data_3WCV
# 
_entry.id   3WCV 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.281 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   3WCV         
RCSB  RCSB096175   
WWPDB D_1000096175 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.db_id 
_pdbx_database_related.details 
_pdbx_database_related.content_type 
PDB 3WCT . unspecified 
PDB 3WCU . unspecified 
PDB 3WCW . unspecified 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        3WCV 
_pdbx_database_status.recvd_initial_deposition_date   2013-06-01 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Numoto, N.'   1  
'Nakagawa, T.' 2  
'Ohara, R.'    3  
'Hasegawa, T.' 4  
'Kita, A.'     5  
'Yoshida, T.'  6  
'Maruyama, T.' 7  
'Imai, K.'     8  
'Fukumori, Y.' 9  
'Miki, K.'     10 
# 
_citation.id                        primary 
_citation.title                     
'The structure of a deoxygenated 400 kDa haemoglobin reveals ternary- and quaternary-structural changes of giant haemoglobins' 
_citation.journal_abbrev            'Acta Crystallogr.,Sect.D' 
_citation.journal_volume            70 
_citation.page_first                1823 
_citation.page_last                 1831 
_citation.year                      2014 
_citation.journal_id_ASTM           ABCRE6 
_citation.country                   DK 
_citation.journal_id_ISSN           0907-4449 
_citation.journal_id_CSD            0766 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   25004960 
_citation.pdbx_database_id_DOI      10.1107/S1399004714008475 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Numoto, N.'   1  
primary 'Nakagawa, T.' 2  
primary 'Ohara, R.'    3  
primary 'Hasegawa, T.' 4  
primary 'Kita, A.'     5  
primary 'Yoshida, T.'  6  
primary 'Maruyama, T.' 7  
primary 'Imai, K.'     8  
primary 'Fukumori, Y.' 9  
primary 'Miki, K.'     10 
# 
_cell.entry_id           3WCV 
_cell.length_a           108.944 
_cell.length_b           108.944 
_cell.length_c           195.016 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_cell.angle_gamma        120.00 
_cell.Z_PDB              12 
_cell.pdbx_unique_axis   ? 
_cell.length_a_esd       ? 
_cell.length_b_esd       ? 
_cell.length_c_esd       ? 
_cell.angle_alpha_esd    ? 
_cell.angle_beta_esd     ? 
_cell.angle_gamma_esd    ? 
# 
_symmetry.entry_id                         3WCV 
_symmetry.space_group_name_H-M             'P 63' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                173 
_symmetry.space_group_name_Hall            ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1  polymer     nat 'A1 globin chain of giant V2 hemoglobin' 16368.704 2  ? ? ? ? 
2  polymer     nat 'A2 globin chain of giant V2 hemoglobin' 15951.922 2  ? ? ? ? 
3  polymer     nat 'B2 globin chain of giant V2 hemoglobin' 16519.531 2  ? ? ? ? 
4  polymer     nat 'B1 globin chain of giant V2 hemoglobin' 16228.627 2  ? ? ? ? 
5  non-polymer syn 'PROTOPORPHYRIN IX CONTAINING FE'        616.487   8  ? ? ? ? 
6  non-polymer syn 'OXYGEN MOLECULE'                        31.999    8  ? ? ? ? 
7  non-polymer syn 'CALCIUM ION'                            40.078    6  ? ? ? ? 
8  non-polymer man N-ACETYL-D-GLUCOSAMINE                   221.208   4  ? ? ? ? 
9  non-polymer man ALPHA-D-MANNOSE                          180.156   6  ? ? ? ? 
10 non-polymer man ALPHA-L-FUCOSE                           164.156   2  ? ? ? ? 
11 water       nat water                                    18.015    59 ? ? ? ? 
# 
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 
;DCNILQRLKVKMQWAKAYGFGTERAKFGNSLWTSIFNYAPDARDLFKSVKSEDMRSPQFKAHIARVIGGLDRVISMFDNE
DALNADLEHLKSQHDPRGLDALNFVVFGKALFATVGGQFGVCFDLPAWESCYKVIAMGITGNDMFS
;
;DCNILQRLKVKMQWAKAYGFGTERAKFGNSLWTSIFNYAPDARDLFKSVKSEDMRSPQFKAHIARVIGGLDRVISMFDNE
DALNADLEHLKSQHDPRGLDALNFVVFGKALFATVGGQFGVCFDLPAWESCYKVIAMGITGNDMFS
;
A,E ? 
2 'polypeptide(L)' no no 
;SECGPLQRLKVKRQWAEAYGSGNGREEFGHFIWANVFKVAPSARDMFKRVRGDNIYTPAFRAHATRVLGGLDMCVALLDD
ESVLNTQLAHLASQHSSRGVSAEQYNVVEHAVMMGVEHEIGQNVFDKDAWQACLDVITSGIQGN
;
;SECGPLQRLKVKRQWAEAYGSGNGREEFGHFIWANVFKVAPSARDMFKRVRGDNIYTPAFRAHATRVLGGLDMCVALLDD
ESVLNTQLAHLASQHSSRGVSAEQYNVVEHAVMMGVEHEIGQNVFDKDAWQACLDVITSGIQGN
;
B,F ? 
3 'polypeptide(L)' no no 
;SSNSCTTEDRREMQLMWANVWSAQFTGRRLAIAQAVFKDLFAHVPDAVGLFDRVHGTEIDSSEFKAHCIRVVNGLDSAIG
LLSDPSTLNEQLSHLATQHQERAGVTKGGFSAIAQSFLRVMPQVASCFNPDAWSRCFNRITNGMTEGLAE
;
;SSNSCTTEDRREMQLMWANVWSAQFTGRRLAIAQAVFKDLFAHVPDAVGLFDRVHGTEIDSSEFKAHCIRVVNGLDSAIG
LLSDPSTLNEQLSHLATQHQERAGVTKGGFSAIAQSFLRVMPQVASCFNPDAWSRCFNRITNGMTEGLAE
;
C,G ? 
4 'polypeptide(L)' no no 
;SEFCSEADATIVIKQWNQIYNAGIGAKSRWTMGNEIFSSLFKLKPESEVLFNNVNVANMSSGAFHAHTVRVLSGLDMGIN
YLNDAGTLTSLTAHLAAQHVARTGLKAVYFDAMGKVLMTVLPSLIDNFNPDAWRNCLLPLKNAIAKGLP
;
;SEFCSEADATIVIKQWNQIYNAGIGAKSRWTMGNEIFSSLFKLKPESEVLFNNVNVANMSSGAFHAHTVRVLSGLDMGIN
YLNDAGTLTSLTAHLAAQHVARTGLKAVYFDAMGKVLMTVLPSLIDNFNPDAWRNCLLPLKNAIAKGLP
;
D,H ? 
# 
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   CYS n 
1 3   ASN n 
1 4   ILE n 
1 5   LEU n 
1 6   GLN n 
1 7   ARG n 
1 8   LEU n 
1 9   LYS n 
1 10  VAL n 
1 11  LYS n 
1 12  MET n 
1 13  GLN n 
1 14  TRP n 
1 15  ALA n 
1 16  LYS n 
1 17  ALA n 
1 18  TYR n 
1 19  GLY n 
1 20  PHE n 
1 21  GLY n 
1 22  THR n 
1 23  GLU n 
1 24  ARG n 
1 25  ALA n 
1 26  LYS n 
1 27  PHE n 
1 28  GLY n 
1 29  ASN n 
1 30  SER n 
1 31  LEU n 
1 32  TRP n 
1 33  THR n 
1 34  SER n 
1 35  ILE n 
1 36  PHE n 
1 37  ASN n 
1 38  TYR n 
1 39  ALA n 
1 40  PRO n 
1 41  ASP n 
1 42  ALA n 
1 43  ARG n 
1 44  ASP n 
1 45  LEU n 
1 46  PHE n 
1 47  LYS n 
1 48  SER n 
1 49  VAL n 
1 50  LYS n 
1 51  SER n 
1 52  GLU n 
1 53  ASP n 
1 54  MET n 
1 55  ARG n 
1 56  SER n 
1 57  PRO n 
1 58  GLN n 
1 59  PHE n 
1 60  LYS n 
1 61  ALA n 
1 62  HIS n 
1 63  ILE n 
1 64  ALA n 
1 65  ARG n 
1 66  VAL n 
1 67  ILE n 
1 68  GLY n 
1 69  GLY n 
1 70  LEU n 
1 71  ASP n 
1 72  ARG n 
1 73  VAL n 
1 74  ILE n 
1 75  SER n 
1 76  MET n 
1 77  PHE n 
1 78  ASP n 
1 79  ASN n 
1 80  GLU n 
1 81  ASP n 
1 82  ALA n 
1 83  LEU n 
1 84  ASN n 
1 85  ALA n 
1 86  ASP n 
1 87  LEU n 
1 88  GLU n 
1 89  HIS n 
1 90  LEU n 
1 91  LYS n 
1 92  SER n 
1 93  GLN n 
1 94  HIS n 
1 95  ASP n 
1 96  PRO n 
1 97  ARG n 
1 98  GLY n 
1 99  LEU n 
1 100 ASP n 
1 101 ALA n 
1 102 LEU n 
1 103 ASN n 
1 104 PHE n 
1 105 VAL n 
1 106 VAL n 
1 107 PHE n 
1 108 GLY n 
1 109 LYS n 
1 110 ALA n 
1 111 LEU n 
1 112 PHE n 
1 113 ALA n 
1 114 THR n 
1 115 VAL n 
1 116 GLY n 
1 117 GLY n 
1 118 GLN n 
1 119 PHE n 
1 120 GLY n 
1 121 VAL n 
1 122 CYS n 
1 123 PHE n 
1 124 ASP n 
1 125 LEU n 
1 126 PRO n 
1 127 ALA n 
1 128 TRP n 
1 129 GLU n 
1 130 SER n 
1 131 CYS n 
1 132 TYR n 
1 133 LYS n 
1 134 VAL n 
1 135 ILE n 
1 136 ALA n 
1 137 MET n 
1 138 GLY n 
1 139 ILE n 
1 140 THR n 
1 141 GLY n 
1 142 ASN n 
1 143 ASP n 
1 144 MET n 
1 145 PHE n 
1 146 SER n 
2 1   SER n 
2 2   GLU n 
2 3   CYS n 
2 4   GLY n 
2 5   PRO n 
2 6   LEU n 
2 7   GLN n 
2 8   ARG n 
2 9   LEU n 
2 10  LYS n 
2 11  VAL n 
2 12  LYS n 
2 13  ARG n 
2 14  GLN n 
2 15  TRP n 
2 16  ALA n 
2 17  GLU n 
2 18  ALA n 
2 19  TYR n 
2 20  GLY n 
2 21  SER n 
2 22  GLY n 
2 23  ASN n 
2 24  GLY n 
2 25  ARG n 
2 26  GLU n 
2 27  GLU n 
2 28  PHE n 
2 29  GLY n 
2 30  HIS n 
2 31  PHE n 
2 32  ILE n 
2 33  TRP n 
2 34  ALA n 
2 35  ASN n 
2 36  VAL n 
2 37  PHE n 
2 38  LYS n 
2 39  VAL n 
2 40  ALA n 
2 41  PRO n 
2 42  SER n 
2 43  ALA n 
2 44  ARG n 
2 45  ASP n 
2 46  MET n 
2 47  PHE n 
2 48  LYS n 
2 49  ARG n 
2 50  VAL n 
2 51  ARG n 
2 52  GLY n 
2 53  ASP n 
2 54  ASN n 
2 55  ILE n 
2 56  TYR n 
2 57  THR n 
2 58  PRO n 
2 59  ALA n 
2 60  PHE n 
2 61  ARG n 
2 62  ALA n 
2 63  HIS n 
2 64  ALA n 
2 65  THR n 
2 66  ARG n 
2 67  VAL n 
2 68  LEU n 
2 69  GLY n 
2 70  GLY n 
2 71  LEU n 
2 72  ASP n 
2 73  MET n 
2 74  CYS n 
2 75  VAL n 
2 76  ALA n 
2 77  LEU n 
2 78  LEU n 
2 79  ASP n 
2 80  ASP n 
2 81  GLU n 
2 82  SER n 
2 83  VAL n 
2 84  LEU n 
2 85  ASN n 
2 86  THR n 
2 87  GLN n 
2 88  LEU n 
2 89  ALA n 
2 90  HIS n 
2 91  LEU n 
2 92  ALA n 
2 93  SER n 
2 94  GLN n 
2 95  HIS n 
2 96  SER n 
2 97  SER n 
2 98  ARG n 
2 99  GLY n 
2 100 VAL n 
2 101 SER n 
2 102 ALA n 
2 103 GLU n 
2 104 GLN n 
2 105 TYR n 
2 106 ASN n 
2 107 VAL n 
2 108 VAL n 
2 109 GLU n 
2 110 HIS n 
2 111 ALA n 
2 112 VAL n 
2 113 MET n 
2 114 MET n 
2 115 GLY n 
2 116 VAL n 
2 117 GLU n 
2 118 HIS n 
2 119 GLU n 
2 120 ILE n 
2 121 GLY n 
2 122 GLN n 
2 123 ASN n 
2 124 VAL n 
2 125 PHE n 
2 126 ASP n 
2 127 LYS n 
2 128 ASP n 
2 129 ALA n 
2 130 TRP n 
2 131 GLN n 
2 132 ALA n 
2 133 CYS n 
2 134 LEU n 
2 135 ASP n 
2 136 VAL n 
2 137 ILE n 
2 138 THR n 
2 139 SER n 
2 140 GLY n 
2 141 ILE n 
2 142 GLN n 
2 143 GLY n 
2 144 ASN n 
3 1   SER n 
3 2   SER n 
3 3   ASN n 
3 4   SER n 
3 5   CYS n 
3 6   THR n 
3 7   THR n 
3 8   GLU n 
3 9   ASP n 
3 10  ARG n 
3 11  ARG n 
3 12  GLU n 
3 13  MET n 
3 14  GLN n 
3 15  LEU n 
3 16  MET n 
3 17  TRP n 
3 18  ALA n 
3 19  ASN n 
3 20  VAL n 
3 21  TRP n 
3 22  SER n 
3 23  ALA n 
3 24  GLN n 
3 25  PHE n 
3 26  THR n 
3 27  GLY n 
3 28  ARG n 
3 29  ARG n 
3 30  LEU n 
3 31  ALA n 
3 32  ILE n 
3 33  ALA n 
3 34  GLN n 
3 35  ALA n 
3 36  VAL n 
3 37  PHE n 
3 38  LYS n 
3 39  ASP n 
3 40  LEU n 
3 41  PHE n 
3 42  ALA n 
3 43  HIS n 
3 44  VAL n 
3 45  PRO n 
3 46  ASP n 
3 47  ALA n 
3 48  VAL n 
3 49  GLY n 
3 50  LEU n 
3 51  PHE n 
3 52  ASP n 
3 53  ARG n 
3 54  VAL n 
3 55  HIS n 
3 56  GLY n 
3 57  THR n 
3 58  GLU n 
3 59  ILE n 
3 60  ASP n 
3 61  SER n 
3 62  SER n 
3 63  GLU n 
3 64  PHE n 
3 65  LYS n 
3 66  ALA n 
3 67  HIS n 
3 68  CYS n 
3 69  ILE n 
3 70  ARG n 
3 71  VAL n 
3 72  VAL n 
3 73  ASN n 
3 74  GLY n 
3 75  LEU n 
3 76  ASP n 
3 77  SER n 
3 78  ALA n 
3 79  ILE n 
3 80  GLY n 
3 81  LEU n 
3 82  LEU n 
3 83  SER n 
3 84  ASP n 
3 85  PRO n 
3 86  SER n 
3 87  THR n 
3 88  LEU n 
3 89  ASN n 
3 90  GLU n 
3 91  GLN n 
3 92  LEU n 
3 93  SER n 
3 94  HIS n 
3 95  LEU n 
3 96  ALA n 
3 97  THR n 
3 98  GLN n 
3 99  HIS n 
3 100 GLN n 
3 101 GLU n 
3 102 ARG n 
3 103 ALA n 
3 104 GLY n 
3 105 VAL n 
3 106 THR n 
3 107 LYS n 
3 108 GLY n 
3 109 GLY n 
3 110 PHE n 
3 111 SER n 
3 112 ALA n 
3 113 ILE n 
3 114 ALA n 
3 115 GLN n 
3 116 SER n 
3 117 PHE n 
3 118 LEU n 
3 119 ARG n 
3 120 VAL n 
3 121 MET n 
3 122 PRO n 
3 123 GLN n 
3 124 VAL n 
3 125 ALA n 
3 126 SER n 
3 127 CYS n 
3 128 PHE n 
3 129 ASN n 
3 130 PRO n 
3 131 ASP n 
3 132 ALA n 
3 133 TRP n 
3 134 SER n 
3 135 ARG n 
3 136 CYS n 
3 137 PHE n 
3 138 ASN n 
3 139 ARG n 
3 140 ILE n 
3 141 THR n 
3 142 ASN n 
3 143 GLY n 
3 144 MET n 
3 145 THR n 
3 146 GLU n 
3 147 GLY n 
3 148 LEU n 
