119 ? 49.39725  33.59107  13.04864  1.000 72.54904  ?  86  HIS D CE1 1 
ATOM   2319 N NE2 . HIS B 2 119 ? 49.02646  33.00243  11.92584  1.000 88.57060  ?  86  HIS D NE2 1 
ATOM   2320 N N   . THR B 2 120 ? 55.34874  30.96835  13.60204  1.000 58.36831  ?  87  THR D N   1 
ATOM   2321 C CA  . THR B 2 120 ? 56.77071  30.76385  13.35420  1.000 59.52635  ?  87  THR D CA  1 
ATOM   2322 C C   . THR B 2 120 ? 57.37885  29.72886  14.29431  1.000 66.55906  ?  87  THR D C   1 
ATOM   2323 O O   . THR B 2 120 ? 57.47096  28.54704  13.94647  1.000 63.86169  ?  87  THR D O   1 
ATOM   2324 C CB  . THR B 2 120 ? 57.52737  32.08929  13.47937  1.000 48.53511  ?  87  THR D CB  1 
ATOM   2325 O OG1 . THR B 2 120 ? 57.27597  32.66718  14.76626  1.000 50.05859  ?  87  THR D OG1 1 
ATOM   2326 C CG2 . THR B 2 120 ? 57.08240  33.06048  12.39825  1.000 46.27579  ?  87  THR D CG2 1 
ATOM   2327 N N   . SER B 2 121 ? 57.79592  30.16532  15.48586  1.000 58.51019  ?  88  SER D N   1 
ATOM   2328 C CA  . SER B 2 121 ? 58.57731  29.30164  16.36794  1.000 52.22718  ?  88  SER D CA  1 
ATOM   2329 C C   . SER B 2 121 ? 57.76584  28.10108  16.83922  1.000 56.06405  ?  88  SER D C   1 
ATOM   2330 O O   . SER B 2 121 ? 58.22610  26.95612  16.75867  1.000 64.00204  ?  88  SER D O   1 
ATOM   2331 C CB  . SER B 2 121 ? 59.08972  30.10299  17.56343  1.000 51.11185  ?  88  SER D CB  1 
ATOM   2332 O OG  . SER B 2 121 ? 59.79659  31.25579  17.14276  1.000 66.28211  ?  88  SER D OG  1 
ATOM   2333 N N   . LEU B 2 122 ? 56.55178  28.34317  17.33688  1.000 49.68676  ?  89  LEU D N   1 
ATOM   2334 C CA  . LEU B 2 122 ? 55.71824  27.26523  17.85597  1.000 54.63449  ?  89  LEU D CA  1 
ATOM   2335 C C   . LEU B 2 122 ? 55.26202  26.29110  16.77691  1.000 55.12853  ?  89  LEU D C   1 
ATOM   2336 O O   . LEU B 2 122 ? 54.65679  25.26679  17.11040  1.000 61.71243  ?  89  LEU D O   1 
ATOM   2337 C CB  . LEU B 2 122 ? 54.50128  27.84939  18.57515  1.000 52.46427  ?  89  LEU D CB  1 
ATOM   2338 C CG  . LEU B 2 122 ? 54.81008  28.77559  19.75360  1.000 54.07040  ?  89  LEU D CG  1 
ATOM   2339 C CD1 . LEU B 2 122 ? 53.52774  29.31599  20.36605  1.000 63.04310  ?  89  LEU D CD1 1 
ATOM   2340 C CD2 . LEU B 2 122 ? 55.64412  28.05263  20.79921  1.000 54.69260  ?  89  LEU D CD2 1 
ATOM   2341 N N   . ARG B 2 123 ? 55.53602  26.57853  15.50266  1.000 64.52144  ?  90  ARG D N   1 
ATOM   2342 C CA  . ARG B 2 123 ? 55.16630  25.69509  14.40738  1.000 71.62971  ?  90  ARG D CA  1 
ATOM   2343 C C   . ARG B 2 123 ? 56.35432  24.98502  13.77338  1.000 64.85960  ?  90  ARG D C   1 
ATOM   2344 O O   . ARG B 2 123 ? 56.16322  23.93922  13.14430  1.000 69.71427  ?  90  ARG D O   1 
ATOM   2345 C CB  . ARG B 2 123 ? 54.40849  26.48521  13.32705  1.000 69.20495  ?  90  ARG D CB  1 
ATOM   2346 C CG  . ARG B 2 123 ? 53.83125  25.64251  12.19983  1.000 90.71728  ?  90  ARG D CG  1 
ATOM   2347 C CD  . ARG B 2 123 ? 52.74198  26.38825  11.45132  1.000 97.22883  ?  90  ARG D CD  1 
ATOM   2348 N NE  . ARG B 2 123 ? 51.56328  26.59282  12.28427  1.000 122.87989 ?  90  ARG D NE  1 
ATOM   2349 C CZ  . ARG B 2 123 ? 50.58928  25.70519  12.43183  1.000 135.78525 ?  90  ARG D CZ  1 
ATOM   2350 N NH1 . ARG B 2 123 ? 50.61972  24.53636  11.81243  1.000 125.37101 ?  90  ARG D NH1 1 
ATOM   2351 N NH2 . ARG B 2 123 ? 49.55985  25.99659  13.22198  1.000 137.16013 ?  90  ARG D NH2 1 
ATOM   2352 N N   . ARG B 2 124 ? 57.56705  25.50883  13.93849  1.000 65.43895  ?  91  ARG D N   1 
ATOM   2353 C CA  . ARG B 2 124 ? 58.74398  24.89385  13.33721  1.000 68.40496  ?  91  ARG D CA  1 
ATOM   2354 C C   . ARG B 2 124 ? 58.97478  23.49978  13.90573  1.000 67.86363  ?  91  ARG D C   1 
ATOM   2355 O O   . ARG B 2 124 ? 59.07837  23.32327  15.12367  1.000 71.80600  ?  91  ARG D O   1 
ATOM   2356 C CB  . ARG B 2 124 ? 59.97276  25.77111  13.57048  1.000 62.02211  ?  91  ARG D CB  1 
ATOM   2357 C CG  . ARG B 2 124 ? 61.28092  25.10674  13.17281  1.000 67.47852  ?  91  ARG D CG  1 
ATOM   2358 C CD  . ARG B 2 124 ? 62.46418  26.03707  13.36996  1.000 56.60374  ?  91  ARG D CD  1 
ATOM   2359 N NE  . ARG B 2 124 ? 63.72666  25.38554  13.04249  1.000 51.51673  ?  91  ARG D NE  1 
ATOM   2360 C CZ  . ARG B 2 124 ? 64.22480  25.28918  11.81744  1.000 52.39339  ?  91  ARG D CZ  1 
ATOM   2361 N NH1 . ARG B 2 124 ? 63.58420  25.78181  10.76999  1.000 52.60990  ?  91  ARG D NH1 1 
ATOM   2362 N NH2 . ARG B 2 124 ? 65.39477  24.68222  11.63860  1.000 57.54544  ?  91  ARG D NH2 1 
ATOM   2363 N N   . LEU B 2 125 ? 59.05409  22.51055  13.01775  1.000 72.71855  ?  92  LEU D N   1 
ATOM   2364 C CA  . LEU B 2 125 ? 59.34282  21.13260  13.39894  1.000 69.98572  ?  92  LEU D CA  1 
ATOM   2365 C C   . LEU B 2 125 ? 60.36692  20.56825  12.42835  1.000 76.65846  ?  92  LEU D C   1 
ATOM   2366 O O   . LEU B 2 125 ? 60.14252  20.57525  11.21430  1.000 75.35496  ?  92  LEU D O   1 
ATOM   2367 C CB  . LEU B 2 125 ? 58.07457  20.27270  13.40069  1.000 65.62493  ?  92  LEU D CB  1 
ATOM   2368 C CG  . LEU B 2 125 ? 57.06385  20.52399  14.52106  1.000 65.43371  ?  92  LEU D CG  1 
ATOM   2369 C CD1 . LEU B 2 125 ? 55.90732  19.54181  14.42644  1.000 68.95365  ?  92  LEU D CD1 1 
ATOM   2370 C CD2 . LEU B 2 125 ? 57.73725  20.43114  15.88051  1.000 71.05930  ?  92  LEU D CD2 1 
ATOM   2371 N N   . GLU B 2 126 ? 61.48678  20.08659  12.96118  1.000 87.66162  ?  93  GLU D N   1 
ATOM   2372 C CA  . GLU B 2 126 ? 62.54312  19.47105  12.16781  1.000 75.89939  ?  93  GLU D CA  1 
ATOM   2373 C C   . GLU B 2 126 ? 62.75466  18.05013  12.66746  1.000 85.54432  ?  93  GLU D C   1 
ATOM   2374 O O   . GLU B 2 126 ? 63.02951  17.84078  13.85391  1.000 88.43213  ?  93  GLU D O   1 
ATOM   2375 C CB  . GLU B 2 126 ? 63.83999  20.27882  12.25348  1.000 82.31625  ?  93  GLU D CB  1 
ATOM   2376 C CG  . GLU B 2 126 ? 63.74029  21.67364  11.65447  1.000 82.53224  ?  93  GLU D CG  1 
ATOM   2377 C CD  . GLU B 2 126 ? 63.51678  21.65180  10.15350  1.000 94.01804  ?  93  GLU D CD  1 
ATOM   2378 O OE1 . GLU B 2 126 ? 63.97661  20.69514  9.49501   1.000 104.13751 ?  93  GLU D OE1 1 
ATOM   2379 O OE2 . GLU B 2 126 ? 62.87824  22.59020  9.63174   1.000 102.24559 -1 93  GLU D OE2 1 
ATOM   2380 N N   . GLN B 2 127 ? 62.62266  17.08053  11.76587  1.000 89.35750  ?  94  GLN D N   1 
ATOM   2381 C CA  . GLN B 2 127 ? 62.73448  15.68052  12.14967  1.000 87.72599  ?  94  GLN D CA  1 
ATOM   2382 C C   . GLN B 2 127 ? 64.19666  15.31145  12.39527  1.000 93.38780  ?  94  GLN D C   1 
ATOM   2383 O O   . GLN B 2 127 ? 65.08527  15.77339  11.67451  1.000 92.35938  ?  94  GLN D O   1 
ATOM   2384 C CB  . GLN B 2 127 ? 62.14238  14.78057  11.06951  1.000 101.19269 ?  94  GLN D CB  1 
ATOM   2385 C CG  . GLN B 2 127 ? 60.65835  15.00451  10.83587  1.000 100.17362 ?  94  GLN D CG  1 
ATOM   2386 C CD  . GLN B 2 127 ? 60.12353  14.19044  9.67795   1.000 93.41621  ?  94  GLN D CD  1 
ATOM   2387 O OE1 . GLN B 2 127 ? 60.88326  13.54691  8.95441   1.000 82.98721  ?  94  GLN D OE1 1 
ATOM   2388 N NE2 . GLN B 2 127 ? 58.80832  14.21398  9.49532   1.000 103.45047 ?  94  GLN D NE2 1 
ATOM   2389 N N   . PRO B 2 128 ? 64.46983  14.48860  13.40148  1.000 87.12869  ?  95  PRO D N   1 
ATOM   2390 C CA  . PRO B 2 128 ? 65.85641  14.15955  13.73898  1.000 83.18180  ?  95  PRO D CA  1 
ATOM   2391 C C   . PRO B 2 128 ? 66.42701  13.07157  12.84002  1.000 88.33588  ?  95  PRO D C   1 
ATOM   2392 O O   . PRO B 2 128 ? 65.70708  12.27375  12.23718  1.000 94.53891  ?  95  PRO D O   1 
ATOM   2393 C CB  . PRO B 2 128 ? 65.76290  13.66572  15.19032  1.000 77.66581  ?  95  PRO D CB  1 
ATOM   2394 C CG  . PRO B 2 128 ? 64.34168  13.93826  15.63403  1.000 88.15903  ?  95  PRO D CG  1 
ATOM   2395 C CD  . PRO B 2 128 ? 63.52445  13.94909  14.38903  1.000 91.15734  ?  95  PRO D CD  1 
ATOM   2396 N N   A ASN B 2 129 ? 67.75507  13.06150  12.75928  0.500 89.06119  ?  96  ASN D N   1 
ATOM   2397 N N   B ASN B 2 129 ? 67.75487  13.05223  12.76566  0.500 89.05998  ?  96  ASN D N   1 
ATOM   2398 C CA  A ASN B 2 129 ? 68.50815  12.03733  12.04730  0.500 83.69541  ?  96  ASN D CA  1 
ATOM   2399 C CA  B ASN B 2 129 ? 68.49380  12.02756  12.04051  0.500 83.72496  ?  96  ASN D CA  1 
ATOM   2400 C C   A ASN B 2 129 ? 69.27464  11.19788  13.05925  0.500 93.28866  ?  96  ASN D C   1 
ATOM   2401 C C   B ASN B 2 129 ? 69.29120  11.19758  13.03673  0.500 93.29639  ?  96  ASN D C   1 
ATOM   2402 O O   A ASN B 2 129 ? 69.96354  11.74443  13.92658  0.500 92.70453  ?  96  ASN D O   1 
ATOM   2403 O O   B ASN B 2 129 ? 70.01537  11.75046  13.87089  0.500 92.75834  ?  96  ASN D O   1 
ATOM   2404 C CB  A ASN B 2 129 ? 69.47527  12.66236  11.03843  0.500 82.58799  ?  96  ASN D CB  1 
ATOM   2405 C CB  B ASN B 2 129 ? 69.42551  12.64939  10.99794  0.500 82.63485  ?  96  ASN D CB  1 
ATOM   2406 C CG  A ASN B 2 129 ? 68.76503  13.27291  9.84742   0.500 81.39973  ?  96  ASN D CG  1 
ATOM   2407 C CG  B ASN B 2 129 ? 69.89995  11.64245  9.96798   0.500 95.59917  ?  96  ASN D CG  1 
ATOM   2408 O OD1 A ASN B 2 129 ? 67.77978  12.72777  9.35100   0.500 83.13647  ?  96  ASN D OD1 1 
ATOM   2409 O OD1 B ASN B 2 129 ? 69.17652  10.70947  9.61682   0.500 89.72652  ?  96  ASN D OD1 1 
ATOM   2410 N ND2 A ASN B 2 129 ? 69.26528  14.41079  9.38014   0.500 78.66414  ?  96  ASN D ND2 1 
ATOM   2411 N ND2 B ASN B 2 129 ? 71.12135  11.82451  9.47979   0.500 90.98378  ?  96  ASN D ND2 1 
ATOM   2412 N N   . VAL B 2 130 ? 69.15755  9.87699   12.94842  1.000 98.16215  ?  97  VAL D N   1 
ATOM   2413 C CA  . VAL B 2 130 ? 69.75856  8.94971   13.90069  1.000 93.44266  ?  97  VAL D CA  1 
ATOM   2414 C C   . VAL B 2 130 ? 70.79090  8.09321   13.18034  1.000 96.29072  ?  97  VAL D C   1 
ATOM   2415 O O   . VAL B 2 130 ? 70.49232  7.48852   12.14424  1.000 113.95349 ?  97  VAL D O   1 
ATOM   2416 C CB  . VAL B 2 130 ? 68.69101  8.06900   14.57469  1.000 99.66004  ?  97  VAL D CB  1 
ATOM   2417 C CG1 . VAL B 2 130 ? 69.32288  7.19461   15.64192  1.000 105.26290 ?  97  VAL D CG1 1 
ATOM   2418 C CG2 . VAL B 2 130 ? 67.58691  8.93195   15.17096  1.000 92.14562  ?  97  VAL D CG2 1 
ATOM   2419 N N   . VAL B 2 131 ? 72.00405  8.04514   13.72670  1.000 105.54814 ?  98  VAL D N   1 
ATOM   2420 C CA  . VAL B 2 131 ? 73.05045  7.14885   13.25212  1.000 111.44735 ?  98  VAL D CA  1 
ATOM   2421 C C   . VAL B 2 131 ? 73.59409  6.39802   14.45434  1.000 107.23033 ?  98  VAL D C   1 
ATOM   2422 O O   . VAL B 2 131 ? 73.54563  6.88878   15.58613  1.000 114.37648 ?  98  VAL D O   1 
ATOM   2423 C CB  . VAL B 2 131 ? 74.18174  7.89330   12.50987  1.000 116.45180 ?  98  VAL D CB  1 
ATOM   2424 C CG1 . VAL B 2 131 ? 73.67058  8.43165   11.18941  1.000 126.23668 ?  98  VAL D CG1 1 
ATOM   2425 C CG2 . VAL B 2 131 ? 74.74741  9.01014   13.37702  1.000 123.87017 ?  98  VAL D CG2 1 
ATOM   2426 N N   . ILE B 2 132 ? 74.11545  5.20090   14.21015  1.000 119.30499 ?  99  ILE D N   1 
ATOM   2427 C CA  . ILE B 2 132 ? 74.34798  4.28577   15.31474  1.000 125.94800 ?  99  ILE D CA  1 
ATOM   2428 C C   . ILE B 2 132 ? 75.78638  3.76597   15.34316  1.000 122.84928 ?  99  ILE D C   1 
ATOM   2429 O O   . ILE B 2 132 ? 76.07950  2.77545   16.01849  1.000 126.36732 ?  99  ILE D O   1 
ATOM   2430 C CB  . ILE B 2 132 ? 73.31827  3.14037   15.28525  1.000 119.17787 ?  99  ILE D CB  1 
ATOM   2431 C CG1 . ILE B 2 132 ? 73.08255  2.63772   16.70666  1.000 116.71688 ?  99  ILE D CG1 1 
ATOM   2432 C CG2 . ILE B 2 132 ? 73.70719  2.04580   14.27593  1.000 125.02428 ?  99  ILE D CG2 1 
ATOM   2433 C CD1 . ILE B 2 132 ? 72.89770  3.77359   17.68834  1.000 128.76440 ?  99  ILE D CD1 1 
ATOM   2434 N N   . SER B 2 133 ? 76.69623  4.44866   14.64881  1.000 127.44235 ?  100 SER D N   1 
ATOM   2435 C CA  . SER B 2 133 ? 78.10236  4.06223   14.64757  1.000 134.73853 ?  100 SER D CA  1 
ATOM   2436 C C   . SER B 2 133 ? 78.64862  3.97836   16.06882  1.000 133.80286 ?  100 SER D C   1 
ATOM   2437 O O   . SER B 2 133 ? 78.25303  4.73603   16.95852  1.000 136.71398 ?  100 SER D O   1 
ATOM   2438 C CB  . SER B 2 133 ? 78.92795  5.05893   13.82880  1.000 132.90223 ?  100 SER D CB  1 
ATOM   2439 O OG  . SER B 2 133 ? 78.91596  6.34647   14.42112  1.000 137.45752 ?  100 SER D OG  1 
ATOM   2440 N N   . LEU B 2 134 ? 79.57034  3.04081   16.27262  1.000 123.01760 ?  101 LEU D N   1 
ATOM   2441 C CA  . LEU B 2 134 ? 80.11469  2.73966   17.58592  1.000 134.52375 ?  101 LEU D CA  1 
ATOM   2442 C C   . LEU B 2 134 ? 81.62943  2.88444   17.57871  1.000 140.80578 ?  101 LEU D C   1 
ATOM   2443 O O   . LEU B 2 134 ? 82.28733  2.67038   16.55582  1.000 130.16150 ?  101 LEU D O   1 
ATOM   2444 C CB  . LEU B 2 134 ? 79.74137  1.32078   18.02917  1.000 138.27124 ?  101 LEU D CB  1 
ATOM   2445 N N   . SER B 2 135 ? 82.16960  3.24671   18.73954  1.000 141.94504 ?  102 SER D N   1 
ATOM   2446 C CA  . SER B 2 135 ? 83.60036  3.38470   18.97524  1.000 153.84788 ?  102 SER D CA  1 
ATOM   2447 C C   . SER B 2 135 ? 83.80973  3.58279   20.46835  1.000 164.69165 ?  102 SER D C   1 
ATOM   2448 O O   . SER B 2 135 ? 82.99735  4.23002   21.13560  1.000 170.67637 ?  102 SER D O   1 
ATOM   2449 C CB  . SER B 2 135 ? 84.19769  4.55711   18.18578  1.000 151.51441 ?  102 SER D CB  1 
ATOM   2450 O OG  . SER B 2 135 ? 83.51332  5.76437   18.46889  1.000 137.39564 ?  102 SER D OG  1 
ATOM   2451 N N   . ARG B 2 136 ? 84.89985  3.01835   20.98496  1.000 153.22690 ?  103 ARG D N   1 
ATOM   2452 C CA  . ARG B 2 136 ? 85.16771  3.03584   22.41553  1.000 155.11291 ?  103 ARG D CA  1 
ATOM   2453 C C   . ARG B 2 136 ? 86.65719  3.23201   22.66072  1.000 174.99520 ?  103 ARG D C   1 
ATOM   2454 O O   . ARG B 2 136 ? 87.48223  3.13086   21.74875  1.000 186.21122 ?  103 ARG D O   1 
ATOM   2455 C CB  . ARG B 2 136 ? 84.68435  1.74592   23.08975  1.000 177.40073 ?  103 ARG D CB  1 
ATOM   2456 N N   . THR B 2 137 ? 86.99339  3.51548   23.91607  1.000 182.02906 ?  104 THR D N   1 
ATOM   2457 C CA  . THR B 2 137 ? 88.38236  3.68011   24.32916  1.000 174.14373 ?  104 THR D CA  1 
ATOM   2458 C C   . THR B 2 137 ? 88.70980  2.75409   25.49662  1.000 151.04122 ?  104 THR D C   1 
ATOM   2459 O O   . THR B 2 137 ? 89.50918  3.09530   26.36838  1.000 152.35390 ?  104 THR D O   1 
ATOM   2460 C CB  . THR B 2 137 ? 88.68826  5.13504   24.73630  1.000 176.79025 ?  104 THR D CB  1 
ATOM   2461 O OG1 . THR B 2 137 ? 87.82967  5.52433   25.81567  1.000 173.93084 ?  104 THR D OG1 1 
ATOM   2462 C CG2 . THR B 2 137 ? 88.47738  6.07639   23.55979  1.000 150.23639 ?  104 THR D CG2 1 
ATOM   2463 N N   . THR B 2 145 ? 81.56587  4.04472   24.17641  1.000 157.33878 ?  112 THR D N   1 
ATOM   2464 C CA  . THR B 2 145 ? 81.15228  2.75992   23.62510  1.000 158.20241 ?  112 THR D CA  1 
ATOM   2465 C C   . THR B 2 145 ? 79.72548  2.82794   23.09081  1.000 172.53275 ?  112 THR D C   1 
ATOM   2466 O O   . THR B 2 145 ? 78.81011  3.20073   23.82069  1.000 179.99636 ?  112 THR D O   1 
ATOM   2467 C CB  . THR B 2 145 ? 81.23352  1.63596   24.67920  1.000 173.20621 ?  112 THR D CB  1 
ATOM   2468 O OG1 . THR B 2 145 ? 82.49212  1.69965   25.36095  1.000 176.23225 ?  112 THR D OG1 1 
ATOM   2469 C CG2 . THR B 2 145 ? 81.09083  0.27326   24.01731  1.000 165.34528 ?  112 THR D CG2 1 
ATOM   2470 N N   . LEU B 2 146 ? 79.55526  2.47622   21.81606  1.000 159.47924 ?  113 LEU D N   1 
ATOM   2471 C CA  . LEU B 2 146 ? 78.24705  2.34330   21.17005  1.000 152.36754 ?  113 LEU D CA  1 
ATOM   2472 C C   . LEU B 2 146 ? 77.34432  3.54033   21.48749  1.000 144.56646 ?  113 LEU D C   1 
ATOM   2473 O O   . LEU B 2 146 ? 76.41167  3.46992   22.28805  1.000 147.10348 ?  113 LEU D O   1 
ATOM   2474 C CB  . LEU B 2 146 ? 77.58797  1.02089   21.57711  1.000 128.71106 ?  113 LEU D CB  1 
ATOM   2475 C CG  . LEU B 2 146 ? 76.29669  0.60253   20.86900  1.000 128.63084 ?  113 LEU D CG  1 
ATOM   2476 C CD1 . LEU B 2 146 ? 76.43064  0.75222   19.36431  1.000 134.54918 ?  113 LEU D CD1 1 
ATOM   2477 C CD2 . LEU B 2 146 ? 75.93974  -0.83126  21.22963  1.000 146.76817 ?  113 LEU D CD2 1 
ATOM   2478 N N   . VAL B 2 147 ? 77.65696  4.65289   20.83275  1.000 127.26674 ?  114 VAL D N   1 
ATOM   2479 C CA  . VAL B 2 147 ? 76.94144  5.90439   21.04443  1.000 138.99330 ?  114 VAL D CA  1 
ATOM   2480 C C   . VAL B 2 147 ? 75.92847  6.09857   19.92575  1.000 128.33690 ?  114 VAL D C   1 
ATOM   2481 O O   . VAL B 2 147 ? 76.12171  5.64902   18.78993  1.000 119.58825 ?  114 VAL D O   1 
ATOM   2482 C CB  . VAL B 2 147 ? 77.91199  7.10196   21.13738  1.000 130.38719 ?  114 VAL D CB  1 
ATOM   2483 C CG1 . VAL B 2 147 ? 78.89320  6.89922   22.28161  1.000 133.16629 ?  114 VAL D CG1 1 
ATOM   2484 C CG2 . VAL B 2 147 ? 78.65242  7.29709   19.82368  1.000 128.61789 ?  114 VAL D CG2 1 
ATOM   2485 N N   . CYS B 2 148 ? 74.82856  6.76951   20.25688  1.000 119.34817 ?  115 CYS D N   1 
ATOM   2486 C CA  . CYS B 2 148 ? 73.76009  7.07651   19.31361  1.000 109.66242 ?  115 CYS D CA  1 
ATOM   2487 C C   . CYS B 2 148 ? 73.72987  8.58286   19.09322  1.000 96.80312  ?  115 CYS D C   1 
ATOM   2488 O O   . CYS B 2 148 ? 73.61177  9.35007   20.05421  1.000 97.92089  ?  115 CYS D O   1 
ATOM   2489 C CB  . CYS B 2 148 ? 72.41303  6.57150   19.83368  1.000 119.36829 ?  115 CYS D CB  1 
ATOM   2490 S SG  . CYS B 2 148 ? 70.99975  6.86586   18.73836  1.000 130.94567 ?  115 CYS D SG  1 
ATOM   2491 N N   . SER B 2 149 ? 73.84648  9.00238   17.83603  1.000 101.99158 ?  116 SER D N   1 
ATOM   2492 C CA  . SER B 2 149 ? 73.91444  10.41389  17.47685  1.000 93.76525  ?  116 SER D CA  1 
ATOM   2493 C C   . SER B 2 149 ? 72.58789  10.84295  16.86517  1.000 93.52371  ?  116 SER D C   1 
ATOM   2494 O O   . SER B 2 149 ? 72.18548  10.32384  15.81846  1.000 99.36848  ?  116 SER D O   1 
ATOM   2495 C CB  . SER B 2 149 ? 75.06318  10.67653  16.50367  1.000 104.86028 ?  116 SER D CB  1 
ATOM   2496 O OG  . SER B 2 149 ? 76.29885  10.24343  17.04382  1.000 131.13002 ?  116 SER D OG  1 
ATOM   2497 N N   . VAL B 2 150 ? 71.91876  11.79047  17.51535  1.000 84.17402  ?  117 VAL D N   1 
ATOM   2498 C CA  . VAL B 2 150 ? 70.64718  12.33569  17.05403  1.000 81.94144  ?  117 VAL D CA  1 
ATOM   2499 C C   . VAL B 2 150 ? 70.88188  13.80776  16.74889  1.000 88.21869  ?  117 VAL D C   1 
ATOM   2500 O O   . VAL B 2 150 ? 71.08654  14.61157  17.66730  1.000 79.63857  ?  117 VAL D O   1 
ATOM   2501 C CB  . VAL B 2 150 ? 69.53435  12.15451  18.09363  1.000 82.01199  ?  117 VAL D CB  1 
ATOM   2502 C CG1 . VAL B 2 150 ? 68.20576  12.60052  17.52716  1.000 80.39308  ?  117 VAL D CG1 1 
ATOM   2503 C CG2 . VAL B 2 150 ? 69.46801  10.70534  18.54903  1.000 86.52201  ?  117 VAL D CG2 1 
ATOM   2504 N N   . THR B 2 151 ? 70.85434  14.16640  15.46642  1.000 89.31921  ?  118 THR D N   1 
ATOM   2505 C CA  . THR B 2 151 ? 71.26752  15.49156  15.02870  1.000 81.83296  ?  118 THR D CA  1 
ATOM   2506 C C   . THR B 2 151 ? 70.16422  16.17170  14.23048  1.000 75.48882  ?  118 THR D C   1 
ATOM   2507 O O   . THR B 2 151 ? 69.29766  15.51943  13.64325  1.000 76.28761  ?  118 THR D O   1 
ATOM   2508 C CB  . THR B 2 151 ? 72.54566  15.42572  14.17694  1.000 84.88561  ?  118 THR D CB  1 
ATOM   2509 O OG1 . THR B 2 151 ? 72.29584  14.65488  12.99504  1.000 80.63651  ?  118 THR D OG1 1 
ATOM   2510 C CG2 . THR B 2 151 ? 73.67944  14.78419  14.96267  1.000 76.80591  ?  118 THR D CG2 1 
ATOM   2511 N N   . ASP B 2 152 ? 70.21890  17.50653  14.22664  1.000 91.67481  ?  119 ASP D N   1 
ATOM   2512 C CA  . ASP B 2 152 ? 69.35478  18.35455  13.41104  1.000 88.64572  ?  119 ASP D CA  1 
ATOM   2513 C C   . ASP B 2 152 ? 67.87641  18.12904  13.70302  1.000 86.19036  ?  119 ASP D C   1 
ATOM   2514 O O   . ASP B 2 152 ? 67.17475  17.47765  12.92249  1.000 108.67932 ?  119 ASP D O   1 
ATOM   2515 C CB  . ASP B 2 152 ? 69.64073  18.12894  11.92383  1.000 87.75968  ?  119 ASP D CB  1 
ATOM   2516 C CG  . ASP B 2 152 ? 71.06897  18.47379  11.54695  1.000 100.75394 ?  119 ASP D CG  1 
ATOM   2517 O OD1 . ASP B 2 152 ? 71.82315  18.93659  12.42892  1.000 90.54873  ?  119 ASP D OD1 1 
ATOM   2518 O OD2 . ASP B 2 152 ? 71.43798  18.28028  10.36907  1.000 103.50293 -1 119 ASP D OD2 1 
ATOM   2519 N N   . PHE B 2 153 ? 67.39287  18.67305  14.81752  1.000 70.05532  ?  120 PHE D N   1 
ATOM   2520 C CA  . PHE B 2 153 ? 65.98328  18.57287  15.16268  1.000 66.34312  ?  120 PHE D CA  1 
ATOM   2521 C C   . PHE B 2 153 ? 65.56350  19.82327  15.92074  1.000 73.82900  ?  120 PHE D C   1 
ATOM   2522 O O   . PHE B 2 153 ? 66.39611  20.56647  16.44700  1.000 66.16780  ?  120 PHE D O   1 
ATOM   2523 C CB  . PHE B 2 153 ? 65.68739  17.31418  15.98982  1.000 67.49072  ?  120 PHE D CB  1 
ATOM   2524 C CG  . PHE B 2 153 ? 66.45301  17.23764  17.28117  1.000 70.85362  ?  120 PHE D CG  1 
ATOM   2525 C CD1 . PHE B 2 153 ? 65.93445  17.78296  18.44485  1.000 65.65436  ?  120 PHE D CD1 1 
ATOM   2526 C CD2 . PHE B 2 153 ? 67.68662  16.61003  17.33389  1.000 75.15613  ?  120 PHE D CD2 1 
ATOM   2527 C CE1 . PHE B 2 153 ? 66.63507  17.71178  19.63362  1.000 65.65177  ?  120 PHE D CE1 1 
ATOM   2528 C CE2 . PHE B 2 153 ? 68.39180  16.53468  18.52045  1.000 69.01961  ?  120 PHE D CE2 1 
ATOM   2529 C CZ  . PHE B 2 153 ? 67.86479  17.08641  19.67161  1.000 67.35856  ?  120 PHE D CZ  1 
ATOM   2530 N N   . TYR B 2 154 ? 64.24719  20.04437  15.96989  1.000 77.26532  ?  121 TYR D N   1 
ATOM   2531 C CA  . TYR B 2 154 ? 63.67474  21.18581  16.66713  1.000 64.01278  ?  121 TYR D CA  1 
ATOM   2532 C C   . TYR B 2 154 ? 62.23106  20.85560  16.99799  1.000 66.00930  ?  121 TYR D C   1 
ATOM   2533 O O   . TYR B 2 154 ? 61.51712  20.34399  16.12447  1.000 82.79361  ?  121 TYR D O   1 
ATOM   2534 C CB  . TYR B 2 154 ? 63.75149  22.45764  15.81444  1.000 66.30901  ?  121 TYR D CB  1 
ATOM   2535 C CG  . TYR B 2 154 ? 63.42829  23.72660  16.57025  1.000 72.32122  ?  121 TYR D CG  1 
ATOM   2536 C CD1 . TYR B 2 154 ? 62.12645  24.20408  16.64170  1.000 63.19706  ?  121 TYR D CD1 1 
ATOM   2537 C CD2 . TYR B 2 154 ? 64.42655  24.44789  17.21170  1.000 64.27603  ?  121 TYR D CD2 1 
ATOM   2538 C CE1 . TYR B 2 154 ? 61.82782  25.36244  17.33252  1.000 59.66388  ?  121 TYR D CE1 1 
ATOM   2539 C CE2 . TYR B 2 154 ? 64.13754  25.60773  17.90439  1.000 63.41777  ?  121 TYR D CE2 1 
ATOM   2540 C CZ  . TYR B 2 154 ? 62.83678  26.06004  17.96162  1.000 67.18098  ?  121 TYR D CZ  1 
ATOM   2541 O OH  . TYR B 2 154 ? 62.54373  27.21455  18.65031  1.000 88.66322  ?  121 TYR D OH  1 
ATOM   2542 N N   . PRO B 2 155 ? 61.75682  21.13969  18.21987  1.000 67.69045  ?  122 PRO D N   1 
ATOM   2543 C CA  . PRO B 2 155 ? 62.44477  21.82112  19.32690  1.000 67.29948  ?  122 PRO D CA  1 
ATOM   2544 C C   . PRO B 2 155 ? 63.40840  20.91928  20.08882  1.000 73.96280  ?  122 PRO D C   1 
ATOM   2545 O O   . PRO B 2 155 ? 63.65943  19.78288  19.69995  1.000 66.08076  ?  122 PRO D O   1 
ATOM   2546 C CB  . PRO B 2 155 ? 61.27869  22.27780  20.21076  1.000 59.82113  ?  122 PRO D CB  1 
ATOM   2547 C CG  . PRO B 2 155 ? 60.25724  21.19662  20.02955  1.000 72.83267  ?  122 PRO D CG  1 
ATOM   2548 C CD  . PRO B 2 155 ? 60.36769  20.79524  18.57660  1.000 65.02526  ?  122 PRO D CD  1 
ATOM   2549 N N   . ALA B 2 156 ? 63.96091  21.41063  21.19925  1.000 76.38447  ?  123 ALA D N   1 
ATOM   2550 C CA  . ALA B 2 156 ? 64.96038  20.64585  21.93406  1.000 69.67970  ?  123 ALA D CA  1 
ATOM   2551 C C   . ALA B 2 156 ? 64.35105  19.50930  22.74413  1.000 89.71005  ?  123 ALA D C   1 
ATOM   2552 O O   . ALA B 2 156 ? 65.08903  18.62892  23.19738  1.000 94.50137  ?  123 ALA D O   1 
ATOM   2553 C CB  . ALA B 2 156 ? 65.75882  21.57790  22.84931  1.000 55.97500  ?  123 ALA D CB  1 
ATOM   2554 N N   . LYS B 2 157 ? 63.03227  19.50337  22.93056  1.000 77.16588  ?  124 LYS D N   1 
ATOM   2555 C CA  . LYS B 2 157 ? 62.36589  18.44417  23.68375  1.000 80.39962  ?  124 LYS D CA  1 
ATOM   2556 C C   . LYS B 2 157 ? 62.44558  17.13825  22.90126  1.000 84.51297  ?  124 LYS D C   1 
ATOM   2557 O O   . LYS B 2 157 ? 61.84326  17.00877  21.83048  1.000 90.91168  ?  124 LYS D O   1 
ATOM   2558 C CB  . LYS B 2 157 ? 60.91570  18.82784  23.96504  1.000 80.36972  ?  124 LYS D CB  1 
ATOM   2559 N N   . ILE B 2 158 ? 63.18751  16.16710  23.43371  1.000 71.89011  ?  125 ILE D N   1 
ATOM   2560 C CA  . ILE B 2 158 ? 63.40399  14.89525  22.75560  1.000 87.56771  ?  125 ILE D CA  1 
ATOM   2561 C C   . ILE B 2 158 ? 63.74678  13.84514  23.80239  1.000 91.74340  ?  125 ILE D C   1 
ATOM   2562 O O   . ILE B 2 158 ? 64.31327  14.15285  24.85459  1.000 103.49574 ?  125 ILE D O   1 
ATOM   2563 C CB  . ILE B 2 158 ? 64.51302  15.00507  21.68103  1.000 73.40244  ?  125 ILE D CB  1 
ATOM   2564 C CG1 . ILE B 2 158 ? 64.51313  13.77108  20.77701  1.000 83.04038  ?  125 ILE D CG1 1 
ATOM   2565 C CG2 . ILE B 2 158 ? 65.87607  15.19173  22.33286  1.000 72.76157  ?  125 ILE D CG2 1 
ATOM   2566 C CD1 . ILE B 2 158 ? 65.50741  13.85095  19.64574  1.000 76.48696  ?  125 ILE D CD1 1 
ATOM   2567 N N   . LYS B 2 159 ? 63.38657  12.59598  23.51096  1.000 98.15221  ?  126 LYS D N   1 
ATOM   2568 C CA  . LYS B 2 159 ? 63.63882  11.46939  24.40229  1.000 113.85547 ?  126 LYS D CA  1 
ATOM   2569 C C   . LYS B 2 159 ? 64.35524  10.37813  23.62212  1.000 96.70599  ?  126 LYS D C   1 
ATOM   2570 O O   . LYS B 2 159 ? 63.83354  9.88771   22.61546  1.000 94.82704  ?  126 LYS D O   1 
ATOM   2571 C CB  . LYS B 2 159 ? 62.33432  10.93385  25.00042  1.000 93.45202  ?  126 LYS D CB  1 
ATOM   2572 N N   . VAL B 2 160 ? 65.54411  9.99988   24.08416  1.000 91.93283  ?  127 VAL D N   1 
ATOM   2573 C CA  . VAL B 2 160 ? 66.34331  8.95754   23.45369  1.000 106.61697 ?  127 VAL D CA  1 
ATOM   2574 C C   . VAL B 2 160 ? 66.45847  7.78819   24.42026  1.000 109.31155 ?  127 VAL D C   1 
ATOM   2575 O O   . VAL B 2 160 ? 66.62461  7.98485   25.62927  1.000 113.70882 ?  127 VAL D O   1 
ATOM   2576 C CB  . VAL B 2 160 ? 67.73857  9.47393   23.04600  1.000 103.15227 ?  127 VAL D CB  1 
ATOM   2577 C CG1 . VAL B 2 160 ? 68.41442  8.48585   22.10857  1.000 94.10883  ?  127 VAL D CG1 1 
ATOM   2578 C CG2 . VAL B 2 160 ? 67.62880  10.84582  22.39838  1.000 86.15867  ?  127 VAL D CG2 1 
ATOM   2579 N N   . ARG B 2 161 ? 66.36760  6.57136   23.88617  1.000 108.55035 ?  128 ARG D N   1 
ATOM   2580 C CA  . ARG B 2 161 ? 66.38104  5.37101   24.70736  1.000 105.94689 ?  128 ARG D CA  1 
ATOM   2581 C C   . ARG B 2 161 ? 67.19207  4.27869   24.02521  1.000 109.93061 ?  128 ARG D C   1 
ATOM   2582 O O   . ARG B 2 161 ? 67.27549  4.21292   22.79517  1.000 111.09820 ?  128 ARG D O   1 
ATOM   2583 C CB  . ARG B 2 161 ? 64.96105  4.86404   24.98992  1.000 107.96293 ?  128 ARG D CB  1 
ATOM   2584 N N   . TRP B 2 162 ? 67.78970  3.42275   24.84874  1.000 127.42875 ?  129 TRP D N   1 
ATOM   2585 C CA  . TRP B 2 162 ? 68.55044  2.26639   24.40171  1.000 125.80898 ?  129 TRP D CA  1 
ATOM   2586 C C   . TRP B 2 162 ? 67.80717  0.99627   24.78053  1.000 132.86869 ?  129 TRP D C   1 
ATOM   2587 O O   . TRP B 2 162 ? 67.31429  0.87331   25.90442  1.000 140.16378 ?  129 TRP D O   1 
ATOM   2588 C CB  . TRP B 2 162 ? 69.94788  2.25001   25.02693  1.000 121.32694 ?  129 TRP D CB  1 
ATOM   2589 C CG  . TRP B 2 162 ? 70.99174  2.87984   24.17497  1.000 128.84187 ?  129 TRP D CG  1 
ATOM   2590 C CD1 . TRP B 2 162 ? 71.67638  4.03147   24.42904  1.000 127.74359 ?  129 TRP D CD1 1 
ATOM   2591 C CD2 . TRP B 2 162 ? 71.47186  2.39370   22.91909  1.000 134.40995 ?  129 TRP D CD2 1 
ATOM   2592 N NE1 . TRP B 2 162 ? 72.55848  4.29099   23.40804  1.000 119.51188 ?  129 TRP D NE1 1 
ATOM   2593 C CE2 . TRP B 2 162 ? 72.45095  3.30013   22.46747  1.000 125.41665 ?  129 TRP D CE2 1 
ATOM   2594 C CE3 . TRP B 2 162 ? 71.16916  1.27799   22.13232  1.000 135.49556 ?  129 TRP D CE3 1 
ATOM   2595 C CZ2 . TRP B 2 162 ? 73.12815  3.12578   21.26445  1.000 115.89648 ?  129 TRP D CZ2 1 
ATOM   2596 C CZ3 . TRP B 2 162 ? 71.84159  1.10720   20.94002  1.000 136.82834 ?  129 TRP D CZ3 1 
ATOM   2597 C CH2 . TRP B 2 162 ? 72.81145  2.02331   20.51956  1.000 133.17808 ?  129 TRP D CH2 1 
ATOM   2598 N N   . PHE B 2 163 ? 67.73603  0.04614   23.84488  1.000 135.79917 ?  130 PHE D N   1 
ATOM   2599 C CA  . PHE B 2 163 ? 66.99529  -1.18929  24.09797  1.000 151.47511 ?  130 PHE D CA  1 
ATOM   2600 C C   . PHE B 2 163 ? 67.45836  -2.25671  23.10536  1.000 145.63519 ?  130 PHE D C   1 
ATOM   2601 O O   . PHE B 2 163 ? 67.10721  -2.19732  21.92535  1.000 148.41646 ?  130 PHE D O   1 
ATOM   2602 C CB  . PHE B 2 163 ? 65.49729  -0.95440  23.99629  1.000 132.68398 ?  130 PHE D CB  1 
ATOM   2603 N N   . ARG B 2 164 ? 68.23556  -3.22208  23.59778  1.000 153.99445 ?  131 ARG D N   1 
ATOM   2604 C CA  . ARG B 2 164 ? 68.51778  -4.41949  22.81194  1.000 153.84687 ?  131 ARG D CA  1 
ATOM   2605 C C   . ARG B 2 164 ? 67.27937  -5.30237  22.72606  1.000 159.75782 ?  131 ARG D C   1 
ATOM   2606 O O   . ARG B 2 164 ? 66.80981  -5.63881  21.63284  1.000 158.61614 ?  131 ARG D O   1 
ATOM   2607 C CB  . ARG B 2 164 ? 69.68943  -5.18740  23.42668  1.000 146.16806 ?  131 ARG D CB  1 
ATOM   2608 N N   . ASN B 2 165 ? 66.74544  -5.69703  23.88020  1.000 141.11324 ?  132 ASN D N   1 
ATOM   2609 C CA  . ASN B 2 165 ? 65.43478  -6.32584  23.96775  1.000 133.70207 ?  132 ASN D CA  1 
ATOM   2610 C C   . ASN B 2 165 ? 64.59879  -5.55010  24.97653  1.000 138.20341 ?  132 ASN D C   1 
ATOM   2611 O O   . ASN B 2 165 ? 63.43023  -5.23740  24.72573  1.000 120.74266 ?  132 ASN D O   1 
ATOM   2612 C CB  . ASN B 2 165 ? 65.55754  -7.79674  24.36922  1.000 123.22164 ?  132 ASN D CB  1 
ATOM   2613 N N   . GLY B 2 166 ? 65.20047  -5.23624  26.11654  1.000 140.22932 ?  133 GLY D N   1 
ATOM   2614 C CA  . GLY B 2 166 ? 64.58819  -4.34916  27.08348  1.000 133.30234 ?  133 GLY D CA  1 
ATOM   2615 C C   . GLY B 2 166 ? 65.53911  -3.22659  27.43786  1.000 139.49121 ?  133 GLY D C   1 
ATOM   2616 O O   . GLY B 2 166 ? 66.75852  -3.39556  27.44640  1.000 135.57985 ?  133 GLY D O   1 
ATOM   2617 N N   . GLN B 2 167 ? 64.95911  -2.06368  27.72757  1.000 143.55743 ?  134 GLN D N   1 
ATOM   2618 C CA  . GLN B 2 167 ? 65.76152  -0.87990  28.00541  1.000 143.49382 ?  134 GLN D CA  1 
ATOM   2619 C C   . GLN B 2 167 ? 66.59186  -1.07046  29.26909  1.000 131.05432 ?  134 GLN D C   1 
ATOM   2620 O O   . GLN B 2 167 ? 66.12007  -1.62100  30.26752  1.000 127.63229 ?  134 GLN D O   1 
ATOM   2621 C CB  . GLN B 2 167 ? 64.86211  0.34906   28.14466  1.000 126.48397 ?  134 GLN D CB  1 
ATOM   2622 N N   . GLU B 2 168 ? 67.83998  -0.61023  29.21840  1.000 126.56206 ?  135 GLU D N   1 
ATOM   2623 C CA  . GLU B 2 168 ? 68.77509  -0.72598  30.32908  1.000 139.23121 ?  135 GLU D CA  1 
ATOM   2624 C C   . GLU B 2 168 ? 69.25724  0.66041   30.72873  1.000 129.84286 ?  135 GLU D C   1 
ATOM   2625 O O   . GLU B 2 168 ? 69.76242  1.41246   29.88844  1.000 109.96718 ?  135 GLU D O   1 
ATOM   2626 C CB  . GLU B 2 168 ? 69.96576  -1.61499  29.95764  1.000 128.12832 ?  135 GLU D CB  1 
ATOM   2627 N N   . GLU B 2 169 ? 69.10087  0.99362   32.01163  1.000 134.55108 ?  136 GLU D N   1 
ATOM   2628 C CA  . GLU B 2 169 ? 69.54398  2.29636   32.49758  1.000 120.04558 ?  136 GLU D CA  1 
ATOM   2629 C C   . GLU B 2 169 ? 71.06482  2.37221   32.55243  1.000 127.16572 ?  136 GLU D C   1 
ATOM   2630 O O   . GLU B 2 169 ? 71.66964  3.28789   31.98263  1.000 131.79018 ?  136 GLU D O   1 
ATOM   2631 C CB  . GLU B 2 169 ? 68.93806  2.57715   33.87299  1.000 104.70254 ?  136 GLU D CB  1 
ATOM   2632 N N   . THR B 2 170 ? 71.69491  1.41759   33.23544  1.000 137.65059 ?  137 THR D N   1 
ATOM   2633 C CA  . THR B 2 170 ? 73.15213  1.34009   33.35265  1.000 136.72190 ?  137 THR D CA  1 
ATOM   2634 C C   . THR B 2 170 ? 73.76458  2.64614   33.85524  1.000 128.23196 ?  137 THR D C   1 
ATOM   2635 O O   . THR B 2 170 ? 74.52400  2.65538   34.82409  1.000 122.10850 ?  137 THR D O   1 
ATOM   2636 C CB  . THR B 2 170 ? 73.80651  0.96418   32.00665  1.000 123.17647 ?  137 THR D CB  1 
ATOM   2637 O OG1 . THR B 2 170 ? 73.35575  -0.33256  31.59571  1.000 120.92753 ?  137 THR D OG1 1 
ATOM   2638 C CG2 . THR B 2 170 ? 75.32318  0.95754   32.12926  1.000 102.79117 ?  137 THR D CG2 1 
ATOM   2639 N N   . VAL B 2 173 ? 75.88444  4.33235   31.55858  1.000 131.68438 ?  140 VAL D N   1 
ATOM   2640 C CA  . VAL B 2 173 ? 75.29361  5.09738   30.46790  1.000 144.29753 ?  140 VAL D CA  1 
ATOM   2641 C C   . VAL B 2 173 ? 75.18592  6.57076   30.83424  1.000 140.55445 ?  140 VAL D C   1 
ATOM   2642 O O   . VAL B 2 173 ? 74.56880  6.93231   31.83653  1.000 140.81412 ?  140 VAL D O   1 
ATOM   2643 C CB  . VAL B 2 173 ? 73.91410  4.53744   30.07803  1.000 140.15932 ?  140 VAL D CB  1 
ATOM   2644 C CG1 . VAL B 2 173 ? 73.13353  5.55525   29.25780  1.000 115.24359 ?  140 VAL D CG1 1 
ATOM   2645 C CG2 . VAL B 2 173 ? 74.07404  3.25013   29.30010  1.000 133.13928 ?  140 VAL D CG2 1 
ATOM   2646 N N   . SER B 2 174 ? 75.79742  7.41727   30.01098  1.000 130.72235 ?  141 SER D N   1 
ATOM   2647 C CA  . SER B 2 174 ? 75.71113  8.86017   30.15878  1.000 133.08702 ?  141 SER D CA  1 
ATOM   2648 C C   . SER B 2 174 ? 75.44846  9.48456   28.79722  1.000 138.55085 ?  141 SER D C   1 
ATOM   2649 O O   . SER B 2 174 ? 75.79745  8.91781   27.75814  1.000 137.76117 ?  141 SER D O   1 
ATOM   2650 C CB  . SER B 2 174 ? 76.99262  9.44689   30.76811  1.000 124.84578 ?  141 SER D CB  1 
ATOM   2651 O OG  . SER B 2 174 ? 78.10094  9.25722   29.90636  1.000 123.94366 ?  141 SER D OG  1 
ATOM   2652 N N   . SER B 2 175 ? 74.82203  10.65674  28.81167  1.000 127.13871 ?  142 SER D N   1 
ATOM   2653 C CA  . SER B 2 175 ? 74.51495  11.38882  27.59413  1.000 122.16410 ?  142 SER D CA  1 
ATOM   2654 C C   . SER B 2 175 ? 75.09051  12.79292  27.68762  1.000 119.96168 ?  142 SER D C   1 
ATOM   2655 O O   . SER B 2 175 ? 75.20689  13.36291  28.77581  1.000 120.74042 ?  142 SER D O   1 
ATOM   2656 C CB  . SER B 2 175 ? 73.00241  11.46141  27.34295  1.000 121.11544 ?  142 SER D CB  1 
ATOM   2657 O OG  . SER B 2 175 ? 72.35074  12.19369  28.36610  1.000 123.68761 ?  142 SER D OG  1 
ATOM   2658 N N   . THR B 2 176 ? 75.45539  13.34293  26.53367  1.000 113.70040 ?  143 THR D N   1 
ATOM   2659 C CA  . THR B 2 176 ? 75.95571  14.70596  26.48966  1.000 120.56893 ?  143 THR D CA  1 
ATOM   2660 C C   . THR B 2 176 ? 74.81754  15.69526  26.72069  1.000 110.71890 ?  143 THR D C   1 
ATOM   2661 O O   . THR B 2 176 ? 73.63414  15.36578  26.59984  1.000 99.73014  ?  143 THR D O   1 
ATOM   2662 C CB  . THR B 2 176 ? 76.62749  14.99548  25.14660  1.000 98.44104  ?  143 THR D CB  1 
ATOM   2663 O OG1 . THR B 2 176 ? 75.63436  15.04578  24.11463  1.000 90.22580  ?  143 THR D OG1 1 
ATOM   2664 C CG2 . THR B 2 176 ? 77.63890  13.91018  24.81289  1.000 108.63832 ?  143 THR D CG2 1 
ATOM   2665 N N   . GLN B 2 177 ? 75.19081  16.92372  27.06415  1.000 101.11183 ?  144 GLN D N   1 
ATOM   2666 C CA  . GLN B 2 177 ? 74.20285  17.97861  27.20646  1.000 101.70123 ?  144 GLN D CA  1 
ATOM   2667 C C   . GLN B 2 177 ? 73.62960  18.34977  25.84146  1.000 104.19736 ?  144 GLN D C   1 
ATOM   2668 O O   . GLN B 2 177 ? 74.20151  18.04208  24.79150  1.000 105.05117 ?  144 GLN D O   1 
ATOM   2669 C CB  . GLN B 2 177 ? 74.81981  19.20747  27.87458  1.000 111.64992 ?  144 GLN D CB  1 
ATOM   2670 N N   . LEU B 2 178 ? 72.47614  19.01270  25.86659  1.000 86.02939  ?  145 LEU D N   1 
ATOM   2671 C CA  . LEU B 2 178 ? 71.83606  19.44675  24.63174  1.000 83.18192  ?  145 LEU D CA  1 
ATOM   2672 C C   . LEU B 2 178 ? 72.72200  20.44770  23.90268  1.000 81.24019  ?  145 LEU D C   1 
ATOM   2673 O O   . LEU B 2 178 ? 73.01061  21.53040  24.42184  1.000 94.58947  ?  145 LEU D O   1 
ATOM   2674 C CB  . LEU B 2 178 ? 70.46979  20.05909  24.93490  1.000 80.10258  ?  145 LEU D CB  1 
ATOM   2675 C CG  . LEU B 2 178 ? 69.36824  19.07198  25.32417  1.000 104.64049 ?  145 LEU D CG  1 
ATOM   2676 C CD1 . LEU B 2 178 ? 68.12335  19.80838  25.79418  1.000 95.22211  ?  145 LEU D CD1 1 
ATOM   2677 C CD2 . LEU B 2 178 ? 69.04183  18.15674  24.15364  1.000 93.50528  ?  145 LEU D CD2 1 
ATOM   2678 N N   . ILE B 2 179 ? 73.15918  20.07987  22.70309  1.000 63.29783  ?  146 ILE D N   1 
ATOM   2679 C CA  . ILE B 2 179 ? 74.02312  20.93051  21.89432  1.000 66.73456  ?  146 ILE D CA  1 
ATOM   2680 C C   . ILE B 2 179 ? 73.15242  21.84707  21.04773  1.000 70.77372  ?  146 ILE D C   1 
ATOM   2681 O O   . ILE B 2 179 ? 72.27532  21.38209  20.30975  1.000 71.09980  ?  146 ILE D O   1 
ATOM   2682 C CB  . ILE B 2 179 ? 74.95742  20.08801  21.01120  1.000 73.15859  ?  146 ILE D CB  1 
ATOM   2683 C CG1 . ILE B 2 179 ? 75.65528  19.00914  21.84275  1.000 79.13073  ?  146 ILE D CG1 1 
ATOM   2684 C CG2 . ILE B 2 179 ? 75.97914  20.97688  20.32008  1.000 61.78131  ?  146 ILE D CG2 1 
ATOM   2685 C CD1 . ILE B 2 179 ? 76.53989  19.55685  22.93852  1.000 83.03378  ?  146 ILE D CD1 1 
ATOM   2686 N N   . ARG B 2 180 ? 73.39273  23.15024  21.15427  1.000 56.88290  ?  147 ARG D N   1 
ATOM   2687 C CA  . ARG B 2 180 ? 72.64070  24.15746  20.41545  1.000 60.21035  ?  147 ARG D CA  1 
ATOM   2688 C C   . ARG B 2 180 ? 73.48258  24.61197  19.22786  1.000 60.83361  ?  147 ARG D C   1 
ATOM   2689 O O   . ARG B 2 180 ? 74.49149  25.30332  19.40149  1.000 64.06464  ?  147 ARG D O   1 
ATOM   2690 C CB  . ARG B 2 180 ? 72.27683  25.32907  21.32493  1.000 55.96067  ?  147 ARG D CB  1 
ATOM   2691 C CG  . ARG B 2 180 ? 71.68738  26.52602  20.60458  1.000 59.15111  ?  147 ARG D CG  1 
ATOM   2692 C CD  . ARG B 2 180 ? 71.34082  27.63236  21.58531  1.000 55.69277  ?  147 ARG D CD  1 
ATOM   2693 N NE  . ARG B 2 180 ? 71.24470  28.92955  20.92714  1.000 79.33225  ?  147 ARG D NE  1 
ATOM   2694 C CZ  . ARG B 2 180 ? 72.24763  29.79109  20.82450  1.000 67.88577  ?  147 ARG D CZ  1 
ATOM   2695 N NH1 . ARG B 2 180 ? 73.43876  29.52994  21.33814  1.000 67.30407  ?  147 ARG D NH1 1 
ATOM   2696 N NH2 . ARG B 2 180 ? 72.05055  30.94396  20.19178  1.000 69.60640  ?  147 ARG D NH2 1 
ATOM   2697 N N   . ASN B 2 181 ? 73.06720  24.21884  18.02075  1.000 53.39477  ?  148 ASN D N   1 
ATOM   2698 C CA  . ASN B 2 181 ? 73.82536  24.55703  16.82162  1.000 50.95315  ?  148 ASN D CA  1 
ATOM   2699 C C   . ASN B 2 181 ? 73.75389  26.03971  16.48302  1.000 64.80414  ?  148 ASN D C   1 
ATOM   2700 O O   . ASN B 2 181 ? 74.63158  26.54124  15.77267  1.000 68.58773  ?  148 ASN D O   1 
ATOM   2701 C CB  . ASN B 2 181 ? 73.32906  23.73334  15.63169  1.000 52.70814  ?  148 ASN D CB  1 
ATOM   2702 C CG  . ASN B 2 181 ? 73.59526  22.25055  15.79537  1.000 57.24484  ?  148 ASN D CG  1 
ATOM   2703 O OD1 . ASN B 2 181 ? 74.54335  21.84835  16.46927  1.000 58.74995  ?  148 ASN D OD1 1 
ATOM   2704 N ND2 . ASN B 2 181 ? 72.75837  21.42774  15.17422  1.000 73.91125  ?  148 ASN D ND2 1 
ATOM   2705 N N   . GLY B 2 182 ? 72.73464  26.74871  16.96695  1.000 70.47411  ?  149 GLY D N   1 
ATOM   2706 C CA  . GLY B 2 182 ? 72.58447  28.16087  16.69701  1.000 59.81082  ?  149 GLY D CA  1 
ATOM   2707 C C   . GLY B 2 182 ? 71.76743  28.49898  15.46925  1.000 57.38263  ?  149 GLY D C   1 
ATOM   2708 O O   . GLY B 2 182 ? 71.44444  29.67665  15.26664  1.000 66.16846  ?  149 GLY D O   1 
ATOM   2709 N N   . ASP B 2 183 ? 71.42526  27.51304  14.64341  1.000 61.32521  ?  150 ASP D N   1 
ATOM   2710 C CA  . ASP B 2 183 ? 70.61079  27.71858  13.45062  1.000 56.19763  ?  150 ASP D CA  1 
ATOM   2711 C C   . ASP B 2 183 ? 69.23791  27.06936  13.60072  1.000 53.82614  ?  150 ASP D C   1 
ATOM   2712 O O   . ASP B 2 183 ? 68.70027  26.48972  12.65482  1.000 61.06468  ?  150 ASP D O   1 
ATOM   2713 C CB  . ASP B 2 183 ? 71.32328  27.18770  12.20885  1.000 65.60827  ?  150 ASP D CB  1 
ATOM   2714 C CG  . ASP B 2 183 ? 71.65566  25.70957  12.30923  1.000 64.34764  ?  150 ASP D CG  1 
ATOM   2715 O OD1 . ASP B 2 183 ? 71.45031  25.11871  13.39004  1.000 57.97325  ?  150 ASP D OD1 1 
ATOM   2716 O OD2 . ASP B 2 183 ? 72.12149  25.13673  11.30168  1.000 78.18973  -1 150 ASP D OD2 1 
ATOM   2717 N N   . TRP B 2 184 ? 68.66674  27.15930  14.80409  1.000 57.56873  ?  151 TRP D N   1 
ATOM   2718 C CA  . TRP B 2 184 ? 67.35824  26.58371  15.12030  1.000 58.16673  ?  151 TRP D CA  1 
ATOM   2719 C C   . TRP B 2 184 ? 67.35158  25.06538  14.96290  1.000 61.02909  ?  151 TRP D C   1 
ATOM   2720 O O   . TRP B 2 184 ? 66.33820  24.47315  14.58400  1.000 65.70067  ?  151 TRP D O   1 
ATOM   2721 C CB  . TRP B 2 184 ? 66.24890  27.22030  14.27684  1.000 51.35431  ?  151 TRP D CB  1 
ATOM   2722 C CG  . TRP B 2 184 ? 66.05861  28.67854  14.55866  1.000 58.53844  ?  151 TRP D CG  1 
ATOM   2723 C CD1 . TRP B 2 184 ? 66.85087  29.70560  14.13505  1.000 65.43009  ?  151 TRP D CD1 1 
ATOM   2724 C CD2 . TRP B 2 184 ? 65.00672  29.27413  15.32705  1.000 58.52836  ?  151 TRP D CD2 1 
ATOM   2725 N NE1 . TRP B 2 184 ? 66.35912  30.90316  14.59379  1.000 65.45710  ?  151 TRP D NE1 1 
ATOM   2726 C CE2 . TRP B 2 184 ? 65.22652  30.66588  15.32729  1.000 64.78419  ?  151 TRP D CE2 1 
ATOM   2727 C CE3 . TRP B 2 184 ? 63.90045  28.76587  16.01465  1.000 66.78891  ?  151 TRP D CE3 1 
ATOM   2728 C CZ2 . TRP B 2 184 ? 64.38154  31.55508  15.98871  1.000 64.30145  ?  151 TRP D CZ2 1 
ATOM   2729 C CZ3 . TRP B 2 184 ? 63.06264  29.65041  16.67014  1.000 57.15974  ?  151 TRP D CZ3 1 
ATOM   2730 C CH2 . TRP B 2 184 ? 63.30796  31.02876  16.65268  1.000 50.80886  ?  151 TRP D CH2 1 
ATOM   2731 N N   . THR B 2 185 ? 68.48507  24.42703  15.24962  1.000 55.57493  ?  152 THR D N   1 
ATOM   2732 C CA  . THR B 2 185 ? 68.58394  22.97499  15.27754  1.000 65.48369  ?  152 THR D CA  1 
ATOM   2733 C C   . THR B 2 185 ? 69.38792  22.56109  16.50119  1.000 66.16988  ?  152 THR D C   1 
ATOM   2734 O O   . THR B 2 185 ? 70.13164  23.35711  17.07967  1.000 66.18693  ?  152 THR D O   1 
ATOM   2735 C CB  . THR B 2 185 ? 69.23963  22.40677  14.00820  1.000 64.56059  ?  152 THR D CB  1 
ATOM   2736 O OG1 . THR B 2 185 ? 70.51458  23.02801  13.80378  1.000 70.63185  ?  152 THR D OG1 1 
ATOM   2737 C CG2 . THR B 2 185 ? 68.35781  22.63854  12.78874  1.000 63.34421  ?  152 THR D CG2 1 
ATOM   2738 N N   . PHE B 2 186 ? 69.23029  21.29792  16.89012  1.000 64.64962  ?  153 PHE D N   1 
ATOM   2739 C CA  . PHE B 2 186 ? 69.92975  20.75061  18.04220  1.000 56.35983  ?  153 PHE D CA  1 
ATOM   2740 C C   . PHE B 2 186 ? 70.47993  19.37538  17.69480  1.000 67.39302  ?  153 PHE D C   1 
ATOM   2741 O O   . PHE B 2 186 ? 70.07925  18.75176  16.70912  1.000 76.89189  ?  153 PHE D O   1 
ATOM   2742 C CB  . PHE B 2 186 ? 69.01362  20.64924  19.27111  1.000 57.74918  ?  153 PHE D CB  1 
ATOM   2743 C CG  . PHE B 2 186 ? 68.46450  21.96877  19.73302  1.000 74.29625  ?  153 PHE D CG  1 
ATOM   2744 C CD1 . PHE B 2 186 ? 67.28625  22.46822  19.20308  1.000 75.26485  ?  153 PHE D CD1 1 
ATOM   2745 C CD2 . PHE B 2 186 ? 69.12171  22.70568  20.70382  1.000 68.25334  ?  153 PHE D CD2 1 
ATOM   2746 C CE1 . PHE B 2 186 ? 66.77795  23.68065  19.62767  1.000 60.58917  ?  153 PHE D CE1 1 
ATOM   2747 C CE2 . PHE B 2 186 ? 68.61739  23.91819  21.13280  1.000 59.28312  ?  153 PHE D CE2 1 
ATOM   2748 C CZ  . PHE B 2 186 ? 67.44406  24.40608  20.59349  1.000 66.83652  ?  153 PHE D CZ  1 
ATOM   2749 N N   . GLN B 2 187 ? 71.41129  18.90982  18.52382  1.000 67.17159  ?  154 GLN D N   1 
ATOM   2750 C CA  . GLN B 2 187 ? 71.95656  17.56703  18.39921  1.000 68.60765  ?  154 GLN D CA  1 
ATOM   2751 C C   . GLN B 2 187 ? 72.33424  17.06707  19.78482  1.000 65.02639  ?  154 GLN D C   1 
ATOM   2752 O O   . GLN B 2 187 ? 72.63887  17.85672  20.68230  1.000 71.52955  ?  154 GLN D O   1 
ATOM   2753 C CB  . GLN B 2 187 ? 73.16911  17.52357  17.45986  1.000 62.12995  ?  154 GLN D CB  1 
ATOM   2754 C CG  . GLN B 2 187 ? 74.32818  18.40380  17.88750  1.000 70.41580  ?  154 GLN D CG  1 
ATOM   2755 C CD  . GLN B 2 187 ? 75.47457  18.38106  16.89500  1.000 73.52543  ?  154 GLN D CD  1 
ATOM   2756 O OE1 . GLN B 2 187 ? 75.73723  17.36324  16.25475  1.000 94.15454  ?  154 GLN D OE1 1 
ATOM   2757 N NE2 . GLN B 2 187 ? 76.15995  19.51036  16.75702  1.000 77.02785  ?  154 GLN D NE2 1 
ATOM   2758 N N   . VAL B 2 188 ? 72.30305  15.74609  19.95438  1.000 72.40727  ?  155 VAL D N   1 
ATOM   2759 C CA  . VAL B 2 188 ? 72.58710  15.13018  21.24429  1.000 79.78351  ?  155 VAL D CA  1 
ATOM   2760 C C   . VAL B 2 188 ? 73.27396  13.79341  21.00214  1.000 83.37817  ?  155 VAL D C   1 
ATOM   2761 O O   . VAL B 2 188 ? 73.08107  13.15292  19.96486  1.000 79.03263  ?  155 VAL D O   1 
ATOM   2762 C CB  . VAL B 2 188 ? 71.29833  14.96721  22.08805  1.000 76.81507  ?  155 VAL D CB  1 
ATOM   2763 C CG1 . VAL B 2 188 ? 70.40862  13.87196  21.51488  1.000 82.52513  ?  155 VAL D CG1 1 
ATOM   2764 C CG2 . VAL B 2 188 ? 71.63504  14.70016  23.54993  1.000 98.47014  ?  155 VAL D CG2 1 
ATOM   2765 N N   . LEU B 2 189 ? 74.09572  13.38234  21.96674  1.000 97.62462  ?  156 LEU D N   1 
ATOM   2766 C CA  . LEU B 2 189 ? 74.84710  12.13500  21.89286  1.000 100.03607 ?  156 LEU D CA  1 
ATOM   2767 C C   . LEU B 2 189 ? 74.64706  11.36958  23.19138  1.000 99.93182  ?  156 LEU D C   1 
ATOM   2768 O O   . LEU B 2 189 ? 75.01983  11.85695  24.26356  1.000 104.12675 ?  156 LEU D O   1 
ATOM   2769 C CB  . LEU B 2 189 ? 76.33721  12.40029  21.65568  1.000 95.31412  ?  156 LEU D CB  1 
ATOM   2770 C CG  . LEU B 2 189 ? 76.71764  13.35516  20.52230  1.000 95.23023  ?  156 LEU D CG  1 
ATOM   2771 C CD1 . LEU B 2 189 ? 78.21372  13.63050  20.53717  1.000 95.73899  ?  156 LEU D CD1 1 
ATOM   2772 C CD2 . LEU B 2 189 ? 76.28900  12.79565  19.17759  1.000 92.08896  ?  156 LEU D CD2 1 
ATOM   2773 N N   . VAL B 2 190 ? 74.06244  10.17844  23.09728  1.000 101.88270 ?  157 VAL D N   1 
ATOM   2774 C CA  . VAL B 2 190 ? 73.86325  9.29828   24.24310  1.000 110.04379 ?  157 VAL D CA  1 
ATOM   2775 C C   . VAL B 2 190 ? 74.83411  8.13176   24.11881  1.000 119.00402 ?  157 VAL D C   1 
ATOM   2776 O O   . VAL B 2 190 ? 74.96330  7.53341   23.04368  1.000 121.84116 ?  157 VAL D O   1 
ATOM   2777 C CB  . VAL B 2 190 ? 72.40491  8.81311   24.33838  1.000 114.54779 ?  157 VAL D CB  1 
ATOM   2778 C CG1 . VAL B 2 190 ? 71.93478  8.24642   23.00767  1.000 114.66804 ?  157 VAL D CG1 1 
ATOM   2779 C CG2 . VAL B 2 190 ? 72.25232  7.78422   25.45047  1.000 131.41156 ?  157 VAL D CG2 1 
ATOM   2780 N N   . MET B 2 191 ? 75.52689  7.82062   25.21054  1.000 121.10302 ?  158 MET D N   1 
ATOM   2781 C CA  . MET B 2 191 ? 76.55263  6.78675   25.22736  1.000 125.91161 ?  158 MET D CA  1 
ATOM   2782 C C   . MET B 2 191 ? 76.07046  5.59349   26.03993  1.000 121.79950 ?  158 MET D C   1 
ATOM   2783 O O   . MET B 2 191 ? 75.57226  5.75879   27.15819  1.000 128.25565 ?  158 MET D O   1 
ATOM   2784 C CB  . MET B 2 191 ? 77.86202  7.32669   25.80717  1.000 118.70514 ?  158 MET D CB  1 
ATOM   2785 N N   . LEU B 2 192 ? 76.22425  4.39687   25.47612  1.000 132.59361 ?  159 LEU D N   1 
ATOM   2786 C CA  . LEU B 2 192 ? 75.85664  3.14715   26.14020  1.000 138.21559 ?  159 LEU D CA  1 
ATOM   2787 C C   . LEU B 2 192 ? 77.12316  2.53957   26.73470  1.000 140.11563 ?  159 LEU D C   1 
ATOM   2788 O O   . LEU B 2 192 ? 77.95365  1.98245   26.01338  1.000 147.83352 ?  159 LEU D O   1 
ATOM   2789 C CB  . LEU B 2 192 ? 75.18126  2.19219   25.16067  1.000 125.50195 ?  159 LEU D CB  1 
ATOM   2790 C CG  . LEU B 2 192 ? 74.93719  0.75325   25.62533  1.000 142.14920 ?  159 LEU D CG  1 
ATOM   2791 C CD1 . LEU B 2 192 ? 73.96854  0.70515   26.79427  1.000 128.19243 ?  159 LEU D CD1 1 
ATOM   2792 C CD2 . LEU B 2 192 ? 74.42878  -0.10097  24.47554  1.000 142.87962 ?  159 LEU D CD2 1 
ATOM   2793 N N   . GLU B 2 193 ? 77.26547  2.64600   28.05918  1.000 140.74734 ?  160 GLU D N   1 
ATOM   2794 C CA  . GLU B 2 193 ? 78.46317  2.13744   28.72389  1.000 155.08796 ?  160 GLU D CA  1 
ATOM   2795 C C   . GLU B 2 193 ? 78.68121  0.65748   28.43023  1.000 164.46747 ?  160 GLU D C   1 
ATOM   2796 O O   . GLU B 2 193 ? 79.81935  0.22077   28.21971  1.000 177.70619 ?  160 GLU D O   1 
ATOM   2797 C CB  . GLU B 2 193 ? 78.36725  2.38346   30.23152  1.000 163.22598 ?  160 GLU D CB  1 
ATOM   2798 C CG  . GLU B 2 193 ? 79.04518  1.32859   31.10445  1.000 173.58909 ?  160 GLU D CG  1 
ATOM   2799 C CD  . GLU B 2 193 ? 80.56047  1.32532   30.98345  1.000 181.02903 ?  160 GLU D CD  1 
ATOM   2800 O OE1 . GLU B 2 193 ? 81.12708  2.30629   30.45688  1.000 180.71544 ?  160 GLU D OE1 1 
ATOM   2801 O OE2 . GLU B 2 193 ? 81.18539  0.33405   31.41727  1.000 160.53394 ?  160 GLU D OE2 1 
ATOM   2802 N N   . MET B 2 194 ? 77.60574  -0.12579  28.40072  1.000 164.69860 ?  161 MET D N   1 
ATOM   2803 C CA  . MET B 2 194 ? 77.72811  -1.54900  28.11959  1.000 162.70085 ?  161 MET D CA  1 
ATOM   2804 C C   . MET B 2 194 ? 78.24606  -1.77482  26.70295  1.000 162.95906 ?  161 MET D C   1 
ATOM   2805 O O   . MET B 2 194 ? 77.98593  -0.98940  25.78730  1.000 156.05660 ?  161 MET D O   1 
ATOM   2806 C CB  . MET B 2 194 ? 76.37984  -2.24585  28.30471  1.000 157.75705 ?  161 MET D CB  1 
ATOM   2807 N N   . THR B 2 195 ? 78.99139  -2.86240  26.53120  1.000 158.13968 ?  162 THR D N   1 
ATOM   2808 C CA  . THR B 2 195 ? 79.57818  -3.20005  25.23877  1.000 157.28505 ?  162 THR D CA  1 
ATOM   2809 C C   . THR B 2 195 ? 78.50220  -3.52319  24.20684  1.000 148.96158 ?  162 THR D C   1 
ATOM   2810 O O   . THR B 2 195 ? 78.19370  -2.70390  23.34084  1.000 131.33410 ?  162 THR D O   1 
ATOM   2811 C CB  . THR B 2 195 ? 80.54093  -4.39756  25.35269  1.000 142.69266 ?  162 THR D CB  1 
ATOM   2812 N N   . VAL B 2 201 ? 71.20541  -7.61638  18.56432  1.000 147.62413 ?  168 VAL D N   1 
ATOM   2813 C CA  . VAL B 2 201 ? 70.21721  -6.74603  17.94036  1.000 144.07905 ?  168 VAL D CA  1 
ATOM   2814 C C   . VAL B 2 201 ? 69.86145  -5.59327  18.87264  1.000 139.33407 ?  168 VAL D C   1 
ATOM   2815 O O   . VAL B 2 201 ? 68.93287  -5.69398  19.67398  1.000 141.32456 ?  168 VAL D O   1 
ATOM   2816 C CB  . VAL B 2 201 ? 68.95616  -7.53213  17.54267  1.000 148.02827 ?  168 VAL D CB  1 
ATOM   2817 N N   . TYR B 2 202 ? 70.60715  -4.49979  18.76248  1.000 134.07623 ?  169 TYR D N   1 
ATOM   2818 C CA  . TYR B 2 202 ? 70.39278  -3.31045  19.57214  1.000 142.67881 ?  169 TYR D CA  1 
ATOM   2819 C C   . TYR B 2 202 ? 69.60498  -2.27233  18.78056  1.000 125.10667 ?  169 TYR D C   1 
ATOM   2820 O O   . TYR B 2 202 ? 69.61048  -2.26213  17.54735  1.000 123.97796 ?  169 TYR D O   1 
ATOM   2821 C CB  . TYR B 2 202 ? 71.72925  -2.72120  20.03535  1.000 139.16308 ?  169 TYR D CB  1 
ATOM   2822 C CG  . TYR B 2 202 ? 72.62549  -3.70869  20.75267  1.000 136.79966 ?  169 TYR D CG  1 
ATOM   2823 C CD1 . TYR B 2 202 ? 73.46714  -4.55723  20.04315  1.000 134.51519 ?  169 TYR D CD1 1 
ATOM   2824 C CD2 . TYR B 2 202 ? 72.63515  -3.78745  22.13874  1.000 136.54681 ?  169 TYR D CD2 1 
ATOM   2825 C CE1 . TYR B 2 202 ? 74.28647  -5.46049  20.69383  1.000 145.92339 ?  169 TYR D CE1 1 
ATOM   2826 C CE2 . TYR B 2 202 ? 73.45166  -4.68739  22.79823  1.000 138.09199 ?  169 TYR D CE2 1 
ATOM   2827 C CZ  . TYR B 2 202 ? 74.27528  -5.52069  22.07118  1.000 143.15117 ?  169 TYR D CZ  1 
ATOM   2828 O OH  . TYR B 2 202 ? 75.09011  -6.41719  22.72437  1.000 156.52754 ?  169 TYR D OH  1 
ATOM   2829 N N   . THR B 2 203 ? 68.91217  -1.39770  19.50916  1.000 124.39226 ?  170 THR D N   1 
ATOM   2830 C CA  . THR B 2 203 ? 68.07895  -0.37025  18.89582  1.000 133.30053 ?  170 THR D CA  1 
ATOM   2831 C C   . THR B 2 203 ? 68.18902  0.92328   19.68735  1.000 128.99590 ?  170 THR D C   1 
ATOM   2832 O O   . THR B 2 203 ? 68.11321  0.90911   20.91957  1.000 115.96665 ?  170 THR D O   1 
ATOM   2833 C CB  . THR B 2 203 ? 66.60703  -0.80390  18.82290  1.000 131.99890 ?  170 THR D CB  1 
ATOM   2834 O OG1 . THR B 2 203 ? 66.18136  -1.28577  20.10358  1.000 146.59399 ?  170 THR D OG1 1 
ATOM   2835 C CG2 . THR B 2 203 ? 66.40640  -1.89282  17.77603  1.000 139.96737 ?  170 THR D CG2 1 
ATOM   2836 N N   . CYS B 2 204 ? 68.36656  2.03453   18.97704  1.000 120.49661 ?  171 CYS D N   1 
ATOM   2837 C CA  . CYS B 2 204 ? 68.31282  3.36589   19.56637  1.000 111.59143 ?  171 CYS D CA  1 
ATOM   2838 C C   . CYS B 2 204 ? 66.91111  3.92299   19.34793  1.000 114.31863 ?  171 CYS D C   1 
ATOM   2839 O O   . CYS B 2 204 ? 66.48101  4.10290   18.20321  1.000 114.08605 ?  171 CYS D O   1 
ATOM   2840 C CB  . CYS B 2 204 ? 69.37116  4.28471   18.95380  1.000 127.29429 ?  171 CYS D CB  1 
ATOM   2841 S SG  . CYS B 2 204 ? 69.42666  5.95844   19.65744  1.000 154.14208 ?  171 CYS D SG  1 
ATOM   2842 N N   . HIS B 2 205 ? 66.20042  4.18140   20.44130  1.000 117.25925 ?  172 HIS D N   1 
ATOM   2843 C CA  . HIS B 2 205 ? 64.80341  4.59529   20.39585  1.000 111.10701 ?  172 HIS D CA  1 
ATOM   2844 C C   . HIS B 2 205 ? 64.71652  6.10045   20.61796  1.000 114.87527 ?  172 HIS D C   1 
ATOM   2845 O O   . HIS B 2 205 ? 65.22627  6.61260   21.61937  1.000 118.76275 ?  172 HIS D O   1 
ATOM   2846 C CB  . HIS B 2 205 ? 63.99227  3.84053   21.44828  1.000 127.13843 ?  172 HIS D CB  1 
ATOM   2847 C CG  . HIS B 2 205 ? 62.51121  3.97726   21.28858  1.000 132.66115 ?  172 HIS D CG  1 
ATOM   2848 N ND1 . HIS B 2 205 ? 61.72974  4.68246   22.17797  1.000 139.63998 ?  172 HIS D ND1 1 
ATOM   2849 C CD2 . HIS B 2 205 ? 61.66746  3.49450   20.34612  1.000 133.57299 ?  172 HIS D CD2 1 
ATOM   2850 C CE1 . HIS B 2 205 ? 60.46838  4.62986   21.78931  1.000 151.68995 ?  172 HIS D CE1 1 
ATOM   2851 N NE2 . HIS B 2 205 ? 60.40338  3.91479   20.68063  1.000 140.28970 ?  172 HIS D NE2 1 
ATOM   2852 N N   . VAL B 2 206 ? 64.07152  6.80262   19.68764  1.000 116.23110 ?  173 VAL D N   1 
ATOM   2853 C CA  . VAL B 2 206 ? 63.98387  8.25848   19.70967  1.000 102.18257 ?  173 VAL D CA  1 
ATOM   2854 C C   . VAL B 2 206 ? 62.52831  8.66798   19.53499  1.000 99.04394  ?  173 VAL D C   1 
ATOM   2855 O O   . VAL B 2 206 ? 61.85673  8.20922   18.60430  1.000 103.20790 ?  173 VAL D O   1 
ATOM   2856 C CB  . VAL B 2 206 ? 64.85838  8.89911   18.61412  1.000 93.02593  ?  173 VAL D CB  1 
ATOM   2857 C CG1 . VAL B 2 206 ? 64.53245  10.37688  18.46597  1.000 88.15734  ?  173 VAL D CG1 1 
ATOM   2858 C CG2 . VAL B 2 206 ? 66.33197  8.70705   18.93325  1.000 96.14087  ?  173 VAL D CG2 1 
ATOM   2859 N N   . GLU B 2 207 ? 62.04634  9.53148   20.42652  1.000 103.41485 ?  174 GLU D N   1 
ATOM   2860 C CA  . GLU B 2 207 ? 60.70454  10.09353  20.35092  1.000 108.74710 ?  174 GLU D CA  1 
ATOM   2861 C C   . GLU B 2 207 ? 60.80750  11.61168  20.32453  1.000 110.27083 ?  174 GLU D C   1 
ATOM   2862 O O   . GLU B 2 207 ? 61.44151  12.20922  21.20077  1.000 111.13244 ?  174 GLU D O   1 
ATOM   2863 C CB  . GLU B 2 207 ? 59.84567  9.63606   21.53314  1.000 114.68143 ?  174 GLU D CB  1 
ATOM   2864 N N   . HIS B 2 208 ? 60.18565  12.22965  19.32530  1.000 108.05895 ?  175 HIS D N   1 
ATOM   2865 C CA  . HIS B 2 208 ? 60.26911  13.66629  19.11428  1.000 90.34285  ?  175 HIS D CA  1 
ATOM   2866 C C   . HIS B 2 208 ? 58.91391  14.18785  18.66057  1.000 87.00204  ?  175 HIS D C   1 
ATOM   2867 O O   . HIS B 2 208 ? 58.17365  13.47737  17.96981  1.000 85.36018  ?  175 HIS D O   1 
ATOM   2868 C CB  . HIS B 2 208 ? 61.34092  14.01397  18.06735  1.000 79.98980  ?  175 HIS D CB  1 
ATOM   2869 C CG  . HIS B 2 208 ? 61.69729  15.46704  18.02253  1.000 89.01656  ?  175 HIS D CG  1 
ATOM   2870 N ND1 . HIS B 2 208 ? 61.12605  16.34630  17.12834  1.000 85.20356  ?  175 HIS D ND1 1 
ATOM   2871 C CD2 . HIS B 2 208 ? 62.56287  16.19627  18.76602  1.000 84.27174  ?  175 HIS D CD2 1 
ATOM   2872 C CE1 . HIS B 2 208 ? 61.62650  17.55366  17.32041  1.000 75.20535  ?  175 HIS D CE1 1 
ATOM   2873 N NE2 . HIS B 2 208 ? 62.50054  17.49010  18.30857  1.000 68.03757  ?  175 HIS D NE2 1 
ATOM   2874 N N   . PRO B 2 209 ? 58.55801  15.41878  19.04195  1.000 92.77268  ?  176 PRO D N   1 
ATOM   2875 C CA  . PRO B 2 209 ? 57.26092  15.97373  18.61581  1.000 81.50969  ?  176 PRO D CA  1 
ATOM   2876 C C   . PRO B 2 209 ? 57.09330  16.08179  17.10854  1.000 84.52427  ?  176 PRO D C   1 
ATOM   2877 O O   . PRO B 2 209 ? 55.95503  16.19925  16.63809  1.000 110.02426 ?  176 PRO D O   1 
ATOM   2878 C CB  . PRO B 2 209 ? 57.24007  17.35803  19.27742  1.000 89.30503  ?  176 PRO D CB  1 
ATOM   2879 C CG  . PRO B 2 209 ? 58.13060  17.21819  20.46186  1.000 79.07238  ?  176 PRO D CG  1 
ATOM   2880 C CD  . PRO B 2 209 ? 59.21950  16.27265  20.04424  1.000 91.79862  ?  176 PRO D CD  1 
ATOM   2881 N N   . SER B 2 210 ? 58.17934  16.05243  16.33641  1.000 82.86137  ?  177 SER D N   1 
ATOM   2882 C CA  . SER B 2 210 ? 58.07949  16.13206  14.88504  1.000 89.97378  ?  177 SER D CA  1 
ATOM   2883 C C   . SER B 2 210 ? 57.77202  14.78979  14.23603  1.000 97.60406  ?  177 SER D C   1 
ATOM   2884 O O   . SER B 2 210 ? 57.50096  14.75132  13.03079  1.000 101.38282 ?  177 SER D O   1 
ATOM   2885 C CB  . SER B 2 210 ? 59.37760  16.69125  14.29807  1.000 102.80872 ?  177 SER D CB  1 
ATOM   2886 O OG  . SER B 2 210 ? 60.46526  15.81827  14.55104  1.000 84.64990  ?  177 SER D OG  1 
ATOM   2887 N N   . LEU B 2 211 ? 57.80182  13.69993  14.99651  1.000 97.63543  ?  178 LEU D N   1 
ATOM   2888 C CA  . LEU B 2 211 ? 57.61840  12.35614  14.46700  1.000 102.88137 ?  178 LEU D CA  1 
ATOM   2889 C C   . LEU B 2 211 ? 56.23621  11.83821  14.83848  1.000 102.58779 ?  178 LEU D C   1 
ATOM   2890 O O   . LEU B 2 211 ? 55.82193  11.93742  15.99877  1.000 109.97735 ?  178 LEU D O   1 
ATOM   2891 C CB  . LEU B 2 211 ? 58.69382  11.41131  15.00542  1.000 101.38700 ?  178 LEU D CB  1 
ATOM   2892 C CG  . LEU B 2 211 ? 60.14445  11.83444  14.77197  1.000 98.02870  ?  178 LEU D CG  1 
ATOM   2893 C CD1 . LEU B 2 211 ? 61.09331  10.94446  15.55861  1.000 93.93515  ?  178 LEU D CD1 1 
ATOM   2894 C CD2 . LEU B 2 211 ? 60.47517  11.80110  13.28845  1.000 103.24065 ?  178 LEU D CD2 1 
ATOM   2895 N N   . LYS B 2 212 ? 55.52639  11.28549  13.85146  1.000 109.28173 ?  179 LYS D N   1 
ATOM   2896 C CA  . LYS B 2 212 ? 54.23836  10.66148  14.13422  1.000 120.53834 ?  179 LYS D CA  1 
ATOM   2897 C C   . LYS B 2 212 ? 54.40888  9.36140   14.90851  1.000 115.06131 ?  179 LYS D C   1 
ATOM   2898 O O   . LYS B 2 212 ? 53.54841  9.00769   15.72247  1.000 118.75831 ?  179 LYS D O   1 
ATOM   2899 C CB  . LYS B 2 212 ? 53.47619  10.40999  12.83286  1.000 102.00569 ?  179 LYS D CB  1 
ATOM   2900 N N   . SER B 2 213 ? 55.50279  8.64509   14.67208  1.000 117.97722 ?  180 SER D N   1 
ATOM   2901 C CA  . SER B 2 213 ? 55.83363  7.42059   15.38170  1.000 111.44408 ?  180 SER D CA  1 
ATOM   2902 C C   . SER B 2 213 ? 57.30751  7.45423   15.74881  1.000 123.37223 ?  180 SER D C   1 
ATOM   2903 O O   . SER B 2 213 ? 58.11675  8.04891   15.02479  1.000 103.59886 ?  180 SER D O   1 
ATOM   2904 C CB  . SER B 2 213 ? 55.53221  6.17237   14.53587  1.000 112.11509 ?  180 SER D CB  1 
ATOM   2905 O OG  . SER B 2 213 ? 56.26412  6.18578   13.32293  1.000 133.66605 ?  180 SER D OG  1 
ATOM   2906 N N   . PRO B 2 214 ? 57.68681  6.84048   16.87011  1.000 123.34988 ?  181 PRO D N   1 
ATOM   2907 C CA  . PRO B 2 214 ? 59.09267  6.87733   17.29032  1.000 117.11181 ?  181 PRO D CA  1 
ATOM   2908 C C   . PRO B 2 214 ? 60.00197  6.20444   16.27148  1.000 118.47095 ?  181 PRO D C   1 
ATOM   2909 O O   . PRO B 2 214 ? 59.63721  5.20695   15.64578  1.000 131.60723 ?  181 PRO D O   1 
ATOM   2910 C CB  . PRO B 2 214 ? 59.08460  6.12169   18.62404  1.000 126.30974 ?  181 PRO D CB  1 
ATOM   2911 C CG  . PRO B 2 214 ? 57.67214  6.21208   19.10631  1.000 117.58247 ?  181 PRO D CG  1 
ATOM   2912 C CD  . PRO B 2 214 ? 56.82725  6.18333   17.86995  1.000 111.77275 ?  181 PRO D CD  1 
ATOM   2913 N N   . ILE B 2 215 ? 61.19685  6.76540   16.11063  1.000 127.63796 ?  182 ILE D N   1 
ATOM   2914 C CA  . ILE B 2 215 ? 62.17639  6.26248   15.15425  1.000 120.41308 ?  182 ILE D CA  1 
ATOM   2915 C C   . ILE B 2 215 ? 62.99751  5.16228   15.81194  1.000 117.89299 ?  182 ILE D C   1 
ATOM   2916 O O   . ILE B 2 215 ? 63.52727  5.34099   16.91553  1.000 108.51735 ?  182 ILE D O   1 
ATOM   2917 C CB  . ILE B 2 215 ? 63.08109  7.39743   14.64391  1.000 109.91142 ?  182 ILE D CB  1 
ATOM   2918 C CG1 . ILE B 2 215 ? 62.35893  8.21475   13.57121  1.000 109.32298 ?  182 ILE D CG1 1 
ATOM   2919 C CG2 . ILE B 2 215 ? 64.39321  6.84432   14.10327  1.000 91.68401  ?  182 ILE D CG2 1 
ATOM   2920 C CD1 . ILE B 2 215 ? 63.21078  9.30671   12.96107  1.000 94.62777  ?  182 ILE D CD1 1 
ATOM   2921 N N   . THR B 2 216 ? 63.10042  4.02187   15.13482  1.000 123.49353 ?  183 THR D N   1 
ATOM   2922 C CA  . THR B 2 216 ? 63.91237  2.90077   15.58238  1.000 120.89399 ?  183 THR D CA  1 
ATOM   2923 C C   . THR B 2 216 ? 64.94320  2.56799   14.51352  1.000 117.95947 ?  183 THR D C   1 
ATOM   2924 O O   . THR B 2 216 ? 64.62192  2.52151   13.32187  1.000 127.87669 ?  183 THR D O   1 
ATOM   2925 C CB  . THR B 2 216 ? 63.05040  1.66741   15.87628  1.000 120.89419 ?  183 THR D CB  1 
ATOM   2926 O OG1 . THR B 2 216 ? 62.33175  1.29187   14.69459  1.000 126.89908 ?  183 THR D OG1 1 
ATOM   2927 C CG2 . THR B 2 216 ? 62.06078  1.96120   16.99395  1.000 115.37436 ?  183 THR D CG2 1 
ATOM   2928 N N   . VAL B 2 217 ? 66.18225  2.34148   14.94219  1.000 112.63858 ?  184 VAL D N   1 
ATOM   2929 C CA  . VAL B 2 217 ? 67.27681  1.99959   14.04285  1.000 133.04805 ?  184 VAL D CA  1 
ATOM   2930 C C   . VAL B 2 217 ? 67.91269  0.70031   14.51494  1.000 134.74506 ?  184 VAL D C   1 
ATOM   2931 O O   . VAL B 2 217 ? 68.12095  0.49813   15.71649  1.000 125.91679 ?  184 VAL D O   1 
ATOM   2932 C CB  . VAL B 2 217 ? 68.32802  3.12686   13.96235  1.000 121.57122 ?  184 VAL D CB  1 
ATOM   2933 C CG1 . VAL B 2 217 ? 67.79765  4.28323   13.13105  1.000 107.47619 ?  184 VAL D CG1 1 
ATOM   2934 C CG2 . VAL B 2 217 ? 68.70752  3.60194   15.35573  1.000 124.81334 ?  184 VAL D CG2 1 
ATOM   2935 N N   . GLU B 2 218 ? 68.22000  -0.17992  13.56556  1.000 132.93645 ?  185 GLU D N   1 
ATOM   2936 C CA  . GLU B 2 218 ? 68.79755  -1.48743  13.87007  1.000 147.59665 ?  185 GLU D CA  1 
ATOM   2937 C C   . GLU B 2 218 ? 70.30206  -1.32658  14.04925  1.000 145.72252 ?  185 GLU D C   1 
ATOM   2938 O O   . GLU B 2 218 ? 71.04818  -1.19499  13.07580  1.000 146.53874 ?  185 GLU D O   1 
ATOM   2939 C CB  . GLU B 2 218 ? 68.47039  -2.49011  12.76831  1.000 153.32406 ?  185 GLU D CB  1 
ATOM   2940 C CG  . GLU B 2 218 ? 66.99264  -2.85930  12.66319  1.000 145.75052 ?  185 GLU D CG  1 
ATOM   2941 C CD  . GLU B 2 218 ? 66.14791  -1.76386  12.03630  1.000 153.78928 ?  185 GLU D CD  1 
ATOM   2942 O OE1 . GLU B 2 218 ? 66.72607  -0.78959  11.50985  1.000 142.68916 ?  185 GLU D OE1 1 
ATOM   2943 O OE2 . GLU B 2 218 ? 64.90448  -1.87663  12.07171  1.000 164.97331 ?  185 GLU D OE2 1 
ATOM   2944 N N   . TRP B 2 219 ? 70.75041  -1.34048  15.30212  1.000 132.01418 ?  186 TRP D N   1 
ATOM   2945 C CA  . TRP B 2 219 ? 72.16746  -1.18287  15.59634  1.000 136.19992 ?  186 TRP D CA  1 
ATOM   2946 C C   . TRP B 2 219 ? 72.93577  -2.45171  15.25086  1.000 155.80972 ?  186 TRP D C   1 
ATOM   2947 O O   . TRP B 2 219 ? 72.45481  -3.56877  15.46138  1.000 150.37807 ?  186 TRP D O   1 
ATOM   2948 C CB  . TRP B 2 219 ? 72.36956  -0.83750  17.07119  1.000 138.76156 ?  186 TRP D CB  1 
ATOM   2949 N N   . THR B 2 220 ? 74.14322  -2.27112  14.71688  1.000 152.35635 ?  187 THR D N   1 
ATOM   2950 C CA  . THR B 2 220 ? 75.01551  -3.38900  14.38901  1.000 161.49614 ?  187 THR D CA  1 
ATOM   2951 C C   . THR B 2 220 ? 76.14228  -3.57600  15.39556  1.000 171.51790 ?  187 THR D C   1 
ATOM   2952 O O   . THR B 2 220 ? 76.76539  -4.64319  15.41535  1.000 151.77222 ?  187 THR D O   1 
ATOM   2953 C CB  . THR B 2 220 ? 75.61532  -3.20241  12.98824  1.000 161.69911 ?  187 THR D CB  1 
ATOM   2954 O OG1 . THR B 2 220 ? 74.65969  -2.55313  12.14090  1.000 160.40665 ?  187 THR D OG1 1 
ATOM   2955 C CG2 . THR B 2 220 ? 75.97685  -4.54939  12.37679  1.000 158.90021 ?  187 THR D CG2 1 
ATOM   2956 N N   . GLY B 2 221 ? 76.40801  -2.57834  16.23188  1.000 173.23671 ?  188 GLY D N   1 
ATOM   2957 C CA  . GLY B 2 221 ? 77.48049  -2.66324  17.20399  1.000 172.72599 ?  188 GLY D CA  1 
ATOM   2958 C C   . GLY B 2 221 ? 78.61194  -1.70430  16.89559  1.000 166.22726 ?  188 GLY D C   1 
ATOM   2959 O O   . GLY B 2 221 ? 78.47437  -0.82812  16.04159  1.000 147.33192 ?  188 GLY D O   1 
ATOM   2960 N N   . GLY C 3 2   ? 48.54481  48.60141  12.33825  1.000 89.68325  ?  1   GLY A N   1 
ATOM   2961 C CA  . GLY C 3 2   ? 47.60889  49.70796  12.41465  1.000 99.24865  ?  1   GLY A CA  1 
ATOM   2962 C C   . GLY C 3 2   ? 47.55868  50.52703  11.14151  1.000 97.34109  ?  1   GLY A C   1 
ATOM   2963 O O   . GLY C 3 2   ? 48.34053  51.46028  10.96236  1.000 126.60825 ?  1   GLY A O   1 
ATOM   2964 N N   . ASP C 3 3   ? 46.62841  50.17983  10.25332  1.000 90.06415  ?  2   ASP A N   1 
ATOM   2965 C CA  . ASP C 3 3   ? 46.53427  50.83384  8.95226   1.000 88.39988  ?  2   ASP A CA  1 
ATOM   2966 C C   . ASP C 3 3   ? 45.61519  52.05262  8.98170   1.000 79.35084  ?  2   ASP A C   1 
ATOM   2967 O O   . ASP C 3 3   ? 46.07007  53.18498  8.79276   1.000 86.93708  ?  2   ASP A O   1 
ATOM   2968 C CB  . ASP C 3 3   ? 46.05220  49.83497  7.89307   1.000 97.65626  ?  2   ASP A CB  1 
ATOM   2969 C CG  . ASP C 3 3   ? 47.15618  48.91673  7.41073   1.000 109.34894 ?  2   ASP A CG  1 
ATOM   2970 O OD1 . ASP C 3 3   ? 48.25027  48.93075  8.01297   1.000 110.40803 ?  2   ASP A OD1 1 
ATOM   2971 O OD2 . ASP C 3 3   ? 46.93121  48.18662  6.42232   1.000 120.08195 -1 2   ASP A OD2 1 
ATOM   2972 N N   . SER C 3 4   ? 44.32446  51.83623  9.21870   1.000 72.14337  ?  3   SER A N   1 
ATOM   2973 C CA  . SER C 3 4   ? 43.31126  52.84432  8.95384   1.000 85.54017  ?  3   SER A CA  1 
ATOM   2974 C C   . SER C 3 4   ? 42.52329  53.19762  10.20926  1.000 71.75131  ?  3   SER A C   1 
ATOM   2975 O O   . SER C 3 4   ? 42.48609  52.44565  11.18751  1.000 66.11941  ?  3   SER A O   1 
ATOM   2976 C CB  . SER C 3 4   ? 42.34683  52.36612  7.86132   1.000 82.36065  ?  3   SER A CB  1 
ATOM   2977 O OG  . SER C 3 4   ? 41.81424  51.09246  8.18303   1.000 90.71546  ?  3   SER A OG  1 
ATOM   2978 N N   . VAL C 3 5   ? 41.89283  54.37150  10.15695  1.000 75.80446  ?  4   VAL A N   1 
ATOM   2979 C CA  . VAL C 3 5   ? 40.95971  54.84619  11.17510  1.000 78.32579  ?  4   VAL A CA  1 
ATOM   2980 C C   . VAL C 3 5   ? 39.80173  55.50294  10.43326  1.000 73.78047  ?  4   VAL A C   1 
ATOM   2981 O O   . VAL C 3 5   ? 39.97888  56.55907  9.81557   1.000 81.93037  ?  4   VAL A O   1 
ATOM   2982 C CB  . VAL C 3 5   ? 41.60010  55.83959  12.15712  1.000 64.51377  ?  4   VAL A CB  1 
ATOM   2983 C CG1 . VAL C 3 5   ? 40.53770  56.44990  13.05795  1.000 77.72555  ?  4   VAL A CG1 1 
ATOM   2984 C CG2 . VAL C 3 5   ? 42.67190  55.15990  12.98996  1.000 62.37427  ?  4   VAL A CG2 1 
ATOM   2985 N N   . THR C 3 6   ? 38.62488  54.88393  10.48454  1.000 71.59925  ?  5   THR A N   1 
ATOM   2986 C CA  . THR C 3 6   ? 37.45110  55.39727  9.78989   1.000 74.02889  ?  5   THR A CA  1 
ATOM   2987 C C   . THR C 3 6   ? 36.64190  56.28430  10.72812  1.000 75.79142  ?  5   THR A C   1 
ATOM   2988 O O   . THR C 3 6   ? 36.38214  55.91147  11.87667  1.000 76.78774  ?  5   THR A O   1 
ATOM   2989 C CB  . THR C 3 6   ? 36.58695  54.24990  9.26416   1.000 77.28352  ?  5   THR A CB  1 
ATOM   2990 O OG1 . THR C 3 6   ? 37.36932  53.42236  8.39425   1.000 106.30080 ?  5   THR A OG1 1 
ATOM   2991 C CG2 . THR C 3 6   ? 35.39166  54.79014  8.49266   1.000 91.53974  ?  5   THR A CG2 1 
ATOM   2992 N N   . GLN C 3 7   ? 36.24385  57.45403  10.23372  1.000 74.52941  ?  6   GLN A N   1 
ATOM   2993 C CA  . GLN C 3 7   ? 35.54656  58.45182  11.02961  1.000 74.76188  ?  6   GLN A CA  1 
ATOM   2994 C C   . GLN C 3 7   ? 34.24289  58.83306  10.33701  1.000 80.76060  ?  6   GLN A C   1 
ATOM   2995 O O   . GLN C 3 7   ? 34.02185  58.52486  9.16255   1.000 79.14140  ?  6   GLN A O   1 
ATOM   2996 C CB  . GLN C 3 7   ? 36.43153  59.68781  11.25218  1.000 80.38860  ?  6   GLN A CB  1 
ATOM   2997 C CG  . GLN C 3 7   ? 36.06388  60.52789  12.46365  1.000 89.40106  ?  6   GLN A CG  1 
ATOM   2998 C CD  . GLN C 3 7   ? 37.07229  61.62622  12.73177  1.000 76.09023  ?  6   GLN A CD  1 
ATOM   2999 O OE1 . GLN C 3 7   ? 38.23373  61.52748  12.33517  1.000 68.75470  ?  6   GLN A OE1 1 
ATOM   3000 N NE2 . GLN C 3 7   ? 36.63240  62.68315  13.40515  1.000 72.62829  ?  6   GLN A NE2 1 
ATOM   3001 N N   . THR C 3 8   ? 33.37073  59.50716  11.08438  1.000 78.54404  ?  7   THR A N   1 
ATOM   3002 C CA  . THR C 3 8   ? 32.08653  59.93585  10.54547  1.000 81.31407  ?  7   THR A CA  1 
ATOM   3003 C C   . THR C 3 8   ? 32.28646  60.99394  9.46752   1.000 86.31401  ?  7   THR A C   1 
ATOM   3004 O O   . THR C 3 8   ? 32.97864  61.99373  9.68274   1.000 88.77248  ?  7   THR A O   1 
ATOM   3005 C CB  . THR C 3 8   ? 31.19773  60.48624  11.66103  1.000 82.33208  ?  7   THR A CB  1 
ATOM   3006 O OG1 . THR C 3 8   ? 30.85314  59.43150  12.56672  1.000 103.50191 ?  7   THR A OG1 1 
ATOM   3007 C CG2 . THR C 3 8   ? 29.92428  61.08761  11.08523  1.000 85.11621  ?  7   THR A CG2 1 
ATOM   3008 N N   . GLU C 3 9   ? 31.67763  60.77040  8.30548   1.000 89.19844  ?  8   GLU A N   1 
ATOM   3009 C CA  . GLU C 3 9   ? 31.74610  61.73487  7.21528   1.000 86.81032  ?  8   GLU A CA  1 
ATOM   3010 C C   . GLU C 3 9   ? 30.94250  62.97789  7.57667   1.000 100.25452 ?  8   GLU A C   1 
ATOM   3011 O O   . GLU C 3 9   ? 29.71791  62.91199  7.72778   1.000 118.05959 ?  8   GLU A O   1 
ATOM   3012 C CB  . GLU C 3 9   ? 31.21553  61.11207  5.92732   1.000 86.83825  ?  8   GLU A CB  1 
ATOM   3013 C CG  . GLU C 3 9   ? 31.37548  61.98726  4.69427   1.000 87.82924  ?  8   GLU A CG  1 
ATOM   3014 C CD  . GLU C 3 9   ? 32.66995  61.71806  3.95248   1.000 124.87080 ?  8   GLU A CD  1 
ATOM   3015 O OE1 . GLU C 3 9   ? 33.37071  60.74709  4.30853   1.000 136.11072 ?  8   GLU A OE1 1 
ATOM   3016 O OE2 . GLU C 3 9   ? 32.98521  62.47513  3.01053   1.000 144.29857 -1 8   GLU A OE2 1 
ATOM   3017 N N   . GLY C 3 10  ? 31.62771  64.10893  7.71537   1.000 97.96493  ?  9   GLY A N   1 
ATOM   3018 C CA  . GLY C 3 10  ? 30.97684  65.35349  8.04489   1.000 104.90827 ?  9   GLY A CA  1 
ATOM   3019 C C   . GLY C 3 10  ? 30.32025  65.99367  6.83913   1.000 92.79201  ?  9   GLY A C   1 
ATOM   3020 O O   . GLY C 3 10  ? 30.22987  65.39721  5.76134   1.000 88.56774  ?  9   GLY A O   1 
ATOM   3021 N N   . PRO C 3 11  ? 29.84465  67.23446  6.99934   1.000 88.60376  ?  10  PRO A N   1 
ATOM   3022 C CA  . PRO C 3 11  ? 29.86351  68.05564  8.21526   1.000 87.97829  ?  10  PRO A CA  1 
ATOM   3023 C C   . PRO C 3 11  ? 28.64601  67.79913  9.09700   1.000 89.41584  ?  10  PRO A C   1 
ATOM   3024 O O   . PRO C 3 11  ? 27.56376  67.49698  8.60193   1.000 91.65369  ?  10  PRO A O   1 
ATOM   3025 C CB  . PRO C 3 11  ? 29.88277  69.49601  7.66392   1.000 89.40034  ?  10  PRO A CB  1 
ATOM   3026 C CG  . PRO C 3 11  ? 29.71871  69.38848  6.14116   1.000 90.97815  ?  10  PRO A CG  1 
ATOM   3027 C CD  . PRO C 3 11  ? 29.27970  67.98095  5.86800   1.000 91.09463  ?  10  PRO A CD  1 
ATOM   3028 N N   . VAL C 3 12  ? 28.79821  67.91547  10.41246  1.000 89.23298  ?  11  VAL A N   1 
ATOM   3029 C CA  . VAL C 3 12  ? 27.71400  67.68312  11.35938  1.000 90.05765  ?  11  VAL A CA  1 
ATOM   3030 C C   . VAL C 3 12  ? 27.14419  69.03240  11.77418  1.000 95.93091  ?  11  VAL A C   1 
ATOM   3031 O O   . VAL C 3 12  ? 27.86140  69.87662  12.32495  1.000 95.36181  ?  11  VAL A O   1 
ATOM   3032 C CB  . VAL C 3 12  ? 28.19733  66.88730  12.58168  1.000 89.95580  ?  11  VAL A CB  1 
ATOM   3033 C CG1 . VAL C 3 12  ? 27.05933  66.68897  13.56897  1.000 94.54851  ?  11  VAL A CG1 1 
ATOM   3034 C CG2 . VAL C 3 12  ? 28.77207  65.54789  12.14768  1.000 109.55879 ?  11  VAL A CG2 1 
ATOM   3035 N N   . THR C 3 13  ? 25.85591  69.23714  11.51146  1.000 94.60600  ?  12  THR A N   1 
ATOM   3036 C CA  . THR C 3 13  ? 25.15848  70.47079  11.85935  1.000 98.25448  ?  12  THR A CA  1 
ATOM   3037 C C   . THR C 3 13  ? 24.15870  70.15943  12.96628  1.000 98.54971  ?  12  THR A C   1 
ATOM   3038 O O   . THR C 3 13  ? 23.19573  69.41567  12.75011  1.000 100.17919 ?  12  THR A O   1 
ATOM   3039 C CB  . THR C 3 13  ? 24.45881  71.07028  10.64153  1.000 98.97889  ?  12  THR A CB  1 
ATOM   3040 O OG1 . THR C 3 13  ? 25.42534  71.34107  9.61873   1.000 97.69663  ?  12  THR A OG1 1 
ATOM   3041 C CG2 . THR C 3 13  ? 23.75295  72.36372  11.01912  1.000 101.44420 ?  12  THR A CG2 1 
ATOM   3042 N N   . LEU C 3 14  ? 24.38799  70.72820  14.14707  1.000 98.57198  ?  13  LEU A N   1 
ATOM   3043 C CA  . LEU C 3 14  ? 23.53198  70.50718  15.30099  1.000 100.49583 ?  13  LEU A CA  1 
ATOM   3044 C C   . LEU C 3 14  ? 23.13425  71.84356  15.91044  1.000 105.63722 ?  13  LEU A C   1 
ATOM   3045 O O   . LEU C 3 14  ? 23.81633  72.85728  15.74143  1.000 102.23260 ?  13  LEU A O   1 
ATOM   3046 C CB  . LEU C 3 14  ? 24.22534  69.64103  16.36255  1.000 98.72514  ?  13  LEU A CB  1 
ATOM   3047 C CG  . LEU C 3 14  ? 24.67013  68.23841  15.94702  1.000 96.75702  ?  13  LEU A CG  1 
ATOM   3048 C CD1 . LEU C 3 14  ? 25.31040  67.51720  17.12169  1.000 98.28716  ?  13  LEU A CD1 1 
ATOM   3049 C CD2 . LEU C 3 14  ? 23.49982  67.43958  15.39709  1.000 98.95882  ?  13  LEU A CD2 1 
ATOM   3050 N N   . SER C 3 15  ? 22.01314  71.83138  16.62342  1.000 112.64787 ?  14  SER A N   1 
ATOM   3051 C CA  . SER C 3 15  ? 21.56636  72.99044  17.37841  1.000 108.07788 ?  14  SER A CA  1 
ATOM   3052 C C   . SER C 3 15  ? 22.16144  72.95399  18.77981  1.000 112.89883 ?  14  SER A C   1 
ATOM   3053 O O   . SER C 3 15  ? 22.37943  71.88336  19.35357  1.000 106.61784 ?  14  SER A O   1 
ATOM   3054 C CB  . SER C 3 15  ? 20.03983  73.03243  17.45736  1.000 111.67528 ?  14  SER A CB  1 
ATOM   3055 O OG  . SER C 3 15  ? 19.46348  73.03499  16.16330  1.000 127.50001 ?  14  SER A OG  1 
ATOM   3056 N N   . GLU C 3 16  ? 22.43020  74.13840  19.32527  1.000 112.89080 ?  15  GLU A N   1 
ATOM   3057 C CA  . GLU C 3 16  ? 23.03342  74.22893  20.64896  1.000 109.09275 ?  15  GLU A CA  1 
ATOM   3058 C C   . GLU C 3 16  ? 22.09785  73.63678  21.69408  1.000 111.57578 ?  15  GLU A C   1 
ATOM   3059 O O   . GLU C 3 16  ? 20.95071  74.07239  21.83518  1.000 114.92252 ?  15  GLU A O   1 
ATOM   3060 C CB  . GLU C 3 16  ? 23.36323  75.68200  20.98482  1.000 110.87190 ?  15  GLU A CB  1 
ATOM   3061 C CG  . GLU C 3 16  ? 24.14595  75.84649  22.27837  1.000 111.04951 ?  15  GLU A CG  1 
ATOM   3062 C CD  . GLU C 3 16  ? 24.51430  77.28913  22.56158  1.000 131.41301 ?  15  GLU A CD  1 
ATOM   3063 O OE1 . GLU C 3 16  ? 23.98906  78.18628  21.86920  1.000 136.72504 ?  15  GLU A OE1 1 
ATOM   3064 O OE2 . GLU C 3 16  ? 25.33180  77.52541  23.47615  1.000 136.28637 -1 15  GLU A OE2 1 
ATOM   3065 N N   . GLY C 3 17  ? 22.59125  72.63813  22.42264  1.000 110.16760 ?  16  GLY A N   1 
ATOM   3066 C CA  . GLY C 3 17  ? 21.80848  71.90317  23.39109  1.000 112.52036 ?  16  GLY A CA  1 
ATOM   3067 C C   . GLY C 3 17  ? 21.57684  70.45394  23.02337  1.000 111.31884 ?  16  GLY A C   1 
ATOM   3068 O O   . GLY C 3 17  ? 21.18972  69.66212  23.89281  1.000 112.93815 ?  16  GLY A O   1 
ATOM   3069 N N   . THR C 3 18  ? 21.79706  70.08518  21.76362  1.000 112.82515 ?  17  THR A N   1 
ATOM   3070 C CA  . THR C 3 18  ? 21.64313  68.70708  21.32747  1.000 114.08910 ?  17  THR A CA  1 
ATOM   3071 C C   . THR C 3 18  ? 22.85397  67.88002  21.75749  1.000 115.76908 ?  17  THR A C   1 
ATOM   3072 O O   . THR C 3 18  ? 23.78136  68.37098  22.40775  1.000 105.15505 ?  17  THR A O   1 
ATOM   3073 C CB  . THR C 3 18  ? 21.45201  68.64347  19.81317  1.000 106.97226 ?  17  THR A CB  1 
ATOM   3074 O OG1 . THR C 3 18  ? 22.58432  69.23256  19.16197  1.000 125.67990 ?  17  THR A OG1 1 
ATOM   3075 C CG2 . THR C 3 18  ? 20.19427  69.38912  19.39965  1.000 110.14682 ?  17  THR A CG2 1 
ATOM   3076 N N   . SER C 3 19  ? 22.84780  66.60369  21.38464  1.000 115.15076 ?  18  SER A N   1 
ATOM   3077 C CA  . SER C 3 19  ? 23.92203  65.68041  21.71717  1.000 120.03880 ?  18  SER A CA  1 
ATOM   3078 C C   . SER C 3 19  ? 24.71758  65.33416  20.46622  1.000 113.23598 ?  18  SER A C   1 
ATOM   3079 O O   . SER C 3 19  ? 24.14740  65.14705  19.38665  1.000 119.92726 ?  18  SER A O   1 
ATOM   3080 C CB  . SER C 3 19  ? 23.37290  64.40161  22.35580  1.000 111.85000 ?  18  SER A CB  1 
ATOM   3081 O OG  . SER C 3 19  ? 22.57790  63.67314  21.43704  1.000 135.66334 ?  18  SER A OG  1 
ATOM   3082 N N   . LEU C 3 20  ? 26.03459  65.25050  20.61871  1.000 95.30410  ?  19  LEU A N   1 
ATOM   3083 C CA  . LEU C 3 20  ? 26.93299  64.90760  19.52804  1.000 98.11632  ?  19  LEU A CA  1 
ATOM   3084 C C   . LEU C 3 20  ? 27.29188  63.42831  19.58854  1.000 101.40984 ?  19  LEU A C   1 
ATOM   3085 O O   . LEU C 3 20  ? 27.40197  62.84054  20.66727  1.000 106.16455 ?  19  LEU A O   1 
ATOM   3086 C CB  . LEU C 3 20  ? 28.20647  65.75566  19.58426  1.000 89.61927  ?  19  LEU A CB  1 
ATOM   3087 C CG  . LEU C 3 20  ? 29.24288  65.54331  18.47832  1.000 94.41596  ?  19  LEU A CG  1 
ATOM   3088 C CD1 . LEU C 3 20  ? 28.67330  65.93384  17.12247  1.000 97.54680  ?  19  LEU A CD1 1 
ATOM   3089 C CD2 . LEU C 3 20  ? 30.51947  66.31612  18.77470  1.000 92.80174  ?  19  LEU A CD2 1 
ATOM   3090 N N   . THR C 3 21  ? 27.46523  62.82697  18.41100  1.000 103.60639 ?  20  THR A N   1 
ATOM   3091 C CA  . THR C 3 21  ? 27.88389  61.42896  18.31825  1.000 96.27649  ?  20  THR A CA  1 
ATOM   3092 C C   . THR C 3 21  ? 28.71571  61.28466  17.04667  1.000 98.63219  ?  20  THR A C   1 
ATOM   3093 O O   . THR C 3 21  ? 28.16202  61.17551  15.94858  1.000 100.05237 ?  20  THR A O   1 
ATOM   3094 C CB  . THR C 3 21  ? 26.68775  60.48645  18.31500  1.000 92.82246  ?  20  THR A CB  1 
ATOM   3095 O OG1 . THR C 3 21  ? 25.95186  60.64193  19.53491  1.000 121.76340 ?  20  THR A OG1 1 
ATOM   3096 C CG2 . THR C 3 21  ? 27.15085  59.04196  18.19457  1.000 92.41296  ?  20  THR A CG2 1 
ATOM   3097 N N   . VAL C 3 22  ? 30.03509  61.29179  17.20388  1.000 86.10117  ?  21  VAL A N   1 
ATOM   3098 C CA  . VAL C 3 22  ? 30.96712  61.12065  16.09594  1.000 87.45960  ?  21  VAL A CA  1 
ATOM   3099 C C   . VAL C 3 22  ? 31.50095  59.69609  16.16372  1.000 83.31761  ?  21  VAL A C   1 
ATOM   3100 O O   . VAL C 3 22  ? 32.21970  59.33453  17.10192  1.000 79.75442  ?  21  VAL A O   1 
ATOM   3101 C CB  . VAL C 3 22  ? 32.10587  62.14786  16.14709  1.000 79.29182  ?  21  VAL A CB  1 
ATOM   3102 C CG1 . VAL C 3 22  ? 32.98778  62.02275  14.91370  1.000 77.48749  ?  21  VAL A CG1 1 
ATOM   3103 C CG2 . VAL C 3 22  ? 31.54578  63.55633  16.26895  1.000 88.56740  ?  21  VAL A CG2 1 
ATOM   3104 N N   . ASN C 3 23  ? 31.14988  58.88324  15.17256  1.000 94.42755  ?  22  ASN A N   1 
ATOM   3105 C CA  . ASN C 3 23  ? 31.58137  57.49516  15.14799  1.000 86.73390  ?  22  ASN A CA  1 
ATOM   3106 C C   . ASN C 3 23  ? 33.04592  57.39100  14.74304  1.000 78.94612  ?  22  ASN A C   1 
ATOM   3107 O O   . ASN C 3 23  ? 33.55817  58.19567  13.95955  1.000 89.17953  ?  22  ASN A O   1 
ATOM   3108 C CB  . ASN C 3 23  ? 30.72093  56.67869  14.18330  1.000 93.79655  ?  22  ASN A CB  1 
ATOM   3109 C CG  . ASN C 3 23  ? 29.24455  56.75515  14.51183  1.000 97.06713  ?  22  ASN A CG  1 
ATOM   3110 O OD1 . ASN C 3 23  ? 28.85830  56.81432  15.67922  1.000 96.18517  ?  22  ASN A OD1 1 
ATOM   3111 N ND2 . ASN C 3 23  ? 28.40885  56.75700  13.47968  1.000 90.68244  ?  22  ASN A ND2 1 
ATOM   3112 N N   . CYS C 3 24  ? 33.71994  56.38459  15.29394  1.000 94.78703  ?  23  CYS A N   1 
ATOM   3113 C CA  . CYS C 3 24  ? 35.09839  56.08382  14.93331  1.000 83.11840  ?  23  CYS A CA  1 
ATOM   3114 C C   . CYS C 3 24  ? 35.33212  54.59468  15.12521  1.000 83.64454  ?  23  CYS A C   1 
ATOM   3115 O O   . CYS C 3 24  ? 35.00921  54.04690  16.18292  1.000 85.09370  ?  23  CYS A O   1 
ATOM   3116 C CB  . CYS C 3 24  ? 36.09295  56.89337  15.77401  1.000 72.60737  ?  23  CYS A CB  1 
ATOM   3117 S SG  . CYS C 3 24  ? 37.82215  56.42618  15.50379  1.000 80.70372  ?  23  CYS A SG  1 
ATOM   3118 N N   . SER C 3 25  ? 35.88240  53.94677  14.10122  1.000 83.39211  ?  24  SER A N   1 
ATOM   3119 C CA  . SER C 3 25  ? 36.20316  52.52563  14.14767  1.000 76.69326  ?  24  SER A CA  1 
ATOM   3120 C C   . SER C 3 25  ? 37.62306  52.33710  13.63991  1.000 78.69888  ?  24  SER A C   1 
ATOM   3121 O O   . SER C 3 25  ? 37.93356  52.71393  12.50507  1.000 75.60425  ?  24  SER A O   1 
ATOM   3122 C CB  . SER C 3 25  ? 35.21754  51.70490  13.31184  1.000 80.36998  ?  24  SER A CB  1 
ATOM   3123 O OG  . SER C 3 25  ? 35.29921  52.05337  11.94133  1.000 86.42072  ?  24  SER A OG  1 
ATOM   3124 N N   . TYR C 3 26  ? 38.47859  51.75973  14.47412  1.000 77.37854  ?  25  TYR A N   1 
ATOM   3125 C CA  . TYR C 3 26  ? 39.87513  51.55014  14.13007  1.000 71.50138  ?  25  TYR A CA  1 
ATOM   3126 C C   . TYR C 3 26  ? 40.11589  50.10595  13.70740  1.000 71.59993  ?  25  TYR A C   1 
ATOM   3127 O O   . TYR C 3 26  ? 39.38165  49.18904  14.08281  1.000 74.30974  ?  25  TYR A O   1 
ATOM   3128 C CB  . TYR C 3 26  ? 40.78467  51.91376  15.30722  1.000 70.60391  ?  25  TYR A CB  1 
ATOM   3129 C CG  . TYR C 3 26  ? 40.58528  51.06474  16.54352  1.000 70.49484  ?  25  TYR A CG  1 
ATOM   3130 C CD1 . TYR C 3 26  ? 39.65369  51.41935  17.51013  1.000 69.75038  ?  25  TYR A CD1 1 
ATOM   3131 C CD2 . TYR C 3 26  ? 41.33839  49.91559  16.75046  1.000 68.14486  ?  25  TYR A CD2 1 
ATOM   3132 C CE1 . TYR C 3 26  ? 39.47190  50.64958  18.64363  1.000 73.21487  ?  25  TYR A CE1 1 
ATOM   3133 C CE2 . TYR C 3 26  ? 41.16198  49.13897  17.87944  1.000 69.41866  ?  25  TYR A CE2 1 
ATOM   3134 C CZ  . TYR C 3 26  ? 40.22764  49.51035  18.82271  1.000 73.09643  ?  25  TYR A CZ  1 
ATOM   3135 O OH  . TYR C 3 26  ? 40.04890  48.74032  19.94921  1.000 79.48530  ?  25  TYR A OH  1 
ATOM   3136 N N   . GLU C 3 27  ? 41.16512  49.91766  12.91030  1.000 70.20521  ?  26  GLU A N   1 
ATOM   3137 C CA  . GLU C 3 27  ? 41.57616  48.59503  12.44745  1.000 71.63801  ?  26  GLU A CA  1 
ATOM   3138 C C   . GLU C 3 27  ? 43.08861  48.50383  12.59035  1.000 71.53728  ?  26  GLU A C   1 
ATOM   3139 O O   . GLU C 3 27  ? 43.82286  49.20912  11.89133  1.000 66.83554  ?  26  GLU A O   1 
ATOM   3140 C CB  . GLU C 3 27  ? 41.14288  48.35155  11.00175  1.000 74.15594  ?  26  GLU A CB  1 
ATOM   3141 C CG  . GLU C 3 27  ? 41.58197  47.00948  10.44127  1.000 85.21345  ?  26  GLU A CG  1 
ATOM   3142 C CD  . GLU C 3 27  ? 41.04762  46.75818  9.04535   1.000 99.18257  ?  26  GLU A CD  1 
ATOM   3143 O OE1 . GLU C 3 27  ? 40.12775  47.48774  8.61899   1.000 84.63644  ?  26  GLU A OE1 1 
ATOM   3144 O OE2 . GLU C 3 27  ? 41.54844  45.83179  8.37372   1.000 118.32297 -1 26  GLU A OE2 1 
ATOM   3145 N N   . THR C 3 28  ? 43.55234  47.64206  13.49322  1.000 89.60130  ?  27  THR A N   1 
ATOM   3146 C CA  . THR C 3 28  ? 44.97225  47.51909  13.78476  1.000 71.35376  ?  27  THR A CA  1 
ATOM   3147 C C   . THR C 3 28  ? 45.31470  46.06455  14.06963  1.000 67.09040  ?  27  THR A C   1 
ATOM   3148 O O   . THR C 3 28  ? 44.44008  45.23719  14.33782  1.000 85.41543  ?  27  THR A O   1 
ATOM   3149 C CB  . THR C 3 28  ? 45.38340  48.39050  14.97966  1.000 62.85266  ?  27  THR A CB  1 
ATOM   3150 O OG1 . THR C 3 28  ? 46.77198  48.18540  15.26723  1.000 89.70576  ?  27  THR A OG1 1 
ATOM   3151 C CG2 . THR C 3 28  ? 44.56003  48.03169  16.20572  1.000 68.70937  ?  27  THR A CG2 1 
ATOM   3152 N N   . LYS C 3 29  ? 46.61267  45.76362  14.00640  1.000 77.19653  ?  28  LYS A N   1 
ATOM   3153 C CA  . LYS C 3 29  ? 47.12132  44.44216  14.34703  1.000 66.26194  ?  28  LYS A CA  1 
ATOM   3154 C C   . LYS C 3 29  ? 47.79648  44.39605  15.71017  1.000 68.94372  ?  28  LYS A C   1 
ATOM   3155 O O   . LYS C 3 29  ? 48.00536  43.30115  16.24350  1.000 74.52336  ?  28  LYS A O   1 
ATOM   3156 C CB  . LYS C 3 29  ? 48.11418  43.96109  13.28149  1.000 66.12407  ?  28  LYS A CB  1 
ATOM   3157 C CG  . LYS C 3 29  ? 47.52490  43.83848  11.88659  1.000 68.80021  ?  28  LYS A CG  1 
ATOM   3158 C CD  . LYS C 3 29  ? 48.56719  43.35399  10.89184  1.000 95.27143  ?  28  LYS A CD  1 
ATOM   3159 C CE  . LYS C 3 29  ? 47.98867  43.24944  9.49069   1.000 120.18391 ?  28  LYS A CE  1 
ATOM   3160 N NZ  . LYS C 3 29  ? 49.00409  42.78553  8.50528   1.000 138.99161 ?  28  LYS A NZ  1 
ATOM   3161 N N   . GLN C 3 30  ? 48.14061  45.54797  16.27904  1.000 62.09086  ?  29  GLN A N   1 
ATOM   3162 C CA  . GLN C 3 30  ? 48.77319  45.63395  17.58458  1.000 59.46575  ?  29  GLN A CA  1 
ATOM   3163 C C   . GLN C 3 30  ? 47.94462  46.52370  18.50063  1.000 59.44081  ?  29  GLN A C   1 
ATOM   3164 O O   . GLN C 3 30  ? 47.10439  47.30327  18.04647  1.000 62.54600  ?  29  GLN A O   1 
ATOM   3165 C CB  . GLN C 3 30  ? 50.20147  46.18081  17.47593  1.000 61.62043  ?  29  GLN A CB  1 
ATOM   3166 C CG  . GLN C 3 30  ? 51.17511  45.23817  16.79725  1.000 56.16730  ?  29  GLN A CG  1 
ATOM   3167 C CD  . GLN C 3 30  ? 52.50841  45.89435  16.50812  1.000 58.21584  ?  29  GLN A CD  1 
ATOM   3168 O OE1 . GLN C 3 30  ? 52.59015  46.83642  15.72055  1.000 87.31394  ?  29  GLN A OE1 1 
ATOM   3169 N NE2 . GLN C 3 30  ? 53.56437  45.39611  17.14126  1.000 56.08590  ?  29  GLN A NE2 1 
ATOM   3170 N N   . TYR C 3 31  ? 48.19856  46.39852  19.79826  1.000 59.02069  ?  36  TYR A N   1 
ATOM   3171 C CA  . TYR C 3 31  ? 47.46009  47.14293  20.81040  1.000 59.45035  ?  36  TYR A CA  1 
ATOM   3172 C C   . TYR C 3 31  ? 47.65984  48.64246  20.62111  1.000 59.48794  ?  36  TYR A C   1 
ATOM   3173 O O   . TYR C 3 31  ? 48.79536  49.12765  20.74023  1.000 63.56337  ?  36  TYR A O   1 
ATOM   3174 C CB  . TYR C 3 31  ? 47.91549  46.72231  22.20678  1.000 59.44745  ?  36  TYR A CB  1 
ATOM   3175 C CG  . TYR C 3 31  ? 47.13762  47.35800  23.34041  1.000 60.56128  ?  36  TYR A CG  1 
ATOM   3176 C CD1 . TYR C 3 31  ? 47.48772  48.60825  23.83763  1.000 64.08708  ?  36  TYR A CD1 1 
ATOM   3177 C CD2 . TYR C 3 31  ? 46.06212  46.70125  23.92281  1.000 63.93915  ?  36  TYR A CD2 1 
ATOM   3178 C CE1 . TYR C 3 31  ? 46.78224  49.18939  24.87326  1.000 69.13846  ?  36  TYR A CE1 1 
ATOM   3179 C CE2 . TYR C 3 31  ? 45.35172  47.27412  24.96099  1.000 65.29708  ?  36  TYR A CE2 1 
ATOM   3180 C CZ  . TYR C 3 31  ? 45.71612  48.51767  25.43146  1.000 72.96880  ?  36  TYR A CZ  1 
ATOM   3181 O OH  . TYR C 3 31  ? 45.01206  49.09263  26.46394  1.000 91.23157  ?  36  TYR A OH  1 
ATOM   3182 N N   . PRO C 3 32  ? 46.60675  49.40664  20.32877  1.000 58.26383  ?  37  PRO A N   1 
ATOM   3183 C CA  . PRO C 3 32  ? 46.77458  50.85373  20.16806  1.000 56.61113  ?  37  PRO A CA  1 
ATOM   3184 C C   . PRO C 3 32  ? 46.37015  51.63671  21.40638  1.000 61.32647  ?  37  PRO A C   1 
ATOM   3185 O O   . PRO C 3 32  ? 45.74711  51.09384  22.32431  1.000 58.80439  ?  37  PRO A O   1 
ATOM   3186 C CB  . PRO C 3 32  ? 45.84851  51.16584  18.99035  1.000 57.96766  ?  37  PRO A CB  1 
ATOM   3187 C CG  . PRO C 3 32  ? 44.70578  50.20855  19.19867  1.000 60.88123  ?  37  PRO A CG  1 
ATOM   3188 C CD  . PRO C 3 32  ? 45.27897  48.96446  19.86652  1.000 61.22952  ?  37  PRO A CD  1 
ATOM   3189 N N   . THR C 3 33  ? 46.73264  52.91551  21.43871  1.000 70.41568  ?  38  THR A N   1 
ATOM   3190 C CA  . THR C 3 33  ? 46.21232  53.87245  22.40670  1.000 58.77614  ?  38  THR A CA  1 
ATOM   3191 C C   . THR C 3 33  ? 45.39361  54.89825  21.63722  1.000 60.55578  ?  38  THR A C   1 
ATOM   3192 O O   . THR C 3 33  ? 45.90403  55.52623  20.70474  1.000 67.31343  ?  38  THR A O   1 
ATOM   3193 C CB  . THR C 3 33  ? 47.33793  54.54958  23.18837  1.000 54.58533  ?  38  THR A CB  1 
ATOM   3194 O OG1 . THR C 3 33  ? 47.91513  53.61299  24.10642  1.000 62.95379  ?  38  THR A OG1 1 
ATOM   3195 C CG2 . THR C 3 33  ? 46.80525  55.74679  23.96084  1.000 65.06430  ?  38  THR A CG2 1 
ATOM   3196 N N   . LEU C 3 34  ? 44.12978  55.05734  22.01626  1.000 59.24054  ?  39  LEU A N   1 
ATOM   3197 C CA  . LEU C 3 34  ? 43.19389  55.85785  21.24059  1.000 60.28918  ?  39  LEU A CA  1 
ATOM   3198 C C   . LEU C 3 34  ? 43.17548  57.30185  21.72590  1.000 64.34607  ?  39  LEU A C   1 
ATOM   3199 O O   . LEU C 3 34  ? 43.27994  57.57051  22.92626  1.000 63.85046  ?  39  LEU A O   1 
ATOM   3200 C CB  . LEU C 3 34  ? 41.79274  55.25234  21.31738  1.000 72.96520  ?  39  LEU A CB  1 
ATOM   3201 C CG  . LEU C 3 34  ? 41.72111  53.77933  20.90710  1.000 65.65675  ?  39  LEU A CG  1 
ATOM   3202 C CD1 . LEU C 3 34  ? 40.28786  53.27696  20.92628  1.000 71.38682  ?  39  LEU A CD1 1 
ATOM   3203 C CD2 . LEU C 3 34  ? 42.35047  53.56945  19.53728  1.000 62.45669  ?  39  LEU A CD2 1 
ATOM   3204 N N   . PHE C 3 35  ? 43.03939  58.22913  20.77874  1.000 66.78541  ?  40  PHE A N   1 
ATOM   3205 C CA  . PHE C 3 35  ? 43.06545  59.65643  21.05905  1.000 67.65322  ?  40  PHE A CA  1 
ATOM   3206 C C   . PHE C 3 35  ? 41.88496  60.34427  20.38701  1.000 62.26034  ?  40  PHE A C   1 
ATOM   3207 O O   . PHE C 3 35  ? 41.27561  59.81586  19.45354  1.000 73.12813  ?  40  PHE A O   1 
ATOM   3208 C CB  . PHE C 3 35  ? 44.36722  60.31116  20.56819  1.000 68.84409  ?  40  PHE A CB  1 
ATOM   3209 C CG  . PHE C 3 35  ? 45.61079  59.76365  21.20734  1.000 63.26405  ?  40  PHE A CG  1 
ATOM   3210 C CD1 . PHE C 3 35  ? 46.24378  58.65057  20.68255  1.000 55.14364  ?  40  PHE A CD1 1 
ATOM   3211 C CD2 . PHE C 3 35  ? 46.16064  60.37767  22.31958  1.000 66.69022  ?  40  PHE A CD2 1 
ATOM   3212 C CE1 . PHE C 3 35  ? 47.39453  58.15218  21.26458  1.000 66.13336  ?  40  PHE A CE1 1 
ATOM   3213 C CE2 . PHE C 3 35  ? 47.30996  59.88311  22.90572  1.000 65.23059  ?  40  PHE A CE2 1 
ATOM   3214 C CZ  . PHE C 3 35  ? 47.92714  58.76890  22.37729  1.000 70.30843  ?  40  PHE A CZ  1 
ATOM   3215 N N   . TRP C 3 36  ? 41.57446  61.54298  20.87746  1.000 63.24123  ?  41  TRP A N   1 
ATOM   3216 C CA  . TRP C 3 36  ? 40.64236  62.45574  20.22480  1.000 64.85217  ?  41  TRP A CA  1 
ATOM   3217 C C   . TRP C 3 36  ? 41.28312  63.83392  20.19034  1.000 64.71353  ?  41  TRP A C   1 
ATOM   3218 O O   . TRP C 3 36  ? 41.67570  64.36274  21.23532  1.000 66.28304  ?  41  TRP A O   1 
ATOM   3219 C CB  . TRP C 3 36  ? 39.29178  62.50716  20.94811  1.000 67.45343  ?  41  TRP A CB  1 
ATOM   3220 C CG  . TRP C 3 36  ? 38.26516  61.56840  20.38433  1.000 68.59950  ?  41  TRP A CG  1 
ATOM   3221 C CD1 . TRP C 3 36  ? 37.73963  60.46843  20.99348  1.000 74.91685  ?  41  TRP A CD1 1 
ATOM   3222 C CD2 . TRP C 3 36  ? 37.64203  61.64814  19.09523  1.000 70.58885  ?  41  TRP A CD2 1 
ATOM   3223 N NE1 . TRP C 3 36  ? 36.82839  59.85654  20.16627  1.000 74.41446  ?  41  TRP A NE1 1 
ATOM   3224 C CE2 . TRP C 3 36  ? 36.75052  60.56132  18.99425  1.000 70.66961  ?  41  TRP A CE2 1 
ATOM   3225 C CE3 . TRP C 3 36  ? 37.75106  62.53268  18.01795  1.000 72.26079  ?  41  TRP A CE3 1 
ATOM   3226 C CZ2 . TRP C 3 36  ? 35.97467  60.33435  17.85885  1.000 71.85714  ?  41  TRP A CZ2 1 
ATOM   3227 C CZ3 . TRP C 3 36  ? 36.97915  62.30630  16.89205  1.000 70.05061  ?  41  TRP A CZ3 1 
ATOM   3228 C CH2 . TRP C 3 36  ? 36.10223  61.21646  16.82183  1.000 71.46257  ?  41  TRP A CH2 1 
ATOM   3229 N N   . TYR C 3 37  ? 41.39826  64.40694  18.99565  1.000 64.55086  ?  42  TYR A N   1 
ATOM   3230 C CA  . TYR C 3 37  ? 42.00270  65.71722  18.80397  1.000 70.34719  ?  42  TYR A CA  1 
ATOM   3231 C C   . TYR C 3 37  ? 40.97537  66.68406  18.23408  1.000 67.10189  ?  42  TYR A C   1 
ATOM   3232 O O   . TYR C 3 37  ? 40.14226  66.30389  17.40539  1.000 76.06108  ?  42  TYR A O   1 
ATOM   3233 C CB  . TYR C 3 37  ? 43.21827  65.63821  17.87289  1.000 65.59962  ?  42  TYR A CB  1 
ATOM   3234 C CG  . TYR C 3 37  ? 44.49041  65.18936  18.55667  1.000 73.18312  ?  42  TYR A CG  1 
ATOM   3235 C CD1 . TYR C 3 37  ? 44.76091  63.84151  18.75191  1.000 69.22923  ?  42  TYR A CD1 1 
ATOM   3236 C CD2 . TYR C 3 37  ? 45.42339  66.11578  19.00309  1.000 70.10996  ?  42  TYR A CD2 1 
ATOM   3237 C CE1 . TYR C 3 37  ? 45.92343  63.42967  19.37612  1.000 62.61743  ?  42  TYR A CE1 1 
ATOM   3238 C CE2 . TYR C 3 37  ? 46.58811  65.71388  19.62748  1.000 70.72512  ?  42  TYR A CE2 1 
ATOM   3239 C CZ  . TYR C 3 37  ? 46.83361  64.37043  19.81131  1.000 71.01397  ?  42  TYR A CZ  1 
ATOM   3240 O OH  . TYR C 3 37  ? 47.99382  63.96828  20.43256  1.000 68.80769  ?  42  TYR A OH  1 
ATOM   3241 N N   . VAL C 3 38  ? 41.04021  67.93457  18.68342  1.000 68.64031  ?  43  VAL A N   1 
ATOM   3242 C CA  . VAL C 3 38  ? 40.15432  68.99409  18.21953  1.000 71.03909  ?  43  VAL A CA  1 
ATOM   3243 C C   . VAL C 3 38  ? 41.00544  70.11786  17.64427  1.000 71.54896  ?  43  VAL A C   1 
ATOM   3244 O O   . VAL C 3 38  ? 42.02953  70.49496  18.22503  1.000 71.18460  ?  43  VAL A O   1 
ATOM   3245 C CB  . VAL C 3 38  ? 39.24035  69.50901  19.35342  1.000 73.37247  ?  43  VAL A CB  1 
ATOM   3246 C CG1 . VAL C 3 38  ? 40.06032  69.90678  20.57432  1.000 73.55864  ?  43  VAL A CG1 1 
ATOM   3247 C CG2 . VAL C 3 38  ? 38.38644  70.67135  18.87062  1.000 80.50272  ?  43  VAL A CG2 1 
ATOM   3248 N N   . GLN C 3 39  ? 40.59117  70.63814  16.49025  1.000 72.67526  ?  44  GLN A N   1 
ATOM   3249 C CA  . GLN C 3 39  ? 41.29963  71.72235  15.82096  1.000 73.75642  ?  44  GLN A CA  1 
ATOM   3250 C C   . GLN C 3 39  ? 40.31908  72.84639  15.52819  1.000 87.69087  ?  44  GLN A C   1 
ATOM   3251 O O   . GLN C 3 39  ? 39.37242  72.66244  14.75629  1.000 82.10360  ?  44  GLN A O   1 
ATOM   3252 C CB  . GLN C 3 39  ? 41.96328  71.24070  14.52827  1.000 72.36937  ?  44  GLN A CB  1 
ATOM   3253 C CG  . GLN C 3 39  ? 42.81712  72.30043  13.85061  1.000 78.99194  ?  44  GLN A CG  1 
ATOM   3254 C CD  . GLN C 3 39  ? 43.45665  71.80612  12.56963  1.000 79.04679  ?  44  GLN A CD  1 
ATOM   3255 O OE1 . GLN C 3 39  ? 43.01427  70.81965  11.98160  1.000 79.60041  ?  44  GLN A OE1 1 
ATOM   3256 N NE2 . GLN C 3 39  ? 44.50729  72.48983  12.13123  1.000 85.76595  ?  44  GLN A NE2 1 
ATOM   3257 N N   . TYR C 3 40  ? 40.55006  74.00309  16.13743  1.000 99.73928  ?  45  TYR A N   1 
ATOM   3258 C CA  . TYR C 3 40  ? 39.71194  75.16917  15.92445  1.000 90.50360  ?  45  TYR A CA  1 
ATOM   3259 C C   . TYR C 3 40  ? 40.11812  75.88404  14.63667  1.000 106.06949 ?  45  TYR A C   1 
ATOM   3260 O O   . TYR C 3 40  ? 41.24294  75.72135  14.15647  1.000 98.27380  ?  45  TYR A O   1 
ATOM   3261 C CB  . TYR C 3 40  ? 39.81048  76.09727  17.13240  1.000 85.46450  ?  45  TYR A CB  1 
ATOM   3262 C CG  . TYR C 3 40  ? 39.27530  75.46604  18.39935  1.000 87.11991  ?  45  TYR A CG  1 
ATOM   3263 C CD1 . TYR C 3 40  ? 37.92768  75.55079  18.72523  1.000 99.11669  ?  45  TYR A CD1 1 
ATOM   3264 C CD2 . TYR C 3 40  ? 40.11377  74.76921  19.25956  1.000 109.16861 ?  45  TYR A CD2 1 
ATOM   3265 C CE1 . TYR C 3 40  ? 37.43241  74.96789  19.87768  1.000 106.09367 ?  45  TYR A CE1 1 
ATOM   3266 C CE2 . TYR C 3 40  ? 39.62777  74.18333  20.41384  1.000 97.49903  ?  45  TYR A CE2 1 
ATOM   3267 C CZ  . TYR C 3 40  ? 38.28746  74.28564  20.71781  1.000 111.69459 ?  45  TYR A CZ  1 
ATOM   3268 O OH  . TYR C 3 40  ? 37.80189  73.70339  21.86610  1.000 122.90965 ?  45  TYR A OH  1 
ATOM   3269 N N   . PRO C 3 41  ? 39.21118  76.67430  14.04862  1.000 118.52872 ?  46  PRO A N   1 
ATOM   3270 C CA  . PRO C 3 41  ? 39.47340  77.22569  12.70532  1.000 120.59770 ?  46  PRO A CA  1 
ATOM   3271 C C   . PRO C 3 41  ? 40.75397  78.03758  12.58552  1.000 115.74363 ?  46  PRO A C   1 
ATOM   3272 O O   . PRO C 3 41  ? 41.26624  78.18405  11.46889  1.000 127.02935 ?  46  PRO A O   1 
ATOM   3273 C CB  . PRO C 3 41  ? 38.23903  78.09831  12.44100  1.000 94.52984  ?  46  PRO A CB  1 
ATOM   3274 C CG  . PRO C 3 41  ? 37.16725  77.48356  13.26583  1.000 90.00747  ?  46  PRO A CG  1 
ATOM   3275 C CD  . PRO C 3 41  ? 37.84623  76.98907  14.51022  1.000 98.36971  ?  46  PRO A CD  1 
ATOM   3276 N N   . GLY C 3 42  ? 41.29047  78.56650  13.68132  1.000 119.53192 ?  47  GLY A N   1 
ATOM   3277 C CA  . GLY C 3 42  ? 42.49251  79.37241  13.59360  1.000 126.48377 ?  47  GLY A CA  1 
ATOM   3278 C C   . GLY C 3 42  ? 43.63864  78.87469  14.44908  1.000 106.42401 ?  47  GLY A C   1 
ATOM   3279 O O   . GLY C 3 42  ? 44.57808  79.62424  14.73172  1.000 121.04879 ?  47  GLY A O   1 
ATOM   3280 N N   . GLU C 3 43  ? 43.57969  77.61213  14.86427  1.000 104.46595 ?  48  GLU A N   1 
ATOM   3281 C CA  . GLU C 3 43  ? 44.57615  77.03025  15.75190  1.000 113.82977 ?  48  GLU A CA  1 
ATOM   3282 C C   . GLU C 3 43  ? 45.04577  75.69557  15.18478  1.000 96.22364  ?  48  GLU A C   1 
ATOM   3283 O O   . GLU C 3 43  ? 44.54864  75.21629  14.16106  1.000 90.30937  ?  48  GLU A O   1 
ATOM   3284 C CB  . GLU C 3 43  ? 44.01439  76.84782  17.16816  1.000 118.02252 ?  48  GLU A CB  1 
ATOM   3285 C CG  . GLU C 3 43  ? 43.45209  78.11699  17.78598  1.000 125.16619 ?  48  GLU A CG  1 
ATOM   3286 C CD  . GLU C 3 43  ? 42.79090  77.86792  19.12656  1.000 138.91496 ?  48  GLU A CD  1 
ATOM   3287 O OE1 . GLU C 3 43  ? 42.94104  76.75145  19.66659  1.000 134.11480 ?  48  GLU A OE1 1 
ATOM   3288 O OE2 . GLU C 3 43  ? 42.11782  78.78748  19.63840  1.000 131.94992 -1 48  GLU A OE2 1 
ATOM   3289 N N   . GLY C 3 44  ? 46.01894  75.09450  15.86381  1.000 77.43764  ?  49  GLY A N   1 
ATOM   3290 C CA  . GLY C 3 44  ? 46.49445  73.77920  15.51362  1.000 76.32043  ?  49  GLY A CA  1 
ATOM   3291 C C   . GLY C 3 44  ? 45.77826  72.70858  16.30952  1.000 87.15083  ?  49  GLY A C   1 
ATOM   3292 O O   . GLY C 3 44  ? 45.09678  72.99321  17.29958  1.000 103.79146 ?  49  GLY A O   1 
ATOM   3293 N N   . PRO C 3 45  ? 45.91243  71.45136  15.88731  1.000 81.08145  ?  50  PRO A N   1 
ATOM   3294 C CA  . PRO C 3 45  ? 45.23227  70.35882  16.59771  1.000 72.75509  ?  50  PRO A CA  1 
ATOM   3295 C C   . PRO C 3 45  ? 45.79538  70.18700  18.00100  1.000 78.27448  ?  50  PRO A C   1 
ATOM   3296 O O   . PRO C 3 45  ? 47.00840  70.07412  18.18928  1.000 88.72252  ?  50  PRO A O   1 
ATOM   3297 C CB  . PRO C 3 45  ? 45.51498  69.13103  15.72218  1.000 66.76528  ?  50  PRO A CB  1 
ATOM   3298 C CG  . PRO C 3 45  ? 45.92174  69.68542  14.38868  1.000 81.33800  ?  50  PRO A CG  1 
ATOM   3299 C CD  . PRO C 3 45  ? 46.61812  70.97511  14.68731  1.000 74.11025  ?  50  PRO A CD  1 
ATOM   3300 N N   . GLN C 3 46  ? 44.90334  70.17142  18.98733  1.000 67.99953  ?  51  GLN A N   1 
ATOM   3301 C CA  . GLN C 3 46  ? 45.28110  69.99315  20.38007  1.000 78.83940  ?  51  GLN A CA  1 
ATOM   3302 C C   . GLN C 3 46  ? 44.55778  68.78817  20.96519  1.000 73.32004  ?  51  GLN A C   1 
ATOM   3303 O O   . GLN C 3 46  ? 43.43003  68.46883  20.57671  1.000 75.42439  ?  51  GLN A O   1 
ATOM   3304 C CB  . GLN C 3 46  ? 44.97712  71.24916  21.20633  1.000 77.55206  ?  51  GLN A CB  1 
ATOM   3305 C CG  . GLN C 3 46  ? 43.65130  71.91049  20.88123  1.000 78.09867  ?  51  GLN A CG  1 
ATOM   3306 C CD  . GLN C 3 46  ? 43.47656  73.23192  21.60220  1.000 93.85420  ?  51  GLN A CD  1 
ATOM   3307 O OE1 . GLN C 3 46  ? 43.94571  73.40454  22.72709  1.000 96.82039  ?  51  GLN A OE1 1 
ATOM   3308 N NE2 . GLN C 3 46  ? 42.80871  74.17741  20.95226  1.000 95.21233  ?  51  GLN A NE2 1 
ATOM   3309 N N   . LEU C 3 47  ? 45.22361  68.12072  21.90418  1.000 76.39386  ?  52  LEU A N   1 
ATOM   3310 C CA  . LEU C 3 47  ? 44.69173  66.89109  22.47486  1.000 66.35089  ?  52  LEU A CA  1 
ATOM   3311 C C   . LEU C 3 47  ? 43.48248  67.18164  23.35318  1.000 73.11971  ?  52  LEU A C   1 
ATOM   3312 O O   . LEU C 3 47  ? 43.54303  68.01991  24.25784  1.000 83.56611  ?  52  LEU A O   1 
ATOM   3313 C CB  . LEU C 3 47  ? 45.76845  66.17565  23.28834  1.000 72.85073  ?  52  LEU A CB  1 
ATOM   3314 C CG  . LEU C 3 47  ? 45.31758  64.89859  24.00064  1.000 68.08301  ?  52  LEU A CG  1 
ATOM   3315 C CD1 . LEU C 3 47  ? 44.92337  63.83191  22.99063  1.000 61.37419  ?  52  LEU A CD1 1 
ATOM   3316 C CD2 . LEU C 3 47  ? 46.40187  64.38580  24.93560  1.000 82.08525  ?  52  LEU A CD2 1 
ATOM   3317 N N   . LEU C 3 48  ? 42.37974  66.48304  23.08305  1.000 79.04690  ?  53  LEU A N   1 
ATOM   3318 C CA  . LEU C 3 48  ? 41.21109  66.56686  23.95129  1.000 78.22267  ?  53  LEU A CA  1 
ATOM   3319 C C   . LEU C 3 48  ? 41.36639  65.63451  25.14839  1.000 82.70179  ?  53  LEU A C   1 
ATOM   3320 O O   . LEU C 3 48  ? 41.35399  66.07757  26.30177  1.000 94.38719  ?  53  LEU A O   1 
ATOM   3321 C CB  . LEU C 3 48  ? 39.94389  66.23634  23.15729  1.000 78.47022  ?  53  LEU A CB  1 
ATOM   3322 C CG  . LEU C 3 48  ? 38.60129  66.58427  23.80034  1.000 80.01296  ?  53  LEU A CG  1 
ATOM   3323 C CD1 . LEU C 3 48  ? 38.52407  68.07198  24.10327  1.000 99.79285  ?  53  LEU A CD1 1 
ATOM   3324 C CD2 . LEU C 3 48  ? 37.45478  66.15885  22.89718  1.000 83.31230  ?  53  LEU A CD2 1 
ATOM   3325 N N   . PHE C 3 49  ? 41.52785  64.33900  24.88649  1.000 69.69996  ?  54  PHE A N   1 
ATOM   3326 C CA  . PHE C 3 49  ? 41.80349  63.35901  25.92845  1.000 78.83076  ?  54  PHE A CA  1 
ATOM   3327 C C   . PHE C 3 49  ? 42.33977  62.09593  25.27202  1.000 78.69986  ?  54  PHE A C   1 
ATOM   3328 O O   . PHE C 3 49  ? 42.21869  61.90584  24.05882  1.000 73.28578  ?  54  PHE A O   1 
ATOM   3329 C CB  . PHE C 3 49  ? 40.55741  63.04953  26.76806  1.000 90.19924  ?  54  PHE A CB  1 
ATOM   3330 C CG  . PHE C 3 49  ? 39.40306  62.51379  25.97056  1.000 92.12673  ?  54  PHE A CG  1 
ATOM   3331 C CD1 . PHE C 3 49  ? 38.49390  63.37524  25.38093  1.000 90.24165  ?  54  PHE A CD1 1 
ATOM   3332 C CD2 . PHE C 3 49  ? 39.22203  61.14950  25.81678  1.000 85.60964  ?  54  PHE A CD2 1 
ATOM   3333 C CE1 . PHE C 3 49  ? 37.43061  62.88860  24.64909  1.000 89.41367  ?  54  PHE A CE1 1 
ATOM   3334 C CE2 . PHE C 3 49  ? 38.16042  60.65733  25.08500  1.000 84.27711  ?  54  PHE A CE2 1 
ATOM   3335 C CZ  . PHE C 3 49  ? 37.26374  61.52912  24.50139  1.000 75.85000  ?  54  PHE A CZ  1 
ATOM   3336 N N   . LYS C 3 50  ? 42.93644  61.23344  26.09208  1.000 67.67276  ?  55  LYS A N   1 
ATOM   3337 C CA  . LYS C 3 50  ? 43.50457  59.97957  25.62192  1.000 63.07180  ?  55  LYS A CA  1 
ATOM   3338 C C   . LYS C 3 50  ? 43.02995  58.83472  26.50360  1.000 71.82124  ?  55  LYS A C   1 
ATOM   3339 O O   . LYS C 3 50  ? 42.73014  59.02075  27.68629  1.000 76.01348  ?  55  LYS A O   1 
ATOM   3340 C CB  . LYS C 3 50  ? 45.04011  60.02034  25.60851  1.000 71.32738  ?  55  LYS A CB  1 
ATOM   3341 C CG  . LYS C 3 50  ? 45.67933  60.15593  26.98053  1.000 76.64525  ?  55  LYS A CG  1 
ATOM   3342 C CD  . LYS C 3 50  ? 47.19537  60.08541  26.88870  1.000 67.86290  ?  55  LYS A CD  1 
ATOM   3343 C CE  . LYS C 3 50  ? 47.83801  60.17158  28.26346  1.000 88.60672  ?  55  LYS A CE  1 
ATOM   3344 N NZ  . LYS C 3 50  ? 49.31625  60.00604  28.19588  1.000 94.39739  ?  55  LYS A NZ  1 
ATOM   3345 N N   . VAL C 3 51  ? 42.95697  57.64724  25.91053  1.000 66.88856  ?  56  VAL A N   1 
ATOM   3346 C CA  . VAL C 3 51  ? 42.57702  56.43717  26.63470  1.000 67.29033  ?  56  VAL A CA  1 
ATOM   3347 C C   . VAL C 3 51  ? 43.63117  55.36777  26.37347  1.000 71.47167  ?  56  VAL A C   1 
ATOM   3348 O O   . VAL C 3 51  ? 43.62330  54.73751  25.30593  1.000 70.36797  ?  56  VAL A O   1 
ATOM   3349 C CB  . VAL C 3 51  ? 41.17711  55.95048  26.22747  1.000 67.81849  ?  56  VAL A CB  1 
ATOM   3350 C CG1 . VAL C 3 51  ? 40.79694  54.71796  27.02703  1.000 69.99964  ?  56  VAL A CG1 1 
ATOM   3351 C CG2 . VAL C 3 51  ? 40.14821  57.05095  26.42965  1.000 69.83904  ?  56  VAL A CG2 1 
ATOM   3352 N N   . PRO C 3 52  ? 44.56120  55.14043  27.30250  1.000 81.66761  ?  57  PRO A N   1 
ATOM   3353 C CA  . PRO C 3 52  ? 45.59499  54.11974  27.08067  1.000 79.00967  ?  57  PRO A CA  1 
ATOM   3354 C C   . PRO C 3 52  ? 45.09495  52.70539  27.33209  1.000 82.64727  ?  57  PRO A C   1 
ATOM   3355 O O   . PRO C 3 52  ? 45.42736  51.78069  26.58365  1.000 80.77013  ?  57  PRO A O   1 
ATOM   3356 C CB  . PRO C 3 52  ? 46.69391  54.50629  28.08290  1.000 82.99162  ?  57  PRO A CB  1 
ATOM   3357 C CG  . PRO C 3 52  ? 46.33590  55.89268  28.56541  1.000 85.39715  ?  57  PRO A CG  1 
ATOM   3358 C CD  . PRO C 3 52  ? 44.84896  55.96299  28.48619  1.000 84.39021  ?  57  PRO A CD  1 
ATOM   3359 N N   . LYS C 3 53  ? 44.30060  52.52473  28.38428  1.000 77.60206  ?  58  LYS A N   1 
ATOM   3360 C CA  . LYS C 3 53  ? 43.82307  51.20560  28.77679  1.000 81.49573  ?  58  LYS A CA  1 
ATOM   3361 C C   . LYS C 3 53  ? 42.52589  50.88037  28.04746  1.000 85.43533  ?  58  LYS A C   1 
ATOM   3362 O O   . LYS C 3 53  ? 41.60286  51.70033  28.01177  1.000 96.37715  ?  58  LYS A O   1 
ATOM   3363 C CB  . LYS C 3 53  ? 43.61120  51.13727  30.28949  1.000 80.56633  ?  58  LYS A CB  1 
ATOM   3364 C CG  . LYS C 3 53  ? 43.32100  49.73987  30.81235  1.000 96.08237  ?  58  LYS A CG  1 
ATOM   3365 C CD  . LYS C 3 53  ? 43.03873  49.75682  32.30577  1.000 115.06462 ?  58  LYS A CD  1 
ATOM   3366 C CE  . LYS C 3 53  ? 44.19221  50.37082  33.08198  1.000 123.66192 ?  58  LYS A CE  1 
ATOM   3367 N NZ  . LYS C 3 53  ? 43.89579  50.45284  34.53902  1.000 131.13204 ?  58  LYS A NZ  1 
ATOM   3368 N N   . ALA C 3 54  ? 42.45950  49.68180  27.47410  1.000 85.01128  ?  59  ALA A N   1 
ATOM   3369 C CA  . ALA C 3 54  ? 41.28017  49.26643  26.73284  1.000 73.34691  ?  59  ALA A CA  1 
ATOM   3370 C C   . ALA C 3 54  ? 40.09519  49.05831  27.67209  1.000 77.50184  ?  59  ALA A C   1 
ATOM   3371 O O   . ALA C 3 54  ? 40.25072  48.82262  28.87392  1.000 87.76075  ?  59  ALA A O   1 
ATOM   3372 C CB  . ALA C 3 54  ? 41.56210  47.98460  25.94931  1.000 76.47680  ?  59  ALA A CB  1 
ATOM   3373 N N   . ASN C 3 55  ? 38.89371  49.15700  27.09786  1.000 94.32058  ?  63  ASN A N   1 
ATOM   3374 C CA  . ASN C 3 55  ? 37.63379  48.98432  27.82525  1.000 85.17504  ?  63  ASN A CA  1 
ATOM   3375 C C   . ASN C 3 55  ? 37.46844  50.01560  28.93882  1.000 89.72296  ?  63  ASN A C   1 
ATOM   3376 O O   . ASN C 3 55  ? 36.78232  49.76744  29.93325  1.000 103.14338 ?  63  ASN A O   1 
ATOM   3377 C CB  . ASN C 3 55  ? 37.49944  47.56261  28.37868  1.000 87.29241  ?  63  ASN A CB  1 
ATOM   3378 C CG  . ASN C 3 55  ? 37.35974  46.52534  27.28213  1.000 100.96800 ?  63  ASN A CG  1 
ATOM   3379 O OD1 . ASN C 3 55  ? 36.73457  46.77729  26.25104  1.000 88.22033  ?  63  ASN A OD1 1 
ATOM   3380 N ND2 . ASN C 3 55  ? 37.94628  45.35282  27.49631  1.000 100.53243 ?  63  ASN A ND2 1 
ATOM   3381 N N   . GLU C 3 56  ? 38.08980  51.17811  28.77826  1.000 86.94774  ?  64  GLU A N   1 
ATOM   3382 C CA  . GLU C 3 56  ? 37.91878  52.31199  29.67580  1.000 83.27444  ?  64  GLU A CA  1 
ATOM   3383 C C   . GLU C 3 56  ? 37.45035  53.52294  28.87482  1.000 92.42013  ?  64  GLU A C   1 
ATOM   3384 O O   . GLU C 3 56  ? 37.35084  53.48497  27.64576  1.000 79.70291  ?  64  GLU A O   1 
ATOM   3385 C CB  . GLU C 3 56  ? 39.21364  52.62051  30.43364  1.000 79.69446  ?  64  GLU A CB  1 
ATOM   3386 C CG  . GLU C 3 56  ? 39.48149  51.69517  31.60947  1.000 101.59719 ?  64  GLU A CG  1 
ATOM   3387 C CD  . GLU C 3 56  ? 40.57872  52.21329  32.51980  1.000 131.63172 ?  64  GLU A CD  1 
ATOM   3388 O OE1 . GLU C 3 56  ? 41.19957  53.24261  32.17902  1.000 129.85270 ?  64  GLU A OE1 1 
ATOM   3389 O OE2 . GLU C 3 56  ? 40.81825  51.59320  33.57784  1.000 120.66747 -1 64  GLU A OE2 1 
ATOM   3390 N N   . LYS C 3 57  ? 37.15965  54.60866  29.58696  1.000 84.87532  ?  65  LYS A N   1 
ATOM   3391 C CA  . LYS C 3 57  ? 36.63084  55.81845  28.97688  1.000 82.11187  ?  65  LYS A CA  1 
ATOM   3392 C C   . LYS C 3 57  ? 37.42352  57.02831  29.44421  1.000 91.18583  ?  65  LYS A C   1 
ATOM   3393 O O   . LYS C 3 57  ? 37.81242  57.11728  30.61279  1.000 84.29478  ?  65  LYS A O   1 
ATOM   3394 C CB  . LYS C 3 57  ? 35.14695  56.00743  29.31385  1.000 85.41813  ?  65  LYS A CB  1 
ATOM   3395 C CG  . LYS C 3 57  ? 34.27493  54.82781  28.92604  1.000 96.98263  ?  65  LYS A CG  1 
ATOM   3396 C CD  . LYS C 3 57  ? 32.83054  55.04275  29.33608  1.000 123.60096 ?  65  LYS A CD  1 
ATOM   3397 C CE  . LYS C 3 57  ? 31.99754  53.80753  29.04501  1.000 132.20730 ?  65  LYS A CE  1 
ATOM   3398 N NZ  . LYS C 3 57  ? 32.48276  52.62075  29.80337  1.000 131.99912 ?  65  LYS A NZ  1 
ATOM   3399 N N   . GLY C 3 58  ? 37.66000  57.95452  28.52014  1.000 100.02408 ?  66  GLY A N   1 
ATOM   3400 C CA  . GLY C 3 58  ? 38.30108  59.21956  28.82179  1.000 98.36070  ?  66  GLY A CA  1 
ATOM   3401 C C   . GLY C 3 58  ? 37.30161  60.34989  28.67445  1.000 95.44784  ?  66  GLY A C   1 
ATOM   3402 O O   . GLY C 3 58  ? 36.38944  60.28417  27.84709  1.000 89.87111  ?  66  GLY A O   1 
ATOM   3403 N N   . SER C 3 59  ? 37.47304  61.38956  29.48531  1.000 109.02729 ?  67  SER A N   1 
ATOM   3404 C CA  . SER C 3 59  ? 36.54683  62.51047  29.51357  1.000 86.18423  ?  67  SER A CA  1 
ATOM   3405 C C   . SER C 3 59  ? 37.31352  63.82046  29.43427  1.000 88.41390  ?  67  SER A C   1 
ATOM   3406 O O   . SER C 3 59  ? 38.39121  63.95865  30.01958  1.000 89.46800  ?  67  SER A O   1 
ATOM   3407 C CB  . SER C 3 59  ? 35.68888  62.48636  30.78241  1.000 89.60009  ?  67  SER A CB  1 
ATOM   3408 O OG  . SER C 3 59  ? 36.49700  62.60401  31.93979  1.000 93.21304  ?  67  SER A OG  1 
ATOM   3409 N N   . SER C 3 60  ? 36.74951  64.77763  28.70378  1.000 95.71674  ?  68  SER A N   1 
ATOM   3410 C CA  . SER C 3 60  ? 37.31859  66.11688  28.60213  1.000 91.52360  ?  68  SER A CA  1 
ATOM   3411 C C   . SER C 3 60  ? 36.18061  67.08073  28.31807  1.000 87.86842  ?  68  SER A C   1 
ATOM   3412 O O   . SER C 3 60  ? 35.46347  66.90759  27.32772  1.000 84.14699  ?  68  SER A O   1 
ATOM   3413 C CB  . SER C 3 60  ? 38.37993  66.18986  27.50263  1.000 95.09168  ?  68  SER A CB  1 
ATOM   3414 O OG  . SER C 3 60  ? 38.96882  67.47698  27.44983  1.000 97.37272  ?  68  SER A OG  1 
ATOM   3415 N N   . ARG C 3 61  ? 36.01648  68.08311  29.18152  1.000 101.97168 ?  74  ARG A N   1 
ATOM   3416 C CA  . ARG C 3 61  ? 34.88630  69.01446  29.11792  1.000 97.13866  ?  74  ARG A CA  1 
ATOM   3417 C C   . ARG C 3 61  ? 33.61358  68.18600  29.19852  1.000 104.51152 ?  74  ARG A C   1 
ATOM   3418 O O   . ARG C 3 61  ? 33.41698  67.47679  30.19880  1.000 111.88739 ?  74  ARG A O   1 
ATOM   3419 C CB  . ARG C 3 61  ? 34.99782  69.88774  27.87084  1.000 92.22883  ?  74  ARG A CB  1 
ATOM   3420 C CG  . ARG C 3 61  ? 36.38092  70.45984  27.61768  1.000 89.66698  ?  74  ARG A CG  1 
ATOM   3421 C CD  . ARG C 3 61  ? 36.45685  71.16451  26.26301  1.000 96.00136  ?  74  ARG A CD  1 
ATOM   3422 N NE  . ARG C 3 61  ? 37.82871  71.50638  25.90505  1.000 122.07687 ?  74  ARG A NE  1 
ATOM   3423 C CZ  . ARG C 3 61  ? 38.19448  72.02651  24.74139  1.000 130.73650 ?  74  ARG A CZ  1 
ATOM   3424 N NH1 . ARG C 3 61  ? 37.31004  72.28971  23.79304  1.000 127.04292 ?  74  ARG A NH1 1 
ATOM   3425 N NH2 . ARG C 3 61  ? 39.48071  72.28555  24.52248  1.000 120.73796 ?  74  ARG A NH2 1 
ATOM   3426 N N   . GLY C 3 62  ? 32.74567  68.22120  28.19905  1.000 103.27897 ?  75  GLY A N   1 
ATOM   3427 C CA  . GLY C 3 62  ? 31.59235  67.35641  28.14629  1.000 109.85990 ?  75  GLY A CA  1 
ATOM   3428 C C   . GLY C 3 62  ? 31.72959  66.17841  27.20956  1.000 103.39694 ?  75  GLY A C   1 
ATOM   3429 O O   . GLY C 3 62  ? 30.74539  65.46063  26.99931  1.000 109.51935 ?  75  GLY A O   1 
ATOM   3430 N N   . PHE C 3 63  ? 32.91235  65.94911  26.64461  1.000 90.43691  ?  76  PHE A N   1 
ATOM   3431 C CA  . PHE C 3 63  ? 33.11790  64.89458  25.66074  1.000 93.15017  ?  76  PHE A CA  1 
ATOM   3432 C C   . PHE C 3 63  ? 33.52295  63.59124  26.33875  1.000 95.88734  ?  76  PHE A C   1 
ATOM   3433 O O   . PHE C 3 63  ? 34.28680  63.59076  27.30796  1.000 90.91099  ?  76  PHE A O   1 
ATOM   3434 C CB  . PHE C 3 63  ? 34.19002  65.30531  24.64739  1.000 82.87685  ?  76  PHE A CB  1 
ATOM   3435 C CG  . PHE C 3 63  ? 33.85915  66.55797  23.88621  1.000 88.59769  ?  76  PHE A CG  1 
ATOM   3436 C CD1 . PHE C 3 63  ? 34.20338  67.80642  24.38445  1.000 97.81726  ?  76  PHE A CD1 1 
ATOM   3437 C CD2 . PHE C 3 63  ? 33.20324  66.48595  22.67022  1.000 83.68652  ?  76  PHE A CD2 1 
ATOM   3438 C CE1 . PHE C 3 63  ? 33.89409  68.95755  23.68159  1.000 94.69548  ?  76  PHE A CE1 1 
ATOM   3439 C CE2 . PHE C 3 63  ? 32.89311  67.62951  21.96484  1.000 83.08885  ?  76  PHE A CE2 1 
ATOM   3440 C CZ  . PHE C 3 63  ? 33.23824  68.86679  22.46971  1.000 89.31383  ?  76  PHE A CZ  1 
ATOM   3441 N N   . GLU C 3 64  ? 33.00480  62.47873  25.81971  1.000 94.83679  ?  77  GLU A N   1 
ATOM   3442 C CA  . GLU C 3 64  ? 33.34304  61.15251  26.31551  1.000 94.45848  ?  77  GLU A CA  1 
ATOM   3443 C C   . GLU C 3 64  ? 33.55226  60.21853  25.13379  1.000 87.15834  ?  77  GLU A C   1 
ATOM   3444 O O   . GLU C 3 64  ? 32.91796  60.36762  24.08641  1.000 86.92742  ?  77  GLU A O   1 
ATOM   3445 C CB  . GLU C 3 64  ? 32.25254  60.58264  27.23728  1.000 93.89022  ?  77  GLU A CB  1 
ATOM   3446 C CG  . GLU C 3 64  ? 32.02491  61.37512  28.51356  1.000 108.14854 ?  77  GLU A CG  1 
ATOM   3447 C CD  . GLU C 3 64  ? 31.00550  60.72342  29.42636  1.000 120.34743 ?  77  GLU A CD  1 
ATOM   3448 O OE1 . GLU C 3 64  ? 30.66322  59.54508  29.19067  1.000 107.82771 ?  77  GLU A OE1 1 
ATOM   3449 O OE2 . GLU C 3 64  ? 30.54625  61.38942  30.37807  1.000 120.88070 -1 77  GLU A OE2 1 
ATOM   3450 N N   . ALA C 3 65  ? 34.45595  59.25757  25.30988  1.000 80.30066  ?  78  ALA A N   1 
ATOM   3451 C CA  . ALA C 3 65  ? 34.69695  58.23122  24.30700  1.000 78.91410  ?  78  ALA A CA  1 
ATOM   3452 C C   . ALA C 3 65  ? 35.11148  56.95270  25.01519  1.000 87.58253  ?  78  ALA A C   1 
ATOM   3453 O O   . ALA C 3 65  ? 35.83257  56.99571  26.01535  1.000 85.87927  ?  78  ALA A O   1 
ATOM   3454 C CB  . ALA C 3 65  ? 35.77057  58.65414  23.29903  1.000 75.46429  ?  78  ALA A CB  1 
ATOM   3455 N N   . THR C 3 66  ? 34.65366  55.82113  24.49011  1.000 101.34072 ?  79  THR A N   1 
ATOM   3456 C CA  . THR C 3 66  ? 34.87165  54.51933  25.10573  1.000 81.49190  ?  79  THR A CA  1 
ATOM   3457 C C   . THR C 3 66  ? 35.81489  53.69873  24.23752  1.000 83.78019  ?  79  THR A C   1 
ATOM   3458 O O   . THR C 3 66  ? 35.54718  53.48734  23.04952  1.000 81.75271  ?  79  THR A O   1 
ATOM   3459 C CB  . THR C 3 66  ? 33.54907  53.77917  25.29909  1.000 85.71593  ?  79  THR A CB  1 
ATOM   3460 O OG1 . THR C 3 66  ? 32.63606  54.61410  26.02127  1.000 124.13014 ?  79  THR A OG1 1 
ATOM   3461 C CG2 . THR C 3 66  ? 33.77148  52.48911  26.07399  1.000 91.28864  ?  79  THR A CG2 1 
ATOM   3462 N N   . TYR C 3 67  ? 36.91449  53.24152  24.83408  1.000 82.68242  ?  80  TYR A N   1 
ATOM   3463 C CA  . TYR C 3 67  ? 37.82761  52.31242  24.18162  1.000 75.54920  ?  80  TYR A CA  1 
ATOM   3464 C C   . TYR C 3 67  ? 37.17047  50.93953  24.10823  1.000 78.63114  ?  80  TYR A C   1 
ATOM   3465 O O   . TYR C 3 67  ? 37.54253  50.02709  24.85168  1.000 82.59082  ?  80  TYR A O   1 
ATOM   3466 C CB  . TYR C 3 67  ? 39.15364  52.25702  24.94951  1.000 85.56530  ?  80  TYR A CB  1 
ATOM   3467 C CG  . TYR C 3 67  ? 40.32963  51.60823  24.23751  1.000 84.86457  ?  80  TYR A CG  1 
ATOM   3468 C CD1 . TYR C 3 67  ? 40.14918  50.59012  23.30786  1.000 81.85346  ?  80  TYR A CD1 1 
ATOM   3469 C CD2 . TYR C 3 67  ? 41.62917  52.01327  24.51393  1.000 72.25256  ?  80  TYR A CD2 1 
ATOM   3470 C CE1 . TYR C 3 67  ? 41.22440  50.00127  22.67374  1.000 75.71307  ?  80  TYR A CE1 1 
ATOM   3471 C CE2 . TYR C 3 67  ? 42.70956  51.43028  23.88443  1.000 71.06379  ?  80  TYR A CE2 1 
ATOM   3472 C CZ  . TYR C 3 67  ? 42.50157  50.42598  22.96567  1.000 73.08680  ?  80  TYR A CZ  1 
ATOM   3473 O OH  . TYR C 3 67  ? 43.57650  49.84423  22.33828  1.000 70.32029  ?  80  TYR A OH  1 
ATOM   3474 N N   . ASN C 3 68  ? 36.19242  50.78282  23.22078  1.000 80.56787  ?  81  ASN A N   1 
ATOM   3475 C CA  . ASN C 3 68  ? 35.46259  49.52397  23.09227  1.000 84.16570  ?  81  ASN A CA  1 
ATOM   3476 C C   . ASN C 3 68  ? 36.30094  48.56207  22.26136  1.000 82.98464  ?  81  ASN A C   1 
ATOM   3477 O O   . ASN C 3 68  ? 36.31501  48.63341  21.03099  1.000 82.90731  ?  81  ASN A O   1 
ATOM   3478 C CB  . ASN C 3 68  ? 34.09499  49.75850  22.46291  1.000 90.19819  ?  81  ASN A CB  1 
ATOM   3479 C CG  . ASN C 3 68  ? 33.23723  48.51117  22.45530  1.000 91.45702  ?  81  ASN A CG  1 
ATOM   3480 O OD1 . ASN C 3 68  ? 33.29963  47.70666  21.52611  1.000 105.67666 ?  81  ASN A OD1 1 
ATOM   3481 N ND2 . ASN C 3 68  ? 32.42930  48.34294  23.49560  1.000 95.27671  ?  81  ASN A ND2 1 
ATOM   3482 N N   . LYS C 3 69  ? 37.00613  47.65266  22.93916  1.000 84.48159  ?  82  LYS A N   1 
ATOM   3483 C CA  . LYS C 3 69  ? 37.86389  46.70370  22.23696  1.000 82.19142  ?  82  LYS A CA  1 
ATOM   3484 C C   . LYS C 3 69  ? 37.05155  45.66233  21.47673  1.000 92.66800  ?  82  LYS A C   1 
ATOM   3485 O O   . LYS C 3 69  ? 37.52294  45.13035  20.46470  1.000 85.50153  ?  82  LYS A O   1 
ATOM   3486 C CB  . LYS C 3 69  ? 38.81014  46.02315  23.22828  1.000 81.58528  ?  82  LYS A CB  1 
ATOM   3487 C CG  . LYS C 3 69  ? 39.80604  45.06284  22.59310  1.000 88.80988  ?  82  LYS A CG  1 
ATOM   3488 C CD  . LYS C 3 69  ? 40.66143  44.37240  23.64268  1.000 80.32811  ?  82  LYS A CD  1 
ATOM   3489 C CE  . LYS C 3 69  ? 41.62768  43.38677  23.00458  1.000 101.44366 ?  82  LYS A CE  1 
ATOM   3490 N NZ  . LYS C 3 69  ? 42.51323  42.74117  24.01343  1.000 115.50661 ?  82  LYS A NZ  1 
ATOM   3491 N N   . GLU C 3 70  ? 35.83560  45.36390  21.94011  1.000 101.63673 ?  83  GLU A N   1 
ATOM   3492 C CA  . GLU C 3 70  ? 35.01183  44.35177  21.28566  1.000 101.64572 ?  83  GLU A CA  1 
ATOM   3493 C C   . GLU C 3 70  ? 34.69575  44.74539  19.84719  1.000 104.86806 ?  83  GLU A C   1 
ATOM   3494 O O   . GLU C 3 70  ? 35.02960  44.02247  18.90165  1.000 127.45610 ?  83  GLU A O   1 
ATOM   3495 C CB  . GLU C 3 70  ? 33.72370  44.12992  22.08095  1.000 114.95045 ?  83  GLU A CB  1 
ATOM   3496 C CG  . GLU C 3 70  ? 33.93301  43.51456  23.45453  1.000 120.97067 ?  83  GLU A CG  1 