3 149 ALA n 
3 150 GLU n 
4 1   SER n 
4 2   GLU n 
4 3   PHE n 
4 4   CYS n 
4 5   SER n 
4 6   GLU n 
4 7   ALA n 
4 8   ASP n 
4 9   ALA n 
4 10  THR n 
4 11  ILE n 
4 12  VAL n 
4 13  ILE n 
4 14  LYS n 
4 15  GLN n 
4 16  TRP n 
4 17  ASN n 
4 18  GLN n 
4 19  ILE n 
4 20  TYR n 
4 21  ASN n 
4 22  ALA n 
4 23  GLY n 
4 24  ILE n 
4 25  GLY n 
4 26  ALA n 
4 27  LYS n 
4 28  SER n 
4 29  ARG n 
4 30  TRP n 
4 31  THR n 
4 32  MET n 
4 33  GLY n 
4 34  ASN n 
4 35  GLU n 
4 36  ILE n 
4 37  PHE n 
4 38  SER n 
4 39  SER n 
4 40  LEU n 
4 41  PHE n 
4 42  LYS n 
4 43  LEU n 
4 44  LYS n 
4 45  PRO n 
4 46  GLU n 
4 47  SER n 
4 48  GLU n 
4 49  VAL n 
4 50  LEU n 
4 51  PHE n 
4 52  ASN n 
4 53  ASN n 
4 54  VAL n 
4 55  ASN n 
4 56  VAL n 
4 57  ALA n 
4 58  ASN n 
4 59  MET n 
4 60  SER n 
4 61  SER n 
4 62  GLY n 
4 63  ALA n 
4 64  PHE n 
4 65  HIS n 
4 66  ALA n 
4 67  HIS n 
4 68  THR n 
4 69  VAL n 
4 70  ARG n 
4 71  VAL n 
4 72  LEU n 
4 73  SER n 
4 74  GLY n 
4 75  LEU n 
4 76  ASP n 
4 77  MET n 
4 78  GLY n 
4 79  ILE n 
4 80  ASN n 
4 81  TYR n 
4 82  LEU n 
4 83  ASN n 
4 84  ASP n 
4 85  ALA n 
4 86  GLY n 
4 87  THR n 
4 88  LEU n 
4 89  THR n 
4 90  SER n 
4 91  LEU n 
4 92  THR n 
4 93  ALA n 
4 94  HIS n 
4 95  LEU n 
4 96  ALA n 
4 97  ALA n 
4 98  GLN n 
4 99  HIS n 
4 100 VAL n 
4 101 ALA n 
4 102 ARG n 
4 103 THR n 
4 104 GLY n 
4 105 LEU n 
4 106 LYS n 
4 107 ALA n 
4 108 VAL n 
4 109 TYR n 
4 110 PHE n 
4 111 ASP n 
4 112 ALA n 
4 113 MET n 
4 114 GLY n 
4 115 LYS n 
4 116 VAL n 
4 117 LEU n 
4 118 MET n 
4 119 THR n 
4 120 VAL n 
4 121 LEU n 
4 122 PRO n 
4 123 SER n 
4 124 LEU n 
4 125 ILE n 
4 126 ASP n 
4 127 ASN n 
4 128 PHE n 
4 129 ASN n 
4 130 PRO n 
4 131 ASP n 
4 132 ALA n 
4 133 TRP n 
4 134 ARG n 
4 135 ASN n 
4 136 CYS n 
4 137 LEU n 
4 138 LEU n 
4 139 PRO n 
4 140 LEU n 
4 141 LYS n 
4 142 ASN n 
4 143 ALA n 
4 144 ILE n 
4 145 ALA n 
4 146 LYS n 
4 147 GLY n 
4 148 LEU n 
4 149 PRO n 
# 
loop_
_entity_src_nat.entity_id 
_entity_src_nat.pdbx_src_id 
_entity_src_nat.pdbx_alt_source_flag 
_entity_src_nat.pdbx_beg_seq_num 
_entity_src_nat.pdbx_end_seq_num 
_entity_src_nat.common_name 
_entity_src_nat.pdbx_organism_scientific 
_entity_src_nat.pdbx_ncbi_taxonomy_id 
_entity_src_nat.genus 
_entity_src_nat.species 
_entity_src_nat.strain 
_entity_src_nat.tissue 
_entity_src_nat.tissue_fraction 
_entity_src_nat.pdbx_secretion 
_entity_src_nat.pdbx_fragment 
_entity_src_nat.pdbx_variant 
_entity_src_nat.pdbx_cell_line 
_entity_src_nat.pdbx_atcc 
_entity_src_nat.pdbx_cellular_location 
_entity_src_nat.pdbx_organ 
_entity_src_nat.pdbx_organelle 
_entity_src_nat.pdbx_cell 
_entity_src_nat.pdbx_plasmid_name 
_entity_src_nat.pdbx_plasmid_details 
_entity_src_nat.details 
1 1 sample ? ? 'Hydrothermal vent tubeworm' 'Lamellibrachia satsuma' 104711 ? ? ? blood ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample ? ? 'Hydrothermal vent tubeworm' 'Lamellibrachia satsuma' 104711 ? ? ? blood ? ? ? ? ? ? ? ? ? ? ? ? ? 
3 1 sample ? ? 'Hydrothermal vent tubeworm' 'Lamellibrachia satsuma' 104711 ? ? ? blood ? ? ? ? ? ? ? ? ? ? ? ? ? 
4 1 sample ? ? 'Hydrothermal vent tubeworm' 'Lamellibrachia satsuma' 104711 ? ? ? blood ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.entity_id 
_struct_ref.pdbx_align_begin 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_db_isoform 
1 UNP S0BBU7_LAMSA S0BBU7 1 20 
;DCNILQRLKVKMQWAKAYGFGTERAKFGNSLWTSIFNYAPDARDLFKSVKSEDMRSPQFKAHIARVIGGLDRVISMFDNE
DALNADLEHLKSQHDPRGLDALNFVVFGKALFATVGGQFGVCFDLPAWESCYKVIAMGITGNDMFS
;
? 
2 UNP S0BBR6_LAMSA S0BBR6 2 17 
;SECGPLQRLKVKRQWAEAYGSGNGREEFGHFIWANVFKVAPSARDMFKRVRGDNIYTPAFRAHATRVLGGLDMCVALLDD
ESVLNTQLAHLASQHSSRGVSAEQYNVVEHAVMMGVEHEIGQNVFDKDAWQACLDVITSGIQGN
;
? 
3 UNP S0BCU7_LAMSA S0BCU7 3 17 
;SSNSCTTEDRREMQLMWANVWSAQFTGRRLAIAQAVFKDLFAHVPDAVGLFDRVHGTEIDSSEFKAHCIRVVNGLDSAIG
LLSDPSTLNEQLSHLATQHQERAGVTKGGFSAIAQSFLRVMPQVASCFNPDAWSRCFNRITNGMTEGLAE
;
? 
4 UNP S0BAP9_LAMSA S0BAP9 4 20 
;SEFCSEADATIVIKQWNQIYNAGIGAKSRWTMGNEIFSSLFKLKPESEVLFNNVNVANMSSGAFHAHTVRVLSGLDMGIN
YLNDAGTLTSLTAHLAAQHVARTGLKAVYFDAMGKVLMTVLPSLIDNFNPDAWRNCLLPLKNAIAKGLP
;
? 
# 
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 3WCV A 1 ? 146 ? S0BBU7 20 ? 165 ? 1 146 
2 2 3WCV B 1 ? 144 ? S0BBR6 17 ? 160 ? 1 144 
3 3 3WCV C 1 ? 150 ? S0BCU7 17 ? 166 ? 1 150 
4 4 3WCV D 1 ? 149 ? S0BAP9 20 ? 168 ? 1 149 
5 1 3WCV E 1 ? 146 ? S0BBU7 20 ? 165 ? 1 146 
6 2 3WCV F 1 ? 144 ? S0BBR6 17 ? 160 ? 1 144 
7 3 3WCV G 1 ? 150 ? S0BCU7 17 ? 166 ? 1 150 
8 4 3WCV H 1 ? 149 ? S0BAP9 20 ? 168 ? 1 149 
# 
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 
CA  non-polymer         . 'CALCIUM ION'                     ?    'Ca 2'             40.078  
CYS 'L-peptide linking' y CYSTEINE                          ?    'C3 H7 N O2 S'     121.158 
FUC saccharide          . ALPHA-L-FUCOSE                    ?    'C6 H12 O5'        164.156 
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  
HEM non-polymer         . 'PROTOPORPHYRIN IX CONTAINING FE' HEME 'C34 H32 Fe N4 O4' 616.487 
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 
MAN D-saccharide        . ALPHA-D-MANNOSE                   ?    'C6 H12 O6'        180.156 
MET 'L-peptide linking' y METHIONINE                        ?    'C5 H11 N O2 S'    149.211 
NAG D-saccharide        . N-ACETYL-D-GLUCOSAMINE            ?    'C8 H15 N O6'      221.208 
OXY non-polymer         . 'OXYGEN MOLECULE'                 ?    O2                 31.999  
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 
# 
_exptl.entry_id          3WCV 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.57 
_exptl_crystal.density_percent_sol   52.09 
_exptl_crystal.description           ? 
_exptl_crystal.F_000                 ? 
_exptl_crystal.preparation           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.temp            293 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              7.5 
_exptl_crystal_grow.pdbx_details    
'13-18% PEG 3350, 0-5mM Ca acetate/Mg acetate, 100mM HEPES-NaOH, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K' 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           90 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               CCD 
_diffrn_detector.type                   'RAYONIX MX225HE' 
_diffrn_detector.pdbx_collection_date   2009-10-12 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    'Rotated-inclined double-crystal monochromator, Si (111)' 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.0000 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'SPRING-8 BEAMLINE BL41XU' 
_diffrn_source.pdbx_synchrotron_site       SPring-8 
_diffrn_source.pdbx_synchrotron_beamline   BL41XU 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_wavelength_list        1.0000 
# 
_reflns.entry_id                     3WCV 
_reflns.observed_criterion_sigma_I   -3.0 
_reflns.observed_criterion_sigma_F   0 
_reflns.d_resolution_low             50 
_reflns.d_resolution_high            2.60 
_reflns.number_obs                   40209 
_reflns.number_all                   40209 
_reflns.percent_possible_obs         99.9 
_reflns.pdbx_Rmerge_I_obs            ? 
_reflns.pdbx_Rsym_value              0.065 
_reflns.pdbx_netI_over_sigmaI        22.9 
_reflns.B_iso_Wilson_estimate        54.8 
_reflns.pdbx_redundancy              5.7 
_reflns.R_free_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.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.pdbx_chi_squared             ? 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_ordinal                 1 
_reflns.pdbx_diffrn_id               1 
# 
_reflns_shell.d_res_high                  2.60 
_reflns_shell.d_res_low                   2.69 
_reflns_shell.percent_possible_all        100 
_reflns_shell.Rmerge_I_obs                ? 
_reflns_shell.pdbx_Rsym_value             0.337 
_reflns_shell.meanI_over_sigI_obs         5.1 
_reflns_shell.pdbx_redundancy             5.6 
_reflns_shell.percent_possible_obs        ? 
_reflns_shell.number_unique_all           3997 
_reflns_shell.number_measured_all         ? 
_reflns_shell.number_measured_obs         ? 
_reflns_shell.number_unique_obs           ? 
_reflns_shell.pdbx_chi_squared            ? 
_reflns_shell.pdbx_rejects                ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs   ? 
_reflns_shell.number_possible             ? 
_reflns_shell.Rmerge_F_all                ? 
_reflns_shell.Rmerge_F_obs                ? 
_reflns_shell.Rmerge_I_all                ? 
_reflns_shell.meanI_over_sigI_all         ? 
_reflns_shell.pdbx_Rrim_I_all             ? 
_reflns_shell.pdbx_Rpim_I_all             ? 
_reflns_shell.pdbx_ordinal                1 
_reflns_shell.pdbx_diffrn_id              1 
# 
_refine.entry_id                                 3WCV 
_refine.ls_number_reflns_obs                     40167 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.0 
_refine.pdbx_data_cutoff_high_absF               2813630.66 
_refine.pdbx_data_cutoff_low_absF                0.000000 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             36.33 
_refine.ls_d_res_high                            2.60 
_refine.ls_percent_reflns_obs                    99.8 
_refine.ls_R_factor_obs                          0.235 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.235 
_refine.ls_R_factor_R_free                       0.267 
_refine.ls_R_factor_R_free_error                 0.006 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.1 
_refine.ls_number_reflns_R_free                  2037 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.B_iso_mean                               61.7216 
_refine.solvent_model_param_bsol                 31.5345 
_refine.solvent_model_param_ksol                 0.3000 
_refine.aniso_B[1][1]                            -4.38 
_refine.aniso_B[2][2]                            -4.38 
_refine.aniso_B[3][3]                            8.76 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            0.00 
_refine.aniso_B[2][3]                            0.00 
_refine.solvent_model_details                    'FLAT MODEL' 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  'BULK SOLVENT MODEL USED' 
_refine.pdbx_starting_model                      3WCT 
_refine.pdbx_method_to_determine_struct          'FOURIER SYNTHESIS' 
_refine.pdbx_isotropic_thermal_model             RESTRAINED 
_refine.pdbx_stereochemistry_target_values       'Engh & Huber' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.B_iso_min                                ? 
_refine.B_iso_max                                ? 
_refine.overall_SU_R_free                        ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_analyze.entry_id                        3WCV 
_refine_analyze.Luzzati_coordinate_error_obs    0.38 
_refine_analyze.Luzzati_sigma_a_obs             0.45 
_refine_analyze.Luzzati_d_res_low_obs           5.00 
_refine_analyze.Luzzati_coordinate_error_free   0.45 
_refine_analyze.Luzzati_sigma_a_free            0.59 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
_refine_analyze.pdbx_Luzzati_d_res_high_obs     ? 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        9117 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         508 
_refine_hist.number_atoms_solvent             59 
_refine_hist.number_atoms_total               9684 
_refine_hist.d_res_high                       2.60 
_refine_hist.d_res_low                        36.33 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.type 
_refine_ls_restr.number 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' c_bond_d           ? 0.010  ?     ? ? 
'X-RAY DIFFRACTION' c_angle_deg        ? 1.300  ?     ? ? 
'X-RAY DIFFRACTION' c_dihedral_angle_d ? 18.200 ?     ? ? 
'X-RAY DIFFRACTION' c_improper_angle_d ? 0.870  ?     ? ? 
'X-RAY DIFFRACTION' c_mcbond_it        ? 1.560  1.500 ? ? 
'X-RAY DIFFRACTION' c_mcangle_it       ? 2.740  2.000 ? ? 
'X-RAY DIFFRACTION' c_scbond_it        ? 2.070  2.000 ? ? 
'X-RAY DIFFRACTION' c_scangle_it       ? 3.180  2.500 ? ? 
# 
_refine_ls_shell.d_res_high                       2.6000 
_refine_ls_shell.d_res_low                        2.6900 
_refine_ls_shell.pdbx_total_number_of_bins_used   10 
_refine_ls_shell.percent_reflns_obs               100.0000 
_refine_ls_shell.number_reflns_R_work             3786 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_R_work                  0.3320 
_refine_ls_shell.R_factor_R_free                  0.3790 
_refine_ls_shell.percent_reflns_R_free            5.2000 
_refine_ls_shell.number_reflns_R_free             208 
_refine_ls_shell.R_factor_R_free_error            0.0260 
_refine_ls_shell.number_reflns_all                3994 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.redundancy_reflns_obs            ? 
# 
loop_
_pdbx_xplor_file.pdbx_refine_id 
_pdbx_xplor_file.serial_no 
_pdbx_xplor_file.param_file 
_pdbx_xplor_file.topol_file 
'X-RAY DIFFRACTION' 1 protein_rep.param  protein.top      
'X-RAY DIFFRACTION' 2 hem_o2.param       hem_o2.top       
'X-RAY DIFFRACTION' 3 ca_patch.param     ca_patch_4.top   
'X-RAY DIFFRACTION' 4 carbohydrate.param carbohydrate.top 
'X-RAY DIFFRACTION' 5 water_rep.param    water.top        
# 
_struct.entry_id                  3WCV 
_struct.title                     
;The structure of a deoxygenated 400 kda hemoglobin provides a more accurate description of the cooperative mechanism of giant hemoglobins: CA bound form
;
_struct.pdbx_descriptor           
;A1 globin chain of giant V2 hemoglobin, A2 globin chain of giant V2 hemoglobin, B2 globin chain of giant V2 hemoglobin, B1 globin chain of giant V2 hemoglobin
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        3WCV 
_struct_keywords.pdbx_keywords   'OXYGEN TRANSPORT' 
_struct_keywords.text            'globin fold, oxygen transport, oxygen binding, blood' 
# 
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 1  ? 
F  N N 2  ? 
G  N N 3  ? 
H  N N 4  ? 
I  N N 5  ? 
J  N N 6  ? 
K  N N 7  ? 
L  N N 5  ? 
M  N N 6  ? 
N  N N 7  ? 
O  N N 7  ? 
P  N N 5  ? 
Q  N N 6  ? 
R  N N 5  ? 
S  N N 6  ? 
T  N N 8  ? 
U  N N 8  ? 
V  N N 9  ? 
W  N N 9  ? 
X  N N 9  ? 
Y  N N 10 ? 
Z  N N 5  ? 
AA N N 6  ? 
BA N N 5  ? 
CA N N 6  ? 
DA N N 7  ? 
EA N N 7  ? 
FA N N 7  ? 
GA N N 5  ? 
HA N N 6  ? 
IA N N 5  ? 
JA N N 6  ? 
KA N N 8  ? 
LA N N 8  ? 
MA N N 9  ? 
NA N N 9  ? 
OA N N 9  ? 
PA N N 10 ? 
QA N N 11 ? 
RA N N 11 ? 
SA N N 11 ? 
TA N N 11 ? 
UA N N 11 ? 
VA N N 11 ? 
WA N N 11 ? 
XA N N 11 ? 
# 
_struct_biol.id        1 
_struct_biol.details   ? 
# 
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  1  ASN A 3   ? GLY A 19  ? ASN A 3   GLY A 19  1 ? 17 
HELX_P HELX_P2  2  THR A 22  ? ALA A 39  ? THR A 22  ALA A 39  1 ? 18 
HELX_P HELX_P3  3  PRO A 40  ? LYS A 50  ? PRO A 40  LYS A 50  5 ? 11 
HELX_P HELX_P4  4  SER A 56  ? MET A 76  ? SER A 56  MET A 76  1 ? 21 
HELX_P HELX_P5  5  ASN A 79  ? ASP A 95  ? ASN A 79  ASP A 95  1 ? 17 
HELX_P HELX_P6  6  PRO A 96  ? GLY A 98  ? PRO A 96  GLY A 98  5 ? 3  
HELX_P HELX_P7  7  ALA A 101 ? GLY A 120 ? ALA A 101 GLY A 120 1 ? 20 
HELX_P HELX_P8  8  ASP A 124 ? GLY A 141 ? ASP A 124 GLY A 141 1 ? 18 
HELX_P HELX_P9  9  GLY B 4   ? GLY B 20  ? GLY B 4   GLY B 20  1 ? 17 
HELX_P HELX_P10 10 GLY B 24  ? ALA B 40  ? GLY B 24  ALA B 40  1 ? 17 
HELX_P HELX_P11 11 PRO B 41  ? ARG B 51  ? PRO B 41  ARG B 51  5 ? 11 
HELX_P HELX_P12 12 THR B 57  ? LEU B 78  ? THR B 57  LEU B 78  1 ? 22 
HELX_P HELX_P13 13 ASP B 80  ? SER B 96  ? ASP B 80  SER B 96  1 ? 17 
HELX_P HELX_P14 14 SER B 97  ? GLY B 99  ? SER B 97  GLY B 99  5 ? 3  
HELX_P HELX_P15 15 SER B 101 ? GLY B 121 ? SER B 101 GLY B 121 1 ? 21 
HELX_P HELX_P16 16 ASP B 126 ? GLN B 142 ? ASP B 126 GLN B 142 1 ? 17 
HELX_P HELX_P17 17 THR C 6   ? TRP C 21  ? THR C 6   TRP C 21  1 ? 16 
HELX_P HELX_P18 18 PHE C 25  ? VAL C 44  ? PHE C 25  VAL C 44  1 ? 20 
HELX_P HELX_P19 19 PRO C 45  ? HIS C 55  ? PRO C 45  HIS C 55  5 ? 11 
HELX_P HELX_P20 20 SER C 61  ? LEU C 82  ? SER C 61  LEU C 82  1 ? 22 
HELX_P HELX_P21 21 ASP C 84  ? GLN C 100 ? ASP C 84  GLN C 100 1 ? 17 
HELX_P HELX_P22 22 THR C 106 ? ALA C 125 ? THR C 106 ALA C 125 1 ? 20 
HELX_P HELX_P23 23 ASN C 129 ? THR C 145 ? ASN C 129 THR C 145 1 ? 17 
HELX_P HELX_P24 24 SER D 5   ? TYR D 20  ? SER D 5   TYR D 20  1 ? 16 
HELX_P HELX_P25 25 GLY D 25  ? LYS D 44  ? GLY D 25  LYS D 44  1 ? 20 
HELX_P HELX_P26 26 PRO D 45  ? ASN D 55  ? PRO D 45  ASN D 55  5 ? 11 
HELX_P HELX_P27 27 SER D 61  ? ASN D 80  ? SER D 61  ASN D 80  1 ? 20 
HELX_P HELX_P28 28 ASP D 84  ? ALA D 101 ? ASP D 84  ALA D 101 1 ? 18 
HELX_P HELX_P29 29 LYS D 106 ? ILE D 125 ? LYS D 106 ILE D 125 1 ? 20 
HELX_P HELX_P30 30 ASN D 129 ? ALA D 145 ? ASN D 129 ALA D 145 1 ? 17 
HELX_P HELX_P31 31 ASN E 3   ? GLY E 19  ? ASN E 3   GLY E 19  1 ? 17 
HELX_P HELX_P32 32 THR E 22  ? ALA E 39  ? THR E 22  ALA E 39  1 ? 18 
HELX_P HELX_P33 33 ASP E 41  ? LYS E 50  ? ASP E 41  LYS E 50  5 ? 10 
HELX_P HELX_P34 34 SER E 56  ? MET E 76  ? SER E 56  MET E 76  1 ? 21 
HELX_P HELX_P35 35 ASN E 79  ? ASP E 95  ? ASN E 79  ASP E 95  1 ? 17 
HELX_P HELX_P36 36 PRO E 96  ? GLY E 98  ? PRO E 96  GLY E 98  5 ? 3  
HELX_P HELX_P37 37 ALA E 101 ? GLY E 120 ? ALA E 101 GLY E 120 1 ? 20 
HELX_P HELX_P38 38 ASP E 124 ? GLY E 141 ? ASP E 124 GLY E 141 1 ? 18 
HELX_P HELX_P39 39 ASN E 142 ? SER E 146 ? ASN E 142 SER E 146 5 ? 5  
HELX_P HELX_P40 40 GLY F 4   ? GLY F 20  ? GLY F 4   GLY F 20  1 ? 17 
HELX_P HELX_P41 41 GLY F 24  ? ALA F 40  ? GLY F 24  ALA F 40  1 ? 17 
HELX_P HELX_P42 42 PRO F 41  ? MET F 46  ? PRO F 41  MET F 46  5 ? 6  
HELX_P HELX_P43 43 PHE F 47  ? ARG F 51  ? PHE F 47  ARG F 51  5 ? 5  
HELX_P HELX_P44 44 THR F 57  ? LEU F 78  ? THR F 57  LEU F 78  1 ? 22 
HELX_P HELX_P45 45 ASP F 80  ? SER F 96  ? ASP F 80  SER F 96  1 ? 17 
HELX_P HELX_P46 46 SER F 97  ? GLY F 99  ? SER F 97  GLY F 99  5 ? 3  
HELX_P HELX_P47 47 SER F 101 ? GLY F 121 ? SER F 101 GLY F 121 1 ? 21 
HELX_P HELX_P48 48 ASP F 126 ? GLN F 142 ? ASP F 126 GLN F 142 1 ? 17 
HELX_P HELX_P49 49 THR G 6   ? VAL G 20  ? THR G 6   VAL G 20  1 ? 15 
HELX_P HELX_P50 50 THR G 26  ? VAL G 44  ? THR G 26  VAL G 44  1 ? 19 
HELX_P HELX_P51 51 ASP G 46  ? HIS G 55  ? ASP G 46  HIS G 55  5 ? 10 
HELX_P HELX_P52 52 SER G 61  ? LEU G 81  ? SER G 61  LEU G 81  1 ? 21 
HELX_P HELX_P53 53 ASP G 84  ? GLN G 100 ? ASP G 84  GLN G 100 1 ? 17 
HELX_P HELX_P54 54 THR G 106 ? ALA G 125 ? THR G 106 ALA G 125 1 ? 20 
HELX_P HELX_P55 55 ASN G 129 ? THR G 145 ? ASN G 129 THR G 145 1 ? 17 
HELX_P HELX_P56 56 SER H 5   ? TYR H 20  ? SER H 5   TYR H 20  1 ? 16 
HELX_P HELX_P57 57 GLY H 25  ? LYS H 44  ? GLY H 25  LYS H 44  1 ? 20 
HELX_P HELX_P58 58 PRO H 45  ? ASN H 55  ? PRO H 45  ASN H 55  5 ? 11 
HELX_P HELX_P59 59 SER H 61  ? TYR H 81  ? SER H 61  TYR H 81  1 ? 21 
HELX_P HELX_P60 60 ASP H 84  ? ALA H 101 ? ASP H 84  ALA H 101 1 ? 18 
HELX_P HELX_P61 61 LYS H 106 ? LEU H 121 ? LYS H 106 LEU H 121 1 ? 16 
HELX_P HELX_P62 62 PRO H 122 ? LEU H 124 ? PRO H 122 LEU H 124 5 ? 3  
HELX_P HELX_P63 63 ASN H 129 ? ALA H 145 ? ASN H 129 ALA H 145 1 ? 17 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
disulf1  disulf ? ? A  CYS 2   SG  ? ? ? 1_555 A  CYS 131 SG ? ? A CYS 2   A CYS 131 1_555 ? ? ? ? ? ? ? 2.028 ? 
disulf2  disulf ? ? A  CYS 122 SG  ? ? ? 1_555 C  CYS 127 SG ? ? A CYS 122 C CYS 127 1_555 ? ? ? ? ? ? ? 2.038 ? 
disulf3  disulf ? ? B  CYS 3   SG  ? ? ? 1_555 B  CYS 133 SG ? ? B CYS 3   B CYS 133 1_555 ? ? ? ? ? ? ? 2.047 ? 
disulf4  disulf ? ? C  CYS 5   SG  ? ? ? 1_555 C  CYS 136 SG ? ? C CYS 5   C CYS 136 1_555 ? ? ? ? ? ? ? 2.043 ? 
disulf5  disulf ? ? D  CYS 4   SG  ? ? ? 1_555 D  CYS 136 SG ? ? D CYS 4   D CYS 136 1_555 ? ? ? ? ? ? ? 2.041 ? 
disulf6  disulf ? ? E  CYS 2   SG  ? ? ? 1_555 E  CYS 131 SG ? ? E CYS 2   E CYS 131 1_555 ? ? ? ? ? ? ? 2.033 ? 
disulf7  disulf ? ? E  CYS 122 SG  ? ? ? 1_555 G  CYS 127 SG ? ? E CYS 122 G CYS 127 1_555 ? ? ? ? ? ? ? 2.036 ? 
disulf8  disulf ? ? F  CYS 3   SG  ? ? ? 1_555 F  CYS 133 SG ? ? F CYS 3   F CYS 133 1_555 ? ? ? ? ? ? ? 2.044 ? 
disulf9  disulf ? ? G  CYS 5   SG  ? ? ? 1_555 G  CYS 136 SG ? ? G CYS 5   G CYS 136 1_555 ? ? ? ? ? ? ? 2.019 ? 
disulf10 disulf ? ? H  CYS 4   SG  ? ? ? 1_555 H  CYS 136 SG ? ? H CYS 4   H CYS 136 1_555 ? ? ? ? ? ? ? 2.022 ? 
covale1  covale ? ? U  NAG .   O4  ? ? ? 1_555 V  MAN .   C1 ? ? D NAG 204 D MAN 205 1_555 ? ? ? ? ? ? ? 1.382 ? 
covale2  covale ? ? T  NAG .   O4  ? ? ? 1_555 U  NAG .   C1 ? ? D NAG 203 D NAG 204 1_555 ? ? ? ? ? ? ? 1.384 ? 