ATOM   3497 C CD  . GLU C 3 70  ? 32.62507  43.22785  24.16723  1.000 143.76737 ?  83  GLU A CD  1 
ATOM   3498 O OE1 . GLU C 3 70  ? 31.56576  43.65903  23.66480  1.000 139.72772 ?  83  GLU A OE1 1 
ATOM   3499 O OE2 . GLU C 3 70  ? 32.65523  42.56890  25.22788  1.000 147.72602 -1 83  GLU A OE2 1 
ATOM   3500 N N   . ALA C 3 71  ? 34.05154  45.89417  19.66299  1.000 96.53340  ?  84  ALA A N   1 
ATOM   3501 C CA  . ALA C 3 71  ? 33.67669  46.36846  18.33831  1.000 105.91748 ?  84  ALA A CA  1 
ATOM   3502 C C   . ALA C 3 71  ? 34.74100  47.24736  17.69580  1.000 106.67766 ?  84  ALA A C   1 
ATOM   3503 O O   . ALA C 3 71  ? 34.52193  47.74092  16.58413  1.000 113.53974 ?  84  ALA A O   1 
ATOM   3504 C CB  . ALA C 3 71  ? 32.35241  47.13578  18.40805  1.000 99.31513  ?  84  ALA A CB  1 
ATOM   3505 N N   . THR C 3 72  ? 35.88112  47.44068  18.35791  1.000 108.00005 ?  85  THR A N   1 
ATOM   3506 C CA  . THR C 3 72  ? 36.95160  48.32183  17.88952  1.000 104.37058 ?  85  THR A CA  1 
ATOM   3507 C C   . THR C 3 72  ? 36.39784  49.69690  17.51444  1.000 86.51817  ?  85  THR A C   1 
ATOM   3508 O O   . THR C 3 72  ? 36.47432  50.14402  16.36898  1.000 87.16613  ?  85  THR A O   1 
ATOM   3509 C CB  . THR C 3 72  ? 37.71702  47.69818  16.71739  1.000 79.75601  ?  85  THR A CB  1 
ATOM   3510 O OG1 . THR C 3 72  ? 36.84998  47.57127  15.58337  1.000 98.04943  ?  85  THR A OG1 1 
ATOM   3511 C CG2 . THR C 3 72  ? 38.25341  46.32793  17.09919  1.000 80.96398  ?  85  THR A CG2 1 
ATOM   3512 N N   . SER C 3 73  ? 35.82706  50.36496  18.51346  1.000 79.97675  ?  86  SER A N   1 
ATOM   3513 C CA  . SER C 3 73  ? 35.21261  51.66834  18.32371  1.000 85.69233  ?  86  SER A CA  1 
ATOM   3514 C C   . SER C 3 73  ? 35.73949  52.64552  19.36459  1.000 77.37282  ?  86  SER A C   1 
ATOM   3515 O O   . SER C 3 73  ? 36.28256  52.25478  20.40096  1.000 87.53542  ?  86  SER A O   1 
ATOM   3516 C CB  . SER C 3 73  ? 33.68198  51.58989  18.40862  1.000 83.53364  ?  86  SER A CB  1 
ATOM   3517 O OG  . SER C 3 73  ? 33.25953  51.26981  19.72184  1.000 94.10320  ?  86  SER A OG  1 
ATOM   3518 N N   . PHE C 3 74  ? 35.56824  53.92922  19.07013  1.000 78.27252  ?  87  PHE A N   1 
ATOM   3519 C CA  . PHE C 3 74  ? 35.98250  55.01319  19.95006  1.000 74.71926  ?  87  PHE A CA  1 
ATOM   3520 C C   . PHE C 3 74  ? 35.07203  56.21026  19.67877  1.000 75.78731  ?  87  PHE A C   1 
ATOM   3521 O O   . PHE C 3 74  ? 35.50704  57.29761  19.30565  1.000 74.06003  ?  87  PHE A O   1 
ATOM   3522 C CB  . PHE C 3 74  ? 37.45881  55.34088  19.73841  1.000 71.16722  ?  87  PHE A CB  1 
ATOM   3523 C CG  . PHE C 3 74  ? 38.09401  56.06233  20.89222  1.000 69.87263  ?  87  PHE A CG  1 
ATOM   3524 C CD1 . PHE C 3 74  ? 37.92810  55.60366  22.18852  1.000 71.20498  ?  87  PHE A CD1 1 
ATOM   3525 C CD2 . PHE C 3 74  ? 38.87378  57.18605  20.67975  1.000 67.71720  ?  87  PHE A CD2 1 
ATOM   3526 C CE1 . PHE C 3 74  ? 38.51667  56.26018  23.25196  1.000 70.38010  ?  87  PHE A CE1 1 
ATOM   3527 C CE2 . PHE C 3 74  ? 39.46706  57.84436  21.74006  1.000 66.94617  ?  87  PHE A CE2 1 
ATOM   3528 C CZ  . PHE C 3 74  ? 39.28664  57.38197  23.02652  1.000 68.25607  ?  87  PHE A CZ  1 
ATOM   3529 N N   . HIS C 3 75  ? 33.77126  56.00312  19.87013  1.000 82.11604  ?  88  HIS A N   1 
ATOM   3530 C CA  . HIS C 3 75  ? 32.77923  57.00661  19.50895  1.000 83.07388  ?  88  HIS A CA  1 
ATOM   3531 C C   . HIS C 3 75  ? 32.81943  58.18198  20.47743  1.000 86.28327  ?  88  HIS A C   1 
ATOM   3532 O O   . HIS C 3 75  ? 32.80430  57.99749  21.69814  1.000 84.33575  ?  88  HIS A O   1 
ATOM   3533 C CB  . HIS C 3 75  ? 31.38568  56.38143  19.49418  1.000 84.26820  ?  88  HIS A CB  1 
ATOM   3534 C CG  . HIS C 3 75  ? 31.26465  55.19946  18.58393  1.000 85.29984  ?  88  HIS A CG  1 
ATOM   3535 N ND1 . HIS C 3 75  ? 31.97907  55.08758  17.41098  1.000 83.35525  ?  88  HIS A ND1 1 
ATOM   3536 C CD2 . HIS C 3 75  ? 30.51848  54.07359  18.67824  1.000 88.49798  ?  88  HIS A CD2 1 
ATOM   3537 C CE1 . HIS C 3 75  ? 31.67380  53.94712  16.81846  1.000 85.30316  ?  88  HIS A CE1 1 
ATOM   3538 N NE2 . HIS C 3 75  ? 30.79065  53.31219  17.56763  1.000 88.46237  ?  88  HIS A NE2 1 
ATOM   3539 N N   . LEU C 3 76  ? 32.86574  59.39271  19.92715  1.000 79.28525  ?  89  LEU A N   1 
ATOM   3540 C CA  . LEU C 3 76  ? 32.85685  60.61277  20.72202  1.000 83.18725  ?  89  LEU A CA  1 
ATOM   3541 C C   . LEU C 3 76  ? 31.41877  61.04936  20.96582  1.000 85.21105  ?  89  LEU A C   1 
ATOM   3542 O O   . LEU C 3 76  ? 30.61303  61.09859  20.03129  1.000 92.15793  ?  89  LEU A O   1 
ATOM   3543 C CB  . LEU C 3 76  ? 33.63292  61.72294  20.01337  1.000 82.49020  ?  89  LEU A CB  1 
ATOM   3544 C CG  . LEU C 3 76  ? 33.82493  63.03378  20.77630  1.000 81.71928  ?  89  LEU A CG  1 
ATOM   3545 C CD1 . LEU C 3 76  ? 34.70896  62.81779  21.99403  1.000 79.72012  ?  89  LEU A CD1 1 
ATOM   3546 C CD2 . LEU C 3 76  ? 34.40898  64.10195  19.86507  1.000 89.36401  ?  89  LEU A CD2 1 
ATOM   3547 N N   . GLN C 3 77  ? 31.09982  61.36541  22.21917  1.000 88.04311  ?  90  GLN A N   1 
ATOM   3548 C CA  . GLN C 3 77  ? 29.75000  61.76352  22.58899  1.000 87.97724  ?  90  GLN A CA  1 
ATOM   3549 C C   . GLN C 3 77  ? 29.79708  62.89906  23.59896  1.000 107.02856 ?  90  GLN A C   1 
ATOM   3550 O O   . GLN C 3 77  ? 30.63228  62.90067  24.50768  1.000 106.07496 ?  90  GLN A O   1 
ATOM   3551 C CB  . GLN C 3 77  ? 28.95534  60.58660  23.17102  1.000 92.50704  ?  90  GLN A CB  1 
ATOM   3552 C CG  . GLN C 3 77  ? 28.54816  59.53932  22.14818  1.000 96.54064  ?  90  GLN A CG  1 
ATOM   3553 C CD  . GLN C 3 77  ? 27.63653  58.47945  22.73403  1.000 114.03328 ?  90  GLN A CD  1 
ATOM   3554 O OE1 . GLN C 3 77  ? 27.49812  58.36715  23.95222  1.000 106.38974 ?  90  GLN A OE1 1 
ATOM   3555 N NE2 . GLN C 3 77  ? 27.00394  57.69821  21.86654  1.000 115.32989 ?  90  GLN A NE2 1 
ATOM   3556 N N   . LYS C 3 78  ? 28.89285  63.86224  23.43063  1.000 105.12691 ?  91  LYS A N   1 
ATOM   3557 C CA  . LYS C 3 78  ? 28.71365  64.95771  24.37163  1.000 108.02346 ?  91  LYS A CA  1 
ATOM   3558 C C   . LYS C 3 78  ? 27.22607  65.15509  24.61992  1.000 117.63983 ?  91  LYS A C   1 
ATOM   3559 O O   . LYS C 3 78  ? 26.41888  65.08392  23.68863  1.000 112.96813 ?  91  LYS A O   1 
ATOM   3560 C CB  . LYS C 3 78  ? 29.34209  66.25959  23.85512  1.000 92.53237  ?  91  LYS A CB  1 
ATOM   3561 C CG  . LYS C 3 78  ? 29.28570  67.40471  24.85503  1.000 99.61283  ?  91  LYS A CG  1 
ATOM   3562 C CD  . LYS C 3 78  ? 30.08208  68.60887  24.38363  1.000 92.16575  ?  91  LYS A CD  1 
ATOM   3563 C CE  . LYS C 3 78  ? 30.11264  69.69101  25.45216  1.000 110.14989 ?  91  LYS A CE  1 
ATOM   3564 N NZ  . LYS C 3 78  ? 30.86390  70.89840  25.01230  1.000 134.70067 ?  91  LYS A NZ  1 
ATOM   3565 N N   . ALA C 3 79  ? 26.86833  65.39909  25.88177  1.000 108.34814 ?  92  ALA A N   1 
ATOM   3566 C CA  . ALA C 3 79  ? 25.46076  65.52598  26.24620  1.000 128.50799 ?  92  ALA A CA  1 
ATOM   3567 C C   . ALA C 3 79  ? 24.84845  66.79008  25.65334  1.000 133.00388 ?  92  ALA A C   1 
ATOM   3568 O O   . ALA C 3 79  ? 23.89581  66.72550  24.86762  1.000 124.95390 ?  92  ALA A O   1 
ATOM   3569 C CB  . ALA C 3 79  ? 25.31201  65.51178  27.76875  1.000 140.41333 ?  92  ALA A CB  1 
ATOM   3570 N N   . SER C 3 80  ? 25.38264  67.95300  26.02041  1.000 125.67329 ?  93  SER A N   1 
ATOM   3571 C CA  . SER C 3 80  ? 24.87243  69.24157  25.56149  1.000 118.85098 ?  93  SER A CA  1 
ATOM   3572 C C   . SER C 3 80  ? 25.97771  69.95521  24.79447  1.000 126.74946 ?  93  SER A C   1 
ATOM   3573 O O   . SER C 3 80  ? 26.94835  70.43033  25.39390  1.000 131.85056 ?  93  SER A O   1 
ATOM   3574 C CB  . SER C 3 80  ? 24.38570  70.08785  26.73721  1.000 136.36449 ?  93  SER A CB  1 
ATOM   3575 O OG  . SER C 3 80  ? 23.37883  69.41208  27.47043  1.000 151.97929 ?  93  SER A OG  1 
ATOM   3576 N N   . VAL C 3 81  ? 25.82873  70.03237  23.47253  1.000 118.28602 ?  94  VAL A N   1 
ATOM   3577 C CA  . VAL C 3 81  ? 26.82033  70.70528  22.64382  1.000 112.29303 ?  94  VAL A CA  1 
ATOM   3578 C C   . VAL C 3 81  ? 26.68957  72.21700  22.80197  1.000 111.89839 ?  94  VAL A C   1 
ATOM   3579 O O   . VAL C 3 81  ? 25.70245  72.73616  23.32955  1.000 133.90135 ?  94  VAL A O   1 
ATOM   3580 C CB  . VAL C 3 81  ? 26.68671  70.28473  21.16970  1.000 98.27444  ?  94  VAL A CB  1 
ATOM   3581 C CG1 . VAL C 3 81  ? 26.87410  68.78504  21.03022  1.000 109.25577 ?  94  VAL A CG1 1 
ATOM   3582 C CG2 . VAL C 3 81  ? 25.33665  70.71176  20.61771  1.000 117.98198 ?  94  VAL A CG2 1 
ATOM   3583 N N   . GLN C 3 82  ? 27.70809  72.93214  22.33020  1.000 99.51961  ?  95  GLN A N   1 
ATOM   3584 C CA  . GLN C 3 82  ? 27.75418  74.38150  22.44178  1.000 112.73572 ?  95  GLN A CA  1 
ATOM   3585 C C   . GLN C 3 82  ? 28.35832  74.95813  21.16966  1.000 111.77251 ?  95  GLN A C   1 
ATOM   3586 O O   . GLN C 3 82  ? 29.05462  74.26669  20.42172  1.000 105.41792 ?  95  GLN A O   1 
ATOM   3587 C CB  . GLN C 3 82  ? 28.56204  74.82057  23.67178  1.000 119.73105 ?  95  GLN A CB  1 
ATOM   3588 C CG  . GLN C 3 82  ? 27.97233  76.00352  24.42173  1.000 133.89526 ?  95  GLN A CG  1 
ATOM   3589 C CD  . GLN C 3 82  ? 28.62563  76.21797  25.77471  1.000 143.60185 ?  95  GLN A CD  1 
ATOM   3590 O OE1 . GLN C 3 82  ? 29.59333  75.54086  26.12527  1.000 126.41187 ?  95  GLN A OE1 1 
ATOM   3591 N NE2 . GLN C 3 82  ? 28.09486  77.16115  26.54485  1.000 122.75123 ?  95  GLN A NE2 1 
ATOM   3592 N N   . GLU C 3 83  ? 28.07467  76.24168  20.92656  1.000 102.78234 ?  96  GLU A N   1 
ATOM   3593 C CA  . GLU C 3 83  ? 28.62740  76.90804  19.75038  1.000 106.81830 ?  96  GLU A CA  1 
ATOM   3594 C C   . GLU C 3 83  ? 30.14811  76.92289  19.78813  1.000 110.17927 ?  96  GLU A C   1 
ATOM   3595 O O   . GLU C 3 83  ? 30.80485  76.75294  18.75397  1.000 118.46797 ?  96  GLU A O   1 
ATOM   3596 C CB  . GLU C 3 83  ? 28.09758  78.33639  19.64586  1.000 105.77933 ?  96  GLU A CB  1 
ATOM   3597 C CG  . GLU C 3 83  ? 26.79013  78.48152  18.89811  1.000 119.39113 ?  96  GLU A CG  1 
ATOM   3598 C CD  . GLU C 3 83  ? 26.44898  79.93439  18.63842  1.000 140.75699 ?  96  GLU A CD  1 
ATOM   3599 O OE1 . GLU C 3 83  ? 26.96771  80.50443  17.65497  1.000 140.73103 ?  96  GLU A OE1 1 
ATOM   3600 O OE2 . GLU C 3 83  ? 25.68249  80.51480  19.43445  1.000 119.28295 ?  96  GLU A OE2 1 
ATOM   3601 N N   . SER C 3 84  ? 30.72597  77.12536  20.97400  1.000 104.22545 ?  97  SER A N   1 
ATOM   3602 C CA  . SER C 3 84  ? 32.17540  77.18721  21.11246  1.000 105.50432 ?  97  SER A CA  1 
ATOM   3603 C C   . SER C 3 84  ? 32.86193  75.87665  20.75448  1.000 101.41297 ?  97  SER A C   1 
ATOM   3604 O O   . SER C 3 84  ? 34.09173  75.85684  20.63787  1.000 115.85500 ?  97  SER A O   1 
ATOM   3605 C CB  . SER C 3 84  ? 32.54822  77.58841  22.54113  1.000 102.47989 ?  97  SER A CB  1 
ATOM   3606 O OG  . SER C 3 84  ? 32.04669  76.65447  23.48161  1.000 112.86501 ?  97  SER A OG  1 
ATOM   3607 N N   . ASP C 3 85  ? 32.11157  74.79070  20.58400  1.000 94.53213  ?  98  ASP A N   1 
ATOM   3608 C CA  . ASP C 3 85  ? 32.67167  73.50576  20.19229  1.000 103.80885 ?  98  ASP A CA  1 
ATOM   3609 C C   . ASP C 3 85  ? 32.63806  73.28447  18.68491  1.000 94.40862  ?  98  ASP A C   1 
ATOM   3610 O O   . ASP C 3 85  ? 32.87590  72.16080  18.23018  1.000 91.37912  ?  98  ASP A O   1 
ATOM   3611 C CB  . ASP C 3 85  ? 31.92999  72.37028  20.90255  1.000 96.93964  ?  98  ASP A CB  1 
ATOM   3612 C CG  . ASP C 3 85  ? 31.97793  72.49906  22.41238  1.000 105.30194 ?  98  ASP A CG  1 
ATOM   3613 O OD1 . ASP C 3 85  ? 33.00367  72.98163  22.93642  1.000 118.52962 ?  98  ASP A OD1 1 
ATOM   3614 O OD2 . ASP C 3 85  ? 30.98864  72.12189  23.07510  1.000 107.16636 -1 98  ASP A OD2 1 
ATOM   3615 N N   . SER C 3 86  ? 32.34805  74.32267  17.90499  1.000 90.09127  ?  99  SER A N   1 
ATOM   3616 C CA  . SER C 3 86  ? 32.32083  74.21407  16.44819  1.000 89.34944  ?  99  SER A CA  1 
ATOM   3617 C C   . SER C 3 86  ? 33.75190  74.14294  15.93407  1.000 94.58828  ?  99  SER A C   1 
ATOM   3618 O O   . SER C 3 86  ? 34.44454  75.15849  15.83892  1.000 89.49835  ?  99  SER A O   1 
ATOM   3619 C CB  . SER C 3 86  ? 31.57315  75.39395  15.83878  1.000 92.37891  ?  99  SER A CB  1 
ATOM   3620 O OG  . SER C 3 86  ? 30.22114  75.41114  16.26130  1.000 106.94978 ?  99  SER A OG  1 
ATOM   3621 N N   . ALA C 3 87  ? 34.19943  72.93843  15.59815  1.000 86.05335  ?  100 ALA A N   1 
ATOM   3622 C CA  . ALA C 3 87  ? 35.56039  72.71643  15.12866  1.000 82.07220  ?  100 ALA A CA  1 
ATOM   3623 C C   . ALA C 3 87  ? 35.59503  71.38971  14.37823  1.000 79.96406  ?  100 ALA A C   1 
ATOM   3624 O O   . ALA C 3 87  ? 34.55473  70.77333  14.12393  1.000 91.66801  ?  100 ALA A O   1 
ATOM   3625 C CB  . ALA C 3 87  ? 36.55057  72.74370  16.29765  1.000 82.56864  ?  100 ALA A CB  1 
ATOM   3626 N N   . VAL C 3 88  ? 36.79812  70.95045  14.01880  1.000 77.77368  ?  101 VAL A N   1 
ATOM   3627 C CA  . VAL C 3 88  ? 37.01718  69.66539  13.36595  1.000 75.87141  ?  101 VAL A CA  1 
ATOM   3628 C C   . VAL C 3 88  ? 37.61827  68.71522  14.39059  1.000 73.70984  ?  101 VAL A C   1 
ATOM   3629 O O   . VAL C 3 88  ? 38.57267  69.07220  15.09203  1.000 72.81213  ?  101 VAL A O   1 
ATOM   3630 C CB  . VAL C 3 88  ? 37.93089  69.80239  12.13583  1.000 75.29062  ?  101 VAL A CB  1 
ATOM   3631 C CG1 . VAL C 3 88  ? 38.05758  68.46781  11.41680  1.000 73.85674  ?  101 VAL A CG1 1 
ATOM   3632 C CG2 . VAL C 3 88  ? 37.39797  70.87225  11.19612  1.000 77.83643  ?  101 VAL A CG2 1 
ATOM   3633 N N   . TYR C 3 89  ? 37.06008  67.51218  14.48006  1.000 73.18815  ?  102 TYR A N   1 
ATOM   3634 C CA  . TYR C 3 89  ? 37.48348  66.51463  15.45314  1.000 76.69496  ?  102 TYR A CA  1 
ATOM   3635 C C   . TYR C 3 89  ? 38.13401  65.34198  14.73224  1.000 73.72255  ?  102 TYR A C   1 
ATOM   3636 O O   . TYR C 3 89  ? 37.60195  64.84890  13.73175  1.000 70.88577  ?  102 TYR A O   1 
ATOM   3637 C CB  . TYR C 3 89  ? 36.29698  66.04285  16.29665  1.000 78.63880  ?  102 TYR A CB  1 
ATOM   3638 C CG  . TYR C 3 89  ? 35.68218  67.14537  17.13098  1.000 75.06892  ?  102 TYR A CG  1 
ATOM   3639 C CD1 . TYR C 3 89  ? 34.69044  67.96769  16.61080  1.000 79.99432  ?  102 TYR A CD1 1 
ATOM   3640 C CD2 . TYR C 3 89  ? 36.10102  67.37036  18.43579  1.000 79.05662  ?  102 TYR A CD2 1 
ATOM   3641 C CE1 . TYR C 3 89  ? 34.12967  68.97983  17.36910  1.000 79.46477  ?  102 TYR A CE1 1 
ATOM   3642 C CE2 . TYR C 3 89  ? 35.54623  68.37929  19.20142  1.000 85.56157  ?  102 TYR A CE2 1 
ATOM   3643 C CZ  . TYR C 3 89  ? 34.56146  69.18063  18.66330  1.000 79.49558  ?  102 TYR A CZ  1 
ATOM   3644 O OH  . TYR C 3 89  ? 34.00771  70.18551  19.42261  1.000 82.02120  ?  102 TYR A OH  1 
ATOM   3645 N N   . TYR C 3 90  ? 39.28227  64.90194  15.24186  1.000 68.10204  ?  103 TYR A N   1 
ATOM   3646 C CA  . TYR C 3 90  ? 40.08001  63.85607  14.61667  1.000 67.12599  ?  103 TYR A CA  1 
ATOM   3647 C C   . TYR C 3 90  ? 40.20526  62.66549  15.55521  1.000 77.77372  ?  103 TYR A C   1 
ATOM   3648 O O   . TYR C 3 90  ? 40.60058  62.82231  16.71536  1.000 74.04795  ?  103 TYR A O   1 
ATOM   3649 C CB  . TYR C 3 90  ? 41.47584  64.36961  14.25081  1.000 73.11520  ?  103 TYR A CB  1 
ATOM   3650 C CG  . TYR C 3 90  ? 41.49837  65.41314  13.15834  1.000 65.66515  ?  103 TYR A CG  1 
ATOM   3651 C CD1 . TYR C 3 90  ? 41.39825  66.76483  13.45937  1.000 69.01338  ?  103 TYR A CD1 1 
ATOM   3652 C CD2 . TYR C 3 90  ? 41.63448  65.04674  11.82588  1.000 74.11512  ?  103 TYR A CD2 1 
ATOM   3653 C CE1 . TYR C 3 90  ? 41.42492  67.72222  12.46255  1.000 78.07300  ?  103 TYR A CE1 1 
ATOM   3654 C CE2 . TYR C 3 90  ? 41.66255  65.99634  10.82257  1.000 67.87408  ?  103 TYR A CE2 1 
ATOM   3655 C CZ  . TYR C 3 90  ? 41.55701  67.33187  11.14627  1.000 68.95551  ?  103 TYR A CZ  1 
ATOM   3656 O OH  . TYR C 3 90  ? 41.58399  68.27966  10.14973  1.000 84.69009  ?  103 TYR A OH  1 
ATOM   3657 N N   . CYS C 3 91  ? 39.87623  61.48070  15.04835  1.000 65.83246  ?  104 CYS A N   1 
ATOM   3658 C CA  . CYS C 3 91  ? 40.12785  60.23399  15.75650  1.000 64.36114  ?  104 CYS A CA  1 
ATOM   3659 C C   . CYS C 3 91  ? 41.54129  59.76722  15.42890  1.000 69.67916  ?  104 CYS A C   1 
ATOM   3660 O O   . CYS C 3 91  ? 41.94226  59.76259  14.26042  1.000 61.86268  ?  104 CYS A O   1 
ATOM   3661 C CB  . CYS C 3 91  ? 39.10133  59.17231  15.35764  1.000 66.16892  ?  104 CYS A CB  1 
ATOM   3662 S SG  . CYS C 3 91  ? 38.90801  57.80588  16.52748  1.000 84.49928  ?  104 CYS A SG  1 
ATOM   3663 N N   . ALA C 3 92  ? 42.29816  59.38753  16.45642  1.000 66.64130  ?  105 ALA A N   1 
ATOM   3664 C CA  . ALA C 3 92  ? 43.69721  59.03150  16.27242  1.000 68.11338  ?  105 ALA A CA  1 
ATOM   3665 C C   . ALA C 3 92  ? 44.06974  57.87577  17.18929  1.000 62.13403  ?  105 ALA A C   1 
ATOM   3666 O O   . ALA C 3 92  ? 43.43882  57.64468  18.22385  1.000 65.70958  ?  105 ALA A O   1 
ATOM   3667 C CB  . ALA C 3 92  ? 44.62086  60.22880  16.53494  1.000 64.21986  ?  105 ALA A CB  1 
ATOM   3668 N N   . LEU C 3 93  ? 45.11388  57.14910  16.79110  1.000 56.38253  ?  106 LEU A N   1 
ATOM   3669 C CA  . LEU C 3 93  ? 45.66629  56.06743  17.59279  1.000 55.59459  ?  106 LEU A CA  1 
ATOM   3670 C C   . LEU C 3 93  ? 47.17987  56.04473  17.43231  1.000 60.31195  ?  106 LEU A C   1 
ATOM   3671 O O   . LEU C 3 93  ? 47.74575  56.69378  16.54906  1.000 60.93170  ?  106 LEU A O   1 
ATOM   3672 C CB  . LEU C 3 93  ? 45.06082  54.70490  17.21380  1.000 58.79666  ?  106 LEU A CB  1 
ATOM   3673 C CG  . LEU C 3 93  ? 45.13006  54.16124  15.77943  1.000 57.52661  ?  106 LEU A CG  1 
ATOM   3674 C CD1 . LEU C 3 93  ? 46.50804  53.62895  15.40034  1.000 57.02309  ?  106 LEU A CD1 1 
ATOM   3675 C CD2 . LEU C 3 93  ? 44.09692  53.06919  15.60745  1.000 59.99831  ?  106 LEU A CD2 1 
ATOM   3676 N N   . SER C 3 94  ? 47.83280  55.27218  18.29752  1.000 73.68528  ?  107 SER A N   1 
ATOM   3677 C CA  . SER C 3 94  ? 49.26787  55.04626  18.21221  1.000 69.45123  ?  107 SER A CA  1 
ATOM   3678 C C   . SER C 3 94  ? 49.57228  53.67385  18.79070  1.000 72.52773  ?  107 SER A C   1 
ATOM   3679 O O   . SER C 3 94  ? 49.00358  53.28710  19.81512  1.000 70.29972  ?  107 SER A O   1 
ATOM   3680 C CB  . SER C 3 94  ? 50.06095  56.12272  18.96057  1.000 67.68022  ?  107 SER A CB  1 
ATOM   3681 O OG  . SER C 3 94  ? 49.88855  55.99903  20.36119  1.000 80.96156  ?  107 SER A OG  1 
ATOM   3682 N N   . LEU C 3 95  ? 50.46667  52.94396  18.12964  1.000 65.36559  ?  108 LEU A N   1 
ATOM   3683 C CA  . LEU C 3 95  ? 50.81345  51.60305  18.57964  1.000 49.59766  ?  108 LEU A CA  1 
ATOM   3684 C C   . LEU C 3 95  ? 51.68724  51.67493  19.82572  1.000 48.34112  ?  108 LEU A C   1 
ATOM   3685 O O   . LEU C 3 95  ? 52.68412  52.40246  19.85838  1.000 57.76847  ?  108 LEU A O   1 
ATOM   3686 C CB  . LEU C 3 95  ? 51.53010  50.84017  17.46748  1.000 49.31822  ?  108 LEU A CB  1 
ATOM   3687 C CG  . LEU C 3 95  ? 50.77518  50.73833  16.14044  1.000 53.57381  ?  108 LEU A CG  1 
ATOM   3688 C CD1 . LEU C 3 95  ? 51.55757  49.90360  15.14061  1.000 56.72916  ?  108 LEU A CD1 1 
ATOM   3689 C CD2 . LEU C 3 95  ? 49.38245  50.16493  16.35203  1.000 53.40997  ?  108 LEU A CD2 1 
ATOM   3690 N N   . ASN C 3 96  ? 51.30863  50.91562  20.85628  1.000 55.76217  ?  109 ASN A N   1 
ATOM   3691 C CA  . ASN C 3 96  ? 52.05991  50.94191  22.10643  1.000 55.02136  ?  109 ASN A CA  1 
ATOM   3692 C C   . ASN C 3 96  ? 53.39682  50.22474  21.98346  1.000 53.78690  ?  109 ASN A C   1 
ATOM   3693 O O   . ASN C 3 96  ? 54.37039  50.62107  22.63376  1.000 58.60078  ?  109 ASN A O   1 
ATOM   3694 C CB  . ASN C 3 96  ? 51.23574  50.31837  23.23251  1.000 50.43757  ?  109 ASN A CB  1 
ATOM   3695 C CG  . ASN C 3 96  ? 50.15863  51.24678  23.74860  1.000 59.29164  ?  109 ASN A CG  1 
ATOM   3696 O OD1 . ASN C 3 96  ? 49.81330  52.23576  23.10216  1.000 84.45544  ?  109 ASN A OD1 1 
ATOM   3697 N ND2 . ASN C 3 96  ? 49.62142  50.93423  24.92280  1.000 55.64543  ?  109 ASN A ND2 1 
ATOM   3698 N N   . SER C 3 97  ? 53.46947  49.17856  21.16603  1.000 48.43655  ?  110 SER A N   1 
ATOM   3699 C CA  . SER C 3 97  ? 54.67274  48.35931  21.06185  1.000 47.89229  ?  110 SER A CA  1 
ATOM   3700 C C   . SER C 3 97  ? 54.95715  48.02391  19.60210  1.000 49.65196  ?  110 SER A C   1 
ATOM   3701 O O   . SER C 3 97  ? 55.17620  46.86994  19.23396  1.000 47.30423  ?  110 SER A O   1 
ATOM   3702 C CB  . SER C 3 97  ? 54.53353  47.09145  21.90112  1.000 49.73021  ?  110 SER A CB  1 
ATOM   3703 O OG  . SER C 3 97  ? 54.21611  47.40708  23.24531  1.000 58.30876  ?  110 SER A OG  1 
ATOM   3704 N N   . GLY C 3 98  ? 54.96372  49.04350  18.74917  1.000 56.79715  ?  111 GLY A N   1 
ATOM   3705 C CA  . GLY C 3 98  ? 55.22902  48.82460  17.34192  1.000 45.91371  ?  111 GLY A CA  1 
ATOM   3706 C C   . GLY C 3 98  ? 55.61779  50.07838  16.58757  1.000 62.37889  ?  111 GLY A C   1 
ATOM   3707 O O   . GLY C 3 98  ? 55.02163  51.14233  16.78228  1.000 60.74002  ?  111 GLY A O   1 
ATOM   3708 N N   . GLY C 3 99  ? 56.62619  49.96247  15.72471  1.000 49.38874  ?  112 GLY A N   1 
ATOM   3709 C CA  . GLY C 3 99  ? 57.01094  51.06994  14.87378  1.000 44.10517  ?  112 GLY A CA  1 
ATOM   3710 C C   . GLY C 3 99  ? 57.64667  52.21447  15.64511  1.000 50.68188  ?  112 GLY A C   1 
ATOM   3711 O O   . GLY C 3 99  ? 58.26339  52.03421  16.69942  1.000 46.89960  ?  112 GLY A O   1 
ATOM   3712 N N   . SER C 3 100 ? 57.48346  53.41728  15.10295  1.000 48.66456  ?  113 SER A N   1 
ATOM   3713 C CA  . SER C 3 100 ? 58.09584  54.60641  15.66944  1.000 52.45998  ?  113 SER A CA  1 
ATOM   3714 C C   . SER C 3 100 ? 57.24757  55.17314  16.80411  1.000 50.11530  ?  113 SER A C   1 
ATOM   3715 O O   . SER C 3 100 ? 56.03836  54.94294  16.89137  1.000 72.04200  ?  113 SER A O   1 
ATOM   3716 C CB  . SER C 3 100 ? 58.29374  55.67016  14.58918  1.000 58.75123  ?  113 SER A CB  1 
ATOM   3717 O OG  . SER C 3 100 ? 58.72057  56.89663  15.15452  1.000 52.44883  ?  113 SER A OG  1 
ATOM   3718 N N   . ASN C 3 101 ? 57.90603  55.92503  17.68165  1.000 41.72307  ?  114 ASN A N   1 
ATOM   3719 C CA  . ASN C 3 101 ? 57.21561  56.65090  18.73358  1.000 42.26311  ?  114 ASN A CA  1 
ATOM   3720 C C   . ASN C 3 101 ? 56.66171  57.96683  18.19343  1.000 54.58821  ?  114 ASN A C   1 
ATOM   3721 O O   . ASN C 3 101 ? 57.09838  58.47603  17.15718  1.000 45.66438  ?  114 ASN A O   1 
ATOM   3722 C CB  . ASN C 3 101 ? 58.15344  56.91888  19.91153  1.000 50.55938  ?  114 ASN A CB  1 
ATOM   3723 C CG  . ASN C 3 101 ? 58.52656  55.65476  20.65936  1.000 51.77573  ?  114 ASN A CG  1 
ATOM   3724 O OD1 . ASN C 3 101 ? 57.71880  54.73574  20.78566  1.000 52.53825  ?  114 ASN A OD1 1 
ATOM   3725 N ND2 . ASN C 3 101 ? 59.75533  55.60251  21.16087  1.000 39.69729  ?  114 ASN A ND2 1 
ATOM   3726 N N   . ALA C 3 102 ? 55.68156  58.51317  18.91789  1.000 58.14457  ?  115 ALA A N   1 
ATOM   3727 C CA  . ALA C 3 102 ? 55.02028  59.76734  18.54819  1.000 55.60101  ?  115 ALA A CA  1 
ATOM   3728 C C   . ALA C 3 102 ? 54.47035  59.70985  17.12403  1.000 54.55228  ?  115 ALA A C   1 
ATOM   3729 O O   . ALA C 3 102 ? 54.56901  60.67194  16.35952  1.000 62.57274  ?  115 ALA A O   1 
ATOM   3730 C CB  . ALA C 3 102 ? 55.96039  60.96250  18.72092  1.000 59.19766  ?  115 ALA A CB  1 
ATOM   3731 N N   . LYS C 3 103 ? 53.88422  58.57025  16.76346  1.000 47.25411  ?  116 LYS A N   1 
ATOM   3732 C CA  . LYS C 3 103 ? 53.33568  58.34651  15.42923  1.000 47.39795  ?  116 LYS A CA  1 
ATOM   3733 C C   . LYS C 3 103 ? 51.83878  58.09762  15.55896  1.000 52.12670  ?  116 LYS A C   1 
ATOM   3734 O O   . LYS C 3 103 ? 51.41931  57.03046  16.01992  1.000 68.10278  ?  116 LYS A O   1 
ATOM   3735 C CB  . LYS C 3 103 ? 54.03402  57.17327  14.74310  1.000 46.71236  ?  116 LYS A CB  1 
ATOM   3736 C CG  . LYS C 3 103 ? 53.51304  56.85639  13.35281  1.000 48.06585  ?  116 LYS A CG  1 
ATOM   3737 C CD  . LYS C 3 103 ? 54.25362  55.67042  12.75870  1.000 47.72147  ?  116 LYS A CD  1 
ATOM   3738 C CE  . LYS C 3 103 ? 53.66996  55.25888  11.41716  1.000 49.55011  ?  116 LYS A CE  1 
ATOM   3739 N NZ  . LYS C 3 103 ? 54.34131  54.04128  10.88005  1.000 56.16504  ?  116 LYS A NZ  1 
ATOM   3740 N N   . LEU C 3 104 ? 51.03809  59.07778  15.15400  1.000 58.27636  ?  117 LEU A N   1 
ATOM   3741 C CA  . LEU C 3 104 ? 49.58807  58.98616  15.23068  1.000 51.40187  ?  117 LEU A CA  1 
ATOM   3742 C C   . LEU C 3 104 ? 48.99973  58.72270  13.85138  1.000 53.44458  ?  117 LEU A C   1 
ATOM   3743 O O   . LEU C 3 104 ? 49.48245  59.25047  12.84499  1.000 53.01485  ?  117 LEU A O   1 
ATOM   3744 C CB  . LEU C 3 104 ? 48.98864  60.26772  15.81285  1.000 52.40396  ?  117 LEU A CB  1 
ATOM   3745 C CG  . LEU C 3 104 ? 49.27985  60.56191  17.28474  1.000 51.90858  ?  117 LEU A CG  1 
ATOM   3746 C CD1 . LEU C 3 104 ? 48.70556  61.91092  17.68252  1.000 69.06998  ?  117 LEU A CD1 1 
ATOM   3747 C CD2 . LEU C 3 104 ? 48.71841  59.46215  18.16742  1.000 57.33005  ?  117 LEU A CD2 1 
ATOM   3748 N N   . THR C 3 105 ? 47.95528  57.89972  13.81378  1.000 64.67833  ?  118 THR A N   1 
ATOM   3749 C CA  . THR C 3 105 ? 47.19837  57.62274  12.59775  1.000 58.39020  ?  118 THR A CA  1 
ATOM   3750 C C   . THR C 3 105 ? 45.84219  58.30308  12.73341  1.000 57.09733  ?  118 THR A C   1 
ATOM   3751 O O   . THR C 3 105 ? 45.01627  57.89344  13.55590  1.000 77.94187  ?  118 THR A O   1 
ATOM   3752 C CB  . THR C 3 105 ? 47.04384  56.11997  12.37143  1.000 55.95035  ?  118 THR A CB  1 
ATOM   3753 O OG1 . THR C 3 105 ? 48.32465  55.54365  12.08628  1.000 54.66094  ?  118 THR A OG1 1 
ATOM   3754 C CG2 . THR C 3 105 ? 46.10189  55.84985  11.20735  1.000 69.44815  ?  118 THR A CG2 1 
ATOM   3755 N N   . PHE C 3 106 ? 45.61829  59.34044  11.93387  1.000 60.76045  ?  119 PHE A N   1 
ATOM   3756 C CA  . PHE C 3 106 ? 44.40587  60.14049  12.00917  1.000 59.73250  ?  119 PHE A CA  1 
ATOM   3757 C C   . PHE C 3 106 ? 43.37979  59.67817  10.98286  1.000 65.80451  ?  119 PHE A C   1 
ATOM   3758 O O   . PHE C 3 106 ? 43.72054  59.10481  9.94511   1.000 62.24456  ?  119 PHE A O   1 
ATOM   3759 C CB  . PHE C 3 106 ? 44.71331  61.62286  11.78250  1.000 60.04063  ?  119 PHE A CB  1 
ATOM   3760 C CG  . PHE C 3 106 ? 45.46191  62.27012  12.91049  1.000 58.77271  ?  119 PHE A CG  1 
ATOM   3761 C CD1 . PHE C 3 106 ? 44.78120  62.82626  13.98035  1.000 66.58463  ?  119 PHE A CD1 1 
ATOM   3762 C CD2 . PHE C 3 106 ? 46.84472  62.33188  12.89745  1.000 57.32253  ?  119 PHE A CD2 1 
ATOM   3763 C CE1 . PHE C 3 106 ? 45.46591  63.42701  15.01957  1.000 60.88171  ?  119 PHE A CE1 1 
ATOM   3764 C CE2 . PHE C 3 106 ? 47.53473  62.93212  13.93318  1.000 64.75903  ?  119 PHE A CE2 1 
ATOM   3765 C CZ  . PHE C 3 106 ? 46.84413  63.47982  14.99577  1.000 58.10651  ?  119 PHE A CZ  1 
ATOM   3766 N N   . GLY C 3 107 ? 42.11259  59.93760  11.28673  1.000 67.58732  ?  120 GLY A N   1 
ATOM   3767 C CA  . GLY C 3 107 ? 41.04900  59.76594  10.32456  1.000 73.33205  ?  120 GLY A CA  1 
ATOM   3768 C C   . GLY C 3 107 ? 40.94366  60.96821  9.40574   1.000 74.10539  ?  120 GLY A C   1 
ATOM   3769 O O   . GLY C 3 107 ? 41.74931  61.89951  9.44414   1.000 87.72115  ?  120 GLY A O   1 
ATOM   3770 N N   . LYS C 3 108 ? 39.91490  60.93980  8.55793   1.000 69.06750  ?  121 LYS A N   1 
ATOM   3771 C CA  . LYS C 3 108 ? 39.69691  62.04668  7.63510   1.000 70.55776  ?  121 LYS A CA  1 
ATOM   3772 C C   . LYS C 3 108 ? 39.23085  63.31051  8.34581   1.000 70.81849  ?  121 LYS A C   1 
ATOM   3773 O O   . LYS C 3 108 ? 39.33088  64.40039  7.77287   1.000 78.18508  ?  121 LYS A O   1 
ATOM   3774 C CB  . LYS C 3 108 ? 38.68403  61.64566  6.56183   1.000 92.57436  ?  121 LYS A CB  1 
ATOM   3775 C CG  . LYS C 3 108 ? 39.13219  60.47963  5.69624   1.000 99.24168  ?  121 LYS A CG  1 
ATOM   3776 C CD  . LYS C 3 108 ? 38.07862  60.12323  4.66178   1.000 106.18881 ?  121 LYS A CD  1 
ATOM   3777 C CE  . LYS C 3 108 ? 37.80365  61.29065  3.72898   1.000 116.83501 ?  121 LYS A CE  1 
ATOM   3778 N NZ  . LYS C 3 108 ? 36.74365  60.96568  2.73485   1.000 135.52081 ?  121 LYS A NZ  1 
ATOM   3779 N N   . GLY C 3 109 ? 38.73756  63.19358  9.56891   1.000 70.31933  ?  122 GLY A N   1 
ATOM   3780 C CA  . GLY C 3 109 ? 38.24996  64.35235  10.29909  1.000 70.94915  ?  122 GLY A CA  1 
ATOM   3781 C C   . GLY C 3 109 ? 36.77509  64.60342  10.06241  1.000 73.42569  ?  122 GLY A C   1 
ATOM   3782 O O   . GLY C 3 109 ? 36.23328  64.36485  8.98344   1.000 75.01002  ?  122 GLY A O   1 
ATOM   3783 N N   . THR C 3 110 ? 36.11034  65.09804  11.10430  1.000 74.01085  ?  123 THR A N   1 
ATOM   3784 C CA  . THR C 3 110 ? 34.68462  65.39879  11.05709  1.000 76.46660  ?  123 THR A CA  1 
ATOM   3785 C C   . THR C 3 110 ? 34.47549  66.83602  11.50602  1.000 77.44450  ?  123 THR A C   1 
ATOM   3786 O O   . THR C 3 110 ? 34.85807  67.20106  12.62259  1.000 76.66935  ?  123 THR A O   1 
ATOM   3787 C CB  . THR C 3 110 ? 33.88333  64.43900  11.94209  1.000 81.14851  ?  123 THR A CB  1 
ATOM   3788 O OG1 . THR C 3 110 ? 34.16321  63.08607  11.56104  1.000 76.32861  ?  123 THR A OG1 1 
ATOM   3789 C CG2 . THR C 3 110 ? 32.39336  64.70123  11.79372  1.000 79.79489  ?  123 THR A CG2 1 
ATOM   3790 N N   . LYS C 3 111 ? 33.87250  67.64594  10.64026  1.000 79.43960  ?  124 LYS A N   1 
ATOM   3791 C CA  . LYS C 3 111 ? 33.60141  69.04195  10.94944  1.000 80.92042  ?  124 LYS A CA  1 
ATOM   3792 C C   . LYS C 3 111 ? 32.27763  69.16818  11.69110  1.000 82.80309  ?  124 LYS A C   1 
ATOM   3793 O O   . LYS C 3 111 ? 31.29326  68.50701  11.34836  1.000 83.99859  ?  124 LYS A O   1 
ATOM   3794 C CB  . LYS C 3 111 ? 33.56821  69.88252  9.67175   1.000 82.54710  ?  124 LYS A CB  1 
ATOM   3795 C CG  . LYS C 3 111 ? 33.41449  71.37537  9.91514   1.000 84.37505  ?  124 LYS A CG  1 
ATOM   3796 C CD  . LYS C 3 111 ? 33.39294  72.15054  8.60902   1.000 86.29144  ?  124 LYS A CD  1 
ATOM   3797 C CE  . LYS C 3 111 ? 33.36397  73.65063  8.85831   1.000 110.02360 ?  124 LYS A CE  1 
ATOM   3798 N NZ  . LYS C 3 111 ? 32.18498  74.06007  9.67043   1.000 107.06846 ?  124 LYS A NZ  1 
ATOM   3799 N N   . LEU C 3 112 ? 32.26163  70.02089  12.71228  1.000 83.38710  ?  125 LEU A N   1 
ATOM   3800 C CA  . LEU C 3 112 ? 31.07367  70.26695  13.51731  1.000 85.47281  ?  125 LEU A CA  1 
ATOM   3801 C C   . LEU C 3 112 ? 30.70198  71.73968  13.43460  1.000 93.44140  ?  125 LEU A C   1 
ATOM   3802 O O   . LEU C 3 112 ? 31.53634  72.61133  13.70018  1.000 92.84623  ?  125 LEU A O   1 
ATOM   3803 C CB  . LEU C 3 112 ? 31.29828  69.85981  14.97625  1.000 88.72394  ?  125 LEU A CB  1 
ATOM   3804 C CG  . LEU C 3 112 ? 30.13868  70.15237  15.93221  1.000 96.08646  ?  125 LEU A CG  1 
ATOM   3805 C CD1 . LEU C 3 112 ? 28.87747  69.42680  15.48876  1.000 88.70788  ?  125 LEU A CD1 1 
ATOM   3806 C CD2 . LEU C 3 112 ? 30.50409  69.77594  17.35986  1.000 86.56171  ?  125 LEU A CD2 1 
ATOM   3807 N N   . SER C 3 113 ? 29.45320  72.01102  13.06411  1.000 94.54351  ?  126 SER A N   1 
ATOM   3808 C CA  . SER C 3 113 ? 28.91239  73.36376  13.01456  1.000 104.42611 ?  126 SER A CA  1 
ATOM   3809 C C   . SER C 3 113 ? 27.69172  73.42236  13.91990  1.000 98.73779  ?  126 SER A C   1 
ATOM   3810 O O   . SER C 3 113 ? 26.70718  72.71385  13.68450  1.000 107.21360 ?  126 SER A O   1 
ATOM   3811 C CB  . SER C 3 113 ? 28.54540  73.76234  11.58345  1.000 104.75238 ?  126 SER A CB  1 
ATOM   3812 O OG  . SER C 3 113 ? 29.68273  73.73887  10.73858  1.000 121.50077 ?  126 SER A OG  1 
ATOM   3813 N N   . VAL C 3 114 ? 27.75694  74.25910  14.95026  1.000 96.32542  ?  127 VAL A N   1 
ATOM   3814 C CA  . VAL C 3 114 ? 26.69794  74.37140  15.94630  1.000 102.54441 ?  127 VAL A CA  1 
ATOM   3815 C C   . VAL C 3 114 ? 26.02079  75.72213  15.76116  1.000 107.46770 ?  127 VAL A C   1 
ATOM   3816 O O   . VAL C 3 114 ? 26.63486  76.77255  15.98586  1.000 120.33134 ?  127 VAL A O   1 
ATOM   3817 C CB  . VAL C 3 114 ? 27.23736  74.21266  17.37372  1.000 108.52361 ?  127 VAL A CB  1 
ATOM   3818 C CG1 . VAL C 3 114 ? 26.09988  74.29675  18.38076  1.000 111.53747 ?  127 VAL A CG1 1 
ATOM   3819 C CG2 . VAL C 3 114 ? 27.98618  72.89615  17.51328  1.000 99.71543  ?  127 VAL A CG2 1 
ATOM   3820 N N   . LYS C 3 115 ? 24.75462  75.69785  15.35403  1.000 109.03135 ?  128 LYS A N   1 
ATOM   3821 C CA  . LYS C 3 115 ? 23.96276  76.91078  15.21401  1.000 107.42220 ?  128 LYS A CA  1 
ATOM   3822 C C   . LYS C 3 115 ? 23.17773  77.16746  16.49318  1.000 121.14503 ?  128 LYS A C   1 
ATOM   3823 O O   . LYS C 3 115 ? 22.63836  76.23879  17.10224  1.000 124.56890 ?  128 LYS A O   1 
ATOM   3824 C CB  . LYS C 3 115 ? 23.00806  76.80052  14.02434  1.000 113.37604 ?  128 LYS A CB  1 
ATOM   3825 N N   . SER C 3 116 ? 23.11558  78.43464  16.89359  1.000 131.32078 ?  129 SER A N   1 
ATOM   3826 C CA  . SER C 3 116 ? 22.46229  78.79325  18.14347  1.000 132.97045 ?  129 SER A CA  1 
ATOM   3827 C C   . SER C 3 116 ? 20.96060  78.54539  18.06758  1.000 130.05365 ?  129 SER A C   1 
ATOM   3828 O O   . SER C 3 116 ? 20.34620  78.61030  16.99926  1.000 131.06971 ?  129 SER A O   1 
ATOM   3829 C CB  . SER C 3 116 ? 22.72412  80.25868  18.48621  1.000 119.41590 ?  129 SER A CB  1 
ATOM   3830 O OG  . SER C 3 116 ? 22.26922  80.56001  19.79420  1.000 115.95607 ?  129 SER A OG  1 
ATOM   3831 N N   . HIS C 3 117 ? 20.37002  78.26093  19.22838  1.000 124.56905 ?  130 HIS A N   1 
ATOM   3832 C CA  . HIS C 3 117 ? 18.93088  78.04250  19.30039  1.000 120.33317 ?  130 HIS A CA  1 
ATOM   3833 C C   . HIS C 3 117 ? 18.17439  79.36533  19.30601  1.000 123.41446 ?  130 HIS A C   1 
ATOM   3834 O O   . HIS C 3 117 ? 17.26777  79.57246  18.49140  1.000 121.74690 ?  130 HIS A O   1 
ATOM   3835 C CB  . HIS C 3 117 ? 18.59083  77.21945  20.54314  1.000 125.51289 ?  130 HIS A CB  1 
ATOM   3836 C CG  . HIS C 3 117 ? 17.60516  76.12387  20.28776  1.000 126.98605 ?  130 HIS A CG  1 
ATOM   3837 N ND1 . HIS C 3 117 ? 17.82246  74.82164  20.68255  1.000 119.17548 ?  130 HIS A ND1 1 
ATOM   3838 C CD2 . HIS C 3 117 ? 16.39812  76.13526  19.67462  1.000 130.22678 ?  130 HIS A CD2 1 
ATOM   3839 C CE1 . HIS C 3 117 ? 16.79183  74.07785  20.32309  1.000 119.56762 ?  130 HIS A CE1 1 
ATOM   3840 N NE2 . HIS C 3 117 ? 15.91307  74.85074  19.71092  1.000 127.38410 ?  130 HIS A NE2 1 
ATOM   3841 N N   . ILE C 3 118 ? 18.54127  80.26722  20.21483  1.000 115.41486 ?  131 ILE A N   1 
ATOM   3842 C CA  . ILE C 3 118 ? 17.93170  81.59115  20.32351  1.000 107.51383 ?  131 ILE A CA  1 
ATOM   3843 C C   . ILE C 3 118 ? 16.41917  81.49231  20.49315  1.000 110.74113 ?  131 ILE A C   1 
ATOM   3844 O O   . ILE C 3 118 ? 15.65868  81.94307  19.63667  1.000 112.17198 ?  131 ILE A O   1 
ATOM   3845 C CB  . ILE C 3 118 ? 18.28611  82.46866  19.10694  1.000 106.19385 ?  131 ILE A CB  1 
ATOM   3846 N N   . PRO C 3 121 ? 13.51815  87.54395  17.03148  1.000 150.70981 ?  134 PRO A N   1 
ATOM   3847 C CA  . PRO C 3 121 ? 13.56132  88.15643  18.36272  1.000 160.26507 ?  134 PRO A CA  1 
ATOM   3848 C C   . PRO C 3 121 ? 13.79286  89.66292  18.30622  1.000 157.04493 ?  134 PRO A C   1 
ATOM   3849 O O   . PRO C 3 121 ? 12.84007  90.42514  18.14001  1.000 136.65241 ?  134 PRO A O   1 
ATOM   3850 C CB  . PRO C 3 121 ? 14.74204  87.44881  19.03331  1.000 146.16580 ?  134 PRO A CB  1 
ATOM   3851 N N   . ASP C 3 122 ? 15.04812  90.08401  18.44357  1.000 159.37218 ?  135 ASP A N   1 
ATOM   3852 C CA  . ASP C 3 122 ? 15.42391  91.49641  18.38788  1.000 150.31645 ?  135 ASP A CA  1 
ATOM   3853 C C   . ASP C 3 122 ? 16.65025  91.66333  17.49895  1.000 154.44723 ?  135 ASP A C   1 
ATOM   3854 O O   . ASP C 3 122 ? 17.75887  91.91615  17.98626  1.000 147.11404 ?  135 ASP A O   1 
ATOM   3855 C CB  . ASP C 3 122 ? 15.68667  92.04671  19.78987  1.000 146.24437 ?  135 ASP A CB  1 
ATOM   3856 N N   . PRO C 3 123 ? 16.48817  91.52462  16.18459  1.000 160.95190 ?  136 PRO A N   1 
ATOM   3857 C CA  . PRO C 3 123 ? 17.60712  91.78141  15.27239  1.000 142.72611 ?  136 PRO A CA  1 
ATOM   3858 C C   . PRO C 3 123 ? 17.87981  93.27344  15.16541  1.000 138.66319 ?  136 PRO A C   1 
ATOM   3859 O O   . PRO C 3 123 ? 17.07924  94.11617  15.57537  1.000 151.94799 ?  136 PRO A O   1 
ATOM   3860 C CB  . PRO C 3 123 ? 17.12904  91.20240  13.93468  1.000 136.20651 ?  136 PRO A CB  1 
ATOM   3861 C CG  . PRO C 3 123 ? 15.90452  90.38583  14.26477  1.000 159.96999 ?  136 PRO A CG  1 
ATOM   3862 C CD  . PRO C 3 123 ? 15.30086  91.05136  15.45681  1.000 165.22251 ?  136 PRO A CD  1 
ATOM   3863 N N   . ALA C 3 124 ? 19.04143  93.59565  14.60021  1.000 117.73479 ?  137 ALA A N   1 
ATOM   3864 C CA  . ALA C 3 124 ? 19.45324  94.98699  14.46966  1.000 109.77606 ?  137 ALA A CA  1 
ATOM   3865 C C   . ALA C 3 124 ? 20.45940  95.10887  13.33630  1.000 116.69440 ?  137 ALA A C   1 
ATOM   3866 O O   . ALA C 3 124 ? 21.46227  94.38952  13.31681  1.000 130.56572 ?  137 ALA A O   1 
ATOM   3867 C CB  . ALA C 3 124 ? 20.05642  95.50161  15.77973  1.000 114.18052 ?  137 ALA A CB  1 
ATOM   3868 N N   . VAL C 3 125 ? 20.19143  96.01633  12.40098  1.000 106.80391 ?  138 VAL A N   1 
ATOM   3869 C CA  . VAL C 3 125 ? 21.08156  96.28796  11.27691  1.000 107.57463 ?  138 VAL A CA  1 
ATOM   3870 C C   . VAL C 3 125 ? 21.46309  97.76044  11.32952  1.000 116.49674 ?  138 VAL A C   1 
ATOM   3871 O O   . VAL C 3 125 ? 20.58714  98.63376  11.29735  1.000 113.65428 ?  138 VAL A O   1 
ATOM   3872 C CB  . VAL C 3 125 ? 20.43222  95.94005  9.92773   1.000 103.93520 ?  138 VAL A CB  1 
ATOM   3873 C CG1 . VAL C 3 125 ? 21.43787  96.11132  8.80078   1.000 102.40690 ?  138 VAL A CG1 1 
ATOM   3874 C CG2 . VAL C 3 125 ? 19.88057  94.52277  9.94612   1.000 102.84587 ?  138 VAL A CG2 1 
ATOM   3875 N N   . TYR C 3 126 ? 22.76329  98.03646  11.40733  1.000 103.77752 ?  139 TYR A N   1 
ATOM   3876 C CA  . TYR C 3 126 ? 23.26922  99.39717  11.50519  1.000 115.74360 ?  139 TYR A CA  1 
ATOM   3877 C C   . TYR C 3 126 ? 24.15220  99.72020  10.30738  1.000 116.93031 ?  139 TYR A C   1 
ATOM   3878 O O   . TYR C 3 126 ? 24.74568  98.82878  9.69398   1.000 123.56315 ?  139 TYR A O   1 
ATOM   3879 C CB  . TYR C 3 126 ? 24.06801  99.60516  12.79934  1.000 135.99834 ?  139 TYR A CB  1 
ATOM   3880 C CG  . TYR C 3 126 ? 23.35565  99.14391  14.05035  1.000 127.56245 ?  139 TYR A CG  1 
ATOM   3881 C CD1 . TYR C 3 126 ? 23.63888  97.90772  14.61639  1.000 111.61400 ?  139 TYR A CD1 1 
ATOM   3882 C CD2 . TYR C 3 126 ? 22.40253  99.94447  14.66700  1.000 127.89303 ?  139 TYR A CD2 1 
ATOM   3883 C CE1 . TYR C 3 126 ? 22.99368  97.48060  15.76098  1.000 113.59343 ?  139 TYR A CE1 1 
ATOM   3884 C CE2 . TYR C 3 126 ? 21.74866  99.52423  15.81198  1.000 130.56767 ?  139 TYR A CE2 1 
ATOM   3885 C CZ  . TYR C 3 126 ? 22.05008  98.29222  16.35548  1.000 128.72810 ?  139 TYR A CZ  1 
ATOM   3886 O OH  . TYR C 3 126 ? 21.40599  97.86733  17.49601  1.000 135.21561 ?  139 TYR A OH  1 
ATOM   3887 N N   . GLN C 3 127 ? 24.23932  101.00786 9.98393   1.000 113.55172 ?  140 GLN A N   1 
ATOM   3888 C CA  . GLN C 3 127 ? 25.10202  101.49991 8.91736   1.000 105.90124 ?  140 GLN A CA  1 
ATOM   3889 C C   . GLN C 3 127 ? 26.17485  102.40266 9.51110   1.000 109.45711 ?  140 GLN A C   1 
ATOM   3890 O O   . GLN C 3 127 ? 25.87357  103.27543 10.33291  1.000 124.43898 ?  140 GLN A O   1 
ATOM   3891 C CB  . GLN C 3 127 ? 24.29554  102.25390 7.85613   1.000 101.50637 ?  140 GLN A CB  1 
ATOM   3892 N N   . LEU C 3 128 ? 27.42098  102.18729 9.09267   1.000 98.10285  ?  141 LEU A N   1 
ATOM   3893 C CA  . LEU C 3 128 ? 28.56791  102.91746 9.60757   1.000 99.46838  ?  141 LEU A CA  1 
ATOM   3894 C C   . LEU C 3 128 ? 29.51443  103.25349 8.46233   1.000 115.65655 ?  141 LEU A C   1 
ATOM   3895 O O   . LEU C 3 128 ? 29.57490  102.54084 7.45674   1.000 128.90753 ?  141 LEU A O   1 
ATOM   3896 C CB  . LEU C 3 128 ? 29.31287  102.11794 10.69956  1.000 104.28004 ?  141 LEU A CB  1 
ATOM   3897 C CG  . LEU C 3 128 ? 29.39126  100.58872 10.76607  1.000 105.72422 ?  141 LEU A CG  1 
ATOM   3898 C CD1 . LEU C 3 128 ? 30.59270  100.18803 11.60693  1.000 103.60603 ?  141 LEU A CD1 1 
ATOM   3899 C CD2 . LEU C 3 128 ? 28.12392  99.98825  11.36204  1.000 97.64600  ?  141 LEU A CD2 1 
ATOM   3900 N N   . ARG C 3 129 ? 30.25160  104.35210 8.62163   1.000 115.30438 ?  142 ARG A N   1 
ATOM   3901 C CA  . ARG C 3 129 ? 31.12741  104.85507 7.57047   1.000 127.47277 ?  142 ARG A CA  1 
ATOM   3902 C C   . ARG C 3 129 ? 32.16294  105.78084 8.18837   1.000 132.38503 ?  142 ARG A C   1 
ATOM   3903 O O   . ARG C 3 129 ? 31.92147  106.38583 9.23522   1.000 140.76372 ?  142 ARG A O   1 
ATOM   3904 C CB  . ARG C 3 129 ? 30.33243  105.59383 6.48571   1.000 117.81851 ?  142 ARG A CB  1 
ATOM   3905 N N   . ASP C 3 130 ? 33.31570  105.88626 7.52840   1.000 129.25955 ?  143 ASP A N   1 
ATOM   3906 C CA  . ASP C 3 130 ? 34.38770  106.74906 8.02036   1.000 139.29410 ?  143 ASP A CA  1 
ATOM   3907 C C   . ASP C 3 130 ? 35.33169  107.09113 6.87828   1.000 150.96084 ?  143 ASP A C   1 
ATOM   3908 O O   . ASP C 3 130 ? 35.85929  106.18813 6.21694   1.000 143.85701 ?  143 ASP A O   1 
ATOM   3909 C CB  . ASP C 3 130 ? 35.14885  106.06678 9.16438   1.000 127.26103 ?  143 ASP A CB  1 
ATOM   3910 C CG  . ASP C 3 130 ? 36.25013  106.93912 9.74188   1.000 136.08238 ?  143 ASP A CG  1 
ATOM   3911 O OD1 . ASP C 3 130 ? 36.24456  108.16119 9.48375   1.000 140.45095 ?  143 ASP A OD1 1 
ATOM   3912 O OD2 . ASP C 3 130 ? 37.12615  106.39968 10.45169  1.000 131.44481 ?  143 ASP A OD2 1 
ATOM   3913 N N   . SER C 3 131 ? 35.52575  108.39160 6.64545   1.000 151.26692 ?  144 SER A N   1 
ATOM   3914 C CA  . SER C 3 131 ? 36.60665  108.94407 5.82645   1.000 139.08800 ?  144 SER A CA  1 
ATOM   3915 C C   . SER C 3 131 ? 36.59162  108.45321 4.38330   1.000 140.51638 ?  144 SER A C   1 
ATOM   3916 O O   . SER C 3 131 ? 37.61860  108.50498 3.70167   1.000 124.98154 ?  144 SER A O   1 
ATOM   3917 C CB  . SER C 3 131 ? 37.97802  108.65169 6.45068   1.000 136.23344 ?  144 SER A CB  1 
ATOM   3918 O OG  . SER C 3 131 ? 38.35310  107.30136 6.23511   1.000 140.64193 ?  144 SER A OG  1 
ATOM   3919 N N   . LYS C 3 132 ? 35.46104  107.96694 3.88812   1.000 151.04132 ?  145 LYS A N   1 
ATOM   3920 C CA  . LYS C 3 132 ? 35.41056  107.50737 2.50643   1.000 152.01181 ?  145 LYS A CA  1 
ATOM   3921 C C   . LYS C 3 132 ? 34.20811  108.12236 1.80961   1.000 158.60867 ?  145 LYS A C   1 
ATOM   3922 O O   . LYS C 3 132 ? 34.27878  108.48975 0.63293   1.000 169.10998 ?  145 LYS A O   1 
ATOM   3923 C CB  . LYS C 3 132 ? 35.34628  105.97432 2.45275   1.000 145.55867 ?  145 LYS A CB  1 
ATOM   3924 N N   . SER C 3 133 ? 33.11211  108.24865 2.55343   1.000 157.58590 ?  146 SER A N   1 
ATOM   3925 C CA  . SER C 3 133 ? 31.86342  108.83801 2.07906   1.000 153.05362 ?  146 SER A CA  1 
ATOM   3926 C C   . SER C 3 133 ? 31.36455  108.12996 0.82371   1.000 147.12731 ?  146 SER A C   1 
ATOM   3927 O O   . SER C 3 133 ? 31.48620  106.91142 0.70467   1.000 140.70499 ?  146 SER A O   1 
ATOM   3928 C CB  . SER C 3 133 ? 32.03670  110.33798 1.81652   1.000 139.70150 ?  146 SER A CB  1 
ATOM   3929 N N   . LYS C 3 136 ? 33.34332  103.09899 0.98870   1.000 124.28394 ?  149 LYS A N   1 
ATOM   3930 C CA  . LYS C 3 136 ? 32.19929  102.20484 0.84941   1.000 127.67065 ?  149 LYS A CA  1 
ATOM   3931 C C   . LYS C 3 136 ? 31.26669  102.32541 2.05301   1.000 136.87400 ?  149 LYS A C   1 
ATOM   3932 O O   . LYS C 3 136 ? 31.42438  103.22162 2.88327   1.000 136.50703 ?  149 LYS A O   1 
ATOM   3933 C CB  . LYS C 3 136 ? 32.67121  100.75742 0.68011   1.000 111.52823 ?  149 LYS A CB  1 
ATOM   3934 C CG  . LYS C 3 136 ? 33.36356  100.17624 1.90575   1.000 96.16655  ?  149 LYS A CG  1 
ATOM   3935 C CD  . LYS C 3 136 ? 34.24003  98.98437  1.54532   1.000 92.67656  ?  149 LYS A CD  1 
ATOM   3936 C CE  . LYS C 3 136 ? 35.52370  99.43001  0.85935   1.000 97.70451  ?  149 LYS A CE  1 
ATOM   3937 N NZ  . LYS C 3 136 ? 36.40246  98.28066  0.50270   1.000 97.63097  ?  149 LYS A NZ  1 
ATOM   3938 N N   . SER C 3 137 ? 30.29197  101.42327 2.14063   1.000 125.38661 ?  150 SER A N   1 
ATOM   3939 C CA  . SER C 3 137 ? 29.34672  101.38592 3.24843   1.000 122.76465 ?  150 SER A CA  1 
ATOM   3940 C C   . SER C 3 137 ? 29.41700  100.02163 3.91703   1.000 121.79786 ?  150 SER A C   1 
ATOM   3941 O O   . SER C 3 137 ? 29.43901  98.99200  3.23457   1.000 122.63385 ?  150 SER A O   1 
ATOM   3942 C CB  . SER C 3 137 ? 27.91929  101.66883 2.77342   1.000 118.36635 ?  150 SER A CB  1 
ATOM   3943 O OG  . SER C 3 137 ? 27.42271  100.60181 1.98597   1.000 119.23885 ?  150 SER A OG  1 
ATOM   3944 N N   . VAL C 3 138 ? 29.44753  100.01646 5.24686   1.000 103.12303 ?  151 VAL A N   1 
ATOM   3945 C CA  . VAL C 3 138 ? 29.55583  98.79416  6.03361   1.000 97.99457  ?  151 VAL A CA  1 
ATOM   3946 C C   . VAL C 3 138 ? 28.28953  98.63800  6.86244   1.000 93.10963  ?  151 VAL A C   1 
ATOM   3947 O O   . VAL C 3 138 ? 27.84164  99.59271  7.50890   1.000 106.80544 ?  151 VAL A O   1 
ATOM   3948 C CB  . VAL C 3 138 ? 30.80380  98.80970  6.93400   1.000 91.50196  ?  151 VAL A CB  1 
ATOM   3949 C CG1 . VAL C 3 138 ? 30.89294  97.52418  7.74502   1.000 87.12474  ?  151 VAL A CG1 1 
ATOM   3950 C CG2 . VAL C 3 138 ? 32.05015  99.00372  6.09022   1.000 83.32153  ?  151 VAL A CG2 1 
ATOM   3951 N N   . CYS C 3 139 ? 27.71707  97.43721  6.84117   1.000 92.04262  ?  152 CYS A N   1 
ATOM   3952 C CA  . CYS C 3 139 ? 26.50112  97.13061  7.57544   1.000 96.19836  ?  152 CYS A CA  1 
ATOM   3953 C C   . CYS C 3 139 ? 26.76372  95.98715  8.54583   1.000 100.09943 ?  152 CYS A C   1 
ATOM   3954 O O   . CYS C 3 139 ? 27.56111  95.08519  8.26966   1.000 109.84575 ?  152 CYS A O   1 
ATOM   3955 C CB  . CYS C 3 139 ? 25.35648  96.76911  6.62116   1.000 101.50545 ?  152 CYS A CB  1 
ATOM   3956 S SG  . CYS C 3 139 ? 24.97694  98.06696  5.41735   1.000 115.17965 ?  152 CYS A SG  1 
ATOM   3957 N N   . LEU C 3 140 ? 26.08737  96.03583  9.69036   1.000 98.73681  ?  153 LEU A N   1 
ATOM   3958 C CA  . LEU C 3 140 ? 26.30402  95.09254  10.78003  1.000 92.68281  ?  153 LEU A CA  1 
ATOM   3959 C C   . LEU C 3 140 ? 24.99558  94.37307  11.07034  1.000 103.74939 ?  153 LEU A C   1 
ATOM   3960 O O   . LEU C 3 140 ? 23.97583  95.01842  11.33338  1.000 112.73033 ?  153 LEU A O   1 
ATOM   3961 C CB  . LEU C 3 140 ? 26.81624  95.81532  12.02762  1.000 98.31062  ?  153 LEU A CB  1 
ATOM   3962 C CG  . LEU C 3 140 ? 27.73481  95.02062  12.95475  1.000 94.83701  ?  153 LEU A CG  1 
ATOM   3963 C CD1 . LEU C 3 140 ? 28.97792  94.57258  12.20474  1.000 103.32597 ?  153 LEU A CD1 1 
ATOM   3964 C CD2 . LEU C 3 140 ? 28.11180  95.84212  14.17662  1.000 87.76464  ?  153 LEU A CD2 1 
ATOM   3965 N N   . PHE C 3 141 ? 25.02646  93.04304  11.02591  1.000 105.39796 ?  154 PHE A N   1 
ATOM   3966 C CA  . PHE C 3 141 ? 23.83766  92.21491  11.19461  1.000 112.57240 ?  154 PHE A CA  1 
ATOM   3967 C C   . PHE C 3 141 ? 23.99198  91.37289  12.45176  1.000 115.62530 ?  154 PHE A C   1 
ATOM   3968 O O   . PHE C 3 141 ? 24.91377  90.55634  12.54345  1.000 118.79413 ?  154 PHE A O   1 
ATOM   3969 C CB  . PHE C 3 141 ? 23.61795  91.31136  9.97850   1.000 107.58327 ?  154 PHE A CB  1 
ATOM   3970 C CG  . PHE C 3 141 ? 23.40946  92.05806  8.69209   1.000 101.01275 ?  154 PHE A CG  1 
ATOM   3971 C CD1 . PHE C 3 141 ? 24.48247  92.61075  8.01297   1.000 102.74713 ?  154 PHE A CD1 1 
ATOM   3972 C CD2 . PHE C 3 141 ? 22.14171  92.19410  8.15332   1.000 112.70841 ?  154 PHE A CD2 1 
ATOM   3973 C CE1 . PHE C 3 141 ? 24.29272  93.29605  6.82963   1.000 97.60790  ?  154 PHE A CE1 1 
ATOM   3974 C CE2 . PHE C 3 141 ? 21.94692  92.87591  6.96727   1.000 104.30418 ?  154 PHE A CE2 1 
ATOM   3975 C CZ  . PHE C 3 141 ? 23.02466  93.42689  6.30469   1.000 86.24078  ?  154 PHE A CZ  1 
ATOM   3976 N N   . THR C 3 142 ? 23.08591  91.56196  13.41161  1.000 117.73904 ?  155 THR A N   1 
ATOM   3977 C CA  . THR C 3 142 ? 23.07699  90.78730  14.64668  1.000 120.15867 ?  155 THR A CA  1 
ATOM   3978 C C   . THR C 3 142 ? 21.99764  89.70892  14.63731  1.000 143.02039 ?  155 THR A C   1 
ATOM   3979 O O   . THR C 3 142 ? 21.48518  89.33232  15.69638  1.000 136.94924 ?  155 THR A O   1 
ATOM   3980 C CB  . THR C 3 142 ? 22.88823  91.70821  15.85207  1.000 111.42863 ?  155 THR A CB  1 
ATOM   3981 O OG1 . THR C 3 142 ? 21.51251  92.09670  15.94209  1.000 124.61615 ?  155 THR A OG1 1 
ATOM   3982 C CG2 . THR C 3 142 ? 23.74783  92.95625  15.70832  1.000 100.08743 ?  155 THR A CG2 1 
ATOM   3983 N N   . ASP C 3 143 ? 21.65112  89.19833  13.45852  1.000 157.94496 ?  156 ASP A N   1 
ATOM   3984 C CA  . ASP C 3 143 ? 20.49814  88.31846  13.32268  1.000 150.64299 ?  156 ASP A CA  1 
ATOM   3985 C C   . ASP C 3 143 ? 20.74544  86.97317  13.99347  1.000 136.58901 ?  156 ASP A C   1 
ATOM   3986 O O   . ASP C 3 143 ? 21.82275  86.38378  13.86840  1.000 127.96700 ?  156 ASP A O   1 
ATOM   3987 C CB  . ASP C 3 143 ? 20.17034  88.10900  11.84517  1.000 141.75482 ?  156 ASP A CB  1 
ATOM   3988 C CG  . ASP C 3 143 ? 19.92211  89.41527  11.11097  1.000 133.27670 ?  156 ASP A CG  1 
ATOM   3989 O OD1 . ASP C 3 143 ? 19.14591  90.25415  11.61476  1.000 138.12312 ?  156 ASP A OD1 1 
ATOM   3990 O OD2 . ASP C 3 143 ? 20.51010  89.60391  10.02500  1.000 122.77802 ?  156 ASP A OD2 1 
ATOM   3991 N N   . PHE C 3 144 ? 19.73135  86.48669  14.71214  1.000 132.67361 ?  157 PHE A N   1 
ATOM   3992 C CA  . PHE C 3 144 ? 19.80884  85.14132  15.26913  1.000 128.11312 ?  157 PHE A CA  1 
ATOM   3993 C C   . PHE C 3 144 ? 19.72786  84.09177  14.16851  1.000 130.38320 ?  157 PHE A C   1 
ATOM   3994 O O   . PHE C 3 144 ? 20.35973  83.03316  14.26395  1.000 140.24955 ?  157 PHE A O   1 
ATOM   3995 C CB  . PHE C 3 144 ? 18.69833  84.93252  16.29864  1.000 120.11268 ?  157 PHE A CB  1 
ATOM   3996 N N   . ASP C 3 145 ? 18.96651  84.37111  13.11450  1.000 129.86134 ?  158 ASP A N   1 
ATOM   3997 C CA  . ASP C 3 145 ? 18.84319  83.45039  11.99067  1.000 133.94363 ?  158 ASP A CA  1 
ATOM   3998 C C   . ASP C 3 145 ? 18.37298  84.17957  10.73435  1.000 115.00840 ?  158 ASP A C   1 
ATOM   3999 O O   . ASP C 3 145 ? 17.22872  84.62738  10.65447  1.000 104.90699 ?  158 ASP A O   1 
ATOM   4000 C CB  . ASP C 3 145 ? 17.87967  82.31260  12.33441  1.000 135.16618 ?  158 ASP A CB  1 
ATOM   4001 C CG  . ASP C 3 145 ? 18.41747  80.95268  11.93365  1.000 130.20925 ?  158 ASP A CG  1 
ATOM   4002 O OD1 . ASP C 3 145 ? 19.51429  80.89607  11.33894  1.000 124.07399 ?  158 ASP A OD1 1 
ATOM   4003 O OD2 . ASP C 3 145 ? 17.74560  79.93937  12.21805  1.000 133.78209 ?  158 ASP A OD2 1 
ATOM   4004 N N   . SER C 3 153 ? 25.03766  86.55571  -0.15890  1.000 97.40699  ?  166 SER A N   1 
ATOM   4005 C CA  . SER C 3 153 ? 23.83665  87.13093  -0.75298  1.000 119.27538 ?  166 SER A CA  1 
ATOM   4006 C C   . SER C 3 153 ? 23.83237  86.95187  -2.26679  1.000 116.65758 ?  166 SER A C   1 
ATOM   4007 O O   . SER C 3 153 ? 24.85816  86.63293  -2.86785  1.000 111.34628 ?  166 SER A O   1 
ATOM   4008 C CB  . SER C 3 153 ? 23.72048  88.61491  -0.40066  1.000 123.60763 ?  166 SER A CB  1 
ATOM   4009 O OG  . SER C 3 153 ? 22.54450  89.18076  -0.95256  1.000 117.41289 ?  166 SER A OG  1 
ATOM   4010 N N   . LYS C 3 154 ? 22.66684  87.16351  -2.87940  1.000 120.24440 ?  167 LYS A N   1 
ATOM   4011 C CA  . LYS C 3 154 ? 22.53418  87.00727  -4.32162  1.000 127.08944 ?  167 LYS A CA  1 
ATOM   4012 C C   . LYS C 3 154 ? 23.01127  88.22892  -5.09505  1.000 121.76250 ?  167 LYS A C   1 
ATOM   4013 O O   . LYS C 3 154 ? 23.28525  88.11578  -6.29482  1.000 115.35883 ?  167 LYS A O   1 
ATOM   4014 C CB  . LYS C 3 154 ? 21.07809  86.70733  -4.68619  1.000 122.62621 ?  167 LYS A CB  1 
ATOM   4015 N N   . ASP C 3 155 ? 23.11989  89.38343  -4.44435  1.000 105.44245 ?  168 ASP A N   1 
ATOM   4016 C CA  . ASP C 3 155 ? 23.51265  90.60313  -5.13280  1.000 107.80151 ?  168 ASP A CA  1 
ATOM   4017 C C   . ASP C 3 155 ? 25.00940  90.61416  -5.42015  1.000 90.76595  ?  168 ASP A C   1 
ATOM   4018 O O   . ASP C 3 155 ? 25.81928  90.09191  -4.64859  1.000 86.44667  ?  168 ASP A O   1 
ATOM   4019 C CB  . ASP C 3 155 ? 23.12935  91.83396  -4.31027  1.000 99.90345  ?  168 ASP A CB  1 
ATOM   4020 C CG  . ASP C 3 155 ? 21.68474  92.24693  -4.51921  1.000 108.01535 ?  168 ASP A CG  1 
ATOM   4021 O OD1 . ASP C 3 155 ? 20.78200  91.45068  -4.18670  1.000 121.77743 ?  168 ASP A OD1 1 
ATOM   4022 O OD2 . ASP C 3 155 ? 21.45225  93.36886  -5.01763  1.000 102.31046 ?  168 ASP A OD2 1 
ATOM   4023 N N   . SER C 3 156 ? 25.36893  91.22092  -6.54850  1.000 83.44352  ?  169 SER A N   1 
ATOM   4024 C CA  . SER C 3 156 ? 26.76023  91.31774  -6.95675  1.000 81.12148  ?  169 SER A CA  1 
ATOM   4025 C C   . SER C 3 156 ? 27.46093  92.45187  -6.21576  1.000 83.82908  ?  169 SER A C   1 
ATOM   4026 O O   . SER C 3 156 ? 26.83275  93.40158  -5.73880  1.000 89.68355  ?  169 SER A O   1 
ATOM   4027 C CB  . SER C 3 156 ? 26.86775  91.54082  -8.46506  1.000 85.28227  ?  169 SER A CB  1 
ATOM   4028 O OG  . SER C 3 156 ? 26.30614  92.78633  -8.83667  1.000 88.38476  ?  169 SER A OG  1 
ATOM   4029 N N   . ASP C 3 157 ? 28.78829  92.33690  -6.12727  1.000 89.94405  ?  170 ASP A N   1 
ATOM   4030 C CA  . ASP C 3 157 ? 29.63400  93.31445  -5.43932  1.000 84.76442  ?  170 ASP A CA  1 
ATOM   4031 C C   . ASP C 3 157 ? 29.20783  93.51346  -3.98739  1.000 79.75345  ?  170 ASP A C   1 
ATOM   4032 O O   . ASP C 3 157 ? 29.44864  94.56888  -3.39728  1.000 88.44436  ?  170 ASP A O   1 
ATOM   4033 C CB  . ASP C 3 157 ? 29.65487  94.65473  -6.18069  1.000 81.86701  ?  170 ASP A CB  1 
ATOM   4034 C CG  . ASP C 3 157 ? 30.35205  94.56550  -7.52397  1.000 102.36607 ?  170 ASP A CG  1 
ATOM   4035 O OD1 . ASP C 3 157 ? 31.31278  93.77576  -7.64371  1.000 98.80027  ?  170 ASP A OD1 1 
ATOM   4036 O OD2 . ASP C 3 157 ? 29.93996  95.28355  -8.45950  1.000 101.15819 -1 170 ASP A OD2 1 
ATOM   4037 N N   . VAL C 3 158 ? 28.57361  92.50013  -3.40397  1.000 83.75577  ?  171 VAL A N   1 
ATOM   4038 C CA  . VAL C 3 158 ? 28.13859  92.52091  -2.01262  1.000 81.67836  ?  171 VAL A CA  1 
ATOM   4039 C C   . VAL C 3 158 ? 28.79887  91.34747  -1.30581  1.000 82.30745  ?  171 VAL A C   1 
ATOM   4040 O O   . VAL C 3 158 ? 28.57249  90.18730  -1.67265  1.000 82.39406  ?  171 VAL A O   1 
ATOM   4041 C CB  . VAL C 3 158 ? 26.60880  92.44776  -1.88711  1.000 89.43672  ?  171 VAL A CB  1 
ATOM   4042 C CG1 . VAL C 3 158 ? 26.20589  92.25486  -0.43400  1.000 92.68558  ?  171 VAL A CG1 1 
ATOM   4043 C CG2 . VAL C 3 158 ? 25.96935  93.70436  -2.45819  1.000 96.42734  ?  171 VAL A CG2 1 
ATOM   4044 N N   . TYR C 3 159 ? 29.61425  91.64668  -0.30041  1.000 76.77045  ?  172 TYR A N   1 
ATOM   4045 C CA  . TYR C 3 159 ? 30.35130  90.63754  0.44782   1.000 74.35185  ?  172 TYR A CA  1 
ATOM   4046 C C   . TYR C 3 159 ? 29.79184  90.56812  1.86105   1.000 79.79681  ?  172 TYR A C   1 
ATOM   4047 O O   . TYR C 3 159 ? 29.78645  91.57372  2.57830   1.000 91.13827  ?  172 TYR A O   1 
ATOM   4048 C CB  . TYR C 3 159 ? 31.84447  90.96130  0.47547   1.000 69.22316  ?  172 TYR A CB  1 
ATOM   4049 C CG  . TYR C 3 159 ? 32.43309  91.24945  -0.88647  1.000 77.01147  ?  172 TYR A CG  1 
ATOM   4050 C CD1 . TYR C 3 159 ? 32.81343  90.21647  -1.73260  1.000 72.98362  ?  172 TYR A CD1 1 
ATOM   4051 C CD2 . TYR C 3 159 ? 32.61070  92.55514  -1.32539  1.000 83.47525  ?  172 TYR A CD2 1 
ATOM   4052 C CE1 . TYR C 3 159 ? 33.35318  90.47469  -2.97840  1.000 81.40768  ?  172 TYR A CE1 1 
ATOM   4053 C CE2 . TYR C 3 159 ? 33.14968  92.82365  -2.56982  1.000 87.31175  ?  172 TYR A CE2 1 
ATOM   4054 C CZ  . TYR C 3 159 ? 33.51910  91.77956  -3.39182  1.000 84.46902  ?  172 TYR A CZ  1 
ATOM   4055 O OH  . TYR C 3 159 ? 34.05634  92.04053  -4.63140  1.000 90.22865  ?  172 TYR A OH  1 
ATOM   4056 N N   . ILE C 3 160 ? 29.32427  89.38726  2.25608   1.000 79.94490  ?  173 ILE A N   1 
ATOM   4057 C CA  . ILE C 3 160 ? 28.78213  89.15387  3.58958   1.000 73.29814  ?  173 ILE A CA  1 
ATOM   4058 C C   . ILE C 3 160 ? 29.67742  88.14281  4.28929   1.000 72.47411  ?  173 ILE A C   1 
ATOM   4059 O O   . ILE C 3 160 ? 29.89730  87.03944  3.77401   1.000 86.04281  ?  173 ILE A O   1 
ATOM   4060 C CB  . ILE C 3 160 ? 27.32943  88.65629  3.54120   1.000 71.07668  ?  173 ILE A CB  1 
ATOM   4061 C CG1 . ILE C 3 160 ? 26.43995  89.67685  2.82934   1.000 84.95096  ?  173 ILE A CG1 1 
ATOM   4062 C CG2 . ILE C 3 160 ? 26.81541  88.38056  4.94673   1.000 69.69747  ?  173 ILE A CG2 1 
ATOM   4063 C CD1 . ILE C 3 160 ? 24.96449  89.35674  2.90311   1.000 81.91602  ?  173 ILE A CD1 1 
ATOM   4064 N N   . THR C 3 161 ? 30.19013  88.51549  5.45783   1.000 75.42200  ?  174 THR A N   1 
ATOM   4065 C CA  . THR C 3 161 ? 31.04649  87.62082  6.21701   1.000 75.72787  ?  174 THR A CA  1 
ATOM   4066 C C   . THR C 3 161 ? 30.21115  86.63365  7.02576   1.000 87.38234  ?  174 THR A C   1 
ATOM   4067 O O   . THR C 3 161 ? 29.01910  86.83719  7.27289   1.000 96.31227  ?  174 THR A O   1 
ATOM   4068 C CB  . THR C 3 161 ? 31.96284  88.40643  7.15658   1.000 80.07191  ?  174 THR A CB  1 
ATOM   4069 O OG1 . THR C 3 161 ? 31.18344  88.99202  8.20715   1.000 81.69476  ?  174 THR A OG1 1 
ATOM   4070 C CG2 . THR C 3 161 ? 32.68913  89.50652  6.39872   1.000 79.33295  ?  174 THR A CG2 1 
ATOM   4071 N N   . ASP C 3 162 ? 30.85919  85.54676  7.43242   1.000 90.25010  ?  175 ASP A N   1 
ATOM   4072 C CA  . ASP C 3 162 ? 30.22587  84.57875  8.31259   1.000 87.19404  ?  175 ASP A CA  1 
ATOM   4073 C C   . ASP C 3 162 ? 29.99075  85.19830  9.68599   1.000 97.23752  ?  175 ASP A C   1 
ATOM   4074 O O   . ASP C 3 162 ? 30.77659  86.02124  10.16355  1.000 107.73643 ?  175 ASP A O   1 
ATOM   4075 C CB  . ASP C 3 162 ? 31.09678  83.32938  8.43748   1.000 110.01806 ?  175 ASP A CB  1 
ATOM   4076 C CG  . ASP C 3 162 ? 31.88528  83.04155  7.17258   1.000 121.80875 ?  175 ASP A CG  1 
ATOM   4077 O OD1 . ASP C 3 162 ? 32.60109  83.95002  6.69877   1.000 104.69806 ?  175 ASP A OD1 1 
ATOM   4078 O OD2 . ASP C 3 162 ? 31.79807  81.90764  6.65667   1.000 128.08916 -1 175 ASP A OD2 1 
ATOM   4079 N N   . LYS C 3 163 ? 28.89223  84.79817  10.32093  1.000 94.43212  ?  176 LYS A N   1 
ATOM   4080 C CA  . LYS C 3 163 ? 28.52231  85.37377  11.60764  1.000 100.36774 ?  176 LYS A CA  1 
ATOM   4081 C C   . LYS C 3 163 ? 29.52149  84.97026  12.68560  1.000 98.17189  ?  176 LYS A C   1 
ATOM   4082 O O   . LYS C 3 163 ? 29.78105  83.78112  12.89459  1.000 91.37873  ?  176 LYS A O   1 
ATOM   4083 C CB  . LYS C 3 163 ? 27.11368  84.93122  12.00107  1.000 90.80704  ?  176 LYS A CB  1 
ATOM   4084 N N   . CYS C 3 164 ? 30.08336  85.96468  13.36963  1.000 104.98505 ?  177 CYS A N   1 
ATOM   4085 C CA  . CYS C 3 164 ? 30.98382  85.70073  14.48230  1.000 107.94461 ?  177 CYS A CA  1 
ATOM   4086 C C   . CYS C 3 164 ? 30.19447  85.32469  15.72935  1.000 120.90465 ?  177 CYS A C   1 
ATOM   4087 O O   . CYS C 3 164 ? 29.10020  85.84303  15.97126  1.000 118.08904 ?  177 CYS A O   1 
ATOM   4088 C CB  . CYS C 3 164 ? 31.86289  86.91688  14.77671  1.000 85.34800  ?  177 CYS A CB  1 
ATOM   4089 S SG  . CYS C 3 164 ? 32.39300  86.97842  16.50649  1.000 140.53809 ?  177 CYS A SG  1 
ATOM   4090 N N   . VAL C 3 165 ? 30.76235  84.41902  16.52564  1.000 113.65951 ?  178 VAL A N   1 
ATOM   4091 C CA  . VAL C 3 165 ? 30.09729  83.97531  17.74581  1.000 109.02292 ?  178 VAL A CA  1 
ATOM   4092 C C   . VAL C 3 165 ? 30.26792  85.00280  18.85701  1.000 125.46033 ?  178 VAL A C   1 
ATOM   4093 O O   . VAL C 3 165 ? 29.30772  85.34176  19.55836  1.000 124.61436 ?  178 VAL A O   1 
ATOM   4094 C CB  . VAL C 3 165 ? 30.62864  82.59396  18.16882  1.000 125.97824 ?  178 VAL A CB  1 
ATOM   4095 N N   . LEU C 3 166 ? 31.48831  85.50786  19.02993  1.000 129.98613 ?  179 LEU A N   1 
ATOM   4096 C CA  . LEU C 3 166 ? 31.81135  86.49655  20.06062  1.000 128.79742 ?  179 LEU A CA  1 
ATOM   4097 C C   . LEU C 3 166 ? 31.40450  86.02230  21.45311  1.000 128.86927 ?  179 LEU A C   1 
ATOM   4098 O O   . LEU C 3 166 ? 30.67410  86.71091  22.16456  1.000 133.42712 ?  179 LEU A O   1 
ATOM   4099 C CB  . LEU C 3 166 ? 31.14406  87.83998  19.74982  1.000 118.91179 ?  179 LEU A CB  1 
ATOM   4100 N N   . LYS C 3 174 ? 25.49048  85.22035  24.50561  1.000 110.37077 ?  187 LYS A N   1 
ATOM   4101 C CA  . LYS C 3 174 ? 26.43772  85.49922  23.43241  1.000 105.65733 ?  187 LYS A CA  1 
ATOM   4102 C C   . LYS C 3 174 ? 25.79167  86.35003  22.34414  1.000 115.38233 ?  187 LYS A C   1 
ATOM   4103 O O   . LYS C 3 174 ? 24.61103  86.18824  22.03549  1.000 116.37307 ?  187 LYS A O   1 
ATOM   4104 C CB  . LYS C 3 174 ? 26.97371  84.19613  22.83682  1.000 104.56008 ?  187 LYS A CB  1 
ATOM   4105 N N   . SER C 3 175 ? 26.57492  87.25368  21.76232  1.000 118.94964 ?  188 SER A N   1 
ATOM   4106 C CA  . SER C 3 175 ? 26.09303  88.19442  20.75885  1.000 99.02454  ?  188 SER A CA  1 
ATOM   4107 C C   . SER C 3 175 ? 26.70860  87.84761  19.41009  1.000 96.59467  ?  188 SER A C   1 
ATOM   4108 O O   . SER C 3 175 ? 27.93563  87.77705  19.28428  1.000 114.57675 ?  188 SER A O   1 
ATOM   4109 C CB  . SER C 3 175 ? 26.43763  89.63056  21.15184  1.000 102.95452 ?  188 SER A CB  1 
ATOM   4110 O OG  . SER C 3 175 ? 25.98740  89.92299  22.46321  1.000 124.06698 ?  188 SER A OG  1 
ATOM   4111 N N   . ASN C 3 176 ? 25.86005  87.63868  18.40888  1.000 93.55082  ?  189 ASN A N   1 
ATOM   4112 C CA  . ASN C 3 176 ? 26.30093  87.34183  17.05479  1.000 97.74720  ?  189 ASN A CA  1 
ATOM   4113 C C   . ASN C 3 176 ? 26.32710  88.61562  16.21936  1.000 100.15488 ?  189 ASN A C   1 
ATOM   4114 O O   . ASN C 3 176 ? 25.56405  89.55437  16.46101  1.000 104.50198 ?  189 ASN A O   1 
ATOM   4115 C CB  . ASN C 3 176 ? 25.38619  86.30678  16.39611  1.000 86.73314  ?  189 ASN A CB  1 
ATOM   4116 C CG  . ASN C 3 176 ? 25.31836  85.00851  17.17614  1.000 120.25941 ?  189 ASN A CG  1 
ATOM   4117 O OD1 . ASN C 3 176 ? 24.26526  84.63665  17.69391  1.000 132.05772 ?  189 ASN A OD1 1 
ATOM   4118 N ND2 . ASN C 3 176 ? 26.44441  84.30963  17.26217  1.000 118.55779 ?  189 ASN A ND2 1 
ATOM   4119 N N   . SER C 3 177 ? 27.21713  88.63960  15.22869  1.000 97.96328  ?  190 SER A N   1 
ATOM   4120 C CA  . SER C 3 177 ? 27.34136  89.79921  14.35453  1.000 91.51691  ?  190 SER A CA  1 
ATOM   4121 C C   . SER C 3 177 ? 28.00827  89.37891  13.05425  1.000 94.12432  ?  190 SER A C   1 
ATOM   4122 O O   . SER C 3 177 ? 29.05464  88.72398  13.07566  1.000 95.98493  ?  190 SER A O   1 
ATOM   4123 C CB  . SER C 3 177 ? 28.14228  90.91769  15.02953  1.000 95.46164  ?  190 SER A CB  1 
ATOM   4124 O OG  . SER C 3 177 ? 29.42708  90.46244  15.41162  1.000 110.58968 ?  190 SER A OG  1 
ATOM   4125 N N   . ALA C 3 178 ? 27.40112  89.75668  11.93187  1.000 101.24011 ?  191 ALA A N   1 
ATOM   4126 C CA  . ALA C 3 178 ? 27.94540  89.50363  10.60600  1.000 95.41865  ?  191 ALA A CA  1 
ATOM   4127 C C   . ALA C 3 178 ? 28.15017  90.82841  9.88575   1.000 93.31328  ?  191 ALA A C   1 
ATOM   4128 O O   . ALA C 3 178 ? 27.31915  91.73634  9.98906   1.000 98.53658  ?  191 ALA A O   1 
ATOM   4129 C CB  . ALA C 3 178 ? 27.02252  88.59559  9.78700   1.000 84.49427  ?  191 ALA A CB  1 
ATOM   4130 N N   . VAL C 3 179 ? 29.25765  90.93508  9.15648   1.000 90.06033  ?  192 VAL A N   1 
ATOM   4131 C CA  . VAL C 3 179 ? 29.64126  92.16747  8.47700   1.000 85.47337  ?  192 VAL A CA  1 
ATOM   4132 C C   . VAL C 3 179 ? 29.34683  92.02671  6.99081   1.000 85.90618  ?  192 VAL A C   1 
ATOM   4133 O O   . VAL C 3 179 ? 29.72674  91.02925  6.36403   1.000 72.52761  ?  192 VAL A O   1 
ATOM   4134 C CB  . VAL C 3 179 ? 31.12587  92.49435  8.71342   1.000 85.75344  ?  192 VAL A CB  1 
ATOM   4135 C CG1 . VAL C 3 179 ? 31.51969  93.75668  7.96147   1.000 82.95700  ?  192 VAL A CG1 1 
ATOM   4136 C CG2 . VAL C 3 179 ? 31.40500  92.64646  10.19948  1.000 80.27570  ?  192 VAL A CG2 1 
ATOM   4137 N N   . ALA C 3 180 ? 28.67107  93.02490  6.42661   1.000 82.41207  ?  193 ALA A N   1 
ATOM   4138 C CA  . ALA C 3 180 ? 28.40234  93.08733  4.99839   1.000 84.57923  ?  193 ALA A CA  1 
ATOM   4139 C C   . ALA C 3 180 ? 28.74943  94.47490  4.48333   1.000 88.94431  ?  193 ALA A C   1 
ATOM   4140 O O   . ALA C 3 180 ? 28.44439  95.48115  5.13063   1.000 93.33783  ?  193 ALA A O   1 
ATOM   4141 C CB  . ALA C 3 180 ? 26.93988  92.76219  4.68330   1.000 84.86438  ?  193 ALA A CB  1 
ATOM   4142 N N   . TRP C 3 181 ? 29.39070  94.52391  3.31821   1.000 87.20129  ?  194 TRP A N   1 
ATOM   4143 C CA  . TRP C 3 181 ? 29.79048  95.79199  2.72952   1.000 95.26896  ?  194 TRP A CA  1 
ATOM   4144 C C   . TRP C 3 181 ? 29.68647  95.69670  1.21542   1.000 99.89707  ?  194 TRP A C   1 
ATOM   4145 O O   . TRP C 3 181 ? 29.63729  94.60553  0.64145   1.000 92.89366  ?  194 TRP A O   1 
ATOM   4146 C CB  . TRP C 3 181 ? 31.21451  96.18409  3.14348   1.000 91.82380  ?  194 TRP A CB  1 
ATOM   4147 C CG  . TRP C 3 181 ? 32.28713  95.40757  2.43800   1.000 85.20957  ?  194 TRP A CG  1 
ATOM   4148 C CD1 . TRP C 3 181 ? 32.92601  95.75675  1.28354   1.000 87.41771  ?  194 TRP A CD1 1 
ATOM   4149 C CD2 . TRP C 3 181 ? 32.84938  94.15327  2.84296   1.000 79.41531  ?  194 TRP A CD2 1 
ATOM   4150 N NE1 . TRP C 3 181 ? 33.84883  94.79833  0.94386   1.000 78.01205  ?  194 TRP A NE1 1 
ATOM   4151 C CE2 . TRP C 3 181 ? 33.82187  93.80323  1.88496   1.000 82.02616  ?  194 TRP A CE2 1 
ATOM   4152 C CE3 . TRP C 3 181 ? 32.62503  93.29259  3.92158   1.000 77.81320  ?  194 TRP A CE3 1 
ATOM   4153 C CZ2 . TRP C 3 181 ? 34.56890  92.63069  1.97325   1.000 80.96865  ?  194 TRP A CZ2 1 
ATOM   4154 C CZ3 . TRP C 3 181 ? 33.36708  92.12826  4.00649   1.000 83.50765  ?  194 TRP A CZ3 1 
ATOM   4155 C CH2 . TRP C 3 181 ? 34.32700  91.80824  3.03832   1.000 76.91807  ?  194 TRP A CH2 1 
ATOM   4156 N N   . SER C 3 182 ? 29.65671  96.86200  0.57455   1.000 99.71388  ?  195 SER A N   1 
ATOM   4157 C CA  . SER C 3 182 ? 29.60177  96.93893  -0.87698  1.000 93.87637  ?  195 SER A CA  1 
ATOM   4158 C C   . SER C 3 182 ? 30.13953  98.29239  -1.31244  1.000 101.02415 ?  195 SER A C   1 
ATOM   4159 O O   . SER C 3 182 ? 30.00898  99.28678  -0.59392  1.000 111.30885 ?  195 SER A O   1 
ATOM   4160 C CB  . SER C 3 182 ? 28.17704  96.73335  -1.40068  1.000 101.56168 ?  195 SER A CB  1 
ATOM   4161 O OG  . SER C 3 182 ? 28.14023  96.81848  -2.81360  1.000 105.86321 ?  195 SER A OG  1 
ATOM   4162 N N   . ASN C 3 183 ? 30.74391  98.31699  -2.49764  1.000 106.80254 ?  196 ASN A N   1 
ATOM   4163 C CA  . ASN C 3 183 ? 31.35456  99.52383  -3.03541  1.000 111.84319 ?  196 ASN A CA  1 
ATOM   4164 C C   . ASN C 3 183 ? 30.52583  100.17957 -4.13186  1.000 109.46139 ?  196 ASN A C   1 
ATOM   4165 O O   . ASN C 3 183 ? 30.94985  101.20266 -4.67773  1.000 120.53149 ?  196 ASN A O   1 
ATOM   4166 C CB  . ASN C 3 183 ? 32.75925  99.21160  -3.56182  1.000 114.63958 ?  196 ASN A CB  1 
ATOM   4167 C CG  . ASN C 3 183 ? 32.80481  97.93567  -4.37655  1.000 118.21852 ?  196 ASN A CG  1 
ATOM   4168 O OD1 . ASN C 3 183 ? 32.91681  96.83949  -3.82709  1.000 112.65051 ?  196 ASN A OD1 1 
ATOM   4169 N ND2 . ASN C 3 183 ? 32.72059  98.07093  -5.69465  1.000 111.65207 ?  196 ASN A ND2 1 
ATOM   4170 N N   . LYS C 3 184 ? 29.36487  99.62514  -4.46958  1.000 115.51032 ?  197 LYS A N   1 
ATOM   4171 C CA  . LYS C 3 184 ? 28.48525  100.27479 -5.42860  1.000 116.61503 ?  197 LYS A CA  1 
ATOM   4172 C C   . LYS C 3 184 ? 27.67834  101.37095 -4.74165  1.000 123.71689 ?  197 LYS A C   1 
ATOM   4173 O O   . LYS C 3 184 ? 27.34635  101.27933 -3.55597  1.000 122.35402 ?  197 LYS A O   1 
ATOM   4174 C CB  . LYS C 3 184 ? 27.55647  99.25818  -6.09631  1.000 117.53004 ?  197 LYS A CB  1 
ATOM   4175 C CG  . LYS C 3 184 ? 26.69961  98.44167  -5.14555  1.000 114.16475 ?  197 LYS A CG  1 
ATOM   4176 C CD  . LYS C 3 184 ? 25.97269  97.33559  -5.89800  1.000 94.59113  ?  197 LYS A CD  1 
ATOM   4177 C CE  . LYS C 3 184 ? 25.15064  96.46462  -4.96378  1.000 105.55235 ?  197 LYS A CE  1 
ATOM   4178 N NZ  . LYS C 3 184 ? 24.50807  95.33441  -5.69090  1.000 88.80674  ?  197 LYS A NZ  1 
ATOM   4179 N N   . SER C 3 185 ? 27.36732  102.41961 -5.50758  1.000 141.28147 ?  198 SER A N   1 
ATOM   4180 C CA  . SER C 3 185 ? 26.80879  103.63621 -4.92322  1.000 139.29325 ?  198 SER A CA  1 
ATOM   4181 C C   . SER C 3 185 ? 25.43838  103.38448 -4.30541  1.000 131.97567 ?  198 SER A C   1 
ATOM   4182 O O   . SER C 3 185 ? 25.20631  103.69948 -3.13249  1.000 130.27868 ?  198 SER A O   1 
ATOM   4183 C CB  . SER C 3 185 ? 26.72772  104.73369 -5.98507  1.000 111.41361 ?  198 SER A CB  1 
ATOM   4184 N N   . ASP C 3 186 ? 24.51562  102.81824 -5.07952  1.000 134.34803 ?  199 ASP A N   1 
ATOM   4185 C CA  . ASP C 3 186 ? 23.13823  102.62680 -4.62411  1.000 134.93663 ?  199 ASP A CA  1 
ATOM   4186 C C   . ASP C 3 186 ? 23.00136  101.32746 -3.82638  1.000 136.72358 ?  199 ASP A C   1 
ATOM   4187 O O   . ASP C 3 186 ? 22.24384  100.42202 -4.17309  1.000 131.26929 ?  199 ASP A O   1 
ATOM   4188 C CB  . ASP C 3 186 ? 22.18417  102.65110 -5.81286  1.000 117.86984 ?  199 ASP A CB  1 
ATOM   4189 N N   . PHE C 3 187 ? 23.75157  101.25190 -2.72929  1.000 136.06183 ?  200 PHE A N   1 
ATOM   4190 C CA  . PHE C 3 187 ? 23.69588  100.11807 -1.81612  1.000 133.26400 ?  200 PHE A CA  1 
ATOM   4191 C C   . PHE C 3 187 ? 23.19708  100.58560 -0.45732  1.000 128.17543 ?  200 PHE A C   1 
ATOM   4192 O O   . PHE C 3 187 ? 23.73284  101.54331 0.11114   1.000 126.09967 ?  200 PHE A O   1 
ATOM   4193 C CB  . PHE C 3 187 ? 25.06356  99.44440  -1.67251  1.000 133.00287 ?  200 PHE A CB  1 
ATOM   4194 C CG  . PHE C 3 187 ? 25.08807  98.33466  -0.65588  1.000 129.42695 ?  200 PHE A CG  1 
ATOM   4195 C CD1 . PHE C 3 187 ? 24.36328  97.17155  -0.86090  1.000 120.83980 ?  200 PHE A CD1 1 
ATOM   4196 C CD2 . PHE C 3 187 ? 25.83979  98.45232  0.50089   1.000 127.45966 ?  200 PHE A CD2 1 
ATOM   4197 C CE1 . PHE C 3 187 ? 24.38497  96.14987  0.07171   1.000 110.92906 ?  200 PHE A CE1 1 
ATOM   4198 C CE2 . PHE C 3 187 ? 25.86824  97.43345  1.43603   1.000 119.91554 ?  200 PHE A CE2 1 
ATOM   4199 C CZ  . PHE C 3 187 ? 25.13912  96.28114  1.22111   1.000 112.37664 ?  200 PHE A CZ  1 
ATOM   4200 N N   . ALA C 3 188 ? 22.17241  99.90905  0.05531   1.000 102.11450 ?  201 ALA A N   1 
ATOM   4201 C CA  . ALA C 3 188 ? 21.60699  100.20197 1.36197   1.000 107.19447 ?  201 ALA A CA  1 
ATOM   4202 C C   . ALA C 3 188 ? 21.52903  98.92103  2.17696   1.000 120.27031 ?  201 ALA A C   1 
ATOM   4203 O O   . ALA C 3 188 ? 21.42138  97.82247  1.62402   1.000 124.56191 ?  201 ALA A O   1 
ATOM   4204 C CB  . ALA C 3 188 ? 20.21019  100.82678 1.24892   1.000 118.17298 ?  201 ALA A CB  1 
ATOM   4205 N N   . CYS C 3 189 ? 21.59186  99.07537  3.50238   1.000 115.76088 ?  202 CYS A N   1 
ATOM   4206 C CA  . CYS C 3 189 ? 21.40847  97.93581  4.39594   1.000 113.67005 ?  202 CYS A CA  1 
ATOM   4207 C C   . CYS C 3 189 ? 20.10352  97.21197  4.08872   1.000 129.54560 ?  202 CYS A C   1 
ATOM   4208 O O   . CYS C 3 189 ? 20.08087  95.98547  3.93326   1.000 106.36313 ?  202 CYS A O   1 
ATOM   4209 C CB  . CYS C 3 189 ? 21.43882  98.40327  5.85152   1.000 114.99522 ?  202 CYS A CB  1 
ATOM   4210 N N   . ALA C 3 190 ? 19.00852  97.96581  3.99507   1.000 144.43651 ?  203 ALA A N   1 
ATOM   4211 C CA  . ALA C 3 190 ? 17.71958  97.46987  3.51101   1.000 130.61165 ?  203 ALA A CA  1 
ATOM   4212 C C   . ALA C 3 190 ? 17.26733  96.18930  4.20615   1.000 136.99836 ?  203 ALA A C   1 
ATOM   4213 O O   . ALA C 3 190 ? 17.19971  95.12944  3.58299   1.000 144.41163 ?  203 ALA A O   1 
ATOM   4214 C CB  . ALA C 3 190 ? 17.78054  97.25418  2.00414   1.000 139.26888 ?  203 ALA A CB  1 
ATOM   4215 N N   . VAL D 4 2   ? 51.72347  75.80105  29.27699  1.000 135.63081 ?  1   VAL B N   1 
ATOM   4216 C CA  . VAL D 4 2   ? 52.25816  76.79044  28.34997  1.000 127.50164 ?  1   VAL B CA  1 
ATOM   4217 C C   . VAL D 4 2   ? 52.73282  76.11592  27.06780  1.000 109.95215 ?  1   VAL B C   1 
ATOM   4218 O O   . VAL D 4 2   ? 52.41567  74.95443  26.81207  1.000 112.27383 ?  1   VAL B O   1 
ATOM   4219 C CB  . VAL D 4 2   ? 53.39845  77.59694  28.99463  1.000 116.25536 ?  1   VAL B CB  1 
ATOM   4220 C CG1 . VAL D 4 2   ? 52.87305  78.41191  30.16602  1.000 98.59764  ?  1   VAL B CG1 1 
ATOM   4221 C CG2 . VAL D 4 2   ? 54.51784  76.66839  29.44379  1.000 103.47648 ?  1   VAL B CG2 1 
ATOM   4222 N N   . THR D 4 3   ? 53.49554  76.85337  26.26467  1.000 101.50376 ?  2   THR B N   1 
ATOM   4223 C CA  . THR D 4 3   ? 54.00624  76.33364  25.00265  1.000 100.37592 ?  2   THR B CA  1 
ATOM   4224 C C   . THR D 4 3   ? 55.27242  75.52302  25.25367  1.000 96.74798  ?  2   THR B C   1 
ATOM   4225 O O   . THR D 4 3   ? 56.28077  76.06207  25.72339  1.000 100.72034 ?  2   THR B O   1 
ATOM   4226 C CB  . THR D 4 3   ? 54.28694  77.47449  24.02725  1.000 98.59094  ?  2   THR B CB  1 
ATOM   4227 O OG1 . THR D 4 3   ? 55.22711  78.38493  24.61104  1.000 82.88662  ?  2   THR B OG1 1 
ATOM   4228 C CG2 . THR D 4 3   ? 53.00241  78.22088  23.69707  1.000 114.36214 ?  2   THR B CG2 1 
ATOM   4229 N N   . LEU D 4 4   ? 55.21873  74.22970  24.94126  1.000 87.27166  ?  3   LEU B N   1 
ATOM   4230 C CA  . LEU D 4 4   ? 56.37409  73.35222  25.06021  1.000 77.83253  ?  3   LEU B CA  1 
ATOM   4231 C C   . LEU D 4 4   ? 57.28196  73.39970  23.83926  1.000 64.25718  ?  3   LEU B C   1 
ATOM   4232 O O   . LEU D 4 4   ? 58.38281  72.83975  23.88288  1.000 64.25937  ?  3   LEU B O   1 
ATOM   4233 C CB  . LEU D 4 4   ? 55.91914  71.90669  25.29243  1.000 68.80308  ?  3   LEU B CB  1 
ATOM   4234 C CG  . LEU D 4 4   ? 54.97583  71.65946  26.47114  1.000 84.23483  ?  3   LEU B CG  1 
ATOM   4235 C CD1 . LEU D 4 4   ? 54.57170  70.19405  26.53700  1.000 67.60246  ?  3   LEU B CD1 1 
ATOM   4236 C CD2 . LEU D 4 4   ? 55.62011  72.10204  27.77510  1.000 108.29618 ?  3   LEU B CD2 1 
ATOM   4237 N N   . LEU D 4 5   ? 56.85207  74.04826  22.75995  1.000 59.42803  ?  4   LEU B N   1 
ATOM   4238 C CA  . LEU D 4 5   ? 57.60954  74.11056  21.52053  1.000 50.68211  ?  4   LEU B CA  1 
ATOM   4239 C C   . LEU D 4 5   ? 57.67023  75.54731  21.02273  1.000 63.70078  ?  4   LEU B C   1 
ATOM   4240 O O   . LEU D 4 5   ? 57.03193  76.45177  21.56800  1.000 86.09689  ?  4   LEU B O   1 
ATOM   4241 C CB  . LEU D 4 5   ? 56.99394  73.21131  20.44077  1.000 49.18744  ?  4   LEU B CB  1 
ATOM   4242 C CG  . LEU D 4 5   ? 57.16063  71.70405  20.61347  1.000 64.31044  ?  4   LEU B CG  1 
ATOM   4243 C CD1 . LEU D 4 5   ? 56.35047  70.96264  19.56579  1.000 72.77387  ?  4   LEU B CD1 1 
ATOM   4244 C CD2 . LEU D 4 5   ? 58.62861  71.32096  20.52737  1.000 77.93000  ?  4   LEU B CD2 1 
ATOM   4245 N N   . GLU D 4 6   ? 58.45355  75.74190  19.96488  1.000 54.74273  ?  5   GLU B N   1 
ATOM   4246 C CA  . GLU D 4 6   ? 58.57118  77.04026  19.30794  1.000 63.10945  ?  5   GLU B CA  1 
ATOM   4247 C C   . GLU D 4 6   ? 58.93837  76.77675  17.85555  1.000 64.07359  ?  5   GLU B C   1 
ATOM   4248 O O   . GLU D 4 6   ? 60.03517  76.28558  17.57288  1.000 68.72762  ?  5   GLU B O   1 
ATOM   4249 C CB  . GLU D 4 6   ? 59.61491  77.91868  19.99282  1.000 66.77549  ?  5   GLU B CB  1 
ATOM   4250 N N   . GLN D 4 7   ? 58.02292  77.09002  16.94341  1.000 65.43697  ?  6   GLN B N   1 
ATOM   4251 C CA  . GLN D 4 7   ? 58.20828  76.84604  15.52020  1.000 57.38095  ?  6   GLN B CA  1 
ATOM   4252 C C   . GLN D 4 7   ? 58.12425  78.16636  14.77035  1.000 79.02958  ?  6   GLN B C   1 
ATOM   4253 O O   . GLN D 4 7   ? 57.18949  78.94650  14.98113  1.000 73.42986  ?  6   GLN B O   1 
ATOM   4254 C CB  . GLN D 4 7   ? 57.15979  75.86454  14.99155  1.000 63.33132  ?  6   GLN B CB  1 
ATOM   4255 C CG  . GLN D 4 7   ? 57.30580  75.52719  13.51883  1.000 59.97889  ?  6   GLN B CG  1 
ATOM   4256 C CD  . GLN D 4 7   ? 56.19465  74.62500  13.02157  1.000 63.86043  ?  6   GLN B CD  1 
ATOM   4257 O OE1 . GLN D 4 7   ? 55.27946  74.28013  13.76893  1.000 61.05370  ?  6   GLN B OE1 1 
ATOM   4258 N NE2 . GLN D 4 7   ? 56.26843  74.23759  11.75386  1.000 71.54820  ?  6   GLN B NE2 1 
ATOM   4259 N N   . ASN D 4 8   ? 59.10125  78.41251  13.89777  1.000 87.14258  ?  7   ASN B N   1 
ATOM   4260 C CA  . ASN D 4 8   ? 59.16564  79.63512  13.11748  1.000 73.63994  ?  7   ASN B CA  1 
ATOM   4261 C C   . ASN D 4 8   ? 59.55509  79.29169  11.68644  1.000 79.83543  ?  7   ASN B C   1 
ATOM   4262 O O   . ASN D 4 8   ? 60.36580  78.37897  11.46638  1.000 74.19137  ?  7   ASN B O   1 
ATOM   4263 C CB  . ASN D 4 8   ? 60.17691  80.62782  13.70797  1.000 101.61018 ?  7   ASN B CB  1 
ATOM   4264 C CG  . ASN D 4 8   ? 59.93917  80.89421  15.18165  1.000 103.71857 ?  7   ASN B CG  1 
ATOM   4265 O OD1 . ASN D 4 8   ? 59.11581  81.73296  15.54846  1.000 86.73347  ?  7   ASN B OD1 1 
ATOM   4266 N ND2 . ASN D 4 8   ? 60.66232  80.17860  16.03616  1.000 94.96079  ?  7   ASN B ND2 1 
ATOM   4267 N N   . PRO D 4 9   ? 59.00059  79.99974  10.69488  1.000 75.18017  ?  8   PRO B N   1 
ATOM   4268 C CA  . PRO D 4 9   ? 58.02292  81.08995  10.80691  1.000 82.72224  ?  8   PRO B CA  1 
ATOM   4269 C C   . PRO D 4 9   ? 56.58319  80.58796  10.83766  1.000 82.21715  ?  8   PRO B C   1 
ATOM   4270 O O   . PRO D 4 9   ? 56.33380  79.38600  10.81517  1.000 75.57941  ?  8   PRO B O   1 
ATOM   4271 C CB  . PRO D 4 9   ? 58.30879  81.91850  9.55146   1.000 94.90511  ?  8   PRO B CB  1 
ATOM   4272 C CG  . PRO D 4 9   ? 58.69098  80.88009  8.53306   1.000 80.35346  ?  8   PRO B CG  1 
ATOM   4273 C CD  . PRO D 4 9   ? 59.45234  79.82023  9.30252   1.000 69.18710  ?  8   PRO B CD  1 
ATOM   4274 N N   . ARG D 4 10  ? 55.61355  81.50120  10.88834  1.000 72.06960  ?  9   ARG B N   1 
ATOM   4275 C CA  . ARG D 4 10  ? 54.20346  81.13186  10.88048  1.000 71.78331  ?  9   ARG B CA  1 
ATOM   4276 C C   . ARG D 4 10  ? 53.65232  81.00170  9.46585   1.000 70.76459  ?  9   ARG B C   1 
ATOM   4277 O O   . ARG D 4 10  ? 52.86879  80.08726  9.18786   1.000 71.96946  ?  9   ARG B O   1 
ATOM   4278 C CB  . ARG D 4 10  ? 53.38567  82.16290  11.66323  1.000 85.94426  ?  9   ARG B CB  1 
ATOM   4279 C CG  . ARG D 4 10  ? 51.93552  81.76731  11.89293  1.000 89.01509  ?  9   ARG B CG  1 
ATOM   4280 C CD  . ARG D 4 10  ? 51.81460  80.62925  12.89876  1.000 97.87070  ?  9   ARG B CD  1 
ATOM   4281 N NE  . ARG D 4 10  ? 52.24389  81.02663  14.23510  1.000 96.87553  ?  9   ARG B NE  1 
ATOM   4282 C CZ  . ARG D 4 10  ? 53.42385  80.73255  14.76476  1.000 100.60632 ?  9   ARG B CZ  1 
ATOM   4283 N NH1 . ARG D 4 10  ? 54.32154  80.02128  14.10231  1.000 90.86448  ?  9   ARG B NH1 1 
ATOM   4284 N NH2 . ARG D 4 10  ? 53.70784  81.15753  15.99269  1.000 112.69801 ?  9   ARG B NH2 1 
ATOM   4285 N N   . TRP D 4 11  ? 54.04741  81.90103  8.56747   1.000 74.39791  ?  10  TRP B N   1 
ATOM   4286 C CA  . TRP D 4 11  ? 53.61331  81.87601  7.18003   1.000 60.85247  ?  10  TRP B CA  1 
ATOM   4287 C C   . TRP D 4 11  ? 54.83501  81.86822  6.27278   1.000 59.08266  ?  10  TRP B C   1 
ATOM   4288 O O   . TRP D 4 11  ? 55.92990  82.27573  6.66875   1.000 52.31367  ?  10  TRP B O   1 
ATOM   4289 C CB  . TRP D 4 11  ? 52.72271  83.08022  6.84331   1.000 71.17670  ?  10  TRP B CB  1 
ATOM   4290 C CG  . TRP D 4 11  ? 51.75334  83.43460  7.92581   1.000 76.22997  ?  10  TRP B CG  1 
ATOM   4291 C CD1 . TRP D 4 11  ? 51.96203  84.29893  8.96013   1.000 86.10683  ?  10  TRP B CD1 1 
ATOM   4292 C CD2 . TRP D 4 11  ? 50.41972  82.93631  8.08228   1.000 76.94170  ?  10  TRP B CD2 1 
ATOM   4293 N NE1 . TRP D 4 11  ? 50.84175  84.36991  9.75175   1.000 107.04193 ?  10  TRP B NE1 1 
ATOM   4294 C CE2 . TRP D 4 11  ? 49.88029  83.54239  9.23444   1.000 91.95477  ?  10  TRP B CE2 1 
ATOM   4295 C CE3 . TRP D 4 11  ? 49.62968  82.03663  7.36089   1.000 86.20599  ?  10  TRP B CE3 1 
ATOM   4296 C CZ2 . TRP D 4 11  ? 48.58767  83.27769  9.68171   1.000 93.45961  ?  10  TRP B CZ2 1 
ATOM   4297 C CZ3 . TRP D 4 11  ? 48.34653  81.77547  7.80665   1.000 98.48003  ?  10  TRP B CZ3 1 
ATOM   4298 C CH2 . TRP D 4 11  ? 47.83851  82.39345  8.95581   1.000 96.30371  ?  10  TRP B CH2 1 
ATOM   4299 N N   . ARG D 4 12  ? 54.63367  81.40348  5.04070   1.000 63.05642  ?  11  ARG B N   1 
ATOM   4300 C CA  . ARG D 4 12  ? 55.71449  81.35105  4.06414   1.000 53.74739  ?  11  ARG B CA  1 
ATOM   4301 C C   . ARG D 4 12  ? 55.13319  81.36213  2.66089   1.000 73.95607  ?  11  ARG B C   1 
ATOM   4302 O O   . ARG D 4 12  ? 54.26010  80.54922  2.34277   1.000 74.50430  ?  11  ARG B O   1 
ATOM   4303 C CB  . ARG D 4 12  ? 56.58056  80.10509  4.25890   1.000 59.27245  ?  11  ARG B CB  1 
ATOM   4304 C CG  . ARG D 4 12  ? 57.83268  80.35161  5.06303   1.000 69.77850  ?  11  ARG B CG  1 
ATOM   4305 C CD  . ARG D 4 12  ? 58.69527  81.42256  4.41918   1.000 74.61828  ?  11  ARG B CD  1 
ATOM   4306 N NE  . ARG D 4 12  ? 59.83083  81.75656  5.26776   1.000 97.58722  ?  11  ARG B NE  1 
ATOM   4307 C CZ  . ARG D 4 12  ? 60.92569  81.01716  5.37220   1.000 108.68858 ?  11  ARG B CZ  1 
ATOM   4308 N NH1 . ARG D 4 12  ? 61.07915  79.90680  4.66982   1.000 113.12745 ?  11  ARG B NH1 1 
ATOM   4309 N NH2 . ARG D 4 12  ? 61.88564  81.39543  6.20985   1.000 108.89541 ?  11  ARG B NH2 1 
ATOM   4310 N N   . LEU D 4 13  ? 55.62568  82.27397  1.82892   1.000 73.75515  ?  12  LEU B N   1 
ATOM   4311 C CA  . LEU D 4 13  ? 55.28574  82.31598  0.41397   1.000 71.67278  ?  12  LEU B CA  1 
ATOM   4312 C C   . LEU D 4 13  ? 56.40331  81.63318  -0.36441  1.000 73.49923  ?  12  LEU B C   1 
ATOM   4313 O O   . LEU D 4 13  ? 57.54825  82.09861  -0.35083  1.000 78.58385  ?  12  LEU B O   1 
ATOM   4314 C CB  . LEU D 4 13  ? 55.08914  83.75516  -0.05913  1.000 79.95611  ?  12  LEU B CB  1 
ATOM   4315 C CG  . LEU D 4 13  ? 54.52199  83.91136  -1.46831  1.000 70.34295  ?  12  LEU B CG  1 
ATOM   4316 C CD1 . LEU D 4 13  ? 53.27110  83.06714  -1.61766  1.000 83.46341  ?  12  LEU B CD1 1 
ATOM   4317 C CD2 . LEU D 4 13  ? 54.22128  85.37024  -1.75834  1.000 98.01392  ?  12  LEU B CD2 1 
ATOM   4318 N N   . VAL D 4 14  ? 56.07345  80.53422  -1.03259  1.000 63.93171  ?  13  VAL B N   1 
ATOM   4319 C CA  . VAL D 4 14  ? 57.05579  79.66958  -1.67089  1.000 70.09241  ?  13  VAL B CA  1 
ATOM   4320 C C   . VAL D 4 14  ? 56.80674  79.67146  -3.17445  1.000 74.37534  ?  13  VAL B C   1 
ATOM   4321 O O   . VAL D 4 14  ? 55.73035  79.26702  -3.62160  1.000 76.69156  ?  13  VAL B O   1 
ATOM   4322 C CB  . VAL D 4 14  ? 56.99716  78.23492  -1.12001  1.000 64.98803  ?  13  VAL B CB  1 
ATOM   4323 C CG1 . VAL D 4 14  ? 58.19505  77.42910  -1.60263  1.000 55.75507  ?  13  VAL B CG1 1 
ATOM   4324 C CG2 . VAL D 4 14  ? 56.91711  78.25164  0.39846   1.000 64.26108  ?  13  VAL B CG2 1 
ATOM   4325 N N   . PRO D 4 15  ? 57.75583  80.11731  -3.99284  1.000 79.19653  ?  14  PRO B N   1 
ATOM   4326 C CA  . PRO D 4 15  ? 57.63346  79.91266  -5.43888  1.000 75.79363  ?  14  PRO B CA  1 
ATOM   4327 C C   . PRO D 4 15  ? 57.70002  78.43214  -5.78155  1.000 85.65365  ?  14  PRO B C   1 
ATOM   4328 O O   . PRO D 4 15  ? 58.19547  77.60669  -5.01100  1.000 98.71050  ?  14  PRO B O   1 
ATOM   4329 C CB  . PRO D 4 15  ? 58.83464  80.67244  -6.01373  1.000 72.11263  ?  14  PRO B CB  1 
ATOM   4330 C CG  . PRO D 4 15  ? 59.22084  81.64612  -4.94232  1.000 75.90879  ?  14  PRO B CG  1 
ATOM   4331 C CD  . PRO D 4 15  ? 58.91715  80.95324  -3.64858  1.000 73.00367  ?  14  PRO B CD  1 
ATOM   4332 N N   . ARG D 4 16  ? 57.18509  78.10043  -6.96275  1.000 80.76053  ?  15  ARG B N   1 
ATOM   4333 C CA  . ARG D 4 16  ? 57.12563  76.70599  -7.38071  1.000 91.73508  ?  15  ARG B CA  1 
ATOM   4334 C C   . ARG D 4 16  ? 58.52769  76.16391  -7.63235  1.000 98.73403  ?  15  ARG B C   1 
ATOM   4335 O O   . ARG D 4 16  ? 59.31342  76.75974  -8.37574  1.000 97.39862  ?  15  ARG B O   1 
ATOM   4336 C CB  . ARG D 4 16  ? 56.26685  76.56038  -8.63561  1.000 86.62624  ?  15  ARG B CB  1 
ATOM   4337 C CG  . ARG D 4 16  ? 56.08365  75.11945  -9.08490  1.000 91.99057  ?  15  ARG B CG  1 
ATOM   4338 C CD  . ARG D 4 16  ? 55.07621  75.00726  -10.21614 1.000 88.03919  ?  15  ARG B CD  1 
ATOM   4339 N NE  . ARG D 4 16  ? 54.86229  73.62057  -10.61268 1.000 104.68223 ?  15  ARG B NE  1 
ATOM   4340 C CZ  . ARG D 4 16  ? 53.99091  73.22961  -11.53246 1.000 126.11460 ?  15  ARG B CZ  1 
ATOM   4341 N NH1 . ARG D 4 16  ? 53.22629  74.09816  -12.17382 1.000 127.70605 ?  15  ARG B NH1 1 
ATOM   4342 N NH2 . ARG D 4 16  ? 53.88316  71.93442  -11.81521 1.000 121.76390 ?  15  ARG B NH2 1 
ATOM   4343 N N   . GLY D 4 17  ? 58.83918  75.02991  -7.00681  1.000 94.21772  ?  16  GLY B N   1 
ATOM   4344 C CA  . GLY D 4 17  ? 60.13130  74.39663  -7.15244  1.000 81.32850  ?  16  GLY B CA  1 
ATOM   4345 C C   . GLY D 4 17  ? 61.19424  74.86321  -6.18269  1.000 98.07030  ?  16  GLY B C   1 
ATOM   4346 O O   . GLY D 4 17  ? 62.30751  74.32250  -6.20512  1.000 112.86961 ?  16  GLY B O   1 
ATOM   4347 N N   . GLN D 4 18  ? 60.89269  75.83983  -5.33168  1.000 94.13587  ?  17  GLN B N   1 
ATOM   4348 C CA  . GLN D 4 18  ? 61.88062  76.37241  -4.40899  1.000 89.62973  ?  17  GLN B CA  1 
ATOM   4349 C C   . GLN D 4 18  ? 61.95643  75.51423  -3.14673  1.000 86.40474  ?  17  GLN B C   1 
ATOM   4350 O O   . GLN D 4 18  ? 61.13114  74.62795  -2.90930  1.000 80.54972  ?  17  GLN B O   1 
ATOM   4351 C CB  . GLN D 4 18  ? 61.55077  77.82103  -4.05216  1.000 94.42708  ?  17  GLN B CB  1 
ATOM   4352 C CG  . GLN D 4 18  ? 62.74785  78.75568  -4.09140  1.000 96.73113  ?  17  GLN B CG  1 
ATOM   4353 C CD  . GLN D 4 18  ? 63.33935  78.88221  -5.48221  1.000 109.84686 ?  17  GLN B CD  1 
ATOM   4354 O OE1 . GLN D 4 18  ? 64.27988  78.17133  -5.83726  1.000 120.83415 ?  17  GLN B OE1 1 
ATOM   4355 N NE2 . GLN D 4 18  ? 62.78853  79.79117  -6.27857  1.000 97.91288  ?  17  GLN B NE2 1 
ATOM   4356 N N   . ALA D 4 19  ? 62.96834  75.79102  -2.32893  1.000 84.69260  ?  18  ALA B N   1 
ATOM   4357 C CA  . ALA D 4 19  ? 63.20698  75.06580  -1.09104  1.000 68.41815  ?  18  ALA B CA  1 
ATOM   4358 C C   . ALA D 4 19  ? 62.89018  75.94816  0.11003   1.000 76.89560  ?  18  ALA B C   1 
ATOM   4359 O O   . ALA D 4 19  ? 62.95554  77.17835  0.03403   1.000 98.40052  ?  18  ALA B O   1 
ATOM   4360 C CB  . ALA D 4 19  ? 64.65568  74.57540  -1.00874  1.000 74.48283  ?  18  ALA B CB  1 
ATOM   4361 N N   . VAL D 4 20  ? 62.54278  75.30450  1.22306   1.000 69.24329  ?  19  VAL B N   1 
ATOM   4362 C CA  . VAL D 4 20  ? 62.17407  75.99230  2.45668   1.000 65.93749  ?  19  VAL B CA  1 
ATOM   4363 C C   . VAL D 4 20  ? 62.82448  75.26805  3.62643   1.000 64.48503  ?  19  VAL B C   1 
ATOM   4364 O O   . VAL D 4 20  ? 62.76957  74.03685  3.70764   1.000 71.69009  ?  19  VAL B O   1 
ATOM   4365 C CB  . VAL D 4 20  ? 60.64450  76.05482  2.64530   1.000 64.81327  ?  19  VAL B CB  1 
ATOM   4366 C CG1 . VAL D 4 20  ? 60.29384  76.58335  4.02769   1.000 63.92681  ?  19  VAL B CG1 1 
ATOM   4367 C CG2 . VAL D 4 20  ? 60.01487  76.92429  1.57546   1.000 76.43983  ?  19  VAL B CG2 1 
ATOM   4368 N N   . ASN D 4 21  ? 63.43779  76.02790  4.52960   1.000 56.41865  ?  20  ASN B N   1 
ATOM   4369 C CA  . ASN D 4 21  ? 64.06403  75.48788  5.72840   1.000 49.12097  ?  20  ASN B CA  1 
ATOM   4370 C C   . ASN D 4 21  ? 63.28497  75.94794  6.95319   1.000 58.23550  ?  20  ASN B C   1 
ATOM   4371 O O   . ASN D 4 21  ? 63.06069  77.14932  7.13504   1.000 68.75709  ?  20  ASN B O   1 
ATOM   4372 C CB  . ASN D 4 21  ? 65.52550  75.92941  5.82682   1.000 49.40791  ?  20  ASN B CB  1 
ATOM   4373 C CG  . ASN D 4 21  ? 66.35267  75.47434  4.64060   1.000 62.46687  ?  20  ASN B CG  1 
ATOM   4374 O OD1 . ASN D 4 21  ? 66.93960  74.39228  4.65632   1.000 64.53316  ?  20  ASN B OD1 1 
ATOM   4375 N ND2 . ASN D 4 21  ? 66.40295  76.30075  3.60279   1.000 66.19216  ?  20  ASN B ND2 1 
ATOM   4376 N N   . LEU D 4 22  ? 62.87707  74.99432  7.78838   1.000 55.48927  ?  21  LEU B N   1 
ATOM   4377 C CA  . LEU D 4 22  ? 62.06117  75.27017  8.96113   1.000 53.29906  ?  21  LEU B CA  1 
ATOM   4378 C C   . LEU D 4 22  ? 62.79912  74.86173  10.22943  1.000 51.92657  ?  21  LEU B C   1 
ATOM   4379 O O   . LEU D 4 22  ? 63.60486  73.92654  10.22596  1.000 49.72488  ?  21  LEU B O   1 
ATOM   4380 C CB  . LEU D 4 22  ? 60.71729  74.53554  8.88510   1.000 51.89224  ?  21  LEU B CB  1 
ATOM   4381 C CG  . LEU D 4 22  ? 59.82522  74.87773  7.69040   1.000 57.38332  ?  21  LEU B CG  1 
ATOM   4382 C CD1 . LEU D 4 22  ? 58.53794  74.06902  7.73121   1.000 42.90185  ?  21  LEU B CD1 1 
ATOM   4383 C CD2 . LEU D 4 22  ? 59.52576  76.36816  7.65746   1.000 79.23002  ?  21  LEU B CD2 1 
ATOM   4384 N N   . ARG D 4 23  ? 62.51038  75.57193  11.31786  1.000 61.80075  ?  22  ARG B N   1 
ATOM   4385 C CA  . ARG D 4 23  ? 63.11778  75.32004  12.61511  1.000 39.77794  ?  22  ARG B CA  1 
ATOM   4386 C C   . ARG D 4 23  ? 62.06079  74.89370  13.62389  1.000 54.93518  ?  22  ARG B C   1 
ATOM   4387 O O   . ARG D 4 23  ? 60.85925  75.09351  13.42410  1.000 76.79608  ?  22  ARG B O   1 
ATOM   4388 C CB  . ARG D 4 23  ? 63.84292  76.56042  13.15263  1.000 63.41711  ?  22  ARG B CB  1 
ATOM   4389 C CG  . ARG D 4 23  ? 65.14630  76.89372  12.46250  1.000 59.56142  ?  22  ARG B CG  1 
ATOM   4390 C CD  . ARG D 4 23  ? 65.84610  78.03268  13.18286  1.000 66.94411  ?  22  ARG B CD  1 
ATOM   4391 N NE  . ARG D 4 23  ? 66.20135  77.66735  14.54908  1.000 56.57895  ?  22  ARG B NE  1 
ATOM   4392 C CZ  . ARG D 4 23  ? 66.56670  78.53191  15.48573  1.000 65.55863  ?  22  ARG B CZ  1 
ATOM   4393 N NH1 . ARG D 4 23  ? 66.61097  79.83266  15.24689  1.000 50.97934  ?  22  ARG B NH1 1 
ATOM   4394 N NH2 . ARG D 4 23  ? 66.89196  78.08050  16.69367  1.000 47.26553  ?  22  ARG B NH2 1 
ATOM   4395 N N   . CYS D 4 24  ? 62.53355  74.31035  14.72403  1.000 44.61165  ?  23  CYS B N   1 
ATOM   4396 C CA  . CYS D 4 24  ? 61.67441  73.97145  15.85096  1.000 47.50636  ?  23  CYS B CA  1 
ATOM   4397 C C   . CYS D 4 24  ? 62.54986  73.77826  17.07861  1.000 54.66087  ?  23  CYS B C   1 
ATOM   4398 O O   . CYS D 4 24  ? 63.53738  73.03890  17.02649  1.000 56.51952  ?  23  CYS B O   1 
ATOM   4399 C CB  . CYS D 4 24  ? 60.85218  72.71021  15.57287  1.000 44.04492  ?  23  CYS B CB  1 
ATOM   4400 S SG  . CYS D 4 24  ? 59.59233  72.37592  16.82388  1.000 74.23905  ?  23  CYS B SG  1 
ATOM   4401 N N   . ILE D 4 25  ? 62.18796  74.44100  18.17362  1.000 60.42601  ?  24  ILE B N   1 
ATOM   4402 C CA  . ILE D 4 25  ? 62.96238  74.41955  19.40789  1.000 49.91674  ?  24  ILE B CA  1 
ATOM   4403 C C   . ILE D 4 25  ? 62.12892  73.75007  20.48981  1.000 51.63784  ?  24  ILE B C   1 
ATOM   4404 O O   . ILE D 4 25  ? 60.96241  74.10643  20.69232  1.000 60.22789  ?  24  ILE B O   1 
ATOM   4405 C CB  . ILE D 4 25  ? 63.37923  75.83679  19.84042  1.000 52.67528  ?  24  ILE B CB  1 
ATOM   4406 C CG1 . ILE D 4 25  ? 64.07578  76.56275  18.68804  1.000 40.86505  ?  24  ILE B CG1 1 
ATOM   4407 C CG2 . ILE D 4 25  ? 64.28717  75.77699  21.05927  1.000 49.46330  ?  24  ILE B CG2 1 
ATOM   4408 C CD1 . ILE D 4 25  ? 64.43161  77.99970  19.00053  1.000 75.40166  ?  24  ILE B CD1 1 
ATOM   4409 N N   . LEU D 4 26  ? 62.72833  72.78604  21.18215  1.000 58.37295  ?  25  LEU B N   1 
ATOM   4410 C CA  . LEU D 4 26  ? 62.07087  72.09193  22.28012  1.000 49.58177  ?  25  LEU B CA  1 
ATOM   4411 C C   . LEU D 4 26  ? 62.35022  72.82474  23.58609  1.000 55.62811  ?  25  LEU B C   1 
ATOM   4412 O O   . LEU D 4 26  ? 63.48856  73.22535  23.85079  1.000 61.48124  ?  25  LEU B O   1 
ATOM   4413 C CB  . LEU D 4 26  ? 62.55271  70.64361  22.36532  1.000 47.82146  ?  25  LEU B CB  1 
ATOM   4414 C CG  . LEU D 4 26  ? 61.96852  69.78498  23.48728  1.000 52.96931  ?  25  LEU B CG  1 
ATOM   4415 C CD1 . LEU D 4 26  ? 60.45970  69.67607  23.34624  1.000 54.44259  ?  25  LEU B CD1 1 
ATOM   4416 C CD2 . LEU D 4 26  ? 62.61125  68.40618  23.50507  1.000 44.96032  ?  25  LEU B CD2 1 
ATOM   4417 N N   . LYS D 4 27  ? 61.30884  73.00306  24.39613  1.000 60.25722  ?  26  LYS B N   1 
ATOM   4418 C CA  . LYS D 4 27  ? 61.41804  73.72979  25.65272  1.000 63.36338  ?  26  LYS B CA  1 
ATOM   4419 C C   . LYS D 4 27  ? 61.16325  72.85994  26.87486  1.000 63.67166  ?  26  LYS B C   1 
ATOM   4420 O O   . LYS D 4 27  ? 61.17787  73.37605  27.99796  1.000 82.22483  ?  26  LYS B O   1 
ATOM   4421 C CB  . LYS D 4 27  ? 60.45261  74.92076  25.65802  1.000 56.79933  ?  26  LYS B CB  1 
ATOM   4422 C CG  . LYS D 4 27  ? 60.77685  75.98750  24.62702  1.000 48.74138  ?  26  LYS B CG  1 
ATOM   4423 C CD  . LYS D 4 27  ? 59.85083  77.18435  24.76803  1.000 94.03734  ?  26  LYS B CD  1 
ATOM   4424 C CE  . LYS D 4 27  ? 60.21218  78.28297  23.78098  1.000 107.85000 ?  26  LYS B CE  1 
ATOM   4425 N NZ  . LYS D 4 27  ? 59.33482  79.47604  23.93703  1.000 109.12174 ?  26  LYS B NZ  1 
ATOM   4426 N N   . ASN D 4 28  ? 60.92694  71.56257  26.69104  1.000 59.46702  ?  27  ASN B N   1 
ATOM   4427 C CA  . ASN D 4 28  ? 60.68480  70.64765  27.80051  1.000 53.66520  ?  27  ASN B CA  1 
ATOM   4428 C C   . ASN D 4 28  ? 61.44622  69.35848  27.53700  1.000 61.51829  ?  27  ASN B C   1 
ATOM   4429 O O   . ASN D 4 28  ? 61.24322  68.71647  26.50167  1.000 65.75230  ?  27  ASN B O   1 
ATOM   4430 C CB  . ASN D 4 28  ? 59.18949  70.36705  27.97266  1.000 64.74606  ?  27  ASN B CB  1 
ATOM   4431 C CG  . ASN D 4 28  ? 58.85278  69.82344  29.34623  1.000 74.45721  ?  27  ASN B CG  1 
ATOM   4432 O OD1 . ASN D 4 28  ? 59.66930  69.15954  29.98390  1.000 91.16609  ?  27  ASN B OD1 1 
ATOM   4433 N ND2 . ASN D 4 28  ? 57.64244  70.10719  29.81137  1.000 85.98241  ?  27  ASN B ND2 1 
ATOM   4434 N N   . SER D 4 29  ? 62.31719  68.98118  28.47719  1.000 76.20866  ?  28  SER B N   1 
ATOM   4435 C CA  . SER D 4 29  ? 63.13688  67.78520  28.31491  1.000 63.37657  ?  28  SER B CA  1 
ATOM   4436 C C   . SER D 4 29  ? 62.31905  66.49985  28.37799  1.000 75.49477  ?  28  SER B C   1 
ATOM   4437 O O   . SER D 4 29  ? 62.74115  65.48354  27.81468  1.000 71.27614  ?  28  SER B O   1 
ATOM   4438 C CB  . SER D 4 29  ? 64.23335  67.75043  29.38177  1.000 73.89451  ?  28  SER B CB  1 
ATOM   4439 O OG  . SER D 4 29  ? 65.06095  68.90001  29.30454  1.000 103.58561 ?  28  SER B OG  1 
ATOM   4440 N N   . GLN D 4 30  ? 61.16524  66.51496  29.04544  1.000 65.79461  ?  29  GLN B N   1 
ATOM   4441 C CA  . GLN D 4 30  ? 60.33160  65.32431  29.16385  1.000 63.15079  ?  29  GLN B CA  1 
ATOM   4442 C C   . GLN D 4 30  ? 59.55054  65.01485  27.89330  1.000 62.63789  ?  29  GLN B C   1 
ATOM   4443 O O   . GLN D 4 30  ? 58.72424  64.09657  27.90120  1.000 74.10426  ?  29  GLN B O   1 
ATOM   4444 C CB  . GLN D 4 30  ? 59.36422  65.46777  30.34203  1.000 74.31022  ?  29  GLN B CB  1 
ATOM   4445 C CG  . GLN D 4 30  ? 60.03443  65.44012  31.70632  1.000 86.06376  ?  29  GLN B CG  1 
ATOM   4446 C CD  . GLN D 4 30  ? 59.03573  65.36127  32.84609  1.000 92.10710  ?  29  GLN B CD  1 
ATOM   4447 O OE1 . GLN D 4 30  ? 57.82736  65.47688  32.63921  1.000 108.16412 ?  29  GLN B OE1 1 
ATOM   4448 N NE2 . GLN D 4 30  ? 59.53796  65.15775  34.05844  1.000 112.09885 ?  29  GLN B NE2 1 
ATOM   4449 N N   . TYR D 4 31  ? 59.78747  65.75262  26.81191  1.000 60.10468  ?  36  TYR B N   1 
ATOM   4450 C CA  . TYR D 4 31  ? 59.15095  65.49741  25.51899  1.000 55.65101  ?  36  TYR B CA  1 
ATOM   4451 C C   . TYR D 4 31  ? 60.22252  65.40370  24.43831  1.000 53.69058  ?  36  TYR B C   1 
ATOM   4452 O O   . TYR D 4 31  ? 60.23787  66.19083  23.48775  1.000 61.44320  ?  36  TYR B O   1 
ATOM   4453 C CB  . TYR D 4 31  ? 58.13501  66.59164  25.19234  1.000 61.82284  ?  36  TYR B CB  1 
ATOM   4454 C CG  . TYR D 4 31  ? 57.01254  66.72238  26.20074  1.000 65.46499  ?  36  TYR B CG  1 
ATOM   4455 C CD1 . TYR D 4 31  ? 57.20257  67.39550  27.40159  1.000 68.77959  ?  36  TYR B CD1 1 
ATOM   4456 C CD2 . TYR D 4 31  ? 55.75961  66.18365  25.94571  1.000 64.10024  ?  36  TYR B CD2 1 
ATOM   4457 C CE1 . TYR D 4 31  ? 56.18008  67.51637  28.32386  1.000 64.87161  ?  36  TYR B CE1 1 
ATOM   4458 C CE2 . TYR D 4 31  ? 54.73056  66.30060  26.86097  1.000 69.82874  ?  36  TYR B CE2 1 
ATOM   4459 C CZ  . TYR D 4 31  ? 54.94591  66.96841  28.04768  1.000 71.05781  ?  36  TYR B CZ  1 
ATOM   4460 O OH  . TYR D 4 31  ? 53.92339  67.08848  28.96114  1.000 82.34870  ?  36  TYR B OH  1 
ATOM   4461 N N   . PRO D 4 32  ? 61.13983  64.43475  24.54945  1.000 58.30782  ?  37  PRO B N   1 
ATOM   4462 C CA  . PRO D 4 32  ? 62.29682  64.42140  23.64317  1.000 51.07019  ?  37  PRO B CA  1 
ATOM   4463 C C   . PRO D 4 32  ? 61.98496  63.92621  22.24323  1.000 57.63933  ?  37  PRO B C   1 
ATOM   4464 O O   . PRO D 4 32  ? 62.72164  64.27184  21.30937  1.000 52.07507  ?  37  PRO B O   1 
ATOM   4465 C CB  . PRO D 4 32  ? 63.27725  63.47965  24.35117  1.000 50.66928  ?  37  PRO B CB  1 
ATOM   4466 C CG  . PRO D 4 32  ? 62.38741  62.50834  25.05069  1.000 49.32305  ?  37  PRO B CG  1 
ATOM   4467 C CD  . PRO D 4 32  ? 61.14180  63.26917  25.45362  1.000 59.51030  ?  37  PRO B CD  1 
ATOM   4468 N N   . TRP D 4 33  ? 60.93038  63.13543  22.06391  1.000 53.45942  ?  38  TRP B N   1 
ATOM   4469 C CA  . TRP D 4 33  ? 60.58636  62.58840  20.75365  1.000 47.79172  ?  38  TRP B CA  1 
ATOM   4470 C C   . TRP D 4 33  ? 59.89505  63.67470  19.94037  1.000 47.02313  ?  38  TRP B C   1 
ATOM   4471 O O   . TRP D 4 33  ? 58.68989  63.89923  20.07292  1.000 49.50762  ?  38  TRP B O   1 
ATOM   4472 C CB  . TRP D 4 33  ? 59.70810  61.35220  20.90529  1.000 44.34864  ?  38  TRP B CB  1 
ATOM   4473 C CG  . TRP D 4 33  ? 60.32020  60.31582  21.79112  1.000 49.74740  ?  38  TRP B CG  1 
ATOM   4474 C CD1 . TRP D 4 33  ? 60.17824  60.20669  23.14328  1.000 53.49091  ?  38  TRP B CD1 1 
ATOM   4475 C CD2 . TRP D 4 33  ? 61.18646  59.24770  21.39078  1.000 51.55913  ?  38  TRP B CD2 1 
ATOM   4476 N NE1 . TRP D 4 33  ? 60.89809  59.13389  23.60942  1.000 65.93420  ?  38  TRP B NE1 1 
ATOM   4477 C CE2 . TRP D 4 33  ? 61.52654  58.52859  22.55307  1.000 56.54107  ?  38  TRP B CE2 1 
ATOM   4478 C CE3 . TRP D 4 33  ? 61.70509  58.82814  20.16228  1.000 47.03014  ?  38  TRP B CE3 1 
ATOM   4479 C CZ2 . TRP D 4 33  ? 62.36121  57.41408  22.52340  1.000 59.12890  ?  38  TRP B CZ2 1 
ATOM   4480 C CZ3 . TRP D 4 33  ? 62.53338  57.72110  20.13531  1.000 57.52709  ?  38  TRP B CZ3 1 
ATOM   4481 C CH2 . TRP D 4 33  ? 62.85380  57.02768  21.30792  1.000 46.20271  ?  38  TRP B CH2 1 
ATOM   4482 N N   . MET D 4 34  ? 60.66425  64.35773  19.09773  1.000 45.01336  ?  39  MET B N   1 
ATOM   4483 C CA  . MET D 4 34  ? 60.13384  65.40338  18.23661  1.000 50.32110  ?  39  MET B CA  1 
ATOM   4484 C C   . MET D 4 34  ? 59.77058  64.81824  16.87890  1.000 46.69335  ?  39  MET B C   1 
ATOM   4485 O O   . MET D 4 34  ? 60.44560  63.91418  16.37841  1.000 53.58691  ?  39  MET B O   1 
ATOM   4486 C CB  . MET D 4 34  ? 61.15091  66.53366  18.07292  1.000 47.81677  ?  39  MET B CB  1 
ATOM   4487 C CG  . MET D 4 34  ? 61.70831  67.05232  19.38932  1.000 47.81171  ?  39  MET B CG  1 
ATOM   4488 S SD  . MET D 4 34  ? 62.85161  68.43064  19.18173  1.000 59.91609  ?  39  MET B SD  1 
ATOM   4489 C CE  . MET D 4 34  ? 61.73963  69.70465  18.59131  1.000 66.91255  ?  39  MET B CE  1 
ATOM   4490 N N   . SER D 4 35  ? 58.69802  65.33751  16.28577  1.000 45.62334  ?  40  SER B N   1 
ATOM   4491 C CA  . SER D 4 35  ? 58.17347  64.78821  15.04540  1.000 52.83287  ?  40  SER B CA  1 
ATOM   4492 C C   . SER D 4 35  ? 57.69382  65.91527  14.14270  1.000 46.35055  ?  40  SER B C   1 
ATOM   4493 O O   . SER D 4 35  ? 57.45376  67.04021  14.58776  1.000 54.31787  ?  40  SER B O   1 
ATOM   4494 C CB  . SER D 4 35  ? 57.02328  63.80470  15.30884  1.000 42.89255  ?  40  SER B CB  1 
ATOM   4495 O OG  . SER D 4 35  ? 57.37198  62.85524  16.30085  1.000 52.44768  ?  40  SER B OG  1 
ATOM   4496 N N   . TRP D 4 36  ? 57.55953  65.59386  12.85942  1.000 42.92018  ?  41  TRP B N   1 
ATOM   4497 C CA  . TRP D 4 36  ? 56.96618  66.48364  11.87112  1.000 43.90479  ?  41  TRP B CA  1 
ATOM   4498 C C   . TRP D 4 36  ? 55.67472  65.86371  11.35737  1.000 52.17957  ?  41  TRP B C   1 
ATOM   4499 O O   . TRP D 4 36  ? 55.64487  64.67685  11.01478  1.000 58.91051  ?  41  TRP B O   1 
ATOM   4500 C CB  . TRP D 4 36  ? 57.92128  66.74015  10.70259  1.000 44.71772  ?  41  TRP B CB  1 
ATOM   4501 C CG  . TRP D 4 36  ? 59.05870  67.65565  11.02401  1.000 52.05350  ?  41  TRP B CG  1 
ATOM   4502 C CD1 . TRP D 4 36  ? 60.37190  67.31342  11.16699  1.000 54.89007  ?  41  TRP B CD1 1 
ATOM   4503 C CD2 . TRP D 4 36  ? 58.98693  69.07002  11.23836  1.000 62.01332  ?  41  TRP B CD2 1 
ATOM   4504 N NE1 . TRP D 4 36  ? 61.12216  68.42679  11.45682  1.000 51.34040  ?  41  TRP B NE1 1 
ATOM   4505 C CE2 . TRP D 4 36  ? 60.29530  69.51809  11.50878  1.000 59.43050  ?  41  TRP B CE2 1 
ATOM   4506 C CE3 . TRP D 4 36  ? 57.94344  70.00048  11.22987  1.000 57.38541  ?  41  TRP B CE3 1 
ATOM   4507 C CZ2 . TRP D 4 36  ? 60.58794  70.85578  11.76717  1.000 54.86363  ?  41  TRP B CZ2 1 
ATOM   4508 C CZ3 . TRP D 4 36  ? 58.23599  71.32818  11.48658  1.000 61.02240  ?  41  TRP B CZ3 1 
ATOM   4509 C CH2 . TRP D 4 36  ? 59.54707  71.74311  11.75169  1.000 56.82921  ?  41  TRP B CH2 1 
ATOM   4510 N N   . TYR D 4 37  ? 54.61414  66.66337  11.30844  1.000 39.79474  ?  42  TYR B N   1 
ATOM   4511 C CA  . TYR D 4 37  ? 53.33569  66.23924  10.76104  1.000 46.54878  ?  42  TYR B CA  1 
ATOM   4512 C C   . TYR D 4 37  ? 52.93164  67.16701  9.62402   1.000 47.96727  ?  42  TYR B C   1 
ATOM   4513 O O   . TYR D 4 37  ? 53.22443  68.36645  9.64381   1.000 45.77976  ?  42  TYR B O   1 
ATOM   4514 C CB  . TYR D 4 37  ? 52.24283  66.21959  11.83605  1.000 49.31233  ?  42  TYR B CB  1 
ATOM   4515 C CG  . TYR D 4 37  ? 52.26752  64.98938  12.71586  1.000 50.79769  ?  42  TYR B CG  1 
ATOM   4516 C CD1 . TYR D 4 37  ? 53.18862  64.86639  13.74809  1.000 49.30507  ?  42  TYR B CD1 1 
ATOM   4517 C CD2 . TYR D 4 37  ? 51.36382  63.95268  12.51735  1.000 47.39517  ?  42  TYR B CD2 1 
ATOM   4518 C CE1 . TYR D 4 37  ? 53.21163  63.74288  14.55535  1.000 41.68434  ?  42  TYR B CE1 1 
ATOM   4519 C CE2 . TYR D 4 37  ? 51.37847  62.82698  13.31950  1.000 46.16011  ?  42  TYR B CE2 1 
ATOM   4520 C CZ  . TYR D 4 37  ? 52.30416  62.72731  14.33581  1.000 49.36182  ?  42  TYR B CZ  1 
ATOM   4521 O OH  . TYR D 4 37  ? 52.32167  61.60837  15.13581  1.000 52.88742  ?  42  TYR B OH  1 
ATOM   4522 N N   . GLN D 4 38  ? 52.25794  66.59827  8.62972   1.000 52.65649  ?  43  GLN B N   1 
ATOM   4523 C CA  . GLN D 4 38  ? 51.82219  67.32811  7.44759   1.000 49.47911  ?  43  GLN B CA  1 
ATOM   4524 C C   . GLN D 4 38  ? 50.30178  67.37735  7.40685   1.000 63.89132  ?  43  GLN B C   1 
ATOM   4525 O O   . GLN D 4 38  ? 49.63676  66.36143  7.63720   1.000 60.92248  ?  43  GLN B O   1 
ATOM   4526 C CB  . GLN D 4 38  ? 52.35880  66.67427  6.17196   1.000 44.96313  ?  43  GLN B CB  1 
ATOM   4527 C CG  . GLN D 4 38  ? 51.83020  67.29630  4.88973   1.000 49.24371  ?  43  GLN B CG  1 
ATOM   4528 C CD  . GLN D 4 38  ? 52.13700  66.46007  3.66376   1.000 61.76187  ?  43  GLN B CD  1 
ATOM   4529 O OE1 . GLN D 4 38  ? 53.16964  66.63848  3.01855   1.000 72.58109  ?  43  GLN B OE1 1 
ATOM   4530 N NE2 . GLN D 4 38  ? 51.23633  65.54115  3.33413   1.000 72.27992  ?  43  GLN B NE2 1 
ATOM   4531 N N   . GLN D 4 39  ? 49.75805  68.55689  7.11638   1.000 60.02021  ?  44  GLN B N   1 
ATOM   4532 C CA  . GLN D 4 39  ? 48.32918  68.73782  6.89334   1.000 64.57535  ?  44  GLN B CA  1 
ATOM   4533 C C   . GLN D 4 39  ? 48.14077  69.39127  5.53267   1.000 66.34036  ?  44  GLN B C   1 
ATOM   4534 O O   . GLN D 4 39  ? 48.55853  70.53612  5.32783   1.000 67.88958  ?  44  GLN B O   1 
ATOM   4535 C CB  . GLN D 4 39  ? 47.69404  69.58496  7.99773   1.000 54.25544  ?  44  GLN B CB  1 
ATOM   4536 C CG  . GLN D 4 39  ? 46.17458  69.61948  7.94140   1.000 73.44651  ?  44  GLN B CG  1 
ATOM   4537 C CD  . GLN D 4 39  ? 45.55565  70.33903  9.12426   1.000 69.36901  ?  44  GLN B CD  1 
ATOM   4538 O OE1 . GLN D 4 39  ? 46.17815  71.20844  9.73381   1.000 76.09937  ?  44  GLN B OE1 1 
ATOM   4539 N NE2 . GLN D 4 39  ? 44.32309  69.97427  9.45802   1.000 67.41538  ?  44  GLN B NE2 1 
ATOM   4540 N N   . ASP D 4 40  ? 47.52011  68.66380  4.60734   1.000 63.83372  ?  45  ASP B N   1 
ATOM   4541 C CA  . ASP D 4 40  ? 47.35480  69.14049  3.24375   1.000 73.99795  ?  45  ASP B CA  1 
ATOM   4542 C C   . ASP D 4 40  ? 46.21406  70.15389  3.16636   1.000 76.28689  ?  45  ASP B C   1 
ATOM   4543 O O   . ASP D 4 40  ? 45.61114  70.53621  4.17339   1.000 75.99421  ?  45  ASP B O   1 
ATOM   4544 C CB  . ASP D 4 40  ? 47.11260  67.96511  2.29940   1.000 84.88434  ?  45  ASP B CB  1 
ATOM   4545 C CG  . ASP D 4 40  ? 45.84436  67.20487  2.63031   1.000 90.75871  ?  45  ASP B CG  1 
ATOM   4546 O OD1 . ASP D 4 40  ? 45.33599  67.36402  3.75905   1.000 97.72893  ?  45  ASP B OD1 1 
ATOM   4547 O OD2 . ASP D 4 40  ? 45.35788  66.44640  1.76512   1.000 102.72667 -1 45  ASP B OD2 1 
ATOM   4548 N N   . LEU D 4 41  ? 45.90829  70.58997  1.94163   1.000 80.04639  ?  46  LEU B N   1 
ATOM   4549 C CA  . LEU D 4 41  ? 44.84608  71.56750  1.73535   1.000 97.03836  ?  46  LEU B CA  1 
ATOM   4550 C C   . LEU D 4 41  ? 43.47015  71.01517  2.08373   1.000 90.25043  ?  46  LEU B C   1 
ATOM   4551 O O   . LEU D 4 41  ? 42.53630  71.79805  2.28764   1.000 89.88423  ?  46  LEU B O   1 
ATOM   4552 C CB  . LEU D 4 41  ? 44.86002  72.05861  0.28697   1.000 82.94767  ?  46  LEU B CB  1 
ATOM   4553 C CG  . LEU D 4 41  ? 46.14221  72.75825  -0.16827  1.000 65.42749  ?  46  LEU B CG  1 
ATOM   4554 C CD1 . LEU D 4 41  ? 46.04093  73.17404  -1.62723  1.000 93.53665  ?  46  LEU B CD1 1 
ATOM   4555 C CD2 . LEU D 4 41  ? 46.43776  73.95942  0.71509   1.000 64.34489  ?  46  LEU B CD2 1 
ATOM   4556 N N   . GLN D 4 42  ? 43.32299  69.69379  2.15523   1.000 80.16977  ?  47  GLN B N   1 
ATOM   4557 C CA  . GLN D 4 42  ? 42.06962  69.06284  2.54139   1.000 85.98186  ?  47  GLN B CA  1 
ATOM   4558 C C   . GLN D 4 42  ? 42.02273  68.71731  4.02454   1.000 79.89899  ?  47  GLN B C   1 
ATOM   4559 O O   . GLN D 4 42  ? 41.14324  67.95860  4.44529   1.000 73.65226  ?  47  GLN B O   1 
ATOM   4560 C CB  . GLN D 4 42  ? 41.83132  67.80833  1.69872   1.000 85.76900  ?  47  GLN B CB  1 
ATOM   4561 C CG  . GLN D 4 42  ? 41.62360  68.09351  0.21922   1.000 105.96464 ?  47  GLN B CG  1 
ATOM   4562 C CD  . GLN D 4 42  ? 41.41660  66.83292  -0.59649  1.000 127.65814 ?  47  GLN B CD  1 
ATOM   4563 O OE1 . GLN D 4 42  ? 41.82887  65.74468  -0.19493  1.000 134.74189 ?  47  GLN B OE1 1 
ATOM   4564 N NE2 . GLN D 4 42  ? 40.77087  66.97339  -1.74870  1.000 113.16102 ?  47  GLN B NE2 1 
ATOM   4565 N N   . LYS D 4 43  ? 42.95158  69.25522  4.81887   1.000 74.83797  ?  48  LYS B N   1 
ATOM   4566 C CA  . LYS D 4 43  ? 42.98809  69.05103  6.26876   1.000 87.76885  ?  48  LYS B CA  1 
ATOM   4567 C C   . LYS D 4 43  ? 43.10698  67.56852  6.62367   1.000 78.77343  ?  48  LYS B C   1 
ATOM   4568 O O   . LYS D 4 43  ? 42.30847  67.01965  7.38555   1.000 89.85475  ?  48  LYS B O   1 
ATOM   4569 C CB  . LYS D 4 43  ? 41.76881  69.68431  6.94478   1.000 77.20791  ?  48  LYS B CB  1 
ATOM   4570 C CG  . LYS D 4 43  ? 41.68912  71.19252  6.77880   1.000 97.90418  ?  48  LYS B CG  1 
ATOM   4571 C CD  . LYS D 4 43  ? 40.55328  71.78311  7.59640   1.000 106.86157 ?  48  LYS B CD  1 
ATOM   4572 C CE  . LYS D 4 43  ? 40.50380  73.29521  7.45170   1.000 120.68216 ?  48  LYS B CE  1 
ATOM   4573 N NZ  . LYS D 4 43  ? 41.79117  73.93077  7.84774   1.000 107.54421 ?  48  LYS B NZ  1 
ATOM   4574 N N   . GLN D 4 44  ? 44.12647  66.91961  6.06508   1.000 76.27158  ?  49  GLN B N   1 
ATOM   4575 C CA  . GLN D 4 44  ? 44.42308  65.51705  6.34031   1.000 75.41845  ?  49  GLN B CA  1 
ATOM   4576 C C   . GLN D 4 44  ? 45.77980  65.44456  7.02796   1.000 76.51698  ?  49  GLN B C   1 
ATOM   4577 O O   . GLN D 4 44  ? 46.80720  65.77035  6.42284   1.000 57.02970  ?  49  GLN B O   1 
ATOM   4578 C CB  . GLN D 4 44  ? 44.40905  64.68693  5.05758   1.000 69.60172  ?  49  GLN B CB  1 
ATOM   4579 C CG  . GLN D 4 44  ? 43.07914  64.70976  4.32443   1.000 82.20087  ?  49  GLN B CG  1 
ATOM   4580 C CD  . GLN D 4 44  ? 41.96337  64.07176  5.12771   1.000 98.54234  ?  49  GLN B CD  1 
ATOM   4581 O OE1 . GLN D 4 44  ? 42.20223  63.18180  5.94406   1.000 118.85457 ?  49  GLN B OE1 1 
ATOM   4582 N NE2 . GLN D 4 44  ? 40.73624  64.52689  4.90291   1.000 80.87390  ?  49  GLN B NE2 1 
ATOM   4583 N N   . LEU D 4 45  ? 45.78048  65.02131  8.28839   1.000 79.28437  ?  50  LEU B N   1 
ATOM   4584 C CA  . LEU D 4 45  ? 47.00990  64.92763  9.06038   1.000 67.60963  ?  50  LEU B CA  1 
ATOM   4585 C C   . LEU D 4 45  ? 47.74498  63.63345  8.73863   1.000 67.36344  ?  50  LEU B C   1 
ATOM   4586 O O   . LEU D 4 45  ? 47.13770  62.56274  8.64711   1.000 74.52756  ?  50  LEU B O   1 
ATOM   4587 C CB  . LEU D 4 45  ? 46.70175  65.00039  10.55533  1.000 61.92642  ?  50  LEU B CB  1 
ATOM   4588 C CG  . LEU D 4 45  ? 46.07240  66.30701  11.04008  1.000 65.10967  ?  50  LEU B CG  1 
ATOM   4589 C CD1 . LEU D 4 45  ? 45.57304  66.16688  12.46867  1.000 80.62172  ?  50  LEU B CD1 1 
ATOM   4590 C CD2 . LEU D 4 45  ? 47.07266  67.44675  10.92998  1.000 57.94956  ?  50  LEU B CD2 1 
ATOM   4591 N N   . GLN D 4 46  ? 49.06162  63.73718  8.56704   1.000 58.39825  ?  51  GLN B N   1 
ATOM   4592 C CA  . GLN D 4 46  ? 49.88939  62.58320  8.24321   1.000 71.19750  ?  51  GLN B CA  1 
ATOM   4593 C C   . GLN D 4 46  ? 51.24529  62.72437  8.91618   1.000 65.44539  ?  51  GLN B C   1 
ATOM   4594 O O   . GLN D 4 46  ? 51.87541  63.78302  8.83643   1.000 57.36871  ?  51  GLN B O   1 
ATOM   4595 C CB  . GLN D 4 46  ? 50.06252  62.43171  6.72727   1.000 69.23021  ?  51  GLN B CB  1 
ATOM   4596 C CG  . GLN D 4 46  ? 50.82655  61.18468  6.31397   1.000 72.23616  ?  51  GLN B CG  1 
ATOM   4597 C CD  . GLN D 4 46  ? 50.85924  60.99355  4.81112   1.000 99.20265  ?  51  GLN B CD  1 
ATOM   4598 O OE1 . GLN D 4 46  ? 50.24059  61.75141  4.06405   1.000 115.57922 ?  51  GLN B OE1 1 
ATOM   4599 N NE2 . GLN D 4 46  ? 51.58298  59.97572  4.35936   1.000 124.98508 ?  51  GLN B NE2 1 
ATOM   4600 N N   . TRP D 4 47  ? 51.68542  61.65507  9.57409   1.000 60.58244  ?  52  TRP B N   1 
ATOM   4601 C CA  . TRP D 4 47  ? 52.97638  61.63982  10.24655  1.000 46.80366  ?  52  TRP B CA  1 
ATOM   4602 C C   . TRP D 4 47  ? 54.10414  61.50246  9.23190   1.000 48.80485  ?  52  TRP B C   1 
ATOM   4603 O O   . TRP D 4 47  ? 53.99647  60.74895  8.26030   1.000 54.45106  ?  52  TRP B O   1 
ATOM   4604 C CB  . TRP D 4 47  ? 53.02499  60.49226  11.25677  1.000 47.93592  ?  52  TRP B CB  1 
ATOM   4605 C CG  . TRP D 4 47  ? 54.39174  60.17301  11.77840  1.000 49.74433  ?  52  TRP B CG  1 
ATOM   4606 C CD1 . TRP D 4 47  ? 55.02274  60.75399  12.83979  1.000 43.63416  ?  52  TRP B CD1 1 
ATOM   4607 C CD2 . TRP D 4 47  ? 55.29076  59.17965  11.27180  1.000 47.14366  ?  52  TRP B CD2 1 
ATOM   4608 N NE1 . TRP D 4 47  ? 56.26232  60.18902  13.02023  1.000 43.02834  ?  52  TRP B NE1 1 
ATOM   4609 C CE2 . TRP D 4 47  ? 56.45093  59.22030  12.06988  1.000 45.12755  ?  52  TRP B CE2 1 
ATOM   4610 C CE3 . TRP D 4 47  ? 55.22914  58.26376  10.21721  1.000 50.09496  ?  52  TRP B CE3 1 
ATOM   4611 C CZ2 . TRP D 4 47  ? 57.53916  58.37968  11.84742  1.000 53.55336  ?  52  TRP B CZ2 1 
ATOM   4612 C CZ3 . TRP D 4 47  ? 56.31059  57.43003  9.99842   1.000 50.91939  ?  52  TRP B CZ3 1 
ATOM   4613 C CH2 . TRP D 4 47  ? 57.44957  57.49353  10.80944  1.000 48.77990  ?  52  TRP B CH2 1 
ATOM   4614 N N   . LEU D 4 48  ? 55.19135  62.23914  9.46249   1.000 48.93319  ?  53  LEU B N   1 
ATOM   4615 C CA  . LEU D 4 48  ? 56.34100  62.23890  8.56200   1.000 50.48799  ?  53  LEU B CA  1 
ATOM   4616 C C   . LEU D 4 48  ? 57.53938  61.55078  9.20080   1.000 56.10305  ?  53  LEU B C   1 
ATOM   4617 O O   . LEU D 4 48  ? 57.91413  60.45181  8.78359   1.000 51.87802  ?  53  LEU B O   1 
ATOM   4618 C CB  . LEU D 4 48  ? 56.68762  63.66920  8.13954   1.000 48.32791  ?  53  LEU B CB  1 
ATOM   4619 C CG  . LEU D 4 48  ? 55.63931  64.42105  7.31843   1.000 50.94295  ?  53  LEU B CG  1 
ATOM   4620 C CD1 . LEU D 4 48  ? 56.17985  65.76934  6.86807   1.000 49.38270  ?  53  LEU B CD1 1 
ATOM   4621 C CD2 . LEU D 4 48  ? 55.19596  63.59153  6.12491   1.000 45.56778  ?  53  LEU B CD2 1 
ATOM   4622 N N   . PHE D 4 49  ? 58.16429  62.16614  10.20278  1.000 57.38268  ?  54  PHE B N   1 
ATOM   4623 C CA  . PHE D 4 49  ? 59.35283  61.61901  10.83790  1.000 48.24001  ?  54  PHE B CA  1 
ATOM   4624 C C   . PHE D 4 49  ? 59.20595  61.67973  12.35062  1.000 64.00763  ?  54  PHE B C   1 
ATOM   4625 O O   . PHE D 4 49  ? 58.31204  62.33674  12.88875  1.000 57.18510  ?  54  PHE B O   1 
ATOM   4626 C CB  . PHE D 4 49  ? 60.62192  62.38044  10.43104  1.000 74.25706  ?  54  PHE B CB  1 
ATOM   4627 C CG  . PHE D 4 49  ? 60.66522  62.77264  8.98722   1.000 56.97877  ?  54  PHE B CG  1 
ATOM   4628 C CD1 . PHE D 4 49  ? 61.19185  61.91437  8.04055   1.000 55.98334  ?  54  PHE B CD1 1 
ATOM   4629 C CD2 . PHE D 4 49  ? 60.19604  64.00970  8.57887   1.000 47.20148  ?  54  PHE B CD2 1 
ATOM   4630 C CE1 . PHE D 4 49  ? 61.24364  62.27701  6.71366   1.000 66.23907  ?  54  PHE B CE1 1 
ATOM   4631 C CE2 . PHE D 4 49  ? 60.24287  64.37766  7.25199   1.000 49.78719  ?  54  PHE B CE2 1 
ATOM   4632 C CZ  . PHE D 4 49  ? 60.76763  63.50924  6.31829   1.000 67.29192  ?  54  PHE B CZ  1 
ATOM   4633 N N   . THR D 4 50  ? 60.11388  60.98466  13.03283  1.000 62.28278  ?  55  THR B N   1 
ATOM   4634 C CA  . THR D 4 50  ? 60.28625  61.10624  14.47795  1.000 46.83244  ?  55  THR B CA  1 
ATOM   4635 C C   . THR D 4 50  ? 61.77107  60.94806  14.76881  1.000 50.97695  ?  55  THR B C   1 
ATOM   4636 O O   . THR D 4 50  ? 62.33080  59.86449  14.57487  1.000 60.68087  ?  55  THR B O   1 
ATOM   4637 C CB  . THR D 4 50  ? 59.46645  60.06738  15.24246  1.000 56.64669  ?  55  THR B CB  1 
ATOM   4638 O OG1 . THR D 4 50  ? 58.06946  60.35855  15.10451  1.000 51.37717  ?  55  THR B OG1 1 
ATOM   4639 C CG2 . THR D 4 50  ? 59.84093  60.08301  16.71847  1.000 44.52745  ?  55  THR B CG2 1 
ATOM   4640 N N   . LEU D 4 51  ? 62.40753  62.02467  15.21840  1.000 53.67749  ?  56  LEU B N   1 
ATOM   4641 C CA  . LEU D 4 51  ? 63.83488  62.03776  15.49900  1.000 49.04910  ?  56  LEU B CA  1 
ATOM   4642 C C   . LEU D 4 51  ? 64.06370  62.22011  16.99276  1.000 52.42083  ?  56  LEU B C   1 
ATOM   4643 O O   . LEU D 4 51  ? 63.33450  62.96410  17.65633  1.000 56.18073  ?  56  LEU B O   1 
ATOM   4644 C CB  . LEU D 4 51  ? 64.53523  63.14849  14.71311  1.000 48.70264  ?  56  LEU B CB  1 
ATOM   4645 C CG  . LEU D 4 51  ? 64.32079  63.09670  13.19817  1.000 44.50324  ?  56  LEU B CG  1 
ATOM   4646 C CD1 . LEU D 4 51  ? 65.13062  64.17323  12.49821  1.000 59.31630  ?  56  LEU B CD1 1 
ATOM   4647 C CD2 . LEU D 4 51  ? 64.66881  61.72164  12.65269  1.000 52.82443  ?  56  LEU B CD2 1 
ATOM   4648 N N   . ARG D 4 52  ? 65.08235  61.53900  17.51631  1.000 56.82369  ?  57  ARG B N   1 
ATOM   4649 C CA  . ARG D 4 52  ? 65.31823  61.50989  18.95432  1.000 45.61811  ?  57  ARG B CA  1 
ATOM   4650 C C   . ARG D 4 52  ? 66.74094  61.92702  19.30635  1.000 57.22693  ?  57  ARG B C   1 
ATOM   4651 O O   . ARG D 4 52  ? 66.94485  62.83648  20.11683  1.000 60.97557  ?  57  ARG B O   1 
ATOM   4652 C CB  . ARG D 4 52  ? 65.02912  60.11099  19.50225  1.000 51.17162  ?  57  ARG B CB  1 
ATOM   4653 C CG  . ARG D 4 52  ? 65.38893  59.92180  20.96516  1.000 65.35137  ?  57  ARG B CG  1 
ATOM   4654 C CD  . ARG D 4 52  ? 64.57328  60.83458  21.86418  1.000 62.46927  ?  57  ARG B CD  1 
ATOM   4655 N NE  . ARG D 4 52  ? 64.88963  60.62596  23.27183  1.000 58.17288  ?  57  ARG B NE  1 
ATOM   4656 C CZ  . ARG D 4 52  ? 65.87798  61.23319  23.91387  1.000 56.86145  ?  57  ARG B CZ  1 
ATOM   4657 N NH1 . ARG D 4 52  ? 66.66765  62.10179  23.30364  1.000 59.80466  ?  57  ARG B NH1 1 
ATOM   4658 N NH2 . ARG D 4 52  ? 66.07851  60.96304  25.20051  1.000 58.29282  ?  57  ARG B NH2 1 
ATOM   4659 N N   A SER D 4 53  ? 67.73205  61.26776  18.70094  0.500 57.43369  ?  58  SER B N   1 
ATOM   4660 N N   B SER D 4 53  ? 67.73724  61.25986  18.70249  0.500 57.48138  ?  58  SER B N   1 
ATOM   4661 C CA  A SER D 4 53  ? 69.12305  61.55483  19.01171  0.500 57.36785  ?  58  SER B CA  1 
ATOM   4662 C CA  B SER D 4 53  ? 69.12963  61.54882  19.00603  0.500 57.03435  ?  58  SER B CA  1 
ATOM   4663 C C   A SER D 4 53  ? 69.69389  62.58906  18.04533  0.500 55.50363  ?  58  SER B C   1 
ATOM   4664 C C   B SER D 4 53  ? 69.68817  62.59564  18.04670  0.500 54.31459  ?  58  SER B C   1 
ATOM   4665 O O   A SER D 4 53  ? 69.27151  62.66765  16.88704  0.500 48.84789  ?  58  SER B O   1 
ATOM   4666 O O   B SER D 4 53  ? 69.25186  62.68911  16.89464  0.500 52.10695  ?  58  SER B O   1 
ATOM   4667 C CB  A SER D 4 53  ? 69.95568  60.27701  18.94632  0.500 56.57877  ?  58  SER B CB  1 
ATOM   4668 C CB  B SER D 4 53  ? 69.96890  60.27637  18.91819  0.500 57.17031  ?  58  SER B CB  1 
ATOM   4669 O OG  A SER D 4 53  ? 69.79672  59.62764  17.69723  0.500 57.73481  ?  58  SER B OG  1 
ATOM   4670 O OG  B SER D 4 53  ? 69.56497  59.32889  19.89156  0.500 51.05182  ?  58  SER B OG  1 
ATOM   4671 N N   . PRO D 4 54  ? 70.64620  63.40159  18.50267  1.000 50.48086  ?  63  PRO B N   1 
ATOM   4672 C CA  . PRO D 4 54  ? 71.26818  64.38088  17.60406  1.000 48.67304  ?  63  PRO B CA  1 
ATOM   4673 C C   . PRO D 4 54  ? 72.03575  63.69094  16.48610  1.000 57.67398  ?  63  PRO B C   1 
ATOM   4674 O O   . PRO D 4 54  ? 72.72961  62.69532  16.70380  1.000 65.03393  ?  63  PRO B O   1 
ATOM   4675 C CB  . PRO D 4 54  ? 72.20563  65.16776  18.52803  1.000 44.76700  ?  63  PRO B CB  1 