covale3  covale ? ? KA NAG .   O4  ? ? ? 1_555 LA NAG .   C1 ? ? H NAG 203 H NAG 204 1_555 ? ? ? ? ? ? ? 1.386 ? 
covale4  covale ? ? KA NAG .   O6  ? ? ? 1_555 PA FUC .   C1 ? ? H NAG 203 H FUC 208 1_555 ? ? ? ? ? ? ? 1.390 ? 
covale5  covale ? ? LA NAG .   O4  ? ? ? 1_555 MA MAN .   C1 ? ? H NAG 204 H MAN 205 1_555 ? ? ? ? ? ? ? 1.393 ? 
covale6  covale ? ? T  NAG .   O6  ? ? ? 1_555 Y  FUC .   C1 ? ? D NAG 203 D FUC 208 1_555 ? ? ? ? ? ? ? 1.403 ? 
covale7  covale ? ? V  MAN .   O6  ? ? ? 1_555 X  MAN .   C1 ? ? D MAN 205 D MAN 207 1_555 ? ? ? ? ? ? ? 1.405 ? 
covale8  covale ? ? MA MAN .   O6  ? ? ? 1_555 OA MAN .   C1 ? ? H MAN 205 H MAN 207 1_555 ? ? ? ? ? ? ? 1.405 ? 
covale9  covale ? ? V  MAN .   O3  ? ? ? 1_555 W  MAN .   C1 ? ? D MAN 205 D MAN 206 1_555 ? ? ? ? ? ? ? 1.407 ? 
covale10 covale ? ? MA MAN .   O3  ? ? ? 1_555 NA MAN .   C1 ? ? H MAN 205 H MAN 206 1_555 ? ? ? ? ? ? ? 1.415 ? 
covale11 covale ? ? D  ASN 58  ND2 ? ? ? 1_555 T  NAG .   C1 ? ? D ASN 58  D NAG 203 1_555 ? ? ? ? ? ? ? 1.427 ? 
covale12 covale ? ? H  ASN 58  ND2 ? ? ? 1_555 KA NAG .   C1 ? ? H ASN 58  H NAG 203 1_555 ? ? ? ? ? ? ? 1.432 ? 
metalc1  metalc ? ? Z  HEM .   FE  ? ? ? 1_555 AA OXY .   O1 ? ? E HEM 200 E OXY 201 1_555 ? ? ? ? ? ? ? 1.781 ? 
metalc2  metalc ? ? R  HEM .   FE  ? ? ? 1_555 S  OXY .   O1 ? ? D HEM 201 D OXY 202 1_555 ? ? ? ? ? ? ? 1.785 ? 
metalc3  metalc ? ? BA HEM .   FE  ? ? ? 1_555 CA OXY .   O1 ? ? F HEM 201 F OXY 202 1_555 ? ? ? ? ? ? ? 1.789 ? 
metalc4  metalc ? ? P  HEM .   FE  ? ? ? 1_555 Q  OXY .   O1 ? ? C HEM 200 C OXY 201 1_555 ? ? ? ? ? ? ? 1.789 ? 
metalc5  metalc ? ? IA HEM .   FE  ? ? ? 1_555 JA OXY .   O1 ? ? H HEM 201 H OXY 202 1_555 ? ? ? ? ? ? ? 1.790 ? 
metalc6  metalc ? ? L  HEM .   FE  ? ? ? 1_555 M  OXY .   O1 ? ? B HEM 201 B OXY 202 1_555 ? ? ? ? ? ? ? 1.801 ? 
metalc7  metalc ? ? GA HEM .   FE  ? ? ? 1_555 HA OXY .   O1 ? ? G HEM 200 G OXY 201 1_555 ? ? ? ? ? ? ? 1.811 ? 
metalc8  metalc ? ? I  HEM .   FE  ? ? ? 1_555 J  OXY .   O1 ? ? A HEM 201 A OXY 202 1_555 ? ? ? ? ? ? ? 1.874 ? 
metalc9  metalc ? ? D  HIS 99  NE2 ? ? ? 1_555 R  HEM .   FE ? ? D HIS 99  D HEM 201 1_555 ? ? ? ? ? ? ? 2.082 ? 
metalc10 metalc ? ? G  HIS 99  NE2 ? ? ? 1_555 GA HEM .   FE ? ? G HIS 99  G HEM 200 1_555 ? ? ? ? ? ? ? 2.089 ? 
metalc11 metalc ? ? C  HIS 99  NE2 ? ? ? 1_555 P  HEM .   FE ? ? C HIS 99  C HEM 200 1_555 ? ? ? ? ? ? ? 2.098 ? 
metalc12 metalc ? ? F  HIS 95  NE2 ? ? ? 1_555 BA HEM .   FE ? ? F HIS 95  F HEM 201 1_555 ? ? ? ? ? ? ? 2.128 ? 
metalc13 metalc ? ? B  HIS 95  NE2 ? ? ? 1_555 L  HEM .   FE ? ? B HIS 95  B HEM 201 1_555 ? ? ? ? ? ? ? 2.129 ? 
metalc14 metalc ? ? H  HIS 99  NE2 ? ? ? 1_555 IA HEM .   FE ? ? H HIS 99  H HEM 201 1_555 ? ? ? ? ? ? ? 2.130 ? 
metalc15 metalc ? ? E  HIS 94  NE2 ? ? ? 1_555 Z  HEM .   FE ? ? E HIS 94  E HEM 200 1_555 ? ? ? ? ? ? ? 2.136 ? 
metalc16 metalc ? ? A  HIS 94  NE2 ? ? ? 1_555 I  HEM .   FE ? ? A HIS 94  A HEM 201 1_555 ? ? ? ? ? ? ? 2.144 ? 
metalc17 metalc ? ? F  GLU 119 OE2 ? ? ? 1_555 EA CA  .   CA ? ? F GLU 119 F CA  204 1_555 ? ? ? ? ? ? ? 2.334 ? 
metalc18 metalc ? ? B  ASP 135 OD1 ? ? ? 1_555 N  CA  .   CA ? ? B ASP 135 B CA  203 1_555 ? ? ? ? ? ? ? 2.370 ? 
metalc19 metalc ? ? B  ASN 106 OD1 ? ? ? 1_555 N  CA  .   CA ? ? B ASN 106 B CA  203 1_555 ? ? ? ? ? ? ? 2.375 ? 
metalc20 metalc ? ? B  GLU 109 OE2 ? ? ? 1_555 N  CA  .   CA ? ? B GLU 109 B CA  203 1_555 ? ? ? ? ? ? ? 2.383 ? 
metalc21 metalc ? ? F  ASN 106 OD1 ? ? ? 1_555 DA CA  .   CA ? ? F ASN 106 F CA  203 1_555 ? ? ? ? ? ? ? 2.387 ? 
metalc22 metalc ? ? F  ASP 135 OD1 ? ? ? 1_555 DA CA  .   CA ? ? F ASP 135 F CA  203 1_555 ? ? ? ? ? ? ? 2.389 ? 
metalc23 metalc ? ? F  GLY 99  O   ? ? ? 1_555 FA CA  .   CA ? ? F GLY 99  F CA  205 1_555 ? ? ? ? ? ? ? 2.421 ? 
metalc24 metalc ? ? F  GLU 109 OE2 ? ? ? 1_555 DA CA  .   CA ? ? F GLU 109 F CA  203 1_555 ? ? ? ? ? ? ? 2.456 ? 
metalc25 metalc ? ? F  GLU 109 OE1 ? ? ? 1_555 DA CA  .   CA ? ? F GLU 109 F CA  203 1_555 ? ? ? ? ? ? ? 2.511 ? 
metalc26 metalc ? ? B  GLU 119 OE2 ? ? ? 1_555 O  CA  .   CA ? ? B GLU 119 B CA  204 1_555 ? ? ? ? ? ? ? 2.643 ? 
metalc27 metalc ? ? B  GLU 109 OE1 ? ? ? 1_555 N  CA  .   CA ? ? B GLU 109 B CA  203 1_555 ? ? ? ? ? ? ? 2.678 ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
metalc ? ? 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          SER 
_struct_mon_prot_cis.label_seq_id           1 
_struct_mon_prot_cis.label_asym_id          C 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           SER 
_struct_mon_prot_cis.auth_seq_id            1 
_struct_mon_prot_cis.auth_asym_id           C 
_struct_mon_prot_cis.pdbx_label_comp_id_2   SER 
_struct_mon_prot_cis.pdbx_label_seq_id_2    2 
_struct_mon_prot_cis.pdbx_label_asym_id_2   C 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    SER 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    C 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       0.29 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software ? ? ? ? 17 'BINDING SITE FOR RESIDUE HEM A 201'                                      
AC2 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE OXY A 202'                                      
AC3 Software ? ? ? ? 16 'BINDING SITE FOR RESIDUE HEM B 201'                                      
AC4 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE OXY B 202'                                      
AC5 Software ? ? ? ? 3  'BINDING SITE FOR RESIDUE CA B 203'                                       
AC6 Software ? ? ? ? 1  'BINDING SITE FOR RESIDUE CA B 204'                                       
AC7 Software ? ? ? ? 16 'BINDING SITE FOR RESIDUE HEM C 200'                                      
AC8 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE OXY C 201'                                      
AC9 Software ? ? ? ? 17 'BINDING SITE FOR RESIDUE HEM D 201'                                      
BC1 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE OXY D 202'                                      
BC2 Software ? ? ? ? 16 'BINDING SITE FOR RESIDUE HEM E 200'                                      
BC3 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE OXY E 201'                                      
BC4 Software ? ? ? ? 14 'BINDING SITE FOR RESIDUE HEM F 201'                                      
BC5 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE OXY F 202'                                      
BC6 Software ? ? ? ? 3  'BINDING SITE FOR RESIDUE CA F 203'                                       
BC7 Software ? ? ? ? 1  'BINDING SITE FOR RESIDUE CA F 204'                                       
BC8 Software ? ? ? ? 1  'BINDING SITE FOR RESIDUE CA F 205'                                       
BC9 Software ? ? ? ? 16 'BINDING SITE FOR RESIDUE HEM G 200'                                      
CC1 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE OXY G 201'                                      
CC2 Software ? ? ? ? 15 'BINDING SITE FOR RESIDUE HEM H 201'                                      
CC3 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE OXY H 202'                                      
CC4 Software ? ? ? ? 2  'BINDING SITE FOR CHAIN D OF SUGAR BOUND TO ASN D 58 RESIDUES 203 TO 208' 
CC5 Software ? ? ? ? 2  'BINDING SITE FOR CHAIN H OF SUGAR BOUND TO ASN H 58 RESIDUES 203 TO 208' 
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1   AC1 17 LEU A  45  ? LEU A 45  . ? 1_555 ? 
2   AC1 17 PHE A  46  ? PHE A 46  . ? 1_555 ? 
3   AC1 17 SER A  48  ? SER A 48  . ? 1_555 ? 
4   AC1 17 VAL A  49  ? VAL A 49  . ? 1_555 ? 
5   AC1 17 HIS A  62  ? HIS A 62  . ? 1_555 ? 
6   AC1 17 ARG A  65  ? ARG A 65  . ? 1_555 ? 
7   AC1 17 GLN A  93  ? GLN A 93  . ? 1_555 ? 
8   AC1 17 HIS A  94  ? HIS A 94  . ? 1_555 ? 
9   AC1 17 ARG A  97  ? ARG A 97  . ? 1_555 ? 
10  AC1 17 LEU A  99  ? LEU A 99  . ? 1_555 ? 
11  AC1 17 PHE A  104 ? PHE A 104 . ? 1_555 ? 
12  AC1 17 PHE A  107 ? PHE A 107 . ? 1_555 ? 
13  AC1 17 ILE A  139 ? ILE A 139 . ? 1_555 ? 
14  AC1 17 ASP A  143 ? ASP A 143 . ? 3_555 ? 
15  AC1 17 OXY J  .   ? OXY A 202 . ? 1_555 ? 
16  AC1 17 HIS D  94  ? HIS D 94  . ? 1_555 ? 
17  AC1 17 GLN D  98  ? GLN D 98  . ? 1_555 ? 
18  AC2 5  TRP A  32  ? TRP A 32  . ? 1_555 ? 
19  AC2 5  PHE A  46  ? PHE A 46  . ? 1_555 ? 
20  AC2 5  HIS A  62  ? HIS A 62  . ? 1_555 ? 
21  AC2 5  VAL A  66  ? VAL A 66  . ? 1_555 ? 
22  AC2 5  HEM I  .   ? HEM A 201 . ? 1_555 ? 
23  AC3 16 MET B  46  ? MET B 46  . ? 1_555 ? 
24  AC3 16 PHE B  47  ? PHE B 47  . ? 1_555 ? 
25  AC3 16 ARG B  49  ? ARG B 49  . ? 1_555 ? 
26  AC3 16 VAL B  50  ? VAL B 50  . ? 1_555 ? 
27  AC3 16 HIS B  63  ? HIS B 63  . ? 1_555 ? 
28  AC3 16 ARG B  66  ? ARG B 66  . ? 1_555 ? 
29  AC3 16 GLN B  94  ? GLN B 94  . ? 1_555 ? 
30  AC3 16 HIS B  95  ? HIS B 95  . ? 1_555 ? 
31  AC3 16 ARG B  98  ? ARG B 98  . ? 1_555 ? 
32  AC3 16 VAL B  100 ? VAL B 100 . ? 1_555 ? 
33  AC3 16 GLN B  104 ? GLN B 104 . ? 1_555 ? 
34  AC3 16 TYR B  105 ? TYR B 105 . ? 1_555 ? 
35  AC3 16 VAL B  108 ? VAL B 108 . ? 1_555 ? 
36  AC3 16 OXY M  .   ? OXY B 202 . ? 1_555 ? 
37  AC3 16 HIS C  94  ? HIS C 94  . ? 1_555 ? 
38  AC3 16 GLN C  98  ? GLN C 98  . ? 1_555 ? 
39  AC4 5  TRP B  33  ? TRP B 33  . ? 1_555 ? 
40  AC4 5  PHE B  47  ? PHE B 47  . ? 1_555 ? 
41  AC4 5  HIS B  63  ? HIS B 63  . ? 1_555 ? 
42  AC4 5  VAL B  67  ? VAL B 67  . ? 1_555 ? 
43  AC4 5  HEM L  .   ? HEM B 201 . ? 1_555 ? 
44  AC5 3  ASN B  106 ? ASN B 106 . ? 1_555 ? 
45  AC5 3  GLU B  109 ? GLU B 109 . ? 1_555 ? 
46  AC5 3  ASP B  135 ? ASP B 135 . ? 1_555 ? 
47  AC6 1  GLU B  119 ? GLU B 119 . ? 1_555 ? 
48  AC7 16 HIS B  90  ? HIS B 90  . ? 1_555 ? 
49  AC7 16 GLN B  94  ? GLN B 94  . ? 1_555 ? 
50  AC7 16 LEU C  50  ? LEU C 50  . ? 1_555 ? 
51  AC7 16 PHE C  51  ? PHE C 51  . ? 1_555 ? 
52  AC7 16 ARG C  53  ? ARG C 53  . ? 1_555 ? 
53  AC7 16 VAL C  54  ? VAL C 54  . ? 1_555 ? 
54  AC7 16 ARG C  70  ? ARG C 70  . ? 1_555 ? 
55  AC7 16 VAL C  71  ? VAL C 71  . ? 1_555 ? 
56  AC7 16 LEU C  75  ? LEU C 75  . ? 1_555 ? 
57  AC7 16 GLN C  98  ? GLN C 98  . ? 1_555 ? 
58  AC7 16 HIS C  99  ? HIS C 99  . ? 1_555 ? 
59  AC7 16 ARG C  102 ? ARG C 102 . ? 1_555 ? 
60  AC7 16 GLY C  109 ? GLY C 109 . ? 1_555 ? 
61  AC7 16 PHE C  110 ? PHE C 110 . ? 1_555 ? 
62  AC7 16 MET C  144 ? MET C 144 . ? 1_555 ? 
63  AC7 16 OXY Q  .   ? OXY C 201 . ? 1_555 ? 
64  AC8 5  PHE C  37  ? PHE C 37  . ? 1_555 ? 
65  AC8 5  PHE C  51  ? PHE C 51  . ? 1_555 ? 
66  AC8 5  HIS C  67  ? HIS C 67  . ? 1_555 ? 
67  AC8 5  VAL C  71  ? VAL C 71  . ? 1_555 ? 
68  AC8 5  HEM P  .   ? HEM C 200 . ? 1_555 ? 
69  AC9 17 HIS A  89  ? HIS A 89  . ? 1_555 ? 
70  AC9 17 GLN A  93  ? GLN A 93  . ? 1_555 ? 
71  AC9 17 LEU D  50  ? LEU D 50  . ? 1_555 ? 
72  AC9 17 PHE D  51  ? PHE D 51  . ? 1_555 ? 
73  AC9 17 ASN D  53  ? ASN D 53  . ? 1_555 ? 
74  AC9 17 VAL D  54  ? VAL D 54  . ? 1_555 ? 
75  AC9 17 HIS D  67  ? HIS D 67  . ? 1_555 ? 
76  AC9 17 ARG D  70  ? ARG D 70  . ? 1_555 ? 
77  AC9 17 VAL D  71  ? VAL D 71  . ? 1_555 ? 
78  AC9 17 GLN D  98  ? GLN D 98  . ? 1_555 ? 
79  AC9 17 HIS D  99  ? HIS D 99  . ? 1_555 ? 
80  AC9 17 ARG D  102 ? ARG D 102 . ? 1_555 ? 
81  AC9 17 TYR D  109 ? TYR D 109 . ? 1_555 ? 
82  AC9 17 PHE D  110 ? PHE D 110 . ? 1_555 ? 
83  AC9 17 MET D  113 ? MET D 113 . ? 1_555 ? 
84  AC9 17 OXY S  .   ? OXY D 202 . ? 1_555 ? 
85  AC9 17 HOH TA .   ? HOH D 309 . ? 1_555 ? 
86  BC1 5  PHE D  37  ? PHE D 37  . ? 1_555 ? 
87  BC1 5  PHE D  51  ? PHE D 51  . ? 1_555 ? 
88  BC1 5  HIS D  67  ? HIS D 67  . ? 1_555 ? 
89  BC1 5  VAL D  71  ? VAL D 71  . ? 1_555 ? 
90  BC1 5  HEM R  .   ? HEM D 201 . ? 1_555 ? 
91  BC2 16 LEU E  45  ? LEU E 45  . ? 1_555 ? 
92  BC2 16 PHE E  46  ? PHE E 46  . ? 1_555 ? 
93  BC2 16 SER E  48  ? SER E 48  . ? 1_555 ? 
94  BC2 16 VAL E  49  ? VAL E 49  . ? 1_555 ? 
95  BC2 16 ARG E  65  ? ARG E 65  . ? 1_555 ? 
96  BC2 16 GLN E  93  ? GLN E 93  . ? 1_555 ? 
97  BC2 16 HIS E  94  ? HIS E 94  . ? 1_555 ? 
98  BC2 16 ARG E  97  ? ARG E 97  . ? 1_555 ? 
99  BC2 16 PHE E  104 ? PHE E 104 . ? 1_555 ? 
100 BC2 16 PHE E  107 ? PHE E 107 . ? 1_555 ? 
101 BC2 16 TYR E  132 ? TYR E 132 . ? 1_555 ? 
102 BC2 16 ILE E  139 ? ILE E 139 . ? 1_555 ? 
103 BC2 16 OXY AA .   ? OXY E 201 . ? 1_555 ? 
104 BC2 16 HOH UA .   ? HOH E 302 . ? 1_555 ? 
105 BC2 16 HIS H  94  ? HIS H 94  . ? 1_555 ? 
106 BC2 16 GLN H  98  ? GLN H 98  . ? 1_555 ? 
107 BC3 5  TRP E  32  ? TRP E 32  . ? 1_555 ? 
108 BC3 5  PHE E  46  ? PHE E 46  . ? 1_555 ? 
109 BC3 5  HIS E  62  ? HIS E 62  . ? 1_555 ? 
110 BC3 5  VAL E  66  ? VAL E 66  . ? 1_555 ? 
111 BC3 5  HEM Z  .   ? HEM E 200 . ? 1_555 ? 
112 BC4 14 MET F  46  ? MET F 46  . ? 1_555 ? 
113 BC4 14 PHE F  47  ? PHE F 47  . ? 1_555 ? 
114 BC4 14 ARG F  49  ? ARG F 49  . ? 1_555 ? 
115 BC4 14 HIS F  63  ? HIS F 63  . ? 1_555 ? 
116 BC4 14 ARG F  66  ? ARG F 66  . ? 1_555 ? 
117 BC4 14 HIS F  95  ? HIS F 95  . ? 1_555 ? 
118 BC4 14 ARG F  98  ? ARG F 98  . ? 1_555 ? 
119 BC4 14 VAL F  100 ? VAL F 100 . ? 1_555 ? 
120 BC4 14 GLN F  104 ? GLN F 104 . ? 1_555 ? 
121 BC4 14 TYR F  105 ? TYR F 105 . ? 1_555 ? 
122 BC4 14 VAL F  108 ? VAL F 108 . ? 1_555 ? 
123 BC4 14 OXY CA .   ? OXY F 202 . ? 1_555 ? 
124 BC4 14 HIS G  94  ? HIS G 94  . ? 1_555 ? 
125 BC4 14 GLN G  98  ? GLN G 98  . ? 1_555 ? 
126 BC5 5  TRP F  33  ? TRP F 33  . ? 1_555 ? 
127 BC5 5  PHE F  47  ? PHE F 47  . ? 1_555 ? 
128 BC5 5  HIS F  63  ? HIS F 63  . ? 1_555 ? 
129 BC5 5  VAL F  67  ? VAL F 67  . ? 1_555 ? 
130 BC5 5  HEM BA .   ? HEM F 201 . ? 1_555 ? 
131 BC6 3  ASN F  106 ? ASN F 106 . ? 1_555 ? 
132 BC6 3  GLU F  109 ? GLU F 109 . ? 1_555 ? 
133 BC6 3  ASP F  135 ? ASP F 135 . ? 1_555 ? 
134 BC7 1  GLU F  119 ? GLU F 119 . ? 1_555 ? 
135 BC8 1  GLY F  99  ? GLY F 99  . ? 1_555 ? 
136 BC9 16 HIS F  90  ? HIS F 90  . ? 1_555 ? 
137 BC9 16 GLN F  94  ? GLN F 94  . ? 1_555 ? 
138 BC9 16 LEU G  50  ? LEU G 50  . ? 1_555 ? 
139 BC9 16 PHE G  51  ? PHE G 51  . ? 1_555 ? 
140 BC9 16 ARG G  53  ? ARG G 53  . ? 1_555 ? 
141 BC9 16 VAL G  54  ? VAL G 54  . ? 1_555 ? 
142 BC9 16 HIS G  67  ? HIS G 67  . ? 1_555 ? 
143 BC9 16 ARG G  70  ? ARG G 70  . ? 1_555 ? 
144 BC9 16 GLN G  98  ? GLN G 98  . ? 1_555 ? 
145 BC9 16 HIS G  99  ? HIS G 99  . ? 1_555 ? 
146 BC9 16 ARG G  102 ? ARG G 102 . ? 1_555 ? 
147 BC9 16 GLY G  109 ? GLY G 109 . ? 1_555 ? 
148 BC9 16 PHE G  110 ? PHE G 110 . ? 1_555 ? 
149 BC9 16 ILE G  113 ? ILE G 113 . ? 1_555 ? 
150 BC9 16 MET G  144 ? MET G 144 . ? 1_555 ? 
151 BC9 16 OXY HA .   ? OXY G 201 . ? 1_555 ? 
152 CC1 5  PHE G  37  ? PHE G 37  . ? 1_555 ? 
153 CC1 5  PHE G  51  ? PHE G 51  . ? 1_555 ? 
154 CC1 5  HIS G  67  ? HIS G 67  . ? 1_555 ? 
155 CC1 5  VAL G  71  ? VAL G 71  . ? 1_555 ? 
156 CC1 5  HEM GA .   ? HEM G 200 . ? 1_555 ? 
157 CC2 15 HIS E  89  ? HIS E 89  . ? 1_555 ? 
158 CC2 15 GLN E  93  ? GLN E 93  . ? 1_555 ? 
159 CC2 15 LEU H  50  ? LEU H 50  . ? 1_555 ? 
160 CC2 15 PHE H  51  ? PHE H 51  . ? 1_555 ? 
161 CC2 15 ASN H  53  ? ASN H 53  . ? 1_555 ? 
162 CC2 15 VAL H  54  ? VAL H 54  . ? 1_555 ? 
163 CC2 15 HIS H  67  ? HIS H 67  . ? 1_555 ? 
164 CC2 15 ARG H  70  ? ARG H 70  . ? 1_555 ? 
165 CC2 15 VAL H  71  ? VAL H 71  . ? 1_555 ? 
166 CC2 15 GLN H  98  ? GLN H 98  . ? 1_555 ? 
167 CC2 15 HIS H  99  ? HIS H 99  . ? 1_555 ? 
168 CC2 15 ARG H  102 ? ARG H 102 . ? 1_555 ? 
169 CC2 15 TYR H  109 ? TYR H 109 . ? 1_555 ? 
170 CC2 15 PHE H  110 ? PHE H 110 . ? 1_555 ? 
171 CC2 15 OXY JA .   ? OXY H 202 . ? 1_555 ? 
172 CC3 5  PHE H  37  ? PHE H 37  . ? 1_555 ? 
173 CC3 5  PHE H  51  ? PHE H 51  . ? 1_555 ? 
174 CC3 5  HIS H  67  ? HIS H 67  . ? 1_555 ? 
175 CC3 5  VAL H  71  ? VAL H 71  . ? 1_555 ? 
176 CC3 5  HEM IA .   ? HEM H 201 . ? 1_555 ? 
177 CC4 2  ASN D  58  ? ASN D 58  . ? 1_555 ? 
178 CC4 2  SER D  61  ? SER D 61  . ? 1_555 ? 
179 CC5 2  ASN H  58  ? ASN H 58  . ? 1_555 ? 
180 CC5 2  SER H  61  ? SER H 61  . ? 1_555 ? 
# 
_database_PDB_matrix.entry_id          3WCV 
_database_PDB_matrix.origx[1][1]       1.000000 
_database_PDB_matrix.origx[1][2]       0.000000 
_database_PDB_matrix.origx[1][3]       0.000000 
_database_PDB_matrix.origx[2][1]       0.000000 
_database_PDB_matrix.origx[2][2]       1.000000 
_database_PDB_matrix.origx[2][3]       0.000000 
_database_PDB_matrix.origx[3][1]       0.000000 
_database_PDB_matrix.origx[3][2]       0.000000 
_database_PDB_matrix.origx[3][3]       1.000000 
_database_PDB_matrix.origx_vector[1]   0.00000 
_database_PDB_matrix.origx_vector[2]   0.00000 
_database_PDB_matrix.origx_vector[3]   0.00000 
# 
_atom_sites.entry_id                    3WCV 
_atom_sites.fract_transf_matrix[1][1]   0.009179 
_atom_sites.fract_transf_matrix[1][2]   0.005300 
_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]   0.010599 
_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]   0.005128 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
CA 
FE 
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . ASP A  1  1   ? 3.590  24.440  -13.451 1.00 76.25  ? 1   ASP A N   1 
ATOM   2    C  CA  . ASP A  1  1   ? 4.711  25.380  -13.735 1.00 75.38  ? 1   ASP A CA  1 
ATOM   3    C  C   . ASP A  1  1   ? 5.886  24.662  -14.416 1.00 72.04  ? 1   ASP A C   1 
ATOM   4    O  O   . ASP A  1  1   ? 5.678  23.751  -15.219 1.00 71.99  ? 1   ASP A O   1 
ATOM   5    C  CB  . ASP A  1  1   ? 5.189  26.028  -12.437 1.00 79.89  ? 1   ASP A CB  1 
ATOM   6    C  CG  . ASP A  1  1   ? 5.198  27.535  -12.515 1.00 83.14  ? 1   ASP A CG  1 