ATOM   4676 C CG  . PRO D 4 54  ? 71.68499  64.92123  19.91078  1.000 56.46796  ?  63  PRO B CG  1 
ATOM   4677 C CD  . PRO D 4 54  ? 71.13401  63.53034  19.88549  1.000 60.29666  ?  63  PRO B CD  1 
ATOM   4678 N N   . GLY D 4 55  ? 71.89926  64.23020  15.27698  1.000 44.25685  ?  64  GLY B N   1 
ATOM   4679 C CA  . GLY D 4 55  ? 72.52440  63.65909  14.10416  1.000 46.23098  ?  64  GLY B CA  1 
ATOM   4680 C C   . GLY D 4 55  ? 71.63242  62.76527  13.27142  1.000 56.31444  ?  64  GLY B C   1 
ATOM   4681 O O   . GLY D 4 55  ? 72.07302  62.29540  12.21524  1.000 60.29140  ?  64  GLY B O   1 
ATOM   4682 N N   . ASP D 4 56  ? 70.40120  62.51139  13.70988  1.000 57.87073  ?  65  ASP B N   1 
ATOM   4683 C CA  . ASP D 4 56  ? 69.48193  61.69442  12.93018  1.000 53.07018  ?  65  ASP B CA  1 
ATOM   4684 C C   . ASP D 4 56  ? 69.07798  62.41973  11.65289  1.000 52.58694  ?  65  ASP B C   1 
ATOM   4685 O O   . ASP D 4 56  ? 68.88640  63.63884  11.64365  1.000 61.41850  ?  65  ASP B O   1 
ATOM   4686 C CB  . ASP D 4 56  ? 68.24169  61.35014  13.75444  1.000 61.37255  ?  65  ASP B CB  1 
ATOM   4687 C CG  . ASP D 4 56  ? 68.55416  60.44199  14.92607  1.000 69.71477  ?  65  ASP B CG  1 
ATOM   4688 O OD1 . ASP D 4 56  ? 69.71946  60.00977  15.05000  1.000 79.84474  ?  65  ASP B OD1 1 
ATOM   4689 O OD2 . ASP D 4 56  ? 67.63559  60.16407  15.72610  1.000 66.64020  -1 65  ASP B OD2 1 
ATOM   4690 N N   . LYS D 4 57  ? 68.94443  61.65841  10.56915  1.000 51.03140  ?  66  LYS B N   1 
ATOM   4691 C CA  . LYS D 4 57  ? 68.64776  62.21613  9.25477   1.000 51.56058  ?  66  LYS B CA  1 
ATOM   4692 C C   . LYS D 4 57  ? 67.72373  61.25891  8.51893   1.000 64.96454  ?  66  LYS B C   1 
ATOM   4693 O O   . LYS D 4 57  ? 68.10893  60.12092  8.23402   1.000 82.34179  ?  66  LYS B O   1 
ATOM   4694 C CB  . LYS D 4 57  ? 69.93767  62.44953  8.46124   1.000 53.46122  ?  66  LYS B CB  1 
ATOM   4695 C CG  . LYS D 4 57  ? 69.75441  63.15830  7.13130   1.000 74.68335  ?  66  LYS B CG  1 
ATOM   4696 C CD  . LYS D 4 57  ? 71.09548  63.34428  6.43615   1.000 63.24742  ?  66  LYS B CD  1 
ATOM   4697 C CE  . LYS D 4 57  ? 70.93480  63.98978  5.07043   1.000 96.71894  ?  66  LYS B CE  1 
ATOM   4698 N NZ  . LYS D 4 57  ? 72.24304  64.14284  4.37489   1.000 74.35271  ?  66  LYS B NZ  1 
ATOM   4699 N N   . GLU D 4 58  ? 66.50920  61.71559  8.21656   1.000 66.91714  ?  67  GLU B N   1 
ATOM   4700 C CA  . GLU D 4 58  ? 65.51191  60.89997  7.53957   1.000 75.01580  ?  67  GLU B CA  1 
ATOM   4701 C C   . GLU D 4 58  ? 64.98309  61.63473  6.31597   1.000 60.32621  ?  67  GLU B C   1 
ATOM   4702 O O   . GLU D 4 58  ? 64.95653  62.86759  6.27394   1.000 62.98220  ?  67  GLU B O   1 
ATOM   4703 C CB  . GLU D 4 58  ? 64.34970  60.54046  8.47612   1.000 68.21530  ?  67  GLU B CB  1 
ATOM   4704 C CG  . GLU D 4 58  ? 64.74072  59.64958  9.64439   1.000 74.54945  ?  67  GLU B CG  1 
ATOM   4705 C CD  . GLU D 4 58  ? 65.12560  58.24817  9.21045   1.000 100.70794 ?  67  GLU B CD  1 
ATOM   4706 O OE1 . GLU D 4 58  ? 64.70899  57.82687  8.11051   1.000 113.67871 ?  67  GLU B OE1 1 
ATOM   4707 O OE2 . GLU D 4 58  ? 65.84628  57.56717  9.97024   1.000 106.73602 -1 67  GLU B OE2 1 
ATOM   4708 N N   . VAL D 4 59  ? 64.55672  60.86071  5.31937   1.000 75.42404  ?  68  VAL B N   1 
ATOM   4709 C CA  . VAL D 4 59  ? 64.07699  61.39069  4.04821   1.000 73.83399  ?  68  VAL B CA  1 
ATOM   4710 C C   . VAL D 4 59  ? 62.71829  60.77492  3.74353   1.000 58.10659  ?  68  VAL B C   1 
ATOM   4711 O O   . VAL D 4 59  ? 62.53514  59.56121  3.88816   1.000 86.90289  ?  68  VAL B O   1 
ATOM   4712 C CB  . VAL D 4 59  ? 65.06751  61.10609  2.90128   1.000 65.04885  ?  68  VAL B CB  1 
ATOM   4713 C CG1 . VAL D 4 59  ? 64.48564  61.54663  1.56631   1.000 93.83575  ?  68  VAL B CG1 1 
ATOM   4714 C CG2 . VAL D 4 59  ? 66.39435  61.80126  3.15864   1.000 65.07891  ?  68  VAL B CG2 1 
ATOM   4715 N N   . LYS D 4 60  ? 61.76906  61.61151  3.32738   1.000 62.55027  ?  69  LYS B N   1 
ATOM   4716 C CA  . LYS D 4 60  ? 60.45911  61.15725  2.87950   1.000 74.18695  ?  69  LYS B CA  1 
ATOM   4717 C C   . LYS D 4 60  ? 60.05306  61.98361  1.67059   1.000 75.78805  ?  69  LYS B C   1 
ATOM   4718 O O   . LYS D 4 60  ? 60.16658  63.21264  1.69205   1.000 76.69560  ?  69  LYS B O   1 
ATOM   4719 C CB  . LYS D 4 60  ? 59.40831  61.28600  3.98826   1.000 67.77816  ?  69  LYS B CB  1 
ATOM   4720 C CG  . LYS D 4 60  ? 58.64041  60.00717  4.28083   1.000 55.73815  ?  69  LYS B CG  1 
ATOM   4721 C CD  . LYS D 4 60  ? 57.67229  60.20509  5.43798   1.000 71.14897  ?  69  LYS B CD  1 
ATOM   4722 C CE  . LYS D 4 60  ? 56.90240  58.93096  5.74734   1.000 67.92346  ?  69  LYS B CE  1 
ATOM   4723 N NZ  . LYS D 4 60  ? 57.80499  57.82239  6.16279   1.000 96.40646  ?  69  LYS B NZ  1 
ATOM   4724 N N   . SER D 4 61  ? 59.58382  61.31186  0.62143   1.000 88.54795  ?  70  SER B N   1 
ATOM   4725 C CA  . SER D 4 61  ? 59.20824  61.96785  -0.63012  1.000 69.54549  ?  70  SER B CA  1 
ATOM   4726 C C   . SER D 4 61  ? 57.77797  61.56915  -0.98151  1.000 81.50448  ?  70  SER B C   1 
ATOM   4727 O O   . SER D 4 61  ? 57.55068  60.52034  -1.59198  1.000 105.68348 ?  70  SER B O   1 
ATOM   4728 C CB  . SER D 4 61  ? 60.17617  61.60241  -1.75117  1.000 68.71341  ?  70  SER B CB  1 
ATOM   4729 O OG  . SER D 4 61  ? 59.83179  62.26241  -2.95648  1.000 100.00381 ?  70  SER B OG  1 
ATOM   4730 N N   . LEU D 4 62  ? 56.82114  62.40352  -0.59670  1.000 66.80015  ?  71  LEU B N   1 
ATOM   4731 C CA  . LEU D 4 62  ? 55.42108  62.22671  -0.94080  1.000 92.53548  ?  71  LEU B CA  1 
ATOM   4732 C C   . LEU D 4 62  ? 55.01287  63.24785  -1.99948  1.000 85.78077  ?  71  LEU B C   1 
ATOM   4733 O O   . LEU D 4 62  ? 55.68921  64.26617  -2.18029  1.000 83.86960  ?  71  LEU B O   1 
ATOM   4734 C CB  . LEU D 4 62  ? 54.53928  62.36035  0.31216   1.000 76.95989  ?  71  LEU B CB  1 
ATOM   4735 C CG  . LEU D 4 62  ? 54.35521  63.71102  1.00318   1.000 73.88051  ?  71  LEU B CG  1 
ATOM   4736 C CD1 . LEU D 4 62  ? 53.08949  64.39887  0.51475   1.000 100.92867 ?  71  LEU B CD1 1 
ATOM   4737 C CD2 . LEU D 4 62  ? 54.31241  63.52156  2.50966   1.000 59.13865  ?  71  LEU B CD2 1 
ATOM   4738 N N   . PRO D 4 63  ? 53.92492  63.00265  -2.73437  1.000 93.83830  ?  72  PRO B N   1 
ATOM   4739 C CA  . PRO D 4 63  ? 53.57640  63.89115  -3.85708  1.000 95.86405  ?  72  PRO B CA  1 
ATOM   4740 C C   . PRO D 4 63  ? 53.32469  65.32117  -3.40553  1.000 94.44674  ?  72  PRO B C   1 
ATOM   4741 O O   . PRO D 4 63  ? 52.49174  65.58283  -2.53447  1.000 101.36397 ?  72  PRO B O   1 
ATOM   4742 C CB  . PRO D 4 63  ? 52.30931  63.24839  -4.43407  1.000 96.14783  ?  72  PRO B CB  1 
ATOM   4743 C CG  . PRO D 4 63  ? 51.76712  62.41240  -3.32777  1.000 99.90969  ?  72  PRO B CG  1 
ATOM   4744 C CD  . PRO D 4 63  ? 52.97295  61.88443  -2.62239  1.000 105.45152 ?  72  PRO B CD  1 
ATOM   4745 N N   . GLY D 4 64  ? 54.05750  66.25176  -4.01470  1.000 88.59076  ?  73  GLY B N   1 
ATOM   4746 C CA  . GLY D 4 64  ? 53.92173  67.66632  -3.74947  1.000 95.28458  ?  73  GLY B CA  1 
ATOM   4747 C C   . GLY D 4 64  ? 55.11923  68.29707  -3.07272  1.000 83.37752  ?  73  GLY B C   1 
ATOM   4748 O O   . GLY D 4 64  ? 55.31553  69.51289  -3.20413  1.000 76.34438  ?  73  GLY B O   1 
ATOM   4749 N N   . ALA D 4 65  ? 55.92784  67.51403  -2.36041  1.000 75.06022  ?  74  ALA B N   1 
ATOM   4750 C CA  . ALA D 4 65  ? 57.04272  68.07167  -1.60952  1.000 68.05746  ?  74  ALA B CA  1 
ATOM   4751 C C   . ALA D 4 65  ? 58.01139  66.96295  -1.22446  1.000 64.37481  ?  74  ALA B C   1 
ATOM   4752 O O   . ALA D 4 65  ? 57.59088  65.87747  -0.81701  1.000 66.72975  ?  74  ALA B O   1 
ATOM   4753 C CB  . ALA D 4 65  ? 56.55098  68.79983  -0.35367  1.000 50.35626  ?  74  ALA B CB  1 
ATOM   4754 N N   . ASP D 4 66  ? 59.30467  67.25018  -1.35137  1.000 71.75461  ?  75  ASP B N   1 
ATOM   4755 C CA  . ASP D 4 66  ? 60.36402  66.36252  -0.88967  1.000 63.58712  ?  75  ASP B CA  1 
ATOM   4756 C C   . ASP D 4 66  ? 60.87378  66.85953  0.45666   1.000 57.87052  ?  75  ASP B C   1 
ATOM   4757 O O   . ASP D 4 66  ? 61.21354  68.03890  0.59857   1.000 67.23785  ?  75  ASP B O   1 
ATOM   4758 C CB  . ASP D 4 66  ? 61.50946  66.30057  -1.90133  1.000 72.84261  ?  75  ASP B CB  1 
ATOM   4759 C CG  . ASP D 4 66  ? 61.07170  65.75354  -3.24574  1.000 87.27058  ?  75  ASP B CG  1 
ATOM   4760 O OD1 . ASP D 4 66  ? 60.14516  64.91652  -3.27563  1.000 104.88223 ?  75  ASP B OD1 1 
ATOM   4761 O OD2 . ASP D 4 66  ? 61.65522  66.15983  -4.27280  1.000 89.67742  -1 75  ASP B OD2 1 
ATOM   4762 N N   . TYR D 4 67  ? 60.92781  65.96420  1.43757   1.000 57.56887  ?  76  TYR B N   1 
ATOM   4763 C CA  . TYR D 4 67  ? 61.26129  66.32919  2.80528   1.000 49.03707  ?  76  TYR B CA  1 
ATOM   4764 C C   . TYR D 4 67  ? 62.65182  65.83917  3.18846   1.000 50.11016  ?  76  TYR B C   1 
ATOM   4765 O O   . TYR D 4 67  ? 63.19293  64.89549  2.60584   1.000 69.56104  ?  76  TYR B O   1 
ATOM   4766 C CB  . TYR D 4 67  ? 60.23082  65.76734  3.78887   1.000 54.04316  ?  76  TYR B CB  1 
ATOM   4767 C CG  . TYR D 4 67  ? 58.87273  66.41694  3.69365   1.000 55.51198  ?  76  TYR B CG  1 
ATOM   4768 C CD1 . TYR D 4 67  ? 58.66556  67.70459  4.16818   1.000 51.57911  ?  76  TYR B CD1 1 
ATOM   4769 C CD2 . TYR D 4 67  ? 57.79492  65.74043  3.13916   1.000 56.88452  ?  76  TYR B CD2 1 
ATOM   4770 C CE1 . TYR D 4 67  ? 57.42573  68.30383  4.08680   1.000 57.50491  ?  76  TYR B CE1 1 
ATOM   4771 C CE2 . TYR D 4 67  ? 56.54978  66.33155  3.05385   1.000 59.11747  ?  76  TYR B CE2 1 
ATOM   4772 C CZ  . TYR D 4 67  ? 56.37162  67.61310  3.52958   1.000 63.92554  ?  76  TYR B CZ  1 
ATOM   4773 O OH  . TYR D 4 67  ? 55.13514  68.20730  3.44870   1.000 63.61431  ?  76  TYR B OH  1 
ATOM   4774 N N   . LEU D 4 68  ? 63.22085  66.50526  4.19658   1.000 63.60538  ?  77  LEU B N   1 
ATOM   4775 C CA  . LEU D 4 68  ? 64.52756  66.13258  4.73673   1.000 49.53074  ?  77  LEU B CA  1 
ATOM   4776 C C   . LEU D 4 68  ? 64.60221  66.70825  6.15137   1.000 50.75370  ?  77  LEU B C   1 
ATOM   4777 O O   . LEU D 4 68  ? 64.87552  67.89955  6.32067   1.000 65.56289  ?  77  LEU B O   1 
ATOM   4778 C CB  . LEU D 4 68  ? 65.65827  66.64755  3.86022   1.000 57.29306  ?  77  LEU B CB  1 
ATOM   4779 C CG  . LEU D 4 68  ? 67.08260  66.49115  4.40112   1.000 63.06049  ?  77  LEU B CG  1 
ATOM   4780 C CD1 . LEU D 4 68  ? 67.39952  65.03255  4.68551   1.000 72.93409  ?  77  LEU B CD1 1 
ATOM   4781 C CD2 . LEU D 4 68  ? 68.09334  67.08173  3.43020   1.000 61.41860  ?  77  LEU B CD2 1 
ATOM   4782 N N   . ALA D 4 69  ? 64.34761  65.86329  7.14573   1.000 48.55274  ?  78  ALA B N   1 
ATOM   4783 C CA  . ALA D 4 69  ? 64.34100  66.27338  8.54141   1.000 45.65406  ?  78  ALA B CA  1 
ATOM   4784 C C   . ALA D 4 69  ? 65.67876  65.95923  9.19710   1.000 50.37429  ?  78  ALA B C   1 
ATOM   4785 O O   . ALA D 4 69  ? 66.35575  64.99214  8.83911   1.000 52.16610  ?  78  ALA B O   1 
ATOM   4786 C CB  . ALA D 4 69  ? 63.21256  65.58364  9.30955   1.000 55.66164  ?  78  ALA B CB  1 
ATOM   4787 N N   . THR D 4 70  ? 66.04948  66.78668  10.17267  1.000 53.19320  ?  79  THR B N   1 
ATOM   4788 C CA  . THR D 4 70  ? 67.33299  66.65882  10.84917  1.000 51.04866  ?  79  THR B CA  1 
ATOM   4789 C C   . THR D 4 70  ? 67.17504  67.03250  12.31467  1.000 57.72613  ?  79  THR B C   1 
ATOM   4790 O O   . THR D 4 70  ? 66.52824  68.03334  12.63847  1.000 59.87553  ?  79  THR B O   1 
ATOM   4791 C CB  . THR D 4 70  ? 68.39696  67.54733  10.19226  1.000 47.02911  ?  79  THR B CB  1 
ATOM   4792 O OG1 . THR D 4 70  ? 68.46328  67.25928  8.79039   1.000 78.99044  ?  79  THR B OG1 1 
ATOM   4793 C CG2 . THR D 4 70  ? 69.76236  67.29994  10.81580  1.000 70.33221  ?  79  THR B CG2 1 
ATOM   4794 N N   . ARG D 4 71  ? 67.75691  66.22000  13.19377  1.000 58.13192  ?  80  ARG B N   1 
ATOM   4795 C CA  . ARG D 4 71  ? 67.82929  66.51389  14.62324  1.000 55.89323  ?  80  ARG B CA  1 
ATOM   4796 C C   . ARG D 4 71  ? 69.24400  67.00993  14.90506  1.000 55.94601  ?  80  ARG B C   1 
ATOM   4797 O O   . ARG D 4 71  ? 70.16988  66.21398  15.07900  1.000 53.51707  ?  80  ARG B O   1 
ATOM   4798 C CB  . ARG D 4 71  ? 67.48192  65.28142  15.45165  1.000 41.05520  ?  80  ARG B CB  1 
ATOM   4799 C CG  . ARG D 4 71  ? 67.42125  65.52624  16.95105  1.000 44.28633  ?  80  ARG B CG  1 
ATOM   4800 C CD  . ARG D 4 71  ? 66.30283  66.49056  17.31512  1.000 41.82573  ?  80  ARG B CD  1 
ATOM   4801 N NE  . ARG D 4 71  ? 66.16123  66.64389  18.75871  1.000 49.34580  ?  80  ARG B NE  1 
ATOM   4802 C CZ  . ARG D 4 71  ? 65.32528  65.93927  19.50981  1.000 45.97236  ?  80  ARG B CZ  1 
ATOM   4803 N NH1 . ARG D 4 71  ? 64.53061  65.02099  18.98519  1.000 44.98182  ?  80  ARG B NH1 1 
ATOM   4804 N NH2 . ARG D 4 71  ? 65.28458  66.16248  20.82034  1.000 43.43907  ?  80  ARG B NH2 1 
ATOM   4805 N N   . VAL D 4 72  ? 69.41059  68.33243  14.94055  1.000 57.67785  ?  81  VAL B N   1 
ATOM   4806 C CA  . VAL D 4 72  ? 70.74723  68.91440  15.04174  1.000 54.69725  ?  81  VAL B CA  1 
ATOM   4807 C C   . VAL D 4 72  ? 71.30518  68.73636  16.44956  1.000 66.19995  ?  81  VAL B C   1 
ATOM   4808 O O   . VAL D 4 72  ? 72.33753  68.08594  16.64950  1.000 72.68560  ?  81  VAL B O   1 
ATOM   4809 C CB  . VAL D 4 72  ? 70.72252  70.39500  14.62537  1.000 49.31258  ?  81  VAL B CB  1 
ATOM   4810 C CG1 . VAL D 4 72  ? 72.06653  71.04301  14.89264  1.000 50.30523  ?  81  VAL B CG1 1 
ATOM   4811 C CG2 . VAL D 4 72  ? 70.36321  70.51677  13.15717  1.000 40.99959  ?  81  VAL B CG2 1 
ATOM   4812 N N   . THR D 4 73  ? 70.64037  69.31810  17.44105  1.000 67.52669  ?  83  THR B N   1 
ATOM   4813 C CA  . THR D 4 73  ? 71.05770  69.21158  18.83273  1.000 57.70248  ?  83  THR B CA  1 
ATOM   4814 C C   . THR D 4 73  ? 69.95191  68.53485  19.64207  1.000 50.92211  ?  83  THR B C   1 
ATOM   4815 O O   . THR D 4 73  ? 69.00562  67.96649  19.09013  1.000 49.61281  ?  83  THR B O   1 
ATOM   4816 C CB  . THR D 4 73  ? 71.40811  70.58807  19.40642  1.000 49.76954  ?  83  THR B CB  1 
ATOM   4817 O OG1 . THR D 4 73  ? 70.22363  71.38931  19.50038  1.000 57.37585  ?  83  THR B OG1 1 
ATOM   4818 C CG2 . THR D 4 73  ? 72.42115  71.29457  18.51985  1.000 52.39319  ?  83  THR B CG2 1 
ATOM   4819 N N   . ASP D 4 74  ? 70.07999  68.60424  20.96915  1.000 64.36083  ?  84  ASP B N   1 
ATOM   4820 C CA  . ASP D 4 74  ? 69.08246  68.00997  21.85056  1.000 50.59238  ?  84  ASP B CA  1 
ATOM   4821 C C   . ASP D 4 74  ? 67.73418  68.71070  21.75715  1.000 60.81356  ?  84  ASP B C   1 
ATOM   4822 O O   . ASP D 4 74  ? 66.71648  68.12034  22.13488  1.000 51.20842  ?  84  ASP B O   1 
ATOM   4823 C CB  . ASP D 4 74  ? 69.57802  68.03511  23.29775  1.000 70.77986  ?  84  ASP B CB  1 
ATOM   4824 C CG  . ASP D 4 74  ? 70.86832  67.26165  23.48630  1.000 105.05364 ?  84  ASP B CG  1 
ATOM   4825 O OD1 . ASP D 4 74  ? 71.01119  66.18236  22.87448  1.000 112.04104 ?  84  ASP B OD1 1 
ATOM   4826 O OD2 . ASP D 4 74  ? 71.74142  67.73477  24.24422  1.000 116.60076 -1 84  ASP B OD2 1 
ATOM   4827 N N   . THR D 4 75  ? 67.70253  69.95183  21.26662  1.000 61.35830  ?  85  THR B N   1 
ATOM   4828 C CA  . THR D 4 75  ? 66.46699  70.71358  21.17169  1.000 51.26187  ?  85  THR B CA  1 
ATOM   4829 C C   . THR D 4 75  ? 66.22095  71.31184  19.79329  1.000 54.73921  ?  85  THR B C   1 
ATOM   4830 O O   . THR D 4 75  ? 65.20423  71.98915  19.60779  1.000 56.51845  ?  85  THR B O   1 
ATOM   4831 C CB  . THR D 4 75  ? 66.45188  71.84486  22.21242  1.000 56.42245  ?  85  THR B CB  1 
ATOM   4832 O OG1 . THR D 4 75  ? 67.60509  72.67678  22.03371  1.000 69.52436  ?  85  THR B OG1 1 
ATOM   4833 C CG2 . THR D 4 75  ? 66.45379  71.27738  23.62423  1.000 55.06722  ?  85  THR B CG2 1 
ATOM   4834 N N   . GLU D 4 76  ? 67.10715  71.08523  18.82747  1.000 58.00791  ?  86  GLU B N   1 
ATOM   4835 C CA  . GLU D 4 76  ? 66.99293  71.67961  17.50156  1.000 55.05892  ?  86  GLU B CA  1 
ATOM   4836 C C   . GLU D 4 76  ? 66.49554  70.63048  16.51441  1.000 64.84545  ?  86  GLU B C   1 
ATOM   4837 O O   . GLU D 4 76  ? 67.12502  69.57982  16.34738  1.000 62.81070  ?  86  GLU B O   1 
ATOM   4838 C CB  . GLU D 4 76  ? 68.33513  72.25129  17.04516  1.000 68.72711  ?  86  GLU B CB  1 
ATOM   4839 C CG  . GLU D 4 76  ? 68.27280  73.04166  15.74663  1.000 60.29379  ?  86  GLU B CG  1 
ATOM   4840 C CD  . GLU D 4 76  ? 67.63176  74.40494  15.91987  1.000 61.11085  ?  86  GLU B CD  1 
ATOM   4841 O OE1 . GLU D 4 76  ? 67.45869  74.84162  17.07750  1.000 65.11642  ?  86  GLU B OE1 1 
ATOM   4842 O OE2 . GLU D 4 76  ? 67.30298  75.04179  14.89686  1.000 64.88632  -1 86  GLU B OE2 1 
ATOM   4843 N N   . LEU D 4 77  ? 65.37175  70.92080  15.86187  1.000 56.07845  ?  87  LEU B N   1 
ATOM   4844 C CA  . LEU D 4 77  ? 64.79252  70.04635  14.84922  1.000 47.32819  ?  87  LEU B CA  1 
ATOM   4845 C C   . LEU D 4 77  ? 64.59818  70.85362  13.57569  1.000 45.57528  ?  87  LEU B C   1 
ATOM   4846 O O   . LEU D 4 77  ? 63.91811  71.88487  13.59111  1.000 62.41280  ?  87  LEU B O   1 
ATOM   4847 C CB  . LEU D 4 77  ? 63.46165  69.45554  15.32323  1.000 55.07244  ?  87  LEU B CB  1 
ATOM   4848 C CG  . LEU D 4 77  ? 62.74265  68.50780  14.36072  1.000 50.53975  ?  87  LEU B CG  1 
ATOM   4849 C CD1 . LEU D 4 77  ? 63.49856  67.19472  14.22154  1.000 49.02062  ?  87  LEU B CD1 1 
ATOM   4850 C CD2 . LEU D 4 77  ? 61.31071  68.26510  14.81261  1.000 48.13494  ?  87  LEU B CD2 1 
ATOM   4851 N N   . ARG D 4 78  ? 65.19267  70.38944  12.48177  1.000 42.45305  ?  88  ARG B N   1 
ATOM   4852 C CA  . ARG D 4 78  ? 65.13945  71.07858  11.20251  1.000 46.42070  ?  88  ARG B CA  1 
ATOM   4853 C C   . ARG D 4 78  ? 64.30354  70.28515  10.20704  1.000 53.28225  ?  88  ARG B C   1 
ATOM   4854 O O   . ARG D 4 78  ? 64.04596  69.09165  10.38608  1.000 60.64989  ?  88  ARG B O   1 
ATOM   4855 C CB  . ARG D 4 78  ? 66.54740  71.29573  10.63791  1.000 51.12651  ?  88  ARG B CB  1 
ATOM   4856 C CG  . ARG D 4 78  ? 67.50960  71.96867  11.59876  1.000 48.95826  ?  88  ARG B CG  1 
ATOM   4857 C CD  . ARG D 4 78  ? 67.38999  73.48032  11.56159  1.000 46.81559  ?  88  ARG B CD  1 
ATOM   4858 N NE  . ARG D 4 78  ? 68.31699  74.11204  12.49337  1.000 67.01486  ?  88  ARG B NE  1 
ATOM   4859 C CZ  . ARG D 4 78  ? 69.60634  74.30812  12.25222  1.000 56.42408  ?  88  ARG B CZ  1 
ATOM   4860 N NH1 . ARG D 4 78  ? 70.16279  73.92873  11.11350  1.000 57.91016  ?  88  ARG B NH1 1 
ATOM   4861 N NH2 . ARG D 4 78  ? 70.35725  74.89658  13.17842  1.000 54.62429  ?  88  ARG B NH2 1 
ATOM   4862 N N   . LEU D 4 79  ? 63.88310  70.97014  9.14511   1.000 51.09522  ?  89  LEU B N   1 
ATOM   4863 C CA  . LEU D 4 79  ? 63.12966  70.33521  8.07137   1.000 53.34551  ?  89  LEU B CA  1 
ATOM   4864 C C   . LEU D 4 79  ? 63.31154  71.14884  6.80096   1.000 55.93474  ?  89  LEU B C   1 
ATOM   4865 O O   . LEU D 4 79  ? 63.07379  72.36048  6.80089   1.000 55.06623  ?  89  LEU B O   1 
ATOM   4866 C CB  . LEU D 4 79  ? 61.64204  70.22228  8.42137   1.000 60.47656  ?  89  LEU B CB  1 
ATOM   4867 C CG  . LEU D 4 79  ? 60.74917  69.63281  7.32662   1.000 49.97318  ?  89  LEU B CG  1 
ATOM   4868 C CD1 . LEU D 4 79  ? 61.19137  68.22026  6.97400   1.000 57.56154  ?  89  LEU B CD1 1 
ATOM   4869 C CD2 . LEU D 4 79  ? 59.29015  69.65153  7.74926   1.000 54.75669  ?  89  LEU B CD2 1 
ATOM   4870 N N   . GLN D 4 80  ? 63.73180  70.48511  5.72903   1.000 49.58536  ?  90  GLN B N   1 
ATOM   4871 C CA  . GLN D 4 80  ? 63.89226  71.11271  4.42570   1.000 47.69404  ?  90  GLN B CA  1 
ATOM   4872 C C   . GLN D 4 80  ? 62.83212  70.57238  3.47740   1.000 52.80993  ?  90  GLN B C   1 
ATOM   4873 O O   . GLN D 4 80  ? 62.65686  69.35469  3.36355   1.000 65.97481  ?  90  GLN B O   1 
ATOM   4874 C CB  . GLN D 4 80  ? 65.29141  70.86406  3.86021   1.000 46.94251  ?  90  GLN B CB  1 
ATOM   4875 C CG  . GLN D 4 80  ? 65.50916  71.46236  2.48090   1.000 70.72429  ?  90  GLN B CG  1 
ATOM   4876 C CD  . GLN D 4 80  ? 66.93879  71.32137  2.00283   1.000 75.80231  ?  90  GLN B CD  1 
ATOM   4877 O OE1 . GLN D 4 80  ? 67.87793  71.72604  2.68870   1.000 74.66013  ?  90  GLN B OE1 1 
ATOM   4878 N NE2 . GLN D 4 80  ? 67.11233  70.74092  0.82085   1.000 81.09258  ?  90  GLN B NE2 1 
ATOM   4879 N N   . VAL D 4 81  ? 62.12665  71.47755  2.80605   1.000 55.73615  ?  91  VAL B N   1 
ATOM   4880 C CA  . VAL D 4 81  ? 61.04269  71.12842  1.89559   1.000 54.31874  ?  91  VAL B CA  1 
ATOM   4881 C C   . VAL D 4 81  ? 61.40513  71.68127  0.52497   1.000 54.13696  ?  91  VAL B C   1 
ATOM   4882 O O   . VAL D 4 81  ? 61.32218  72.89489  0.29737   1.000 64.47770  ?  91  VAL B O   1 
ATOM   4883 C CB  . VAL D 4 81  ? 59.69249  71.67850  2.37294   1.000 51.07141  ?  91  VAL B CB  1 
ATOM   4884 C CG1 . VAL D 4 81  ? 58.55434  70.94136  1.69721   1.000 49.65695  ?  91  VAL B CG1 1 
ATOM   4885 C CG2 . VAL D 4 81  ? 59.58088  71.57553  3.88523   1.000 47.03204  ?  91  VAL B CG2 1 
ATOM   4886 N N   . ALA D 4 82  ? 61.80160  70.79933  -0.38740  1.000 54.73512  ?  92  ALA B N   1 
ATOM   4887 C CA  . ALA D 4 82  ? 62.24312  71.18429  -1.71926  1.000 64.43194  ?  92  ALA B CA  1 
ATOM   4888 C C   . ALA D 4 82  ? 61.29223  70.62838  -2.77210  1.000 70.53430  ?  92  ALA B C   1 
ATOM   4889 O O   . ALA D 4 82  ? 60.47491  69.74373  -2.50235  1.000 71.85067  ?  92  ALA B O   1 
ATOM   4890 C CB  . ALA D 4 82  ? 63.67377  70.69966  -1.98699  1.000 74.91385  ?  92  ALA B CB  1 
ATOM   4891 N N   . ASN D 4 83  ? 61.41951  71.16596  -3.98841  1.000 73.26377  ?  93  ASN B N   1 
ATOM   4892 C CA  . ASN D 4 83  ? 60.59215  70.76573  -5.12933  1.000 74.44459  ?  93  ASN B CA  1 
ATOM   4893 C C   . ASN D 4 83  ? 59.10653  70.85771  -4.79325  1.000 77.36175  ?  93  ASN B C   1 
ATOM   4894 O O   . ASN D 4 83  ? 58.31752  69.96345  -5.10499  1.000 90.01955  ?  93  ASN B O   1 
ATOM   4895 C CB  . ASN D 4 83  ? 60.95785  69.35991  -5.61026  1.000 64.58855  ?  93  ASN B CB  1 
ATOM   4896 C CG  . ASN D 4 83  ? 62.36242  69.28436  -6.17549  1.000 87.93434  ?  93  ASN B CG  1 
ATOM   4897 O OD1 . ASN D 4 83  ? 62.59077  69.59683  -7.34436  1.000 101.63578 ?  93  ASN B OD1 1 
ATOM   4898 N ND2 . ASN D 4 83  ? 63.31258  68.86509  -5.34734  1.000 83.73833  ?  93  ASN B ND2 1 
ATOM   4899 N N   . MET D 4 84  ? 58.72208  71.95667  -4.15145  1.000 85.83551  ?  94  MET B N   1 
ATOM   4900 C CA  . MET D 4 84  ? 57.35310  72.12777  -3.68467  1.000 83.96456  ?  94  MET B CA  1 
ATOM   4901 C C   . MET D 4 84  ? 56.47964  72.64874  -4.81918  1.000 86.70278  ?  94  MET B C   1 
ATOM   4902 O O   . MET D 4 84  ? 56.78237  73.68547  -5.42019  1.000 86.44005  ?  94  MET B O   1 
ATOM   4903 C CB  . MET D 4 84  ? 57.31394  73.08177  -2.49410  1.000 84.01691  ?  94  MET B CB  1 
ATOM   4904 C CG  . MET D 4 84  ? 56.20286  72.78629  -1.50235  1.000 85.95084  ?  94  MET B CG  1 
ATOM   4905 S SD  . MET D 4 84  ? 56.13238  74.00093  -0.17440  1.000 95.52514  ?  94  MET B SD  1 
ATOM   4906 C CE  . MET D 4 84  ? 57.87141  74.17247  0.21421   1.000 82.24216  ?  94  MET B CE  1 
ATOM   4907 N N   . SER D 4 85  ? 55.39798  71.92592  -5.11232  1.000 91.69084  ?  95  SER B N   1 
ATOM   4908 C CA  . SER D 4 85  ? 54.42505  72.34494  -6.10841  1.000 88.16288  ?  95  SER B CA  1 
ATOM   4909 C C   . SER D 4 85  ? 53.00549  72.43105  -5.56899  1.000 81.35376  ?  95  SER B C   1 
ATOM   4910 O O   . SER D 4 85  ? 52.11101  72.86448  -6.30386  1.000 84.08592  ?  95  SER B O   1 
ATOM   4911 C CB  . SER D 4 85  ? 54.44323  71.39217  -7.31446  1.000 84.57298  ?  95  SER B CB  1 
ATOM   4912 O OG  . SER D 4 85  ? 54.14855  70.06498  -6.91756  1.000 90.62103  ?  95  SER B OG  1 
ATOM   4913 N N   . GLN D 4 86  ? 52.77101  72.03052  -4.32063  1.000 84.05239  ?  98  GLN B N   1 
ATOM   4914 C CA  . GLN D 4 86  ? 51.45444  72.10293  -3.70156  1.000 79.95425  ?  98  GLN B CA  1 
ATOM   4915 C C   . GLN D 4 86  ? 51.61225  72.62697  -2.28330  1.000 77.36551  ?  98  GLN B C   1 
ATOM   4916 O O   . GLN D 4 86  ? 52.45134  72.12883  -1.52712  1.000 82.74415  ?  98  GLN B O   1 
ATOM   4917 C CB  . GLN D 4 86  ? 50.76691  70.73110  -3.68716  1.000 96.80764  ?  98  GLN B CB  1 
ATOM   4918 C CG  . GLN D 4 86  ? 50.57939  70.10481  -5.06217  1.000 111.82498 ?  98  GLN B CG  1 
ATOM   4919 C CD  . GLN D 4 86  ? 50.01465  68.69798  -4.99228  1.000 113.82459 ?  98  GLN B CD  1 
ATOM   4920 O OE1 . GLN D 4 86  ? 49.57678  68.24359  -3.93519  1.000 105.85916 ?  98  GLN B OE1 1 
ATOM   4921 N NE2 . GLN D 4 86  ? 50.02628  67.99892  -6.12172  1.000 107.11223 ?  98  GLN B NE2 1 
ATOM   4922 N N   . GLY D 4 87  ? 50.81143  73.62957  -1.92845  1.000 83.89297  ?  99  GLY B N   1 
ATOM   4923 C CA  . GLY D 4 87  ? 50.88804  74.19633  -0.59924  1.000 68.92737  ?  99  GLY B CA  1 
ATOM   4924 C C   . GLY D 4 87  ? 50.38078  73.24596  0.46766   1.000 69.52267  ?  99  GLY B C   1 
ATOM   4925 O O   . GLY D 4 87  ? 49.57063  72.35212  0.21892   1.000 77.17327  ?  99  GLY B O   1 
ATOM   4926 N N   . ARG D 4 88  ? 50.87061  73.45441  1.68686   1.000 61.74460  ?  100 ARG B N   1 
ATOM   4927 C CA  . ARG D 4 88  ? 50.53757  72.58890  2.81172   1.000 56.63710  ?  100 ARG B CA  1 
ATOM   4928 C C   . ARG D 4 88  ? 50.99662  73.26317  4.09682   1.000 56.10100  ?  100 ARG B C   1 
ATOM   4929 O O   . ARG D 4 88  ? 51.71568  74.26535  4.07429   1.000 56.44447  ?  100 ARG B O   1 
ATOM   4930 C CB  . ARG D 4 88  ? 51.18013  71.20851  2.66060   1.000 57.82680  ?  100 ARG B CB  1 
ATOM   4931 C CG  . ARG D 4 88  ? 52.67131  71.25594  2.37970   1.000 57.93216  ?  100 ARG B CG  1 
ATOM   4932 C CD  . ARG D 4 88  ? 53.14178  69.96645  1.73789   1.000 57.30228  ?  100 ARG B CD  1 
ATOM   4933 N NE  . ARG D 4 88  ? 52.41531  69.68443  0.50609   1.000 81.41481  ?  100 ARG B NE  1 
ATOM   4934 C CZ  . ARG D 4 88  ? 52.57390  68.58931  -0.22402  1.000 92.85258  ?  100 ARG B CZ  1 
ATOM   4935 N NH1 . ARG D 4 88  ? 53.43370  67.64602  0.12286   1.000 72.19651  ?  100 ARG B NH1 1 
ATOM   4936 N NH2 . ARG D 4 88  ? 51.84928  68.43566  -1.32851  1.000 107.20044 ?  100 ARG B NH2 1 
ATOM   4937 N N   . THR D 4 89  ? 50.56936  72.69499  5.22151   1.000 61.18005  ?  101 THR B N   1 
ATOM   4938 C CA  . THR D 4 89  ? 50.95463  73.16317  6.54451   1.000 58.55481  ?  101 THR B CA  1 
ATOM   4939 C C   . THR D 4 89  ? 51.74803  72.07290  7.25067   1.000 57.71491  ?  101 THR B C   1 
ATOM   4940 O O   . THR D 4 89  ? 51.37606  70.89580  7.20890   1.000 64.15718  ?  101 THR B O   1 
ATOM   4941 C CB  . THR D 4 89  ? 49.72828  73.54610  7.38282   1.000 64.66615  ?  101 THR B CB  1 
ATOM   4942 O OG1 . THR D 4 89  ? 48.91003  74.46335  6.64577   1.000 81.99924  ?  101 THR B OG1 1 
ATOM   4943 C CG2 . THR D 4 89  ? 50.15792  74.20114  8.68772   1.000 46.68045  ?  101 THR B CG2 1 
ATOM   4944 N N   . LEU D 4 90  ? 52.84422  72.46810  7.89380   1.000 60.12636  ?  102 LEU B N   1 
ATOM   4945 C CA  . LEU D 4 90  ? 53.73615  71.54369  8.58321   1.000 51.13466  ?  102 LEU B CA  1 
ATOM   4946 C C   . LEU D 4 90  ? 53.75351  71.88217  10.06585  1.000 48.01517  ?  102 LEU B C   1 
ATOM   4947 O O   . LEU D 4 90  ? 54.09794  73.00619  10.44613  1.000 52.56863  ?  102 LEU B O   1 
ATOM   4948 C CB  . LEU D 4 90  ? 55.14728  71.60575  7.99647   1.000 51.90729  ?  102 LEU B CB  1 
ATOM   4949 C CG  . LEU D 4 90  ? 55.30563  70.96390  6.61784   1.000 56.70562  ?  102 LEU B CG  1 
ATOM   4950 C CD1 . LEU D 4 90  ? 56.59812  71.41151  5.96414   1.000 85.21854  ?  102 LEU B CD1 1 
ATOM   4951 C CD2 . LEU D 4 90  ? 55.26251  69.44838  6.73543   1.000 41.21543  ?  102 LEU B CD2 1 
ATOM   4952 N N   . TYR D 4 91  ? 53.38635  70.91172  10.89620  1.000 59.18877  ?  103 TYR B N   1 
ATOM   4953 C CA  . TYR D 4 91  ? 53.34040  71.07954  12.34141  1.000 61.80662  ?  103 TYR B CA  1 
ATOM   4954 C C   . TYR D 4 91  ? 54.50874  70.34433  12.98049  1.000 57.12533  ?  103 TYR B C   1 
ATOM   4955 O O   . TYR D 4 91  ? 54.72757  69.15974  12.70550  1.000 59.47179  ?  103 TYR B O   1 
ATOM   4956 C CB  . TYR D 4 91  ? 52.02171  70.55614  12.91546  1.000 54.81431  ?  103 TYR B CB  1 
ATOM   4957 C CG  . TYR D 4 91  ? 50.82368  71.42640  12.61825  1.000 55.16704  ?  103 TYR B CG  1 
ATOM   4958 C CD1 . TYR D 4 91  ? 50.47004  72.46565  13.46837  1.000 57.17468  ?  103 TYR B CD1 1 
ATOM   4959 C CD2 . TYR D 4 91  ? 50.04088  71.20440  11.49330  1.000 60.16436  ?  103 TYR B CD2 1 
ATOM   4960 C CE1 . TYR D 4 91  ? 49.37349  73.26370  13.20382  1.000 69.67115  ?  103 TYR B CE1 1 
ATOM   4961 C CE2 . TYR D 4 91  ? 48.94199  71.99671  11.22045  1.000 66.45605  ?  103 TYR B CE2 1 
ATOM   4962 C CZ  . TYR D 4 91  ? 48.61335  73.02478  12.07870  1.000 65.19059  ?  103 TYR B CZ  1 
ATOM   4963 O OH  . TYR D 4 91  ? 47.52080  73.81641  11.81105  1.000 82.58621  ?  103 TYR B OH  1 
ATOM   4964 N N   . CYS D 4 92  ? 55.25569  71.04760  13.82627  1.000 60.20235  ?  104 CYS B N   1 
ATOM   4965 C CA  . CYS D 4 92  ? 56.27439  70.42340  14.65732  1.000 44.53142  ?  104 CYS B CA  1 
ATOM   4966 C C   . CYS D 4 92  ? 55.62966  69.94262  15.94914  1.000 56.43317  ?  104 CYS B C   1 
ATOM   4967 O O   . CYS D 4 92  ? 54.86056  70.67830  16.57598  1.000 61.27474  ?  104 CYS B O   1 
ATOM   4968 C CB  . CYS D 4 92  ? 57.40739  71.39935  14.96846  1.000 51.59935  ?  104 CYS B CB  1 
ATOM   4969 S SG  . CYS D 4 92  ? 58.62553  70.73536  16.12398  1.000 71.72502  ?  104 CYS B SG  1 
ATOM   4970 N N   . THR D 4 93  ? 55.93934  68.71103  16.34313  1.000 50.29567  ?  105 THR B N   1 
ATOM   4971 C CA  . THR D 4 93  ? 55.33232  68.10639  17.51721  1.000 53.87102  ?  105 THR B CA  1 
ATOM   4972 C C   . THR D 4 93  ? 56.40955  67.55820  18.44150  1.000 50.76342  ?  105 THR B C   1 
ATOM   4973 O O   . THR D 4 93  ? 57.53161  67.26491  18.02265  1.000 57.36729  ?  105 THR B O   1 
ATOM   4974 C CB  . THR D 4 93  ? 54.36056  66.98073  17.13854  1.000 64.17778  ?  105 THR B CB  1 
ATOM   4975 O OG1 . THR D 4 93  ? 55.07864  65.92337  16.49360  1.000 59.42241  ?  105 THR B OG1 1 
ATOM   4976 C CG2 . THR D 4 93  ? 53.28302  67.49540  16.20099  1.000 52.64592  ?  105 THR B CG2 1 
ATOM   4977 N N   . CYS D 4 94  ? 56.04610  67.42882  19.71508  1.000 51.21120  ?  106 CYS B N   1 
ATOM   4978 C CA  . CYS D 4 94  ? 56.88878  66.81202  20.72674  1.000 51.53059  ?  106 CYS B CA  1 
ATOM   4979 C C   . CYS D 4 94  ? 56.03815  65.86504  21.56017  1.000 57.79977  ?  106 CYS B C   1 
ATOM   4980 O O   . CYS D 4 94  ? 54.83456  66.07867  21.73297  1.000 60.14058  ?  106 CYS B O   1 
ATOM   4981 C CB  . CYS D 4 94  ? 57.55297  67.85913  21.63078  1.000 50.53181  ?  106 CYS B CB  1 
ATOM   4982 S SG  . CYS D 4 94  ? 56.39540  68.83867  22.61356  1.000 64.91129  ?  106 CYS B SG  1 
ATOM   4983 N N   . SER D 4 95  ? 56.67188  64.81381  22.07735  1.000 54.16034  ?  107 SER B N   1 
ATOM   4984 C CA  . SER D 4 95  ? 55.95082  63.78419  22.81232  1.000 58.65283  ?  107 SER B CA  1 
ATOM   4985 C C   . SER D 4 95  ? 56.94253  62.97716  23.63159  1.000 57.21444  ?  107 SER B C   1 
ATOM   4986 O O   . SER D 4 95  ? 58.10804  62.85440  23.23890  1.000 56.09092  ?  107 SER B O   1 
ATOM   4987 C CB  . SER D 4 95  ? 55.17852  62.86416  21.85512  1.000 60.99038  ?  107 SER B CB  1 
ATOM   4988 O OG  . SER D 4 95  ? 54.65905  61.73416  22.53423  1.000 63.79947  ?  107 SER B OG  1 
ATOM   4989 N N   . PRO D 4 96  ? 56.52477  62.43231  24.76742  1.000 61.47735  ?  108 PRO B N   1 
ATOM   4990 C CA  . PRO D 4 96  ? 57.34544  61.45324  25.48370  1.000 67.40968  ?  108 PRO B CA  1 
ATOM   4991 C C   . PRO D 4 96  ? 57.21891  60.09160  24.80795  1.000 67.88744  ?  108 PRO B C   1 
ATOM   4992 O O   . PRO D 4 96  ? 56.52976  59.93357  23.80217  1.000 68.91145  ?  108 PRO B O   1 
ATOM   4993 C CB  . PRO D 4 96  ? 56.74208  61.44134  26.89552  1.000 57.07477  ?  108 PRO B CB  1 
ATOM   4994 C CG  . PRO D 4 96  ? 55.75938  62.58994  26.93429  1.000 55.23470  ?  108 PRO B CG  1 
ATOM   4995 C CD  . PRO D 4 96  ? 55.31522  62.78372  25.52486  1.000 55.88046  ?  108 PRO B CD  1 
ATOM   4996 N N   . GLN D 4 97  ? 57.90223  59.09668  25.37872  1.000 66.85663  ?  109 GLN B N   1 
ATOM   4997 C CA  . GLN D 4 97  ? 57.77385  57.74332  24.84886  1.000 60.80596  ?  109 GLN B CA  1 
ATOM   4998 C C   . GLN D 4 97  ? 56.35362  57.22740  25.02684  1.000 69.44057  ?  109 GLN B C   1 
ATOM   4999 O O   . GLN D 4 97  ? 55.78787  56.61424  24.11384  1.000 70.92824  ?  109 GLN B O   1 
ATOM   5000 C CB  . GLN D 4 97  ? 58.78279  56.80898  25.51322  1.000 66.04268  ?  109 GLN B CB  1 
ATOM   5001 C CG  . GLN D 4 97  ? 58.96810  55.49908  24.76474  1.000 63.17669  ?  109 GLN B CG  1 
ATOM   5002 C CD  . GLN D 4 97  ? 60.15925  54.70503  25.25494  1.000 71.36975  ?  109 GLN B CD  1 
ATOM   5003 O OE1 . GLN D 4 97  ? 61.11231  54.47452  24.51061  1.000 75.79957  ?  109 GLN B OE1 1 
ATOM   5004 N NE2 . GLN D 4 97  ? 60.11017  54.27572  26.51096  1.000 82.22140  ?  109 GLN B NE2 1 
ATOM   5005 N N   . THR D 4 98  ? 55.76259  57.46682  26.19416  1.000 67.15062  ?  110 THR B N   1 
ATOM   5006 C CA  . THR D 4 98  ? 54.32420  57.29873  26.36370  1.000 66.60369  ?  110 THR B CA  1 
ATOM   5007 C C   . THR D 4 98  ? 53.62485  58.32885  25.48730  1.000 77.54133  ?  110 THR B C   1 
ATOM   5008 O O   . THR D 4 98  ? 53.65908  59.52736  25.78238  1.000 90.40292  ?  110 THR B O   1 
ATOM   5009 C CB  . THR D 4 98  ? 53.93139  57.45810  27.83024  1.000 71.12622  ?  110 THR B CB  1 
ATOM   5010 O OG1 . THR D 4 98  ? 54.60661  56.46855  28.61786  1.000 78.52503  ?  110 THR B OG1 1 
ATOM   5011 C CG2 . THR D 4 98  ? 52.43114  57.29693  28.00323  1.000 91.58725  ?  110 THR B CG2 1 
ATOM   5012 N N   . THR D 4 99  ? 53.00369  57.86385  24.40489  1.000 65.46879  ?  111 THR B N   1 
ATOM   5013 C CA  . THR D 4 99  ? 52.55734  58.75202  23.33726  1.000 57.95413  ?  111 THR B CA  1 
ATOM   5014 C C   . THR D 4 99  ? 51.58346  59.80292  23.85550  1.000 72.50523  ?  111 THR B C   1 
ATOM   5015 O O   . THR D 4 99  ? 50.48120  59.47901  24.30867  1.000 74.78502  ?  111 THR B O   1 
ATOM   5016 C CB  . THR D 4 99  ? 51.91529  57.93866  22.21505  1.000 60.63841  ?  111 THR B CB  1 
ATOM   5017 O OG1 . THR D 4 99  ? 52.88461  57.03731  21.66588  1.000 89.38524  ?  111 THR B OG1 1 
ATOM   5018 C CG2 . THR D 4 99  ? 51.41205  58.85913  21.11413  1.000 62.96872  ?  111 THR B CG2 1 
ATOM   5019 N N   . GLU D 4 100 ? 52.00713  61.06634  23.78897  1.000 71.98438  ?  112 GLU B N   1 
ATOM   5020 C CA  . GLU D 4 100 ? 51.17013  62.21726  24.13458  1.000 72.06727  ?  112 GLU B CA  1 
ATOM   5021 C C   . GLU D 4 100 ? 51.67184  63.38043  23.27602  1.000 67.19955  ?  112 GLU B C   1 
ATOM   5022 O O   . GLU D 4 100 ? 52.50300  64.17936  23.71278  1.000 70.48124  ?  112 GLU B O   1 
ATOM   5023 C CB  . GLU D 4 100 ? 51.23162  62.53710  25.62089  1.000 82.57392  ?  112 GLU B CB  1 
ATOM   5024 C CG  . GLU D 4 100 ? 50.28150  63.63998  26.06023  1.000 84.67442  ?  112 GLU B CG  1 
ATOM   5025 C CD  . GLU D 4 100 ? 50.31033  63.87228  27.55830  1.000 103.31242 ?  112 GLU B CD  1 
ATOM   5026 O OE1 . GLU D 4 100 ? 51.07842  63.17630  28.25552  1.000 96.45036  ?  112 GLU B OE1 1 
ATOM   5027 O OE2 . GLU D 4 100 ? 49.56373  64.75058  28.03904  1.000 122.12200 -1 112 GLU B OE2 1 
ATOM   5028 N N   . VAL D 4 101 ? 51.16190  63.45271  22.05107  1.000 65.35848  ?  113 VAL B N   1 
ATOM   5029 C CA  . VAL D 4 101 ? 51.68820  64.37051  21.04667  1.000 57.27550  ?  113 VAL B CA  1 
ATOM   5030 C C   . VAL D 4 101 ? 51.13153  65.76809  21.28638  1.000 67.81667  ?  113 VAL B C   1 
ATOM   5031 O O   . VAL D 4 101 ? 49.92401  65.94546  21.48828  1.000 58.33183  ?  113 VAL B O   1 
ATOM   5032 C CB  . VAL D 4 101 ? 51.35038  63.87078  19.63326  1.000 65.09374  ?  113 VAL B CB  1 
ATOM   5033 C CG1 . VAL D 4 101 ? 51.89816  64.81943  18.58640  1.000 67.02731  ?  113 VAL B CG1 1 
ATOM   5034 C CG2 . VAL D 4 101 ? 51.89954  62.46742  19.42452  1.000 49.89311  ?  113 VAL B CG2 1 
ATOM   5035 N N   . PHE D 4 102 ? 52.01475  66.76534  21.25987  1.000 61.17241  ?  114 PHE B N   1 
ATOM   5036 C CA  . PHE D 4 102 ? 51.64906  68.16795  21.42184  1.000 64.75221  ?  114 PHE B CA  1 
ATOM   5037 C C   . PHE D 4 102 ? 52.05111  68.91996  20.16157  1.000 57.04536  ?  114 PHE B C   1 
ATOM   5038 O O   . PHE D 4 102 ? 53.23713  68.97233  19.81973  1.000 68.71101  ?  114 PHE B O   1 
ATOM   5039 C CB  . PHE D 4 102 ? 52.32547  68.77418  22.65480  1.000 69.34320  ?  114 PHE B CB  1 
ATOM   5040 C CG  . PHE D 4 102 ? 52.14704  70.26256  22.77904  1.000 82.18279  ?  114 PHE B CG  1 
ATOM   5041 C CD1 . PHE D 4 102 ? 50.99783  70.79151  23.34265  1.000 75.41787  ?  114 PHE B CD1 1 
ATOM   5042 C CD2 . PHE D 4 102 ? 53.13472  71.13260  22.34184  1.000 77.77002  ?  114 PHE B CD2 1 
ATOM   5043 C CE1 . PHE D 4 102 ? 50.83229  72.16041  23.46119  1.000 63.92463  ?  114 PHE B CE1 1 
ATOM   5044 C CE2 . PHE D 4 102 ? 52.97503  72.50211  22.45708  1.000 63.63158  ?  114 PHE B CE2 1 
ATOM   5045 C CZ  . PHE D 4 102 ? 51.82239  73.01620  23.01813  1.000 62.13614  ?  114 PHE B CZ  1 
ATOM   5046 N N   . PHE D 4 103 ? 51.07019  69.50083  19.47824  1.000 58.03108  ?  115 PHE B N   1 
ATOM   5047 C CA  . PHE D 4 103 ? 51.31445  70.20448  18.22831  1.000 53.74737  ?  115 PHE B CA  1 
ATOM   5048 C C   . PHE D 4 103 ? 51.67966  71.65971  18.48484  1.000 66.98168  ?  115 PHE B C   1 
ATOM   5049 O O   . PHE D 4 103 ? 51.18102  72.29192  19.41953  1.000 79.68513  ?  115 PHE B O   1 
ATOM   5050 C CB  . PHE D 4 103 ? 50.08604  70.13638  17.31779  1.000 60.51125  ?  115 PHE B CB  1 
ATOM   5051 C CG  . PHE D 4 103 ? 49.90516  68.81060  16.63873  1.000 64.50407  ?  115 PHE B CG  1 
ATOM   5052 C CD1 . PHE D 4 103 ? 49.48121  67.70288  17.35324  1.000 59.12505  ?  115 PHE B CD1 1 
ATOM   5053 C CD2 . PHE D 4 103 ? 50.14843  68.67563  15.28187  1.000 52.68133  ?  115 PHE B CD2 1 
ATOM   5054 C CE1 . PHE D 4 103 ? 49.31327  66.48151  16.73023  1.000 54.64220  ?  115 PHE B CE1 1 
ATOM   5055 C CE2 . PHE D 4 103 ? 49.98319  67.45696  14.65316  1.000 73.27989  ?  115 PHE B CE2 1 
ATOM   5056 C CZ  . PHE D 4 103 ? 49.56415  66.35848  15.37797  1.000 70.17900  ?  115 PHE B CZ  1 
ATOM   5057 N N   . GLY D 4 104 ? 52.55946  72.18635  17.63864  1.000 66.91016  ?  116 GLY B N   1 
ATOM   5058 C CA  . GLY D 4 104 ? 52.92564  73.58345  17.69072  1.000 72.90455  ?  116 GLY B CA  1 
ATOM   5059 C C   . GLY D 4 104 ? 51.93604  74.45407  16.93890  1.000 74.48248  ?  116 GLY B C   1 
ATOM   5060 O O   . GLY D 4 104 ? 50.87317  74.01422  16.49750  1.000 83.39936  ?  116 GLY B O   1 
ATOM   5061 N N   . LYS D 4 105 ? 52.30810  75.72835  16.79135  1.000 70.52718  ?  117 LYS B N   1 
ATOM   5062 C CA  . LYS D 4 105 ? 51.43785  76.67009  16.09413  1.000 66.93791  ?  117 LYS B CA  1 
ATOM   5063 C C   . LYS D 4 105 ? 51.33832  76.35105  14.60752  1.000 61.95142  ?  117 LYS B C   1 
ATOM   5064 O O   . LYS D 4 105 ? 50.32102  76.65879  13.97571  1.000 69.66604  ?  117 LYS B O   1 
ATOM   5065 C CB  . LYS D 4 105 ? 51.93786  78.09928  16.29955  1.000 62.14850  ?  117 LYS B CB  1 
ATOM   5066 C CG  . LYS D 4 105 ? 52.06452  78.51393  17.75733  1.000 68.74533  ?  117 LYS B CG  1 
ATOM   5067 C CD  . LYS D 4 105 ? 50.71538  78.51905  18.45717  1.000 82.83176  ?  117 LYS B CD  1 
ATOM   5068 C CE  . LYS D 4 105 ? 50.85167  78.95518  19.90781  1.000 103.12333 ?  117 LYS B CE  1 
ATOM   5069 N NZ  . LYS D 4 105 ? 49.53512  79.00984  20.60136  1.000 119.28211 ?  117 LYS B NZ  1 
ATOM   5070 N N   . GLY D 4 106 ? 52.37025  75.74177  14.03664  1.000 62.46174  ?  118 GLY B N   1 
ATOM   5071 C CA  . GLY D 4 106 ? 52.35188  75.34489  12.64576  1.000 58.22336  ?  118 GLY B CA  1 
ATOM   5072 C C   . GLY D 4 106 ? 52.91406  76.41012  11.71966  1.000 61.65468  ?  118 GLY B C   1 
ATOM   5073 O O   . GLY D 4 106 ? 52.98480  77.59424  12.04525  1.000 75.54780  ?  118 GLY B O   1 
ATOM   5074 N N   . THR D 4 107 ? 53.32104  75.96081  10.53422  1.000 51.67350  ?  119 THR B N   1 
ATOM   5075 C CA  . THR D 4 107 ? 53.85588  76.83163  9.49199   1.000 41.03755  ?  119 THR B CA  1 
ATOM   5076 C C   . THR D 4 107 ? 53.09249  76.55333  8.20466   1.000 61.47261  ?  119 THR B C   1 
ATOM   5077 O O   . THR D 4 107 ? 53.17622  75.44911  7.65671   1.000 62.87865  ?  119 THR B O   1 
ATOM   5078 C CB  . THR D 4 107 ? 55.35599  76.60617  9.29469   1.000 61.23125  ?  119 THR B CB  1 
ATOM   5079 O OG1 . THR D 4 107 ? 56.05905  76.97503  10.48787  1.000 77.07150  ?  119 THR B OG1 1 
ATOM   5080 C CG2 . THR D 4 107 ? 55.87267  77.43727  8.12990   1.000 54.70194  ?  119 THR B CG2 1 
ATOM   5081 N N   . ARG D 4 108 ? 52.34863  77.54689  7.72529   1.000 51.55500  ?  120 ARG B N   1 
ATOM   5082 C CA  . ARG D 4 108 ? 51.57400  77.41111  6.49840   1.000 57.69448  ?  120 ARG B CA  1 
ATOM   5083 C C   . ARG D 4 108 ? 52.45308  77.76367  5.30473   1.000 62.29034  ?  120 ARG B C   1 
ATOM   5084 O O   . ARG D 4 108 ? 52.99869  78.87034  5.23400   1.000 75.08526  ?  120 ARG B O   1 
ATOM   5085 C CB  . ARG D 4 108 ? 50.33419  78.30357  6.53203   1.000 59.51148  ?  120 ARG B CB  1 
ATOM   5086 C CG  . ARG D 4 108 ? 49.48913  78.21629  5.27020   1.000 81.64652  ?  120 ARG B CG  1 
ATOM   5087 C CD  . ARG D 4 108 ? 48.30909  79.17452  5.30856   1.000 89.79443  ?  120 ARG B CD  1 
ATOM   5088 N NE  . ARG D 4 108 ? 47.38732  78.87187  6.39653   1.000 98.63251  ?  120 ARG B NE  1 
ATOM   5089 C CZ  . ARG D 4 108 ? 46.22196  79.47748  6.57879   1.000 103.49564 ?  120 ARG B CZ  1 
ATOM   5090 N NH1 . ARG D 4 108 ? 45.79904  80.42348  5.75655   1.000 106.17047 ?  120 ARG B NH1 1 
ATOM   5091 N NH2 . ARG D 4 108 ? 45.46168  79.12490  7.61152   1.000 109.32129 ?  120 ARG B NH2 1 
ATOM   5092 N N   . LEU D 4 109 ? 52.58861  76.82501  4.37254   1.000 61.05713  ?  121 LEU B N   1 
ATOM   5093 C CA  . LEU D 4 109 ? 53.36344  77.02079  3.15399   1.000 56.22530  ?  121 LEU B CA  1 
ATOM   5094 C C   . LEU D 4 109 ? 52.40035  77.21040  1.99037   1.000 65.67137  ?  121 LEU B C   1 
ATOM   5095 O O   . LEU D 4 109 ? 51.56467  76.33978  1.72435   1.000 70.65934  ?  121 LEU B O   1 
ATOM   5096 C CB  . LEU D 4 109 ? 54.29206  75.83419  2.89347   1.000 54.37750  ?  121 LEU B CB  1 
ATOM   5097 C CG  . LEU D 4 109 ? 55.22862  75.40703  4.02527   1.000 51.76135  ?  121 LEU B CG  1 
ATOM   5098 C CD1 . LEU D 4 109 ? 56.11118  74.25265  3.57823   1.000 55.07343  ?  121 LEU B CD1 1 
ATOM   5099 C CD2 . LEU D 4 109 ? 56.07396  76.57371  4.50024   1.000 45.73744  ?  121 LEU B CD2 1 
ATOM   5100 N N   . THR D 4 110 ? 52.51621  78.34322  1.30467   1.000 71.74880  ?  122 THR B N   1 
ATOM   5101 C CA  . THR D 4 110 ? 51.68833  78.65824  0.14732   1.000 71.69247  ?  122 THR B CA  1 
ATOM   5102 C C   . THR D 4 110 ? 52.56979  78.67541  -1.09356  1.000 78.26171  ?  122 THR B C   1 
ATOM   5103 O O   . THR D 4 110 ? 53.54197  79.43578  -1.15783  1.000 79.92348  ?  122 THR B O   1 
ATOM   5104 C CB  . THR D 4 110 ? 50.98115  80.00223  0.32329   1.000 79.24391  ?  122 THR B CB  1 
ATOM   5105 O OG1 . THR D 4 110 ? 50.05392  79.91745  1.41264   1.000 78.03822  ?  122 THR B OG1 1 
ATOM   5106 C CG2 . THR D 4 110 ? 50.23312  80.38178  -0.94611  1.000 88.71383  ?  122 THR B CG2 1 
ATOM   5107 N N   . VAL D 4 111 ? 52.23091  77.84070  -2.07082  1.000 75.49428  ?  123 VAL B N   1 
ATOM   5108 C CA  . VAL D 4 111 ? 52.99155  77.72411  -3.30895  1.000 67.09509  ?  123 VAL B CA  1 
ATOM   5109 C C   . VAL D 4 111 ? 52.29731  78.55361  -4.37954  1.000 77.04238  ?  123 VAL B C   1 
ATOM   5110 O O   . VAL D 4 111 ? 51.10708  78.35830  -4.65456  1.000 82.43229  ?  123 VAL B O   1 
ATOM   5111 C CB  . VAL D 4 111 ? 53.13011  76.25856  -3.74808  1.000 67.49242  ?  123 VAL B CB  1 
ATOM   5112 C CG1 . VAL D 4 111 ? 53.91804  76.16761  -5.04611  1.000 62.95991  ?  123 VAL B CG1 1 
ATOM   5113 C CG2 . VAL D 4 111 ? 53.79853  75.44231  -2.65482  1.000 73.80543  ?  123 VAL B CG2 1 
ATOM   5114 N N   . VAL D 4 112 ? 53.03857  79.47892  -4.98381  1.000 81.98167  ?  124 VAL B N   1 
ATOM   5115 C CA  . VAL D 4 112 ? 52.53270  80.32605  -6.05566  1.000 96.68962  ?  124 VAL B CA  1 
ATOM   5116 C C   . VAL D 4 112 ? 53.38873  80.10947  -7.29522  1.000 96.65881  ?  124 VAL B C   1 
ATOM   5117 O O   . VAL D 4 112 ? 54.61891  80.02434  -7.20771  1.000 90.80319  ?  124 VAL B O   1 
ATOM   5118 C CB  . VAL D 4 112 ? 52.51773  81.81600  -5.65218  1.000 81.57037  ?  124 VAL B CB  1 
ATOM   5119 C CG1 . VAL D 4 112 ? 51.43028  82.07325  -4.62191  1.000 90.84658  ?  124 VAL B CG1 1 
ATOM   5120 C CG2 . VAL D 4 112 ? 53.87585  82.23960  -5.11290  1.000 74.12209  ?  124 VAL B CG2 1 
ATOM   5121 N N   . GLU D 4 113 ? 52.73162  80.00778  -8.44970  1.000 92.95963  ?  125 GLU B N   1 
ATOM   5122 C CA  . GLU D 4 113 ? 53.43772  79.86986  -9.71647  1.000 97.18435  ?  125 GLU B CA  1 
ATOM   5123 C C   . GLU D 4 113 ? 53.84465  81.21368  -10.30274 1.000 97.80473  ?  125 GLU B C   1 
ATOM   5124 O O   . GLU D 4 113 ? 54.86398  81.29635  -10.99797 1.000 109.49547 ?  125 GLU B O   1 
ATOM   5125 C CB  . GLU D 4 113 ? 52.57105  79.10810  -10.72340 1.000 88.28574  ?  125 GLU B CB  1 
ATOM   5126 N N   . ASP D 4 114 ? 53.07384  82.26491  -10.03500 1.000 98.39594  ?  126 ASP B N   1 
ATOM   5127 C CA  . ASP D 4 114 ? 53.38878  83.61493  -10.47668 1.000 109.84948 ?  126 ASP B CA  1 
ATOM   5128 C C   . ASP D 4 114 ? 53.28406  84.56101  -9.29141  1.000 108.72515 ?  126 ASP B C   1 
ATOM   5129 O O   . ASP D 4 114 ? 52.32222  84.49690  -8.51971  1.000 105.35288 ?  126 ASP B O   1 
ATOM   5130 C CB  . ASP D 4 114 ? 52.44918  84.07498  -11.59714 1.000 101.42948 ?  126 ASP B CB  1 
ATOM   5131 N N   . LEU D 4 115 ? 54.27513  85.43840  -9.15340  1.000 103.77034 ?  127 LEU B N   1 
ATOM   5132 C CA  . LEU D 4 115 ? 54.33693  86.37967  -8.04385  1.000 97.48736  ?  127 LEU B CA  1 
ATOM   5133 C C   . LEU D 4 115 ? 53.52746  87.64749  -8.29224  1.000 92.92949  ?  127 LEU B C   1 
ATOM   5134 O O   . LEU D 4 115 ? 53.44957  88.49898  -7.40007  1.000 91.80808  ?  127 LEU B O   1 
ATOM   5135 C CB  . LEU D 4 115 ? 55.79688  86.74760  -7.74128  1.000 92.55968  ?  127 LEU B CB  1 
ATOM   5136 C CG  . LEU D 4 115 ? 56.70279  85.66613  -7.13204  1.000 103.83584 ?  127 LEU B CG  1 
ATOM   5137 C CD1 . LEU D 4 115 ? 57.26218  84.71599  -8.18936  1.000 103.28195 ?  127 LEU B CD1 1 
ATOM   5138 C CD2 . LEU D 4 115 ? 57.83167  86.28867  -6.31761  1.000 89.44695  ?  127 LEU B CD2 1 
ATOM   5139 N N   . ASN D 4 116 ? 52.92114  87.79326  -9.47252  1.000 97.85959  ?  128 ASN B N   1 
ATOM   5140 C CA  . ASN D 4 116 ? 52.10282  88.96154  -9.77133  1.000 97.59315  ?  128 ASN B CA  1 
ATOM   5141 C C   . ASN D 4 116 ? 50.74026  88.92165  -9.08988  1.000 95.59768  ?  128 ASN B C   1 
ATOM   5142 O O   . ASN D 4 116 ? 49.99245  89.90145  -9.17960  1.000 100.40453 ?  128 ASN B O   1 
ATOM   5143 C CB  . ASN D 4 116 ? 51.91787  89.10083  -11.28634 1.000 111.19967 ?  128 ASN B CB  1 
ATOM   5144 C CG  . ASN D 4 116 ? 53.23905  89.20115  -12.03112 1.000 125.51611 ?  128 ASN B CG  1 
ATOM   5145 O OD1 . ASN D 4 116 ? 53.87086  90.25791  -12.05956 1.000 123.54795 ?  128 ASN B OD1 1 
ATOM   5146 N ND2 . ASN D 4 116 ? 53.65796  88.10000  -12.64548 1.000 130.54856 ?  128 ASN B ND2 1 
ATOM   5147 N N   . LYS D 4 117 ? 50.40293  87.82546  -8.41480  1.000 83.31271  ?  129 LYS B N   1 
ATOM   5148 C CA  . LYS D 4 117 ? 49.13296  87.69001  -7.71489  1.000 80.87334  ?  129 LYS B CA  1 
ATOM   5149 C C   . LYS D 4 117 ? 49.20966  88.10268  -6.25073  1.000 88.02665  ?  129 LYS B C   1 
ATOM   5150 O O   . LYS D 4 117 ? 48.19851  88.01811  -5.54627  1.000 98.98624  ?  129 LYS B O   1 
ATOM   5151 C CB  . LYS D 4 117 ? 48.63267  86.24553  -7.81470  1.000 92.49792  ?  129 LYS B CB  1 
ATOM   5152 C CG  . LYS D 4 117 ? 47.99551  85.90337  -9.15019  1.000 95.75260  ?  129 LYS B CG  1 
ATOM   5153 C CD  . LYS D 4 117 ? 48.36601  84.50316  -9.61121  1.000 106.76293 ?  129 LYS B CD  1 
ATOM   5154 C CE  . LYS D 4 117 ? 47.36042  83.99011  -10.62707 1.000 110.24500 ?  129 LYS B CE  1 
ATOM   5155 N NZ  . LYS D 4 117 ? 46.78338  85.10502  -11.42860 1.000 112.28524 ?  129 LYS B NZ  1 
ATOM   5156 N N   . VAL D 4 118 ? 50.37155  88.54017  -5.77641  1.000 83.65561  ?  130 VAL B N   1 
ATOM   5157 C CA  . VAL D 4 118 ? 50.51976  88.96025  -4.38772  1.000 74.11512  ?  130 VAL B CA  1 
ATOM   5158 C C   . VAL D 4 118 ? 50.04067  90.39900  -4.25290  1.000 80.86963  ?  130 VAL B C   1 
ATOM   5159 O O   . VAL D 4 118 ? 50.45520  91.27911  -5.01670  1.000 80.41663  ?  130 VAL B O   1 
ATOM   5160 C CB  . VAL D 4 118 ? 51.97819  88.81256  -3.92750  1.000 81.33630  ?  130 VAL B CB  1 
ATOM   5161 C CG1 . VAL D 4 118 ? 52.09335  89.05807  -2.42909  1.000 87.58221  ?  130 VAL B CG1 1 
ATOM   5162 C CG2 . VAL D 4 118 ? 52.51131  87.43812  -4.29366  1.000 73.69211  ?  130 VAL B CG2 1 
ATOM   5163 N N   . PHE D 4 119 ? 49.16012  90.64191  -3.28111  1.000 77.91208  ?  131 PHE B N   1 
ATOM   5164 C CA  . PHE D 4 119 ? 48.59299  91.96200  -3.05105  1.000 84.29387  ?  131 PHE B CA  1 
ATOM   5165 C C   . PHE D 4 119 ? 48.53717  92.24969  -1.55723  1.000 78.43665  ?  131 PHE B C   1 
ATOM   5166 O O   . PHE D 4 119 ? 48.21048  91.35456  -0.76374  1.000 72.55852  ?  131 PHE B O   1 
ATOM   5167 C CB  . PHE D 4 119 ? 47.18374  92.08444  -3.64785  1.000 79.26437  ?  131 PHE B CB  1 
ATOM   5168 C CG  . PHE D 4 119 ? 47.16147  92.13357  -5.14801  1.000 81.94916  ?  131 PHE B CG  1 
ATOM   5169 C CD1 . PHE D 4 119 ? 47.09781  90.96816  -5.89255  1.000 81.23515  ?  131 PHE B CD1 1 
ATOM   5170 C CD2 . PHE D 4 119 ? 47.20001  93.34723  -5.81419  1.000 85.68740  ?  131 PHE B CD2 1 
ATOM   5171 C CE1 . PHE D 4 119 ? 47.07660  91.01173  -7.27380  1.000 89.07281  ?  131 PHE B CE1 1 
ATOM   5172 C CE2 . PHE D 4 119 ? 47.17844  93.39751  -7.19481  1.000 88.58862  ?  131 PHE B CE2 1 
ATOM   5173 C CZ  . PHE D 4 119 ? 47.11680  92.22812  -7.92545  1.000 87.94064  ?  131 PHE B CZ  1 
ATOM   5174 N N   . PRO D 4 120 ? 48.85636  93.47272  -1.14617  1.000 81.48614  ?  132 PRO B N   1 
ATOM   5175 C CA  . PRO D 4 120 ? 48.71652  93.84443  0.26195   1.000 79.37443  ?  132 PRO B CA  1 
ATOM   5176 C C   . PRO D 4 120 ? 47.28954  94.25865  0.57005   1.000 80.87980  ?  132 PRO B C   1 
ATOM   5177 O O   . PRO D 4 120 ? 46.55390  94.69801  -0.32682  1.000 87.38297  ?  132 PRO B O   1 
ATOM   5178 C CB  . PRO D 4 120 ? 49.68496  95.02541  0.40690   1.000 91.80497  ?  132 PRO B CB  1 
ATOM   5179 C CG  . PRO D 4 120 ? 49.67258  95.66071  -0.94250  1.000 81.30846  ?  132 PRO B CG  1 
ATOM   5180 C CD  . PRO D 4 120 ? 49.49327  94.53879  -1.94005  1.000 90.20395  ?  132 PRO B CD  1 
ATOM   5181 N N   . PRO D 4 121 ? 46.85770  94.13281  1.82117   1.000 79.04449  ?  133 PRO B N   1 
ATOM   5182 C CA  . PRO D 4 121 ? 45.48195  94.49731  2.16741   1.000 85.52956  ?  133 PRO B CA  1 
ATOM   5183 C C   . PRO D 4 121 ? 45.31792  95.99149  2.39399   1.000 86.94061  ?  133 PRO B C   1 
ATOM   5184 O O   . PRO D 4 121 ? 46.24892  96.69765  2.78785   1.000 94.35162  ?  133 PRO B O   1 
ATOM   5185 C CB  . PRO D 4 121 ? 45.23331  93.71782  3.46349   1.000 80.43731  ?  133 PRO B CB  1 
ATOM   5186 C CG  . PRO D 4 121 ? 46.58155  93.63828  4.09405   1.000 83.32725  ?  133 PRO B CG  1 
ATOM   5187 C CD  . PRO D 4 121 ? 47.57335  93.52947  2.95945   1.000 76.31027  ?  133 PRO B CD  1 
ATOM   5188 N N   . GLU D 4 122 ? 44.10234  96.46597  2.13522   1.000 71.14630  ?  134 GLU B N   1 
ATOM   5189 C CA  . GLU D 4 122 ? 43.71668  97.84544  2.40241   1.000 81.08017  ?  134 GLU B CA  1 
ATOM   5190 C C   . GLU D 4 122 ? 42.84375  97.86882  3.65134   1.000 93.21817  ?  134 GLU B C   1 
ATOM   5191 O O   . GLU D 4 122 ? 41.78497  97.23243  3.68471   1.000 89.80516  ?  134 GLU B O   1 
ATOM   5192 C CB  . GLU D 4 122 ? 42.97525  98.44873  1.20965   1.000 76.18608  ?  134 GLU B CB  1 
ATOM   5193 N N   . VAL D 4 123 ? 43.28700  98.59843  4.67104   1.000 92.93958  ?  135 VAL B N   1 
ATOM   5194 C CA  . VAL D 4 123 ? 42.63801  98.60950  5.97776   1.000 91.66571  ?  135 VAL B CA  1 
ATOM   5195 C C   . VAL D 4 123 ? 41.82231  99.88508  6.12545   1.000 86.60590  ?  135 VAL B C   1 
ATOM   5196 O O   . VAL D 4 123 ? 42.28063  100.97727 5.76581   1.000 94.41762  ?  135 VAL B O   1 
ATOM   5197 C CB  . VAL D 4 123 ? 43.67860  98.48079  7.10661   1.000 97.61456  ?  135 VAL B CB  1 
ATOM   5198 C CG1 . VAL D 4 123 ? 42.99924  98.47358  8.46649   1.000 93.73513  ?  135 VAL B CG1 1 
ATOM   5199 C CG2 . VAL D 4 123 ? 44.50715  97.22195  6.91320   1.000 79.96853  ?  135 VAL B CG2 1 
ATOM   5200 N N   . ALA D 4 124 ? 40.60868  99.74844  6.65753   1.000 78.48296  ?  136 ALA B N   1 
ATOM   5201 C CA  . ALA D 4 124 ? 39.72795  100.89146 6.87422   1.000 85.55735  ?  136 ALA B CA  1 
ATOM   5202 C C   . ALA D 4 124 ? 38.84628  100.61070 8.08021   1.000 89.06821  ?  136 ALA B C   1 
ATOM   5203 O O   . ALA D 4 124 ? 38.14229  99.59678  8.11109   1.000 88.25069  ?  136 ALA B O   1 
ATOM   5204 C CB  . ALA D 4 124 ? 38.87395  101.17259 5.63608   1.000 70.39593  ?  136 ALA B CB  1 
ATOM   5205 N N   . VAL D 4 125 ? 38.88815  101.50203 9.06591   1.000 84.12719  ?  137 VAL B N   1 
ATOM   5206 C CA  . VAL D 4 125 ? 38.04254  101.40695 10.24990  1.000 83.49235  ?  137 VAL B CA  1 
ATOM   5207 C C   . VAL D 4 125 ? 36.79125  102.24004 10.01500  1.000 86.92122  ?  137 VAL B C   1 
ATOM   5208 O O   . VAL D 4 125 ? 36.81860  103.25199 9.30724   1.000 105.01611 ?  137 VAL B O   1 
ATOM   5209 C CB  . VAL D 4 125 ? 38.80346  101.86389 11.51332  1.000 89.25079  ?  137 VAL B CB  1 
ATOM   5210 C CG1 . VAL D 4 125 ? 37.99820  101.56196 12.76986  1.000 92.40426  ?  137 VAL B CG1 1 
ATOM   5211 C CG2 . VAL D 4 125 ? 40.16456  101.19622 11.58089  1.000 90.30818  ?  137 VAL B CG2 1 
ATOM   5212 N N   . PHE D 4 126 ? 35.67783  101.81279 10.60767  1.000 83.09139  ?  138 PHE B N   1 
ATOM   5213 C CA  . PHE D 4 126 ? 34.39075  102.47239 10.42235  1.000 107.19345 ?  138 PHE B CA  1 
ATOM   5214 C C   . PHE D 4 126 ? 33.78070  102.77205 11.78417  1.000 108.16245 ?  138 PHE B C   1 
ATOM   5215 O O   . PHE D 4 126 ? 33.59151  101.86073 12.59672  1.000 96.54995  ?  138 PHE B O   1 
ATOM   5216 C CB  . PHE D 4 126 ? 33.45615  101.60661 9.57123   1.000 95.13456  ?  138 PHE B CB  1 
ATOM   5217 C CG  . PHE D 4 126 ? 33.93666  101.41498 8.15698   1.000 100.24946 ?  138 PHE B CG  1 
ATOM   5218 C CD1 . PHE D 4 126 ? 34.85473  100.42318 7.84706   1.000 93.06237  ?  138 PHE B CD1 1 
ATOM   5219 C CD2 . PHE D 4 126 ? 33.47932  102.23626 7.13995   1.000 115.17072 ?  138 PHE B CD2 1 
ATOM   5220 C CE1 . PHE D 4 126 ? 35.30260  100.25250 6.54783   1.000 90.39120  ?  138 PHE B CE1 1 
ATOM   5221 C CE2 . PHE D 4 126 ? 33.92131  102.07000 5.83985   1.000 115.45344 ?  138 PHE B CE2 1 
ATOM   5222 C CZ  . PHE D 4 126 ? 34.83414  101.07723 5.54346   1.000 95.92912  ?  138 PHE B CZ  1 
ATOM   5223 N N   . GLU D 4 127 ? 33.47709  104.04727 12.02567  1.000 108.61804 ?  139 GLU B N   1 
ATOM   5224 C CA  . GLU D 4 127 ? 32.95772  104.47456 13.31797  1.000 97.29855  ?  139 GLU B CA  1 
ATOM   5225 C C   . GLU D 4 127 ? 31.54472  103.93909 13.53208  1.000 109.45127 ?  139 GLU B C   1 
ATOM   5226 O O   . GLU D 4 127 ? 30.74309  103.91624 12.59560  1.000 108.68715 ?  139 GLU B O   1 
ATOM   5227 C CB  . GLU D 4 127 ? 32.94303  105.99855 13.41101  1.000 110.67561 ?  139 GLU B CB  1 
ATOM   5228 C CG  . GLU D 4 127 ? 34.27861  106.65950 13.14231  1.000 112.33284 ?  139 GLU B CG  1 
ATOM   5229 C CD  . GLU D 4 127 ? 34.20407  108.16770 13.25423  1.000 119.77708 ?  139 GLU B CD  1 
ATOM   5230 O OE1 . GLU D 4 127 ? 33.08164  108.69723 13.39684  1.000 119.43325 ?  139 GLU B OE1 1 
ATOM   5231 O OE2 . GLU D 4 127 ? 35.26545  108.82307 13.20285  1.000 131.20523 ?  139 GLU B OE2 1 
ATOM   5232 N N   . PRO D 4 128 ? 31.19969  103.53938 14.75589  1.000 111.03093 ?  140 PRO B N   1 
ATOM   5233 C CA  . PRO D 4 128 ? 29.88273  102.94079 14.99895  1.000 115.42992 ?  140 PRO B CA  1 
ATOM   5234 C C   . PRO D 4 128 ? 28.74969  103.91585 14.71249  1.000 113.45301 ?  140 PRO B C   1 
ATOM   5235 O O   . PRO D 4 128 ? 28.92612  105.13616 14.69215  1.000 118.44490 ?  140 PRO B O   1 
ATOM   5236 C CB  . PRO D 4 128 ? 29.93141  102.56766 16.48520  1.000 102.51357 ?  140 PRO B CB  1 
ATOM   5237 C CG  . PRO D 4 128 ? 30.94446  103.49620 17.06663  1.000 105.80487 ?  140 PRO B CG  1 
ATOM   5238 C CD  . PRO D 4 128 ? 31.97834  103.68523 15.99754  1.000 103.89820 ?  140 PRO B CD  1 
ATOM   5239 N N   . SER D 4 129 ? 27.56670  103.35064 14.48923  1.000 112.77660 ?  141 SER B N   1 
ATOM   5240 C CA  . SER D 4 129 ? 26.39693  104.14023 14.13826  1.000 127.31981 ?  141 SER B CA  1 
ATOM   5241 C C   . SER D 4 129 ? 25.82913  104.84817 15.36182  1.000 127.65573 ?  141 SER B C   1 
ATOM   5242 O O   . SER D 4 129 ? 25.88927  104.34212 16.48628  1.000 120.99721 ?  141 SER B O   1 
ATOM   5243 C CB  . SER D 4 129 ? 25.31886  103.25486 13.51251  1.000 125.54173 ?  141 SER B CB  1 
ATOM   5244 O OG  . SER D 4 129 ? 24.81834  102.31977 14.45263  1.000 121.55196 ?  141 SER B OG  1 
ATOM   5245 N N   . GLU D 4 130 ? 25.26659  106.03606 15.12745  1.000 112.81907 ?  142 GLU B N   1 
ATOM   5246 C CA  . GLU D 4 130 ? 24.60522  106.77112 16.19774  1.000 106.96209 ?  142 GLU B CA  1 
ATOM   5247 C C   . GLU D 4 130 ? 23.29392  106.12134 16.61690  1.000 120.28490 ?  142 GLU B C   1 
ATOM   5248 O O   . GLU D 4 130 ? 22.77887  106.43443 17.69541  1.000 121.90001 ?  142 GLU B O   1 
ATOM   5249 C CB  . GLU D 4 130 ? 24.35475  108.21724 15.76841  1.000 109.82566 ?  142 GLU B CB  1 
ATOM   5250 N N   . ALA D 4 131 ? 22.74191  105.22960 15.79161  1.000 118.73988 ?  143 ALA B N   1 
ATOM   5251 C CA  . ALA D 4 131 ? 21.51387  104.53710 16.16122  1.000 122.39501 ?  143 ALA B CA  1 
ATOM   5252 C C   . ALA D 4 131 ? 21.76900  103.43682 17.18309  1.000 129.64473 ?  143 ALA B C   1 
ATOM   5253 O O   . ALA D 4 131 ? 20.91567  103.18359 18.04094  1.000 131.17825 ?  143 ALA B O   1 
ATOM   5254 C CB  . ALA D 4 131 ? 20.84073  103.95855 14.91547  1.000 120.68554 ?  143 ALA B CB  1 
ATOM   5255 N N   . GLU D 4 132 ? 22.93014  102.78037 17.11160  1.000 126.14539 ?  144 GLU B N   1 
ATOM   5256 C CA  . GLU D 4 132 ? 23.26460  101.75435 18.09315  1.000 121.68855 ?  144 GLU B CA  1 
ATOM   5257 C C   . GLU D 4 132 ? 23.59805  102.36403 19.44811  1.000 128.14363 ?  144 GLU B C   1 
ATOM   5258 O O   . GLU D 4 132 ? 23.29291  101.76919 20.48846  1.000 125.66133 ?  144 GLU B O   1 
ATOM   5259 C CB  . GLU D 4 132 ? 24.43884  100.91254 17.59183  1.000 123.29120 ?  144 GLU B CB  1 
ATOM   5260 C CG  . GLU D 4 132 ? 24.79269  99.74337  18.49323  1.000 121.27892 ?  144 GLU B CG  1 
ATOM   5261 C CD  . GLU D 4 132 ? 26.11724  99.10511  18.12494  1.000 116.27264 ?  144 GLU B CD  1 
ATOM   5262 O OE1 . GLU D 4 132 ? 26.73973  99.54858  17.13661  1.000 123.46864 ?  144 GLU B OE1 1 
ATOM   5263 O OE2 . GLU D 4 132 ? 26.53763  98.16122  18.82695  1.000 102.90277 -1 144 GLU B OE2 1 
ATOM   5264 N N   . ILE D 4 133 ? 24.21882  103.54505 19.45404  1.000 128.24821 ?  145 ILE B N   1 
ATOM   5265 C CA  . ILE D 4 133 ? 24.61471  104.18020 20.70659  1.000 127.90840 ?  145 ILE B CA  1 
ATOM   5266 C C   . ILE D 4 133 ? 23.38822  104.57601 21.51937  1.000 134.70650 ?  145 ILE B C   1 
ATOM   5267 O O   . ILE D 4 133 ? 23.38242  104.47174 22.75188  1.000 147.96361 ?  145 ILE B O   1 
ATOM   5268 C CB  . ILE D 4 133 ? 25.52371  105.38868 20.41638  1.000 134.44398 ?  145 ILE B CB  1 
ATOM   5269 C CG1 . ILE D 4 133 ? 26.78240  104.93525 19.67465  1.000 117.86521 ?  145 ILE B CG1 1 
ATOM   5270 C CG2 . ILE D 4 133 ? 25.88383  106.11981 21.70197  1.000 133.61087 ?  145 ILE B CG2 1 
ATOM   5271 C CD1 . ILE D 4 133 ? 27.70821  106.06786 19.29159  1.000 125.02239 ?  145 ILE B CD1 1 
ATOM   5272 N N   . SER D 4 134 ? 22.32747  105.01863 20.84750  1.000 137.51859 ?  146 SER B N   1 
ATOM   5273 C CA  . SER D 4 134 ? 21.11369  105.45602 21.52220  1.000 140.76347 ?  146 SER B CA  1 
ATOM   5274 C C   . SER D 4 134 ? 20.12715  104.32497 21.78238  1.000 141.46234 ?  146 SER B C   1 
ATOM   5275 O O   . SER D 4 134 ? 19.14295  104.53891 22.49826  1.000 142.38322 ?  146 SER B O   1 
ATOM   5276 C CB  . SER D 4 134 ? 20.42390  106.55377 20.70437  1.000 135.27290 ?  146 SER B CB  1 
ATOM   5277 O OG  . SER D 4 134 ? 20.10092  106.09423 19.40364  1.000 132.66703 ?  146 SER B OG  1 
ATOM   5278 N N   . HIS D 4 135 ? 20.36178  103.13638 21.23066  1.000 132.55017 ?  147 HIS B N   1 
ATOM   5279 C CA  . HIS D 4 135 ? 19.46015  102.00157 21.39749  1.000 126.62405 ?  147 HIS B CA  1 
ATOM   5280 C C   . HIS D 4 135 ? 19.98701  100.94261 22.35156  1.000 123.64391 ?  147 HIS B C   1 
ATOM   5281 O O   . HIS D 4 135 ? 19.21931  100.40997 23.15574  1.000 122.33326 ?  147 HIS B O   1 
ATOM   5282 C CB  . HIS D 4 135 ? 19.17016  101.35210 20.03866  1.000 127.93460 ?  147 HIS B CB  1 
ATOM   5283 C CG  . HIS D 4 135 ? 18.14948  100.25798 20.09622  1.000 132.88058 ?  147 HIS B CG  1 
ATOM   5284 N ND1 . HIS D 4 135 ? 18.47808  98.94569  20.35994  1.000 131.15611 ?  147 HIS B ND1 1 
ATOM   5285 C CD2 . HIS D 4 135 ? 16.80687  100.28124 19.92173  1.000 134.59749 ?  147 HIS B CD2 1 
ATOM   5286 C CE1 . HIS D 4 135 ? 17.38228  98.20797  20.34716  1.000 133.62779 ?  147 HIS B CE1 1 
ATOM   5287 N NE2 . HIS D 4 135 ? 16.35427  98.99420  20.08343  1.000 142.15804 ?  147 HIS B NE2 1 
ATOM   5288 N N   . THR D 4 136 ? 21.27847  100.61979 22.28484  1.000 129.55308 ?  148 THR B N   1 
ATOM   5289 C CA  . THR D 4 136 ? 21.86766  99.59513  23.13452  1.000 129.21683 ?  148 THR B CA  1 
ATOM   5290 C C   . THR D 4 136 ? 22.93094  100.13262 24.08077  1.000 126.34338 ?  148 THR B C   1 
ATOM   5291 O O   . THR D 4 136 ? 23.47573  99.35610  24.87509  1.000 115.63575 ?  148 THR B O   1 
ATOM   5292 C CB  . THR D 4 136 ? 22.47975  98.47671  22.27899  1.000 130.82206 ?  148 THR B CB  1 
ATOM   5293 O OG1 . THR D 4 136 ? 23.48219  99.02795  21.41584  1.000 129.81192 ?  148 THR B OG1 1 
ATOM   5294 C CG2 . THR D 4 136 ? 21.40961  97.79888  21.43867  1.000 130.94811 ?  148 THR B CG2 1 
ATOM   5295 N N   . GLN D 4 137 ? 23.24355  101.42931 24.01752  1.000 131.94430 ?  149 GLN B N   1 
ATOM   5296 C CA  . GLN D 4 137 ? 24.28997  102.04272 24.83810  1.000 127.29249 ?  149 GLN B CA  1 
ATOM   5297 C C   . GLN D 4 137 ? 25.64120  101.36320 24.63082  1.000 114.92968 ?  149 GLN B C   1 
ATOM   5298 O O   . GLN D 4 137 ? 26.47632  101.32420 25.53773  1.000 109.40255 ?  149 GLN B O   1 
ATOM   5299 C CB  . GLN D 4 137 ? 23.91070  102.04215 26.32272  1.000 114.88271 ?  149 GLN B CB  1 
ATOM   5300 N N   . LYS D 4 138 ? 25.86342  100.82310 23.43441  1.000 124.16485 ?  150 LYS B N   1 
ATOM   5301 C CA  . LYS D 4 138 ? 27.11159  100.15917 23.09230  1.000 117.36384 ?  150 LYS B CA  1 
ATOM   5302 C C   . LYS D 4 138 ? 27.54752  100.60532 21.70634  1.000 114.77346 ?  150 LYS B C   1 
ATOM   5303 O O   . LYS D 4 138 ? 26.71378  100.79803 20.81745  1.000 113.50293 ?  150 LYS B O   1 
ATOM   5304 C CB  . LYS D 4 138 ? 26.96689  98.63188  23.13357  1.000 103.58493 ?  150 LYS B CB  1 
ATOM   5305 N N   . ALA D 4 139 ? 28.85497  100.77091 21.53009  1.000 112.49100 ?  151 ALA B N   1 
ATOM   5306 C CA  . ALA D 4 139 ? 29.43426  101.20691 20.26768  1.000 107.41974 ?  151 ALA B CA  1 
ATOM   5307 C C   . ALA D 4 139 ? 30.30287  100.09317 19.70417  1.000 102.95377 ?  151 ALA B C   1 
ATOM   5308 O O   . ALA D 4 139 ? 31.17382  99.56601  20.40435  1.000 98.25370  ?  151 ALA B O   1 
ATOM   5309 C CB  . ALA D 4 139 ? 30.25646  102.48335 20.45247  1.000 110.15787 ?  151 ALA B CB  1 
ATOM   5310 N N   . THR D 4 140 ? 30.06660  99.73933  18.44261  1.000 104.11877 ?  152 THR B N   1 
ATOM   5311 C CA  . THR D 4 140 ? 30.77355  98.64546  17.78383  1.000 104.12997 ?  152 THR B CA  1 
ATOM   5312 C C   . THR D 4 140 ? 31.52819  99.19728  16.58140  1.000 96.54938  ?  152 THR B C   1 
ATOM   5313 O O   . THR D 4 140 ? 30.91352  99.60637  15.59028  1.000 104.62035 ?  152 THR B O   1 
ATOM   5314 C CB  . THR D 4 140 ? 29.80667  97.54183  17.35714  1.000 103.51395 ?  152 THR B CB  1 
ATOM   5315 O OG1 . THR D 4 140 ? 29.05384  97.09723  18.49271  1.000 109.87201 ?  152 THR B OG1 1 
ATOM   5316 C CG2 . THR D 4 140 ? 30.57515  96.36564  16.77598  1.000 94.06162  ?  152 THR B CG2 1 
ATOM   5317 N N   . LEU D 4 141 ? 32.85536  99.20595  16.66926  1.000 83.76320  ?  153 LEU B N   1 
ATOM   5318 C CA  . LEU D 4 141 ? 33.70278  99.60336  15.55477  1.000 83.94104  ?  153 LEU B CA  1 
ATOM   5319 C C   . LEU D 4 141 ? 33.99412  98.39355  14.67826  1.000 91.83606  ?  153 LEU B C   1 
ATOM   5320 O O   . LEU D 4 141 ? 34.16731  97.27812  15.17722  1.000 96.13201  ?  153 LEU B O   1 
ATOM   5321 C CB  . LEU D 4 141 ? 35.01433  100.21724 16.05113  1.000 83.65549  ?  153 LEU B CB  1 
ATOM   5322 C CG  . LEU D 4 141 ? 34.99618  101.63968 16.62081  1.000 95.25746  ?  153 LEU B CG  1 
ATOM   5323 C CD1 . LEU D 4 141 ? 34.37655  101.68812 18.01213  1.000 103.78151 ?  153 LEU B CD1 1 
ATOM   5324 C CD2 . LEU D 4 141 ? 36.40200  102.22279 16.63790  1.000 97.07140  ?  153 LEU B CD2 1 
ATOM   5325 N N   . VAL D 4 142 ? 34.04674  98.61914  13.36865  1.000 91.49067  ?  154 VAL B N   1 
ATOM   5326 C CA  . VAL D 4 142 ? 34.26090  97.55607  12.39335  1.000 84.76571  ?  154 VAL B CA  1 
ATOM   5327 C C   . VAL D 4 142 ? 35.49437  97.89830  11.57143  1.000 79.30336  ?  154 VAL B C   1 
ATOM   5328 O O   . VAL D 4 142 ? 35.56889  98.97797  10.97122  1.000 95.34776  ?  154 VAL B O   1 
ATOM   5329 C CB  . VAL D 4 142 ? 33.03696  97.35604  11.48607  1.000 75.41027  ?  154 VAL B CB  1 
ATOM   5330 C CG1 . VAL D 4 142 ? 33.36016  96.37704  10.36920  1.000 66.28100  ?  154 VAL B CG1 1 
ATOM   5331 C CG2 . VAL D 4 142 ? 31.85279  96.86275  12.30071  1.000 84.98324  ?  154 VAL B CG2 1 
ATOM   5332 N N   . CYS D 4 143 ? 36.45800  96.98414  11.54942  1.000 80.49421  ?  155 CYS B N   1 
ATOM   5333 C CA  . CYS D 4 143 ? 37.63487  97.09825  10.70397  1.000 90.16233  ?  155 CYS B CA  1 
ATOM   5334 C C   . CYS D 4 143 ? 37.49953  96.15683  9.51446   1.000 84.75959  ?  155 CYS B C   1 
ATOM   5335 O O   . CYS D 4 143 ? 36.82957  95.12401  9.59187   1.000 86.09575  ?  155 CYS B O   1 
ATOM   5336 C CB  . CYS D 4 143 ? 38.90787  96.77678  11.48834  1.000 91.55434  ?  155 CYS B CB  1 
ATOM   5337 S SG  . CYS D 4 143 ? 40.43697  97.03403  10.56556  1.000 88.13266  ?  155 CYS B SG  1 
ATOM   5338 N N   . LEU D 4 144 ? 38.14235  96.52202  8.40772   1.000 91.24692  ?  156 LEU B N   1 
ATOM   5339 C CA  . LEU D 4 144 ? 37.99076  95.76683  7.17150   1.000 79.29335  ?  156 LEU B CA  1 
ATOM   5340 C C   . LEU D 4 144 ? 39.29741  95.78284  6.39365   1.000 77.44228  ?  156 LEU B C   1 
ATOM   5341 O O   . LEU D 4 144 ? 39.85325  96.85327  6.13087   1.000 84.25107  ?  156 LEU B O   1 
ATOM   5342 C CB  . LEU D 4 144 ? 36.85606  96.34404  6.31810   1.000 67.39903  ?  156 LEU B CB  1 
ATOM   5343 C CG  . LEU D 4 144 ? 36.40007  95.50589  5.12496   1.000 69.58454  ?  156 LEU B CG  1 
ATOM   5344 C CD1 . LEU D 4 144 ? 35.86318  94.16448  5.59513   1.000 84.63800  ?  156 LEU B CD1 1 
ATOM   5345 C CD2 . LEU D 4 144 ? 35.35241  96.25334  4.31590   1.000 87.92068  ?  156 LEU B CD2 1 
ATOM   5346 N N   . ALA D 4 145 ? 39.77817  94.59578  6.03004   1.000 65.52012  ?  157 ALA B N   1 
ATOM   5347 C CA  . ALA D 4 145 ? 40.95959  94.43167  5.19153   1.000 62.20339  ?  157 ALA B CA  1 
ATOM   5348 C C   . ALA D 4 145 ? 40.55867  93.63403  3.96000   1.000 70.17510  ?  157 ALA B C   1 
ATOM   5349 O O   . ALA D 4 145 ? 40.10595  92.49091  4.08038   1.000 67.69550  ?  157 ALA B O   1 
ATOM   5350 C CB  . ALA D 4 145 ? 42.08574  93.72874  5.95173   1.000 65.45188  ?  157 ALA B CB  1 
ATOM   5351 N N   . THR D 4 146 ? 40.72104  94.23335  2.78170   1.000 72.26036  ?  158 THR B N   1 
ATOM   5352 C CA  . THR D 4 146 ? 40.23756  93.64606  1.54121   1.000 72.21229  ?  158 THR B CA  1 
ATOM   5353 C C   . THR D 4 146 ? 41.34559  93.60072  0.49910   1.000 68.43307  ?  158 THR B C   1 
ATOM   5354 O O   . THR D 4 146 ? 42.29417  94.38916  0.53760   1.000 77.29335  ?  158 THR B O   1 
ATOM   5355 C CB  . THR D 4 146 ? 39.04487  94.43157  0.97383   1.000 57.84263  ?  158 THR B CB  1 
ATOM   5356 O OG1 . THR D 4 146 ? 39.42160  95.80041  0.78057   1.000 66.93273  ?  158 THR B OG1 1 
ATOM   5357 C CG2 . THR D 4 146 ? 37.85795  94.36532  1.92177   1.000 71.51176  ?  158 THR B CG2 1 
ATOM   5358 N N   . GLY D 4 147 ? 41.20779  92.66218  -0.43578  1.000 72.64272  ?  159 GLY B N   1 
ATOM   5359 C CA  . GLY D 4 147 ? 42.07916  92.57859  -1.59147  1.000 56.63106  ?  159 GLY B CA  1 
ATOM   5360 C C   . GLY D 4 147 ? 43.52102  92.23016  -1.28956  1.000 53.62660  ?  159 GLY B C   1 
ATOM   5361 O O   . GLY D 4 147 ? 44.43368  92.95590  -1.69487  1.000 85.21651  ?  159 GLY B O   1 
ATOM   5362 N N   . PHE D 4 148 ? 43.74634  91.12214  -0.58804  1.000 63.54691  ?  160 PHE B N   1 
ATOM   5363 C CA  . PHE D 4 148 ? 45.09292  90.65991  -0.29162  1.000 68.87184  ?  160 PHE B CA  1 
ATOM   5364 C C   . PHE D 4 148 ? 45.23089  89.19135  -0.66354  1.000 65.43682  ?  160 PHE B C   1 
ATOM   5365 O O   . PHE D 4 148 ? 44.28330  88.40962  -0.54606  1.000 68.77225  ?  160 PHE B O   1 
ATOM   5366 C CB  . PHE D 4 148 ? 45.45761  90.86423  1.19027   1.000 63.29939  ?  160 PHE B CB  1 
ATOM   5367 C CG  . PHE D 4 148 ? 44.58280  90.10457  2.14929   1.000 60.44879  ?  160 PHE B CG  1 
ATOM   5368 C CD1 . PHE D 4 148 ? 43.43140  90.67917  2.66041   1.000 71.42216  ?  160 PHE B CD1 1 
ATOM   5369 C CD2 . PHE D 4 148 ? 44.92185  88.82338  2.55461   1.000 66.56396  ?  160 PHE B CD2 1 
ATOM   5370 C CE1 . PHE D 4 148 ? 42.62857  89.98682  3.54769   1.000 60.93629  ?  160 PHE B CE1 1 
ATOM   5371 C CE2 . PHE D 4 148 ? 44.12252  88.12605  3.43958   1.000 60.30344  ?  160 PHE B CE2 1 
ATOM   5372 C CZ  . PHE D 4 148 ? 42.97478  88.70868  3.93710   1.000 67.80838  ?  160 PHE B CZ  1 
ATOM   5373 N N   . TYR D 4 149 ? 46.43025  88.82715  -1.12001  1.000 62.70585  ?  161 TYR B N   1 
ATOM   5374 C CA  . TYR D 4 149 ? 46.76021  87.45684  -1.45136  1.000 66.37634  ?  161 TYR B CA  1 
ATOM   5375 C C   . TYR D 4 149 ? 48.25170  87.27787  -1.20334  1.000 76.49193  ?  161 TYR B C   1 
ATOM   5376 O O   . TYR D 4 149 ? 49.04139  88.14164  -1.61645  1.000 80.39862  ?  161 TYR B O   1 
ATOM   5377 C CB  . TYR D 4 149 ? 46.42318  87.10007  -2.89969  1.000 56.35250  ?  161 TYR B CB  1 
ATOM   5378 C CG  . TYR D 4 149 ? 46.75112  85.66846  -3.26289  1.000 72.17792  ?  161 TYR B CG  1 
ATOM   5379 C CD1 . TYR D 4 149 ? 45.83962  84.64738  -3.02937  1.000 77.42803  ?  161 TYR B CD1 1 
ATOM   5380 C CD2 . TYR D 4 149 ? 47.97340  85.33682  -3.83476  1.000 67.12173  ?  161 TYR B CD2 1 
ATOM   5381 C CE1 . TYR D 4 149 ? 46.13396  83.33694  -3.35645  1.000 74.61533  ?  161 TYR B CE1 1 
ATOM   5382 C CE2 . TYR D 4 149 ? 48.27721  84.02906  -4.16393  1.000 79.19792  ?  161 TYR B CE2 1 
ATOM   5383 C CZ  . TYR D 4 149 ? 47.35376  83.03361  -3.92295  1.000 79.63763  ?  161 TYR B CZ  1 
ATOM   5384 O OH  . TYR D 4 149 ? 47.65056  81.73024  -4.24946  1.000 76.94755  ?  161 TYR B OH  1 
ATOM   5385 N N   . PRO D 4 150 ? 48.66820  86.19118  -0.54210  1.000 69.00396  ?  162 PRO B N   1 
ATOM   5386 C CA  . PRO D 4 150 ? 47.84191  85.12370  0.04344   1.000 74.87430  ?  162 PRO B CA  1 
ATOM   5387 C C   . PRO D 4 150 ? 47.18953  85.56010  1.34916   1.000 75.25822  ?  162 PRO B C   1 
ATOM   5388 O O   . PRO D 4 150 ? 47.32508  86.70791  1.76432   1.000 68.81834  ?  162 PRO B O   1 
ATOM   5389 C CB  . PRO D 4 150 ? 48.85005  83.98063  0.27219   1.000 78.13371  ?  162 PRO B CB  1 
ATOM   5390 C CG  . PRO D 4 150 ? 50.08111  84.35175  -0.51825  1.000 83.37525  ?  162 PRO B CG  1 
ATOM   5391 C CD  . PRO D 4 150 ? 50.09647  85.84645  -0.50265  1.000 71.68627  ?  162 PRO B CD  1 
ATOM   5392 N N   . ASP D 4 151 ? 46.47892  84.65827  2.02327   1.000 76.04975  ?  163 ASP B N   1 
ATOM   5393 C CA  . ASP D 4 151 ? 45.85184  84.96314  3.30852   1.000 73.96377  ?  163 ASP B CA  1 
ATOM   5394 C C   . ASP D 4 151 ? 46.83849  84.92814  4.47007   1.000 76.91406  ?  163 ASP B C   1 
ATOM   5395 O O   . ASP D 4 151 ? 46.49859  84.48101  5.56819   1.000 71.98351  ?  163 ASP B O   1 
ATOM   5396 C CB  . ASP D 4 151 ? 44.69486  83.99600  3.54847   1.000 65.57036  ?  163 ASP B CB  1 
ATOM   5397 C CG  . ASP D 4 151 ? 45.11947  82.54451  3.45430   1.000 102.12127 ?  163 ASP B CG  1 
ATOM   5398 O OD1 . ASP D 4 151 ? 46.08408  82.25282  2.71623   1.000 110.30542 ?  163 ASP B OD1 1 
ATOM   5399 O OD2 . ASP D 4 151 ? 44.48738  81.69453  4.11669   1.000 105.24082 -1 163 ASP B OD2 1 
ATOM   5400 N N   . HIS D 4 152 ? 48.06619  85.39560  4.25092   1.000 76.39600  ?  164 HIS B N   1 
ATOM   5401 C CA  . HIS D 4 152 ? 49.09050  85.42102  5.29449   1.000 87.62644  ?  164 HIS B CA  1 
ATOM   5402 C C   . HIS D 4 152 ? 49.02710  86.73902  6.06832   1.000 80.36315  ?  164 HIS B C   1 
ATOM   5403 O O   . HIS D 4 152 ? 49.97140  87.52721  6.10521   1.000 95.43020  ?  164 HIS B O   1 
ATOM   5404 C CB  . HIS D 4 152 ? 50.47123  85.20104  4.68612   1.000 90.45385  ?  164 HIS B CB  1 
ATOM   5405 C CG  . HIS D 4 152 ? 50.64384  83.86134  4.04033   1.000 82.00665  ?  164 HIS B CG  1 
ATOM   5406 N ND1 . HIS D 4 152 ? 51.83514  83.45561  3.47835   1.000 76.88660  ?  164 HIS B ND1 1 
ATOM   5407 C CD2 . HIS D 4 152 ? 49.77793  82.83458  3.86805   1.000 78.45566  ?  164 HIS B CD2 1 
ATOM   5408 C CE1 . HIS D 4 152 ? 51.69555  82.23735  2.98702   1.000 84.00702  ?  164 HIS B CE1 1 
ATOM   5409 N NE2 . HIS D 4 152 ? 50.45657  81.83767  3.21017   1.000 80.66688  ?  164 HIS B NE2 1 
ATOM   5410 N N   . VAL D 4 153 ? 47.87253  86.97004  6.69331   1.000 67.71643  ?  165 VAL B N   1 
ATOM   5411 C CA  . VAL D 4 153 ? 47.63106  88.17942  7.46557   1.000 82.93940  ?  165 VAL B CA  1 
ATOM   5412 C C   . VAL D 4 153 ? 47.17876  87.79269  8.86581   1.000 90.69324  ?  165 VAL B C   1 
ATOM   5413 O O   . VAL D 4 153 ? 46.74125  86.66794  9.11814   1.000 100.13964 ?  165 VAL B O   1 
ATOM   5414 C CB  . VAL D 4 153 ? 46.58068  89.10133  6.80755   1.000 70.85490  ?  165 VAL B CB  1 
ATOM   5415 C CG1 . VAL D 4 153 ? 47.00042  89.47219  5.39602   1.000 72.05327  ?  165 VAL B CG1 1 
ATOM   5416 C CG2 . VAL D 4 153 ? 45.21418  88.43399  6.81069   1.000 69.88360  ?  165 VAL B CG2 1 
ATOM   5417 N N   . GLU D 4 154 ? 47.29307  88.75114  9.78244   1.000 104.96071 ?  166 GLU B N   1 
ATOM   5418 C CA  . GLU D 4 154 ? 46.75478  88.59554  11.12630  1.000 99.42198  ?  166 GLU B CA  1 
ATOM   5419 C C   . GLU D 4 154 ? 46.42806  89.97380  11.67782  1.000 97.17159  ?  166 GLU B C   1 
ATOM   5420 O O   . GLU D 4 154 ? 47.26279  90.88128  11.62121  1.000 90.92509  ?  166 GLU B O   1 
ATOM   5421 C CB  . GLU D 4 154 ? 47.73419  87.86169  12.04670  1.000 108.40991 ?  166 GLU B CB  1 
ATOM   5422 C CG  . GLU D 4 154 ? 47.07346  87.33267  13.30496  1.000 130.59266 ?  166 GLU B CG  1 
ATOM   5423 C CD  . GLU D 4 154 ? 45.79413  86.57135  13.00357  1.000 135.55088 ?  166 GLU B CD  1 
ATOM   5424 O OE1 . GLU D 4 154 ? 45.82303  85.67089  12.13763  1.000 128.51271 ?  166 GLU B OE1 1 
ATOM   5425 O OE2 . GLU D 4 154 ? 44.75501  86.88331  13.62242  1.000 136.84719 ?  166 GLU B OE2 1 
ATOM   5426 N N   . LEU D 4 155 ? 45.21819  90.12150  12.20582  1.000 99.28402  ?  167 LEU B N   1 
ATOM   5427 C CA  . LEU D 4 155 ? 44.69306  91.40833  12.63382  1.000 99.46553  ?  167 LEU B CA  1 
ATOM   5428 C C   . LEU D 4 155 ? 44.72500  91.52157  14.15327  1.000 97.13389  ?  167 LEU B C   1 
ATOM   5429 O O   . LEU D 4 155 ? 44.58220  90.52972  14.87282  1.000 95.22597  ?  167 LEU B O   1 
ATOM   5430 C CB  . LEU D 4 155 ? 43.26232  91.59678  12.11679  1.000 91.82067  ?  167 LEU B CB  1 
ATOM   5431 C CG  . LEU D 4 155 ? 42.60801  92.98008  12.14625  1.000 106.32204 ?  167 LEU B CG  1 
ATOM   5432 C CD1 . LEU D 4 155 ? 41.59746  93.08825  11.01761  1.000 89.64404  ?  167 LEU B CD1 1 
ATOM   5433 C CD2 . LEU D 4 155 ? 41.92876  93.24791  13.47977  1.000 111.38535 ?  167 LEU B CD2 1 
ATOM   5434 N N   . SER D 4 156 ? 44.91565  92.74936  14.63324  1.000 89.14421  ?  168 SER B N   1 
ATOM   5435 C CA  . SER D 4 156 ? 44.90314  93.03361  16.05973  1.000 102.69860 ?  168 SER B CA  1 
ATOM   5436 C C   . SER D 4 156 ? 44.45602  94.47201  16.27522  1.000 101.85578 ?  168 SER B C   1 
ATOM   5437 O O   . SER D 4 156 ? 44.74163  95.35477  15.46152  1.000 104.76301 ?  168 SER B O   1 
ATOM   5438 C CB  . SER D 4 156 ? 46.27992  92.80559  16.69443  1.000 101.78199 ?  168 SER B CB  1 
ATOM   5439 O OG  . SER D 4 156 ? 47.25266  93.66116  16.12047  1.000 118.86692 ?  168 SER B OG  1 
ATOM   5440 N N   . TRP D 4 157 ? 43.74935  94.69736  17.37840  1.000 100.85020 ?  169 TRP B N   1 
ATOM   5441 C CA  . TRP D 4 157 ? 43.28617  96.02377  17.75603  1.000 100.76765 ?  169 TRP B CA  1 
ATOM   5442 C C   . TRP D 4 157 ? 44.22537  96.64008  18.78509  1.000 114.39437 ?  169 TRP B C   1 
ATOM   5443 O O   . TRP D 4 157 ? 44.81146  95.94223  19.61637  1.000 123.82155 ?  169 TRP B O   1 
ATOM   5444 C CB  . TRP D 4 157 ? 41.86493  95.97134  18.32105  1.000 106.69675 ?  169 TRP B CB  1 
ATOM   5445 C CG  . TRP D 4 157 ? 40.80165  95.77592  17.28344  1.000 102.63472 ?  169 TRP B CG  1 
ATOM   5446 C CD1 . TRP D 4 157 ? 40.35350  94.58954  16.78220  1.000 92.70389  ?  169 TRP B CD1 1 
ATOM   5447 C CD2 . TRP D 4 157 ? 40.04530  96.80030  16.62591  1.000 91.15008  ?  169 TRP B CD2 1 
ATOM   5448 N NE1 . TRP D 4 157 ? 39.36767  94.81047  15.85139  1.000 83.19659  ?  169 TRP B NE1 1 
ATOM   5449 C CE2 . TRP D 4 157 ? 39.15984  96.15978  15.73700  1.000 89.91494  ?  169 TRP B CE2 1 
ATOM   5450 C CE3 . TRP D 4 157 ? 40.03295  98.19644  16.70077  1.000 91.27285  ?  169 TRP B CE3 1 
ATOM   5451 C CZ2 . TRP D 4 157 ? 38.27037  96.86675  14.93036  1.000 96.48472  ?  169 TRP B CZ2 1 
ATOM   5452 C CZ3 . TRP D 4 157 ? 39.14905  98.89655  15.89868  1.000 91.69811  ?  169 TRP B CZ3 1 
ATOM   5453 C CH2 . TRP D 4 157 ? 38.28104  98.23103  15.02479  1.000 86.61756  ?  169 TRP B CH2 1 
ATOM   5454 N N   . TRP D 4 158 ? 44.35990  97.96285  18.72120  1.000 122.42472 ?  170 TRP B N   1 
ATOM   5455 C CA  . TRP D 4 158 ? 45.21569  98.71295  19.63027  1.000 129.75812 ?  170 TRP B CA  1 
ATOM   5456 C C   . TRP D 4 158 ? 44.45277  99.91930  20.15347  1.000 125.09082 ?  170 TRP B C   1 
ATOM   5457 O O   . TRP D 4 158 ? 43.87928  100.68262 19.36985  1.000 129.67694 ?  170 TRP B O   1 
ATOM   5458 C CB  . TRP D 4 158 ? 46.50558  99.16350  18.93575  1.000 123.89234 ?  170 TRP B CB  1 
ATOM   5459 C CG  . TRP D 4 158 ? 47.37741  98.03072  18.49186  1.000 123.34706 ?  170 TRP B CG  1 
ATOM   5460 C CD1 . TRP D 4 158 ? 47.24271  97.29017  17.35418  1.000 123.63027 ?  170 TRP B CD1 1 
ATOM   5461 C CD2 . TRP D 4 158 ? 48.52459  97.51139  19.17534  1.000 123.56992 ?  170 TRP B CD2 1 
ATOM   5462 N NE1 . TRP D 4 158 ? 48.23262  96.33975  17.28799  1.000 132.52851 ?  170 TRP B NE1 1 
ATOM   5463 C CE2 . TRP D 4 158 ? 49.03294  96.45478  18.39407  1.000 124.43740 ?  170 TRP B CE2 1 
ATOM   5464 C CE3 . TRP D 4 158 ? 49.17012  97.83635  20.37232  1.000 130.95801 ?  170 TRP B CE3 1 
ATOM   5465 C CZ2 . TRP D 4 158 ? 50.15618  95.72129  18.77037  1.000 122.89822 ?  170 TRP B CZ2 1 
ATOM   5466 C CZ3 . TRP D 4 158 ? 50.28519  97.10677  20.74430  1.000 129.92609 ?  170 TRP B CZ3 1 
ATOM   5467 C CH2 . TRP D 4 158 ? 50.76660  96.06176  19.94584  1.000 125.45600 ?  170 TRP B CH2 1 
ATOM   5468 N N   . VAL D 4 159 ? 44.44692  100.08754 21.47258  1.000 124.02782 ?  171 VAL B N   1 
ATOM   5469 C CA  . VAL D 4 159 ? 43.79358  101.21473 22.12810  1.000 127.89624 ?  171 VAL B CA  1 
ATOM   5470 C C   . VAL D 4 159 ? 44.84310  101.92464 22.97114  1.000 134.79786 ?  171 VAL B C   1 
ATOM   5471 O O   . VAL D 4 159 ? 45.29536  101.38874 23.99182  1.000 124.19913 ?  171 VAL B O   1 
ATOM   5472 C CB  . VAL D 4 159 ? 42.60017  100.77462 22.98613  1.000 129.46897 ?  171 VAL B CB  1 
ATOM   5473 C CG1 . VAL D 4 159 ? 42.02333  101.96391 23.73952  1.000 136.37036 ?  171 VAL B CG1 1 
ATOM   5474 C CG2 . VAL D 4 159 ? 41.53488  100.12486 22.11694  1.000 109.02170 ?  171 VAL B CG2 1 
ATOM   5475 N N   . ASN D 4 160 ? 45.23377  103.12676 22.54126  1.000 138.07737 ?  172 ASN B N   1 
ATOM   5476 C CA  . ASN D 4 160 ? 46.21486  103.94896 23.25255  1.000 138.49728 ?  172 ASN B CA  1 
ATOM   5477 C C   . ASN D 4 160 ? 47.55162  103.22388 23.39864  1.000 140.17559 ?  172 ASN B C   1 
ATOM   5478 O O   . ASN D 4 160 ? 48.22989  103.33155 24.42237  1.000 135.73109 ?  172 ASN B O   1 
ATOM   5479 C CB  . ASN D 4 160 ? 45.68077  104.39092 24.61734  1.000 145.34603 ?  172 ASN B CB  1 
ATOM   5480 C CG  . ASN D 4 160 ? 44.38847  105.17661 24.50973  1.000 143.27335 ?  172 ASN B CG  1 
ATOM   5481 O OD1 . ASN D 4 160 ? 44.18735  105.93613 23.56208  1.000 145.66865 ?  172 ASN B OD1 1 
ATOM   5482 N ND2 . ASN D 4 160 ? 43.50217  104.99421 25.48163  1.000 137.86954 ?  172 ASN B ND2 1 
ATOM   5483 N N   . GLY D 4 161 ? 47.93386  102.47818 22.36422  1.000 125.42991 ?  173 GLY B N   1 
ATOM   5484 C CA  . GLY D 4 161 ? 49.20908  101.79209 22.35393  1.000 130.75759 ?  173 GLY B CA  1 
ATOM   5485 C C   . GLY D 4 161 ? 49.23332  100.44881 23.04531  1.000 131.17544 ?  173 GLY B C   1 
ATOM   5486 O O   . GLY D 4 161 ? 50.31872  99.88498  23.22556  1.000 144.40386 ?  173 GLY B O   1 
ATOM   5487 N N   . LYS D 4 162 ? 48.07923  99.91492  23.43832  1.000 123.26536 ?  174 LYS B N   1 
ATOM   5488 C CA  . LYS D 4 162 ? 47.99944  98.62267  24.10564  1.000 122.80429 ?  174 LYS B CA  1 
ATOM   5489 C C   . LYS D 4 162 ? 47.01340  97.73762  23.36007  1.000 116.07700 ?  174 LYS B C   1 
ATOM   5490 O O   . LYS D 4 162 ? 45.89669  98.16819  23.05490  1.000 115.39884 ?  174 LYS B O   1 
ATOM   5491 C CB  . LYS D 4 162 ? 47.57373  98.77864  25.56977  1.000 127.33860 ?  174 LYS B CB  1 
ATOM   5492 N N   . GLU D 4 163 ? 47.42722  96.50701  23.06766  1.000 114.14156 ?  175 GLU B N   1 
ATOM   5493 C CA  . GLU D 4 163 ? 46.55920  95.57430  22.36216  1.000 108.37397 ?  175 GLU B CA  1 
ATOM   5494 C C   . GLU D 4 163 ? 45.44013  95.10159  23.28136  1.000 120.83196 ?  175 GLU B C   1 
ATOM   5495 O O   . GLU D 4 163 ? 45.69455  94.58673  24.37457  1.000 132.49491 ?  175 GLU B O   1 
ATOM   5496 C CB  . GLU D 4 163 ? 47.36465  94.38249  21.84771  1.000 112.22749 ?  175 GLU B CB  1 
ATOM   5497 C CG  . GLU D 4 163 ? 46.55294  93.40001  21.01888  1.000 116.72246 ?  175 GLU B CG  1 
ATOM   5498 C CD  . GLU D 4 163 ? 47.38935  92.25236  20.48773  1.000 120.21440 ?  175 GLU B CD  1 
ATOM   5499 O OE1 . GLU D 4 163 ? 48.54234  92.09438  20.94099  1.000 110.22727 ?  175 GLU B OE1 1 
ATOM   5500 O OE2 . GLU D 4 163 ? 46.89427  91.50941  19.61421  1.000 123.82611 -1 175 GLU B OE2 1 
ATOM   5501 N N   . VAL D 4 164 ? 44.19995  95.27636  22.83593  1.000 127.53123 ?  176 VAL B N   1 
ATOM   5502 C CA  . VAL D 4 164 ? 43.03111  94.92921  23.62970  1.000 132.38727 ?  176 VAL B CA  1 
ATOM   5503 C C   . VAL D 4 164 ? 42.37578  93.68534  23.04444  1.000 119.01601 ?  176 VAL B C   1 
ATOM   5504 O O   . VAL D 4 164 ? 42.56017  93.33721  21.87392  1.000 116.29488 ?  176 VAL B O   1 
ATOM   5505 C CB  . VAL D 4 164 ? 42.02136  96.09240  23.70855  1.000 127.29764 ?  176 VAL B CB  1 
ATOM   5506 C CG1 . VAL D 4 164 ? 42.65745  97.30178  24.37576  1.000 124.33846 ?  176 VAL B CG1 1 
ATOM   5507 C CG2 . VAL D 4 164 ? 41.51128  96.44542  22.31978  1.000 117.32424 ?  176 VAL B CG2 1 
ATOM   5508 N N   . HIS D 4 165 ? 41.59568  93.00646  23.88615  1.000 122.56642 ?  177 HIS B N   1 
ATOM   5509 C CA  . HIS D 4 165 ? 40.87139  91.81295  23.46801  1.000 118.45382 ?  177 HIS B CA  1 
ATOM   5510 C C   . HIS D 4 165 ? 39.42650  91.77319  23.93919  1.000 110.81359 ?  177 HIS B C   1 
ATOM   5511 O O   . HIS D 4 165 ? 38.67514  90.91668  23.46363  1.000 111.07985 ?  177 HIS B O   1 
ATOM   5512 C CB  . HIS D 4 165 ? 41.58813  90.54825  23.96491  1.000 128.23968 ?  177 HIS B CB  1 
ATOM   5513 C CG  . HIS D 4 165 ? 43.01635  90.45064  23.52678  1.000 127.53412 ?  177 HIS B CG  1 
ATOM   5514 N ND1 . HIS D 4 165 ? 44.03070  91.16128  24.13161  1.000 129.46274 ?  177 HIS B ND1 1 
ATOM   5515 C CD2 . HIS D 4 165 ? 43.59967  89.72721  22.54197  1.000 127.36543 ?  177 HIS B CD2 1 
ATOM   5516 C CE1 . HIS D 4 165 ? 45.17729  90.87905  23.53932  1.000 127.34045 ?  177 HIS B CE1 1 
ATOM   5517 N NE2 . HIS D 4 165 ? 44.94343  90.01143  22.57127  1.000 130.95855 ?  177 HIS B NE2 1 
ATOM   5518 N N   . SER D 4 166 ? 39.00861  92.65316  24.84619  1.000 111.16566 ?  178 SER B N   1 
ATOM   5519 C CA  . SER D 4 166 ? 37.63205  92.65498  25.32484  1.000 116.40425 ?  178 SER B CA  1 
ATOM   5520 C C   . SER D 4 166 ? 36.70249  93.15711  24.22709  1.000 111.82666 ?  178 SER B C   1 
ATOM   5521 O O   . SER D 4 166 ? 36.83752  94.29298  23.76003  1.000 111.81283 ?  178 SER B O   1 
ATOM   5522 C CB  . SER D 4 166 ? 37.50871  93.52457  26.57325  1.000 122.00609 ?  178 SER B CB  1 
ATOM   5523 O OG  . SER D 4 166 ? 37.87778  94.86510  26.29925  1.000 123.05701 ?  178 SER B OG  1 
ATOM   5524 N N   . GLY D 4 167 ? 35.76008  92.31263  23.81692  1.000 119.01262 ?  179 GLY B N   1 
ATOM   5525 C CA  . GLY D 4 167 ? 34.83515  92.68501  22.76404  1.000 104.18300 ?  179 GLY B CA  1 
ATOM   5526 C C   . GLY D 4 167 ? 35.44513  92.71605  21.38187  1.000 99.78110  ?  179 GLY B C   1 
ATOM   5527 O O   . GLY D 4 167 ? 34.95573  93.44336  20.51255  1.000 98.97421  ?  179 GLY B O   1 
ATOM   5528 N N   . VAL D 4 168 ? 36.50281  91.94277  21.15322  1.000 102.93629 ?  180 VAL B N   1 
ATOM   5529 C CA  . VAL D 4 168 ? 37.19822  91.89748  19.87191  1.000 88.52901  ?  180 VAL B CA  1 
ATOM   5530 C C   . VAL D 4 168 ? 36.90800  90.55281  19.22195  1.000 88.82750  ?  180 VAL B C   1 
ATOM   5531 O O   . VAL D 4 168 ? 37.22510  89.50033  19.79034  1.000 105.59483 ?  180 VAL B O   1 
ATOM   5532 C CB  . VAL D 4 168 ? 38.71089  92.10643  20.04039  1.000 84.79503  ?  180 VAL B CB  1 
ATOM   5533 C CG1 . VAL D 4 168 ? 39.42577  91.88775  18.71727  1.000 81.83049  ?  180 VAL B CG1 1 
ATOM   5534 C CG2 . VAL D 4 168 ? 39.00006  93.49400  20.58643  1.000 92.99047  ?  180 VAL B CG2 1 
ATOM   5535 N N   . CYS D 4 169 ? 36.30761  90.58268  18.03363  1.000 84.39503  ?  181 CYS B N   1 
ATOM   5536 C CA  . CYS D 4 169 ? 36.08776  89.37444  17.25305  1.000 88.65294  ?  181 CYS B CA  1 
ATOM   5537 C C   . CYS D 4 169 ? 36.62023  89.56460  15.84264  1.000 87.87320  ?  181 CYS B C   1 
ATOM   5538 O O   . CYS D 4 169 ? 36.41916  90.61531  15.22643  1.000 98.52719  ?  181 CYS B O   1 
ATOM   5539 C CB  . CYS D 4 169 ? 34.60823  88.98318  17.18033  1.000 90.22922  ?  181 CYS B CB  1 
ATOM   5540 S SG  . CYS D 4 169 ? 34.38719  87.34656  16.43661  1.000 132.28897 ?  181 CYS B SG  1 
ATOM   5541 N N   . THR D 4 170 ? 37.29400  88.53626  15.33904  1.000 78.23506  ?  182 THR B N   1 
ATOM   5542 C CA  . THR D 4 170 ? 37.79139  88.49993  13.97476  1.000 74.73399  ?  182 THR B CA  1 
ATOM   5543 C C   . THR D 4 170 ? 37.25314  87.25178  13.28917  1.000 80.89384  ?  182 THR B C   1 
ATOM   5544 O O   . THR D 4 170 ? 37.02797  86.22227  13.93292  1.000 95.60310  ?  182 THR B O   1 
ATOM   5545 C CB  . THR D 4 170 ? 39.32698  88.50536  13.94058  1.000 69.60910  ?  182 THR B CB  1 
ATOM   5546 O OG1 . THR D 4 170 ? 39.82114  89.48014  14.86715  1.000 72.06701  ?  182 THR B OG1 1 
ATOM   5547 C CG2 . THR D 4 170 ? 39.83417  88.84782  12.54753  1.000 70.56673  ?  182 THR B CG2 1 
ATOM   5548 N N   . ASP D 4 171 ? 37.03143  87.35551  11.98396  1.000 83.52953  ?  183 ASP B N   1 
ATOM   5549 C CA  . ASP D 4 171 ? 36.51874  86.22346  11.22673  1.000 83.83140  ?  183 ASP B CA  1 
ATOM   5550 C C   . ASP D 4 171 ? 37.50639  85.06273  11.29702  1.000 91.09727  ?  183 ASP B C   1 
ATOM   5551 O O   . ASP D 4 171 ? 38.70199  85.25581  11.03409  1.000 93.81468  ?  183 ASP B O   1 
ATOM   5552 C CB  . ASP D 4 171 ? 36.27142  86.61777  9.77171   1.000 87.74808  ?  183 ASP B CB  1 
ATOM   5553 C CG  . ASP D 4 171 ? 35.23586  87.71524  9.63351   1.000 95.35895  ?  183 ASP B CG  1 
ATOM   5554 O OD1 . ASP D 4 171 ? 34.29241  87.75048  10.45126  1.000 97.86464  ?  183 ASP B OD1 1 
ATOM   5555 O OD2 . ASP D 4 171 ? 35.36553  88.54333  8.70747   1.000 95.53384  -1 183 ASP B OD2 1 
ATOM   5556 N N   . PRO D 4 172 ? 37.06057  83.85816  11.66131  1.000 82.20594  ?  184 PRO B N   1 
ATOM   5557 C CA  . PRO D 4 172 ? 37.99189  82.71945  11.70156  1.000 76.51476  ?  184 PRO B CA  1 
ATOM   5558 C C   . PRO D 4 172 ? 38.57991  82.38112  10.34501  1.000 80.34855  ?  184 PRO B C   1 
ATOM   5559 O O   . PRO D 4 172 ? 39.72743  81.92398  10.27172  1.000 90.87365  ?  184 PRO B O   1 
ATOM   5560 C CB  . PRO D 4 172 ? 37.12256  81.57428  12.24183  1.000 82.29754  ?  184 PRO B CB  1 
ATOM   5561 C CG  . PRO D 4 172 ? 35.97194  82.24777  12.92471  1.000 79.21342  ?  184 PRO B CG  1 
ATOM   5562 C CD  . PRO D 4 172 ? 35.71672  83.49505  12.13912  1.000 72.99897  ?  184 PRO B CD  1 
ATOM   5563 N N   . GLN D 4 173 ? 37.82814  82.59428  9.26674   1.000 88.94790  ?  185 GLN B N   1 
ATOM   5564 C CA  . GLN D 4 173 ? 38.28848  82.32276  7.91682   1.000 89.93265  ?  185 GLN B CA  1 
ATOM   5565 C C   . GLN D 4 173 ? 37.98659  83.51527  7.02051   1.000 80.06714  ?  185 GLN B C   1 
ATOM   5566 O O   . GLN D 4 173 ? 36.91694  84.12634  7.13581   1.000 93.01901  ?  185 GLN B O   1 
ATOM   5567 C CB  . GLN D 4 173 ? 37.61925  81.06276  7.34933   1.000 99.62130  ?  185 GLN B CB  1 
ATOM   5568 C CG  . GLN D 4 173 ? 37.93455  79.79255  8.12138   1.000 104.69270 ?  185 GLN B CG  1 
ATOM   5569 C CD  . GLN D 4 173 ? 37.12373  78.60532  7.64387   1.000 127.99151 ?  185 GLN B CD  1 
ATOM   5570 O OE1 . GLN D 4 173 ? 36.18111  78.75520  6.86632   1.000 133.96490 ?  185 GLN B OE1 1 
ATOM   5571 N NE2 . GLN D 4 173 ? 37.48701  77.41535  8.10821   1.000 135.83557 ?  185 GLN B NE2 1 
ATOM   5572 N N   . PRO D 4 174 ? 38.90302  83.87224  6.12532   1.000 74.56632  ?  186 PRO B N   1 
ATOM   5573 C CA  . PRO D 4 174 ? 38.66828  85.01895  5.24198   1.000 64.25719  ?  186 PRO B CA  1 
ATOM   5574 C C   . PRO D 4 174 ? 37.66981  84.68346  4.14354   1.000 69.42248  ?  186 PRO B C   1 
ATOM   5575 O O   . PRO D 4 174 ? 37.30796  83.52866  3.90981   1.000 78.20853  ?  186 PRO B O   1 
ATOM   5576 C CB  . PRO D 4 174 ? 40.05607  85.31021  4.66698   1.000 77.02469  ?  186 PRO B CB  1 
ATOM   5577 C CG  . PRO D 4 174 ? 40.74595  83.98662  4.69404   1.000 78.61004  ?  186 PRO B CG  1 
ATOM   5578 C CD  . PRO D 4 174 ? 40.23734  83.28021  5.92367   1.000 75.07800  ?  186 PRO B CD  1 
ATOM   5579 N N   A LEU D 4 175 ? 37.19999  85.73475  3.48109   0.500 64.14088  ?  187 LEU B N   1 
ATOM   5580 N N   B LEU D 4 175 ? 37.24406  85.73005  3.44185   0.500 64.56956  ?  187 LEU B N   1 
ATOM   5581 C CA  A LEU D 4 175 ? 36.29283  85.61044  2.35184   0.500 61.67940  ?  187 LEU B CA  1 
ATOM   5582 C CA  B LEU D 4 175 ? 36.27905  85.62449  2.35724   0.500 61.62912  ?  187 LEU B CA  1 
ATOM   5583 C C   A LEU D 4 175 ? 37.07106  85.69583  1.04711   0.500 66.13973  ?  187 LEU B C   1 
ATOM   5584 C C   B LEU D 4 175 ? 36.98095  85.79284  1.01521   0.500 66.20344  ?  187 LEU B C   1 
ATOM   5585 O O   A LEU D 4 175 ? 38.07551  86.40407  0.94718   0.500 69.31191  ?  187 LEU B O   1 
ATOM   5586 O O   B LEU D 4 175 ? 37.85167  86.65543  0.86317   0.500 69.24742  ?  187 LEU B O   1 
ATOM   5587 C CB  A LEU D 4 175 ? 35.21981  86.70112  2.37849   0.500 58.37150  ?  187 LEU B CB  1 
ATOM   5588 C CB  B LEU D 4 175 ? 35.17296  86.67377  2.51580   0.500 58.34111  ?  187 LEU B CB  1 
ATOM   5589 C CG  A LEU D 4 175 ? 34.05185  86.54848  3.35138   0.500 58.80828  ?  187 LEU B CG  1 
ATOM   5590 C CG  B LEU D 4 175 ? 34.15285  86.84399  1.38949   0.500 57.30126  ?  187 LEU B CG  1 
ATOM   5591 C CD1 A LEU D 4 175 ? 33.09891  87.72130  3.19705   0.500 52.95546  ?  187 LEU B CD1 1 
ATOM   5592 C CD1 B LEU D 4 175 ? 32.75147  86.96835  1.96170   0.500 63.68295  ?  187 LEU B CD1 1 
ATOM   5593 C CD2 A LEU D 4 175 ? 33.32776  85.23235  3.11992   0.500 54.16884  ?  187 LEU B CD2 1 
ATOM   5594 C CD2 B LEU D 4 175 ? 34.49092  88.06433  0.54749   0.500 57.21006  ?  187 LEU B CD2 1 
ATOM   5595 N N   . LYS D 4 176 ? 36.59579  84.96611  0.04397   1.000 64.41782  ?  188 LYS B N   1 
ATOM   5596 C CA  . LYS D 4 176 ? 37.18745  85.01061  -1.28722  1.000 69.00728  ?  188 LYS B CA  1 
ATOM   5597 C C   . LYS D 4 176 ? 36.48472  86.07624  -2.11992  1.000 65.44143  ?  188 LYS B C   1 
ATOM   5598 O O   . LYS D 4 176 ? 35.26404  86.02275  -2.30519  1.000 68.01665  ?  188 LYS B O   1 
ATOM   5599 C CB  . LYS D 4 176 ? 37.09297  83.64690  -1.96925  1.000 78.33048  ?  188 LYS B CB  1 
ATOM   5600 C CG  . LYS D 4 176 ? 38.11210  82.62979  -1.48263  1.000 75.32070  ?  188 LYS B CG  1 
ATOM   5601 C CD  . LYS D 4 176 ? 38.11098  81.39186  -2.36669  1.000 71.29872  ?  188 LYS B CD  1 
ATOM   5602 C CE  . LYS D 4 176 ? 39.20369  80.41667  -1.96090  1.000 95.65519  ?  188 LYS B CE  1 
ATOM   5603 N NZ  . LYS D 4 176 ? 39.23326  79.21999  -2.84710  1.000 100.12189 ?  188 LYS B NZ  1 
ATOM   5604 N N   . GLU D 4 177 ? 37.25520  87.04507  -2.62030  1.000 66.35331  ?  189 GLU B N   1 
ATOM   5605 C CA  . GLU D 4 177 ? 36.68809  88.07811  -3.47884  1.000 63.08810  ?  189 GLU B CA  1 
ATOM   5606 C C   . GLU D 4 177 ? 36.38829  87.56177  -4.87991  1.000 57.78953  ?  189 GLU B C   1 
ATOM   5607 O O   . GLU D 4 177 ? 35.56247  88.15429  -5.58220  1.000 72.38494  ?  189 GLU B O   1 
ATOM   5608 C CB  . GLU D 4 177 ? 37.63316  89.27760  -3.55203  1.000 55.77577  ?  189 GLU B CB  1 
ATOM   5609 C CG  . GLU D 4 177 ? 37.87757  89.95231  -2.21184  1.000 60.06792  ?  189 GLU B CG  1 
ATOM   5610 C CD  . GLU D 4 177 ? 38.84269  91.11651  -2.31336  1.000 72.34447  ?  189 GLU B CD  1 
ATOM   5611 O OE1 . GLU D 4 177 ? 39.51189  91.24552  -3.36018  1.000 73.67883  ?  189 GLU B OE1 1 
ATOM   5612 O OE2 . GLU D 4 177 ? 38.92981  91.90431  -1.34796  1.000 78.88963  -1 189 GLU B OE2 1 
ATOM   5613 N N   . GLN D 4 178 ? 37.04104  86.47972  -5.30054  1.000 54.58229  ?  190 GLN B N   1 
ATOM   5614 C CA  . GLN D 4 178 ? 36.75969  85.81300  -6.57141  1.000 60.80139  ?  190 GLN B CA  1 
ATOM   5615 C C   . GLN D 4 178 ? 36.49638  84.34458  -6.26561  1.000 64.56265  ?  190 GLN B C   1 
ATOM   5616 O O   . GLN D 4 178 ? 37.38124  83.49379  -6.43001  1.000 61.78977  ?  190 GLN B O   1 
ATOM   5617 C CB  . GLN D 4 178 ? 37.91153  85.98663  -7.56304  1.000 66.02070  ?  190 GLN B CB  1 
ATOM   5618 C CG  . GLN D 4 178 ? 38.19950  87.43433  -7.94038  1.000 64.70775  ?  190 GLN B CG  1 
ATOM   5619 C CD  . GLN D 4 178 ? 39.43079  87.99044  -7.25160  1.000 67.53732  ?  190 GLN B CD  1 
ATOM   5620 O OE1 . GLN D 4 178 ? 40.30471  87.24149  -6.81571  1.000 69.09336  ?  190 GLN B OE1 1 
ATOM   5621 N NE2 . GLN D 4 178 ? 39.50606  89.31260  -7.15167  1.000 67.16564  ?  190 GLN B NE2 1 
ATOM   5622 N N   . PRO D 4 179 ? 35.28021  84.01075  -5.82427  1.000 64.63889  ?  191 PRO B N   1 
ATOM   5623 C CA  . PRO D 4 179 ? 35.02120  82.64725  -5.32695  1.000 62.25635  ?  191 PRO B CA  1 
ATOM   5624 C C   . PRO D 4 179 ? 35.25231  81.54876  -6.35186  1.000 55.12368  ?  191 PRO B C   1 
ATOM   5625 O O   . PRO D 4 179 ? 35.41525  80.38719  -5.95823  1.000 73.18404  ?  191 PRO B O   1 
ATOM   5626 C CB  . PRO D 4 179 ? 33.54757  82.70554  -4.89854  1.000 72.38070  ?  191 PRO B CB  1 
ATOM   5627 C CG  . PRO D 4 179 ? 33.26921  84.15910  -4.67344  1.000 65.05288  ?  191 PRO B CG  1 
ATOM   5628 C CD  . PRO D 4 179 ? 34.10462  84.88548  -5.68284  1.000 57.54472  ?  191 PRO B CD  1 
ATOM   5629 N N   . ALA D 4 180 ? 35.27078  81.86701  -7.64354  1.000 59.09558  ?  192 ALA B N   1 
ATOM   5630 C CA  . ALA D 4 180 ? 35.49857  80.87094  -8.68188  1.000 69.43189  ?  192 ALA B CA  1 
ATOM   5631 C C   . ALA D 4 180 ? 36.97599  80.63209  -8.96493  1.000 71.13659  ?  192 ALA B C   1 
ATOM   5632 O O   . ALA D 4 180 ? 37.30206  79.76539  -9.78242  1.000 76.28480  ?  192 ALA B O   1 
ATOM   5633 C CB  . ALA D 4 180 ? 34.79028  81.28327  -9.97650  1.000 64.52459  ?  192 ALA B CB  1 
ATOM   5634 N N   . LEU D 4 181 ? 37.87107  81.37087  -8.31605  1.000 69.42172  ?  193 LEU B N   1 
ATOM   5635 C CA  . LEU D 4 181 ? 39.30565  81.24967  -8.53132  1.000 68.44595  ?  193 LEU B CA  1 
ATOM   5636 C C   . LEU D 4 181 ? 39.97346  80.67809  -7.28796  1.000 83.28689  ?  193 LEU B C   1 
ATOM   5637 O O   . LEU D 4 181 ? 39.56967  80.98050  -6.16016  1.000 88.71817  ?  193 LEU B O   1 
ATOM   5638 C CB  . LEU D 4 181 ? 39.92637  82.60862  -8.87623  1.000 67.68576  ?  193 LEU B CB  1 
ATOM   5639 C CG  . LEU D 4 181 ? 39.94010  83.06244  -10.34121 1.000 71.71808  ?  193 LEU B CG  1 
ATOM   5640 C CD1 . LEU D 4 181 ? 38.54674  83.07721  -10.95269 1.000 61.88813  ?  193 LEU B CD1 1 
ATOM   5641 C CD2 . LEU D 4 181 ? 40.58796  84.43357  -10.46794 1.000 56.06297  ?  193 LEU B CD2 1 
ATOM   5642 N N   . ASN D 4 182 ? 40.99851  79.84848  -7.49808  1.000 79.25365  ?  194 ASN B N   1 
ATOM   5643 C CA  . ASN D 4 182 ? 41.76197  79.32827  -6.36842  1.000 91.73105  ?  194 ASN B CA  1 
ATOM   5644 C C   . ASN D 4 182 ? 42.79797  80.33424  -5.88407  1.000 76.86673  ?  194 ASN B C   1 
ATOM   5645 O O   . ASN D 4 182 ? 43.07845  80.41166  -4.68344  1.000 80.36354  ?  194 ASN B O   1 
ATOM   5646 C CB  . ASN D 4 182 ? 42.43587  78.00662  -6.74066  1.000 96.88414  ?  194 ASN B CB  1 
ATOM   5647 C CG  . ASN D 4 182 ? 43.22644  78.08865  -8.03547  1.000 113.64001 ?  194 ASN B CG  1 
ATOM   5648 O OD1 . ASN D 4 182 ? 43.94558  79.05570  -8.29147  1.000 122.28373 ?  194 ASN B OD1 1 
ATOM   5649 N ND2 . ASN D 4 182 ? 43.09052  77.06169  -8.86397  1.000 103.85907 ?  194 ASN B ND2 1 
ATOM   5650 N N   . ASP D 4 183 ? 43.37221  81.11360  -6.79730  1.000 70.19090  ?  195 ASP B N   1 
ATOM   5651 C CA  . ASP D 4 183 ? 44.32448  82.14755  -6.41559  1.000 84.44923  ?  195 ASP B CA  1 
ATOM   5652 C C   . ASP D 4 183 ? 43.59066  83.45337  -6.14671  1.000 90.86531  ?  195 ASP B C   1 
ATOM   5653 O O   . ASP D 4 183 ? 44.10200  84.54297  -6.43073  1.000 85.80365  ?  195 ASP B O   1 
ATOM   5654 C CB  . ASP D 4 183 ? 45.37460  82.32948  -7.50310  1.000 73.82053  ?  195 ASP B CB  1 
ATOM   5655 C CG  . ASP D 4 183 ? 44.76300  82.58406  -8.86134  1.000 85.63200  ?  195 ASP B CG  1 
ATOM   5656 O OD1 . ASP D 4 183 ? 44.27218  83.70741  -9.09178  1.000 96.29480  ?  195 ASP B OD1 1 
ATOM   5657 O OD2 . ASP D 4 183 ? 44.76829  81.65848  -9.70191  1.000 104.81620 ?  195 ASP B OD2 1 
ATOM   5658 N N   . SER D 4 184 ? 42.38715  83.34023  -5.59523  1.000 79.18888  ?  196 SER B N   1 
ATOM   5659 C CA  . SER D 4 184 ? 41.54470  84.49894  -5.36592  1.000 56.25835  ?  196 SER B CA  1 
ATOM   5660 C C   . SER D 4 184 ? 42.11552  85.37146  -4.25759  1.000 59.36413  ?  196 SER B C   1 
ATOM   5661 O O   . SER D 4 184 ? 42.72740  84.88728  -3.30138  1.000 72.69926  ?  196 SER B O   1 
ATOM   5662 C CB  . SER D 4 184 ? 40.13027  84.05932  -5.00436  1.000 59.25978  ?  196 SER B CB  1 
ATOM   5663 O OG  . SER D 4 184 ? 39.36771  85.15910  -4.54676  1.000 59.70999  ?  196 SER B OG  1 
ATOM   5664 N N   . ARG D 4 185 ? 41.91395  86.67570  -4.40326  1.000 59.56141  ?  197 ARG B N   1 
ATOM   5665 C CA  . ARG D 4 185 ? 42.28806  87.61239  -3.35780  1.000 58.47662  ?  197 ARG B CA  1 
ATOM   5666 C C   . ARG D 4 185 ? 41.28039  87.54596  -2.21666  1.000 60.52851  ?  197 ARG B C   1 
ATOM   5667 O O   . ARG D 4 185 ? 40.08259  87.33989  -2.42726  1.000 65.01184  ?  197 ARG B O   1 
ATOM   5668 C CB  . ARG D 4 185 ? 42.37245  89.03046  -3.92155  1.000 55.61487  ?  197 ARG B CB  1 
ATOM   5669 C CG  . ARG D 4 185 ? 43.37539  89.17154  -5.05594  1.000 61.05116  ?  197 ARG B CG  1 
ATOM   5670 C CD  . ARG D 4 185 ? 43.31024  90.54404  -5.70431  1.000 63.65334  ?  197 ARG B CD  1 
ATOM   5671 N NE  . ARG D 4 185 ? 43.64892  91.61212  -4.77215  1.000 70.31596  ?  197 ARG B NE  1 
ATOM   5672 C CZ  . ARG D 4 185 ? 43.81328  92.88148  -5.11822  1.000 77.54042  ?  197 ARG B CZ  1 
ATOM   5673 N NH1 . ARG D 4 185 ? 43.68349  93.27789  -6.37376  1.000 61.27772  ?  197 ARG B NH1 1 
ATOM   5674 N NH2 . ARG D 4 185 ? 44.11928  93.77494  -4.18183  1.000 88.77067  ?  197 ARG B NH2 1 
ATOM   5675 N N   . TYR D 4 186 ? 41.77813  87.71562  -0.99672  1.000 57.67936  ?  198 TYR B N   1 
ATOM   5676 C CA  . TYR D 4 186 ? 40.99118  87.48459  0.20361   1.000 62.24704  ?  198 TYR B CA  1 
ATOM   5677 C C   . TYR D 4 186 ? 40.60900  88.79665  0.87668   1.000 64.85145  ?  198 TYR B C   1 
ATOM   5678 O O   . TYR D 4 186 ? 41.16648  89.86008  0.59137   1.000 75.80365  ?  198 TYR B O   1 
ATOM   5679 C CB  . TYR D 4 186 ? 41.75585  86.59482  1.18940   1.000 66.23455  ?  198 TYR B CB  1 
ATOM   5680 C CG  . TYR D 4 186 ? 42.01801  85.20294  0.66413   1.000 71.05180  ?  198 TYR B CG  1 
ATOM   5681 C CD1 . TYR D 4 186 ? 41.09107  84.18548  0.84948   1.000 69.63388  ?  198 TYR B CD1 1 
ATOM   5682 C CD2 . TYR D 4 186 ? 43.18817  84.90676  -0.02259  1.000 66.40216  ?  198 TYR B CD2 1 
ATOM   5683 C CE1 . TYR D 4 186 ? 41.32314  82.91121  0.36949   1.000 74.52269  ?  198 TYR B CE1 1 
ATOM   5684 C CE2 . TYR D 4 186 ? 43.42938  83.63439  -0.50594  1.000 71.87245  ?  198 TYR B CE2 1 
ATOM   5685 C CZ  . TYR D 4 186 ? 42.49285  82.64145  -0.30705  1.000 71.24469  ?  198 TYR B CZ  1 
ATOM   5686 O OH  . TYR D 4 186 ? 42.72574  81.37380  -0.78593  1.000 94.29884  ?  198 TYR B OH  1 
ATOM   5687 N N   . ALA D 4 187 ? 39.63482  88.69910  1.78007   1.000 62.93570  ?  199 ALA B N   1 
ATOM   5688 C CA  . ALA D 4 187 ? 39.17241  89.82515  2.57565   1.000 63.19724  ?  199 ALA B CA  1 
ATOM   5689 C C   . ALA D 4 187 ? 38.92126  89.35300  4.00004   1.000 70.58129  ?  199 ALA B C   1 
ATOM   5690 O O   . ALA D 4 187 ? 38.56322  88.19528  4.23071   1.000 78.38069  ?  199 ALA B O   1 
ATOM   5691 C CB  . ALA D 4 187 ? 37.89856  90.44880  1.99216   1.000 63.38404  ?  199 ALA B CB  1 
ATOM   5692 N N   . LEU D 4 188 ? 39.11071  90.26096  4.95541   1.000 70.22301  ?  200 LEU B N   1 
ATOM   5693 C CA  . LEU D 4 188 ? 38.97856  89.92531  6.36587   1.000 56.97600  ?  200 LEU B CA  1 
ATOM   5694 C C   . LEU D 4 188 ? 38.40266  91.11719  7.11570   1.000 64.48404  ?  200 LEU B C   1 
ATOM   5695 O O   . LEU D 4 188 ? 38.78420  92.26238  6.85992   1.000 82.28543  ?  200 LEU B O   1 
ATOM   5696 C CB  . LEU D 4 188 ? 40.33001  89.52122  6.96676   1.000 60.68413  ?  200 LEU B CB  1 
ATOM   5697 C CG  . LEU D 4 188 ? 40.33405  89.03246  8.41581   1.000 71.29295  ?  200 LEU B CG  1 
ATOM   5698 C CD1 . LEU D 4 188 ? 39.51003  87.76333  8.55470   1.000 77.21376  ?  200 LEU B CD1 1 
ATOM   5699 C CD2 . LEU D 4 188 ? 41.75825  88.80557  8.90000   1.000 71.17307  ?  200 LEU B CD2 1 
ATOM   5700 N N   . SER D 4 189 ? 37.48946  90.84002  8.04165   1.000 61.65420  ?  201 SER B N   1 
ATOM   5701 C CA  . SER D 4 189 ? 36.83943  91.86580  8.84285   1.000 73.65588  ?  201 SER B CA  1 
ATOM   5702 C C   . SER D 4 189 ? 37.07665  91.59863  10.32403  1.000 78.30528  ?  201 SER B C   1 
ATOM   5703 O O   . SER D 4 189 ? 37.49662  90.51106  10.72743  1.000 72.17323  ?  201 SER B O   1 
ATOM   5704 C CB  . SER D 4 189 ? 35.33438  91.92646  8.55066   1.000 76.66815  ?  201 SER B CB  1 
ATOM   5705 O OG  . SER D 4 189 ? 34.68178  90.74603  8.98463   1.000 86.75003  ?  201 SER B OG  1 
ATOM   5706 N N   . SER D 4 190 ? 36.79744  92.61451  11.13741  1.000 87.80128  ?  202 SER B N   1 
ATOM   5707 C CA  . SER D 4 190 ? 36.95307  92.50610  12.58089  1.000 80.44858  ?  202 SER B CA  1 
ATOM   5708 C C   . SER D 4 190 ? 36.03792  93.52045  13.24885  1.000 89.03828  ?  202 SER B C   1 
ATOM   5709 O O   . SER D 4 190 ? 35.63207  94.51376  12.63995  1.000 87.44280  ?  202 SER B O   1 
ATOM   5710 C CB  . SER D 4 190 ? 38.40740  92.72277  13.00892  1.000 79.53693  ?  202 SER B CB  1 
ATOM   5711 O OG  . SER D 4 190 ? 38.55673  92.55051  14.40712  1.000 83.26439  ?  202 SER B OG  1 
ATOM   5712 N N   . ARG D 4 191 ? 35.71979  93.25591  14.51480  1.000 82.71475  ?  203 ARG B N   1 
ATOM   5713 C CA  . ARG D 4 191 ? 34.77966  94.06899  15.27161  1.000 87.47667  ?  203 ARG B CA  1 
ATOM   5714 C C   . ARG D 4 191 ? 35.35680  94.39444  16.64256  1.000 85.50975  ?  203 ARG B C   1 
ATOM   5715 O O   . ARG D 4 191 ? 36.14672  93.62705  17.20041  1.000 83.30639  ?  203 ARG B O   1 
ATOM   5716 C CB  . ARG D 4 191 ? 33.43185  93.35238  15.43426  1.000 83.35884  ?  203 ARG B CB  1 
ATOM   5717 C CG  . ARG D 4 191 ? 32.86646  92.78984  14.13959  1.000 88.13299  ?  203 ARG B CG  1 
ATOM   5718 C CD  . ARG D 4 191 ? 32.25708  91.41803  14.36571  1.000 89.72488  ?  203 ARG B CD  1 
ATOM   5719 N NE  . ARG D 4 191 ? 31.77007  90.81584  13.13033  1.000 92.72972  ?  203 ARG B NE  1 
ATOM   5720 C CZ  . ARG D 4 191 ? 32.47932  89.99806  12.36423  1.000 88.51125  ?  203 ARG B CZ  1 
ATOM   5721 N NH1 . ARG D 4 191 ? 33.72285  89.66736  12.67149  1.000 95.79799  ?  203 ARG B NH1 1 
ATOM   5722 N NH2 . ARG D 4 191 ? 31.92602  89.49732  11.26333  1.000 94.13003  ?  203 ARG B NH2 1 
ATOM   5723 N N   . LEU D 4 192 ? 34.94895  95.54269  17.18236  1.000 84.10464  ?  204 LEU B N   1 
ATOM   5724 C CA  . LEU D 4 192 ? 35.35170  95.96833  18.51846  1.000 84.94456  ?  204 LEU B CA  1 
ATOM   5725 C C   . LEU D 4 192 ? 34.16280  96.63116  19.19594  1.000 98.62723  ?  204 LEU B C   1 
ATOM   5726 O O   . LEU D 4 192 ? 33.70419  97.68846  18.75217  1.000 98.99584  ?  204 LEU B O   1 
ATOM   5727 C CB  . LEU D 4 192 ? 36.54337  96.92842  18.46650  1.000 87.81052  ?  204 LEU B CB  1 
ATOM   5728 C CG  . LEU D 4 192 ? 36.88531  97.63509  19.78229  1.000 94.17594  ?  204 LEU B CG  1 
ATOM   5729 C CD1 . LEU D 4 192 ? 37.20867  96.63238  20.87961  1.000 90.04844  ?  204 LEU B CD1 1 
ATOM   5730 C CD2 . LEU D 4 192 ? 38.03531  98.61022  19.59036  1.000 102.97929 ?  204 LEU B CD2 1 
ATOM   5731 N N   . ARG D 4 193 ? 33.67111  96.01673  20.26912  1.000 101.54371 ?  205 ARG B N   1 
ATOM   5732 C CA  . ARG D 4 193 ? 32.54475  96.54229  21.02958  1.000 99.87679  ?  205 ARG B CA  1 
ATOM   5733 C C   . ARG D 4 193 ? 33.04664  97.25565  22.27752  1.000 103.01511 ?  205 ARG B C   1 
ATOM   5734 O O   . ARG D 4 193 ? 33.78944  96.67414  23.07553  1.000 99.48921  ?  205 ARG B O   1 
ATOM   5735 C CB  . ARG D 4 193 ? 31.57783  95.42596  21.42508  1.000 99.47267  ?  205 ARG B CB  1 
ATOM   5736 C CG  . ARG D 4 193 ? 30.57966  95.84835  22.49193  1.000 101.24294 ?  205 ARG B CG  1 
ATOM   5737 C CD  . ARG D 4 193 ? 29.75629  94.67519  22.98844  1.000 107.48840 ?  205 ARG B CD  1 
ATOM   5738 N NE  . ARG D 4 193 ? 28.82570  94.19244  21.97624  1.000 115.94240 ?  205 ARG B NE  1 
ATOM   5739 C CZ  . ARG D 4 193 ? 27.97797  93.18962  22.15824  1.000 112.83336 ?  205 ARG B CZ  1 
ATOM   5740 N NH1 . ARG D 4 193 ? 27.92213  92.53119  23.30464  1.000 90.34542  ?  205 ARG B NH1 1 
ATOM   5741 N NH2 . ARG D 4 193 ? 27.16523  92.83936  21.16571  1.000 118.98278 ?  205 ARG B NH2 1 
ATOM   5742 N N   . VAL D 4 194 ? 32.63687  98.51308  22.44161  1.000 103.87234 ?  206 VAL B N   1 
ATOM   5743 C CA  . VAL D 4 194 ? 32.93656  99.29796  23.63011  1.000 102.20337 ?  206 VAL B CA  1 
ATOM   5744 C C   . VAL D 4 194 ? 31.64588  99.94369  24.11548  1.000 104.02897 ?  206 VAL B C   1 
ATOM   5745 O O   . VAL D 4 194 ? 30.63464  99.97097  23.41343  1.000 110.05639 ?  206 VAL B O   1 
ATOM   5746 C CB  . VAL D 4 194 ? 34.01161  100.37473 23.37698  1.000 101.54232 ?  206 VAL B CB  1 
ATOM   5747 C CG1 . VAL D 4 194 ? 35.33574  99.73207  23.00264  1.000 102.07109 ?  206 VAL B CG1 1 
ATOM   5748 C CG2 . VAL D 4 194 ? 33.54796  101.34002 22.30016  1.000 100.39577 ?  206 VAL B CG2 1 
ATOM   5749 N N   . SER D 4 195 ? 31.69084  100.46441 25.33843  1.000 106.59439 ?  207 SER B N   1 
ATOM   5750 C CA  . SER D 4 195 ? 30.53743  101.17206 25.86571  1.000 109.49662 ?  207 SER B CA  1 
ATOM   5751 C C   . SER D 4 195 ? 30.36960  102.50670 25.14811  1.000 110.51951 ?  207 SER B C   1 
ATOM   5752 O O   . SER D 4 195 ? 31.31606  103.06754 24.58783  1.000 114.81536 ?  207 SER B O   1 
ATOM   5753 C CB  . SER D 4 195 ? 30.67156  101.39244 27.37451  1.000 119.08998 ?  207 SER B CB  1 
ATOM   5754 O OG  . SER D 4 195 ? 31.55725  102.45928 27.66871  1.000 124.89519 ?  207 SER B OG  1 
ATOM   5755 N N   . ALA D 4 196 ? 29.13177  103.00509 25.15878  1.000 116.64041 ?  208 ALA B N   1 
ATOM   5756 C CA  . ALA D 4 196 ? 28.84584  104.29188 24.53498  1.000 124.69594 ?  208 ALA B CA  1 
ATOM   5757 C C   . ALA D 4 196 ? 29.67174  105.40708 25.16401  1.000 128.94500 ?  208 ALA B C   1 
ATOM   5758 O O   . ALA D 4 196 ? 30.15019  106.30608 24.46263  1.000 127.85489 ?  208 ALA B O   1 
ATOM   5759 C CB  . ALA D 4 196 ? 27.35458  104.60192 24.64152  1.000 132.56270 ?  208 ALA B CB  1 
ATOM   5760 N N   . THR D 4 197 ? 29.85025  105.36552 26.48786  1.000 127.89892 ?  209 THR B N   1 
ATOM   5761 C CA  . THR D 4 197 ? 30.65902  106.37745 27.15997  1.000 132.30868 ?  209 THR B CA  1 
ATOM   5762 C C   . THR D 4 197 ? 32.12330  106.28948 26.74683  1.000 136.24877 ?  209 THR B C   1 
ATOM   5763 O O   . THR D 4 197 ? 32.81231  107.31469 26.68502  1.000 142.74179 ?  209 THR B O   1 
ATOM   5764 C CB  . THR D 4 197 ? 30.52828  106.23475 28.67707  1.000 132.62289 ?  209 THR B CB  1 
ATOM   5765 O OG1 . THR D 4 197 ? 31.06454  104.97069 29.08592  1.000 130.20495 ?  209 THR B OG1 1 
ATOM   5766 C CG2 . THR D 4 197 ? 29.06659  106.31573 29.09714  1.000 133.97725 ?  209 THR B CG2 1 
ATOM   5767 N N   . PHE D 4 198 ? 32.61482  105.08111 26.46352  1.000 134.02797 ?  210 PHE B N   1 
ATOM   5768 C CA  . PHE D 4 198 ? 33.99091  104.92981 26.00096  1.000 125.07759 ?  210 PHE B CA  1 
ATOM   5769 C C   . PHE D 4 198 ? 34.17428  105.58099 24.63470  1.000 128.33850 ?  210 PHE B C   1 
ATOM   5770 O O   . PHE D 4 198 ? 35.11918  106.34963 24.42118  1.000 137.02032 ?  210 PHE B O   1 
ATOM   5771 C CB  . PHE D 4 198 ? 34.36415  103.44427 25.95733  1.000 118.41571 ?  210 PHE B CB  1 
ATOM   5772 C CG  . PHE D 4 198 ? 35.84748  103.17008 26.07469  1.000 136.03277 ?  210 PHE B CG  1 
ATOM   5773 C CD1 . PHE D 4 198 ? 36.78905  104.09461 25.64682  1.000 146.10216 ?  210 PHE B CD1 1 
ATOM   5774 C CD2 . PHE D 4 198 ? 36.29575  101.97505 26.61438  1.000 138.34455 ?  210 PHE B CD2 1 
ATOM   5775 C CE1 . PHE D 4 198 ? 38.14445  103.83276 25.75474  1.000 142.30816 ?  210 PHE B CE1 1 
ATOM   5776 C CE2 . PHE D 4 198 ? 37.64996  101.70792 26.72592  1.000 139.55492 ?  210 PHE B CE2 1 
ATOM   5777 C CZ  . PHE D 4 198 ? 38.57476  102.63823 26.29540  1.000 138.12965 ?  210 PHE B CZ  1 
ATOM   5778 N N   . TRP D 4 199 ? 33.26664  105.29301 23.69779  1.000 118.20868 ?  211 TRP B N   1 
ATOM   5779 C CA  . TRP D 4 199 ? 33.37576  105.86162 22.35842  1.000 120.88181 ?  211 TRP B CA  1 
ATOM   5780 C C   . TRP D 4 199 ? 33.21313  107.37691 22.36827  1.000 129.34224 ?  211 TRP B C   1 
ATOM   5781 O O   . TRP D 4 199 ? 33.83614  108.07008 21.55626  1.000 132.61658 ?  211 TRP B O   1 
ATOM   5782 C CB  . TRP D 4 199 ? 32.34097  105.22391 21.43249  1.000 126.40528 ?  211 TRP B CB  1 
ATOM   5783 C CG  . TRP D 4 199 ? 32.20298  105.92992 20.12344  1.000 124.35796 ?  211 TRP B CG  1 
ATOM   5784 C CD1 . TRP D 4 199 ? 31.15270  106.69710 19.71323  1.000 126.49734 ?  211 TRP B CD1 1 
ATOM   5785 C CD2 . TRP D 4 199 ? 33.15710  105.95090 19.05584  1.000 124.60453 ?  211 TRP B CD2 1 
ATOM   5786 N NE1 . TRP D 4 199 ? 31.38923  107.18773 18.45215  1.000 135.12894 ?  211 TRP B NE1 1 
ATOM   5787 C CE2 . TRP D 4 199 ? 32.61396  106.74462 18.02663  1.000 128.77499 ?  211 TRP B CE2 1 
ATOM   5788 C CE3 . TRP D 4 199 ? 34.41640  105.37258 18.86890  1.000 122.10414 ?  211 TRP B CE3 1 
ATOM   5789 C CZ2 . TRP D 4 199 ? 33.28612  106.97507 16.82868  1.000 124.02967 ?  211 TRP B CZ2 1 
ATOM   5790 C CZ3 . TRP D 4 199 ? 35.08206  105.60228 17.67875  1.000 117.63798 ?  211 TRP B CZ3 1 
ATOM   5791 C CH2 . TRP D 4 199 ? 34.51591  106.39638 16.67433  1.000 120.03364 ?  211 TRP B CH2 1 
ATOM   5792 N N   . GLN D 4 200 ? 32.39635  107.90897 23.27501  1.000 122.50804 ?  212 GLN B N   1 
ATOM   5793 C CA  . GLN D 4 200 ? 32.17356  109.34608 23.37093  1.000 128.21345 ?  212 GLN B CA  1 
ATOM   5794 C C   . GLN D 4 200 ? 33.33060  110.08707 24.03157  1.000 140.90962 ?  212 GLN B C   1 
ATOM   5795 O O   . GLN D 4 200 ? 33.20396  111.28736 24.29739  1.000 154.61907 ?  212 GLN B O   1 
ATOM   5796 C CB  . GLN D 4 200 ? 30.87568  109.62619 24.13304  1.000 131.09760 ?  212 GLN B CB  1 
ATOM   5797 C CG  . GLN D 4 200 ? 29.61789  109.22005 23.38041  1.000 130.95290 ?  212 GLN B CG  1 
ATOM   5798 C CD  . GLN D 4 200 ? 28.35952  109.36591 24.21486  1.000 130.21054 ?  212 GLN B CD  1 
ATOM   5799 O OE1 . GLN D 4 200 ? 28.39144  109.90280 25.32278  1.000 137.09269 ?  212 GLN B OE1 1 
ATOM   5800 N NE2 . GLN D 4 200 ? 27.24106  108.88384 23.68477  1.000 127.18003 ?  212 GLN B NE2 1 
ATOM   5801 N N   . ASN D 4 201 ? 34.44286  109.40505 24.30580  1.000 150.99322 ?  213 ASN B N   1 
ATOM   5802 C CA  . ASN D 4 201 ? 35.61691  110.04392 24.87738  1.000 150.67586 ?  213 ASN B CA  1 
ATOM   5803 C C   . ASN D 4 201 ? 36.65331  110.24288 23.78352  1.000 153.39640 ?  213 ASN B C   1 
ATOM   5804 O O   . ASN D 4 201 ? 37.28280  109.26237 23.35564  1.000 156.00702 ?  213 ASN B O   1 
ATOM   5805 C CB  . ASN D 4 201 ? 36.19372  109.19897 26.01040  1.000 148.42711 ?  213 ASN B CB  1 
ATOM   5806 C CG  . ASN D 4 201 ? 37.39456  109.84644 26.66327  1.000 151.76014 ?  213 ASN B CG  1 
ATOM   5807 O OD1 . ASN D 4 201 ? 37.56876  111.06305 26.59836  1.000 154.84733 ?  213 ASN B OD1 1 
ATOM   5808 N ND2 . ASN D 4 201 ? 38.23306  109.03578 27.29588  1.000 157.16155 ?  213 ASN B ND2 1 
ATOM   5809 N N   . PRO D 4 202 ? 36.86356  111.46919 23.29493  1.000 153.05987 ?  214 PRO B N   1 
ATOM   5810 C CA  . PRO D 4 202 ? 37.86020  111.68299 22.23248  1.000 160.40982 ?  214 PRO B CA  1 
ATOM   5811 C C   . PRO D 4 202 ? 39.29319  111.41358 22.66440  1.000 156.30248 ?  214 PRO B C   1 
ATOM   5812 O O   . PRO D 4 202 ? 40.17650  111.35736 21.79870  1.000 153.88996 ?  214 PRO B O   1 
ATOM   5813 C CB  . PRO D 4 202 ? 37.66687  113.16050 21.86084  1.000 160.93157 ?  214 PRO B CB  1 
ATOM   5814 C CG  . PRO D 4 202 ? 36.29658  113.51272 22.36429  1.000 154.85400 ?  214 PRO B CG  1 
ATOM   5815 C CD  . PRO D 4 202 ? 36.10618  112.69314 23.59968  1.000 152.23912 ?  214 PRO B CD  1 
ATOM   5816 N N   . ARG D 4 203 ? 39.55572  111.24818 23.96313  1.000 148.83972 ?  215 ARG B N   1 
ATOM   5817 C CA  . ARG D 4 203 ? 40.91496  110.98377 24.41949  1.000 147.48227 ?  215 ARG B CA  1 
ATOM   5818 C C   . ARG D 4 203 ? 41.37934  109.57452 24.07662  1.000 160.18490 ?  215 ARG B C   1 
ATOM   5819 O O   . ARG D 4 203 ? 42.58408  109.30433 24.12608  1.000 164.31145 ?  215 ARG B O   1 
ATOM   5820 C CB  . ARG D 4 203 ? 41.01793  111.21107 25.92862  1.000 153.47914 ?  215 ARG B CB  1 
ATOM   5821 N N   . ASN D 4 204 ? 40.46001  108.67694 23.73220  1.000 155.28273 ?  216 ASN B N   1 
ATOM   5822 C CA  . ASN D 4 204 ? 40.80655  107.30532 23.39064  1.000 153.99488 ?  216 ASN B CA  1 
ATOM   5823 C C   . ASN D 4 204 ? 41.16272  107.20110 21.91365  1.000 160.46274 ?  216 ASN B C   1 
ATOM   5824 O O   . ASN D 4 204 ? 40.47612  107.76098 21.05398  1.000 155.27563 ?  216 ASN B O   1 
ATOM   5825 C CB  . ASN D 4 204 ? 39.65000  106.35984 23.71864  1.000 152.12988 ?  216 ASN B CB  1 
ATOM   5826 N N   . HIS D 4 205 ? 42.24084  106.47725 21.62645  1.000 156.68993 ?  217 HIS B N   1 
ATOM   5827 C CA  . HIS D 4 205 ? 42.73750  106.29369 20.26864  1.000 139.80613 ?  217 HIS B CA  1 
ATOM   5828 C C   . HIS D 4 205 ? 42.52035  104.84512 19.85347  1.000 139.78293 ?  217 HIS B C   1 
ATOM   5829 O O   . HIS D 4 205 ? 43.05879  103.92849 20.48328  1.000 140.13152 ?  217 HIS B O   1 
ATOM   5830 C CB  . HIS D 4 205 ? 44.21760  106.66464 20.17386  1.000 146.80101 ?  217 HIS B CB  1 
ATOM   5831 C CG  . HIS D 4 205 ? 44.79225  106.51199 18.80014  1.000 138.35914 ?  217 HIS B CG  1 
ATOM   5832 N ND1 . HIS D 4 205 ? 44.55094  107.41556 17.78780  1.000 147.19583 ?  217 HIS B ND1 1 
ATOM   5833 C CD2 . HIS D 4 205 ? 45.59575  105.55946 18.27044  1.000 134.31038 ?  217 HIS B CD2 1 
ATOM   5834 C CE1 . HIS D 4 205 ? 45.18263  107.02757 16.69439  1.000 140.87539 ?  217 HIS B CE1 1 
ATOM   5835 N NE2 . HIS D 4 205 ? 45.82354  105.90366 16.96015  1.000 138.81975 ?  217 HIS B NE2 1 
ATOM   5836 N N   . PHE D 4 206 ? 41.73609  104.64354 18.79909  1.000 141.09068 ?  218 PHE B N   1 
ATOM   5837 C CA  . PHE D 4 206 ? 41.46177  103.31769 18.26467  1.000 120.36070 ?  218 PHE B CA  1 
ATOM   5838 C C   . PHE D 4 206 ? 42.31511  103.07217 17.02754  1.000 119.69934 ?  218 PHE B C   1 
ATOM   5839 O O   . PHE D 4 206 ? 42.44556  103.94743 16.16670  1.000 126.22052 ?  218 PHE B O   1 
ATOM   5840 C CB  . PHE D 4 206 ? 39.97965  103.16310 17.91638  1.000 123.77280 ?  218 PHE B CB  1 
ATOM   5841 C CG  . PHE D 4 206 ? 39.05799  103.33497 19.09079  1.000 131.49464 ?  218 PHE B CG  1 
ATOM   5842 C CD1 . PHE D 4 206 ? 38.57164  104.58705 19.43011  1.000 138.01808 ?  218 PHE B CD1 1 
ATOM   5843 C CD2 . PHE D 4 206 ? 38.67469  102.24386 19.85309  1.000 131.98142 ?  218 PHE B CD2 1 
ATOM   5844 C CE1 . PHE D 4 206 ? 37.72288  104.74806 20.50950  1.000 139.44427 ?  218 PHE B CE1 1 
ATOM   5845 C CE2 . PHE D 4 206 ? 37.82567  102.39829 20.93356  1.000 127.94927 ?  218 PHE B CE2 1 
ATOM   5846 C CZ  . PHE D 4 206 ? 37.34941  103.65205 21.26187  1.000 130.10407 ?  218 PHE B CZ  1 
ATOM   5847 N N   . ARG D 4 207 ? 42.89459  101.87625 16.94339  1.000 119.19793 ?  219 ARG B N   1 
ATOM   5848 C CA  . ARG D 4 207 ? 43.76206  101.51481 15.83224  1.000 116.78546 ?  219 ARG B CA  1 
ATOM   5849 C C   . ARG D 4 207 ? 43.55309  100.05236 15.47210  1.000 112.15233 ?  219 ARG B C   1 
ATOM   5850 O O   . ARG D 4 207 ? 43.46267  99.19337  16.35374  1.000 104.28473 ?  219 ARG B O   1 
ATOM   5851 C CB  . ARG D 4 207 ? 45.23810  101.76428 16.16994  1.000 112.60909 ?  219 ARG B CB  1 
ATOM   5852 N N   . CYS D 4 208 ? 43.47902  99.77861  14.17152  1.000 117.64374 ?  220 CYS B N   1 
ATOM   5853 C CA  . CYS D 4 208 ? 43.32969  98.42635  13.64360  1.000 103.90306 ?  220 CYS B CA  1 
ATOM   5854 C C   . CYS D 4 208 ? 44.58809  98.08249  12.85660  1.000 100.60406 ?  220 CYS B C   1 
ATOM   5855 O O   . CYS D 4 208 ? 44.78669  98.58316  11.74484  1.000 101.87597 ?  220 CYS B O   1 
ATOM   5856 C CB  . CYS D 4 208 ? 42.08618  98.31504  12.76448  1.000 92.24599  ?  220 CYS B CB  1 
ATOM   5857 S SG  . CYS D 4 208 ? 41.90265  96.71906  11.93563  1.000 104.14738 ?  220 CYS B SG  1 
ATOM   5858 N N   . GLN D 4 209 ? 45.43118  97.22943  13.42994  1.000 102.21790 ?  221 GLN B N   1 
ATOM   5859 C CA  . GLN D 4 209 ? 46.69047  96.83418  12.81384  1.000 95.48032  ?  221 GLN B CA  1 
ATOM   5860 C C   . GLN D 4 209 ? 46.51687  95.50710  12.08733  1.000 96.16691  ?  221 GLN B C   1 
ATOM   5861 O O   . GLN D 4 209 ? 45.93992  94.56298  12.63721  1.000 101.99272 ?  221 GLN B O   1 
ATOM   5862 C CB  . GLN D 4 209 ? 47.79639  96.72200  13.86426  1.000 107.10183 ?  221 GLN B CB  1 
ATOM   5863 C CG  . GLN D 4 209 ? 49.12454  96.22706  13.31891  1.000 100.20031 ?  221 GLN B CG  1 
ATOM   5864 C CD  . GLN D 4 209 ? 50.21085  96.19557  14.37449  1.000 108.58190 ?  221 GLN B CD  1 
ATOM   5865 O OE1 . GLN D 4 209 ? 50.06209  96.77154  15.45216  1.000 108.30778 ?  221 GLN B OE1 1 
ATOM   5866 N NE2 . GLN D 4 209 ? 51.31186  95.51860  14.07038  1.000 125.36064 ?  221 GLN B NE2 1 
ATOM   5867 N N   . VAL D 4 210 ? 47.01572  95.44061  10.85505  1.000 96.57642  ?  222 VAL B N   1 
ATOM   5868 C CA  . VAL D 4 210 ? 46.96273  94.23391  10.03626  1.000 87.12194  ?  222 VAL B CA  1 
ATOM   5869 C C   . VAL D 4 210 ? 48.37526  93.94815  9.54627   1.000 93.55155  ?  222 VAL B C   1 
ATOM   5870 O O   . VAL D 4 210 ? 48.92495  94.71247  8.74315   1.000 97.91202  ?  222 VAL B O   1 
ATOM   5871 C CB  . VAL D 4 210 ? 45.99325  94.37121  8.85457   1.000 88.76729  ?  222 VAL B CB  1 
ATOM   5872 C CG1 . VAL D 4 210 ? 46.10814  93.16592  7.93320   1.000 68.30572  ?  222 VAL B CG1 1 
ATOM   5873 C CG2 . VAL D 4 210 ? 44.56648  94.52649  9.35653   1.000 93.51945  ?  222 VAL B CG2 1 
ATOM   5874 N N   . GLN D 4 211 ? 48.96155  92.85442  10.02534  1.000 92.19687  ?  223 GLN B N   1 
ATOM   5875 C CA  . GLN D 4 211 ? 50.30137  92.44536  9.62421   1.000 91.90558  ?  223 GLN B CA  1 
ATOM   5876 C C   . GLN D 4 211 ? 50.20205  91.51911  8.41827   1.000 95.09289  ?  223 GLN B C   1 
ATOM   5877 O O   . GLN D 4 211 ? 49.63081  90.42796  8.51456   1.000 97.65702  ?  223 GLN B O   1 
ATOM   5878 C CB  . GLN D 4 211 ? 51.01993  91.74916  10.77902  1.000 109.41588 ?  223 GLN B CB  1 
ATOM   5879 C CG  . GLN D 4 211 ? 52.39079  91.20065  10.41896  1.000 116.48899 ?  223 GLN B CG  1 
ATOM   5880 C CD  . GLN D 4 211 ? 53.41213  92.29342  10.17904  1.000 115.54456 ?  223 GLN B CD  1 
ATOM   5881 O OE1 . GLN D 4 211 ? 53.81900  92.99148  11.10729  1.000 120.90808 ?  223 GLN B OE1 1 
ATOM   5882 N NE2 . GLN D 4 211 ? 53.83189  92.44838  8.92861   1.000 113.30151 ?  223 GLN B NE2 1 
ATOM   5883 N N   . PHE D 4 212 ? 50.75778  91.95068  7.28998   1.000 96.09118  ?  224 PHE B N   1 
ATOM   5884 C CA  . PHE D 4 212 ? 50.72643  91.18651  6.05015   1.000 90.04147  ?  224 PHE B CA  1 
ATOM   5885 C C   . PHE D 4 212 ? 52.11346  90.63767  5.74969   1.000 96.15286  ?  224 PHE B C   1 
ATOM   5886 O O   . PHE D 4 212 ? 53.09744  91.38481  5.76031   1.000 100.69496 ?  224 PHE B O   1 
ATOM   5887 C CB  . PHE D 4 212 ? 50.23673  92.05013  4.88607   1.000 92.25527  ?  224 PHE B CB  1 
ATOM   5888 C CG  . PHE D 4 212 ? 50.39150  91.39945  3.54001   1.000 89.02691  ?  224 PHE B CG  1 
ATOM   5889 C CD1 . PHE D 4 212 ? 49.60663  90.31556  3.18420   1.000 90.75791  ?  224 PHE B CD1 1 
ATOM   5890 C CD2 . PHE D 4 212 ? 51.31664  91.87771  2.62724   1.000 94.47870  ?  224 PHE B CD2 1 
ATOM   5891 C CE1 . PHE D 4 212 ? 49.74551  89.71594  1.94643   1.000 83.16709  ?  224 PHE B CE1 1 
ATOM   5892 C CE2 . PHE D 4 212 ? 51.45937  91.28352  1.38716   1.000 101.72768 ?  224 PHE B CE2 1 
ATOM   5893 C CZ  . PHE D 4 212 ? 50.67290  90.20093  1.04679   1.000 87.97636  ?  224 PHE B CZ  1 
ATOM   5894 N N   . TYR D 4 213 ? 52.18563  89.33596  5.48134   1.000 94.15488  ?  225 TYR B N   1 
ATOM   5895 C CA  . TYR D 4 213 ? 53.43471  88.66504  5.13961   1.000 95.79162  ?  225 TYR B CA  1 
ATOM   5896 C C   . TYR D 4 213 ? 53.44963  88.42645  3.63390   1.000 98.02363  ?  225 TYR B C   1 
ATOM   5897 O O   . TYR D 4 213 ? 52.75797  87.53406  3.13224   1.000 89.86619  ?  225 TYR B O   1 
ATOM   5898 C CB  . TYR D 4 213 ? 53.57823  87.35414  5.90996   1.000 94.93122  ?  225 TYR B CB  1 
ATOM   5899 C CG  . TYR D 4 213 ? 53.65373  87.52804  7.41063   1.000 100.30068 ?  225 TYR B CG  1 
ATOM   5900 C CD1 . TYR D 4 213 ? 52.50308  87.53094  8.18808   1.000 96.82919  ?  225 TYR B CD1 1 
ATOM   5901 C CD2 . TYR D 4 213 ? 54.87635  87.68752  8.04985   1.000 95.30633  ?  225 TYR B CD2 1 
ATOM   5902 C CE1 . TYR D 4 213 ? 52.56772  87.68853  9.55998   1.000 106.21638 ?  225 TYR B CE1 1 
ATOM   5903 C CE2 . TYR D 4 213 ? 54.95121  87.84601  9.42109   1.000 90.94414  ?  225 TYR B CE2 1 
ATOM   5904 C CZ  . TYR D 4 213 ? 53.79429  87.84585  10.17090  1.000 96.70752  ?  225 TYR B CZ  1 
ATOM   5905 O OH  . TYR D 4 213 ? 53.86418  88.00343  11.53605  1.000 94.81498  ?  225 TYR B OH  1 
ATOM   5906 N N   . GLY D 4 214 ? 54.23551  89.22416  2.91612   1.000 107.99767 ?  226 GLY B N   1 
ATOM   5907 C CA  . GLY D 4 214 ? 54.28009  89.12622  1.47131   1.000 112.80416 ?  226 GLY B CA  1 
ATOM   5908 C C   . GLY D 4 214 ? 55.64193  88.76138  0.92002   1.000 113.03575 ?  226 GLY B C   1 
ATOM   5909 O O   . GLY D 4 214 ? 56.16627  87.67879  1.19922   1.000 107.72568 ?  226 GLY B O   1 
ATOM   5910 N N   . LEU D 4 215 ? 56.22307  89.66027  0.13435   1.000 110.80607 ?  227 LEU B N   1 
ATOM   5911 C CA  . LEU D 4 215 ? 57.49119  89.41925  -0.53443  1.000 111.24919 ?  227 LEU B CA  1 
ATOM   5912 C C   . LEU D 4 215 ? 58.64699  90.01954  0.25635   1.000 120.77763 ?  227 LEU B C   1 
ATOM   5913 O O   . LEU D 4 215 ? 58.46639  90.89018  1.11104   1.000 120.34211 ?  227 LEU B O   1 
ATOM   5914 C CB  . LEU D 4 215 ? 57.47326  90.00092  -1.95087  1.000 96.17849  ?  227 LEU B CB  1 
ATOM   5915 C CG  . LEU D 4 215 ? 56.42010  89.44036  -2.90753  1.000 95.90807  ?  227 LEU B CG  1 
ATOM   5916 C CD1 . LEU D 4 215 ? 56.51736  90.11422  -4.26758  1.000 94.39694  ?  227 LEU B CD1 1 
ATOM   5917 C CD2 . LEU D 4 215 ? 56.56648  87.93348  -3.04132  1.000 91.79214  ?  227 LEU B CD2 1 
ATOM   5918 N N   . SER D 4 216 ? 59.84619  89.53488  -0.04449  1.000 120.70413 ?  228 SER B N   1 
ATOM   5919 C CA  . SER D 4 216 ? 61.08164  90.04772  0.52511   1.000 115.92018 ?  228 SER B CA  1 
ATOM   5920 C C   . SER D 4 216 ? 61.86191  90.80837  -0.53973  1.000 124.65792 ?  228 SER B C   1 
ATOM   5921 O O   . SER D 4 216 ? 61.50448  90.82049  -1.72107  1.000 125.89422 ?  228 SER B O   1 
ATOM   5922 C CB  . SER D 4 216 ? 61.93045  88.90889  1.10158   1.000 111.26513 ?  228 SER B CB  1 
ATOM   5923 N N   . GLU D 4 217 ? 62.94477  91.45002  -0.10509  1.000 118.48782 ?  229 GLU B N   1 
ATOM   5924 C CA  . GLU D 4 217 ? 63.80215  92.20109  -1.01264  1.000 120.52455 ?  229 GLU B CA  1 
ATOM   5925 C C   . GLU D 4 217 ? 64.67902  91.30508  -1.87712  1.000 124.67615 ?  229 GLU B C   1 
ATOM   5926 O O   . GLU D 4 217 ? 65.38357  91.81660  -2.75485  1.000 120.58099 ?  229 GLU B O   1 
ATOM   5927 C CB  . GLU D 4 217 ? 64.68042  93.17370  -0.22313  1.000 108.51113 ?  229 GLU B CB  1 
ATOM   5928 N N   . ASN D 4 218 ? 64.65790  89.99277  -1.64984  1.000 120.36401 ?  230 ASN B N   1 
ATOM   5929 C CA  . ASN D 4 218 ? 65.39506  89.04478  -2.47371  1.000 122.16182 ?  230 ASN B CA  1 
ATOM   5930 C C   . ASN D 4 218 ? 64.64852  88.66449  -3.74473  1.000 118.15363 ?  230 ASN B C   1 
ATOM   5931 O O   . ASN D 4 218 ? 65.20697  87.94500  -4.58005  1.000 101.98229 ?  230 ASN B O   1 
ATOM   5932 C CB  . ASN D 4 218 ? 65.70126  87.77986  -1.66728  1.000 122.04254 ?  230 ASN B CB  1 
ATOM   5933 C CG  . ASN D 4 218 ? 66.21650  88.08593  -0.27608  1.000 116.63211 ?  230 ASN B CG  1 
ATOM   5934 O OD1 . ASN D 4 218 ? 67.05512  88.96825  -0.09144  1.000 119.74953 ?  230 ASN B OD1 1 
ATOM   5935 N ND2 . ASN D 4 218 ? 65.70945  87.36209  0.71362   1.000 123.61224 ?  230 ASN B ND2 1 
ATOM   5936 N N   . ASP D 4 219 ? 63.41230  89.12568  -3.90993  1.000 123.30068 ?  231 ASP B N   1 
ATOM   5937 C CA  . ASP D 4 219 ? 62.57049  88.74683  -5.03581  1.000 129.92258 ?  231 ASP B CA  1 
ATOM   5938 C C   . ASP D 4 219 ? 62.60413  89.83900  -6.09643  1.000 132.19208 ?  231 ASP B C   1 
ATOM   5939 O O   . ASP D 4 219 ? 62.46912  91.02522  -5.77793  1.000 126.77817 ?  231 ASP B O   1 
ATOM   5940 C CB  . ASP D 4 219 ? 61.13330  88.50271  -4.57404  1.000 119.79108 ?  231 ASP B CB  1 
ATOM   5941 C CG  . ASP D 4 219 ? 61.06239  87.67860  -3.30276  1.000 119.91165 ?  231 ASP B CG  1 
ATOM   5942 O OD1 . ASP D 4 219 ? 61.93062  86.80147  -3.11079  1.000 120.18393 ?  231 ASP B OD1 1 
ATOM   5943 O OD2 . ASP D 4 219 ? 60.14147  87.91248  -2.49191  1.000 119.34546 -1 231 ASP B OD2 1 
ATOM   5944 N N   . GLU D 4 220 ? 62.78199  89.43550  -7.35217  1.000 133.95156 ?  232 GLU B N   1 
ATOM   5945 C CA  . GLU D 4 220 ? 62.80150  90.38032  -8.46014  1.000 122.35740 ?  232 GLU B CA  1 
ATOM   5946 C C   . GLU D 4 220 ? 61.38252  90.82951  -8.78477  1.000 131.92788 ?  232 GLU B C   1 
ATOM   5947 O O   . GLU D 4 220 ? 60.46761  90.00553  -8.88193  1.000 134.69834 ?  232 GLU B O   1 
ATOM   5948 C CB  . GLU D 4 220 ? 63.45412  89.74894  -9.68935  1.000 108.25326 ?  232 GLU B CB  1 
ATOM   5949 N N   . TRP D 4 221 ? 61.20153  92.13801  -8.95329  1.000 126.19566 ?  233 TRP B N   1 
ATOM   5950 C CA  . TRP D 4 221 ? 59.88760  92.71448  -9.21564  1.000 109.93047 ?  233 TRP B CA  1 
ATOM   5951 C C   . TRP D 4 221 ? 60.02091  93.76949  -10.30137 1.000 116.42859 ?  233 TRP B C   1 
ATOM   5952 O O   . TRP D 4 221 ? 60.73758  94.75871  -10.12168 1.000 119.45592 ?  233 TRP B O   1 
ATOM   5953 C CB  . TRP D 4 221 ? 59.28916  93.32333  -7.94390  1.000 107.97524 ?  233 TRP B CB  1 
ATOM   5954 C CG  . TRP D 4 221 ? 57.91776  93.89095  -8.13702  1.000 119.84299 ?  233 TRP B CG  1 
ATOM   5955 C CD1 . TRP D 4 221 ? 57.60030  95.18138  -8.44604  1.000 119.67276 ?  233 TRP B CD1 1 
ATOM   5956 C CD2 . TRP D 4 221 ? 56.67517  93.18563  -8.03435  1.000 110.69109 ?  233 TRP B CD2 1 
ATOM   5957 N NE1 . TRP D 4 221 ? 56.23729  95.32364  -8.54138  1.000 117.85491 ?  233 TRP B NE1 1 
ATOM   5958 C CE2 . TRP D 4 221 ? 55.64643  94.11265  -8.29320  1.000 110.58319 ?  233 TRP B CE2 1 
ATOM   5959 C CE3 . TRP D 4 221 ? 56.33285  91.86049  -7.74862  1.000 98.97916  ?  233 TRP B CE3 1 
ATOM   5960 C CZ2 . TRP D 4 221 ? 54.29956  93.75727  -8.27475  1.000 104.68264 ?  233 TRP B CZ2 1 
ATOM   5961 C CZ3 . TRP D 4 221 ? 54.99523  91.50982  -7.73083  1.000 99.40702  ?  233 TRP B CZ3 1 
ATOM   5962 C CH2 . TRP D 4 221 ? 53.99538  92.45411  -7.99275  1.000 103.22398 ?  233 TRP B CH2 1 
ATOM   5963 N N   . THR D 4 222 ? 59.33126  93.55736  -11.42641 1.000 120.33747 ?  234 THR B N   1 
ATOM   5964 C CA  . THR D 4 222 ? 59.33502  94.48864  -12.55465 1.000 121.64707 ?  234 THR B CA  1 
ATOM   5965 C C   . THR D 4 222 ? 57.88698  94.71542  -12.99898 1.000 114.87433 ?  234 THR B C   1 
ATOM   5966 O O   . THR D 4 222 ? 57.44812  94.20959  -14.03360 1.000 111.76974 ?  234 THR B O   1 
ATOM   5967 C CB  . THR D 4 222 ? 60.19800  93.96688  -13.70799 1.000 126.30745 ?  234 THR B CB  1 
ATOM   5968 O OG1 . THR D 4 222 ? 59.74709  92.66224  -14.09400 1.000 118.26129 ?  234 THR B OG1 1 
ATOM   5969 C CG2 . THR D 4 222 ? 61.66353  93.89628  -13.29837 1.000 120.12262 ?  234 THR B CG2 1 
ATOM   5970 N N   . GLN D 4 223 ? 57.14417  95.48296  -12.20500 1.000 120.67266 ?  235 GLN B N   1 
ATOM   5971 C CA  . GLN D 4 223 ? 55.75387  95.80051  -12.49423 1.000 121.87802 ?  235 GLN B CA  1 
ATOM   5972 C C   . GLN D 4 223 ? 55.51423  97.28821  -12.27390 1.000 127.68785 ?  235 GLN B C   1 
ATOM   5973 O O   . GLN D 4 223 ? 56.33076  97.99301  -11.67447 1.000 132.93331 ?  235 GLN B O   1 
ATOM   5974 C CB  . GLN D 4 223 ? 54.79568  94.96874  -11.62986 1.000 119.67956 ?  235 GLN B CB  1 
ATOM   5975 C CG  . GLN D 4 223 ? 54.81701  93.48043  -11.93916 1.000 115.66353 ?  235 GLN B CG  1 
ATOM   5976 C CD  . GLN D 4 223 ? 54.36175  93.17291  -13.35275 1.000 118.60151 ?  235 GLN B CD  1 
ATOM   5977 O OE1 . GLN D 4 223 ? 53.49628  93.85539  -13.90127 1.000 122.80223 ?  235 GLN B OE1 1 
ATOM   5978 N NE2 . GLN D 4 223 ? 54.94822  92.14345  -13.95239 1.000 123.58448 ?  235 GLN B NE2 1 
ATOM   5979 N N   . ASP D 4 224 ? 54.37023  97.76285  -12.76861 1.000 127.45366 ?  236 ASP B N   1 
ATOM   5980 C CA  . ASP D 4 224 ? 54.02661  99.17629  -12.68394 1.000 125.50918 ?  236 ASP B CA  1 
ATOM   5981 C C   . ASP D 4 224 ? 53.46612  99.57797  -11.32588 1.000 117.66069 ?  236 ASP B C   1 
ATOM   5982 O O   . ASP D 4 224 ? 53.29836  100.77674 -11.07653 1.000 119.75682 ?  236 ASP B O   1 
ATOM   5983 C CB  . ASP D 4 224 ? 53.01885  99.53770  -13.77842 1.000 103.69738 ?  236 ASP B CB  1 
ATOM   5984 N N   . ARG D 4 225 ? 53.17314  98.62234  -10.45084 1.000 108.87673 ?  237 ARG B N   1 
ATOM   5985 C CA  . ARG D 4 225 ? 52.64560  98.90680  -9.12520  1.000 107.03925 ?  237 ARG B CA  1 
ATOM   5986 C C   . ARG D 4 225 ? 53.70188  98.61813  -8.06548  1.000 101.60938 ?  237 ARG B C   1 
ATOM   5987 O O   . ARG D 4 225 ? 54.76421  98.05556  -8.34397  1.000 106.28383 ?  237 ARG B O   1 
ATOM   5988 C CB  . ARG D 4 225 ? 51.37355  98.09275  -8.85737  1.000 115.33691 ?  237 ARG B CB  1 
ATOM   5989 C CG  . ARG D 4 225 ? 51.55472  96.58617  -8.94816  1.000 112.25256 ?  237 ARG B CG  1 
ATOM   5990 C CD  . ARG D 4 225 ? 50.22799  95.86716  -8.75299  1.000 97.47161  ?  237 ARG B CD  1 
ATOM   5991 N NE  . ARG D 4 225 ? 50.37166  94.41743  -8.81095  1.000 103.38112 ?  237 ARG B NE  1 
ATOM   5992 C CZ  . ARG D 4 225 ? 50.56813  93.64132  -7.75393  1.000 94.82663  ?  237 ARG B CZ  1 
ATOM   5993 N NH1 . ARG D 4 225 ? 50.64960  94.14397  -6.53284  1.000 91.83290  ?  237 ARG B NH1 1 
ATOM   5994 N NH2 . ARG D 4 225 ? 50.68470  92.32776  -7.92620  1.000 93.97720  ?  237 ARG B NH2 1 
ATOM   5995 N N   . ALA D 4 226 ? 53.39259  99.01696  -6.83425  1.000 92.94826  ?  238 ALA B N   1 
ATOM   5996 C CA  . ALA D 4 226 ? 54.32830  98.85368  -5.73148  1.000 100.55100 ?  238 ALA B CA  1 
ATOM   5997 C C   . ALA D 4 226 ? 54.52119  97.38011  -5.39001  1.000 112.53268 ?  238 ALA B C   1 
ATOM   5998 O O   . ALA D 4 226 ? 53.62972  96.54867  -5.58531  1.000 116.48827 ?  238 ALA B O   1 
ATOM   5999 C CB  . ALA D 4 226 ? 53.83967  99.61436  -4.49897  1.000 88.84302  ?  238 ALA B CB  1 
ATOM   6000 N N   . LYS D 4 227 ? 55.70338  97.06617  -4.87290  1.000 107.06249 ?  239 LYS B N   1 
ATOM   6001 C CA  . LYS D 4 227 ? 56.01482  95.69561  -4.49114  1.000 112.92778 ?  239 LYS B CA  1 
ATOM   6002 C C   . LYS D 4 227 ? 55.16779  95.28491  -3.29136  1.000 110.48459 ?  239 LYS B C   1 
ATOM   6003 O O   . LYS D 4 227 ? 55.15160  95.99483  -2.27775  1.000 115.32342 ?  239 LYS B O   1 
ATOM   6004 C CB  . LYS D 4 227 ? 57.49756  95.55771  -4.14973  1.000 114.20908 ?  239 LYS B CB  1 
ATOM   6005 C CG  . LYS D 4 227 ? 58.44284  96.12086  -5.19699  1.000 115.55512 ?  239 LYS B CG  1 
ATOM   6006 C CD  . LYS D 4 227 ? 59.88620  95.77278  -4.86695  1.000 126.09217 ?  239 LYS B CD  1 
ATOM   6007 C CE  . LYS D 4 227 ? 60.85583  96.42211  -5.84183  1.000 127.37503 ?  239 LYS B CE  1 
ATOM   6008 N NZ  . LYS D 4 227 ? 62.25082  95.94312  -5.62843  1.000 118.18363 ?  239 LYS B NZ  1 
ATOM   6009 N N   . PRO D 4 228 ? 54.45264  94.16207  -3.36176  1.000 98.87578  ?  240 PRO B N   1 
ATOM   6010 C CA  . PRO D 4 228 ? 53.68913  93.67766  -2.19130  1.000 99.19284  ?  240 PRO B CA  1 
ATOM   6011 C C   . PRO D 4 228 ? 54.58484  92.98276  -1.17330  1.000 99.61655  ?  240 PRO B C   1 
ATOM   6012 O O   . PRO D 4 228 ? 54.59057  91.75784  -1.01368  1.000 106.80708 ?  240 PRO B O   1 
ATOM   6013 C CB  . PRO D 4 228 ? 52.67408  92.72775  -2.83534  1.000 92.62218  ?  240 PRO B CB  1 
ATOM   6014 C CG  . PRO D 4 228 ? 53.39032  92.19132  -4.02512  1.000 99.41544  ?  240 PRO B CG  1 
ATOM   6015 C CD  . PRO D 4 228 ? 54.25037  93.31159  -4.54619  1.000 103.57851 ?  240 PRO B CD  1 
ATOM   6016 N N   . VAL D 4 229 ? 55.37205  93.78238  -0.45675  1.000 107.03803 ?  241 VAL B N   1 
ATOM   6017 C CA  . VAL D 4 229 ? 56.32482  93.25925  0.51574   1.000 117.66815 ?  241 VAL B CA  1 
ATOM   6018 C C   . VAL D 4 229 ? 55.66959  93.18378  1.88673   1.000 113.79544 ?  241 VAL B C   1 
ATOM   6019 O O   . VAL D 4 229 ? 54.56890  93.70745  2.08999   1.000 111.16172 ?  241 VAL B O   1 
ATOM   6020 C CB  . VAL D 4 229 ? 57.60158  94.11910  0.56206   1.000 110.19124 ?  241 VAL B CB  1 
ATOM   6021 C CG1 . VAL D 4 229 ? 58.28618  94.12656  -0.79691  1.000 112.51101 ?  241 VAL B CG1 1 
ATOM   6022 C CG2 . VAL D 4 229 ? 57.27123  95.53497  1.01060   1.000 98.27074  ?  241 VAL B CG2 1 
ATOM   6023 N N   . THR D 4 230 ? 56.34168  92.52572  2.83143   1.000 101.07269 ?  242 THR B N   1 
ATOM   6024 C CA  . THR D 4 230 ? 55.84425  92.41349  4.19673   1.000 96.34637  ?  242 THR B CA  1 
ATOM   6025 C C   . THR D 4 230 ? 55.74530  93.79084  4.83866   1.000 100.60301 ?  242 THR B C   1 
ATOM   6026 O O   . THR D 4 230 ? 56.76505  94.44605  5.07635   1.000 119.50937 ?  242 THR B O   1 
ATOM   6027 C CB  . THR D 4 230 ? 56.75092  91.50181  5.02797   1.000 110.71540 ?  242 THR B CB  1 
ATOM   6028 O OG1 . THR D 4 230 ? 56.76366  90.18713  4.45749   1.000 112.84505 ?  242 THR B OG1 1 
ATOM   6029 C CG2 . THR D 4 230 ? 56.25778  91.42225  6.46514   1.000 107.76419 ?  242 THR B CG2 1 
ATOM   6030 N N   . GLN D 4 231 ? 54.52346  94.23930  5.12021   1.000 92.67687  ?  243 GLN B N   1 
ATOM   6031 C CA  . GLN D 4 231 ? 54.28897  95.58179  5.62917   1.000 107.05073 ?  243 GLN B CA  1 
ATOM   6032 C C   . GLN D 4 231 ? 53.19567  95.53448  6.68778   1.000 102.07858 ?  243 GLN B C   1 
ATOM   6033 O O   . GLN D 4 231 ? 52.64209  94.47467  6.99799   1.000 92.75648  ?  243 GLN B O   1 
ATOM   6034 C CB  . GLN D 4 231 ? 53.91306  96.54176  4.49478   1.000 101.91580 ?  243 GLN B CB  1 
ATOM   6035 C CG  . GLN D 4 231 ? 52.72874  96.07646  3.66346   1.000 81.96206  ?  243 GLN B CG  1 
ATOM   6036 C CD  . GLN D 4 231 ? 52.34768  97.06968  2.58498   1.000 87.80987  ?  243 GLN B CD  1 
ATOM   6037 O OE1 . GLN D 4 231 ? 51.95918  98.20089  2.87595   1.000 104.87583 ?  243 GLN B OE1 1 
ATOM   6038 N NE2 . GLN D 4 231 ? 52.46181  96.65250  1.32939   1.000 83.35525  ?  243 GLN B NE2 1 
ATOM   6039 N N   . ILE D 4 232 ? 52.88613  96.70344  7.24351   1.000 111.71280 ?  244 ILE B N   1 
ATOM   6040 C CA  . ILE D 4 232 ? 51.84873  96.86127  8.25621   1.000 109.01226 ?  244 ILE B CA  1 
ATOM   6041 C C   . ILE D 4 232 ? 50.91948  97.97270  7.78885   1.000 95.09007  ?  244 ILE B C   1 
ATOM   6042 O O   . ILE D 4 232 ? 51.31082  99.14639  7.76815   1.000 105.37197 ?  244 ILE B O   1 
ATOM   6043 C CB  . ILE D 4 232 ? 52.42835  97.18357  9.64084   1.000 111.40048 ?  244 ILE B CB  1 
ATOM   6044 C CG1 . ILE D 4 232 ? 53.28611  96.02296  10.14814  1.000 109.10283 ?  244 ILE B CG1 1 
ATOM   6045 C CG2 . ILE D 4 232 ? 51.31243  97.49724  10.62598  1.000 107.52515 ?  244 ILE B CG2 1 
ATOM   6046 C CD1 . ILE D 4 232 ? 53.87821  96.25579  11.52153  1.000 101.48094 ?  244 ILE B CD1 1 
ATOM   6047 N N   . VAL D 4 233 ? 49.69653  97.60980  7.41210   1.000 88.21296  ?  245 VAL B N   1 
ATOM   6048 C CA  . VAL D 4 233 ? 48.67442  98.57043  7.01306   1.000 96.84903  ?  245 VAL B CA  1 
ATOM   6049 C C   . VAL D 4 233 ? 47.69781  98.73241  8.16888   1.000 103.75964 ?  245 VAL B C   1 
ATOM   6050 O O   . VAL D 4 233 ? 47.25512  97.73941  8.76119   1.000 88.71428  ?  245 VAL B O   1 
ATOM   6051 C CB  . VAL D 4 233 ? 47.95028  98.11885  5.73318   1.000 83.26427  ?  245 VAL B CB  1 
ATOM   6052 C CG1 . VAL D 4 233 ? 47.05381  99.23172  5.21031   1.000 96.16696  ?  245 VAL B CG1 1 
ATOM   6053 C CG2 . VAL D 4 233 ? 48.95732  97.69544  4.67470   1.000 74.65710  ?  245 VAL B CG2 1 
ATOM   6054 N N   . SER D 4 234 ? 47.36490  99.98044  8.49552   1.000 98.41197  ?  246 SER B N   1 
ATOM   6055 C CA  . SER D 4 234 ? 46.51524  100.27936 9.63787   1.000 98.52587  ?  246 SER B CA  1 
ATOM   6056 C C   . SER D 4 234 ? 45.63500  101.48038 9.32319   1.000 112.78739 ?  246 SER B C   1 
ATOM   6057 O O   . SER D 4 234 ? 45.76897  102.12639 8.28021   1.000 116.84313 ?  246 SER B O   1 
ATOM   6058 C CB  . SER D 4 234 ? 47.34346  100.54989 10.90019  1.000 104.56501 ?  246 SER B CB  1 
ATOM   6059 O OG  . SER D 4 234 ? 48.17272  99.44649  11.21780  1.000 109.35696 ?  246 SER B OG  1 
ATOM   6060 N N   . ALA D 4 235 ? 44.72806  101.77607 10.25255  1.000 116.44003 ?  247 ALA B N   1 
ATOM   6061 C CA  . ALA D 4 235 ? 43.82721  102.91337 10.13668  1.000 110.69466 ?  247 ALA B CA  1 
ATOM   6062 C C   . ALA D 4 235 ? 43.37591  103.31326 11.53383  1.000 109.62775 ?  247 ALA B C   1 
ATOM   6063 O O   . ALA D 4 235 ? 43.09874  102.45047 12.37073  1.000 102.26765 ?  247 ALA B O   1 
ATOM   6064 C CB  . ALA D 4 235 ? 42.61851  102.58593 9.25283   1.000 92.03451  ?  247 ALA B CB  1 
ATOM   6065 N N   . GLU D 4 236 ? 43.30687  104.61798 11.77744  1.000 131.39274 ?  248 GLU B N   1 
ATOM   6066 C CA  . GLU D 4 236 ? 42.97997  105.15489 13.08873  1.000 124.95635 ?  248 GLU B CA  1 
ATOM   6067 C C   . GLU D 4 236 ? 41.60834  105.81721 13.07224  1.000 123.47939 ?  248 GLU B C   1 
ATOM   6068 O O   . GLU D 4 236 ? 41.06335  106.15083 12.01644  1.000 125.31093 ?  248 GLU B O   1 
ATOM   6069 C CB  . GLU D 4 236 ? 44.04074  106.16217 13.54711  1.000 116.83140 ?  248 GLU B CB  1 
ATOM   6070 N N   . ALA D 4 237 ? 41.05614  106.00363 14.26949  1.000 130.96397 ?  249 ALA B N   1 
ATOM   6071 C CA  . ALA D 4 237 ? 39.75582  106.65032 14.42958  1.000 138.55915 ?  249 ALA B CA  1 
ATOM   6072 C C   . ALA D 4 237 ? 39.63194  107.12032 15.86880  1.000 142.20841 ?  249 ALA B C   1 
ATOM   6073 O O   . ALA D 4 237 ? 39.73483  106.30845 16.79415  1.000 139.14661 ?  249 ALA B O   1 
ATOM   6074 C CB  . ALA D 4 237 ? 38.61699  105.69580 14.07007  1.000 107.57002 ?  249 ALA B CB  1 
ATOM   6075 N N   . TRP D 4 238 ? 39.41577  108.41712 16.05864  1.000 143.13979 ?  250 TRP B N   1 
ATOM   6076 C CA  . TRP D 4 238 ? 39.28503  108.98841 17.38926  1.000 147.98848 ?  250 TRP B CA  1 
ATOM   6077 C C   . TRP D 4 238 ? 37.83812  108.91474 17.86740  1.000 140.90134 ?  250 TRP B C   1 
ATOM   6078 O O   . TRP D 4 238 ? 36.90522  108.71741 17.08513  1.000 134.71248 ?  250 TRP B O   1 
ATOM   6079 C CB  . TRP D 4 238 ? 39.77154  110.43827 17.40442  1.000 155.42474 ?  250 TRP B CB  1 
ATOM   6080 C CG  . TRP D 4 238 ? 41.23112  110.58394 17.09759  1.000 160.57347 ?  250 TRP B CG  1 
ATOM   6081 C CD1 . TRP D 4 238 ? 41.80047  110.71716 15.86476  1.000 159.13567 ?  250 TRP B CD1 1 
ATOM   6082 C CD2 . TRP D 4 238 ? 42.30856  110.61181 18.04206  1.000 161.17377 ?  250 TRP B CD2 1 
ATOM   6083 N NE1 . TRP D 4 238 ? 43.16516  110.82588 15.98258  1.000 157.05003 ?  250 TRP B NE1 1 
ATOM   6084 C CE2 . TRP D 4 238 ? 43.50238  110.76412 17.30910  1.000 156.23485 ?  250 TRP B CE2 1 
ATOM   6085 C CE3 . TRP D 4 238 ? 42.37945  110.52275 19.43583  1.000 157.92064 ?  250 TRP B CE3 1 
ATOM   6086 C CZ2 . TRP D 4 238 ? 44.75178  110.82926 17.92246  1.000 156.86248 ?  250 TRP B CZ2 1 
ATOM   6087 C CZ3 . TRP D 4 238 ? 43.62092  110.58769 20.04284  1.000 145.50178 ?  250 TRP B CZ3 1 
ATOM   6088 C CH2 . TRP D 4 238 ? 44.78981  110.73943 19.28676  1.000 156.51698 ?  250 TRP B CH2 1 
ATOM   6089 N N   . GLY D 4 239 ? 37.66349  109.07907 19.17563  1.000 136.67298 ?  251 GLY B N   1 
ATOM   6090 C CA  . GLY D 4 239 ? 36.33470  108.99645 19.75418  1.000 137.29345 ?  251 GLY B CA  1 
ATOM   6091 C C   . GLY D 4 239 ? 35.50587  110.22931 19.43628  1.000 150.28884 ?  251 GLY B C   1 
ATOM   6092 O O   . GLY D 4 239 ? 35.99221  111.36079 19.47026  1.000 153.92516 ?  251 GLY B O   1 
ATOM   6093 N N   . ARG D 4 240 ? 34.23252  109.99945 19.12551  1.000 146.56738 ?  252 ARG B N   1 
ATOM   6094 C CA  . ARG D 4 240 ? 33.29391  111.06043 18.78758  1.000 152.77182 ?  252 ARG B CA  1 
ATOM   6095 C C   . ARG D 4 240 ? 32.12771  111.02970 19.76390  1.000 142.10694 ?  252 ARG B C   1 
ATOM   6096 O O   . ARG D 4 240 ? 31.58622  109.95844 20.05684  1.000 135.82169 ?  252 ARG B O   1 
ATOM   6097 C CB  . ARG D 4 240 ? 32.78744  110.91148 17.34995  1.000 128.89005 ?  252 ARG B CB  1 
ATOM   6098 N N   . ALA D 4 241 ? 31.74561  112.20109 20.26215  1.000 132.28912 ?  253 ALA B N   1 
ATOM   6099 C CA  . ALA D 4 241 ? 30.63392  112.30960 21.19912  1.000 134.90328 ?  253 ALA B CA  1 
ATOM   6100 C C   . ALA D 4 241 ? 29.42620  112.96516 20.53750  1.000 136.40370 ?  253 ALA B C   1 
ATOM   6101 O O   . ALA D 4 241 ? 28.30458  112.86910 21.03584  1.000 137.32646 ?  253 ALA B O   1 
ATOM   6102 C CB  . ALA D 4 241 ? 31.05422  113.09309 22.43275  1.000 145.09098 ?  253 ALA B CB  1 
HETATM 6103 C C1  . EDO E 5 .   ? 90.66027  48.43478  26.65482  1.000 70.92269  ?  201 EDO C C1  1 
HETATM 6104 O O1  . EDO E 5 .   ? 89.70784  48.41944  27.72415  1.000 58.48280  ?  201 EDO C O1  1 
HETATM 6105 C C2  . EDO E 5 .   ? 89.93981  48.23314  25.32676  1.000 63.33499  ?  201 EDO C C2  1 
HETATM 6106 O O2  . EDO E 5 .   ? 90.89517  48.23132  24.25921  1.000 68.88982  ?  201 EDO C O2  1 
HETATM 6107 C C1  . EDO F 5 .   ? 66.99383  35.17328  28.51435  1.000 93.33619  ?  202 EDO C C1  1 
HETATM 6108 O O1  . EDO F 5 .   ? 66.72033  33.84319  28.96981  1.000 82.22561  ?  202 EDO C O1  1 
HETATM 6109 C C2  . EDO F 5 .   ? 67.62365  35.11487  27.12781  1.000 91.67586  ?  202 EDO C C2  1 
HETATM 6110 O O2  . EDO F 5 .   ? 67.91389  36.44347  26.68005  1.000 62.01621  ?  202 EDO C O2  1 
HETATM 6111 C C1  . NAG G 6 .   ? 91.77422  39.96377  12.15027  1.000 109.56200 ?  203 NAG C C1  1 
HETATM 6112 C C2  . NAG G 6 .   ? 91.51077  39.08317  10.90816  1.000 104.61680 ?  203 NAG C C2  1 
HETATM 6113 C C3  . NAG G 6 .   ? 91.87124  39.82278  9.62243   1.000 124.57893 ?  203 NAG C C3  1 
HETATM 6114 C C4  . NAG G 6 .   ? 91.12067  41.14283  9.56381   1.000 127.45352 ?  203 NAG C C4  1 
HETATM 6115 C C5  . NAG G 6 .   ? 91.52064  42.02913  10.74057  1.000 113.91739 ?  203 NAG C C5  1 
HETATM 6116 C C6  . NAG G 6 .   ? 90.33827  42.64751  11.45065  1.000 89.03593  ?  203 NAG C C6  1 
HETATM 6117 C C7  . NAG G 6 .   ? 93.46513  37.46282  11.03839  1.000 100.78207 ?  203 NAG C C7  1 
HETATM 6118 C C8  . NAG G 6 .   ? 94.45608  38.59998  11.04718  1.000 101.96903 ?  203 NAG C C8  1 
HETATM 6119 N N2  . NAG G 6 .   ? 92.14978  37.76787  10.97692  1.000 108.29050 ?  203 NAG C N2  1 
HETATM 6120 O O3  . NAG G 6 .   ? 91.54003  39.01816  8.49654   1.000 134.47985 ?  203 NAG C O3  1 
HETATM 6121 O O4  . NAG G 6 .   ? 91.42893  41.81789  8.34949   1.000 120.97985 ?  203 NAG C O4  1 
HETATM 6122 O O5  . NAG G 6 .   ? 92.27307  41.29713  11.72719  1.000 123.27092 ?  203 NAG C O5  1 
HETATM 6123 O O6  . NAG G 6 .   ? 90.65165  43.94086  11.94879  1.000 86.07822  ?  203 NAG C O6  1 
HETATM 6124 O O7  . NAG G 6 .   ? 93.84078  36.29652  11.08800  1.000 101.64059 ?  203 NAG C O7  1 
HETATM 6125 C C1  . EDO H 5 .   ? 77.37468  45.93448  20.36685  1.000 38.11200  ?  204 EDO C C1  1 
HETATM 6126 O O1  . EDO H 5 .   ? 76.95363  47.28870  20.17473  1.000 67.08388  ?  204 EDO C O1  1 
HETATM 6127 C C2  . EDO H 5 .   ? 77.73445  45.31622  19.02246  1.000 50.16499  ?  204 EDO C C2  1 
HETATM 6128 O O2  . EDO H 5 .   ? 78.28587  44.01322  19.23673  1.000 58.19770  ?  204 EDO C O2  1 
HETATM 6129 C C1  . NAG I 6 .   ? 47.79580  23.85831  32.27607  1.000 125.35325 ?  301 NAG D C1  1 
HETATM 6130 C C2  . NAG I 6 .   ? 46.75929  23.49759  31.18824  1.000 122.74920 ?  301 NAG D C2  1 
HETATM 6131 C C3  . NAG I 6 .   ? 46.21879  22.07469  31.38215  1.000 124.17239 ?  301 NAG D C3  1 
HETATM 6132 C C4  . NAG I 6 .   ? 47.36241  21.07992  31.52730  1.000 125.91223 ?  301 NAG D C4  1 
HETATM 6133 C C5  . NAG I 6 .   ? 48.31660  21.53262  32.62784  1.000 126.70214 ?  301 NAG D C5  1 
HETATM 6134 C C6  . NAG I 6 .   ? 49.52136  20.63247  32.77363  1.000 133.03169 ?  301 NAG D C6  1 
HETATM 6135 C C7  . NAG I 6 .   ? 44.73751  24.83747  31.94831  1.000 130.01545 ?  301 NAG D C7  1 
HETATM 6136 C C8  . NAG I 6 .   ? 44.76479  24.17806  33.30411  1.000 124.15568 ?  301 NAG D C8  1 
HETATM 6137 N N2  . NAG I 6 .   ? 45.68000  24.47666  31.04976  1.000 130.82892 ?  301 NAG D N2  1 
HETATM 6138 O O3  . NAG I 6 .   ? 45.39891  21.71914  30.27476  1.000 122.17292 ?  301 NAG D O3  1 
HETATM 6139 O O4  . NAG I 6 .   ? 46.84788  19.79432  31.85522  1.000 127.07071 ?  301 NAG D O4  1 
HETATM 6140 O O5  . NAG I 6 .   ? 48.81482  22.84454  32.32897  1.000 122.60014 ?  301 NAG D O5  1 
HETATM 6141 O O6  . NAG I 6 .   ? 50.57494  21.28380  33.47010  1.000 121.98179 ?  301 NAG D O6  1 
HETATM 6142 O O7  . NAG I 6 .   ? 43.88989  25.68057  31.67088  1.000 103.35064 ?  301 NAG D O7  1 
HETATM 6143 C C1  . EDO J 5 .   ? 62.94802  62.48788  29.46281  1.000 57.60581  ?  302 EDO D C1  1 
HETATM 6144 O O1  . EDO J 5 .   ? 62.49311  62.20099  30.79005  1.000 73.21556  ?  302 EDO D O1  1 
HETATM 6145 C C2  . EDO J 5 .   ? 64.47091  62.45438  29.43002  1.000 62.88255  ?  302 EDO D C2  1 
HETATM 6146 O O2  . EDO J 5 .   ? 64.92997  62.72642  28.10118  1.000 77.05539  ?  302 EDO D O2  1 
HETATM 6147 C C1  . EDO K 5 .   ? 62.37231  56.71842  12.01672  1.000 80.25199  ?  401 EDO B C1  1 
HETATM 6148 O O1  . EDO K 5 .   ? 62.61857  55.93792  13.19191  1.000 70.51083  ?  401 EDO B O1  1 
HETATM 6149 C C2  . EDO K 5 .   ? 61.25231  57.71466  12.29275  1.000 58.35231  ?  401 EDO B C2  1 
HETATM 6150 O O2  . EDO K 5 .   ? 60.99913  58.48484  11.11263  1.000 62.75059  ?  401 EDO B O2  1 
HETATM 6151 C C1  . EDO L 5 .   ? 48.91571  77.05851  -1.72241  1.000 85.98452  ?  402 EDO B C1  1 
HETATM 6152 O O1  . EDO L 5 .   ? 48.11485  77.12492  -0.53692  1.000 91.69762  ?  402 EDO B O1  1 
HETATM 6153 C C2  . EDO L 5 .   ? 48.37856  75.97017  -2.64387  1.000 83.84406  ?  402 EDO B C2  1 
HETATM 6154 O O2  . EDO L 5 .   ? 49.19618  75.89628  -3.81702  1.000 75.30557  ?  402 EDO B O2  1 
HETATM 6155 O O   . HOH M 7 .   ? 65.10368  34.10130  24.43793  1.000 54.80399  ?  301 HOH C O   1 
HETATM 6156 O O   . HOH M 7 .   ? 87.80794  19.14192  4.31235   1.000 72.03749  ?  302 HOH C O   1 
HETATM 6157 O O   . HOH M 7 .   ? 86.24958  38.30428  25.63547  1.000 39.85183  ?  303 HOH C O   1 
HETATM 6158 O O   . HOH M 7 .   ? 79.55872  14.96854  6.72054   1.000 68.29733  ?  304 HOH C O   1 
HETATM 6159 O O   . HOH M 7 .   ? 56.93371  53.09436  11.97945  1.000 43.71994  ?  305 HOH C O   1 
HETATM 6160 O O   . HOH M 7 .   ? 90.73050  46.60874  29.95063  1.000 53.55532  ?  306 HOH C O   1 
HETATM 6161 O O   . HOH M 7 .   ? 74.08501  47.12493  12.32971  1.000 68.52044  ?  307 HOH C O   1 
HETATM 6162 O O   . HOH M 7 .   ? 53.31402  38.57197  6.59029   1.000 67.74672  ?  308 HOH C O   1 
HETATM 6163 O O   . HOH M 7 .   ? 59.80164  42.04414  8.62325   1.000 50.95689  ?  309 HOH C O   1 
HETATM 6164 O O   . HOH M 7 .   ? 74.57961  41.65128  13.37891  1.000 43.20468  ?  310 HOH C O   1 
HETATM 6165 O O   . HOH M 7 .   ? 94.26205  38.86238  19.95730  1.000 63.38685  ?  311 HOH C O   1 
HETATM 6166 O O   . HOH M 7 .   ? 62.46010  45.54817  6.93426   1.000 59.20815  ?  312 HOH C O   1 
HETATM 6167 O O   . HOH M 7 .   ? 96.38475  33.44788  4.44293   1.000 65.79271  ?  313 HOH C O   1 
HETATM 6168 O O   . HOH M 7 .   ? 70.95543  61.90882  23.66087  1.000 68.54608  ?  314 HOH C O   1 
HETATM 6169 O O   . HOH M 7 .   ? 76.96735  32.37425  31.52344  1.000 66.53870  ?  315 HOH C O   1 
HETATM 6170 O O   . HOH M 7 .   ? 69.91732  32.91138  28.11600  1.000 84.52596  ?  316 HOH C O   1 
HETATM 6171 O O   . HOH M 7 .   ? 72.61608  55.15871  8.49675   1.000 53.19757  ?  317 HOH C O   1 
HETATM 6172 O O   . HOH M 7 .   ? 88.12699  22.20499  19.33660  1.000 67.77035  ?  318 HOH C O   1 
HETATM 6173 O O   . HOH M 7 .   ? 76.03749  49.74355  14.07263  1.000 81.65868  ?  319 HOH C O   1 
HETATM 6174 O O   . HOH M 7 .   ? 99.155    31.050    19.049    1.000 60.37523  ?  320 HOH C O   1 
HETATM 6175 O O   . HOH M 7 .   ? 53.57877  25.40860  26.50430  1.000 52.57967  ?  321 HOH C O   1 
HETATM 6176 O O   . HOH M 7 .   ? 75.87517  60.31014  24.39333  1.000 65.58928  ?  322 HOH C O   1 
HETATM 6177 O O   . HOH M 7 .   ? 91.27370  47.76771  10.15466  1.000 76.34335  ?  323 HOH C O   1 
HETATM 6178 O O   . HOH M 7 .   ? 90.26856  42.78940  16.51931  1.000 49.03346  ?  324 HOH C O   1 
HETATM 6179 O O   . HOH N 7 .   ? 53.80815  44.04642  34.15617  1.000 48.34987  ?  401 HOH D O   1 
HETATM 6180 O O   . HOH N 7 .   ? 58.59782  23.07272  10.41617  1.000 60.47468  ?  402 HOH D O   1 
HETATM 6181 O O   . HOH N 7 .   ? 43.69032  19.53964  32.57905  1.000 92.87303  ?  403 HOH D O   1 
HETATM 6182 O O   . HOH N 7 .   ? 91.43940  53.36374  25.66208  1.000 74.38304  ?  404 HOH D O   1 
HETATM 6183 O O   . HOH N 7 .   ? 69.72678  36.44152  31.16916  1.000 69.22418  ?  405 HOH D O   1 
HETATM 6184 O O   . HOH N 7 .   ? 46.64991  28.46498  26.64111  1.000 83.21178  ?  406 HOH D O   1 
HETATM 6185 O O   . HOH N 7 .   ? 46.18824  46.19395  28.76613  1.000 51.61597  ?  407 HOH D O   1 
HETATM 6186 O O   . HOH N 7 .   ? 44.33275  40.57390  27.88491  1.000 61.72974  ?  408 HOH D O   1 
HETATM 6187 O O   . HOH N 7 .   ? 43.85589  38.34275  29.42804  1.000 65.09586  ?  409 HOH D O   1 
HETATM 6188 O O   . HOH O 7 .   ? 27.34958  62.24715  7.85734   1.000 62.19662  ?  301 HOH A O   1 
HETATM 6189 O O   . HOH O 7 .   ? 54.07775  52.81160  14.51289  1.000 45.34247  ?  302 HOH A O   1 
HETATM 6190 O O   . HOH O 7 .   ? 51.25064  47.35626  20.34041  1.000 59.45652  ?  303 HOH A O   1 
HETATM 6191 O O   . HOH O 7 .   ? 48.56179  51.25725  28.40546  1.000 41.02886  ?  304 HOH A O   1 
HETATM 6192 O O   . HOH O 7 .   ? 45.06236  43.90168  19.30556  1.000 58.82850  ?  305 HOH A O   1 
HETATM 6193 O O   . HOH O 7 .   ? 11.36420  85.40320  5.63887   1.000 78.15426  ?  306 HOH A O   1 
HETATM 6194 O O   . HOH P 7 .   ? 49.97307  59.54059  10.08044  1.000 45.72034  ?  501 HOH B O   1 
HETATM 6195 O O   . HOH P 7 .   ? 65.57222  57.81331  16.15683  1.000 52.75593  ?  502 HOH B O   1 
HETATM 6196 O O   . HOH P 7 .   ? 65.12614  66.46474  0.17605   1.000 56.20466  ?  503 HOH B O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . ASP A 1   ? 1.52505 1.08896 0.73241 -0.26067 -0.14567 0.32791  1   ASP C N   
2    C CA  . ASP A 1   ? 1.77772 1.37336 1.07160 -0.23229 -0.12400 0.32189  1   ASP C CA  
3    C C   . ASP A 1   ? 1.78632 1.39196 1.06292 -0.24795 -0.05744 0.31049  1   ASP C C   
4    O O   . ASP A 1   ? 1.83152 1.41359 1.03870 -0.28051 -0.03674 0.31628  1   ASP C O   
5    C CB  . ASP A 1   ? 1.90287 1.48243 1.27101 -0.21616 -0.17664 0.35210  1   ASP C CB  
6    C CG  . ASP A 1   ? 1.96829 1.58092 1.43436 -0.18341 -0.16586 0.34232  1   ASP C CG  
7    O OD1 . ASP A 1   ? 1.98849 1.63331 1.49802 -0.15779 -0.17173 0.32329  1   ASP C OD1 
8    O OD2 . ASP A 1   ? 2.08558 1.69097 1.58544 -0.18522 -0.15251 0.35384  1   ASP C OD2 
9    N N   . ILE A 2   ? 1.53183 1.17342 0.87545 -0.22653 -0.02442 0.29350  2   ILE C N   
10   C CA  . ILE A 2   ? 1.55425 1.21507 0.90652 -0.23755 0.03959  0.27696  2   ILE C CA  
11   C C   . ILE A 2   ? 1.41806 1.07336 0.83649 -0.23105 0.03274  0.29863  2   ILE C C   
12   O O   . ILE A 2   ? 1.51180 1.17665 0.99857 -0.20526 0.00339  0.30386  2   ILE C O   
13   C CB  . ILE A 2   ? 1.36959 1.07774 0.75310 -0.22147 0.08573  0.23518  2   ILE C CB  
14   C CG1 . ILE A 2   ? 1.16400 0.87309 0.48892 -0.22800 0.08930  0.21218  2   ILE C CG1 
15   C CG2 . ILE A 2   ? 1.37101 1.10445 0.78611 -0.23058 0.14843  0.21465  2   ILE C CG2 
16   C CD1 . ILE A 2   ? 1.20066 0.95255 0.56259 -0.21168 0.13117  0.17026  2   ILE C CD1 
17   N N   . GLU A 3   ? 1.36019 0.99993 0.76217 -0.25575 0.05933  0.31003  3   GLU C N   
18   C CA  . GLU A 3   ? 1.31804 0.94778 0.78258 -0.25476 0.05501  0.33018  3   GLU C CA  
19   C C   . GLU A 3   ? 1.32163 0.99315 0.84414 -0.25213 0.11409  0.30169  3   GLU C C   
20   O O   . GLU A 3   ? 1.46686 1.16166 0.96851 -0.26650 0.16695  0.27708  3   GLU C O   
21   C CB  . GLU A 3   ? 1.29136 0.87802 0.71012 -0.28519 0.04691  0.36194  3   GLU C CB  
22   N N   . ALA A 4   ? 1.17530 0.86767 0.79299 -0.22600 0.10063  0.29557  4   ALA C N   
23   C CA  . ALA A 4   ? 0.94435 0.68978 0.64646 -0.21107 0.14475  0.25946  4   ALA C CA  
24   C C   . ALA A 4   ? 0.93696 0.69659 0.74280 -0.18241 0.11359  0.25663  4   ALA C C   
25   O O   . ALA A 4   ? 1.27907 1.01350 1.10007 -0.16970 0.06264  0.27571  4   ALA C O   
26   C CB  . ALA A 4   ? 0.87256 0.66904 0.59388 -0.18711 0.16807  0.21841  4   ALA C CB  
27   N N   . ASP A 5   ? 0.88029 0.68072 0.76297 -0.17305 0.14392  0.22964  5   ASP C N   
28   C CA  . ASP A 5   ? 0.76045 0.57863 0.73885 -0.14775 0.11891  0.21815  5   ASP C CA  
29   C C   . ASP A 5   ? 0.67076 0.53475 0.69737 -0.10810 0.10135  0.18557  5   ASP C C   
30   O O   . ASP A 5   ? 0.84836 0.71620 0.92857 -0.08660 0.06849  0.17832  5   ASP C O   
31   C CB  . ASP A 5   ? 0.74921 0.58717 0.78781 -0.15998 0.15360  0.20581  5   ASP C CB  
32   C CG  . ASP A 5   ? 0.98257 0.77350 0.98654 -0.20164 0.16953  0.24001  5   ASP C CG  
33   O OD1 . ASP A 5   ? 1.30466 1.04548 1.22257 -0.22441 0.15546  0.27518  5   ASP C OD1 
34   O OD2 . ASP A 5   ? 1.00135 0.80383 1.06312 -0.21422 0.19390  0.23350  5   ASP C OD2 
35   N N   . HIS A 6   ? 0.70826 0.60546 0.71793 -0.10028 0.12418  0.16467  6   HIS C N   
36   C CA  . HIS A 6   ? 0.59420 0.53179 0.63885 -0.06850 0.10964  0.13838  6   HIS C CA  
37   C C   . HIS A 6   ? 0.61736 0.56134 0.60679 -0.06746 0.11975  0.13413  6   HIS C C   
38   O O   . HIS A 6   ? 0.78458 0.71977 0.72995 -0.08832 0.15227  0.13602  6   HIS C O   
39   C CB  . HIS A 6   ? 0.65939 0.64065 0.77539 -0.05699 0.12428  0.11100  6   HIS C CB  
40   C CG  . HIS A 6   ? 0.66628 0.64387 0.84078 -0.05809 0.11305  0.10927  6   HIS C CG  
41   N ND1 . HIS A 6   ? 0.61201 0.59677 0.82566 -0.03883 0.08187  0.09639  6   HIS C ND1 
42   C CD2 . HIS A 6   ? 0.70346 0.67102 0.90715 -0.07796 0.13092  0.11565  6   HIS C CD2 
43   C CE1 . HIS A 6   ? 0.56488 0.54191 0.82814 -0.04565 0.07823  0.09397  6   HIS C CE1 
44   N NE2 . HIS A 6   ? 0.88350 0.84996 1.14336 -0.06931 0.10624  0.10764  6   HIS C NE2 
45   N N   . VAL A 7   ? 0.52556 0.48518 0.52032 -0.04495 0.09439  0.12527  7   VAL C N   
46   C CA  . VAL A 7   ? 0.60182 0.56879 0.55461 -0.04148 0.09838  0.11940  7   VAL C CA  
47   C C   . VAL A 7   ? 0.67868 0.68985 0.67915 -0.01760 0.09569  0.09528  7   VAL C C   
48   O O   . VAL A 7   ? 0.70677 0.73106 0.73650 -0.00109 0.07109  0.08952  7   VAL C O   
49   C CB  . VAL A 7   ? 0.62072 0.55771 0.52686 -0.04293 0.06546  0.13820  7   VAL C CB  
50   C CG1 . VAL A 7   ? 0.74834 0.69375 0.61521 -0.04078 0.06958  0.12919  7   VAL C CG1 
51   C CG2 . VAL A 7   ? 0.90028 0.78605 0.74992 -0.07099 0.05990  0.16911  7   VAL C CG2 
52   N N   . GLY A 8   ? 0.53698 0.56967 0.54714 -0.01777 0.12113  0.08085  8   GLY C N   
53   C CA  . GLY A 8   ? 0.49646 0.56432 0.54360 0.00035  0.11453  0.06464  8   GLY C CA  
54   C C   . GLY A 8   ? 0.47848 0.54811 0.49491 0.00400  0.11485  0.06136  8   GLY C C   
55   O O   . GLY A 8   ? 0.73552 0.80166 0.74022 -0.00392 0.13867  0.05467  8   GLY C O   
56   N N   . THR A 9   ? 0.49831 0.57392 0.50757 0.01481  0.09084  0.06281  9   THR C N   
57   C CA  . THR A 9   ? 0.59500 0.67274 0.58131 0.01765  0.08773  0.06016  9   THR C CA  
58   C C   . THR A 9   ? 0.46876 0.57608 0.49236 0.02769  0.08796  0.05036  9   THR C C   
59   O O   . THR A 9   ? 0.58188 0.70752 0.61856 0.03543  0.07189  0.04903  9   THR C O   
60   C CB  . THR A 9   ? 0.62134 0.69217 0.59073 0.02173  0.06205  0.06715  9   THR C CB  
61   O OG1 . THR A 9   ? 0.69504 0.74135 0.65390 0.01597  0.04990  0.07981  9   THR C OG1 
62   C CG2 . THR A 9   ? 0.51111 0.56808 0.44058 0.01590  0.05997  0.06849  9   THR C CG2 
63   N N   . TYR A 10  ? 0.66569 0.77646 0.70833 0.02534  0.10649  0.04334  10  TYR C N   
64   C CA  . TYR A 10  ? 0.61799 0.75118 0.70366 0.03328  0.10027  0.03912  10  TYR C CA  
65   C C   . TYR A 10  ? 0.62200 0.75250 0.69784 0.03551  0.09706  0.03824  10  TYR C C   
66   O O   . TYR A 10  ? 0.47216 0.59965 0.57173 0.03561  0.10940  0.03012  10  TYR C O   
67   C CB  . TYR A 10  ? 0.42364 0.56352 0.55825 0.03148  0.11690  0.03126  10  TYR C CB  
68   C CG  . TYR A 10  ? 0.52237 0.66423 0.67110 0.02718  0.11924  0.03243  10  TYR C CG  
69   C CD1 . TYR A 10  ? 0.47622 0.62658 0.62304 0.03108  0.09674  0.03657  10  TYR C CD1 
70   C CD2 . TYR A 10  ? 0.44843 0.58293 0.61328 0.01674  0.14693  0.02680  10  TYR C CD2 
71   C CE1 . TYR A 10  ? 0.41367 0.56294 0.57857 0.02694  0.09715  0.03545  10  TYR C CE1 
72   C CE2 . TYR A 10  ? 0.53761 0.67174 0.71937 0.01073  0.14827  0.02959  10  TYR C CE2 
73   C CZ  . TYR A 10  ? 0.43392 0.57418 0.61737 0.01695  0.12103  0.03417  10  TYR C CZ  
74   O OH  . TYR A 10  ? 0.54805 0.68526 0.75369 0.01086  0.12069  0.03470  10  TYR C OH  
75   N N   . GLY A 11  ? 0.70801 0.84021 0.75720 0.03702  0.08079  0.04442  11  GLY C N   
76   C CA  . GLY A 11  ? 0.45951 0.58861 0.49970 0.03703  0.07524  0.04517  11  GLY C CA  
77   C C   . GLY A 11  ? 0.38121 0.49779 0.38245 0.03331  0.06897  0.04657  11  GLY C C   
78   O O   . GLY A 11  ? 0.41740 0.51160 0.38728 0.02646  0.07734  0.04326  11  GLY C O   
79   N N   . ILE A 12  ? 0.42276 0.55358 0.42569 0.03516  0.05373  0.05111  12  ILE C N   
80   C CA  . ILE A 12  ? 0.55076 0.67461 0.53495 0.03263  0.04222  0.05200  12  ILE C CA  
81   C C   . ILE A 12  ? 0.51391 0.65077 0.51108 0.03075  0.03624  0.05344  12  ILE C C   
82   O O   . ILE A 12  ? 0.57319 0.73344 0.58729 0.03046  0.03390  0.05576  12  ILE C O   
83   C CB  . ILE A 12  ? 0.51811 0.64943 0.50973 0.03603  0.03094  0.05310  12  ILE C CB  
84   C CG1 . ILE A 12  ? 0.60974 0.72114 0.58727 0.03486  0.03370  0.05642  12  ILE C CG1 
85   C CG2 . ILE A 12  ? 0.31696 0.44543 0.30790 0.03454  0.01336  0.05407  12  ILE C CG2 
86   C CD1 . ILE A 12  ? 0.54957 0.66183 0.54485 0.03926  0.01829  0.05816  12  ILE C CD1 
87   N N   . SER A 13  ? 0.57899 0.69929 0.56540 0.02635  0.03552  0.05085  13  SER C N   
88   C CA  . SER A 13  ? 0.49643 0.62368 0.49761 0.02212  0.02893  0.05371  13  SER C CA  
89   C C   . SER A 13  ? 0.57310 0.69751 0.56703 0.01779  0.01486  0.05121  13  SER C C   
90   O O   . SER A 13  ? 0.61120 0.71170 0.57678 0.01446  0.00899  0.04586  13  SER C O   
91   C CB  . SER A 13  ? 0.53037 0.63977 0.53946 0.02058  0.03516  0.04981  13  SER C CB  
92   O OG  . SER A 13  ? 0.75846 0.87267 0.79067 0.02540  0.04188  0.05353  13  SER C OG  
93   N N   . VAL A 14  ? 0.43586 0.58477 0.45510 0.01521  0.00931  0.05433  14  VAL C N   
94   C CA  . VAL A 14  ? 0.44165 0.59443 0.47433 0.01108  -0.00626 0.05116  14  VAL C CA  
95   C C   . VAL A 14  ? 0.38031 0.54832 0.43842 0.00142  -0.00361 0.05453  14  VAL C C   
96   O O   . VAL A 14  ? 0.40994 0.60002 0.48035 -0.00306 0.00900  0.06014  14  VAL C O   
97   C CB  . VAL A 14  ? 0.40445 0.57684 0.46240 0.01665  -0.01363 0.04765  14  VAL C CB  
98   C CG1 . VAL A 14  ? 0.33989 0.51630 0.42619 0.01329  -0.03549 0.04429  14  VAL C CG1 
99   C CG2 . VAL A 14  ? 0.47106 0.62435 0.50501 0.02393  -0.01755 0.04925  14  VAL C CG2 
100  N N   . TYR A 15  ? 0.45894 0.61269 0.51999 -0.00518 -0.01615 0.05170  15  TYR C N   
101  C CA  . TYR A 15  ? 0.37533 0.53903 0.46390 -0.01708 -0.01513 0.05640  15  TYR C CA  
102  C C   . TYR A 15  ? 0.40008 0.56810 0.51455 -0.02305 -0.03403 0.04912  15  TYR C C   
103  O O   . TYR A 15  ? 0.48868 0.63427 0.58292 -0.02061 -0.05364 0.04182  15  TYR C O   
104  C CB  . TYR A 15  ? 0.40570 0.54187 0.48405 -0.02055 -0.01286 0.05998  15  TYR C CB  
105  C CG  . TYR A 15  ? 0.40617 0.54653 0.51376 -0.03507 -0.01406 0.07001  15  TYR C CG  
106  C CD1 . TYR A 15  ? 0.35026 0.50890 0.46626 -0.04472 -0.00319 0.08786  15  TYR C CD1 
107  C CD2 . TYR A 15  ? 0.37651 0.49954 0.49837 -0.04277 -0.02722 0.06254  15  TYR C CD2 
108  C CE1 . TYR A 15  ? 0.41323 0.57179 0.55061 -0.06284 -0.00413 0.10188  15  TYR C CE1 
109  C CE2 . TYR A 15  ? 0.38731 0.51176 0.54033 -0.05817 -0.02861 0.07361  15  TYR C CE2 
110  C CZ  . TYR A 15  ? 0.44527 0.58698 0.60574 -0.06874 -0.01640 0.09522  15  TYR C CZ  
111  O OH  . TYR A 15  ? 0.71669 0.85603 0.90292 -0.08873 -0.01763 0.11092  15  TYR C OH  
112  N N   . GLN A 16  ? 0.44718 0.64375 0.60516 -0.03390 -0.02876 0.05149  16  GLN C N   
113  C CA  . GLN A 16  ? 0.50818 0.71596 0.70956 -0.04081 -0.04687 0.04392  16  GLN C CA  
114  C C   . GLN A 16  ? 0.52643 0.73641 0.75328 -0.05860 -0.04210 0.04977  16  GLN C C   
115  O O   . GLN A 16  ? 0.45820 0.67474 0.68052 -0.06818 -0.02109 0.06268  16  GLN C O   
116  C CB  . GLN A 16  ? 0.46549 0.71427 0.72000 -0.03792 -0.04271 0.03578  16  GLN C CB  
117  C CG  . GLN A 16  ? 0.42460 0.66900 0.66764 -0.02083 -0.05273 0.03116  16  GLN C CG  
118  C CD  . GLN A 16  ? 0.44445 0.72788 0.75982 -0.01640 -0.05165 0.01825  16  GLN C CD  
119  O OE1 . GLN A 16  ? 0.50960 0.79854 0.87630 -0.01481 -0.07982 0.01235  16  GLN C OE1 
120  N NE2 . GLN A 16  ? 0.39724 0.70783 0.72200 -0.01514 -0.02046 0.01135  16  GLN C NE2 
121  N N   A SER A 17  ? 0.59835 0.79957 0.85048 -0.06539 -0.06561 0.04219  17  SER C N   
122  N N   B SER A 17  ? 0.56167 0.76310 0.81405 -0.06540 -0.06559 0.04218  17  SER C N   
123  C CA  A SER A 17  ? 0.52828 0.72968 0.81422 -0.08393 -0.06515 0.04639  17  SER C CA  
124  C CA  B SER A 17  ? 0.51930 0.72061 0.80515 -0.08390 -0.06522 0.04636  17  SER C CA  
125  C C   A SER A 17  ? 0.62389 0.84450 0.96998 -0.09109 -0.08782 0.03485  17  SER C C   
126  C C   B SER A 17  ? 0.62414 0.84462 0.97016 -0.09111 -0.08788 0.03484  17  SER C C   
127  O O   A SER A 17  ? 0.66213 0.86975 1.00080 -0.08232 -0.11885 0.02449  17  SER C O   
128  O O   B SER A 17  ? 0.66232 0.86972 1.00087 -0.08239 -0.11897 0.02447  17  SER C O   
129  C CB  A SER A 17  ? 0.50484 0.65970 0.75692 -0.08598 -0.07465 0.04610  17  SER C CB  
130  C CB  B SER A 17  ? 0.53963 0.69423 0.79110 -0.08576 -0.07481 0.04594  17  SER C CB  
131  O OG  A SER A 17  ? 0.59681 0.72336 0.82035 -0.08005 -0.10102 0.02894  17  SER C OG  
132  O OG  B SER A 17  ? 0.53449 0.68556 0.82368 -0.10440 -0.07514 0.05237  17  SER C OG  
133  N N   . PRO A 18  ? 0.63822 0.88892 1.04538 -0.10947 -0.07498 0.03777  18  PRO C N   
134  C CA  . PRO A 18  ? 0.52883 0.79240 0.93892 -0.12763 -0.04081 0.05460  18  PRO C CA  
135  C C   . PRO A 18  ? 0.57611 0.87636 0.98146 -0.12694 -0.00689 0.05671  18  PRO C C   
136  O O   . PRO A 18  ? 0.67044 0.98720 1.08159 -0.10970 -0.00909 0.04309  18  PRO C O   
137  C CB  . PRO A 18  ? 0.52530 0.80870 1.00774 -0.15068 -0.04306 0.05251  18  PRO C CB  
138  C CG  . PRO A 18  ? 0.55349 0.86382 1.09456 -0.14104 -0.06546 0.03132  18  PRO C CG  
139  C CD  . PRO A 18  ? 0.50662 0.78095 0.98964 -0.11711 -0.09717 0.02511  18  PRO C CD  
140  N N   . GLY A 19  ? 0.47535 0.78554 0.86719 -0.14806 0.02318  0.07385  19  GLY C N   
141  C CA  . GLY A 19  ? 0.42356 0.76355 0.79474 -0.15311 0.05690  0.07428  19  GLY C CA  
142  C C   . GLY A 19  ? 0.42070 0.73212 0.71488 -0.14837 0.05978  0.09342  19  GLY C C   
143  O O   . GLY A 19  ? 0.69579 1.02495 0.95977 -0.16309 0.08666  0.10063  19  GLY C O   
144  N N   . ASP A 20  ? 0.38727 0.65575 0.65118 -0.13019 0.03314  0.09938  20  ASP C N   
145  C CA  . ASP A 20  ? 0.51296 0.75406 0.72121 -0.12341 0.03125  0.11608  20  ASP C CA  
146  C C   . ASP A 20  ? 0.44418 0.70729 0.62487 -0.11308 0.04658  0.10741  20  ASP C C   
147  O O   . ASP A 20  ? 0.81513 1.08279 0.95939 -0.12557 0.06025  0.12164  20  ASP C O   
148  C CB  . ASP A 20  ? 0.66653 0.89208 0.85830 -0.14961 0.03556  0.14733  20  ASP C CB  
149  C CG  . ASP A 20  ? 0.84150 1.03061 0.99576 -0.14033 0.02037  0.16620  20  ASP C CG  
150  O OD1 . ASP A 20  ? 0.95875 1.11562 1.12413 -0.12231 0.00087  0.15997  20  ASP C OD1 
151  O OD2 . ASP A 20  ? 1.04777 1.24081 1.16387 -0.15270 0.02776  0.18523  20  ASP C OD2 
152  N N   . ILE A 21  ? 0.46401 0.73760 0.66112 -0.09207 0.04067  0.08469  21  ILE C N   
153  C CA  . ILE A 21  ? 0.44026 0.73410 0.62521 -0.08082 0.05325  0.07195  21  ILE C CA  
154  C C   . ILE A 21  ? 0.44937 0.71240 0.59845 -0.05871 0.03728  0.07339  21  ILE C C   
155  O O   . ILE A 21  ? 0.54408 0.78410 0.69531 -0.04568 0.01760  0.06791  21  ILE C O   
156  C CB  . ILE A 21  ? 0.59316 0.91975 0.83510 -0.07386 0.05614  0.04698  21  ILE C CB  
157  C CG1 . ILE A 21  ? 0.52209 0.87792 0.81804 -0.09540 0.06924  0.04262  21  ILE C CG1 
158  C CG2 . ILE A 21  ? 0.66469 1.01673 0.90527 -0.06811 0.07635  0.03099  21  ILE C CG2 
159  C CD1 . ILE A 21  ? 0.55917 0.94821 0.93404 -0.08720 0.06635  0.01681  21  ILE C CD1 
160  N N   . GLY A 22  ? 0.44836 0.71093 0.56237 -0.05755 0.04641  0.07964  22  GLY C N   
161  C CA  . GLY A 22  ? 0.40394 0.64195 0.49239 -0.03929 0.03580  0.08041  22  GLY C CA  
162  C C   . GLY A 22  ? 0.42194 0.67685 0.49807 -0.03273 0.04633  0.07076  22  GLY C C   
163  O O   . GLY A 22  ? 0.52587 0.80935 0.60422 -0.04459 0.06384  0.06360  22  GLY C O   
164  N N   . GLN A 23  ? 0.41740 0.65367 0.48075 -0.01598 0.03810  0.06800  23  GLN C N   
165  C CA  . GLN A 23  ? 0.41617 0.66255 0.47151 -0.00871 0.04459  0.05883  23  GLN C CA  
166  C C   . GLN A 23  ? 0.36993 0.59026 0.40947 0.00379  0.03647  0.06353  23  GLN C C   
167  O O   . GLN A 23  ? 0.37917 0.57738 0.41772 0.01120  0.02918  0.06292  23  GLN C O   
168  C CB  . GLN A 23  ? 0.31894 0.58204 0.40545 -0.00034 0.04653  0.03938  23  GLN C CB  
169  C CG  . GLN A 23  ? 0.29588 0.56220 0.38158 0.00934  0.05002  0.02819  23  GLN C CG  
170  C CD  . GLN A 23  ? 0.45423 0.73427 0.58516 0.01831  0.04807  0.00943  23  GLN C CD  
171  O OE1 . GLN A 23  ? 0.39676 0.70586 0.56434 0.01190  0.05998  -0.00573 23  GLN C OE1 
172  N NE2 . GLN A 23  ? 0.32909 0.58756 0.46340 0.03177  0.03300  0.01057  23  GLN C NE2 
173  N N   . TYR A 24  ? 0.27940 0.50304 0.30611 0.00323  0.03889  0.06628  24  TYR C N   
174  C CA  . TYR A 24  ? 0.32794 0.53335 0.35224 0.01362  0.03465  0.06816  24  TYR C CA  
175  C C   . TYR A 24  ? 0.35235 0.56957 0.37538 0.01689  0.03835  0.05836  24  TYR C C   
176  O O   . TYR A 24  ? 0.42133 0.65570 0.43350 0.00687  0.04042  0.05688  24  TYR C O   
177  C CB  . TYR A 24  ? 0.34947 0.54266 0.37549 0.00954  0.02623  0.08387  24  TYR C CB  
178  C CG  . TYR A 24  ? 0.41288 0.58990 0.45447 0.02059  0.02591  0.08116  24  TYR C CG  
179  C CD1 . TYR A 24  ? 0.52766 0.68517 0.57606 0.02702  0.03270  0.07339  24  TYR C CD1 
180  C CD2 . TYR A 24  ? 0.45202 0.63426 0.50213 0.02184  0.02061  0.08356  24  TYR C CD2 
181  C CE1 . TYR A 24  ? 0.50269 0.64873 0.56816 0.03361  0.04077  0.06633  24  TYR C CE1 
182  C CE2 . TYR A 24  ? 0.37628 0.54820 0.45326 0.03062  0.02400  0.07862  24  TYR C CE2 
183  C CZ  . TYR A 24  ? 0.40332 0.55839 0.48901 0.03609  0.03740  0.06913  24  TYR C CZ  
184  O OH  . TYR A 24  ? 0.61597 0.76388 0.73083 0.04141  0.04886  0.05985  24  TYR C OH  
185  N N   . THR A 25  ? 0.37489 0.58039 0.40458 0.02766  0.03919  0.05148  25  THR C N   
186  C CA  . THR A 25  ? 0.36751 0.58025 0.40386 0.03120  0.04136  0.04096  25  THR C CA  
187  C C   . THR A 25  ? 0.39746 0.59196 0.43808 0.03712  0.04172  0.04400  25  THR C C   
188  O O   . THR A 25  ? 0.45194 0.62815 0.48860 0.03885  0.04470  0.04967  25  THR C O   
189  C CB  . THR A 25  ? 0.37231 0.59066 0.42550 0.03620  0.04187  0.02810  25  THR C CB  
190  O OG1 . THR A 25  ? 0.46825 0.66498 0.51945 0.04106  0.03421  0.03505  25  THR C OG1 
191  C CG2 . THR A 25  ? 0.39531 0.64020 0.45834 0.02872  0.04874  0.01771  25  THR C CG2 
192  N N   . PHE A 26  ? 0.54875 0.74926 0.59902 0.03786  0.04151  0.03686  26  PHE C N   
193  C CA  . PHE A 26  ? 0.48939 0.67614 0.55204 0.04108  0.04460  0.03755  26  PHE C CA  
194  C C   . PHE A 26  ? 0.49632 0.67831 0.56869 0.04418  0.04401  0.02886  26  PHE C C   
195  O O   . PHE A 26  ? 0.53479 0.73218 0.61616 0.04412  0.04122  0.01547  26  PHE C O   
196  C CB  . PHE A 26  ? 0.54261 0.73865 0.62066 0.03795  0.03907  0.03847  26  PHE C CB  
197  C CG  . PHE A 26  ? 0.49451 0.68256 0.59016 0.03906  0.04119  0.04705  26  PHE C CG  
198  C CD1 . PHE A 26  ? 0.67051 0.85393 0.75959 0.03886  0.04029  0.05443  26  PHE C CD1 
199  C CD2 . PHE A 26  ? 0.42203 0.60825 0.55151 0.03995  0.04507  0.04476  26  PHE C CD2 
200  C CE1 . PHE A 26  ? 0.53042 0.70595 0.64879 0.04125  0.04335  0.05690  26  PHE C CE1 
201  C CE2 . PHE A 26  ? 0.49939 0.68179 0.66175 0.04187  0.05040  0.04671  26  PHE C CE2 
202  C CZ  . PHE A 26  ? 0.50128 0.67764 0.65939 0.04337  0.04953  0.05155  26  PHE C CZ  
203  N N   . GLU A 27  ? 0.54189 0.70061 0.61251 0.04464  0.04742  0.03558  27  GLU C N   
204  C CA  . GLU A 27  ? 0.63726 0.78289 0.72043 0.04647  0.04144  0.03357  27  GLU C CA  
205  C C   . GLU A 27  ? 0.51436 0.64463 0.60649 0.04130  0.04858  0.03833  27  GLU C C   
206  O O   . GLU A 27  ? 0.57332 0.69836 0.65781 0.03572  0.06197  0.04422  27  GLU C O   
207  C CB  . GLU A 27  ? 0.65718 0.78153 0.72469 0.04689  0.03143  0.04394  27  GLU C CB  
208  C CG  . GLU A 27  ? 0.66978 0.81148 0.74890 0.05240  0.02216  0.03609  27  GLU C CG  
209  C CD  . GLU A 27  ? 0.86532 0.98516 0.94365 0.05346  0.00267  0.04654  27  GLU C CD  
210  O OE1 . GLU A 27  ? 0.90962 0.99742 0.97239 0.04852  -0.00623 0.06169  27  GLU C OE1 
211  O OE2 . GLU A 27  ? 0.93187 1.06543 1.02560 0.05689  -0.00579 0.04133  27  GLU C OE2 
212  N N   . PHE A 28  ? 0.61354 0.73731 0.73022 0.04243  0.04142  0.03313  28  PHE C N   
213  C CA  . PHE A 28  ? 0.52763 0.63257 0.65666 0.03480  0.04711  0.04004  28  PHE C CA  
214  C C   . PHE A 28  ? 0.63392 0.71543 0.78007 0.03597  0.03189  0.04386  28  PHE C C   
215  O O   . PHE A 28  ? 0.77534 0.86880 0.95585 0.04424  0.02170  0.02546  28  PHE C O   
216  C CB  . PHE A 28  ? 0.57991 0.70533 0.74047 0.03355  0.05076  0.02663  28  PHE C CB  
217  C CG  . PHE A 28  ? 0.63979 0.75025 0.82137 0.02346  0.06063  0.03326  28  PHE C CG  
218  C CD1 . PHE A 28  ? 0.56793 0.67898 0.74896 0.01531  0.08053  0.04009  28  PHE C CD1 
219  C CD2 . PHE A 28  ? 0.53440 0.63044 0.74392 0.02090  0.05240  0.03038  28  PHE C CD2 
220  C CE1 . PHE A 28  ? 0.52977 0.63059 0.73572 0.00278  0.09539  0.04432  28  PHE C CE1 
221  C CE2 . PHE A 28  ? 0.58786 0.66958 0.81919 0.00833  0.06297  0.03825  28  PHE C CE2 
222  C CZ  . PHE A 28  ? 0.58249 0.66819 0.81096 -0.00177 0.08619  0.04547  28  PHE C CZ  
223  N N   . ASP A 29  ? 0.63472 0.68086 0.75675 0.02569  0.03002  0.06698  29  ASP C N   
224  C CA  . ASP A 29  ? 0.75726 0.77148 0.89523 0.02483  0.00765  0.07946  29  ASP C CA  
225  C C   . ASP A 29  ? 0.77983 0.80127 0.94079 0.03958  -0.01512 0.07087  29  ASP C C   
226  O O   . ASP A 29  ? 1.00672 1.01825 1.21722 0.04715  -0.03434 0.06500  29  ASP C O   
227  C CB  . ASP A 29  ? 0.89612 0.90568 1.08338 0.02386  0.00600  0.07070  29  ASP C CB  
228  C CG  . ASP A 29  ? 0.90498 0.89867 1.07903 0.00513  0.02531  0.08547  29  ASP C CG  
229  O OD1 . ASP A 29  ? 0.85325 0.82438 0.97581 -0.01057 0.03616  0.10834  29  ASP C OD1 
230  O OD2 . ASP A 29  ? 0.89280 0.89718 1.10836 0.00381  0.03112  0.07190  29  ASP C OD2 
231  N N   . GLY A 30  ? 0.66648 0.70585 0.80179 0.04354  -0.01247 0.06793  30  GLY C N   
232  C CA  . GLY A 30  ? 0.72337 0.77306 0.88558 0.05508  -0.03106 0.05980  30  GLY C CA  
233  C C   . GLY A 30  ? 0.60358 0.69634 0.80681 0.06626  -0.01999 0.02612  30  GLY C C   
234  O O   . GLY A 30  ? 0.55997 0.66981 0.78695 0.07354  -0.02665 0.01548  30  GLY C O   
235  N N   . ASP A 31  ? 0.49802 0.60867 0.70876 0.06484  -0.00342 0.00849  31  ASP C N   
236  C CA  . ASP A 31  ? 0.43968 0.58778 0.67132 0.06856  0.00866  -0.02369 31  ASP C CA  
237  C C   . ASP A 31  ? 0.59739 0.76814 0.78372 0.06177  0.02318  -0.02137 31  ASP C C   
238  O O   . ASP A 31  ? 0.61089 0.77157 0.76637 0.05623  0.02690  -0.00312 31  ASP C O   
239  C CB  . ASP A 31  ? 0.50824 0.65889 0.77096 0.06782  0.01185  -0.04603 31  ASP C CB  
240  C CG  . ASP A 31  ? 0.65685 0.78564 0.97998 0.07589  -0.00398 -0.05344 31  ASP C CG  
241  O OD1 . ASP A 31  ? 0.60587 0.73676 0.96569 0.08500  -0.01372 -0.05959 31  ASP C OD1 
242  O OD2 . ASP A 31  ? 0.75702 0.86576 1.09943 0.07297  -0.00889 -0.05271 31  ASP C OD2 
243  N N   . GLU A 32  ? 0.54607 0.74684 0.73363 0.06069  0.03221  -0.04066 32  GLU C N   
244  C CA  . GLU A 32  ? 0.51237 0.73042 0.65872 0.05231  0.04091  -0.03396 32  GLU C CA  
245  C C   . GLU A 32  ? 0.49788 0.72545 0.62612 0.04338  0.04376  -0.04075 32  GLU C C   
246  O O   . GLU A 32  ? 0.47401 0.71648 0.60960 0.03836  0.04850  -0.06642 32  GLU C O   
247  C CB  . GLU A 32  ? 0.51139 0.75562 0.66225 0.04924  0.05032  -0.04842 32  GLU C CB  
248  C CG  . GLU A 32  ? 0.44841 0.70280 0.55802 0.03908  0.05514  -0.03366 32  GLU C CG  
249  C CD  . GLU A 32  ? 0.62679 0.91130 0.73242 0.02742  0.07108  -0.05159 32  GLU C CD  
250  O OE1 . GLU A 32  ? 0.70266 1.00259 0.79171 0.01564  0.08133  -0.07043 32  GLU C OE1 
251  O OE2 . GLU A 32  ? 0.77882 1.07140 0.89576 0.02710  0.07434  -0.04805 32  GLU C OE2 
252  N N   . LEU A 33  ? 0.50759 0.72645 0.61601 0.04042  0.03974  -0.02030 33  LEU C N   
253  C CA  . LEU A 33  ? 0.45366 0.68212 0.54985 0.03124  0.03415  -0.02226 33  LEU C CA  
254  C C   . LEU A 33  ? 0.47886 0.72707 0.53993 0.01887  0.03451  -0.02540 33  LEU C C   
255  O O   . LEU A 33  ? 0.51368 0.77458 0.55739 0.00692  0.03295  -0.04264 33  LEU C O   
256  C CB  . LEU A 33  ? 0.44078 0.65711 0.54303 0.03258  0.02943  -0.00125 33  LEU C CB  
257  C CG  . LEU A 33  ? 0.53800 0.73818 0.67057 0.03594  0.03190  0.00034  33  LEU C CG  
258  C CD1 . LEU A 33  ? 0.41215 0.60485 0.55577 0.03594  0.03692  0.01614  33  LEU C CD1 
259  C CD2 . LEU A 33  ? 0.38400 0.59120 0.53553 0.03080  0.02290  -0.01591 33  LEU C CD2 
260  N N   . PHE A 34  ? 0.59102 0.83967 0.63651 0.01817  0.03674  -0.00901 34  PHE C N   
261  C CA  . PHE A 34  ? 0.56176 0.82509 0.57130 0.00259  0.03784  -0.00589 34  PHE C CA  
262  C C   . PHE A 34  ? 0.45207 0.71352 0.46186 0.00550  0.04384  0.00737  34  PHE C C   
263  O O   . PHE A 34  ? 0.57284 0.82009 0.60381 0.01875  0.04381  0.01412  34  PHE C O   
264  C CB  . PHE A 34  ? 0.63411 0.89346 0.62045 -0.00906 0.01771  0.01203  34  PHE C CB  
265  C CG  . PHE A 34  ? 0.57086 0.81348 0.58384 0.00169  0.00608  0.03474  34  PHE C CG  
266  C CD1 . PHE A 34  ? 0.50467 0.74005 0.51503 0.00204  0.00480  0.05333  34  PHE C CD1 
267  C CD2 . PHE A 34  ? 0.53426 0.76928 0.58130 0.00996  -0.00077 0.03388  34  PHE C CD2 
268  C CE1 . PHE A 34  ? 0.55546 0.77617 0.59761 0.01170  -0.00148 0.06650  34  PHE C CE1 
269  C CE2 . PHE A 34  ? 0.54701 0.77055 0.62700 0.01828  -0.00423 0.04793  34  PHE C CE2 
270  C CZ  . PHE A 34  ? 0.51146 0.72776 0.58940 0.01974  -0.00385 0.06224  34  PHE C CZ  
271  N N   . TYR A 35  ? 0.46324 0.73745 0.44436 -0.01067 0.04863  0.01118  35  TYR C N   
272  C CA  . TYR A 35  ? 0.50490 0.77626 0.48544 -0.01235 0.05057  0.02712  35  TYR C CA  
273  C C   . TYR A 35  ? 0.54651 0.81527 0.48990 -0.03214 0.04000  0.04957  35  TYR C C   
274  O O   . TYR A 35  ? 0.62163 0.89817 0.52795 -0.05068 0.03724  0.04773  35  TYR C O   
275  C CB  . TYR A 35  ? 0.35356 0.64428 0.35121 -0.01412 0.06962  0.00892  35  TYR C CB  
276  C CG  . TYR A 35  ? 0.38876 0.70534 0.36152 -0.03673 0.08879  -0.00772 35  TYR C CG  
277  C CD1 . TYR A 35  ? 0.47945 0.81172 0.45737 -0.03909 0.10253  -0.03953 35  TYR C CD1 
278  C CD2 . TYR A 35  ? 0.40436 0.72826 0.34737 -0.05875 0.09583  0.00643  35  TYR C CD2 
279  C CE1 . TYR A 35  ? 0.40175 0.75840 0.35097 -0.06378 0.12677  -0.06122 35  TYR C CE1 
280  C CE2 . TYR A 35  ? 0.41779 0.76498 0.32794 -0.08568 0.11928  -0.00957 35  TYR C CE2 
281  C CZ  . TYR A 35  ? 0.43355 0.79818 0.34458 -0.08860 0.13676  -0.04566 35  TYR C CZ  
282  O OH  . TYR A 35  ? 0.51632 0.90493 0.38903 -0.11921 0.16656  -0.06792 35  TYR C OH  
283  N N   . VAL A 36  ? 0.52787 0.78196 0.47920 -0.03018 0.03135  0.07129  36  VAL C N   
284  C CA  . VAL A 36  ? 0.49473 0.73895 0.42050 -0.04822 0.01534  0.09872  36  VAL C CA  
285  C C   . VAL A 36  ? 0.44309 0.69950 0.34977 -0.06718 0.03137  0.10119  36  VAL C C   
286  O O   . VAL A 36  ? 0.64946 0.90539 0.58403 -0.05918 0.03962  0.09878  36  VAL C O   
287  C CB  . VAL A 36  ? 0.53322 0.75228 0.49211 -0.03513 -0.00347 0.11808  36  VAL C CB  
288  C CG1 . VAL A 36  ? 0.47992 0.68418 0.42293 -0.05356 -0.02584 0.14966  36  VAL C CG1 
289  C CG2 . VAL A 36  ? 0.61356 0.82567 0.60038 -0.01907 -0.01327 0.11237  36  VAL C CG2 
290  N N   . ASP A 37  ? 0.50251 0.76982 0.35948 -0.09552 0.03650  0.10495  37  ASP C N   
291  C CA  . ASP A 37  ? 0.58650 0.86643 0.42180 -0.12073 0.05592  0.10938  37  ASP C CA  
292  C C   . ASP A 37  ? 0.75059 1.00443 0.59072 -0.12683 0.03451  0.14630  37  ASP C C   
293  O O   . ASP A 37  ? 0.75181 0.98411 0.55989 -0.14284 0.00790  0.17741  37  ASP C O   
294  C CB  . ASP A 37  ? 0.54491 0.83905 0.31222 -0.15576 0.06905  0.10461  37  ASP C CB  
295  C CG  . ASP A 37  ? 0.80459 1.11634 0.55035 -0.18625 0.09917  0.10388  37  ASP C CG  
296  O OD1 . ASP A 37  ? 0.99531 1.31289 0.78920 -0.17735 0.10925  0.10412  37  ASP C OD1 
297  O OD2 . ASP A 37  ? 0.83100 1.13765 0.52551 -0.21273 0.10758  0.09694  37  ASP C OD2 
298  N N   . LEU A 38  ? 0.62836 0.88141 0.51252 -0.11467 0.04195  0.14308  38  LEU C N   
299  C CA  . LEU A 38  ? 0.61247 0.83789 0.51352 -0.11686 0.02179  0.17213  38  LEU C CA  
300  C C   . LEU A 38  ? 0.72948 0.94959 0.58951 -0.15450 0.02067  0.20156  38  LEU C C   
301  O O   . LEU A 38  ? 0.70271 0.89205 0.56977 -0.16085 -0.00559 0.23397  38  LEU C O   
302  C CB  . LEU A 38  ? 0.49984 0.72577 0.45126 -0.09862 0.03012  0.15703  38  LEU C CB  
303  C CG  . LEU A 38  ? 0.40063 0.62633 0.38166 -0.06712 0.03070  0.13212  38  LEU C CG  
304  C CD1 . LEU A 38  ? 0.40833 0.62601 0.42460 -0.05562 0.03076  0.12304  38  LEU C CD1 
305  C CD2 . LEU A 38  ? 0.47853 0.68261 0.46288 -0.05267 0.01152  0.14004  38  LEU C CD2 
306  N N   . ASP A 39  ? 0.62214 0.86996 0.44177 -0.18155 0.04980  0.19029  39  ASP C N   
307  C CA  . ASP A 39  ? 0.74958 0.99054 0.51899 -0.22307 0.05382  0.21669  39  ASP C CA  
308  C C   . ASP A 39  ? 0.85786 1.07255 0.56636 -0.23904 0.02656  0.23448  39  ASP C C   
309  O O   . ASP A 39  ? 0.95616 1.13856 0.64304 -0.25827 0.00051  0.26884  39  ASP C O   
310  C CB  . ASP A 39  ? 0.81588 1.08951 0.58402 -0.23830 0.09906  0.18201  39  ASP C CB  
311  C CG  . ASP A 39  ? 1.09414 1.39506 0.93327 -0.22549 0.12016  0.16539  39  ASP C CG  
312  O OD1 . ASP A 39  ? 1.27893 1.59199 1.16513 -0.19163 0.11988  0.13839  39  ASP C OD1 
313  O OD2 . ASP A 39  ? 1.14368 1.44354 0.99805 -0.24375 0.13032  0.17501  39  ASP C OD2 
314  N N   . LYS A 40  ? 0.79488 1.02232 0.47918 -0.23260 0.02931  0.21166  40  LYS C N   
315  C CA  . LYS A 40  ? 0.82006 1.02468 0.45024 -0.24844 -0.00040 0.22670  40  LYS C CA  
316  C C   . LYS A 40  ? 0.95710 1.13832 0.61495 -0.22714 -0.04713 0.25206  40  LYS C C   
317  O O   . LYS A 40  ? 0.82895 0.98636 0.45657 -0.23969 -0.08199 0.27127  40  LYS C O   
318  C CB  . LYS A 40  ? 0.89492 1.12316 0.48665 -0.25585 0.02482  0.18722  40  LYS C CB  
319  C CG  . LYS A 40  ? 0.88349 1.13126 0.44834 -0.28069 0.06909  0.16035  40  LYS C CG  
320  C CD  . LYS A 40  ? 0.87190 1.13977 0.40750 -0.28662 0.09245  0.11803  40  LYS C CD  
321  C CE  . LYS A 40  ? 1.27812 1.56591 0.79597 -0.31132 0.13851  0.08848  40  LYS C CE  
322  N NZ  . LYS A 40  ? 1.30730 1.61318 0.80328 -0.31767 0.16224  0.04342  40  LYS C NZ  
323  N N   . LYS A 41  ? 0.90408 1.09169 0.62385 -0.19552 -0.04869 0.25098  41  LYS C N   
324  C CA  . LYS A 41  ? 0.76873 0.93319 0.54242 -0.16731 -0.08666 0.26251  41  LYS C CA  
325  C C   . LYS A 41  ? 0.76983 0.94031 0.52303 -0.16453 -0.10229 0.25166  41  LYS C C   
326  O O   . LYS A 41  ? 0.86605 1.01447 0.62566 -0.16626 -0.14618 0.27738  41  LYS C O   
327  C CB  . LYS A 41  ? 0.68034 0.80626 0.46619 -0.17904 -0.12926 0.31031  41  LYS C CB  
328  C CG  . LYS A 41  ? 0.75920 0.87586 0.56486 -0.18599 -0.11603 0.32217  41  LYS C CG  
329  C CD  . LYS A 41  ? 1.09042 1.16458 0.92000 -0.19551 -0.15763 0.35936  41  LYS C CD  
330  C CE  . LYS A 41  ? 1.01997 1.08387 0.87090 -0.20432 -0.14519 0.37056  41  LYS C CE  
331  N NZ  . LYS A 41  ? 1.32686 1.34888 1.20581 -0.21429 -0.18608 0.40453  41  LYS C NZ  
332  N N   . GLU A 42  ? 0.66954 0.86962 0.40674 -0.16002 -0.06864 0.21223  42  GLU C N   
333  C CA  . GLU A 42  ? 0.63900 0.84665 0.35607 -0.15959 -0.07869 0.19553  42  GLU C CA  
334  C C   . GLU A 42  ? 0.72070 0.94941 0.48807 -0.12792 -0.05013 0.15358  42  GLU C C   
335  O O   . GLU A 42  ? 0.74365 0.98734 0.53453 -0.11682 -0.01723 0.13319  42  GLU C O   
336  C CB  . GLU A 42  ? 0.77316 0.98975 0.39732 -0.19972 -0.06872 0.18922  42  GLU C CB  
337  C CG  . GLU A 42  ? 1.31677 1.49888 0.90103 -0.22838 -0.09751 0.22307  42  GLU C CG  
338  C CD  . GLU A 42  ? 1.60180 1.78650 1.10829 -0.26348 -0.07859 0.20524  42  GLU C CD  
339  O OE1 . GLU A 42  ? 1.58178 1.79504 1.07503 -0.26351 -0.04004 0.16251  42  GLU C OE1 
340  O OE2 . GLU A 42  ? 1.57163 1.72928 1.03385 -0.29158 -0.10223 0.23292  42  GLU C OE2 
341  N N   . THR A 43  ? 0.67050 0.89820 0.45692 -0.11529 -0.06687 0.14330  43  THR C N   
342  C CA  . THR A 43  ? 0.54553 0.78732 0.37598 -0.08928 -0.04499 0.10863  43  THR C CA  
343  C C   . THR A 43  ? 0.52096 0.78352 0.31043 -0.10364 -0.02239 0.07509  43  THR C C   
344  O O   . THR A 43  ? 0.63859 0.90050 0.37381 -0.12795 -0.03749 0.07519  43  THR C O   
345  C CB  . THR A 43  ? 0.64406 0.87506 0.52483 -0.07052 -0.07069 0.11278  43  THR C CB  
346  O OG1 . THR A 43  ? 0.58187 0.79598 0.51256 -0.05596 -0.08446 0.13538  43  THR C OG1 
347  C CG2 . THR A 43  ? 0.54275 0.78424 0.46176 -0.04914 -0.04824 0.08108  43  THR C CG2 
348  N N   . VAL A 44  ? 0.66515 0.94435 0.48285 -0.08970 0.01145  0.04508  44  VAL C N   
349  C CA  . VAL A 44  ? 0.65581 0.95637 0.45544 -0.09957 0.03830  0.00575  44  VAL C CA  
350  C C   . VAL A 44  ? 0.60152 0.90259 0.46033 -0.07172 0.04278  -0.01883 44  VAL C C   
351  O O   . VAL A 44  ? 0.74605 1.04684 0.65446 -0.04987 0.05401  -0.02250 44  VAL C O   
352  C CB  . VAL A 44  ? 0.53783 0.85942 0.33211 -0.11065 0.07412  -0.00976 44  VAL C CB  
353  C CG1 . VAL A 44  ? 0.53445 0.88025 0.31811 -0.12284 0.10527  -0.05689 44  VAL C CG1 
354  C CG2 . VAL A 44  ? 0.63412 0.95052 0.37288 -0.13993 0.06973  0.02164  44  VAL C CG2 
355  N N   . TRP A 45  ? 0.60205 0.90105 0.45325 -0.07523 0.03108  -0.03392 45  TRP C N   
356  C CA  . TRP A 45  ? 0.58970 0.88550 0.49612 -0.05300 0.03351  -0.05494 45  TRP C CA  
357  C C   . TRP A 45  ? 0.50467 0.81748 0.42839 -0.05248 0.06319  -0.09764 45  TRP C C   
358  O O   . TRP A 45  ? 0.57239 0.90118 0.45431 -0.07545 0.07967  -0.12295 45  TRP C O   
359  C CB  . TRP A 45  ? 0.68142 0.96793 0.58361 -0.05772 0.00693  -0.05480 45  TRP C CB  
360  C CG  . TRP A 45  ? 0.61888 0.89112 0.52467 -0.05665 -0.02469 -0.01688 45  TRP C CG  
361  C CD1 . TRP A 45  ? 0.48817 0.75534 0.34778 -0.07651 -0.04803 0.00968  45  TRP C CD1 
362  C CD2 . TRP A 45  ? 0.52542 0.78594 0.49131 -0.03594 -0.03620 -0.00243 45  TRP C CD2 
363  N NE1 . TRP A 45  ? 0.67193 0.92560 0.57194 -0.06564 -0.07629 0.03819  45  TRP C NE1 
364  C CE2 . TRP A 45  ? 0.55389 0.80595 0.51962 -0.04124 -0.06539 0.02825  45  TRP C CE2 
365  C CE3 . TRP A 45  ? 0.48157 0.73663 0.50187 -0.01603 -0.02377 -0.01205 45  TRP C CE3 
366  C CZ2 . TRP A 45  ? 0.56316 0.80681 0.59112 -0.02543 -0.07707 0.04261  45  TRP C CZ2 
367  C CZ3 . TRP A 45  ? 0.48238 0.72769 0.54908 -0.00469 -0.03286 0.00494  45  TRP C CZ3 
368  C CH2 . TRP A 45  ? 0.61725 0.85955 0.69230 -0.00846 -0.05666 0.02863  45  TRP C CH2 
369  N N   . MET A 46  ? 0.61249 0.92027 0.59964 -0.02797 0.06976  -0.10636 46  MET C N   
370  C CA  . MET A 46  ? 0.54551 0.86636 0.57219 -0.02303 0.09201  -0.14741 46  MET C CA  
371  C C   . MET A 46  ? 0.51172 0.83214 0.53659 -0.03068 0.09060  -0.18018 46  MET C C   
372  O O   . MET A 46  ? 0.71631 1.05472 0.73473 -0.04399 0.11351  -0.22200 46  MET C O   
373  C CB  . MET A 46  ? 0.53107 0.83910 0.62577 0.00351  0.08855  -0.14085 46  MET C CB  
374  C CG  . MET A 46  ? 0.44519 0.76201 0.60217 0.01266  0.10316  -0.18072 46  MET C CG  
375  S SD  . MET A 46  ? 0.92023 1.21860 1.15048 0.03908  0.08952  -0.16415 46  MET C SD  
376  C CE  . MET A 46  ? 0.66575 0.98257 0.87977 0.03428  0.09869  -0.14764 46  MET C CE  
377  N N   . LEU A 47  ? 0.71696 1.01791 0.75122 -0.02408 0.06619  -0.16540 47  LEU C N   
378  C CA  . LEU A 47  ? 0.74362 1.04205 0.77296 -0.03419 0.05859  -0.19330 47  LEU C CA  
379  C C   . LEU A 47  ? 0.78587 1.08677 0.74049 -0.05991 0.03998  -0.18032 47  LEU C C   
380  O O   . LEU A 47  ? 0.92223 1.21199 0.87199 -0.05701 0.01449  -0.14167 47  LEU C O   
381  C CB  . LEU A 47  ? 0.71707 0.99360 0.80297 -0.01666 0.04104  -0.18378 47  LEU C CB  
382  C CG  . LEU A 47  ? 0.72909 0.99397 0.88656 0.00467  0.05015  -0.19413 47  LEU C CG  
383  C CD1 . LEU A 47  ? 0.70323 0.94290 0.90214 0.01407  0.03267  -0.17816 47  LEU C CD1 
384  C CD2 . LEU A 47  ? 0.47581 0.75274 0.66035 0.00196  0.06953  -0.24628 47  LEU C CD2 
385  N N   . PRO A 48  ? 0.82305 1.13674 0.71922 -0.08709 0.05045  -0.21126 48  PRO C N   
386  C CA  . PRO A 48  ? 0.86882 1.17883 0.68312 -0.11622 0.02410  -0.19264 48  PRO C CA  
387  C C   . PRO A 48  ? 0.88119 1.17527 0.71195 -0.11421 -0.01626 -0.18021 48  PRO C C   
388  O O   . PRO A 48  ? 0.99207 1.27823 0.78305 -0.12866 -0.05106 -0.14768 48  PRO C O   
389  C CB  . PRO A 48  ? 0.82872 1.15369 0.57569 -0.14864 0.04967  -0.23869 48  PRO C CB  
390  C CG  . PRO A 48  ? 0.86593 1.20930 0.66502 -0.13457 0.09573  -0.27276 48  PRO C CG  
391  C CD  . PRO A 48  ? 0.88027 1.21196 0.78083 -0.09528 0.08771  -0.26472 48  PRO C CD  
392  N N   . GLU A 49  ? 0.95723 1.24551 0.85346 -0.09743 -0.01507 -0.20395 49  GLU C N   
393  C CA  . GLU A 49  ? 0.86789 1.14372 0.79225 -0.09642 -0.05095 -0.19390 49  GLU C CA  
394  C C   . GLU A 49  ? 0.80770 1.07564 0.77708 -0.07798 -0.06940 -0.14558 49  GLU C C   
395  O O   . GLU A 49  ? 0.87205 1.13487 0.85321 -0.08329 -0.10427 -0.12682 49  GLU C O   
396  C CB  . GLU A 49  ? 0.93973 1.20910 0.92830 -0.08481 -0.04211 -0.23041 49  GLU C CB  
397  C CG  . GLU A 49  ? 1.16689 1.44417 1.13160 -0.09883 -0.01711 -0.28787 49  GLU C CG  
398  C CD  . GLU A 49  ? 1.15431 1.43989 1.15648 -0.08157 0.02286  -0.30586 49  GLU C CD  
399  O OE1 . GLU A 49  ? 1.08419 1.36113 1.14794 -0.05527 0.02534  -0.27940 49  GLU C OE1 
400  O OE2 . GLU A 49  ? 1.35411 1.65502 1.32509 -0.09631 0.05151  -0.34753 49  GLU C OE2 
401  N N   . PHE A 50  ? 0.69164 0.95898 0.69057 -0.05749 -0.04689 -0.12800 50  PHE C N   
402  C CA  . PHE A 50  ? 0.71247 0.97231 0.75117 -0.04216 -0.05738 -0.08929 50  PHE C CA  
403  C C   . PHE A 50  ? 0.80763 1.06878 0.80667 -0.05432 -0.08164 -0.05824 50  PHE C C   
404  O O   . PHE A 50  ? 0.80331 1.05953 0.84000 -0.04922 -0.10526 -0.03362 50  PHE C O   
405  C CB  . PHE A 50  ? 0.61572 0.87122 0.68352 -0.02156 -0.02910 -0.08118 50  PHE C CB  
406  C CG  . PHE A 50  ? 0.61602 0.86002 0.73982 -0.00749 -0.01736 -0.09386 50  PHE C CG  
407  C CD1 . PHE A 50  ? 0.70167 0.94196 0.85047 -0.01282 -0.02652 -0.11711 50  PHE C CD1 
408  C CD2 . PHE A 50  ? 0.63483 0.86789 0.78350 0.00825  -0.00076 -0.08031 50  PHE C CD2 
409  C CE1 . PHE A 50  ? 0.47589 0.70073 0.67810 -0.00224 -0.01811 -0.12435 50  PHE C CE1 
410  C CE2 . PHE A 50  ? 0.66531 0.88155 0.85836 0.01698  0.00521  -0.08518 50  PHE C CE2 
411  C CZ  . PHE A 50  ? 0.55521 0.76677 0.77754 0.01197  -0.00294 -0.10594 50  PHE C CZ  
412  N N   . GLY A 51  ? 0.80510 1.07224 0.73444 -0.07181 -0.07590 -0.05904 51  GLY C N   
413  C CA  . GLY A 51  ? 0.58288 0.84540 0.46780 -0.08830 -0.10398 -0.02586 51  GLY C CA  
414  C C   . GLY A 51  ? 0.76042 1.01656 0.62664 -0.10757 -0.15050 -0.01821 51  GLY C C   
415  O O   . GLY A 51  ? 0.81972 1.06649 0.68454 -0.11375 -0.18690 0.01760  51  GLY C O   
416  N N   . GLN A 52  ? 0.84634 1.10552 0.70336 -0.11759 -0.15402 -0.05153 52  GLN C N   
417  C CA  . GLN A 52  ? 0.75936 1.01183 0.60163 -0.13713 -0.20334 -0.04716 52  GLN C CA  
418  C C   . GLN A 52  ? 0.80420 1.05467 0.74796 -0.11659 -0.22891 -0.03197 52  GLN C C   
419  O O   . GLN A 52  ? 0.85747 1.10285 0.80977 -0.12936 -0.27911 -0.01719 52  GLN C O   
420  C CB  . GLN A 52  ? 0.78906 1.04476 0.58689 -0.15701 -0.19692 -0.09410 52  GLN C CB  
421  C CG  . GLN A 52  ? 1.10812 1.36649 0.79216 -0.18997 -0.18007 -0.11184 52  GLN C CG  
422  C CD  . GLN A 52  ? 1.39854 1.64393 0.99936 -0.22173 -0.22465 -0.07212 52  GLN C CD  
423  O OE1 . GLN A 52  ? 1.41258 1.65583 0.97621 -0.22770 -0.21534 -0.04326 52  GLN C OE1 
424  N NE2 . GLN A 52  ? 1.21925 1.45316 0.79210 -0.24399 -0.27770 -0.06824 52  GLN C NE2 
425  N N   . LEU A 53  ? 0.65835 0.91251 0.67912 -0.08793 -0.19619 -0.03537 53  LEU C N   
426  C CA  . LEU A 53  ? 0.57521 0.83040 0.69501 -0.07128 -0.20778 -0.02616 53  LEU C CA  
427  C C   . LEU A 53  ? 0.55910 0.81340 0.72870 -0.05382 -0.20375 0.00535  53  LEU C C   
428  O O   . LEU A 53  ? 0.79404 1.04966 1.02463 -0.05152 -0.23572 0.02369  53  LEU C O   
429  C CB  . LEU A 53  ? 0.69003 0.94591 0.85821 -0.05756 -0.17313 -0.05328 53  LEU C CB  
430  C CG  . LEU A 53  ? 0.64106 0.89585 0.77657 -0.07185 -0.17320 -0.09141 53  LEU C CG  
431  C CD1 . LEU A 53  ? 0.66057 0.91004 0.85052 -0.05681 -0.14052 -0.11224 53  LEU C CD1 
432  C CD2 . LEU A 53  ? 0.56554 0.82091 0.70499 -0.09125 -0.22172 -0.09630 53  LEU C CD2 
433  N N   . ALA A 54  ? 0.63466 0.88692 0.78631 -0.04173 -0.16615 0.00908  54  ALA C N   
434  C CA  . ALA A 54  ? 0.57025 0.81958 0.76316 -0.02643 -0.15741 0.03239  54  ALA C CA  
435  C C   . ALA A 54  ? 0.60062 0.84373 0.73514 -0.03596 -0.17141 0.05530  54  ALA C C   
436  O O   . ALA A 54  ? 0.80035 1.04228 0.85705 -0.05685 -0.18446 0.05442  54  ALA C O   
437  C CB  . ALA A 54  ? 0.57432 0.82150 0.78774 -0.00899 -0.10977 0.02246  54  ALA C CB  
438  N N   . SER A 55  ? 0.64514 0.88293 0.81714 -0.02315 -0.16632 0.07455  55  SER C N   
439  C CA  . SER A 55  ? 0.61588 0.84406 0.74447 -0.03129 -0.17865 0.09915  55  SER C CA  
440  C C   . SER A 55  ? 0.49089 0.71402 0.66177 -0.01206 -0.15110 0.10436  55  SER C C   
441  O O   . SER A 55  ? 0.42947 0.65587 0.66146 0.00454  -0.12737 0.09131  55  SER C O   
442  C CB  . SER A 55  ? 0.48639 0.70516 0.62182 -0.04561 -0.23639 0.12764  55  SER C CB  
443  O OG  . SER A 55  ? 0.76050 0.98063 1.00270 -0.02945 -0.25445 0.13317  55  SER C OG  
444  N N   . PHE A 56  ? 0.64474 0.85838 0.77798 -0.01801 -0.15333 0.12270  56  PHE C N   
445  C CA  . PHE A 56  ? 0.43527 0.64154 0.59903 -0.00298 -0.12927 0.12527  56  PHE C CA  
446  C C   . PHE A 56  ? 0.49052 0.68221 0.62890 -0.01425 -0.15196 0.15393  56  PHE C C   
447  O O   . PHE A 56  ? 0.66785 0.85911 0.73054 -0.03505 -0.15820 0.16366  56  PHE C O   
448  C CB  . PHE A 56  ? 0.44346 0.65521 0.57522 0.00371  -0.08498 0.10397  56  PHE C CB  
449  C CG  . PHE A 56  ? 0.40139 0.60338 0.54758 0.01427  -0.06368 0.10563  56  PHE C CG  
450  C CD1 . PHE A 56  ? 0.46485 0.66183 0.66801 0.02912  -0.04589 0.09534  56  PHE C CD1 
451  C CD2 . PHE A 56  ? 0.43857 0.63673 0.54014 0.00635  -0.05907 0.11455  56  PHE C CD2 
452  C CE1 . PHE A 56  ? 0.41742 0.60317 0.62564 0.03571  -0.02635 0.09239  56  PHE C CE1 
453  C CE2 . PHE A 56  ? 0.43370 0.62153 0.54897 0.01461  -0.04277 0.11390  56  PHE C CE2 
454  C CZ  . PHE A 56  ? 0.37663 0.55696 0.54164 0.02925  -0.02757 0.10198  56  PHE C CZ  
455  N N   . ASP A 57  ? 0.52656 0.70561 0.73077 -0.00257 -0.16189 0.16564  57  ASP C N   
456  C CA  . ASP A 57  ? 0.52997 0.68961 0.72342 -0.01220 -0.18557 0.19505  57  ASP C CA  
457  C C   . ASP A 57  ? 0.58757 0.74606 0.73615 -0.01327 -0.14966 0.18815  57  ASP C C   
458  O O   . ASP A 57  ? 0.59983 0.75819 0.78321 0.00396  -0.11894 0.16862  57  ASP C O   
459  C CB  . ASP A 57  ? 0.51630 0.66185 0.81231 0.00317  -0.20749 0.20420  57  ASP C CB  
460  C CG  . ASP A 57  ? 0.66294 0.78227 0.95818 -0.00981 -0.24989 0.24295  57  ASP C CG  
461  O OD1 . ASP A 57  ? 0.70414 0.81558 0.92094 -0.02815 -0.24508 0.25840  57  ASP C OD1 
462  O OD2 . ASP A 57  ? 0.95677 1.06262 1.33682 -0.00264 -0.28872 0.25844  57  ASP C OD2 
463  N N   . PRO A 58  ? 0.58167 0.73957 0.65283 -0.03590 -0.15206 0.20250  58  PRO C N   
464  C CA  . PRO A 58  ? 0.50607 0.66738 0.54577 -0.03756 -0.11842 0.19380  58  PRO C CA  
465  C C   . PRO A 58  ? 0.56699 0.70788 0.64814 -0.03098 -0.12196 0.20636  58  PRO C C   
466  O O   . PRO A 58  ? 0.59621 0.73951 0.67231 -0.02583 -0.09368 0.19227  58  PRO C O   
467  C CB  . PRO A 58  ? 0.53774 0.70564 0.49328 -0.06812 -0.12058 0.20603  58  PRO C CB  
468  C CG  . PRO A 58  ? 0.54379 0.69656 0.48348 -0.08618 -0.16756 0.23643  58  PRO C CG  
469  C CD  . PRO A 58  ? 0.51628 0.67072 0.52327 -0.06454 -0.18437 0.22588  58  PRO C CD  
470  N N   . GLN A 59  ? 0.71825 0.83756 0.84621 -0.03110 -0.15901 0.23139  59  GLN C N   
471  C CA  . GLN A 59  ? 0.60626 0.70308 0.78498 -0.02390 -0.16302 0.23944  59  GLN C CA  
472  C C   . GLN A 59  ? 0.54853 0.64907 0.78213 0.00168  -0.12866 0.20288  59  GLN C C   
473  O O   . GLN A 59  ? 0.77389 0.86090 1.02655 0.00589  -0.11626 0.19625  59  GLN C O   
474  C CB  . GLN A 59  ? 0.50640 0.57753 0.74214 -0.02643 -0.21414 0.27192  59  GLN C CB  
475  C CG  . GLN A 59  ? 0.84331 0.89943 1.01210 -0.05908 -0.25367 0.31677  59  GLN C CG  
476  C CD  . GLN A 59  ? 0.99769 1.02051 1.22541 -0.06335 -0.30309 0.34411  59  GLN C CD  
477  O OE1 . GLN A 59  ? 1.01303 1.02800 1.34364 -0.03943 -0.31004 0.33007  59  GLN C OE1 
478  N NE2 . GLN A 59  ? 1.22729 1.23113 1.39073 -0.09650 -0.32821 0.37242  59  GLN C NE2 
479  N N   . GLY A 60  ? 0.54230 0.65905 0.79726 0.01543  -0.11263 0.17865  60  GLY C N   
480  C CA  . GLY A 60  ? 0.47840 0.59764 0.76360 0.03236  -0.07503 0.14453  60  GLY C CA  
481  C C   . GLY A 60  ? 0.56261 0.68709 0.78497 0.02862  -0.04524 0.13088  60  GLY C C   
482  O O   . GLY A 60  ? 0.55823 0.67222 0.79030 0.03453  -0.02498 0.11336  60  GLY C O   
483  N N   . GLY A 61  ? 0.48056 0.62104 0.64186 0.01789  -0.04360 0.13627  61  GLY C N   
484  C CA  . GLY A 61  ? 0.42943 0.57676 0.54643 0.01473  -0.02141 0.12475  61  GLY C CA  
485  C C   . GLY A 61  ? 0.40516 0.54237 0.51282 0.00448  -0.02633 0.13715  61  GLY C C   
486  O O   . GLY A 61  ? 0.45625 0.59104 0.55553 0.00651  -0.01093 0.12387  61  GLY C O   
487  N N   . LEU A 62  ? 0.62286 0.75164 0.73103 -0.00913 -0.05097 0.16481  62  LEU C N   
488  C CA  . LEU A 62  ? 0.49626 0.61186 0.60116 -0.02196 -0.05680 0.18040  62  LEU C CA  
489  C C   . LEU A 62  ? 0.57612 0.66911 0.73281 -0.00863 -0.05392 0.16757  62  LEU C C   
490  O O   . LEU A 62  ? 0.52149 0.60995 0.67239 -0.01162 -0.04262 0.15853  62  LEU C O   
491  C CB  . LEU A 62  ? 0.52852 0.63221 0.62116 -0.04259 -0.08817 0.21826  62  LEU C CB  
492  C CG  . LEU A 62  ? 0.51661 0.64005 0.54028 -0.06541 -0.08751 0.22964  62  LEU C CG  
493  C CD1 . LEU A 62  ? 0.76386 0.86760 0.76761 -0.08842 -0.12578 0.27055  62  LEU C CD1 
494  C CD2 . LEU A 62  ? 0.54373 0.68538 0.53006 -0.08025 -0.05937 0.22105  62  LEU C CD2 
495  N N   . GLN A 63  ? 0.47634 0.55588 0.68944 0.00529  -0.06337 0.16284  63  GLN C N   
496  C CA  . GLN A 63  ? 0.51407 0.57332 0.78048 0.01758  -0.05385 0.14102  63  GLN C CA  
497  C C   . GLN A 63  ? 0.48206 0.54832 0.72600 0.02620  -0.01931 0.10472  63  GLN C C   
498  O O   . GLN A 63  ? 0.58605 0.63515 0.85156 0.03045  -0.00636 0.08184  63  GLN C O   
499  C CB  . GLN A 63  ? 0.39686 0.44394 0.74382 0.03000  -0.06987 0.14088  63  GLN C CB  
500  C CG  . GLN A 63  ? 0.52486 0.55567 0.89872 0.01997  -0.11468 0.18228  63  GLN C CG  
501  C CD  . GLN A 63  ? 0.49170 0.50833 0.96744 0.03469  -0.13690 0.18132  63  GLN C CD  
502  O OE1 . GLN A 63  ? 0.49361 0.51831 1.02168 0.05197  -0.11203 0.14567  63  GLN C OE1 
503  N NE2 . GLN A 63  ? 0.58287 0.57755 1.09100 0.02593  -0.18444 0.22109  63  GLN C NE2 
504  N N   . ASN A 64  ? 0.55292 0.64042 0.75199 0.02661  -0.00620 0.09914  64  ASN C N   
505  C CA  . ASN A 64  ? 0.51479 0.60362 0.68085 0.02981  0.01911  0.07339  64  ASN C CA  
506  C C   . ASN A 64  ? 0.51678 0.60339 0.64812 0.02070  0.01791  0.07373  64  ASN C C   
507  O O   . ASN A 64  ? 0.50452 0.57800 0.62118 0.02051  0.02893  0.05356  64  ASN C O   
508  C CB  . ASN A 64  ? 0.49750 0.60547 0.63506 0.03240  0.02776  0.07132  64  ASN C CB  
509  C CG  . ASN A 64  ? 0.49885 0.59968 0.62571 0.03688  0.05240  0.04722  64  ASN C CG  
510  O OD1 . ASN A 64  ? 0.69916 0.79269 0.78459 0.03254  0.06049  0.03796  64  ASN C OD1 
511  N ND2 . ASN A 64  ? 0.69264 0.79483 0.85706 0.04288  0.06310  0.03822  64  ASN C ND2 
512  N N   . ILE A 65  ? 0.58514 0.68474 0.70256 0.01025  0.00485  0.09534  65  ILE C N   
513  C CA  . ILE A 65  ? 0.47942 0.58149 0.58028 0.00017  0.00371  0.09574  65  ILE C CA  
514  C C   . ILE A 65  ? 0.59768 0.67470 0.72841 -0.00407 -0.00421 0.09526  65  ILE C C   
515  O O   . ILE A 65  ? 0.46847 0.53854 0.59276 -0.00857 -0.00304 0.08292  65  ILE C O   
516  C CB  . ILE A 65  ? 0.47759 0.60411 0.56018 -0.01341 -0.00000 0.11497  65  ILE C CB  
517  C CG1 . ILE A 65  ? 0.37343 0.52365 0.43219 -0.00841 0.00995  0.10650  65  ILE C CG1 
518  C CG2 . ILE A 65  ? 0.39002 0.52217 0.47335 -0.02622 0.00021  0.11597  65  ILE C CG2 
519  C CD1 . ILE A 65  ? 0.40060 0.55479 0.45071 -0.00140 0.01717  0.08704  65  ILE C CD1 
520  N N   . ALA A 66  ? 0.49285 0.55382 0.66254 -0.00290 -0.01624 0.10819  66  ALA C N   
521  C CA  . ALA A 66  ? 0.49847 0.53141 0.70883 -0.00572 -0.02544 0.10616  66  ALA C CA  
522  C C   . ALA A 66  ? 0.55799 0.57383 0.77570 0.00312  -0.00871 0.06759  66  ALA C C   
523  O O   . ALA A 66  ? 0.49271 0.48862 0.72534 -0.00247 -0.01191 0.05603  66  ALA C O   
524  C CB  . ALA A 66  ? 0.60385 0.61971 0.86693 -0.00348 -0.04630 0.12733  66  ALA C CB  
525  N N   . VAL A 67  ? 0.51690 0.53870 0.71985 0.01338  0.01023  0.04648  67  VAL C N   
526  C CA  . VAL A 67  ? 0.52449 0.52875 0.71835 0.01559  0.03103  0.00857  67  VAL C CA  
527  C C   . VAL A 67  ? 0.60085 0.60564 0.73295 0.00564  0.03137  -0.00006 67  VAL C C   
528  O O   . VAL A 67  ? 0.54544 0.52896 0.66808 -0.00128 0.03313  -0.02279 67  VAL C O   
529  C CB  . VAL A 67  ? 0.51507 0.52503 0.71268 0.02474  0.05429  -0.00890 67  VAL C CB  
530  C CG1 . VAL A 67  ? 0.50921 0.50088 0.67782 0.01981  0.08192  -0.04894 67  VAL C CG1 
531  C CG2 . VAL A 67  ? 0.41904 0.42784 0.69657 0.03546  0.04884  -0.00361 67  VAL C CG2 
532  N N   . VAL A 68  ? 0.60173 0.62954 0.69618 0.00436  0.02671  0.01630  68  VAL C N   
533  C CA  . VAL A 68  ? 0.61026 0.63860 0.65923 -0.00359 0.02004  0.01033  68  VAL C CA  
534  C C   . VAL A 68  ? 0.51194 0.54061 0.57916 -0.01338 0.00191  0.01798  68  VAL C C   
535  O O   . VAL A 68  ? 0.52140 0.53875 0.56762 -0.02160 -0.00764 0.00461  68  VAL C O   
536  C CB  . VAL A 68  ? 0.43586 0.48784 0.45765 -0.00024 0.01864  0.02333  68  VAL C CB  
537  C CG1 . VAL A 68  ? 0.62364 0.67187 0.62792 0.00630  0.03677  0.01540  68  VAL C CG1 
538  C CG2 . VAL A 68  ? 0.54052 0.62059 0.58775 0.00038  0.01212  0.04695  68  VAL C CG2 
539  N N   . LYS A 69  ? 0.50912 0.54899 0.61332 -0.01591 -0.00478 0.04072  69  LYS C N   
540  C CA  . LYS A 69  ? 0.46176 0.49964 0.58938 -0.02889 -0.01823 0.04890  69  LYS C CA  
541  C C   . LYS A 69  ? 0.45708 0.46038 0.60525 -0.03184 -0.02188 0.02806  69  LYS C C   
542  O O   . LYS A 69  ? 0.57592 0.57181 0.73072 -0.04304 -0.03363 0.02151  69  LYS C O   
543  C CB  . LYS A 69  ? 0.41265 0.46393 0.56522 -0.03651 -0.02243 0.08081  69  LYS C CB  
544  C CG  . LYS A 69  ? 0.62990 0.68036 0.80763 -0.05477 -0.03250 0.09378  69  LYS C CG  
545  C CD  . LYS A 69  ? 0.78336 0.84300 0.96945 -0.06875 -0.03481 0.12915  69  LYS C CD  
546  C CE  . LYS A 69  ? 1.02648 1.08417 1.23715 -0.09170 -0.04099 0.14415  69  LYS C CE  
547  N NZ  . LYS A 69  ? 1.29167 1.35382 1.49599 -0.11251 -0.04221 0.18240  69  LYS C NZ  
548  N N   . HIS A 70  ? 0.52912 0.51199 0.69502 -0.02230 -0.01126 0.01369  70  HIS C N   
549  C CA  . HIS A 70  ? 0.63706 0.58628 0.82768 -0.02425 -0.00921 -0.01566 70  HIS C CA  
550  C C   . HIS A 70  ? 0.68029 0.61692 0.81484 -0.02983 -0.00080 -0.05077 70  HIS C C   
551  O O   . HIS A 70  ? 0.72957 0.64520 0.86165 -0.04067 -0.00960 -0.07108 70  HIS C O   
552  C CB  . HIS A 70  ? 0.61043 0.54534 0.85192 -0.01162 0.00219  -0.02464 70  HIS C CB  
553  C CG  . HIS A 70  ? 0.59767 0.49984 0.86815 -0.01149 0.01391  -0.06706 70  HIS C CG  
554  N ND1 . HIS A 70  ? 0.77902 0.65545 1.10223 -0.01711 -0.00101 -0.07131 70  HIS C ND1 
555  C CD2 . HIS A 70  ? 0.58853 0.47874 0.84285 -0.00891 0.04234  -0.11035 70  HIS C CD2 
556  C CE1 . HIS A 70  ? 0.84315 0.69328 1.18529 -0.01586 0.01715  -0.11906 70  HIS C CE1 
557  N NE2 . HIS A 70  ? 0.81645 0.67548 1.11416 -0.01213 0.04599  -0.14449 70  HIS C NE2 
558  N N   . ASN A 71  ? 0.72653 0.67273 0.81139 -0.02557 0.01375  -0.05686 71  ASN C N   
559  C CA  . ASN A 71  ? 0.66559 0.59439 0.68246 -0.03599 0.01944  -0.08493 71  ASN C CA  
560  C C   . ASN A 71  ? 0.76789 0.70057 0.75236 -0.04776 -0.00978 -0.07557 71  ASN C C   
561  O O   . ASN A 71  ? 0.83724 0.74578 0.77768 -0.06183 -0.01828 -0.09933 71  ASN C O   
562  C CB  . ASN A 71  ? 0.73647 0.67280 0.70849 -0.03198 0.03979  -0.08596 71  ASN C CB  
563  C CG  . ASN A 71  ? 0.71650 0.64927 0.72662 -0.02254 0.07112  -0.10337 71  ASN C CG  
564  O OD1 . ASN A 71  ? 0.76189 0.67819 0.82176 -0.02070 0.08024  -0.12599 71  ASN C OD1 
565  N ND2 . ASN A 71  ? 0.59710 0.54536 0.59428 -0.01641 0.08675  -0.09460 71  ASN C ND2 
566  N N   . LEU A 72  ? 0.63290 0.59601 0.64082 -0.04393 -0.02553 -0.04385 72  LEU C N   
567  C CA  . LEU A 72  ? 0.55017 0.52274 0.54896 -0.05349 -0.05334 -0.03670 72  LEU C CA  
568  C C   . LEU A 72  ? 0.70624 0.66336 0.73537 -0.06584 -0.06942 -0.04825 72  LEU C C   
569  O O   . LEU A 72  ? 0.82575 0.77232 0.83182 -0.07799 -0.09333 -0.05972 72  LEU C O   
570  C CB  . LEU A 72  ? 0.54437 0.55696 0.57551 -0.04727 -0.05790 -0.00726 72  LEU C CB  
571  C CG  . LEU A 72  ? 0.56145 0.59276 0.61043 -0.05507 -0.08416 -0.00106 72  LEU C CG  
572  C CD1 . LEU A 72  ? 0.53522 0.54919 0.53211 -0.05924 -0.10667 -0.01144 72  LEU C CD1 
573  C CD2 . LEU A 72  ? 0.59214 0.66562 0.67875 -0.04936 -0.07758 0.01986  72  LEU C CD2 
574  N N   . GLY A 73  ? 0.62089 0.57376 0.70409 -0.06435 -0.06105 -0.04366 73  GLY C N   
575  C CA  . GLY A 73  ? 0.63314 0.56709 0.75169 -0.07703 -0.07590 -0.05469 73  GLY C CA  
576  C C   . GLY A 73  ? 0.80833 0.70274 0.89176 -0.08473 -0.07548 -0.09666 73  GLY C C   
577  O O   . GLY A 73  ? 1.14195 1.02086 1.22567 -0.09938 -0.09683 -0.11258 73  GLY C O   
578  N N   . VAL A 74  ? 0.70029 0.57867 0.75360 -0.07740 -0.04942 -0.11814 74  VAL C N   
579  C CA  . VAL A 74  ? 0.79675 0.63817 0.80658 -0.08861 -0.03996 -0.16466 74  VAL C CA  
580  C C   . VAL A 74  ? 0.99044 0.82487 0.90973 -0.10426 -0.05812 -0.17243 74  VAL C C   
581  O O   . VAL A 74  ? 1.13176 0.93678 1.01073 -0.12285 -0.07113 -0.20324 74  VAL C O   
582  C CB  . VAL A 74  ? 0.75709 0.58828 0.77027 -0.07832 -0.00027 -0.18798 74  VAL C CB  
583  C CG1 . VAL A 74  ? 0.90841 0.70294 0.87176 -0.09397 0.01878  -0.24332 74  VAL C CG1 
584  C CG2 . VAL A 74  ? 0.71895 0.55305 0.83142 -0.06290 0.00645  -0.17626 74  VAL C CG2 
585  N N   . LEU A 75  ? 0.86692 0.72500 0.75332 -0.09853 -0.06343 -0.14405 75  LEU C N   
586  C CA  . LEU A 75  ? 0.96032 0.80788 0.76537 -0.11352 -0.08864 -0.14381 75  LEU C CA  
587  C C   . LEU A 75  ? 1.03369 0.88852 0.86228 -0.12285 -0.13478 -0.13237 75  LEU C C   
588  O O   . LEU A 75  ? 1.26493 1.09626 1.03255 -0.14181 -0.16524 -0.14415 75  LEU C O   
589  C CB  . LEU A 75  ? 0.95406 0.82194 0.73138 -0.10352 -0.08326 -0.11593 75  LEU C CB  
590  C CG  . LEU A 75  ? 0.82027 0.66740 0.52264 -0.10956 -0.05173 -0.13175 75  LEU C CG  
591  C CD1 . LEU A 75  ? 0.98338 0.82488 0.72107 -0.10210 -0.00623 -0.15956 75  LEU C CD1 
592  C CD2 . LEU A 75  ? 0.93541 0.80422 0.62798 -0.09874 -0.05128 -0.09951 75  LEU C CD2 
593  N N   . THR A 76  ? 1.00822 0.89517 0.92361 -0.11272 -0.14128 -0.10927 76  THR C N   
594  C CA  . THR A 76  ? 1.14093 1.03954 1.09678 -0.12288 -0.17995 -0.10193 76  THR C CA  
595  C C   . THR A 76  ? 1.12198 0.98552 1.07154 -0.14133 -0.19498 -0.13447 76  THR C C   
596  O O   . THR A 76  ? 1.20308 1.05787 1.13874 -0.15724 -0.23528 -0.14121 76  THR C O   
597  C CB  . THR A 76  ? 0.92489 0.86467 0.97251 -0.11339 -0.17258 -0.07416 76  THR C CB  
598  O OG1 . THR A 76  ? 0.76484 0.73618 0.81361 -0.09829 -0.15898 -0.04971 76  THR C OG1 
599  C CG2 . THR A 76  ? 1.13650 1.09378 1.23904 -0.12570 -0.20705 -0.06919 76  THR C CG2 
600  N N   . LYS A 77  ? 0.90829 0.78944 1.06019 -0.05611 -0.03992 -0.26125 77  LYS C N   
601  C CA  . LYS A 77  ? 0.98437 0.84384 1.16657 -0.06570 -0.03730 -0.30977 77  LYS C CA  
602  C C   . LYS A 77  ? 1.18331 1.05649 1.30844 -0.04973 -0.05665 -0.34489 77  LYS C C   
603  O O   . LYS A 77  ? 1.26109 1.11641 1.40215 -0.05406 -0.05619 -0.38934 77  LYS C O   
604  C CB  . LYS A 77  ? 1.05019 0.84900 1.25778 -0.06486 -0.00307 -0.29393 77  LYS C CB  
605  C CG  . LYS A 77  ? 1.31176 1.07565 1.55602 -0.07569 0.02263  -0.25707 77  LYS C CG  
606  C CD  . LYS A 77  ? 1.47256 1.16381 1.72189 -0.06414 0.05326  -0.23827 77  LYS C CD  
607  C CE  . LYS A 77  ? 1.53700 1.17690 1.79731 -0.06796 0.08258  -0.19581 77  LYS C CE  
608  N NZ  . LYS A 77  ? 1.79255 1.34891 2.04282 -0.04792 0.10984  -0.17483 77  LYS C NZ  
609  N N   . ARG A 78  ? 1.16707 1.06379 1.22158 -0.03100 -0.06909 -0.32640 78  ARG C N   
610  C CA  . ARG A 78  ? 1.18839 1.08512 1.16725 -0.01240 -0.07950 -0.35327 78  ARG C CA  
611  C C   . ARG A 78  ? 1.15573 1.08357 1.08358 -0.00108 -0.11822 -0.37299 78  ARG C C   
612  O O   . ARG A 78  ? 1.49823 1.42346 1.37913 0.01187  -0.13929 -0.41754 78  ARG C O   
613  C CB  . ARG A 78  ? 1.23210 1.11531 1.15948 0.00382  -0.05220 -0.31821 78  ARG C CB  
614  C CG  . ARG A 78  ? 1.24424 1.11214 1.08717 0.02195  -0.04646 -0.34258 78  ARG C CG  
615  C CD  . ARG A 78  ? 1.10730 0.96556 0.91588 0.03243  -0.01083 -0.31039 78  ARG C CD  
616  N NE  . ARG A 78  ? 1.18447 1.03442 1.06072 0.02882  0.01538  -0.30010 78  ARG C NE  
617  C CZ  . ARG A 78  ? 1.17813 1.02956 1.05923 0.03632  0.04527  -0.28136 78  ARG C CZ  
618  N NH1 . ARG A 78  ? 0.98767 0.84236 0.81198 0.04211  0.06252  -0.26827 78  ARG C NH1 
619  N NH2 . ARG A 78  ? 1.21374 1.06098 1.16119 0.03969  0.05905  -0.27826 78  ARG C NH2 
620  N N   . SER A 79  ? 1.09119 1.04602 1.02228 -0.00118 -0.13067 -0.34283 79  SER C N   
621  C CA  . SER A 79  ? 1.23749 1.22007 1.11990 0.01620  -0.17086 -0.35833 79  SER C CA  
622  C C   . SER A 79  ? 1.27874 1.30023 1.24051 0.00318  -0.20604 -0.40440 79  SER C C   
623  O O   . SER A 79  ? 1.32816 1.38367 1.27602 0.01748  -0.24343 -0.41518 79  SER C O   
624  C CB  . SER A 79  ? 1.15947 1.15091 1.00837 0.02479  -0.16578 -0.30605 79  SER C CB  
625  O OG  . SER A 79  ? 1.03141 1.04128 0.96359 0.00286  -0.15494 -0.28011 79  SER C OG  
626  N N   . ASN A 80  ? 1.23566 1.25150 1.28595 -0.02298 -0.19278 -0.43443 80  ASN C N   
627  C CA  . ASN A 80  ? 1.38733 1.44006 1.53693 -0.04295 -0.21584 -0.48617 80  ASN C CA  
628  C C   . ASN A 80  ? 1.48481 1.57174 1.69061 -0.05484 -0.21633 -0.46011 80  ASN C C   
629  O O   . ASN A 80  ? 1.34789 1.48414 1.61236 -0.05795 -0.24969 -0.50267 80  ASN C O   
630  C CB  . ASN A 80  ? 1.28305 1.36629 1.40135 -0.02032 -0.27139 -0.55469 80  ASN C CB  
631  C CG  . ASN A 80  ? 1.64430 1.69412 1.72653 -0.01445 -0.26819 -0.59378 80  ASN C CG  
632  O OD1 . ASN A 80  ? 1.65841 1.67487 1.79463 -0.03889 -0.22911 -0.59321 80  ASN C OD1 
633  N ND2 . ASN A 80  ? 1.79462 1.84682 1.77768 0.02160  -0.30852 -0.62778 80  ASN C ND2 
634  N N   . SER A 81  ? 1.38797 1.45135 1.57926 -0.05957 -0.18032 -0.39442 81  SER C N   
635  C CA  . SER A 81  ? 1.28817 1.37464 1.52055 -0.06973 -0.17264 -0.36250 81  SER C CA  
636  C C   . SER A 81  ? 1.29275 1.42740 1.49121 -0.04581 -0.21858 -0.37301 81  SER C C   
637  O O   . SER A 81  ? 1.25429 1.43633 1.52183 -0.05131 -0.24584 -0.41417 81  SER C O   
638  C CB  . SER A 81  ? 1.39792 1.48748 1.74946 -0.10592 -0.14821 -0.38587 81  SER C CB  
639  O OG  . SER A 81  ? 1.31175 1.34101 1.67918 -0.12216 -0.10190 -0.36563 81  SER C OG  
640  N N   . THR A 82  ? 1.31315 1.43190 1.40634 -0.01760 -0.22434 -0.33644 82  THR C N   
641  C CA  . THR A 82  ? 1.18904 1.33422 1.22637 0.01210  -0.26303 -0.33585 82  THR C CA  
642  C C   . THR A 82  ? 1.16909 1.31612 1.20363 0.00984  -0.24268 -0.27979 82  THR C C   
643  O O   . THR A 82  ? 1.31414 1.42694 1.29016 0.01449  -0.21408 -0.23401 82  THR C O   
644  C CB  . THR A 82  ? 1.17767 1.29034 1.08730 0.04717  -0.27781 -0.33577 82  THR C CB  
645  O OG1 . THR A 82  ? 1.03542 1.14421 0.94252 0.05057  -0.29655 -0.39114 82  THR C OG1 
646  C CG2 . THR A 82  ? 1.14577 1.27140 0.98398 0.08454  -0.31836 -0.33383 82  THR C CG2 
647  N N   . PRO A 83  ? 1.04783 1.23596 1.14977 0.00256  -0.25496 -0.28595 83  PRO C N   
648  C CA  . PRO A 83  ? 0.87349 1.06244 0.97201 0.00084  -0.23510 -0.23593 83  PRO C CA  
649  C C   . PRO A 83  ? 0.89253 1.08832 0.91508 0.03585  -0.26537 -0.22273 83  PRO C C   
650  O O   . PRO A 83  ? 1.08274 1.29153 1.06731 0.06431  -0.30927 -0.25665 83  PRO C O   
651  C CB  . PRO A 83  ? 0.72104 0.94693 0.93574 -0.02621 -0.22649 -0.25478 83  PRO C CB  
652  C CG  . PRO A 83  ? 0.67981 0.94318 0.95812 -0.02854 -0.26118 -0.32561 83  PRO C CG  
653  C CD  . PRO A 83  ? 0.72559 0.96589 0.92053 -0.00503 -0.28673 -0.34582 83  PRO C CD  
654  N N   . ALA A 84  ? 0.94095 1.12249 0.93701 0.03660  -0.24179 -0.17364 84  ALA C N   
655  C CA  . ALA A 84  ? 1.17402 1.34947 1.09906 0.06717  -0.25941 -0.15314 84  ALA C CA  
656  C C   . ALA A 84  ? 1.02536 1.24598 1.01577 0.06762  -0.27625 -0.15884 84  ALA C C   
657  O O   . ALA A 84  ? 0.99967 1.23935 1.06962 0.03931  -0.25083 -0.15112 84  ALA C O   
658  C CB  . ALA A 84  ? 1.18264 1.31570 1.04726 0.06667  -0.22120 -0.10276 84  ALA C CB  
659  N N   . THR A 85  ? 0.94360 1.17602 0.89419 0.10342  -0.31771 -0.17248 85  THR C N   
660  C CA  . THR A 85  ? 1.03672 1.31798 1.05535 0.10954  -0.33937 -0.18613 85  THR C CA  
661  C C   . THR A 85  ? 0.91986 1.18714 0.93297 0.10166  -0.30557 -0.13680 85  THR C C   
662  O O   . THR A 85  ? 0.83357 1.05293 0.77513 0.10189  -0.27648 -0.09511 85  THR C O   
663  C CB  . THR A 85  ? 1.07465 1.35670 1.04372 0.15438  -0.38481 -0.20730 85  THR C CB  
664  O OG1 . THR A 85  ? 1.21568 1.43118 1.05490 0.18345  -0.37512 -0.16477 85  THR C OG1 
665  C CG2 . THR A 85  ? 1.21093 1.50308 1.19005 0.16129  -0.41100 -0.25663 85  THR C CG2 
666  N N   . ASN A 86  ? 0.74494 1.05758 0.84226 0.09391  -0.30826 -0.14751 86  ASN C N   
667  C CA  . ASN A 86  ? 0.65920 0.96370 0.75704 0.08803  -0.27965 -0.10827 86  ASN C CA  
668  C C   . ASN A 86  ? 0.65739 0.94303 0.68109 0.12914  -0.30464 -0.09235 86  ASN C C   
669  O O   . ASN A 86  ? 0.67382 0.96349 0.67193 0.16166  -0.34393 -0.11641 86  ASN C O   
670  C CB  . ASN A 86  ? 0.49384 0.84812 0.70617 0.06412  -0.26556 -0.12657 86  ASN C CB  
671  C CG  . ASN A 86  ? 0.55693 0.91318 0.83514 0.02393  -0.23104 -0.13763 86  ASN C CG  
672  O OD1 . ASN A 86  ? 0.80133 1.11623 1.03578 0.01165  -0.20852 -0.11591 86  ASN C OD1 
673  N ND2 . ASN A 86  ? 0.57418 0.97505 0.96121 0.00400  -0.22323 -0.17299 86  ASN C ND2 
674  N N   . GLU A 87  ? 0.72403 0.97749 0.71063 0.12594  -0.27364 -0.05003 87  GLU C N   
675  C CA  . GLU A 87  ? 0.60536 0.82786 0.52308 0.16064  -0.28488 -0.02914 87  GLU C CA  
676  C C   . GLU A 87  ? 0.76834 1.02055 0.74683 0.15688  -0.27678 -0.02348 87  GLU C C   
677  O O   . GLU A 87  ? 0.61976 0.89921 0.66916 0.12381  -0.24842 -0.02232 87  GLU C O   
678  C CB  . GLU A 87  ? 0.83165 0.98567 0.65721 0.15993  -0.25038 0.01046  87  GLU C CB  
679  C CG  . GLU A 87  ? 0.83240 0.94374 0.57436 0.17417  -0.25599 0.00714  87  GLU C CG  
680  C CD  . GLU A 87  ? 0.98599 1.05791 0.65278 0.21345  -0.27777 0.00376  87  GLU C CD  
681  O OE1 . GLU A 87  ? 1.18505 1.25871 0.86231 0.23054  -0.28733 0.00728  87  GLU C OE1 
682  O OE2 . GLU A 87  ? 1.26902 1.30447 0.86752 0.22658  -0.28063 -0.00296 87  GLU C OE2 
683  N N   . ALA A 88  ? 0.89993 1.13525 0.84276 0.19067  -0.29513 -0.01839 88  ALA C N   
684  C CA  . ALA A 88  ? 0.62646 0.88542 0.61817 0.19386  -0.28971 -0.01396 88  ALA C CA  
685  C C   . ALA A 88  ? 0.65092 0.85711 0.58372 0.19138  -0.25475 0.02799  88  ALA C C   
686  O O   . ALA A 88  ? 0.78867 0.93185 0.63252 0.21468  -0.25226 0.04873  88  ALA C O   
687  C CB  . ALA A 88  ? 0.64216 0.90419 0.63753 0.22562  -0.31865 -0.03353 88  ALA C CB  
688  N N   . PRO A 89  ? 0.66225 0.88209 0.64161 0.15863  -0.21861 0.03946  89  PRO C N   
689  C CA  . PRO A 89  ? 0.57569 0.75000 0.51224 0.15225  -0.18518 0.07015  89  PRO C CA  
690  C C   . PRO A 89  ? 0.68473 0.84243 0.60859 0.17981  -0.19099 0.07719  89  PRO C C   
691  O O   . PRO A 89  ? 0.65432 0.84494 0.61453 0.20276  -0.22006 0.05817  89  PRO C O   
692  C CB  . PRO A 89  ? 0.60029 0.80189 0.59172 0.11598  -0.15564 0.07152  89  PRO C CB  
693  C CG  . PRO A 89  ? 0.66690 0.92400 0.73515 0.10882  -0.16706 0.04591  89  PRO C CG  
694  C CD  . PRO A 89  ? 0.46126 0.73247 0.52916 0.12651  -0.20387 0.02287  89  PRO C CD  
695  N N   . GLN A 90  ? 0.78947 0.89554 0.66837 0.17748  -0.16152 0.10121  90  GLN C N   
696  C CA  . GLN A 90  ? 0.68233 0.75782 0.54400 0.20072  -0.15775 0.11117  90  GLN C CA  
697  C C   . GLN A 90  ? 0.66036 0.73304 0.55020 0.17273  -0.12035 0.11821  90  GLN C C   
698  O O   . GLN A 90  ? 0.85843 0.91144 0.73448 0.14878  -0.09384 0.12570  90  GLN C O   
699  C CB  . GLN A 90  ? 0.98012 0.97309 0.74166 0.23317  -0.15627 0.13206  90  GLN C CB  
700  C CG  . GLN A 90  ? 1.26404 1.24974 0.97956 0.26220  -0.19351 0.12215  90  GLN C CG  
701  C CD  . GLN A 90  ? 1.62685 1.52186 1.23711 0.27507  -0.17114 0.14279  90  GLN C CD  
702  O OE1 . GLN A 90  ? 1.64861 1.48637 1.21821 0.26395  -0.12739 0.16742  90  GLN C OE1 
703  N NE2 . GLN A 90  ? 1.79333 1.67387 1.36091 0.29913  -0.19715 0.13020  90  GLN C NE2 
704  N N   . ALA A 91  ? 0.66737 0.76258 0.60000 0.17789  -0.12014 0.11081  91  ALA C N   
705  C CA  . ALA A 91  ? 0.69170 0.78943 0.65122 0.15567  -0.09058 0.11047  91  ALA C CA  
706  C C   . ALA A 91  ? 0.66527 0.70992 0.59857 0.17301  -0.07566 0.11972  91  ALA C C   
707  O O   . ALA A 91  ? 0.72271 0.73934 0.62877 0.20762  -0.09223 0.12555  91  ALA C O   
708  C CB  . ALA A 91  ? 0.85543 1.01380 0.88061 0.14491  -0.09226 0.09303  91  ALA C CB  
709  N N   . THR A 92  ? 0.81980 0.84889 0.76253 0.15122  -0.04564 0.11801  92  THR C N   
710  C CA  . THR A 92  ? 0.67909 0.65545 0.60871 0.16025  -0.02329 0.12202  92  THR C CA  
711  C C   . THR A 92  ? 0.73855 0.74173 0.71537 0.13600  -0.00528 0.10237  92  THR C C   
712  O O   . THR A 92  ? 0.74928 0.77285 0.74060 0.11074  0.00292  0.09263  92  THR C O   
713  C CB  . THR A 92  ? 0.79874 0.69743 0.67155 0.16012  0.00389  0.13926  92  THR C CB  
714  O OG1 . THR A 92  ? 1.21675 1.08474 1.02744 0.18859  -0.01573 0.15715  92  THR C OG1 
715  C CG2 . THR A 92  ? 0.84146 0.67457 0.70335 0.16782  0.03467  0.14323  92  THR C CG2 
716  N N   . VAL A 93  ? 0.74582 0.74922 0.74455 0.14778  -0.00240 0.09349  93  VAL C N   
717  C CA  . VAL A 93  ? 0.65725 0.68477 0.69339 0.13088  0.01106  0.07045  93  VAL C CA  
718  C C   . VAL A 93  ? 0.81462 0.78414 0.84992 0.12993  0.03887  0.06488  93  VAL C C   
719  O O   . VAL A 93  ? 0.89828 0.81744 0.91274 0.15374  0.04449  0.07813  93  VAL C O   
720  C CB  . VAL A 93  ? 0.67442 0.74849 0.74148 0.14177  -0.00030 0.05874  93  VAL C CB  
721  C CG1 . VAL A 93  ? 0.68566 0.77682 0.77412 0.12847  0.01388  0.03408  93  VAL C CG1 
722  C CG2 . VAL A 93  ? 0.70783 0.83204 0.78402 0.13832  -0.01826 0.06201  93  VAL C CG2 
723  N N   . PHE A 94  ? 0.67194 0.64643 0.73215 0.10460  0.05569  0.04232  94  PHE C N   
724  C CA  . PHE A 94  ? 0.77653 0.70103 0.85420 0.09621  0.08721  0.02709  94  PHE C CA  
725  C C   . PHE A 94  ? 0.75478 0.72263 0.87927 0.07413  0.08744  -0.01405 94  PHE C C   
726  O O   . PHE A 94  ? 0.70234 0.72138 0.83104 0.06528  0.06747  -0.02308 94  PHE C O   
727  C CB  . PHE A 94  ? 0.77080 0.62716 0.82346 0.08806  0.11778  0.04370  94  PHE C CB  
728  C CG  . PHE A 94  ? 0.78255 0.66661 0.85076 0.06252  0.12036  0.03344  94  PHE C CG  
729  C CD1 . PHE A 94  ? 0.71645 0.62551 0.75341 0.06734  0.09802  0.05375  94  PHE C CD1 
730  C CD2 . PHE A 94  ? 0.74658 0.63399 0.86917 0.03462  0.14447  -0.00184 94  PHE C CD2 
731  C CE1 . PHE A 94  ? 0.63551 0.56845 0.68897 0.04663  0.10064  0.04321  94  PHE C CE1 
732  C CE2 . PHE A 94  ? 0.66374 0.58197 0.81046 0.01479  0.14448  -0.01608 94  PHE C CE2 
733  C CZ  . PHE A 94  ? 0.58443 0.52315 0.69329 0.02173  0.12316  0.00865  94  PHE C CZ  
734  N N   . PRO A 95  ? 0.75143 0.69797 0.90865 0.06852  0.10694  -0.04187 95  PRO C N   
735  C CA  . PRO A 95  ? 0.77150 0.76233 0.97275 0.05250  0.10004  -0.08960 95  PRO C CA  
736  C C   . PRO A 95  ? 0.79799 0.78468 1.04129 0.02604  0.11676  -0.11484 95  PRO C C   
737  O O   . PRO A 95  ? 0.79517 0.72450 1.04135 0.01483  0.15184  -0.10050 95  PRO C O   
738  C CB  . PRO A 95  ? 0.68242 0.64929 0.90683 0.05811  0.11521  -0.11340 95  PRO C CB  
739  C CG  . PRO A 95  ? 0.67816 0.58360 0.87037 0.07890  0.13129  -0.07376 95  PRO C CG  
740  C CD  . PRO A 95  ? 0.68345 0.56235 0.83694 0.08074  0.13340  -0.03406 95  PRO C CD  
741  N N   . LYS A 96  ? 0.73803 0.78453 1.01250 0.01885  0.09222  -0.15505 96  LYS C N   
742  C CA  . LYS A 96  ? 0.63887 0.69949 0.97308 -0.00451 0.10171  -0.19158 96  LYS C CA  
743  C C   . LYS A 96  ? 0.82590 0.85765 1.23161 -0.02484 0.13620  -0.23689 96  LYS C C   
744  O O   . LYS A 96  ? 0.92056 0.91847 1.37296 -0.04955 0.17621  -0.24723 96  LYS C O   
745  C CB  . LYS A 96  ? 0.65079 0.78537 0.99292 0.00343  0.05601  -0.22383 96  LYS C CB  
746  C CG  . LYS A 96  ? 0.73787 0.90471 1.16200 -0.01554 0.05584  -0.27904 96  LYS C CG  
747  C CD  . LYS A 96  ? 0.63498 0.87047 1.05216 0.00450  0.00132  -0.30916 96  LYS C CD  
748  C CE  . LYS A 96  ? 0.65857 0.93914 1.17491 -0.00837 -0.00827 -0.38087 96  LYS C CE  
749  N NZ  . LYS A 96  ? 0.84982 1.11547 1.42388 -0.03650 0.02971  -0.37719 96  LYS C NZ  
750  N N   . SER A 97  ? 0.76880 0.80979 1.18605 -0.01641 0.12659  -0.26647 97  SER C N   
751  C CA  . SER A 97  ? 0.73795 0.75409 1.22822 -0.03529 0.15690  -0.31666 97  SER C CA  
752  C C   . SER A 97  ? 0.88836 0.83696 1.34713 -0.02417 0.18455  -0.28909 97  SER C C   
753  O O   . SER A 97  ? 0.76706 0.71161 1.15632 0.00214  0.16728  -0.24444 97  SER C O   
754  C CB  . SER A 97  ? 0.97041 1.05766 1.50570 -0.03129 0.11693  -0.38789 97  SER C CB  
755  O OG  . SER A 97  ? 1.00852 1.15773 1.57642 -0.03498 0.08629  -0.41832 97  SER C OG  
756  N N   . PRO A 98  ? 1.03921 0.93221 1.55365 -0.04308 0.22963  -0.31692 98  PRO C N   
757  C CA  . PRO A 98  ? 0.93974 0.76489 1.42524 -0.02746 0.25369  -0.29463 98  PRO C CA  
758  C C   . PRO A 98  ? 0.99573 0.87154 1.46033 -0.00285 0.21305  -0.31262 98  PRO C C   
759  O O   . PRO A 98  ? 1.09850 1.03315 1.60283 -0.00767 0.18743  -0.37173 98  PRO C O   
760  C CB  . PRO A 98  ? 0.94663 0.71182 1.51282 -0.05792 0.30958  -0.33797 98  PRO C CB  
761  C CG  . PRO A 98  ? 1.01678 0.84984 1.67256 -0.08817 0.30015  -0.40326 98  PRO C CG  
762  C CD  . PRO A 98  ? 1.03134 0.91448 1.64353 -0.08028 0.26680  -0.37004 98  PRO C CD  
763  N N   . VAL A 99  ? 0.93947 0.79165 1.34035 0.02625  0.20736  -0.26417 99  VAL C N   
764  C CA  . VAL A 99  ? 0.95331 0.85437 1.32656 0.05035  0.17457  -0.27306 99  VAL C CA  
765  C C   . VAL A 99  ? 1.01682 0.90347 1.43386 0.04828  0.18850  -0.32563 99  VAL C C   
766  O O   . VAL A 99  ? 0.89168 0.70545 1.32731 0.04819  0.22575  -0.32065 99  VAL C O   
767  C CB  . VAL A 99  ? 0.91450 0.79881 1.22917 0.08010  0.16869  -0.21497 99  VAL C CB  
768  C CG1 . VAL A 99  ? 0.92780 0.85958 1.22469 0.10110  0.14689  -0.22845 99  VAL C CG1 
769  C CG2 . VAL A 99  ? 0.82440 0.72737 1.09986 0.08133  0.15198  -0.17072 99  VAL C CG2 
770  N N   . LEU A 100 ? 1.06834 1.01842 1.49478 0.04996  0.15833  -0.37691 100 LEU C N   
771  C CA  . LEU A 100 ? 1.03127 0.97914 1.48750 0.05355  0.16290  -0.43166 100 LEU C CA  
772  C C   . LEU A 100 ? 1.06553 1.06350 1.46041 0.08170  0.13156  -0.43392 100 LEU C C   
773  O O   . LEU A 100 ? 0.92341 0.97621 1.27978 0.08831  0.09732  -0.43869 100 LEU C O   
774  C CB  . LEU A 100 ? 0.98470 0.95673 1.51696 0.02834  0.15877  -0.50876 100 LEU C CB  
775  C CG  . LEU A 100 ? 1.05335 0.96938 1.66489 -0.00623 0.20482  -0.52026 100 LEU C CG  
776  C CD1 . LEU A 100 ? 0.97667 0.93289 1.68356 -0.03128 0.19720  -0.61169 100 LEU C CD1 
777  C CD2 . LEU A 100 ? 0.96267 0.78292 1.57783 -0.00430 0.25593  -0.49374 100 LEU C CD2 
778  N N   . LEU A 101 ? 1.13787 1.11088 1.52088 0.09987  0.14735  -0.42967 101 LEU C N   
779  C CA  . LEU A 101 ? 1.05509 1.06712 1.38112 0.12511  0.13058  -0.43106 101 LEU C CA  
780  C C   . LEU A 101 ? 1.11758 1.17284 1.42922 0.12793  0.10338  -0.49589 101 LEU C C   
781  O O   . LEU A 101 ? 1.30230 1.34997 1.66623 0.11678  0.10528  -0.55608 101 LEU C O   
782  C CB  . LEU A 101 ? 0.94015 0.91739 1.27327 0.14326  0.15673  -0.42491 101 LEU C CB  
783  C CG  . LEU A 101 ? 1.14390 1.10140 1.46372 0.15988  0.16799  -0.36117 101 LEU C CG  
784  C CD1 . LEU A 101 ? 1.04214 0.94783 1.38240 0.14958  0.17970  -0.32271 101 LEU C CD1 
785  C CD2 . LEU A 101 ? 1.25539 1.19156 1.58869 0.18336  0.18789  -0.36880 101 LEU C CD2 
786  N N   . GLY A 102 ? 1.05386 1.15029 1.29161 0.14498  0.07795  -0.48548 102 GLY C N   
787  C CA  . GLY A 102 ? 1.13941 1.27093 1.33523 0.15900  0.04554  -0.54036 102 GLY C CA  
788  C C   . GLY A 102 ? 1.19277 1.35753 1.40192 0.15072  0.00857  -0.56382 102 GLY C C   
789  O O   . GLY A 102 ? 1.21476 1.41048 1.35868 0.17326  -0.02777 -0.58860 102 GLY C O   
790  N N   . GLN A 103 ? 1.04384 1.19884 1.33238 0.12210  0.01851  -0.55742 103 GLN C N   
791  C CA  . GLN A 103 ? 1.22476 1.41602 1.54502 0.11208  -0.01256 -0.58391 103 GLN C CA  
792  C C   . GLN A 103 ? 1.01858 1.21953 1.28689 0.11627  -0.02178 -0.51899 103 GLN C C   
793  O O   . GLN A 103 ? 0.77479 0.94493 1.04531 0.10505  0.00778  -0.45858 103 GLN C O   
794  C CB  . GLN A 103 ? 1.19415 1.36670 1.63033 0.07580  0.01274  -0.61283 103 GLN C CB  
795  N N   . PRO A 104 ? 0.96442 1.20422 1.18355 0.13547  -0.06406 -0.53167 104 PRO C N   
796  C CA  . PRO A 104 ? 0.80262 1.04621 0.96680 0.14126  -0.07073 -0.47034 104 PRO C CA  
797  C C   . PRO A 104 ? 0.82837 1.06222 1.06089 0.11070  -0.05119 -0.43991 104 PRO C C   
798  O O   . PRO A 104 ? 0.94495 1.18398 1.26547 0.08792  -0.04589 -0.47928 104 PRO C O   
799  C CB  . PRO A 104 ? 0.85841 1.13965 0.97135 0.16983  -0.12298 -0.50580 104 PRO C CB  
800  C CG  . PRO A 104 ? 1.08043 1.37165 1.17764 0.19044  -0.14277 -0.57272 104 PRO C CG  
801  C CD  . PRO A 104 ? 1.03314 1.31109 1.23615 0.15886  -0.11073 -0.60450 104 PRO C CD  
802  N N   . ASN A 105 ? 0.75996 0.97753 0.95179 0.11002  -0.03708 -0.37227 105 ASN C N   
803  C CA  . ASN A 105 ? 0.72897 0.92962 0.96312 0.08645  -0.01747 -0.33662 105 ASN C CA  
804  C C   . ASN A 105 ? 0.82062 1.02959 0.99451 0.09580  -0.02860 -0.28380 105 ASN C C   
805  O O   . ASN A 105 ? 0.92336 1.14154 1.02655 0.11749  -0.04160 -0.26971 105 ASN C O   
806  C CB  . ASN A 105 ? 0.64224 0.79269 0.90513 0.07348  0.02427  -0.30987 105 ASN C CB  
807  C CG  . ASN A 105 ? 0.70334 0.82247 1.01115 0.04964  0.04947  -0.28928 105 ASN C CG  
808  O OD1 . ASN A 105 ? 0.82254 0.95489 1.11932 0.04499  0.04030  -0.26585 105 ASN C OD1 
809  N ND2 . ASN A 105 ? 0.80030 0.86969 1.15317 0.03566  0.08572  -0.29745 105 ASN C ND2 
810  N N   . THR A 106 ? 0.66091 0.86043 0.86137 0.07857  -0.01835 -0.25568 106 THR C N   
811  C CA  . THR A 106 ? 0.61679 0.82226 0.77238 0.08352  -0.02710 -0.20962 106 THR C CA  
812  C C   . THR A 106 ? 0.67410 0.84538 0.83214 0.07341  0.00013  -0.16072 106 THR C C   
813  O O   . THR A 106 ? 0.59368 0.73452 0.79269 0.05770  0.02308  -0.16073 106 THR C O   
814  C CB  . THR A 106 ? 0.67170 0.90323 0.85036 0.07832  -0.04835 -0.22693 106 THR C CB  
815  O OG1 . THR A 106 ? 0.94858 1.21428 1.11749 0.09753  -0.08395 -0.27553 106 THR C OG1 
816  C CG2 . THR A 106 ? 0.58097 0.81248 0.71474 0.08263  -0.05434 -0.17941 106 THR C CG2 
817  N N   . LEU A 107 ? 0.61678 0.78941 0.72949 0.08430  -0.00120 -0.12186 107 LEU C N   
818  C CA  . LEU A 107 ? 0.61756 0.76702 0.72882 0.08201  0.01308  -0.08053 107 LEU C CA  
819  C C   . LEU A 107 ? 0.61198 0.76863 0.71012 0.07542  0.00346  -0.05650 107 LEU C C   
820  O O   . LEU A 107 ? 0.67163 0.85279 0.74440 0.07960  -0.01323 -0.05640 107 LEU C O   
821  C CB  . LEU A 107 ? 0.49965 0.65483 0.59006 0.09659  0.01759  -0.06262 107 LEU C CB  
822  C CG  . LEU A 107 ? 0.76447 0.89338 0.87167 0.10390  0.03027  -0.04240 107 LEU C CG  
823  C CD1 . LEU A 107 ? 0.75051 0.84284 0.88391 0.10295  0.04651  -0.06203 107 LEU C CD1 
824  C CD2 . LEU A 107 ? 0.73075 0.88034 0.83576 0.11805  0.03303  -0.03510 107 LEU C CD2 
825  N N   . ILE A 108 ? 0.56960 0.69721 0.67702 0.06809  0.01566  -0.03577 108 ILE C N   
826  C CA  . ILE A 108 ? 0.48138 0.61027 0.57802 0.06092  0.01023  -0.01677 108 ILE C CA  
827  C C   . ILE A 108 ? 0.61101 0.72568 0.68289 0.07048  0.00931  0.01870  108 ILE C C   
828  O O   . ILE A 108 ? 0.79205 0.87356 0.86084 0.07987  0.01986  0.02970  108 ILE C O   
829  C CB  . ILE A 108 ? 0.59295 0.69701 0.71842 0.04418  0.02856  -0.02949 108 ILE C CB  
830  C CG1 . ILE A 108 ? 0.54650 0.67473 0.71690 0.03524  0.02545  -0.07719 108 ILE C CG1 
831  C CG2 . ILE A 108 ? 0.44765 0.55404 0.56024 0.03789  0.02495  -0.01227 108 ILE C CG2 
832  C CD1 . ILE A 108 ? 0.54470 0.65265 0.76594 0.01371  0.05198  -0.09951 108 ILE C CD1 
833  N N   . CYS A 109 ? 0.65507 0.79284 0.71012 0.07095  -0.00515 0.03340  109 CYS C N   
834  C CA  . CYS A 109 ? 0.67832 0.81164 0.71926 0.07907  -0.01197 0.05786  109 CYS C CA  
835  C C   . CYS A 109 ? 0.72884 0.85081 0.75489 0.07073  -0.01413 0.06830  109 CYS C C   
836  O O   . CYS A 109 ? 0.58269 0.72640 0.60866 0.06223  -0.02150 0.06472  109 CYS C O   
837  C CB  . CYS A 109 ? 0.64895 0.81734 0.69373 0.08335  -0.02067 0.06072  109 CYS C CB  
838  S SG  . CYS A 109 ? 0.72537 0.90266 0.77665 0.09398  -0.03447 0.07570  109 CYS C SG  
839  N N   . PHE A 110 ? 0.62945 0.71072 0.63555 0.07651  -0.00597 0.08169  110 PHE C N   
840  C CA  . PHE A 110 ? 0.50856 0.56905 0.49276 0.06984  -0.00079 0.09081  110 PHE C CA  
841  C C   . PHE A 110 ? 0.64641 0.70999 0.60292 0.08432  -0.02148 0.10703  110 PHE C C   
842  O O   . PHE A 110 ? 0.73548 0.77015 0.66420 0.10574  -0.02717 0.11841  110 PHE C O   
843  C CB  . PHE A 110 ? 0.60383 0.60440 0.57249 0.06726  0.03032  0.09397  110 PHE C CB  
844  C CG  . PHE A 110 ? 0.66726 0.63532 0.60298 0.06279  0.04412  0.10510  110 PHE C CG  
845  C CD1 . PHE A 110 ? 0.67378 0.66459 0.63745 0.04233  0.05173  0.08985  110 PHE C CD1 
846  C CD2 . PHE A 110 ? 0.84166 0.75365 0.71371 0.08340  0.04875  0.12885  110 PHE C CD2 
847  C CE1 . PHE A 110 ? 0.63627 0.59686 0.57177 0.03771  0.06931  0.09765  110 PHE C CE1 
848  C CE2 . PHE A 110 ? 0.86613 0.74149 0.69586 0.08123  0.06536  0.13861  110 PHE C CE2 
849  C CZ  . PHE A 110 ? 0.69244 0.59316 0.55736 0.05592  0.07861  0.12276  110 PHE C CZ  
850  N N   . VAL A 111 ? 0.61468 0.71137 0.57901 0.07564  -0.03476 0.10496  111 VAL C N   
851  C CA  . VAL A 111 ? 0.59938 0.70722 0.55127 0.08525  -0.05564 0.11097  111 VAL C CA  
852  C C   . VAL A 111 ? 0.57034 0.65142 0.48794 0.08167  -0.05106 0.11685  111 VAL C C   
853  O O   . VAL A 111 ? 0.62037 0.71028 0.54972 0.06470  -0.04189 0.11139  111 VAL C O   
854  C CB  . VAL A 111 ? 0.49685 0.65190 0.48385 0.07602  -0.06600 0.10294  111 VAL C CB  
855  C CG1 . VAL A 111 ? 0.53824 0.71087 0.53242 0.08458  -0.08712 0.09958  111 VAL C CG1 
856  C CG2 . VAL A 111 ? 0.55748 0.73248 0.57182 0.07662  -0.05943 0.09615  111 VAL C CG2 
857  N N   . ASP A 112 ? 0.60549 0.65167 0.47627 0.10170  -0.05845 0.12636  112 ASP C N   
858  C CA  . ASP A 112 ? 0.62567 0.63519 0.44824 0.10248  -0.04942 0.13264  112 ASP C CA  
859  C C   . ASP A 112 ? 0.66070 0.68587 0.46408 0.11808  -0.08241 0.12785  112 ASP C C   
860  O O   . ASP A 112 ? 0.81180 0.87570 0.64642 0.12850  -0.11083 0.11780  112 ASP C O   
861  C CB  . ASP A 112 ? 0.65229 0.58673 0.41396 0.11632  -0.02199 0.14832  112 ASP C CB  
862  C CG  . ASP A 112 ? 0.99488 0.88730 0.72034 0.10469  0.01025  0.15206  112 ASP C CG  
863  O OD1 . ASP A 112 ? 1.07372 0.99109 0.80291 0.09696  -0.00070 0.14429  112 ASP C OD1 
864  O OD2 . ASP A 112 ? 1.02587 0.85726 0.72267 0.10213  0.05143  0.16104  112 ASP C OD2 
865  N N   . ASN A 113 ? 0.84048 0.83720 0.59851 0.11876  -0.07648 0.12989  113 ASN C N   
866  C CA  . ASN A 113 ? 0.62211 0.62943 0.35642 0.13395  -0.10813 0.11939  113 ASN C CA  
867  C C   . ASN A 113 ? 0.62124 0.69595 0.43143 0.11597  -0.12829 0.09994  113 ASN C C   
868  O O   . ASN A 113 ? 0.66875 0.77627 0.50265 0.12836  -0.16054 0.08301  113 ASN C O   
869  C CB  . ASN A 113 ? 0.69381 0.67659 0.37496 0.17531  -0.13821 0.12114  113 ASN C CB  
870  C CG  . ASN A 113 ? 0.74591 0.72425 0.37973 0.19793  -0.17085 0.10683  113 ASN C CG  
871  O OD1 . ASN A 113 ? 0.92747 0.88526 0.52857 0.18744  -0.15608 0.10628  113 ASN C OD1 
872  N ND2 . ASN A 113 ? 1.02031 1.02206 0.66836 0.22203  -0.21040 0.08759  113 ASN C ND2 
873  N N   . ILE A 114 ? 0.67399 0.76610 0.52378 0.08815  -0.10744 0.10003  114 ILE C N   
874  C CA  . ILE A 114 ? 0.53439 0.67110 0.44352 0.07073  -0.11458 0.08796  114 ILE C CA  
875  C C   . ILE A 114 ? 0.52900 0.66212 0.43042 0.06276  -0.11681 0.07876  114 ILE C C   
876  O O   . ILE A 114 ? 0.63232 0.74548 0.51774 0.05400  -0.09760 0.08399  114 ILE C O   
877  C CB  . ILE A 114 ? 0.56429 0.71283 0.50607 0.05415  -0.09430 0.09447  114 ILE C CB  
878  C CG1 . ILE A 114 ? 0.60674 0.75715 0.55543 0.06188  -0.09059 0.09990  114 ILE C CG1 
879  C CG2 . ILE A 114 ? 0.45509 0.63027 0.43837 0.04024  -0.09442 0.08758  114 ILE C CG2 
880  C CD1 . ILE A 114 ? 0.44580 0.60442 0.41483 0.05059  -0.07424 0.10183  114 ILE C CD1 
881  N N   . PHE A 115 ? 0.68106 0.83657 0.60273 0.06568  -0.14000 0.05978  115 PHE C N   
882  C CA  . PHE A 115 ? 0.62700 0.78248 0.55448 0.05495  -0.14127 0.04640  115 PHE C CA  
883  C C   . PHE A 115 ? 0.72929 0.92227 0.71678 0.04807  -0.15951 0.02010  115 PHE C C   
884  O O   . PHE A 115 ? 0.66074 0.87638 0.66087 0.06422  -0.18720 0.00174  115 PHE C O   
885  C CB  . PHE A 115 ? 0.55150 0.67249 0.41030 0.07094  -0.14735 0.04337  115 PHE C CB  
886  C CG  . PHE A 115 ? 0.78048 0.89766 0.64336 0.05951  -0.14410 0.02899  115 PHE C CG  
887  C CD1 . PHE A 115 ? 0.81245 0.91379 0.67719 0.04515  -0.11619 0.03904  115 PHE C CD1 
888  C CD2 . PHE A 115 ? 0.64365 0.77634 0.51632 0.06467  -0.17113 0.00009  115 PHE C CD2 
889  C CE1 . PHE A 115 ? 0.64078 0.73635 0.51156 0.03711  -0.11265 0.02506  115 PHE C CE1 
890  C CE2 . PHE A 115 ? 0.55677 0.68277 0.43542 0.05362  -0.16635 -0.01552 115 PHE C CE2 
891  C CZ  . PHE A 115 ? 0.66844 0.77325 0.54373 0.04019  -0.13573 -0.00077 115 PHE C CZ  
892  N N   . PRO A 116 ? 0.52435 0.72280 0.55394 0.02570  -0.14364 0.01462  116 PRO C N   
893  C CA  . PRO A 116 ? 0.56282 0.73595 0.58101 0.01334  -0.11770 0.03224  116 PRO C CA  
894  C C   . PRO A 116 ? 0.61545 0.78576 0.63488 0.01117  -0.09926 0.05511  116 PRO C C   
895  O O   . PRO A 116 ? 0.66523 0.85351 0.70540 0.01242  -0.09967 0.05658  116 PRO C O   
896  C CB  . PRO A 116 ? 0.43665 0.61214 0.50051 -0.00419 -0.11027 0.01585  116 PRO C CB  
897  C CG  . PRO A 116 ? 0.41991 0.62950 0.54193 -0.01024 -0.11753 -0.00428 116 PRO C CG  
898  C CD  . PRO A 116 ? 0.52632 0.75558 0.62551 0.01282  -0.15023 -0.01433 116 PRO C CD  
899  N N   . PRO A 117 ? 0.54955 0.70037 0.54954 0.01063  -0.08540 0.06846  117 PRO C N   
900  C CA  . PRO A 117 ? 0.54211 0.69262 0.53880 0.01365  -0.07505 0.08332  117 PRO C CA  
901  C C   . PRO A 117 ? 0.45111 0.59951 0.46576 0.00784  -0.06208 0.08962  117 PRO C C   
902  O O   . PRO A 117 ? 0.55769 0.68586 0.55715 0.01196  -0.05280 0.09920  117 PRO C O   
903  C CB  . PRO A 117 ? 0.56241 0.69887 0.54323 0.01805  -0.07017 0.08530  117 PRO C CB  
904  C CG  . PRO A 117 ? 0.53472 0.65930 0.51677 0.01400  -0.07084 0.07632  117 PRO C CG  
905  C CD  . PRO A 117 ? 0.52317 0.65535 0.50574 0.01091  -0.08187 0.06491  117 PRO C CD  
906  N N   . VAL A 118 ? 0.41462 0.58042 0.45952 0.00110  -0.05981 0.08275  118 VAL C N   
907  C CA  . VAL A 118 ? 0.50861 0.66833 0.57010 -0.00634 -0.03639 0.08856  118 VAL C CA  
908  C C   . VAL A 118 ? 0.40383 0.59323 0.49024 -0.00463 -0.03837 0.08236  118 VAL C C   
909  O O   . VAL A 118 ? 0.57007 0.78825 0.69186 -0.00506 -0.05477 0.06357  118 VAL C O   
910  C CB  . VAL A 118 ? 0.41247 0.56126 0.51013 -0.02351 -0.01876 0.07803  118 VAL C CB  
911  C CG1 . VAL A 118 ? 0.44123 0.57180 0.54980 -0.03256 0.01825  0.08640  118 VAL C CG1 
912  C CG2 . VAL A 118 ? 0.62570 0.74084 0.69910 -0.02251 -0.01740 0.08323  118 VAL C CG2 
913  N N   . ILE A 119 ? 0.45461 0.63739 0.52143 0.00133  -0.02500 0.09477  119 ILE C N   
914  C CA  . ILE A 119 ? 0.42634 0.63491 0.51400 0.00596  -0.02649 0.08883  119 ILE C CA  
915  C C   . ILE A 119 ? 0.52903 0.72308 0.60271 0.00574  0.00273  0.09836  119 ILE C C   
916  O O   . ILE A 119 ? 0.71780 0.87691 0.74566 0.00990  0.01631  0.11307  119 ILE C O   
917  C CB  . ILE A 119 ? 0.49003 0.70340 0.55303 0.02070  -0.04908 0.09126  119 ILE C CB  
918  C CG1 . ILE A 119 ? 0.45467 0.69390 0.54692 0.02919  -0.06006 0.08036  119 ILE C CG1 
919  C CG2 . ILE A 119 ? 0.43287 0.62927 0.45868 0.02790  -0.04229 0.10198  119 ILE C CG2 
920  C CD1 . ILE A 119 ? 0.42205 0.65049 0.48390 0.04477  -0.07748 0.08475  119 ILE C CD1 