ATOM   7    O  OD1 . ASP A  1  1   ? 5.823  28.173  -11.637 1.00 84.41  ? 1   ASP A OD1 1 
ATOM   8    O  OD2 . ASP A  1  1   ? 4.570  28.082  -13.450 1.00 85.35  ? 1   ASP A OD2 1 
ATOM   9    N  N   . CYS A  1  2   ? 7.112  25.061  -14.062 1.00 65.66  ? 2   CYS A N   1 
ATOM   10   C  CA  . CYS A  1  2   ? 8.332  24.504  -14.644 1.00 59.48  ? 2   CYS A CA  1 
ATOM   11   C  C   . CYS A  1  2   ? 8.310  24.642  -16.163 1.00 57.08  ? 2   CYS A C   1 
ATOM   12   O  O   . CYS A  1  2   ? 8.267  23.651  -16.898 1.00 54.37  ? 2   CYS A O   1 
ATOM   13   C  CB  . CYS A  1  2   ? 8.540  23.026  -14.253 1.00 57.12  ? 2   CYS A CB  1 
ATOM   14   S  SG  . CYS A  1  2   ? 10.122 22.333  -14.849 1.00 52.27  ? 2   CYS A SG  1 
ATOM   15   N  N   . ASN A  1  3   ? 8.323  25.896  -16.606 1.00 56.16  ? 3   ASN A N   1 
ATOM   16   C  CA  . ASN A  1  3   ? 8.320  26.255  -18.020 1.00 56.00  ? 3   ASN A CA  1 
ATOM   17   C  C   . ASN A  1  3   ? 9.720  25.977  -18.506 1.00 53.54  ? 3   ASN A C   1 
ATOM   18   O  O   . ASN A  1  3   ? 10.545 25.535  -17.717 1.00 53.48  ? 3   ASN A O   1 
ATOM   19   C  CB  . ASN A  1  3   ? 8.002  27.729  -18.172 1.00 57.64  ? 3   ASN A CB  1 
ATOM   20   C  CG  . ASN A  1  3   ? 8.841  28.588  -17.256 1.00 60.00  ? 3   ASN A CG  1 
ATOM   21   O  OD1 . ASN A  1  3   ? 10.067 28.679  -17.412 1.00 60.21  ? 3   ASN A OD1 1 
ATOM   22   N  ND2 . ASN A  1  3   ? 8.189  29.219  -16.277 1.00 60.18  ? 3   ASN A ND2 1 
ATOM   23   N  N   . ILE A  1  4   ? 9.999  26.248  -19.774 1.00 51.40  ? 4   ILE A N   1 
ATOM   24   C  CA  . ILE A  1  4   ? 11.322 25.961  -20.320 1.00 50.43  ? 4   ILE A CA  1 
ATOM   25   C  C   . ILE A  1  4   ? 12.470 26.774  -19.731 1.00 49.18  ? 4   ILE A C   1 
ATOM   26   O  O   . ILE A  1  4   ? 13.589 26.274  -19.651 1.00 48.12  ? 4   ILE A O   1 
ATOM   27   C  CB  . ILE A  1  4   ? 11.332 26.098  -21.864 1.00 50.00  ? 4   ILE A CB  1 
ATOM   28   C  CG1 . ILE A  1  4   ? 12.722 25.743  -22.405 1.00 51.11  ? 4   ILE A CG1 1 
ATOM   29   C  CG2 . ILE A  1  4   ? 10.889 27.478  -22.259 1.00 46.47  ? 4   ILE A CG2 1 
ATOM   30   C  CD1 . ILE A  1  4   ? 12.822 25.752  -23.937 1.00 52.94  ? 4   ILE A CD1 1 
ATOM   31   N  N   . LEU A  1  5   ? 12.198 28.009  -19.312 1.00 48.83  ? 5   LEU A N   1 
ATOM   32   C  CA  . LEU A  1  5   ? 13.240 28.851  -18.725 1.00 49.11  ? 5   LEU A CA  1 
ATOM   33   C  C   . LEU A  1  5   ? 13.687 28.267  -17.380 1.00 49.71  ? 5   LEU A C   1 
ATOM   34   O  O   . LEU A  1  5   ? 14.880 28.183  -17.115 1.00 50.65  ? 5   LEU A O   1 
ATOM   35   C  CB  . LEU A  1  5   ? 12.740 30.291  -18.539 1.00 47.84  ? 5   LEU A CB  1 
ATOM   36   C  CG  . LEU A  1  5   ? 12.287 31.067  -19.787 1.00 46.42  ? 5   LEU A CG  1 
ATOM   37   C  CD1 . LEU A  1  5   ? 12.099 32.524  -19.420 1.00 44.98  ? 5   LEU A CD1 1 
ATOM   38   C  CD2 . LEU A  1  5   ? 13.303 30.953  -20.904 1.00 44.48  ? 5   LEU A CD2 1 
ATOM   39   N  N   . GLN A  1  6   ? 12.734 27.869  -16.540 1.00 49.86  ? 6   GLN A N   1 
ATOM   40   C  CA  . GLN A  1  6   ? 13.056 27.259  -15.254 1.00 50.13  ? 6   GLN A CA  1 
ATOM   41   C  C   . GLN A  1  6   ? 13.755 25.910  -15.445 1.00 49.31  ? 6   GLN A C   1 
ATOM   42   O  O   . GLN A  1  6   ? 14.582 25.522  -14.623 1.00 48.60  ? 6   GLN A O   1 
ATOM   43   C  CB  . GLN A  1  6   ? 11.788 27.078  -14.413 1.00 49.70  ? 6   GLN A CB  1 
ATOM   44   C  CG  . GLN A  1  6   ? 10.991 28.363  -14.300 1.00 53.28  ? 6   GLN A CG  1 
ATOM   45   C  CD  . GLN A  1  6   ? 9.924  28.331  -13.220 1.00 57.41  ? 6   GLN A CD  1 
ATOM   46   O  OE1 . GLN A  1  6   ? 9.011  27.485  -13.239 1.00 59.91  ? 6   GLN A OE1 1 
ATOM   47   N  NE2 . GLN A  1  6   ? 10.020 29.264  -12.268 1.00 57.95  ? 6   GLN A NE2 1 
ATOM   48   N  N   . ARG A  1  7   ? 13.437 25.199  -16.523 1.00 49.55  ? 7   ARG A N   1 
ATOM   49   C  CA  . ARG A  1  7   ? 14.079 23.909  -16.774 1.00 51.60  ? 7   ARG A CA  1 
ATOM   50   C  C   . ARG A  1  7   ? 15.548 24.124  -17.116 1.00 52.43  ? 7   ARG A C   1 
ATOM   51   O  O   . ARG A  1  7   ? 16.398 23.325  -16.725 1.00 53.38  ? 7   ARG A O   1 
ATOM   52   C  CB  . ARG A  1  7   ? 13.373 23.150  -17.907 1.00 51.72  ? 7   ARG A CB  1 
ATOM   53   C  CG  . ARG A  1  7   ? 11.943 22.777  -17.559 1.00 53.54  ? 7   ARG A CG  1 
ATOM   54   C  CD  . ARG A  1  7   ? 11.230 21.992  -18.659 1.00 54.58  ? 7   ARG A CD  1 
ATOM   55   N  NE  . ARG A  1  7   ? 9.883  21.629  -18.198 1.00 57.56  ? 7   ARG A NE  1 
ATOM   56   C  CZ  . ARG A  1  7   ? 9.285  20.459  -18.423 1.00 57.49  ? 7   ARG A CZ  1 
ATOM   57   N  NH1 . ARG A  1  7   ? 9.899  19.504  -19.119 1.00 58.95  ? 7   ARG A NH1 1 
ATOM   58   N  NH2 . ARG A  1  7   ? 8.078  20.238  -17.923 1.00 56.79  ? 7   ARG A NH2 1 
ATOM   59   N  N   . LEU A  1  8   ? 15.845 25.211  -17.825 1.00 52.03  ? 8   LEU A N   1 
ATOM   60   C  CA  . LEU A  1  8   ? 17.224 25.521  -18.191 1.00 52.14  ? 8   LEU A CA  1 
ATOM   61   C  C   . LEU A  1  8   ? 18.000 25.996  -16.953 1.00 49.83  ? 8   LEU A C   1 
ATOM   62   O  O   . LEU A  1  8   ? 19.167 25.660  -16.757 1.00 47.71  ? 8   LEU A O   1 
ATOM   63   C  CB  . LEU A  1  8   ? 17.245 26.614  -19.264 1.00 55.19  ? 8   LEU A CB  1 
ATOM   64   C  CG  . LEU A  1  8   ? 16.665 26.221  -20.626 1.00 58.90  ? 8   LEU A CG  1 
ATOM   65   C  CD1 . LEU A  1  8   ? 16.601 27.445  -21.549 1.00 60.36  ? 8   LEU A CD1 1 
ATOM   66   C  CD2 . LEU A  1  8   ? 17.520 25.109  -21.236 1.00 59.77  ? 8   LEU A CD2 1 
ATOM   67   N  N   . LYS A  1  9   ? 17.324 26.783  -16.130 1.00 46.63  ? 9   LYS A N   1 
ATOM   68   C  CA  . LYS A  1  9   ? 17.887 27.317  -14.908 1.00 43.87  ? 9   LYS A CA  1 
ATOM   69   C  C   . LYS A  1  9   ? 18.313 26.151  -14.038 1.00 44.27  ? 9   LYS A C   1 
ATOM   70   O  O   . LYS A  1  9   ? 19.447 26.079  -13.576 1.00 41.69  ? 9   LYS A O   1 
ATOM   71   C  CB  . LYS A  1  9   ? 16.815 28.110  -14.189 1.00 42.25  ? 9   LYS A CB  1 
ATOM   72   C  CG  . LYS A  1  9   ? 17.312 28.868  -12.999 1.00 42.58  ? 9   LYS A CG  1 
ATOM   73   C  CD  . LYS A  1  9   ? 18.355 29.891  -13.411 1.00 38.82  ? 9   LYS A CD  1 
ATOM   74   C  CE  . LYS A  1  9   ? 18.342 31.023  -12.456 1.00 38.88  ? 9   LYS A CE  1 
ATOM   75   N  NZ  . LYS A  1  9   ? 16.979 31.571  -12.357 1.00 37.68  ? 9   LYS A NZ  1 
ATOM   76   N  N   . VAL A  1  10  ? 17.360 25.239  -13.826 1.00 44.66  ? 10  VAL A N   1 
ATOM   77   C  CA  . VAL A  1  10  ? 17.555 24.049  -13.014 1.00 43.27  ? 10  VAL A CA  1 
ATOM   78   C  C   . VAL A  1  10  ? 18.713 23.215  -13.554 1.00 44.23  ? 10  VAL A C   1 
ATOM   79   O  O   . VAL A  1  10  ? 19.539 22.742  -12.772 1.00 43.22  ? 10  VAL A O   1 
ATOM   80   C  CB  . VAL A  1  10  ? 16.226 23.208  -12.941 1.00 40.79  ? 10  VAL A CB  1 
ATOM   81   C  CG1 . VAL A  1  10  ? 16.480 21.814  -12.396 1.00 37.07  ? 10  VAL A CG1 1 
ATOM   82   C  CG2 . VAL A  1  10  ? 15.225 23.926  -12.039 1.00 39.82  ? 10  VAL A CG2 1 
ATOM   83   N  N   . LYS A  1  11  ? 18.774 23.035  -14.877 1.00 45.40  ? 11  LYS A N   1 
ATOM   84   C  CA  . LYS A  1  11  ? 19.860 22.274  -15.492 1.00 47.52  ? 11  LYS A CA  1 
ATOM   85   C  C   . LYS A  1  11  ? 21.212 22.891  -15.169 1.00 46.87  ? 11  LYS A C   1 
ATOM   86   O  O   . LYS A  1  11  ? 22.149 22.179  -14.832 1.00 45.07  ? 11  LYS A O   1 
ATOM   87   C  CB  . LYS A  1  11  ? 19.682 22.183  -17.009 1.00 48.30  ? 11  LYS A CB  1 
ATOM   88   C  CG  . LYS A  1  11  ? 18.629 21.167  -17.404 1.00 55.11  ? 11  LYS A CG  1 
ATOM   89   C  CD  . LYS A  1  11  ? 18.534 20.960  -18.920 1.00 57.64  ? 11  LYS A CD  1 
ATOM   90   C  CE  . LYS A  1  11  ? 19.756 20.226  -19.454 1.00 61.52  ? 11  LYS A CE  1 
ATOM   91   N  NZ  . LYS A  1  11  ? 19.671 20.036  -20.926 1.00 63.29  ? 11  LYS A NZ  1 
ATOM   92   N  N   . MET A  1  12  ? 21.297 24.215  -15.257 1.00 47.52  ? 12  MET A N   1 
ATOM   93   C  CA  . MET A  1  12  ? 22.522 24.935  -14.960 1.00 47.55  ? 12  MET A CA  1 
ATOM   94   C  C   . MET A  1  12  ? 22.896 24.691  -13.509 1.00 45.80  ? 12  MET A C   1 
ATOM   95   O  O   . MET A  1  12  ? 23.949 24.129  -13.202 1.00 44.55  ? 12  MET A O   1 
ATOM   96   C  CB  . MET A  1  12  ? 22.313 26.427  -15.135 1.00 54.78  ? 12  MET A CB  1 
ATOM   97   C  CG  . MET A  1  12  ? 21.764 26.821  -16.475 1.00 66.81  ? 12  MET A CG  1 
ATOM   98   S  SD  . MET A  1  12  ? 22.976 26.710  -17.774 1.00 76.53  ? 12  MET A SD  1 
ATOM   99   C  CE  . MET A  1  12  ? 22.556 28.195  -18.717 1.00 77.23  ? 12  MET A CE  1 
ATOM   100  N  N   . GLN A  1  13  ? 22.022 25.120  -12.609 1.00 41.49  ? 13  GLN A N   1 
ATOM   101  C  CA  . GLN A  1  13  ? 22.318 24.978  -11.203 1.00 40.08  ? 13  GLN A CA  1 
ATOM   102  C  C   . GLN A  1  13  ? 22.636 23.527  -10.796 1.00 40.37  ? 13  GLN A C   1 
ATOM   103  O  O   . GLN A  1  13  ? 23.548 23.285  -10.000 1.00 38.81  ? 13  GLN A O   1 
ATOM   104  C  CB  . GLN A  1  13  ? 21.172 25.546  -10.363 1.00 36.90  ? 13  GLN A CB  1 
ATOM   105  C  CG  . GLN A  1  13  ? 20.748 26.937  -10.760 1.00 36.17  ? 13  GLN A CG  1 
ATOM   106  C  CD  . GLN A  1  13  ? 20.080 27.706  -9.628  1.00 39.78  ? 13  GLN A CD  1 
ATOM   107  O  OE1 . GLN A  1  13  ? 19.389 27.124  -8.775  1.00 39.85  ? 13  GLN A OE1 1 
ATOM   108  N  NE2 . GLN A  1  13  ? 20.271 29.023  -9.616  1.00 40.61  ? 13  GLN A NE2 1 
ATOM   109  N  N   . TRP A  1  14  ? 21.903 22.564  -11.338 1.00 38.96  ? 14  TRP A N   1 
ATOM   110  C  CA  . TRP A  1  14  ? 22.164 21.181  -10.994 1.00 38.17  ? 14  TRP A CA  1 
ATOM   111  C  C   . TRP A  1  14  ? 23.567 20.780  -11.398 1.00 38.70  ? 14  TRP A C   1 
ATOM   112  O  O   . TRP A  1  14  ? 24.259 20.095  -10.647 1.00 38.86  ? 14  TRP A O   1 
ATOM   113  C  CB  . TRP A  1  14  ? 21.175 20.239  -11.684 1.00 36.10  ? 14  TRP A CB  1 
ATOM   114  C  CG  . TRP A  1  14  ? 21.686 18.814  -11.758 1.00 33.45  ? 14  TRP A CG  1 
ATOM   115  C  CD1 . TRP A  1  14  ? 22.247 18.193  -12.840 1.00 34.09  ? 14  TRP A CD1 1 
ATOM   116  C  CD2 . TRP A  1  14  ? 21.643 17.831  -10.708 1.00 33.43  ? 14  TRP A CD2 1 