921  N N   . ASN A 120 ? 0.61788 0.83640 0.72649 0.00517  0.01147  0.08842  120 ASN C N   
922  C CA  . ASN A 120 ? 0.59832 0.80404 0.69588 0.00466  0.04507  0.09353  120 ASN C CA  
923  C C   . ASN A 120 ? 0.42570 0.65477 0.52917 0.01756  0.03289  0.08697  120 ASN C C   
924  O O   . ASN A 120 ? 0.69983 0.96302 0.86024 0.01691  0.03092  0.07007  120 ASN C O   
925  C CB  . ASN A 120 ? 0.64892 0.86061 0.80400 -0.01509 0.08166  0.08124  120 ASN C CB  
926  C CG  . ASN A 120 ? 1.09071 1.28765 1.23748 -0.01674 0.12569  0.08409  120 ASN C CG  
927  O OD1 . ASN A 120 ? 0.99676 1.16592 1.07386 -0.00111 0.13010  0.09956  120 ASN C OD1 
928  N ND2 . ASN A 120 ? 1.26686 1.48424 1.49007 -0.03584 0.15988  0.06391  120 ASN C ND2 
929  N N   . ILE A 121 ? 0.46591 0.67775 0.51672 0.03088  0.02306  0.09604  121 ILE C N   
930  C CA  . ILE A 121 ? 0.39083 0.61595 0.44410 0.04241  0.01340  0.08897  121 ILE C CA  
931  C C   . ILE A 121 ? 0.46213 0.67399 0.48751 0.04769  0.03977  0.08872  121 ILE C C   
932  O O   . ILE A 121 ? 0.85007 1.03086 0.81834 0.05323  0.04951  0.09811  121 ILE C O   
933  C CB  . ILE A 121 ? 0.59079 0.80679 0.61684 0.05051  -0.01153 0.09095  121 ILE C CB  
934  C CG1 . ILE A 121 ? 0.56079 0.78014 0.60023 0.04696  -0.03077 0.09277  121 ILE C CG1 
935  C CG2 . ILE A 121 ? 0.51199 0.73268 0.54364 0.06014  -0.01507 0.08232  121 ILE C CG2 
936  C CD1 . ILE A 121 ? 0.37568 0.58029 0.39260 0.05056  -0.04311 0.09390  121 ILE C CD1 
937  N N   . THR A 122 ? 0.54970 0.78177 0.60921 0.05047  0.05003  0.07679  122 THR C N   
938  C CA  . THR A 122 ? 0.60776 0.82724 0.64076 0.05617  0.07905  0.07322  122 THR C CA  
939  C C   . THR A 122 ? 0.57089 0.81039 0.63056 0.06664  0.07069  0.05815  122 THR C C   
940  O O   . THR A 122 ? 0.48583 0.74968 0.59611 0.06916  0.05144  0.05129  122 THR C O   
941  C CB  . THR A 122 ? 0.54919 0.76633 0.60730 0.04300  0.12389  0.07186  122 THR C CB  
942  O OG1 . THR A 122 ? 0.69786 0.95599 0.84457 0.03123  0.11787  0.05778  122 THR C OG1 
943  C CG2 . THR A 122 ? 0.80448 0.97509 0.80369 0.03817  0.14609  0.09106  122 THR C CG2 
944  N N   . TRP A 123 ? 0.61911 0.84264 0.63740 0.07662  0.08426  0.05222  123 TRP C N   
945  C CA  . TRP A 123 ? 0.52568 0.76117 0.56524 0.08689  0.08169  0.03563  123 TRP C CA  
946  C C   . TRP A 123 ? 0.60036 0.84581 0.66460 0.08668  0.12016  0.02444  123 TRP C C   
947  O O   . TRP A 123 ? 0.75711 0.98705 0.79837 0.07942  0.15608  0.03021  123 TRP C O   
948  C CB  . TRP A 123 ? 0.59504 0.81027 0.58065 0.09839  0.06834  0.02690  123 TRP C CB  
949  C CG  . TRP A 123 ? 0.59807 0.81004 0.58222 0.09694  0.03582  0.02854  123 TRP C CG  
950  C CD1 . TRP A 123 ? 0.69399 0.89549 0.64483 0.09550  0.02111  0.03620  123 TRP C CD1 
951  C CD2 . TRP A 123 ? 0.70547 0.91921 0.72381 0.09731  0.02007  0.02125  123 TRP C CD2 
952  N NE1 . TRP A 123 ? 0.72313 0.92693 0.69447 0.09195  -0.00079 0.03074  123 TRP C NE1 
953  C CE2 . TRP A 123 ? 0.57070 0.77662 0.57891 0.09198  0.00154  0.02342  123 TRP C CE2 
954  C CE3 . TRP A 123 ? 0.54135 0.75616 0.59591 0.10343  0.02333  0.01350  123 TRP C CE3 
955  C CZ2 . TRP A 123 ? 0.63722 0.83226 0.66889 0.08859  -0.00607 0.01880  123 TRP C CZ2 
956  C CZ3 . TRP A 123 ? 0.63268 0.82963 0.70084 0.10380  0.01240  0.01259  123 TRP C CZ3 
957  C CH2 . TRP A 123 ? 0.60964 0.79494 0.66570 0.09445  0.00155  0.01559  123 TRP C CH2 
958  N N   . LEU A 124 ? 0.58580 0.85171 0.69678 0.09560  0.11698  0.00801  124 LEU C N   
959  C CA  . LEU A 124 ? 0.62211 0.90344 0.76926 0.09742  0.15346  -0.00891 124 LEU C CA  
960  C C   . LEU A 124 ? 0.65116 0.92765 0.79234 0.11372  0.14889  -0.02565 124 LEU C C   
961  O O   . LEU A 124 ? 0.63981 0.91836 0.80255 0.12310  0.11752  -0.02784 124 LEU C O   
962  C CB  . LEU A 124 ? 0.71413 1.04036 0.96052 0.09333  0.15363  -0.02044 124 LEU C CB  
963  C CG  . LEU A 124 ? 0.61538 0.95451 0.89205 0.07480  0.15905  -0.01385 124 LEU C CG  
964  C CD1 . LEU A 124 ? 0.60365 0.99747 0.98897 0.07756  0.14448  -0.03710 124 LEU C CD1 
965  C CD2 . LEU A 124 ? 0.54985 0.86360 0.79615 0.05779  0.21565  -0.00885 124 LEU C CD2 
966  N N   . ARG A 125 ? 0.70910 0.97134 0.81506 0.11789  0.18392  -0.03744 125 ARG C N   
967  C CA  . ARG A 125 ? 0.72645 0.98566 0.83365 0.13276  0.18649  -0.05963 125 ARG C CA  
968  C C   . ARG A 125 ? 0.71177 0.99704 0.88273 0.13433  0.22552  -0.07788 125 ARG C C   
969  O O   . ARG A 125 ? 0.67158 0.94719 0.81829 0.12741  0.27300  -0.08014 125 ARG C O   
970  C CB  . ARG A 125 ? 0.95919 1.18239 0.97121 0.14115  0.19164  -0.06690 125 ARG C CB  
971  C CG  . ARG A 125 ? 0.80643 1.02587 0.81981 0.15536  0.20045  -0.09615 125 ARG C CG  
972  C CD  . ARG A 125 ? 0.84885 1.03557 0.76354 0.16789  0.20147  -0.11083 125 ARG C CD  
973  N NE  . ARG A 125 ? 1.13164 1.31128 1.02270 0.17006  0.15548  -0.11570 125 ARG C NE  
974  C CZ  . ARG A 125 ? 1.18089 1.34707 1.01261 0.17145  0.13591  -0.10306 125 ARG C CZ  
975  N NH1 . ARG A 125 ? 1.27304 1.42045 1.04955 0.17201  0.15898  -0.07964 125 ARG C NH1 
976  N NH2 . ARG A 125 ? 0.78136 0.95033 0.61339 0.17270  0.09537  -0.11628 125 ARG C NH2 
977  N N   . ASN A 126 ? 0.59310 0.90683 0.84381 0.14569  0.20810  -0.09149 126 ASN C N   
978  C CA  . ASN A 126 ? 0.60162 0.95140 0.93538 0.15137  0.23772  -0.11585 126 ASN C CA  
979  C C   . ASN A 126 ? 0.59666 0.97679 0.98329 0.13238  0.26825  -0.11669 126 ASN C C   
980  O O   . ASN A 126 ? 0.63688 1.02252 1.04087 0.12313  0.32419  -0.13149 126 ASN C O   
981  C CB  . ASN A 126 ? 0.65807 0.98991 0.95884 0.15880  0.27711  -0.13667 126 ASN C CB  
982  C CG  . ASN A 126 ? 0.66532 0.97093 0.93315 0.17577  0.24899  -0.14501 126 ASN C CG  
983  O OD1 . ASN A 126 ? 0.63241 0.93989 0.93667 0.18684  0.21060  -0.14148 126 ASN C OD1 
984  N ND2 . ASN A 126 ? 0.92262 1.19781 1.11721 0.17920  0.27006  -0.15783 126 ASN C ND2 
985  N N   . SER A 127 ? 0.63836 1.03439 1.05091 0.12516  0.23542  -0.10284 127 SER C N   
986  C CA  . SER A 127 ? 0.57812 1.00534 1.05420 0.10494  0.25708  -0.10814 127 SER C CA  
987  C C   . SER A 127 ? 0.70510 1.09279 1.11541 0.08158  0.31453  -0.09402 127 SER C C   
988  O O   . SER A 127 ? 0.76117 1.16538 1.22840 0.06048  0.35540  -0.10332 127 SER C O   
989  C CB  . SER A 127 ? 0.83726 1.32690 1.44503 0.11056  0.27213  -0.14706 127 SER C CB  
990  O OG  . SER A 127 ? 0.66845 1.18578 1.32509 0.14088  0.21472  -0.15798 127 SER C OG  
991  N N   . LYS A 128 ? 0.69751 1.02927 0.98792 0.08715  0.31886  -0.07396 128 LYS C N   
992  C CA  . LYS A 128 ? 0.77117 1.04874 0.96898 0.07599  0.36624  -0.05530 128 LYS C CA  
993  C C   . LYS A 128 ? 0.86430 1.10427 0.96943 0.08009  0.32527  -0.02640 128 LYS C C   
994  O O   . LYS A 128 ? 0.80964 1.04950 0.88663 0.09486  0.27580  -0.02547 128 LYS C O   
995  C CB  . LYS A 128 ? 0.78457 1.02594 0.91063 0.08807  0.41065  -0.06439 128 LYS C CB  
996  N N   . SER A 129 ? 0.99890 1.20520 1.06303 0.06665  0.34970  -0.00540 129 SER C N   
997  C CA  . SER A 129 ? 0.99997 1.17618 0.99100 0.07146  0.31035  0.01939  129 SER C CA  
998  C C   . SER A 129 ? 1.07517 1.20412 0.94278 0.09611  0.29844  0.02546  129 SER C C   
999  O O   . SER A 129 ? 1.20041 1.29303 1.00128 0.10698  0.33954  0.02173  129 SER C O   
1000 C CB  . SER A 129 ? 0.95127 1.09673 0.93032 0.05331  0.34349  0.03912  129 SER C CB  
1001 O OG  . SER A 129 ? 1.47910 1.56357 1.38076 0.05426  0.41051  0.04905  129 SER C OG  
1002 N N   . VAL A 130 ? 1.06400 1.19464 0.90340 0.10627  0.24194  0.03050  130 VAL C N   
1003 C CA  . VAL A 130 ? 1.29404 1.39039 1.03046 0.13145  0.21783  0.02812  130 VAL C CA  
1004 C C   . VAL A 130 ? 1.52233 1.60054 1.21843 0.13514  0.18510  0.04695  130 VAL C C   
1005 O O   . VAL A 130 ? 1.32195 1.43274 1.08051 0.12338  0.15010  0.04833  130 VAL C O   
1006 C CB  . VAL A 130 ? 1.14144 1.26760 0.90587 0.14131  0.18034  0.00059  130 VAL C CB  
1007 C CG1 . VAL A 130 ? 0.83496 1.00523 0.70068 0.12598  0.14977  -0.00121 130 VAL C CG1 
1008 C CG2 . VAL A 130 ? 1.30098 1.40642 0.98487 0.16437  0.14177  -0.01033 130 VAL C CG2 
1009 N N   . ALA A 131 ? 1.66097 1.68167 1.24677 0.15483  0.19817  0.06175  131 ALA C N   
1010 C CA  . ALA A 131 ? 1.66962 1.66696 1.21158 0.16397  0.16956  0.07940  131 ALA C CA  
1011 C C   . ALA A 131 ? 1.74037 1.72325 1.20030 0.19989  0.12136  0.06449  131 ALA C C   
1012 O O   . ALA A 131 ? 1.69605 1.67804 1.14546 0.20888  0.08436  0.06933  131 ALA C O   
1013 C CB  . ALA A 131 ? 1.47545 1.40861 0.95521 0.16256  0.22060  0.11078  131 ALA C CB  
1014 N N   A ASP A 132 ? 1.67284 1.64818 1.08067 0.22194  0.11896  0.04125  132 ASP C N   
1015 N N   B ASP A 132 ? 1.67274 1.64818 1.08079 0.22187  0.11898  0.04123  132 ASP C N   
1016 C CA  A ASP A 132 ? 1.63913 1.60827 0.97623 0.25942  0.06763  0.01582  132 ASP C CA  
1017 C CA  B ASP A 132 ? 1.63907 1.60839 0.97646 0.25934  0.06775  0.01567  132 ASP C CA  
1018 C C   A ASP A 132 ? 1.56650 1.60260 1.00398 0.24739  0.01996  -0.02060 132 ASP C C   
1019 C C   B ASP A 132 ? 1.56633 1.60260 1.00421 0.24727  0.01994  -0.02061 132 ASP C C   
1020 O O   A ASP A 132 ? 1.46272 1.53366 0.98557 0.22219  0.03340  -0.03113 132 ASP C O   
1021 O O   B ASP A 132 ? 1.46228 1.53354 0.98598 0.22195  0.03325  -0.03106 132 ASP C O   
1022 C CB  A ASP A 132 ? 1.72711 1.65290 0.95317 0.29180  0.08627  0.00233  132 ASP C CB  
1023 C CB  B ASP A 132 ? 1.72648 1.65303 0.95415 0.29128  0.08673  0.00202  132 ASP C CB  
1024 C CG  A ASP A 132 ? 1.78038 1.62386 0.90536 0.30224  0.13682  0.03928  132 ASP C CG  
1025 C CG  B ASP A 132 ? 1.66796 1.61709 0.95311 0.26922  0.12678  -0.01122 132 ASP C CG  
1026 O OD1 A ASP A 132 ? 1.67570 1.49608 0.81184 0.28751  0.15544  0.07247  132 ASP C OD1 
1027 O OD1 B ASP A 132 ? 1.45170 1.42517 0.83088 0.23317  0.16068  0.00490  132 ASP C OD1 
1028 O OD2 A ASP A 132 ? 1.74466 1.54637 0.79986 0.31844  0.15718  0.03320  132 ASP C OD2 
1029 O OD2 B ASP A 132 ? 1.75330 1.69754 0.99163 0.29075  0.12150  -0.04160 132 ASP C OD2 
1030 N N   . GLY A 133 ? 1.52761 1.57773 0.95625 0.26699  -0.03303 -0.04121 133 GLY C N   
1031 C CA  . GLY A 133 ? 1.48589 1.59299 1.01280 0.25335  -0.07069 -0.07908 133 GLY C CA  
1032 C C   . GLY A 133 ? 1.31516 1.45277 0.94900 0.21425  -0.06260 -0.06192 133 GLY C C   
1033 O O   . GLY A 133 ? 1.03910 1.20636 0.75434 0.19278  -0.06122 -0.07940 133 GLY C O   
1034 N N   . VAL A 134 ? 1.16262 1.28637 0.79069 0.20709  -0.05589 -0.02816 134 VAL C N   
1035 C CA  . VAL A 134 ? 1.05088 1.19776 0.76400 0.17483  -0.04981 -0.01153 134 VAL C CA  
1036 C C   . VAL A 134 ? 0.83370 0.98484 0.54974 0.18075  -0.07910 -0.01027 134 VAL C C   
1037 O O   . VAL A 134 ? 1.08538 1.20446 0.73151 0.20206  -0.08292 0.00603  134 VAL C O   
1038 C CB  . VAL A 134 ? 0.83294 0.96451 0.55369 0.15581  -0.00820 0.02375  134 VAL C CB  
1039 C CG1 . VAL A 134 ? 0.62535 0.78027 0.42307 0.12953  -0.01067 0.03603  134 VAL C CG1 
1040 C CG2 . VAL A 134 ? 1.09209 1.22511 0.82110 0.15188  0.02177  0.01761  134 VAL C CG2 
1041 N N   . TYR A 135 ? 0.79079 0.97507 0.58489 0.16332  -0.09532 -0.02718 135 TYR C N   
1042 C CA  . TYR A 135 ? 0.60329 0.79844 0.41876 0.16489  -0.11855 -0.03082 135 TYR C CA  
1043 C C   . TYR A 135 ? 0.51662 0.71693 0.38746 0.13433  -0.10013 -0.00768 135 TYR C C   
1044 O O   . TYR A 135 ? 0.59752 0.80429 0.51029 0.11419  -0.08227 -0.00466 135 TYR C O   
1045 C CB  . TYR A 135 ? 0.66618 0.89630 0.52893 0.17260  -0.15128 -0.08044 135 TYR C CB  
1046 C CG  . TYR A 135 ? 0.86507 1.11442 0.77064 0.17121  -0.17081 -0.09093 135 TYR C CG  
1047 C CD1 . TYR A 135 ? 0.81987 1.06154 0.67719 0.20353  -0.20011 -0.09243 135 TYR C CD1 
1048 C CD2 . TYR A 135 ? 0.88573 1.15446 0.87476 0.14050  -0.15681 -0.09902 135 TYR C CD2 
1049 C CE1 . TYR A 135 ? 1.03296 1.29564 0.93737 0.20401  -0.21767 -0.10554 135 TYR C CE1 
1050 C CE2 . TYR A 135 ? 0.73390 1.02025 0.76560 0.13796  -0.16819 -0.11123 135 TYR C CE2 
1051 C CZ  . TYR A 135 ? 0.89049 1.17876 0.88637 0.16913  -0.20001 -0.11642 135 TYR C CZ  
1052 O OH  . TYR A 135 ? 0.82129 1.13052 0.86732 0.16838  -0.21131 -0.13206 135 TYR C OH  
1053 N N   . GLU A 136 ? 0.69873 0.89180 0.56292 0.13537  -0.10639 0.00747  136 GLU C N   
1054 C CA  . GLU A 136 ? 0.64566 0.84004 0.54914 0.11106  -0.09217 0.02722  136 GLU C CA  
1055 C C   . GLU A 136 ? 0.71392 0.91977 0.64326 0.11270  -0.11006 0.01497  136 GLU C C   
1056 O O   . GLU A 136 ? 0.77932 0.97894 0.67652 0.13587  -0.13012 0.01014  136 GLU C O   
1057 C CB  . GLU A 136 ? 0.82353 0.99320 0.69584 0.10613  -0.07115 0.06054  136 GLU C CB  
1058 C CG  . GLU A 136 ? 0.86809 1.04065 0.77566 0.08576  -0.06343 0.07509  136 GLU C CG  
1059 C CD  . GLU A 136 ? 1.08034 1.23570 0.97559 0.07795  -0.04223 0.09738  136 GLU C CD  
1060 O OE1 . GLU A 136 ? 1.09847 1.24360 0.97312 0.08108  -0.02369 0.10254  136 GLU C OE1 
1061 O OE2 . GLU A 136 ? 1.12410 1.27619 1.03498 0.06747  -0.04097 0.10588  136 GLU C OE2 
1062 N N   . THR A 137 ? 0.57692 0.79438 0.55940 0.09143  -0.10089 0.00981  137 THR C N   
1063 C CA  . THR A 137 ? 0.60338 0.83343 0.62101 0.08904  -0.10935 -0.00551 137 THR C CA  
1064 C C   . THR A 137 ? 0.62992 0.84243 0.62915 0.08459  -0.10333 0.02149  137 THR C C   
1065 O O   . THR A 137 ? 0.72964 0.92289 0.69691 0.08120  -0.09274 0.04867  137 THR C O   
1066 C CB  . THR A 137 ? 0.59163 0.83093 0.66815 0.06743  -0.09161 -0.02422 137 THR C CB  
1067 O OG1 . THR A 137 ? 0.47721 0.69213 0.54214 0.05114  -0.06768 0.00441  137 THR C OG1 
1068 C CG2 . THR A 137 ? 0.68553 0.93894 0.78874 0.06841  -0.09370 -0.05453 137 THR C CG2 
1069 N N   . SER A 138 ? 0.66560 0.88733 0.69425 0.08348  -0.10830 0.00859  138 SER C N   
1070 C CA  . SER A 138 ? 0.45678 0.66225 0.47406 0.07843  -0.10217 0.02795  138 SER C CA  
1071 C C   . SER A 138 ? 0.57064 0.76657 0.59941 0.05508  -0.07900 0.03974  138 SER C C   
1072 O O   . SER A 138 ? 0.57428 0.76986 0.61597 0.04507  -0.06608 0.03611  138 SER C O   
1073 C CB  . SER A 138 ? 0.43136 0.65020 0.47527 0.09045  -0.11685 0.00642  138 SER C CB  
1074 O OG  . SER A 138 ? 0.59692 0.82216 0.62177 0.12147  -0.14611 -0.00755 138 SER C OG  
1075 N N   . PHE A 139 ? 0.44191 0.62406 0.45927 0.04991  -0.07449 0.05316  139 PHE C N   
1076 C CA  . PHE A 139 ? 0.50720 0.67566 0.52004 0.03568  -0.05873 0.06213  139 PHE C CA  
1077 C C   . PHE A 139 ? 0.46675 0.63380 0.50501 0.02790  -0.04229 0.04489  139 PHE C C   
1078 O O   . PHE A 139 ? 0.60129 0.77390 0.65686 0.02946  -0.04281 0.03298  139 PHE C O   
1079 C CB  . PHE A 139 ? 0.59397 0.75033 0.58767 0.03387  -0.06196 0.07524  139 PHE C CB  
1080 C CG  . PHE A 139 ? 0.44202 0.59699 0.42297 0.03487  -0.06635 0.08895  139 PHE C CG  
1081 C CD1 . PHE A 139 ? 0.56399 0.71153 0.53430 0.04293  -0.06914 0.09455  139 PHE C CD1 
1082 C CD2 . PHE A 139 ? 0.56448 0.72159 0.54362 0.03004  -0.06513 0.09464  139 PHE C CD2 
1083 C CE1 . PHE A 139 ? 0.38192 0.52175 0.34393 0.03998  -0.06106 0.10601  139 PHE C CE1 
1084 C CE2 . PHE A 139 ? 0.54162 0.70399 0.52664 0.02812  -0.06412 0.10031  139 PHE C CE2 
1085 C CZ  . PHE A 139 ? 0.44923 0.60170 0.42771 0.02994  -0.05726 0.10620  139 PHE C CZ  
1086 N N   . PHE A 140 ? 0.44173 0.59662 0.48383 0.01968  -0.02274 0.04273  140 PHE C N   
1087 C CA  . PHE A 140 ? 0.47801 0.61790 0.53940 0.00827  0.00733  0.02901  140 PHE C CA  
1088 C C   . PHE A 140 ? 0.51494 0.61793 0.52647 0.00679  0.02193  0.04709  140 PHE C C   
1089 O O   . PHE A 140 ? 0.73753 0.82299 0.70354 0.01413  0.01185  0.06762  140 PHE C O   
1090 C CB  . PHE A 140 ? 0.53186 0.65961 0.61312 -0.00029 0.03067  0.01986  140 PHE C CB  
1091 C CG  . PHE A 140 ? 0.50081 0.66741 0.63691 0.00143  0.01593  -0.00878 140 PHE C CG  
1092 C CD1 . PHE A 140 ? 0.57485 0.76947 0.77960 -0.00483 0.02293  -0.04722 140 PHE C CD1 
1093 C CD2 . PHE A 140 ? 0.58445 0.76174 0.70616 0.01130  -0.00565 -0.00254 140 PHE C CD2 
1094 C CE1 . PHE A 140 ? 0.44675 0.68156 0.70224 0.00192  0.00122  -0.08132 140 PHE C CE1 
1095 C CE2 . PHE A 140 ? 0.68941 0.89936 0.85015 0.01733  -0.02243 -0.03218 140 PHE C CE2 
1096 C CZ  . PHE A 140 ? 0.41719 0.65695 0.64361 0.01420  -0.02264 -0.07284 140 PHE C CZ  
1097 N N   A VAL A 141 ? 0.61434 0.70795 0.63622 -0.00000 0.04388  0.03490  141 VAL C N   
1098 N N   B VAL A 141 ? 0.56985 0.66266 0.59135 -0.00018 0.04464  0.03499  141 VAL C N   
1099 C CA  A VAL A 141 ? 0.64682 0.70150 0.61175 0.00174  0.05839  0.04787  141 VAL C CA  
1100 C CA  B VAL A 141 ? 0.63647 0.69136 0.60163 0.00172  0.05836  0.04767  141 VAL C CA  
1101 C C   A VAL A 141 ? 0.70258 0.70220 0.62194 0.00003  0.09517  0.05970  141 VAL C C   
1102 C C   B VAL A 141 ? 0.70934 0.70839 0.62913 -0.00051 0.09690  0.05871  141 VAL C C   
1103 O O   A VAL A 141 ? 0.80112 0.79126 0.75435 -0.01150 0.12608  0.04928  141 VAL C O   
1104 O O   B VAL A 141 ? 0.80420 0.79311 0.75967 -0.01321 0.13121  0.04643  141 VAL C O   
1105 C CB  A VAL A 141 ? 0.67353 0.73538 0.66312 -0.00337 0.07182  0.02917  141 VAL C CB  
1106 C CB  B VAL A 141 ? 0.68942 0.75396 0.68072 -0.00288 0.06922  0.02892  141 VAL C CB  
1107 C CG1 A VAL A 141 ? 0.72046 0.82149 0.73990 0.00446  0.03507  0.02276  141 VAL C CG1 
1108 C CG1 B VAL A 141 ? 0.64120 0.66654 0.56570 0.00180  0.07910  0.03940  141 VAL C CG1 
1109 C CG2 A VAL A 141 ? 0.60137 0.67001 0.65332 -0.01758 0.10921  0.00221  141 VAL C CG2 
1110 C CG2 B VAL A 141 ? 0.71595 0.82433 0.74764 0.00445  0.03318  0.01970  141 VAL C CG2 
1111 N N   . ASN A 142 ? 0.70712 0.66576 0.54686 0.01408  0.09162  0.07961  142 ASN C N   
1112 C CA  . ASN A 142 ? 0.85344 0.74073 0.62099 0.02200  0.12623  0.09644  142 ASN C CA  
1113 C C   . ASN A 142 ? 0.87301 0.71391 0.58405 0.02378  0.15807  0.09588  142 ASN C C   
1114 O O   . ASN A 142 ? 1.00358 0.87305 0.73335 0.02007  0.14642  0.08183  142 ASN C O   
1115 C CB  . ASN A 142 ? 0.89441 0.76346 0.59985 0.04741  0.09283  0.11782  142 ASN C CB  
1116 C CG  . ASN A 142 ? 0.87122 0.77620 0.62687 0.04580  0.07213  0.11848  142 ASN C CG  
1117 O OD1 . ASN A 142 ? 0.95370 0.86990 0.76466 0.02908  0.09391  0.10806  142 ASN C OD1 
1118 N ND2 . ASN A 142 ? 0.88142 0.80716 0.62325 0.06343  0.03047  0.12557  142 ASN C ND2 
1119 N N   . ARG A 143 ? 0.92820 0.68820 0.56205 0.03139  0.20264  0.11223  143 ARG C N   
1120 C CA  . ARG A 143 ? 1.10528 0.80690 0.66912 0.03480  0.24328  0.11329  143 ARG C CA  
1121 C C   . ARG A 143 ? 1.14498 0.83467 0.62017 0.06403  0.20058  0.12069  143 ARG C C   
1122 O O   . ARG A 143 ? 1.30207 0.96907 0.73745 0.06552  0.21917  0.11220  143 ARG C O   
1123 C CB  . ARG A 143 ? 1.22752 0.82958 0.72058 0.03638  0.31223  0.13172  143 ARG C CB  
1124 C CG  . ARG A 143 ? 1.43565 1.04320 1.02658 -0.00099 0.37617  0.10962  143 ARG C CG  
1125 C CD  . ARG A 143 ? 1.80172 1.29946 1.32546 -0.00298 0.45422  0.12858  143 ARG C CD  
1126 N NE  . ARG A 143 ? 1.96496 1.43530 1.46408 0.01190  0.43674  0.14996  143 ARG C NE  
1127 C CZ  . ARG A 143 ? 2.07434 1.46698 1.54574 0.01558  0.47677  0.15767  143 ARG C CZ  
1128 N NH1 . ARG A 143 ? 2.04998 1.37903 1.51102 0.00520  0.53872  0.14725  143 ARG C NH1 
1129 N NH2 . ARG A 143 ? 2.13473 1.50885 1.58785 0.03130  0.45703  0.17520  143 ARG C NH2 
1130 N N   . ASP A 144 ? 1.13617 0.84414 0.58696 0.08726  0.14412  0.13058  144 ASP C N   
1131 C CA  . ASP A 144 ? 1.06218 0.77934 0.45801 0.11302  0.09362  0.12523  144 ASP C CA  
1132 C C   . ASP A 144 ? 1.04759 0.85243 0.53833 0.09637  0.05161  0.10235  144 ASP C C   
1133 O O   . ASP A 144 ? 1.18144 1.01055 0.65858 0.11233  0.00404  0.09180  144 ASP C O   
1134 C CB  . ASP A 144 ? 1.09924 0.79326 0.42857 0.14987  0.05372  0.14020  144 ASP C CB  
1135 C CG  . ASP A 144 ? 1.14061 0.89996 0.55981 0.14162  0.02007  0.13869  144 ASP C CG  
1136 O OD1 . ASP A 144 ? 1.24912 1.04104 0.75304 0.11134  0.04293  0.13639  144 ASP C OD1 
1137 O OD2 . ASP A 144 ? 1.23656 1.01590 0.64267 0.16746  -0.02982 0.13598  144 ASP C OD2 
1138 N N   . TYR A 145 ? 1.10758 0.95673 0.69404 0.06690  0.06857  0.09226  145 TYR C N   
1139 C CA  . TYR A 145 ? 1.06430 0.97971 0.73099 0.05320  0.03858  0.07509  145 TYR C CA  
1140 C C   . TYR A 145 ? 0.93703 0.89602 0.63780 0.05807  -0.00700 0.07751  145 TYR C C   
1141 O O   . TYR A 145 ? 0.97098 0.96996 0.71818 0.05109  -0.03164 0.06584  145 TYR C O   
1142 C CB  . TYR A 145 ? 0.86839 0.77877 0.51047 0.05643  0.03292  0.05881  145 TYR C CB  
1143 C CG  . TYR A 145 ? 0.97355 0.84270 0.58839 0.05004  0.08466  0.05338  145 TYR C CG  
1144 C CD1 . TYR A 145 ? 0.82610 0.70275 0.50239 0.03020  0.12525  0.04925  145 TYR C CD1 
1145 C CD2 . TYR A 145 ? 1.08469 0.90804 0.61514 0.06454  0.09473  0.04769  145 TYR C CD2 
1146 C CE1 . TYR A 145 ? 0.81844 0.66112 0.48530 0.02116  0.17982  0.03886  145 TYR C CE1 
1147 C CE2 . TYR A 145 ? 1.16130 0.94247 0.66565 0.05745  0.15116  0.04199  145 TYR C CE2 
1148 C CZ  . TYR A 145 ? 0.97585 0.76807 0.55448 0.03388  0.19638  0.03737  145 TYR C CZ  
1149 O OH  . TYR A 145 ? 1.08463 0.83898 0.65288 0.02365  0.25925  0.02623  145 TYR C OH  
1150 N N   . SER A 146 ? 0.96670 0.91369 0.64669 0.06972  -0.01330 0.09181  146 SER C N   
1151 C CA  . SER A 146 ? 0.83416 0.82556 0.56399 0.06938  -0.04360 0.09267  146 SER C CA  
1152 C C   . SER A 146 ? 0.79079 0.80442 0.58181 0.05089  -0.02488 0.09513  146 SER C C   
1153 O O   . SER A 146 ? 0.79653 0.80065 0.60384 0.03848  0.00516  0.09051  146 SER C O   
1154 C CB  . SER A 146 ? 0.86864 0.83953 0.55082 0.09537  -0.06303 0.10223  146 SER C CB  
1155 O OG  . SER A 146 ? 0.99223 0.91211 0.63381 0.10106  -0.03052 0.12000  146 SER C OG  
1156 N N   . PHE A 147 ? 0.69579 0.74124 0.52419 0.05036  -0.04265 0.09762  147 PHE C N   
1157 C CA  . PHE A 147 ? 0.64813 0.71636 0.52655 0.03796  -0.03249 0.09573  147 PHE C CA  
1158 C C   . PHE A 147 ? 0.74295 0.80972 0.62297 0.04458  -0.03391 0.10360  147 PHE C C   
1159 O O   . PHE A 147 ? 0.77466 0.83498 0.63049 0.05961  -0.04996 0.11003  147 PHE C O   
1160 C CB  . PHE A 147 ? 0.59239 0.69770 0.51249 0.03093  -0.04861 0.08938  147 PHE C CB  
1161 C CG  . PHE A 147 ? 0.54353 0.64793 0.46822 0.02596  -0.04662 0.08067  147 PHE C CG  
1162 C CD1 . PHE A 147 ? 0.76355 0.86427 0.67271 0.02779  -0.05908 0.07676  147 PHE C CD1 
1163 C CD2 . PHE A 147 ? 0.51215 0.62240 0.46352 0.02130  -0.03458 0.07099  147 PHE C CD2 
1164 C CE1 . PHE A 147 ? 0.79362 0.89008 0.70794 0.02361  -0.05560 0.06710  147 PHE C CE1 
1165 C CE2 . PHE A 147 ? 0.60305 0.71206 0.56217 0.01995  -0.03313 0.06147  147 PHE C CE2 
1166 C CZ  . PHE A 147 ? 0.77348 0.87236 0.71117 0.02037  -0.04166 0.06142  147 PHE C CZ  
1167 N N   . HIS A 148 ? 0.61409 0.68920 0.52719 0.03565  -0.01944 0.09823  148 HIS C N   
1168 C CA  . HIS A 148 ? 0.66596 0.74465 0.59016 0.03991  -0.02039 0.10105  148 HIS C CA  
1169 C C   . HIS A 148 ? 0.55919 0.67279 0.52806 0.03221  -0.02454 0.08772  148 HIS C C   
1170 O O   . HIS A 148 ? 0.52385 0.65093 0.51529 0.02568  -0.02248 0.07473  148 HIS C O   
1171 C CB  . HIS A 148 ? 0.66246 0.69399 0.56327 0.04233  0.00756  0.10629  148 HIS C CB  
1172 C CG  . HIS A 148 ? 0.65181 0.67703 0.58759 0.02484  0.03849  0.08989  148 HIS C CG  
1173 N ND1 . HIS A 148 ? 0.84700 0.84070 0.77010 0.01644  0.06900  0.08693  148 HIS C ND1 
1174 C CD2 . HIS A 148 ? 0.60611 0.65505 0.59567 0.01455  0.04436  0.06958  148 HIS C CD2 
1175 C CE1 . HIS A 148 ? 0.55319 0.55627 0.53335 -0.00086 0.09423  0.06337  148 HIS C CE1 
1176 N NE2 . HIS A 148 ? 0.51113 0.54958 0.53265 -0.00114 0.07598  0.05077  148 HIS C NE2 
1177 N N   . LYS A 149 ? 0.45535 0.58251 0.43315 0.03738  -0.03246 0.08886  149 LYS C N   
1178 C CA  . LYS A 149 ? 0.51710 0.67107 0.51790 0.03697  -0.03964 0.07718  149 LYS C CA  
1179 C C   . LYS A 149 ? 0.52472 0.67791 0.53362 0.04075  -0.03470 0.07242  149 LYS C C   
1180 O O   . LYS A 149 ? 0.71997 0.86037 0.71792 0.04698  -0.03274 0.08317  149 LYS C O   
1181 C CB  . LYS A 149 ? 0.38851 0.55848 0.38171 0.04043  -0.05300 0.08492  149 LYS C CB  
1182 C CG  . LYS A 149 ? 0.69922 0.88158 0.69069 0.04724  -0.05801 0.07819  149 LYS C CG  
1183 C CD  . LYS A 149 ? 0.67185 0.85358 0.64858 0.04917  -0.05646 0.09101  149 LYS C CD  
1184 C CE  . LYS A 149 ? 0.63759 0.80999 0.60606 0.04714  -0.05898 0.09733  149 LYS C CE  
1185 N NZ  . LYS A 149 ? 0.66985 0.83710 0.62283 0.05949  -0.06854 0.09024  149 LYS C NZ  
1186 N N   . LEU A 150 ? 0.43174 0.59960 0.46097 0.04038  -0.03599 0.05232  150 LEU C N   
1187 C CA  . LEU A 150 ? 0.52021 0.68845 0.56029 0.04348  -0.03130 0.04107  150 LEU C CA  
1188 C C   . LEU A 150 ? 0.53210 0.72209 0.56006 0.05417  -0.04562 0.03428  150 LEU C C   
1189 O O   . LEU A 150 ? 0.55256 0.75481 0.57122 0.06052  -0.05941 0.02675  150 LEU C O   
1190 C CB  . LEU A 150 ? 0.48526 0.64808 0.56233 0.03400  -0.01738 0.01425  150 LEU C CB  
1191 C CG  . LEU A 150 ? 0.51365 0.63616 0.59458 0.02293  0.01214  0.02134  150 LEU C CG  
1192 C CD1 . LEU A 150 ? 0.55561 0.67526 0.63769 0.01497  0.01859  0.02299  150 LEU C CD1 
1193 C CD2 . LEU A 150 ? 0.62984 0.73876 0.75300 0.01199  0.03567  -0.00578 150 LEU C CD2 
1194 N N   . SER A 151 ? 0.49671 0.68564 0.51848 0.05968  -0.04069 0.03722  151 SER C N   
1195 C CA  . SER A 151 ? 0.57628 0.77565 0.57610 0.07090  -0.04526 0.03066  151 SER C CA  
1196 C C   . SER A 151 ? 0.52466 0.72541 0.53824 0.07467  -0.04181 0.00677  151 SER C C   
1197 O O   . SER A 151 ? 0.64513 0.83350 0.68342 0.06893  -0.02977 0.00559  151 SER C O   
1198 C CB  . SER A 151 ? 0.53165 0.73051 0.51714 0.07255  -0.03541 0.05137  151 SER C CB  
1199 O OG  . SER A 151 ? 0.56890 0.76643 0.52189 0.08304  -0.02975 0.04767  151 SER C OG  
1200 N N   . TYR A 152 ? 0.54205 0.75190 0.53288 0.08769  -0.05284 -0.01313 152 TYR C N   
1201 C CA  . TYR A 152 ? 0.67812 0.89289 0.68301 0.09252  -0.05432 -0.04530 152 TYR C CA  
1202 C C   . TYR A 152 ? 0.81277 1.02393 0.77151 0.10863  -0.04986 -0.04581 152 TYR C C   
1203 O O   . TYR A 152 ? 0.76155 0.96494 0.66753 0.12048  -0.05053 -0.03005 152 TYR C O   
1204 C CB  . TYR A 152 ? 0.48079 0.71432 0.50653 0.09713  -0.07707 -0.08406 152 TYR C CB  
1205 C CG  . TYR A 152 ? 0.43474 0.67161 0.51374 0.07871  -0.07254 -0.08892 152 TYR C CG  
1206 C CD1 . TYR A 152 ? 0.42048 0.66156 0.49081 0.07903  -0.08149 -0.07360 152 TYR C CD1 
1207 C CD2 . TYR A 152 ? 0.55953 0.78819 0.69549 0.06063  -0.05293 -0.10890 152 TYR C CD2 
1208 C CE1 . TYR A 152 ? 0.49841 0.74045 0.61523 0.06216  -0.07162 -0.07960 152 TYR C CE1 
1209 C CE2 . TYR A 152 ? 0.67470 0.89739 0.85411 0.04247  -0.03793 -0.11265 152 TYR C CE2 
1210 C CZ  . TYR A 152 ? 0.48178 0.71370 0.65130 0.04346  -0.04764 -0.09868 152 TYR C CZ  
1211 O OH  . TYR A 152 ? 0.69511 0.91937 0.90585 0.02543  -0.02750 -0.10404 152 TYR C OH  
1212 N N   . LEU A 153 ? 0.73960 0.94917 0.71561 0.10915  -0.03987 -0.06401 153 LEU C N   
1213 C CA  . LEU A 153 ? 0.76947 0.97390 0.70459 0.12390  -0.02960 -0.06939 153 LEU C CA  
1214 C C   . LEU A 153 ? 0.75266 0.96163 0.70566 0.12923  -0.03582 -0.11197 153 LEU C C   
1215 O O   . LEU A 153 ? 0.77928 0.98328 0.78483 0.11715  -0.02371 -0.12034 153 LEU C O   
1216 C CB  . LEU A 153 ? 0.69136 0.89055 0.63978 0.11796  -0.00243 -0.04357 153 LEU C CB  
1217 C CG  . LEU A 153 ? 0.58749 0.78211 0.51005 0.12969  0.01817  -0.05325 153 LEU C CG  
1218 C CD1 . LEU A 153 ? 0.72670 0.90653 0.57119 0.14388  0.02548  -0.04574 153 LEU C CD1 
1219 C CD2 . LEU A 153 ? 0.63648 0.83685 0.60254 0.12366  0.04135  -0.03839 153 LEU C CD2 
1220 N N   . THR A 154 ? 0.69410 0.90730 0.59917 0.15014  -0.05519 -0.14029 154 THR C N   
1221 C CA  . THR A 154 ? 0.83177 1.05220 0.75081 0.15781  -0.06414 -0.18861 154 THR C CA  
1222 C C   . THR A 154 ? 0.88350 1.08844 0.77375 0.16533  -0.03723 -0.18546 154 THR C C   
1223 O O   . THR A 154 ? 1.00260 1.19253 0.82754 0.17770  -0.02122 -0.16080 154 THR C O   
1224 C CB  . THR A 154 ? 0.81599 1.04968 0.68972 0.18459  -0.10354 -0.22708 154 THR C CB  
1225 O OG1 . THR A 154 ? 1.11714 1.32668 0.88466 0.21174  -0.10239 -0.20290 154 THR C OG1 
1226 C CG2 . THR A 154 ? 0.66691 0.92348 0.58564 0.17809  -0.13032 -0.23719 154 THR C CG2 
1227 N N   . PHE A 155 ? 0.79356 0.99813 0.73609 0.15706  -0.02693 -0.21188 155 PHE C N   
1228 C CA  . PHE A 155 ? 0.95666 1.14871 0.88827 0.16318  0.00096  -0.21121 155 PHE C CA  
1229 C C   . PHE A 155 ? 0.91565 1.10695 0.88519 0.16360  -0.00140 -0.26151 155 PHE C C   
1230 O O   . PHE A 155 ? 0.82513 1.02497 0.84484 0.15324  -0.01897 -0.29420 155 PHE C O   
1231 C CB  . PHE A 155 ? 0.87272 1.05792 0.84610 0.14983  0.02779  -0.17068 155 PHE C CB  
1232 C CG  . PHE A 155 ? 0.85147 1.02595 0.89695 0.13457  0.03074  -0.17232 155 PHE C CG  
1233 C CD1 . PHE A 155 ? 0.79457 0.96757 0.86693 0.11991  0.01851  -0.16465 155 PHE C CD1 
1234 C CD2 . PHE A 155 ? 0.73564 0.89357 0.81664 0.13703  0.05029  -0.18049 155 PHE C CD2 
1235 C CE1 . PHE A 155 ? 0.67827 0.82585 0.80245 0.10706  0.03087  -0.16256 155 PHE C CE1 
1236 C CE2 . PHE A 155 ? 0.78702 0.91777 0.91877 0.12735  0.05806  -0.17720 155 PHE C CE2 
1237 C CZ  . PHE A 155 ? 0.75481 0.87649 0.90355 0.11190  0.05096  -0.16686 155 PHE C CZ  
1238 N N   . ILE A 156 ? 0.78008 0.96102 0.73253 0.17407  0.02056  -0.27112 156 ILE C N   
1239 C CA  . ILE A 156 ? 0.87412 1.04876 0.86414 0.17473  0.02506  -0.31780 156 ILE C CA  
1240 C C   . ILE A 156 ? 0.82006 0.97569 0.87088 0.16418  0.05593  -0.29549 156 ILE C C   
1241 O O   . ILE A 156 ? 0.92855 1.08196 0.96439 0.17307  0.07909  -0.27261 156 ILE C O   
1242 C CB  . ILE A 156 ? 1.18428 1.35672 1.10218 0.20002  0.02611  -0.35065 156 ILE C CB  
1243 C CG1 . ILE A 156 ? 0.91171 1.09489 0.75285 0.22084  -0.01155 -0.37213 156 ILE C CG1 
1244 C CG2 . ILE A 156 ? 0.94037 1.10598 0.90401 0.19955  0.03202  -0.40239 156 ILE C CG2 
1245 C CD1 . ILE A 156 ? 1.05751 1.26444 0.95498 0.21428  -0.05121 -0.42098 156 ILE C CD1 
1246 N N   . PRO A 157 ? 0.74050 0.87843 0.85976 0.14779  0.05934  -0.30217 157 PRO C N   
1247 C CA  . PRO A 157 ? 0.88738 0.99549 1.04925 0.14642  0.08475  -0.27584 157 PRO C CA  
1248 C C   . PRO A 157 ? 0.87742 0.97535 1.04513 0.16175  0.10483  -0.29699 157 PRO C C   
1249 O O   . PRO A 157 ? 0.99804 1.07898 1.19266 0.16016  0.11033  -0.34020 157 PRO C O   
1250 C CB  . PRO A 157 ? 0.72964 0.80584 0.94732 0.12736  0.08973  -0.28676 157 PRO C CB  
1251 C CG  . PRO A 157 ? 0.82896 0.93255 1.04293 0.11423  0.06559  -0.30306 157 PRO C CG  
1252 C CD  . PRO A 157 ? 0.86887 1.00933 1.02879 0.13100  0.04263  -0.33178 157 PRO C CD  
1253 N N   . SER A 158 ? 1.00422 1.11427 1.15526 0.17554  0.11811  -0.27152 158 SER C N   
1254 C CA  . SER A 158 ? 1.04527 1.14827 1.21302 0.19147  0.14135  -0.28816 158 SER C CA  
1255 C C   . SER A 158 ? 1.03926 1.12430 1.25763 0.20049  0.15068  -0.25731 158 SER C C   
1256 O O   . SER A 158 ? 1.09057 1.17758 1.31464 0.19752  0.13953  -0.21906 158 SER C O   
1257 C CB  . SER A 158 ? 1.05810 1.18851 1.17645 0.20292  0.15605  -0.29061 158 SER C CB  
1258 O OG  . SER A 158 ? 1.07669 1.22750 1.20166 0.20268  0.16325  -0.24988 158 SER C OG  
1259 N N   . ASP A 159 ? 1.15450 1.21996 1.40602 0.21601  0.16847  -0.27692 159 ASP C N   
1260 C CA  . ASP A 159 ? 1.21571 1.25828 1.51081 0.23476  0.17214  -0.25227 159 ASP C CA  
1261 C C   . ASP A 159 ? 1.17543 1.26260 1.48511 0.24873  0.17150  -0.22987 159 ASP C C   
1262 O O   . ASP A 159 ? 1.04143 1.11994 1.38429 0.26833  0.16202  -0.20756 159 ASP C O   
1263 C CB  . ASP A 159 ? 1.31343 1.31962 1.64198 0.25100  0.19122  -0.28283 159 ASP C CB  
1264 C CG  . ASP A 159 ? 1.54010 1.57526 1.85868 0.25488  0.20909  -0.32439 159 ASP C CG  
1265 O OD1 . ASP A 159 ? 1.44592 1.52317 1.72426 0.24761  0.20974  -0.32506 159 ASP C OD1 
1266 O OD2 . ASP A 159 ? 1.57589 1.58408 1.92032 0.26677  0.22570  -0.35604 159 ASP C OD2 
1267 N N   . ASP A 160 ? 1.19754 1.32849 1.48259 0.24081  0.18214  -0.23736 160 ASP C N   
1268 C CA  . ASP A 160 ? 1.09021 1.26522 1.40594 0.24949  0.19381  -0.22771 160 ASP C CA  
1269 C C   . ASP A 160 ? 1.03551 1.23711 1.33779 0.23511  0.17973  -0.19561 160 ASP C C   
1270 O O   . ASP A 160 ? 1.01681 1.24885 1.36824 0.24359  0.17548  -0.18334 160 ASP C O   
1271 C CB  . ASP A 160 ? 1.12240 1.31760 1.42049 0.24981  0.22990  -0.25734 160 ASP C CB  
1272 C CG  . ASP A 160 ? 1.10038 1.33726 1.46198 0.26116  0.25442  -0.26165 160 ASP C CG  
1273 O OD1 . ASP A 160 ? 1.20916 1.45048 1.64073 0.28347  0.24743  -0.26810 160 ASP C OD1 
1274 O OD2 . ASP A 160 ? 1.26936 1.53176 1.61258 0.24919  0.28294  -0.26092 160 ASP C OD2 
1275 N N   . ASP A 161 ? 1.07144 1.26437 1.31427 0.21555  0.16979  -0.18617 161 ASP C N   
1276 C CA  . ASP A 161 ? 0.73251 0.94834 0.95676 0.20157  0.16295  -0.15938 161 ASP C CA  
1277 C C   . ASP A 161 ? 0.77775 0.99394 1.03530 0.20396  0.13469  -0.13136 161 ASP C C   
1278 O O   . ASP A 161 ? 0.81371 0.99595 1.07722 0.21151  0.11773  -0.12548 161 ASP C O   
1279 C CB  . ASP A 161 ? 0.92813 1.13068 1.07842 0.18684  0.15505  -0.15869 161 ASP C CB  
1280 C CG  . ASP A 161 ? 1.17446 1.37301 1.26844 0.19115  0.17970  -0.18407 161 ASP C CG  
1281 O OD1 . ASP A 161 ? 1.21110 1.42242 1.31743 0.19745  0.21385  -0.19221 161 ASP C OD1 
1282 O OD2 . ASP A 161 ? 1.11916 1.30151 1.15581 0.19039  0.16496  -0.19900 161 ASP C OD2 
1283 N N   . ILE A 162 ? 0.75738 1.00671 1.03263 0.19808  0.13325  -0.11545 162 ILE C N   
1284 C CA  . ILE A 162 ? 0.56846 0.82363 0.86771 0.20244  0.10389  -0.09255 162 ILE C CA  
1285 C C   . ILE A 162 ? 0.54132 0.80651 0.80549 0.17985  0.09962  -0.07370 162 ILE C C   
1286 O O   . ILE A 162 ? 0.66415 0.95355 0.92848 0.16789  0.12308  -0.07691 162 ILE C O   
1287 C CB  . ILE A 162 ? 0.56327 0.85801 0.93961 0.22220  0.10004  -0.10181 162 ILE C CB  
1288 C CG1 . ILE A 162 ? 0.65041 0.93543 1.06314 0.24857  0.10677  -0.12329 162 ILE C CG1 
1289 C CG2 . ILE A 162 ? 0.54597 0.84248 0.93451 0.23403  0.06149  -0.08239 162 ILE C CG2 
1290 C CD1 . ILE A 162 ? 0.59622 0.93174 1.09783 0.27065  0.10537  -0.14349 162 ILE C CD1 
1291 N N   . TYR A 163 ? 0.57214 0.81274 0.80544 0.17423  0.07520  -0.05426 163 TYR C N   
1292 C CA  . TYR A 163 ? 0.58477 0.82967 0.78326 0.15501  0.06875  -0.03744 163 TYR C CA  
1293 C C   . TYR A 163 ? 0.48643 0.74370 0.70863 0.15777  0.04560  -0.02003 163 TYR C C   
1294 O O   . TYR A 163 ? 0.48787 0.72943 0.72345 0.17624  0.02582  -0.01451 163 TYR C O   
1295 C CB  . TYR A 163 ? 0.51011 0.72330 0.65987 0.14519  0.05995  -0.03575 163 TYR C CB  
1296 C CG  . TYR A 163 ? 0.64501 0.85122 0.76434 0.14424  0.07447  -0.05951 163 TYR C CG  
1297 C CD1 . TYR A 163 ? 0.67692 0.86477 0.80966 0.15299  0.08001  -0.08168 163 TYR C CD1 
1298 C CD2 . TYR A 163 ? 0.57963 0.79164 0.64997 0.13833  0.08180  -0.06115 163 TYR C CD2 
1299 C CE1 . TYR A 163 ? 0.73967 0.92331 0.84308 0.15442  0.08914  -0.10996 163 TYR C CE1 
1300 C CE2 . TYR A 163 ? 0.68257 0.88485 0.71090 0.14483  0.08935  -0.08564 163 TYR C CE2 
1301 C CZ  . TYR A 163 ? 0.75288 0.94513 0.80056 0.15215  0.09131  -0.11255 163 TYR C CZ  
1302 O OH  . TYR A 163 ? 0.84979 1.03456 0.85444 0.16070  0.09488  -0.14321 163 TYR C OH  
1303 N N   . ASP A 164 ? 0.49365 0.77243 0.71374 0.14217  0.04862  -0.01212 164 ASP C N   
1304 C CA  . ASP A 164 ? 0.43796 0.73220 0.67942 0.14239  0.02584  -0.00141 164 ASP C CA  
1305 C C   . ASP A 164 ? 0.47831 0.76095 0.67593 0.12232  0.02352  0.01504  164 ASP C C   
1306 O O   . ASP A 164 ? 0.60338 0.88048 0.76950 0.10914  0.04426  0.01580  164 ASP C O   
1307 C CB  . ASP A 164 ? 0.43066 0.77383 0.74428 0.14357  0.03385  -0.01847 164 ASP C CB  
1308 C CG  . ASP A 164 ? 0.53013 0.89277 0.90059 0.16963  0.02808  -0.03871 164 ASP C CG  
1309 O OD1 . ASP A 164 ? 0.78815 1.12311 1.14172 0.19374  0.00243  -0.03213 164 ASP C OD1 
1310 O OD2 . ASP A 164 ? 0.66643 1.06758 1.09848 0.16716  0.05278  -0.06161 164 ASP C OD2 
1311 N N   . CYS A 165 ? 0.53964 0.81370 0.72830 0.12429  -0.00197 0.02788  165 CYS C N   
1312 C CA  . CYS A 165 ? 0.54286 0.80918 0.69981 0.10749  -0.00632 0.04134  165 CYS C CA  
1313 C C   . CYS A 165 ? 0.54870 0.84430 0.74378 0.10453  -0.01699 0.03876  165 CYS C C   
1314 O O   . CYS A 165 ? 0.69343 0.99173 0.89941 0.11970  -0.04418 0.03843  165 CYS C O   
1315 C CB  . CYS A 165 ? 0.40699 0.63759 0.52385 0.10912  -0.02098 0.05359  165 CYS C CB  
1316 S SG  . CYS A 165 ? 0.78985 1.01409 0.87597 0.09148  -0.02718 0.06615  165 CYS C SG  
1317 N N   . LYS A 166 ? 0.45918 0.77137 0.67073 0.08690  0.00557  0.03498  166 LYS C N   
1318 C CA  . LYS A 166 ? 0.52792 0.87078 0.79145 0.07848  0.00196  0.02456  166 LYS C CA  
1319 C C   . LYS A 166 ? 0.64392 0.96864 0.87230 0.06732  -0.01043 0.03882  166 LYS C C   
1320 O O   . LYS A 166 ? 0.58292 0.87932 0.76192 0.05645  0.00452  0.05397  166 LYS C O   
1321 C CB  . LYS A 166 ? 0.50412 0.86470 0.80917 0.06144  0.04458  0.01193  166 LYS C CB  
1322 C CG  . LYS A 166 ? 0.63218 1.03359 1.02072 0.04994  0.04641  -0.01101 166 LYS C CG  
1323 C CD  . LYS A 166 ? 0.52267 0.93958 0.96602 0.03213  0.10016  -0.02814 166 LYS C CD  
1324 C CE  . LYS A 166 ? 0.62006 1.08312 1.16796 0.01596  0.10629  -0.06026 166 LYS C CE  
1325 N NZ  . LYS A 166 ? 0.86394 1.33875 1.47573 -0.00581 0.17076  -0.07997 166 LYS C NZ  
1326 N N   . VAL A 167 ? 0.52244 0.86300 0.77373 0.07427  -0.04049 0.03120  167 VAL C N   
1327 C CA  . VAL A 167 ? 0.45833 0.78295 0.67938 0.06602  -0.05392 0.04074  167 VAL C CA  
1328 C C   . VAL A 167 ? 0.52081 0.88008 0.80568 0.05506  -0.05700 0.01824  167 VAL C C   
1329 O O   . VAL A 167 ? 0.43260 0.82927 0.77237 0.06948  -0.08124 -0.00688 167 VAL C O   
1330 C CB  . VAL A 167 ? 0.43886 0.73952 0.61358 0.08589  -0.08524 0.05059  167 VAL C CB  
1331 C CG1 . VAL A 167 ? 0.36057 0.64693 0.50731 0.07731  -0.09554 0.05650  167 VAL C CG1 
1332 C CG2 . VAL A 167 ? 0.38167 0.64723 0.50904 0.09095  -0.07475 0.06684  167 VAL C CG2 
1333 N N   . GLU A 168 ? 0.51641 0.86236 0.79738 0.03188  -0.03383 0.02366  168 GLU C N   
1334 C CA  . GLU A 168 ? 0.40966 0.78108 0.75516 0.01535  -0.02964 0.00003  168 GLU C CA  
1335 C C   . GLU A 168 ? 0.34963 0.69825 0.65686 0.01085  -0.04667 0.00826  168 GLU C C   
1336 O O   . GLU A 168 ? 0.51374 0.82140 0.75889 0.00556  -0.03339 0.03424  168 GLU C O   
1337 C CB  . GLU A 168 ? 0.43490 0.79891 0.81340 -0.01021 0.02507  -0.00206 168 GLU C CB  
1338 C CG  . GLU A 168 ? 0.71111 1.10087 1.13847 -0.00871 0.05005  -0.01640 168 GLU C CG  
1339 C CD  . GLU A 168 ? 1.05849 1.43799 1.52707 -0.03643 0.11283  -0.02376 168 GLU C CD  
1340 O OE1 . GLU A 168 ? 1.07373 1.42700 1.54133 -0.05655 0.13413  -0.01998 168 GLU C OE1 
1341 O OE2 . GLU A 168 ? 1.11394 1.50538 1.61372 -0.03801 0.14584  -0.03325 168 GLU C OE2 
1342 N N   . HIS A 169 ? 0.41292 0.79012 0.75858 0.01612  -0.07858 -0.01809 169 HIS C N   
1343 C CA  . HIS A 169 ? 0.35664 0.71381 0.66607 0.01442  -0.09654 -0.01530 169 HIS C CA  
1344 C C   . HIS A 169 ? 0.36448 0.76164 0.75035 0.00769  -0.11434 -0.05760 169 HIS C C   
1345 O O   . HIS A 169 ? 0.66068 1.10754 1.12369 0.01378  -0.12766 -0.09180 169 HIS C O   
1346 C CB  . HIS A 169 ? 0.41207 0.74616 0.64496 0.04120  -0.12925 0.00111  169 HIS C CB  
1347 C CG  . HIS A 169 ? 0.50533 0.80946 0.68848 0.03800  -0.13618 0.00945  169 HIS C CG  
1348 N ND1 . HIS A 169 ? 0.52106 0.83590 0.70750 0.04667  -0.16644 -0.01415 169 HIS C ND1 
1349 C CD2 . HIS A 169 ? 0.49935 0.76563 0.63133 0.02949  -0.11799 0.03434  169 HIS C CD2 
1350 C CE1 . HIS A 169 ? 0.52670 0.80797 0.66333 0.04130  -0.16148 -0.00152 169 HIS C CE1 
1351 N NE2 . HIS A 169 ? 0.57403 0.82787 0.68231 0.03086  -0.13245 0.02726  169 HIS C NE2 
1352 N N   . TRP A 170 ? 0.37612 0.75445 0.74739 -0.00409 -0.11579 -0.06037 170 TRP C N   
1353 C CA  . TRP A 170 ? 0.38478 0.79968 0.83071 -0.01243 -0.13370 -0.10656 170 TRP C CA  
1354 C C   . TRP A 170 ? 0.40174 0.85389 0.84936 0.02271  -0.19466 -0.13699 170 TRP C C   
1355 O O   . TRP A 170 ? 0.50815 1.01398 1.04408 0.02393  -0.21871 -0.18842 170 TRP C O   
1356 C CB  . TRP A 170 ? 0.50803 0.88716 0.92644 -0.02900 -0.12346 -0.10167 170 TRP C CB  
1357 C CG  . TRP A 170 ? 0.51622 0.85646 0.94316 -0.05932 -0.06618 -0.08066 170 TRP C CG  
1358 C CD1 . TRP A 170 ? 0.43826 0.77996 0.91812 -0.07935 -0.02066 -0.08120 170 TRP C CD1 
1359 C CD2 . TRP A 170 ? 0.52388 0.80957 0.89553 -0.06811 -0.04643 -0.05498 170 TRP C CD2 
1360 N NE1 . TRP A 170 ? 0.54775 0.83016 0.99538 -0.09754 0.02654  -0.05389 170 TRP C NE1 
1361 C CE2 . TRP A 170 ? 0.54000 0.78990 0.92444 -0.08935 0.00806  -0.03827 170 TRP C CE2 
1362 C CE3 . TRP A 170 ? 0.57011 0.83057 0.88087 -0.05766 -0.06747 -0.04541 170 TRP C CE3 
1363 C CZ2 . TRP A 170 ? 0.53739 0.72553 0.87141 -0.09526 0.03545  -0.01131 170 TRP C CZ2 
1364 C CZ3 . TRP A 170 ? 0.49226 0.70171 0.76863 -0.06718 -0.03974 -0.02289 170 TRP C CZ3 
1365 C CH2 . TRP A 170 ? 0.51339 0.68640 0.79947 -0.08335 0.00800  -0.00554 170 TRP C CH2 
1366 N N   . GLY A 171 ? 0.45883 0.88012 0.80984 0.05358  -0.21942 -0.10877 171 GLY C N   
1367 C CA  . GLY A 171 ? 0.61995 1.05596 0.94243 0.09586  -0.27520 -0.12888 171 GLY C CA  
1368 C C   . GLY A 171 ? 0.57384 1.04092 0.92854 0.12215  -0.29375 -0.13819 171 GLY C C   
1369 O O   . GLY A 171 ? 0.51759 0.95773 0.80748 0.15844  -0.32347 -0.13533 171 GLY C O   
1370 N N   . LEU A 172 ? 0.53490 1.02932 0.96665 0.09920  -0.25828 -0.14053 172 LEU C N   
1371 C CA  . LEU A 172 ? 0.49084 1.01615 0.96360 0.12131  -0.26885 -0.15133 172 LEU C CA  
1372 C C   . LEU A 172 ? 0.42126 1.00199 1.01965 0.10046  -0.25522 -0.19933 172 LEU C C   
1373 O O   . LEU A 172 ? 0.60545 1.20765 1.28020 0.06056  -0.20976 -0.20740 172 LEU C O   
1374 C CB  . LEU A 172 ? 0.40010 0.89050 0.83425 0.11124  -0.22593 -0.10782 172 LEU C CB  
1375 C CG  . LEU A 172 ? 0.41544 0.83704 0.72639 0.12516  -0.22425 -0.05980 172 LEU C CG  
1376 C CD1 . LEU A 172 ? 0.39045 0.78775 0.68423 0.10918  -0.18084 -0.02901 172 LEU C CD1 
1377 C CD2 . LEU A 172 ? 0.46798 0.87233 0.72155 0.17433  -0.27042 -0.05949 172 LEU C CD2 
1378 N N   . GLU A 173 ? 0.47284 1.06976 1.08966 0.12761  -0.28944 -0.23182 173 GLU C N   
1379 C CA  . GLU A 173 ? 0.48072 1.12956 1.21986 0.11118  -0.27597 -0.28205 173 GLU C CA  
1380 C C   . GLU A 173 ? 0.45940 1.12717 1.25496 0.09708  -0.23336 -0.27389 173 GLU C C   
1381 O O   . GLU A 173 ? 0.56645 1.26210 1.45940 0.06229  -0.18871 -0.29957 173 GLU C O   
1382 C CB  . GLU A 173 ? 0.55181 1.21558 1.29511 0.15067  -0.32867 -0.32267 173 GLU C CB  
1383 N N   . GLU A 174 ? 0.75176 1.39706 1.48310 0.12330  -0.24092 -0.23871 174 GLU C N   
1384 C CA  . GLU A 174 ? 0.66608 1.32338 1.43466 0.11477  -0.20134 -0.22748 174 GLU C CA  
1385 C C   . GLU A 174 ? 0.64612 1.26529 1.33096 0.11904  -0.18820 -0.17628 174 GLU C C   
1386 O O   . GLU A 174 ? 0.63869 1.21614 1.22537 0.14300  -0.22106 -0.14913 174 GLU C O   
1387 C CB  . GLU A 174 ? 0.65041 1.32349 1.43975 0.14942  -0.22724 -0.24748 174 GLU C CB  
1388 C CG  . GLU A 174 ? 0.80747 1.52663 1.69531 0.14749  -0.23965 -0.30719 174 GLU C CG  
1389 C CD  . GLU A 174 ? 0.88464 1.63749 1.88416 0.10400  -0.17764 -0.33288 174 GLU C CD  
1390 O OE1 . GLU A 174 ? 0.87425 1.61319 1.86675 0.08126  -0.12524 -0.30217 174 GLU C OE1 
1391 O OE2 . GLU A 174 ? 0.67936 1.46704 1.76987 0.09346  -0.17799 -0.38555 174 GLU C OE2 
1392 N N   . PRO A 175 ? 0.63028 1.23661 1.32227 0.09277  -0.13110 -0.15700 175 PRO C N   
1393 C CA  . PRO A 175 ? 0.51668 1.05392 1.09192 0.09117  -0.11060 -0.10340 175 PRO C CA  
1394 C C   . PRO A 175 ? 0.56002 1.07650 1.07919 0.13195  -0.14431 -0.08841 175 PRO C C   
1395 O O   . PRO A 175 ? 0.76380 1.31602 1.33773 0.15901  -0.16487 -0.11358 175 PRO C O   
1396 C CB  . PRO A 175 ? 0.50371 1.03451 1.10202 0.06186  -0.04638 -0.09650 175 PRO C CB  
1397 C CG  . PRO A 175 ? 0.37392 0.95037 1.08366 0.03447  -0.01909 -0.13568 175 PRO C CG  
1398 C CD  . PRO A 175 ? 0.52043 1.16170 1.31464 0.05977  -0.07560 -0.18287 175 PRO C CD  
1399 N N   . VAL A 176 ? 0.60563 1.06123 1.01930 0.13661  -0.14701 -0.04914 176 VAL C N   
1400 C CA  . VAL A 176 ? 0.62813 1.04479 0.97757 0.17038  -0.16712 -0.02967 176 VAL C CA  
1401 C C   . VAL A 176 ? 0.59626 0.99375 0.93500 0.16035  -0.12897 -0.01448 176 VAL C C   
1402 O O   . VAL A 176 ? 0.63322 1.01493 0.95110 0.13057  -0.09320 0.00006  176 VAL C O   
1403 C CB  . VAL A 176 ? 0.76995 1.12848 1.02029 0.17730  -0.18127 -0.00056 176 VAL C CB  
1404 C CG1 . VAL A 176 ? 0.88620 1.18796 1.06709 0.20310  -0.18244 0.02407  176 VAL C CG1 
1405 C CG2 . VAL A 176 ? 0.86678 1.23968 1.11489 0.19732  -0.22493 -0.01896 176 VAL C CG2 
1406 N N   . LEU A 177 ? 0.48099 0.87725 0.82997 0.18939  -0.13926 -0.02001 177 LEU C N   
1407 C CA  . LEU A 177 ? 0.52277 0.90376 0.86769 0.18394  -0.10627 -0.01303 177 LEU C CA  
1408 C C   . LEU A 177 ? 0.49617 0.82151 0.77883 0.21301  -0.11942 0.00603  177 LEU C C   
1409 O O   . LEU A 177 ? 0.59155 0.91461 0.88117 0.25182  -0.15059 -0.00180 177 LEU C O   
1410 C CB  . LEU A 177 ? 0.41973 0.85639 0.85904 0.18681  -0.09284 -0.04567 177 LEU C CB  
1411 C CG  . LEU A 177 ? 0.39972 0.88011 0.90468 0.15205  -0.06042 -0.06477 177 LEU C CG  
1412 C CD1 . LEU A 177 ? 0.38550 0.92918 1.00418 0.15907  -0.05233 -0.10642 177 LEU C CD1 
1413 C CD2 . LEU A 177 ? 0.49328 0.93912 0.94656 0.12178  -0.01174 -0.04299 177 LEU C CD2 
1414 N N   . LYS A 178 ? 0.50678 0.78473 0.73064 0.19637  -0.09543 0.02831  178 LYS C N   
1415 C CA  . LYS A 178 ? 0.52784 0.74583 0.70123 0.21500  -0.09316 0.04391  178 LYS C CA  
1416 C C   . LYS A 178 ? 0.60964 0.82847 0.80496 0.20801  -0.06481 0.03408  178 LYS C C   
1417 O O   . LYS A 178 ? 0.46519 0.70198 0.66711 0.18016  -0.04055 0.02879  178 LYS C O   
1418 C CB  . LYS A 178 ? 0.55222 0.71825 0.65794 0.19968  -0.08399 0.06702  178 LYS C CB  
1419 C CG  . LYS A 178 ? 0.61521 0.76249 0.68032 0.21376  -0.10953 0.07870  178 LYS C CG  
1420 C CD  . LYS A 178 ? 0.60596 0.71832 0.64213 0.26108  -0.13600 0.08314  178 LYS C CD  
1421 C CE  . LYS A 178 ? 0.85313 0.94657 0.83726 0.28151  -0.16602 0.09092  178 LYS C CE  
1422 N NZ  . LYS A 178 ? 1.18623 1.23899 1.12573 0.33802  -0.19836 0.09509  178 LYS C NZ  
1423 N N   . HIS A 179 ? 0.75669 0.95068 0.95572 0.23720  -0.06885 0.03107  179 HIS C N   
1424 C CA  . HIS A 179 ? 0.59043 0.78672 0.81602 0.23570  -0.04432 0.01626  179 HIS C CA  
1425 C C   . HIS A 179 ? 0.65348 0.78443 0.83223 0.23051  -0.02505 0.02684  179 HIS C C   
1426 O O   . HIS A 179 ? 0.91915 0.99500 1.04913 0.23588  -0.02853 0.04705  179 HIS C O   
1427 C CB  . HIS A 179 ? 0.58581 0.80226 0.86234 0.27259  -0.05949 -0.00111 179 HIS C CB  
1428 C CG  . HIS A 179 ? 0.58769 0.86278 0.91699 0.28667  -0.08924 -0.01628 179 HIS C CG  
1429 N ND1 . HIS A 179 ? 0.58699 0.92380 0.96820 0.25764  -0.07678 -0.03271 179 HIS C ND1 
1430 C CD2 . HIS A 179 ? 0.78144 1.06120 1.12129 0.32856  -0.13151 -0.02167 179 HIS C CD2 
1431 C CE1 . HIS A 179 ? 0.61752 1.00129 1.05364 0.27578  -0.10822 -0.05208 179 HIS C CE1 
1432 N NE2 . HIS A 179 ? 0.64482 0.99919 1.05613 0.32143  -0.14671 -0.04757 179 HIS C NE2 
1433 N N   . TRP A 180 ? 0.65420 0.78996 0.85006 0.21920  -0.00082 0.00934  180 TRP C N   
1434 C CA  . TRP A 180 ? 0.73084 0.81261 0.90215 0.21229  0.01885  0.00747  180 TRP C CA  
1435 C C   . TRP A 180 ? 0.69570 0.78995 0.89767 0.21453  0.03736  -0.01939 180 TRP C C   
1436 O O   . TRP A 180 ? 0.64619 0.78972 0.86783 0.20471  0.04496  -0.03521 180 TRP C O   
1437 C CB  . TRP A 180 ? 0.70869 0.78485 0.85279 0.17986  0.02744  0.00911  180 TRP C CB  
1438 C CG  . TRP A 180 ? 0.82634 0.85207 0.96283 0.16977  0.04807  -0.00101 180 TRP C CG  
1439 C CD1 . TRP A 180 ? 0.89078 0.85361 1.00430 0.16860  0.05962  0.01374  180 TRP C CD1 
1440 C CD2 . TRP A 180 ? 0.79321 0.82451 0.94845 0.15860  0.06352  -0.03265 180 TRP C CD2 
1441 N NE1 . TRP A 180 ? 0.79686 0.72862 0.92712 0.15319  0.08444  -0.00906 180 TRP C NE1 
1442 C CE2 . TRP A 180 ? 0.67353 0.65013 0.83054 0.14809  0.08254  -0.04005 180 TRP C CE2 
1443 C CE3 . TRP A 180 ? 0.75259 0.82591 0.91986 0.15716  0.06582  -0.05768 180 TRP C CE3 
1444 C CZ2 . TRP A 180 ? 0.74046 0.71207 0.92274 0.13545  0.09762  -0.07723 180 TRP C CZ2 
1445 C CZ3 . TRP A 180 ? 0.72331 0.78740 0.89940 0.14924  0.07814  -0.09120 180 TRP C CZ3 
1446 C CH2 . TRP A 180 ? 0.88317 0.90120 1.07250 0.13810  0.09083  -0.10349 180 TRP C CH2 
1447 N N   . THR A 181 ? 0.81899 0.86068 1.01976 0.22781  0.04925  -0.02429 181 THR C N   
1448 C CA  . THR A 181 ? 0.86522 0.90876 1.09210 0.23035  0.06841  -0.05313 181 THR C CA  
1449 C C   . THR A 181 ? 0.92642 0.91196 1.14013 0.21651  0.08820  -0.06372 181 THR C C   
1450 O O   . THR A 181 ? 0.89399 0.83237 1.08344 0.20836  0.09178  -0.04605 181 THR C O   
1451 C CB  . THR A 181 ? 0.82679 0.86899 1.08809 0.26762  0.06350  -0.05737 181 THR C CB  
1452 O OG1 . THR A 181 ? 0.86319 0.94762 1.14230 0.28420  0.03786  -0.04547 181 THR C OG1 
1453 C CG2 . THR A 181 ? 0.98139 1.05770 1.27894 0.26707  0.08321  -0.09110 181 THR C CG2 
1454 N N   . SER A 182 ? 0.99593 0.98453 1.22974 0.21266  0.10480  -0.09703 182 SER C N   
1455 C CA  . SER A 182 ? 1.01593 0.96023 1.25372 0.19517  0.12390  -0.11998 182 SER C CA  
1456 C C   . SER A 182 ? 1.20911 1.06834 1.44814 0.21014  0.14186  -0.10606 182 SER C C   
1457 O O   . SER A 182 ? 1.49690 1.30772 1.74300 0.19019  0.16436  -0.11935 182 SER C O   
1458 C CB  . SER A 182 ? 1.18240 1.15244 1.43801 0.19127  0.13373  -0.16457 182 SER C CB  
1459 O OG  . SER A 182 ? 1.28633 1.25211 1.56355 0.21813  0.14191  -0.17042 182 SER C OG  
1460 N N   . GLY A 183 ? 1.08444 0.92094 1.31779 0.24648  0.13378  -0.08205 183 GLY C N   
1461 C CA  . GLY A 183 ? 1.16906 0.91009 1.38714 0.26990  0.15155  -0.06513 183 GLY C CA  
1462 C C   . GLY A 183 ? 1.41696 1.10767 1.58150 0.29157  0.14025  -0.01893 183 GLY C C   
1463 O O   . GLY A 183 ? 1.38185 1.00653 1.51943 0.33333  0.13860  0.00288  183 GLY C O   
1464 N N   . LEU A 184 ? 1.38749 1.10383 1.52929 0.26806  0.13118  -0.00455 184 LEU C N   
1465 C CA  . LEU A 184 ? 1.42603 1.09799 1.50827 0.28706  0.11999  0.03635  184 LEU C CA  
1466 C C   . LEU A 184 ? 1.64035 1.23257 1.68988 0.26080  0.15918  0.04864  184 LEU C C   
1467 O O   . LEU A 184 ? 1.75047 1.34210 1.83913 0.22266  0.18881  0.01980  184 LEU C O   
1468 C CB  . LEU A 184 ? 1.26238 1.01969 1.34472 0.28137  0.08348  0.04272  184 LEU C CB  
1469 C CG  . LEU A 184 ? 1.18592 0.99047 1.27926 0.32141  0.04328  0.04718  184 LEU C CG  
1470 C CD1 . LEU A 184 ? 1.29703 1.14683 1.45199 0.33211  0.04333  0.01668  184 LEU C CD1 
1471 C CD2 . LEU A 184 ? 1.02704 0.90788 1.12681 0.30599  0.01659  0.04951  184 LEU C CD2 
1472 N N   . GLU A 185 ? 1.87410 1.39846 1.85235 0.28319  0.15996  0.08811  185 GLU C N   
1473 C CA  . GLU A 185 ? 1.83082 1.27400 1.77054 0.25942  0.20397  0.10413  185 GLU C CA  
1474 C C   . GLU A 185 ? 1.92269 1.37933 1.80776 0.26321  0.18294  0.13161  185 GLU C C   
1475 O O   . GLU A 185 ? 1.97788 1.46185 1.82935 0.30096  0.13785  0.14871  185 GLU C O   
1476 C CB  . GLU A 185 ? 1.88644 1.18695 1.76921 0.28701  0.24701  0.12958  185 GLU C CB  
1477 C CG  . GLU A 185 ? 2.25048 1.47994 2.03104 0.34961  0.22331  0.17606  185 GLU C CG  
1478 C CD  . GLU A 185 ? 2.34095 1.63115 2.13951 0.39817  0.16491  0.16987  185 GLU C CD  
1479 O OE1 . GLU A 185 ? 2.11731 1.46386 1.99433 0.38845  0.16129  0.13636  185 GLU C OE1 
1480 O OE2 . GLU A 185 ? 2.50432 1.78807 2.24184 0.44706  0.12261  0.19407  185 GLU C OE2 
1481 N N   . VAL A 186 ? 2.00163 1.44339 1.88664 0.22372  0.21549  0.12978  186 VAL C N   
1482 C CA  . VAL A 186 ? 1.87835 1.33144 1.71494 0.22235  0.20164  0.15163  186 VAL C CA  
1483 C C   . VAL A 186 ? 1.81094 1.19781 1.63479 0.18713  0.26005  0.15479  186 VAL C C   
1484 O O   . VAL A 186 ? 1.87664 1.17796 1.61429 0.20420  0.28216  0.18950  186 VAL C O   
1485 C CB  . VAL A 186 ? 1.62926 1.21220 1.51802 0.20367  0.15548  0.13037  186 VAL C CB  
1486 C CG1 . VAL A 186 ? 1.43130 1.07424 1.40242 0.15739  0.17011  0.08919  186 VAL C CG1 
1487 C CG2 . VAL A 186 ? 1.41132 1.00253 1.25239 0.20303  0.14164  0.15072  186 VAL C CG2 
1488 N N   . GLN B 1   ? 1.06091 1.19617 1.28215 -0.06352 -0.08511 0.04939  -25 GLN D N   
1489 C CA  . GLN B 1   ? 0.74491 0.89741 0.96727 -0.06345 -0.11902 0.05668  -25 GLN D CA  
1490 C C   . GLN B 1   ? 0.66836 0.80631 0.86051 -0.04926 -0.12750 0.07519  -25 GLN D C   
1491 O O   . GLN B 1   ? 0.92460 1.05390 1.07199 -0.05734 -0.14632 0.08126  -25 GLN D O   
1492 C CB  . GLN B 1   ? 0.52224 0.70385 0.80838 -0.05825 -0.12695 0.05516  -25 GLN D CB  
1493 C CG  . GLN B 1   ? 1.00185 1.20473 1.31427 -0.07878 -0.13605 0.03715  -25 GLN D CG  
1494 C CD  . GLN B 1   ? 1.03059 1.23887 1.30560 -0.09368 -0.17002 0.03350  -25 GLN D CD  
1495 O OE1 . GLN B 1   ? 0.89390 1.10108 1.14471 -0.08593 -0.19619 0.04887  -25 GLN D OE1 
1496 N NE2 . GLN B 1   ? 1.20279 1.41369 1.46925 -0.11624 -0.16989 0.01322  -25 GLN D NE2 
1497 N N   . VAL B 2   ? 0.44720 0.58095 0.66125 -0.03035 -0.11267 0.08357  -24 VAL D N   
1498 C CA  . VAL B 2   ? 0.65338 0.76904 0.84137 -0.01742 -0.11670 0.09820  -24 VAL D CA  
1499 C C   . VAL B 2   ? 0.60630 0.71248 0.80185 -0.00407 -0.08649 0.09897  -24 VAL D C   
1500 O O   . VAL B 2   ? 0.52652 0.64509 0.76266 0.00434  -0.07210 0.09555  -24 VAL D O   
1501 C CB  . VAL B 2   ? 0.69139 0.81402 0.90185 -0.00509 -0.14519 0.10872  -24 VAL D CB  
1502 C CG1 . VAL B 2   ? 0.73704 0.84088 0.94299 0.01315  -0.13891 0.11869  -24 VAL D CG1 
1503 C CG2 . VAL B 2   ? 0.67759 0.79543 0.85272 -0.01756 -0.17950 0.11690  -24 VAL D CG2 
1504 N N   . TYR B 3   ? 0.61179 0.69859 0.76763 -0.00366 -0.07662 0.10313  -23 TYR D N   
1505 C CA  . TYR B 3   ? 0.59481 0.67300 0.75091 0.00833  -0.05209 0.10454  -23 TYR D CA  
1506 C C   . TYR B 3   ? 0.59824 0.66901 0.75556 0.02334  -0.05732 0.11286  -23 TYR D C   
1507 O O   . TYR B 3   ? 0.52875 0.58895 0.66738 0.02228  -0.07760 0.12018  -23 TYR D O   
1508 C CB  . TYR B 3   ? 0.53825 0.60464 0.65823 0.00230  -0.03976 0.10211  -23 TYR D CB  
1509 C CG  . TYR B 3   ? 0.46805 0.53551 0.59598 -0.00414 -0.02332 0.09160  -23 TYR D CG  
1510 C CD1 . TYR B 3   ? 0.49301 0.55502 0.63640 0.00517  -0.00198 0.09262  -23 TYR D CD1 
1511 C CD2 . TYR B 3   ? 0.55181 0.62224 0.66889 -0.02010 -0.02942 0.08059  -23 TYR D CD2 
1512 C CE1 . TYR B 3   ? 0.48209 0.53715 0.63342 -0.00005 0.01171  0.08484  -23 TYR D CE1 
1513 C CE2 . TYR B 3   ? 0.38880 0.45493 0.51553 -0.02526 -0.01434 0.06836  -23 TYR D CE2 
1514 C CZ  . TYR B 3   ? 0.47823 0.53445 0.62384 -0.01459 0.00564  0.07147  -23 TYR D CZ  
1515 O OH  . TYR B 3   ? 0.61930 0.66369 0.77508 -0.01916 0.01929  0.06108  -23 TYR D OH  
1516 N N   . SER B 4   ? 0.56547 0.63900 0.74222 0.03614  -0.03840 0.11145  -22 SER D N   
1517 C CA  . SER B 4   ? 0.43351 0.49895 0.61048 0.05080  -0.03820 0.11423  -22 SER D CA  
1518 C C   . SER B 4   ? 0.58782 0.64003 0.73233 0.05318  -0.02251 0.11549  -22 SER D C   
1519 O O   . SER B 4   ? 0.62606 0.68004 0.76300 0.05008  -0.00596 0.11450  -22 SER D O   
1520 C CB  . SER B 4   ? 0.63684 0.71969 0.85808 0.06305  -0.02725 0.10842  -22 SER D CB  
1521 O OG  . SER B 4   ? 0.59468 0.69523 0.85375 0.06305  -0.04542 0.10619  -22 SER D OG  
1522 N N   . LEU B 5   ? 0.61420 0.65191 0.74120 0.05887  -0.02970 0.11760  -21 LEU D N   
1523 C CA  . LEU B 5   ? 0.61726 0.64553 0.71374 0.05927  -0.02019 0.11763  -21 LEU D CA  
1524 C C   . LEU B 5   ? 0.59930 0.62304 0.69907 0.07300  -0.01146 0.11277  -21 LEU D C   
1525 O O   . LEU B 5   ? 0.60089 0.62298 0.72348 0.08237  -0.01679 0.10893  -21 LEU D O   
1526 C CB  . LEU B 5   ? 0.51142 0.52629 0.57766 0.04760  -0.03523 0.12189  -21 LEU D CB  
1527 C CG  . LEU B 5   ? 0.54196 0.53591 0.60097 0.04998  -0.05044 0.12459  -21 LEU D CG  
1528 C CD1 . LEU B 5   ? 0.67366 0.65547 0.69848 0.03345  -0.05861 0.12944  -21 LEU D CD1 
1529 C CD2 . LEU B 5   ? 0.49520 0.48392 0.57762 0.05480  -0.06883 0.12887  -21 LEU D CD2 
1530 N N   . ILE B 6   ? 0.70060 0.72354 0.77795 0.07485  0.00113  0.11147  -20 ILE D N   
1531 C CA  . ILE B 6   ? 0.59938 0.61781 0.66882 0.08509  0.00962  0.10463  -20 ILE D CA  
1532 C C   . ILE B 6   ? 0.67768 0.67829 0.72642 0.08148  -0.00484 0.10193  -20 ILE D C   
1533 O O   . ILE B 6   ? 0.70750 0.70608 0.73603 0.07028  -0.01199 0.10603  -20 ILE D O   
1534 C CB  . ILE B 6   ? 0.56541 0.59147 0.61615 0.08773  0.02715  0.10626  -20 ILE D CB  
1535 C CG1 . ILE B 6   ? 0.67764 0.71515 0.74882 0.08923  0.04378  0.10999  -20 ILE D CG1 
1536 C CG2 . ILE B 6   ? 0.55983 0.58122 0.59059 0.09504  0.03305  0.09779  -20 ILE D CG2 
1537 C CD1 . ILE B 6   ? 0.64322 0.68096 0.69753 0.08705  0.05379  0.11922  -20 ILE D CD1 
1538 N N   . ARG B 7   ? 0.64673 0.63450 0.70325 0.09018  -0.00797 0.09342  -19 ARG D N   
1539 C CA  . ARG B 7   ? 0.56620 0.53015 0.60518 0.08549  -0.02172 0.09005  -19 ARG D CA  
1540 C C   . ARG B 7   ? 0.66187 0.62460 0.67918 0.08901  -0.01157 0.07780  -19 ARG D C   
1541 O O   . ARG B 7   ? 0.59080 0.55871 0.61558 0.10145  0.00230  0.06683  -19 ARG D O   
1542 C CB  . ARG B 7   ? 0.51271 0.45565 0.57494 0.09350  -0.03567 0.08791  -19 ARG D CB  
1543 C CG  . ARG B 7   ? 0.53763 0.47980 0.61484 0.08830  -0.05242 0.10173  -19 ARG D CG  
1544 C CD  . ARG B 7   ? 0.49306 0.40933 0.59051 0.09760  -0.07232 0.10292  -19 ARG D CD  
1545 N NE  . ARG B 7   ? 0.53968 0.44566 0.63175 0.08655  -0.09519 0.12038  -19 ARG D NE  
1546 C CZ  . ARG B 7   ? 0.64560 0.56450 0.76577 0.09247  -0.10684 0.12626  -19 ARG D CZ  
1547 N NH1 . ARG B 7   ? 0.87258 0.81739 1.03518 0.10898  -0.09652 0.11554  -19 ARG D NH1 
1548 N NH2 . ARG B 7   ? 0.72702 0.63475 0.83154 0.07974  -0.12941 0.14280  -19 ARG D NH2 
1549 N N   . PRO B 8   ? 0.73670 0.69622 0.72738 0.07735  -0.01743 0.07764  -18 PRO D N   
1550 C CA  . PRO B 8   ? 0.51722 0.47755 0.48537 0.07927  -0.01167 0.06463  -18 PRO D CA  
1551 C C   . PRO B 8   ? 0.71082 0.64314 0.67937 0.08222  -0.01741 0.04933  -18 PRO D C   
1552 O O   . PRO B 8   ? 0.59252 0.49903 0.57139 0.07755  -0.03152 0.05237  -18 PRO D O   
1553 C CB  . PRO B 8   ? 0.60242 0.57308 0.55133 0.06430  -0.01960 0.06915  -18 PRO D CB  
1554 C CG  . PRO B 8   ? 0.53463 0.49522 0.49246 0.05135  -0.03125 0.07965  -18 PRO D CG  
1555 C CD  . PRO B 8   ? 0.58091 0.54090 0.56162 0.06028  -0.02875 0.08775  -18 PRO D CD  
1556 N N   . ASN B 9   ? 0.55793 0.49273 0.51234 0.08977  -0.00657 0.03265  -17 ASN D N   
1557 C CA  . ASN B 9   ? 0.72985 0.63679 0.68362 0.09340  -0.00977 0.01253  -17 ASN D CA  
1558 C C   . ASN B 9   ? 0.65900 0.54857 0.59114 0.07542  -0.02503 0.00800  -17 ASN D C   
1559 O O   . ASN B 9   ? 0.79057 0.70008 0.70509 0.06259  -0.02903 0.01520  -17 ASN D O   
1560 C CB  . ASN B 9   ? 0.65191 0.56966 0.59353 0.10540  0.00942  -0.00742 -17 ASN D CB  
1561 C CG  . ASN B 9   ? 0.76961 0.70380 0.73882 0.12089  0.02733  -0.00649 -17 ASN D CG  
1562 O OD1 . ASN B 9   ? 0.70645 0.63396 0.71293 0.12769  0.02185  -0.00039 -17 ASN D OD1 
1563 N ND2 . ASN B 9   ? 0.74282 0.69999 0.69331 0.12506  0.04819  -0.01183 -17 ASN D ND2 
1564 N N   . GLU B 10  ? 0.75297 0.60493 0.69061 0.07458  -0.03368 -0.00498 -16 GLU D N   
1565 C CA  . GLU B 10  ? 0.66319 0.49139 0.58495 0.05402  -0.04839 -0.00922 -16 GLU D CA  
1566 C C   . GLU B 10  ? 0.72715 0.55009 0.62669 0.05227  -0.04467 -0.03738 -16 GLU D C   
1567 O O   . GLU B 10  ? 0.77390 0.59370 0.67417 0.06899  -0.03229 -0.05693 -16 GLU D O   
1568 C CB  . GLU B 10  ? 0.71177 0.49209 0.65067 0.05070  -0.06337 -0.00260 -16 GLU D CB  
1569 C CG  . GLU B 10  ? 0.69527 0.47743 0.65665 0.05783  -0.06832 0.02136  -16 GLU D CG  
1570 C CD  . GLU B 10  ? 0.90052 0.63181 0.87365 0.05535  -0.08727 0.03119  -16 GLU D CD  
1571 O OE1 . GLU B 10  ? 0.84780 0.54837 0.80300 0.03353  -0.09858 0.03433  -16 GLU D OE1 
1572 O OE2 . GLU B 10  ? 1.07524 0.79703 1.07650 0.07469  -0.09182 0.03651  -16 GLU D OE2 
1573 N N   . ASN B 11  ? 0.91042 0.73566 0.79065 0.03032  -0.05489 -0.04135 -15 ASN D N   
1574 C CA  . ASN B 11  ? 1.00984 0.82789 0.86748 0.02379  -0.05600 -0.06983 -15 ASN D CA  
1575 C C   . ASN B 11  ? 1.03704 0.79748 0.90394 0.02082  -0.06296 -0.08699 -15 ASN D C   
1576 O O   . ASN B 11  ? 1.16429 0.89204 1.04483 0.00881  -0.07505 -0.07224 -15 ASN D O   
1577 C CB  . ASN B 11  ? 0.98878 0.83398 0.82941 0.00019  -0.06683 -0.06920 -15 ASN D CB  
1578 C CG  . ASN B 11  ? 0.88345 0.78142 0.70788 0.00779  -0.06157 -0.06358 -15 ASN D CG  
1579 O OD1 . ASN B 11  ? 0.94060 0.86241 0.77566 0.01666  -0.05613 -0.04118 -15 ASN D OD1 
1580 N ND2 . ASN B 11  ? 1.03159 0.94554 0.82862 0.00389  -0.06490 -0.08381 -15 ASN D ND2 
1581 N N   . PRO B 12  ? 0.96601 0.71043 0.82393 0.03122  -0.05536 -0.11804 -14 PRO D N   
1582 C CA  . PRO B 12  ? 1.07855 0.76280 0.94842 0.03096  -0.06194 -0.13769 -14 PRO D CA  
1583 C C   . PRO B 12  ? 1.09757 0.75734 0.95132 0.00018  -0.07726 -0.14818 -14 PRO D C   
1584 O O   . PRO B 12  ? 1.14428 0.83945 0.97410 -0.01713 -0.08006 -0.15501 -14 PRO D O   
1585 C CB  . PRO B 12  ? 1.01882 0.70393 0.88236 0.05214  -0.04445 -0.17230 -14 PRO D CB  
1586 C CG  . PRO B 12  ? 0.94834 0.68955 0.77692 0.04860  -0.03501 -0.17511 -14 PRO D CG  
1587 C CD  . PRO B 12  ? 0.93516 0.71350 0.77000 0.04444  -0.03898 -0.13670 -14 PRO D CD  
1588 N N   . ALA B 13  ? 1.27047 0.86816 1.13978 -0.00680 -0.08853 -0.14864 -13 ALA D N   
1589 C CA  . ALA B 13  ? 1.36367 0.92577 1.22190 -0.03886 -0.10236 -0.15913 -13 ALA D CA  
1590 C C   . ALA B 13  ? 1.48697 1.09034 1.33419 -0.06943 -0.10946 -0.13868 -13 ALA D C   
1591 O O   . ALA B 13  ? 1.40950 1.02804 1.24116 -0.09342 -0.11474 -0.15680 -13 ALA D O   
1592 C CB  . ALA B 13  ? 1.05758 0.61028 0.89677 -0.04092 -0.09856 -0.20412 -13 ALA D CB  
1593 N N   . ARG B 35  ? 0.89087 1.62678 1.20287 -0.25447 -0.14372 -0.14905 2   ARG D N   
1594 C CA  . ARG B 35  ? 0.85018 1.49551 1.09295 -0.24362 -0.14718 -0.13329 2   ARG D CA  
1595 C C   . ARG B 35  ? 0.79439 1.38954 1.00914 -0.22401 -0.12484 -0.10919 2   ARG D C   
1596 O O   . ARG B 35  ? 1.02239 1.55879 1.20504 -0.24582 -0.10813 -0.09859 2   ARG D O   
1597 C CB  . ARG B 35  ? 0.64513 1.24095 0.86025 -0.28756 -0.14561 -0.14101 2   ARG D CB  
1598 N N   . HIS B 36  ? 0.65197 1.26915 0.87947 -0.18301 -0.12665 -0.10031 3   HIS D N   
1599 C CA  . HIS B 36  ? 0.48165 1.05772 0.68718 -0.16220 -0.10785 -0.08005 3   HIS D CA  
1600 C C   . HIS B 36  ? 0.51057 1.03524 0.67148 -0.12765 -0.12011 -0.06514 3   HIS D C   
1601 O O   . HIS B 36  ? 0.48613 1.03354 0.64951 -0.10327 -0.14174 -0.06769 3   HIS D O   
1602 C CB  . HIS B 36  ? 0.46150 1.09526 0.71587 -0.14297 -0.09725 -0.08264 3   HIS D CB  
1603 C CG  . HIS B 36  ? 0.45768 1.05317 0.69263 -0.12933 -0.07571 -0.06641 3   HIS D CG  
1604 N ND1 . HIS B 36  ? 0.60447 1.19141 0.83596 -0.15765 -0.04986 -0.06539 3   HIS D ND1 
1605 C CD2 . HIS B 36  ? 0.42766 0.99138 0.64380 -0.09276 -0.07673 -0.05091 3   HIS D CD2 
1606 C CE1 . HIS B 36  ? 0.47050 1.02410 0.68243 -0.13805 -0.03774 -0.05167 3   HIS D CE1 
1607 N NE2 . HIS B 36  ? 0.51601 1.05496 0.72109 -0.09915 -0.05305 -0.04321 3   HIS D NE2 
1608 N N   . PHE B 37  ? 0.48202 0.93979 0.60221 -0.12649 -0.10663 -0.04927 4   PHE D N   
1609 C CA  . PHE B 37  ? 0.48467 0.89288 0.56367 -0.09828 -0.11299 -0.03634 4   PHE D CA  
1610 C C   . PHE B 37  ? 0.53996 0.91697 0.60893 -0.08083 -0.09535 -0.01800 4   PHE D C   
1611 O O   . PHE B 37  ? 0.52796 0.89421 0.60051 -0.09928 -0.07854 -0.01417 4   PHE D O   
1612 C CB  . PHE B 37  ? 0.65885 1.01194 0.69828 -0.11526 -0.11750 -0.04012 4   PHE D CB  
1613 C CG  . PHE B 37  ? 0.60184 0.97930 0.64783 -0.13699 -0.13474 -0.06123 4   PHE D CG  
1614 C CD1 . PHE B 37  ? 0.81829 1.20698 0.88383 -0.17684 -0.13037 -0.07285 4   PHE D CD1 
1615 C CD2 . PHE B 37  ? 0.71702 1.10588 0.74692 -0.12023 -0.15536 -0.06958 4   PHE D CD2 
1616 C CE1 . PHE B 37  ? 0.66906 1.08084 0.74361 -0.19981 -0.14664 -0.09436 4   PHE D CE1 
1617 C CE2 . PHE B 37  ? 0.84079 1.25385 0.87574 -0.14181 -0.17333 -0.09160 4   PHE D CE2 
1618 C CZ  . PHE B 37  ? 0.86246 1.28742 0.92255 -0.18179 -0.16916 -0.10499 4   PHE D CZ  
1619 N N   . VAL B 38  ? 0.45326 0.81569 0.50717 -0.04749 -0.09957 -0.00653 5   VAL D N   
1620 C CA  . VAL B 38  ? 0.43377 0.76676 0.47930 -0.03001 -0.08477 0.00961  5   VAL D CA  
1621 C C   . VAL B 38  ? 0.50283 0.78423 0.50787 -0.01565 -0.08616 0.01987  5   VAL D C   
1622 O O   . VAL B 38  ? 0.59388 0.87709 0.58201 -0.00151 -0.09890 0.01877  5   VAL D O   
1623 C CB  . VAL B 38  ? 0.44786 0.81606 0.52311 -0.00307 -0.08477 0.01362  5   VAL D CB  
1624 C CG1 . VAL B 38  ? 0.46503 0.80054 0.53251 0.01030  -0.06865 0.02745  5   VAL D CG1 
1625 C CG2 . VAL B 38  ? 0.40635 0.83454 0.52940 -0.01482 -0.08277 -0.00152 5   VAL D CG2 
1626 N N   . TYR B 39  ? 0.48865 0.72721 0.47825 -0.01975 -0.07324 0.02905  6   TYR D N   
1627 C CA  . TYR B 39  ? 0.56593 0.76012 0.52603 -0.00579 -0.07079 0.03715  6   TYR D CA  
1628 C C   . TYR B 39  ? 0.54971 0.73070 0.51428 0.01026  -0.05830 0.05170  6   TYR D C   
1629 O O   . TYR B 39  ? 0.57874 0.76039 0.55656 0.00023  -0.04965 0.05468  6   TYR D O   
1630 C CB  . TYR B 39  ? 0.55518 0.70799 0.49764 -0.02447 -0.07005 0.03284  6   TYR D CB  
1631 C CG  . TYR B 39  ? 0.57397 0.68865 0.49177 -0.00948 -0.06820 0.03423  6   TYR D CG  
1632 C CD1 . TYR B 39  ? 0.58318 0.67334 0.49970 0.00385  -0.05754 0.04654  6   TYR D CD1 
1633 C CD2 . TYR B 39  ? 0.59513 0.70176 0.49278 -0.00983 -0.07622 0.02041  6   TYR D CD2 
1634 C CE1 . TYR B 39  ? 0.54455 0.60680 0.44516 0.01711  -0.05317 0.04525  6   TYR D CE1 
1635 C CE2 . TYR B 39  ? 0.53721 0.61290 0.41376 0.00360  -0.07085 0.01793  6   TYR D CE2 
1636 C CZ  . TYR B 39  ? 0.56322 0.61852 0.44370 0.01735  -0.05844 0.03048  6   TYR D CZ  
1637 O OH  . TYR B 39  ? 0.59789 0.62903 0.46376 0.03032  -0.05056 0.02562  6   TYR D OH  
1638 N N   . GLN B 40  ? 0.59672 0.76571 0.54786 0.03258  -0.05681 0.06012  7   GLN D N   
1639 C CA  . GLN B 40  ? 0.54583 0.70125 0.50231 0.04666  -0.04517 0.07307  7   GLN D CA  
1640 C C   . GLN B 40  ? 0.51373 0.63461 0.44906 0.05477  -0.03847 0.07864  7   GLN D C   
1641 O O   . GLN B 40  ? 0.60747 0.72274 0.52075 0.06060  -0.04196 0.07523  7   GLN D O   
1642 C CB  . GLN B 40  ? 0.59504 0.77240 0.56305 0.06662  -0.04726 0.08020  7   GLN D CB  
1643 C CG  . GLN B 40  ? 0.69596 0.91570 0.69225 0.06432  -0.05522 0.07168  7   GLN D CG  
1644 C CD  . GLN B 40  ? 0.80120 1.03626 0.81273 0.08867  -0.05932 0.07997  7   GLN D CD  
1645 O OE1 . GLN B 40  ? 0.72240 0.93300 0.72928 0.10226  -0.05085 0.09259  7   GLN D OE1 
1646 N NE2 . GLN B 40  ? 0.59905 0.87404 0.63153 0.09426  -0.07351 0.07304  7   GLN D NE2 
1647 N N   . PHE B 41  ? 0.48281 0.58417 0.42588 0.05448  -0.02858 0.08531  8   PHE D N   
1648 C CA  . PHE B 41  ? 0.49766 0.57476 0.43220 0.06429  -0.01965 0.09055  8   PHE D CA  
1649 C C   . PHE B 41  ? 0.42336 0.49842 0.37363 0.07138  -0.00983 0.10127  8   PHE D C   
1650 O O   . PHE B 41  ? 0.55983 0.64117 0.52592 0.06385  -0.00975 0.10164  8   PHE D O   
1651 C CB  . PHE B 41  ? 0.47640 0.52854 0.40942 0.05545  -0.02058 0.08475  8   PHE D CB  
1652 C CG  . PHE B 41  ? 0.65575 0.69051 0.59154 0.06642  -0.01035 0.08767  8   PHE D CG  
1653 C CD1 . PHE B 41  ? 0.72459 0.75493 0.64433 0.07618  -0.00375 0.08199  8   PHE D CD1 
1654 C CD2 . PHE B 41  ? 0.53272 0.55966 0.48775 0.06580  -0.00684 0.09444  8   PHE D CD2 
1655 C CE1 . PHE B 41  ? 0.45220 0.47303 0.37963 0.08509  0.00904  0.08228  8   PHE D CE1 
1656 C CE2 . PHE B 41  ? 0.59697 0.61511 0.56246 0.07527  0.00243  0.09531  8   PHE D CE2 
1657 C CZ  . PHE B 41  ? 0.59188 0.60821 0.54589 0.08494  0.01184  0.08887  8   PHE D CZ  
1658 N N   . MET B 42  ? 0.48477 0.55085 0.42899 0.08356  -0.00030 0.10871  9   MET D N   
1659 C CA  . MET B 42  ? 0.68232 0.74343 0.64219 0.08834  0.00964  0.11816  9   MET D CA  
1660 C C   . MET B 42  ? 0.62737 0.67496 0.58258 0.09424  0.02266  0.12304  9   MET D C   
1661 O O   . MET B 42  ? 0.65894 0.70512 0.59149 0.10025  0.02646  0.12404  9   MET D O   
1662 C CB  . MET B 42  ? 0.62487 0.69632 0.58818 0.09742  0.00828  0.12539  9   MET D CB  
1663 C CG  . MET B 42  ? 0.80604 0.88324 0.74584 0.10796  0.00242  0.13062  9   MET D CG  
1664 S SD  . MET B 42  ? 0.92521 1.01903 0.87746 0.12080  -0.00780 0.13700  9   MET D SD  
1665 C CE  . MET B 42  ? 0.84131 0.91231 0.81165 0.12653  0.00642  0.14839  9   MET D CE  
1666 N N   . GLY B 43  ? 0.52407 0.56497 0.50057 0.09095  0.02975  0.12463  10  GLY D N   
1667 C CA  . GLY B 43  ? 0.57018 0.60480 0.55202 0.09446  0.04465  0.12816  10  GLY D CA  
1668 C C   . GLY B 43  ? 0.63915 0.66950 0.63357 0.09470  0.05453  0.13884  10  GLY D C   
1669 O O   . GLY B 43  ? 0.58390 0.61432 0.59870 0.08905  0.05091  0.13752  10  GLY D O   
1670 N N   . GLU B 44  ? 0.70142 0.72546 0.68086 0.09946  0.06733  0.14926  11  GLU D N   
1671 C CA  . GLU B 44  ? 0.58411 0.59621 0.57036 0.09933  0.07625  0.16223  11  GLU D CA  
1672 C C   . GLU B 44  ? 0.65089 0.65952 0.64934 0.09290  0.09610  0.16575  11  GLU D C   
1673 O O   . GLU B 44  ? 0.74554 0.75931 0.72986 0.09343  0.10749  0.16446  11  GLU D O   
1674 C CB  . GLU B 44  ? 0.67898 0.68225 0.63546 0.10888  0.07312  0.17646  11  GLU D CB  
1675 C CG  . GLU B 44  ? 0.67446 0.68949 0.62498 0.11560  0.05344  0.17103  11  GLU D CG  
1676 C CD  . GLU B 44  ? 0.92549 0.93690 0.84707 0.12727  0.04581  0.18482  11  GLU D CD  
1677 O OE1 . GLU B 44  ? 0.86980 0.86784 0.76427 0.12864  0.05578  0.19900  11  GLU D OE1 
1678 O OE2 . GLU B 44  ? 1.04702 1.07089 0.97291 0.13450  0.02950  0.18176  11  GLU D OE2 
1679 N N   . CYS B 45  ? 0.67191 0.67413 0.69799 0.08549  0.10140  0.16771  12  CYS D N   
1680 C CA  . CYS B 45  ? 0.52379 0.52586 0.56920 0.07592  0.12074  0.17050  12  CYS D CA  
1681 C C   . CYS B 45  ? 0.54284 0.51979 0.58221 0.07221  0.13092  0.18742  12  CYS D C   
1682 O O   . CYS B 45  ? 0.73312 0.69727 0.78680 0.07124  0.12318  0.18697  12  CYS D O   
1683 C CB  . CYS B 45  ? 0.52889 0.54544 0.61656 0.06728  0.11620  0.15670  12  CYS D CB  
1684 S SG  . CYS B 45  ? 0.72994 0.76785 0.82855 0.07223  0.10161  0.14038  12  CYS D SG  
1685 N N   . TYR B 46  ? 0.68594 0.65342 0.70256 0.06938  0.14898  0.20188  13  TYR D N   
1686 C CA  . TYR B 46  ? 0.64199 0.57781 0.64677 0.06479  0.15910  0.22284  13  TYR D CA  
1687 C C   . TYR B 46  ? 0.72180 0.65784 0.75518 0.04550  0.18199  0.22344  13  TYR D C   
1688 O O   . TYR B 46  ? 0.75031 0.70755 0.78610 0.03809  0.19967  0.21916  13  TYR D O   
1689 C CB  . TYR B 46  ? 0.77431 0.69553 0.72589 0.07212  0.16229  0.24319  13  TYR D CB  
1690 C CG  . TYR B 46  ? 0.79660 0.72094 0.72430 0.09015  0.13776  0.24243  13  TYR D CG  
1691 C CD1 . TYR B 46  ? 0.74680 0.69726 0.66063 0.09567  0.13002  0.22795  13  TYR D CD1 
1692 C CD2 . TYR B 46  ? 0.65131 0.55338 0.57514 0.10155  0.12223  0.25428  13  TYR D CD2 
1693 C CE1 . TYR B 46  ? 0.80939 0.76609 0.70530 0.10881  0.10779  0.22575  13  TYR D CE1 
1694 C CE2 . TYR B 46  ? 0.82236 0.73490 0.73210 0.11748  0.09982  0.25163  13  TYR D CE2 
1695 C CZ  . TYR B 46  ? 0.88552 0.82666 0.78100 0.11941  0.09282  0.23754  13  TYR D CZ  
1696 O OH  . TYR B 46  ? 0.90811 0.86281 0.79307 0.13202  0.07072  0.23353  13  TYR D OH  
1697 N N   . PHE B 47  ? 0.63306 0.54740 0.69100 0.03677  0.18249  0.22617  14  PHE D N   
1698 C CA  . PHE B 47  ? 0.68047 0.59526 0.77215 0.01517  0.20205  0.22464  14  PHE D CA  
1699 C C   . PHE B 47  ? 0.77752 0.64671 0.85107 0.00572  0.21591  0.24953  14  PHE D C   
1700 O O   . PHE B 47  ? 0.86673 0.70057 0.92515 0.01656  0.20282  0.26018  14  PHE D O   
1701 C CB  . PHE B 47  ? 0.80288 0.73012 0.94203 0.00830  0.18980  0.20311  14  PHE D CB  
1702 C CG  . PHE B 47  ? 0.67990 0.64400 0.83302 0.01734  0.17223  0.18277  14  PHE D CG  
1703 C CD1 . PHE B 47  ? 0.63757 0.63790 0.81692 0.01245  0.17858  0.17107  14  PHE D CD1 
1704 C CD2 . PHE B 47  ? 0.65182 0.61366 0.79373 0.03048  0.14970  0.17558  14  PHE D CD2 
1705 C CE1 . PHE B 47  ? 0.58870 0.61535 0.77988 0.02182  0.15999  0.15536  14  PHE D CE1 
1706 C CE2 . PHE B 47  ? 0.57681 0.56638 0.72700 0.03593  0.13373  0.16035  14  PHE D CE2 
1707 C CZ  . PHE B 47  ? 0.63359 0.65209 0.80702 0.03224  0.13746  0.15162  14  PHE D CZ  
1708 N N   . THR B 48  ? 0.86892 0.73855 0.94642 -0.01481 0.24295  0.25868  15  THR D N   
1709 C CA  . THR B 48  ? 1.00925 0.83080 1.06581 -0.02841 0.25894  0.28610  15  THR D CA  
1710 C C   . THR B 48  ? 1.15436 0.97060 1.25954 -0.05557 0.27437  0.27897  15  THR D C   
1711 O O   . THR B 48  ? 1.48009 1.26005 1.60105 -0.05807 0.26504  0.27916  15  THR D O   
1712 C CB  . THR B 48  ? 0.96688 0.78673 0.97327 -0.03363 0.28035  0.30820  15  THR D CB  
1713 O OG1 . THR B 48  ? 1.32352 1.15855 1.29048 -0.01010 0.26415  0.30718  15  THR D OG1 
1714 C CG2 . THR B 48  ? 0.91298 0.67613 0.88186 -0.04269 0.28480  0.33844  15  THR D CG2 
1715 N N   . ASN B 49  ? 0.77412 0.62696 0.90684 -0.07631 0.29790  0.27026  16  ASN D N   
1716 C CA  . ASN B 49  ? 1.14445 1.00247 1.33153 -0.10435 0.31098  0.25937  16  ASN D CA  
1717 C C   . ASN B 49  ? 1.16838 1.07839 1.41152 -0.10141 0.29409  0.22503  16  ASN D C   
1718 O O   . ASN B 49  ? 1.35441 1.31055 1.64255 -0.11659 0.30694  0.20943  16  ASN D O   
1719 C CB  . ASN B 49  ? 1.36799 1.23845 1.55558 -0.13141 0.34652  0.26957  16  ASN D CB  
1720 C CG  . ASN B 49  ? 1.43164 1.26191 1.62538 -0.15836 0.35351  0.27747  16  ASN D CG  
1721 O OD1 . ASN B 49  ? 1.34309 1.12771 1.54073 -0.15610 0.33779  0.28042  16  ASN D OD1 
1722 N ND2 . ASN B 49  ? 1.66221 1.50959 1.85735 -0.18455 0.37788  0.27968  16  ASN D ND2 
1723 N N   . GLY B 50  ? 0.87574 0.77902 1.11575 -0.08144 0.26418  0.21377  17  GLY D N   
1724 C CA  . GLY B 50  ? 0.85559 0.80316 1.13423 -0.07591 0.24374  0.18573  17  GLY D CA  
1725 C C   . GLY B 50  ? 0.77169 0.76100 1.04269 -0.05859 0.24020  0.17929  17  GLY D C   
1726 O O   . GLY B 50  ? 1.07019 1.05246 1.30503 -0.03648 0.22469  0.18239  17  GLY D O   
1727 N N   . THR B 51  ? 0.71508 0.74868 1.02366 -0.06858 0.25492  0.16852  18  THR D N   
1728 C CA  . THR B 51  ? 0.70522 0.77598 1.01133 -0.05224 0.25565  0.16025  18  THR D CA  
1729 C C   . THR B 51  ? 0.79593 0.88105 1.09446 -0.06211 0.29125  0.16794  18  THR D C   
1730 O O   . THR B 51  ? 0.81324 0.93178 1.11519 -0.05034 0.29726  0.15694  18  THR D O   
1731 C CB  . THR B 51  ? 0.58767 0.70532 0.95008 -0.04856 0.23719  0.13548  18  THR D CB  
1732 O OG1 . THR B 51  ? 0.91592 1.05838 1.33562 -0.07240 0.24867  0.12619  18  THR D OG1 
1733 C CG2 . THR B 51  ? 0.49382 0.59812 0.84813 -0.03723 0.20197  0.12901  18  THR D CG2 
1734 N N   . GLN B 52  ? 0.70988 0.76856 0.99661 -0.08442 0.31615  0.18601  19  GLN D N   
1735 C CA  . GLN B 52  ? 0.79275 0.86347 1.06410 -0.09809 0.35352  0.19544  19  GLN D CA  
1736 C C   . GLN B 52  ? 0.69210 0.74209 0.88985 -0.08112 0.35684  0.21116  19  GLN D C   
1737 O O   . GLN B 52  ? 0.94160 1.01369 1.12256 -0.08611 0.38455  0.21087  19  GLN D O   
1738 C CB  . GLN B 52  ? 0.96952 1.01050 1.24311 -0.13010 0.37846  0.21415  19  GLN D CB  
1739 C CG  . GLN B 52  ? 1.12308 1.18455 1.47000 -0.15115 0.37553  0.19686  19  GLN D CG  
1740 C CD  . GLN B 52  ? 1.40121 1.41980 1.73799 -0.17980 0.38625  0.21135  19  GLN D CD  
1741 O OE1 . GLN B 52  ? 1.28384 1.26495 1.56229 -0.18634 0.39915  0.23455  19  GLN D OE1 
1742 N NE2 . GLN B 52  ? 1.28613 1.30916 1.67696 -0.19719 0.37719  0.19673  19  GLN D NE2 
1743 N N   . ARG B 53  ? 0.79395 0.80560 0.94879 -0.06206 0.32965  0.22270  20  ARG D N   
1744 C CA  . ARG B 53  ? 0.70776 0.70304 0.79499 -0.04472 0.32595  0.23560  20  ARG D CA  
1745 C C   . ARG B 53  ? 0.65892 0.65168 0.74145 -0.01875 0.28885  0.22508  20  ARG D C   
1746 O O   . ARG B 53  ? 0.97560 0.93495 1.04818 -0.01237 0.26835  0.23499  20  ARG D O   
1747 C CB  . ARG B 53  ? 0.77461 0.71712 0.80384 -0.05319 0.33517  0.27047  20  ARG D CB  
1748 C CG  . ARG B 53  ? 1.23357 1.18076 1.22125 -0.06905 0.36863  0.28331  20  ARG D CG  
1749 C CD  . ARG B 53  ? 1.45550 1.43481 1.41310 -0.05254 0.37105  0.26953  20  ARG D CD  
1750 N NE  . ARG B 53  ? 1.42799 1.42075 1.34809 -0.06927 0.39932  0.27071  20  ARG D NE  
1751 C CZ  . ARG B 53  ? 1.30335 1.32672 1.19826 -0.06094 0.41052  0.25476  20  ARG D CZ  
1752 N NH1 . ARG B 53  ? 1.34114 1.38248 1.24476 -0.03575 0.39373  0.23619  20  ARG D NH1 
1753 N NH2 . ARG B 53  ? 1.29568 1.33220 1.15573 -0.07968 0.43571  0.25413  20  ARG D NH2 
1754 N N   . ILE B 54  ? 0.65296 0.68043 0.74449 -0.00457 0.28169  0.20408  21  ILE D N   
1755 C CA  . ILE B 54  ? 0.73888 0.76657 0.82565 0.01649  0.24930  0.19349  21  ILE D CA  
1756 C C   . ILE B 54  ? 0.63281 0.65941 0.66611 0.03041  0.24782  0.19524  21  ILE D C   
1757 O O   . ILE B 54  ? 0.65704 0.70660 0.68420 0.02928  0.26742  0.18523  21  ILE D O   
1758 C CB  . ILE B 54  ? 0.58732 0.65021 0.73103 0.02067  0.23665  0.16784  21  ILE D CB  
1759 C CG1 . ILE B 54  ? 0.70398 0.77089 0.89861 0.00512  0.23512  0.16445  21  ILE D CG1 
1760 C CG2 . ILE B 54  ? 0.50028 0.55912 0.63194 0.03881  0.20540  0.15996  21  ILE D CG2 
1761 C CD1 . ILE B 54  ? 0.62653 0.72847 0.87563 0.00884  0.21859  0.14209  21  ILE D CD1 
1762 N N   . ARG B 55  ? 0.62171 0.62439 0.61869 0.04306  0.22503  0.20535  22  ARG D N   
1763 C CA  . ARG B 55  ? 0.77338 0.77680 0.72227 0.05609  0.21672  0.20433  22  ARG D CA  
1764 C C   . ARG B 55  ? 0.71859 0.72954 0.68122 0.06994  0.18735  0.18877  22  ARG D C   
1765 O O   . ARG B 55  ? 0.78634 0.78618 0.76571 0.07238  0.16932  0.19175  22  ARG D O   
1766 C CB  . ARG B 55  ? 0.66383 0.63592 0.55550 0.05805  0.21411  0.23155  22  ARG D CB  
1767 C CG  . ARG B 55  ? 0.68668 0.66332 0.52482 0.06855  0.20593  0.23004  22  ARG D CG  
1768 C CD  . ARG B 55  ? 0.89287 0.84016 0.67278 0.07004  0.20202  0.26000  22  ARG D CD  
1769 N NE  . ARG B 55  ? 0.83845 0.79300 0.56745 0.08001  0.18830  0.25697  22  ARG D NE  
1770 C CZ  . ARG B 55  ? 0.84451 0.77951 0.51604 0.08410  0.17849  0.28096  22  ARG D CZ  
1771 N NH1 . ARG B 55  ? 1.15159 1.05319 0.80712 0.08042  0.18124  0.31246  22  ARG D NH1 
1772 N NH2 . ARG B 55  ? 0.84090 0.78819 0.46974 0.09183  0.16366  0.27347  22  ARG D NH2 
1773 N N   . TYR B 56  ? 0.74547 0.77381 0.70016 0.07750  0.18424  0.17121  23  TYR D N   
1774 C CA  . TYR B 56  ? 0.76708 0.80212 0.73746 0.08678  0.15961  0.15547  23  TYR D CA  
1775 C C   . TYR B 56  ? 0.62126 0.65269 0.54569 0.09526  0.14795  0.15279  23  TYR D C   
1776 O O   . TYR B 56  ? 0.61894 0.65667 0.51591 0.09598  0.16127  0.14561  23  TYR D O   
1777 C CB  . TYR B 56  ? 0.73833 0.79460 0.75275 0.08743  0.16371  0.13446  23  TYR D CB  
1778 C CG  . TYR B 56  ? 0.62662 0.68430 0.64816 0.09624  0.14086  0.11941  23  TYR D CG  
1779 C CD1 . TYR B 56  ? 0.77021 0.81896 0.79704 0.09624  0.11692  0.12306  23  TYR D CD1 
1780 C CD2 . TYR B 56  ? 0.70565 0.77191 0.72906 0.10331  0.14486  0.10065  23  TYR D CD2 
1781 C CE1 . TYR B 56  ? 0.64297 0.68981 0.67296 0.10048  0.09755  0.11197  23  TYR D CE1 
1782 C CE2 . TYR B 56  ? 0.72332 0.78350 0.75264 0.10979  0.12368  0.08871  23  TYR D CE2 
1783 C CZ  . TYR B 56  ? 0.66298 0.71277 0.69407 0.10704  0.10006  0.09618  23  TYR D CZ  
1784 O OH  . TYR B 56  ? 0.85584 0.89646 0.88935 0.10984  0.08040  0.08691  23  TYR D OH  
1785 N N   . VAL B 57  ? 0.61694 0.64115 0.53411 0.10035  0.12401  0.15627  24  VAL D N   
1786 C CA  . VAL B 57  ? 0.71348 0.73741 0.59136 0.10663  0.10932  0.15431  24  VAL D CA  
1787 C C   . VAL B 57  ? 0.73163 0.76050 0.62831 0.10842  0.08662  0.14188  24  VAL D C   
1788 O O   . VAL B 57  ? 0.67654 0.70389 0.59958 0.10673  0.07746  0.14554  24  VAL D O   
1789 C CB  . VAL B 57  ? 0.78454 0.79645 0.62876 0.11041  0.10323  0.17665  24  VAL D CB  
1790 C CG1 . VAL B 57  ? 0.72130 0.73972 0.53145 0.11683  0.08316  0.17275  24  VAL D CG1 
1791 C CG2 . VAL B 57  ? 0.69244 0.69395 0.50874 0.10540  0.12620  0.19300  24  VAL D CG2 
1792 N N   . THR B 58  ? 0.65922 0.69269 0.54036 0.10977  0.07887  0.12627  25  THR D N   
1793 C CA  . THR B 58  ? 0.72257 0.75832 0.61272 0.10802  0.05781  0.11643  25  THR D CA  
1794 C C   . THR B 58  ? 0.64932 0.69081 0.50420 0.10977  0.04418  0.11535  25  THR D C   
1795 O O   . THR B 58  ? 0.62279 0.66488 0.44188 0.11222  0.05012  0.11441  25  THR D O   
1796 C CB  . THR B 58  ? 0.61178 0.64369 0.51952 0.10608  0.05667  0.09788  25  THR D CB  
1797 O OG1 . THR B 58  ? 0.64916 0.68019 0.53114 0.10902  0.06489  0.08403  25  THR D OG1 
1798 C CG2 . THR B 58  ? 0.63860 0.67001 0.58438 0.10613  0.06685  0.09855  25  THR D CG2 
1799 N N   . ARG B 59  ? 0.57977 0.62872 0.44471 0.10719  0.02593  0.11440  26  ARG D N   
1800 C CA  . ARG B 59  ? 0.66138 0.72310 0.50283 0.10842  0.00957  0.11279  26  ARG D CA  
1801 C C   . ARG B 59  ? 0.63421 0.70285 0.48843 0.09829  -0.00499 0.09687  26  ARG D C   
1802 O O   . ARG B 59  ? 0.55486 0.62356 0.43775 0.09190  -0.00739 0.09655  26  ARG D O   
1803 C CB  . ARG B 59  ? 0.73788 0.80787 0.58345 0.11647  0.00204  0.13016  26  ARG D CB  
1804 C CG  . ARG B 59  ? 0.81313 0.86857 0.64633 0.12402  0.01608  0.14967  26  ARG D CG  
1805 C CD  . ARG B 59  ? 0.75655 0.81310 0.59721 0.13432  0.00623  0.16671  26  ARG D CD  
1806 N NE  . ARG B 59  ? 0.76017 0.79431 0.59517 0.13818  0.02123  0.18643  26  ARG D NE  
1807 C CZ  . ARG B 59  ? 0.65088 0.67262 0.44556 0.14156  0.02649  0.20283  26  ARG D CZ  
1808 N NH1 . ARG B 59  ? 0.73054 0.76184 0.48411 0.14299  0.01672  0.20081  26  ARG D NH1 
1809 N NH2 . ARG B 59  ? 0.88457 0.88284 0.67727 0.14120  0.04210  0.22161  26  ARG D NH2 
1810 N N   . TYR B 60  ? 0.60426 0.67764 0.43421 0.09451  -0.01422 0.08351  27  TYR D N   
1811 C CA  . TYR B 60  ? 0.51509 0.59421 0.35368 0.08158  -0.02861 0.06830  27  TYR D CA  
1812 C C   . TYR B 60  ? 0.61403 0.72148 0.44427 0.08157  -0.04645 0.06838  27  TYR D C   
1813 O O   . TYR B 60  ? 0.64050 0.75475 0.43814 0.08649  -0.05251 0.06630  27  TYR D O   
1814 C CB  . TYR B 60  ? 0.56798 0.62848 0.39062 0.07554  -0.02647 0.04848  27  TYR D CB  
1815 C CG  . TYR B 60  ? 0.67298 0.70860 0.51130 0.07852  -0.01172 0.04608  27  TYR D CG  
1816 C CD1 . TYR B 60  ? 0.55743 0.58869 0.38860 0.08979  0.00638  0.05006  27  TYR D CD1 
1817 C CD2 . TYR B 60  ? 0.62417 0.64176 0.48532 0.06949  -0.01666 0.04041  27  TYR D CD2 
1818 C CE1 . TYR B 60  ? 0.56723 0.58297 0.42113 0.09376  0.01859  0.04577  27  TYR D CE1 
1819 C CE2 . TYR B 60  ? 0.61227 0.60906 0.49170 0.07505  -0.00761 0.03892  27  TYR D CE2 
1820 C CZ  . TYR B 60  ? 0.67232 0.67128 0.55173 0.08808  0.00970  0.04017  27  TYR D CZ  
1821 O OH  . TYR B 60  ? 0.67700 0.66221 0.58285 0.09479  0.01756  0.03670  27  TYR D OH  
1822 N N   . ILE B 61  ? 0.52144 0.64831 0.38118 0.07594  -0.05503 0.06991  28  ILE D N   
1823 C CA  . ILE B 61  ? 0.58124 0.74274 0.44687 0.07859  -0.07241 0.06984  28  ILE D CA  
1824 C C   . ILE B 61  ? 0.50300 0.68197 0.38426 0.05833  -0.08342 0.05186  28  ILE D C   
1825 O O   . ILE B 61  ? 0.56412 0.73462 0.46577 0.04402  -0.07660 0.04822  28  ILE D O   
1826 C CB  . ILE B 61  ? 0.64470 0.82075 0.53875 0.09092  -0.07105 0.08451  28  ILE D CB  
1827 C CG1 . ILE B 61  ? 0.65197 0.80749 0.52853 0.10874  -0.06155 0.10384  28  ILE D CG1 
1828 C CG2 . ILE B 61  ? 0.78577 1.00296 0.69805 0.09508  -0.09045 0.08110  28  ILE D CG2 
1829 C CD1 . ILE B 61  ? 0.55305 0.68125 0.43982 0.10705  -0.04124 0.10964  28  ILE D CD1 
1830 N N   . TYR B 62  ? 0.55612 0.75927 0.42583 0.05518  -0.10109 0.04136  29  TYR D N   
1831 C CA  . TYR B 62  ? 0.55982 0.78576 0.44726 0.03350  -0.11296 0.02324  29  TYR D CA  
1832 C C   . TYR B 62  ? 0.53388 0.81077 0.43969 0.04025  -0.13282 0.02230  29  TYR D C   
1833 O O   . TYR B 62  ? 0.69763 0.98683 0.57773 0.04906  -0.14905 0.02093  29  TYR D O   
1834 C CB  . TYR B 62  ? 0.56690 0.77104 0.42490 0.01903  -0.11712 0.00452  29  TYR D CB  
1835 C CG  . TYR B 62  ? 0.66674 0.89542 0.53954 -0.00521 -0.13219 -0.01534 29  TYR D CG  
1836 C CD1 . TYR B 62  ? 0.71014 0.93264 0.60928 -0.02884 -0.12617 -0.02067 29  TYR D CD1 
1837 C CD2 . TYR B 62  ? 0.62491 0.88305 0.48337 -0.00685 -0.15297 -0.02834 29  TYR D CD2 
1838 C CE1 . TYR B 62  ? 0.65938 0.90408 0.57359 -0.05507 -0.13782 -0.03862 29  TYR D CE1 
1839 C CE2 . TYR B 62  ? 0.62615 0.90996 0.50242 -0.03173 -0.16711 -0.04848 29  TYR D CE2 
1840 C CZ  . TYR B 62  ? 0.70148 0.97818 0.60727 -0.05662 -0.15813 -0.05371 29  TYR D CZ  
1841 O OH  . TYR B 62  ? 0.83751 1.13946 0.76250 -0.08531 -0.17012 -0.07353 29  TYR D OH  
1842 N N   . ASN B 63  ? 0.54503 0.85331 0.49530 0.03665  -0.13190 0.02230  30  ASN D N   
1843 C CA  . ASN B 63  ? 0.81755 1.18095 0.79991 0.04504  -0.15034 0.01913  30  ASN D CA  
1844 C C   . ASN B 63  ? 0.84424 1.20931 0.81271 0.07703  -0.16101 0.03785  30  ASN D C   
1845 O O   . ASN B 63  ? 0.89952 1.28629 0.85277 0.08596  -0.18423 0.03764  30  ASN D O   
1846 C CB  . ASN B 63  ? 0.76663 1.16198 0.75084 0.02563  -0.17028 -0.00172 30  ASN D CB  
1847 C CG  . ASN B 63  ? 0.81243 1.22346 0.82940 -0.00638 -0.16224 -0.01833 30  ASN D CG  
1848 O OD1 . ASN B 63  ? 0.77643 1.17464 0.81026 -0.01394 -0.14213 -0.01336 30  ASN D OD1 
1849 N ND2 . ASN B 63  ? 0.88564 1.32387 0.90892 -0.02778 -0.17804 -0.03804 30  ASN D ND2 
1850 N N   . ARG B 64  ? 0.72569 1.06505 0.69757 0.09282  -0.14472 0.05500  31  ARG D N   
1851 C CA  . ARG B 64  ? 0.75057 1.08150 0.71125 0.12173  -0.15126 0.07658  31  ARG D CA  
1852 C C   . ARG B 64  ? 0.60699 0.91448 0.50858 0.12759  -0.15978 0.08614  31  ARG D C   
1853 O O   . ARG B 64  ? 0.89937 1.20948 0.78376 0.14803  -0.17522 0.10328  31  ARG D O   
1854 C CB  . ARG B 64  ? 0.58822 0.96701 0.59148 0.13933  -0.17213 0.07699  31  ARG D CB  
1855 C CG  . ARG B 64  ? 0.50776 0.91244 0.57047 0.13713  -0.15986 0.06661  31  ARG D CG  
1856 C CD  . ARG B 64  ? 0.50988 0.95855 0.61916 0.16205  -0.17911 0.06768  31  ARG D CD  
1857 N NE  . ARG B 64  ? 0.51900 0.93582 0.61485 0.19257  -0.18363 0.09282  31  ARG D NE  
1858 C CZ  . ARG B 64  ? 0.59911 1.03837 0.73191 0.22110  -0.20085 0.09963  31  ARG D CZ  
1859 N NH1 . ARG B 64  ? 0.65369 1.15504 0.84435 0.22517  -0.21515 0.08111  31  ARG D NH1 
1860 N NH2 . ARG B 64  ? 0.89701 1.29520 1.01118 0.24608  -0.20367 0.12548  31  ARG D NH2 
1861 N N   . GLU B 65  ? 0.66513 0.94810 0.53359 0.10994  -0.14967 0.07514  32  GLU D N   
1862 C CA  . GLU B 65  ? 0.74805 1.01097 0.55779 0.11243  -0.15332 0.07851  32  GLU D CA  
1863 C C   . GLU B 65  ? 0.79833 1.01713 0.58635 0.10495  -0.12576 0.07723  32  GLU D C   
1864 O O   . GLU B 65  ? 0.83536 1.04395 0.62663 0.08725  -0.11844 0.05805  32  GLU D O   
1865 C CB  . GLU B 65  ? 0.86233 1.15111 0.65500 0.09860  -0.17495 0.05721  32  GLU D CB  
1866 C CG  . GLU B 65  ? 1.02463 1.29345 0.75119 0.09816  -0.17673 0.05523  32  GLU D CG  
1867 C CD  . GLU B 65  ? 1.29389 1.59273 1.00182 0.08591  -0.20324 0.03382  32  GLU D CD  
1868 O OE1 . GLU B 65  ? 1.32552 1.66846 1.06226 0.08968  -0.22952 0.03352  32  GLU D OE1 
1869 O OE2 . GLU B 65  ? 1.33145 1.61157 0.99902 0.07257  -0.19799 0.01495  32  GLU D OE2 
1870 N N   . GLU B 66  ? 0.80019 0.99283 0.56958 0.11843  -0.11120 0.09782  33  GLU D N   
1871 C CA  . GLU B 66  ? 0.73397 0.89162 0.48450 0.11346  -0.08573 0.09628  33  GLU D CA  
1872 C C   . GLU B 66  ? 0.83675 0.98814 0.53974 0.10560  -0.08625 0.08011  33  GLU D C   
1873 O O   . GLU B 66  ? 0.91629 1.07539 0.57648 0.11128  -0.09775 0.08631  33  GLU D O   
1874 C CB  . GLU B 66  ? 0.73996 0.87628 0.48101 0.12715  -0.07068 0.12175  33  GLU D CB  
1875 C CG  . GLU B 66  ? 0.87747 0.98513 0.60767 0.12254  -0.04303 0.12029  33  GLU D CG  
1876 C CD  . GLU B 66  ? 1.00634 1.09510 0.72614 0.13210  -0.02798 0.14558  33  GLU D CD  
1877 O OE1 . GLU B 66  ? 1.02669 1.11784 0.73320 0.14321  -0.04065 0.16579  33  GLU D OE1 
1878 O OE2 . GLU B 66  ? 0.86957 0.94065 0.59684 0.12828  -0.00449 0.14557  33  GLU D OE2 
1879 N N   . TYR B 67  ? 0.78041 0.91621 0.48920 0.09274  -0.07492 0.05878  34  TYR D N   
1880 C CA  . TYR B 67  ? 0.88953 1.01727 0.55848 0.08474  -0.07393 0.03670  34  TYR D CA  
1881 C C   . TYR B 67  ? 0.77076 0.86923 0.42730 0.08621  -0.04622 0.02998  34  TYR D C   
1882 O O   . TYR B 67  ? 0.88520 0.97786 0.49981 0.08400  -0.04014 0.01437  34  TYR D O   
1883 C CB  . TYR B 67  ? 0.74529 0.87944 0.43133 0.06740  -0.08822 0.01067  34  TYR D CB  
1884 C CG  . TYR B 67  ? 0.66647 0.77731 0.39094 0.05841  -0.07634 0.00279  34  TYR D CG  
1885 C CD1 . TYR B 67  ? 0.61323 0.73055 0.38070 0.05685  -0.07668 0.01622  34  TYR D CD1 
1886 C CD2 . TYR B 67  ? 0.75064 0.83185 0.46680 0.05185  -0.06585 -0.01857 34  TYR D CD2 
1887 C CE1 . TYR B 67  ? 0.64993 0.74433 0.44491 0.04742  -0.06841 0.01202  34  TYR D CE1 
1888 C CE2 . TYR B 67  ? 0.65603 0.71201 0.40553 0.04527  -0.05904 -0.02231 34  TYR D CE2 
1889 C CZ  . TYR B 67  ? 0.73036 0.79284 0.51616 0.04223  -0.06122 -0.00530 34  TYR D CZ  
1890 O OH  . TYR B 67  ? 0.70797 0.74378 0.51967 0.03449  -0.05687 -0.00613 34  TYR D OH  
1891 N N   . VAL B 68  ? 0.76718 0.85049 0.45985 0.08973  -0.02954 0.03905  35  VAL D N   
1892 C CA  . VAL B 68  ? 0.85992 0.92265 0.55144 0.09338  -0.00355 0.03386  35  VAL D CA  
1893 C C   . VAL B 68  ? 0.75618 0.81594 0.47206 0.10136  0.01013  0.05872  35  VAL D C   
1894 O O   . VAL B 68  ? 0.65645 0.71919 0.40852 0.10112  0.00253  0.06963  35  VAL D O   
1895 C CB  . VAL B 68  ? 0.75325 0.79666 0.47263 0.08708  0.00001  0.01100  35  VAL D CB  
1896 C CG1 . VAL B 68  ? 0.69333 0.72195 0.43068 0.09479  0.02475  0.00952  35  VAL D CG1 
1897 C CG2 . VAL B 68  ? 0.78668 0.82528 0.47727 0.07895  -0.00769 -0.01775 35  VAL D CG2 
1898 N N   . ARG B 69  ? 0.75064 0.80520 0.44587 0.10625  0.03163  0.06607  36  ARG D N   
1899 C CA  . ARG B 69  ? 0.72263 0.77243 0.44091 0.11078  0.04681  0.08754  36  ARG D CA  
1900 C C   . ARG B 69  ? 0.71720 0.76089 0.43835 0.11087  0.07553  0.07871  36  ARG D C   
1901 O O   . ARG B 69  ? 0.86595 0.91144 0.54787 0.10960  0.08847  0.06778  36  ARG D O   
1902 C CB  . ARG B 69  ? 0.74320 0.79563 0.43352 0.11563  0.04248  0.11496  36  ARG D CB  
1903 C CG  . ARG B 69  ? 0.82819 0.87001 0.53691 0.11755  0.06130  0.13603  36  ARG D CG  
1904 C CD  . ARG B 69  ? 1.14121 1.17710 0.82863 0.12350  0.05288  0.16533  36  ARG D CD  
1905 N NE  . ARG B 69  ? 1.09222 1.12553 0.71681 0.12320  0.05538  0.17531  36  ARG D NE  
1906 C CZ  . ARG B 69  ? 1.14395 1.18438 0.73267 0.12848  0.03080  0.18271  36  ARG D CZ  
1907 N NH1 . ARG B 69  ? 0.92276 0.97692 0.53805 0.13492  0.00344  0.17986  36  ARG D NH1 
1908 N NH2 . ARG B 69  ? 1.31672 1.35323 0.84131 0.12644  0.03361  0.19299  36  ARG D NH2 
1909 N N   . TYR B 70  ? 0.67973 0.71968 0.44812 0.11182  0.08542  0.08149  37  TYR D N   
1910 C CA  . TYR B 70  ? 0.78273 0.82433 0.56561 0.11239  0.11329  0.07699  37  TYR D CA  
1911 C C   . TYR B 70  ? 0.86151 0.90285 0.64618 0.11017  0.12572  0.10354  37  TYR D C   
1912 O O   . TYR B 70  ? 0.80401 0.84080 0.61086 0.11045  0.11315  0.11956  37  TYR D O   
1913 C CB  . TYR B 70  ? 0.71092 0.75060 0.54873 0.11504  0.11384  0.06204  37  TYR D CB  
1914 C CG  . TYR B 70  ? 0.73591 0.78523 0.60261 0.11648  0.14072  0.05832  37  TYR D CG  
1915 C CD1 . TYR B 70  ? 0.85238 0.90953 0.71161 0.11940  0.16248  0.03617  37  TYR D CD1 
1916 C CD2 . TYR B 70  ? 0.66104 0.71473 0.56488 0.11392  0.14533  0.07416  37  TYR D CD2 
1917 C CE1 . TYR B 70  ? 0.81495 0.88830 0.70748 0.12015  0.18904  0.03050  37  TYR D CE1 
1918 C CE2 . TYR B 70  ? 0.66807 0.73623 0.60394 0.11310  0.16950  0.06944  37  TYR D CE2 
1919 C CZ  . TYR B 70  ? 0.83202 0.91212 0.76438 0.11644  0.19176  0.04791  37  TYR D CZ  
1920 O OH  . TYR B 70  ? 0.72332 0.82484 0.69452 0.11514  0.21767  0.04102  37  TYR D OH  
1921 N N   . ASP B 71  ? 0.72018 0.76508 0.48088 0.10644  0.15189  0.10690  38  ASP D N   
1922 C CA  . ASP B 71  ? 0.78530 0.82505 0.54395 0.10083  0.16710  0.13273  38  ASP D CA  
1923 C C   . ASP B 71  ? 0.91011 0.96246 0.69175 0.09462  0.20057  0.12307  38  ASP D C   
1924 O O   . ASP B 71  ? 0.93126 0.99444 0.68927 0.09319  0.21968  0.10549  38  ASP D O   
1925 C CB  . ASP B 71  ? 0.90820 0.93773 0.60128 0.09889  0.16462  0.15481  38  ASP D CB  
1926 C CG  . ASP B 71  ? 0.92871 0.94183 0.62052 0.09400  0.17256  0.18670  38  ASP D CG  
1927 O OD1 . ASP B 71  ? 1.08792 1.10055 0.82911 0.08965  0.18369  0.18851  38  ASP D OD1 
1928 O OD2 . ASP B 71  ? 0.89469 0.89343 0.53574 0.09433  0.16579  0.21025  38  ASP D OD2 
1929 N N   . SER B 72  ? 0.82258 0.87653 0.65252 0.09025  0.20816  0.13188  39  SER D N   
1930 C CA  . SER B 72  ? 0.70645 0.77934 0.57007 0.08326  0.23912  0.12182  39  SER D CA  
1931 C C   . SER B 72  ? 0.72577 0.80047 0.54187 0.07125  0.27052  0.13234  39  SER D C   
1932 O O   . SER B 72  ? 0.96331 1.06096 0.79637 0.06547  0.30102  0.11615  39  SER D O   
1933 C CB  . SER B 72  ? 0.62599 0.70051 0.54736 0.07790  0.23792  0.13099  39  SER D CB  
1934 O OG  . SER B 72  ? 0.90980 0.96207 0.80992 0.06994  0.23614  0.15998  39  SER D OG  
1935 N N   . ASP B 73  ? 0.88178 0.93369 0.63905 0.06730  0.26378  0.15941  40  ASP D N   
1936 C CA  . ASP B 73  ? 0.98501 1.03401 0.68281 0.05444  0.29108  0.17285  40  ASP D CA  
1937 C C   . ASP B 73  ? 0.95120 1.01485 0.60262 0.05706  0.30001  0.14886  40  ASP D C   
1938 O O   . ASP B 73  ? 0.95769 1.03043 0.57003 0.04448  0.33227  0.14811  40  ASP D O   
1939 C CB  . ASP B 73  ? 1.01816 1.03395 0.66409 0.05205  0.27558  0.21135  40  ASP D CB  
1940 C CG  . ASP B 73  ? 1.19149 1.18792 0.87662 0.04573  0.27559  0.23470  40  ASP D CG  
1941 O OD1 . ASP B 73  ? 1.27349 1.28543 1.02541 0.04247  0.28433  0.22011  40  ASP D OD1 
1942 O OD2 . ASP B 73  ? 1.29215 1.25672 0.94178 0.04443  0.26537  0.26701  40  ASP D OD2 
1943 N N   . VAL B 74  ? 1.01478 1.08024 0.66806 0.07090  0.27371  0.12811  41  VAL D N   
1944 C CA  . VAL B 74  ? 1.00861 1.08569 0.62281 0.07325  0.28068  0.09950  41  VAL D CA  
1945 C C   . VAL B 74  ? 0.97385 1.07289 0.64707 0.07976  0.29686  0.06113  41  VAL D C   
1946 O O   . VAL B 74  ? 0.96888 1.08441 0.62353 0.07722  0.32406  0.03564  41  VAL D O   
1947 C CB  . VAL B 74  ? 0.91018 0.97485 0.48986 0.08220  0.24237  0.09791  41  VAL D CB  
1948 C CG1 . VAL B 74  ? 1.00759 1.08143 0.54165 0.08212  0.24864  0.06647  41  VAL D CG1 
1949 C CG2 . VAL B 74  ? 0.97639 1.02224 0.50729 0.07979  0.22319  0.13629  41  VAL D CG2 
1950 N N   . GLY B 75  ? 0.86852 0.96797 0.61276 0.08882  0.28020  0.05615  42  GLY D N   
1951 C CA  . GLY B 75  ? 0.86132 0.97844 0.66802 0.09811  0.28951  0.02397  42  GLY D CA  
1952 C C   . GLY B 75  ? 0.89046 0.99770 0.70094 0.11107  0.26698  -0.00297 42  GLY D C   
1953 O O   . GLY B 75  ? 0.92535 1.04138 0.78831 0.12169  0.27136  -0.02957 42  GLY D O   
1954 N N   . GLU B 76  ? 0.93322 1.02205 0.69301 0.11043  0.24202  0.00298  43  GLU D N   
1955 C CA  . GLU B 76  ? 0.96355 1.03997 0.72390 0.11847  0.22071  -0.02241 43  GLU D CA  
1956 C C   . GLU B 76  ? 0.82819 0.88889 0.55476 0.11509  0.18660  -0.00429 43  GLU D C   
1957 O O   . GLU B 76  ? 0.98437 1.04481 0.67725 0.10914  0.18179  0.02400  43  GLU D O   
1958 C CB  . GLU B 76  ? 0.89821 0.98046 0.62135 0.11893  0.24130  -0.05636 43  GLU D CB  
1959 C CG  . GLU B 76  ? 0.97493 1.06072 0.61382 0.10712  0.25033  -0.04621 43  GLU D CG  
1960 C CD  . GLU B 76  ? 1.28762 1.38191 0.88643 0.10555  0.27458  -0.08323 43  GLU D CD  
1961 O OE1 . GLU B 76  ? 1.18759 1.28624 0.83194 0.11542  0.28862  -0.11782 43  GLU D OE1 
1962 O OE2 . GLU B 76  ? 1.47983 1.57598 1.00095 0.09509  0.27878  -0.07847 43  GLU D OE2 
1963 N N   . HIS B 77  ? 0.88965 0.93700 0.62881 0.11893  0.16292  -0.02108 44  HIS D N   
1964 C CA  . HIS B 77  ? 0.76829 0.80717 0.48231 0.11432  0.13163  -0.00932 44  HIS D CA  
1965 C C   . HIS B 77  ? 0.79402 0.83783 0.43703 0.10843  0.13018  -0.01379 44  HIS D C   
1966 O O   . HIS B 77  ? 0.84154 0.88782 0.45500 0.10747  0.14771  -0.03937 44  HIS D O   
1967 C CB  . HIS B 77  ? 0.72068 0.74326 0.46557 0.11569  0.10956  -0.02692 44  HIS D CB  
1968 C CG  . HIS B 77  ? 0.76558 0.78135 0.57219 0.12038  0.10458  -0.01869 44  HIS D CG  
1969 N ND1 . HIS B 77  ? 0.66810 0.68356 0.51723 0.12936  0.12068  -0.03204 44  HIS D ND1 
1970 C CD2 . HIS B 77  ? 0.65410 0.66551 0.48594 0.11715  0.08459  0.00071  44  HIS D CD2 
1971 C CE1 . HIS B 77  ? 0.72499 0.73473 0.62003 0.13132  0.10768  -0.01915 44  HIS D CE1 
1972 N NE2 . HIS B 77  ? 0.72054 0.72686 0.60297 0.12291  0.08717  0.00036  44  HIS D NE2 
1973 N N   . ARG B 78  ? 0.86884 0.91563 0.48481 0.10511  0.10841  0.01007  45  ARG D N   
1974 C CA  . ARG B 78  ? 0.93786 0.99126 0.48570 0.10017  0.09922  0.01098  45  ARG D CA  
1975 C C   . ARG B 78  ? 0.99430 1.05100 0.54222 0.09825  0.06240  0.01436  45  ARG D C   
1976 O O   . ARG B 78  ? 0.90624 0.96319 0.49562 0.10087  0.04770  0.03140  45  ARG D O   
1977 C CB  . ARG B 78  ? 0.97731 1.03467 0.48581 0.09915  0.11090  0.04300  45  ARG D CB  
1978 C CG  . ARG B 78  ? 0.90981 0.96958 0.40465 0.09576  0.15070  0.03803  45  ARG D CG  
1979 C CD  . ARG B 78  ? 1.09876 1.16437 0.54076 0.09047  0.16428  0.00607  45  ARG D CD  
1980 N NE  . ARG B 78  ? 1.08465 1.15797 0.50079 0.08450  0.20456  0.00477  45  ARG D NE  
1981 C CZ  . ARG B 78  ? 1.40823 1.48269 0.75814 0.07552  0.21483  0.02939  45  ARG D CZ  
1982 N NH1 . ARG B 78  ? 1.34669 1.41414 0.65077 0.07480  0.18484  0.05810  45  ARG D NH1 
1983 N NH2 . ARG B 78  ? 1.67899 1.76239 1.00916 0.06686  0.25600  0.02579  45  ARG D NH2 
1984 N N   . ALA B 79  ? 0.94616 1.00851 0.44852 0.09233  0.04851  -0.00427 46  ALA D N   
1985 C CA  . ALA B 79  ? 0.86856 0.94096 0.37224 0.08810  0.01353  -0.00526 46  ALA D CA  
1986 C C   . ALA B 79  ? 0.88273 0.97032 0.35781 0.09265  -0.00445 0.02745  46  ALA D C   
1987 O O   . ALA B 79  ? 1.09340 1.18591 0.50644 0.09179  -0.00411 0.03379  46  ALA D O   
1988 C CB  . ALA B 79  ? 0.91569 0.98872 0.38510 0.07830  0.00429  -0.04120 46  ALA D CB  
1989 N N   . VAL B 80  ? 0.83396 0.92788 0.35290 0.09796  -0.02047 0.04820  47  VAL D N   
1990 C CA  . VAL B 80  ? 0.84819 0.95471 0.34976 0.10612  -0.04045 0.07829  47  VAL D CA  
1991 C C   . VAL B 80  ? 0.91685 1.04655 0.38620 0.10237  -0.07274 0.06810  47  VAL D C   
1992 O O   . VAL B 80  ? 1.07138 1.20871 0.49088 0.10727  -0.08678 0.08572  47  VAL D O   
1993 C CB  . VAL B 80  ? 0.81995 0.92859 0.38244 0.11376  -0.04693 0.09723  47  VAL D CB  
1994 C CG1 . VAL B 80  ? 0.80801 0.92430 0.35756 0.12628  -0.06552 0.12856  47  VAL D CG1 
1995 C CG2 . VAL B 80  ? 0.92994 1.01788 0.52558 0.11469  -0.01754 0.10255  47  VAL D CG2 
1996 N N   . THR B 81  ? 0.99008 1.13071 0.48644 0.09238  -0.08638 0.04056  48  THR D N   
1997 C CA  . THR B 81  ? 1.00408 1.16950 0.47567 0.08452  -0.11653 0.02383  48  THR D CA  
1998 C C   . THR B 81  ? 1.01398 1.16810 0.46924 0.06878  -0.10855 -0.01611 48  THR D C   
1999 O O   . THR B 81  ? 1.00356 1.13140 0.47454 0.06673  -0.08164 -0.02952 48  THR D O   
2000 C CB  . THR B 81  ? 0.90659 1.10058 0.43289 0.08422  -0.14362 0.02657  48  THR D CB  
2001 O OG1 . THR B 81  ? 1.05096 1.23408 0.63204 0.07473  -0.13142 0.01192  48  THR D OG1 
2002 C CG2 . THR B 81  ? 0.91034 1.11395 0.45597 0.10274  -0.15181 0.06258  48  THR D CG2 
2003 N N   . GLU B 82  ? 1.11734 0.99552 0.63487 0.11594  -0.15539 0.08475  49  GLU D N   
2004 C CA  . GLU B 82  ? 1.19181 1.08059 0.73259 0.10171  -0.15109 0.04589  49  GLU D CA  
2005 C C   . GLU B 82  ? 1.15044 1.05364 0.79616 0.05991  -0.12653 0.03647  49  GLU D C   
2006 O O   . GLU B 82  ? 1.13434 1.02488 0.79141 0.04454  -0.10546 0.02122  49  GLU D O   
2007 C CB  . GLU B 82  ? 1.24376 1.17022 0.77477 0.12772  -0.20227 -0.01351 49  GLU D CB  
2008 C CG  . GLU B 82  ? 1.80756 1.70310 1.20772 0.18240  -0.23288 -0.00821 49  GLU D CG  
2009 C CD  . GLU B 82  ? 2.02731 1.96536 1.41750 0.21712  -0.29229 -0.07740 49  GLU D CD  
2010 O OE1 . GLU B 82  ? 2.01140 2.01076 1.51347 0.19086  -0.30393 -0.13356 49  GLU D OE1 
2011 O OE2 . GLU B 82  ? 2.21470 2.11949 1.48141 0.27306  -0.32543 -0.07960 49  GLU D OE2 
2012 N N   . LEU B 83  ? 1.11882 1.03770 0.83101 0.04395  -0.12619 0.04567  50  LEU D N   
2013 C CA  . LEU B 83  ? 0.88609 0.79587 0.67537 0.00916  -0.09755 0.03909  50  LEU D CA  
2014 C C   . LEU B 83  ? 0.97884 0.84345 0.75020 0.00219  -0.05976 0.07708  50  LEU D C   
2015 O O   . LEU B 83  ? 1.05761 0.89513 0.86086 -0.01574 -0.03594 0.06766  50  LEU D O   
2016 C CB  . LEU B 83  ? 0.85033 0.77737 0.70122 -0.00374 -0.10183 0.04278  50  LEU D CB  
2017 C CG  . LEU B 83  ? 0.99820 0.90363 0.92003 -0.03879 -0.06979 0.02623  50  LEU D CG  
2018 C CD1 . LEU B 83  ? 0.93343 0.86040 0.90621 -0.05632 -0.07092 -0.04204 50  LEU D CD1 
2019 C CD2 . LEU B 83  ? 0.93728 0.84939 0.90365 -0.04940 -0.06768 0.04146  50  LEU D CD2 
2020 N N   . GLY B 84  ? 1.00821 0.86005 0.72860 0.01835  -0.05188 0.11395  51  GLY D N   
2021 C CA  . GLY B 84  ? 0.94414 0.76824 0.66420 0.01564  -0.02075 0.13870  51  GLY D CA  
2022 C C   . GLY B 84  ? 1.02234 0.83122 0.70384 0.02198  -0.00398 0.12848  51  GLY D C   
2023 O O   . GLY B 84  ? 1.03360 0.82885 0.72266 0.02354  0.01966  0.14004  51  GLY D O   
2024 N N   . ARG B 85  ? 1.02591 0.84001 0.67049 0.02758  -0.01658 0.10132  52  ARG D N   
2025 C CA  . ARG B 85  ? 1.14716 0.94387 0.75356 0.03175  0.00278  0.08959  52  ARG D CA  
2026 C C   . ARG B 85  ? 1.14625 0.92879 0.79541 0.02119  0.02081  0.07572  52  ARG D C   
2027 O O   . ARG B 85  ? 1.12033 0.89131 0.76431 0.02546  0.04433  0.07859  52  ARG D O   
2028 C CB  . ARG B 85  ? 1.22770 1.03055 0.78117 0.04339  -0.01877 0.05981  52  ARG D CB  
2029 C CG  . ARG B 85  ? 1.11746 0.90706 0.58437 0.06900  -0.02971 0.07542  52  ARG D CG  
2030 C CD  . ARG B 85  ? 1.45808 1.23642 0.84894 0.08875  -0.04414 0.04547  52  ARG D CD  
2031 N NE  . ARG B 85  ? 1.63965 1.37932 0.91645 0.12244  -0.05017 0.06291  52  ARG D NE  
2032 C CZ  . ARG B 85  ? 1.70663 1.45592 0.93834 0.15502  -0.09797 0.04850  52  ARG D CZ  
2033 N NH1 . ARG B 85  ? 1.63356 1.44347 0.94303 0.15252  -0.14232 0.00927  52  ARG D NH1 
2034 N NH2 . ARG B 85  ? 1.96363 1.65519 1.06708 0.19334  -0.09891 0.06905  52  ARG D NH2 
2035 N N   . PRO B 86  ? 0.96731 0.74364 0.65646 0.00933  0.01496  0.05647  53  PRO D N   
2036 C CA  . PRO B 86  ? 0.94642 0.68849 0.65402 0.00790  0.03451  0.04706  53  PRO D CA  
2037 C C   . PRO B 86  ? 0.95696 0.68103 0.68078 0.01973  0.04511  0.07283  53  PRO D C   
2038 O O   . PRO B 86  ? 1.10318 0.80994 0.82730 0.03311  0.05645  0.06474  53  PRO D O   
2039 C CB  . PRO B 86  ? 0.94778 0.67131 0.68459 -0.00933 0.03494  0.02290  53  PRO D CB  
2040 C CG  . PRO B 86  ? 0.89468 0.66280 0.63630 -0.01661 0.01104  0.00096  53  PRO D CG  
2041 C CD  . PRO B 86  ? 0.96432 0.75847 0.68092 -0.00227 -0.00481 0.03309  53  PRO D CD  
2042 N N   . ASP B 87  ? 1.08084 0.81218 0.82107 0.01867  0.03847  0.09836  54  ASP D N   
2043 C CA  . ASP B 87  ? 1.09251 0.80897 0.84928 0.03378  0.04393  0.11738  54  ASP D CA  
2044 C C   . ASP B 87  ? 1.06326 0.80875 0.82415 0.04531  0.05282  0.11968  54  ASP D C   
2045 O O   . ASP B 87  ? 1.02152 0.76144 0.80221 0.06418  0.05739  0.11057  54  ASP D O   
2046 C CB  . ASP B 87  ? 1.00898 0.72624 0.78306 0.02734  0.03646  0.14181  54  ASP D CB  
2047 C CG  . ASP B 87  ? 1.32841 1.01154 1.10905 0.01097  0.03952  0.13166  54  ASP D CG  
2048 O OD1 . ASP B 87  ? 1.26357 0.90352 1.03196 0.01011  0.05247  0.11077  54  ASP D OD1 
2049 O OD2 . ASP B 87  ? 1.24087 0.93731 1.04169 -0.00245 0.03369  0.14089  54  ASP D OD2 
2050 N N   . ALA B 88  ? 0.94599 0.71726 0.68606 0.03683  0.05775  0.12651  55  ALA D N   
2051 C CA  . ALA B 88  ? 0.98628 0.77318 0.72884 0.04077  0.08167  0.12435  55  ALA D CA  
2052 C C   . ALA B 88  ? 1.09300 0.87623 0.83489 0.04495  0.09829  0.09182  55  ALA D C   
2053 O O   . ALA B 88  ? 0.96891 0.76676 0.74748 0.05231  0.11715  0.07347  55  ALA D O   
2054 C CB  . ALA B 88  ? 0.89643 0.68515 0.59169 0.03373  0.09092  0.14259  55  ALA D CB  
2055 N N   . GLU B 89  ? 1.17947 0.94859 0.88866 0.04035  0.09159  0.07749  56  GLU D N   
2056 C CA  . GLU B 89  ? 1.15765 0.92214 0.86531 0.04356  0.10734  0.04575  56  GLU D CA  
2057 C C   . GLU B 89  ? 1.05192 0.80658 0.80173 0.06167  0.09966  0.02706  56  GLU D C   
2058 O O   . GLU B 89  ? 1.08973 0.85477 0.86572 0.07264  0.11325  -0.00186 56  GLU D O   
2059 C CB  . GLU B 89  ? 1.27164 1.02416 0.93292 0.03542  0.09979  0.03312  56  GLU D CB  
2060 C CG  . GLU B 89  ? 1.67378 1.42511 1.27068 0.03124  0.10501  0.04280  56  GLU D CG  
2061 C CD  . GLU B 89  ? 1.86485 1.60482 1.43266 0.02994  0.14560  0.03331  56  GLU D CD  
2062 O OE1 . GLU B 89  ? 1.91929 1.66592 1.52944 0.02949  0.16546  0.00810  56  GLU D OE1 
2063 O OE2 . GLU B 89  ? 1.89972 1.61758 1.39835 0.03130  0.16044  0.04793  56  GLU D OE2 
2064 N N   . TYR B 90  ? 1.01291 0.74060 0.76462 0.06820  0.07986  0.03970  57  TYR D N   
2065 C CA  . TYR B 90  ? 1.01688 0.71055 0.78004 0.09522  0.07205  0.02517  57  TYR D CA  
2066 C C   . TYR B 90  ? 1.01996 0.73515 0.82291 0.12156  0.06669  0.01969  57  TYR D C   
2067 O O   . TYR B 90  ? 1.01468 0.72845 0.83766 0.15119  0.06167  -0.01181 57  TYR D O   
2068 C CB  . TYR B 90  ? 0.90159 0.53971 0.63976 0.09391  0.06412  0.04106  57  TYR D CB  
2069 C CG  . TYR B 90  ? 1.11582 0.69022 0.83584 0.12988  0.05894  0.03310  57  TYR D CG  
2070 C CD1 . TYR B 90  ? 1.11471 0.65031 0.81374 0.14548  0.06374  0.00693  57  TYR D CD1 
2071 C CD2 . TYR B 90  ? 1.16136 0.70533 0.87380 0.15348  0.04845  0.05152  57  TYR D CD2 
2072 C CE1 . TYR B 90  ? 1.28069 0.74164 0.94350 0.18812  0.05734  0.00029  57  TYR D CE1 
2073 C CE2 . TYR B 90  ? 1.26323 0.73158 0.93500 0.19731  0.04115  0.04457  57  TYR D CE2 
2074 C CZ  . TYR B 90  ? 1.37950 0.80279 1.02237 0.21672  0.04519  0.01944  57  TYR D CZ  
2075 O OH  . TYR B 90  ? 1.56874 0.90122 1.15259 0.26964  0.03635  0.01310  57  TYR D OH  
2076 N N   . TRP B 91  ? 0.95530 0.69451 0.77489 0.11405  0.06526  0.04394  58  TRP D N   
2077 C CA  . TRP B 91  ? 0.92060 0.68682 0.78680 0.13868  0.05893  0.03264  58  TRP D CA  
2078 C C   . TRP B 91  ? 0.98506 0.80406 0.90236 0.13631  0.08158  -0.00549 58  TRP D C   
2079 O O   . TRP B 91  ? 0.99551 0.84109 0.96593 0.16586  0.07361  -0.04342 58  TRP D O   
2080 C CB  . TRP B 91  ? 0.87747 0.65526 0.75016 0.12710  0.05565  0.06757  58  TRP D CB  
2081 C CG  . TRP B 91  ? 0.82034 0.54524 0.65566 0.13159  0.03874  0.09602  58  TRP D CG  
2082 C CD1 . TRP B 91  ? 0.97192 0.63179 0.77001 0.15523  0.02879  0.09075  58  TRP D CD1 
2083 C CD2 . TRP B 91  ? 0.82160 0.54440 0.64949 0.11093  0.03703  0.13111  58  TRP D CD2 
2084 N NE1 . TRP B 91  ? 0.88811 0.50074 0.65596 0.14633  0.02826  0.11951  58  TRP D NE1 
2085 C CE2 . TRP B 91  ? 0.78260 0.44048 0.57573 0.11859  0.03061  0.14235  58  TRP D CE2 
2086 C CE3 . TRP B 91  ? 0.91397 0.67632 0.75718 0.08819  0.04342  0.15239  58  TRP D CE3 
2087 C CZ2 . TRP B 91  ? 0.89255 0.53436 0.67950 0.10009  0.03134  0.16919  58  TRP D CZ2 
2088 C CZ3 . TRP B 91  ? 0.84060 0.59084 0.67606 0.07522  0.03593  0.18064  58  TRP D CZ3 
2089 C CH2 . TRP B 91  ? 0.82258 0.51824 0.63686 0.07911  0.03035  0.18648  58  TRP D CH2 
2090 N N   . ASN B 92  ? 0.91133 0.74230 0.81169 0.10392  0.11162  -0.00173 59  ASN D N   
2091 C CA  . ASN B 92  ? 0.82031 0.68613 0.76163 0.09486  0.14812  -0.04010 59  ASN D CA  
2092 C C   . ASN B 92  ? 0.93390 0.79922 0.88746 0.10754  0.14992  -0.08365 59  ASN D C   
2093 O O   . ASN B 92  ? 0.98351 0.88489 0.99615 0.10819  0.17602  -0.13143 59  ASN D O   
2094 C CB  . ASN B 92  ? 0.94252 0.79758 0.83596 0.06062  0.18609  -0.01749 59  ASN D CB  
2095 C CG  . ASN B 92  ? 1.02611 0.88450 0.91577 0.05048  0.19168  0.01762  59  ASN D CG  
2096 O OD1 . ASN B 92  ? 0.99388 0.87830 0.93960 0.06313  0.17910  0.01396  59  ASN D OD1 
2097 N ND2 . ASN B 92  ? 0.95468 0.78373 0.77279 0.03248  0.20815  0.04956  59  ASN D ND2 
2098 N N   . SER B 93  ? 1.05080 0.87641 0.95640 0.11579  0.12699  -0.07349 60  SER D N   
2099 C CA  . SER B 93  ? 1.03652 0.85604 0.94967 0.13016  0.12712  -0.11340 60  SER D CA  
2100 C C   . SER B 93  ? 1.06002 0.88388 1.01757 0.17855  0.09766  -0.14931 60  SER D C   
2101 O O   . SER B 93  ? 1.03566 0.87067 1.02192 0.19687  0.09858  -0.19596 60  SER D O   
2102 C CB  . SER B 93  ? 0.91192 0.68326 0.75859 0.12088  0.11754  -0.09384 60  SER D CB  
2103 O OG  . SER B 93  ? 1.20129 0.92873 1.02062 0.13673  0.08986  -0.06761 60  SER D OG  
2104 N N   . GLN B 94  ? 1.02931 0.84103 0.98727 0.20447  0.06933  -0.13130 61  GLN D N   
2105 C CA  . GLN B 94  ? 0.96442 0.77155 0.94753 0.26287  0.03416  -0.16659 61  GLN D CA  
2106 C C   . GLN B 94  ? 0.99542 0.88284 1.07590 0.27297  0.03792  -0.21229 61  GLN D C   
2107 O O   . GLN B 94  ? 0.91505 0.82473 1.01378 0.25813  0.04318  -0.18959 61  GLN D O   
2108 C CB  . GLN B 94  ? 1.19594 0.93342 1.11385 0.29030  0.00448  -0.12613 61  GLN D CB  
2109 C CG  . GLN B 94  ? 1.14375 0.80009 0.97710 0.27229  0.01177  -0.08700 61  GLN D CG  
2110 C CD  . GLN B 94  ? 1.54524 1.15147 1.34535 0.30124  0.00591  -0.11465 61  GLN D CD  
2111 O OE1 . GLN B 94  ? 1.75564 1.36971 1.57865 0.35164  -0.01645 -0.15855 61  GLN D OE1 
2112 N NE2 . GLN B 94  ? 1.61357 1.17044 1.36372 0.27180  0.02464  -0.09481 61  GLN D NE2 
2113 N N   . PRO B 95  ? 1.07738 0.91250 0.87022 0.40198  0.21919  0.03436  62  PRO D N   
2114 C CA  . PRO B 95  ? 0.87643 0.82150 0.77391 0.40012  0.23727  0.02968  62  PRO D CA  
2115 C C   . PRO B 95  ? 0.82877 0.79029 0.76446 0.38356  0.20569  0.03871  62  PRO D C   
2116 O O   . PRO B 95  ? 0.89409 0.91956 0.88888 0.35274  0.21949  0.04811  62  PRO D O   
2117 C CB  . PRO B 95  ? 0.90905 0.90079 0.84718 0.45625  0.24581  -0.00110 62  PRO D CB  
2118 C CG  . PRO B 95  ? 0.98126 0.89218 0.83205 0.48016  0.25018  -0.00959 62  PRO D CG  
2119 C CD  . PRO B 95  ? 1.11735 0.91616 0.87399 0.45439  0.21556  0.01257  62  PRO D CD  
2120 N N   . GLU B 96  ? 0.95591 0.84988 0.84745 0.39988  0.16102  0.03647  63  GLU D N   
2121 C CA  . GLU B 96  ? 0.98671 0.88381 0.89963 0.38002  0.12944  0.04471  63  GLU D CA  
2122 C C   . GLU B 96  ? 0.99643 0.88212 0.89001 0.32142  0.13728  0.06311  63  GLU D C   
2123 O O   . GLU B 96  ? 0.97897 0.89424 0.90978 0.29779  0.12622  0.06912  63  GLU D O   
2124 C CB  . GLU B 96  ? 1.01303 0.81532 0.85583 0.40347  0.07539  0.03920  63  GLU D CB  
2125 C CG  . GLU B 96  ? 1.26076 0.94620 0.98086 0.37495  0.06013  0.04906  63  GLU D CG  
2126 C CD  . GLU B 96  ? 1.52399 1.16472 1.18956 0.40062  0.07471  0.04166  63  GLU D CD  
2127 O OE1 . GLU B 96  ? 1.46131 1.15453 1.17829 0.44666  0.09410  0.02517  63  GLU D OE1 
2128 O OE2 . GLU B 96  ? 1.64185 1.19773 1.21201 0.37153  0.06825  0.04994  63  GLU D OE2 
2129 N N   . ILE B 97  ? 0.95658 0.80242 0.79580 0.29969  0.15393  0.06847  64  ILE D N   
2130 C CA  . ILE B 97  ? 0.94359 0.79172 0.77816 0.25106  0.16020  0.07687  64  ILE D CA  
2131 C C   . ILE B 97  ? 0.85739 0.77733 0.75919 0.23914  0.18921  0.08167  64  ILE D C   
2132 O O   . ILE B 97  ? 0.78379 0.73671 0.72371 0.21195  0.18719  0.08530  64  ILE D O   
2133 C CB  . ILE B 97  ? 0.89760 0.67541 0.64922 0.23217  0.15837  0.07621  64  ILE D CB  
2134 C CG1 . ILE B 97  ? 0.87621 0.56877 0.54332 0.22914  0.12547  0.07358  64  ILE D CG1 
2135 C CG2 . ILE B 97  ? 0.85468 0.65480 0.62086 0.18929  0.16622  0.07559  64  ILE D CG2 
2136 C CD1 . ILE B 97  ? 1.06317 0.68860 0.64414 0.19989  0.12284  0.07203  64  ILE D CD1 
2137 N N   . LEU B 98  ? 0.89931 0.83533 0.80604 0.25654  0.21512  0.08080  65  LEU D N   
2138 C CA  . LEU B 98  ? 0.83611 0.82032 0.78336 0.23764  0.23977  0.08719  65  LEU D CA  
2139 C C   . LEU B 98  ? 0.90760 0.96702 0.93226 0.23404  0.24313  0.08821  65  LEU D C   
2140 O O   . LEU B 98  ? 0.87091 0.95571 0.92324 0.20489  0.24708  0.09646  65  LEU D O   
2141 C CB  . LEU B 98  ? 0.75963 0.73649 0.67951 0.25027  0.26867  0.08482  65  LEU D CB  
2142 C CG  . LEU B 98  ? 0.80204 0.80643 0.73597 0.22302  0.29314  0.09286  65  LEU D CG  
2143 C CD1 . LEU B 98  ? 0.87670 0.84257 0.78928 0.19259  0.27441  0.10260  65  LEU D CD1 
2144 C CD2 . LEU B 98  ? 0.76144 0.75007 0.65269 0.23121  0.32398  0.08817  65  LEU D CD2 
2145 N N   . GLU B 99  ? 0.86738 0.95956 0.92640 0.26448  0.23658  0.07809  66  GLU D N   
2146 C CA  . GLU B 99  ? 0.68335 0.85442 0.82220 0.26058  0.23664  0.07673  66  GLU D CA  
2147 C C   . GLU B 99  ? 0.69982 0.85978 0.84889 0.23746  0.20681  0.08563  66  GLU D C   
2148 O O   . GLU B 99  ? 0.76361 0.97565 0.96572 0.21647  0.20845  0.09109  66  GLU D O   
2149 C CB  . GLU B 99  ? 0.67469 0.89016 0.85667 0.30592  0.23181  0.05671  66  GLU D CB  
2150 C CG  . GLU B 99  ? 1.16231 1.41732 1.35394 0.32646  0.27045  0.04006  66  GLU D CG  
2151 C CD  . GLU B 99  ? 1.10715 1.43374 1.33813 0.28774  0.31122  0.04423  66  GLU D CD  
2152 O OE1 . GLU B 99  ? 1.12393 1.50182 1.40853 0.26104  0.30591  0.05190  66  GLU D OE1 
2153 O OE2 . GLU B 99  ? 1.23374 1.55591 1.43102 0.27944  0.34698  0.04057  66  GLU D OE2 
2154 N N   . ARG B 100 ? 0.77833 0.86881 0.87062 0.23564  0.18085  0.08598  67  ARG D N   
2155 C CA  . ARG B 100 ? 0.65107 0.72859 0.74289 0.20727  0.15781  0.09055  67  ARG D CA  
2156 C C   . ARG B 100 ? 0.75148 0.83702 0.84905 0.17170  0.17076  0.09530  67  ARG D C   
2157 O O   . ARG B 100 ? 0.73037 0.83911 0.85931 0.14985  0.16248  0.09801  67  ARG D O   
2158 C CB  . ARG B 100 ? 0.71998 0.71822 0.73642 0.20435  0.13075  0.08668  67  ARG D CB  
2159 C CG  . ARG B 100 ? 0.84856 0.83126 0.85958 0.18236  0.10197  0.08791  67  ARG D CG  
2160 C CD  . ARG B 100 ? 0.87195 0.77498 0.79298 0.15263  0.08648  0.08359  67  ARG D CD  
2161 N NE  . ARG B 100 ? 0.89505 0.81272 0.81501 0.11386  0.10664  0.07715  67  ARG D NE  
2162 C CZ  . ARG B 100 ? 1.01523 0.92332 0.91152 0.10711  0.12429  0.07065  67  ARG D CZ  
2163 N NH1 . ARG B 100 ? 1.18847 1.06399 1.04924 0.13156  0.12737  0.07330  67  ARG D NH1 
2164 N NH2 . ARG B 100 ? 0.72667 0.65852 0.63662 0.07741  0.13625  0.05804  67  ARG D NH2 
2165 N N   . THR B 101 ? 0.73809 0.79894 0.80307 0.16817  0.18613  0.09436  68  THR D N   
2166 C CA  . THR B 101 ? 0.56406 0.62583 0.63471 0.14294  0.18946  0.09436  68  THR D CA  
2167 C C   . THR B 101 ? 0.67874 0.78136 0.79177 0.13401  0.20097  0.10429  68  THR D C   
2168 O O   . THR B 101 ? 0.78038 0.88973 0.91233 0.11298  0.19129  0.10521  68  THR D O   
2169 C CB  . THR B 101 ? 0.70564 0.72590 0.72937 0.14440  0.19517  0.08966  68  THR D CB  
2170 O OG1 . THR B 101 ? 0.77811 0.76089 0.75712 0.14294  0.18470  0.07989  68  THR D OG1 
2171 C CG2 . THR B 101 ? 0.87030 0.88683 0.90269 0.12606  0.18809  0.08451  68  THR D CG2 
2172 N N   . ARG B 102 ? 0.66194 0.79073 0.78541 0.14662  0.22215  0.10909  69  ARG D N   
2173 C CA  . ARG B 102 ? 0.54017 0.70868 0.69370 0.12663  0.23747  0.11769  69  ARG D CA  
2174 C C   . ARG B 102 ? 0.58062 0.79788 0.79011 0.11441  0.22546  0.12052  69  ARG D C   
2175 O O   . ARG B 102 ? 0.58677 0.81078 0.80683 0.08523  0.22244  0.12876  69  ARG D O   
2176 C CB  . ARG B 102 ? 0.57879 0.77976 0.73516 0.13836  0.26921  0.11488  69  ARG D CB  
2177 C CG  . ARG B 102 ? 0.66932 0.81621 0.76078 0.13964  0.28401  0.11574  69  ARG D CG  
2178 C CD  . ARG B 102 ? 0.81925 1.00271 0.91228 0.15212  0.31975  0.10703  69  ARG D CD  
2179 N NE  . ARG B 102 ? 0.90302 1.02866 0.92390 0.14346  0.33580  0.11039  69  ARG D NE  
2180 C CZ  . ARG B 102 ? 0.88938 1.02802 0.88996 0.15298  0.36930  0.10010  69  ARG D CZ  
2181 N NH1 . ARG B 102 ? 0.80365 1.02040 0.86036 0.17719  0.39060  0.08091  69  ARG D NH1 
2182 N NH2 . ARG B 102 ? 0.97176 1.04366 0.89441 0.13957  0.37958  0.10567  69  ARG D NH2 
2183 N N   . ALA B 103 ? 0.50872 0.74959 0.74624 0.13576  0.21294  0.11406  70  ALA D N   
2184 C CA  . ALA B 103 ? 0.54113 0.82695 0.83132 0.12592  0.19717  0.11640  70  ALA D CA  
2185 C C   . ALA B 103 ? 0.50314 0.75457 0.77951 0.10134  0.17408  0.12015  70  ALA D C   
2186 O O   . ALA B 103 ? 0.46430 0.74407 0.77606 0.08618  0.16035  0.12441  70  ALA D O   
2187 C CB  . ALA B 103 ? 0.53305 0.83798 0.84756 0.15977  0.17985  0.10651  70  ALA D CB  
2188 N N   . GLU B 104 ? 0.48633 0.68301 0.71555 0.09675  0.16970  0.11488  71  GLU D N   
2189 C CA  . GLU B 104 ? 0.61812 0.79204 0.83934 0.07557  0.15169  0.10916  71  GLU D CA  
2190 C C   . GLU B 104 ? 0.54460 0.72505 0.78217 0.05278  0.14908  0.11535  71  GLU D C   
2191 O O   . GLU B 104 ? 0.54492 0.71519 0.78585 0.03696  0.13255  0.10951  71  GLU D O   
2192 C CB  . GLU B 104 ? 0.51399 0.64487 0.69174 0.07649  0.15017  0.09354  71  GLU D CB  
2193 C CG  . GLU B 104 ? 0.54349 0.65027 0.68691 0.08361  0.14424  0.08666  71  GLU D CG  
2194 C CD  . GLU B 104 ? 0.71705 0.79122 0.81790 0.07605  0.14704  0.06929  71  GLU D CD  
2195 O OE1 . GLU B 104 ? 0.83661 0.90538 0.93301 0.08362  0.15590  0.06651  71  GLU D OE1 
2196 O OE2 . GLU B 104 ? 0.68227 0.73528 0.75036 0.05823  0.13939  0.05719  71  GLU D OE2 
2197 N N   . LEU B 105 ? 0.50257 0.69142 0.74010 0.04737  0.16394  0.12601  72  LEU D N   
2198 C CA  . LEU B 105 ? 0.49362 0.67444 0.73103 0.01916  0.15651  0.13511  72  LEU D CA  
2199 C C   . LEU B 105 ? 0.58363 0.80904 0.86362 0.00129  0.14940  0.14319  72  LEU D C   
2200 O O   . LEU B 105 ? 0.58092 0.78745 0.85634 -0.02243 0.13223  0.14705  72  LEU D O   
2201 C CB  . LEU B 105 ? 0.53161 0.70334 0.74269 0.00680  0.17531  0.14617  72  LEU D CB  
2202 C CG  . LEU B 105 ? 0.57978 0.71134 0.75846 -0.02837 0.16279  0.15734  72  LEU D CG  
2203 C CD1 . LEU B 105 ? 0.63343 0.70655 0.74925 -0.03408 0.16761  0.16174  72  LEU D CD1 
2204 C CD2 . LEU B 105 ? 0.59244 0.77786 0.80045 -0.06242 0.17518  0.17089  72  LEU D CD2 
2205 N N   . ASP B 106 ? 0.64785 0.92868 0.96847 0.01454  0.15743  0.14375  73  ASP D N   
2206 C CA  . ASP B 106 ? 0.51333 0.84182 0.88151 0.00116  0.14489  0.14878  73  ASP D CA  
2207 C C   . ASP B 106 ? 0.51647 0.82311 0.88231 0.01041  0.11798  0.14211  73  ASP D C   
2208 O O   . ASP B 106 ? 0.57774 0.88200 0.95258 -0.01111 0.09852  0.14603  73  ASP D O   
2209 C CB  . ASP B 106 ? 0.49031 0.89904 0.91333 0.01303  0.16238  0.14675  73  ASP D CB  
2210 C CG  . ASP B 106 ? 0.78295 1.22512 1.20789 -0.01329 0.19363  0.15209  73  ASP D CG  
2211 O OD1 . ASP B 106 ? 0.83032 1.24147 1.22507 -0.05242 0.19052  0.16417  73  ASP D OD1 
2212 O OD2 . ASP B 106 ? 0.57704 1.07040 1.02589 0.00297  0.22035  0.14241  73  ASP D OD2 
2213 N N   . THR B 107 ? 0.45024 0.73193 0.79260 0.03677  0.11568  0.13238  74  THR D N   
2214 C CA  . THR B 107 ? 0.53246 0.78274 0.85465 0.03759  0.09045  0.12639  74  THR D CA  
2215 C C   . THR B 107 ? 0.58982 0.79117 0.87017 0.01595  0.08499  0.11618  74  THR D C   
2216 O O   . THR B 107 ? 0.52733 0.70167 0.78387 0.00357  0.06704  0.11028  74  THR D O   
2217 C CB  . THR B 107 ? 0.47789 0.70528 0.77310 0.06690  0.08677  0.11951  74  THR D CB  
2218 O OG1 . THR B 107 ? 0.55922 0.75121 0.81085 0.07111  0.10496  0.11199  74  THR D OG1 
2219 C CG2 . THR B 107 ? 0.48107 0.76310 0.82490 0.09685  0.09157  0.12061  74  THR D CG2 
2220 N N   . VAL B 108 ? 0.54627 0.67814 0.41895 -0.01172 0.02053  0.16817  75  VAL D N   
2221 C CA  . VAL B 108 ? 0.65477 0.78066 0.50475 -0.02281 0.01566  0.17015  75  VAL D CA  
2222 C C   . VAL B 108 ? 0.57906 0.72820 0.51820 -0.03343 0.03296  0.17152  75  VAL D C   
2223 O O   . VAL B 108 ? 0.51428 0.67513 0.49558 -0.03322 0.01900  0.14759  75  VAL D O   
2224 C CB  . VAL B 108 ? 0.68624 0.75371 0.47776 -0.02644 0.02347  0.16135  75  VAL D CB  
2225 C CG1 . VAL B 108 ? 0.69124 0.74713 0.47009 -0.02996 0.01627  0.14826  75  VAL D CG1 
2226 C CG2 . VAL B 108 ? 0.60822 0.61935 0.34076 -0.01420 0.01411  0.14016  75  VAL D CG2 
2227 N N   . CYS B 109 ? 0.58091 0.73284 0.54504 -0.04324 0.06359  0.19962  76  CYS D N   
2228 C CA  . CYS B 109 ? 0.48226 0.64681 0.52026 -0.05400 0.08200  0.20594  76  CYS D CA  
2229 C C   . CYS B 109 ? 0.59411 0.78218 0.72674 -0.05118 0.07722  0.17587  76  CYS D C   
2230 O O   . CYS B 109 ? 0.55720 0.75280 0.73402 -0.05414 0.06943  0.15796  76  CYS D O   
2231 C CB  . CYS B 109 ? 0.54087 0.68210 0.57565 -0.05831 0.10361  0.21770  76  CYS D CB  
2232 S SG  . CYS B 109 ? 0.72850 0.81064 0.67261 -0.05408 0.09044  0.19421  76  CYS D SG  
2233 N N   . ARG B 110 ? 0.67622 0.87780 0.84250 -0.04596 0.08241  0.16826  77  ARG D N   
2234 C CA  . ARG B 110 ? 0.43229 0.66214 0.69388 -0.04544 0.07969  0.13860  77  ARG D CA  
2235 C C   . ARG B 110 ? 0.43810 0.67793 0.70274 -0.03339 0.04229  0.10053  77  ARG D C   
2236 O O   . ARG B 110 ? 0.49828 0.75693 0.83405 -0.03729 0.03575  0.07499  77  ARG D O   
2237 C CB  . ARG B 110 ? 0.42571 0.67255 0.72149 -0.04208 0.09441  0.13772  77  ARG D CB  
2238 C CG  . ARG B 110 ? 0.60444 0.88568 1.00773 -0.04651 0.09910  0.10967  77  ARG D CG  
2239 C CD  . ARG B 110 ? 0.69467 0.99773 1.13045 -0.04183 0.11309  0.10540  77  ARG D CD  
2240 N NE  . ARG B 110 ? 0.71647 1.00060 1.11712 -0.05138 0.14702  0.14288  77  ARG D NE  
2241 C CZ  . ARG B 110 ? 0.65035 0.93283 1.09344 -0.07149 0.18263  0.16211  77  ARG D CZ  
2242 N NH1 . ARG B 110 ? 0.54463 0.84094 1.06785 -0.08516 0.19108  0.14825  77  ARG D NH1 
2243 N NH2 . ARG B 110 ? 0.77665 1.03430 1.16822 -0.07761 0.20616  0.19176  77  ARG D NH2 
2244 N N   . HIS B 111 ? 0.38793 0.61220 0.57226 -0.01982 0.01749  0.09617  78  HIS D N   
2245 C CA  . HIS B 111 ? 0.39788 0.62659 0.57400 -0.00777 -0.01985 0.06128  78  HIS D CA  
2246 C C   . HIS B 111 ? 0.51931 0.74128 0.69280 -0.01691 -0.02809 0.05229  78  HIS D C   
2247 O O   . HIS B 111 ? 0.45271 0.69078 0.67518 -0.01572 -0.04612 0.02064  78  HIS D O   
2248 C CB  . HIS B 111 ? 0.42242 0.62673 0.50228 0.00790  -0.04240 0.06244  78  HIS D CB  
2249 C CG  . HIS B 111 ? 0.44348 0.64130 0.49165 0.01892  -0.08139 0.03191  78  HIS D CG  
2250 N ND1 . HIS B 111 ? 0.60556 0.78048 0.59104 0.01211  -0.09251 0.03157  78  HIS D ND1 
2251 C CD2 . HIS B 111 ? 0.50659 0.71794 0.57522 0.03616  -0.11224 0.00025  78  HIS D CD2 
2252 C CE1 . HIS B 111 ? 0.58365 0.75449 0.54804 0.02324  -0.12743 0.00182  78  HIS D CE1 
2253 N NE2 . HIS B 111 ? 0.50501 0.69731 0.51842 0.03884  -0.14158 -0.01710 78  HIS D NE2 
2254 N N   . ASN B 112 ? 0.49610 0.69630 0.61410 -0.02610 -0.01502 0.07833  79  ASN D N   
2255 C CA  . ASN B 112 ? 0.46896 0.66361 0.58029 -0.03314 -0.02209 0.06884  79  ASN D CA  
2256 C C   . ASN B 112 ? 0.51814 0.72961 0.72531 -0.04268 -0.00764 0.05986  79  ASN D C   
2257 O O   . ASN B 112 ? 0.54781 0.76452 0.78145 -0.04396 -0.02261 0.03243  79  ASN D O   
2258 C CB  . ASN B 112 ? 0.56927 0.74308 0.60612 -0.04040 -0.00978 0.09846  79  ASN D CB  
2259 C CG  . ASN B 112 ? 0.60026 0.75222 0.53395 -0.03482 -0.02973 0.09744  79  ASN D CG  
2260 O OD1 . ASN B 112 ? 0.64941 0.79700 0.56150 -0.02594 -0.05762 0.07020  79  ASN D OD1 
2261 N ND2 . ASN B 112 ? 0.55171 0.68769 0.41822 -0.04093 -0.01590 0.12709  79  ASN D ND2 
2262 N N   . TYR B 113 ? 0.48607 0.70250 0.74261 -0.05053 0.02208  0.08224  80  TYR D N   
2263 C CA  . TYR B 113 ? 0.40996 0.63476 0.75285 -0.06127 0.03836  0.07612  80  TYR D CA  
2264 C C   . TYR B 113 ? 0.49876 0.74803 0.91499 -0.06006 0.02326  0.03695  80  TYR D C   
2265 O O   . TYR B 113 ? 0.53773 0.79080 0.99528 -0.06475 0.01513  0.01269  80  TYR D O   
2266 C CB  . TYR B 113 ? 0.46652 0.68623 0.83773 -0.07099 0.07375  0.10991  80  TYR D CB  
2267 C CG  . TYR B 113 ? 0.55266 0.76852 0.99695 -0.08334 0.09386  0.11129  80  TYR D CG  
2268 C CD1 . TYR B 113 ? 0.62620 0.85831 1.15656 -0.09144 0.10136  0.09010  80  TYR D CD1 
2269 C CD2 . TYR B 113 ? 0.48086 0.67608 0.90797 -0.08680 0.10536  0.13311  80  TYR D CD2 
2270 C CE1 . TYR B 113 ? 0.46780 0.68958 1.06026 -0.10439 0.12093  0.09148  80  TYR D CE1 
2271 C CE2 . TYR B 113 ? 0.55388 0.73864 1.04365 -0.09614 0.12318  0.13520  80  TYR D CE2 
2272 C CZ  . TYR B 113 ? 0.67182 0.86681 1.24171 -0.10579 0.13154  0.11483  80  TYR D CZ  
2273 O OH  . TYR B 113 ? 0.72742 0.90557 1.35541 -0.11678 0.15044  0.11693  80  TYR D OH  
2274 N N   . GLU B 114 ? 0.38106 0.64884 0.81543 -0.05355 0.01901  0.02871  81  GLU D N   
2275 C CA  . GLU B 114 ? 0.38807 0.68641 0.89711 -0.05197 0.00399  -0.00938 81  GLU D CA  
2276 C C   . GLU B 114 ? 0.48527 0.78828 0.96364 -0.03905 -0.03732 -0.04325 81  GLU D C   
2277 O O   . GLU B 114 ? 0.40837 0.73844 0.94664 -0.03718 -0.05489 -0.07813 81  GLU D O   
2278 C CB  . GLU B 114 ? 0.36286 0.68413 0.90436 -0.04749 0.01344  -0.00813 81  GLU D CB  
2279 C CG  . GLU B 114 ? 0.35636 0.67391 0.93188 -0.06258 0.05565  0.02236  81  GLU D CG  
2280 C CD  . GLU B 114 ? 0.68920 1.03045 1.29225 -0.05826 0.06672  0.02192  81  GLU D CD  
2281 O OE1 . GLU B 114 ? 0.83472 1.19566 1.43081 -0.04066 0.03981  -0.00164 81  GLU D OE1 
2282 O OE2 . GLU B 114 ? 0.71286 1.05200 1.34316 -0.07185 0.10236  0.04479  81  GLU D OE2 
2283 N N   . GLY B 115 ? 0.44847 0.72594 0.83442 -0.03152 -0.05312 -0.03468 82  GLY D N   
2284 C CA  . GLY B 115 ? 0.44650 0.72159 0.78940 -0.01974 -0.09178 -0.06384 82  GLY D CA  
2285 C C   . GLY B 115 ? 0.52779 0.78566 0.83973 -0.02673 -0.10034 -0.07369 82  GLY D C   
2286 O O   . GLY B 115 ? 0.52257 0.79159 0.89389 -0.03492 -0.10257 -0.09760 82  GLY D O   
2287 N N   . PRO B 116 ? 0.61840 0.84880 0.83580 -0.02471 -0.10413 -0.05684 83  PRO D N   
2288 C CA  . PRO B 116 ? 0.52254 0.73881 0.70495 -0.03095 -0.11313 -0.06983 83  PRO D CA  
2289 C C   . PRO B 116 ? 0.53225 0.75052 0.76753 -0.04414 -0.08661 -0.06178 83  PRO D C   
2290 O O   . PRO B 116 ? 0.55977 0.77857 0.81559 -0.04913 -0.09440 -0.08670 83  PRO D O   
2291 C CB  . PRO B 116 ? 0.54587 0.73464 0.61676 -0.02818 -0.11718 -0.04940 83  PRO D CB  
2292 C CG  . PRO B 116 ? 0.62438 0.81128 0.68503 -0.02519 -0.09777 -0.01598 83  PRO D CG  
2293 C CD  . PRO B 116 ? 0.50821 0.71949 0.64511 -0.01782 -0.10069 -0.02853 83  PRO D CD  
2294 N N   . GLU B 117 ? 0.50812 0.72480 0.76346 -0.04923 -0.05589 -0.02783 84  GLU D N   
2295 C CA  . GLU B 117 ? 0.48085 0.69421 0.78230 -0.05903 -0.03185 -0.01763 84  GLU D CA  
2296 C C   . GLU B 117 ? 0.43343 0.65989 0.83090 -0.06544 -0.02938 -0.04368 84  GLU D C   
2297 O O   . GLU B 117 ? 0.65463 0.87373 1.08574 -0.07196 -0.01835 -0.04823 84  GLU D O   
2298 C CB  . GLU B 117 ? 0.39106 0.59758 0.69126 -0.06243 -0.00153 0.02535  84  GLU D CB  
2299 C CG  . GLU B 117 ? 0.55387 0.74784 0.76098 -0.05900 -0.00088 0.05276  84  GLU D CG  
2300 C CD  . GLU B 117 ? 0.70454 0.88935 0.86274 -0.06129 -0.00224 0.05528  84  GLU D CD  
2301 O OE1 . GLU B 117 ? 0.66956 0.85646 0.86449 -0.06362 -0.00405 0.03519  84  GLU D OE1 
2302 O OE2 . GLU B 117 ? 0.70647 0.88296 0.78989 -0.06147 -0.00054 0.07614  84  GLU D OE2 
2303 N N   . THR B 118 ? 0.46590 0.71203 0.90912 -0.06375 -0.03923 -0.06213 85  THR D N   
2304 C CA  . THR B 118 ? 0.50636 0.76786 1.04052 -0.07249 -0.03858 -0.09126 85  THR D CA  
2305 C C   . THR B 118 ? 0.60635 0.86702 1.13575 -0.07277 -0.06364 -0.12916 85  THR D C   
2306 O O   . THR B 118 ? 0.64253 0.90543 1.23647 -0.08288 -0.05804 -0.15009 85  THR D O   
2307 C CB  . THR B 118 ? 0.39316 0.68302 0.97680 -0.07037 -0.04511 -0.10494 85  THR D CB  
2308 O OG1 . THR B 118 ? 0.52657 0.81552 1.10222 -0.06946 -0.02194 -0.07010 85  THR D OG1 
2309 C CG2 . THR B 118 ? 0.72929 1.03682 1.41434 -0.08426 -0.03700 -0.13096 85  THR D CG2 
2310 N N   . HIS B 119 ? 0.68194 0.93587 1.13212 -0.06320 -0.09012 -0.13856 86  HIS D N   
2311 C CA  . HIS B 119 ? 0.66048 0.91058 1.09382 -0.06426 -0.11388 -0.17401 86  HIS D CA  
2312 C C   . HIS B 119 ? 0.70260 0.93106 1.09315 -0.06827 -0.10270 -0.16581 86  HIS D C   
2313 O O   . HIS B 119 ? 0.65196 0.87651 1.04573 -0.07254 -0.11349 -0.19545 86  HIS D O   
2314 C CB  . HIS B 119 ? 0.66867 0.91982 1.03538 -0.05248 -0.15057 -0.19185 86  HIS D CB  
2315 C CG  . HIS B 119 ? 0.69157 0.96818 1.10047 -0.04461 -0.16708 -0.20537 86  HIS D CG  
2316 N ND1 . HIS B 119 ? 0.65481 0.93859 1.06281 -0.03697 -0.15708 -0.17983 86  HIS D ND1 
2317 C CD2 . HIS B 119 ? 0.52230 0.82178 0.97719 -0.04271 -0.19330 -0.24343 86  HIS D CD2 
2318 C CE1 . HIS B 119 ? 0.66347 0.97505 1.11802 -0.02958 -0.17567 -0.20206 86  HIS D CE1 
2319 N NE2 . HIS B 119 ? 0.85260 1.17559 1.33709 -0.03283 -0.19884 -0.24064 86  HIS D NE2 
2320 N N   . THR B 120 ? 0.54961 0.76623 0.90188 -0.06709 -0.08144 -0.12806 87  THR D N   
2321 C CA  . THR B 120 ? 0.58395 0.78615 0.89163 -0.06914 -0.07267 -0.12082 87  THR D CA  
2322 C C   . THR B 120 ? 0.65845 0.85530 1.01519 -0.07287 -0.04095 -0.09646 87  THR D C   
2323 O O   . THR B 120 ? 0.60705 0.80043 1.01897 -0.07726 -0.03361 -0.11376 87  THR D O   
2324 C CB  . THR B 120 ? 0.48090 0.67375 0.68947 -0.06473 -0.07828 -0.09991 87  THR D CB  
2325 O OG1 . THR B 120 ? 0.50117 0.69515 0.70568 -0.06177 -0.06363 -0.06412 87  THR D OG1 
2326 C CG2 . THR B 120 ? 0.47370 0.66234 0.62222 -0.06044 -0.11122 -0.12523 87  THR D CG2 
2327 N N   . SER B 121 ? 0.56523 0.75851 0.89938 -0.07071 -0.02277 -0.05637 88  SER D N   
2328 C CA  . SER B 121 ? 0.47870 0.66343 0.84226 -0.07180 0.00431  -0.02963 88  SER D CA  
2329 C C   . SER B 121 ? 0.49811 0.67889 0.95318 -0.07726 0.02041  -0.03164 88  SER D C   
2330 O O   . SER B 121 ? 0.58878 0.75797 1.08504 -0.07861 0.03254  -0.03603 88  SER D O   
2331 C CB  . SER B 121 ? 0.48116 0.66357 0.79728 -0.06925 0.01778  0.01329  88  SER D CB  
2332 O OG  . SER B 121 ? 0.70178 0.88566 0.93098 -0.06709 0.00404  0.01444  88  SER D OG  
2333 N N   . LEU B 122 ? 0.40363 0.59285 0.89139 -0.08084 0.02179  -0.02938 89  LEU D N   
2334 C CA  . LEU B 122 ? 0.43921 0.62471 1.01194 -0.08988 0.03996  -0.03073 89  LEU D CA  
2335 C C   . LEU B 122 ? 0.42630 0.61325 1.05508 -0.09622 0.03009  -0.07310 89  LEU D C   
2336 O O   . LEU B 122 ? 0.48828 0.66810 1.18842 -0.10632 0.04642  -0.07746 89  LEU D O   
2337 C CB  . LEU B 122 ? 0.39976 0.60015 0.99349 -0.09334 0.04372  -0.02270 89  LEU D CB  
2338 C CG  . LEU B 122 ? 0.43822 0.63511 0.98110 -0.08906 0.05661  0.01898  89  LEU D CG  
2339 C CD1 . LEU B 122 ? 0.53744 0.75111 1.10680 -0.09208 0.06075  0.02082  89  LEU D CD1 
2340 C CD2 . LEU B 122 ? 0.45198 0.62601 1.00007 -0.09177 0.08454  0.05561  89  LEU D CD2 
2341 N N   . ARG B 123 ? 0.55421 0.74767 1.14963 -0.09234 0.00481  -0.10459 90  ARG D N   
2342 C CA  . ARG B 123 ? 0.62877 0.82300 1.26983 -0.09889 -0.00624 -0.14696 90  ARG D CA  
2343 C C   . ARG B 123 ? 0.55357 0.73024 1.18057 -0.09657 -0.00277 -0.15688 90  ARG D C   
2344 O O   . ARG B 123 ? 0.60107 0.76997 1.27779 -0.10335 -0.00186 -0.18577 90  ARG D O   
2345 C CB  . ARG B 123 ? 0.59863 0.81380 1.21704 -0.09707 -0.04017 -0.18154 90  ARG D CB  
2346 C CG  . ARG B 123 ? 0.85309 1.07332 1.52043 -0.10553 -0.05471 -0.22809 90  ARG D CG  
2347 C CD  . ARG B 123 ? 0.92878 1.17434 1.59113 -0.10355 -0.08730 -0.25743 90  ARG D CD  
2348 N NE  . ARG B 123 ? 1.22947 1.49636 1.94304 -0.10584 -0.08153 -0.24866 90  ARG D NE  
2349 C CZ  . ARG B 123 ? 1.35941 1.63938 2.16042 -0.11895 -0.07268 -0.26665 90  ARG D CZ  
2350 N NH1 . ARG B 123 ? 1.21534 1.48593 2.06225 -0.13098 -0.06923 -0.29403 90  ARG D NH1 
2351 N NH2 . ARG B 123 ? 1.35509 1.65788 2.19849 -0.12125 -0.06570 -0.25827 90  ARG D NH2 
2352 N N   . ARG B 124 ? 0.58391 0.75537 1.14711 -0.08780 0.00032  -0.13509 91  ARG D N   
2353 C CA  . ARG B 124 ? 0.62948 0.78978 1.17982 -0.08421 0.00428  -0.14603 91  ARG D CA  
2354 C C   . ARG B 124 ? 0.60760 0.74674 1.22416 -0.08485 0.02926  -0.13674 91  ARG D C   
2355 O O   . ARG B 124 ? 0.65584 0.78500 1.28746 -0.08255 0.04923  -0.09943 91  ARG D O   
2356 C CB  . ARG B 124 ? 0.57293 0.73718 1.04645 -0.07604 0.00524  -0.12176 91  ARG D CB  
2357 C CG  . ARG B 124 ? 0.64627 0.80411 1.11350 -0.07079 0.01421  -0.12834 91  ARG D CG  
2358 C CD  . ARG B 124 ? 0.52998 0.69829 0.92242 -0.06543 0.01462  -0.10759 91  ARG D CD  
2359 N NE  . ARG B 124 ? 0.46517 0.63368 0.85855 -0.05933 0.02449  -0.11480 91  ARG D NE  
2360 C CZ  . ARG B 124 ? 0.48206 0.65476 0.85389 -0.06164 0.01558  -0.15077 91  ARG D CZ  
2361 N NH1 . ARG B 124 ? 0.49393 0.66765 0.83736 -0.07021 -0.00510 -0.18223 91  ARG D NH1 
2362 N NH2 . ARG B 124 ? 0.54405 0.72012 0.92230 -0.05456 0.02743  -0.15588 91  ARG D NH2 
2363 N N   . LEU B 125 ? 0.66070 0.78927 1.31301 -0.08802 0.02798  -0.17080 92  LEU D N   
2364 C CA  . LEU B 125 ? 0.61562 0.71705 1.32647 -0.08730 0.05038  -0.16637 92  LEU D CA  
2365 C C   . LEU B 125 ? 0.70596 0.80018 1.40653 -0.08081 0.04840  -0.19284 92  LEU D C   
2366 O O   . LEU B 125 ? 0.68941 0.79091 1.38282 -0.08683 0.03147  -0.23388 92  LEU D O   
2367 C CB  . LEU B 125 ? 0.53932 0.62980 1.32432 -0.10187 0.05556  -0.18502 92  LEU D CB  
2368 C CG  . LEU B 125 ? 0.52661 0.62067 1.33890 -0.10990 0.06610  -0.15829 92  LEU D CG  
2369 C CD1 . LEU B 125 ? 0.54872 0.63268 1.43852 -0.12722 0.07373  -0.18183 92  LEU D CD1 
2370 C CD2 . LEU B 125 ? 0.60758 0.68287 1.40948 -0.10170 0.08958  -0.10815 92  LEU D CD2 
2371 N N   . GLU B 126 ? 0.85014 0.93106 1.54954 -0.06797 0.06522  -0.17024 93  GLU D N   
2372 C CA  . GLU B 126 ? 0.70409 0.77923 1.40051 -0.05920 0.06743  -0.19351 93  GLU D CA  
2373 C C   . GLU B 126 ? 0.81737 0.85697 1.57596 -0.05240 0.08889  -0.18598 93  GLU D C   
2374 O O   . GLU B 126 ? 0.85516 0.88075 1.62411 -0.04380 0.10408  -0.14531 93  GLU D O   
2375 C CB  . GLU B 126 ? 0.79909 0.89599 1.43257 -0.04726 0.06588  -0.17663 93  GLU D CB  
2376 C CG  . GLU B 126 ? 0.81617 0.94055 1.37914 -0.05473 0.04535  -0.18620 93  GLU D CG  
2377 C CD  . GLU B 126 ? 0.96494 1.09294 1.51437 -0.06360 0.02873  -0.23627 93  GLU D CD  
2378 O OE1 . GLU B 126 ? 1.08728 1.20421 1.66526 -0.06093 0.03531  -0.26361 93  GLU D OE1 
2379 O OE2 . GLU B 126 ? 1.07889 1.21881 1.58716 -0.07252 0.00860  -0.24851 93  GLU D OE2 
2380 N N   . GLN B 127 ? 0.85916 0.88069 1.65532 -0.05634 0.08977  -0.22498 94  GLN D N   
2381 C CA  . GLN B 127 ? 0.83280 0.81274 1.68765 -0.05080 0.10984  -0.22171 94  GLN D CA  
2382 C C   . GLN B 127 ? 0.91012 0.88403 1.75416 -0.02698 0.12040  -0.20659 94  GLN D C   
2383 O O   . GLN B 127 ? 0.90104 0.90144 1.70676 -0.01940 0.11222  -0.22385 94  GLN D O   
2384 C CB  . GLN B 127 ? 0.99580 0.95720 1.89186 -0.06340 0.10741  -0.27088 94  GLN D CB  
2385 C CG  . GLN B 127 ? 0.97292 0.94255 1.89067 -0.08674 0.09657  -0.28870 94  GLN D CG  
2386 C CD  . GLN B 127 ? 0.87995 0.83640 1.83305 -0.10058 0.09114  -0.34082 94  GLN D CD  
2387 O OE1 . GLN B 127 ? 0.75237 0.69393 1.70683 -0.09292 0.09480  -0.36602 94  GLN D OE1 
2388 N NE2 . GLN B 127 ? 0.99453 0.95840 1.97772 -0.12129 0.08247  -0.35889 94  GLN D NE2 
2389 N N   . PRO B 128 ? 0.83145 0.77124 1.70781 -0.01491 0.13833  -0.17504 95  PRO D N   
2390 C CA  . PRO B 128 ? 0.78482 0.72210 1.65361 0.01122  0.14617  -0.15769 95  PRO D CA  
2391 C C   . PRO B 128 ? 0.84659 0.76240 1.74737 0.02185  0.15197  -0.19527 95  PRO D C   
2392 O O   . PRO B 128 ? 0.92228 0.80875 1.86102 0.00954  0.15526  -0.22655 95  PRO D O   
2393 C CB  . PRO B 128 ? 0.71962 0.62170 1.60963 0.01939  0.16133  -0.10857 95  PRO D CB  
2394 C CG  . PRO B 128 ? 0.85153 0.74518 1.75293 -0.00522 0.16256  -0.09914 95  PRO D CG  
2395 C CD  . PRO B 128 ? 0.88133 0.78571 1.79653 -0.02468 0.15173  -0.14923 95  PRO D CD  
2396 N N   A ASN B 129 ? 0.85513 0.78818 1.74061 0.04479  0.15357  -0.19323 96  ASN D N   
2397 N N   B ASN B 129 ? 0.85512 0.78777 1.74098 0.04489  0.15370  -0.19306 96  ASN D N   
2398 C CA  A ASN B 129 ? 0.78320 0.69814 1.69871 0.06104  0.16135  -0.22474 96  ASN D CA  
2399 C CA  B ASN B 129 ? 0.78358 0.69802 1.69957 0.06080  0.16140  -0.22510 96  ASN D CA  
2400 C C   A ASN B 129 ? 0.90579 0.78966 1.84910 0.08962  0.17439  -0.19022 96  ASN D C   
2401 C C   B ASN B 129 ? 0.90575 0.79017 1.84892 0.08979  0.17432  -0.19104 96  ASN D C   
2402 O O   A ASN B 129 ? 0.89883 0.80585 1.81767 0.10428  0.17252  -0.15220 96  ASN D O   
2403 O O   B ASN B 129 ? 0.89907 0.80798 1.81735 0.10484  0.17229  -0.15418 96  ASN D O   
2404 C CB  A ASN B 129 ? 0.76544 0.72872 1.64381 0.06572  0.15340  -0.25594 96  ASN D CB  
2405 C CB  B ASN B 129 ? 0.76612 0.72847 1.64516 0.06465  0.15323  -0.25764 96  ASN D CB  
2406 C CG  A ASN B 129 ? 0.75310 0.73568 1.60404 0.03948  0.14018  -0.29696 96  ASN D CG  
2407 C CG  B ASN B 129 ? 0.92590 0.87060 1.83583 0.07354  0.16077  -0.30366 96  ASN D CG  
2408 O OD1 A ASN B 129 ? 0.77515 0.72962 1.65404 0.02336  0.13923  -0.32223 96  ASN D OD1 
2409 O OD1 B ASN B 129 ? 0.85280 0.75409 1.80231 0.06528  0.16647  -0.32574 96  ASN D OD1 
2410 N ND2 A ASN B 129 ? 0.72185 0.75136 1.51567 0.03441  0.12934  -0.30403 96  ASN D ND2 
2411 N ND2 B ASN B 129 ? 0.86186 0.84080 1.75431 0.08929  0.16208  -0.31988 96  ASN D ND2 
2412 N N   . VAL B 130 ? 0.96938 0.79899 1.96134 0.09771  0.18665  -0.20356 97  VAL D N   
2413 C CA  . VAL B 130 ? 0.91467 0.70160 1.93413 0.12575  0.19833  -0.17093 97  VAL D CA  
2414 C C   . VAL B 130 ? 0.94505 0.72358 1.98998 0.15196  0.20385  -0.20284 97  VAL D C   
2415 O O   . VAL B 130 ? 1.16764 0.92707 2.23500 0.14275  0.20784  -0.24871 97  VAL D O   
2416 C CB  . VAL B 130 ? 1.00514 0.72306 2.05842 0.11355  0.21065  -0.15282 97  VAL D CB  
2417 C CG1 . VAL B 130 ? 1.08660 0.75535 2.15756 0.14325  0.22108  -0.11339 97  VAL D CG1 
2418 C CG2 . VAL B 130 ? 0.91235 0.64408 1.94469 0.08517  0.20666  -0.12857 97  VAL D CG2 
2419 N N   . VAL B 131 ? 1.05778 0.85247 2.10010 0.18485  0.20379  -0.18001 98  VAL D N   
2420 C CA  . VAL B 131 ? 1.12563 0.91020 2.19866 0.21624  0.21027  -0.20440 98  VAL D CA  
2421 C C   . VAL B 131 ? 1.07915 0.82224 2.17288 0.24980  0.21502  -0.15981 98  VAL D C   
2422 O O   . VAL B 131 ? 1.17541 0.92331 2.24707 0.25164  0.21021  -0.11080 98  VAL D O   
2423 C CB  . VAL B 131 ? 1.17170 1.03121 2.22173 0.22618  0.20365  -0.23060 98  VAL D CB  
2424 C CG1 . VAL B 131 ? 1.29364 1.18037 2.32240 0.19492  0.19999  -0.27966 98  VAL D CG1 
2425 C CG2 . VAL B 131 ? 1.26056 1.17458 2.27136 0.23140  0.19346  -0.18949 98  VAL D CG2 
2426 N N   . ILE B 132 ? 1.23329 0.93278 2.36698 0.27719  0.22403  -0.17692 99  ILE D N   
2427 C CA  . ILE B 132 ? 1.33370 0.97570 2.47605 0.30179  0.22662  -0.13400 99  ILE D CA  
2428 C C   . ILE B 132 ? 1.28656 0.94658 2.43457 0.34407  0.22170  -0.13492 99  ILE D C   
2429 O O   . ILE B 132 ? 1.34777 0.95607 2.49754 0.36658  0.22166  -0.10969 99  ILE D O   
2430 C CB  . ILE B 132 ? 1.27128 0.83172 2.42522 0.28184  0.23707  -0.13845 99  ILE D CB  
2431 C CG1 . ILE B 132 ? 1.26327 0.76804 2.40340 0.28898  0.23862  -0.08105 99  ILE D CG1 
2432 C CG2 . ILE B 132 ? 1.34677 0.88358 2.52001 0.29194  0.24244  -0.18281 99  ILE D CG2 
2433 C CD1 . ILE B 132 ? 1.41325 0.94922 2.53000 0.28265  0.23282  -0.03715 99  ILE D CD1 
2434 N N   . SER B 133 ? 1.31972 1.05446 2.46805 0.35495  0.21722  -0.16357 100 SER D N   
2435 C CA  . SER B 133 ? 1.39969 1.16409 2.55567 0.39434  0.21225  -0.16748 100 SER D CA  
2436 C C   . SER B 133 ? 1.39438 1.15011 2.53940 0.42309  0.20201  -0.10992 100 SER D C   
2437 O O   . SER B 133 ? 1.43512 1.19912 2.56026 0.41240  0.19711  -0.06956 100 SER D O   
2438 C CB  . SER B 133 ? 1.34696 1.20422 2.49851 0.39448  0.20980  -0.20186 100 SER D CB  
2439 O OG  . SER B 133 ? 1.39435 1.30551 2.52290 0.38446  0.20235  -0.17392 100 SER D OG  
2440 N N   . LEU B 134 ? 1.26008 0.99842 2.41561 0.46040  0.19807  -0.10696 101 LEU D N   
2441 C CA  . LEU B 134 ? 1.41638 1.13583 2.55907 0.49115  0.18616  -0.05576 101 LEU D CA  
2442 C C   . LEU B 134 ? 1.47016 1.25859 2.62123 0.53029  0.17480  -0.06269 101 LEU D C   
2443 O O   . LEU B 134 ? 1.31690 1.14001 2.48863 0.54077  0.17957  -0.10847 101 LEU D O   
2444 C CB  . LEU B 134 ? 1.49673 1.11702 2.63992 0.50270  0.18975  -0.04016 101 LEU D CB  
2445 N N   . SER B 135 ? 1.48354 1.29285 2.61688 0.55034  0.15984  -0.01736 102 SER D N   
2446 C CA  . SER B 135 ? 1.60991 1.48563 2.74998 0.58893  0.14578  -0.01638 102 SER D CA  
2447 C C   . SER B 135 ? 1.75922 1.62672 2.87160 0.60446  0.12835  0.04255  102 SER D C   
2448 O O   . SER B 135 ? 1.84876 1.70191 2.93425 0.57702  0.12858  0.07686  102 SER D O   
2449 C CB  . SER B 135 ? 1.54278 1.52438 2.68970 0.57704  0.14764  -0.04943 102 SER D CB  
2450 O OG  . SER B 135 ? 1.36253 1.37181 2.48606 0.54247  0.14816  -0.03001 102 SER D OG  
2451 N N   . ARG B 136 ? 1.60942 1.48599 2.72651 0.64859  0.11288  0.05310  103 ARG D N   
2452 C CA  . ARG B 136 ? 1.64847 1.50919 2.73592 0.66681  0.09339  0.10677  103 ARG D CA  
2453 C C   . ARG B 136 ? 1.86979 1.81037 2.96885 0.70712  0.07379  0.10316  103 ARG D C   
2454 O O   . ARG B 136 ? 1.98227 1.97891 3.11400 0.72517  0.07740  0.05991  103 ARG D O   
2455 C CB  . ARG B 136 ? 1.97349 1.72164 3.04529 0.68043  0.09187  0.13303  103 ARG D CB  
2456 N N   . THR B 137 ? 1.96635 1.91309 3.03684 0.71953  0.05320  0.14823  104 THR D N   
2457 C CA  . THR B 137 ? 1.83887 1.85898 2.91881 0.75794  0.03033  0.14877  104 THR D CA  
2458 C C   . THR B 137 ? 1.57478 1.53003 2.63406 0.79446  0.00807  0.18581  104 THR D C   
2459 O O   . THR B 137 ? 1.58120 1.57907 2.62849 0.81440  -0.01637 0.20828  104 THR D O   
2460 C CB  . THR B 137 ? 1.84740 1.95908 2.91075 0.73661  0.02157  0.16377  104 THR D CB  
2461 O OG1 . THR B 137 ? 1.84334 1.90620 2.85904 0.71071  0.01802  0.21544  104 THR D OG1 
2462 C CG2 . THR B 137 ? 1.48284 1.66239 2.56307 0.70290  0.04185  0.12479  104 THR D CG2 
2463 N N   . THR B 145 ? 1.75431 1.47254 2.75131 0.55782  0.11631  0.20438  112 THR D N   
2464 C CA  . THR B 145 ? 1.78430 1.42542 2.80126 0.56212  0.12781  0.18078  112 THR D CA  
2465 C C   . THR B 145 ? 1.97806 1.57836 2.99903 0.51660  0.14890  0.16715  112 THR D C   
2466 O O   . THR B 145 ? 2.09153 1.66338 3.08413 0.48799  0.15368  0.20018  112 THR D O   
2467 C CB  . THR B 145 ? 2.01071 1.56806 3.00227 0.58560  0.11899  0.21644  112 THR D CB  
2468 O OG1 . THR B 145 ? 2.03888 1.63606 3.02109 0.62628  0.09548  0.23493  112 THR D OG1 
2469 C CG2 . THR B 145 ? 1.92719 1.41394 2.94124 0.59810  0.12873  0.18733  112 THR D CG2 
2470 N N   . LEU B 146 ? 1.80114 1.40191 2.85643 0.50956  0.16100  0.11660  113 LEU D N   
2471 C CA  . LEU B 146 ? 1.72177 1.28095 2.78656 0.46908  0.17938  0.09496  113 LEU D CA  
2472 C C   . LEU B 146 ? 1.62038 1.20574 2.66675 0.43138  0.18334  0.11440  113 LEU D C   
2473 O O   . LEU B 146 ? 1.67687 1.21226 2.70013 0.40875  0.18900  0.14749  113 LEU D O   
2474 C CB  . LEU B 146 ? 1.45883 0.91540 2.51621 0.46639  0.18745  0.10799  113 LEU D CB  
2475 C CG  . LEU B 146 ? 1.46924 0.87714 2.54100 0.42709  0.20633  0.08068  113 LEU D CG  
2476 C CD1 . LEU B 146 ? 1.51854 0.96904 2.62468 0.42080  0.21204  0.02084  113 LEU D CD1 
2477 C CD2 . LEU B 146 ? 1.73363 1.04467 2.79822 0.43210  0.21311  0.09015  113 LEU D CD2 
2478 N N   . VAL B 147 ? 1.37133 1.03793 2.42630 0.42491  0.18080  0.09165  114 VAL D N   
2479 C CA  . VAL B 147 ? 1.51435 1.21526 2.55150 0.39395  0.18271  0.10689  114 VAL D CA  
2480 C C   . VAL B 147 ? 1.37420 1.07072 2.43130 0.35992  0.19554  0.06358  114 VAL D C   
2481 O O   . VAL B 147 ? 1.25303 0.95470 2.33608 0.36228  0.20001  0.01452  114 VAL D O   
2482 C CB  . VAL B 147 ? 1.37781 1.17254 2.40378 0.40679  0.17050  0.11312  114 VAL D CB  
2483 C CG1 . VAL B 147 ? 1.41802 1.21838 2.42332 0.43940  0.15522  0.15511  114 VAL D CG1 
2484 C CG2 . VAL B 147 ? 1.32752 1.18580 2.37358 0.41206  0.17021  0.05685  114 VAL D CG2 
2485 N N   . CYS B 148 ? 1.27109 0.96285 2.30075 0.32240  0.19845  0.08004  115 CYS D N   
2486 C CA  . CYS B 148 ? 1.14662 0.84267 2.17738 0.28286  0.20477  0.04226  115 CYS D CA  
2487 C C   . CYS B 148 ? 0.97118 0.74743 1.95947 0.25979  0.19422  0.03855  115 CYS D C   
2488 O O   . CYS B 148 ? 0.99138 0.78447 1.94470 0.25273  0.18910  0.07943  115 CYS D O   
2489 C CB  . CYS B 148 ? 1.29167 0.91495 2.32883 0.25694  0.21734  0.06046  115 CYS D CB  
2490 S SG  . CYS B 148 ? 1.43403 1.06200 2.47931 0.20896  0.22312  0.01420  115 CYS D SG  
2491 N N   . SER B 149 ? 1.02198 0.84370 2.00953 0.24790  0.19137  -0.01020 116 SER D N   
2492 C CA  . SER B 149 ? 0.90836 0.80259 1.85170 0.22735  0.18123  -0.01861 116 SER D CA  
2493 C C   . SER B 149 ? 0.91106 0.79851 1.84390 0.18837  0.18214  -0.04077 116 SER D C   
2494 O O   . SER B 149 ? 0.98270 0.85334 1.93951 0.17849  0.18621  -0.08435 116 SER D O   
2495 C CB  . SER B 149 ? 1.02971 0.98284 1.97166 0.24113  0.17681  -0.05681 116 SER D CB  
2496 O OG  . SER B 149 ? 1.35284 1.31775 2.31175 0.27937  0.17505  -0.03957 116 SER D OG  
2497 N N   . VAL B 150 ? 0.79969 0.70142 1.69713 0.16720  0.17767  -0.01192 117 VAL D N   
2498 C CA  . VAL B 150 ? 0.77500 0.67749 1.66091 0.13237  0.17586  -0.02894 117 VAL D CA  
2499 C C   . VAL B 150 ? 0.85076 0.81874 1.68241 0.11957  0.16299  -0.03298 117 VAL D C   
2500 O O   . VAL B 150 ? 0.74648 0.73623 1.54319 0.12015  0.15911  0.00511  117 VAL D O   
2501 C CB  . VAL B 150 ? 0.78828 0.64618 1.68162 0.11748  0.18377  0.00684  117 VAL D CB  
2502 C CG1 . VAL B 150 ? 0.76682 0.62848 1.65927 0.08384  0.18156  -0.01697 117 VAL D CG1 
2503 C CG2 . VAL B 150 ? 0.85386 0.64109 1.79249 0.13192  0.19777  0.01784  117 VAL D CG2 
2504 N N   . THR B 151 ? 0.85919 0.85496 1.67958 0.10714  0.15663  -0.07888 118 THR D N   
2505 C CA  . THR B 151 ? 0.76370 0.81725 1.52833 0.09702  0.14520  -0.08731 118 THR D CA  
2506 C C   . THR B 151 ? 0.68895 0.74854 1.43073 0.06771  0.13617  -0.11362 118 THR D C   
2507 O O   . THR B 151 ? 0.69827 0.72764 1.47267 0.05671  0.13779  -0.14041 118 THR D O   
2508 C CB  . THR B 151 ? 0.79201 0.88099 1.55227 0.11186  0.14496  -0.11866 118 THR D CB  
2509 O OG1 . THR B 151 ? 0.73487 0.80414 1.52481 0.10790  0.14833  -0.16701 118 THR D OG1 
2510 C CG2 . THR B 151 ? 0.68098 0.77050 1.46679 0.14439  0.15122  -0.09386 118 THR D CG2 
2511 N N   . ASP B 152 ? 0.90027 0.99892 1.58404 0.05558  0.12571  -0.10565 119 ASP D N   
2512 C CA  . ASP B 152 ? 0.86928 0.98005 1.51880 0.03138  0.11322  -0.13040 119 ASP D CA  
2513 C C   . ASP B 152 ? 0.83929 0.91882 1.51673 0.01645  0.11250  -0.12513 119 ASP D C   
2514 O O   . ASP B 152 ? 1.11991 1.17905 1.83036 0.00737  0.11136  -0.15892 119 ASP D O   
2515 C CB  . ASP B 152 ? 0.85607 0.97586 1.50253 0.02688  0.10907  -0.18360 119 ASP D CB  
2516 C CG  . ASP B 152 ? 1.01843 1.17579 1.63397 0.03757  0.11108  -0.19344 119 ASP D CG  
2517 O OD1 . ASP B 152 ? 0.88813 1.06775 1.48456 0.04795  0.11368  -0.15935 119 ASP D OD1 
2518 O OD2 . ASP B 152 ? 1.05204 1.21816 1.66244 0.03439  0.11061  -0.23649 119 ASP D OD2 
2519 N N   . PHE B 153 ? 0.63976 0.71752 1.30450 0.01256  0.11374  -0.08471 120 PHE D N   
2520 C CA  . PHE B 153 ? 0.59167 0.64690 1.28217 -0.00304 0.11458  -0.07916 120 PHE D CA  
2521 C C   . PHE B 153 ? 0.69488 0.76999 1.34030 -0.01151 0.10883  -0.04818 120 PHE D C   
2522 O O   . PHE B 153 ? 0.60549 0.70237 1.20622 -0.00394 0.10784  -0.02255 120 PHE D O   
2523 C CB  . PHE B 153 ? 0.60163 0.61166 1.35106 0.00305  0.13218  -0.05935 120 PHE D CB  
2524 C CG  . PHE B 153 ? 0.64965 0.65197 1.39049 0.01994  0.14237  -0.01097 120 PHE D CG  
2525 C CD1 . PHE B 153 ? 0.59037 0.58946 1.31474 0.01324  0.14677  0.02945  120 PHE D CD1 
2526 C CD2 . PHE B 153 ? 0.70236 0.70130 1.45193 0.04324  0.14706  -0.00687 120 PHE D CD2 
2527 C CE1 . PHE B 153 ? 0.59718 0.58789 1.30940 0.02808  0.15472  0.07399  120 PHE D CE1 
2528 C CE2 . PHE B 153 ? 0.62940 0.62257 1.37046 0.06027  0.15333  0.03756  120 PHE D CE2 
2529 C CZ  . PHE B 153 ? 0.61705 0.60498 1.33729 0.05198  0.15673  0.07853  120 PHE D CZ  
2530 N N   . TYR B 154 ? 0.73596 0.80449 1.39528 -0.02763 0.10530  -0.05248 121 TYR D N   
2531 C CA  . TYR B 154 ? 0.57513 0.65932 1.19775 -0.03568 0.10076  -0.02663 121 TYR D CA  
2532 C C   . TYR B 154 ? 0.59065 0.65804 1.25937 -0.04980 0.10576  -0.02783 121 TYR D C   
2533 O O   . TYR B 154 ? 0.79292 0.85497 1.49789 -0.05906 0.09991  -0.06484 121 TYR D O   
2534 C CB  . TYR B 154 ? 0.61440 0.73035 1.17468 -0.04128 0.08055  -0.04653 121 TYR D CB  
2535 C CG  . TYR B 154 ? 0.70184 0.83250 1.21354 -0.04570 0.07634  -0.01727 121 TYR D CG  
2536 C CD1 . TYR B 154 ? 0.58330 0.71533 1.10257 -0.05661 0.06959  -0.02132 121 TYR D CD1 
2537 C CD2 . TYR B 154 ? 0.61270 0.75723 1.07227 -0.03883 0.07917  0.01277  121 TYR D CD2 
2538 C CE1 . TYR B 154 ? 0.54954 0.69284 1.02458 -0.05910 0.06669  0.00405  121 TYR D CE1 
2539 C CE2 . TYR B 154 ? 0.61418 0.76861 1.02679 -0.04363 0.07630  0.03845  121 TYR D CE2 
2540 C CZ  . TYR B 154 ? 0.66022 0.81222 1.08012 -0.05305 0.07051  0.03410  121 TYR D CZ  
2541 O OH  . TYR B 154 ? 0.94522 1.10503 1.31855 -0.05633 0.06853  0.05832  121 TYR D OH  
2542 N N   . PRO B 155 ? 0.61409 0.67496 1.28288 -0.05333 0.11686  0.00954  122 PRO D N   
2543 C CA  . PRO B 155 ? 0.62210 0.68935 1.24562 -0.04527 0.12303  0.05394  122 PRO D CA  
2544 C C   . PRO B 155 ? 0.70952 0.75267 1.34806 -0.03073 0.13821  0.08215  122 PRO D C   
2545 O O   . PRO B 155 ? 0.60324 0.62348 1.28405 -0.02450 0.14388  0.06651  122 PRO D O   
2546 C CB  . PRO B 155 ? 0.52599 0.59066 1.15629 -0.05792 0.13035  0.07442  122 PRO D CB  
2547 C CG  . PRO B 155 ? 0.67498 0.71630 1.37602 -0.06923 0.13979  0.05464  122 PRO D CG  
2548 C CD  . PRO B 155 ? 0.56855 0.61640 1.28571 -0.06876 0.12492  0.00714  122 PRO D CD  
2549 N N   . ALA B 156 ? 0.75107 0.79734 1.35385 -0.02421 0.14420  0.12421  123 ALA D N   
2550 C CA  . ALA B 156 ? 0.67009 0.69672 1.28069 -0.00726 0.15449  0.15263  123 ALA D CA  
2551 C C   . ALA B 156 ? 0.92355 0.90196 1.58306 -0.00958 0.17330  0.17223  123 ALA D C   
2552 O O   . ALA B 156 ? 0.98802 0.93987 1.66272 0.00634  0.18090  0.19043  123 ALA D O   
2553 C CB  . ALA B 156 ? 0.50871 0.55650 1.06159 -0.00068 0.15266  0.19035  123 ALA D CB  
2554 N N   . LYS B 157 ? 0.76067 0.72661 1.44467 -0.02890 0.18109  0.16830  124 LYS D N   
2555 C CA  . LYS B 157 ? 0.80276 0.72078 1.53129 -0.03628 0.20173  0.18504  124 LYS D CA  
2556 C C   . LYS B 157 ? 0.84772 0.73518 1.62821 -0.03203 0.20487  0.15575  124 LYS D C   
2557 O O   . LYS B 157 ? 0.91591 0.81386 1.72446 -0.04259 0.19766  0.11327  124 LYS D O   
2558 C CB  . LYS B 157 ? 0.79581 0.71697 1.54090 -0.06027 0.20961  0.18158  124 LYS D CB  
2559 N N   . ILE B 158 ? 0.69732 0.54513 1.48905 -0.01584 0.21478  0.17801  125 ILE D N   
2560 C CA  . ILE B 158 ? 0.89239 0.70529 1.72950 -0.00813 0.21871  0.15264  125 ILE D CA  
2561 C C   . ILE B 158 ? 0.96122 0.71436 1.81025 0.00355  0.23552  0.19021  125 ILE D C   
2562 O O   . ILE B 158 ? 1.12290 0.87291 1.93655 0.01503  0.23732  0.23330  125 ILE D O   
2563 C CB  . ILE B 158 ? 0.70609 0.55046 1.53241 0.01129  0.20192  0.12343  125 ILE D CB  
2564 C CG1 . ILE B 158 ? 0.82252 0.63414 1.69850 0.01483  0.20591  0.08685  125 ILE D CG1 
2565 C CG2 . ILE B 158 ? 0.70612 0.56060 1.49789 0.03756  0.19790  0.15647  125 ILE D CG2 
2566 C CD1 . ILE B 158 ? 0.73170 0.57463 1.59982 0.03102  0.19202  0.05285  125 ILE D CD1 
2567 N N   . LYS B 159 ? 1.04358 0.74591 1.93984 -0.00003 0.24743  0.17364  126 LYS D N   
2568 C CA  . LYS B 159 ? 1.26143 0.89500 2.16955 0.01056  0.26382  0.20607  126 LYS D CA  
2569 C C   . LYS B 159 ? 1.04387 0.64760 1.98292 0.03140  0.26171  0.18062  126 LYS D C   
2570 O O   . LYS B 159 ? 1.00967 0.60688 1.98644 0.01897  0.26302  0.13710  126 LYS D O   
2571 C CB  . LYS B 159 ? 1.00929 0.61323 1.92824 -0.01691 0.28143  0.20942  126 LYS D CB  
2572 N N   . VAL B 160 ? 0.99420 0.58089 1.91794 0.06362  0.25793  0.20647  127 VAL D N   
2573 C CA  . VAL B 160 ? 1.18056 0.73780 2.13260 0.08905  0.25628  0.18572  127 VAL D CA  
2574 C C   . VAL B 160 ? 1.23882 0.73155 2.18297 0.09907  0.26676  0.21674  127 VAL D C   
2575 O O   . VAL B 160 ? 1.30991 0.79907 2.21144 0.10287  0.26650  0.26014  127 VAL D O   
2576 C CB  . VAL B 160 ? 1.12508 0.73780 2.05644 0.12001  0.23734  0.17963  127 VAL D CB  
2577 C CG1 . VAL B 160 ? 1.00497 0.59828 1.97246 0.14223  0.23624  0.14422  127 VAL D CG1 
2578 C CG2 . VAL B 160 ? 0.89247 0.58404 1.79713 0.10463  0.22342  0.15752  127 VAL D CG2 
2579 N N   . ARG B 161 ? 1.23425 0.68304 2.20713 0.10133  0.27321  0.19081  128 ARG D N   
2580 C CA  . ARG B 161 ? 1.22741 0.61437 2.18372 0.10740  0.28143  0.21386  128 ARG D CA  
2581 C C   . ARG B 161 ? 1.28107 0.63477 2.26102 0.13474  0.27837  0.19093  128 ARG D C   
2582 O O   . ARG B 161 ? 1.27819 0.64825 2.29479 0.13562  0.27618  0.14639  128 ARG D O   
2583 C CB  . ARG B 161 ? 1.26265 0.61679 2.22266 0.06986  0.29868  0.20885  128 ARG D CB  
2584 N N   . TRP B 162 ? 1.52686 0.83332 2.48153 0.15730  0.27729  0.22041  129 TRP D N   
2585 C CA  . TRP B 162 ? 1.51492 0.78032 2.48493 0.18562  0.27457  0.20438  129 TRP D CA  
2586 C C   . TRP B 162 ? 1.63269 0.81971 2.59600 0.17001  0.28909  0.20805  129 TRP D C   
2587 O O   . TRP B 162 ? 1.74747 0.90362 2.67450 0.15677  0.29531  0.24331  129 TRP D O   
2588 C CB  . TRP B 162 ? 1.46443 0.73612 2.40932 0.22944  0.25825  0.23420  129 TRP D CB  
2589 C CG  . TRP B 162 ? 1.53081 0.86580 2.49880 0.25614  0.24469  0.21064  129 TRP D CG  
2590 C CD1 . TRP B 162 ? 1.50002 0.90013 2.45352 0.26941  0.23185  0.22755  129 TRP D CD1 
2591 C CD2 . TRP B 162 ? 1.58593 0.92807 2.59296 0.27142  0.24347  0.16328  129 TRP D CD2 
2592 N NE1 . TRP B 162 ? 1.36972 0.81911 2.35208 0.29215  0.22317  0.19304  129 TRP D NE1 
2593 C CE2 . TRP B 162 ? 1.44503 0.86048 2.45976 0.29368  0.23026  0.15241  129 TRP D CE2 
2594 C CE3 . TRP B 162 ? 1.60658 0.90167 2.63996 0.26719  0.25283  0.12772  129 TRP D CE3 
2595 C CZ2 . TRP B 162 ? 1.30392 0.74875 2.35087 0.31115  0.22694  0.10581  129 TRP D CZ2 
2596 C CZ3 . TRP B 162 ? 1.60418 0.92606 2.66862 0.28494  0.24877  0.08268  129 TRP D CZ3 
2597 C CH2 . TRP B 162 ? 1.53098 0.92766 2.60152 0.30653  0.23629  0.07149  129 TRP D CH2 
2598 N N   . PHE B 163 ? 1.67022 0.82451 2.66501 0.17092  0.29468  0.17039  130 PHE D N   
2599 C CA  . PHE B 163 ? 1.89607 0.97384 2.88546 0.15390  0.30947  0.17003  130 PHE D CA  
2600 C C   . PHE B 163 ? 1.82464 0.86724 2.84159 0.17166  0.30976  0.13318  130 PHE D C   
2601 O O   . PHE B 163 ? 1.83892 0.90690 2.89333 0.15659  0.31306  0.08749  130 PHE D O   
2602 C CB  . PHE B 163 ? 1.65151 0.73667 2.65321 0.10527  0.32504  0.15611  130 PHE D CB  
2603 N N   . ARG B 164 ? 2.11995 1.97498 1.75616 -0.01659 0.12314  0.43208  131 ARG D N   
2604 C CA  . ARG B 164 ? 2.15043 1.97796 1.71709 -0.02815 0.13065  0.41506  131 ARG D CA  
2605 C C   . ARG B 164 ? 2.23801 2.03404 1.79801 -0.04152 0.11960  0.42282  131 ARG D C   
2606 O O   . ARG B 164 ? 2.23917 2.02171 1.76580 -0.07264 0.10370  0.42996  131 ARG D O   
2607 C CB  . ARG B 164 ? 2.06584 1.88522 1.60267 0.00481  0.15996  0.38202  131 ARG D CB  
2608 N N   . ASN B 165 ? 1.99572 1.77896 1.58697 -0.01786 0.12829  0.42093  132 ASN D N   
2609 C CA  . ASN B 165 ? 1.90616 1.66397 1.50993 -0.02960 0.11747  0.43237  132 ASN D CA  
2610 C C   . ASN B 165 ? 1.93427 1.70614 1.61069 -0.01817 0.11167  0.45087  132 ASN D C   
2611 O O   . ASN B 165 ? 1.70165 1.47317 1.41286 -0.04002 0.09012  0.47254  132 ASN D O   
2612 C CB  . ASN B 165 ? 1.79850 1.52022 1.36314 -0.01286 0.13752  0.41008  132 ASN D CB  
2613 N N   . GLY B 166 ? 1.94785 1.73226 1.64797 0.01657  0.13033  0.44113  133 GLY D N   
2614 C CA  . GLY B 166 ? 1.83091 1.63428 1.59968 0.02986  0.12627  0.45631  133 GLY D CA  
2615 C C   . GLY B 166 ? 1.88922 1.72791 1.68289 0.04746  0.12987  0.45315  133 GLY D C   
2616 O O   . GLY B 166 ? 1.84966 1.69217 1.60959 0.06401  0.14562  0.43248  133 GLY D O   
2617 N N   . GLN B 167 ? 1.91077 1.77584 1.76792 0.04360  0.11435  0.47316  134 GLN D N   
2618 C CA  . GLN B 167 ? 1.88726 1.78809 1.77676 0.05722  0.11398  0.47266  134 GLN D CA  
2619 C C   . GLN B 167 ? 1.72865 1.63068 1.62014 0.10153  0.13935  0.44979  134 GLN D C   
2620 O O   . GLN B 167 ? 1.68819 1.57254 1.58871 0.12322  0.15161  0.44514  134 GLN D O   
2621 C CB  . GLN B 167 ? 1.63911 1.56569 1.60102 0.04546  0.09135  0.49832  134 GLN D CB  
2622 N N   . GLU B 168 ? 1.66795 1.59015 1.55068 0.11499  0.14713  0.43537  135 GLU D N   
2623 C CA  . GLU B 168 ? 1.82733 1.75238 1.71044 0.15749  0.16849  0.41135  135 GLU D CA  
2624 C C   . GLU B 168 ? 1.67643 1.64127 1.61574 0.17015  0.16206  0.41445  135 GLU D C   
2625 O O   . GLU B 168 ? 1.41503 1.40307 1.36015 0.15118  0.15209  0.42035  135 GLU D O   
2626 C CB  . GLU B 168 ? 1.71300 1.62284 1.53246 0.16632  0.18606  0.38458  135 GLU D CB  
2627 N N   . GLU B 169 ? 1.72007 1.69206 1.70020 0.20225  0.16812  0.41038  136 GLU D N   
2628 C CA  . GLU B 169 ? 1.50465 1.51425 1.54229 0.21762  0.16174  0.41104  136 GLU D CA  
2629 C C   . GLU B 169 ? 1.59723 1.61868 1.61581 0.23942  0.17477  0.38527  136 GLU D C   
2630 O O   . GLU B 169 ? 1.63877 1.68913 1.67953 0.22821  0.16644  0.38845  136 GLU D O   
2631 C CB  . GLU B 169 ? 1.29409 1.30665 1.37747 0.24705  0.16517  0.41179  136 GLU D CB  
2632 N N   . THR B 170 ? 1.75071 1.74941 1.72998 0.27056  0.19504  0.35962  137 THR D N   
2633 C CA  . THR B 170 ? 1.74293 1.74912 1.70276 0.29425  0.20825  0.33131  137 THR D CA  
2634 C C   . THR B 170 ? 1.60228 1.64762 1.62233 0.31275  0.20229  0.32724  137 THR D C   
2635 O O   . THR B 170 ? 1.52104 1.56958 1.54894 0.35175  0.21245  0.30404  137 THR D O   
2636 C CB  . THR B 170 ? 1.58768 1.59115 1.50132 0.26579  0.21035  0.32660  137 THR D CB  
2637 O OG1 . THR B 170 ? 1.59104 1.55692 1.44673 0.25276  0.21675  0.32538  137 THR D OG1 
2638 C CG2 . THR B 170 ? 1.32976 1.34426 1.23157 0.28988  0.22442  0.29635  137 THR D CG2 
2639 N N   . VAL B 173 ? 1.61833 1.72774 1.65734 0.26733  0.19458  0.32506  140 VAL D N   
2640 C CA  . VAL B 173 ? 1.76762 1.89202 1.82301 0.22458  0.17680  0.35577  140 VAL D CA  
2641 C C   . VAL B 173 ? 1.68196 1.84295 1.81552 0.22805  0.16137  0.36969  140 VAL D C   
2642 O O   . VAL B 173 ? 1.66896 1.83516 1.84618 0.24843  0.15453  0.37358  140 VAL D O   
2643 C CB  . VAL B 173 ? 1.73133 1.83030 1.76378 0.19804  0.16562  0.37939  140 VAL D CB  
2644 C CG1 . VAL B 173 ? 1.39803 1.51525 1.46545 0.16072  0.14155  0.41321  140 VAL D CG1 
2645 C CG2 . VAL B 173 ? 1.67858 1.74591 1.63420 0.18289  0.17704  0.36971  140 VAL D CG2 
2646 N N   . SER B 174 ? 1.54328 1.72925 1.69432 0.20786  0.15665  0.37690  141 SER D N   
2647 C CA  . SER B 174 ? 1.53684 1.75764 1.76222 0.20520  0.14028  0.39278  141 SER D CA  
2648 C C   . SER B 174 ? 1.60392 1.83366 1.82672 0.15903  0.12585  0.42201  141 SER D C   
2649 O O   . SER B 174 ? 1.61789 1.83394 1.78246 0.13495  0.13382  0.42191  141 SER D O   
2650 C CB  . SER B 174 ? 1.41112 1.65823 1.67422 0.23666  0.15070  0.36719  141 SER D CB  
2651 O OG  . SER B 174 ? 1.40985 1.66029 1.63916 0.22482  0.16500  0.35459  141 SER D OG  
2652 N N   . SER B 175 ? 1.43114 1.68303 1.71652 0.14716  0.10402  0.44692  142 SER D N   
2653 C CA  . SER B 175 ? 1.36389 1.62443 1.65336 0.10467  0.08675  0.47763  142 SER D CA  
2654 C C   . SER B 175 ? 1.30038 1.59781 1.65981 0.10777  0.07897  0.48343  142 SER D C   
2655 O O   . SER B 175 ? 1.28345 1.60048 1.70366 0.13906  0.07706  0.47227  142 SER D O   
2656 C CB  . SER B 175 ? 1.35183 1.59984 1.65017 0.08008  0.06229  0.50796  142 SER D CB  
2657 O OG  . SER B 175 ? 1.35435 1.61922 1.72599 0.09944  0.04880  0.51345  142 SER D OG  
2658 N N   . THR B 176 ? 1.39902 1.26300 1.65807 0.23814  0.08664  0.43052  143 THR D N   
2659 C CA  . THR B 176 ? 1.47609 1.39848 1.70650 0.22709  0.05467  0.42323  143 THR D CA  
2660 C C   . THR B 176 ? 1.36491 1.27777 1.56414 0.19988  0.06536  0.41081  143 THR D C   
2661 O O   . THR B 176 ? 1.22885 1.11038 1.45006 0.18711  0.09727  0.39948  143 THR D O   
2662 C CB  . THR B 176 ? 1.15678 1.14576 1.43777 0.22507  0.03474  0.39283  143 THR D CB  
2663 O OG1 . THR B 176 ? 1.03937 1.02652 1.36228 0.20554  0.05305  0.35539  143 THR D OG1 
2664 C CG2 . THR B 176 ? 1.27050 1.26916 1.58810 0.25718  0.03013  0.40226  143 THR D CG2 
2665 N N   . GLN B 177 ? 1.25150 1.19212 1.39817 0.19148  0.03703  0.41329  144 GLN D N   
2666 C CA  . GLN B 177 ? 1.27398 1.20740 1.38281 0.17058  0.04252  0.39881  144 GLN D CA  
2667 C C   . GLN B 177 ? 1.27683 1.24433 1.43786 0.15179  0.04611  0.35441  144 GLN D C   
2668 O O   . GLN B 177 ? 1.25829 1.26095 1.47223 0.15353  0.03661  0.33545  144 GLN D O   
2669 C CB  . GLN B 177 ? 1.42240 1.36723 1.45256 0.16694  0.00625  0.41151  144 GLN D CB  
2670 N N   . LEU B 178 ? 1.05681 1.01256 1.19935 0.13711  0.06033  0.33778  145 LEU D N   
2671 C CA  . LEU B 178 ? 0.99795 0.98140 1.18118 0.12136  0.06141  0.29452  145 LEU D CA  
2672 C C   . LEU B 178 ? 0.96541 0.99181 1.12953 0.11377  0.02399  0.27701  145 LEU D C   
2673 O O   . LEU B 178 ? 1.15764 1.18474 1.25159 0.10783  0.00049  0.28515  145 LEU D O   
2674 C CB  . LEU B 178 ? 0.97257 0.93919 1.13177 0.11167  0.08096  0.28296  145 LEU D CB  
2675 C CG  . LEU B 178 ? 1.27939 1.21626 1.48021 0.11129  0.12375  0.29146  145 LEU D CG  
2676 C CD1 . LEU B 178 ? 1.17250 1.10327 1.34224 0.10578  0.14247  0.28573  145 LEU D CD1 
2677 C CD2 . LEU B 178 ? 1.10440 1.05207 1.39630 0.10382  0.13527  0.26347  145 LEU D CD2 
2678 N N   . ILE B 179 ? 0.70831 0.76612 0.93060 0.11365  0.01877  0.25383  146 ILE D N   
2679 C CA  . ILE B 179 ? 0.74065 0.84220 0.95276 0.10508  -0.01160 0.23780  146 ILE D CA  
2680 C C   . ILE B 179 ? 0.79468 0.89833 0.99608 0.08907  -0.01347 0.19853  146 ILE D C   
2681 O O   . ILE B 179 ? 0.78543 0.88129 1.03475 0.08918  0.00583  0.17105  146 ILE D O   
2682 C CB  . ILE B 179 ? 0.79019 0.92484 1.06466 0.11778  -0.01363 0.23347  146 ILE D CB  
2683 C CG1 . ILE B 179 ? 0.86467 0.98934 1.15259 0.14008  -0.00821 0.27036  146 ILE D CG1 
2684 C CG2 . ILE B 179 ? 0.63306 0.81921 0.89514 0.10793  -0.04263 0.22485  146 ILE D CG2 
2685 C CD1 . ILE B 179 ? 0.92894 1.06483 1.16114 0.14138  -0.03372 0.30504  146 ILE D CD1 
2686 N N   . ARG B 180 ? 0.63870 0.74884 0.77375 0.07557  -0.03922 0.19541  147 ARG D N   
2687 C CA  . ARG B 180 ? 0.69144 0.79715 0.79913 0.06311  -0.04555 0.15949  147 ARG D CA  
2688 C C   . ARG B 180 ? 0.68458 0.82531 0.80151 0.05334  -0.06616 0.13944  147 ARG D C   
2689 O O   . ARG B 180 ? 0.73267 0.89209 0.80941 0.04196  -0.09237 0.15468  147 ARG D O   
2690 C CB  . ARG B 180 ? 0.67845 0.75471 0.69309 0.05650  -0.05974 0.16869  147 ARG D CB  
2691 C CG  . ARG B 180 ? 0.73734 0.80457 0.70556 0.04603  -0.07331 0.13370  147 ARG D CG  
2692 C CD  . ARG B 180 ? 0.74024 0.76892 0.60691 0.04460  -0.08762 0.14470  147 ARG D CD  
2693 N NE  . ARG B 180 ? 1.06560 1.08132 0.86735 0.03258  -0.11252 0.11743  147 ARG D NE  
2694 C CZ  . ARG B 180 ? 0.93977 0.95472 0.68487 0.01390  -0.14651 0.12396  147 ARG D CZ  
2695 N NH1 . ARG B 180 ? 0.92389 0.95906 0.67430 0.00543  -0.16190 0.15617  147 ARG D NH1 
2696 N NH2 . ARG B 180 ? 0.99013 0.98323 0.67137 0.00286  -0.16659 0.09786  147 ARG D NH2 
2697 N N   . ASN B 181 ? 0.57037 0.71903 0.73936 0.05692  -0.05445 0.10582  148 ASN D N   
2698 C CA  . ASN B 181 ? 0.52634 0.70516 0.70449 0.05110  -0.06837 0.08646  148 ASN D CA  
2699 C C   . ASN B 181 ? 0.72951 0.89974 0.83302 0.03214  -0.09153 0.06892  148 ASN D C   
2700 O O   . ASN B 181 ? 0.77280 0.96853 0.86469 0.02110  -0.10695 0.06458  148 ASN D O   
2701 C CB  . ASN B 181 ? 0.52712 0.70512 0.77043 0.06335  -0.05075 0.05359  148 ASN D CB  
2702 C CG  . ASN B 181 ? 0.56086 0.74187 0.87231 0.08209  -0.03136 0.06994  148 ASN D CG  
2703 O OD1 . ASN B 181 ? 0.57204 0.77159 0.88859 0.08886  -0.03419 0.10403  148 ASN D OD1 
2704 N ND2 . ASN B 181 ? 0.76253 0.92189 1.12387 0.09107  -0.01399 0.04511  148 ASN D ND2 
2705 N N   . GLY B 182 ? 0.83131 0.96488 0.88151 0.02914  -0.09320 0.05948  149 GLY D N   
2706 C CA  . GLY B 182 ? 0.73086 0.84331 0.69837 0.01462  -0.11615 0.04215  149 GLY D CA  
2707 C C   . GLY B 182 ? 0.70389 0.80347 0.67292 0.01805  -0.11381 -0.00348 149 GLY D C   
2708 O O   . GLY B 182 ? 0.85017 0.92132 0.74261 0.01022  -0.13165 -0.02088 149 GLY D O   
2709 N N   . ASP B 183 ? 0.72311 0.83653 0.77044 0.03087  -0.09495 -0.02409 150 ASP D N   
2710 C CA  . ASP B 183 ? 0.66071 0.76032 0.71422 0.03719  -0.09460 -0.06938 150 ASP D CA  
2711 C C   . ASP B 183 ? 0.61781 0.70708 0.72025 0.05067  -0.07544 -0.08645 150 ASP D C   
2712 O O   . ASP B 183 ? 0.69179 0.78154 0.84685 0.05942  -0.06835 -0.11721 150 ASP D O   
2713 C CB  . ASP B 183 ? 0.75839 0.87833 0.85609 0.04090  -0.09249 -0.08435 150 ASP D CB  
2714 C CG  . ASP B 183 ? 0.70647 0.84792 0.89053 0.05375  -0.07221 -0.06846 150 ASP D CG  
2715 O OD1 . ASP B 183 ? 0.61816 0.75907 0.82548 0.05637  -0.06050 -0.04199 150 ASP D OD1 
2716 O OD2 . ASP B 183 ? 0.86512 1.01838 1.08735 0.06331  -0.06757 -0.08234 150 ASP D OD2 
2717 N N   . TRP B 184 ? 0.67414 0.75418 0.75903 0.05189  -0.06708 -0.06567 151 TRP D N   
2718 C CA  . TRP B 184 ? 0.66634 0.74423 0.79950 0.06126  -0.04542 -0.07532 151 TRP D CA  
2719 C C   . TRP B 184 ? 0.66580 0.75663 0.89639 0.06433  -0.02347 -0.06934 151 TRP D C   
2720 O O   . TRP B 184 ? 0.70500 0.79690 0.99442 0.06777  -0.01046 -0.09190 151 TRP D O   
2721 C CB  . TRP B 184 ? 0.58679 0.65629 0.70815 0.06816  -0.05324 -0.12087 151 TRP D CB  
2722 C CG  . TRP B 184 ? 0.71987 0.76610 0.73823 0.06952  -0.07276 -0.12661 151 TRP D CG  
2723 C CD1 . TRP B 184 ? 0.84036 0.86714 0.77854 0.06132  -0.09880 -0.13120 151 TRP D CD1 
2724 C CD2 . TRP B 184 ? 0.73615 0.77198 0.71569 0.08056  -0.06745 -0.12780 151 TRP D CD2 
2725 N NE1 . TRP B 184 ? 0.88166 0.87795 0.72746 0.06621  -0.11276 -0.13604 151 TRP D NE1 
2726 C CE2 . TRP B 184 ? 0.86350 0.86607 0.73193 0.08106  -0.09360 -0.13455 151 TRP D CE2 
2727 C CE3 . TRP B 184 ? 0.81978 0.87132 0.84657 0.09029  -0.04172 -0.12282 151 TRP D CE3 
2728 C CZ2 . TRP B 184 ? 0.88812 0.86878 0.68627 0.09600  -0.09612 -0.13792 151 TRP D CZ2 
2729 C CZ3 . TRP B 184 ? 0.72261 0.76232 0.68688 0.10475  -0.04114 -0.12497 151 TRP D CZ3 
2730 C CH2 . TRP B 184 ? 0.69313 0.69579 0.54159 0.10998  -0.06883 -0.13317 151 TRP D CH2 
2731 N N   . THR B 185 ? 0.58845 0.68783 0.83531 0.06330  -0.02120 -0.03916 152 THR D N   
2732 C CA  . THR B 185 ? 0.68741 0.78848 1.01219 0.06897  -0.00111 -0.02733 152 THR D CA  
2733 C C   . THR B 185 ? 0.69973 0.80136 1.01307 0.07042  0.00582  0.02095  152 THR D C   
2734 O O   . THR B 185 ? 0.71852 0.82590 0.97039 0.06627  -0.01023 0.04232  152 THR D O   
2735 C CB  . THR B 185 ? 0.66048 0.76867 1.02386 0.07577  -0.00704 -0.04792 152 THR D CB  
2736 O OG1 . THR B 185 ? 0.74528 0.87277 1.06563 0.07422  -0.02439 -0.03605 152 THR D OG1 
2737 C CG2 . THR B 185 ? 0.64316 0.74263 1.02100 0.07735  -0.01381 -0.09708 152 THR D CG2 
2738 N N   . PHE B 186 ? 0.66529 0.75605 1.03504 0.07599  0.02778  0.03777  153 PHE D N   
2739 C CA  . PHE B 186 ? 0.56565 0.64979 0.92597 0.08158  0.03564  0.08301  153 PHE D CA  
2740 C C   . PHE B 186 ? 0.68755 0.76542 1.10765 0.09348  0.04598  0.09054  153 PHE D C   
2741 O O   . PHE B 186 ? 0.79349 0.86379 1.26427 0.09550  0.05142  0.06190  153 PHE D O   
2742 C CB  . PHE B 186 ? 0.59510 0.65677 0.94234 0.07882  0.05733  0.10522  153 PHE D CB  
2743 C CG  . PHE B 186 ? 0.82722 0.88916 1.10655 0.07359  0.04866  0.10063  153 PHE D CG  
2744 C CD1 . PHE B 186 ? 0.83512 0.90130 1.12329 0.06937  0.05266  0.06635  153 PHE D CD1 
2745 C CD2 . PHE B 186 ? 0.77843 0.83340 0.98149 0.07520  0.03424  0.12996  153 PHE D CD2 
2746 C CE1 . PHE B 186 ? 0.67371 0.73587 0.89254 0.07009  0.04448  0.06160  153 PHE D CE1 
2747 C CE2 . PHE B 186 ? 0.69256 0.73732 0.82261 0.07329  0.02471  0.12520  153 PHE D CE2 
2748 C CZ  . PHE B 186 ? 0.78519 0.83283 0.92147 0.07237  0.03094  0.09112  153 PHE D CZ  
2749 N N   . GLN B 187 ? 0.68911 0.76579 1.09732 0.10381  0.04626  0.12896  154 GLN D N   
2750 C CA  . GLN B 187 ? 0.69665 0.75965 1.15048 0.12055  0.05669  0.14175  154 GLN D CA  
2751 C C   . GLN B 187 ? 0.66574 0.70820 1.09676 0.12943  0.06547  0.18766  154 GLN D C   
2752 O O   . GLN B 187 ? 0.76341 0.81479 1.13959 0.12601  0.05446  0.21023  154 GLN D O   
2753 C CB  . GLN B 187 ? 0.59943 0.69628 1.06495 0.13460  0.03943  0.13319  154 GLN D CB  
2754 C CG  . GLN B 187 ? 0.70521 0.84414 1.12613 0.13418  0.01663  0.15560  154 GLN D CG  
2755 C CD  . GLN B 187 ? 0.72344 0.90611 1.16408 0.14632  0.00393  0.14703  154 GLN D CD  
2756 O OE1 . GLN B 187 ? 0.97231 1.14887 1.45626 0.16714  0.01397  0.13980  154 GLN D OE1 
2757 N NE2 . GLN B 187 ? 0.76527 0.99018 1.17126 0.13336  -0.01759 0.14831  154 GLN D NE2 
2758 N N   . VAL B 188 ? 0.75916 0.76623 1.22575 0.14168  0.08382  0.20097  155 VAL D N   
2759 C CA  . VAL B 188 ? 0.87110 0.84676 1.31355 0.15281  0.09478  0.24423  155 VAL D CA  
2760 C C   . VAL B 188 ? 0.91390 0.86576 1.38833 0.17696  0.09967  0.25470  155 VAL D C   
2761 O O   . VAL B 188 ? 0.84754 0.78834 1.36700 0.18025  0.10409  0.22800  155 VAL D O   
2762 C CB  . VAL B 188 ? 0.84903 0.78403 1.28557 0.13710  0.12306  0.25489  155 VAL D CB  
2763 C CG1 . VAL B 188 ? 0.91275 0.81176 1.41108 0.12892  0.14647  0.23764  155 VAL D CG1 
2764 C CG2 . VAL B 188 ? 1.15010 1.05379 1.53752 0.14851  0.13133  0.30177  155 VAL D CG2 
2765 N N   . LEU B 189 ? 1.10823 1.04806 1.55300 0.19701  0.09654  0.29318  156 LEU D N   
2766 C CA  . LEU B 189 ? 1.14140 1.05536 1.60415 0.22686  0.09917  0.30778  156 LEU D CA  
2767 C C   . LEU B 189 ? 1.17123 1.02292 1.60280 0.23497  0.11722  0.34684  156 LEU D C   
2768 O O   . LEU B 189 ? 1.23907 1.09634 1.62093 0.23926  0.10885  0.37643  156 LEU D O   
2769 C CB  . LEU B 189 ? 1.06360 1.03662 1.52127 0.25179  0.07162  0.31589  156 LEU D CB  
2770 C CG  . LEU B 189 ? 1.03372 1.07516 1.50943 0.24244  0.05295  0.28462  156 LEU D CG  
2771 C CD1 . LEU B 189 ? 1.01999 1.12627 1.49138 0.26344  0.02814  0.30172  156 LEU D CD1 
2772 C CD2 . LEU B 189 ? 0.98335 1.01043 1.50518 0.24515  0.06338  0.24717  156 LEU D CD2 
2773 N N   . VAL B 190 ? 1.20968 0.99643 1.66497 0.23647  0.14083  0.34723  157 VAL D N   
2774 C CA  . VAL B 190 ? 1.34712 1.06271 1.77133 0.24435  0.16162  0.38471  157 VAL D CA  
2775 C C   . VAL B 190 ? 1.47211 1.15384 1.89566 0.28291  0.15535  0.39822  157 VAL D C   
2776 O O   . VAL B 190 ? 1.49728 1.17274 1.95939 0.29259  0.15273  0.37289  157 VAL D O   
2777 C CB  . VAL B 190 ? 1.41476 1.07550 1.86203 0.21283  0.19545  0.37920  157 VAL D CB  
2778 C CG1 . VAL B 190 ? 1.39930 1.04979 1.90777 0.20240  0.19742  0.34027  157 VAL D CG1 
2779 C CG2 . VAL B 190 ? 1.66710 1.24570 2.08024 0.22077  0.21995  0.41962  157 VAL D CG2 
2780 N N   . MET B 191 ? 1.52320 1.18052 1.89764 0.30859  0.15134  0.43730  158 MET D N   
2781 C CA  . MET B 191 ? 1.59691 1.22588 1.96128 0.35266  0.14205  0.45357  158 MET D CA  
2782 C C   . MET B 191 ? 1.59155 1.11295 1.92332 0.35857  0.16842  0.48189  158 MET D C   
2783 O O   . MET B 191 ? 1.69906 1.18555 1.98852 0.34515  0.18399  0.50939  158 MET D O   
2784 C CB  . MET B 191 ? 1.49639 1.18448 1.82939 0.38269  0.11119  0.47625  158 MET D CB  
2785 N N   . LEU B 192 ? 1.74302 1.20670 2.08824 0.37961  0.17387  0.47570  159 LEU D N   
2786 C CA  . LEU B 192 ? 1.86397 1.21380 2.17379 0.38682  0.19720  0.50208  159 LEU D CA  
2787 C C   . LEU B 192 ? 1.91135 1.24133 2.17108 0.44207  0.17883  0.53053  159 LEU D C   
2788 O O   . LEU B 192 ? 2.00181 1.34268 2.27252 0.47737  0.16105  0.51554  159 LEU D O   
2789 C CB  . LEU B 192 ? 1.71158 0.99813 2.05879 0.37324  0.21147  0.47587  159 LEU D CB  
2790 C CG  . LEU B 192 ? 1.97643 1.14164 2.28295 0.37969  0.22895  0.49500  159 LEU D CG  
2791 C CD1 . LEU B 192 ? 1.82659 0.94314 2.10100 0.34186  0.25864  0.52184  159 LEU D CD1 
2792 C CD2 . LEU B 192 ? 1.99130 1.10379 2.33368 0.36747  0.23215  0.46192  159 LEU D CD2 
2793 N N   . GLU B 193 ? 1.94650 1.25757 2.14368 0.44455  0.17887  0.56157  160 GLU D N   
2794 C CA  . GLU B 193 ? 2.14777 1.45347 2.29140 0.48942  0.15391  0.57897  160 GLU D CA  
2795 C C   . GLU B 193 ? 2.30008 1.52345 2.42548 0.51429  0.15669  0.57350  160 GLU D C   
2796 O O   . GLU B 193 ? 2.46356 1.70843 2.58003 0.55966  0.13098  0.57059  160 GLU D O   
2797 C CB  . GLU B 193 ? 2.28357 1.56175 2.35652 0.48261  0.15623  0.60956  160 GLU D CB  
2798 C CG  . GLU B 193 ? 2.45960 1.67134 2.46465 0.51683  0.14585  0.62869  160 GLU D CG  
2799 C CD  . GLU B 193 ? 2.53289 1.80783 2.53756 0.56650  0.10472  0.62747  160 GLU D CD  
2800 O OE1 . GLU B 193 ? 2.47978 1.85813 2.52845 0.57046  0.08287  0.61693  160 GLU D OE1 
2801 O OE2 . GLU B 193 ? 2.30466 1.52828 2.26662 0.60049  0.09406  0.63707  160 GLU D OE2 
2802 N N   . MET B 194 ? 2.33562 1.46659 2.45559 0.48406  0.18629  0.57131  161 MET D N   
2803 C CA  . MET B 194 ? 2.34877 1.38931 2.44381 0.50309  0.18708  0.56578  161 MET D CA  
2804 C C   . MET B 194 ? 2.32536 1.39847 2.46786 0.52809  0.17028  0.53268  161 MET D C   
2805 O O   . MET B 194 ? 2.19493 1.33462 2.39989 0.51169  0.17058  0.50930  161 MET D O   
2806 C CB  . MET B 194 ? 2.32148 1.26383 2.40874 0.45575  0.22105  0.56851  161 MET D CB  
2807 N N   . THR B 195 ? 2.29183 1.31635 2.40041 0.56970  0.15495  0.52975  162 THR D N   
2808 C CA  . THR B 195 ? 2.26192 1.31166 2.40254 0.60056  0.13817  0.49820  162 THR D CA  
2809 C C   . THR B 195 ? 2.16197 1.15971 2.33819 0.56441  0.15421  0.46890  162 THR D C   
2810 O O   . THR B 195 ? 1.89666 0.96085 2.13259 0.54577  0.15571  0.44490  162 THR D O   
2811 C CB  . THR B 195 ? 2.11143 1.10911 2.20113 0.65341  0.11935  0.50225  162 THR D CB  
2812 N N   . VAL B 201 ? 2.26380 0.76932 2.57593 0.28465  0.17586  0.27648  168 VAL D N   
2813 C CA  . VAL B 201 ? 2.16889 0.74358 2.56187 0.23559  0.18142  0.24855  168 VAL D CA  
2814 C C   . VAL B 201 ? 2.06101 0.72937 2.50369 0.20834  0.20982  0.27380  168 VAL D C   
2815 O O   . VAL B 201 ? 2.08736 0.73704 2.54529 0.15849  0.23412  0.29537  168 VAL D O   
2816 C CB  . VAL B 201 ? 2.24103 0.73588 2.64749 0.17630  0.17891  0.23101  168 VAL D CB  
2817 N N   . TYR B 202 ? 1.95379 0.72278 2.41771 0.24164  0.20608  0.27149  169 TYR D N   
2818 C CA  . TYR B 202 ? 2.02074 0.87813 2.52228 0.22344  0.22722  0.29356  169 TYR D CA  
2819 C C   . TYR B 202 ? 1.74518 0.68205 2.32625 0.18869  0.22496  0.25891  169 TYR D C   
2820 O O   . TYR B 202 ? 1.72102 0.66720 2.32237 0.19555  0.20241  0.21726  169 TYR D O   
2821 C CB  . TYR B 202 ? 1.96663 0.88449 2.43644 0.28011  0.22067  0.31573  169 TYR D CB  
2822 C CG  . TYR B 202 ? 1.98615 0.83504 2.37657 0.32253  0.21650  0.34556  169 TYR D CG  
2823 C CD1 . TYR B 202 ? 1.98525 0.78980 2.33591 0.36991  0.19242  0.32908  169 TYR D CD1 
2824 C CD2 . TYR B 202 ? 2.00317 0.83132 2.35366 0.31776  0.23494  0.38870  169 TYR D CD2 
2825 C CE1 . TYR B 202 ? 2.17391 0.91715 2.45336 0.41098  0.18554  0.35423  169 TYR D CE1 
2826 C CE2 . TYR B 202 ? 2.06886 0.83336 2.34465 0.35762  0.22761  0.41346  169 TYR D CE2 
2827 C CZ  . TYR B 202 ? 2.15741 0.88083 2.40085 0.40410  0.20233  0.39593  169 TYR D CZ  
2828 O OH  . TYR B 202 ? 2.37088 1.03362 2.54283 0.44563  0.19260  0.41895  169 TYR D OH  
2829 N N   . THR B 203 ? 1.70504 0.69703 2.32427 0.15313  0.24763  0.27575  170 THR D N   
2830 C CA  . THR B 203 ? 1.76834 0.83528 2.46120 0.11897  0.24640  0.24490  170 THR D CA  
2831 C C   . THR B 203 ? 1.68106 0.84960 2.37059 0.11762  0.25571  0.26258  170 THR D C   
2832 O O   . THR B 203 ? 1.52998 0.68559 2.19063 0.11115  0.27952  0.30390  170 THR D O   
2833 C CB  . THR B 203 ? 1.74592 0.78493 2.48451 0.05589  0.25879  0.23257  170 THR D CB  
2834 O OG1 . THR B 203 ? 1.95233 0.95155 2.66602 0.03172  0.28989  0.27603  170 THR D OG1 
2835 C CG2 . THR B 203 ? 1.87298 0.84019 2.60495 0.05089  0.23492  0.19916  170 THR D CG2 
2836 N N   . CYS B 204 ? 1.53499 0.79665 2.24668 0.12449  0.23634  0.23137  171 CYS D N   
2837 C CA  . CYS B 204 ? 1.39166 0.74693 2.10138 0.11719  0.24093  0.24021  171 CYS D CA  
2838 C C   . CYS B 204 ? 1.39446 0.78746 2.16167 0.06778  0.25079  0.21714  171 CYS D C   
2839 O O   . CYS B 204 ? 1.37106 0.78354 2.18016 0.05671  0.23292  0.17355  171 CYS D O   
2840 C CB  . CYS B 204 ? 1.57034 1.00198 2.26428 0.15291  0.21376  0.22213  171 CYS D CB  
2841 S SG  . CYS B 204 ? 1.88139 1.41649 2.55881 0.14541  0.21320  0.23265  171 CYS D SG  
2842 N N   . HIS B 205 ? 1.42831 0.83135 2.19566 0.04111  0.27919  0.24633  172 HIS D N   
2843 C CA  . HIS B 205 ? 1.31893 0.75843 2.14420 -0.00484 0.29439  0.23078  172 HIS D CA  
2844 C C   . HIS B 205 ? 1.33784 0.87267 2.15423 -0.00147 0.29059  0.22404  172 HIS D C   
2845 O O   . HIS B 205 ? 1.39935 0.95055 2.16254 0.01577  0.29971  0.25702  172 HIS D O   
2846 C CB  . HIS B 205 ? 1.53721 0.92368 2.36979 -0.03724 0.33332  0.26879  172 HIS D CB  
2847 C CG  . HIS B 205 ? 1.57154 0.99029 2.47869 -0.08738 0.35026  0.25239  172 HIS D CG  
2848 N ND1 . HIS B 205 ? 1.63894 1.11120 2.55554 -0.10711 0.37993  0.27232  172 HIS D ND1 
2849 C CD2 . HIS B 205 ? 1.56353 0.97121 2.54043 -0.12037 0.34059  0.21791  172 HIS D CD2 
2850 C CE1 . HIS B 205 ? 1.75583 1.25674 2.75096 -0.14974 0.38954  0.25145  172 HIS D CE1 
2851 N NE2 . HIS B 205 ? 1.61111 1.07371 2.64555 -0.16042 0.36427  0.21794  172 HIS D NE2 
2852 N N   . VAL B 206 ? 1.32106 0.91191 2.18329 -0.01652 0.27484  0.18086  173 VAL D N   
2853 C CA  . VAL B 206 ? 1.11999 0.79383 1.96866 -0.01124 0.26604  0.16768  173 VAL D CA  
2854 C C   . VAL B 206 ? 1.04582 0.76212 1.95528 -0.04701 0.27757  0.14565  173 VAL D C   
2855 O O   . VAL B 206 ? 1.08133 0.78915 2.05095 -0.06753 0.26746  0.11207  173 VAL D O   
2856 C CB  . VAL B 206 ? 0.99884 0.70566 1.83006 0.01632  0.22901  0.13319  173 VAL D CB  
2857 C CG1 . VAL B 206 ? 0.91498 0.69771 1.73689 0.01423  0.21838  0.11254  173 VAL D CG1 
2858 C CG2 . VAL B 206 ? 1.06393 0.75204 1.83695 0.05365  0.21930  0.15914  173 VAL D CG2 
2859 N N   . GLU B 207 ? 1.09168 0.85375 1.98387 -0.05214 0.29710  0.16399  174 GLU D N   
2860 C CA  . GLU B 207 ? 1.12313 0.94045 2.06832 -0.07868 0.30909  0.14494  174 GLU D CA  
2861 C C   . GLU B 207 ? 1.13457 1.01718 2.03804 -0.05912 0.29350  0.12947  174 GLU D C   
2862 O O   . GLU B 207 ? 1.16811 1.05358 2.00084 -0.03862 0.29837  0.15861  174 GLU D O   
2863 C CB  . GLU B 207 ? 1.19553 1.00261 2.15923 -0.10368 0.35490  0.18469  174 GLU D CB  
2864 N N   . HIS B 208 ? 1.07843 1.00707 2.02025 -0.06502 0.27249  0.08344  175 HIS D N   
2865 C CA  . HIS B 208 ? 0.85114 0.83217 1.74930 -0.04623 0.25289  0.06267  175 HIS D CA  
2866 C C   . HIS B 208 ? 0.77138 0.80736 1.72693 -0.06232 0.25347  0.02893  175 HIS D C   
2867 O O   . HIS B 208 ? 0.72470 0.76003 1.75857 -0.08530 0.25108  0.00501  175 HIS D O   
2868 C CB  . HIS B 208 ? 0.73385 0.70796 1.59743 -0.02400 0.21368  0.03468  175 HIS D CB  
2869 C CG  . HIS B 208 ? 0.85707 0.86958 1.65557 -0.00482 0.19424  0.02349  175 HIS D CG  
2870 N ND1 . HIS B 208 ? 0.79378 0.84320 1.60038 -0.00355 0.17291  -0.02025 175 HIS D ND1 
2871 C CD2 . HIS B 208 ? 0.82276 0.83669 1.54249 0.01297  0.19068  0.05029  175 HIS D CD2 
2872 C CE1 . HIS B 208 ? 0.68594 0.75344 1.41809 0.01348  0.15857  -0.01918 175 HIS D CE1 
2873 N NE2 . HIS B 208 ? 0.61907 0.66667 1.29937 0.02204  0.16813  0.02314  175 HIS D NE2 
2874 N N   . PRO B 209 ? 0.84197 0.92445 1.75852 -0.04957 0.25467  0.02599  176 PRO D N   
2875 C CA  . PRO B 209 ? 0.66228 0.80317 1.63154 -0.05872 0.25396  -0.00719 176 PRO D CA  
2876 C C   . PRO B 209 ? 0.68463 0.83585 1.69106 -0.05914 0.21541  -0.06250 176 PRO D C   
2877 O O   . PRO B 209 ? 0.97137 1.16611 2.04293 -0.07151 0.21261  -0.09221 176 PRO D O   
2878 C CB  . PRO B 209 ? 0.77667 0.94887 1.66763 -0.03418 0.25587  0.00068  176 PRO D CB  
2879 C CG  . PRO B 209 ? 0.68382 0.81609 1.50448 -0.02429 0.27455  0.05129  176 PRO D CG  
2880 C CD  . PRO B 209 ? 0.86148 0.94187 1.68458 -0.02690 0.26034  0.05758  176 PRO D CD  
2881 N N   . SER B 210 ? 0.68881 0.80370 1.65585 -0.04442 0.18582  -0.07718 177 SER D N   
2882 C CA  . SER B 210 ? 0.77051 0.88592 1.76216 -0.04136 0.14996  -0.12892 177 SER D CA  
2883 C C   . SER B 210 ? 0.85232 0.93429 1.92190 -0.06362 0.14674  -0.14259 177 SER D C   
2884 O O   . SER B 210 ? 0.89170 0.97117 1.98922 -0.06316 0.11702  -0.18761 177 SER D O   
2885 C CB  . SER B 210 ? 0.96679 1.05869 1.88078 -0.01536 0.12244  -0.13815 177 SER D CB  
2886 O OG  . SER B 210 ? 0.75757 0.80326 1.65548 -0.01183 0.12897  -0.10862 177 SER D OG  
2887 N N   . LEU B 211 ? 0.85410 0.90321 1.95239 -0.08241 0.17480  -0.10546 178 LEU D N   
2888 C CA  . LEU B 211 ? 0.91621 0.91715 2.07566 -0.10443 0.17133  -0.11365 178 LEU D CA  
2889 C C   . LEU B 211 ? 0.87347 0.90178 2.12262 -0.14300 0.19382  -0.10992 178 LEU D C   
2890 O O   . LEU B 211 ? 0.95689 1.01111 2.21064 -0.15366 0.23054  -0.07261 178 LEU D O   
2891 C CB  . LEU B 211 ? 0.93206 0.86537 2.05482 -0.09792 0.18508  -0.07425 178 LEU D CB  
2892 C CG  . LEU B 211 ? 0.92293 0.83750 1.96421 -0.06073 0.16698  -0.07049 178 LEU D CG  
2893 C CD1 . LEU B 211 ? 0.90050 0.75981 1.90879 -0.05246 0.18503  -0.02531 178 LEU D CD1 
2894 C CD2 . LEU B 211 ? 0.99442 0.89151 2.03674 -0.04650 0.13003  -0.11763 178 LEU D CD2 
2895 N N   . LYS B 212 ? 0.93646 0.95938 2.25637 -0.16412 0.17159  -0.14815 179 LYS D N   
2896 C CA  . LYS B 212 ? 1.03790 1.08727 2.45474 -0.20723 0.19060  -0.14451 179 LYS D CA  
2897 C C   . LYS B 212 ? 0.98470 0.97038 2.41673 -0.23436 0.22154  -0.10021 179 LYS D C   
2898 O O   . LYS B 212 ? 1.00524 1.01682 2.49021 -0.26655 0.25615  -0.07286 179 LYS D O   
2899 C CB  . LYS B 212 ? 0.77867 0.83491 2.26217 -0.22263 0.15177  -0.19883 179 LYS D CB  
2900 N N   . SER B 213 ? 1.06657 0.96862 2.44741 -0.21927 0.21051  -0.09178 180 SER D N   
2901 C CA  . SER B 213 ? 1.01083 0.83738 2.38615 -0.23678 0.23637  -0.04967 180 SER D CA  
2902 C C   . SER B 213 ? 1.21025 0.98900 2.48833 -0.19536 0.23729  -0.02325 180 SER D C   
2903 O O   . SER B 213 ? 0.97429 0.75759 2.20440 -0.15989 0.20785  -0.04824 180 SER D O   
2904 C CB  . SER B 213 ? 1.02954 0.79158 2.43875 -0.25902 0.21290  -0.07165 180 SER D CB  
2905 O OG  . SER B 213 ? 1.32616 1.05057 2.70198 -0.22957 0.17080  -0.11107 180 SER D OG  
2906 N N   . PRO B 214 ? 1.23490 0.96970 2.48213 -0.19855 0.27065  0.02779  181 PRO D N   
2907 C CA  . PRO B 214 ? 1.19849 0.89473 2.35650 -0.15766 0.26993  0.05454  181 PRO D CA  
2908 C C   . PRO B 214 ? 1.24559 0.87637 2.37939 -0.13468 0.23737  0.03158  181 PRO D C   
2909 O O   . PRO B 214 ? 1.41818 0.99180 2.59049 -0.15510 0.22675  0.01465  181 PRO D O   
2910 C CB  . PRO B 214 ? 1.33604 0.98611 2.47705 -0.17182 0.31141  0.11084  181 PRO D CB  
2911 C CG  . PRO B 214 ? 1.18614 0.88391 2.39755 -0.21476 0.34105  0.11761  181 PRO D CG  
2912 C CD  . PRO B 214 ? 1.07686 0.80259 2.36740 -0.23871 0.31239  0.06534  181 PRO D CD  
2913 N N   . ILE B 215 ? 1.38078 1.02015 2.44873 -0.09164 0.22137  0.03155  182 ILE D N   
2914 C CA  . ILE B 215 ? 1.31588 0.90517 2.35409 -0.06111 0.19322  0.01134  182 ILE D CA  
2915 C C   . ILE B 215 ? 1.32396 0.83388 2.32155 -0.04605 0.20764  0.05139  182 ILE D C   
2916 O O   . ILE B 215 ? 1.21726 0.73367 2.17224 -0.03318 0.22812  0.09336  182 ILE D O   
2917 C CB  . ILE B 215 ? 1.18040 0.82382 2.17191 -0.02357 0.17109  -0.00641 182 ILE D CB  
2918 C CG1 . ILE B 215 ? 1.14545 0.83814 2.17019 -0.03212 0.14697  -0.05763 182 ILE D CG1 
2919 C CG2 . ILE B 215 ? 0.98021 0.57699 1.92637 0.01616  0.15482  -0.00664 182 ILE D CG2 
2920 C CD1 . ILE B 215 ? 0.96098 0.69770 1.93674 0.00118  0.12515  -0.07694 182 ILE D CD1 
2921 N N   . THR B 216 ? 1.41939 0.84866 2.42414 -0.04530 0.19481  0.03772  183 THR D N   
2922 C CA  . THR B 216 ? 1.43070 0.77250 2.39022 -0.02468 0.20329  0.06994  183 THR D CA  
2923 C C   . THR B 216 ? 1.41727 0.72353 2.34112 0.02017  0.17382  0.04452  183 THR D C   
2924 O O   . THR B 216 ? 1.53775 0.83512 2.48587 0.01771  0.14874  -0.00007 183 THR D O   
2925 C CB  . THR B 216 ? 1.44804 0.70582 2.43956 -0.06582 0.21900  0.08292  183 THR D CB  
2926 O OG1 . THR B 216 ? 1.51601 0.76595 2.53962 -0.08639 0.19055  0.03614  183 THR D OG1 
2927 C CG2 . THR B 216 ? 1.35346 0.65010 2.38014 -0.10858 0.25454  0.11306  183 THR D CG2 
2928 N N   . VAL B 217 ? 1.37566 0.66330 2.24079 0.06355  0.17674  0.07295  184 VAL D N   
2929 C CA  . VAL B 217 ? 1.65569 0.91588 2.48365 0.11301  0.15408  0.05536  184 VAL D CA  
2930 C C   . VAL B 217 ? 1.72454 0.89208 2.50308 0.13669  0.16087  0.08561  184 VAL D C   
2931 O O   . VAL B 217 ? 1.62536 0.77385 2.38506 0.13735  0.18376  0.13042  184 VAL D O   
2932 C CB  . VAL B 217 ? 1.48938 0.84056 2.28921 0.14997  0.14570  0.05644  184 VAL D CB  
2933 C CG1 . VAL B 217 ? 1.27559 0.70177 2.10624 0.13402  0.13058  0.01590  184 VAL D CG1 
2934 C CG2 . VAL B 217 ? 1.52522 0.91674 2.30038 0.15112  0.16572  0.10335  184 VAL D CG2 
2935 N N   . GLU B 218 ? 1.73248 0.84338 2.47512 0.15772  0.13891  0.06057  185 GLU D N   
2936 C CA  . GLU B 218 ? 1.97027 0.98663 2.65110 0.18294  0.13950  0.08255  185 GLU D CA  
2937 C C   . GLU B 218 ? 1.95292 0.99651 2.58736 0.24651  0.13713  0.10178  185 GLU D C   
2938 O O   . GLU B 218 ? 1.96241 1.03033 2.57506 0.28577  0.11797  0.07638  185 GLU D O   
2939 C CB  . GLU B 218 ? 2.07810 1.01588 2.73164 0.18074  0.11538  0.04753  185 GLU D CB  
2940 C CG  . GLU B 218 ? 1.97882 0.88336 2.67567 0.11599  0.11509  0.03279  185 GLU D CG  
2941 C CD  . GLU B 218 ? 2.02829 1.02128 2.79371 0.08447  0.10685  -0.00163 185 GLU D CD  
2942 O OE1 . GLU B 218 ? 1.86260 0.92851 2.63043 0.11402  0.09785  -0.01912 185 GLU D OE1 
2943 O OE2 . GLU B 218 ? 2.15379 1.14553 2.96891 0.03049  0.10875  -0.01092 185 GLU D OE2 
2944 N N   . TRP B 219 ? 1.78532 0.82885 2.40177 0.25698  0.15660  0.14776  186 TRP D N   
2945 C CA  . TRP B 219 ? 1.83950 0.91907 2.41640 0.31547  0.15269  0.16961  186 TRP D CA  
2946 C C   . TRP B 219 ? 2.13664 1.13563 2.64779 0.36050  0.13849  0.16806  186 TRP D C   
2947 O O   . TRP B 219 ? 2.11265 1.00831 2.59272 0.34554  0.14016  0.17368  186 TRP D O   
2948 C CB  . TRP B 219 ? 1.86795 0.96777 2.43658 0.31312  0.17387  0.21925  186 TRP D CB  
2949 N N   . THR B 220 ? 2.08423 1.13216 2.57246 0.41594  0.12381  0.16053  187 THR D N   
2950 C CA  . THR B 220 ? 2.24234 1.22662 2.66716 0.46827  0.10850  0.15874  187 THR D CA  
2951 C C   . THR B 220 ? 2.37397 1.37770 2.76523 0.51177  0.11110  0.19859  187 THR D C   
2952 O O   . THR B 220 ? 2.16325 1.10157 2.50184 0.55107  0.09931  0.20356  187 THR D O   
2953 C CB  . THR B 220 ? 2.23395 1.25808 2.65180 0.50446  0.08841  0.11945  187 THR D CB  
2954 O OG1 . THR B 220 ? 2.19670 1.24341 2.65461 0.46301  0.08641  0.08452  187 THR D OG1 
2955 C CG2 . THR B 220 ? 2.25297 1.17677 2.60774 0.54263  0.06869  0.10400  187 THR D CG2 
2956 N N   . GLY B 221 ? 2.35776 1.44811 2.77633 0.50564  0.12274  0.22599  188 GLY D N   
2957 C CA  . GLY B 221 ? 2.35259 1.47115 2.73905 0.54505  0.12113  0.26290  188 GLY D CA  
2958 C C   . GLY B 221 ? 2.21971 1.46742 2.62875 0.57902  0.10980  0.26084  188 GLY D C   
2959 O O   . GLY B 221 ? 1.94353 1.26068 2.39373 0.56612  0.10737  0.23459  188 GLY D O   
2960 N N   . GLY C 2   ? 0.83522 1.10244 1.46990 0.02873  -0.28828 -0.05197 1   GLY A N   
2961 C CA  . GLY C 2   ? 0.94183 1.22277 1.60640 0.02435  -0.25928 -0.02384 1   GLY A CA  
2962 C C   . GLY C 2   ? 0.90348 1.23981 1.55523 0.04703  -0.27458 -0.02711 1   GLY A C   
2963 O O   . GLY C 2   ? 1.28849 1.63825 1.88380 0.05531  -0.25688 -0.01568 1   GLY A O   
2964 N N   . ASP C 3   ? 0.78504 1.15217 1.48481 0.05705  -0.30425 -0.04041 2   ASP A N   
2965 C CA  . ASP C 3   ? 0.75966 1.17575 1.42339 0.08070  -0.31034 -0.04211 2   ASP A CA  
2966 C C   . ASP C 3   ? 0.62311 1.06185 1.33001 0.08020  -0.28665 -0.01101 2   ASP A C   
2967 O O   . ASP C 3   ? 0.71954 1.18187 1.40181 0.09009  -0.26924 0.01034  2   ASP A O   
2968 C CB  . ASP C 3   ? 0.87464 1.30157 1.53428 0.09238  -0.34176 -0.07222 2   ASP A CB  
2969 C CG  . ASP C 3   ? 1.04724 1.46534 1.64219 0.10402  -0.36138 -0.10035 2   ASP A CG  
2970 O OD1 . ASP C 3   ? 1.07969 1.48014 1.63517 0.10022  -0.35195 -0.09767 2   ASP A OD1 
2971 O OD2 . ASP C 3   ? 1.18324 1.61158 1.76775 0.11789  -0.38539 -0.12536 2   ASP A OD2 
2972 N N   . SER C 4   ? 0.51246 0.94299 1.28567 0.06874  -0.28470 -0.00558 3   SER A N   
2973 C CA  . SER C 4   ? 0.66178 1.11953 1.46882 0.07360  -0.26700 0.01831  3   SER A CA  
2974 C C   . SER C 4   ? 0.47483 0.90487 1.34652 0.05197  -0.23397 0.04827  3   SER A C   
2975 O O   . SER C 4   ? 0.41024 0.80022 1.30178 0.03201  -0.22609 0.04870  3   SER A O   
2976 C CB  . SER C 4   ? 0.60658 1.09462 1.42813 0.08532  -0.29311 -0.00090 3   SER A CB  
2977 O OG  . SER C 4   ? 0.70866 1.16518 1.57293 0.06932  -0.31310 -0.02030 3   SER A OG  
2978 N N   . VAL C 5   ? 0.51630 0.96304 1.40089 0.05781  -0.20741 0.07510  4   VAL A N   
2979 C CA  . VAL C 5   ? 0.54360 0.96602 1.46640 0.04357  -0.16899 0.10304  4   VAL A CA  
2980 C C   . VAL C 5   ? 0.45826 0.92273 1.42233 0.05673  -0.17083 0.11492  4   VAL A C   
2981 O O   . VAL C 5   ? 0.56291 1.05073 1.49934 0.07393  -0.16250 0.12643  4   VAL A O   
2982 C CB  . VAL C 5   ? 0.40020 0.78184 1.26919 0.03849  -0.12318 0.12342  4   VAL A CB  
2983 C CG1 . VAL C 5   ? 0.55894 0.92773 1.46655 0.03305  -0.08614 0.15014  4   VAL A CG1 
2984 C CG2 . VAL C 5   ? 0.40245 0.74139 1.22610 0.02529  -0.11829 0.11146  4   VAL A CG2 
2985 N N   . THR C 6   ? 0.41287 0.87955 1.42802 0.04779  -0.17862 0.11271  5   THR A N   
2986 C CA  . THR C 6   ? 0.42445 0.92451 1.46379 0.05869  -0.17951 0.11975  5   THR A CA  
2987 C C   . THR C 6   ? 0.43893 0.92894 1.51185 0.05375  -0.13661 0.15565  5   THR A C   
2988 O O   . THR C 6   ? 0.44988 0.91337 1.55434 0.03711  -0.11592 0.16982  5   THR A O   
2989 C CB  . THR C 6   ? 0.44899 0.96024 1.52719 0.05286  -0.21358 0.09674  5   THR A CB  
2990 O OG1 . THR C 6   ? 0.82699 1.34567 1.86628 0.06165  -0.25227 0.06008  5   THR A OG1 
2991 C CG2 . THR C 6   ? 0.60798 1.16036 1.70975 0.06579  -0.21600 0.10215  5   THR A CG2 
2992 N N   . GLN C 7   ? 0.41861 0.93171 1.48145 0.07091  -0.12224 0.17108  6   GLN A N   
2993 C CA  . GLN C 7   ? 0.41806 0.92124 1.50131 0.07253  -0.08137 0.20257  6   GLN A CA  
2994 C C   . GLN C 7   ? 0.47325 1.01111 1.58417 0.08321  -0.08549 0.20902  6   GLN A C   
2995 O O   . GLN C 7   ? 0.44246 1.01543 1.54913 0.09292  -0.11756 0.18957  6   GLN A O   
2996 C CB  . GLN C 7   ? 0.50799 0.99552 1.55089 0.08411  -0.05492 0.21821  6   GLN A CB  
2997 C CG  . GLN C 7   ? 0.62658 1.08744 1.68282 0.08479  -0.01046 0.24312  6   GLN A CG  
2998 C CD  . GLN C 7   ? 0.49158 0.91421 1.48529 0.09124  0.01126  0.24744  6   GLN A CD  
2999 O OE1 . GLN C 7   ? 0.41721 0.83016 1.36500 0.08879  -0.00306 0.23501  6   GLN A OE1 
3000 N NE2 . GLN C 7   ? 0.45414 0.85614 1.44927 0.10052  0.04434  0.26460  6   GLN A NE2 
3001 N N   . THR C 8   ? 0.43877 0.97002 1.57553 0.08420  -0.05233 0.23501  7   THR A N   
3002 C CA  . THR C 8   ? 0.45373 1.01767 1.61816 0.09457  -0.05253 0.24410  7   THR A CA  
3003 C C   . THR C 8   ? 0.52067 1.10844 1.65043 0.11776  -0.05630 0.24591  7   THR A C   
3004 O O   . THR C 8   ? 0.56922 1.13649 1.66724 0.12686  -0.03428 0.26046  7   THR A O   
3005 C CB  . THR C 8   ? 0.46167 1.01292 1.65365 0.09397  -0.01367 0.27259  7   THR A CB  
3006 O OG1 . THR C 8   ? 0.72149 1.26099 1.95012 0.07406  -0.01094 0.27585  7   THR A OG1 
3007 C CG2 . THR C 8   ? 0.47753 1.06346 1.69303 0.10746  -0.01199 0.28358  7   THR A CG2 
3008 N N   . GLU C 9   ? 0.53972 1.17197 1.67745 0.12832  -0.08433 0.23164  8   GLU A N   
3009 C CA  . GLU C 9   ? 0.50941 1.17265 1.61633 0.15308  -0.08769 0.23584  8   GLU A CA  
3010 C C   . GLU C 9   ? 0.67736 1.33477 1.79709 0.16316  -0.05386 0.26691  8   GLU A C   
3011 O O   . GLU C 9   ? 0.88426 1.55829 2.04318 0.16241  -0.04955 0.27287  8   GLU A O   
3012 C CB  . GLU C 9   ? 0.48921 1.20803 1.60221 0.16561  -0.12607 0.20890  8   GLU A CB  
3013 C CG  . GLU C 9   ? 0.50067 1.25918 1.57726 0.19481  -0.13248 0.21032  8   GLU A CG  
3014 C CD  . GLU C 9   ? 0.98301 1.75356 2.00795 0.20575  -0.15401 0.19092  8   GLU A CD  
3015 O OE1 . GLU C 9   ? 1.13384 1.88627 2.15148 0.19143  -0.16859 0.17165  8   GLU A OE1 
3016 O OE2 . GLU C 9   ? 1.23108 2.02853 2.22308 0.22907  -0.15603 0.19616  8   GLU A OE2 
3017 N N   . GLY C 10  ? 0.66671 1.30019 1.75532 0.17296  -0.03079 0.28688  9   GLY A N   
3018 C CA  . GLY C 10  ? 0.75552 1.37756 1.85295 0.18516  -0.00003 0.31447  9   GLY A CA  
3019 C C   . GLY C 10  ? 0.58857 1.25378 1.68333 0.20636  -0.00955 0.32090  9   GLY A C   
3020 O O   . GLY C 10  ? 0.52204 1.23187 1.61126 0.21304  -0.04068 0.30067  9   GLY A O   
3021 N N   . PRO C 11  ? 0.53824 1.19166 1.63664 0.22002  0.01670  0.34732  10  PRO A N   
3022 C CA  . PRO C 11  ? 0.54488 1.14835 1.64955 0.21939  0.05216  0.36661  10  PRO A CA  
3023 C C   . PRO C 11  ? 0.55052 1.15519 1.69169 0.21586  0.06716  0.36898  10  PRO A C   
3024 O O   . PRO C 11  ? 0.55710 1.20245 1.72287 0.21943  0.05589  0.36687  10  PRO A O   
3025 C CB  . PRO C 11  ? 0.56846 1.16743 1.66092 0.23997  0.06579  0.39166  10  PRO A CB  
3026 C CG  . PRO C 11  ? 0.57404 1.22830 1.65441 0.25179  0.03953  0.38850  10  PRO A CG  
3027 C CD  . PRO C 11  ? 0.55852 1.25017 1.65250 0.24166  0.01119  0.35825  10  PRO A CD  
3028 N N   . VAL C 12  ? 0.56037 1.12466 1.70541 0.21068  0.09283  0.37335  11  VAL A N   
3029 C CA  . VAL C 12  ? 0.55944 1.12765 1.73469 0.20958  0.11075  0.37925  11  VAL A CA  
3030 C C   . VAL C 12  ? 0.63953 1.19154 1.81387 0.23268  0.13941  0.39771  11  VAL A C   
3031 O O   . VAL C 12  ? 0.65368 1.16218 1.80745 0.24194  0.15768  0.40070  11  VAL A O   
3032 C CB  . VAL C 12  ? 0.56658 1.10799 1.74334 0.19347  0.12160  0.37171  11  VAL A CB  
3033 C CG1 . VAL C 12  ? 0.61141 1.16370 1.81731 0.19535  0.14271  0.38352  11  VAL A CG1 
3034 C CG2 . VAL C 12  ? 0.80971 1.36359 1.98944 0.17105  0.09104  0.35265  11  VAL A CG2 
3035 N N   . THR C 13  ? 0.60327 1.18954 1.80179 0.24297  0.14171  0.40801  12  THR A N   
3036 C CA  . THR C 13  ? 0.65235 1.22858 1.85230 0.26718  0.16671  0.42443  12  THR A CA  
3037 C C   . THR C 13  ? 0.64489 1.23224 1.86731 0.26959  0.18655  0.43011  12  THR A C   
3038 O O   . THR C 13  ? 0.64075 1.27153 1.89407 0.26137  0.17652  0.43322  12  THR A O   
3039 C CB  . THR C 13  ? 0.64763 1.25887 1.85425 0.28132  0.15538  0.43476  12  THR A CB  
3040 O OG1 . THR C 13  ? 0.64071 1.24762 1.82370 0.28099  0.13839  0.43329  12  THR A OG1 
3041 C CG2 . THR C 13  ? 0.68266 1.28025 1.89151 0.30724  0.18072  0.45156  12  THR A CG2 
3042 N N   . LEU C 14  ? 0.66233 1.21315 1.86980 0.28249  0.21378  0.43100  13  LEU A N   
3043 C CA  . LEU C 14  ? 0.67788 1.24199 1.89852 0.29003  0.23597  0.43807  13  LEU A CA  
3044 C C   . LEU C 14  ? 0.75476 1.29804 1.96093 0.32325  0.26139  0.44279  13  LEU A C   
3045 O O   . LEU C 14  ? 0.73263 1.23447 1.91727 0.33662  0.26390  0.43673  13  LEU A O   
3046 C CB  . LEU C 14  ? 0.66429 1.21085 1.87597 0.27599  0.24409  0.42954  13  LEU A CB  
3047 C CG  . LEU C 14  ? 0.62949 1.19031 1.85652 0.24335  0.21919  0.42271  13  LEU A CG  
3048 C CD1 . LEU C 14  ? 0.65875 1.20047 1.87524 0.23369  0.23228  0.41798  13  LEU A CD1 
3049 C CD2 . LEU C 14  ? 0.62562 1.23806 1.89630 0.23098  0.20292  0.43278  13  LEU A CD2 
3050 N N   . SER C 15  ? 0.82897 1.40179 2.04934 0.33711  0.27883  0.45389  14  SER A N   
3051 C CA  . SER C 15  ? 0.78167 1.33875 1.98605 0.37235  0.30284  0.45437  14  SER A CA  
3052 C C   . SER C 15  ? 0.86154 1.39002 2.03808 0.38342  0.32268  0.44065  14  SER A C   
3053 O O   . SER C 15  ? 0.77625 1.31891 1.95583 0.36581  0.32485  0.44176  14  SER A O   
3054 C CB  . SER C 15  ? 0.80123 1.41077 2.03115 0.38605  0.31194  0.47318  14  SER A CB  
3055 O OG  . SER C 15  ? 0.98342 1.62307 2.23793 0.37746  0.29261  0.48316  14  SER A OG  
3056 N N   . GLU C 16  ? 0.88423 1.37158 2.03352 0.41420  0.33548  0.42617  15  GLU A N   
3057 C CA  . GLU C 16  ? 0.85662 1.31533 1.97309 0.43084  0.35184  0.40618  15  GLU A CA  
3058 C C   . GLU C 16  ? 0.87041 1.37965 1.98931 0.44286  0.37158  0.41810  15  GLU A C   
3059 O O   . GLU C 16  ? 0.89839 1.44081 2.02734 0.46521  0.38171  0.43040  15  GLU A O   
3060 C CB  . GLU C 16  ? 0.90581 1.31033 1.99649 0.46494  0.35660  0.38392  15  GLU A CB  
3061 C CG  . GLU C 16  ? 0.93307 1.30125 1.98506 0.48398  0.36753  0.35424  15  GLU A CG  
3062 C CD  . GLU C 16  ? 1.21839 1.52540 2.24930 0.51640  0.36507  0.32626  15  GLU A CD  
3063 O OE1 . GLU C 16  ? 1.28306 1.58116 2.33070 0.52767  0.35920  0.33435  15  GLU A OE1 
3064 O OE2 . GLU C 16  ? 1.30425 1.57108 2.30294 0.53081  0.36711  0.29497  15  GLU A OE2 
3065 N N   . GLY C 17  ? 0.85274 1.37018 1.96295 0.42839  0.37725  0.41710  16  GLY A N   
3066 C CA  . GLY C 17  ? 0.86351 1.43257 1.97918 0.43455  0.39521  0.43539  16  GLY A CA  
3067 C C   . GLY C 17  ? 0.82268 1.42951 1.97742 0.39470  0.38500  0.46035  16  GLY A C   
3068 O O   . GLY C 17  ? 0.82927 1.47192 1.98994 0.39356  0.39870  0.47816  16  GLY A O   
3069 N N   . THR C 18  ? 0.83487 1.43515 2.01683 0.36362  0.35952  0.46185  17  THR A N   
3070 C CA  . THR C 18  ? 0.82835 1.45717 2.04935 0.32589  0.34281  0.47792  17  THR A CA  
3071 C C   . THR C 18  ? 0.86428 1.46595 2.06848 0.30590  0.33940  0.46640  17  THR A C   
3072 O O   . THR C 18  ? 0.75632 1.32088 1.91820 0.32153  0.35117  0.44649  17  THR A O   
3073 C CB  . THR C 18  ? 0.72654 1.36117 1.97675 0.30541  0.31354  0.47714  17  THR A CB  
3074 O OG1 . THR C 18  ? 0.98824 1.57603 2.21099 0.30395  0.30095  0.45470  17  THR A OG1 
3075 C CG2 . THR C 18  ? 0.75004 1.41671 2.01833 0.32507  0.31750  0.49051  17  THR A CG2 
3076 N N   . SER C 19  ? 0.83911 1.45809 2.07800 0.27168  0.32120  0.47691  18  SER A N   
3077 C CA  . SER C 19  ? 0.91181 1.50860 2.14052 0.25005  0.31525  0.46837  18  SER A CA  
3078 C C   . SER C 19  ? 0.83079 1.40480 2.06686 0.22313  0.28184  0.44980  18  SER A C   
3079 O O   . SER C 19  ? 0.89806 1.49223 2.16640 0.21032  0.25839  0.45241  18  SER A O   
3080 C CB  . SER C 19  ? 0.78533 1.41590 2.04855 0.23285  0.31874  0.49504  18  SER A CB  
3081 O OG  . SER C 19  ? 1.05932 1.71708 2.37819 0.20801  0.29329  0.50741  18  SER A OG  
3082 N N   . LEU C 20  ? 0.62713 1.16299 1.83100 0.21704  0.27915  0.42989  19  LEU A N   
3083 C CA  . LEU C 20  ? 0.66944 1.18565 1.87288 0.19452  0.24829  0.41166  19  LEU A CA  
3084 C C   . LEU C 20  ? 0.70251 1.22376 1.92684 0.16422  0.23125  0.41226  19  LEU A C   
3085 O O   . LEU C 20  ? 0.76362 1.28530 1.98485 0.16252  0.24876  0.42220  19  LEU A O   
3086 C CB  . LEU C 20  ? 0.59223 1.06279 1.75011 0.20624  0.25342  0.38985  19  LEU A CB  
3087 C CG  . LEU C 20  ? 0.66140 1.11416 1.81182 0.18758  0.22344  0.37298  19  LEU A CG  
3088 C CD1 . LEU C 20  ? 0.68830 1.16178 1.85625 0.18768  0.20115  0.37625  19  LEU A CD1 
3089 C CD2 . LEU C 20  ? 0.66976 1.07692 1.77936 0.19865  0.23231  0.35559  19  LEU A CD2 
3090 N N   . THR C 21  ? 0.72194 1.24822 1.96641 0.14271  0.19568  0.40104  20  THR A N   
3091 C CA  . THR C 21  ? 0.62270 1.14749 1.88788 0.11455  0.17276  0.39558  20  THR A CA  
3092 C C   . THR C 21  ? 0.65974 1.17456 1.91327 0.10360  0.13695  0.36922  20  THR A C   
3093 O O   . THR C 21  ? 0.66224 1.20092 1.93837 0.10005  0.11034  0.36328  20  THR A O   
3094 C CB  . THR C 21  ? 0.54877 1.10657 1.87150 0.10024  0.16268  0.41471  20  THR A CB  
3095 O OG1 . THR C 21  ? 0.90818 1.48090 2.23738 0.11357  0.19758  0.44325  20  THR A OG1 
3096 C CG2 . THR C 21  ? 0.53823 1.08690 1.88614 0.07191  0.13573  0.40708  20  THR A CG2 
3097 N N   . VAL C 22  ? 0.52368 1.00789 1.73988 0.10088  0.13650  0.35323  21  VAL A N   
3098 C CA  . VAL C 22  ? 0.54914 1.02656 1.74736 0.09296  0.10380  0.32967  21  VAL A CA  
3099 C C   . VAL C 22  ? 0.49444 0.96560 1.70565 0.06905  0.08080  0.31779  21  VAL A C   
3100 O O   . VAL C 22  ? 0.46207 0.91064 1.65759 0.06323  0.09636  0.31858  21  VAL A O   
3101 C CB  . VAL C 22  ? 0.47134 0.91992 1.62147 0.10684  0.11668  0.32120  21  VAL A CB  
3102 C CG1 . VAL C 22  ? 0.45418 0.90542 1.58457 0.10187  0.08266  0.30240  21  VAL A CG1 
3103 C CG2 . VAL C 22  ? 0.59240 1.03842 1.73434 0.13164  0.14153  0.33403  21  VAL A CG2 
3104 N N   . ASN C 23  ? 0.61919 1.11015 1.85847 0.05711  0.04296  0.30485  22  ASN A N   
3105 C CA  . ASN C 23  ? 0.51909 1.00072 1.77568 0.03576  0.01588  0.29058  22  ASN A CA  
3106 C C   . ASN C 23  ? 0.44193 0.90448 1.65318 0.03471  -0.00153 0.26561  22  ASN A C   
3107 O O   . ASN C 23  ? 0.58129 1.04986 1.75726 0.04871  -0.00842 0.25530  22  ASN A O   
3108 C CB  . ASN C 23  ? 0.58486 1.09221 1.88676 0.02667  -0.02224 0.27893  22  ASN A CB  
3109 C CG  . ASN C 23  ? 0.60197 1.13289 1.95325 0.02680  -0.00757 0.30471  22  ASN A CG  
3110 O OD1 . ASN C 23  ? 0.58877 1.11358 1.95225 0.02604  0.02583  0.33293  22  ASN A OD1 
3111 N ND2 . ASN C 23  ? 0.50175 1.06457 1.87920 0.03029  -0.03237 0.29514  22  ASN A ND2 
3112 N N   . CYS C 24  ? 0.64933 1.09025 1.86190 0.01879  -0.00815 0.25886  23  CYS A N   
3113 C CA  . CYS C 24  ? 0.52011 0.94518 1.69282 0.01621  -0.02855 0.23399  23  CYS A CA  
3114 C C   . CYS C 24  ? 0.52394 0.93379 1.72038 -0.00359 -0.05332 0.22226  23  CYS A C   
3115 O O   . CYS C 24  ? 0.53755 0.93436 1.76126 -0.01498 -0.03309 0.24282  23  CYS A O   
3116 C CB  . CYS C 24  ? 0.41884 0.81142 1.52849 0.02300  0.00565  0.23830  23  CYS A CB  
3117 S SG  . CYS C 24  ? 0.55871 0.91651 1.59116 0.01677  -0.01620 0.20722  23  CYS A SG  
3118 N N   . SER C 25  ? 0.52439 0.93645 1.70768 -0.00471 -0.09677 0.19016  24  SER A N   
3119 C CA  . SER C 25  ? 0.44016 0.83196 1.64188 -0.02058 -0.12627 0.17284  24  SER A CA  
3120 C C   . SER C 25  ? 0.48748 0.86970 1.63301 -0.01480 -0.14994 0.14260  24  SER A C   
3121 O O   . SER C 25  ? 0.45307 0.85680 1.56275 0.00129  -0.17328 0.12071  24  SER A O   
3122 C CB  . SER C 25  ? 0.46676 0.87135 1.71559 -0.02508 -0.16320 0.15792  24  SER A CB  
3123 O OG  . SER C 25  ? 0.54408 0.97679 1.76272 -0.00762 -0.19272 0.12931  24  SER A OG  
3124 N N   . TYR C 26  ? 0.48372 0.83791 1.61840 -0.02582 -0.14268 0.14334  25  TYR A N   
3125 C CA  . TYR C 26  ? 0.44060 0.77522 1.50090 -0.02025 -0.16020 0.11518  25  TYR A CA  
3126 C C   . TYR C 26  ? 0.43551 0.76160 1.52336 -0.02757 -0.20644 0.08704  25  TYR A C   
3127 O O   . TYR C 26  ? 0.45687 0.76652 1.60004 -0.04220 -0.21244 0.09466  25  TYR A O   
3128 C CB  . TYR C 26  ? 0.46578 0.75949 1.45735 -0.02419 -0.11921 0.12776  25  TYR A CB  
3129 C CG  . TYR C 26  ? 0.46204 0.73044 1.48600 -0.04049 -0.10029 0.14714  25  TYR A CG  
3130 C CD1 . TYR C 26  ? 0.43781 0.71189 1.50050 -0.04373 -0.06157 0.18272  25  TYR A CD1 
3131 C CD2 . TYR C 26  ? 0.44353 0.68651 1.45915 -0.04962 -0.12014 0.13251  25  TYR A CD2 
3132 C CE1 . TYR C 26  ? 0.47582 0.73637 1.56964 -0.05521 -0.04182 0.20683  25  TYR A CE1 
3133 C CE2 . TYR C 26  ? 0.45516 0.67862 1.50382 -0.06298 -0.10124 0.15608  25  TYR A CE2 
3134 C CZ  . TYR C 26  ? 0.48470 0.71966 1.57297 -0.06552 -0.06131 0.19508  25  TYR A CZ  
3135 O OH  . TYR C 26  ? 0.55743 0.78232 1.68033 -0.07558 -0.04022 0.22467  25  TYR A OH  
3136 N N   . GLU C 27  ? 0.43650 0.76456 1.46641 -0.01466 -0.23603 0.05424  26  GLU A N   
3137 C CA  . GLU C 27  ? 0.46431 0.77159 1.48602 -0.01519 -0.27717 0.02024  26  GLU A CA  
3138 C C   . GLU C 27  ? 0.48925 0.78440 1.44444 -0.00906 -0.28165 0.00469  26  GLU A C   
3139 O O   . GLU C 27  ? 0.44278 0.76176 1.33491 0.00965  -0.28552 -0.00673 26  GLU A O   
3140 C CB  . GLU C 27  ? 0.49225 0.82353 1.50181 0.00230  -0.31429 -0.01165 26  GLU A CB  
3141 C CG  . GLU C 27  ? 0.64453 0.95292 1.64027 0.00699  -0.35578 -0.05077 26  GLU A CG  
3142 C CD  . GLU C 27  ? 0.81474 1.15055 1.80320 0.02585  -0.38854 -0.08172 26  GLU A CD  
3143 O OE1 . GLU C 27  ? 0.61158 0.98226 1.62195 0.03036  -0.38065 -0.06966 26  GLU A OE1 
3144 O OE2 . GLU C 27  ? 1.07057 1.39443 2.03073 0.03798  -0.42095 -0.11802 26  GLU A OE2 
3145 N N   . THR C 28  ? 0.72860 0.98555 1.69029 -0.02390 -0.27783 0.00743  27  THR A N   
3146 C CA  . THR C 28  ? 0.53428 0.76628 1.41056 -0.01911 -0.27199 -0.00485 27  THR A CA  
3147 C C   . THR C 28  ? 0.48223 0.68268 1.38422 -0.02758 -0.30017 -0.02150 27  THR A C   
3148 O O   . THR C 28  ? 0.68921 0.87855 1.67765 -0.04225 -0.31292 -0.01340 27  THR A O   
3149 C CB  . THR C 28  ? 0.45233 0.66002 1.27576 -0.02657 -0.21450 0.02610  27  THR A CB  
3150 O OG1 . THR C 28  ? 0.82586 1.01128 1.57127 -0.02283 -0.21201 0.01249  27  THR A OG1 
3151 C CG2 . THR C 28  ? 0.51430 0.70033 1.39601 -0.04497 -0.18429 0.05906  27  THR A CG2 
3152 N N   . LYS C 29  ? 0.63949 0.82578 1.46785 -0.01795 -0.30983 -0.04294 28  LYS A N   
3153 C CA  . LYS C 29  ? 0.50873 0.66036 1.34856 -0.02333 -0.33328 -0.05826 28  LYS A CA  
3154 C C   . LYS C 29  ? 0.56950 0.68325 1.36679 -0.03528 -0.28952 -0.03223 28  LYS A C   
3155 O O   . LYS C 29  ? 0.64249 0.72433 1.46474 -0.04353 -0.29955 -0.03219 28  LYS A O   
3156 C CB  . LYS C 29  ? 0.52607 0.68521 1.30114 0.00129  -0.37398 -0.10324 28  LYS A CB  
3157 C CG  . LYS C 29  ? 0.55617 0.73421 1.32372 0.02052  -0.39935 -0.12939 28  LYS A CG  
3158 C CD  . LYS C 29  ? 0.91846 1.10023 1.60118 0.04784  -0.42169 -0.16681 28  LYS A CD  
3159 C CE  . LYS C 29  ? 1.22732 1.43499 1.90413 0.06833  -0.44325 -0.19121 28  LYS A CE  
3160 N NZ  . LYS C 29  ? 1.48900 1.70573 2.08632 0.09648  -0.45815 -0.22274 28  LYS A NZ  
3161 N N   . GLN C 30  ? 0.50171 0.61902 1.23844 -0.03473 -0.24332 -0.01112 29  GLN A N   
3162 C CA  . GLN C 30  ? 0.49309 0.58170 1.18464 -0.04186 -0.20108 0.01061  29  GLN A CA  
3163 C C   . GLN C 30  ? 0.48470 0.57668 1.19710 -0.04990 -0.15220 0.04841  29  GLN A C   
3164 O O   . GLN C 30  ? 0.50612 0.62227 1.24808 -0.04832 -0.14816 0.05580  29  GLN A O   
3165 C CB  . GLN C 30  ? 0.55439 0.64380 1.14311 -0.02964 -0.19458 -0.00666 29  GLN A CB  
3166 C CG  . GLN C 30  ? 0.49699 0.58347 1.05364 -0.01825 -0.23696 -0.04137 29  GLN A CG  
3167 C CD  . GLN C 30  ? 0.55002 0.65047 1.01145 -0.00491 -0.23231 -0.05543 29  GLN A CD  
3168 O OE1 . GLN C 30  ? 0.91524 1.04878 1.35352 0.00481  -0.23450 -0.05872 29  GLN A OE1 
3169 N NE2 . GLN C 30  ? 0.54772 0.62609 0.95720 -0.00407 -0.22567 -0.06076 29  GLN A NE2 
3170 N N   . TYR C 31  ? 0.49225 0.56344 1.18683 -0.05496 -0.11543 0.07164  36  TYR A N   
3171 C CA  . TYR C 31  ? 0.49030 0.56780 1.20074 -0.05712 -0.06823 0.10654  36  TYR A CA  
3172 C C   . TYR C 31  ? 0.50485 0.59471 1.16070 -0.04735 -0.04801 0.10094  36  TYR A C   
3173 O O   . TYR C 31  ? 0.58568 0.66584 1.16360 -0.04080 -0.04074 0.08542  36  TYR A O   
3174 C CB  . TYR C 31  ? 0.50430 0.56395 1.19047 -0.05731 -0.03473 0.12771  36  TYR A CB  
3175 C CG  . TYR C 31  ? 0.50811 0.58145 1.21149 -0.05362 0.01350  0.16403  36  TYR A CG  
3176 C CD1 . TYR C 31  ? 0.57308 0.65008 1.21185 -0.04118 0.04535  0.16067  36  TYR A CD1 
3177 C CD2 . TYR C 31  ? 0.51890 0.60417 1.30632 -0.06066 0.02590  0.20190  36  TYR A CD2 
3178 C CE1 . TYR C 31  ? 0.62772 0.72048 1.27874 -0.03196 0.08700  0.18913  36  TYR A CE1 
3179 C CE2 . TYR C 31  ? 0.52451 0.63145 1.32503 -0.05211 0.07079  0.23656  36  TYR A CE2 
3180 C CZ  . TYR C 31  ? 0.64430 0.75517 1.37301 -0.03578 0.10069  0.22758  36  TYR A CZ  
3181 O OH  . TYR C 31  ? 0.86419 0.99964 1.60256 -0.02166 0.14305  0.25745  36  TYR A OH  
3182 N N   . PRO C 32  ? 0.46840 0.57925 1.16611 -0.04622 -0.03949 0.11397  37  PRO A N   
3183 C CA  . PRO C 32  ? 0.45993 0.57835 1.11268 -0.03655 -0.02072 0.11093  37  PRO A CA  
3184 C C   . PRO C 32  ? 0.52340 0.63803 1.16870 -0.03104 0.02634  0.13428  37  PRO A C   
3185 O O   . PRO C 32  ? 0.47801 0.59494 1.16135 -0.03313 0.04661  0.15861  37  PRO A O   
3186 C CB  . PRO C 32  ? 0.45031 0.59696 1.15524 -0.03500 -0.04420 0.10911  37  PRO A CB  
3187 C CG  . PRO C 32  ? 0.45531 0.60991 1.24798 -0.04509 -0.05113 0.12696  37  PRO A CG  
3188 C CD  . PRO C 32  ? 0.46824 0.59866 1.25954 -0.05340 -0.05609 0.12698  37  PRO A CD  
3189 N N   . THR C 33  ? 0.65509 0.76643 1.25396 -0.02188 0.04290  0.12765  38  THR A N   
3190 C CA  . THR C 33  ? 0.50869 0.61995 1.10458 -0.01117 0.08183  0.14328  38  THR A CA  
3191 C C   . THR C 33  ? 0.51575 0.64293 1.14216 -0.00600 0.07979  0.14802  38  THR A C   
3192 O O   . THR C 33  ? 0.60924 0.73624 1.21213 -0.00525 0.06216  0.13367  38  THR A O   
3193 C CB  . THR C 33  ? 0.48817 0.57733 1.00850 -0.00300 0.10103  0.12813  38  THR A CB  
3194 O OG1 . THR C 33  ? 0.60523 0.68547 1.10126 -0.00380 0.10993  0.12921  38  THR A OG1 
3195 C CG2 . THR C 33  ? 0.62208 0.71121 1.13886 0.01270  0.13354  0.13530  38  THR A CG2 
3196 N N   . LEU C 34  ? 0.47502 0.62037 1.15549 -0.00103 0.09840  0.17137  39  LEU A N   
3197 C CA  . LEU C 34  ? 0.46849 0.63372 1.18850 0.00411  0.09448  0.17886  39  LEU A CA  
3198 C C   . LEU C 34  ? 0.53359 0.68803 1.22324 0.02044  0.12201  0.17869  39  LEU A C   
3199 O O   . LEU C 34  ? 0.53941 0.68308 1.20354 0.03135  0.15117  0.18118  39  LEU A O   
3200 C CB  . LEU C 34  ? 0.59209 0.78673 1.39352 0.00085  0.09717  0.20470  39  LEU A CB  
3201 C CG  . LEU C 34  ? 0.48238 0.68375 1.32853 -0.01619 0.06694  0.20457  39  LEU A CG  
3202 C CD1 . LEU C 34  ? 0.51365 0.74634 1.45239 -0.02154 0.06744  0.23217  39  LEU A CD1 
3203 C CD2 . LEU C 34  ? 0.44693 0.64806 1.27807 -0.02107 0.02405  0.17629  39  LEU A CD2 
3204 N N   . PHE C 35  ? 0.56128 0.72050 1.25576 0.02460  0.11115  0.17529  40  PHE A N   
3205 C CA  . PHE C 35  ? 0.58466 0.72836 1.25749 0.03934  0.13080  0.17344  40  PHE A CA  
3206 C C   . PHE C 35  ? 0.49142 0.65886 1.21534 0.04824  0.13129  0.18980  40  PHE A C   
3207 O O   . PHE C 35  ? 0.60461 0.80162 1.37231 0.04185  0.11029  0.19779  40  PHE A O   
3208 C CB  . PHE C 35  ? 0.62459 0.74471 1.24646 0.03601  0.11763  0.15509  40  PHE A CB  
3209 C CG  . PHE C 35  ? 0.57949 0.67732 1.14693 0.02867  0.11694  0.13730  40  PHE A CG  
3210 C CD1 . PHE C 35  ? 0.47796 0.58345 1.03380 0.01547  0.09263  0.12997  40  PHE A CD1 
3211 C CD2 . PHE C 35  ? 0.64527 0.71596 1.17269 0.03757  0.13853  0.12514  40  PHE A CD2 
3212 C CE1 . PHE C 35  ? 0.64046 0.72710 1.14520 0.01020  0.09239  0.11442  40  PHE A CE1 
3213 C CE2 . PHE C 35  ? 0.64910 0.70330 1.12607 0.03214  0.13752  0.10828  40  PHE A CE2 
3214 C CZ  . PHE C 35  ? 0.71464 0.77688 1.17988 0.01787  0.11560  0.10468  40  PHE A CZ  
3215 N N   . TRP C 36  ? 0.51001 0.66455 1.22831 0.06522  0.15379  0.19223  41  TRP A N   
3216 C CA  . TRP C 36  ? 0.51224 0.68267 1.26918 0.07688  0.15528  0.20600  41  TRP A CA  
3217 C C   . TRP C 36  ? 0.53173 0.66891 1.25817 0.08674  0.16013  0.19624  41  TRP A C   
3218 O O   . TRP C 36  ? 0.57226 0.67916 1.26704 0.09686  0.17834  0.18284  41  TRP A O   
3219 C CB  . TRP C 36  ? 0.52380 0.71688 1.32224 0.09177  0.17997  0.22430  41  TRP A CB  
3220 C CG  . TRP C 36  ? 0.50316 0.73973 1.36358 0.08260  0.16798  0.24323  41  TRP A CG  
3221 C CD1 . TRP C 36  ? 0.56537 0.82338 1.45775 0.07546  0.17444  0.25668  41  TRP A CD1 
3222 C CD2 . TRP C 36  ? 0.50406 0.77042 1.40758 0.08013  0.14562  0.25132  41  TRP A CD2 
3223 N NE1 . TRP C 36  ? 0.52487 0.82028 1.48226 0.06614  0.15522  0.27053  41  TRP A NE1 
3224 C CE2 . TRP C 36  ? 0.47344 0.77611 1.43558 0.07022  0.13684  0.26504  41  TRP A CE2 
3225 C CE3 . TRP C 36  ? 0.52496 0.79423 1.42639 0.08662  0.13190  0.25014  41  TRP A CE3 
3226 C CZ2 . TRP C 36  ? 0.45780 0.79880 1.47365 0.06726  0.11237  0.27148  41  TRP A CZ2 
3227 C CZ3 . TRP C 36  ? 0.46671 0.77825 1.41665 0.08633  0.11053  0.25967  41  TRP A CZ3 
3228 C CH2 . TRP C 36  ? 0.45447 0.80111 1.45967 0.07703  0.09977  0.26724  41  TRP A CH2 
3229 N N   . TYR C 37  ? 0.52277 0.66785 1.26202 0.08522  0.14257  0.20329  42  TYR A N   
3230 C CA  . TYR C 37  ? 0.61120 0.72641 1.33526 0.09187  0.14397  0.20086  42  TYR A CA  
3231 C C   . TYR C 37  ? 0.55084 0.67982 1.31890 0.10814  0.14918  0.22064  42  TYR A C   
3232 O O   . TYR C 37  ? 0.63801 0.80897 1.44300 0.10924  0.13976  0.23678  42  TYR A O   
3233 C CB  . TYR C 37  ? 0.55888 0.67470 1.25892 0.07752  0.12016  0.19873  42  TYR A CB  
3234 C CG  . TYR C 37  ? 0.68117 0.76939 1.33007 0.06515  0.11824  0.17697  42  TYR A CG  
3235 C CD1 . TYR C 37  ? 0.63299 0.73428 1.26313 0.05384  0.11022  0.16727  42  TYR A CD1 
3236 C CD2 . TYR C 37  ? 0.66381 0.71265 1.28739 0.06502  0.12278  0.16592  42  TYR A CD2 
3237 C CE1 . TYR C 37  ? 0.57287 0.65136 1.15495 0.04444  0.10908  0.14833  42  TYR A CE1 
3238 C CE2 . TYR C 37  ? 0.69402 0.72162 1.27159 0.05446  0.12023  0.14517  42  TYR A CE2 
3239 C CZ  . TYR C 37  ? 0.70004 0.74394 1.25423 0.04504  0.11451  0.13704  42  TYR A CZ  
3240 O OH  . TYR C 37  ? 0.69411 0.71914 1.20113 0.03635  0.11259  0.11730  42  TYR A OH  
3241 N N   . VAL C 38  ? 0.58289 0.67619 1.34894 0.12202  0.16231  0.21750  43  VAL A N   
3242 C CA  . VAL C 38  ? 0.59829 0.69662 1.40424 0.14006  0.16836  0.23584  43  VAL A CA  
3243 C C   . VAL C 38  ? 0.61474 0.68350 1.42029 0.13878  0.15897  0.24156  43  VAL A C   
3244 O O   . VAL C 38  ? 0.63377 0.65993 1.41099 0.13266  0.15833  0.22338  43  VAL A O   
3245 C CB  . VAL C 38  ? 0.62969 0.71363 1.44451 0.16367  0.19351  0.22887  43  VAL A CB  
3246 C CG1 . VAL C 38  ? 0.66203 0.69676 1.43610 0.16905  0.20283  0.19930  43  VAL A CG1 
3247 C CG2 . VAL C 38  ? 0.70645 0.79119 1.56110 0.18430  0.19883  0.24661  43  VAL A CG2 
3248 N N   . GLN C 39  ? 0.60843 0.70349 1.44941 0.14474  0.15102  0.26898  44  GLN A N   
3249 C CA  . GLN C 39  ? 0.62451 0.70017 1.47773 0.14447  0.14305  0.28551  44  GLN A CA  
3250 C C   . GLN C 39  ? 0.78670 0.85998 1.68518 0.16682  0.15272  0.30670  44  GLN A C   
3251 O O   . GLN C 39  ? 0.69053 0.81210 1.61693 0.17677  0.15160  0.32773  44  GLN A O   
3252 C CB  . GLN C 39  ? 0.59312 0.71339 1.44319 0.13226  0.12209  0.30535  44  GLN A CB  
3253 C CG  . GLN C 39  ? 0.67610 0.78370 1.54153 0.13060  0.11520  0.32975  44  GLN A CG  
3254 C CD  . GLN C 39  ? 0.65984 0.82429 1.51928 0.12455  0.09605  0.35223  44  GLN A CD  
3255 O OE1 . GLN C 39  ? 0.65130 0.86875 1.50440 0.12736  0.08560  0.35092  44  GLN A OE1 
3256 N NE2 . GLN C 39  ? 0.74581 0.90257 1.61033 0.11789  0.08988  0.37289  44  GLN A NE2 
3257 N N   . TYR C 40  ? 0.95490 0.97221 1.86253 0.17587  0.16010  0.29934  45  TYR A N   
3258 C CA  . TYR C 40  ? 0.82729 0.83271 1.77872 0.19884  0.16830  0.31775  45  TYR A CA  
3259 C C   . TYR C 40  ? 1.00825 1.02803 1.99387 0.19617  0.15670  0.35763  45  TYR A C   
3260 O O   . TYR C 40  ? 0.91212 0.93584 1.88600 0.17714  0.14351  0.36621  45  TYR A O   
3261 C CB  . TYR C 40  ? 0.78679 0.72403 1.73644 0.21254  0.17724  0.28897  45  TYR A CB  
3262 C CG  . TYR C 40  ? 0.81898 0.75458 1.73660 0.22370  0.19208  0.25522  45  TYR A CG  
3263 C CD1 . TYR C 40  ? 0.95815 0.91527 1.89257 0.24961  0.20848  0.25805  45  TYR A CD1 
3264 C CD2 . TYR C 40  ? 1.11890 1.03834 1.99067 0.21018  0.19081  0.22434  45  TYR A CD2 
3265 C CE1 . TYR C 40  ? 1.05234 1.01791 1.96083 0.26227  0.22416  0.23408  45  TYR A CE1 
3266 C CE2 . TYR C 40  ? 0.97811 0.90415 1.82226 0.22337  0.20638  0.19953  45  TYR A CE2 
3267 C CZ  . TYR C 40  ? 1.14312 1.09396 2.00680 0.24961  0.22348  0.20611  45  TYR A CZ  
3268 O OH  . TYR C 40  ? 1.28805 1.25451 2.12745 0.26510  0.24098  0.18782  45  TYR A OH  
3269 N N   . PRO C 41  ? 1.14692 1.18058 2.17605 0.21712  0.16237  0.38593  46  PRO A N   
3270 C CA  . PRO C 41  ? 1.15108 1.21644 2.21464 0.21840  0.15323  0.43213  46  PRO A CA  
3271 C C   . PRO C 41  ? 1.09914 1.12215 2.17644 0.20442  0.14445  0.44546  46  PRO A C   
3272 O O   . PRO C 41  ? 1.22285 1.28531 2.31837 0.20016  0.13568  0.48547  46  PRO A O   
3273 C CB  . PRO C 41  ? 0.80811 0.87949 1.90410 0.24126  0.16393  0.44931  46  PRO A CB  
3274 C CG  . PRO C 41  ? 0.75255 0.83159 1.83573 0.25419  0.17612  0.42177  46  PRO A CG  
3275 C CD  . PRO C 41  ? 0.88514 0.91930 1.93316 0.24304  0.17814  0.38098  46  PRO A CD  
3276 N N   . GLY C 42  ? 1.17333 1.12285 2.24549 0.19865  0.14547  0.41436  47  GLY A N   
3277 C CA  . GLY C 42  ? 1.26751 1.17491 2.36339 0.18333  0.13464  0.42683  47  GLY A CA  
3278 C C   . GLY C 42  ? 1.03856 0.91229 2.09278 0.16026  0.12663  0.38827  47  GLY A C   
3279 O O   . GLY C 42  ? 1.23316 1.05675 2.30939 0.14817  0.11723  0.38574  47  GLY A O   
3280 N N   . GLU C 43  ? 1.02314 0.92449 2.02160 0.15382  0.12919  0.35914  48  GLU A N   
3281 C CA  . GLU C 43  ? 1.16599 1.04014 2.11889 0.13527  0.12369  0.32053  48  GLU A CA  
3282 C C   . GLU C 43  ? 0.93711 0.87049 1.84846 0.11898  0.11700  0.32563  48  GLU A C   
3283 O O   . GLU C 43  ? 0.83979 0.83414 1.75742 0.12399  0.11512  0.35372  48  GLU A O   
3284 C CB  . GLU C 43  ? 1.24092 1.07887 2.16452 0.14920  0.13524  0.27158  48  GLU A CB  
3285 C CG  . GLU C 43  ? 1.33791 1.11998 2.29786 0.17237  0.14019  0.25912  48  GLU A CG  
3286 C CD  . GLU C 43  ? 1.52921 1.29276 2.45617 0.19371  0.15328  0.21370  48  GLU A CD  
3287 O OE1 . GLU C 43  ? 1.47692 1.26418 2.35465 0.18650  0.15842  0.19270  48  GLU A OE1 
3288 O OE2 . GLU C 43  ? 1.44461 1.17298 2.39591 0.22017  0.15856  0.20071  48  GLU A OE2 
3289 N N   . GLY C 44  ? 0.71924 0.63507 1.58797 0.10173  0.11153  0.29556  49  GLY A N   
3290 C CA  . GLY C 44  ? 0.70387 0.66699 1.52897 0.08815  0.10429  0.29232  49  GLY A CA  
3291 C C   . GLY C 44  ? 0.85056 0.82157 1.63921 0.09353  0.11384  0.26068  49  GLY A C   
3292 O O   . GLY C 44  ? 1.07181 1.01054 1.86126 0.10720  0.12751  0.23819  49  GLY A O   
3293 N N   . PRO C 45  ? 0.76819 0.78511 1.52743 0.08482  0.10615  0.25985  50  PRO A N   
3294 C CA  . PRO C 45  ? 0.66757 0.69474 1.40205 0.08759  0.11423  0.23604  50  PRO A CA  
3295 C C   . PRO C 45  ? 0.76490 0.74754 1.46164 0.08332  0.12281  0.19987  50  PRO A C   
3296 O O   . PRO C 45  ? 0.91224 0.87864 1.58017 0.06876  0.11402  0.18780  50  PRO A O   
3297 C CB  . PRO C 45  ? 0.58005 0.66032 1.29641 0.07735  0.09745  0.24267  50  PRO A CB  
3298 C CG  . PRO C 45  ? 0.74653 0.85935 1.48460 0.07855  0.08384  0.27571  50  PRO A CG  
3299 C CD  . PRO C 45  ? 0.66558 0.73198 1.41829 0.07540  0.08869  0.28296  50  PRO A CD  
3300 N N   . GLN C 46  ? 0.63921 0.60828 1.33618 0.09875  0.14036  0.18373  51  GLN A N   
3301 C CA  . GLN C 46  ? 0.79946 0.73644 1.45964 0.10243  0.15081  0.14975  51  GLN A CA  
3302 C C   . GLN C 46  ? 0.72473 0.69147 1.36962 0.10683  0.16308  0.14466  51  GLN A C   
3303 O O   . GLN C 46  ? 0.73015 0.73041 1.40522 0.11384  0.16842  0.16350  51  GLN A O   
3304 C CB  . GLN C 46  ? 0.79317 0.68579 1.46766 0.12376  0.16129  0.13306  51  GLN A CB  
3305 C CG  . GLN C 46  ? 0.78203 0.68453 1.50083 0.14455  0.17117  0.15233  51  GLN A CG  
3306 C CD  . GLN C 46  ? 0.99262 0.84635 1.72706 0.16733  0.17658  0.13330  51  GLN A CD  
3307 O OE1 . GLN C 46  ? 1.05033 0.87238 1.75603 0.17655  0.17943  0.09771  51  GLN A OE1 
3308 N NE2 . GLN C 46  ? 0.99618 0.84451 1.77695 0.17898  0.17626  0.15520  51  GLN A NE2 
3309 N N   . LEU C 47  ? 0.78136 0.73787 1.38339 0.10260  0.16717  0.12128  52  LEU A N   
3310 C CA  . LEU C 47  ? 0.64836 0.63378 1.23890 0.10423  0.17836  0.12155  52  LEU A CA  
3311 C C   . LEU C 47  ? 0.72574 0.71863 1.33384 0.13081  0.20233  0.12246  52  LEU A C   
3312 O O   . LEU C 47  ? 0.87179 0.83726 1.46608 0.15136  0.21341  0.10176  52  LEU A O   
3313 C CB  . LEU C 47  ? 0.75168 0.72520 1.29112 0.09598  0.17809  0.09892  52  LEU A CB  
3314 C CG  . LEU C 47  ? 0.68542 0.68652 1.21491 0.09835  0.19128  0.10251  52  LEU A CG  
3315 C CD1 . LEU C 47  ? 0.57991 0.61520 1.13683 0.08072  0.17697  0.12485  52  LEU A CD1 
3316 C CD2 . LEU C 47  ? 0.88520 0.87220 1.36147 0.09600  0.19398  0.07937  52  LEU A CD2 
3317 N N   . LEU C 48  ? 0.77637 0.80972 1.41733 0.13216  0.20870  0.14557  53  LEU A N   
3318 C CA  . LEU C 48  ? 0.75347 0.80638 1.41225 0.15750  0.23347  0.15204  53  LEU A CA  
3319 C C   . LEU C 48  ? 0.81552 0.88189 1.44489 0.16290  0.24966  0.14527  53  LEU A C   
3320 O O   . LEU C 48  ? 0.97452 1.03298 1.57879 0.18883  0.26800  0.12859  53  LEU A O   
3321 C CB  . LEU C 48  ? 0.72400 0.81922 1.43829 0.15594  0.23309  0.18284  53  LEU A CB  
3322 C CG  . LEU C 48  ? 0.72500 0.84597 1.46916 0.18404  0.25763  0.19601  53  LEU A CG  
3323 C CD1 . LEU C 48  ? 0.98879 1.07682 1.72607 0.21060  0.26502  0.18056  53  LEU A CD1 
3324 C CD2 . LEU C 48  ? 0.73236 0.89812 1.53501 0.17732  0.25258  0.22630  53  LEU A CD2 
3325 N N   . PHE C 49  ? 0.64226 0.73078 1.27525 0.14122  0.24192  0.15773  54  PHE A N   
3326 C CA  . PHE C 49  ? 0.76219 0.86333 1.36969 0.14329  0.25555  0.15637  54  PHE A CA  
3327 C C   . PHE C 49  ? 0.75735 0.86558 1.36730 0.11317  0.23506  0.16348  54  PHE A C   
3328 O O   . PHE C 49  ? 0.67717 0.79171 1.31565 0.09531  0.21245  0.17167  54  PHE A O   
3329 C CB  . PHE C 49  ? 0.88186 1.02509 1.52021 0.16530  0.28331  0.18019  54  PHE A CB  
3330 C CG  . PHE C 49  ? 0.87169 1.05172 1.57699 0.15367  0.27851  0.21292  54  PHE A CG  
3331 C CD1 . PHE C 49  ? 0.83276 1.02146 1.57455 0.16405  0.27871  0.22188  54  PHE A CD1 
3332 C CD2 . PHE C 49  ? 0.77042 0.97618 1.50618 0.13301  0.27203  0.23389  54  PHE A CD2 
3333 C CE1 . PHE C 49  ? 0.78868 1.01508 1.59355 0.15419  0.27262  0.24988  54  PHE A CE1 
3334 C CE2 . PHE C 49  ? 0.71950 0.95919 1.52346 0.12177  0.26358  0.26047  54  PHE A CE2 
3335 C CZ  . PHE C 49  ? 0.59748 0.84964 1.43483 0.13251  0.26398  0.26789  54  PHE A CZ  
3336 N N   . LYS C 50  ? 0.62757 0.73711 1.20658 0.11113  0.24228  0.15911  55  LYS A N   
3337 C CA  . LYS C 50  ? 0.56854 0.68112 1.14678 0.08600  0.22303  0.16298  55  LYS A CA  
3338 C C   . LYS C 50  ? 0.66363 0.80457 1.26068 0.08907  0.24069  0.18561  55  LYS A C   
3339 O O   . LYS C 50  ? 0.71604 0.87145 1.30068 0.11292  0.26973  0.19152  55  LYS A O   
3340 C CB  . LYS C 50  ? 0.70430 0.78451 1.22130 0.07646  0.20895  0.13469  55  LYS A CB  
3341 C CG  . LYS C 50  ? 0.79231 0.86219 1.25767 0.09422  0.22984  0.11788  55  LYS A CG  
3342 C CD  . LYS C 50  ? 0.70847 0.75094 1.11907 0.08176  0.21319  0.09157  55  LYS A CD  
3343 C CE  . LYS C 50  ? 0.99021 1.02712 1.34932 0.10116  0.23200  0.07225  55  LYS A CE  
3344 N NZ  . LYS C 50  ? 1.08786 1.10272 1.39609 0.08802  0.21548  0.04803  55  LYS A NZ  
3345 N N   . VAL C 51  ? 0.58649 0.73807 1.21691 0.06690  0.22186  0.19914  56  VAL A N   
3346 C CA  . VAL C 51  ? 0.57377 0.74949 1.23347 0.06475  0.23433  0.22556  56  VAL A CA  
3347 C C   . VAL C 51  ? 0.64084 0.79741 1.27735 0.04492  0.21173  0.21417  56  VAL A C   
3348 O O   . VAL C 51  ? 0.61732 0.77115 1.28518 0.02455  0.18020  0.21178  56  VAL A O   
3349 C CB  . VAL C 51  ? 0.53971 0.75070 1.28638 0.05778  0.23263  0.25896  56  VAL A CB  
3350 C CG1 . VAL C 51  ? 0.54538 0.78215 1.33213 0.05449  0.24657  0.29259  56  VAL A CG1 
3351 C CG2 . VAL C 51  ? 0.55163 0.78356 1.31837 0.07957  0.25440  0.26947  56  VAL A CG2 
3352 N N   . PRO C 52  ? 0.79238 0.93758 1.37304 0.05299  0.22507  0.20447  57  PRO A N   
3353 C CA  . PRO C 52  ? 0.77300 0.90018 1.32883 0.03640  0.20407  0.19356  57  PRO A CA  
3354 C C   . PRO C 52  ? 0.79471 0.93935 1.40616 0.02638  0.20353  0.22497  57  PRO A C   
3355 O O   . PRO C 52  ? 0.76891 0.90119 1.39879 0.00693  0.17279  0.21945  57  PRO A O   
3356 C CB  . PRO C 52  ? 0.85419 0.96741 1.33171 0.05227  0.22170  0.17296  57  PRO A CB  
3357 C CG  . PRO C 52  ? 0.88956 1.00547 1.34968 0.07497  0.24297  0.16346  57  PRO A CG  
3358 C CD  . PRO C 52  ? 0.84392 0.98969 1.37283 0.08034  0.25526  0.19441  57  PRO A CD  
3359 N N   . LYS C 53  ? 0.71044 0.88595 1.35214 0.04130  0.23643  0.25898  58  LYS A N   
3360 C CA  . LYS C 53  ? 0.73295 0.92818 1.43534 0.03264  0.24046  0.29729  58  LYS A CA  
3361 C C   . LYS C 53  ? 0.74363 0.95933 1.54320 0.01736  0.22672  0.32262  58  LYS A C   
3362 O O   . LYS C 53  ? 0.86627 1.10497 1.69065 0.02781  0.24075  0.33247  58  LYS A O   
3363 C CB  . LYS C 53  ? 0.71353 0.94280 1.40482 0.05898  0.28459  0.32849  58  LYS A CB  
3364 C CG  . LYS C 53  ? 0.88360 1.13332 1.63377 0.05112  0.29172  0.37363  58  LYS A CG  
3365 C CD  . LYS C 53  ? 1.11185 1.40850 1.85158 0.08306  0.33904  0.41041  58  LYS A CD  
3366 C CE  . LYS C 53  ? 1.25949 1.54611 1.89299 0.10882  0.35450  0.37626  58  LYS A CE  
3367 N NZ  . LYS C 53  ? 1.34109 1.68224 1.95910 0.14738  0.39999  0.40831  58  LYS A NZ  
3368 N N   . ALA C 54  ? 0.72206 0.92948 1.57850 -0.00615 0.19745  0.33124  59  ALA A N   
3369 C CA  . ALA C 54  ? 0.53504 0.76110 1.49071 -0.02281 0.17767  0.35103  59  ALA A CA  
3370 C C   . ALA C 54  ? 0.54841 0.82115 1.57516 -0.01476 0.21277  0.40657  59  ALA A C   
3371 O O   . ALA C 54  ? 0.67789 0.96869 1.68793 0.00078  0.24736  0.43495  59  ALA A O   
3372 C CB  . ALA C 54  ? 0.56697 0.77017 1.56863 -0.04772 0.13361  0.34184  59  ALA A CB  
3373 N N   . ASN C 55  ? 0.72828 1.02453 1.83095 -0.02241 0.20256  0.42214  63  ASN A N   
3374 C CA  . ASN C 55  ? 0.58780 0.91599 1.73248 -0.00958 0.22250  0.46606  63  ASN A CA  
3375 C C   . ASN C 55  ? 0.65273 1.01148 1.74485 0.02388  0.27136  0.48059  63  ASN A C   
3376 O O   . ASN C 55  ? 0.80844 1.19710 1.91344 0.04129  0.29602  0.52036  63  ASN A O   
3377 C CB  . ASN C 55  ? 0.60020 0.92617 1.79034 -0.01745 0.21571  0.49958  63  ASN A CB  
3378 C CG  . ASN C 55  ? 0.76063 1.05936 2.01633 -0.04568 0.16376  0.48544  63  ASN A CG  
3379 O OD1 . ASN C 55  ? 0.58803 0.88585 1.87810 -0.05560 0.13623  0.46767  63  ASN A OD1 
3380 N ND2 . ASN C 55  ? 0.75683 1.03412 2.02883 -0.05585 0.14890  0.49124  63  ASN A ND2 
3381 N N   . GLU C 56  ? 0.63889 0.99184 1.67289 0.03585  0.28361  0.44754  64  GLU A N   
3382 C CA  . GLU C 56  ? 0.60123 0.97869 1.58413 0.07153  0.32333  0.44912  64  GLU A CA  
3383 C C   . GLU C 56  ? 0.71813 1.09340 1.70001 0.07677  0.31644  0.42560  64  GLU A C   
3384 O O   . GLU C 56  ? 0.55433 0.90969 1.56433 0.05392  0.28122  0.40745  64  GLU A O   
3385 C CB  . GLU C 56  ? 0.59504 0.95103 1.48195 0.08978  0.33888  0.42167  64  GLU A CB  
3386 C CG  . GLU C 56  ? 0.86450 1.24561 1.75012 0.10034  0.36418  0.45601  64  GLU A CG  
3387 C CD  . GLU C 56  ? 1.28247 1.65293 2.06601 0.12838  0.38359  0.42743  64  GLU A CD  
3388 O OE1 . GLU C 56  ? 1.29358 1.62921 2.01102 0.13457  0.37261  0.37858  64  GLU A OE1 
3389 O OE2 . GLU C 56  ? 1.13940 1.53609 1.90932 0.14474  0.40734  0.45381  64  GLU A OE2 
3390 N N   . LYS C 57  ? 0.62888 1.02352 1.57247 0.11075  0.34767  0.42383  65  LYS A N   
3391 C CA  . LYS C 57  ? 0.59627 0.98737 1.53624 0.12114  0.34387  0.40510  65  LYS A CA  
3392 C C   . LYS C 57  ? 0.75153 1.11342 1.59969 0.14852  0.35549  0.36513  65  LYS A C   
3393 O O   . LYS C 57  ? 0.67603 1.04939 1.47740 0.17479  0.38185  0.36475  65  LYS A O   
3394 C CB  . LYS C 57  ? 0.60881 1.04308 1.59362 0.13629  0.35991  0.44102  65  LYS A CB  
3395 C CG  . LYS C 57  ? 0.72644 1.17323 1.78522 0.10919  0.33885  0.47553  65  LYS A CG  
3396 C CD  . LYS C 57  ? 1.03940 1.52593 2.13095 0.12534  0.35392  0.51074  65  LYS A CD  
3397 C CE  . LYS C 57  ? 1.11881 1.61641 2.28806 0.09985  0.33296  0.54609  65  LYS A CE  
3398 N NZ  . LYS C 57  ? 1.11517 1.61077 2.28943 0.09352  0.33631  0.56927  65  LYS A NZ  
3399 N N   . GLY C 58  ? 0.88238 1.20891 1.70917 0.14335  0.33434  0.33214  66  GLY A N   
3400 C CA  . GLY C 58  ? 0.89528 1.19028 1.65170 0.16657  0.34044  0.29468  66  GLY A CA  
3401 C C   . GLY C 58  ? 0.84609 1.15590 1.62460 0.18926  0.35111  0.29752  66  GLY A C   
3402 O O   . GLY C 58  ? 0.74877 1.07791 1.58801 0.17729  0.34135  0.31730  66  GLY A O   
3403 N N   . SER C 59  ? 1.03708 1.33845 1.76701 0.22415  0.36945  0.27543  67  SER A N   
3404 C CA  . SER C 59  ? 0.73820 1.05253 1.48388 0.25280  0.38169  0.27562  67  SER A CA  
3405 C C   . SER C 59  ? 0.80215 1.06218 1.49500 0.26634  0.37104  0.22990  67  SER A C   
3406 O O   . SER C 59  ? 0.84451 1.07507 1.47979 0.27205  0.36912  0.19932  67  SER A O   
3407 C CB  . SER C 59  ? 0.75967 1.13245 1.51227 0.29332  0.41889  0.29990  67  SER A CB  
3408 O OG  . SER C 59  ? 0.82901 1.19682 1.51585 0.32004  0.43332  0.27640  67  SER A OG  
3409 N N   . SER C 60  ? 0.89047 1.13825 1.60808 0.27121  0.36314  0.22671  68  SER A N   
3410 C CA  . SER C 60  ? 0.86594 1.06218 1.54936 0.28530  0.35290  0.18894  68  SER A CA  
3411 C C   . SER C 60  ? 0.80331 1.01175 1.52353 0.30907  0.36019  0.19848  68  SER A C   
3412 O O   . SER C 60  ? 0.73322 0.96013 1.50385 0.29166  0.35199  0.22467  68  SER A O   
3413 C CB  . SER C 60  ? 0.93080 1.07868 1.60357 0.24876  0.32131  0.17315  68  SER A CB  
3414 O OG  . SER C 60  ? 0.98435 1.08234 1.63303 0.26033  0.31132  0.14122  68  SER A OG  
3415 N N   . ARG C 61  ? 0.99317 1.19305 1.68824 0.35106  0.37383  0.17510  74  ARG A N   
3416 C CA  . ARG C 61  ? 0.91675 1.13179 1.64229 0.38246  0.38417  0.18250  74  ARG A CA  
3417 C C   . ARG C 61  ? 0.96937 1.25860 1.74298 0.38625  0.40507  0.22921  74  ARG A C   
3418 O O   . ARG C 61  ? 1.05154 1.38577 1.81391 0.40171  0.42673  0.24286  74  ARG A O   
3419 C CB  . ARG C 61  ? 0.86178 1.03146 1.61103 0.36487  0.36030  0.17712  74  ARG A CB  
3420 C CG  . ARG C 61  ? 0.86383 0.96478 1.57833 0.34838  0.33658  0.14163  74  ARG A CG  
3421 C CD  . ARG C 61  ? 0.94380 1.01261 1.69120 0.32778  0.31474  0.14978  74  ARG A CD  
3422 N NE  . ARG C 61  ? 1.30066 1.31406 2.02365 0.30465  0.29182  0.12650  74  ARG A NE  
3423 C CZ  . ARG C 61  ? 1.41132 1.39835 2.15772 0.28345  0.27174  0.13593  74  ARG A CZ  
3424 N NH1 . ARG C 61  ? 1.34229 1.35098 2.13378 0.28349  0.27057  0.16528  74  ARG A NH1 
3425 N NH2 . ARG C 61  ? 1.30614 1.24955 2.03180 0.26314  0.25289  0.11797  74  ARG A NH2 
3426 N N   . GLY C 62  ? 0.92917 1.23693 1.75804 0.37244  0.39879  0.25647  75  GLY A N   
3427 C CA  . GLY C 62  ? 0.97712 1.34762 1.84944 0.36262  0.40801  0.29907  75  GLY A CA  
3428 C C   . GLY C 62  ? 0.87634 1.25910 1.79317 0.31663  0.39074  0.32254  75  GLY A C   
3429 O O   . GLY C 62  ? 0.92607 1.35154 1.88363 0.30159  0.38984  0.35563  75  GLY A O   
3430 N N   . PHE C 63  ? 0.73480 1.07229 1.62910 0.28850  0.36841  0.30137  76  PHE A N   
3431 C CA  . PHE C 63  ? 0.75670 1.09934 1.68323 0.24586  0.34407  0.31487  76  PHE A CA  
3432 C C   . PHE C 63  ? 0.78748 1.14664 1.70916 0.23050  0.34967  0.32571  76  PHE A C   
3433 O O   . PHE C 63  ? 0.74792 1.08987 1.61642 0.24333  0.36216  0.30871  76  PHE A O   
3434 C CB  . PHE C 63  ? 0.65428 0.94283 1.55184 0.22396  0.31409  0.28779  76  PHE A CB  
3435 C CG  . PHE C 63  ? 0.72883 1.00047 1.63702 0.23678  0.30716  0.28270  76  PHE A CG  
3436 C CD1 . PHE C 63  ? 0.87101 1.10272 1.74288 0.26340  0.31555  0.25879  76  PHE A CD1 
3437 C CD2 . PHE C 63  ? 0.64187 0.93826 1.59958 0.22379  0.29057  0.30131  76  PHE A CD2 
3438 C CE1 . PHE C 63  ? 0.83208 1.04565 1.72026 0.27521  0.30888  0.25775  76  PHE A CE1 
3439 C CE2 . PHE C 63  ? 0.63453 0.91897 1.60350 0.23747  0.28570  0.30113  76  PHE A CE2 
3440 C CZ  . PHE C 63  ? 0.73881 0.98010 1.67461 0.26241  0.29555  0.28141  76  PHE A CZ  
3441 N N   . GLU C 64  ? 0.74312 1.13618 1.72407 0.20389  0.33872  0.35366  77  GLU A N   
3442 C CA  . GLU C 64  ? 0.73068 1.13734 1.72097 0.18520  0.33988  0.36861  77  GLU A CA  
3443 C C   . GLU C 64  ? 0.62796 1.02710 1.65656 0.14545  0.30328  0.36879  77  GLU A C   
3444 O O   . GLU C 64  ? 0.60547 1.01805 1.67933 0.13604  0.28416  0.37317  77  GLU A O   
3445 C CB  . GLU C 64  ? 0.70005 1.15261 1.71474 0.19531  0.36099  0.40654  77  GLU A CB  
3446 C CG  . GLU C 64  ? 0.89175 1.35871 1.85869 0.23834  0.39439  0.40517  77  GLU A CG  
3447 C CD  . GLU C 64  ? 1.02435 1.53935 2.00895 0.24732  0.41227  0.44616  77  GLU A CD  
3448 O OE1 . GLU C 64  ? 0.84497 1.37399 1.87801 0.21814  0.39991  0.47555  77  GLU A OE1 
3449 O OE2 . GLU C 64  ? 1.03445 1.57271 1.98575 0.28494  0.43653  0.44850  77  GLU A OE2 
3450 N N   . ALA C 65  ? 0.55427 0.93391 1.56288 0.12542  0.29237  0.36182  78  ALA A N   
3451 C CA  . ALA C 65  ? 0.52685 0.90056 1.57097 0.09139  0.25595  0.35898  78  ALA A CA  
3452 C C   . ALA C 65  ? 0.63322 1.00920 1.68532 0.07753  0.25905  0.37297  78  ALA A C   
3453 O O   . ALA C 65  ? 0.63529 0.99672 1.63101 0.09049  0.28026  0.36744  78  ALA A O   
3454 C CB  . ALA C 65  ? 0.51498 0.84440 1.50791 0.08070  0.22593  0.32083  78  ALA A CB  
3455 N N   . THR C 66  ? 0.78021 1.17098 1.89930 0.05243  0.23486  0.38901  79  THR A N   
3456 C CA  . THR C 66  ? 0.52511 0.91233 1.65888 0.03818  0.23284  0.40676  79  THR A CA  
3457 C C   . THR C 66  ? 0.56125 0.92123 1.70078 0.01157  0.19440  0.38115  79  THR A C   
3458 O O   . THR C 66  ? 0.52509 0.88290 1.69824 -0.00325 0.15706  0.36590  79  THR A O   
3459 C CB  . THR C 66  ? 0.54980 0.96128 1.74573 0.03252  0.22958  0.44361  79  THR A CB  
3460 O OG1 . THR C 66  ? 1.02866 1.47046 2.21727 0.05923  0.26313  0.46626  79  THR A OG1 
3461 C CG2 . THR C 66  ? 0.61600 1.02364 1.82892 0.02269  0.23133  0.46778  79  THR A CG2 
3462 N N   . TYR C 67  ? 0.57382 0.90656 1.66118 0.00983  0.19938  0.37126  80  TYR A N   
3463 C CA  . TYR C 67  ? 0.49744 0.79789 1.57519 -0.01193 0.16188  0.34690  80  TYR A CA  
3464 C C   . TYR C 67  ? 0.50123 0.81600 1.67039 -0.03260 0.14298  0.37334  80  TYR A C   
3465 O O   . TYR C 67  ? 0.55455 0.85912 1.72441 -0.03723 0.14951  0.38935  80  TYR A O   
3466 C CB  . TYR C 67  ? 0.66388 0.93216 1.65505 -0.00477 0.17541  0.33066  80  TYR A CB  
3467 C CG  . TYR C 67  ? 0.67944 0.91093 1.63410 -0.02053 0.13854  0.29681  80  TYR A CG  
3468 C CD1 . TYR C 67  ? 0.62212 0.85182 1.63612 -0.04120 0.09715  0.29086  80  TYR A CD1 
3469 C CD2 . TYR C 67  ? 0.56078 0.76182 1.42267 -0.01255 0.14369  0.26912  80  TYR A CD2 
3470 C CE1 . TYR C 67  ? 0.56651 0.76662 1.54362 -0.05023 0.06307  0.25809  80  TYR A CE1 
3471 C CE2 . TYR C 67  ? 0.56664 0.74006 1.39340 -0.02417 0.11163  0.24025  80  TYR A CE2 
3472 C CZ  . TYR C 67  ? 0.57368 0.74746 1.45582 -0.04141 0.07193  0.23475  80  TYR A CZ  
3473 O OH  . TYR C 67  ? 0.55922 0.70918 1.40345 -0.04810 0.03909  0.20400  80  TYR A OH  
3474 N N   . ASN C 68  ? 0.50454 0.82914 1.72752 -0.04048 0.11470  0.37273  81  ASN A N   
3475 C CA  . ASN C 68  ? 0.52822 0.85031 1.81938 -0.05558 0.08927  0.39002  81  ASN A CA  
3476 C C   . ASN C 68  ? 0.52093 0.81261 1.81949 -0.07379 0.04299  0.35686  81  ASN A C   
3477 O O   . ASN C 68  ? 0.51804 0.80720 1.82486 -0.07913 0.00475  0.32357  81  ASN A O   
3478 C CB  . ASN C 68  ? 0.57928 0.92445 1.92339 -0.05562 0.07689  0.39912  81  ASN A CB  
3479 C CG  . ASN C 68  ? 0.56960 0.91424 1.99111 -0.06958 0.05469  0.42152  81  ASN A CG  
3480 O OD1 . ASN C 68  ? 0.74418 1.07047 2.20059 -0.08480 0.00941  0.39683  81  ASN A OD1 
3481 N ND2 . ASN C 68  ? 0.60130 0.96780 2.05099 -0.06190 0.08537  0.46817  81  ASN A ND2 
3482 N N   . LYS C 69  ? 0.54882 0.81981 1.84128 -0.07989 0.04574  0.36535  82  LYS A N   
3483 C CA  . LYS C 69  ? 0.52927 0.76896 1.82466 -0.09427 0.00186  0.33275  82  LYS A CA  
3484 C C   . LYS C 69  ? 0.63963 0.87113 2.01020 -0.10561 -0.04294 0.32790  82  LYS A C   
3485 O O   . LYS C 69  ? 0.55469 0.76618 1.92780 -0.11209 -0.08960 0.28780  82  LYS A O   
3486 C CB  . LYS C 69  ? 0.53739 0.75684 1.80564 -0.09596 0.01939  0.34592  82  LYS A CB  
3487 C CG  . LYS C 69  ? 0.64210 0.82666 1.90561 -0.10832 -0.02428 0.31129  82  LYS A CG  
3488 C CD  . LYS C 69  ? 0.54936 0.71467 1.78807 -0.10899 -0.00381 0.32970  82  LYS A CD  
3489 C CE  . LYS C 69  ? 0.83063 0.95879 2.06497 -0.11950 -0.04951 0.29423  82  LYS A CE  
3490 N NZ  . LYS C 69  ? 1.02507 1.13293 2.23072 -0.11927 -0.02871 0.31260  82  LYS A NZ  
3491 N N   . GLU C 70  ? 0.72740 0.97575 2.15858 -0.10569 -0.03078 0.36675  83  GLU A N   
3492 C CA  . GLU C 70  ? 0.70395 0.94378 2.21434 -0.11672 -0.07218 0.36459  83  GLU A CA  
3493 C C   . GLU C 70  ? 0.74217 0.98632 2.25602 -0.11770 -0.11070 0.32197  83  GLU A C   
3494 O O   . GLU C 70  ? 1.03178 1.25324 2.55774 -0.12282 -0.15889 0.28297  83  GLU A O   
3495 C CB  . GLU C 70  ? 0.84269 1.10782 2.41709 -0.11536 -0.04781 0.41860  83  GLU A CB  
3496 C CG  . GLU C 70  ? 0.91566 1.18294 2.49773 -0.11126 -0.01567 0.46392  83  GLU A CG  
3497 C CD  . GLU C 70  ? 1.17083 1.46931 2.82237 -0.10796 0.00380  0.51928  83  GLU A CD  
3498 O OE1 . GLU C 70  ? 1.10155 1.42017 2.78729 -0.10902 -0.00210 0.52274  83  GLU A OE1 
3499 O OE2 . GLU C 70  ? 1.21133 1.51763 2.88395 -0.10329 0.02498  0.56087  83  GLU A OE2 
3500 N N   . ALA C 71  ? 0.63077 0.90624 2.13081 -0.10925 -0.09016 0.32787  84  ALA A N   
3501 C CA  . ALA C 71  ? 0.74506 1.03384 2.24548 -0.10644 -0.12172 0.29230  84  ALA A CA  
3502 C C   . ALA C 71  ? 0.77942 1.07063 2.20321 -0.09601 -0.12642 0.25472  84  ALA A C   
3503 O O   . ALA C 71  ? 0.86392 1.17269 2.27738 -0.08858 -0.15001 0.22646  84  ALA A O   
3504 C CB  . ALA C 71  ? 0.63941 0.96411 2.17000 -0.10118 -0.09923 0.32004  84  ALA A CB  
3505 N N   . THR C 72  ? 0.81847 1.09586 2.18918 -0.09383 -0.10484 0.25518  85  THR A N   
3506 C CA  . THR C 72  ? 0.79444 1.07633 2.09483 -0.08342 -0.10506 0.22600  85  THR A CA  
3507 C C   . THR C 72  ? 0.56320 0.87707 1.84703 -0.06924 -0.08614 0.23032  85  THR A C   
3508 O O   . THR C 72  ? 0.57272 0.90155 1.83764 -0.05990 -0.11245 0.20200  85  THR A O   
3509 C CB  . THR C 72  ? 0.49359 0.76245 1.77433 -0.08247 -0.15855 0.17735  85  THR A CB  
3510 O OG1 . THR C 72  ? 0.71002 0.99429 2.02112 -0.07843 -0.19292 0.15762  85  THR A OG1 
3511 C CG2 . THR C 72  ? 0.51504 0.74780 1.81343 -0.09429 -0.17818 0.17231  85  THR A CG2 