ATOM   117  N  NE1 . TRP A  1  14  ? 22.544 16.874  -12.536 1.00 32.00  ? 14  TRP A NE1 1 
ATOM   118  C  CE2 . TRP A  1  14  ? 22.178 16.629  -11.237 1.00 30.87  ? 14  TRP A CE2 1 
ATOM   119  C  CE3 . TRP A  1  14  ? 21.201 17.850  -9.376  1.00 31.31  ? 14  TRP A CE3 1 
ATOM   120  C  CZ2 . TRP A  1  14  ? 22.273 15.461  -10.481 1.00 30.56  ? 14  TRP A CZ2 1 
ATOM   121  C  CZ3 . TRP A  1  14  ? 21.293 16.701  -8.631  1.00 31.14  ? 14  TRP A CZ3 1 
ATOM   122  C  CH2 . TRP A  1  14  ? 21.826 15.511  -9.186  1.00 33.90  ? 14  TRP A CH2 1 
ATOM   123  N  N   . ALA A  1  15  ? 23.972 21.189  -12.597 1.00 38.72  ? 15  ALA A N   1 
ATOM   124  C  CA  . ALA A  1  15  ? 25.295 20.841  -13.106 1.00 39.95  ? 15  ALA A CA  1 
ATOM   125  C  C   . ALA A  1  15  ? 26.388 21.391  -12.199 1.00 40.19  ? 15  ALA A C   1 
ATOM   126  O  O   . ALA A  1  15  ? 27.346 20.700  -11.900 1.00 40.55  ? 15  ALA A O   1 
ATOM   127  C  CB  . ALA A  1  15  ? 25.472 21.350  -14.537 1.00 36.92  ? 15  ALA A CB  1 
ATOM   128  N  N   . LYS A  1  16  ? 26.234 22.630  -11.757 1.00 41.21  ? 16  LYS A N   1 
ATOM   129  C  CA  . LYS A  1  16  ? 27.201 23.241  -10.863 1.00 43.25  ? 16  LYS A CA  1 
ATOM   130  C  C   . LYS A  1  16  ? 27.222 22.444  -9.539  1.00 42.60  ? 16  LYS A C   1 
ATOM   131  O  O   . LYS A  1  16  ? 28.225 21.856  -9.184  1.00 41.70  ? 16  LYS A O   1 
ATOM   132  C  CB  . LYS A  1  16  ? 26.813 24.713  -10.630 1.00 44.67  ? 16  LYS A CB  1 
ATOM   133  C  CG  . LYS A  1  16  ? 27.770 25.514  -9.757  1.00 50.77  ? 16  LYS A CG  1 
ATOM   134  C  CD  . LYS A  1  16  ? 29.179 25.565  -10.363 1.00 54.22  ? 16  LYS A CD  1 
ATOM   135  C  CE  . LYS A  1  16  ? 30.126 26.401  -9.515  1.00 54.89  ? 16  LYS A CE  1 
ATOM   136  N  NZ  . LYS A  1  16  ? 31.518 26.398  -10.047 1.00 55.53  ? 16  LYS A NZ  1 
ATOM   137  N  N   . ALA A  1  17  ? 26.090 22.406  -8.842  1.00 43.53  ? 17  ALA A N   1 
ATOM   138  C  CA  . ALA A  1  17  ? 25.945 21.725  -7.554  1.00 44.04  ? 17  ALA A CA  1 
ATOM   139  C  C   . ALA A  1  17  ? 26.358 20.261  -7.511  1.00 46.27  ? 17  ALA A C   1 
ATOM   140  O  O   . ALA A  1  17  ? 26.895 19.773  -6.509  1.00 43.22  ? 17  ALA A O   1 
ATOM   141  C  CB  . ALA A  1  17  ? 24.522 21.830  -7.108  1.00 43.38  ? 17  ALA A CB  1 
ATOM   142  N  N   . TYR A  1  18  ? 26.072 19.561  -8.599  1.00 49.47  ? 18  TYR A N   1 
ATOM   143  C  CA  . TYR A  1  18  ? 26.360 18.135  -8.739  1.00 51.37  ? 18  TYR A CA  1 
ATOM   144  C  C   . TYR A  1  18  ? 27.854 17.856  -8.933  1.00 53.28  ? 18  TYR A C   1 
ATOM   145  O  O   . TYR A  1  18  ? 28.387 16.894  -8.387  1.00 50.87  ? 18  TYR A O   1 
ATOM   146  C  CB  . TYR A  1  18  ? 25.559 17.609  -9.920  1.00 51.08  ? 18  TYR A CB  1 
ATOM   147  C  CG  . TYR A  1  18  ? 25.701 16.147  -10.210 1.00 50.47  ? 18  TYR A CG  1 
ATOM   148  C  CD1 . TYR A  1  18  ? 25.397 15.200  -9.237  1.00 50.05  ? 18  TYR A CD1 1 
ATOM   149  C  CD2 . TYR A  1  18  ? 26.029 15.699  -11.500 1.00 50.95  ? 18  TYR A CD2 1 
ATOM   150  C  CE1 . TYR A  1  18  ? 25.403 13.843  -9.528  1.00 49.74  ? 18  TYR A CE1 1 
ATOM   151  C  CE2 . TYR A  1  18  ? 26.040 14.339  -11.806 1.00 50.62  ? 18  TYR A CE2 1 
ATOM   152  C  CZ  . TYR A  1  18  ? 25.718 13.417  -10.810 1.00 52.05  ? 18  TYR A CZ  1 
ATOM   153  O  OH  . TYR A  1  18  ? 25.684 12.069  -11.106 1.00 55.96  ? 18  TYR A OH  1 
ATOM   154  N  N   . GLY A  1  19  ? 28.506 18.697  -9.726  1.00 56.39  ? 19  GLY A N   1 
ATOM   155  C  CA  . GLY A  1  19  ? 29.928 18.558  -9.967  1.00 61.27  ? 19  GLY A CA  1 
ATOM   156  C  C   . GLY A  1  19  ? 30.412 17.294  -10.644 1.00 65.25  ? 19  GLY A C   1 
ATOM   157  O  O   . GLY A  1  19  ? 29.639 16.442  -11.089 1.00 64.84  ? 19  GLY A O   1 
ATOM   158  N  N   . PHE A  1  20  ? 31.730 17.185  -10.707 1.00 69.40  ? 20  PHE A N   1 
ATOM   159  C  CA  . PHE A  1  20  ? 32.389 16.048  -11.319 1.00 72.95  ? 20  PHE A CA  1 
ATOM   160  C  C   . PHE A  1  20  ? 32.987 15.084  -10.280 1.00 72.96  ? 20  PHE A C   1 
ATOM   161  O  O   . PHE A  1  20  ? 33.015 15.362  -9.074  1.00 73.55  ? 20  PHE A O   1 
ATOM   162  C  CB  . PHE A  1  20  ? 33.494 16.560  -12.244 1.00 75.93  ? 20  PHE A CB  1 
ATOM   163  C  CG  . PHE A  1  20  ? 33.005 17.484  -13.319 1.00 80.06  ? 20  PHE A CG  1 
ATOM   164  C  CD1 . PHE A  1  20  ? 32.472 16.977  -14.495 1.00 82.28  ? 20  PHE A CD1 1 
ATOM   165  C  CD2 . PHE A  1  20  ? 33.106 18.866  -13.171 1.00 82.53  ? 20  PHE A CD2 1 
ATOM   166  C  CE1 . PHE A  1  20  ? 32.049 17.839  -15.519 1.00 84.84  ? 20  PHE A CE1 1 
ATOM   167  C  CE2 . PHE A  1  20  ? 32.686 19.738  -14.187 1.00 84.49  ? 20  PHE A CE2 1 
ATOM   168  C  CZ  . PHE A  1  20  ? 32.158 19.224  -15.364 1.00 84.54  ? 20  PHE A CZ  1 
ATOM   169  N  N   . GLY A  1  21  ? 33.448 13.944  -10.780 1.00 72.34  ? 21  GLY A N   1 
ATOM   170  C  CA  . GLY A  1  21  ? 34.084 12.926  -9.960  1.00 71.21  ? 21  GLY A CA  1 
ATOM   171  C  C   . GLY A  1  21  ? 33.584 12.645  -8.563  1.00 69.52  ? 21  GLY A C   1 
ATOM   172  O  O   . GLY A  1  21  ? 32.392 12.520  -8.333  1.00 69.89  ? 21  GLY A O   1 
ATOM   173  N  N   . THR A  1  22  ? 34.524 12.541  -7.631  1.00 69.00  ? 22  THR A N   1 
ATOM   174  C  CA  . THR A  1  22  ? 34.240 12.238  -6.232  1.00 68.53  ? 22  THR A CA  1 
ATOM   175  C  C   . THR A  1  22  ? 33.348 13.243  -5.505  1.00 66.44  ? 22  THR A C   1 
ATOM   176  O  O   . THR A  1  22  ? 32.747 12.907  -4.494  1.00 65.02  ? 22  THR A O   1 
ATOM   177  C  CB  . THR A  1  22  ? 35.559 12.106  -5.440  1.00 70.47  ? 22  THR A CB  1 
ATOM   178  O  OG1 . THR A  1  22  ? 36.201 13.389  -5.353  1.00 71.97  ? 22  THR A OG1 1 
ATOM   179  C  CG2 . THR A  1  22  ? 36.507 11.138  -6.155  1.00 72.08  ? 22  THR A CG2 1 
ATOM   180  N  N   . GLU A  1  23  ? 33.268 14.475  -6.001  1.00 65.39  ? 23  GLU A N   1 
ATOM   181  C  CA  . GLU A  1  23  ? 32.435 15.487  -5.356  1.00 64.65  ? 23  GLU A CA  1 
ATOM   182  C  C   . GLU A  1  23  ? 30.970 15.084  -5.459  1.00 62.76  ? 23  GLU A C   1 
ATOM   183  O  O   . GLU A  1  23  ? 30.118 15.513  -4.674  1.00 62.48  ? 23  GLU A O   1 
ATOM   184  C  CB  . GLU A  1  23  ? 32.657 16.858  -6.008  1.00 66.20  ? 23  GLU A CB  1 
ATOM   185  C  CG  . GLU A  1  23  ? 33.941 17.547  -5.577  1.00 69.63  ? 23  GLU A CG  1 
ATOM   186  C  CD  . GLU A  1  23  ? 34.163 17.475  -4.063  1.00 73.69  ? 23  GLU A CD  1 
ATOM   187  O  OE1 . GLU A  1  23  ? 34.528 16.380  -3.569  1.00 74.37  ? 23  GLU A OE1 1 
ATOM   188  O  OE2 . GLU A  1  23  ? 33.967 18.502  -3.365  1.00 74.66  ? 23  GLU A OE2 1 
ATOM   189  N  N   . ARG A  1  24  ? 30.710 14.239  -6.445  1.00 59.74  ? 24  ARG A N   1 
ATOM   190  C  CA  . ARG A  1  24  ? 29.400 13.704  -6.730  1.00 55.99  ? 24  ARG A CA  1 
ATOM   191  C  C   . ARG A  1  24  ? 28.929 12.819  -5.562  1.00 54.80  ? 24  ARG A C   1 
ATOM   192  O  O   . ARG A  1  24  ? 27.802 12.964  -5.077  1.00 54.60  ? 24  ARG A O   1 
ATOM   193  C  CB  . ARG A  1  24  ? 29.509 12.914  -8.028  1.00 56.12  ? 24  ARG A CB  1 
ATOM   194  C  CG  . ARG A  1  24  ? 28.239 12.406  -8.608  1.00 56.14  ? 24  ARG A CG  1 
ATOM   195  C  CD  . ARG A  1  24  ? 28.540 11.861  -9.991  1.00 56.82  ? 24  ARG A CD  1 
ATOM   196  N  NE  . ARG A  1  24  ? 28.994 12.902  -10.912 1.00 54.76  ? 24  ARG A NE  1 
ATOM   197  C  CZ  . ARG A  1  24  ? 29.215 12.699  -12.214 1.00 54.63  ? 24  ARG A CZ  1 
ATOM   198  N  NH1 . ARG A  1  24  ? 29.022 11.492  -12.737 1.00 54.15  ? 24  ARG A NH1 1 
ATOM   199  N  NH2 . ARG A  1  24  ? 29.627 13.699  -12.989 1.00 49.11  ? 24  ARG A NH2 1 
ATOM   200  N  N   . ALA A  1  25  ? 29.792 11.917  -5.099  1.00 51.90  ? 25  ALA A N   1 
ATOM   201  C  CA  . ALA A  1  25  ? 29.428 11.042  -3.995  1.00 50.01  ? 25  ALA A CA  1 
ATOM   202  C  C   . ALA A  1  25  ? 29.111 11.868  -2.741  1.00 49.98  ? 25  ALA A C   1 
ATOM   203  O  O   . ALA A  1  25  ? 28.154 11.586  -2.033  1.00 50.70  ? 25  ALA A O   1 
ATOM   204  C  CB  . ALA A  1  25  ? 30.558 10.046  -3.723  1.00 47.90  ? 25  ALA A CB  1 
ATOM   205  N  N   . LYS A  1  26  ? 29.901 12.902  -2.483  1.00 50.00  ? 26  LYS A N   1 
ATOM   206  C  CA  . LYS A  1  26  ? 29.687 13.759  -1.316  1.00 49.90  ? 26  LYS A CA  1 
ATOM   207  C  C   . LYS A  1  26  ? 28.283 14.373  -1.357  1.00 47.67  ? 26  LYS A C   1 
ATOM   208  O  O   . LYS A  1  26  ? 27.557 14.356  -0.362  1.00 46.51  ? 26  LYS A O   1 
ATOM   209  C  CB  . LYS A  1  26  ? 30.740 14.872  -1.295  1.00 54.04  ? 26  LYS A CB  1 
ATOM   210  C  CG  . LYS A  1  26  ? 30.677 15.810  -0.081  1.00 55.60  ? 26  LYS A CG  1 
ATOM   211  C  CD  . LYS A  1  26  ? 31.687 16.950  -0.218  1.00 60.26  ? 26  LYS A CD  1 
ATOM   212  C  CE  . LYS A  1  26  ? 31.442 18.054  0.813   1.00 62.00  ? 26  LYS A CE  1 
ATOM   213  N  NZ  . LYS A  1  26  ? 32.425 19.182  0.752   1.00 62.80  ? 26  LYS A NZ  1 
ATOM   214  N  N   . PHE A  1  27  ? 27.932 14.944  -2.508  1.00 44.57  ? 27  PHE A N   1 
ATOM   215  C  CA  . PHE A  1  27  ? 26.617 15.551  -2.728  1.00 43.50  ? 27  PHE A CA  1 
ATOM   216  C  C   . PHE A  1  27  ? 25.550 14.474  -2.479  1.00 43.73  ? 27  PHE A C   1 
ATOM   217  O  O   . PHE A  1  27  ? 24.536 14.696  -1.788  1.00 40.87  ? 27  PHE A O   1 
ATOM   218  C  CB  . PHE A  1  27  ? 26.529 16.062  -4.176  1.00 42.90  ? 27  PHE A CB  1 
ATOM   219  C  CG  . PHE A  1  27  ? 25.159 16.476  -4.600  1.00 42.65  ? 27  PHE A CG  1 
ATOM   220  C  CD1 . PHE A  1  27  ? 24.255 15.546  -5.082  1.00 43.37  ? 27  PHE A CD1 1 
ATOM   221  C  CD2 . PHE A  1  27  ? 24.756 17.803  -4.490  1.00 43.73  ? 27  PHE A CD2 1 
ATOM   222  C  CE1 . PHE A  1  27  ? 22.963 15.936  -5.445  1.00 45.06  ? 27  PHE A CE1 1 
ATOM   223  C  CE2 . PHE A  1  27  ? 23.473 18.199  -4.848  1.00 42.80  ? 27  PHE A CE2 1 
ATOM   224  C  CZ  . PHE A  1  27  ? 22.575 17.264  -5.323  1.00 43.95  ? 27  PHE A CZ  1 
ATOM   225  N  N   . GLY A  1  28  ? 25.809 13.301  -3.055  1.00 42.35  ? 28  GLY A N   1 
ATOM   226  C  CA  . GLY A  1  28  ? 24.920 12.173  -2.909  1.00 40.96  ? 28  GLY A CA  1 