3512 N N   . SER C 73  ? 0.47524 0.80080 1.76271 -0.06405 -0.03925 0.26724  86  SER A N   
3513 C CA  . SER C 73  ? 0.54287 0.89480 1.81825 -0.04864 -0.01713 0.27569  86  SER A CA  
3514 C C   . SER C 73  ? 0.45417 0.80431 1.68134 -0.03568 0.03160  0.29176  86  SER A C   
3515 O O   . SER C 73  ? 0.59324 0.92842 1.80428 -0.03872 0.05434  0.30467  86  SER A O   
3516 C CB  . SER C 73  ? 0.48921 0.86218 1.82251 -0.04960 -0.01121 0.30247  86  SER A CB  
3517 O OG  . SER C 73  ? 0.61701 0.98924 1.96924 -0.05086 0.02358  0.34158  86  SER A OG  
3518 N N   . PHE C 74  ? 0.46863 0.83361 1.67176 -0.01884 0.04702  0.28980  87  PHE A N   
3519 C CA  . PHE C 74  ? 0.45181 0.79994 1.58725 -0.00102 0.08873  0.29548  87  PHE A CA  
3520 C C   . PHE C 74  ? 0.45220 0.82550 1.60188 0.01676  0.10453  0.30639  87  PHE A C   
3521 O O   . PHE C 74  ? 0.45282 0.81134 1.54979 0.03044  0.10841  0.29136  87  PHE A O   
3522 C CB  . PHE C 74  ? 0.45031 0.75838 1.49533 0.00126  0.08040  0.26361  87  PHE A CB  
3523 C CG  . PHE C 74  ? 0.46519 0.74703 1.44262 0.01472  0.11829  0.26493  87  PHE A CG  
3524 C CD1 . PHE C 74  ? 0.47909 0.76353 1.46284 0.01734  0.14781  0.28641  87  PHE A CD1 
3525 C CD2 . PHE C 74  ? 0.46806 0.72575 1.37914 0.02614  0.12280  0.24509  87  PHE A CD2 
3526 C CE1 . PHE C 74  ? 0.49637 0.76182 1.41594 0.03427  0.17979  0.28260  87  PHE A CE1 
3527 C CE2 . PHE C 74  ? 0.48584 0.71839 1.33942 0.03913  0.15271  0.24065  87  PHE A CE2 
3528 C CZ  . PHE C 74  ? 0.50039 0.73772 1.35530 0.04474  0.18045  0.25658  87  PHE A CZ  
3529 N N   . HIS C 75  ? 0.50455 0.90517 1.71032 0.01678  0.11152  0.33197  88  HIS A N   
3530 C CA  . HIS C 75  ? 0.50620 0.92823 1.72200 0.03277  0.12084  0.34091  88  HIS A CA  
3531 C C   . HIS C 75  ? 0.56028 0.97918 1.73891 0.05790  0.16500  0.35165  88  HIS A C   
3532 O O   . HIS C 75  ? 0.53922 0.95752 1.70764 0.06462  0.19474  0.36832  88  HIS A O   
3533 C CB  . HIS C 75  ? 0.49343 0.94004 1.76834 0.02506  0.11425  0.36361  88  HIS A CB  
3534 C CG  . HIS C 75  ? 0.49250 0.93923 1.80928 0.00280  0.06892  0.34931  88  HIS A CG  
3535 N ND1 . HIS C 75  ? 0.47541 0.91550 1.77621 -0.00176 0.03175  0.31498  88  HIS A ND1 
3536 C CD2 . HIS C 75  ? 0.51198 0.96452 1.88602 -0.01347 0.05331  0.36338  88  HIS A CD2 
3537 C CE1 . HIS C 75  ? 0.48566 0.92668 1.82879 -0.01832 -0.00570 0.30382  88  HIS A CE1 
3538 N NE2 . HIS C 75  ? 0.50798 0.95352 1.89967 -0.02719 0.00621  0.33298  88  HIS A NE2 
3539 N N   . LEU C 76  ? 0.47926 0.89652 1.63670 0.07475  0.16801  0.34152  89  LEU A N   
3540 C CA  . LEU C 76  ? 0.54363 0.95113 1.66598 0.10206  0.20419  0.34520  89  LEU A CA  
3541 C C   . LEU C 76  ? 0.55010 0.98650 1.70103 0.11706  0.22073  0.36864  89  LEU A C   
3542 O O   . LEU C 76  ? 0.62116 1.07706 1.80337 0.11229  0.20107  0.37275  89  LEU A O   
3543 C CB  . LEU C 76  ? 0.56448 0.93709 1.63268 0.11052  0.19418  0.32110  89  LEU A CB  
3544 C CG  . LEU C 76  ? 0.58001 0.92378 1.60117 0.13699  0.22299  0.31490  89  LEU A CG  
3545 C CD1 . LEU C 76  ? 0.58291 0.89584 1.55025 0.13934  0.24057  0.30216  89  LEU A CD1 
3546 C CD2 . LEU C 76  ? 0.69584 1.01163 1.68796 0.14185  0.20873  0.29970  89  LEU A CD2 
3547 N N   . GLN C 77  ? 0.58963 1.03122 1.72439 0.13745  0.25586  0.38239  90  GLN A N   
3548 C CA  . GLN C 77  ? 0.57176 1.04387 1.72710 0.15449  0.27345  0.40573  90  GLN A CA  
3549 C C   . GLN C 77  ? 0.83014 1.29465 1.94180 0.19121  0.30793  0.40138  90  GLN A C   
3550 O O   . GLN C 77  ? 0.83691 1.28422 1.90923 0.20193  0.32509  0.39066  90  GLN A O   
3551 C CB  . GLN C 77  ? 0.60621 1.10816 1.80048 0.14124  0.27649  0.43581  90  GLN A CB  
3552 C CG  . GLN C 77  ? 0.63587 1.14745 1.88478 0.10955  0.23947  0.43956  90  GLN A CG  
3553 C CD  . GLN C 77  ? 0.83250 1.37102 2.12922 0.09855  0.24261  0.47315  90  GLN A CD  
3554 O OE1 . GLN C 77  ? 0.73591 1.28640 2.02002 0.11239  0.27240  0.49582  90  GLN A OE1 
3555 N NE2 . GLN C 77  ? 0.82649 1.37644 2.17908 0.07571  0.21081  0.47667  90  GLN A NE2 
3556 N N   . LYS C 78  ? 0.79995 1.27732 1.91707 0.21248  0.31610  0.40688  91  LYS A N   
3557 C CA  . LYS C 78  ? 0.85055 1.32356 1.93028 0.25151  0.34514  0.40095  91  LYS A CA  
3558 C C   . LYS C 78  ? 0.94935 1.46596 2.05446 0.26697  0.35777  0.42726  91  LYS A C   
3559 O O   . LYS C 78  ? 0.87028 1.40607 2.01592 0.25381  0.34143  0.43982  91  LYS A O   
3560 C CB  . LYS C 78  ? 0.67751 1.10804 1.73026 0.26787  0.34024  0.37306  91  LYS A CB  
3561 C CG  . LYS C 78  ? 0.78605 1.20116 1.79763 0.31004  0.36470  0.35772  91  LYS A CG  
3562 C CD  . LYS C 78  ? 0.71742 1.07783 1.70663 0.32231  0.35581  0.32899  91  LYS A CD  
3563 C CE  . LYS C 78  ? 0.96700 1.30415 1.91405 0.36481  0.37459  0.30558  91  LYS A CE  
3564 N NZ  . LYS C 78  ? 1.30347 1.57885 2.23569 0.37504  0.36259  0.27816  91  LYS A NZ  
3565 N N   . ALA C 79  ? 0.83405 1.36984 1.91285 0.29699  0.38600  0.43454  92  ALA A N   
3566 C CA  . ALA C 79  ? 1.06600 1.64974 2.16697 0.31392  0.40010  0.46257  92  ALA A CA  
3567 C C   . ALA C 79  ? 1.12457 1.70321 2.22576 0.33538  0.39846  0.45257  92  ALA A C   
3568 O O   . ALA C 79  ? 1.00006 1.60413 2.14349 0.32431  0.38758  0.47073  92  ALA A O   
3569 C CB  . ALA C 79  ? 1.22018 1.82966 2.28523 0.34546  0.42969  0.47115  92  ALA A CB  
3570 N N   . SER C 80  ? 1.05859 1.60258 2.11384 0.36706  0.40745  0.42249  93  SER A N   
3571 C CA  . SER C 80  ? 0.97719 1.50882 2.02978 0.39146  0.40623  0.41156  93  SER A CA  
3572 C C   . SER C 80  ? 1.10295 1.57294 2.14001 0.38566  0.38896  0.38184  93  SER A C   
3573 O O   . SER C 80  ? 1.19499 1.62343 2.19130 0.40158  0.39346  0.35286  93  SER A O   
3574 C CB  . SER C 80  ? 1.20707 1.75110 2.22306 0.43953  0.42962  0.40207  93  SER A CB  
3575 O OG  . SER C 80  ? 1.37942 1.98562 2.40948 0.44575  0.44647  0.43451  93  SER A OG  
3576 N N   . VAL C 81  ? 0.98641 1.45222 2.05569 0.36390  0.36799  0.38939  94  VAL A N   
3577 C CA  . VAL C 81  ? 0.93132 1.34482 1.99048 0.35741  0.35066  0.36901  94  VAL A CA  
3578 C C   . VAL C 81  ? 0.94434 1.32372 1.98357 0.39318  0.35717  0.35255  94  VAL A C   
3579 O O   . VAL C 81  ? 1.21611 1.61818 2.25335 0.42194  0.37178  0.35732  94  VAL A O   
3580 C CB  . VAL C 81  ? 0.73677 1.16482 1.83240 0.32626  0.32484  0.38333  94  VAL A CB  
3581 C CG1 . VAL C 81  ? 0.86037 1.31454 1.97631 0.29186  0.31303  0.39290  94  VAL A CG1 
3582 C CG2 . VAL C 81  ? 0.96511 1.42915 2.08852 0.33652  0.32459  0.40252  94  VAL A CG2 
3583 N N   . GLN C 82  ? 0.81053 1.13376 1.83700 0.39119  0.34430  0.33340  95  GLN A N   
3584 C CA  . GLN C 82  ? 0.99795 1.27570 2.00979 0.42138  0.34513  0.31533  95  GLN A CA  
3585 C C   . GLN C 82  ? 0.99207 1.23459 2.02019 0.40422  0.32398  0.31972  95  GLN A C   
3586 O O   . GLN C 82  ? 0.90749 1.15279 1.94512 0.37315  0.30937  0.32740  95  GLN A O   
3587 C CB  . GLN C 82  ? 1.11554 1.34862 2.08508 0.44527  0.35341  0.27928  95  GLN A CB  
3588 C CG  . GLN C 82  ? 1.30636 1.52318 2.25787 0.49014  0.36196  0.25914  95  GLN A CG  
3589 C CD  . GLN C 82  ? 1.45372 1.64279 2.35971 0.51721  0.36891  0.21998  95  GLN A CD  
3590 O OE1 . GLN C 82  ? 1.24639 1.42333 2.13335 0.50110  0.36833  0.20859  95  GLN A OE1 
3591 N NE2 . GLN C 82  ? 1.19858 1.38007 2.08534 0.56077  0.37384  0.19673  95  GLN A NE2 
3592 N N   . GLU C 83  ? 0.88719 1.09948 1.91859 0.42632  0.32169  0.31613  96  GLU A N   
3593 C CA  . GLU C 83  ? 0.94334 1.12408 1.99119 0.41261  0.30332  0.32577  96  GLU A CA  
3594 C C   . GLU C 83  ? 1.00863 1.13602 2.04166 0.39558  0.29157  0.30832  96  GLU A C   
3595 O O   . GLU C 83  ? 1.10971 1.23570 2.15584 0.37053  0.27573  0.32367  96  GLU A O   
3596 C CB  . GLU C 83  ? 0.93769 1.08904 1.99240 0.44102  0.30375  0.32421  96  GLU A CB  
3597 C CG  . GLU C 83  ? 1.08491 1.28673 2.16468 0.44812  0.30668  0.35228  96  GLU A CG  
3598 C CD  . GLU C 83  ? 1.36430 1.53073 2.45310 0.47333  0.30424  0.35273  96  GLU A CD  
3599 O OE1 . GLU C 83  ? 1.36669 1.50896 2.47148 0.46096  0.29077  0.36727  96  GLU A OE1 
3600 O OE2 . GLU C 83  ? 1.09600 1.26015 2.17605 0.50680  0.31532  0.33914  96  GLU A OE2 
3601 N N   . SER C 84  ? 0.95642 1.04347 1.96020 0.41058  0.29812  0.27551  97  SER A N   
3602 C CA  . SER C 84  ? 0.99567 1.02878 1.98423 0.39524  0.28630  0.25522  97  SER A CA  
3603 C C   . SER C 84  ? 0.93514 0.99579 1.92230 0.36298  0.28149  0.26517  97  SER A C   
3604 O O   . SER C 84  ? 1.13751 1.15960 2.10485 0.34100  0.26701  0.25224  97  SER A O   
3605 C CB  . SER C 84  ? 0.98273 0.97483 1.93621 0.42136  0.29348  0.21285  97  SER A CB  
3606 O OG  . SER C 84  ? 1.10566 1.14516 2.03754 0.43292  0.31283  0.20785  97  SER A OG  
3607 N N   . ASP C 85  ? 0.82310 0.94784 1.82084 0.35347  0.28825  0.28439  98  ASP A N   
3608 C CA  . ASP C 85  ? 0.93407 1.08538 1.92481 0.31893  0.27761  0.29047  98  ASP A CA  
3609 C C   . ASP C 85  ? 0.79498 0.97609 1.81603 0.29860  0.25827  0.31697  98  ASP A C   
3610 O O   . ASP C 85  ? 0.74637 0.95938 1.76624 0.27272  0.24600  0.32193  98  ASP A O   
3611 C CB  . ASP C 85  ? 0.82861 1.03207 1.82258 0.31958  0.29306  0.29611  98  ASP A CB  
3612 C CG  . ASP C 85  ? 0.95120 1.13869 1.91110 0.34430  0.31375  0.27271  98  ASP A CG  
3613 O OD1 . ASP C 85  ? 1.15003 1.28297 2.07059 0.34635  0.30899  0.24295  98  ASP A OD1 
3614 O OD2 . ASP C 85  ? 0.95699 1.18947 1.92538 0.36093  0.33255  0.28355  98  ASP A OD2 
3615 N N   . SER C 86  ? 0.73626 0.90849 1.77831 0.30980  0.25317  0.33209  99  SER A N   
3616 C CA  . SER C 86  ? 0.70939 0.91487 1.77062 0.29432  0.23443  0.35690  99  SER A CA  
3617 C C   . SER C 86  ? 0.78755 0.96863 1.83774 0.27533  0.21763  0.35561  99  SER A C   
3618 O O   . SER C 86  ? 0.73946 0.87316 1.78791 0.27896  0.21453  0.35632  99  SER A O   
3619 C CB  . SER C 86  ? 0.74274 0.94643 1.82080 0.31185  0.23591  0.37456  99  SER A CB  
3620 O OG  . SER C 86  ? 0.91501 1.14738 2.00122 0.32922  0.25010  0.37679  99  SER A OG  
3621 N N   . ALA C 87  ? 0.67466 0.88575 1.70922 0.25047  0.20378  0.35166  100 ALA A N   
3622 C CA  . ALA C 87  ? 0.63924 0.83314 1.64599 0.22795  0.18582  0.34689  100 ALA A CA  
3623 C C   . ALA C 87  ? 0.59452 0.84369 1.60006 0.20984  0.16712  0.34926  100 ALA A C   
3624 O O   . ALA C 87  ? 0.71691 1.01493 1.75113 0.21411  0.16591  0.35637  100 ALA A O   
3625 C CB  . ALA C 87  ? 0.67915 0.81436 1.64372 0.21879  0.19168  0.31686  100 ALA A CB  
3626 N N   . VAL C 88  ? 0.57913 0.82151 1.55440 0.19058  0.15048  0.34198  101 VAL A N   
3627 C CA  . VAL C 88  ? 0.54243 0.82999 1.51035 0.17504  0.12883  0.33697  101 VAL A CA  
3628 C C   . VAL C 88  ? 0.53615 0.79633 1.46817 0.15653  0.13097  0.30966  101 VAL A C   
3629 O O   . VAL C 88  ? 0.55271 0.76383 1.44998 0.15012  0.13784  0.29600  101 VAL A O   
3630 C CB  . VAL C 88  ? 0.53055 0.84140 1.48876 0.17193  0.10758  0.35062  101 VAL A CB  
3631 C CG1 . VAL C 88  ? 0.49747 0.85972 1.44903 0.16245  0.08167  0.34047  101 VAL A CG1 
3632 C CG2 . VAL C 88  ? 0.54218 0.87900 1.53625 0.19328  0.10925  0.38325  101 VAL A CG2 
3633 N N   . TYR C 89  ? 0.51450 0.80712 1.45920 0.14832  0.12410  0.30257  102 TYR A N   
3634 C CA  . TYR C 89  ? 0.57412 0.84715 1.49279 0.13241  0.12741  0.28226  102 TYR A CA  
3635 C C   . TYR C 89  ? 0.53235 0.82967 1.43910 0.11520  0.09834  0.27192  102 TYR A C   
3636 O O   . TYR C 89  ? 0.46989 0.81534 1.40811 0.11693  0.07703  0.27757  102 TYR A O   
3637 C CB  . TYR C 89  ? 0.58287 0.87156 1.53349 0.13728  0.14499  0.28629  102 TYR A CB  
3638 C CG  . TYR C 89  ? 0.54318 0.81015 1.49895 0.15934  0.17410  0.29234  102 TYR A CG  
3639 C CD1 . TYR C 89  ? 0.58539 0.87467 1.57936 0.17849  0.17948  0.31110  102 TYR A CD1 
3640 C CD2 . TYR C 89  ? 0.61872 0.84539 1.53969 0.16465  0.19483  0.27714  102 TYR A CD2 
3641 C CE1 . TYR C 89  ? 0.58426 0.85288 1.58215 0.20221  0.20427  0.31399  102 TYR A CE1 
3642 C CE2 . TYR C 89  ? 0.70615 0.91498 1.62982 0.19008  0.21834  0.27740  102 TYR A CE2 
3643 C CZ  . TYR C 89  ? 0.60997 0.83812 1.57238 0.20872  0.22272  0.29556  102 TYR A CZ  
3644 O OH  . TYR C 89  ? 0.64744 0.85709 1.61190 0.23735  0.24443  0.29338  102 TYR A OH  
3645 N N   . TYR C 90  ? 0.48687 0.75262 1.34808 0.10125  0.09582  0.25426  103 TYR A N   
3646 C CA  . TYR C 90  ? 0.47549 0.75816 1.31684 0.08763  0.06799  0.24133  103 TYR A CA  
3647 C C   . TYR C 90  ? 0.61858 0.88663 1.44984 0.07310  0.07021  0.22582  103 TYR A C   
3648 O O   . TYR C 90  ? 0.59370 0.82359 1.39620 0.07073  0.09203  0.21897  103 TYR A O   
3649 C CB  . TYR C 90  ? 0.57281 0.83668 1.36855 0.08455  0.06055  0.23773  103 TYR A CB  
3650 C CG  . TYR C 90  ? 0.46619 0.75300 1.27579 0.09810  0.05473  0.25947  103 TYR A CG  
3651 C CD1 . TYR C 90  ? 0.51567 0.77260 1.33392 0.10731  0.07524  0.27416  103 TYR A CD1 
3652 C CD2 . TYR C 90  ? 0.55329 0.89392 1.36883 0.10449  0.02776  0.26573  103 TYR A CD2 
3653 C CE1 . TYR C 90  ? 0.61708 0.89521 1.45413 0.11979  0.07093  0.29993  103 TYR A CE1 
3654 C CE2 . TYR C 90  ? 0.46000 0.82974 1.28916 0.12001  0.02453  0.29148  103 TYR A CE2 
3655 C CZ  . TYR C 90  ? 0.48021 0.81752 1.32227 0.12621  0.04714  0.31122  103 TYR A CZ  
3656 O OH  . TYR C 90  ? 0.66320 1.02966 1.52498 0.14170  0.04490  0.34250  103 TYR A OH  
3657 N N   . CYS C 91  ? 0.44804 0.74778 1.30551 0.06520  0.04615  0.22006  104 CYS A N   
3658 C CA  . CYS C 91  ? 0.43527 0.72240 1.28776 0.04999  0.04230  0.20773  104 CYS A CA  
3659 C C   . CYS C 91  ? 0.52475 0.79835 1.32439 0.04201  0.02216  0.18814  104 CYS A C   
3660 O O   . CYS C 91  ? 0.41934 0.71957 1.21159 0.04695  -0.00441 0.18272  104 CYS A O   
3661 C CB  . CYS C 91  ? 0.42473 0.74870 1.34069 0.04433  0.02202  0.21008  104 CYS A CB  
3662 S SG  . CYS C 91  ? 0.65410 0.96323 1.59326 0.02696  0.02896  0.21077  104 CYS A SG  
3663 N N   . ALA C 92  ? 0.51081 0.74890 1.27236 0.03287  0.03529  0.17857  105 ALA A N   
3664 C CA  . ALA C 92  ? 0.55243 0.77613 1.25944 0.02635  0.01999  0.16082  105 ALA A CA  
3665 C C   . ALA C 92  ? 0.48827 0.69132 1.18122 0.01453  0.02211  0.15022  105 ALA A C   
3666 O O   . ALA C 92  ? 0.53010 0.72290 1.24366 0.01285  0.04505  0.16004  105 ALA A O   
3667 C CB  . ALA C 92  ? 0.52777 0.72415 1.18814 0.03028  0.03646  0.16104  105 ALA A CB  
3668 N N   . LEU C 93  ? 0.42772 0.62907 1.08549 0.00887  -0.00157 0.13248  106 LEU A N   
3669 C CA  . LEU C 93  ? 0.43164 0.61136 1.06934 -0.00106 -0.00146 0.12214  106 LEU A CA  
3670 C C   . LEU C 93  ? 0.51786 0.68489 1.08883 -0.00225 -0.01191 0.10460  106 LEU A C   
3671 O O   . LEU C 93  ? 0.52802 0.71032 1.07679 0.00379  -0.02430 0.10202  106 LEU A O   
3672 C CB  . LEU C 93  ? 0.44971 0.64620 1.13810 -0.00785 -0.02872 0.11805  106 LEU A CB  
3673 C CG  . LEU C 93  ? 0.41808 0.64617 1.12150 -0.00331 -0.07358 0.10055  106 LEU A CG  
3674 C CD1 . LEU C 93  ? 0.43284 0.65563 1.07815 -0.00155 -0.09646 0.07728  106 LEU A CD1 
3675 C CD2 . LEU C 93  ? 0.42007 0.66188 1.19771 -0.01006 -0.09530 0.10012  106 LEU A CD2 
3676 N N   . SER C 94  ? 0.70489 0.84842 1.24639 -0.00904 -0.00611 0.09589  107 SER A N   
3677 C CA  . SER C 94  ? 0.67500 0.80897 1.15487 -0.01051 -0.01741 0.07851  107 SER A CA  
3678 C C   . SER C 94  ? 0.72058 0.84061 1.19454 -0.01698 -0.02461 0.06966  107 SER A C   
3679 O O   . SER C 94  ? 0.68943 0.79562 1.18602 -0.02054 -0.00326 0.08158  107 SER A O   
3680 C CB  . SER C 94  ? 0.67620 0.78697 1.10838 -0.00946 0.00874  0.07817  107 SER A CB  
3681 O OG  . SER C 94  ? 0.85479 0.94134 1.28004 -0.00993 0.03760  0.08078  107 SER A OG  
3682 N N   . LEU C 95  ? 0.63717 0.76424 1.08218 -0.01606 -0.05436 0.05110  108 LEU A N   
3683 C CA  . LEU C 95  ? 0.44393 0.55556 0.88500 -0.02078 -0.06540 0.04163  108 LEU A CA  
3684 C C   . LEU C 95  ? 0.45468 0.53955 0.84251 -0.02302 -0.03717 0.04211  108 LEU A C   
3685 O O   . LEU C 95  ? 0.59322 0.67579 0.92593 -0.02033 -0.03057 0.03402  108 LEU A O   
3686 C CB  . LEU C 95  ? 0.44076 0.56979 0.86332 -0.01421 -0.10791 0.01782  108 LEU A CB  
3687 C CG  . LEU C 95  ? 0.46769 0.63141 0.93646 -0.00612 -0.14145 0.01094  108 LEU A CG  
3688 C CD1 . LEU C 95  ? 0.50921 0.69315 0.95310 0.00654  -0.18480 -0.01731 108 LEU A CD1 
3689 C CD2 . LEU C 95  ? 0.43988 0.59970 0.98975 -0.01423 -0.14386 0.02139  108 LEU A CD2 
3690 N N   . ASN C 96  ? 0.54727 0.61590 0.95554 -0.02711 -0.02085 0.05348  109 ASN A N   
3691 C CA  . ASN C 96  ? 0.56065 0.61052 0.91939 -0.02498 0.00718  0.05468  109 ASN A CA  
3692 C C   . ASN C 96  ? 0.56592 0.60800 0.86974 -0.02429 -0.01148 0.03460  109 ASN A C   
3693 O O   . ASN C 96  ? 0.64933 0.68296 0.89428 -0.02093 0.00451  0.02684  109 ASN A O   
3694 C CB  . ASN C 96  ? 0.49087 0.53561 0.88992 -0.02553 0.03204  0.07906  109 ASN A CB  
3695 C CG  . ASN C 96  ? 0.58895 0.64356 1.02029 -0.02043 0.06218  0.09911  109 ASN A CG  
3696 O OD1 . ASN C 96  ? 0.90252 0.96494 1.34146 -0.01886 0.05924  0.09540  109 ASN A OD1 
3697 N ND2 . ASN C 96  ? 0.53511 0.59321 0.98595 -0.01505 0.09203  0.12261  109 ASN A ND2 
3698 N N   . SER C 97  ? 0.49059 0.53657 0.81321 -0.02560 -0.04685 0.02369  110 SER A N   
3699 C CA  . SER C 97  ? 0.50221 0.54143 0.77605 -0.02193 -0.06632 0.00448  110 SER A CA  
3700 C C   . SER C 97  ? 0.51765 0.57736 0.79153 -0.01553 -0.11060 -0.01764 110 SER A C   
3701 O O   . SER C 97  ? 0.48662 0.54170 0.76903 -0.01177 -0.14079 -0.03244 110 SER A O   
3702 C CB  . SER C 97  ? 0.52481 0.54326 0.82145 -0.02474 -0.06267 0.01420  110 SER A CB  
3703 O OG  . SER C 97  ? 0.63602 0.64674 0.93271 -0.02526 -0.02029 0.03772  110 SER A OG  
3704 N N   . GLY C 98  ? 0.60256 0.68787 0.86760 -0.01123 -0.11568 -0.01993 111 GLY A N   
3705 C CA  . GLY C 98  ? 0.45539 0.57245 0.71667 0.00084  -0.15563 -0.03856 111 GLY A CA  
3706 C C   . GLY C 98  ? 0.66212 0.81168 0.89631 0.00740  -0.15288 -0.03394 111 GLY A C   
3707 O O   . GLY C 98  ? 0.63471 0.78372 0.88941 0.00159  -0.12876 -0.01547 111 GLY A O   
3708 N N   . GLY C 99  ? 0.50193 0.68232 0.69230 0.02118  -0.17743 -0.04833 112 GLY A N   
3709 C CA  . GLY C 99  ? 0.42761 0.64819 0.59999 0.02941  -0.17776 -0.03801 112 GLY A CA  
3710 C C   . GLY C 99  ? 0.52596 0.73129 0.66843 0.01730  -0.14294 -0.02110 112 GLY A C   
3711 O O   . GLY C 99  ? 0.49894 0.67338 0.60966 0.00834  -0.12521 -0.02549 112 GLY A O   
3712 N N   . SER C 100 ? 0.48811 0.71640 0.64452 0.01838  -0.13467 -0.00193 113 SER A N   
3713 C CA  . SER C 100 ? 0.54654 0.76205 0.68464 0.00765  -0.10791 0.01300  113 SER A CA  
3714 C C   . SER C 100 ? 0.52241 0.69269 0.68905 -0.00518 -0.07651 0.01966  113 SER A C   
3715 O O   . SER C 100 ? 0.78879 0.94964 0.99884 -0.00511 -0.07333 0.02271  113 SER A O   
3716 C CB  . SER C 100 ? 0.60808 0.86747 0.75673 0.01500  -0.11318 0.03508  113 SER A CB  
3717 O OG  . SER C 100 ? 0.53497 0.77492 0.68293 0.00217  -0.08889 0.05072  113 SER A OG  
3718 N N   . ASN C 101 ? 0.43212 0.57815 0.57502 -0.01427 -0.05453 0.02084  114 ASN A N   
3719 C CA  . ASN C 101 ? 0.44401 0.55327 0.60852 -0.02064 -0.02565 0.02473  114 ASN A CA  
3720 C C   . ASN C 101 ? 0.58481 0.70087 0.78843 -0.02034 -0.01944 0.04417  114 ASN A C   
3721 O O   . ASN C 101 ? 0.45992 0.60789 0.66723 -0.01773 -0.03319 0.05780  114 ASN A O   
3722 C CB  . ASN C 101 ? 0.57182 0.65385 0.69535 -0.02652 -0.00854 0.01200  114 ASN A CB  
3723 C CG  . ASN C 101 ? 0.60229 0.67373 0.69122 -0.02489 -0.00828 -0.00386 114 ASN A CG  
3724 O OD1 . ASN C 101 ? 0.60636 0.67370 0.71615 -0.02184 -0.00955 -0.00300 114 ASN A OD1 
3725 N ND2 . ASN C 101 ? 0.46662 0.53463 0.50707 -0.02711 -0.00712 -0.01643 114 ASN A ND2 
3726 N N   . ALA C 102 ? 0.62869 0.71776 0.86278 -0.02059 0.00229  0.04778  115 ALA A N   
3727 C CA  . ALA C 102 ? 0.58304 0.67147 0.85807 -0.01854 0.01044  0.06543  115 ALA A CA  
3728 C C   . ALA C 102 ? 0.54517 0.67566 0.85191 -0.01139 -0.00891 0.08304  115 ALA A C   
3729 O O   . ALA C 102 ? 0.63439 0.78282 0.96026 -0.00892 -0.01196 0.10246  115 ALA A O   
3730 C CB  . ALA C 102 ? 0.63661 0.71110 0.90154 -0.02465 0.01580  0.06817  115 ALA A CB  
3731 N N   . LYS C 103 ? 0.44368 0.59207 0.75969 -0.00666 -0.02336 0.07666  116 LYS A N   
3732 C CA  . LYS C 103 ? 0.42114 0.61447 0.76530 0.00407  -0.04635 0.08608  116 LYS A CA  
3733 C C   . LYS C 103 ? 0.46560 0.65494 0.86004 0.00631  -0.04123 0.08925  116 LYS A C   
3734 O O   . LYS C 103 ? 0.66879 0.84748 1.07132 0.00298  -0.04497 0.07705  116 LYS A O   
3735 C CB  . LYS C 103 ? 0.41219 0.63594 0.72673 0.01056  -0.07639 0.07043  116 LYS A CB  
3736 C CG  . LYS C 103 ? 0.40338 0.67995 0.74295 0.02728  -0.10496 0.07325  116 LYS A CG  
3737 C CD  . LYS C 103 ? 0.40075 0.70514 0.70731 0.03797  -0.13710 0.05131  116 LYS A CD  
3738 C CE  . LYS C 103 ? 0.39709 0.75669 0.72890 0.05954  -0.16982 0.04636  116 LYS A CE  
3739 N NZ  . LYS C 103 ? 0.48306 0.86727 0.78369 0.07407  -0.20485 0.01841  116 LYS A NZ  
3740 N N   . LEU C 104 ? 0.52747 0.72688 0.95988 0.01191  -0.03274 0.10830  117 LEU A N   
3741 C CA  . LEU C 104 ? 0.42266 0.62410 0.90628 0.01510  -0.02663 0.11467  117 LEU A CA  
3742 C C   . LEU C 104 ? 0.42090 0.67384 0.93591 0.02757  -0.05386 0.11979  117 LEU A C   
3743 O O   . LEU C 104 ? 0.40690 0.69479 0.91263 0.03795  -0.06621 0.13031  117 LEU A O   
3744 C CB  . LEU C 104 ? 0.43605 0.61324 0.94182 0.01640  0.00231  0.13021  117 LEU A CB  
3745 C CG  . LEU C 104 ? 0.45344 0.58306 0.93579 0.01018  0.02946  0.12096  117 LEU A CG  
3746 C CD1 . LEU C 104 ? 0.66980 0.77897 1.17557 0.01689  0.05193  0.13244  117 LEU A CD1 
3747 C CD2 . LEU C 104 ? 0.52324 0.64323 1.01181 0.00699  0.03710  0.11224  117 LEU A CD2 
3748 N N   . THR C 105 ? 0.54671 0.80864 1.10213 0.02788  -0.06376 0.11356  118 THR A N   
3749 C CA  . THR C 105 ? 0.43783 0.74918 1.03156 0.04119  -0.09110 0.11385  118 THR A CA  
3750 C C   . THR C 105 ? 0.40283 0.71649 1.05012 0.04344  -0.07304 0.13264  118 THR A C   
3751 O O   . THR C 105 ? 0.66301 0.95591 1.34252 0.03439  -0.06022 0.13303  118 THR A O   
3752 C CB  . THR C 105 ? 0.39878 0.72036 1.00671 0.03988  -0.12279 0.08906  118 THR A CB  
3753 O OG1 . THR C 105 ? 0.39846 0.72464 0.95377 0.04323  -0.14241 0.07092  118 THR A OG1 
3754 C CG2 . THR C 105 ? 0.53673 0.90903 1.19296 0.05473  -0.15280 0.08472  118 THR A CG2 
3755 N N   . PHE C 106 ? 0.43590 0.77842 1.09430 0.05695  -0.07104 0.15147  119 PHE A N   
3756 C CA  . PHE C 106 ? 0.40619 0.75217 1.11120 0.06224  -0.05272 0.17116  119 PHE A CA  
3757 C C   . PHE C 106 ? 0.44937 0.84855 1.20235 0.07480  -0.07875 0.16959  119 PHE A C   
3758 O O   . PHE C 106 ? 0.39259 0.83459 1.13783 0.08623  -0.11184 0.15659  119 PHE A O   
3759 C CB  . PHE C 106 ? 0.41421 0.75706 1.11000 0.07046  -0.03417 0.19547  119 PHE A CB  
3760 C CG  . PHE C 106 ? 0.42766 0.71406 1.09137 0.05883  -0.00743 0.19567  119 PHE A CG  
3761 C CD1 . PHE C 106 ? 0.53375 0.78184 1.21433 0.05649  0.02108  0.19933  119 PHE A CD1 
3762 C CD2 . PHE C 106 ? 0.42812 0.70427 1.04560 0.05288  -0.01228 0.19072  119 PHE A CD2 
3763 C CE1 . PHE C 106 ? 0.48772 0.68679 1.13872 0.04995  0.04195  0.19364  119 PHE A CE1 
3764 C CE2 . PHE C 106 ? 0.54761 0.77362 1.13932 0.04267  0.00894  0.18717  119 PHE A CE2 
3765 C CZ  . PHE C 106 ? 0.47102 0.65770 1.07907 0.04198  0.03492  0.18644  119 PHE A CZ  
3766 N N   . GLY C 107 ? 0.45503 0.85506 1.25792 0.07516  -0.06464 0.18140  120 GLY A N   
3767 C CA  . GLY C 107 ? 0.49323 0.94613 1.34692 0.08856  -0.08586 0.18350  120 GLY A CA  
3768 C C   . GLY C 107 ? 0.49093 0.97919 1.34555 0.10949  -0.08171 0.20662  120 GLY A C   
3769 O O   . GLY C 107 ? 0.68051 1.15201 1.50049 0.11214  -0.06514 0.22217  120 GLY A O   
3770 N N   . LYS C 108 ? 0.40028 0.93404 1.28993 0.12338  -0.09688 0.20789  121 LYS A N   
3771 C CA  . LYS C 108 ? 0.41436 0.97624 1.29027 0.14320  -0.09096 0.22776  121 LYS A CA  
3772 C C   . LYS C 108 ? 0.41943 0.95176 1.31959 0.14335  -0.05319 0.25926  121 LYS A C   
3773 O O   . LYS C 108 ? 0.51339 1.05548 1.40181 0.15701  -0.04325 0.28215  121 LYS A O   
3774 C CB  . LYS C 108 ? 0.67421 1.28307 1.56012 0.15741  -0.11558 0.21146  121 LYS A CB  
3775 C CG  . LYS C 108 ? 0.75648 1.39914 1.61511 0.16542  -0.15587 0.17436  121 LYS A CG  
3776 C CD  . LYS C 108 ? 0.82328 1.51527 1.69614 0.18297  -0.18036 0.15398  121 LYS A CD  
3777 C CE  . LYS C 108 ? 0.95201 1.67621 1.81098 0.20659  -0.17165 0.17321  121 LYS A CE  
3778 N NZ  . LYS C 108 ? 1.16630 1.94076 2.04212 0.22613  -0.19637 0.14986  121 LYS A NZ  
3779 N N   . GLY C 109 ? 0.41400 0.91103 1.34678 0.13060  -0.03183 0.26058  122 GLY A N   
3780 C CA  . GLY C 109 ? 0.42934 0.89263 1.37378 0.13406  0.00344  0.28183  122 GLY A CA  
3781 C C   . GLY C 109 ? 0.43960 0.92710 1.42314 0.14388  0.00825  0.29154  122 GLY A C   
3782 O O   . GLY C 109 ? 0.44592 0.97493 1.42919 0.15206  -0.01401 0.28621  122 GLY A O   
3783 N N   . THR C 110 ? 0.44801 0.90770 1.45637 0.14438  0.03816  0.30232  123 THR A N   
3784 C CA  . THR C 110 ? 0.46372 0.93998 1.50169 0.15264  0.04708  0.31224  123 THR A CA  
3785 C C   . THR C 110 ? 0.48458 0.93293 1.52502 0.16843  0.07766  0.33320  123 THR A C   
3786 O O   . THR C 110 ? 0.48879 0.89666 1.52763 0.16890  0.10159  0.33324  123 THR A O   
3787 C CB  . THR C 110 ? 0.51275 0.98861 1.58192 0.13961  0.05232  0.30476  123 THR A CB  
3788 O OG1 . THR C 110 ? 0.44504 0.93829 1.51681 0.12393  0.02128  0.28374  123 THR A OG1 
3789 C CG2 . THR C 110 ? 0.47665 0.97754 1.57764 0.14805  0.05859  0.31641  123 THR A CG2 
3790 N N   . LYS C 111 ? 0.50158 0.97114 1.54563 0.18352  0.07593  0.34853  124 LYS A N   
3791 C CA  . LYS C 111 ? 0.52735 0.96955 1.57771 0.20007  0.10133  0.36845  124 LYS A CA  
3792 C C   . LYS C 111 ? 0.54230 0.98484 1.61900 0.20733  0.12069  0.37152  124 LYS A C   
3793 O O   . LYS C 111 ? 0.53847 1.01963 1.63347 0.20428  0.10983  0.36881  124 LYS A O   
3794 C CB  . LYS C 111 ? 0.54235 1.00873 1.58533 0.21369  0.09204  0.38760  124 LYS A CB  
3795 C CG  . LYS C 111 ? 0.57338 1.00596 1.62653 0.22988  0.11536  0.40987  124 LYS A CG  
3796 C CD  . LYS C 111 ? 0.58981 1.05067 1.63819 0.24217  0.10689  0.43365  124 LYS A CD  
3797 C CE  . LYS C 111 ? 0.89864 1.31907 1.96268 0.25606  0.12820  0.45714  124 LYS A CE  
3798 N NZ  . LYS C 111 ? 0.85996 1.26322 1.94494 0.26790  0.14763  0.45382  124 LYS A NZ  
3799 N N   . LEU C 112 ? 0.56306 0.96361 1.64166 0.21869  0.14810  0.37563  125 LEU A N   
3800 C CA  . LEU C 112 ? 0.58321 0.98440 1.67997 0.23074  0.16955  0.37928  125 LEU A CA  
3801 C C   . LEU C 112 ? 0.69037 1.07009 1.78989 0.25408  0.18446  0.39347  125 LEU A C   
3802 O O   . LEU C 112 ? 0.70208 1.03554 1.79012 0.26125  0.19190  0.39282  125 LEU A O   
3803 C CB  . LEU C 112 ? 0.63532 1.00926 1.72653 0.22870  0.18951  0.36606  125 LEU A CB  
3804 C CG  . LEU C 112 ? 0.72312 1.10150 1.82623 0.24574  0.21440  0.37090  125 LEU A CG  
3805 C CD1 . LEU C 112 ? 0.60206 1.03422 1.73422 0.23863  0.20560  0.38203  125 LEU A CD1 
3806 C CD2 . LEU C 112 ? 0.61488 0.97067 1.70340 0.24784  0.23470  0.35795  125 LEU A CD2 
3807 N N   . SER C 113 ? 0.68776 1.09931 1.80516 0.26553  0.18707  0.40556  126 SER A N   
3808 C CA  . SER C 113 ? 0.81658 1.21135 1.93978 0.28927  0.20135  0.41920  126 SER A CA  
3809 C C   . SER C 113 ? 0.73695 1.14201 1.87263 0.30393  0.22116  0.41849  126 SER A C   
3810 O O   . SER C 113 ? 0.82240 1.27543 1.97579 0.29886  0.21601  0.42341  126 SER A O   
3811 C CB  . SER C 113 ? 0.80663 1.23682 1.93666 0.29386  0.18609  0.43788  126 SER A CB  
3812 O OG  . SER C 113 ? 1.02450 1.45242 2.13956 0.28359  0.16907  0.44184  126 SER A OG  
3813 N N   . VAL C 114 ? 0.72396 1.08562 1.85034 0.32328  0.24195  0.41102  127 VAL A N   
3814 C CA  . VAL C 114 ? 0.79774 1.17014 1.92834 0.34244  0.26262  0.40887  127 VAL A CA  
3815 C C   . VAL C 114 ? 0.86256 1.22211 1.99861 0.37028  0.27097  0.41769  127 VAL A C   
3816 O O   . VAL C 114 ? 1.04702 1.35275 2.17227 0.38412  0.27436  0.40970  127 VAL A O   
3817 C CB  . VAL C 114 ? 0.89195 1.23095 2.00050 0.34910  0.27910  0.38790  127 VAL A CB  
3818 C CG1 . VAL C 114 ? 0.92225 1.28414 2.03153 0.37259  0.30061  0.38847  127 VAL A CG1 
3819 C CG2 . VAL C 114 ? 0.77849 1.12784 1.88240 0.32105  0.27059  0.38093  127 VAL A CG2 
3820 N N   . LYS C 115 ? 0.86014 1.26725 2.01530 0.37815  0.27253  0.43326  128 LYS A N   
3821 C CA  . LYS C 115 ? 0.83950 1.24098 2.00107 0.40644  0.28139  0.44247  128 LYS A CA  
3822 C C   . LYS C 115 ? 1.01538 1.41716 2.17042 0.43269  0.30315  0.43297  128 LYS A C   
3823 O O   . LYS C 115 ? 1.04464 1.48474 2.20366 0.42705  0.31078  0.43368  128 LYS A O   
3824 C CB  . LYS C 115 ? 0.88928 1.34567 2.07282 0.40375  0.27061  0.46397  128 LYS A CB  
3825 N N   . SER C 116 ? 1.51811 1.86293 1.60856 0.17084  0.19465  -0.05465 129 SER A N   
3826 C CA  . SER C 116 ? 1.54961 1.86959 1.63308 0.17756  0.21675  -0.04316 129 SER A CA  
3827 C C   . SER C 116 ? 1.48921 1.82805 1.62419 0.16650  0.23357  -0.04123 129 SER A C   
3828 O O   . SER C 116 ? 1.47179 1.85833 1.64993 0.15042  0.22069  -0.04432 129 SER A O   
3829 C CB  . SER C 116 ? 1.38932 1.70559 1.44235 0.18642  0.21005  -0.03478 129 SER A CB  
3830 O OG  . SER C 116 ? 1.37094 1.64065 1.39422 0.19306  0.23763  -0.02365 129 SER A OG  
3831 N N   . HIS C 117 ? 1.43202 1.73858 1.56246 0.17256  0.26172  -0.03135 130 HIS A N   
3832 C CA  . HIS C 117 ? 1.35257 1.68430 1.53524 0.16374  0.28028  -0.02024 130 HIS A CA  
3833 C C   . HIS C 117 ? 1.37321 1.73427 1.58171 0.17840  0.29009  -0.00064 130 HIS A C   
3834 O O   . HIS C 117 ? 1.31020 1.73629 1.57934 0.16811  0.28500  0.01265  130 HIS A O   
3835 C CB  . HIS C 117 ? 1.43824 1.72368 1.60700 0.16756  0.30972  -0.01479 130 HIS A CB  
3836 C CG  . HIS C 117 ? 1.43615 1.74170 1.64704 0.14293  0.31759  -0.01313 130 HIS A CG  
3837 N ND1 . HIS C 117 ? 1.35965 1.62120 1.54727 0.13295  0.32860  -0.02321 130 HIS A ND1 
3838 C CD2 . HIS C 117 ? 1.43672 1.80345 1.70785 0.12196  0.31577  0.00178  130 HIS A CD2 
3839 C CE1 . HIS C 117 ? 1.34503 1.63002 1.56797 0.10296  0.33265  -0.01933 130 HIS A CE1 
3840 N NE2 . HIS C 117 ? 1.40275 1.75813 1.67914 0.09327  0.32252  -0.00196 130 HIS A NE2 
3841 N N   . ILE C 118 ? 1.30590 1.61647 1.46287 0.20044  0.30672  0.00519  131 ILE A N   
3842 C CA  . ILE C 118 ? 1.20461 1.51600 1.36443 0.22080  0.32773  0.02476  131 ILE A CA  
3843 C C   . ILE C 118 ? 1.20997 1.55990 1.43778 0.22919  0.35954  0.05423  131 ILE A C   
3844 O O   . ILE C 118 ? 1.18246 1.60480 1.47476 0.23052  0.35696  0.07505  131 ILE A O   
3845 C CB  . ILE C 118 ? 1.16803 1.52503 1.34182 0.21955  0.29976  0.02113  131 ILE A CB  
3846 N N   . PRO C 121 ? 1.56845 2.16132 1.99651 0.34723  0.43133  0.21473  134 PRO A N   
3847 C CA  . PRO C 121 ? 1.76257 2.22666 2.10011 0.38246  0.49041  0.21767  134 PRO A CA  
3848 C C   . PRO C 121 ? 1.76578 2.16175 2.03946 0.41672  0.52496  0.22781  134 PRO A C   
3849 O O   . PRO C 121 ? 1.48078 1.90882 1.80257 0.45728  0.57283  0.27996  134 PRO A O   
3850 C CB  . PRO C 121 ? 1.64324 2.02073 1.88966 0.35171  0.46098  0.16285  134 PRO A CB  
3851 N N   . ASP C 122 ? 1.86233 2.16614 2.02695 0.39994  0.50300  0.18324  135 ASP A N   
3852 C CA  . ASP C 122 ? 1.80305 2.02438 1.88391 0.42165  0.53101  0.18533  135 ASP A CA  
3853 C C   . ASP C 122 ? 1.85857 2.09869 1.91103 0.38780  0.46593  0.14583  135 ASP A C   
3854 O O   . ASP C 122 ? 1.83567 1.98032 1.77367 0.36513  0.45102  0.11200  135 ASP A O   
3855 C CB  . ASP C 122 ? 1.85664 1.90691 1.79307 0.43253  0.58601  0.17719  135 ASP A CB  
3856 N N   . PRO C 123 ? 1.86538 2.23141 2.01865 0.38028  0.42522  0.15296  136 PRO A N   
3857 C CA  . PRO C 123 ? 1.63661 2.02106 1.76527 0.35385  0.36891  0.11983  136 PRO A CA  
3858 C C   . PRO C 123 ? 1.63435 1.94648 1.68774 0.37553  0.39671  0.12656  136 PRO A C   
3859 O O   . PRO C 123 ? 1.82493 2.08697 1.86143 0.41576  0.46206  0.16195  136 PRO A O   
3860 C CB  . PRO C 123 ? 1.46102 1.99589 1.71832 0.34008  0.32714  0.13158  136 PRO A CB  
3861 C CG  . PRO C 123 ? 1.71387 2.30872 2.05554 0.34599  0.35086  0.16496  136 PRO A CG  
3862 C CD  . PRO C 123 ? 1.82722 2.33047 2.12001 0.38808  0.42426  0.19356  136 PRO A CD  
3863 N N   . ALA C 124 ? 1.38910 1.69161 1.39267 0.34943  0.34978  0.09458  137 ALA A N   
3864 C CA  . ALA C 124 ? 1.34280 1.56826 1.25993 0.36059  0.36953  0.09536  137 ALA A CA  
3865 C C   . ALA C 124 ? 1.40649 1.69272 1.33465 0.33309  0.30396  0.06982  137 ALA A C   
3866 O O   . ALA C 124 ? 1.58464 1.88342 1.49285 0.29759  0.25272  0.03921  137 ALA A O   
3867 C CB  . ALA C 124 ? 1.50759 1.56747 1.26328 0.34928  0.40234  0.08021  137 ALA A CB  
3868 N N   . VAL C 125 ? 1.25708 1.58241 1.21858 0.35269  0.30909  0.08688  138 VAL A N   
3869 C CA  . VAL C 125 ? 1.24587 1.62539 1.21608 0.33085  0.25238  0.06589  138 VAL A CA  
3870 C C   . VAL C 125 ? 1.42644 1.70769 1.29222 0.34141  0.28016  0.06810  138 VAL A C   
3871 O O   . VAL C 125 ? 1.39651 1.65283 1.26901 0.38173  0.33718  0.10180  138 VAL A O   
3872 C CB  . VAL C 125 ? 1.10223 1.63272 1.21412 0.33637  0.22409  0.08337  138 VAL A CB  
3873 C CG1 . VAL C 125 ? 1.06595 1.64528 1.17976 0.31133  0.16418  0.05744  138 VAL A CG1 
3874 C CG2 . VAL C 125 ? 1.03278 1.64241 1.23249 0.32182  0.20687  0.08534  138 VAL A CG2 
3875 N N   . TYR C 126 ? 1.31661 1.54235 1.08412 0.30515  0.24278  0.03719  139 TYR A N   
3876 C CA  . TYR C 126 ? 1.54466 1.66296 1.19011 0.30173  0.26356  0.03476  139 TYR A CA  
3877 C C   . TYR C 126 ? 1.52922 1.71811 1.19550 0.28149  0.20399  0.01899  139 TYR A C   
3878 O O   . TYR C 126 ? 1.55740 1.84587 1.29157 0.25916  0.14305  0.00226  139 TYR A O   
3879 C CB  . TYR C 126 ? 1.90442 1.87693 1.38596 0.26536  0.27450  0.01779  139 TYR A CB  
3880 C CG  . TYR C 126 ? 1.83169 1.73115 1.28395 0.27808  0.32644  0.02819  139 TYR A CG  
3881 C CD1 . TYR C 126 ? 1.60838 1.54432 1.08812 0.25525  0.29605  0.01628  139 TYR A CD1 
3882 C CD2 . TYR C 126 ? 1.89145 1.68144 1.28645 0.31624  0.41067  0.05271  139 TYR A CD2 
3883 C CE1 . TYR C 126 ? 1.66421 1.53438 1.11744 0.26611  0.34250  0.02545  139 TYR A CE1 
3884 C CE2 . TYR C 126 ? 1.95773 1.67869 1.32456 0.32961  0.46084  0.06357  139 TYR A CE2 
3885 C CZ  . TYR C 126 ? 1.91016 1.67379 1.30714 0.30234  0.42361  0.04827  139 TYR A CZ  
3886 O OH  . TYR C 126 ? 2.02408 1.72014 1.39335 0.31477  0.47237  0.05865  139 TYR A OH  
3887 N N   . GLN C 127 ? 1.52842 1.65661 1.12942 0.29118  0.22685  0.02559  140 GLN A N   
3888 C CA  . GLN C 127 ? 1.41441 1.59217 1.01719 0.27187  0.17581  0.01176  140 GLN A CA  
3889 C C   . GLN C 127 ? 1.56138 1.60618 0.99130 0.23220  0.17366  -0.00398 140 GLN A C   
3890 O O   . GLN C 127 ? 1.84058 1.73926 1.14828 0.23823  0.23523  0.00440  140 GLN A O   
3891 C CB  . GLN C 127 ? 1.31230 1.54927 0.99521 0.31330  0.19832  0.03648  140 GLN A CB  
3892 N N   . LEU C 128 ? 1.40694 1.49945 0.82107 0.18942  0.10525  -0.02318 141 LEU A N   
3893 C CA  . LEU C 128 ? 1.51075 1.50193 0.76666 0.13782  0.08835  -0.03330 141 LEU A CA  
3894 C C   . LEU C 128 ? 1.68102 1.75254 0.96086 0.11794  0.02817  -0.04122 141 LEU A C   
3895 O O   . LEU C 128 ? 1.75803 1.96834 1.17153 0.13287  -0.01360 -0.04440 141 LEU A O   
3896 C CB  . LEU C 128 ? 1.60234 1.56569 0.79413 0.09278  0.06393  -0.03836 141 LEU A CB  
3897 C CG  . LEU C 128 ? 1.54594 1.62040 0.85070 0.09661  0.03017  -0.03971 141 LEU A CG  
3898 C CD1 . LEU C 128 ? 1.55546 1.60864 0.77246 0.04088  -0.00774 -0.03757 141 LEU A CD1 
3899 C CD2 . LEU C 128 ? 1.43058 1.48859 0.79093 0.13524  0.08251  -0.03331 141 LEU A CD2 
3900 N N   . ARG C 129 ? 1.48577 1.58078 1.31449 0.30764  -0.03369 0.17797  142 ARG A N   
3901 C CA  . ARG C 129 ? 1.68301 1.72269 1.43768 0.28305  -0.03954 0.22175  142 ARG A CA  
3902 C C   . ARG C 129 ? 1.72000 1.78118 1.52884 0.28825  -0.00848 0.20316  142 ARG A C   
3903 O O   . ARG C 129 ? 1.77099 1.87696 1.70043 0.31097  -0.00398 0.16727  142 ARG A O   
3904 C CB  . ARG C 129 ? 1.58093 1.55344 1.34219 0.26281  -0.11063 0.27438  142 ARG A CB  
3905 N N   . ASP C 130 ? 1.71724 1.75498 1.43905 0.26147  0.01660  0.21983  143 ASP A N   
3906 C CA  . ASP C 130 ? 1.82241 1.88287 1.58726 0.25976  0.05028  0.19907  143 ASP A CA  
3907 C C   . ASP C 130 ? 2.01961 2.03477 1.68144 0.20837  0.06101  0.22989  143 ASP A C   
3908 O O   . ASP C 130 ? 1.96383 1.98429 1.51779 0.18773  0.08653  0.22559  143 ASP A O   
3909 C CB  . ASP C 130 ? 1.63876 1.77674 1.41984 0.29121  0.10463  0.14055  143 ASP A CB  
3910 C CG  . ASP C 130 ? 1.72030 1.89526 1.55494 0.29152  0.14027  0.11086  143 ASP A CG  
3911 O OD1 . ASP C 130 ? 1.77016 1.91211 1.65422 0.27158  0.12328  0.13142  143 ASP A OD1 
3912 O OD2 . ASP C 130 ? 1.64452 1.87707 1.47272 0.31149  0.18044  0.06663  143 ASP A OD2 
3913 N N   . SER C 131 ? 2.02711 1.99730 1.72303 0.18202  0.04151  0.25633  144 SER A N   
3914 C CA  . SER C 131 ? 1.91352 1.84999 1.52120 0.12152  0.06459  0.27463  144 SER A CA  
3915 C C   . SER C 131 ? 2.00116 1.88369 1.45413 0.06139  0.05006  0.31911  144 SER A C   
3916 O O   . SER C 131 ? 1.83625 1.72021 1.19227 0.00266  0.08981  0.31366  144 SER A O   
3917 C CB  . SER C 131 ? 1.84728 1.86999 1.45898 0.12934  0.14130  0.20818  144 SER A CB  
3918 O OG  . SER C 131 ? 1.91224 1.98128 1.45023 0.13770  0.17342  0.17614  144 SER A OG  
3919 N N   . LYS C 132 ? 2.15600 2.00025 1.58263 0.06813  -0.00262 0.35587  145 LYS A N   
3920 C CA  . LYS C 132 ? 2.23436 2.03184 1.50956 0.00542  -0.01797 0.39701  145 LYS A CA  
3921 C C   . LYS C 132 ? 2.35365 2.05311 1.61965 -0.01192 -0.11230 0.47273  145 LYS A C   
3922 O O   . LYS C 132 ? 2.55392 2.17616 1.69533 -0.08584 -0.14547 0.53123  145 LYS A O   
3923 C CB  . LYS C 132 ? 2.14757 2.00574 1.37726 0.02758  0.01544  0.35702  145 LYS A CB  
3924 N N   . SER C 133 ? 2.29411 1.99958 1.69386 0.05243  -0.15811 0.46711  146 SER A N   
3925 C CA  . SER C 133 ? 2.25061 1.87656 1.68817 0.05546  -0.25810 0.52278  146 SER A CA  
3926 C C   . SER C 133 ? 2.23589 1.82140 1.53287 0.01127  -0.29472 0.56870  146 SER A C   
3927 O O   . SER C 133 ? 2.15586 1.80169 1.38860 0.01214  -0.24553 0.53629  146 SER A O   
3928 C CB  . SER C 133 ? 2.10672 1.63412 1.56719 0.02462  -0.31305 0.57368  146 SER A CB  
3929 N N   . LYS C 136 ? 1.93098 1.78564 1.00560 0.02817  -0.03104 0.37211  149 LYS A N   
3930 C CA  . LYS C 136 ? 1.97563 1.82821 1.04706 0.04904  -0.06230 0.37688  149 LYS A CA  
3931 C C   . LYS C 136 ? 2.04068 1.91069 1.24922 0.11462  -0.08628 0.36315  149 LYS A C   
3932 O O   . LYS C 136 ? 2.00094 1.87877 1.30694 0.14045  -0.08746 0.35666  149 LYS A O   
3933 C CB  . LYS C 136 ? 1.77740 1.67414 0.78602 0.05002  -0.00987 0.32555  149 LYS A CB  
3934 C CG  . LYS C 136 ? 1.54201 1.49083 0.62105 0.10661  0.04047  0.26306  149 LYS A CG  
3935 C CD  . LYS C 136 ? 1.50733 1.48980 0.52416 0.09912  0.08888  0.20834  149 LYS A CD  
3936 C CE  . LYS C 136 ? 1.57951 1.58762 0.54520 0.04885  0.12902  0.18626  149 LYS A CE  
3937 N NZ  . LYS C 136 ? 1.57431 1.62987 0.50535 0.04427  0.17565  0.11440  149 LYS A NZ  
3938 N N   . SER C 137 ? 1.88869 1.77072 1.10472 0.13435  -0.10153 0.35215  150 SER A N   
3939 C CA  . SER C 137 ? 1.80596 1.71771 1.14083 0.18212  -0.11581 0.32692  150 SER A CA  
3940 C C   . SER C 137 ? 1.78875 1.73636 1.10266 0.20367  -0.06939 0.28000  150 SER A C   
3941 O O   . SER C 137 ? 1.83346 1.77042 1.05565 0.18503  -0.05838 0.27727  150 SER A O   
3942 C CB  . SER C 137 ? 1.74392 1.63393 1.11953 0.17942  -0.18786 0.35469  150 SER A CB  
3943 O OG  . SER C 137 ? 1.78701 1.67093 1.07259 0.15752  -0.19367 0.35957  150 SER A OG  
3944 N N   . VAL C 138 ? 1.51289 1.49779 0.90752 0.23805  -0.04552 0.24331  151 VAL A N   
3945 C CA  . VAL C 138 ? 1.45116 1.45314 0.81905 0.25445  -0.01006 0.20567  151 VAL A CA  
3946 C C   . VAL C 138 ? 1.35726 1.38503 0.79546 0.26186  -0.02454 0.18561  151 VAL A C   
3947 O O   . VAL C 138 ? 1.48338 1.54456 1.03018 0.27228  -0.03779 0.17402  151 VAL A O   
3948 C CB  . VAL C 138 ? 1.35811 1.38149 0.73705 0.27714  0.03113  0.17715  151 VAL A CB  
3949 C CG1 . VAL C 138 ? 1.31661 1.33662 0.65711 0.29225  0.05150  0.14721  151 VAL A CG1 
3950 C CG2 . VAL C 138 ? 1.27626 1.29065 0.59892 0.26375  0.05037  0.18230  151 VAL A CG2 
3951 N N   . CYS C 139 ? 1.36664 1.38293 0.74763 0.25172  -0.01957 0.17396  152 CYS A N   
3952 C CA  . CYS C 139 ? 1.39303 1.43831 0.82377 0.24435  -0.02527 0.14683  152 CYS A CA  
3953 C C   . CYS C 139 ? 1.46687 1.49973 0.83672 0.24060  0.00951  0.12188  152 CYS A C   
3954 O O   . CYS C 139 ? 1.63626 1.62308 0.91429 0.24499  0.02317  0.12871  152 CYS A O   
3955 C CB  . CYS C 139 ? 1.46807 1.50544 0.88323 0.22387  -0.05926 0.15703  152 CYS A CB  
3956 S SG  . CYS C 139 ? 1.62557 1.65568 1.09505 0.22392  -0.12168 0.19777  152 CYS A SG  
3957 N N   . LEU C 140 ? 1.41869 1.49140 0.84145 0.22844  0.02029  0.08936  153 LEU A N   
3958 C CA  . LEU C 140 ? 1.37043 1.42370 0.72739 0.21379  0.04657  0.07154  153 LEU A CA  
3959 C C   . LEU C 140 ? 1.51276 1.57557 0.85368 0.17085  0.04898  0.04741  153 LEU A C   
3960 O O   . LEU C 140 ? 1.57033 1.70297 1.00994 0.15407  0.04537  0.01499  153 LEU A O   
3961 C CB  . LEU C 140 ? 1.40773 1.50539 0.82223 0.22085  0.06544  0.05024  153 LEU A CB  
3962 C CG  . LEU C 140 ? 1.40746 1.46271 0.73321 0.22137  0.08028  0.05149  153 LEU A CG  
3963 C CD1 . LEU C 140 ? 1.55512 1.55176 0.81903 0.25823  0.07246  0.07629  153 LEU A CD1 
3964 C CD2 . LEU C 140 ? 1.27752 1.39137 0.66576 0.22124  0.09743  0.02700  153 LEU A CD2 
3965 N N   . PHE C 141 ? 1.59510 1.58950 0.82004 0.15161  0.05421  0.05631  154 PHE A N   
3966 C CA  . PHE C 141 ? 1.69941 1.69027 0.88756 0.10207  0.05976  0.03507  154 PHE A CA  
3967 C C   . PHE C 141 ? 1.78308 1.72944 0.88072 0.06443  0.07887  0.02750  154 PHE A C   
3968 O O   . PHE C 141 ? 1.88514 1.74299 0.88550 0.07890  0.07149  0.05420  154 PHE A O   
3969 C CB  . PHE C 141 ? 1.67804 1.61358 0.79605 0.10026  0.04542  0.05378  154 PHE A CB  
3970 C CG  . PHE C 141 ? 1.56247 1.53261 0.74294 0.12391  0.02002  0.06760  154 PHE A CG  
3971 C CD1 . PHE C 141 ? 1.58881 1.54443 0.77068 0.16147  0.01064  0.09682  154 PHE A CD1 
3972 C CD2 . PHE C 141 ? 1.67837 1.69401 0.91003 0.10258  0.00218  0.05022  154 PHE A CD2 
3973 C CE1 . PHE C 141 ? 1.50629 1.48056 0.72181 0.16968  -0.01742 0.11726  154 PHE A CE1 
3974 C CE2 . PHE C 141 ? 1.55084 1.58536 0.82689 0.12088  -0.03400 0.07087  154 PHE A CE2 
3975 C CZ  . PHE C 141 ? 1.33691 1.34448 0.59536 0.15061  -0.04453 0.10900  154 PHE A CZ  
3976 N N   . THR C 142 ? 1.74011 1.55180 1.18164 0.32666  0.04669  0.03060  155 THR A N   
3977 C CA  . THR C 142 ? 1.79388 1.57456 1.19705 0.29876  0.04277  0.02189  155 THR A CA  
3978 C C   . THR C 142 ? 2.03406 1.88577 1.51429 0.31670  0.04230  0.03378  155 THR A C   
3979 O O   . THR C 142 ? 1.98003 1.79325 1.43017 0.30839  0.06558  0.03355  155 THR A O   
3980 C CB  . THR C 142 ? 1.76048 1.41803 1.05527 0.28447  0.09884  0.01545  155 THR A CB  
3981 O OG1 . THR C 142 ? 1.92140 1.56753 1.24591 0.32701  0.16125  0.03462  155 THR A OG1 
3982 C CG2 . THR C 142 ? 1.66818 1.24954 0.88515 0.26560  0.11372  0.00274  155 THR A CG2 
3983 N N   . ASP C 143 ? 2.15955 2.11099 1.73065 0.33419  0.01748  0.04257  156 ASP A N   
3984 C CA  . ASP C 143 ? 2.01731 2.04370 1.66273 0.34479  0.02160  0.05416  156 ASP A CA  
3985 C C   . ASP C 143 ? 1.84233 1.86568 1.48175 0.31519  0.00108  0.04020  156 ASP A C   
3986 O O   . ASP C 143 ? 1.73902 1.75805 1.36510 0.29341  -0.03495 0.02803  156 ASP A O   
3987 C CB  . ASP C 143 ? 1.84248 1.97523 1.56832 0.35543  -0.00532 0.06458  156 ASP A CB  
3988 C CG  . ASP C 143 ? 1.72856 1.87113 1.46421 0.39006  0.01348  0.08765  156 ASP A CG  
3989 O OD1 . ASP C 143 ? 1.80088 1.91318 1.53399 0.42145  0.06364  0.11034  156 ASP A OD1 
3990 O OD2 . ASP C 143 ? 1.58238 1.75608 1.32655 0.38796  -0.01566 0.08552  156 ASP A OD2 
3991 N N   . PHE C 144 ? 1.78725 1.81225 1.44149 0.31774  0.02987  0.04658  157 PHE A N   
3992 C CA  . PHE C 144 ? 1.72996 1.75354 1.38421 0.29315  0.01720  0.03716  157 PHE A CA  
3993 C C   . PHE C 144 ? 1.70628 1.81493 1.43276 0.28125  -0.01153 0.03100  157 PHE A C   
3994 O O   . PHE C 144 ? 1.83753 1.93364 1.55767 0.26089  -0.02911 0.02085  157 PHE A O   
3995 C CB  . PHE C 144 ? 1.63928 1.63679 1.28767 0.29695  0.06233  0.04434  157 PHE A CB  
3996 N N   . ASP C 145 ? 1.65052 1.84271 1.44091 0.29153  -0.01335 0.03989  158 ASP A N   
3997 C CA  . ASP C 145 ? 1.65992 1.92823 1.50110 0.26770  -0.03874 0.03037  158 ASP A CA  
3998 C C   . ASP C 145 ? 1.37615 1.73041 1.26324 0.27883  -0.05293 0.04589  158 ASP A C   
3999 O O   . ASP C 145 ? 1.20951 1.62974 1.14674 0.29568  -0.03736 0.07171  158 ASP A O   
4000 C CB  . ASP C 145 ? 1.65345 1.95360 1.52865 0.24426  -0.02228 0.02615  158 ASP A CB  
4001 C CG  . ASP C 145 ? 1.59615 1.88551 1.46570 0.20754  -0.03448 0.00216  158 ASP A CG  
4002 O OD1 . ASP C 145 ? 1.53366 1.79840 1.38218 0.20416  -0.05478 -0.00807 158 ASP A OD1 
4003 O OD2 . ASP C 145 ? 1.63279 1.93157 1.51874 0.18218  -0.01632 -0.00582 158 ASP A OD2 
4004 N N   . SER C 153 ? 1.22141 1.56815 0.91146 0.19093  -0.19115 -0.02541 166 SER A N   
4005 C CA  . SER C 153 ? 1.46826 1.90206 1.16160 0.19464  -0.21344 0.00729  166 SER A CA  
4006 C C   . SER C 153 ? 1.44292 1.90158 1.08795 0.15336  -0.22782 0.00174  166 SER A C   
4007 O O   . SER C 153 ? 1.41212 1.80230 1.01624 0.13123  -0.21190 -0.02815 166 SER A O   
4008 C CB  . SER C 153 ? 1.52039 1.95213 1.22400 0.25124  -0.20828 0.04348  166 SER A CB  
4009 O OG  . SER C 153 ? 1.40481 1.92967 1.12667 0.26517  -0.22577 0.08810  166 SER A OG  
4010 N N   . LYS C 154 ? 1.45267 2.01337 1.10270 0.14134  -0.25680 0.03449  167 LYS A N   
4011 C CA  . LYS C 154 ? 1.54727 2.14313 1.13842 0.09225  -0.27771 0.03407  167 LYS A CA  
4012 C C   . LYS C 154 ? 1.49743 2.07480 1.05419 0.12472  -0.27973 0.05994  167 LYS A C   
4013 O O   . LYS C 154 ? 1.44202 2.01077 0.93032 0.08367  -0.28789 0.05035  167 LYS A O   
4014 C CB  . LYS C 154 ? 1.43790 2.17125 1.05009 0.05735  -0.31617 0.06586  167 LYS A CB  
4015 N N   . ASP C 155 ? 1.28491 1.84455 0.87687 0.19293  -0.26661 0.09050  168 ASP A N   
4016 C CA  . ASP C 155 ? 1.33429 1.86911 0.89256 0.22676  -0.26122 0.11832  168 ASP A CA  
4017 C C   . ASP C 155 ? 1.17450 1.59123 0.68296 0.21577  -0.23292 0.07396  168 ASP A C   
4018 O O   . ASP C 155 ? 1.13639 1.48626 0.66193 0.21176  -0.21108 0.03580  168 ASP A O   
4019 C CB  . ASP C 155 ? 1.21849 1.75464 0.82274 0.29990  -0.24282 0.16315  168 ASP A CB  
4020 C CG  . ASP C 155 ? 1.26599 1.90953 0.92857 0.31518  -0.25765 0.22380  168 ASP A CG  
4021 O OD1 . ASP C 155 ? 1.39851 2.11865 1.10983 0.28945  -0.27526 0.22641  168 ASP A OD1 
4022 O OD2 . ASP C 155 ? 1.19182 1.83842 0.85709 0.35105  -0.24646 0.26890  168 ASP A OD2 
4023 N N   . SER C 156 ? 1.10733 1.50532 0.55783 0.21164  -0.23311 0.08488  169 SER A N   
4024 C CA  . SER C 156 ? 1.12774 1.42033 0.53418 0.20119  -0.20242 0.04801  169 SER A CA  
4025 C C   . SER C 156 ? 1.17702 1.40395 0.60416 0.25400  -0.17363 0.05550  169 SER A C   
4026 O O   . SER C 156 ? 1.23621 1.48579 0.68557 0.30067  -0.17206 0.09537  169 SER A O   
4027 C CB  . SER C 156 ? 1.20876 1.49766 0.53392 0.17173  -0.20925 0.05544  169 SER A CB  
4028 O OG  . SER C 156 ? 1.23814 1.56623 0.55385 0.21506  -0.22058 0.11274  169 SER A OG  
4029 N N   . ASP C 157 ? 1.28512 1.42801 0.70433 0.24282  -0.14556 0.01766  170 ASP A N   
4030 C CA  . ASP C 157 ? 1.23762 1.31478 0.66826 0.27408  -0.11837 0.01588  170 ASP A CA  
4031 C C   . ASP C 157 ? 1.15450 1.24324 0.63252 0.30116  -0.11932 0.02522  170 ASP A C   
4032 O O   . ASP C 157 ? 1.28229 1.32488 0.75332 0.32825  -0.09768 0.03523  170 ASP A O   
4033 C CB  . ASP C 157 ? 1.22743 1.27416 0.60899 0.30088  -0.10309 0.04498  170 ASP A CB  
4034 C CG  . ASP C 157 ? 1.51845 1.52868 0.84231 0.27166  -0.09313 0.03014  170 ASP A CG  
4035 O OD1 . ASP C 157 ? 1.48358 1.45656 0.81382 0.23850  -0.07885 -0.00987 170 ASP A OD1 
4036 O OD2 . ASP C 157 ? 1.51814 1.53499 0.79042 0.28373  -0.09553 0.06244  170 ASP A OD2 
4037 N N   . VAL C 158 ? 1.17543 1.31517 0.69174 0.28904  -0.13874 0.01968  171 VAL A N   
4038 C CA  . VAL C 158 ? 1.13375 1.28103 0.68862 0.30872  -0.13799 0.02577  171 VAL A CA  
4039 C C   . VAL C 158 ? 1.13519 1.27054 0.72157 0.28138  -0.14116 -0.00691 171 VAL A C   
4040 O O   . VAL C 158 ? 1.12256 1.28824 0.71980 0.25402  -0.15160 -0.02063 171 VAL A O   
4041 C CB  . VAL C 158 ? 1.19715 1.42447 0.77657 0.32623  -0.15459 0.05994  171 VAL A CB  
4042 C CG1 . VAL C 158 ? 1.22688 1.45230 0.84245 0.33964  -0.14794 0.05938  171 VAL A CG1 
4043 C CG2 . VAL C 158 ? 1.28619 1.52943 0.84818 0.36594  -0.14590 0.10675  171 VAL A CG2 
4044 N N   . TYR C 159 ? 1.07677 1.16680 0.67336 0.28564  -0.13005 -0.01658 172 TYR A N   
4045 C CA  . TYR C 159 ? 1.03599 1.12035 0.66870 0.26618  -0.13374 -0.03541 172 TYR A CA  
4046 C C   . TYR C 159 ? 1.09810 1.18943 0.74439 0.27596  -0.14003 -0.02719 172 TYR A C   
4047 O O   . TYR C 159 ? 1.26113 1.31941 0.88230 0.28827  -0.13040 -0.01930 172 TYR A O   
4048 C CB  . TYR C 159 ? 0.98284 1.02635 0.62097 0.25503  -0.12219 -0.04678 172 TYR A CB  
4049 C CG  . TYR C 159 ? 1.09575 1.11786 0.71248 0.24760  -0.10684 -0.05459 172 TYR A CG  
4050 C CD1 . TYR C 159 ? 1.03972 1.06344 0.66988 0.22872  -0.09743 -0.06898 172 TYR A CD1 
4051 C CD2 . TYR C 159 ? 1.20333 1.19044 0.77791 0.25798  -0.09353 -0.04817 172 TYR A CD2 
4052 C CE1 . TYR C 159 ? 1.16669 1.16001 0.76642 0.21835  -0.07763 -0.07788 172 TYR A CE1 
4053 C CE2 . TYR C 159 ? 1.26918 1.23088 0.81739 0.25031  -0.07703 -0.05455 172 TYR A CE2 
4054 C CZ  . TYR C 159 ? 1.22786 1.19398 0.78760 0.22947  -0.07042 -0.06996 172 TYR A CZ  
4055 O OH  . TYR C 159 ? 1.32490 1.25539 0.84799 0.21836  -0.04849 -0.07804 172 TYR A OH  
4056 N N   . ILE C 160 ? 1.07965 1.20208 0.75581 0.26676  -0.14955 -0.03094 173 ILE A N   
4057 C CA  . ILE C 160 ? 0.99101 1.11691 0.67708 0.27292  -0.15319 -0.02406 173 ILE A CA  
4058 C C   . ILE C 160 ? 0.97384 1.09089 0.68896 0.25696  -0.15813 -0.03158 173 ILE A C   
4059 O O   . ILE C 160 ? 1.13297 1.26119 0.87507 0.24496  -0.15444 -0.04008 173 ILE A O   
4060 C CB  . ILE C 160 ? 0.94169 1.11713 0.64177 0.27796  -0.15723 -0.01493 173 ILE A CB  
4061 C CG1 . ILE C 160 ? 1.11282 1.31585 0.79908 0.30006  -0.15416 0.00704  173 ILE A CG1 
4062 C CG2 . ILE C 160 ? 0.92371 1.09296 0.63151 0.28357  -0.15419 -0.00937 173 ILE A CG2 
4063 C CD1 . ILE C 160 ? 1.04221 1.31339 0.75684 0.30725  -0.15956 0.02681  173 ILE A CD1 
4064 N N   . THR C 161 ? 1.02216 1.11632 0.72721 0.25483  -0.16305 -0.02540 174 THR A N   
4065 C CA  . THR C 161 ? 1.01352 1.11300 0.75080 0.24306  -0.17290 -0.01953 174 THR A CA  
4066 C C   . THR C 161 ? 1.15443 1.26416 0.90154 0.24567  -0.17402 -0.01425 174 THR A C   
4067 O O   . THR C 161 ? 1.27397 1.38539 1.00007 0.25356  -0.16858 -0.01526 174 THR A O   
4068 C CB  . THR C 161 ? 1.08193 1.16384 0.79660 0.22826  -0.18517 -0.01138 174 THR A CB  
4069 O OG1 . THR C 161 ? 1.13034 1.18316 0.79053 0.22658  -0.18325 -0.01008 174 THR A OG1 
4070 C CG2 . THR C 161 ? 1.08425 1.14853 0.78151 0.22156  -0.17837 -0.01939 174 THR A CG2 
4071 N N   . ASP C 162 ? 1.17546 1.29298 0.96065 0.24151  -0.17647 -0.00409 175 ASP A N   
4072 C CA  . ASP C 162 ? 1.13495 1.25241 0.92561 0.24304  -0.17427 0.00376  175 ASP A CA  
4073 C C   . ASP C 162 ? 1.28264 1.38368 1.02826 0.23861  -0.18769 0.01432  175 ASP A C   
4074 O O   . ASP C 162 ? 1.42709 1.51927 1.14714 0.22662  -0.20285 0.02140  175 ASP A O   
4075 C CB  . ASP C 162 ? 1.40545 1.52724 1.24750 0.24554  -0.16699 0.02068  175 ASP A CB  
4076 C CG  . ASP C 162 ? 1.54222 1.66392 1.42204 0.24681  -0.14773 0.01376  175 ASP A CG  
4077 O OD1 . ASP C 162 ? 1.32333 1.45192 1.20280 0.24433  -0.15603 0.01192  175 ASP A OD1 
4078 O OD2 . ASP C 162 ? 1.61946 1.72441 1.52293 0.24726  -0.11772 0.00853  175 ASP A OD2 
4079 N N   . LYS C 163 ? 1.25540 1.34796 0.98463 0.24195  -0.17837 0.01345  176 LYS A N   
4080 C CA  . LYS C 163 ? 1.35970 1.42109 1.03272 0.23544  -0.18034 0.01988  176 LYS A CA  
4081 C C   . LYS C 163 ? 1.33688 1.39417 0.99903 0.21964  -0.20264 0.04250  176 LYS A C   
4082 O O   . LYS C 163 ? 1.23233 1.30571 0.93393 0.22522  -0.20486 0.05947  176 LYS A O   
4083 C CB  . LYS C 163 ? 1.24204 1.29841 0.90981 0.24360  -0.15946 0.01605  176 LYS A CB  
4084 N N   . CYS C 164 ? 1.44956 1.48491 1.05449 0.19697  -0.21732 0.04581  177 CYS A N   
4085 C CA  . CYS C 164 ? 1.49143 1.53531 1.07466 0.17184  -0.24709 0.07270  177 CYS A CA  
4086 C C   . CYS C 164 ? 1.68760 1.69337 1.21285 0.16444  -0.23996 0.07929  177 CYS A C   
4087 O O   . CYS C 164 ? 1.68528 1.64173 1.15983 0.16731  -0.21025 0.05873  177 CYS A O   
4088 C CB  . CYS C 164 ? 1.22697 1.26063 0.75524 0.13435  -0.26644 0.07032  177 CYS A CB  
4089 S SG  . CYS C 164 ? 1.95849 1.98070 1.40061 0.08326  -0.30014 0.09566  177 CYS A SG  
4090 N N   . VAL C 165 ? 1.58439 1.61372 1.12043 0.15758  -0.26358 0.11327  178 VAL A N   
4091 C CA  . VAL C 165 ? 1.55926 1.54887 1.03425 0.14862  -0.25712 0.12324  178 VAL A CA  
4092 C C   . VAL C 165 ? 1.82239 1.76482 1.17971 0.10096  -0.26994 0.12022  178 VAL A C   
4093 O O   . VAL C 165 ? 1.86182 1.73400 1.13896 0.09142  -0.23982 0.10258  178 VAL A O   
4094 C CB  . VAL C 165 ? 1.74430 1.77176 1.27055 0.16222  -0.27368 0.16720  178 VAL A CB  
4095 N N   . LEU C 166 ? 1.87284 1.85063 1.21541 0.06560  -0.31026 0.13694  179 LEU A N   
4096 C CA  . LEU C 166 ? 1.91488 1.84738 1.13146 0.00301  -0.32554 0.13187  179 LEU A CA  
4097 C C   . LEU C 166 ? 1.95956 1.85004 1.08684 -0.02124 -0.32933 0.14962  179 LEU A C   
4098 O O   . LEU C 166 ? 2.08820 1.88360 1.09782 -0.04966 -0.29633 0.12218  179 LEU A O   
4099 C CB  . LEU C 166 ? 1.84234 1.68930 0.98647 -0.00729 -0.27953 0.08349  179 LEU A CB  
4100 N N   . LYS C 174 ? 1.93907 1.45327 0.80125 0.02311  -0.08825 0.07971  187 LYS A N   
4101 C CA  . LYS C 174 ? 1.82588 1.42060 0.76802 0.03156  -0.13044 0.08215  187 LYS A CA  
4102 C C   . LYS C 174 ? 1.93217 1.52332 0.92851 0.06477  -0.08964 0.05210  187 LYS A C   
4103 O O   . LYS C 174 ? 1.93131 1.51484 0.97550 0.10215  -0.04343 0.04204  187 LYS A O   
4104 C CB  . LYS C 174 ? 1.73793 1.43232 0.80255 0.06419  -0.17120 0.11307  187 LYS A CB  
4105 N N   . SER C 175 ? 1.97470 1.57827 0.96657 0.04991  -0.10770 0.04253  188 SER A N   
4106 C CA  . SER C 175 ? 1.71312 1.30719 0.74217 0.07921  -0.07035 0.02031  188 SER A CA  
4107 C C   . SER C 175 ? 1.60865 1.30305 0.75846 0.10756  -0.10839 0.02679  188 SER A C   
4108 O O   . SER C 175 ? 1.81912 1.55641 0.97787 0.08354  -0.15632 0.03790  188 SER A O   
4109 C CB  . SER C 175 ? 1.83367 1.33543 0.74270 0.03670  -0.04475 -0.00033 188 SER A CB  
4110 O OG  . SER C 175 ? 2.18151 1.57488 0.95758 -0.00073 -0.00611 -0.00872 188 SER A OG  
4111 N N   . ASN C 176 ? 1.52646 1.26077 0.76727 0.15463  -0.08584 0.02206  189 ASN A N   
4112 C CA  . ASN C 176 ? 1.51944 1.33431 0.86020 0.17820  -0.11201 0.02362  189 ASN A CA  
4113 C C   . ASN C 176 ? 1.55721 1.35644 0.89178 0.18781  -0.09327 0.01024  189 ASN A C   
4114 O O   . ASN C 176 ? 1.64918 1.38650 0.93492 0.19608  -0.04637 0.00292  189 ASN A O   
4115 C CB  . ASN C 176 ? 1.33094 1.20174 0.76279 0.21166  -0.10255 0.02629  189 ASN A CB  
4116 C CG  . ASN C 176 ? 1.75243 1.62717 1.18971 0.20478  -0.11118 0.03949  189 ASN A CG  
4117 O OD1 . ASN C 176 ? 1.91080 1.76539 1.34140 0.21169  -0.08089 0.03844  189 ASN A OD1 
4118 N ND2 . ASN C 176 ? 1.71609 1.61784 1.17073 0.19377  -0.14828 0.05658  189 ASN A ND2 
4119 N N   . SER C 177 ? 1.49598 1.34543 0.88074 0.18946  -0.12310 0.01004  190 SER A N   
4120 C CA  . SER C 177 ? 1.42130 1.25569 0.80024 0.19884  -0.10651 -0.00029 190 SER A CA  
4121 C C   . SER C 177 ? 1.40320 1.30924 0.86386 0.21134  -0.13545 0.00119  190 SER A C   
4122 O O   . SER C 177 ? 1.40540 1.34740 0.89419 0.19399  -0.17025 0.00844  190 SER A O   
4123 C CB  . SER C 177 ? 1.52895 1.29042 0.80774 0.15634  -0.10096 -0.01054 190 SER A CB  
4124 O OG  . SER C 177 ? 1.70942 1.50626 0.98622 0.11700  -0.15081 -0.00264 190 SER A OG  
4125 N N   . ALA C 178 ? 1.47387 1.40077 0.97202 0.24170  -0.11802 -0.00117 191 ALA A N   
4126 C CA  . ALA C 178 ? 1.36331 1.34221 0.91995 0.24996  -0.13673 -0.00326 191 ALA A CA  
4127 C C   . ALA C 178 ? 1.35626 1.30501 0.88422 0.25739  -0.11882 -0.00764 191 ALA A C   
4128 O O   . ALA C 178 ? 1.44650 1.35638 0.94106 0.27677  -0.08365 -0.00280 191 ALA A O   
4129 C CB  . ALA C 178 ? 1.18387 1.22211 0.80442 0.27085  -0.13682 -0.00035 191 ALA A CB  
4130 N N   . VAL C 179 ? 1.30511 1.26781 0.84896 0.24487  -0.13619 -0.01344 192 VAL A N   
4131 C CA  . VAL C 179 ? 1.26978 1.19644 0.78137 0.24667  -0.11821 -0.01875 192 VAL A CA  
4132 C C   . VAL C 179 ? 1.24544 1.21567 0.80293 0.27226  -0.11864 -0.01505 192 VAL A C   
4133 O O   . VAL C 179 ? 1.04320 1.06147 0.65104 0.26713  -0.13966 -0.01835 192 VAL A O   
4134 C CB  . VAL C 179 ? 1.28488 1.19643 0.77694 0.20741  -0.13481 -0.02739 192 VAL A CB  
4135 C CG1 . VAL C 179 ? 1.27661 1.14318 0.73219 0.20629  -0.11024 -0.03571 192 VAL A CG1 
4136 C CG2 . VAL C 179 ? 1.24783 1.12241 0.67987 0.17012  -0.14093 -0.02874 192 VAL A CG2 
4137 N N   . ALA C 180 ? 1.21620 1.16443 0.75065 0.29866  -0.09112 -0.00538 193 ALA A N   
4138 C CA  . ALA C 180 ? 1.22168 1.20932 0.78262 0.31856  -0.09355 0.00349  193 ALA A CA  
4139 C C   . ALA C 180 ? 1.31177 1.24180 0.82590 0.32934  -0.06472 0.00777  193 ALA A C   
4140 O O   . ALA C 180 ? 1.40521 1.26980 0.87140 0.34037  -0.02845 0.01435  193 ALA A O   
4141 C CB  . ALA C 180 ? 1.19425 1.24091 0.78930 0.34683  -0.09281 0.02632  193 ALA A CB  
4142 N N   . TRP C 181 ? 1.28332 1.22562 0.80431 0.32465  -0.07297 0.00315  194 TRP A N   
4143 C CA  . TRP C 181 ? 1.42042 1.30412 0.89524 0.33348  -0.04338 0.00707  194 TRP A CA  
4144 C C   . TRP C 181 ? 1.46170 1.38428 0.94965 0.34647  -0.05233 0.01816  194 TRP A C   
4145 O O   . TRP C 181 ? 1.34060 1.32375 0.86519 0.33410  -0.08116 0.01215  194 TRP A O   
4146 C CB  . TRP C 181 ? 1.40425 1.23434 0.85030 0.29378  -0.03891 -0.01881 194 TRP A CB  
4147 C CG  . TRP C 181 ? 1.29297 1.16298 0.78162 0.26978  -0.06433 -0.03341 194 TRP A CG  
4148 C CD1 . TRP C 181 ? 1.32697 1.18457 0.80993 0.26759  -0.05405 -0.03764 194 TRP A CD1 
4149 C CD2 . TRP C 181 ? 1.18402 1.10511 0.72828 0.24818  -0.09484 -0.04181 194 TRP A CD2 
4150 N NE1 . TRP C 181 ? 1.17820 1.07392 0.71199 0.24559  -0.07232 -0.04992 194 TRP A NE1 
4151 C CE2 . TRP C 181 ? 1.20169 1.13769 0.77725 0.23611  -0.09632 -0.05005 194 TRP A CE2 
4152 C CE3 . TRP C 181 ? 1.14552 1.09580 0.71523 0.24056  -0.11541 -0.03968 194 TRP A CE3 
4153 C CZ2 . TRP C 181 ? 1.15305 1.13168 0.79171 0.22145  -0.11235 -0.05280 194 TRP A CZ2 
4154 C CZ3 . TRP C 181 ? 1.18301 1.17800 0.81190 0.22581  -0.13643 -0.04100 194 TRP A CZ3 
4155 C CH2 . TRP C 181 ? 1.08243 1.09120 0.74890 0.21865  -0.13233 -0.04589 194 TRP A CH2 
4156 N N   . SER C 182 ? 1.48823 1.36527 0.93518 0.36818  -0.02230 0.03446  195 SER A N   
4157 C CA  . SER C 182 ? 1.40728 1.31093 0.84867 0.37818  -0.02865 0.04883  195 SER A CA  
4158 C C   . SER C 182 ? 1.54459 1.36456 0.92931 0.38979  0.01242  0.05498  195 SER A C   
4159 O O   . SER C 182 ? 1.71012 1.45939 1.05972 0.40532  0.05256  0.06233  195 SER A O   
4160 C CB  . SER C 182 ? 1.46999 1.45310 0.93580 0.41013  -0.04408 0.08975  195 SER A CB  
4161 O OG  . SER C 182 ? 1.52158 1.53273 0.96801 0.41142  -0.05526 0.10613  195 SER A OG  
4162 N N   . ASN C 183 ? 1.62448 1.44133 0.99220 0.37904  0.00927  0.05016  196 ASN A N   
4163 C CA  . ASN C 183 ? 1.73468 1.46862 1.04623 0.38553  0.04997  0.05347  196 ASN A CA  
4164 C C   . ASN C 183 ? 1.71105 1.45438 0.99361 0.42833  0.06157  0.10122  196 ASN A C   
4165 O O   . ASN C 183 ? 1.89328 1.56261 1.12376 0.43936  0.09993  0.11007  196 ASN A O   
4166 C CB  . ASN C 183 ? 1.77767 1.49036 1.08775 0.34250  0.04733  0.01646  196 ASN A CB  
4167 C CG  . ASN C 183 ? 1.78891 1.57081 1.13205 0.32460  0.01172  0.00718  196 ASN A CG  
4168 O OD1 . ASN C 183 ? 1.68646 1.51430 1.07945 0.30476  -0.01396 -0.01079 196 ASN A OD1 
4169 N ND2 . ASN C 183 ? 1.71869 1.49883 1.02475 0.32884  0.01513  0.01985  196 ASN A ND2 
4170 N N   . LYS C 184 ? 1.74569 1.58250 1.06068 0.45011  0.02903  0.13587  197 LYS A N   
4171 C CA  . LYS C 184 ? 1.75578 1.62318 1.05188 0.49294  0.03371  0.19516  197 LYS A CA  
4172 C C   . LYS C 184 ? 1.85701 1.68761 1.15606 0.55122  0.08085  0.24108  197 LYS A C   
4173 O O   . LYS C 184 ? 1.83353 1.65427 1.16109 0.55698  0.09378  0.23219  197 LYS A O   
4174 C CB  . LYS C 184 ? 1.71295 1.70946 1.04319 0.48381  -0.02320 0.21869  197 LYS A CB  
4175 C CG  . LYS C 184 ? 1.62249 1.69573 1.01951 0.48354  -0.04829 0.21957  197 LYS A CG  
4176 C CD  . LYS C 184 ? 1.32724 1.52080 0.74599 0.45391  -0.10443 0.23027  197 LYS A CD  
4177 C CE  . LYS C 184 ? 1.41954 1.68642 0.90455 0.44793  -0.12619 0.22734  197 LYS A CE  
4178 N NZ  . LYS C 184 ? 1.16734 1.54315 0.66376 0.40451  -0.17755 0.22939  197 LYS A NZ  
4179 N N   . SER C 185 ? 2.10050 1.90234 1.36521 0.59601  0.11334  0.29321  198 SER A N   
4180 C CA  . SER C 185 ? 2.10276 1.83197 1.35778 0.65547  0.18167  0.33674  198 SER A CA  
4181 C C   . SER C 185 ? 1.95515 1.77447 1.28486 0.69783  0.17487  0.38512  198 SER A C   
4182 O O   . SER C 185 ? 1.95160 1.70995 1.28845 0.71250  0.22006  0.37711  198 SER A O   
4183 C CB  . SER C 185 ? 1.77950 1.46620 0.98752 0.70067  0.21878  0.39264  198 SER A CB  
4184 N N   . ASP C 186 ? 1.91638 1.88329 1.30495 0.70614  0.12116  0.43032  199 ASP A N   
4185 C CA  . ASP C 186 ? 1.85409 1.92973 1.34316 0.72592  0.11735  0.46866  199 ASP A CA  
4186 C C   . ASP C 186 ? 1.84383 1.98044 1.37061 0.68918  0.07072  0.42919  199 ASP A C   
4187 O O   . ASP C 186 ? 1.70885 1.97885 1.29994 0.65977  0.01630  0.43770  199 ASP A O   
4188 C CB  . ASP C 186 ? 1.57338 1.78452 1.12062 0.72660  0.08183  0.52459  199 ASP A CB  
4189 N N   . PHE C 187 ? 1.88455 1.91497 1.37021 0.67839  0.09611  0.37890  200 PHE A N   
4190 C CA  . PHE C 187 ? 1.82413 1.89291 1.34638 0.63782  0.06385  0.33348  200 PHE A CA  
4191 C C   . PHE C 187 ? 1.77688 1.78219 1.31101 0.66823  0.12114  0.33999  200 PHE A C   
4192 O O   . PHE C 187 ? 1.81691 1.68498 1.28932 0.67701  0.18435  0.32448  200 PHE A O   
4193 C CB  . PHE C 187 ? 1.85366 1.86644 1.33340 0.57096  0.03952  0.25497  200 PHE A CB  
4194 C CG  . PHE C 187 ? 1.78903 1.82721 1.30140 0.53439  0.01357  0.21356  200 PHE A CG  
4195 C CD1 . PHE C 187 ? 1.62236 1.77801 1.19100 0.51809  -0.03575 0.21951  200 PHE A CD1 
4196 C CD2 . PHE C 187 ? 1.80625 1.75023 1.28641 0.51121  0.03870  0.17031  200 PHE A CD2 
4197 C CE1 . PHE C 187 ? 1.48353 1.65295 1.07832 0.48719  -0.05339 0.18401  200 PHE A CE1 
4198 C CE2 . PHE C 187 ? 1.69399 1.66183 1.20042 0.48020  0.01415  0.13932  200 PHE A CE2 
4199 C CZ  . PHE C 187 ? 1.54284 1.61897 1.10799 0.47209  -0.02895 0.14663  200 PHE A CZ  
4200 N N   . ALA C 188 ? 1.39187 1.49034 0.99768 0.67827  0.10357  0.36067  201 ALA A N   
4201 C CA  . ALA C 188 ? 1.47042 1.51343 1.08904 0.70361  0.15897  0.36600  201 ALA A CA  
4202 C C   . ALA C 188 ? 1.61039 1.70078 1.25856 0.65731  0.11785  0.32230  201 ALA A C   
4203 O O   . ALA C 188 ? 1.61452 1.81542 1.30284 0.62400  0.05145  0.31232  201 ALA A O   
4204 C CB  . ALA C 188 ? 1.56215 1.67161 1.25627 0.76120  0.19951  0.44211  201 ALA A CB  
4205 N N   . CYS C 189 ? 1.59548 1.59048 1.21243 0.65171  0.16293  0.29566  202 CYS A N   
4206 C CA  . CYS C 189 ? 1.54859 1.57948 1.19087 0.61567  0.13365  0.26284  202 CYS A CA  
4207 C C   . CYS C 189 ? 1.66499 1.84778 1.40937 0.63669  0.10446  0.30752  202 CYS A C   
4208 O O   . CYS C 189 ? 1.33237 1.59980 1.10913 0.59508  0.04605  0.28368  202 CYS A O   
4209 C CB  . CYS C 189 ? 1.62658 1.53000 1.21271 0.61408  0.19725  0.24195  202 CYS A CB  
4210 N N   . ALA C 190 ? 1.82343 2.04272 1.62178 0.70009  0.14907  0.37564  203 ALA A N   
4211 C CA  . ALA C 190 ? 1.55722 1.94128 1.46415 0.70964  0.12068  0.42651  203 ALA A CA  
4212 C C   . ALA C 190 ? 1.59982 2.05375 1.55174 0.68192  0.08803  0.40504  203 ALA A C   
4213 O O   . ALA C 190 ? 1.64854 2.20879 1.62965 0.63502  0.02045  0.38970  203 ALA A O   
4214 C CB  . ALA C 190 ? 1.62630 2.11380 1.55147 0.67965  0.05890  0.43855  203 ALA A CB  
4215 N N   . VAL D 2   ? 2.02750 1.66015 1.46570 0.45464  0.32672  0.17242  1   VAL B N   
4216 C CA  . VAL D 2   ? 1.94092 1.53202 1.37154 0.42416  0.28352  0.13619  1   VAL B CA  
4217 C C   . VAL D 2   ? 1.65555 1.31718 1.20495 0.36076  0.24832  0.13612  1   VAL B C   
4218 O O   . VAL D 2   ? 1.62710 1.36760 1.27120 0.34508  0.26060  0.16471  1   VAL B O   
4219 C CB  . VAL D 2   ? 1.87967 1.36351 1.17400 0.42134  0.24266  0.09120  1   VAL B CB  
4220 C CG1 . VAL D 2   ? 1.72997 1.12649 0.88980 0.48884  0.27522  0.08465  1   VAL B CG1 
4221 C CG2 . VAL D 2   ? 1.71757 1.21273 1.00133 0.38864  0.21118  0.08440  1   VAL B CG2 
4222 N N   . THR D 3   ? 1.56256 1.19122 1.10290 0.32558  0.20465  0.10476  2   THR B N   
4223 C CA  . THR D 3   ? 1.49629 1.18402 1.13352 0.27038  0.17294  0.10192  2   THR B CA  
4224 C C   . THR D 3   ? 1.45019 1.14491 1.08087 0.23670  0.14147  0.08876  2   THR B C   
4225 O O   . THR D 3   ? 1.54712 1.18121 1.09858 0.22765  0.11015  0.06248  2   THR B O   
4226 C CB  . THR D 3   ? 1.48643 1.14110 1.11847 0.24922  0.14396  0.08039  2   THR B CB  
4227 O OG1 . THR D 3   ? 1.35252 0.91762 0.87917 0.24737  0.11395  0.04888  2   THR B OG1 
4228 C CG2 . THR D 3   ? 1.68023 1.33472 1.33029 0.28355  0.17436  0.09728  2   THR B CG2 
4229 N N   . LEU D 4   ? 1.27769 1.04433 0.99390 0.21811  0.14720  0.10833  3   LEU B N   
4230 C CA  . LEU D 4   ? 1.14981 0.93204 0.87543 0.18848  0.12000  0.09982  3   LEU B CA  
4231 C C   . LEU D 4   ? 0.95493 0.75853 0.72802 0.14238  0.08268  0.08081  3   LEU B C   
4232 O O   . LEU D 4   ? 0.94970 0.76379 0.72807 0.11902  0.05791  0.07194  3   LEU B O   
4233 C CB  . LEU D 4   ? 0.99322 0.83451 0.78648 0.19184  0.14323  0.13008  3   LEU B CB  
4234 C CG  . LEU D 4   ? 1.20024 1.03743 0.96287 0.23720  0.18719  0.15986  3   LEU B CG  
4235 C CD1 . LEU D 4   ? 0.94089 0.84005 0.78765 0.23111  0.20486  0.19394  3   LEU B CD1 
4236 C CD2 . LEU D 4   ? 1.56853 1.33785 1.20838 0.26220  0.18242  0.14568  3   LEU B CD2 
4237 N N   . LEU D 5   ? 0.87921 0.69206 0.68672 0.13155  0.07987  0.07742  4   LEU B N   
4238 C CA  . LEU D 5   ? 0.74601 0.58299 0.59670 0.09193  0.05075  0.06387  4   LEU B CA  
4239 C C   . LEU D 5   ? 0.93757 0.73113 0.75165 0.08684  0.03620  0.05034  4   LEU B C   
4240 O O   . LEU D 5   ? 1.25595 0.99947 1.01588 0.11568  0.04909  0.05007  4   LEU B O   
4241 C CB  . LEU D 5   ? 0.67485 0.57641 0.61764 0.07837  0.05901  0.07754  4   LEU B CB  
4242 C CG  . LEU D 5   ? 0.83661 0.77914 0.82776 0.07204  0.06334  0.08777  4   LEU B CG  
4243 C CD1 . LEU D 5   ? 0.90084 0.89101 0.97323 0.06045  0.06756  0.09984  4   LEU B CD1 
4244 C CD2 . LEU D 5   ? 1.01078 0.95600 0.99421 0.04883  0.03743  0.07090  4   LEU B CD2 
4245 N N   . GLU D 6   ? 0.80832 0.62000 0.65166 0.05191  0.01087  0.04088  5   GLU B N   
4246 C CA  . GLU D 6   ? 0.93312 0.71023 0.75452 0.04057  -0.00509 0.03301  5   GLU B CA  
4247 C C   . GLU D 6   ? 0.90669 0.73680 0.79101 0.00881  -0.01642 0.03519  5   GLU B C   
4248 O O   . GLU D 6   ? 0.95012 0.80751 0.85371 -0.01611 -0.03252 0.03007  5   GLU B O   
4249 C CB  . GLU D 6   ? 1.02425 0.73750 0.77541 0.03007  -0.03407 0.01668  5   GLU B CB  
4250 N N   . GLN D 7   ? 0.90878 0.75455 0.82297 0.01264  -0.00727 0.04441  6   GLN B N   
4251 C CA  . GLN D 7   ? 0.77537 0.66703 0.73781 -0.01222 -0.01639 0.04692  6   GLN B CA  
4252 C C   . GLN D 7   ? 1.06486 0.92856 1.00935 -0.02008 -0.02732 0.04961  6   GLN B C   
4253 O O   . GLN D 7   ? 1.01120 0.84169 0.93711 0.00235  -0.01812 0.05624  6   GLN B O   
4254 C CB  . GLN D 7   ? 0.81601 0.75564 0.83465 -0.00416 -0.00205 0.05809  6   GLN B CB  
4255 C CG  . GLN D 7   ? 0.74835 0.72751 0.80306 -0.02657 -0.01392 0.05716  6   GLN B CG  
4256 C CD  . GLN D 7   ? 0.76837 0.78397 0.87406 -0.02121 -0.00848 0.06717  6   GLN B CD  
4257 O OE1 . GLN D 7   ? 0.72513 0.74403 0.85061 -0.00193 0.00663  0.08001  6   GLN B OE1 
4258 N NE2 . GLN D 7   ? 0.84997 0.89240 0.97613 -0.03835 -0.02185 0.06317  6   GLN B NE2 
4259 N N   . ASN D 8   ? 1.16024 1.03865 1.11213 -0.04957 -0.04467 0.04773  7   ASN B N   
4260 C CA  . ASN D 8   ? 1.00198 0.85613 0.93987 -0.06177 -0.05658 0.05466  7   ASN B CA  
4261 C C   . ASN D 8   ? 1.05098 0.95848 1.02392 -0.08387 -0.06054 0.06135  7   ASN B C   
4262 O O   . ASN D 8   ? 0.95862 0.90751 0.95280 -0.09636 -0.06036 0.05634  7   ASN B O   
4263 C CB  . ASN D 8   ? 1.38837 1.18850 1.28386 -0.07765 -0.07746 0.04968  7   ASN B CB  
4264 C CG  . ASN D 8   ? 1.45303 1.19148 1.29633 -0.05423 -0.07672 0.03800  7   ASN B CG  
4265 O OD1 . ASN D 8   ? 1.26880 0.95183 1.07485 -0.03005 -0.07088 0.03770  7   ASN B OD1 
4266 N ND2 . ASN D 8   ? 1.34213 1.08802 1.17793 -0.05784 -0.08187 0.02901  7   ASN B ND2 
4267 N N   . PRO D 9   ? 0.99188 0.89772 0.96690 -0.08569 -0.06318 0.07338  8   PRO B N   
4268 C CA  . PRO D 9   ? 1.10934 0.96912 1.06461 -0.06790 -0.06265 0.08245  8   PRO B CA  
4269 C C   . PRO D 9   ? 1.08751 0.96717 1.06920 -0.04039 -0.04787 0.08850  8   PRO B C   
4270 O O   . PRO D 9   ? 0.97788 0.90160 0.99219 -0.03850 -0.04100 0.08494  8   PRO B O   
4271 C CB  . PRO D 9   ? 1.26296 1.12569 1.21731 -0.08782 -0.07456 0.09738  8   PRO B CB  
4272 C CG  . PRO D 9   ? 1.04724 0.97593 1.02990 -0.10213 -0.07243 0.09695  8   PRO B CG  
4273 C CD  . PRO D 9   ? 0.89573 0.84496 0.88811 -0.10518 -0.06722 0.08088  8   PRO B CD  
4274 N N   . ARG D 10  ? 0.97260 0.82026 0.94546 -0.01866 -0.04372 0.10048  9   ARG B N   
4275 C CA  . ARG D 10  ? 0.94753 0.82227 0.95764 0.00763  -0.03007 0.11406  9   ARG B CA  
4276 C C   . ARG D 10  ? 0.90776 0.82675 0.95422 -0.00356 -0.04255 0.12878  9   ARG B C   
4277 O O   . ARG D 10  ? 0.89208 0.85809 0.98434 0.00009  -0.04158 0.13564  9   ARG B O   
4278 C CB  . ARG D 10  ? 1.15284 0.97469 1.13795 0.04363  -0.01615 0.12258  9   ARG B CB  
4279 C CG  . ARG D 10  ? 1.16440 1.02120 1.19657 0.07602  0.00418  0.14235  9   ARG B CG  
4280 C CD  . ARG D 10  ? 1.26251 1.14466 1.31147 0.08658  0.02318  0.13817  9   ARG B CD  
4281 N NE  . ARG D 10  ? 1.29100 1.11286 1.27696 0.10755  0.03750  0.12390  9   ARG B NE  
4282 C CZ  . ARG D 10  ? 1.35882 1.15817 1.30560 0.08864  0.02771  0.10196  9   ARG B CZ  
4283 N NH1 . ARG D 10  ? 1.21622 1.05174 1.18448 0.05152  0.00907  0.09282  9   ARG B NH1 
4284 N NH2 . ARG D 10  ? 1.55385 1.29216 1.43600 0.10996  0.03638  0.08952  9   ARG B NH2 
4285 N N   . TRP D 11  ? 0.96635 0.86874 0.99169 -0.01843 -0.05699 0.13551  10  TRP B N   
4286 C CA  . TRP D 11  ? 0.77623 0.71439 0.82150 -0.02873 -0.07157 0.14995  10  TRP B CA  
4287 C C   . TRP D 11  ? 0.75863 0.70667 0.77957 -0.05947 -0.08271 0.14448  10  TRP B C   
4288 O O   . TRP D 11  ? 0.69045 0.61204 0.68520 -0.07301 -0.08135 0.13740  10  TRP B O   
4289 C CB  . TRP D 11  ? 0.91593 0.82822 0.96023 -0.01042 -0.07525 0.17329  10  TRP B CB  
4290 C CG  . TRP D 11  ? 0.98445 0.87206 1.03989 0.02672  -0.05678 0.18027  10  TRP B CG  
4291 C CD1 . TRP D 11  ? 1.14550 0.96654 1.15963 0.04601  -0.04452 0.17353  10  TRP B CD1 
4292 C CD2 . TRP D 11  ? 0.96161 0.89020 1.07162 0.05130  -0.04762 0.19727  10  TRP B CD2 
4293 N NE1 . TRP D 11  ? 1.40581 1.22301 1.43828 0.08651  -0.02293 0.18412  10  TRP B NE1 
4294 C CE2 . TRP D 11  ? 1.16872 1.05763 1.26751 0.08958  -0.02308 0.20206  10  TRP B CE2 
4295 C CE3 . TRP D 11  ? 1.03808 1.03173 1.20563 0.04423  -0.05967 0.21026  10  TRP B CE3 
4296 C CZ2 . TRP D 11  ? 1.15912 1.08183 1.31010 0.12306  -0.00409 0.22417  10  TRP B CZ2 
4297 C CZ3 . TRP D 11  ? 1.16313 1.18965 1.38902 0.07127  -0.04746 0.23272  10  TRP B CZ3 
4298 C CH2 . TRP D 11  ? 1.14720 1.14348 1.36842 0.11135  -0.01686 0.24186  10  TRP B CH2 
4299 N N   . ARG D 12  ? 0.79307 0.78032 0.82246 -0.06968 -0.09454 0.14990  11  ARG B N   
4300 C CA  . ARG D 12  ? 0.67873 0.68166 0.68177 -0.09265 -0.09949 0.14846  11  ARG B CA  
4301 C C   . ARG D 12  ? 0.92908 0.95569 0.92522 -0.09490 -0.11524 0.16212  11  ARG B C   
4302 O O   . ARG D 12  ? 0.92074 0.97244 0.93765 -0.08848 -0.12613 0.15806  11  ARG B O   
4303 C CB  . ARG D 12  ? 0.73840 0.76916 0.74453 -0.10184 -0.09188 0.12580  11  ARG B CB  
4304 C CG  . ARG D 12  ? 0.87997 0.89498 0.87631 -0.11262 -0.08209 0.11935  11  ARG B CG  
4305 C CD  . ARG D 12  ? 0.95194 0.95696 0.92625 -0.13084 -0.08513 0.13779  11  ARG B CD  
4306 N NE  . ARG D 12  ? 1.24887 1.23671 1.22228 -0.14490 -0.08277 0.13549  11  ARG B NE  
4307 C CZ  . ARG D 12  ? 1.37508 1.39600 1.35859 -0.15568 -0.07565 0.12744  11  ARG B CZ  
4308 N NH1 . ARG D 12  ? 1.41456 1.48100 1.40276 -0.15118 -0.06675 0.11828  11  ARG B NH1 
4309 N NH2 . ARG D 12  ? 1.38163 1.38641 1.36948 -0.17004 -0.07970 0.12854  11  ARG B NH2 
4310 N N   . LEU D 13  ? 0.93947 0.95684 0.90605 -0.10559 -0.11905 0.18026  12  LEU B N   
4311 C CA  . LEU D 13  ? 0.91336 0.95157 0.85830 -0.10863 -0.13391 0.19441  12  LEU B CA  
4312 C C   . LEU D 13  ? 0.93819 1.00405 0.85040 -0.12191 -0.12638 0.18409  12  LEU B C   
4313 O O   . LEU D 13  ? 1.00761 1.07156 0.90666 -0.13452 -0.11202 0.19205  12  LEU B O   
4314 C CB  . LEU D 13  ? 1.03242 1.04314 0.96241 -0.10872 -0.14041 0.22618  12  LEU B CB  
4315 C CG  . LEU D 13  ? 0.91253 0.94150 0.81868 -0.10786 -0.15939 0.24596  12  LEU B CG  
4316 C CD1 . LEU D 13  ? 1.06217 1.11486 0.99420 -0.09561 -0.17919 0.23755  12  LEU B CD1 
4317 C CD2 . LEU D 13  ? 1.27628 1.27257 1.17523 -0.10465 -0.16566 0.28042  12  LEU B CD2 
4318 N N   . VAL D 14  ? 0.81298 0.90303 0.71311 -0.11817 -0.13656 0.16773  13  VAL B N   
4319 C CA  . VAL D 14  ? 0.89539 1.00729 0.76050 -0.12196 -0.12599 0.15142  13  VAL B CA  
4320 C C   . VAL D 14  ? 0.96477 1.08530 0.77586 -0.11961 -0.14059 0.16013  13  VAL B C   
4321 O O   . VAL D 14  ? 0.99604 1.11419 0.80370 -0.11453 -0.16818 0.15481  13  VAL B O   
4322 C CB  . VAL D 14  ? 0.82198 0.94146 0.70581 -0.11657 -0.12586 0.11845  13  VAL B CB  
4323 C CG1 . VAL D 14  ? 0.71076 0.84761 0.56007 -0.11521 -0.10800 0.10184  13  VAL B CG1 
4324 C CG2 . VAL D 14  ? 0.79950 0.90787 0.73426 -0.11546 -0.11622 0.11333  13  VAL B CG2 
4325 N N   . PRO D 15  ? 1.03644 1.16833 0.80434 -0.12328 -0.12445 0.17628  14  PRO B N   
4326 C CA  . PRO D 15  ? 1.01340 1.15266 0.71375 -0.11642 -0.13476 0.18006  14  PRO B CA  
4327 C C   . PRO D 15  ? 1.14834 1.29042 0.81569 -0.10548 -0.13931 0.14187  14  PRO B C   
4328 O O   . PRO D 15  ? 1.30337 1.44937 0.99781 -0.10349 -0.12493 0.11756  14  PRO B O   
4329 C CB  . PRO D 15  ? 0.97100 1.12748 0.64147 -0.12142 -0.10568 0.20910  14  PRO B CB  
4330 C CG  . PRO D 15  ? 1.00236 1.15005 0.73178 -0.13662 -0.09463 0.22862  14  PRO B CG  
4331 C CD  . PRO D 15  ? 0.95218 1.08966 0.73197 -0.13491 -0.09858 0.19785  14  PRO B CD  
4332 N N   . ARG D 16  ? 1.11037 1.24446 0.71371 -0.09762 -0.16260 0.13655  15  ARG B N   
4333 C CA  . ARG D 16  ? 1.26812 1.38915 0.82824 -0.08666 -0.17523 0.09721  15  ARG B CA  
4334 C C   . ARG D 16  ? 1.36655 1.50041 0.88449 -0.07263 -0.13484 0.08437  15  ARG B C   
4335 O O   . ARG D 16  ? 1.35879 1.51092 0.83100 -0.06622 -0.10892 0.10786  15  ARG B O   
4336 C CB  . ARG D 16  ? 1.23330 1.33511 0.72300 -0.08198 -0.21524 0.09457  15  ARG B CB  
4337 C CG  . ARG D 16  ? 1.32825 1.40085 0.76612 -0.07249 -0.23850 0.05031  15  ARG B CG  
4338 C CD  . ARG D 16  ? 1.30807 1.35548 0.68154 -0.07277 -0.29061 0.04731  15  ARG B CD  
4339 N NE  . ARG D 16  ? 1.54995 1.55657 0.87093 -0.06651 -0.32047 0.00195  15  ARG B NE  
4340 C CZ  . ARG D 16  ? 1.85255 1.82590 1.11333 -0.06905 -0.37567 -0.01106 15  ARG B CZ  
4341 N NH1 . ARG D 16  ? 1.87407 1.85658 1.12160 -0.07630 -0.40685 0.01978  15  ARG B NH1 
4342 N NH2 . ARG D 16  ? 1.82972 1.75537 1.04138 -0.06452 -0.40380 -0.05572 15  ARG B NH2 
4343 N N   . GLY D 17  ? 1.30503 1.43215 0.84266 -0.06632 -0.12778 0.05100  16  GLY B N   
4344 C CA  . GLY D 17  ? 1.14725 1.28826 0.65460 -0.04832 -0.08902 0.03787  16  GLY B CA  
4345 C C   . GLY D 17  ? 1.32468 1.50239 0.89915 -0.05554 -0.05118 0.05792  16  GLY B C   
4346 O O   . GLY D 17  ? 1.50842 1.70682 1.07329 -0.04007 -0.01768 0.05133  16  GLY B O   
4347 N N   . GLN D 18  ? 1.25074 1.43482 0.89117 -0.07694 -0.05709 0.08215  17  GLN B N   
4348 C CA  . GLN D 18  ? 1.16513 1.37625 0.86415 -0.08780 -0.02981 0.10153  17  GLN B CA  
4349 C C   . GLN D 18  ? 1.10810 1.31375 0.86114 -0.08773 -0.03008 0.07575  17  GLN B C   
4350 O O   . GLN D 18  ? 1.04172 1.22208 0.79672 -0.08239 -0.05154 0.04761  17  GLN B O   
4351 C CB  . GLN D 18  ? 1.21602 1.42242 0.94936 -0.10882 -0.03873 0.13603  17  GLN B CB  
4352 C CG  . GLN D 18  ? 1.22984 1.46609 0.97941 -0.12099 -0.01166 0.17269  17  GLN B CG  
4353 C CD  . GLN D 18  ? 1.40724 1.67018 1.09626 -0.11006 0.00957  0.19353  17  GLN B CD  
4354 O OE1 . GLN D 18  ? 1.54210 1.83618 1.21286 -0.09411 0.03857  0.18798  17  GLN B OE1 
4355 N NE2 . GLN D 18  ? 1.27116 1.52239 0.92670 -0.11517 -0.00267 0.21989  17  GLN B NE2 
4356 N N   . ALA D 19  ? 1.06277 1.29301 0.86215 -0.09549 -0.00826 0.08891  18  ALA B N   
4357 C CA  . ALA D 19  ? 0.84083 1.06958 0.68916 -0.09510 -0.00644 0.07009  18  ALA B CA  
4358 C C   . ALA D 19  ? 0.93636 1.15045 0.83488 -0.11440 -0.01843 0.08350  18  ALA B C   
4359 O O   . ALA D 19  ? 1.20810 1.41998 1.11070 -0.12932 -0.02057 0.11088  18  ALA B O   
4360 C CB  . ALA D 19  ? 0.90015 1.16823 0.76163 -0.08581 0.02469  0.07323  18  ALA B CB  
4361 N N   . VAL D 20  ? 0.83354 1.03230 0.76509 -0.11213 -0.02606 0.06431  19  VAL B N   
4362 C CA  . VAL D 20  ? 0.78708 0.96418 0.75407 -0.12323 -0.03584 0.07159  19  VAL B CA  
4363 C C   . VAL D 20  ? 0.75575 0.93926 0.75513 -0.12073 -0.02842 0.05933  19  VAL B C   
4364 O O   . VAL D 20  ? 0.84469 1.03200 0.84720 -0.10751 -0.02556 0.03832  19  VAL B O   
4365 C CB  . VAL D 20  ? 0.78173 0.92888 0.75200 -0.11895 -0.05570 0.06598  19  VAL B CB  
4366 C CG1 . VAL D 20  ? 0.76888 0.89152 0.76853 -0.12126 -0.05887 0.06996  19  VAL B CG1 
4367 C CG2 . VAL D 20  ? 0.94028 1.08133 0.88276 -0.12205 -0.06665 0.08324  19  VAL B CG2 
4368 N N   . ASN D 21  ? 0.64775 0.82745 0.66845 -0.13385 -0.02878 0.07279  20  ASN B N   
4369 C CA  . ASN D 21  ? 0.54496 0.72831 0.59311 -0.13307 -0.02674 0.06478  20  ASN B CA  
4370 C C   . ASN D 21  ? 0.67337 0.81414 0.72517 -0.13371 -0.03980 0.06151  20  ASN B C   
4371 O O   . ASN D 21  ? 0.81966 0.93197 0.86082 -0.14376 -0.04911 0.07429  20  ASN B O   
4372 C CB  . ASN D 21  ? 0.53140 0.74626 0.59962 -0.14794 -0.02049 0.08397  20  ASN B CB  
4373 C CG  . ASN D 21  ? 0.68136 0.94513 0.74697 -0.14108 0.00047  0.09178  20  ASN B CG  
4374 O OD1 . ASN D 21  ? 0.69450 0.98548 0.77198 -0.12553 0.01414  0.08101  20  ASN B OD1 
4375 N ND2 . ASN D 21  ? 0.73163 1.00497 0.77840 -0.14930 0.00520  0.11216  20  ASN B ND2 
4376 N N   . LEU D 22  ? 0.63717 0.77040 0.70077 -0.12059 -0.03888 0.04575  21  LEU B N   
4377 C CA  . LEU D 22  ? 0.62217 0.71841 0.68455 -0.11388 -0.04471 0.04357  21  LEU B CA  
4378 C C   . LEU D 22  ? 0.60311 0.69611 0.67375 -0.11261 -0.04497 0.03903  21  LEU B C   
4379 O O   . LEU D 22  ? 0.55925 0.68233 0.64774 -0.11098 -0.03953 0.03404  21  LEU B O   
4380 C CB  . LEU D 22  ? 0.60284 0.69410 0.67474 -0.09876 -0.04340 0.03626  21  LEU B CB  
4381 C CG  . LEU D 22  ? 0.67392 0.76747 0.73892 -0.09941 -0.04974 0.04156  21  LEU B CG  
4382 C CD1 . LEU D 22  ? 0.48305 0.57661 0.57042 -0.08858 -0.05392 0.03790  21  LEU B CD1 
4383 C CD2 . LEU D 22  ? 0.96471 1.03291 1.01276 -0.10376 -0.05472 0.05736  21  LEU B CD2 
4384 N N   . ARG D 23  ? 0.74756 0.80040 0.80019 -0.11034 -0.05180 0.04085  22  ARG B N   
4385 C CA  . ARG D 23  ? 0.47460 0.51472 0.52207 -0.10825 -0.05684 0.03702  22  ARG B CA  
4386 C C   . ARG D 23  ? 0.67892 0.69263 0.71573 -0.08547 -0.04850 0.03207  22  ARG B C   
4387 O O   . ARG D 23  ? 0.96050 0.96162 0.99578 -0.07308 -0.04054 0.03483  22  ARG B O   
4388 C CB  . ARG D 23  ? 0.79372 0.79982 0.81602 -0.12509 -0.07593 0.04304  22  ARG B CB  
4389 C CG  . ARG D 23  ? 0.72573 0.76639 0.77094 -0.15098 -0.08517 0.05549  22  ARG B CG  
4390 C CD  . ARG D 23  ? 0.83932 0.83978 0.86448 -0.17184 -0.11185 0.06225  22  ARG B CD  
4391 N NE  . ARG D 23  ? 0.72048 0.69965 0.72962 -0.16651 -0.12515 0.05330  22  ARG B NE  
4392 C CZ  . ARG D 23  ? 0.86455 0.78878 0.83760 -0.17820 -0.15334 0.05144  22  ARG B CZ  
4393 N NH1 . ARG D 23  ? 0.70176 0.58134 0.65388 -0.19671 -0.17168 0.05748  22  ARG B NH1 
4394 N NH2 . ARG D 23  ? 0.64511 0.55287 0.59790 -0.17101 -0.16605 0.04330  22  ARG B NH2 
4395 N N   . CYS D 24  ? 0.55110 0.56059 0.58335 -0.07919 -0.04989 0.02885  23  CYS B N   
4396 C CA  . CYS D 24  ? 0.60197 0.58559 0.61747 -0.05620 -0.03951 0.02895  23  CYS B CA  
4397 C C   . CYS D 24  ? 0.70563 0.67400 0.69723 -0.05491 -0.04988 0.02677  23  CYS B C   
4398 O O   . CYS D 24  ? 0.70949 0.71107 0.72692 -0.06420 -0.05624 0.02681  23  CYS B O   
4399 C CB  . CYS D 24  ? 0.53486 0.54845 0.59020 -0.04424 -0.02328 0.03160  23  CYS B CB  
4400 S SG  . CYS D 24  ? 0.92731 0.91935 0.97408 -0.01550 -0.00390 0.04258  23  CYS B SG  
4401 N N   . ILE D 25  ? 0.81347 0.73009 0.75234 -0.04062 -0.05198 0.02526  24  ILE B N   
4402 C CA  . ILE D 25  ? 0.70240 0.59242 0.60178 -0.03870 -0.06783 0.02206  24  ILE B CA  
4403 C C   . ILE D 25  ? 0.73685 0.61196 0.61319 -0.00734 -0.04674 0.02689  24  ILE B C   
4404 O O   . ILE D 25  ? 0.86041 0.71151 0.71646 0.01545  -0.02602 0.03063  24  ILE B O   
4405 C CB  . ILE D 25  ? 0.77796 0.60608 0.61738 -0.04862 -0.09382 0.01427  24  ILE B CB  
4406 C CG1 . ILE D 25  ? 0.61220 0.45806 0.48243 -0.08098 -0.11112 0.01689  24  ILE B CG1 
4407 C CG2 . ILE D 25  ? 0.76073 0.56111 0.55755 -0.05121 -0.11943 0.01007  24  ILE B CG2 
4408 C CD1 . ILE D 25  ? 1.08930 0.86823 0.90739 -0.09547 -0.14022 0.01159  24  ILE B CD1 
4409 N N   . LEU D 26  ? 0.81419 0.70684 0.69687 -0.00449 -0.05029 0.03088  25  LEU B N   
4410 C CA  . LEU D 26  ? 0.71446 0.59527 0.57415 0.02429  -0.03035 0.04065  25  LEU B CA  
4411 C C   . LEU D 26  ? 0.84190 0.66008 0.61163 0.03782  -0.04480 0.03428  25  LEU B C   
4412 O O   . LEU D 26  ? 0.92977 0.73164 0.67459 0.01861  -0.07938 0.02547  25  LEU B O   
4413 C CB  . LEU D 26  ? 0.66065 0.58669 0.56966 0.02234  -0.02766 0.05032  25  LEU B CB  
4414 C CG  . LEU D 26  ? 0.73322 0.65277 0.62660 0.04935  -0.00719 0.06682  25  LEU B CG  
4415 C CD1 . LEU D 26  ? 0.74414 0.66766 0.65677 0.06817  0.02643  0.08037  25  LEU B CD1 
4416 C CD2 . LEU D 26  ? 0.60229 0.56041 0.54559 0.04464  -0.01026 0.07610  25  LEU B CD2 
4417 N N   . LYS D 27  ? 0.92881 0.71166 0.64903 0.07171  -0.01917 0.04011  26  LYS B N   
4418 C CA  . LYS D 27  ? 1.02692 0.73767 0.64293 0.09268  -0.02914 0.03115  26  LYS B CA  
4419 C C   . LYS D 27  ? 1.04363 0.75133 0.62427 0.12265  -0.01003 0.04646  26  LYS B C   
4420 O O   . LYS D 27  ? 1.33307 0.97713 0.81397 0.14650  -0.01501 0.03950  26  LYS B O   
4421 C CB  . LYS D 27  ? 0.97953 0.63552 0.54307 0.11589  -0.01299 0.02366  26  LYS B CB  
4422 C CG  . LYS D 27  ? 0.87776 0.51849 0.45570 0.08774  -0.03704 0.00912  26  LYS B CG  
4423 C CD  . LYS D 27  ? 1.49351 1.06886 1.01062 0.11600  -0.02247 0.00191  26  LYS B CD  
4424 C CE  . LYS D 27  ? 1.67208 1.22538 1.20034 0.08691  -0.04905 -0.00963 26  LYS B CE  
4425 N NZ  . LYS D 27  ? 1.73285 1.21411 1.19916 0.11738  -0.03640 -0.01680 26  LYS B NZ  
4426 N N   . ASN D 28  ? 0.94559 0.71440 0.59948 0.12292  0.01062  0.06747  27  ASN B N   
4427 C CA  . ASN D 28  ? 0.87912 0.65054 0.50937 0.14935  0.03037  0.08862  27  ASN B CA  
4428 C C   . ASN D 28  ? 0.93637 0.76164 0.63941 0.12854  0.01822  0.09938  27  ASN B C   
4429 O O   . ASN D 28  ? 0.94385 0.81820 0.73624 0.11190  0.02638  0.10445  27  ASN B O   
4430 C CB  . ASN D 28  ? 1.00860 0.79454 0.65692 0.18145  0.08091  0.11379  27  ASN B CB  
4431 C CG  . ASN D 28  ? 1.15591 0.92598 0.74715 0.21753  0.10587  0.13721  27  ASN B CG  
4432 O OD1 . ASN D 28  ? 1.37418 1.14383 0.94589 0.21357  0.08781  0.14155  27  ASN B OD1 
4433 N ND2 . ASN D 28  ? 1.31411 1.07389 0.87894 0.25544  0.14938  0.15588  27  ASN B ND2 
4434 N N   . SER D 29  ? 1.14131 0.95279 0.80148 0.13167  -0.00296 0.10247  28  SER B N   
4435 C CA  . SER D 29  ? 0.94171 0.79976 0.66656 0.11648  -0.01604 0.11369  28  SER B CA  
4436 C C   . SER D 29  ? 1.06477 0.95678 0.84690 0.13129  0.01959  0.14251  28  SER B C   
4437 O O   . SER D 29  ? 0.97309 0.90478 0.83031 0.11705  0.01478  0.14895  28  SER B O   
4438 C CB  . SER D 29  ? 1.10345 0.93781 0.76640 0.11811  -0.05050 0.11373  28  SER B CB  
4439 O OG  . SER D 29  ? 1.50438 1.30740 1.12400 0.09774  -0.09118 0.08949  28  SER B OG  
4440 N N   . GLN D 30  ? 0.95784 0.83400 0.70805 0.16038  0.05556  0.16195  29  GLN B N   
4441 C CA  . GLN D 30  ? 0.89324 0.80230 0.70390 0.17154  0.08865  0.19617  29  GLN B CA  
4442 C C   . GLN D 30  ? 0.84178 0.78879 0.74939 0.15383  0.10209  0.19808  29  GLN B C   
4443 O O   . GLN D 30  ? 0.95897 0.93142 0.92524 0.15856  0.12658  0.22777  29  GLN B O   
4444 C CB  . GLN D 30  ? 1.06336 0.94975 0.81034 0.21057  0.12616  0.22317  29  GLN B CB  
4445 C CG  . GLN D 30  ? 1.25768 1.10640 0.90595 0.23220  0.11518  0.22871  29  GLN B CG  
4446 C CD  . GLN D 30  ? 1.35925 1.19220 0.94820 0.27544  0.16032  0.26227  29  GLN B CD  
4447 O OE1 . GLN D 30  ? 1.54522 1.39681 1.16771 0.29053  0.20119  0.28148  29  GLN B OE1 
4448 N NE2 . GLN D 30  ? 1.65202 1.45394 1.15329 0.29709  0.15364  0.27273  29  GLN B NE2 
4449 N N   . TYR D 31  ? 0.80293 0.75284 0.72793 0.13234  0.08420  0.16953  36  TYR B N   
4450 C CA  . TYR D 31  ? 0.70838 0.69031 0.71579 0.11379  0.08930  0.16747  36  TYR B CA  
4451 C C   . TYR D 31  ? 0.66810 0.66436 0.70753 0.08550  0.05857  0.14055  36  TYR B C   
4452 O O   . TYR D 31  ? 0.76372 0.76206 0.80878 0.07095  0.04911  0.12074  36  TYR B O   
4453 C CB  . TYR D 31  ? 0.79374 0.76736 0.78789 0.12214  0.10564  0.16497  36  TYR B CB  
4454 C CG  . TYR D 31  ? 0.85164 0.81738 0.81835 0.15632  0.14336  0.19494  36  TYR B CG  
4455 C CD1 . TYR D 31  ? 0.94145 0.86347 0.80839 0.18521  0.15126  0.19363  36  TYR B CD1 
4456 C CD2 . TYR D 31  ? 0.79807 0.79992 0.83753 0.16075  0.17061  0.22619  36  TYR B CD2 
4457 C CE1 . TYR D 31  ? 0.90508 0.82017 0.73957 0.22315  0.19196  0.22248  36  TYR B CE1 
4458 C CE2 . TYR D 31  ? 0.87540 0.87988 0.89790 0.19495  0.21074  0.26011  36  TYR B CE2 
4459 C CZ  . TYR D 31  ? 0.94058 0.90186 0.85743 0.22889  0.22466  0.25798  36  TYR B CZ  
4460 O OH  . TYR D 31  ? 1.09082 1.05472 0.98333 0.26945  0.27063  0.29305  36  TYR B OH  
4461 N N   . PRO D 32  ? 0.71522 0.72332 0.77690 0.08000  0.04485  0.14223  37  PRO B N   
4462 C CA  . PRO D 32  ? 0.61037 0.63489 0.69518 0.05999  0.01981  0.11942  37  PRO B CA  
4463 C C   . PRO D 32  ? 0.66539 0.71114 0.81350 0.04517  0.02125  0.10921  37  PRO B C   
4464 O O   . PRO D 32  ? 0.58764 0.64641 0.74457 0.03110  0.00717  0.08907  37  PRO B O   
4465 C CB  . PRO D 32  ? 0.60200 0.63254 0.69065 0.06661  0.00882  0.13003  37  PRO B CB  
4466 C CG  . PRO D 32  ? 0.58152 0.60657 0.68596 0.08260  0.03104  0.15846  37  PRO B CG  
4467 C CD  . PRO D 32  ? 0.72628 0.73614 0.79870 0.09394  0.05411  0.16873  37  PRO B CD  
4468 N N   . TRP D 33  ? 0.59726 0.64599 0.78797 0.04740  0.03617  0.12401  38  TRP B N   
4469 C CA  . TRP D 33  ? 0.50460 0.56365 0.74762 0.03270  0.03108  0.11254  38  TRP B CA  
4470 C C   . TRP D 33  ? 0.49608 0.55831 0.73227 0.02329  0.03145  0.10154  38  TRP B C   
4471 O O   . TRP D 33  ? 0.52278 0.58585 0.77243 0.02663  0.04438  0.11787  38  TRP B O   
4472 C CB  . TRP D 33  ? 0.44489 0.50112 0.73904 0.03389  0.03940  0.13493  38  TRP B CB  
4473 C CG  . TRP D 33  ? 0.51401 0.56313 0.81304 0.04527  0.04038  0.15079  38  TRP B CG  
4474 C CD1 . TRP D 33  ? 0.57070 0.61517 0.84654 0.06173  0.05442  0.17898  38  TRP B CD1 
4475 C CD2 . TRP D 33  ? 0.53035 0.57397 0.85469 0.04476  0.02756  0.14075  38  TRP B CD2 
4476 N NE1 . TRP D 33  ? 0.72602 0.76441 1.01477 0.06879  0.04870  0.18912  38  TRP B NE1 
4477 C CE2 . TRP D 33  ? 0.59660 0.63391 0.91780 0.05942  0.03259  0.16578  38  TRP B CE2 
4478 C CE3 . TRP D 33  ? 0.46735 0.50812 0.81147 0.03727  0.01409  0.11355  38  TRP B CE3 
4479 C CZ2 . TRP D 33  ? 0.62442 0.65347 0.96874 0.06617  0.02339  0.16540  38  TRP B CZ2 
4480 C CZ3 . TRP D 33  ? 0.59766 0.62802 0.96009 0.04691  0.00781  0.11097  38  TRP B CZ3 
4481 C CH2 . TRP D 33  ? 0.45483 0.47984 0.82083 0.06087  0.01185  0.13719  38  TRP B CH2 
4482 N N   . MET D 34  ? 0.47444 0.54213 0.69374 0.01262  0.01833  0.07800  39  MET B N   
4483 C CA  . MET D 34  ? 0.54395 0.61326 0.75477 0.00319  0.01620  0.06819  39  MET B CA  
4484 C C   . MET D 34  ? 0.48262 0.56073 0.73078 -0.00920 0.00784  0.05684  39  MET B C   
4485 O O   . MET D 34  ? 0.56426 0.64439 0.82741 -0.01120 0.00057  0.04508  39  MET B O   
4486 C CB  . MET D 34  ? 0.52602 0.59424 0.69656 -0.00352 0.00568  0.05361  39  MET B CB  
4487 C CG  . MET D 34  ? 0.54689 0.59748 0.67226 0.00569  0.00375  0.05993  39  MET B CG  
4488 S SD  . MET D 34  ? 0.71524 0.75964 0.80166 -0.00972 -0.01685 0.04617  39  MET B SD  
4489 C CE  . MET D 34  ? 0.81720 0.84100 0.88417 -0.01180 -0.01075 0.04314  39  MET B CE  
4490 N N   . SER D 35  ? 0.46469 0.54487 0.72392 -0.01511 0.00763  0.06027  40  SER B N   
4491 C CA  . SER D 35  ? 0.54508 0.62802 0.83431 -0.02772 -0.00590 0.05094  40  SER B CA  
4492 C C   . SER D 35  ? 0.46570 0.55443 0.74098 -0.03552 -0.01203 0.04561  40  SER B C   
4493 O O   . SER D 35  ? 0.57395 0.66213 0.82775 -0.02960 -0.00303 0.05438  40  SER B O   
4494 C CB  . SER D 35  ? 0.40221 0.48394 0.74357 -0.02999 -0.00633 0.07142  40  SER B CB  
4495 O OG  . SER D 35  ? 0.52146 0.59614 0.87517 -0.02115 0.00218  0.08346  40  SER B OG  
4496 N N   . TRP D 36  ? 0.42017 0.50863 0.70198 -0.04697 -0.02876 0.03061  41  TRP B N   
4497 C CA  . TRP D 36  ? 0.43377 0.52785 0.70657 -0.05523 -0.03878 0.02852  41  TRP B CA  
4498 C C   . TRP D 36  ? 0.52360 0.61886 0.84013 -0.06500 -0.05579 0.03787  41  TRP B C   
4499 O O   . TRP D 36  ? 0.60723 0.68906 0.94203 -0.07175 -0.07035 0.02876  41  TRP B O   
4500 C CB  . TRP D 36  ? 0.45697 0.55074 0.69136 -0.06036 -0.04676 0.00521  41  TRP B CB  
4501 C CG  . TRP D 36  ? 0.55847 0.65924 0.76008 -0.05710 -0.03476 0.00324  41  TRP B CG  
4502 C CD1 . TRP D 36  ? 0.59607 0.70358 0.78592 -0.05317 -0.02865 -0.00608 41  TRP B CD1 
4503 C CD2 . TRP D 36  ? 0.69162 0.79198 0.87263 -0.05875 -0.03067 0.01313  41  TRP B CD2 
4504 N NE1 . TRP D 36  ? 0.55575 0.67091 0.72404 -0.05655 -0.02406 -0.00072 41  TRP B NE1 
4505 C CE2 . TRP D 36  ? 0.66492 0.76989 0.82328 -0.06040 -0.02608 0.00920  41  TRP B CE2 
4506 C CE3 . TRP D 36  ? 0.63447 0.72938 0.81653 -0.05808 -0.03157 0.02643  41  TRP B CE3 
4507 C CZ2 . TRP D 36  ? 0.61808 0.71476 0.75172 -0.06531 -0.02633 0.01622  41  TRP B CZ2 
4508 C CZ3 . TRP D 36  ? 0.69418 0.77782 0.84657 -0.05777 -0.02791 0.03157  41  TRP B CZ3 
4509 C CH2 . TRP D 36  ? 0.65052 0.73137 0.77736 -0.06327 -0.02722 0.02550  41  TRP B CH2 
4510 N N   . TYR D 37  ? 0.35579 0.46500 0.69123 -0.06568 -0.05629 0.05722  42  TYR B N   
4511 C CA  . TYR D 37  ? 0.42122 0.54039 0.80703 -0.07786 -0.07711 0.07168  42  TYR B CA  
4512 C C   . TYR D 37  ? 0.44278 0.56857 0.81118 -0.08442 -0.09427 0.06819  42  TYR B C   
4513 O O   . TYR D 37  ? 0.42560 0.55385 0.75997 -0.07538 -0.08120 0.06898  42  TYR B O   
4514 C CB  . TYR D 37  ? 0.42950 0.57096 0.87319 -0.06967 -0.06025 0.10966  42  TYR B CB  
4515 C CG  . TYR D 37  ? 0.43803 0.57527 0.91679 -0.06972 -0.05271 0.12113  42  TYR B CG  
4516 C CD1 . TYR D 37  ? 0.43355 0.55926 0.88056 -0.05442 -0.02881 0.11713  42  TYR B CD1 
4517 C CD2 . TYR D 37  ? 0.37062 0.51402 0.91616 -0.08690 -0.07296 0.13877  42  TYR B CD2 
4518 C CE1 . TYR D 37  ? 0.32841 0.44939 0.80602 -0.05324 -0.02195 0.13109  42  TYR B CE1 
4519 C CE2 . TYR D 37  ? 0.34561 0.48216 0.92611 -0.08830 -0.06642 0.15340  42  TYR B CE2 
4520 C CZ  . TYR D 37  ? 0.40170 0.52737 0.94645 -0.06992 -0.03918 0.14988  42  TYR B CZ  
4521 O OH  . TYR D 37  ? 0.43784 0.55587 1.01577 -0.07009 -0.03268 0.16766  42  TYR B OH  
4522 N N   . GLN D 38  ? 0.49573 0.61962 0.88535 -0.10115 -0.12716 0.06498  43  GLN B N   
4523 C CA  . GLN D 38  ? 0.45994 0.58881 0.83123 -0.10866 -0.15004 0.06266  43  GLN B CA  
4524 C C   . GLN D 38  ? 0.60949 0.76605 1.05204 -0.11690 -0.16824 0.09567  43  GLN B C   
4525 O O   . GLN D 38  ? 0.55100 0.71197 1.05181 -0.12949 -0.18396 0.10839  43  GLN B O   
4526 C CB  . GLN D 38  ? 0.42850 0.52864 0.75125 -0.11992 -0.17887 0.02925  43  GLN B CB  
4527 C CG  . GLN D 38  ? 0.49002 0.59249 0.78852 -0.12846 -0.20794 0.02819  43  GLN B CG  
4528 C CD  . GLN D 38  ? 0.67754 0.74435 0.92478 -0.13776 -0.24082 -0.00432 43  GLN B CD  
4529 O OE1 . GLN D 38  ? 0.84373 0.89465 1.01937 -0.12830 -0.23097 -0.02857 43  GLN B OE1 
4530 N NE2 . GLN D 38  ? 0.80380 0.85615 1.08636 -0.15564 -0.28058 -0.00362 43  GLN B NE2 
4531 N N   . GLN D 39  ? 0.55350 0.72999 0.99700 -0.11002 -0.16682 0.11293  44  GLN B N   
4532 C CA  . GLN D 39  ? 0.57658 0.78702 1.08997 -0.11592 -0.18663 0.14719  44  GLN B CA  
4533 C C   . GLN D 39  ? 0.61130 0.81907 1.09025 -0.12433 -0.21879 0.13991  44  GLN B C   
4534 O O   . GLN D 39  ? 0.64831 0.85141 1.07978 -0.11092 -0.20324 0.13717  44  GLN B O   
4535 C CB  . GLN D 39  ? 0.42173 0.66274 0.97699 -0.09112 -0.14906 0.18352  44  GLN B CB  
4536 C CG  . GLN D 39  ? 0.61807 0.90661 1.26595 -0.09353 -0.16317 0.22753  44  GLN B CG  
4537 C CD  . GLN D 39  ? 0.54332 0.86165 1.23074 -0.06114 -0.11788 0.26467  44  GLN B CD  
4538 O OE1 . GLN D 39  ? 0.65585 0.95082 1.28477 -0.03574 -0.08333 0.25424  44  GLN B OE1 
4539 N NE2 . GLN D 39  ? 0.47698 0.83561 1.24889 -0.06006 -0.11634 0.30615  44  GLN B NE2 
4540 N N   . ASP D 40  ? 0.57308 0.77946 1.07285 -0.14748 -0.26635 0.13768  45  ASP B N   
4541 C CA  . ASP D 40  ? 0.71865 0.91762 1.17531 -0.15635 -0.30288 0.12897  45  ASP B CA  
4542 C C   . ASP D 40  ? 0.71476 0.95712 1.22667 -0.14964 -0.30871 0.17051  45  ASP B C   
4543 O O   . ASP D 40  ? 0.67758 0.95419 1.25566 -0.13401 -0.27913 0.20408  45  ASP B O   
4544 C CB  . ASP D 40  ? 0.86930 1.04018 1.31574 -0.18217 -0.35606 0.10806  45  ASP B CB  
4545 C CG  . ASP D 40  ? 0.91464 1.09675 1.43702 -0.19130 -0.36680 0.13544  45  ASP B CG  
4546 O OD1 . ASP D 40  ? 0.96772 1.18491 1.56062 -0.18065 -0.33458 0.16920  45  ASP B OD1 
4547 O OD2 . ASP D 40  ? 1.08022 1.23436 1.58856 -0.20829 -0.40745 0.12460  45  ASP B OD2 
4548 N N   . LEU D 41  ? 0.77335 1.01363 1.25442 -0.15822 -0.34652 0.16957  46  LEU B N   
4549 C CA  . LEU D 41  ? 0.96108 1.23834 1.48759 -0.14913 -0.35302 0.20866  46  LEU B CA  
4550 C C   . LEU D 41  ? 0.83903 1.14022 1.44985 -0.15365 -0.35746 0.24026  46  LEU B C   
4551 O O   . LEU D 41  ? 0.80451 1.14198 1.46870 -0.13939 -0.34704 0.27854  46  LEU B O   
4552 C CB  . LEU D 41  ? 0.80998 1.07112 1.27053 -0.15670 -0.39127 0.19881  46  LEU B CB  
4553 C CG  . LEU D 41  ? 0.63323 0.86187 0.99085 -0.14662 -0.37214 0.17197  46  LEU B CG  
4554 C CD1 . LEU D 41  ? 1.01395 1.23124 1.30878 -0.15403 -0.41281 0.16893  46  LEU B CD1 
4555 C CD2 . LEU D 41  ? 0.61509 0.85162 0.97810 -0.12055 -0.32041 0.18936  46  LEU B CD2 
4556 N N   . GLN D 42  ? 0.71389 0.99423 1.33796 -0.17217 -0.37251 0.22768  47  GLN B N   
4557 C CA  . GLN D 42  ? 0.75307 1.05463 1.45922 -0.17990 -0.37806 0.26157  47  GLN B CA  
4558 C C   . GLN D 42  ? 0.65091 0.97176 1.41313 -0.16651 -0.33225 0.28231  47  GLN B C   
4559 O O   . GLN D 42  ? 0.54673 0.87952 1.37220 -0.17479 -0.33504 0.30922  47  GLN B O   
4560 C CB  . GLN D 42  ? 0.76906 1.03180 1.45798 -0.20864 -0.42726 0.24093  47  GLN B CB  
4561 C CG  . GLN D 42  ? 1.04871 1.29304 1.68442 -0.22064 -0.47500 0.22641  47  GLN B CG  
4562 C CD  . GLN D 42  ? 1.34774 1.54503 1.95766 -0.24642 -0.52439 0.20291  47  GLN B CD  
4563 O OE1 . GLN D 42  ? 1.44939 1.61474 2.05545 -0.25422 -0.52309 0.18381  47  GLN B OE1 
4564 N NE2 . GLN D 42  ? 1.17319 1.36278 1.76363 -0.25875 -0.56961 0.20472  47  GLN B NE2 
4565 N N   . LYS D 43  ? 0.59406 0.91716 1.33228 -0.14602 -0.29149 0.27241  48  LYS B N   
4566 C CA  . LYS D 43  ? 0.73921 1.07844 1.51717 -0.12815 -0.24392 0.29132  48  LYS B CA  
4567 C C   . LYS D 43  ? 0.62914 0.94397 1.41992 -0.14611 -0.25227 0.28167  48  LYS B C   
4568 O O   . LYS D 43  ? 0.74292 1.07613 1.59502 -0.14401 -0.23812 0.31529  48  LYS B O   
4569 C CB  . LYS D 43  ? 0.56725 0.95179 1.41451 -0.10629 -0.21524 0.34273  48  LYS B CB  
4570 C CG  . LYS D 43  ? 0.82675 1.23108 1.66208 -0.08075 -0.19952 0.35410  48  LYS B CG  
4571 C CD  . LYS D 43  ? 0.90659 1.35034 1.80332 -0.05232 -0.16159 0.40274  48  LYS B CD  
4572 C CE  . LYS D 43  ? 1.08424 1.53798 1.96315 -0.02175 -0.14446 0.41186  48  LYS B CE  
4573 N NZ  . LYS D 43  ? 0.94821 1.37443 1.76355 -0.00159 -0.12191 0.38347  48  LYS B NZ  
4574 N N   . GLN D 44  ? 0.63191 0.90341 1.36266 -0.16197 -0.27466 0.23714  49  GLN B N   
4575 C CA  . GLN D 44  ? 0.63117 0.87013 1.36426 -0.17649 -0.28383 0.22236  49  GLN B CA  
4576 C C   . GLN D 44  ? 0.66445 0.88618 1.35666 -0.16572 -0.25317 0.19558  49  GLN B C   
4577 O O   . GLN D 44  ? 0.44680 0.64613 1.07393 -0.16699 -0.26096 0.15933  49  GLN B O   
4578 C CB  . GLN D 44  ? 0.58477 0.77947 1.28031 -0.20197 -0.33839 0.19233  49  GLN B CB  
4579 C CG  . GLN D 44  ? 0.72616 0.93535 1.46174 -0.21587 -0.37473 0.21872  49  GLN B CG  
4580 C CD  . GLN D 44  ? 0.89430 1.12914 1.72072 -0.22036 -0.36887 0.26492  49  GLN B CD  
4581 O OE1 . GLN D 44  ? 1.14858 1.37154 1.99581 -0.22106 -0.35402 0.26787  49  GLN B OE1 
4582 N NE2 . GLN D 44  ? 0.63946 0.91116 1.52222 -0.22284 -0.38039 0.30437  49  GLN B NE2 
4583 N N   . LEU D 45  ? 0.68328 0.91630 1.41287 -0.15473 -0.21863 0.21603  50  LEU B N   
4584 C CA  . LEU D 45  ? 0.55050 0.77001 1.24835 -0.14405 -0.18859 0.19615  50  LEU B CA  
4585 C C   . LEU D 45  ? 0.57244 0.74366 1.24340 -0.16115 -0.21232 0.16295  50  LEU B C   
4586 O O   . LEU D 45  ? 0.65852 0.81276 1.36043 -0.17518 -0.23469 0.17161  50  LEU B O   
4587 C CB  . LEU D 45  ? 0.45495 0.70303 1.19494 -0.12209 -0.14142 0.23292  50  LEU B CB  
4588 C CG  . LEU D 45  ? 0.47563 0.76453 1.23371 -0.09600 -0.10922 0.26412  50  LEU B CG  
4589 C CD1 . LEU D 45  ? 0.65309 0.96349 1.44668 -0.07218 -0.06466 0.30274  50  LEU B CD1 
4590 C CD2 . LEU D 45  ? 0.41460 0.68843 1.09878 -0.07965 -0.09296 0.23581  50  LEU B CD2 
4591 N N   . GLN D 46  ? 0.49013 0.63376 1.09498 -0.15551 -0.20493 0.12498  51  GLN B N   
4592 C CA  . GLN D 46  ? 0.68144 0.77422 1.24953 -0.16350 -0.22188 0.09002  51  GLN B CA  
4593 C C   . GLN D 46  ? 0.63204 0.71179 1.14279 -0.13983 -0.18227 0.07022  51  GLN B C   
4594 O O   . GLN D 46  ? 0.54355 0.63317 1.00303 -0.12461 -0.16117 0.05994  51  GLN B O   
4595 C CB  . GLN D 46  ? 0.68784 0.74378 1.19881 -0.17639 -0.26478 0.05332  51  GLN B CB  
4596 C CG  . GLN D 46  ? 0.76053 0.75530 1.22882 -0.17996 -0.28364 0.01541  51  GLN B CG  
4597 C CD  . GLN D 46  ? 1.13787 1.08978 1.54159 -0.18959 -0.32765 -0.02036 51  GLN B CD  
4598 O OE1 . GLN D 46  ? 1.34114 1.31216 1.73818 -0.19770 -0.34882 -0.01367 51  GLN B OE1 
4599 N NE2 . GLN D 46  ? 1.50271 1.39304 1.85312 -0.18556 -0.34144 -0.05837 51  GLN B NE2 
4600 N N   . TRP D 47  ? 0.57358 0.63098 1.09729 -0.13845 -0.17546 0.06775  52  TRP B N   
4601 C CA  . TRP D 47  ? 0.41771 0.46486 0.89575 -0.11732 -0.14333 0.05219  52  TRP B CA  
4602 C C   . TRP D 47  ? 0.47840 0.49284 0.88313 -0.11165 -0.15289 0.00817  52  TRP B C   
4603 O O   . TRP D 47  ? 0.56720 0.54494 0.95675 -0.12227 -0.18516 -0.01465 52  TRP B O   
4604 C CB  . TRP D 47  ? 0.42251 0.45702 0.94182 -0.11645 -0.13482 0.06834  52  TRP B CB  
4605 C CG  . TRP D 47  ? 0.46583 0.48283 0.94139 -0.09713 -0.11299 0.04964  52  TRP B CG  
4606 C CD1 . TRP D 47  ? 0.38730 0.42544 0.84515 -0.07823 -0.07929 0.06077  52  TRP B CD1 
4607 C CD2 . TRP D 47  ? 0.45761 0.43130 0.90234 -0.09317 -0.12552 0.01790  52  TRP B CD2 
4608 N NE1 . TRP D 47  ? 0.39684 0.41504 0.82300 -0.06557 -0.07236 0.04105  52  TRP B NE1 
4609 C CE2 . TRP D 47  ? 0.43834 0.41863 0.85767 -0.07197 -0.09713 0.01532  52  TRP B CE2 
4610 C CE3 . TRP D 47  ? 0.51525 0.44105 0.94709 -0.10328 -0.15935 -0.00934 52  TRP B CE3 
4611 C CZ2 . TRP D 47  ? 0.56464 0.51402 0.95613 -0.05857 -0.09767 -0.00958 52  TRP B CZ2 
4612 C CZ3 . TRP D 47  ? 0.55174 0.43763 0.94533 -0.08719 -0.15785 -0.03812 52  TRP B CZ3 
4613 C CH2 . TRP D 47  ? 0.52424 0.42636 0.90282 -0.06407 -0.12530 -0.03616 52  TRP B CH2 
4614 N N   . LEU D 48  ? 0.49154 0.51824 0.84946 -0.09400 -0.12509 -0.00237 53  LEU B N   
4615 C CA  . LEU D 48  ? 0.53836 0.54777 0.83218 -0.08444 -0.12496 -0.03638 53  LEU B CA  
4616 C C   . LEU D 48  ? 0.61621 0.61591 0.89955 -0.06755 -0.10514 -0.04576 53  LEU B C   
4617 O O   . LEU D 48  ? 0.57864 0.54243 0.85006 -0.06237 -0.11614 -0.06657 53  LEU B O   
4618 C CB  . LEU D 48  ? 0.51472 0.55112 0.77040 -0.08075 -0.11255 -0.03657 53  LEU B CB  
4619 C CG  . LEU D 48  ? 0.54451 0.58969 0.80140 -0.09375 -0.13318 -0.02885 53  LEU B CG  
4620 C CD1 . LEU D 48  ? 0.53283 0.59715 0.74634 -0.08862 -0.11970 -0.02952 53  LEU B CD1 
4621 C CD2 . LEU D 48  ? 0.49284 0.50517 0.73335 -0.10451 -0.16979 -0.04974 53  LEU B CD2 
4622 N N   . PHE D 49  ? 0.62283 0.64976 0.90769 -0.05750 -0.07858 -0.03124 54  PHE B N   
4623 C CA  . PHE D 49  ? 0.50969 0.53528 0.78793 -0.04150 -0.06225 -0.03594 54  PHE B CA  
4624 C C   . PHE D 49  ? 0.69491 0.73411 1.00297 -0.03796 -0.04716 -0.00807 54  PHE B C   
4625 O O   . PHE D 49  ? 0.59842 0.65102 0.92334 -0.04376 -0.04291 0.01335  54  PHE B O   
4626 C CB  . PHE D 49  ? 0.84521 0.89312 1.08310 -0.03154 -0.04782 -0.04792 54  PHE B CB  
4627 C CG  . PHE D 49  ? 0.64025 0.68524 0.83945 -0.03402 -0.05598 -0.06731 54  PHE B CG  
4628 C CD1 . PHE D 49  ? 0.64538 0.66631 0.81542 -0.02157 -0.06003 -0.09283 54  PHE B CD1 
4629 C CD2 . PHE D 49  ? 0.51508 0.57762 0.70075 -0.04535 -0.05841 -0.05940 54  PHE B CD2 
4630 C CE1 . PHE D 49  ? 0.79256 0.80878 0.91545 -0.02026 -0.06558 -0.10988 54  PHE B CE1 
4631 C CE2 . PHE D 49  ? 0.56193 0.62219 0.70756 -0.04671 -0.06575 -0.07376 54  PHE B CE2 
4632 C CZ  . PHE D 49  ? 0.80241 0.84046 0.91392 -0.03408 -0.06891 -0.09891 54  PHE B CZ  
4633 N N   . THR D 50  ? 0.67356 0.70877 0.98413 -0.02468 -0.03782 -0.00751 55  THR B N   
4634 C CA  . THR D 50  ? 0.47022 0.51783 0.79136 -0.01712 -0.02315 0.01661  55  THR B CA  
4635 C C   . THR D 50  ? 0.52504 0.58281 0.82904 -0.00284 -0.01600 0.00919  55  THR B C   
4636 O O   . THR D 50  ? 0.64963 0.69242 0.96356 0.00763  -0.01828 0.00023  55  THR B O   
4637 C CB  . THR D 50  ? 0.58617 0.61693 0.94921 -0.01804 -0.02399 0.03879  55  THR B CB  
4638 O OG1 . THR D 50  ? 0.50897 0.54375 0.89938 -0.03171 -0.02868 0.05453  55  THR B OG1 
4639 C CG2 . THR D 50  ? 0.43020 0.47072 0.79092 -0.00501 -0.00748 0.06261  55  THR B CG2 
4640 N N   . LEU D 51  ? 0.55915 0.64052 0.83983 -0.00226 -0.00960 0.01397  56  LEU B N   
4641 C CA  . LEU D 51  ? 0.49649 0.59764 0.76952 0.00726  -0.00689 0.01231  56  LEU B CA  
4642 C C   . LEU D 51  ? 0.54010 0.64399 0.80766 0.01224  -0.00535 0.03321  56  LEU B C   
4643 O O   . LEU D 51  ? 0.59630 0.69223 0.84608 0.00795  -0.00308 0.04427  56  LEU B O   
4644 C CB  . LEU D 51  ? 0.49069 0.61708 0.74271 -0.00040 -0.00714 0.00262  56  LEU B CB  
4645 C CG  . LEU D 51  ? 0.44129 0.56485 0.68478 -0.00300 -0.00740 -0.01690 56  LEU B CG  
4646 C CD1 . LEU D 51  ? 0.62472 0.77863 0.85040 -0.00933 -0.00383 -0.01901 56  LEU B CD1 
4647 C CD2 . LEU D 51  ? 0.54849 0.65662 0.80198 0.01346  -0.00566 -0.03134 56  LEU B CD2 
4648 N N   . ARG D 52  ? 0.58900 0.70239 0.86765 0.02447  -0.00654 0.03896  57  ARG B N   
4649 C CA  . ARG D 52  ? 0.45101 0.56255 0.71973 0.03141  -0.00879 0.05961  57  ARG B CA  
4650 C C   . ARG D 52  ? 0.59036 0.73051 0.85349 0.03275  -0.01952 0.06290  57  ARG B C   
4651 O O   . ARG D 52  ? 0.64836 0.78808 0.88035 0.02629  -0.02966 0.07057  57  ARG B O   
4652 C CB  . ARG D 52  ? 0.51899 0.61169 0.81360 0.04481  -0.00447 0.07318  57  ARG B CB  
4653 C CG  . ARG D 52  ? 0.70348 0.79507 0.98451 0.05575  -0.00672 0.09716  57  ARG B CG  
4654 C CD  . ARG D 52  ? 0.68467 0.76391 0.92496 0.05282  -0.00198 0.10945  57  ARG B CD  
4655 N NE  . ARG D 52  ? 0.64147 0.71366 0.85517 0.06621  -0.00448 0.13184  57  ARG B NE  
4656 C CZ  . ARG D 52  ? 0.63378 0.71370 0.81299 0.06713  -0.02161 0.13228  57  ARG B CZ  
4657 N NH1 . ARG D 52  ? 0.66619 0.76461 0.84151 0.05350  -0.03645 0.11478  57  ARG B NH1 
4658 N NH2 . ARG D 52  ? 0.66604 0.73462 0.81420 0.08069  -0.02618 0.15331  57  ARG B NH2 
4659 N N   A SER D 53  ? 0.57508 0.73880 0.86834 0.04209  -0.01869 0.05806  58  SER B N   
4660 N N   B SER D 53  ? 0.57560 0.73937 0.86906 0.04221  -0.01869 0.05811  58  SER B N   
4661 C CA  A SER D 53  ? 0.55755 0.75968 0.86248 0.04355  -0.02947 0.06782  58  SER B CA  
4662 C CA  B SER D 53  ? 0.55317 0.75550 0.85838 0.04366  -0.02941 0.06779  58  SER B CA  
4663 C C   A SER D 53  ? 0.52259 0.75687 0.82943 0.02881  -0.03036 0.05961  58  SER B C   
4664 C C   B SER D 53  ? 0.50767 0.74178 0.81426 0.02869  -0.03039 0.05958  58  SER B C   
4665 O O   A SER D 53  ? 0.43996 0.67104 0.74500 0.02687  -0.01797 0.04368  58  SER B O   
4666 O O   B SER D 53  ? 0.48165 0.71221 0.78596 0.02645  -0.01814 0.04365  58  SER B O   
4667 C CB  A SER D 53  ? 0.52937 0.74697 0.87339 0.06697  -0.02447 0.07360  58  SER B CB  
4668 C CB  B SER D 53  ? 0.53650 0.75470 0.88101 0.06706  -0.02424 0.07330  58  SER B CB  
4669 O OG  A SER D 53  ? 0.54205 0.75198 0.89963 0.07795  -0.00856 0.05455  58  SER B OG  
4670 O OG  B SER D 53  ? 0.46823 0.65756 0.81394 0.07971  -0.02559 0.08665  58  SER B OG  
4671 N N   . PRO D 54  ? 0.44802 0.71213 0.75790 0.01662  -0.04748 0.07257  63  PRO B N   
4672 C CA  . PRO D 54  ? 0.40972 0.70893 0.73070 -0.00000 -0.04850 0.07203  63  PRO B CA  
4673 C C   . PRO D 54  ? 0.49592 0.83738 0.85805 0.01730  -0.02799 0.07098  63  PRO B C   
4674 O O   . PRO D 54  ? 0.57129 0.93344 0.96626 0.03937  -0.02318 0.07940  63  PRO B O   
4675 C CB  . PRO D 54  ? 0.35201 0.67203 0.67690 -0.01731 -0.07775 0.09105  63  PRO B CB  
4676 C CG  . PRO D 54  ? 0.52700 0.80419 0.81434 -0.01175 -0.09201 0.09391  63  PRO B CG  
4677 C CD  . PRO D 54  ? 0.57635 0.83905 0.87560 0.01449  -0.07058 0.09005  63  PRO B CD  
4678 N N   . GLY D 55  ? 0.32466 0.67654 0.68036 0.01068  -0.01432 0.06145  64  GLY B N   
4679 C CA  . GLY D 55  ? 0.33071 0.71645 0.70942 0.03149  0.01020  0.05807  64  GLY B CA  
4680 C C   . GLY D 55  ? 0.48193 0.82449 0.83327 0.05095  0.02718  0.03130  64  GLY B C   
4681 O O   . GLY D 55  ? 0.52619 0.88481 0.87980 0.07236  0.04847  0.02324  64  GLY B O   
4682 N N   . ASP D 56  ? 0.52866 0.81648 0.85369 0.04493  0.01775  0.01877  65  ASP B N   
4683 C CA  . ASP D 56  ? 0.49001 0.73316 0.79326 0.05665  0.02530  -0.00500 65  ASP B CA  
4684 C C   . ASP D 56  ? 0.49415 0.73697 0.76695 0.04722  0.03133  -0.01845 65  ASP B C   
4685 O O   . ASP D 56  ? 0.60501 0.86092 0.86769 0.02441  0.02502  -0.01009 65  ASP B O   
4686 C CB  . ASP D 56  ? 0.61379 0.80904 0.90906 0.04789  0.01260  -0.00632 65  ASP B CB  
4687 C CG  . ASP D 56  ? 0.71370 0.90221 1.03293 0.06109  0.00868  0.00771  65  ASP B CG  
4688 O OD1 . ASP D 56  ? 0.82381 1.04259 1.16734 0.07855  0.01371  0.01607  65  ASP B OD1 
4689 O OD2 . ASP D 56  ? 0.68641 0.84287 1.00274 0.05541  0.00176  0.01411  65  ASP B OD2 
4690 N N   . LYS D 57  ? 0.48839 0.70983 0.74074 0.06628  0.04182  -0.03977 66  LYS B N   
4691 C CA  . LYS D 57  ? 0.50817 0.72804 0.72286 0.06260  0.04784  -0.05283 66  LYS B CA  
4692 C C   . LYS D 57  ? 0.70932 0.86893 0.89010 0.07304  0.04062  -0.08172 66  LYS B C   
4693 O O   . LYS D 57  ? 0.93919 1.07556 1.11386 0.10063  0.04821  -0.09679 66  LYS B O   
4694 C CB  . LYS D 57  ? 0.51400 0.78606 0.73123 0.08047  0.07257  -0.04469 66  LYS B CB  
4695 C CG  . LYS D 57  ? 0.79512 1.07294 0.96957 0.07727  0.08198  -0.05139 66  LYS B CG  
4696 C CD  . LYS D 57  ? 0.62687 0.96513 0.81111 0.09802  0.11257  -0.03552 66  LYS B CD  
4697 C CE  . LYS D 57  ? 1.06583 1.40907 1.19997 0.09874  0.12556  -0.03938 66  LYS B CE  
4698 N NZ  . LYS D 57  ? 0.75683 1.16524 0.90299 0.12230  0.16171  -0.01820 66  LYS B NZ  
4699 N N   . GLU D 58  ? 0.75035 0.88200 0.91020 0.05138  0.02333  -0.08867 67  GLU B N   
4700 C CA  . GLU D 58  ? 0.88148 0.95506 1.01371 0.05317  0.00669  -0.11337 67  GLU B CA  
4701 C C   . GLU D 58  ? 0.71222 0.78126 0.79864 0.04372  0.00035  -0.12386 67  GLU B C   
4702 O O   . GLU D 58  ? 0.73412 0.83795 0.82097 0.02733  0.00364  -0.10724 67  GLU B O   
4703 C CB  . GLU D 58  ? 0.79466 0.83816 0.95905 0.03437  -0.01445 -0.10567 67  GLU B CB  
4704 C CG  . GLU D 58  ? 0.86389 0.90189 1.06675 0.04504  -0.01055 -0.09473 67  GLU B CG  
4705 C CD  . GLU D 58  ? 1.21297 1.20806 1.40542 0.07050  -0.01046 -0.11598 67  GLU B CD  
4706 O OE1 . GLU D 58  ? 1.40449 1.35688 1.55790 0.07469  -0.02168 -0.14231 67  GLU B OE1 
4707 O OE2 . GLU D 58  ? 1.27908 1.27827 1.49813 0.08774  -0.00118 -0.10681 67  GLU B OE2 
4708 N N   . VAL D 59  ? 0.93450 0.95417 0.97710 0.05437  -0.01182 -0.15171 68  VAL B N   
4709 C CA  . VAL D 59  ? 0.93683 0.94468 0.92385 0.04958  -0.02133 -0.16447 68  VAL B CA  
4710 C C   . VAL D 59  ? 0.76119 0.70929 0.73730 0.03379  -0.05995 -0.18173 68  VAL B C   
4711 O O   . VAL D 59  ? 1.14173 1.03953 1.12066 0.04166  -0.07385 -0.19909 68  VAL B O   
4712 C CB  . VAL D 59  ? 0.84652 0.85274 0.77230 0.08330  0.00187  -0.18288 68  VAL B CB  
4713 C CG1 . VAL D 59  ? 1.24172 1.22613 1.09748 0.08005  -0.01165 -0.19745 68  VAL B CG1 
4714 C CG2 . VAL D 59  ? 0.81459 0.89264 0.76548 0.09476  0.03915  -0.15731 68  VAL B CG2 
4715 N N   . LYS D 60  ? 0.81817 0.77170 0.78676 0.01053  -0.07957 -0.17419 69  LYS B N   
4716 C CA  . LYS D 60  ? 0.98367 0.88964 0.94546 -0.00765 -0.12099 -0.18619 69  LYS B CA  
4717 C C   . LYS D 60  ? 1.02149 0.92985 0.92826 -0.01381 -0.13435 -0.19062 69  LYS B C   
4718 O O   . LYS D 60  ? 1.01496 0.97094 0.92818 -0.02087 -0.11905 -0.16814 69  LYS B O   
4719 C CB  . LYS D 60  ? 0.87253 0.79134 0.91140 -0.03418 -0.13601 -0.15955 69  LYS B CB  
4720 C CG  . LYS D 60  ? 0.72649 0.59489 0.79641 -0.04404 -0.16584 -0.16722 69  LYS B CG  
4721 C CD  . LYS D 60  ? 0.88591 0.78036 1.03707 -0.06629 -0.17089 -0.13240 69  LYS B CD  
4722 C CE  . LYS D 60  ? 0.84609 0.69549 1.03921 -0.07982 -0.20023 -0.13219 69  LYS B CE  
4723 N NZ  . LYS D 60  ? 1.22019 1.03540 1.40742 -0.05990 -0.18757 -0.14672 69  LYS B NZ  
4724 N N   . SER D 61  ? 1.22137 1.07295 1.07010 -0.01121 -0.16567 -0.21936 70  SER B N   
4725 C CA  . SER D 61  ? 1.00472 0.85049 0.78720 -0.01407 -0.18278 -0.22603 70  SER B CA  
4726 C C   . SER D 61  ? 1.16805 0.97091 0.95784 -0.04093 -0.24000 -0.23270 70  SER B C   
4727 O O   . SER D 61  ? 1.51288 1.24686 1.25575 -0.03686 -0.27201 -0.26495 70  SER B O   
4728 C CB  . SER D 61  ? 1.03689 0.85402 0.71989 0.02097  -0.16510 -0.25586 70  SER B CB  
4729 O OG  . SER D 61  ? 1.45895 1.27074 1.06999 0.01985  -0.18036 -0.25958 70  SER B OG  
4730 N N   . LEU D 62  ? 0.94893 0.79062 0.79855 -0.06758 -0.25438 -0.20130 71  LEU B N   
4731 C CA  . LEU D 62  ? 1.27473 1.09447 1.14673 -0.09539 -0.30858 -0.19709 71  LEU B CA  
4732 C C   . LEU D 62  ? 1.20050 1.03554 1.02324 -0.10001 -0.32520 -0.19023 71  LEU B C   
4733 O O   . LEU D 62  ? 1.17250 1.04636 0.96781 -0.08663 -0.28976 -0.17821 71  LEU B O   
4734 C CB  . LEU D 62  ? 1.02700 0.88450 1.01263 -0.11833 -0.31109 -0.16048 71  LEU B CB  
4735 C CG  . LEU D 62  ? 0.94862 0.87366 0.98484 -0.12150 -0.28220 -0.12204 71  LEU B CG  
4736 C CD1 . LEU D 62  ? 1.27668 1.22052 1.33762 -0.14129 -0.31712 -0.09983 71  LEU B CD1 
4737 C CD2 . LEU D 62  ? 0.72622 0.67669 0.84408 -0.12320 -0.25691 -0.09883 71  LEU B CD2 
4738 N N   . PRO D 63  ? 1.31659 1.12101 1.12782 -0.12011 -0.38174 -0.19530 72  PRO B N   
4739 C CA  . PRO D 63  ? 1.35950 1.17198 1.11092 -0.12178 -0.40191 -0.19046 72  PRO B CA  
4740 C C   . PRO D 63  ? 1.29916 1.18304 1.10635 -0.12737 -0.37699 -0.14724 72  PRO B C   
4741 O O   . PRO D 63  ? 1.34303 1.26163 1.24671 -0.14479 -0.38237 -0.11662 72  PRO B O   
4742 C CB  . PRO D 63  ? 1.37521 1.14567 1.13230 -0.14888 -0.47514 -0.19790 72  PRO B CB  
4743 C CG  . PRO D 63  ? 1.38677 1.15969 1.24965 -0.16646 -0.47904 -0.18440 72  PRO B CG  
4744 C CD  . PRO D 63  ? 1.46535 1.22433 1.31699 -0.14414 -0.43461 -0.20380 72  PRO B CD  
4745 N N   . GLY D 64  ? 1.23973 1.14285 0.98347 -0.11040 -0.34811 -0.14334 73  GLY B N   
4746 C CA  . GLY D 64  ? 1.29453 1.25193 1.07392 -0.11364 -0.32656 -0.10540 73  GLY B CA  
4747 C C   . GLY D 64  ? 1.12994 1.12035 0.91767 -0.09858 -0.26774 -0.09493 73  GLY B C   
4748 O O   . GLY D 64  ? 1.03218 1.05349 0.81506 -0.09727 -0.24902 -0.06996 73  GLY B O   
4749 N N   . ALA D 65  ? 1.02231 1.00536 0.82428 -0.08846 -0.24153 -0.11135 74  ALA B N   
4750 C CA  . ALA D 65  ? 0.91570 0.93311 0.73707 -0.07801 -0.19225 -0.09866 74  ALA B CA  
4751 C C   . ALA D 65  ? 0.87691 0.87807 0.69097 -0.06161 -0.17098 -0.12324 74  ALA B C   
4752 O O   . ALA D 65  ? 0.90830 0.87922 0.74791 -0.06504 -0.18998 -0.13925 74  ALA B O   
4753 C CB  . ALA D 65  ? 0.65320 0.70149 0.55861 -0.09075 -0.18314 -0.06879 74  ALA B CB  
4754 N N   . ASP D 66  ? 0.97252 0.99609 0.75773 -0.04404 -0.13188 -0.12206 75  ASP B N   
4755 C CA  . ASP D 66  ? 0.86863 0.88965 0.65774 -0.02481 -0.10508 -0.13771 75  ASP B CA  
4756 C C   . ASP D 66  ? 0.75865 0.82005 0.62011 -0.03190 -0.08003 -0.11366 75  ASP B C   
4757 O O   . ASP D 66  ? 0.86122 0.95873 0.73478 -0.03967 -0.06415 -0.08824 75  ASP B O   
4758 C CB  . ASP D 66  ? 1.00834 1.03507 0.72427 0.00273  -0.07626 -0.14798 75  ASP B CB  
4759 C CG  . ASP D 66  ? 1.23840 1.21455 0.86294 0.01515  -0.10106 -0.17649 75  ASP B CG  
4760 O OD1 . ASP D 66  ? 1.47942 1.40452 1.10110 0.00619  -0.14139 -0.19894 75  ASP B OD1 
4761 O OD2 . ASP D 66  ? 1.28918 1.27514 0.84302 0.03338  -0.08165 -0.17489 75  ASP B OD2 
4762 N N   . TYR D 67  ? 0.74409 0.79405 0.64921 -0.02968 -0.07938 -0.12125 76  TYR B N   
4763 C CA  . TYR D 67  ? 0.60557 0.68479 0.57283 -0.03651 -0.06280 -0.10046 76  TYR B CA  
4764 C C   . TYR D 67  ? 0.61083 0.70899 0.58413 -0.01757 -0.03371 -0.10354 76  TYR B C   
4765 O O   . TYR D 67  ? 0.87404 0.95431 0.81466 0.00424  -0.02651 -0.12498 76  TYR B O   
4766 C CB  . TYR D 67  ? 0.65813 0.71772 0.67755 -0.04827 -0.08227 -0.09769 76  TYR B CB  
4767 C CG  . TYR D 67  ? 0.67159 0.72915 0.70846 -0.06669 -0.10615 -0.08340 76  TYR B CG  
4768 C CD1 . TYR D 67  ? 0.60671 0.69034 0.66272 -0.07491 -0.09733 -0.05836 76  TYR B CD1 
4769 C CD2 . TYR D 67  ? 0.69903 0.72668 0.73564 -0.07531 -0.13976 -0.09366 76  TYR B CD2 
4770 C CE1 . TYR D 67  ? 0.67492 0.75931 0.75070 -0.08629 -0.11606 -0.04268 76  TYR B CE1 
4771 C CE2 . TYR D 67  ? 0.71586 0.75088 0.77945 -0.09115 -0.16214 -0.07530 76  TYR B CE2 
4772 C CZ  . TYR D 67  ? 0.75973 0.82543 0.84372 -0.09412 -0.14749 -0.04919 76  TYR B CZ  
4773 O OH  . TYR D 67  ? 0.74247 0.81788 0.85670 -0.10454 -0.16666 -0.02851 76  TYR B OH  
4774 N N   . LEU D 68  ? 0.75658 0.88893 0.77120 -0.02473 -0.01876 -0.08130 77  LEU B N   
4775 C CA  . LEU D 68  ? 0.56228 0.72178 0.59788 -0.01046 0.00442  -0.07698 77  LEU B CA  
4776 C C   . LEU D 68  ? 0.55640 0.73235 0.63966 -0.02547 0.00308  -0.05611 77  LEU B C   
4777 O O   . LEU D 68  ? 0.73452 0.93347 0.82310 -0.03981 0.00580  -0.03672 77  LEU B O   
4778 C CB  . LEU D 68  ? 0.65570 0.85392 0.66726 0.00009  0.02879  -0.06791 77  LEU B CB  
4779 C CG  . LEU D 68  ? 0.70181 0.94486 0.74934 0.01198  0.05282  -0.05335 77  LEU B CG  
4780 C CD1 . LEU D 68  ? 0.83096 1.05465 0.88555 0.03813  0.05830  -0.07287 77  LEU B CD1 
4781 C CD2 . LEU D 68  ? 0.67109 0.96063 0.70190 0.02089  0.07909  -0.03679 77  LEU B CD2 
4782 N N   . ALA D 69  ? 0.52488 0.68308 0.63683 -0.02167 -0.00263 -0.05997 78  ALA B N   
4783 C CA  . ALA D 69  ? 0.47509 0.64013 0.61942 -0.03129 -0.00478 -0.04270 78  ALA B CA  
4784 C C   . ALA D 69  ? 0.51792 0.71143 0.68465 -0.02144 0.00726  -0.03472 78  ALA B C   
4785 O O   . ALA D 69  ? 0.53781 0.73708 0.70719 -0.00195 0.01762  -0.04437 78  ALA B O   
4786 C CB  . ALA D 69  ? 0.60598 0.73925 0.76966 -0.03263 -0.01658 -0.04440 78  ALA B CB  
4787 N N   . THR D 70  ? 0.54390 0.75207 0.72513 -0.03366 0.00366  -0.01686 79  THR B N   
4788 C CA  . THR D 70  ? 0.49743 0.73768 0.70451 -0.02941 0.00790  -0.00435 79  THR B CA  
4789 C C   . THR D 70  ? 0.58465 0.81070 0.79798 -0.03878 -0.00580 0.00693  79  THR B C   
4790 O O   . THR D 70  ? 0.62516 0.83063 0.81920 -0.05304 -0.01495 0.01102  79  THR B O   
4791 C CB  . THR D 70  ? 0.42989 0.71427 0.64273 -0.03820 0.01511  0.01027  79  THR B CB  
4792 O OG1 . THR D 70  ? 0.83762 1.13213 1.03152 -0.02547 0.03153  0.00051  79  THR B OG1 
4793 C CG2 . THR D 70  ? 0.69762 1.02472 0.94996 -0.03366 0.01735  0.02712  79  THR B CG2 
4794 N N   . ARG D 71  ? 0.58034 0.81346 0.81495 -0.02742 -0.00685 0.01194  80  ARG B N   
4795 C CA  . ARG D 71  ? 0.55680 0.77808 0.78881 -0.03295 -0.02078 0.02379  80  ARG B CA  
4796 C C   . ARG D 71  ? 0.53736 0.79845 0.78988 -0.04198 -0.03056 0.03965  80  ARG B C   
4797 O O   . ARG D 71  ? 0.48554 0.77766 0.77021 -0.02918 -0.02771 0.04714  80  ARG B O   
4798 C CB  . ARG D 71  ? 0.37211 0.57421 0.61359 -0.01552 -0.01862 0.02365  80  ARG B CB  
4799 C CG  . ARG D 71  ? 0.42427 0.60851 0.64990 -0.01683 -0.03091 0.03627  80  ARG B CG  
4800 C CD  . ARG D 71  ? 0.41739 0.56631 0.60549 -0.02521 -0.03311 0.03509  80  ARG B CD  
4801 N NE  . ARG D 71  ? 0.53068 0.65453 0.68971 -0.01954 -0.04086 0.04523  80  ARG B NE  
4802 C CZ  . ARG D 71  ? 0.49676 0.59952 0.65046 -0.00460 -0.03065 0.05248  80  ARG B CZ  
4803 N NH1 . ARG D 71  ? 0.47450 0.57679 0.65781 0.00193  -0.01658 0.05138  80  ARG B NH1 
4804 N NH2 . ARG D 71  ? 0.48501 0.56461 0.60087 0.00348  -0.03609 0.06269  80  ARG B NH2 
4805 N N   . VAL D 72  ? 0.56444 0.82429 0.80276 -0.06459 -0.04409 0.04709  81  VAL B N   
4806 C CA  . VAL D 72  ? 0.50328 0.80469 0.77027 -0.08041 -0.05777 0.06622  81  VAL B CA  
4807 C C   . VAL D 72  ? 0.64941 0.94628 0.91961 -0.08165 -0.08138 0.07614  81  VAL B C   
4808 O O   . VAL D 72  ? 0.70273 1.04362 1.01536 -0.07420 -0.08369 0.08988  81  VAL B O   
4809 C CB  . VAL D 72  ? 0.44325 0.73599 0.69442 -0.10776 -0.06934 0.07261  81  VAL B CB  
4810 C CG1 . VAL D 72  ? 0.43091 0.76258 0.71788 -0.13070 -0.09099 0.09688  81  VAL B CG1 
4811 C CG2 . VAL D 72  ? 0.33348 0.64065 0.58367 -0.10507 -0.04623 0.06802  81  VAL B CG2 
4812 N N   . THR D 73  ? 0.70006 0.94334 0.92231 -0.08820 -0.09907 0.07044  83  THR B N   
4813 C CA  . THR D 73  ? 0.58624 0.81363 0.79256 -0.08781 -0.12428 0.07776  83  THR B CA  
4814 C C   . THR D 73  ? 0.52864 0.71073 0.69544 -0.06487 -0.11280 0.06807  83  THR B C   
4815 O O   . THR D 73  ? 0.51387 0.68775 0.68344 -0.05085 -0.08694 0.05874  83  THR B O   
4816 C CB  . THR D 73  ? 0.50666 0.70428 0.68007 -0.11509 -0.15952 0.08169  83  THR B CB  
4817 O OG1 . THR D 73  ? 0.64412 0.77864 0.75726 -0.11448 -0.15529 0.06594  83  THR B OG1 
4818 C CG2 . THR D 73  ? 0.50749 0.75331 0.72991 -0.14184 -0.16921 0.09755  83  THR B CG2 
4819 N N   . ASP D 74  ? 0.72105 0.87387 0.85050 -0.06189 -0.13398 0.07294  84  ASP B N   
4820 C CA  . ASP D 74  ? 0.57300 0.68626 0.66302 -0.03877 -0.12073 0.07057  84  ASP B CA  
4821 C C   . ASP D 74  ? 0.73288 0.79989 0.77786 -0.03458 -0.10482 0.05900  84  ASP B C   
4822 O O   . ASP D 74  ? 0.62172 0.67006 0.65390 -0.01451 -0.08305 0.06094  84  ASP B O   
4823 C CB  . ASP D 74  ? 0.85080 0.94045 0.89806 -0.03474 -0.14803 0.07953  84  ASP B CB  
4824 C CG  . ASP D 74  ? 1.25130 1.39097 1.34930 -0.03569 -0.16522 0.09590  84  ASP B CG  
4825 O OD1 . ASP D 74  ? 1.30775 1.48661 1.46269 -0.02265 -0.14340 0.10088  84  ASP B OD1 
4826 O OD2 . ASP D 74  ? 1.40418 1.54145 1.48467 -0.04863 -0.20271 0.10405  84  ASP B OD2 
4827 N N   . THR D 75  ? 0.75160 0.80198 0.77776 -0.05252 -0.11483 0.05095  85  THR B N   
4828 C CA  . THR D 75  ? 0.65191 0.65863 0.63717 -0.04588 -0.10078 0.04200  85  THR B CA  
4829 C C   . THR D 75  ? 0.68163 0.70416 0.69405 -0.06053 -0.09279 0.03669  85  THR B C   
4830 O O   . THR D 75  ? 0.72382 0.71433 0.70930 -0.05491 -0.08228 0.03155  85  THR B O   
4831 C CB  . THR D 75  ? 0.76419 0.70778 0.67183 -0.04643 -0.12330 0.03631  85  THR B CB  
4832 O OG1 . THR D 75  ? 0.92826 0.87383 0.83952 -0.07605 -0.15871 0.03603  85  THR B OG1 
4833 C CG2 . THR D 75  ? 0.77034 0.68925 0.63272 -0.02559 -0.12736 0.04146  85  THR B CG2 
4834 N N   . GLU D 76  ? 0.68960 0.76162 0.75282 -0.07589 -0.09557 0.04024  86  GLU B N   
4835 C CA  . GLU D 76  ? 0.64043 0.72892 0.72265 -0.08947 -0.08857 0.03824  86  GLU B CA  
4836 C C   . GLU D 76  ? 0.74211 0.86173 0.85999 -0.07694 -0.06351 0.03395  86  GLU B C   
4837 O O   . GLU D 76  ? 0.69324 0.84771 0.84557 -0.06957 -0.05748 0.03583  86  GLU B O   
4838 C CB  . GLU D 76  ? 0.79296 0.91548 0.90288 -0.11449 -0.10693 0.04898  86  GLU B CB  
4839 C CG  . GLU D 76  ? 0.67784 0.81374 0.79931 -0.12974 -0.10037 0.05207  86  GLU B CG  
4840 C CD  . GLU D 76  ? 0.72286 0.80097 0.79811 -0.14038 -0.11342 0.04878  86  GLU B CD  
4841 O OE1 . GLU D 76  ? 0.80548 0.83211 0.83654 -0.13784 -0.13092 0.04327  86  GLU B OE1 
4842 O OE2 . GLU D 76  ? 0.76917 0.84924 0.84698 -0.14867 -0.10616 0.05174  86  GLU B OE2 
4843 N N   . LEU D 77  ? 0.63986 0.74306 0.74781 -0.07373 -0.05174 0.02820  87  LEU B N   
4844 C CA  . LEU D 77  ? 0.51413 0.63652 0.64761 -0.06566 -0.03589 0.02198  87  LEU B CA  
4845 C C   . LEU D 77  ? 0.49109 0.62036 0.62021 -0.07748 -0.03498 0.02044  87  LEU B C   
4846 O O   . LEU D 77  ? 0.72122 0.82337 0.82681 -0.08235 -0.03904 0.02293  87  LEU B O   
4847 C CB  . LEU D 77  ? 0.62031 0.71954 0.75265 -0.05045 -0.02608 0.02152  87  LEU B CB  
4848 C CG  . LEU D 77  ? 0.55045 0.66012 0.70971 -0.04606 -0.01833 0.01513  87  LEU B CG  
4849 C CD1 . LEU D 77  ? 0.51707 0.64447 0.70102 -0.03871 -0.01576 0.00958  87  LEU B CD1 
4850 C CD2 . LEU D 77  ? 0.52375 0.61466 0.69050 -0.03740 -0.01196 0.02278  87  LEU B CD2 
4851 N N   . ARG D 78  ? 0.43419 0.59722 0.58161 -0.07866 -0.02824 0.01747  88  ARG B N   
4852 C CA  . ARG D 78  ? 0.48377 0.65769 0.62231 -0.08807 -0.02572 0.01885  88  ARG B CA  
4853 C C   . ARG D 78  ? 0.57216 0.74419 0.70813 -0.07744 -0.01883 0.00603  88  ARG B C   
4854 O O   . ARG D 78  ? 0.66288 0.83033 0.81121 -0.06462 -0.01582 -0.00409 88  ARG B O   
4855 C CB  . ARG D 78  ? 0.52397 0.74029 0.67831 -0.09647 -0.02176 0.02946  88  ARG B CB  
4856 C CG  . ARG D 78  ? 0.49059 0.71288 0.65673 -0.11176 -0.03622 0.04422  88  ARG B CG  
4857 C CD  . ARG D 78  ? 0.47802 0.67611 0.62466 -0.13373 -0.05059 0.05505  88  ARG B CD  
4858 N NE  . ARG D 78  ? 0.73235 0.92700 0.88691 -0.15196 -0.07237 0.06737  88  ARG B NE  
4859 C CZ  . ARG D 78  ? 0.57042 0.81123 0.76220 -0.16830 -0.07747 0.08709  88  ARG B CZ  
4860 N NH1 . ARG D 78  ? 0.56105 0.85724 0.78203 -0.16395 -0.05571 0.09745  88  ARG B NH1 
4861 N NH2 . ARG D 78  ? 0.54833 0.77971 0.74744 -0.18854 -0.10568 0.09824  88  ARG B NH2 
4862 N N   . LEU D 79  ? 0.55071 0.72208 0.66860 -0.08420 -0.01999 0.00755  89  LEU B N   
4863 C CA  . LEU D 79  ? 0.58456 0.75098 0.69135 -0.07702 -0.02053 -0.00492 89  LEU B CA  
4864 C C   . LEU D 79  ? 0.62178 0.80081 0.70268 -0.08396 -0.01892 0.00115  89  LEU B C   
4865 O O   . LEU D 79  ? 0.61564 0.78774 0.68888 -0.09616 -0.02426 0.01560  89  LEU B O   
4866 C CB  . LEU D 79  ? 0.68161 0.82075 0.79547 -0.07598 -0.03103 -0.00611 89  LEU B CB  
4867 C CG  . LEU D 79  ? 0.55405 0.68481 0.65989 -0.07415 -0.04167 -0.01699 89  LEU B CG  
4868 C CD1 . LEU D 79  ? 0.65144 0.77933 0.75630 -0.06348 -0.04031 -0.03620 89  LEU B CD1 
4869 C CD2 . LEU D 79  ? 0.61207 0.72737 0.74106 -0.07601 -0.05292 -0.00902 89  LEU B CD2 
4870 N N   . GLN D 80  ? 0.54289 0.73581 0.60531 -0.07371 -0.01079 -0.00921 90  GLN B N   
4871 C CA  . GLN D 80  ? 0.52598 0.73146 0.55472 -0.07587 -0.00628 -0.00256 90  GLN B CA  
4872 C C   . GLN D 80  ? 0.61029 0.79019 0.60606 -0.06902 -0.02015 -0.01991 90  GLN B C   
4873 O O   . GLN D 80  ? 0.78448 0.94776 0.77450 -0.05624 -0.02399 -0.04182 90  GLN B O   
4874 C CB  . GLN D 80  ? 0.50519 0.74923 0.52918 -0.06537 0.01719  0.00258  90  GLN B CB  
4875 C CG  . GLN D 80  ? 0.81433 1.07475 0.79813 -0.06394 0.02744  0.01339  90  GLN B CG  
4876 C CD  . GLN D 80  ? 0.86113 1.17007 0.84895 -0.05149 0.05728  0.02703  90  GLN B CD  
4877 O OE1 . GLN D 80  ? 0.81979 1.16317 0.85379 -0.06197 0.06507  0.04864  90  GLN B OE1 
4878 N NE2 . GLN D 80  ? 0.94350 1.25556 0.88209 -0.02768 0.07347  0.01579  90  GLN B NE2 
4879 N N   . VAL D 81  ? 0.65676 0.82981 0.63116 -0.07842 -0.03143 -0.00922 91  VAL B N   
4880 C CA  . VAL D 81  ? 0.65650 0.80649 0.60087 -0.07604 -0.05255 -0.02140 91  VAL B CA  
4881 C C   . VAL D 81  ? 0.66871 0.82945 0.55879 -0.07283 -0.04697 -0.01434 91  VAL B C   
4882 O O   . VAL D 81  ? 0.79764 0.96772 0.68451 -0.08390 -0.04689 0.00976  91  VAL B O   
4883 C CB  . VAL D 81  ? 0.61115 0.74570 0.58362 -0.08739 -0.07387 -0.01039 91  VAL B CB  
4884 C CG1 . VAL D 81  ? 0.60377 0.71746 0.56551 -0.08706 -0.10199 -0.02404 91  VAL B CG1 
4885 C CG2 . VAL D 81  ? 0.54429 0.67624 0.56647 -0.08897 -0.06821 -0.00615 91  VAL B CG2 
4886 N N   . ALA D 82  ? 0.69409 0.84899 0.53660 -0.05545 -0.04157 -0.03448 92  ALA B N   
4887 C CA  . ALA D 82  ? 0.83451 0.99992 0.61369 -0.04586 -0.03048 -0.02818 92  ALA B CA  
4888 C C   . ALA D 82  ? 0.94508 1.07186 0.66304 -0.03914 -0.05978 -0.05040 92  ALA B C   
4889 O O   . ALA D 82  ? 0.96930 1.06258 0.69812 -0.04128 -0.08704 -0.07324 92  ALA B O   
4890 C CB  . ALA D 82  ? 0.96353 1.15675 0.72610 -0.02422 0.00656  -0.03035 92  ALA B CB  
4891 N N   . ASN D 83  ? 0.99995 1.13116 0.65258 -0.03236 -0.05606 -0.04086 93  ASN B N   
4892 C CA  . ASN D 83  ? 1.05240 1.14506 0.63110 -0.02576 -0.08765 -0.06016 93  ASN B CA  
4893 C C   . ASN D 83  ? 1.08391 1.15446 0.70103 -0.04785 -0.13388 -0.05993 93  ASN B C   
4894 O O   . ASN D 83  ? 1.26423 1.29584 0.86027 -0.04837 -0.16977 -0.08573 93  ASN B O   
4895 C CB  . ASN D 83  ? 0.95942 1.01562 0.47903 0.00017  -0.08641 -0.10046 93  ASN B CB  
4896 C CG  . ASN D 83  ? 1.26277 1.34434 0.73399 0.02994  -0.03763 -0.09753 93  ASN B CG  
4897 O OD1 . ASN D 83  ? 1.46347 1.54496 0.85327 0.04591  -0.02776 -0.09243 93  ASN B OD1 
4898 N ND2 . ASN D 83  ? 1.18408 1.29113 0.70646 0.03937  -0.00582 -0.09736 93  ASN B ND2 
4899 N N   . MET D 84  ? 1.16358 1.25821 0.83957 -0.06564 -0.13375 -0.02873 94  MET B N   
4900 C CA  . MET D 84  ? 1.12604 1.21092 0.85332 -0.08220 -0.16906 -0.02125 94  MET B CA  
4901 C C   . MET D 84  ? 1.17883 1.25422 0.86126 -0.08632 -0.20221 -0.01036 94  MET B C   
4902 O O   . MET D 84  ? 1.18119 1.27149 0.83165 -0.08497 -0.19043 0.01390  94  MET B O   
4903 C CB  . MET D 84  ? 1.09482 1.20230 0.89514 -0.09254 -0.15243 0.00567  94  MET B CB  
4904 C CG  . MET D 84  ? 1.09775 1.19966 0.96833 -0.10089 -0.17198 0.00711  94  MET B CG  
4905 S SD  . MET D 84  ? 1.19334 1.30982 1.12636 -0.10505 -0.15084 0.03615  94  MET B SD  
4906 C CE  . MET D 84  ? 1.02660 1.15486 0.94337 -0.10218 -0.11220 0.03302  94  MET B CE  
4907 N N   . SER D 85  ? 1.25013 1.30079 0.93291 -0.09302 -0.24652 -0.02539 95  SER B N   
4908 C CA  . SER D 85  ? 1.21919 1.26176 0.86883 -0.09943 -0.28778 -0.01378 95  SER B CA  
4909 C C   . SER D 85  ? 1.10239 1.15382 0.83485 -0.11640 -0.32458 0.00337  95  SER B C   
4910 O O   . SER D 85  ? 1.14041 1.19292 0.86155 -0.12289 -0.36187 0.01954  95  SER B O   
4911 C CB  . SER D 85  ? 1.22005 1.22071 0.77263 -0.09101 -0.31717 -0.04716 95  SER B CB  
4912 O OG  . SER D 85  ? 1.30030 1.26921 0.87367 -0.09562 -0.33957 -0.07894 95  SER B OG  
4913 N N   . GLN D 86  ? 1.10536 1.16676 0.92148 -0.12201 -0.31441 0.00385  98  GLN B N   
4914 C CA  . GLN D 86  ? 1.01794 1.09705 0.92290 -0.13430 -0.34025 0.02619  98  GLN B CA  
4915 C C   . GLN D 86  ? 0.95318 1.05618 0.93018 -0.12926 -0.29984 0.04465  98  GLN B C   
4916 O O   . GLN D 86  ? 1.02155 1.11901 1.00334 -0.12439 -0.26977 0.02819  98  GLN B O   
4917 C CB  . GLN D 86  ? 1.22950 1.28807 1.16069 -0.14762 -0.38005 0.00628  98  GLN B CB  
4918 C CG  . GLN D 86  ? 1.45990 1.48001 1.30894 -0.15293 -0.42806 -0.01840 98  GLN B CG  
4919 C CD  . GLN D 86  ? 1.48829 1.47558 1.36095 -0.16887 -0.47010 -0.04133 98  GLN B CD  
4920 O OE1 . GLN D 86  ? 1.35132 1.35457 1.31628 -0.17865 -0.46586 -0.03016 98  GLN B OE1 
4921 N NE2 . GLN D 86  ? 1.44837 1.38616 1.23524 -0.16951 -0.50693 -0.07240 98  GLN B NE2 
4922 N N   . GLY D 87  ? 1.01117 1.13734 1.03904 -0.12773 -0.30002 0.07858  99  GLY B N   
4923 C CA  . GLY D 87  ? 0.79904 0.93821 0.88168 -0.11868 -0.26345 0.09461  99  GLY B CA  
4924 C C   . GLY D 87  ? 0.78035 0.92804 0.93315 -0.12097 -0.26126 0.09256  99  GLY B C   
4925 O O   . GLY D 87  ? 0.86469 1.01656 1.05098 -0.13275 -0.29477 0.09132  99  GLY B O   
4926 N N   . ARG D 88  ? 0.67438 0.82276 0.84888 -0.11072 -0.22315 0.09441  100 ARG B N   
4927 C CA  . ARG D 88  ? 0.58731 0.74336 0.82128 -0.10979 -0.21313 0.09528  100 ARG B CA  
4928 C C   . ARG D 88  ? 0.57848 0.73231 0.82079 -0.09355 -0.17165 0.10334  100 ARG B C   
4929 O O   . ARG D 88  ? 0.60139 0.74198 0.80127 -0.08738 -0.15481 0.10265  100 ARG B O   
4930 C CB  . ARG D 88  ? 0.61541 0.75278 0.82897 -0.11947 -0.22133 0.06391  100 ARG B CB  
4931 C CG  . ARG D 88  ? 0.64681 0.76523 0.78912 -0.11456 -0.20035 0.03799  100 ARG B CG  
4932 C CD  . ARG D 88  ? 0.65829 0.75330 0.76563 -0.11975 -0.21698 0.00638  100 ARG B CD  
4933 N NE  . ARG D 88  ? 0.97576 1.05876 1.05888 -0.12999 -0.26000 0.00064  100 ARG B NE  
4934 C CZ  . ARG D 88  ? 1.14492 1.19526 1.18780 -0.13425 -0.28517 -0.02855 100 ARG B CZ  
4935 N NH1 . ARG D 88  ? 0.89595 0.92445 0.92275 -0.12699 -0.26877 -0.05358 100 ARG B NH1 
4936 N NH2 . ARG D 88  ? 1.34128 1.37603 1.35582 -0.14452 -0.33012 -0.03310 100 ARG B NH2 
4937 N N   . THR D 89  ? 0.62189 0.78566 0.91701 -0.08747 -0.15746 0.11232  101 THR B N   
4938 C CA  . THR D 89  ? 0.59133 0.74692 0.88657 -0.06999 -0.12065 0.11745  101 THR B CA  
4939 C C   . THR D 89  ? 0.58476 0.73146 0.87668 -0.07330 -0.10873 0.09817  101 THR B C   
4940 O O   . THR D 89  ? 0.65183 0.80659 0.97926 -0.08307 -0.12281 0.09595  101 THR B O   
4941 C CB  . THR D 89  ? 0.64209 0.81820 0.99673 -0.05162 -0.10678 0.15079  101 THR B CB  
4942 O OG1 . THR D 89  ? 0.85352 1.04182 1.22026 -0.04713 -0.12130 0.17161  101 THR B OG1 
4943 C CG2 . THR D 89  ? 0.42914 0.58394 0.76057 -0.02869 -0.06961 0.15246  101 THR B CG2 
4944 N N   . LEU D 90  ? 0.63509 0.76306 0.88637 -0.06640 -0.08626 0.08597  102 LEU B N   
4945 C CA  . LEU D 90  ? 0.52595 0.64642 0.77052 -0.06728 -0.07491 0.06952  102 LEU B CA  
4946 C C   . LEU D 90  ? 0.48790 0.60010 0.73636 -0.04988 -0.04836 0.08084  102 LEU B C   
4947 O O   . LEU D 90  ? 0.56313 0.65695 0.77729 -0.04100 -0.03721 0.08263  102 LEU B O   
4948 C CB  . LEU D 90  ? 0.55617 0.66660 0.74947 -0.07503 -0.07526 0.04642  102 LEU B CB  
4949 C CG  . LEU D 90  ? 0.62210 0.73488 0.79758 -0.08629 -0.09652 0.02995  102 LEU B CG  
4950 C CD1 . LEU D 90  ? 1.00065 1.11198 1.12528 -0.08860 -0.08928 0.01738  102 LEU B CD1 
4951 C CD2 . LEU D 90  ? 0.42015 0.52809 0.61776 -0.08891 -0.10478 0.01649  102 LEU B CD2 
4952 N N   . TYR D 91  ? 0.61443 0.73489 0.89958 -0.04486 -0.03983 0.08888  103 TYR B N   
4953 C CA  . TYR D 91  ? 0.65123 0.76338 0.93376 -0.02497 -0.01332 0.10120  103 TYR B CA  
4954 C C   . TYR D 91  ? 0.60360 0.70364 0.86326 -0.02716 -0.00794 0.08475  103 TYR B C   
4955 O O   . TYR D 91  ? 0.62314 0.73076 0.90575 -0.03788 -0.01767 0.07711  103 TYR B O   
4956 C CB  . TYR D 91  ? 0.53374 0.67039 0.87857 -0.01447 -0.00269 0.13162  103 TYR B CB  
4957 C CG  . TYR D 91  ? 0.52296 0.67681 0.89633 -0.00344 -0.00064 0.15602  103 TYR B CG  
4958 C CD1 . TYR D 91  ? 0.55972 0.70111 0.91155 0.02605  0.02660  0.17048  103 TYR B CD1 
4959 C CD2 . TYR D 91  ? 0.56258 0.74190 0.98150 -0.02015 -0.02762 0.16474  103 TYR B CD2 
4960 C CE1 . TYR D 91  ? 0.70267 0.86066 1.08385 0.04145  0.03115  0.19501  103 TYR B CE1 
4961 C CE2 . TYR D 91  ? 0.62401 0.82475 1.07627 -0.00880 -0.02746 0.19114  103 TYR B CE2 
4962 C CZ  . TYR D 91  ? 0.61609 0.80824 1.05262 0.02344  0.00412  0.20728  103 TYR B CZ  
4963 O OH  . TYR D 91  ? 0.81701 1.03121 1.28968 0.03983  0.00687  0.23557  103 TYR B OH  
4964 N N   . CYS D 92  ? 0.66549 0.74284 0.87909 -0.01669 0.00435  0.07952  104 CYS B N   
4965 C CA  . CYS D 92  ? 0.47604 0.54467 0.67128 -0.01530 0.00910  0.07034  104 CYS B CA  
4966 C C   . CYS D 92  ? 0.62263 0.69011 0.83147 0.00436  0.02944  0.09037  104 CYS B C   
4967 O O   . CYS D 92  ? 0.69092 0.74888 0.88836 0.02419  0.04621  0.10591  104 CYS B O   
4968 C CB  . CYS D 92  ? 0.59199 0.63629 0.73226 -0.01704 0.00569  0.05741  104 CYS B CB  
4969 S SG  . CYS D 92  ? 0.85651 0.89285 0.97587 -0.01406 0.00688  0.05112  104 CYS B SG  
4970 N N   . THR D 93  ? 0.53465 0.61051 0.76585 0.00191  0.03026  0.09202  105 THR B N   
4971 C CA  . THR D 93  ? 0.57298 0.65207 0.82180 0.01918  0.05072  0.11636  105 THR B CA  
4972 C C   . THR D 93  ? 0.54849 0.61354 0.76675 0.02420  0.05261  0.11030  105 THR B C   
4973 O O   . THR D 93  ? 0.63619 0.69946 0.84404 0.01125  0.03634  0.08991  105 THR B O   
4974 C CB  . THR D 93  ? 0.67006 0.77531 0.99309 0.00996  0.04813  0.13567  105 THR B CB  
4975 O OG1 . THR D 93  ? 0.60557 0.70834 0.94387 -0.00849 0.02771  0.11732  105 THR B OG1 
4976 C CG2 . THR D 93  ? 0.50591 0.62972 0.86468 0.00308  0.04012  0.14448  105 THR B CG2 
4977 N N   . CYS D 94  ? 0.56136 0.61920 0.76524 0.04591  0.07410  0.13134  106 CYS B N   
4978 C CA  . CYS D 94  ? 0.57846 0.62436 0.75511 0.05366  0.07604  0.13283  106 CYS B CA  
4979 C C   . CYS D 94  ? 0.64169 0.70075 0.85369 0.06788  0.09868  0.16718  106 CYS B C   
4980 O O   . CYS D 94  ? 0.65830 0.73130 0.89547 0.08026  0.11983  0.19219  106 CYS B O   
4981 C CB  . CYS D 94  ? 0.60487 0.61611 0.69900 0.06842  0.07623  0.12242  106 CYS B CB  
4982 S SG  . CYS D 94  ? 0.81067 0.79799 0.85767 0.10385  0.10758  0.14146  106 CYS B SG  
4983 N N   . SER D 95  ? 0.59374 0.65155 0.81256 0.06693  0.09523  0.17257  107 SER B N   
4984 C CA  . SER D 95  ? 0.63295 0.70338 0.89221 0.07646  0.11479  0.20920  107 SER B CA  
4985 C C   . SER D 95  ? 0.62688 0.68420 0.86281 0.08217  0.11012  0.21181  107 SER B C   
4986 O O   . SER D 95  ? 0.62009 0.66950 0.84162 0.07111  0.08669  0.18513  107 SER B O   
4987 C CB  . SER D 95  ? 0.62562 0.71825 0.97349 0.05432  0.10555  0.21993  107 SER B CB  
4988 O OG  . SER D 95  ? 0.64239 0.74448 1.03722 0.05743  0.11890  0.25700  107 SER B OG  
4989 N N   . PRO D 96  ? 0.68148 0.73972 0.91466 0.10107  0.13307  0.24687  108 PRO B N   
4990 C CA  . PRO D 96  ? 0.76257 0.81132 0.98737 0.10536  0.12722  0.25640  108 PRO B CA  
4991 C C   . PRO D 96  ? 0.73774 0.79582 1.04585 0.08512  0.11564  0.26498  108 PRO B C   
4992 O O   . PRO D 96  ? 0.72791 0.79710 1.09331 0.06632  0.10865  0.26106  108 PRO B O   
4993 C CB  . PRO D 96  ? 0.64459 0.69062 0.83337 0.13508  0.16020  0.29577  108 PRO B CB  
4994 C CG  . PRO D 96  ? 0.62772 0.67778 0.79317 0.15061  0.18396  0.29993  108 PRO B CG  
4995 C CD  . PRO D 96  ? 0.60802 0.67695 0.83824 0.12451  0.16899  0.28251  108 PRO B CD  
4996 N N   . GLN D 97  ? 0.72719 0.77510 1.03796 0.08969  0.11038  0.27656  109 GLN B N   
4997 C CA  . GLN D 97  ? 0.62744 0.67136 1.01155 0.07364  0.09900  0.28601  109 GLN B CA  
4998 C C   . GLN D 97  ? 0.71066 0.76880 1.15896 0.06795  0.11774  0.32903  109 GLN B C   
4999 O O   . GLN D 97  ? 0.70724 0.76440 1.22331 0.04461  0.10259  0.32824  109 GLN B O   
5000 C CB  . GLN D 97  ? 0.70260 0.73059 1.07613 0.08389  0.09127  0.29415  109 GLN B CB  
5001 C CG  . GLN D 97  ? 0.65138 0.66123 1.08781 0.06928  0.07249  0.28956  109 GLN B CG  
5002 C CD  . GLN D 97  ? 0.76465 0.75891 1.18816 0.08294  0.06220  0.29067  109 GLN B CD  
5003 O OE1 . GLN D 97  ? 0.82307 0.80879 1.24817 0.08175  0.04316  0.25855  109 GLN B OE1 
5004 N NE2 . GLN D 97  ? 0.90686 0.89957 1.31760 0.09885  0.07646  0.33065  109 GLN B NE2 
5005 N N   . THR D 98  ? 0.68423 0.75559 1.11160 0.08938  0.14982  0.36861  110 THR B N   
5006 C CA  . THR D 98  ? 0.64709 0.74654 1.13701 0.08725  0.17465  0.41431  110 THR B CA  
5007 C C   . THR D 98  ? 0.77509 0.89378 1.27734 0.07915  0.17331  0.39573  110 THR B C   
5008 O O   . THR D 98  ? 0.95930 1.07940 1.39619 0.09981  0.18837  0.38248  110 THR B O   
5009 C CB  . THR D 98  ? 0.71385 0.82491 1.16372 0.12025  0.21598  0.46019  110 THR B CB  
5010 O OG1 . THR D 98  ? 0.81780 0.91028 1.25552 0.12713  0.21409  0.47971  110 THR B OG1 
5011 C CG2 . THR D 98  ? 0.93435 1.08938 1.45617 0.12120  0.24217  0.50304  110 THR B CG2 
5012 N N   . THR D 99  ? 0.59253 0.72029 1.17469 0.04926  0.15176  0.39417  111 THR B N   
5013 C CA  . THR D 99  ? 0.48988 0.63043 1.08169 0.03720  0.13881  0.36852  111 THR B CA  
5014 C C   . THR D 99  ? 0.66557 0.83938 1.24992 0.06020  0.17419  0.39617  111 THR B C   
5015 O O   . THR D 99  ? 0.66170 0.87008 1.30971 0.06409  0.19836  0.44805  111 THR B O   
5016 C CB  . THR D 99  ? 0.49366 0.63650 1.17382 0.00141  0.10720  0.37029  111 THR B CB  
5017 O OG1 . THR D 99  ? 0.87411 0.97572 1.54640 -0.01346 0.07559  0.33736  111 THR B OG1 
5018 C CG2 . THR D 99  ? 0.51558 0.67354 1.20340 -0.01020 0.09180  0.34746  111 THR B CG2 
5019 N N   . GLU D 100 ? 0.68815 0.85061 1.19632 0.07674  0.17787  0.36347  112 GLU B N   
5020 C CA  . GLU D 100 ? 0.68915 0.87149 1.17759 0.10281  0.20881  0.37980  112 GLU B CA  
5021 C C   . GLU D 100 ? 0.65128 0.81376 1.08823 0.09833  0.18772  0.33100  112 GLU B C   
5022 O O   . GLU D 100 ? 0.73349 0.86374 1.08073 0.11523  0.18944  0.30376  112 GLU B O   
5023 C CB  . GLU D 100 ? 0.84914 1.02194 1.26636 0.14374  0.24896  0.40272  112 GLU B CB  
5024 C CG  . GLU D 100 ? 0.87806 1.06686 1.27232 0.17898  0.28759  0.42332  112 GLU B CG  
5025 C CD  . GLU D 100 ? 1.14713 1.31933 1.45894 0.22425  0.32923  0.44608  112 GLU B CD  
5026 O OE1 . GLU D 100 ? 1.07972 1.23063 1.35433 0.22521  0.32478  0.44729  112 GLU B OE1 
5027 O OE2 . GLU D 100 ? 1.39437 1.57177 1.67395 0.26175  0.36502  0.46156  112 GLU B OE2 
5028 N N   . VAL D 101 ? 0.60282 0.78297 1.09754 0.07356  0.16472  0.32246  113 VAL B N   
5029 C CA  . VAL D 101 ? 0.51940 0.68200 0.97481 0.06310  0.14005  0.27847  113 VAL B CA  
5030 C C   . VAL D 101 ? 0.66472 0.82932 1.08269 0.08994  0.16297  0.28307  113 VAL B C   
5031 O O   . VAL D 101 ? 0.51713 0.71531 0.98391 0.10434  0.18666  0.32064  113 VAL B O   
5032 C CB  . VAL D 101 ? 0.59203 0.76766 1.11358 0.02841  0.10473  0.26794  113 VAL B CB  
5033 C CG1 . VAL D 101 ? 0.63665 0.79646 1.11362 0.01964  0.08259  0.22701  113 VAL B CG1 
5034 C CG2 . VAL D 101 ? 0.39495 0.55573 0.94503 0.00658  0.08247  0.26072  113 VAL B CG2 
5035 N N   . PHE D 102 ? 0.62040 0.74856 0.95531 0.09721  0.15546  0.24703  114 PHE B N   
5036 C CA  . PHE D 102 ? 0.68710 0.79997 0.97322 0.12231  0.17143  0.24357  114 PHE B CA  
5037 C C   . PHE D 102 ? 0.59640 0.69833 0.87274 0.10028  0.14061  0.21060  114 PHE B C   
5038 O O   . PHE D 102 ? 0.76548 0.84334 1.00189 0.08270  0.11667  0.17779  114 PHE B O   
5039 C CB  . PHE D 102 ? 0.79420 0.86111 0.97941 0.15173  0.18797  0.23276  114 PHE B CB  
5040 C CG  . PHE D 102 ? 0.99083 1.02207 1.10968 0.17642  0.19726  0.21978  114 PHE B CG  
5041 C CD1 . PHE D 102 ? 0.90306 0.94146 1.02102 0.21526  0.23572  0.24904  114 PHE B CD1 
5042 C CD2 . PHE D 102 ? 0.96876 0.95806 1.02808 0.16229  0.16852  0.18094  114 PHE B CD2 
5043 C CE1 . PHE D 102 ? 0.79382 0.78948 0.84555 0.24222  0.24440  0.23537  114 PHE B CE1 
5044 C CE2 . PHE D 102 ? 0.82472 0.77104 0.82194 0.18354  0.17365  0.16908  114 PHE B CE2 
5045 C CZ  . PHE D 102 ? 0.80880 0.75375 0.79834 0.22495  0.21117  0.19407  114 PHE B CZ  
5046 N N   . PHE D 103 ? 0.58852 0.71214 0.90426 0.10235  0.14218  0.22349  115 PHE B N   
5047 C CA  . PHE D 103 ? 0.53859 0.65527 0.84830 0.08249  0.11406  0.19874  115 PHE B CA  
5048 C C   . PHE D 103 ? 0.74722 0.82003 0.97774 0.10218  0.12025  0.18144  115 PHE B C   
5049 O O   . PHE D 103 ? 0.92521 0.98036 1.12211 0.13750  0.14941  0.19561  115 PHE B O   
5050 C CB  . PHE D 103 ? 0.58298 0.74274 0.97343 0.07361  0.10638  0.22254  115 PHE B CB  
5051 C CG  . PHE D 103 ? 0.60046 0.78893 1.06148 0.04183  0.08165  0.22771  115 PHE B CG  
5052 C CD1 . PHE D 103 ? 0.50791 0.71801 1.02056 0.04230  0.09465  0.25594  115 PHE B CD1 
5053 C CD2 . PHE D 103 ? 0.44759 0.63573 0.91833 0.01243  0.04456  0.20501  115 PHE B CD2 
5054 C CE1 . PHE D 103 ? 0.42540 0.65017 1.00058 0.01146  0.06724  0.25935  115 PHE B CE1 
5055 C CE2 . PHE D 103 ? 0.68670 0.88746 1.21013 -0.01491 0.01809  0.20514  115 PHE B CE2 
5056 C CZ  . PHE D 103 ? 0.62437 0.84052 1.20159 -0.01666 0.02748  0.23140  115 PHE B CZ  
5057 N N   . GLY D 104 ? 0.76388 0.81581 0.96259 0.08014  0.09290  0.15170  116 GLY B N   
5058 C CA  . GLY D 104 ? 0.87722 0.88375 1.00907 0.09074  0.09078  0.13609  116 GLY B CA  
5059 C C   . GLY D 104 ? 0.88608 0.90140 1.04252 0.09927  0.09214  0.14945  116 GLY B C   
5060 O O   . GLY D 104 ? 0.96021 1.02115 1.18743 0.10011  0.09644  0.17423  116 GLY B O   
5061 N N   . LYS D 105 ? 0.87032 0.83967 0.96972 0.10430  0.08503  0.13480  117 LYS B N   
5062 C CA  . LYS D 105 ? 0.81885 0.78940 0.93509 0.11532  0.08542  0.14804  117 LYS B CA  
5063 C C   . LYS D 105 ? 0.72410 0.73613 0.89364 0.08293  0.05814  0.14933  117 LYS B C   
5064 O O   . LYS D 105 ? 0.79858 0.83647 1.01194 0.08993  0.05702  0.17023  117 LYS B O   
5065 C CB  . LYS D 105 ? 0.80753 0.70815 0.84568 0.12656  0.08107  0.13149  117 LYS B CB  
5066 C CG  . LYS D 105 ? 0.93440 0.77776 0.89985 0.16079  0.10276  0.12467  117 LYS B CG  
5067 C CD  . LYS D 105 ? 1.10104 0.95957 1.08662 0.20792  0.14259  0.15343  117 LYS B CD  
5068 C CE  . LYS D 105 ? 1.40982 1.20314 1.30525 0.24780  0.16641  0.14443  117 LYS B CE  
5069 N NZ  . LYS D 105 ? 1.60344 1.41394 1.51480 0.30091  0.21300  0.17613  117 LYS B NZ  
5070 N N   . GLY D 106 ? 0.73028 0.74888 0.89410 0.05042  0.03614  0.12845  118 GLY B N   
5071 C CA  . GLY D 106 ? 0.65423 0.70519 0.85281 0.02310  0.01117  0.12597  118 GLY B CA  
5072 C C   . GLY D 106 ? 0.71781 0.74630 0.87848 0.01022  -0.00576 0.11614  118 GLY B C   
5073 O O   . GLY D 106 ? 0.92020 0.90878 1.04149 0.02358  -0.00009 0.11730  118 GLY B O   
5074 N N   . THR D 107 ? 0.58112 0.63175 0.75049 -0.01518 -0.02687 0.10713  119 THR B N   
5075 C CA  . THR D 107 ? 0.46078 0.49973 0.59873 -0.02958 -0.04198 0.10302  119 THR B CA  
5076 C C   . THR D 107 ? 0.69947 0.76978 0.86642 -0.03882 -0.06143 0.11214  119 THR B C   
5077 O O   . THR D 107 ? 0.70397 0.79787 0.88726 -0.05240 -0.07358 0.10220  119 THR B O   
5078 C CB  . THR D 107 ? 0.72892 0.76307 0.83452 -0.04960 -0.04654 0.08335  119 THR B CB  
5079 O OG1 . THR D 107 ? 0.94943 0.95187 1.02707 -0.04369 -0.03611 0.07677  119 THR B OG1 
5080 C CG2 . THR D 107 ? 0.65600 0.68687 0.73556 -0.06507 -0.05901 0.08596  119 THR B CG2 
5081 N N   . ARG D 108 ? 0.57465 0.64008 0.74412 -0.03041 -0.06712 0.13056  120 ARG B N   
5082 C CA  . ARG D 108 ? 0.63521 0.72863 0.82829 -0.03869 -0.09085 0.14230  120 ARG B CA  
5083 C C   . ARG D 108 ? 0.71165 0.79805 0.85705 -0.05756 -0.10579 0.13275  120 ARG B C   
5084 O O   . ARG D 108 ? 0.89429 0.95396 1.00464 -0.05733 -0.10042 0.13745  120 ARG B O   
5085 C CB  . ARG D 108 ? 0.64697 0.74392 0.87028 -0.01775 -0.09001 0.17161  120 ARG B CB  
5086 C CG  . ARG D 108 ? 0.90793 1.03601 1.15826 -0.02702 -0.12050 0.18752  120 ARG B CG  
5087 C CD  . ARG D 108 ? 0.99684 1.13236 1.28258 -0.00321 -0.11892 0.22082  120 ARG B CD  
5088 N NE  . ARG D 108 ? 1.08171 1.23879 1.42709 0.02026  -0.09734 0.23908  120 ARG B NE  
5089 C CZ  . ARG D 108 ? 1.12076 1.29715 1.51446 0.04696  -0.09010 0.27259  120 ARG B CZ  
5090 N NH1 . ARG D 108 ? 1.15642 1.33035 1.54722 0.05317  -0.10613 0.29092  120 ARG B NH1 
5091 N NH2 . ARG D 108 ? 1.16818 1.36950 1.61603 0.07040  -0.06410 0.29159  120 ARG B NH2 
5092 N N   . LEU D 109 ? 0.69053 0.79738 0.83198 -0.07289 -0.12426 0.12063  121 LEU B N   
5093 C CA  . LEU D 109 ? 0.64651 0.75175 0.73804 -0.08625 -0.13498 0.11337  121 LEU B CA  
5094 C C   . LEU D 109 ? 0.76156 0.87938 0.85428 -0.08854 -0.16359 0.12818  121 LEU B C   
5095 O O   . LEU D 109 ? 0.80905 0.94364 0.93204 -0.09191 -0.18546 0.12648  121 LEU B O   
5096 C CB  . LEU D 109 ? 0.62806 0.73971 0.69833 -0.09563 -0.13356 0.08645  121 LEU B CB  
5097 C CG  . LEU D 109 ? 0.59489 0.70083 0.67097 -0.09372 -0.11018 0.07249  121 LEU B CG  
5098 C CD1 . LEU D 109 ? 0.64121 0.75475 0.69659 -0.09866 -0.10938 0.04863  121 LEU B CD1 
5099 C CD2 . LEU D 109 ? 0.53096 0.62061 0.58624 -0.09465 -0.09390 0.08101  121 LEU B CD2 
5100 N N   . THR D 110 ? 0.85213 0.96043 0.91357 -0.08847 -0.16683 0.14489  122 THR B N   
5101 C CA  . THR D 110 ? 0.85035 0.96911 0.90452 -0.08983 -0.19579 0.16232  122 THR B CA  
5102 C C   . THR D 110 ? 0.95768 1.07342 0.94249 -0.10041 -0.20186 0.15480  122 THR B C   
5103 O O   . THR D 110 ? 0.99361 1.09753 0.94559 -0.10308 -0.18203 0.16060  122 THR B O   
5104 C CB  . THR D 110 ? 0.94265 1.05175 1.01650 -0.07621 -0.19428 0.19400  122 THR B CB  
5105 O OG1 . THR D 110 ? 0.90388 1.02055 1.04067 -0.06003 -0.18548 0.20336  122 THR B OG1 
5106 C CG2 . THR D 110 ? 1.06231 1.18370 1.12472 -0.07786 -0.22634 0.21530  122 THR B CG2 
5107 N N   . VAL D 111 ? 0.92747 1.05224 0.88873 -0.10612 -0.22977 0.14349  123 VAL B N   
5108 C CA  . VAL D 111 ? 0.84830 0.96877 0.73224 -0.11019 -0.23412 0.13468  123 VAL B CA  
5109 C C   . VAL D 111 ? 0.98267 1.10441 0.84018 -0.10946 -0.26065 0.16164  123 VAL B C   
5110 O O   . VAL D 111 ? 1.03909 1.16873 0.92423 -0.11027 -0.29616 0.17013  123 VAL B O   
5111 C CB  . VAL D 111 ? 0.86445 0.98032 0.71963 -0.11296 -0.24957 0.10043  123 VAL B CB  
5112 C CG1 . VAL D 111 ? 0.84043 0.94842 0.60334 -0.10962 -0.24899 0.09115  123 VAL B CG1 
5113 C CG2 . VAL D 111 ? 0.93463 1.04921 0.82043 -0.11194 -0.22360 0.07760  123 VAL B CG2 
5114 N N   . VAL D 112 ? 1.06311 1.17991 0.87191 -0.10899 -0.24499 0.17917  124 VAL B N   
5115 C CA  . VAL D 112 ? 1.26124 1.37718 1.03534 -0.10732 -0.26717 0.20844  124 VAL B CA  
5116 C C   . VAL D 112 ? 1.29199 1.40679 0.97382 -0.10724 -0.26323 0.20262  124 VAL B C   
5117 O O   . VAL D 112 ? 1.22541 1.34315 0.88155 -0.10756 -0.22810 0.19466  124 VAL B O   
5118 C CB  . VAL D 112 ? 1.06415 1.17005 0.86510 -0.10448 -0.25170 0.24433  124 VAL B CB  
5119 C CG1 . VAL D 112 ? 1.15550 1.26049 1.03577 -0.09580 -0.25853 0.25334  124 VAL B CG1 
5120 C CG2 . VAL D 112 ? 0.97582 1.07247 0.76801 -0.11057 -0.21202 0.24316  124 VAL B CG2 
5121 N N   . GLU D 113 ? 1.26274 1.37517 0.89413 -0.10505 -0.29949 0.20844  125 GLU B N   
5122 C CA  . GLU D 113 ? 1.35188 1.45958 0.88110 -0.09941 -0.29589 0.20587  125 GLU B CA  
5123 C C   . GLU D 113 ? 1.36848 1.48032 0.86734 -0.09820 -0.27906 0.24976  125 GLU B C   
5124 O O   . GLU D 113 ? 1.53751 1.65414 0.96868 -0.09321 -0.25170 0.25550  125 GLU B O   
5125 C CB  . GLU D 113 ? 1.26205 1.35669 0.73572 -0.09740 -0.34756 0.18970  125 GLU B CB  
5126 N N   . ASP D 114 ? 1.35967 1.46982 0.90911 -0.10084 -0.29289 0.28363  126 ASP B N   
5127 C CA  . ASP D 114 ? 1.51195 1.61838 1.04345 -0.10132 -0.27943 0.32890  126 ASP B CA  
5128 C C   . ASP D 114 ? 1.47389 1.56858 1.08859 -0.10532 -0.26364 0.34707  126 ASP B C   
5129 O O   . ASP D 114 ? 1.41058 1.50216 1.09018 -0.10090 -0.28046 0.34128  126 ASP B O   
5130 C CB  . ASP D 114 ? 1.42009 1.52399 0.90978 -0.09542 -0.32028 0.35709  126 ASP B CB  
5131 N N   . LEU D 115 ? 1.41509 1.50149 1.02622 -0.11294 -0.23168 0.37043  127 LEU B N   
5132 C CA  . LEU D 115 ? 1.32283 1.38396 0.99729 -0.11751 -0.21802 0.38439  127 LEU B CA  
5133 C C   . LEU D 115 ? 1.26932 1.30530 0.95628 -0.11088 -0.23659 0.42574  127 LEU B C   
5134 O O   . LEU D 115 ? 1.25123 1.25396 0.98309 -0.10998 -0.22881 0.43663  127 LEU B O   
5135 C CB  . LEU D 115 ? 1.26210 1.32137 0.93338 -0.13336 -0.18188 0.39188  127 LEU B CB  
5136 C CG  . LEU D 115 ? 1.39460 1.47543 1.07526 -0.13847 -0.15846 0.35439  127 LEU B CG  
5137 C CD1 . LEU D 115 ? 1.39802 1.51228 1.01394 -0.13308 -0.14915 0.34213  127 LEU B CD1 
5138 C CD2 . LEU D 115 ? 1.20459 1.27522 0.91877 -0.15588 -0.13282 0.36527  127 LEU B CD2 
5139 N N   . ASN D 116 ? 1.34276 1.38886 0.98660 -0.10411 -0.26250 0.44847  128 ASN B N   
5140 C CA  . ASN D 116 ? 1.34218 1.36670 0.99921 -0.09480 -0.28252 0.49078  128 ASN B CA  
5141 C C   . ASN D 116 ? 1.29501 1.31789 1.01937 -0.07769 -0.30628 0.48582  128 ASN B C   
5142 O O   . ASN D 116 ? 1.35343 1.35735 1.10414 -0.06318 -0.31559 0.51254  128 ASN B O   
5143 C CB  . ASN D 116 ? 1.53128 1.56798 1.12582 -0.08860 -0.29587 0.50481  128 ASN B CB  
5144 C CG  . ASN D 116 ? 1.73180 1.77440 1.26285 -0.09883 -0.26491 0.51348  128 ASN B CG  
5145 O OD1 . ASN D 116 ? 1.71117 1.73396 1.24913 -0.10576 -0.24257 0.54226  128 ASN B OD1 
5146 N ND2 . ASN D 116 ? 1.80705 1.87550 1.27770 -0.09807 -0.26275 0.48854  128 ASN B ND2 
5147 N N   . LYS D 117 ? 1.12060 1.16413 0.88077 -0.07598 -0.30884 0.44732  129 LYS B N   
5148 C CA  . LYS D 117 ? 1.06224 1.11486 0.89572 -0.05948 -0.32607 0.44618  129 LYS B CA  
5149 C C   . LYS D 117 ? 1.14364 1.16802 1.03295 -0.04973 -0.29619 0.43716  129 LYS B C   
5150 O O   . LYS D 117 ? 1.25849 1.29178 1.21076 -0.03122 -0.30132 0.43839  129 LYS B O   
5151 C CB  . LYS D 117 ? 1.19297 1.28344 1.03809 -0.06434 -0.34881 0.41455  129 LYS B CB  
5152 C CG  . LYS D 117 ? 1.24049 1.35311 1.04456 -0.06708 -0.39466 0.42646  129 LYS B CG  
5153 C CD  . LYS D 117 ? 1.39167 1.51728 1.14756 -0.08083 -0.40754 0.38593  129 LYS B CD  
5154 C CE  . LYS D 117 ? 1.43532 1.57570 1.17779 -0.08037 -0.45429 0.38195  129 LYS B CE  
5155 N NZ  . LYS D 117 ? 1.46495 1.60195 1.19943 -0.06837 -0.46543 0.41760  129 LYS B NZ  
5156 N N   . VAL D 118 ? 1.10660 1.09805 0.97389 -0.06097 -0.26617 0.42996  130 VAL B N   
5157 C CA  . VAL D 118 ? 0.98596 0.93960 0.89048 -0.05225 -0.24207 0.41832  130 VAL B CA  
5158 C C   . VAL D 118 ? 1.08428 0.98874 0.99966 -0.03419 -0.24402 0.45309  130 VAL B C   
5159 O O   . VAL D 118 ? 1.09802 0.97918 0.97827 -0.04325 -0.24902 0.48289  130 VAL B O   
5160 C CB  . VAL D 118 ? 1.09143 1.02891 0.97007 -0.07473 -0.21650 0.39676  130 VAL B CB  
5161 C CG1 . VAL D 118 ? 1.17382 1.07096 1.08295 -0.06587 -0.19762 0.37796  130 VAL B CG1 
5162 C CG2 . VAL D 118 ? 0.98530 0.97003 0.84463 -0.08899 -0.21430 0.36721  130 VAL B CG2 
5163 N N   . PHE D 119 ? 1.03682 0.92366 0.99983 -0.00598 -0.23814 0.45150  131 PHE B N   
5164 C CA  . PHE D 119 ? 1.13165 0.96528 1.10586 0.02000  -0.23792 0.48133  131 PHE B CA  
5165 C C   . PHE D 119 ? 1.06805 0.85143 1.06076 0.04219  -0.21271 0.46046  131 PHE B C   
5166 O O   . PHE D 119 ? 0.97318 0.78653 0.99718 0.05184  -0.20060 0.43513  131 PHE B O   
5167 C CB  . PHE D 119 ? 1.04249 0.91234 1.05685 0.04624  -0.26110 0.51338  131 PHE B CB  
5168 C CG  . PHE D 119 ? 1.07679 0.97810 1.05880 0.02990  -0.28634 0.53265  131 PHE B CG  
5169 C CD1 . PHE D 119 ? 1.05068 1.01290 1.02299 0.01161  -0.30834 0.52282  131 PHE B CD1 
5170 C CD2 . PHE D 119 ? 1.14542 1.00975 1.10056 0.03447  -0.28765 0.55722  131 PHE B CD2 
5171 C CE1 . PHE D 119 ? 1.15708 1.14060 1.08668 0.00033  -0.32995 0.53537  131 PHE B CE1 
5172 C CE2 . PHE D 119 ? 1.18471 1.07671 1.10455 0.02239  -0.30785 0.57428  131 PHE B CE2 
5173 C CZ  . PHE D 119 ? 1.16232 1.11303 1.06599 0.00642  -0.32848 0.56255  131 PHE B CZ  
5174 N N   . PRO D 120 ? 1.14165 0.84389 1.11056 0.05084  -0.20555 0.47058  132 PRO B N   
5175 C CA  . PRO D 120 ? 1.13447 0.77523 1.10616 0.07855  -0.18412 0.44997  132 PRO B CA  
5176 C C   . PRO D 120 ? 1.14064 0.77893 1.15350 0.13040  -0.17872 0.47041  132 PRO B C   
5177 O O   . PRO D 120 ? 1.20948 0.87052 1.24016 0.14206  -0.19363 0.50146  132 PRO B O   
5178 C CB  . PRO D 120 ? 1.33955 0.88631 1.26232 0.06247  -0.18657 0.45430  132 PRO B CB  
5179 C CG  . PRO D 120 ? 1.20612 0.76337 1.11986 0.04908  -0.20502 0.49229  132 PRO B CG  
5180 C CD  . PRO D 120 ? 1.28017 0.93657 1.21061 0.03206  -0.21739 0.49985  132 PRO B CD  
5181 N N   . PRO D 121 ? 1.12022 0.73670 1.14642 0.16425  -0.15384 0.45045  133 PRO B N   
5182 C CA  . PRO D 121 ? 1.18550 0.80869 1.25555 0.21894  -0.14104 0.47079  133 PRO B CA  
5183 C C   . PRO D 121 ? 1.24972 0.77512 1.27851 0.24877  -0.13539 0.47481  133 PRO B C   
5184 O O   . PRO D 121 ? 1.39471 0.82593 1.36429 0.23720  -0.13591 0.46130  133 PRO B O   
5185 C CB  . PRO D 121 ? 1.10989 0.74741 1.19895 0.24229  -0.11094 0.44503  133 PRO B CB  
5186 C CG  . PRO D 121 ? 1.18756 0.76636 1.21213 0.21083  -0.10651 0.40512  133 PRO B CG  
5187 C CD  . PRO D 121 ? 1.09964 0.69688 1.10292 0.15521  -0.13432 0.40833  133 PRO B CD  
5188 N N   . GLU D 122 ? 1.07783 0.93635 0.68905 -0.08078 -0.12843 0.06752  134 GLU B N   
5189 C CA  . GLU D 122 ? 1.23207 1.02566 0.82294 -0.10242 -0.10711 0.04976  134 GLU B CA  
5190 C C   . GLU D 122 ? 1.39618 1.17560 0.97009 -0.09138 -0.10415 0.03976  134 GLU B C   
5191 O O   . GLU D 122 ? 1.35507 1.12334 0.93378 -0.05911 -0.10726 0.05818  134 GLU B O   
5192 C CB  . GLU D 122 ? 1.19319 0.91665 0.78488 -0.09045 -0.09184 0.06811  134 GLU B CB  
5193 N N   . VAL D 123 ? 1.39757 1.18214 0.95157 -0.12075 -0.09712 0.00848  135 VAL B N   
5194 C CA  . VAL D 123 ? 1.38751 1.17321 0.92216 -0.11356 -0.09490 -0.00549 135 VAL B CA  
5195 C C   . VAL D 123 ? 1.35994 1.05758 0.87311 -0.11968 -0.06821 -0.02180 135 VAL B C   
5196 O O   . VAL D 123 ? 1.47836 1.12791 0.98117 -0.14972 -0.05048 -0.03966 135 VAL B O   
5197 C CB  . VAL D 123 ? 1.44039 1.30438 0.96414 -0.13911 -0.10636 -0.03205 135 VAL B CB  
5198 C CG1 . VAL D 123 ? 1.39696 1.26747 0.89707 -0.13047 -0.10368 -0.04573 135 VAL B CG1 
5199 C CG2 . VAL D 123 ? 1.18157 1.13128 0.72559 -0.12471 -0.13079 -0.01178 135 VAL B CG2 
5200 N N   . ALA D 124 ? 1.26740 0.94169 0.77291 -0.09059 -0.06274 -0.01521 136 ALA B N   
5201 C CA  . ALA D 124 ? 1.39108 0.98431 0.87540 -0.08647 -0.03620 -0.02927 136 ALA B CA  
5202 C C   . ALA D 124 ? 1.43435 1.04450 0.90534 -0.06746 -0.03503 -0.03691 136 ALA B C   
5203 O O   . ALA D 124 ? 1.40744 1.05202 0.89367 -0.03752 -0.04699 -0.01118 136 ALA B O   
5204 C CB  . ALA D 124 ? 1.21536 0.74815 0.71122 -0.05725 -0.02505 -0.00006 136 ALA B CB  
5205 N N   . VAL D 125 ? 1.38972 0.97554 0.83120 -0.08743 -0.01871 -0.07383 137 VAL B N   
5206 C CA  . VAL D 125 ? 1.38331 0.98194 0.80708 -0.07079 -0.01322 -0.08529 137 VAL B CA  
5207 C C   . VAL D 125 ? 1.45683 0.97332 0.87246 -0.04257 0.01329  -0.08299 137 VAL B C   
5208 O O   . VAL D 125 ? 1.71450 1.15246 1.12317 -0.04732 0.03332  -0.08789 137 VAL B O   
5209 C CB  . VAL D 125 ? 1.45579 1.08588 0.84945 -0.10731 -0.01099 -0.13066 137 VAL B CB  
5210 C CG1 . VAL D 125 ? 1.49142 1.15327 0.86625 -0.08825 -0.00876 -0.13859 137 VAL B CG1 
5211 C CG2 . VAL D 125 ? 1.43731 1.15321 0.84077 -0.13424 -0.03626 -0.13257 137 VAL B CG2 
5212 N N   . PHE D 126 ? 1.40182 0.93770 0.81758 -0.01083 0.01528  -0.07332 138 PHE B N   
5213 C CA  . PHE D 126 ? 1.72793 1.20481 1.14013 0.02434  0.03879  -0.06774 138 PHE B CA  
5214 C C   . PHE D 126 ? 1.74682 1.23061 1.13225 0.03042  0.05328  -0.09556 138 PHE B C   
5215 O O   . PHE D 126 ? 1.57521 1.13089 0.96237 0.03382  0.03968  -0.09050 138 PHE B O   
5216 C CB  . PHE D 126 ? 1.55447 1.05909 1.00111 0.06140  0.02798  -0.02445 138 PHE B CB  
5217 C CG  . PHE D 126 ? 1.61508 1.10910 1.08484 0.05952  0.01690  0.00100  138 PHE B CG  
5218 C CD1 . PHE D 126 ? 1.50025 1.04844 0.98725 0.03999  -0.00837 0.01256  138 PHE B CD1 
5219 C CD2 . PHE D 126 ? 1.82440 1.25553 1.29603 0.08065  0.03319  0.01442  138 PHE B CD2 
5220 C CE1 . PHE D 126 ? 1.46202 1.00378 0.96866 0.03864  -0.01727 0.03353  138 PHE B CE1 
5221 C CE2 . PHE D 126 ? 1.82348 1.25012 1.31310 0.07927  0.02367  0.03831  138 PHE B CE2 
5222 C CZ  . PHE D 126 ? 1.55144 1.03440 1.05903 0.05667  -0.00164 0.04606  138 PHE B CZ  
5223 N N   . GLU D 127 ? 1.78786 1.19319 1.14594 0.03285  0.08322  -0.12416 139 GLU B N   
5224 C CA  . GLU D 127 ? 1.65462 1.05982 0.98246 0.03710  0.10074  -0.15770 139 GLU B CA  
5225 C C   . GLU D 127 ? 1.79167 1.23236 1.13462 0.08382  0.10366  -0.13282 139 GLU B C   
5226 O O   . GLU D 127 ? 1.78019 1.20192 1.14750 0.11876  0.10751  -0.10117 139 GLU B O   
5227 C CB  . GLU D 127 ? 1.87107 1.16907 1.16503 0.03116  0.13658  -0.19490 139 GLU B CB  
5228 C CG  . GLU D 127 ? 1.91202 1.16529 1.19083 -0.02075 0.14003  -0.22251 139 GLU B CG  
5229 C CD  . GLU D 127 ? 2.05909 1.19123 1.30067 -0.02869 0.18124  -0.26034 139 GLU B CD  
5230 O OE1 . GLU D 127 ? 2.07645 1.15528 1.30619 0.01534  0.20660  -0.25894 139 GLU B OE1 
5231 O OE2 . GLU D 127 ? 2.22382 1.31371 1.44768 -0.07907 0.19024  -0.29214 139 GLU B OE2 
5232 N N   . PRO D 128 ? 1.79763 1.29528 1.12576 0.08479  0.10326  -0.14721 140 PRO B N   
5233 C CA  . PRO D 128 ? 1.83263 1.37570 1.17749 0.12352  0.10653  -0.12309 140 PRO B CA  
5234 C C   . PRO D 128 ? 1.82863 1.31091 1.17116 0.16515  0.13655  -0.12614 140 PRO B C   
5235 O O   . PRO D 128 ? 1.92928 1.32611 1.24498 0.16499  0.16071  -0.15476 140 PRO B O   
5236 C CB  . PRO D 128 ? 1.65730 1.26253 0.97522 0.11019  0.10557  -0.14548 140 PRO B CB  
5237 C CG  . PRO D 128 ? 1.72453 1.29181 1.00376 0.07453  0.11387  -0.19456 140 PRO B CG  
5238 C CD  . PRO D 128 ? 1.70911 1.23647 1.00209 0.04954  0.10204  -0.18841 140 PRO B CD  
5239 N N   . SER D 129 ? 1.79520 1.32373 1.16607 0.20160  0.13651  -0.09597 141 SER B N   
5240 C CA  . SER D 129 ? 1.99013 1.48196 1.36549 0.24999  0.16232  -0.09147 141 SER B CA  
5241 C C   . SER D 129 ? 2.00973 1.48939 1.35121 0.26499  0.19054  -0.12786 141 SER B C   
5242 O O   . SER D 129 ? 1.91103 1.44845 1.23787 0.24688  0.18635  -0.14372 141 SER B O   
5243 C CB  . SER D 129 ? 1.92832 1.49304 1.34865 0.28019  0.15167  -0.05033 141 SER B CB  
5244 O OG  . SER D 129 ? 1.84731 1.49715 1.27397 0.27419  0.14621  -0.04775 141 SER B OG  
5245 N N   . GLU D 130 ? 1.85265 1.25492 1.17904 0.30165  0.22133  -0.13988 142 GLU B N   
5246 C CA  . GLU D 130 ? 1.79492 1.17965 1.08951 0.32439  0.25250  -0.17508 142 GLU B CA  
5247 C C   . GLU D 130 ? 1.92334 1.40424 1.24269 0.36047  0.25468  -0.15631 142 GLU B C   
5248 O O   . GLU D 130 ? 1.94681 1.44303 1.24180 0.37310  0.27571  -0.18482 142 GLU B O   
5249 C CB  . GLU D 130 ? 1.87921 1.14422 1.14945 0.35930  0.28845  -0.19013 142 GLU B CB  
5250 N N   . ALA D 131 ? 1.86521 1.41438 1.23198 0.37461  0.23490  -0.11162 143 ALA B N   
5251 C CA  . ALA D 131 ? 1.86877 1.51851 1.26317 0.40039  0.23707  -0.09425 143 ALA B CA  
5252 C C   . ALA D 131 ? 1.93551 1.66445 1.32594 0.36088  0.22170  -0.09698 143 ALA B C   
5253 O O   . ALA D 131 ? 1.93357 1.72719 1.32342 0.37476  0.23493  -0.10147 143 ALA B O   
5254 C CB  . ALA D 131 ? 1.81313 1.51308 1.25929 0.42314  0.22218  -0.04998 143 ALA B CB  
5255 N N   . GLU D 132 ? 1.89320 1.62027 1.27948 0.31453  0.19557  -0.09227 144 GLU B N   
5256 C CA  . GLU D 132 ? 1.81719 1.61293 1.19349 0.28145  0.18217  -0.09085 144 GLU B CA  
5257 C C   . GLU D 132 ? 1.91964 1.70442 1.24481 0.27072  0.19843  -0.13450 144 GLU B C   
5258 O O   . GLU D 132 ? 1.86956 1.72293 1.18207 0.26429  0.20109  -0.13539 144 GLU B O   
5259 C CB  . GLU D 132 ? 1.83396 1.63120 1.21935 0.24245  0.15067  -0.07208 144 GLU B CB  
5260 C CG  . GLU D 132 ? 1.78860 1.65509 1.16435 0.21483  0.13655  -0.06086 144 GLU B CG  
5261 C CD  . GLU D 132 ? 1.72741 1.58737 1.10305 0.18140  0.10854  -0.04919 144 GLU B CD  
5262 O OE1 . GLU D 132 ? 1.83304 1.63911 1.21910 0.17627  0.09972  -0.05059 144 GLU B OE1 
5263 O OE2 . GLU D 132 ? 1.54520 1.45560 0.90903 0.16277  0.09678  -0.03682 144 GLU B OE2 
5264 N N   . ILE D 133 ? 1.96008 1.65930 1.25347 0.26661  0.21116  -0.17180 145 ILE B N   
5265 C CA  . ILE D 133 ? 1.97709 1.66367 1.21918 0.25061  0.22683  -0.22119 145 ILE B CA  
5266 C C   . ILE D 133 ? 2.05885 1.77094 1.28844 0.28840  0.25723  -0.23739 145 ILE B C   
5267 O O   . ILE D 133 ? 2.22212 1.98093 1.41890 0.27730  0.26454  -0.26240 145 ILE B O   
5268 C CB  . ILE D 133 ? 2.10514 1.68495 1.31817 0.23298  0.23740  -0.26009 145 ILE B CB  
5269 C CG1 . ILE D 133 ? 1.89363 1.46444 1.12027 0.19273  0.20693  -0.24448 145 ILE B CG1 
5270 C CG2 . ILE D 133 ? 2.11759 1.68305 1.27597 0.21350  0.25646  -0.31930 145 ILE B CG2 
5271 C CD1 . ILE D 133 ? 2.02623 1.49538 1.22867 0.16852  0.21796  -0.27944 145 ILE B CD1 
5272 N N   . SER D 134 ? 2.09306 1.78383 1.34819 0.33598  0.27535  -0.22238 146 SER B N   
5273 C CA  . SER D 134 ? 2.12777 1.84548 1.37511 0.37886  0.30638  -0.23691 146 SER B CA  
5274 C C   . SER D 134 ? 2.08532 1.92233 1.36728 0.38954  0.30012  -0.20138 146 SER B C   
5275 O O   . SER D 134 ? 2.08433 1.96553 1.36005 0.41982  0.32489  -0.21326 146 SER B O   
5276 C CB  . SER D 134 ? 2.08093 1.72188 1.33694 0.43209  0.33214  -0.23782 146 SER B CB  
5277 O OG  . SER D 134 ? 2.02557 1.68345 1.33171 0.44874  0.31464  -0.18976 146 SER B OG  
5278 N N   . HIS D 135 ? 1.94365 1.83187 1.26078 0.36418  0.27045  -0.15998 147 HIS B N   
5279 C CA  . HIS D 135 ? 1.82221 1.81551 1.17342 0.36621  0.26640  -0.12548 147 HIS B CA  
5280 C C   . HIS D 135 ? 1.77152 1.82319 1.10319 0.32512  0.25286  -0.11745 147 HIS B C   
5281 O O   . HIS D 135 ? 1.72927 1.85819 1.06064 0.32868  0.26552  -0.10954 147 HIS B O   
5282 C CB  . HIS D 135 ? 1.81452 1.82525 1.22117 0.36951  0.24725  -0.08308 147 HIS B CB  
5283 C CG  . HIS D 135 ? 1.82955 1.94416 1.27514 0.36863  0.24709  -0.05154 147 HIS B CG  
5284 N ND1 . HIS D 135 ? 1.78980 1.95147 1.24206 0.32790  0.23011  -0.02651 147 HIS B ND1 
5285 C CD2 . HIS D 135 ? 1.81763 1.99898 1.29749 0.40218  0.26392  -0.04138 147 HIS B CD2 
5286 C CE1 . HIS D 135 ? 1.78119 2.02685 1.26921 0.33114  0.23816  -0.00379 147 HIS B CE1 
5287 N NE2 . HIS D 135 ? 1.87568 2.14257 1.38311 0.37468  0.25738  -0.01334 147 HIS B NE2 
5288 N N   . THR D 136 ? 1.86249 1.88292 1.17701 0.28823  0.22868  -0.11706 148 THR B N   
5289 C CA  . THR D 136 ? 1.84719 1.92177 1.14069 0.25502  0.21460  -0.10392 148 THR B CA  
5290 C C   . THR D 136 ? 1.83593 1.89086 1.07368 0.23394  0.21267  -0.14359 148 THR B C   
5291 O O   . THR D 136 ? 1.69123 1.79748 0.90492 0.21106  0.20114  -0.13342 148 THR B O   
5292 C CB  . THR D 136 ? 1.85623 1.93413 1.18028 0.23065  0.18528  -0.06250 148 THR B CB  
5293 O OG1 . THR D 136 ? 1.86709 1.87264 1.19253 0.22102  0.16891  -0.07412 148 THR B OG1 
5294 C CG2 . THR D 136 ? 1.82866 1.94054 1.20623 0.24356  0.18709  -0.02631 148 THR B CG2 
5295 N N   . GLN D 137 ? 1.93831 1.92156 1.15341 0.24050  0.22485  -0.18835 149 GLN B N   
5296 C CA  . GLN D 137 ? 1.90343 1.86639 1.06671 0.21394  0.22389  -0.23460 149 GLN B CA  
5297 C C   . GLN D 137 ? 1.74373 1.71814 0.90494 0.17560  0.19055  -0.22004 149 GLN B C   
5298 O O   . GLN D 137 ? 1.67541 1.68458 0.79681 0.15016  0.18242  -0.24342 149 GLN B O   
5299 C CB  . GLN D 137 ? 1.73872 1.76713 0.85917 0.21628  0.24121  -0.25881 149 GLN B CB  
5300 N N   . LYS D 138 ? 1.85381 1.80638 1.05751 0.17322  0.17113  -0.18216 150 LYS B N   
5301 C CA  . LYS D 138 ? 1.76329 1.72537 0.97063 0.14280  0.14053  -0.16530 150 LYS B CA  
5302 C C   . LYS D 138 ? 1.74546 1.63261 0.98280 0.13966  0.13178  -0.16143 150 LYS B C   
5303 O O   . LYS D 138 ? 1.72982 1.58273 1.00004 0.16519  0.14108  -0.14441 150 LYS B O   
5304 C CB  . LYS D 138 ? 1.55983 1.58902 0.78691 0.14204  0.12432  -0.11172 150 LYS B CB  
5305 N N   . ALA D 139 ? 1.72616 1.59633 0.95165 0.10877  0.11422  -0.17676 151 ALA B N   
5306 C CA  . ALA D 139 ? 1.67673 1.47912 0.92560 0.10019  0.10631  -0.17437 151 ALA B CA  
5307 C C   . ALA D 139 ? 1.60002 1.43975 0.87201 0.08345  0.07503  -0.13815 151 ALA B C   
5308 O O   . ALA D 139 ? 1.52849 1.42445 0.78026 0.06274  0.05872  -0.14093 151 ALA B O   
5309 C CB  . ALA D 139 ? 1.74211 1.48499 0.95840 0.07439  0.11726  -0.22817 151 ALA B CB  
5310 N N   . THR D 140 ? 1.61034 1.42269 0.92302 0.09520  0.06730  -0.10467 152 THR B N   
5311 C CA  . THR D 140 ? 1.59287 1.43340 0.93019 0.08438  0.04067  -0.06941 152 THR B CA  
5312 C C   . THR D 140 ? 1.51020 1.29410 0.86414 0.07213  0.03319  -0.07380 152 THR B C   
5313 O O   . THR D 140 ? 1.62095 1.35606 0.99809 0.08989  0.04200  -0.06354 152 THR B O   
5314 C CB  . THR D 140 ? 1.56465 1.43303 0.93538 0.10527  0.03825  -0.02518 152 THR B CB  
5315 O OG1 . THR D 140 ? 1.63406 1.55263 0.98795 0.11449  0.04976  -0.02081 152 THR B OG1 
5316 C CG2 . THR D 140 ? 1.43082 1.32205 0.82104 0.09437  0.01381  0.00779  152 THR B CG2 
5317 N N   . LEU D 141 ? 1.34766 1.14557 0.68939 0.04278  0.01744  -0.08773 153 LEU B N   
5318 C CA  . LEU D 141 ? 1.35864 1.11438 0.71636 0.02629  0.00946  -0.08937 153 LEU B CA  
5319 C C   . LEU D 141 ? 1.43745 1.22300 0.82891 0.03230  -0.01317 -0.04665 153 LEU B C   
5320 O O   . LEU D 141 ? 1.47195 1.31721 0.86341 0.03551  -0.02722 -0.02533 153 LEU B O   
5321 C CB  . LEU D 141 ? 1.36048 1.12637 0.69168 -0.01226 0.00472  -0.12857 153 LEU B CB  
5322 C CG  . LEU D 141 ? 1.53651 1.24888 0.83395 -0.02980 0.02990  -0.18081 153 LEU B CG  
5323 C CD1 . LEU D 141 ? 1.64307 1.39160 0.90855 -0.02125 0.04128  -0.20233 153 LEU B CD1 
5324 C CD2 . LEU D 141 ? 1.56319 1.27823 0.84685 -0.07640 0.02403  -0.21639 153 LEU B CD2 
5325 N N   . VAL D 142 ? 1.43952 1.18006 0.85665 0.03533  -0.01457 -0.03383 154 VAL B N   
5326 C CA  . VAL D 142 ? 1.33693 1.09761 0.78617 0.04162  -0.03325 0.00231  154 VAL B CA  
5327 C C   . VAL D 142 ? 1.27097 1.01587 0.72633 0.01896  -0.04350 -0.00471 154 VAL B C   
5328 O O   . VAL D 142 ? 1.49442 1.18112 0.94723 0.01169  -0.03064 -0.01984 154 VAL B O   
5329 C CB  . VAL D 142 ? 1.21654 0.95433 0.69438 0.06892  -0.02625 0.02757  154 VAL B CB  
5330 C CG1 . VAL D 142 ? 1.08593 0.83810 0.59435 0.07013  -0.04420 0.05701  154 VAL B CG1 
5331 C CG2 . VAL D 142 ? 1.32805 1.09646 0.80447 0.08738  -0.01662 0.03630  154 VAL B CG2 
5332 N N   . CYS D 143 ? 1.26675 1.06275 0.72891 0.00950  -0.06433 0.00779  155 CYS B N   
5333 C CA  . CYS D 143 ? 1.38500 1.18206 0.85870 -0.00972 -0.07574 0.00584  155 CYS B CA  
5334 C C   . CYS D 143 ? 1.30562 1.10341 0.81145 0.00759  -0.08695 0.04084  155 CYS B C   
5335 O O   . CYS D 143 ? 1.31288 1.12910 0.82927 0.02798  -0.09109 0.06539  155 CYS B O   
5336 C CB  . CYS D 143 ? 1.38473 1.24989 0.84402 -0.03008 -0.09122 -0.00756 155 CYS B CB  
5337 S SG  . CYS D 143 ? 1.33096 1.21279 0.80489 -0.05840 -0.10315 -0.01613 155 CYS B SG  
5338 N N   . LEU D 144 ? 1.39012 1.16694 0.90991 -0.00335 -0.08984 0.04132  156 LEU B N   
5339 C CA  . LEU D 144 ? 1.23002 1.00464 0.77813 0.01190  -0.09851 0.06950  156 LEU B CA  
5340 C C   . LEU D 144 ? 1.19800 0.98895 0.75551 -0.00590 -0.10912 0.06781  156 LEU B C   
5341 O O   . LEU D 144 ? 1.29551 1.06049 0.84516 -0.02852 -0.10056 0.04904  156 LEU B O   
5342 C CB  . LEU D 144 ? 1.09328 0.81590 0.65168 0.02853  -0.08471 0.07804  156 LEU B CB  
5343 C CG  . LEU D 144 ? 1.10928 0.83885 0.69576 0.04613  -0.09293 0.10468  156 LEU B CG  
5344 C CD1 . LEU D 144 ? 1.28482 1.05054 0.88050 0.05830  -0.10045 0.11997  156 LEU B CD1 
5345 C CD2 . LEU D 144 ? 1.35218 1.04275 0.94565 0.06388  -0.07972 0.11151  156 LEU B CD2 
5346 N N   . ALA D 145 ? 1.02823 0.85963 0.60161 0.00401  -0.12506 0.08705  157 ALA B N   
5347 C CA  . ALA D 145 ? 0.97363 0.82969 0.56012 -0.00663 -0.13541 0.08890  157 ALA B CA  
5348 C C   . ALA D 145 ? 1.07056 0.91544 0.68034 0.01297  -0.13987 0.11273  157 ALA B C   
5349 O O   . ALA D 145 ? 1.03288 0.88972 0.64952 0.03248  -0.14530 0.12942  157 ALA B O   
5350 C CB  . ALA D 145 ? 0.99333 0.91891 0.57463 -0.00955 -0.15022 0.08663  157 ALA B CB  
5351 N N   . THR D 146 ? 1.10174 0.92258 0.72124 0.00614  -0.13574 0.11358  158 THR B N   
5352 C CA  . THR D 146 ? 1.09765 0.90965 0.73644 0.02309  -0.13863 0.13206  158 THR B CA  
5353 C C   . THR D 146 ? 1.03923 0.87215 0.68876 0.01408  -0.14479 0.13381  158 THR B C   
5354 O O   . THR D 146 ? 1.15118 0.99143 0.79419 -0.00904 -0.14180 0.12100  158 THR B O   
5355 C CB  . THR D 146 ? 0.93099 0.69690 0.56986 0.03237  -0.12563 0.13692  158 THR B CB  
5356 O OG1 . THR D 146 ? 1.06247 0.79288 0.68779 0.01594  -0.11280 0.12671  158 THR B OG1 
5357 C CG2 . THR D 146 ? 1.10989 0.86478 0.74246 0.04485  -0.11895 0.13617  158 THR B CG2 
5358 N N   . GLY D 147 ? 1.08319 0.92784 0.74906 0.03006  -0.15185 0.14744  159 GLY B N   
5359 C CA  . GLY D 147 ? 0.87021 0.73476 0.54675 0.02597  -0.15595 0.15035  159 GLY B CA  
5360 C C   . GLY D 147 ? 0.81461 0.72958 0.49338 0.01708  -0.16463 0.14351  159 GLY B C   
5361 O O   . GLY D 147 ? 1.20932 1.13996 0.88856 -0.00337 -0.16184 0.13605  159 GLY B O   
5362 N N   . PHE D 148 ? 0.93043 0.87389 0.61017 0.03312  -0.17365 0.14746  160 PHE B N   
5363 C CA  . PHE D 148 ? 0.97705 0.98000 0.65977 0.03417  -0.18299 0.14446  160 PHE B CA  
5364 C C   . PHE D 148 ? 0.92635 0.94195 0.61800 0.06446  -0.18913 0.15822  160 PHE B C   
5365 O O   . PHE D 148 ? 0.98103 0.96123 0.67077 0.08098  -0.18639 0.16796  160 PHE B O   
5366 C CB  . PHE D 148 ? 0.90129 0.93485 0.56895 0.02712  -0.18646 0.13574  160 PHE B CB  
5367 C CG  . PHE D 148 ? 0.87544 0.88985 0.53149 0.04788  -0.18635 0.14692  160 PHE B CG  
5368 C CD1 . PHE D 148 ? 1.03295 1.00259 0.67818 0.04087  -0.17721 0.14318  160 PHE B CD1 
5369 C CD2 . PHE D 148 ? 0.94485 0.98517 0.59911 0.07594  -0.19289 0.16267  160 PHE B CD2 
5370 C CE1 . PHE D 148 ? 0.90782 0.86490 0.54258 0.05716  -0.17507 0.15400  160 PHE B CE1 
5371 C CE2 . PHE D 148 ? 0.87749 0.89552 0.51825 0.09266  -0.18928 0.17599  160 PHE B CE2 
5372 C CZ  . PHE D 148 ? 0.98832 0.96790 0.62019 0.08104  -0.18062 0.17112  160 PHE B CZ  
5373 N N   . TYR D 149 ? 0.87184 0.93767 0.57303 0.07053  -0.19515 0.15753  161 TYR B N   
5374 C CA  . TYR D 149 ? 0.91255 0.98984 0.61961 0.10256  -0.19848 0.16859  161 TYR B CA  
5375 C C   . TYR D 149 ? 1.01307 1.16829 0.72498 0.11092  -0.20648 0.16679  161 TYR B C   
5376 O O   . TYR D 149 ? 1.04551 1.24297 0.76630 0.08700  -0.20770 0.15466  161 TYR B O   
5377 C CB  . TYR D 149 ? 0.79041 0.84164 0.50908 0.10760  -0.19435 0.16861  161 TYR B CB  
5378 C CG  . TYR D 149 ? 0.98932 1.04180 0.71131 0.14000  -0.19416 0.17541  161 TYR B CG  
5379 C CD1 . TYR D 149 ? 1.07565 1.07548 0.79078 0.15631  -0.18809 0.18303  161 TYR B CD1 
5380 C CD2 . TYR D 149 ? 0.90504 1.00907 0.63621 0.15371  -0.19728 0.17320  161 TYR B CD2 
5381 C CE1 . TYR D 149 ? 1.04478 1.03114 0.75913 0.18511  -0.18341 0.18772  161 TYR B CE1 
5382 C CE2 . TYR D 149 ? 1.06007 1.15754 0.79155 0.18770  -0.19404 0.17837  161 TYR B CE2 
5383 C CZ  . TYR D 149 ? 1.09062 1.12308 0.81216 0.20317  -0.18624 0.18535  161 TYR B CZ  
5384 O OH  . TYR D 149 ? 1.06454 1.07635 0.78276 0.23610  -0.17869 0.18901  161 TYR B OH  
5385 N N   . PRO D 150 ? 0.91252 1.09090 0.61842 0.14477  -0.21042 0.17977  162 PRO B N   
5386 C CA  . PRO D 150 ? 1.00899 1.13499 0.70090 0.17173  -0.20530 0.19688  162 PRO B CA  
5387 C C   . PRO D 150 ? 1.02356 1.13805 0.69786 0.16051  -0.20520 0.19928  162 PRO B C   
5388 O O   . PRO D 150 ? 0.93388 1.07463 0.60628 0.13154  -0.20871 0.18441  162 PRO B O   
5389 C CB  . PRO D 150 ? 1.03765 1.20424 0.72683 0.21437  -0.20795 0.21186  162 PRO B CB  
5390 C CG  . PRO D 150 ? 1.07378 1.31242 0.78169 0.21082  -0.21438 0.20004  162 PRO B CG  
5391 C CD  . PRO D 150 ? 0.91594 1.17812 0.62970 0.16309  -0.21801 0.18078  162 PRO B CD  
5392 N N   . ASP D 151 ? 1.05244 1.12539 0.71172 0.18166  -0.19878 0.21687  163 ASP B N   
5393 C CA  . ASP D 151 ? 1.03458 1.10111 0.67460 0.17457  -0.19718 0.22117  163 ASP B CA  
5394 C C   . ASP D 151 ? 1.05230 1.19328 0.67680 0.18972  -0.20662 0.22781  163 ASP B C   
5395 O O   . ASP D 151 ? 0.99811 1.13332 0.60361 0.20293  -0.20253 0.24226  163 ASP B O   
5396 C CB  . ASP D 151 ? 0.95511 0.95141 0.58486 0.18813  -0.18403 0.23878  163 ASP B CB  
5397 C CG  . ASP D 151 ? 1.42600 1.40516 1.04898 0.22663  -0.17802 0.26086  163 ASP B CG  
5398 O OD1 . ASP D 151 ? 1.51627 1.52320 1.15163 0.24150  -0.18246 0.25781  163 ASP B OD1 
5399 O OD2 . ASP D 151 ? 1.48489 1.41986 1.09392 0.23863  -0.16519 0.27888  163 ASP B OD2 
5400 N N   . HIS D 152 ? 1.01682 1.23361 0.65227 0.18461  -0.21767 0.21543  164 HIS B N   
5401 C CA  . HIS D 152 ? 1.13299 1.43133 0.76509 0.19090  -0.22481 0.21251  164 HIS B CA  
5402 C C   . HIS D 152 ? 1.03176 1.37325 0.64843 0.15481  -0.23295 0.19118  164 HIS B C   
5403 O O   . HIS D 152 ? 1.19480 1.61176 0.81935 0.13093  -0.24183 0.16927  164 HIS B O   
5404 C CB  . HIS D 152 ? 1.13825 1.50408 0.79450 0.20137  -0.22968 0.20637  164 HIS B CB  
5405 C CG  . HIS D 152 ? 1.03981 1.36979 0.70628 0.24054  -0.22024 0.22506  164 HIS B CG  
5406 N ND1 . HIS D 152 ? 0.94959 1.33576 0.63599 0.25991  -0.22129 0.22305  164 HIS B ND1 
5407 C CD2 . HIS D 152 ? 1.02621 1.27075 0.68400 0.26272  -0.20768 0.24411  164 HIS B CD2 
5408 C CE1 . HIS D 152 ? 1.05744 1.39045 0.74399 0.29540  -0.20994 0.23998  164 HIS B CE1 
5409 N NE2 . HIS D 152 ? 1.05022 1.29531 0.71945 0.29553  -0.20134 0.25225  164 HIS B NE2 
5410 N N   . VAL D 153 ? 0.89625 1.18144 0.49523 0.14515  -0.22512 0.19233  165 VAL B N   
5411 C CA  . VAL D 153 ? 1.08837 1.38776 0.67519 0.10837  -0.22497 0.16599  165 VAL B CA  
5412 C C   . VAL D 153 ? 1.19241 1.50440 0.74912 0.12560  -0.22424 0.17929  165 VAL B C   
5413 O O   . VAL D 153 ? 1.32558 1.60553 0.87374 0.15978  -0.21832 0.20984  165 VAL B O   
5414 C CB  . VAL D 153 ? 0.96032 1.17686 0.55498 0.07695  -0.21260 0.14940  165 VAL B CB  
5415 C CG1 . VAL D 153 ? 0.97119 1.17508 0.59142 0.06214  -0.21186 0.14077  165 VAL B CG1 
5416 C CG2 . VAL D 153 ? 0.97549 1.11505 0.56472 0.09527  -0.20157 0.16999  165 VAL B CG2 
5417 N N   . GLU D 154 ? 1.36442 1.71832 0.90529 0.09803  -0.22704 0.15343  166 GLU B N   
5418 C CA  . GLU D 154 ? 1.30071 1.66690 0.80997 0.10818  -0.22465 0.16069  166 GLU B CA  
5419 C C   . GLU D 154 ? 1.27645 1.64145 0.77419 0.06480  -0.21986 0.12070  166 GLU B C   
5420 O O   . GLU D 154 ? 1.17897 1.59331 0.68247 0.03167  -0.22577 0.08762  166 GLU B O   
5421 C CB  . GLU D 154 ? 1.38958 1.83194 0.89756 0.13368  -0.23055 0.17191  166 GLU B CB  
5422 C CG  . GLU D 154 ? 1.68249 2.11454 1.16489 0.15250  -0.22195 0.19002  166 GLU B CG  
5423 C CD  . GLU D 154 ? 1.77964 2.11485 1.25582 0.17016  -0.20733 0.22004  166 GLU B CD  
5424 O OE1 . GLU D 154 ? 1.69918 1.98836 1.19536 0.18994  -0.20243 0.24096  166 GLU B OE1 
5425 O OE2 . GLU D 154 ? 1.81339 2.12102 1.26516 0.16217  -0.19922 0.22001  166 GLU B OE2 
5426 N N   . LEU D 155 ? 1.32776 1.63558 0.80899 0.06405  -0.20691 0.12241  167 LEU B N   
5427 C CA  . LEU D 155 ? 1.34201 1.62589 0.81133 0.02824  -0.19703 0.08524  167 LEU B CA  
5428 C C   . LEU D 155 ? 1.30375 1.64955 0.73734 0.02844  -0.19931 0.07491  167 LEU B C   
5429 O O   . LEU D 155 ? 1.27599 1.65071 0.69145 0.06195  -0.20221 0.10670  167 LEU B O   
5430 C CB  . LEU D 155 ? 1.27613 1.45934 0.75330 0.02911  -0.17949 0.09130  167 LEU B CB  
5431 C CG  . LEU D 155 ? 1.47871 1.61085 0.95019 -0.00142 -0.16460 0.05627  167 LEU B CG  
5432 C CD1 . LEU D 155 ? 1.28840 1.33528 0.78238 0.00433  -0.15266 0.06785  167 LEU B CD1 
5433 C CD2 . LEU D 155 ? 1.55007 1.69219 0.98988 -0.00114 -0.15597 0.04458  167 LEU B CD2 
5434 N N   . SER D 156 ? 1.20103 1.56424 0.62180 -0.01006 -0.19591 0.02963  168 SER B N   
5435 C CA  . SER D 156 ? 1.36498 1.78775 0.74935 -0.01628 -0.19663 0.01021  168 SER B CA  
5436 C C   . SER D 156 ? 1.37350 1.75013 0.74642 -0.05816 -0.18053 -0.03986 168 SER B C   
5437 O O   . SER D 156 ? 1.41828 1.75355 0.80869 -0.09027 -0.17429 -0.06621 168 SER B O   
5438 C CB  . SER D 156 ? 1.31355 1.86582 0.68788 -0.01739 -0.21747 0.00243  168 SER B CB  
5439 O OG  . SER D 156 ? 1.51388 2.09520 0.90732 -0.05865 -0.22249 -0.03517 168 SER B OG  
5440 N N   . TRP D 157 ? 1.37030 1.75036 0.71119 -0.05615 -0.17127 -0.05177 169 TRP B N   
5441 C CA  . TRP D 157 ? 1.38994 1.72573 0.71304 -0.09071 -0.15305 -0.10129 169 TRP B CA  
5442 C C   . TRP D 157 ? 1.54050 1.97035 0.83562 -0.12439 -0.16080 -0.14828 169 TRP B C   
5443 O O   . TRP D 157 ? 1.63020 2.16624 0.90822 -0.10882 -0.17836 -0.13624 169 TRP B O   
5444 C CB  . TRP D 157 ? 1.48875 1.77145 0.79380 -0.06881 -0.13514 -0.09112 169 TRP B CB  
5445 C CG  . TRP D 157 ? 1.46069 1.64539 0.79357 -0.04864 -0.12244 -0.06204 169 TRP B CG  
5446 C CD1 . TRP D 157 ? 1.33269 1.50438 0.68526 -0.01493 -0.12714 -0.01185 169 TRP B CD1 
5447 C CD2 . TRP D 157 ? 1.34361 1.43356 0.68612 -0.06048 -0.10192 -0.08238 169 TRP B CD2 
5448 N NE1 . TRP D 157 ? 1.23292 1.31926 0.60891 -0.00831 -0.11319 -0.00267 169 TRP B NE1 
5449 C CE2 . TRP D 157 ? 1.33635 1.37358 0.70642 -0.03209 -0.09815 -0.04253 169 TRP B CE2 
5450 C CE3 . TRP D 157 ? 1.36563 1.40815 0.69417 -0.09136 -0.08457 -0.13039 169 TRP B CE3 
5451 C CZ2 . TRP D 157 ? 1.44288 1.39527 0.82783 -0.02943 -0.08050 -0.04651 169 TRP B CZ2 
5452 C CZ3 . TRP D 157 ? 1.39973 1.34365 0.74072 -0.08573 -0.06418 -0.13134 169 TRP B CZ3 
5453 C CH2 . TRP D 157 ? 1.33847 1.24467 0.70793 -0.05296 -0.06369 -0.08832 169 TRP B CH2 
5454 N N   . TRP D 158 ? 1.65762 2.04763 0.94634 -0.17080 -0.14610 -0.20242 170 TRP B N   
5455 C CA  . TRP D 158 ? 1.73221 2.20319 0.99482 -0.21451 -0.14963 -0.25878 170 TRP B CA  
5456 C C   . TRP D 158 ? 1.70807 2.10313 0.94168 -0.24166 -0.12198 -0.30879 170 TRP B C   
5457 O O   . TRP D 158 ? 1.80238 2.07792 1.04684 -0.25191 -0.09941 -0.31791 170 TRP B O   
5458 C CB  . TRP D 158 ? 1.63758 2.14604 0.92373 -0.25722 -0.15819 -0.28393 170 TRP B CB  
5459 C CG  . TRP D 158 ? 1.59227 2.18915 0.90521 -0.22972 -0.18491 -0.24069 170 TRP B CG  
5460 C CD1 . TRP D 158 ? 1.60064 2.14958 0.94717 -0.19741 -0.18887 -0.19146 170 TRP B CD1 
5461 C CD2 . TRP D 158 ? 1.54622 2.27371 0.87516 -0.22166 -0.20374 -0.23615 170 TRP B CD2 
5462 N NE1 . TRP D 158 ? 1.67292 2.32852 1.03405 -0.17542 -0.21320 -0.16428 170 TRP B NE1 
5463 C CE2 . TRP D 158 ? 1.53712 2.29172 0.89922 -0.18467 -0.21896 -0.18633 170 TRP B CE2 
5464 C CE3 . TRP D 158 ? 1.61090 2.42614 0.93877 -0.23775 -0.20497 -0.26620 170 TRP B CE3 
5465 C CZ2 . TRP D 158 ? 1.47207 2.33302 0.86449 -0.16142 -0.23294 -0.16633 170 TRP B CZ2 
5466 C CZ3 . TRP D 158 ? 1.54924 2.47969 0.90767 -0.21630 -0.22108 -0.24462 170 TRP B CZ3 
5467 C CH2 . TRP D 158 ? 1.47560 2.42588 0.86528 -0.17741 -0.23388 -0.19521 170 TRP B CH2 
5468 N N   . VAL D 159 ? 1.68425 2.14949 0.87876 -0.24997 -0.12264 -0.34029 171 VAL B N   
5469 C CA  . VAL D 159 ? 1.76462 2.16927 0.92558 -0.27528 -0.09563 -0.39437 171 VAL B CA  
5470 C C   . VAL D 159 ? 1.82875 2.31726 0.97569 -0.32526 -0.09931 -0.45439 171 VAL B C   
5471 O O   . VAL D 159 ? 1.65689 2.25395 0.80816 -0.30845 -0.11554 -0.44256 171 VAL B O   
5472 C CB  . VAL D 159 ? 1.79514 2.19422 0.92987 -0.23271 -0.08718 -0.37344 171 VAL B CB  
5473 C CG1 . VAL D 159 ? 1.91224 2.26001 1.00920 -0.25830 -0.05877 -0.43541 171 VAL B CG1 
5474 C CG2 . VAL D 159 ? 1.55559 1.86698 0.71977 -0.18535 -0.08044 -0.31287 171 VAL B CG2 
5475 N N   . ASN D 160 ? 1.89127 2.31384 1.04121 -0.37933 -0.08002 -0.50669 172 ASN B N   
5476 C CA  . ASN D 160 ? 1.87460 2.35323 1.03443 -0.42726 -0.07632 -0.55790 172 ASN B CA  
5477 C C   . ASN D 160 ? 1.83419 2.45811 1.03374 -0.42654 -0.10655 -0.53495 172 ASN B C   
5478 O O   . ASN D 160 ? 1.74258 2.46781 0.94677 -0.44024 -0.11327 -0.55668 172 ASN B O   
5479 C CB  . ASN D 160 ? 1.96807 2.46001 1.09441 -0.42572 -0.06349 -0.59207 172 ASN B CB  
5480 C CG  . ASN D 160 ? 2.00217 2.35054 1.09102 -0.42314 -0.02910 -0.61825 172 ASN B CG  
5481 O OD1 . ASN D 160 ? 2.07327 2.29994 1.16153 -0.44682 -0.00579 -0.63654 172 ASN B OD1 
5482 N ND2 . ASN D 160 ? 1.94030 2.30026 0.99785 -0.39135 -0.02318 -0.61772 172 ASN B ND2 
5483 N N   . GLY D 161 ? 1.63380 2.26977 0.86220 -0.40856 -0.12328 -0.49095 173 GLY B N   
5484 C CA  . GLY D 161 ? 1.64500 2.40913 0.91407 -0.40292 -0.14795 -0.46752 173 GLY B CA  
5485 C C   . GLY D 161 ? 1.61677 2.47744 0.88986 -0.34113 -0.17123 -0.41302 173 GLY B C   
5486 O O   . GLY D 161 ? 1.73612 2.70979 1.04078 -0.33171 -0.18854 -0.39589 173 GLY B O   
5487 N N   . LYS D 162 ? 1.54110 2.35902 0.78340 -0.29823 -0.16889 -0.38415 174 LYS B N   
5488 C CA  . LYS D 162 ? 1.51118 2.40104 0.75379 -0.23933 -0.18521 -0.32813 174 LYS B CA  
5489 C C   . LYS D 162 ? 1.45418 2.26614 0.69007 -0.19313 -0.18570 -0.27244 174 LYS B C   
5490 O O   . LYS D 162 ? 1.48691 2.20187 0.69585 -0.19738 -0.16921 -0.28278 174 LYS B O   
5491 C CB  . LYS D 162 ? 1.56567 2.49659 0.77603 -0.23364 -0.17901 -0.34575 174 LYS B CB  
5492 N N   . GLU D 163 ? 1.40746 2.26096 0.66844 -0.14894 -0.20182 -0.21473 175 GLU B N   
5493 C CA  . GLU D 163 ? 1.35862 2.14128 0.61782 -0.10565 -0.20128 -0.15941 175 GLU B CA  
5494 C C   . GLU D 163 ? 1.53395 2.29748 0.75964 -0.07335 -0.19134 -0.13542 175 GLU B C   
5495 O O   . GLU D 163 ? 1.66019 2.49438 0.87963 -0.05218 -0.19534 -0.12052 175 GLU B O   
5496 C CB  . GLU D 163 ? 1.38140 2.20561 0.67712 -0.06777 -0.21689 -0.10776 175 GLU B CB  
5497 C CG  . GLU D 163 ? 1.46351 2.20855 0.76287 -0.02702 -0.21455 -0.05256 175 GLU B CG  
5498 C CD  . GLU D 163 ? 1.48597 2.26069 0.82094 0.00920  -0.22589 -0.00766 175 GLU B CD  
5499 O OE1 . GLU D 163 ? 1.32234 2.19009 0.67570 0.01143  -0.23537 -0.01298 175 GLU B OE1 
5500 O OE2 . GLU D 163 ? 1.55119 2.25746 0.89618 0.03574  -0.22348 0.03123  175 GLU B OE2 
5501 N N   . VAL D 164 ? 1.65609 2.32893 0.86059 -0.06964 -0.17682 -0.13103 176 VAL B N   
5502 C CA  . VAL D 164 ? 1.73514 2.38628 0.90870 -0.04335 -0.16306 -0.11130 176 VAL B CA  
5503 C C   . VAL D 164 ? 1.57704 2.18290 0.76212 0.00115  -0.16220 -0.04413 176 VAL B C   
5504 O O   . VAL D 164 ? 1.54621 2.11524 0.75722 0.00725  -0.16886 -0.02229 176 VAL B O   
5505 C CB  . VAL D 164 ? 1.70297 2.28706 0.84670 -0.07062 -0.14059 -0.15954 176 VAL B CB  
5506 C CG1 . VAL D 164 ? 1.65851 2.27853 0.78725 -0.11716 -0.13739 -0.22952 176 VAL B CG1 
5507 C CG2 . VAL D 164 ? 1.60395 2.06435 0.78949 -0.07579 -0.12795 -0.15363 176 VAL B CG2 
5508 N N   . HIS D 165 ? 1.62786 2.23483 0.79428 0.03023  -0.15184 -0.01197 177 HIS B N   
5509 C CA  . HIS D 165 ? 1.58925 2.14570 0.76575 0.06734  -0.14519 0.04958  177 HIS B CA  
5510 C C   . HIS D 165 ? 1.51447 2.03173 0.66421 0.07765  -0.12284 0.06061  177 HIS B C   
5511 O O   . HIS D 165 ? 1.53170 1.99484 0.69399 0.10001  -0.11307 0.10572  177 HIS B O   
5512 C CB  . HIS D 165 ? 1.69383 2.29363 0.88507 0.09962  -0.15338 0.09570  177 HIS B CB  
5513 C CG  . HIS D 165 ? 1.65867 2.30724 0.87981 0.09704  -0.17304 0.08997  177 HIS B CG  
5514 N ND1 . HIS D 165 ? 1.65480 2.38839 0.87581 0.07467  -0.18460 0.04913  177 HIS B ND1 
5515 C CD2 . HIS D 165 ? 1.65238 2.28058 0.90634 0.11347  -0.18129 0.11823  177 HIS B CD2 
5516 C CE1 . HIS D 165 ? 1.60520 2.37425 0.85890 0.07804  -0.19899 0.05436  177 HIS B CE1 
5517 N NE2 . HIS D 165 ? 1.66599 2.37097 0.93887 0.10288  -0.19724 0.09576  177 HIS B NE2 
5518 N N   . SER D 166 ? 1.52182 2.06237 0.63960 0.06075  -0.11207 0.01930  178 SER B N   
5519 C CA  . SER D 166 ? 1.60574 2.10960 0.70750 0.07071  -0.08761 0.02699  178 SER B CA  
5520 C C   . SER D 166 ? 1.56981 1.96624 0.71285 0.06193  -0.07182 0.01731  178 SER B C   
5521 O O   . SER D 166 ? 1.57831 1.93662 0.73345 0.03663  -0.06926 -0.02979 178 SER B O   
5522 C CB  . SER D 166 ? 1.67306 2.23017 0.73244 0.05528  -0.07934 -0.02052 178 SER B CB  
5523 O OG  . SER D 166 ? 1.69203 2.22932 0.75425 0.01904  -0.07908 -0.08615 178 SER B OG  
5524 N N   . GLY D 167 ? 1.66983 2.01909 0.83301 0.08240  -0.05989 0.06213  179 GLY B N   
5525 C CA  . GLY D 167 ? 1.49734 1.76052 0.70062 0.07832  -0.04655 0.05745  179 GLY B CA  
5526 C C   . GLY D 167 ? 1.44333 1.66097 0.68693 0.07064  -0.06053 0.05944  179 GLY B C   
5527 O O   . GLY D 167 ? 1.44488 1.59987 0.71582 0.06206  -0.05250 0.04035  179 GLY B O   
5528 N N   . VAL D 168 ? 1.47136 1.72192 0.71783 0.07689  -0.08027 0.08379  180 VAL B N   
5529 C CA  . VAL D 168 ? 1.28760 1.50600 0.57010 0.07073  -0.09410 0.08651  180 VAL B CA  
5530 C C   . VAL D 168 ? 1.29374 1.48305 0.59825 0.09325  -0.09406 0.13865  180 VAL B C   
5531 O O   . VAL D 168 ? 1.50043 1.72610 0.78559 0.11387  -0.09770 0.17490  180 VAL B O   
5532 C CB  . VAL D 168 ? 1.22197 1.50619 0.49367 0.05951  -0.11583 0.06863  180 VAL B CB  
5533 C CG1 . VAL D 168 ? 1.18078 1.43841 0.49000 0.05692  -0.12876 0.07805  180 VAL B CG1 
5534 C CG2 . VAL D 168 ? 1.32574 1.63013 0.57734 0.02807  -0.11315 0.00952  180 VAL B CG2 
5535 N N   . CYS D 169 ? 1.24712 1.37006 0.58945 0.08996  -0.08847 0.14231  181 CYS B N   
5536 C CA  . CYS D 169 ? 1.30417 1.39407 0.67016 0.10461  -0.08806 0.18290  181 CYS B CA  
5537 C C   . CYS D 169 ? 1.29367 1.35000 0.69511 0.09710  -0.09957 0.17507  181 CYS B C   
5538 O O   . CYS D 169 ? 1.43257 1.46075 0.85026 0.08158  -0.09780 0.14562  181 CYS B O   
5539 C CB  . CYS D 169 ? 1.33293 1.38416 0.71121 0.10756  -0.06714 0.19925  181 CYS B CB  
5540 S SG  . CYS D 169 ? 1.87157 1.88442 1.27039 0.11958  -0.06291 0.24656  181 CYS B SG  
5541 N N   . THR D 170 ? 1.16830 1.22538 0.57890 0.11072  -0.10918 0.20315  182 THR B N   
5542 C CA  . THR D 170 ? 1.12246 1.15146 0.56563 0.10694  -0.11892 0.20071  182 THR B CA  
5543 C C   . THR D 170 ? 1.20898 1.19449 0.67013 0.12002  -0.11141 0.23353  182 THR B C   
5544 O O   . THR D 170 ? 1.40130 1.38649 0.84469 0.13557  -0.10273 0.26404  182 THR B O   
5545 C CB  . THR D 170 ? 1.04243 1.12198 0.48042 0.10980  -0.13818 0.19607  182 THR B CB  
5546 O OG1 . THR D 170 ? 1.06399 1.19616 0.47807 0.09488  -0.14334 0.16582  182 THR B OG1 
5547 C CG2 . THR D 170 ? 1.05160 1.10741 0.52221 0.09899  -0.14648 0.18349  182 THR B CG2 
5548 N N   . ASP D 171 ? 1.24422 1.19135 0.73817 0.11220  -0.11277 0.22651  183 ASP B N   
5549 C CA  . ASP D 171 ? 1.25556 1.16167 0.76798 0.11858  -0.10519 0.24944  183 ASP B CA  
5550 C C   . ASP D 171 ? 1.34980 1.26101 0.85047 0.13999  -0.11039 0.27618  183 ASP B C   
5551 O O   . ASP D 171 ? 1.37400 1.31532 0.87521 0.14681  -0.12605 0.27002  183 ASP B O   
5552 C CB  . ASP D 171 ? 1.30303 1.18093 0.85006 0.10730  -0.10893 0.23372  183 ASP B CB  
5553 C CG  . ASP D 171 ? 1.39834 1.26845 0.95642 0.09434  -0.10167 0.21270  183 ASP B CG  
5554 O OD1 . ASP D 171 ? 1.43208 1.30596 0.98037 0.09350  -0.08844 0.21526  183 ASP B OD1 
5555 O OD2 . ASP D 171 ? 1.39795 1.25878 0.97313 0.08759  -0.10757 0.19549  183 ASP B OD2 
5556 N N   . PRO D 172 ? 1.25061 1.13332 0.73952 0.15191  -0.09559 0.30667  184 PRO B N   
5557 C CA  . PRO D 172 ? 1.18530 1.06205 0.65985 0.17925  -0.09689 0.33554  184 PRO B CA  
5558 C C   . PRO D 172 ? 1.23310 1.08573 0.73405 0.18261  -0.10463 0.32922  184 PRO B C   
5559 O O   . PRO D 172 ? 1.36055 1.23321 0.85902 0.20394  -0.11332 0.33794  184 PRO B O   
5560 C CB  . PRO D 172 ? 1.27978 1.10962 0.73753 0.18451  -0.07229 0.36759  184 PRO B CB  
5561 C CG  . PRO D 172 ? 1.23755 1.07991 0.69229 0.16329  -0.06230 0.35648  184 PRO B CG  
5562 C CD  . PRO D 172 ? 1.14406 1.00029 0.62928 0.14188  -0.07439 0.31746  184 PRO B CD  
5563 N N   . GLN D 173 ? 1.34321 1.16186 0.87454 0.16082  -0.10137 0.31067  185 GLN B N   
5564 C CA  . GLN D 173 ? 1.35414 1.15318 0.90971 0.16153  -0.10786 0.30145  185 GLN B CA  
5565 C C   . GLN D 173 ? 1.21588 1.02811 0.79819 0.13872  -0.11768 0.27069  185 GLN B C   
5566 O O   . GLN D 173 ? 1.37884 1.18707 0.96839 0.12141  -0.11136 0.25996  185 GLN B O   
5567 C CB  . GLN D 173 ? 1.49579 1.23121 1.05816 0.15992  -0.08961 0.31378  185 GLN B CB  
5568 C CG  . GLN D 173 ? 1.58065 1.28393 1.11326 0.18545  -0.07452 0.34862  185 GLN B CG  
5569 C CD  . GLN D 173 ? 1.89928 1.52771 1.43610 0.17496  -0.05058 0.35690  185 GLN B CD  
5570 O OE1 . GLN D 173 ? 1.97122 1.58464 1.53419 0.14487  -0.04619 0.33496  185 GLN B OE1 
5571 N NE2 . GLN D 173 ? 2.02317 1.60511 1.53286 0.19976  -0.03354 0.38841  185 GLN B NE2 
5572 N N   . PRO D 174 ? 1.13596 0.96525 0.73197 0.14067  -0.13135 0.25821  186 PRO B N   
5573 C CA  . PRO D 174 ? 0.99598 0.83256 0.61294 0.12144  -0.13818 0.23391  186 PRO B CA  
5574 C C   . PRO D 174 ? 1.06487 0.86827 0.70460 0.11120  -0.13103 0.22862  186 PRO B C   
5575 O O   . PRO D 174 ? 1.18547 0.95845 0.82765 0.11443  -0.12142 0.23846  186 PRO B O   
5576 C CB  . PRO D 174 ? 1.14561 1.01357 0.76741 0.12699  -0.15238 0.22675  186 PRO B CB  
5577 C CG  . PRO D 174 ? 1.16973 1.03274 0.78435 0.15207  -0.15118 0.24629  186 PRO B CG  
5578 C CD  . PRO D 174 ? 1.13799 0.98555 0.72909 0.16324  -0.13983 0.26778  186 PRO B CD  
5579 N N   A LEU D 175 ? 0.99077 0.80085 0.64544 0.09824  -0.13431 0.21220  187 LEU B N   
5580 N N   B LEU D 175 ? 0.99600 0.80636 0.65099 0.09845  -0.13475 0.21205  187 LEU B N   
5581 C CA  A LEU D 175 ? 0.95634 0.75382 0.63337 0.08965  -0.13090 0.20488  187 LEU B CA  
5582 C CA  B LEU D 175 ? 0.95566 0.75325 0.63272 0.08953  -0.13084 0.20479  187 LEU B CA  
5583 C C   A LEU D 175 ? 1.00649 0.81072 0.69580 0.09136  -0.14076 0.19713  187 LEU B C   
5584 C C   B LEU D 175 ? 1.00677 0.81160 0.69706 0.09037  -0.14064 0.19625  187 LEU B C   
5585 O O   A LEU D 175 ? 1.04229 0.86417 0.72708 0.09329  -0.14950 0.19333  187 LEU B O   
5586 O O   B LEU D 175 ? 1.04091 0.86248 0.72769 0.09073  -0.14891 0.19125  187 LEU B O   
5587 C CB  A LEU D 175 ? 0.90929 0.71503 0.59353 0.08185  -0.12704 0.19604  187 LEU B CB  
5588 C CB  B LEU D 175 ? 0.90953 0.71490 0.59227 0.08188  -0.12610 0.19684  187 LEU B CB  
5589 C CG  A LEU D 175 ? 0.91638 0.72126 0.59681 0.07810  -0.11416 0.20058  187 LEU B CG  
5590 C CG  B LEU D 175 ? 0.88655 0.69810 0.59254 0.07640  -0.12450 0.18913  187 LEU B CG  
5591 C CD1 A LEU D 175 ? 0.83494 0.65278 0.52434 0.07755  -0.11076 0.19083  187 LEU B CD1 
5592 C CD1 B LEU D 175 ? 0.96235 0.78319 0.67412 0.07222  -0.11300 0.18915  187 LEU B CD1 
5593 C CD2 A LEU D 175 ? 0.85830 0.65025 0.54962 0.07010  -0.10435 0.20658  187 LEU B CD2 
5594 C CD2 B LEU D 175 ? 0.88137 0.70116 0.59119 0.07990  -0.13193 0.18196  187 LEU B CD2 
5595 N N   . LYS D 176 ? 0.98304 0.77701 0.68753 0.08772  -0.13808 0.19274  188 LYS B N   
5596 C CA  . LYS D 176 ? 1.03401 0.83844 0.74951 0.08916  -0.14599 0.18399  188 LYS B CA  
5597 C C   . LYS D 176 ? 0.97869 0.80141 0.70637 0.08222  -0.14902 0.17600  188 LYS B C   
5598 O O   . LYS D 176 ? 1.00612 0.83362 0.74458 0.07581  -0.14392 0.17244  188 LYS B O   
5599 C CB  . LYS D 176 ? 1.15659 0.94120 0.87841 0.08918  -0.14044 0.17978  188 LYS B CB  
5600 C CG  . LYS D 176 ? 1.13043 0.89343 0.83798 0.10574  -0.13713 0.19010  188 LYS B CG  
5601 C CD  . LYS D 176 ? 1.08750 0.82191 0.79962 0.10670  -0.12917 0.18128  188 LYS B CD  
5602 C CE  . LYS D 176 ? 1.40967 1.11920 1.10560 0.13187  -0.12399 0.19400  188 LYS B CE  
5603 N NZ  . LYS D 176 ? 1.47866 1.14956 1.17595 0.13432  -0.11268 0.18223  188 LYS B NZ  
5604 N N   . GLU D 177 ? 0.98663 0.82249 0.71200 0.08418  -0.15589 0.17463  189 GLU B N   
5605 C CA  . GLU D 177 ? 0.93935 0.78646 0.67125 0.08312  -0.15650 0.17263  189 GLU B CA  
5606 C C   . GLU D 177 ? 0.86157 0.72730 0.60687 0.08343  -0.15990 0.16670  189 GLU B C   
5607 O O   . GLU D 177 ? 1.03826 0.92180 0.79023 0.08596  -0.15982 0.16705  189 GLU B O   
5608 C CB  . GLU D 177 ? 0.85049 0.69676 0.57198 0.08152  -0.15832 0.17442  189 GLU B CB  
5609 C CG  . GLU D 177 ? 0.91437 0.74698 0.62096 0.07691  -0.15433 0.17393  189 GLU B CG  
5610 C CD  . GLU D 177 ? 1.07434 0.90369 0.77073 0.06732  -0.15335 0.17063  189 GLU B CD  
5611 O OE1 . GLU D 177 ? 1.08594 0.92652 0.78701 0.06488  -0.15634 0.17185  189 GLU B OE1 
5612 O OE2 . GLU D 177 ? 1.16632 0.98213 0.84899 0.05964  -0.14786 0.16508  189 GLU B OE2 
5613 N N   . GLN D 178 ? 0.82052 0.68532 0.56804 0.08343  -0.16219 0.16083  190 GLN B N   
5614 C CA  . GLN D 178 ? 0.89007 0.77213 0.64798 0.08106  -0.16404 0.14921  190 GLN B CA  
5615 C C   . GLN D 178 ? 0.94478 0.80313 0.70517 0.07533  -0.15695 0.14050  190 GLN B C   
5616 O O   . GLN D 178 ? 0.91680 0.75885 0.67208 0.08147  -0.15547 0.13679  190 GLN B O   
5617 C CB  . GLN D 178 ? 0.95159 0.85036 0.70653 0.08682  -0.16984 0.14732  190 GLN B CB  
5618 C CG  . GLN D 178 ? 0.93181 0.84537 0.68142 0.08878  -0.17241 0.15774  190 GLN B CG  
5619 C CD  . GLN D 178 ? 0.97370 0.87863 0.71378 0.08770  -0.17260 0.16435  190 GLN B CD  
5620 O OE1 . GLN D 178 ? 0.99399 0.89836 0.73289 0.09094  -0.17420 0.16165  190 GLN B OE1 
5621 N NE2 . GLN D 178 ? 0.97334 0.87291 0.70574 0.08342  -0.16959 0.17247  190 GLN B NE2 
5622 N N   . PRO D 179 ? 0.94475 0.79895 0.71228 0.06388  -0.14991 0.13739  191 PRO B N   
5623 C CA  . PRO D 179 ? 0.92717 0.74521 0.69308 0.05448  -0.13783 0.13232  191 PRO B CA  
5624 C C   . PRO D 179 ? 0.83950 0.64678 0.60816 0.04843  -0.13407 0.11305  191 PRO B C   
5625 O O   . PRO D 179 ? 1.08667 0.84656 0.84742 0.04594  -0.12112 0.11111  191 PRO B O   
5626 C CB  . PRO D 179 ? 1.04694 0.87881 0.82439 0.03788  -0.13077 0.12970  191 PRO B CB  
5627 C CG  . PRO D 179 ? 0.94331 0.80623 0.72217 0.04827  -0.13849 0.14030  191 PRO B CG  
5628 C CD  . PRO D 179 ? 0.84295 0.72426 0.61923 0.06034  -0.15004 0.14020  191 PRO B CD  
5629 N N   . ALA D 180 ? 0.87417 0.72054 0.65065 0.04720  -0.14286 0.09904  192 ALA B N   
5630 C CA  . ALA D 180 ? 1.00670 0.84762 0.78378 0.04085  -0.13901 0.07564  192 ALA B CA  
5631 C C   . ALA D 180 ? 1.03779 0.86222 0.80286 0.06232  -0.14089 0.07885  192 ALA B C   
5632 O O   . ALA D 180 ? 1.10740 0.92121 0.86986 0.06169  -0.13556 0.05868  192 ALA B O   
5633 C CB  . ALA D 180 ? 0.91980 0.82288 0.70895 0.03025  -0.14781 0.05765  192 ALA B CB  
5634 N N   . LEU D 181 ? 1.01761 0.84437 0.77573 0.08021  -0.14735 0.10086  193 LEU B N   
5635 C CA  . LEU D 181 ? 1.00742 0.83555 0.75766 0.10079  -0.15005 0.10492  193 LEU B CA  
5636 C C   . LEU D 181 ? 1.21194 1.00207 0.95051 0.11751  -0.14344 0.12157  193 LEU B C   
5637 O O   . LEU D 181 ? 1.28597 1.06414 1.02078 0.11444  -0.14234 0.13669  193 LEU B O   
5638 C CB  . LEU D 181 ? 0.98180 0.85618 0.73377 0.10514  -0.16237 0.11520  193 LEU B CB  
5639 C CG  . LEU D 181 ? 1.01723 0.93417 0.77356 0.10151  -0.16813 0.10410  193 LEU B CG  
5640 C CD1 . LEU D 181 ? 0.88486 0.81789 0.64872 0.08610  -0.16860 0.09189  193 LEU B CD1 
5641 C CD2 . LEU D 181 ? 0.80949 0.75712 0.56352 0.10391  -0.17507 0.11998  193 LEU B CD2 
5642 N N   . ASN D 182 ? 1.16820 0.94369 0.89939 0.13862  -0.13842 0.11956  194 ASN B N   
5643 C CA  . ASN D 182 ? 1.33894 1.08948 1.05693 0.16296  -0.13313 0.13962  194 ASN B CA  
5644 C C   . ASN D 182 ? 1.13295 0.93622 0.85142 0.17456  -0.14696 0.15462  194 ASN B C   
5645 O O   . ASN D 182 ? 1.18057 0.98326 0.88962 0.18496  -0.14781 0.17305  194 ASN B O   
5646 C CB  . ASN D 182 ? 1.42013 1.13256 1.12846 0.18735  -0.11971 0.13337  194 ASN B CB  
5647 C CG  . ASN D 182 ? 1.61714 1.36812 1.33254 0.19571  -0.12491 0.11540  194 ASN B CG  
5648 O OD1 . ASN D 182 ? 1.70362 1.51575 1.42685 0.19808  -0.13875 0.11978  194 ASN B OD1 
5649 N ND2 . ASN D 182 ? 1.50704 1.22087 1.21826 0.19774  -0.11150 0.09331  194 ASN B ND2 
5650 N N   . ASP D 183 ? 1.02890 0.88107 0.75697 0.17036  -0.15670 0.14614  195 ASP B N   
5651 C CA  . ASP D 183 ? 1.19166 1.09528 0.92175 0.17184  -0.16745 0.15591  195 ASP B CA  
5652 C C   . ASP D 183 ? 1.26932 1.18108 1.00207 0.14604  -0.17298 0.15837  195 ASP B C   
5653 O O   . ASP D 183 ? 1.19198 1.13975 0.92842 0.13515  -0.17894 0.15829  195 ASP B O   
5654 C CB  . ASP D 183 ? 1.03898 0.98921 0.77666 0.17848  -0.17115 0.14719  195 ASP B CB  
5655 C CG  . ASP D 183 ? 1.18550 1.13896 0.92917 0.16262  -0.17067 0.13213  195 ASP B CG  
5656 O OD1 . ASP D 183 ? 1.31490 1.28242 1.06144 0.14213  -0.17538 0.13462  195 ASP B OD1 
5657 O OD2 . ASP D 183 ? 1.43248 1.37435 1.17570 0.17238  -0.16446 0.11765  195 ASP B OD2 
5658 N N   . SER D 184 ? 1.13437 1.01010 0.86434 0.13641  -0.16836 0.16058  196 SER B N   
5659 C CA  . SER D 184 ? 0.84240 0.72096 0.57420 0.11758  -0.17084 0.16231  196 SER B CA  
5660 C C   . SER D 184 ? 0.87923 0.77339 0.60294 0.11496  -0.17480 0.17104  196 SER B C   
5661 O O   . SER D 184 ? 1.04958 0.94789 0.76477 0.12717  -0.17531 0.17865  196 SER B O   
5662 C CB  . SER D 184 ? 0.89099 0.73677 0.62384 0.10954  -0.16365 0.16137  196 SER B CB  
5663 O OG  . SER D 184 ? 0.89528 0.74521 0.62822 0.09836  -0.16459 0.16525  196 SER B OG  
5664 N N   . ARG D 185 ? 0.87859 0.78169 0.60279 0.09958  -0.17636 0.16948  197 ARG B N   
5665 C CA  . ARG D 185 ? 0.86524 0.77661 0.58000 0.09031  -0.17739 0.17135  197 ARG B CA  
5666 C C   . ARG D 185 ? 0.90268 0.78797 0.60916 0.09013  -0.17279 0.17534  197 ARG B C   
5667 O O   . ARG D 185 ? 0.96545 0.82805 0.67665 0.08970  -0.16779 0.17594  197 ARG B O   
5668 C CB  . ARG D 185 ? 0.82815 0.74247 0.54249 0.07318  -0.17529 0.16777  197 ARG B CB  
5669 C CG  . ARG D 185 ? 0.88488 0.82875 0.60604 0.07024  -0.17748 0.16564  197 ARG B CG  
5670 C CD  . ARG D 185 ? 0.92240 0.85675 0.63940 0.05357  -0.17084 0.16698  197 ARG B CD  
5671 N NE  . ARG D 185 ? 1.01347 0.93851 0.71971 0.03443  -0.16578 0.16231  197 ARG B NE  
5672 C CZ  . ARG D 185 ? 1.11372 1.02060 0.81186 0.01582  -0.15559 0.16235  197 ARG B CZ  
5673 N NH1 . ARG D 185 ? 0.91001 0.80977 0.60849 0.01704  -0.15001 0.17177  197 ARG B NH1 
5674 N NH2 . ARG D 185 ? 1.26417 1.15782 0.95089 -0.00501 -0.14906 0.15250  197 ARG B NH2 
5675 N N   . TYR D 186 ? 0.86657 0.76424 0.56074 0.08980  -0.17437 0.17707  198 TYR B N   
5676 C CA  . TYR D 186 ? 0.93399 0.81433 0.61679 0.09253  -0.16943 0.18254  198 TYR B CA  
5677 C C   . TYR D 186 ? 0.97164 0.84761 0.64482 0.07731  -0.16584 0.17417  198 TYR B C   
5678 O O   . TYR D 186 ? 1.10803 0.99208 0.78009 0.06331  -0.16661 0.16430  198 TYR B O   
5679 C CB  . TYR D 186 ? 0.98223 0.88181 0.65257 0.10857  -0.17241 0.19279  198 TYR B CB  
5680 C CG  . TYR D 186 ? 1.04563 0.93343 0.72058 0.12891  -0.17074 0.20270  198 TYR B CG  
5681 C CD1 . TYR D 186 ? 1.04271 0.88851 0.71455 0.13555  -0.16016 0.21205  198 TYR B CD1 
5682 C CD2 . TYR D 186 ? 0.97493 0.89138 0.65667 0.14027  -0.17701 0.20112  198 TYR B CD2 
5683 C CE1 . TYR D 186 ? 1.11239 0.93411 0.78502 0.15234  -0.15438 0.21837  198 TYR B CE1 
5684 C CE2 . TYR D 186 ? 1.04969 0.94813 0.73301 0.16213  -0.17255 0.20804  198 TYR B CE2 
5685 C CZ  . TYR D 186 ? 1.06136 0.90686 0.73876 0.16778  -0.16049 0.21604  198 TYR B CZ  
5686 O OH  . TYR D 186 ? 1.36416 1.17892 1.03984 0.18769  -0.15199 0.22031  198 TYR B OH  
5687 N N   . ALA D 187 ? 0.95570 0.81507 0.62050 0.07930  -0.15909 0.17753  199 ALA B N   
5688 C CA  . ALA D 187 ? 0.96577 0.81731 0.61812 0.06907  -0.15290 0.16803  199 ALA B CA  
5689 C C   . ALA D 187 ? 1.06218 0.92226 0.69733 0.07461  -0.14995 0.17321  199 ALA B C   
5690 O O   . ALA D 187 ? 1.16234 1.01781 0.79796 0.08629  -0.14776 0.18804  199 ALA B O   
5691 C CB  . ALA D 187 ? 0.97440 0.79817 0.63573 0.06885  -0.14404 0.16640  199 ALA B CB  
5692 N N   . LEU D 188 ? 1.06025 0.93034 0.67756 0.06479  -0.14778 0.16029  200 LEU B N   
5693 C CA  . LEU D 188 ? 0.89348 0.78167 0.48969 0.06981  -0.14547 0.16394  200 LEU B CA  
5694 C C   . LEU D 188 ? 0.99709 0.87483 0.57817 0.05833  -0.13576 0.14501  200 LEU B C   
5695 O O   . LEU D 188 ? 1.22662 1.09464 0.80520 0.04268  -0.13397 0.12522  200 LEU B O   
5696 C CB  . LEU D 188 ? 0.92837 0.86548 0.51186 0.07354  -0.15713 0.16612  200 LEU B CB  
5697 C CG  . LEU D 188 ? 1.06148 1.02833 0.61900 0.08414  -0.15641 0.17537  200 LEU B CG  
5698 C CD1 . LEU D 188 ? 1.14551 1.08571 0.70256 0.10339  -0.14795 0.20320  200 LEU B CD1 
5699 C CD2 . LEU D 188 ? 1.04246 1.07297 0.58882 0.08990  -0.17011 0.17578  200 LEU B CD2 
5700 N N   . SER D 189 ? 0.96564 0.84193 0.53500 0.06565  -0.12684 0.15077  201 SER B N   
5701 C CA  . SER D 189 ? 1.12617 0.99331 0.67911 0.05937  -0.11511 0.13232  201 SER B CA  
5702 C C   . SER D 189 ? 1.18216 1.08678 0.70630 0.06066  -0.11507 0.13119  201 SER B C   
5703 O O   . SER D 189 ? 1.09737 1.02990 0.61499 0.07153  -0.12185 0.15193  201 SER B O   
5704 C CB  . SER D 189 ? 1.16902 1.00864 0.73538 0.06883  -0.10168 0.13830  201 SER B CB  
5705 O OG  . SER D 189 ? 1.29185 1.14395 0.86031 0.07790  -0.09807 0.15920  201 SER B OG  
5706 N N   . SER D 190 ? 1.30954 1.21311 0.81340 0.05169  -0.10568 0.10703  202 SER B N   
5707 C CA  . SER D 190 ? 1.21297 1.15823 0.68548 0.05181  -0.10463 0.10154  202 SER B CA  
5708 C C   . SER D 190 ? 1.33361 1.25936 0.79008 0.04790  -0.08708 0.07749  202 SER B C   
5709 O O   . SER D 190 ? 1.32552 1.20591 0.79099 0.04297  -0.07723 0.06007  202 SER B O   
5710 C CB  . SER D 190 ? 1.19024 1.18506 0.64674 0.03807  -0.11911 0.08571  202 SER B CB  
5711 O OG  . SER D 190 ? 1.23092 1.27786 0.65488 0.04082  -0.11975 0.08211  202 SER B OG  
5712 N N   . ARG D 191 ? 1.25090 1.21095 0.68093 0.05337  -0.08154 0.07829  203 ARG B N   
5713 C CA  . ARG D 191 ? 1.32092 1.26947 0.73332 0.05403  -0.06292 0.05665  203 ARG B CA  
5714 C C   . ARG D 191 ? 1.29286 1.29096 0.66516 0.04399  -0.06395 0.03327  203 ARG B C   
5715 O O   . ARG D 191 ? 1.25143 1.30474 0.60909 0.04590  -0.07777 0.04780  203 ARG B O   
5716 C CB  . ARG D 191 ? 1.26631 1.21242 0.68853 0.07243  -0.04985 0.08259  203 ARG B CB  
5717 C CG  . ARG D 191 ? 1.32394 1.23906 0.78565 0.08014  -0.05100 0.10653  203 ARG B CG  
5718 C CD  . ARG D 191 ? 1.33586 1.26897 0.80430 0.08866  -0.04728 0.14115  203 ARG B CD  
5719 N NE  . ARG D 191 ? 1.36966 1.27872 0.87493 0.09059  -0.04871 0.15873  203 ARG B NE  
5720 C CZ  . ARG D 191 ? 1.31476 1.21481 0.83345 0.08903  -0.06158 0.17528  203 ARG B CZ  
5721 N NH1 . ARG D 191 ? 1.40780 1.32326 0.90883 0.08913  -0.07465 0.17998  203 ARG B NH1 
5722 N NH2 . ARG D 191 ? 1.38163 1.26287 0.93201 0.08852  -0.06101 0.18579  203 ARG B NH2 
5723 N N   . LEU D 192 ? 1.28769 1.26750 0.64040 0.03562  -0.04824 -0.00359 204 LEU B N   
5724 C CA  . LEU D 192 ? 1.29608 1.32373 0.60770 0.02365  -0.04626 -0.03380 204 LEU B CA  
5725 C C   . LEU D 192 ? 1.48223 1.48853 0.77663 0.03268  -0.02171 -0.05355 204 LEU B C   
5726 O O   . LEU D 192 ? 1.50575 1.45016 0.80547 0.03057  -0.00566 -0.07905 204 LEU B O   
5727 C CB  . LEU D 192 ? 1.33532 1.36560 0.63547 -0.00820 -0.05310 -0.07589 204 LEU B CB  
5728 C CG  . LEU D 192 ? 1.41581 1.48995 0.67250 -0.02771 -0.04770 -0.12096 204 LEU B CG  
5729 C CD1 . LEU D 192 ? 1.33988 1.50971 0.57184 -0.01599 -0.06149 -0.10026 204 LEU B CD1 
5730 C CD2 . LEU D 192 ? 1.53037 1.60171 0.78066 -0.06719 -0.05183 -0.16624 204 LEU B CD2 
5731 N N   . ARG D 193 ? 1.50977 1.56672 0.78171 0.04532  -0.01685 -0.04014 205 ARG B N   
5732 C CA  . ARG D 193 ? 1.49658 1.54796 0.75032 0.05603  0.00719  -0.05774 205 ARG B CA  
5733 C C   . ARG D 193 ? 1.53867 1.63054 0.74490 0.03987  0.01114  -0.10256 205 ARG B C   
5734 O O   . ARG D 193 ? 1.47830 1.64274 0.65910 0.03428  -0.00336 -0.09603 205 ARG B O   
5735 C CB  . ARG D 193 ? 1.47911 1.56274 0.73765 0.07751  0.01430  -0.01505 205 ARG B CB  
5736 C CG  . ARG D 193 ? 1.50346 1.60779 0.73552 0.08749  0.03801  -0.03308 205 ARG B CG  
5737 C CD  . ARG D 193 ? 1.56858 1.71398 0.80151 0.10243  0.04604  0.01076  205 ARG B CD  
5738 N NE  . ARG D 193 ? 1.67146 1.78329 0.95054 0.11251  0.05238  0.04019  205 ARG B NE  
5739 C CZ  . ARG D 193 ? 1.62058 1.75620 0.91037 0.11970  0.06290  0.07722  205 ARG B CZ  
5740 N NH1 . ARG D 193 ? 1.33007 1.51650 0.58614 0.12126  0.06985  0.09540  205 ARG B NH1 
5741 N NH2 . ARG D 193 ? 1.69200 1.80268 1.02612 0.12365  0.06774  0.09630  205 ARG B NH2 
5742 N N   . VAL D 194 ? 1.56948 1.61532 0.76187 0.03417  0.03184  -0.14841 206 VAL B N   
5743 C CA  . VAL D 194 ? 1.55402 1.62999 0.69925 0.01716  0.04109  -0.19967 206 VAL B CA  
5744 C C   . VAL D 194 ? 1.59172 1.63715 0.72376 0.03728  0.07189  -0.21945 206 VAL B C   
5745 O O   . VAL D 194 ? 1.67414 1.67109 0.83642 0.06192  0.08524  -0.19833 206 VAL B O   
5746 C CB  . VAL D 194 ? 1.56032 1.60290 0.69492 -0.01937 0.03846  -0.25063 206 VAL B CB  
5747 C CG1 . VAL D 194 ? 1.54621 1.63871 0.69332 -0.03879 0.00788  -0.23358 206 VAL B CG1 
5748 C CG2 . VAL D 194 ? 1.57520 1.50665 0.73273 -0.01624 0.05754  -0.26332 206 VAL B CG2 
5749 N N   . SER D 195 ? 1.62715 1.70984 0.71311 0.02781  0.08318  -0.26187 207 SER B N   
5750 C CA  . SER D 195 ? 1.67864 1.73394 0.74779 0.04770  0.11480  -0.28772 207 SER B CA  
5751 C C   . SER D 195 ? 1.72563 1.67247 0.80114 0.04563  0.13598  -0.32670 207 SER B C   
5752 O O   . SER D 195 ? 1.79456 1.69600 0.87190 0.01712  0.12868  -0.34958 207 SER B O   
5753 C CB  . SER D 195 ? 1.79520 1.92057 0.80911 0.03738  0.12231  -0.32678 207 SER B CB  
5754 O OG  . SER D 195 ? 1.88642 1.98991 0.86912 0.00228  0.12525  -0.39164 207 SER B OG  
5755 N N   . ALA D 196 ? 1.81572 1.72166 0.89443 0.07826  0.16454  -0.33157 208 ALA B N   
5756 C CA  . ALA D 196 ? 1.95399 1.75032 1.03356 0.08646  0.19011  -0.36421 208 ALA B CA  
5757 C C   . ALA D 196 ? 2.03620 1.79447 1.06866 0.05033  0.20299  -0.43452 208 ALA B C   
5758 O O   . ALA D 196 ? 2.05319 1.71857 1.08614 0.03371  0.21275  -0.45893 208 ALA B O   
5759 C CB  . ALA D 196 ? 2.05769 1.83544 1.14365 0.13376  0.21984  -0.35898 208 ALA B CB  
5760 N N   . THR D 197 ? 2.01336 1.84334 1.00288 0.03539  0.20474  -0.46876 209 THR B N   
5761 C CA  . THR D 197 ? 2.09252 1.89945 1.03516 -0.00550 0.21627  -0.54221 209 THR B CA  
5762 C C   . THR D 197 ? 2.13595 1.95643 1.08446 -0.05491 0.18898  -0.55032 209 THR B C   
5763 O O   . THR D 197 ? 2.24618 2.00371 1.17365 -0.09314 0.20197  -0.60574 209 THR B O   
5764 C CB  . THR D 197 ? 2.08103 1.98197 0.97606 -0.00982 0.22072  -0.57442 209 THR B CB  
5765 O OG1 . THR D 197 ? 2.00841 2.03156 0.90722 -0.01755 0.18583  -0.53376 209 THR B OG1 
5766 C CG2 . THR D 197 ? 2.10144 1.99700 0.99208 0.03920  0.24959  -0.56666 209 THR B CG2 
5767 N N   . PHE D 198 ? 2.07168 1.97267 1.04810 -0.05543 0.15356  -0.49692 210 PHE B N   
5768 C CA  . PHE D 198 ? 1.94708 1.87082 0.93448 -0.09659 0.12694  -0.49967 210 PHE B CA  
5769 C C   . PHE D 198 ? 2.01638 1.82507 1.03484 -0.10425 0.13561  -0.49594 210 PHE B C   
5770 O O   . PHE D 198 ? 2.14209 1.91386 1.15019 -0.14887 0.13866  -0.53835 210 PHE B O   
5771 C CB  . PHE D 198 ? 1.82059 1.84766 0.83101 -0.08456 0.09087  -0.43774 210 PHE B CB  
5772 C CG  . PHE D 198 ? 2.01986 2.12346 1.02531 -0.12409 0.06159  -0.44952 210 PHE B CG  
5773 C CD1 . PHE D 198 ? 2.16213 2.22282 1.16627 -0.16986 0.06404  -0.49654 210 PHE B CD1 
5774 C CD2 . PHE D 198 ? 2.01117 2.23232 1.01297 -0.11411 0.03335  -0.41165 210 PHE B CD2 
5775 C CE1 . PHE D 198 ? 2.08579 2.23210 1.08917 -0.20654 0.03692  -0.50823 210 PHE B CE1 
5776 C CE2 . PHE D 198 ? 2.00007 2.30371 0.99867 -0.14385 0.00600  -0.42025 210 PHE B CE2 
5777 C CZ  . PHE D 198 ? 1.99139 2.26407 0.99283 -0.19097 0.00676  -0.46998 210 PHE B CZ  
5778 N N   . TRP D 199 ? 1.89360 1.64850 0.94929 -0.06254 0.14093  -0.44576 211 TRP B N   
5779 C CA  . TRP D 199 ? 1.95277 1.60390 1.03629 -0.06342 0.14907  -0.43489 211 TRP B CA  
5780 C C   . TRP D 199 ? 2.10897 1.64271 1.16273 -0.07431 0.18797  -0.49031 211 TRP B C   
5781 O O   . TRP D 199 ? 2.17565 1.62881 1.23437 -0.09992 0.19590  -0.50284 211 TRP B O   
5782 C CB  . TRP D 199 ? 2.01440 1.64746 1.14097 -0.01359 0.14675  -0.37181 211 TRP B CB  
5783 C CG  . TRP D 199 ? 2.01725 1.54197 1.16582 -0.00365 0.16087  -0.36044 211 TRP B CG  
5784 C CD1 . TRP D 199 ? 2.07262 1.51157 1.22213 0.03488  0.19130  -0.35890 211 TRP B CD1 
5785 C CD2 . TRP D 199 ? 2.02325 1.51760 1.19355 -0.02963 0.14652  -0.34704 211 TRP B CD2 
5786 N NE1 . TRP D 199 ? 2.20370 1.55869 1.37189 0.03578  0.19658  -0.34249 211 TRP B NE1 
5787 C CE2 . TRP D 199 ? 2.10837 1.49493 1.28956 -0.00569 0.16982  -0.33579 211 TRP B CE2 
5788 C CE3 . TRP D 199 ? 1.96844 1.52138 1.14958 -0.06784 0.11708  -0.34196 211 TRP B CE3 
5789 C CZ2 . TRP D 199 ? 2.05944 1.39325 1.25987 -0.02176 0.16516  -0.31933 211 TRP B CZ2 
5790 C CZ3 . TRP D 199 ? 1.92106 1.42426 1.12438 -0.08448 0.11250  -0.32840 211 TRP B CZ3 
5791 C CH2 . TRP D 199 ? 1.98513 1.37867 1.19693 -0.06304 0.13668  -0.31707 211 TRP B CH2 
5792 N N   . GLN D 200 ? 2.03849 1.55704 1.05922 -0.05528 0.21511  -0.52379 212 GLN B N   
5793 C CA  . GLN D 200 ? 2.16218 1.56023 1.14912 -0.06064 0.25712  -0.57886 212 GLN B CA  
5794 C C   . GLN D 200 ? 2.33877 1.73022 1.28493 -0.12698 0.26317  -0.65128 212 GLN B C   
5795 O O   . GLN D 200 ? 2.55815 1.84876 1.46790 -0.13889 0.30142  -0.70728 212 GLN B O   
5796 C CB  . GLN D 200 ? 2.20853 1.59846 1.17412 -0.01366 0.28550  -0.59128 212 GLN B CB  
5797 C CG  . GLN D 200 ? 2.19809 1.57431 1.20321 0.05142  0.28968  -0.52996 212 GLN B CG  
5798 C CD  . GLN D 200 ? 2.18803 1.58353 1.17584 0.09710  0.31500  -0.54051 212 GLN B CD  
5799 O OE1 . GLN D 200 ? 2.28881 1.68942 1.23067 0.08304  0.33406  -0.59716 212 GLN B OE1 
5800 N NE2 . GLN D 200 ? 2.13119 1.54487 1.15621 0.15084  0.31572  -0.48805 212 GLN B NE2 
5801 N N   . ASN D 201 ? 2.42948 1.92733 1.38024 -0.16972 0.22796  -0.65287 213 ASN B N   
5802 C CA  . ASN D 201 ? 2.43144 1.94450 1.34905 -0.23803 0.22964  -0.72180 213 ASN B CA  
5803 C C   . ASN D 201 ? 2.47104 1.94208 1.41524 -0.27809 0.22031  -0.71383 213 ASN B C   
5804 O O   . ASN D 201 ? 2.46320 2.02278 1.44158 -0.28205 0.18280  -0.66988 213 ASN B O   
5805 C CB  . ASN D 201 ? 2.35340 2.03131 1.25485 -0.25740 0.19721  -0.73233 213 ASN B CB  
5806 C CG  . ASN D 201 ? 2.38766 2.10669 1.27184 -0.32236 0.19250  -0.79533 213 ASN B CG  
5807 O OD1 . ASN D 201 ? 2.46133 2.08115 1.34102 -0.34962 0.22019  -0.83909 213 ASN B OD1 
5808 N ND2 . ASN D 201 ? 2.40210 2.27243 1.29690 -0.33763 0.15358  -0.78281 213 ASN B ND2 
5809 N N   . PRO D 202 ? 2.51701 1.85285 1.44572 -0.30727 0.25534  -0.75321 214 PRO B N   
5810 C CA  . PRO D 202 ? 2.61529 1.91114 1.56842 -0.34854 0.24947  -0.74435 214 PRO B CA  
5811 C C   . PRO D 202 ? 2.52269 1.93824 1.47785 -0.41547 0.22035  -0.77682 214 PRO B C   
5812 O O   . PRO D 202 ? 2.48410 1.89829 1.46473 -0.44834 0.20893  -0.76321 214 PRO B O   
5813 C CB  . PRO D 202 ? 2.68786 1.80912 1.61769 -0.36320 0.30010  -0.78249 214 PRO B CB  
5814 C CG  . PRO D 202 ? 2.64053 1.69844 1.54477 -0.30460 0.32990  -0.78727 214 PRO B CG  
5815 C CD  . PRO D 202 ? 2.56403 1.76663 1.45373 -0.29624 0.30539  -0.79972 214 PRO B CD  
5816 N N   . ARG D 203 ? 2.39198 1.92520 1.33805 -0.42702 0.20404  -0.80540 215 ARG B N   
5817 C CA  . ARG D 203 ? 2.32255 1.99077 1.29033 -0.47580 0.17171  -0.81961 215 ARG B CA  
5818 C C   . ARG D 203 ? 2.43396 2.22726 1.42508 -0.46097 0.12779  -0.76759 215 ARG B C   
5819 O O   . ARG D 203 ? 2.44286 2.33917 1.46105 -0.49575 0.10134  -0.76809 215 ARG B O   
5820 C CB  . ARG D 203 ? 2.37564 2.13173 1.32414 -0.48618 0.16812  -0.86083 215 ARG B CB  
5821 N N   . ASN D 204 ? 2.37484 2.16404 1.36116 -0.40696 0.12061  -0.71858 216 ASN B N   
5822 C CA  . ASN D 204 ? 2.30941 2.20857 1.33312 -0.37904 0.07894  -0.65221 216 ASN B CA  
5823 C C   . ASN D 204 ? 2.39671 2.23501 1.46513 -0.37908 0.07394  -0.61025 216 ASN B C   
5824 O O   . ASN D 204 ? 2.37175 2.07800 1.45001 -0.36041 0.09966  -0.59504 216 ASN B O   
5825 C CB  . ASN D 204 ? 2.27516 2.20208 1.30300 -0.31113 0.07132  -0.59758 216 ASN B CB  
5826 N N   . HIS D 205 ? 2.30624 2.24703 1.40023 -0.39674 0.04112  -0.59055 217 HIS B N   
5827 C CA  . HIS D 205 ? 2.09023 1.99573 1.22604 -0.40019 0.03325  -0.55305 217 HIS B CA  
5828 C C   . HIS D 205 ? 2.05642 2.02846 1.22624 -0.34542 0.00182  -0.47804 217 HIS B C   
5829 O O   . HIS D 205 ? 2.01766 2.11933 1.18738 -0.33828 -0.02750 -0.46501 217 HIS B O   
5830 C CB  . HIS D 205 ? 2.15619 2.12473 1.29685 -0.46743 0.02400  -0.59371 217 HIS B CB  
5831 C CG  . HIS D 205 ? 2.04526 1.98463 1.22712 -0.47416 0.01769  -0.55814 217 HIS B CG  
5832 N ND1 . HIS D 205 ? 2.20328 1.99883 1.39066 -0.48747 0.04868  -0.55933 217 HIS B ND1 
5833 C CD2 . HIS D 205 ? 1.94996 1.98610 1.16712 -0.46662 -0.01446 -0.51936 217 HIS B CD2 
5834 C CE1 . HIS D 205 ? 2.10622 1.91591 1.33049 -0.49063 0.03506  -0.52352 217 HIS B CE1 
5835 N NE2 . HIS D 205 ? 2.02545 1.97976 1.26930 -0.47819 -0.00306 -0.50055 217 HIS B NE2 
5836 N N   . PHE D 206 ? 2.09356 1.97705 1.29019 -0.30642 0.00934  -0.42952 218 PHE B N   
5837 C CA  . PHE D 206 ? 1.80551 1.73249 1.03516 -0.25844 -0.01552 -0.36162 218 PHE B CA  
5838 C C   . PHE D 206 ? 1.78484 1.71212 1.05107 -0.27108 -0.02884 -0.33700 218 PHE B C   
5839 O O   . PHE D 206 ? 1.89485 1.73297 1.16798 -0.29402 -0.00959 -0.34949 218 PHE B O   
5840 C CB  . PHE D 206 ? 1.87320 1.71928 1.11032 -0.20713 -0.00007 -0.32540 218 PHE B CB  
5841 C CG  . PHE D 206 ? 1.98061 1.83095 1.18463 -0.18945 0.01438  -0.34500 218 PHE B CG  
5842 C CD1 . PHE D 206 ? 2.10121 1.86676 1.27609 -0.20264 0.04737  -0.39222 218 PHE B CD1 
5843 C CD2 . PHE D 206 ? 1.95985 1.89514 1.15970 -0.15855 -0.00219 -0.31544 218 PHE B CD2 
5844 C CE1 . PHE D 206 ? 2.12696 1.90047 1.27082 -0.18450 0.06201  -0.41216 218 PHE B CE1 
5845 C CE2 . PHE D 206 ? 1.91600 1.86089 1.08460 -0.14288 0.01254  -0.33251 218 PHE B CE2 
5846 C CZ  . PHE D 206 ? 1.97800 1.84591 1.11945 -0.15541 0.04389  -0.38217 218 PHE B CZ  
5847 N N   . ARG D 207 ? 1.73870 1.76431 1.02596 -0.25378 -0.05963 -0.30055 219 ARG B N   
5848 C CA  . ARG D 207 ? 1.69080 1.73382 1.01270 -0.26191 -0.07416 -0.27696 219 ARG B CA  
5849 C C   . ARG D 207 ? 1.60868 1.69718 0.95542 -0.21183 -0.09716 -0.21614 219 ARG B C   
5850 O O   . ARG D 207 ? 1.48803 1.65162 0.82269 -0.18720 -0.11181 -0.20031 219 ARG B O   
5851 C CB  . ARG D 207 ? 1.60650 1.74618 0.92595 -0.31180 -0.08730 -0.31498 219 ARG B CB  
5852 N N   . CYS D 208 ? 1.68391 1.72354 1.06248 -0.19750 -0.09814 -0.18255 220 CYS B N   
5853 C CA  . CYS D 208 ? 1.49180 1.56056 0.89548 -0.15499 -0.11661 -0.12900 220 CYS B CA  
5854 C C   . CYS D 208 ? 1.42375 1.54593 0.85282 -0.16841 -0.13329 -0.12103 220 CYS B C   
5855 O O   . CYS D 208 ? 1.45134 1.52044 0.89904 -0.18392 -0.12505 -0.12107 220 CYS B O   
5856 C CB  . CYS D 208 ? 1.36996 1.34535 0.78962 -0.12404 -0.10373 -0.09785 220 CYS B CB  
5857 S SG  . CYS D 208 ? 1.50296 1.49975 0.95442 -0.08104 -0.12213 -0.03956 220 CYS B SG  
5858 N N   . GLN D 209 ? 1.40833 1.63863 0.83685 -0.15927 -0.15555 -0.11217 221 GLN B N   
5859 C CA  . GLN D 209 ? 1.29151 1.59239 0.74392 -0.16716 -0.17237 -0.10542 221 GLN B CA  
5860 C C   . GLN D 209 ? 1.29297 1.59268 0.76825 -0.11877 -0.18404 -0.05249 221 GLN B C   
5861 O O   . GLN D 209 ? 1.36703 1.67596 0.83227 -0.08027 -0.18906 -0.02292 221 GLN B O   
5862 C CB  . GLN D 209 ? 1.39969 1.83175 0.83794 -0.18289 -0.18965 -0.12866 221 GLN B CB  
5863 C CG  . GLN D 209 ? 1.27246 1.79778 0.73691 -0.18465 -0.20827 -0.12000 221 GLN B CG  
5864 C CD  . GLN D 209 ? 1.33474 2.00490 0.78598 -0.20030 -0.22591 -0.14551 221 GLN B CD  
5865 O OE1 . GLN D 209 ? 1.33249 2.02880 0.75391 -0.22313 -0.22234 -0.18012 221 GLN B OE1 
5866 N NE2 . GLN D 209 ? 1.50699 2.26957 0.98657 -0.18396 -0.24187 -0.12801 221 GLN B NE2 
5867 N N   . VAL D 210 ? 1.29335 1.57890 0.79721 -0.12272 -0.18591 -0.04185 222 VAL B N   
5868 C CA  . VAL D 210 ? 1.16740 1.44944 0.69339 -0.08151 -0.19515 0.00162  222 VAL B CA  
5869 C C   . VAL D 210 ? 1.21368 1.58081 0.76004 -0.08765 -0.20955 0.00089  222 VAL B C   
5870 O O   . VAL D 210 ? 1.26662 1.62517 0.82842 -0.12157 -0.20377 -0.01802 222 VAL B O   
5871 C CB  . VAL D 210 ? 1.21803 1.39503 0.75969 -0.07383 -0.18143 0.01763  222 VAL B CB  
5872 C CG1 . VAL D 210 ? 0.95000 1.13072 0.51458 -0.03903 -0.19067 0.05394  222 VAL B CG1 
5873 C CG2 . VAL D 210 ? 1.30660 1.41501 0.83170 -0.06124 -0.16811 0.02156  222 VAL B CG2 
5874 N N   . GLN D 211 ? 1.16931 1.61902 0.71473 -0.05306 -0.22630 0.02326  223 GLN B N   
5875 C CA  . GLN D 211 ? 1.12742 1.67159 0.69298 -0.04850 -0.24070 0.02629  223 GLN B CA  
5876 C C   . GLN D 211 ? 1.17413 1.67606 0.76291 -0.01332 -0.24055 0.06090  223 GLN B C   
5877 O O   . GLN D 211 ? 1.21883 1.69011 0.80159 0.03132  -0.24131 0.09492  223 GLN B O   
5878 C CB  . GLN D 211 ? 1.31546 1.97573 0.86612 -0.02209 -0.25765 0.03440  223 GLN B CB  
5879 C CG  . GLN D 211 ? 1.36594 2.10611 0.95400 -0.00589 -0.26304 0.04048  223 GLN B CG  
5880 C CD  . GLN D 211 ? 1.32488 2.13593 0.92936 -0.06126 -0.26447 -0.00170 223 GLN B CD  
5881 O OE1 . GLN D 211 ? 1.37558 2.24503 0.97335 -0.09359 -0.26404 -0.03455 223 GLN B OE1 
5882 N NE2 . GLN D 211 ? 1.29080 2.09692 0.91722 -0.07514 -0.26405 -0.00209 223 GLN B NE2 
5883 N N   . PHE D 212 ? 1.17953 1.67869 0.79280 -0.03558 -0.23752 0.05093  224 PHE B N   
5884 C CA  . PHE D 212 ? 1.10751 1.57141 0.74225 -0.00752 -0.23640 0.07704  224 PHE B CA  
5885 C C   . PHE D 212 ? 1.14331 1.71305 0.79701 0.00729  -0.24915 0.08126  224 PHE B C   
5886 O O   . PHE D 212 ? 1.17191 1.81815 0.83589 -0.02927 -0.25248 0.05455  224 PHE B O   
5887 C CB  . PHE D 212 ? 1.15950 1.53989 0.80589 -0.03799 -0.22158 0.06710  224 PHE B CB  
5888 C CG  . PHE D 212 ? 1.11706 1.48012 0.78544 -0.01641 -0.22117 0.08689  224 PHE B CG  
5889 C CD1 . PHE D 212 ? 1.15647 1.46682 0.82510 0.02480  -0.22062 0.11448  224 PHE B CD1 
5890 C CD2 . PHE D 212 ? 1.16725 1.56763 0.85489 -0.04056 -0.21942 0.07555  224 PHE B CD2 
5891 C CE1 . PHE D 212 ? 1.05932 1.35492 0.74573 0.04270  -0.21938 0.12745  224 PHE B CE1 
5892 C CE2 . PHE D 212 ? 1.25695 1.64585 0.96238 -0.01999 -0.21834 0.09189  224 PHE B CE2 
5893 C CZ  . PHE D 212 ? 1.10069 1.43716 0.80484 0.02223  -0.21882 0.11638  224 PHE B CZ  
5894 N N   . TYR D 213 ? 1.11520 1.68889 0.77337 0.06016  -0.25414 0.11352  225 TYR B N   
5895 C CA  . TYR D 213 ? 1.10209 1.75082 0.78674 0.08443  -0.25729 0.11880  225 TYR B CA  
5896 C C   . TYR D 213 ? 1.13592 1.75123 0.83730 0.09099  -0.25416 0.12750  225 TYR B C   
5897 O O   . TYR D 213 ? 1.05823 1.59933 0.75695 0.12502  -0.24847 0.15030  225 TYR B O   
5898 C CB  . TYR D 213 ? 1.09056 1.74238 0.77402 0.13788  -0.25396 0.14411  225 TYR B CB  
5899 C CG  . TYR D 213 ? 1.14889 1.84612 0.81596 0.13513  -0.25672 0.13804  225 TYR B CG  
5900 C CD1 . TYR D 213 ? 1.13561 1.77006 0.77340 0.13634  -0.25388 0.14630  225 TYR B CD1 
5901 C CD2 . TYR D 213 ? 1.04336 1.85314 0.72470 0.13149  -0.26104 0.12365  225 TYR B CD2 
5902 C CE1 . TYR D 213 ? 1.24499 1.92481 0.86594 0.13443  -0.25577 0.14024  225 TYR B CE1 
5903 C CE2 . TYR D 213 ? 0.97719 1.83507 0.64320 0.12940  -0.26336 0.11712  225 TYR B CE2 
5904 C CZ  . TYR D 213 ? 1.08282 1.87400 0.71763 0.13111  -0.26098 0.12540  225 TYR B CZ  
5905 O OH  . TYR D 213 ? 1.04731 1.88992 0.66531 0.12957  -0.26273 0.11846  225 TYR B OH  
5906 N N   . GLY D 214 ? 1.23862 1.90715 0.95765 0.05486  -0.25528 0.10714  226 GLY B N   
5907 C CA  . GLY D 214 ? 1.30542 1.93727 1.04335 0.05530  -0.24707 0.11148  226 GLY B CA  
5908 C C   . GLY D 214 ? 1.26562 2.00084 1.02839 0.06841  -0.25183 0.10998  226 GLY B C   
5909 O O   . GLY D 214 ? 1.18616 1.94728 0.95965 0.11521  -0.24983 0.12315  226 GLY B O   
5910 N N   . LEU D 215 ? 1.22101 1.98883 1.00028 0.02448  -0.24657 0.09099  227 LEU B N   
5911 C CA  . LEU D 215 ? 1.18416 2.05262 0.99018 0.03121  -0.24809 0.08756  227 LEU B CA  
5912 C C   . LEU D 215 ? 1.26132 2.24370 1.08398 -0.00072 -0.24923 0.06282  227 LEU B C   
5913 O O   . LEU D 215 ? 1.25806 2.24719 1.06721 -0.04281 -0.25178 0.04293  227 LEU B O   
5914 C CB  . LEU D 215 ? 1.00203 1.83255 0.81976 0.00086  -0.23468 0.08247  227 LEU B CB  
5915 C CG  . LEU D 215 ? 1.03951 1.75557 0.84899 0.02890  -0.22658 0.10141  227 LEU B CG  
5916 C CD1 . LEU D 215 ? 1.02426 1.71880 0.84360 -0.00246 -0.21279 0.09646  227 LEU B CD1 
5917 C CD2 . LEU D 215 ? 0.98209 1.71173 0.79386 0.09585  -0.23276 0.12125  227 LEU B CD2 
5918 N N   . SER D 216 ? 1.21993 2.29475 1.07153 0.01956  -0.24562 0.06223  228 SER B N   
5919 C CA  . SER D 216 ? 1.11042 2.31038 0.98364 -0.00989 -0.24402 0.03871  228 SER B CA  
5920 C C   . SER D 216 ? 1.19323 2.45442 1.08878 -0.05741 -0.23666 0.02151  228 SER B C   
5921 O O   . SER D 216 ? 1.22570 2.43779 1.11991 -0.05922 -0.23370 0.03127  228 SER B O   
5922 C CB  . SER D 216 ? 1.02191 2.29619 0.90947 0.05072  -0.24318 0.05230  228 SER B CB  
5923 N N   . GLU D 217 ? 1.07115 2.44447 0.98638 -0.09812 -0.23214 -0.00448 229 GLU B N   
5924 C CA  . GLU D 217 ? 1.06602 2.50951 1.00385 -0.15021 -0.22171 -0.02277 229 GLU B CA  
5925 C C   . GLU D 217 ? 1.08656 2.59987 1.05070 -0.10283 -0.21641 -0.00748 229 GLU B C   
5926 O O   . GLU D 217 ? 1.00824 2.58175 0.99154 -0.14037 -0.20646 -0.01873 229 GLU B O   
5927 C CB  . GLU D 217 ? 0.87781 2.41828 0.82684 -0.21332 -0.21496 -0.05874 229 GLU B CB  
5928 N N   . ASN D 218 ? 1.03532 2.53955 0.99842 -0.02371 -0.22043 0.01685  230 ASN B N   
5929 C CA  . ASN D 218 ? 1.03495 2.58989 1.01676 0.02797  -0.21371 0.03076  230 ASN B CA  
5930 C C   . ASN D 218 ? 1.01830 2.47934 0.99166 0.04832  -0.21218 0.04764  230 ASN B C   
5931 O O   . ASN D 218 ? 0.79712 2.29378 0.78397 0.08703  -0.20505 0.05581  230 ASN B O   
5932 C CB  . ASN D 218 ? 1.02682 2.60476 1.00548 0.10323  -0.21539 0.04873  230 ASN B CB  
5933 C CG  . ASN D 218 ? 0.93107 2.58972 0.91070 0.08951  -0.21883 0.03580  230 ASN B CG  
5934 O OD1 . ASN D 218 ? 0.93045 2.69233 0.92715 0.03694  -0.21483 0.00983  230 ASN B OD1 
5935 N ND2 . ASN D 218 ? 1.04135 2.65442 1.00094 0.13431  -0.22475 0.05314  230 ASN B ND2 
5936 N N   . ASP D 219 ? 1.12965 2.47644 1.07877 0.02443  -0.21776 0.05194  231 ASP B N   
5937 C CA  . ASP D 219 ? 1.24916 2.50236 1.18495 0.04541  -0.21668 0.06846  231 ASP B CA  
5938 C C   . ASP D 219 ? 1.27335 2.53760 1.21175 -0.01629 -0.21165 0.05874  231 ASP B C   
5939 O O   . ASP D 219 ? 1.21188 2.46050 1.14461 -0.08197 -0.20669 0.04283  231 ASP B O   
5940 C CB  . ASP D 219 ? 1.17527 2.29735 1.07889 0.06192  -0.22418 0.08256  231 ASP B CB  
5941 C CG  . ASP D 219 ? 1.18211 2.29512 1.07887 0.10593  -0.22836 0.09115  231 ASP B CG  
5942 O OD1 . ASP D 219 ? 1.15928 2.33642 1.07075 0.15093  -0.22433 0.09648  231 ASP B OD1 
5943 O OD2 . ASP D 219 ? 1.20548 2.24951 1.07960 0.09612  -0.23447 0.09381  231 ASP B OD2 
5944 N N   . GLU D 220 ? 1.29235 2.55881 1.23838 0.00419  -0.20352 0.06706  232 GLU B N   
5945 C CA  . GLU D 220 ? 1.15368 2.39345 1.10189 -0.04878 -0.18436 0.06189  232 GLU B CA  
5946 C C   . GLU D 220 ? 1.33870 2.41691 1.25705 -0.06370 -0.17611 0.07205  232 GLU B C   
5947 O O   . GLU D 220 ? 1.40701 2.40146 1.30945 -0.01683 -0.18163 0.08597  232 GLU B O   
5948 C CB  . GLU D 220 ? 0.95017 2.24853 0.91443 -0.01755 -0.17664 0.06727  232 GLU B CB  
5949 N N   . TRP D 221 ? 1.28294 2.31856 1.19336 -0.12894 -0.16111 0.06496  233 TRP B N   
5950 C CA  . TRP D 221 ? 1.13476 2.02540 1.01670 -0.14312 -0.15179 0.07572  233 TRP B CA  
5951 C C   . TRP D 221 ? 1.22704 2.09244 1.10427 -0.19174 -0.12794 0.07920  233 TRP B C   
5952 O O   . TRP D 221 ? 1.24912 2.15611 1.13355 -0.25055 -0.11503 0.06501  233 TRP B O   
5953 C CB  . TRP D 221 ? 1.13337 1.96928 0.99992 -0.16811 -0.15621 0.06612  233 TRP B CB  
5954 C CG  . TRP D 221 ? 1.34054 2.03397 1.17898 -0.17571 -0.14659 0.07769  233 TRP B CG  
5955 C CD1 . TRP D 221 ? 1.36696 1.99026 1.18981 -0.22600 -0.12570 0.07689  233 TRP B CD1 
5956 C CD2 . TRP D 221 ? 1.25893 1.86543 1.08140 -0.13000 -0.15567 0.09256  233 TRP B CD2 
5957 N NE1 . TRP D 221 ? 1.39158 1.89598 1.19039 -0.20865 -0.12280 0.09175  233 TRP B NE1 
5958 C CE2 . TRP D 221 ? 1.30135 1.79889 1.10141 -0.15283 -0.14171 0.09995  233 TRP B CE2 
5959 C CE3 . TRP D 221 ? 1.10919 1.71813 0.93344 -0.07269 -0.17195 0.10062  233 TRP B CE3 
5960 C CZ2 . TRP D 221 ? 1.26230 1.66931 1.04586 -0.12115 -0.14597 0.11322  233 TRP B CZ2 
5961 C CZ3 . TRP D 221 ? 1.15344 1.66353 0.96005 -0.04751 -0.17415 0.11248  233 TRP B CZ3 
5962 C CH2 . TRP D 221 ? 1.23856 1.65643 1.02705 -0.07216 -0.16247 0.11776  233 TRP B CH2 
5963 N N   . THR D 222 ? 1.30341 2.10210 1.16676 -0.16871 -0.12074 0.09788  234 THR B N   
5964 C CA  . THR D 222 ? 1.33446 2.10078 1.18679 -0.20541 -0.09703 0.10888  234 THR B CA  
5965 C C   . THR D 222 ? 1.30225 1.93823 1.12422 -0.18970 -0.09266 0.12863  234 THR B C   
5966 O O   . THR D 222 ? 1.27152 1.88962 1.08560 -0.15750 -0.09224 0.14275  234 THR B O   
5967 C CB  . THR D 222 ? 1.35851 2.21382 1.22678 -0.19003 -0.09157 0.11246  234 THR B CB  
5968 O OG1 . THR D 222 ? 1.25890 2.10809 1.12640 -0.12460 -0.10638 0.11798  234 THR B OG1 
5969 C CG2 . THR D 222 ? 1.22236 2.21868 1.12308 -0.20977 -0.09328 0.09327  234 THR B CG2 
5970 N N   . GLN D 223 ? 1.40951 1.96119 1.21432 -0.21188 -0.08920 0.12767  235 GLN B N   
5971 C CA  . GLN D 223 ? 1.47261 1.90811 1.25009 -0.19676 -0.08459 0.14610  235 GLN B CA  
5972 C C   . GLN D 223 ? 1.57904 1.93695 1.33556 -0.24650 -0.06111 0.14927  235 GLN B C   
5973 O O   . GLN D 223 ? 1.63379 2.02024 1.39684 -0.29530 -0.05088 0.13138  235 GLN B O   
5974 C CB  . GLN D 223 ? 1.45841 1.85518 1.23369 -0.15569 -0.10575 0.14292  235 GLN B CB  
5975 C CG  . GLN D 223 ? 1.38766 1.83073 1.17630 -0.10346 -0.12378 0.14269  235 GLN B CG  
5976 C CD  . GLN D 223 ? 1.43342 1.85968 1.21322 -0.08092 -0.11868 0.15742  235 GLN B CD  
5977 O OE1 . GLN D 223 ? 1.51617 1.87416 1.27560 -0.08746 -0.10848 0.17291  235 GLN B OE1 
5978 N NE2 . GLN D 223 ? 1.46999 1.96219 1.26346 -0.05169 -0.12510 0.15226  235 GLN B NE2 
5979 N N   . ASP D 224 ? 1.61768 1.87716 1.34782 -0.23313 -0.05124 0.17128  236 ASP B N   
5980 C CA  . ASP D 224 ? 1.63242 1.79973 1.33662 -0.27088 -0.02450 0.17968  236 ASP B CA  
5981 C C   . ASP D 224 ? 1.55543 1.66347 1.25167 -0.28095 -0.02726 0.16259  236 ASP B C   
5982 O O   . ASP D 224 ? 1.61535 1.64488 1.28998 -0.31632 -0.00277 0.16249  236 ASP B O   
5983 C CB  . ASP D 224 ? 1.39026 1.48247 1.06730 -0.24457 -0.01205 0.21396  236 ASP B CB  
5984 N N   . ARG D 225 ? 1.42922 1.56821 1.13939 -0.25070 -0.05362 0.14858  237 ARG B N   
5985 C CA  . ARG D 225 ? 1.42361 1.51773 1.12566 -0.25724 -0.05760 0.13172  237 ARG B CA  
5986 C C   . ARG D 225 ? 1.31840 1.50177 1.04053 -0.28200 -0.06997 0.10104  237 ARG B C   
5987 O O   . ARG D 225 ? 1.33643 1.62019 1.08168 -0.28512 -0.07833 0.09480  237 ARG B O   
5988 C CB  . ARG D 225 ? 1.54209 1.59976 1.24043 -0.20412 -0.07591 0.14198  237 ARG B CB  
5989 C CG  . ARG D 225 ? 1.47062 1.60353 1.19094 -0.16388 -0.10145 0.14161  237 ARG B CG  
5990 C CD  . ARG D 225 ? 1.30056 1.38757 1.01535 -0.12002 -0.11420 0.15132  237 ARG B CD  
5991 N NE  . ARG D 225 ? 1.35116 1.49376 1.08309 -0.08390 -0.13401 0.14993  237 ARG B NE  
5992 C CZ  . ARG D 225 ? 1.22913 1.40425 0.96960 -0.07038 -0.14867 0.13888  237 ARG B CZ  
5993 N NH1 . ARG D 225 ? 1.19490 1.36471 0.92963 -0.09064 -0.14882 0.12594  237 ARG B NH1 
5994 N NH2 . ARG D 225 ? 1.20232 1.41398 0.95441 -0.03462 -0.16180 0.14098  237 ARG B NH2 
5995 N N   . ALA D 226 ? 1.22234 1.37469 0.93458 -0.29730 -0.07088 0.08151  238 ALA B N   
5996 C CA  . ALA D 226 ? 1.28424 1.52506 1.01118 -0.32237 -0.08265 0.05096  238 ALA B CA  
5997 C C   . ALA D 226 ? 1.40037 1.72767 1.14769 -0.27276 -0.11271 0.05446  238 ALA B C   
5998 O O   . ALA D 226 ? 1.46335 1.75507 1.20761 -0.22269 -0.12412 0.07385  238 ALA B O   
5999 C CB  . ALA D 226 ? 1.16186 1.34532 0.86844 -0.34726 -0.07600 0.02837  238 ALA B CB  
6000 N N   . LYS D 227 ? 1.28589 1.72859 1.05340 -0.28742 -0.12374 0.03532  239 LYS B N   
6001 C CA  . LYS D 227 ? 1.32659 1.85332 1.11083 -0.23740 -0.14930 0.04059  239 LYS B CA  
6002 C C   . LYS D 227 ? 1.31252 1.80377 1.08162 -0.21044 -0.16257 0.03967  239 LYS B C   
6003 O O   . LYS D 227 ? 1.37929 1.86595 1.13653 -0.24337 -0.15979 0.01786  239 LYS B O   
6004 C CB  . LYS D 227 ? 1.28718 1.95645 1.09580 -0.25767 -0.15725 0.02098  239 LYS B CB  
6005 C CG  . LYS D 227 ? 1.28301 1.99982 1.10775 -0.29666 -0.14085 0.01701  239 LYS B CG  
6006 C CD  . LYS D 227 ? 1.35283 2.23107 1.20703 -0.30642 -0.15193 -0.00092 239 LYS B CD  
6007 C CE  . LYS D 227 ? 1.34501 2.27810 1.21656 -0.35400 -0.13271 -0.00769 239 LYS B CE  
6008 N NZ  . LYS D 227 ? 1.15957 2.26617 1.06470 -0.35459 -0.14479 -0.02282 239 LYS B NZ  
6009 N N   . PRO D 228 ? 1.17478 1.63977 0.94228 -0.15406 -0.17496 0.06102  240 PRO B N   
6010 C CA  . PRO D 228 ? 1.19241 1.63094 0.94552 -0.12792 -0.18615 0.06287  240 PRO B CA  
6011 C C   . PRO D 228 ? 1.15880 1.70625 0.91992 -0.11168 -0.20379 0.05557  240 PRO B C   
6012 O O   . PRO D 228 ? 1.23995 1.81367 1.00456 -0.06063 -0.21633 0.07316  240 PRO B O   
6013 C CB  . PRO D 228 ? 1.13212 1.50460 0.88250 -0.07969 -0.18882 0.08838  240 PRO B CB  
6014 C CG  . PRO D 228 ? 1.19691 1.61467 0.96575 -0.06511 -0.18898 0.09663  240 PRO B CG  
6015 C CD  . PRO D 228 ? 1.23578 1.68768 1.01205 -0.11528 -0.17635 0.08285  240 PRO B CD  
6016 N N   . VAL D 229 ? 1.23024 1.84414 0.99258 -0.15580 -0.20348 0.02880  241 VAL B N   
6017 C CA  . VAL D 229 ? 1.32057 2.05952 1.09077 -0.14394 -0.22102 0.01970  241 VAL B CA  
6018 C C   . VAL D 229 ? 1.28576 2.00605 1.03190 -0.13403 -0.22879 0.01586  241 VAL B C   
6019 O O   . VAL D 229 ? 1.29418 1.90935 1.02010 -0.14571 -0.21852 0.01423  241 VAL B O   
6020 C CB  . VAL D 229 ? 1.18544 2.02905 0.97228 -0.20067 -0.21773 -0.01136 241 VAL B CB  
6021 C CG1 . VAL D 229 ? 1.19764 2.06885 1.00842 -0.20829 -0.20883 -0.00490 241 VAL B CG1 
6022 C CG2 . VAL D 229 ? 1.06015 1.84448 0.82921 -0.26692 -0.20129 -0.04183 241 VAL B CG2 
6023 N N   . THR D 230 ? 1.08854 1.91609 0.83567 -0.10903 -0.24634 0.01601  242 THR B N   
6024 C CA  . THR D 230 ? 1.03660 1.86552 0.75860 -0.09823 -0.25439 0.01337  242 THR B CA  
6025 C C   . THR D 230 ? 1.09957 1.91547 0.80742 -0.16403 -0.24494 -0.02619 242 THR B C   
6026 O O   . THR D 230 ? 1.30373 2.21525 1.02183 -0.20920 -0.24652 -0.05761 242 THR B O   
6027 C CB  . THR D 230 ? 1.17995 2.10978 0.91695 -0.05605 -0.26252 0.02203  242 THR B CB  
6028 O OG1 . THR D 230 ? 1.21021 2.11793 0.95946 0.00714  -0.26209 0.05724  242 THR B OG1 
6029 C CG2 . THR D 230 ? 1.15237 2.07668 0.86550 -0.04554 -0.26535 0.02024  242 THR B CG2 
6030 N N   . GLN D 231 ? 1.04579 1.74531 0.73019 -0.17091 -0.23341 -0.02718 243 GLN B N   
6031 C CA  . GLN D 231 ? 1.24685 1.90665 0.91394 -0.23014 -0.21890 -0.06500 243 GLN B CA  
6032 C C   . GLN D 231 ? 1.21291 1.81582 0.84978 -0.21264 -0.21856 -0.06382 243 GLN B C   
6033 O O   . GLN D 231 ? 1.09945 1.69495 0.72992 -0.15861 -0.22880 -0.03228 243 GLN B O   
6034 C CB  . GLN D 231 ? 1.21634 1.76881 0.88718 -0.26541 -0.19501 -0.06962 243 GLN B CB  
6035 C CG  . GLN D 231 ? 1.00197 1.44131 0.67090 -0.22316 -0.18876 -0.03359 243 GLN B CG  
6036 C CD  . GLN D 231 ? 1.10921 1.44973 0.77743 -0.25319 -0.16517 -0.03485 243 GLN B CD  
6037 O OE1 . GLN D 231 ? 1.35443 1.62679 1.00359 -0.29069 -0.14644 -0.05696 243 GLN B OE1 
6038 N NE2 . GLN D 231 ? 1.05006 1.38085 0.73621 -0.23460 -0.16427 -0.01049 243 GLN B NE2 
6039 N N   . ILE D 232 ? 1.35618 1.91544 0.97295 -0.26024 -0.20387 -0.09948 244 ILE B N   
6040 C CA  . ILE D 232 ? 1.35032 1.85491 0.93674 -0.25061 -0.19956 -0.10524 244 ILE B CA  
6041 C C   . ILE D 232 ? 1.22406 1.59073 0.79820 -0.27774 -0.17250 -0.11749 244 ILE B C   
6042 O O   . ILE D 232 ? 1.36310 1.70976 0.93079 -0.33380 -0.15565 -0.15454 244 ILE B O   
6043 C CB  . ILE D 232 ? 1.35407 1.95720 0.92144 -0.27760 -0.20838 -0.14240 244 ILE B CB  
6044 C CG1 . ILE D 232 ? 1.27473 2.01968 0.85100 -0.23916 -0.23565 -0.12311 244 ILE B CG1 
6045 C CG2 . ILE D 232 ? 1.33805 1.87584 0.87158 -0.27235 -0.19946 -0.15249 244 ILE B CG2 
6046 C CD1 . ILE D 232 ? 1.14731 1.99668 0.71182 -0.25623 -0.24292 -0.15414 244 ILE B CD1 
6047 N N   . VAL D 233 ? 1.16958 1.44223 0.73988 -0.23814 -0.16661 -0.08660 245 VAL B N   
6048 C CA  . VAL D 233 ? 1.32565 1.47137 0.88280 -0.24994 -0.14167 -0.09158 245 VAL B CA  
6049 C C   . VAL D 233 ? 1.43363 1.54595 0.96282 -0.23855 -0.13652 -0.10251 245 VAL B C   
6050 O O   . VAL D 233 ? 1.23306 1.37860 0.75908 -0.19875 -0.15082 -0.08089 245 VAL B O   
6051 C CB  . VAL D 233 ? 1.17116 1.24757 0.74493 -0.21425 -0.13829 -0.05169 245 VAL B CB  
6052 C CG1 . VAL D 233 ? 1.37882 1.33560 0.93948 -0.22594 -0.11162 -0.05538 245 VAL B CG1 
6053 C CG2 . VAL D 233 ? 1.03565 1.16443 0.63656 -0.21697 -0.14696 -0.03829 245 VAL B CG2 
6054 N N   . SER D 234 ? 1.39625 1.43974 0.90322 -0.27322 -0.11349 -0.13592 246 SER B N   
6055 C CA  . SER D 234 ? 1.41672 1.43221 0.89461 -0.26706 -0.10551 -0.15389 246 SER B CA  
6056 C C   . SER D 234 ? 1.64610 1.53244 1.10686 -0.27842 -0.07389 -0.16709 246 SER B C   
6057 O O   . SER D 234 ? 1.71673 1.53764 1.18514 -0.29445 -0.05788 -0.16277 246 SER B O   
6058 C CB  . SER D 234 ? 1.46942 1.57518 0.92839 -0.30309 -0.11271 -0.19752 246 SER B CB  
6059 O OG  . SER D 234 ? 1.48347 1.71536 0.95624 -0.28556 -0.14164 -0.18165 246 SER B OG  
6060 N N   . ALA D 235 ? 1.71271 1.56361 1.14787 -0.26681 -0.06334 -0.18161 247 ALA B N   
6061 C CA  . ALA D 235 ? 1.68708 1.41733 1.10148 -0.26972 -0.03139 -0.19581 247 ALA B CA  
6062 C C   . ALA D 235 ? 1.68387 1.41627 1.06522 -0.27577 -0.02232 -0.23240 247 ALA B C   
6063 O O   . ALA D 235 ? 1.56807 1.37136 0.94628 -0.25048 -0.04034 -0.22300 247 ALA B O   
6064 C CB  . ALA D 235 ? 1.46855 1.13143 0.89691 -0.21809 -0.02657 -0.15023 247 ALA B CB  
6065 N N   . GLU D 236 ? 1.99569 1.64677 1.34986 -0.30909 0.00795  -0.27382 248 GLU B N   
6066 C CA  . GLU D 236 ? 1.92693 1.57530 1.24555 -0.32211 0.02063  -0.31848 248 GLU B CA  
6067 C C   . GLU D 236 ? 1.95323 1.48504 1.25338 -0.28811 0.05023  -0.31474 248 GLU B C   
6068 O O   . GLU D 236 ? 2.00262 1.44540 1.31322 -0.26521 0.06573  -0.28564 248 GLU B O   
6069 C CB  . GLU D 236 ? 1.82997 1.48189 1.12720 -0.39283 0.03493  -0.38039 248 GLU B CB  
6070 N N   . ALA D 237 ? 2.05463 1.59542 1.32598 -0.28221 0.05811  -0.34416 249 ALA B N   
6071 C CA  . ALA D 237 ? 2.19023 1.63269 1.44169 -0.24765 0.08756  -0.34628 249 ALA B CA  
6072 C C   . ALA D 237 ? 2.24376 1.70383 1.45568 -0.26576 0.09966  -0.40053 249 ALA B C   
6073 O O   . ALA D 237 ? 2.17010 1.73839 1.37845 -0.26085 0.07631  -0.40218 249 ALA B O   
6074 C CB  . ALA D 237 ? 1.78398 1.24306 1.06013 -0.18355 0.07477  -0.28984 249 ALA B CB  
6075 N N   . TRP D 238 ? 2.30230 1.65467 1.48170 -0.28526 0.13767  -0.44421 250 TRP B N   
6076 C CA  . TRP D 238 ? 2.37595 1.73348 1.51346 -0.30516 0.15402  -0.50340 250 TRP B CA  
6077 C C   . TRP D 238 ? 2.29939 1.62881 1.42541 -0.24546 0.16769  -0.48924 250 TRP B C   
6078 O O   . TRP D 238 ? 2.22996 1.51094 1.37756 -0.19341 0.17258  -0.44074 250 TRP B O   
6079 C CB  . TRP D 238 ? 2.51786 1.76526 1.62232 -0.35871 0.19280  -0.56356 250 TRP B CB  
6080 C CG  . TRP D 238 ? 2.56659 1.85436 1.68011 -0.42770 0.18235  -0.58771 250 TRP B CG  
6081 C CD1 . TRP D 238 ? 2.55446 1.79875 1.69321 -0.44404 0.18395  -0.56034 250 TRP B CD1 
6082 C CD2 . TRP D 238 ? 2.54486 1.93608 1.64294 -0.49009 0.16892  -0.64479 250 TRP B CD2 
6083 N NE1 . TRP D 238 ? 2.50378 1.81744 1.64596 -0.51399 0.17342  -0.59704 250 TRP B NE1 
6084 C CE2 . TRP D 238 ? 2.46994 1.87790 1.58837 -0.54336 0.16319  -0.64980 250 TRP B CE2 
6085 C CE3 . TRP D 238 ? 2.48391 1.96397 1.55238 -0.50580 0.16107  -0.69230 250 TRP B CE3 
6086 C CZ2 . TRP D 238 ? 2.44256 1.95947 1.55802 -0.61062 0.14901  -0.70004 250 TRP B CZ2 
6087 C CZ3 . TRP D 238 ? 2.28755 1.87986 1.36100 -0.56489 0.14438  -0.73322 250 TRP B CZ3 
6088 C CH2 . TRP D 238 ? 2.40845 2.02424 1.51425 -0.61148 0.13761  -0.73087 250 TRP B CH2 
6089 N N   . GLY D 239 ? 2.24377 1.61377 1.33541 -0.25435 0.17390  -0.53398 251 GLY B N   
6090 C CA  . GLY D 239 ? 2.25950 1.61821 1.33882 -0.20086 0.18761  -0.52499 251 GLY B CA  
6091 C C   . GLY D 239 ? 2.48122 1.68941 1.53967 -0.17878 0.23379  -0.54279 251 GLY B C   
6092 O O   . GLY D 239 ? 2.56783 1.68406 1.59657 -0.21879 0.26334  -0.59321 251 GLY B O   
6093 N N   . ARG D 240 ? 2.43710 1.62093 1.51086 -0.11370 0.24172  -0.50068 252 ARG B N   
6094 C CA  . ARG D 240 ? 2.56539 1.61683 1.62242 -0.07576 0.28460  -0.50649 252 ARG B CA  
6095 C C   . ARG D 240 ? 2.42754 1.50506 1.46682 -0.03146 0.29912  -0.51781 252 ARG B C   
6096 O O   . ARG D 240 ? 2.30490 1.48840 1.36730 -0.00308 0.27417  -0.48262 252 ARG B O   
6097 C CB  . ARG D 240 ? 2.26697 1.26862 1.36164 -0.03203 0.28313  -0.44230 252 ARG B CB  
6098 N N   . ALA D 241 ? 2.35035 1.32850 1.34753 -0.02639 0.34199  -0.56729 253 ALA B N   
6099 C CA  . ALA D 241 ? 2.38436 1.38036 1.36099 0.01707  0.36148  -0.58390 253 ALA B CA  
6100 C C   . ALA D 241 ? 2.43568 1.32999 1.41705 0.08657  0.39588  -0.55775 253 ALA B C   
6101 O O   . ALA D 241 ? 2.43782 1.36212 1.41784 0.13812  0.40816  -0.55192 253 ALA B O   
6102 C CB  . ALA D 241 ? 2.53885 1.51424 1.45972 -0.02503 0.38512  -0.66607 253 ALA B CB  
# 