ATOM   227  C  C   . GLY A  1  28  ? 24.728 11.825  -1.455  1.00 39.33  ? 28  GLY A C   1 
ATOM   228  O  O   . GLY A  1  28  ? 23.595 11.614  -1.009  1.00 39.33  ? 28  GLY A O   1 
ATOM   229  N  N   . ASN A  1  29  ? 25.829 11.779  -0.710  1.00 38.09  ? 29  ASN A N   1 
ATOM   230  C  CA  . ASN A  1  29  ? 25.756 11.442  0.706   1.00 37.12  ? 29  ASN A CA  1 
ATOM   231  C  C   . ASN A  1  29  ? 24.993 12.486  1.529   1.00 36.98  ? 29  ASN A C   1 
ATOM   232  O  O   . ASN A  1  29  ? 24.264 12.133  2.471   1.00 35.88  ? 29  ASN A O   1 
ATOM   233  C  CB  . ASN A  1  29  ? 27.161 11.221  1.293   1.00 36.94  ? 29  ASN A CB  1 
ATOM   234  C  CG  . ASN A  1  29  ? 27.122 10.935  2.798   1.00 38.42  ? 29  ASN A CG  1 
ATOM   235  O  OD1 . ASN A  1  29  ? 27.108 11.864  3.612   1.00 40.20  ? 29  ASN A OD1 1 
ATOM   236  N  ND2 . ASN A  1  29  ? 27.070 9.644   3.171   1.00 38.04  ? 29  ASN A ND2 1 
ATOM   237  N  N   . SER A  1  30  ? 25.145 13.762  1.171   1.00 36.02  ? 30  SER A N   1 
ATOM   238  C  CA  . SER A  1  30  ? 24.456 14.824  1.898   1.00 35.06  ? 30  SER A CA  1 
ATOM   239  C  C   . SER A  1  30  ? 22.958 14.772  1.633   1.00 35.27  ? 30  SER A C   1 
ATOM   240  O  O   . SER A  1  30  ? 22.134 14.943  2.549   1.00 35.67  ? 30  SER A O   1 
ATOM   241  C  CB  . SER A  1  30  ? 25.017 16.192  1.516   1.00 33.76  ? 30  SER A CB  1 
ATOM   242  O  OG  . SER A  1  30  ? 26.201 16.441  2.234   1.00 31.79  ? 30  SER A OG  1 
ATOM   243  N  N   . LEU A  1  31  ? 22.604 14.516  0.378   1.00 33.67  ? 31  LEU A N   1 
ATOM   244  C  CA  . LEU A  1  31  ? 21.213 14.413  0.029   1.00 34.98  ? 31  LEU A CA  1 
ATOM   245  C  C   . LEU A  1  31  ? 20.554 13.358  0.927   1.00 35.24  ? 31  LEU A C   1 
ATOM   246  O  O   . LEU A  1  31  ? 19.558 13.627  1.609   1.00 36.89  ? 31  LEU A O   1 
ATOM   247  C  CB  . LEU A  1  31  ? 21.072 13.999  -1.432  1.00 33.43  ? 31  LEU A CB  1 
ATOM   248  C  CG  . LEU A  1  31  ? 19.618 13.704  -1.818  1.00 33.85  ? 31  LEU A CG  1 
ATOM   249  C  CD1 . LEU A  1  31  ? 18.757 14.938  -1.600  1.00 28.76  ? 31  LEU A CD1 1 
ATOM   250  C  CD2 . LEU A  1  31  ? 19.580 13.267  -3.281  1.00 34.43  ? 31  LEU A CD2 1 
ATOM   251  N  N   . TRP A  1  32  ? 21.140 12.173  0.962   1.00 33.82  ? 32  TRP A N   1 
ATOM   252  C  CA  . TRP A  1  32  ? 20.568 11.107  1.756   1.00 34.12  ? 32  TRP A CA  1 
ATOM   253  C  C   . TRP A  1  32  ? 20.669 11.297  3.284   1.00 35.60  ? 32  TRP A C   1 
ATOM   254  O  O   . TRP A  1  32  ? 19.821 10.793  4.035   1.00 34.35  ? 32  TRP A O   1 
ATOM   255  C  CB  . TRP A  1  32  ? 21.137 9.787   1.263   1.00 30.68  ? 32  TRP A CB  1 
ATOM   256  C  CG  . TRP A  1  32  ? 20.510 9.447   -0.045  1.00 31.97  ? 32  TRP A CG  1 
ATOM   257  C  CD1 . TRP A  1  32  ? 21.020 9.685   -1.285  1.00 32.80  ? 32  TRP A CD1 1 
ATOM   258  C  CD2 . TRP A  1  32  ? 19.213 8.873   -0.252  1.00 29.16  ? 32  TRP A CD2 1 
ATOM   259  N  NE1 . TRP A  1  32  ? 20.131 9.294   -2.253  1.00 30.38  ? 32  TRP A NE1 1 
ATOM   260  C  CE2 . TRP A  1  32  ? 19.010 8.792   -1.645  1.00 31.30  ? 32  TRP A CE2 1 
ATOM   261  C  CE3 . TRP A  1  32  ? 18.206 8.421   0.611   1.00 28.65  ? 32  TRP A CE3 1 
ATOM   262  C  CZ2 . TRP A  1  32  ? 17.822 8.268   -2.206  1.00 32.19  ? 32  TRP A CZ2 1 
ATOM   263  C  CZ3 . TRP A  1  32  ? 17.035 7.907   0.067   1.00 29.70  ? 32  TRP A CZ3 1 
ATOM   264  C  CH2 . TRP A  1  32  ? 16.849 7.832   -1.333  1.00 32.05  ? 32  TRP A CH2 1 
ATOM   265  N  N   . THR A  1  33  ? 21.672 12.039  3.744   1.00 35.79  ? 33  THR A N   1 
ATOM   266  C  CA  . THR A  1  33  ? 21.778 12.318  5.169   1.00 36.21  ? 33  THR A CA  1 
ATOM   267  C  C   . THR A  1  33  ? 20.628 13.277  5.542   1.00 37.69  ? 33  THR A C   1 
ATOM   268  O  O   . THR A  1  33  ? 20.074 13.204  6.639   1.00 36.76  ? 33  THR A O   1 
ATOM   269  C  CB  . THR A  1  33  ? 23.126 12.982  5.506   1.00 36.61  ? 33  THR A CB  1 
ATOM   270  O  OG1 . THR A  1  33  ? 24.164 11.997  5.430   1.00 38.41  ? 33  THR A OG1 1 
ATOM   271  C  CG2 . THR A  1  33  ? 23.109 13.575  6.911   1.00 34.37  ? 33  THR A CG2 1 
ATOM   272  N  N   . SER A  1  34  ? 20.260 14.178  4.635   1.00 38.50  ? 34  SER A N   1 
ATOM   273  C  CA  . SER A  1  34  ? 19.172 15.089  4.960   1.00 39.03  ? 34  SER A CA  1 
ATOM   274  C  C   . SER A  1  34  ? 17.868 14.305  4.978   1.00 38.76  ? 34  SER A C   1 
ATOM   275  O  O   . SER A  1  34  ? 17.088 14.382  5.944   1.00 38.46  ? 34  SER A O   1 
ATOM   276  C  CB  . SER A  1  34  ? 19.090 16.235  3.944   1.00 39.38  ? 34  SER A CB  1 
ATOM   277  O  OG  . SER A  1  34  ? 19.966 17.304  4.287   1.00 41.15  ? 34  SER A OG  1 
ATOM   278  N  N   . ILE A  1  35  ? 17.641 13.523  3.920   1.00 37.15  ? 35  ILE A N   1 
ATOM   279  C  CA  . ILE A  1  35  ? 16.410 12.749  3.837   1.00 36.91  ? 35  ILE A CA  1 
ATOM   280  C  C   . ILE A  1  35  ? 16.142 11.985  5.123   1.00 39.66  ? 35  ILE A C   1 
ATOM   281  O  O   . ILE A  1  35  ? 15.052 12.096  5.689   1.00 40.31  ? 35  ILE A O   1 
ATOM   282  C  CB  . ILE A  1  35  ? 16.428 11.752  2.686   1.00 35.05  ? 35  ILE A CB  1 
ATOM   283  C  CG1 . ILE A  1  35  ? 16.594 12.492  1.357   1.00 34.09  ? 35  ILE A CG1 1 
ATOM   284  C  CG2 . ILE A  1  35  ? 15.130 10.972  2.693   1.00 32.28  ? 35  ILE A CG2 1 
ATOM   285  C  CD1 . ILE A  1  35  ? 16.651 11.599  0.104   1.00 32.88  ? 35  ILE A CD1 1 
ATOM   286  N  N   . PHE A  1  36  ? 17.129 11.226  5.597   1.00 39.74  ? 36  PHE A N   1 
ATOM   287  C  CA  . PHE A  1  36  ? 16.945 10.477  6.820   1.00 41.20  ? 36  PHE A CA  1 
ATOM   288  C  C   . PHE A  1  36  ? 16.857 11.337  8.077   1.00 43.39  ? 36  PHE A C   1 
ATOM   289  O  O   . PHE A  1  36  ? 16.283 10.897  9.081   1.00 45.07  ? 36  PHE A O   1 
ATOM   290  C  CB  . PHE A  1  36  ? 18.057 9.445   6.982   1.00 40.17  ? 36  PHE A CB  1 
ATOM   291  C  CG  . PHE A  1  36  ? 18.081 8.414   5.903   1.00 38.70  ? 36  PHE A CG  1 
ATOM   292  C  CD1 . PHE A  1  36  ? 16.933 8.146   5.151   1.00 38.42  ? 36  PHE A CD1 1 
ATOM   293  C  CD2 . PHE A  1  36  ? 19.225 7.660   5.670   1.00 37.02  ? 36  PHE A CD2 1 
ATOM   294  C  CE1 . PHE A  1  36  ? 16.924 7.140   4.189   1.00 37.18  ? 36  PHE A CE1 1 
ATOM   295  C  CE2 . PHE A  1  36  ? 19.222 6.656   4.711   1.00 36.66  ? 36  PHE A CE2 1 
ATOM   296  C  CZ  . PHE A  1  36  ? 18.064 6.395   3.968   1.00 37.09  ? 36  PHE A CZ  1 
ATOM   297  N  N   . ASN A  1  37  ? 17.427 12.540  8.054   1.00 44.97  ? 37  ASN A N   1 
ATOM   298  C  CA  . ASN A  1  37  ? 17.325 13.391  9.239   1.00 47.45  ? 37  ASN A CA  1 
ATOM   299  C  C   . ASN A  1  37  ? 15.919 13.999  9.236   1.00 48.07  ? 37  ASN A C   1 
ATOM   300  O  O   . ASN A  1  37  ? 15.269 14.077  10.277  1.00 47.75  ? 37  ASN A O   1 
ATOM   301  C  CB  . ASN A  1  37  ? 18.410 14.491  9.253   1.00 49.70  ? 37  ASN A CB  1 
ATOM   302  C  CG  . ASN A  1  37  ? 19.763 13.991  9.814   1.00 51.37  ? 37  ASN A CG  1 
ATOM   303  O  OD1 . ASN A  1  37  ? 19.797 13.115  10.679  1.00 53.70  ? 37  ASN A OD1 1 
ATOM   304  N  ND2 . ASN A  1  37  ? 20.865 14.563  9.340   1.00 49.62  ? 37  ASN A ND2 1 
ATOM   305  N  N   . TYR A  1  38  ? 15.440 14.377  8.048   1.00 47.69  ? 38  TYR A N   1 
ATOM   306  C  CA  . TYR A  1  38  ? 14.116 14.974  7.896   1.00 46.90  ? 38  TYR A CA  1 
ATOM   307  C  C   . TYR A  1  38  ? 12.997 13.998  8.250   1.00 47.81  ? 38  TYR A C   1 
ATOM   308  O  O   . TYR A  1  38  ? 11.978 14.389  8.807   1.00 46.46  ? 38  TYR A O   1 
ATOM   309  C  CB  . TYR A  1  38  ? 13.915 15.459  6.455   1.00 44.68  ? 38  TYR A CB  1 
ATOM   310  C  CG  . TYR A  1  38  ? 14.696 16.698  6.060   1.00 41.94  ? 38  TYR A CG  1 
ATOM   311  C  CD1 . TYR A  1  38  ? 15.469 17.394  6.988   1.00 37.98  ? 38  TYR A CD1 1 
ATOM   312  C  CD2 . TYR A  1  38  ? 14.624 17.196  4.748   1.00 40.58  ? 38  TYR A CD2 1 
ATOM   313  C  CE1 . TYR A  1  38  ? 16.142 18.549  6.622   1.00 39.80  ? 38  TYR A CE1 1 
ATOM   314  C  CE2 . TYR A  1  38  ? 15.302 18.351  4.374   1.00 40.00  ? 38  TYR A CE2 1 
ATOM   315  C  CZ  . TYR A  1  38  ? 16.054 19.021  5.315   1.00 39.99  ? 38  TYR A CZ  1 
ATOM   316  O  OH  . TYR A  1  38  ? 16.715 20.170  4.969   1.00 40.82  ? 38  TYR A OH  1 
ATOM   317  N  N   . ALA A  1  39  ? 13.186 12.728  7.909   1.00 49.13  ? 39  ALA A N   1 
ATOM   318  C  CA  . ALA A  1  39  ? 12.186 11.705  8.176   1.00 51.96  ? 39  ALA A CA  1 
ATOM   319  C  C   . ALA A  1  39  ? 12.889 10.400  8.537   1.00 55.13  ? 39  ALA A C   1 
ATOM   320  O  O   . ALA A  1  39  ? 13.000 9.486   7.714   1.00 55.29  ? 39  ALA A O   1 
ATOM   321  C  CB  . ALA A  1  39  ? 11.313 11.507  6.956   1.00 51.77  ? 39  ALA A CB  1 
ATOM   322  N  N   . PRO A  1  40  ? 13.363 10.297  9.786   1.00 57.35  ? 40  PRO A N   1 
ATOM   323  C  CA  . PRO A  1  40  ? 14.072 9.118   10.284  1.00 58.00  ? 40  PRO A CA  1 
ATOM   324  C  C   . PRO A  1  40  ? 13.412 7.783   9.981   1.00 58.76  ? 40  PRO A C   1 
ATOM   325  O  O   . PRO A  1  40  ? 14.097 6.763   9.882   1.00 59.39  ? 40  PRO A O   1 
ATOM   326  C  CB  . PRO A  1  40  ? 14.179 9.392   11.779  1.00 57.73  ? 40  PRO A CB  1 
ATOM   327  C  CG  . PRO A  1  40  ? 14.337 10.893  11.813  1.00 58.14  ? 40  PRO A CG  1 
ATOM   328  C  CD  . PRO A  1  40  ? 13.247 11.318  10.845  1.00 58.08  ? 40  PRO A CD  1 
ATOM   329  N  N   . ASP A  1  41  ? 12.100 7.767   9.824   1.00 58.72  ? 41  ASP A N   1 
ATOM   330  C  CA  . ASP A  1  41  ? 11.442 6.494   9.543   1.00 59.34  ? 41  ASP A CA  1 
ATOM   331  C  C   . ASP A  1  41  ? 11.715 5.980   8.136   1.00 57.70  ? 41  ASP A C   1 
ATOM   332  O  O   . ASP A  1  41  ? 11.722 4.770   7.906   1.00 57.96  ? 41  ASP A O   1 
ATOM   333  C  CB  . ASP A  1  41  ? 9.934  6.601   9.770   1.00 60.75  ? 41  ASP A CB  1 
ATOM   334  C  CG  . ASP A  1  41  ? 9.595  6.913   11.208  1.00 64.21  ? 41  ASP A CG  1 
ATOM   335  O  OD1 . ASP A  1  41  ? 10.265 6.343   12.102  1.00 61.39  ? 41  ASP A OD1 1 
ATOM   336  O  OD2 . ASP A  1  41  ? 8.659  7.714   11.449  1.00 68.24  ? 41  ASP A OD2 1 
ATOM   337  N  N   . ALA A  1  42  ? 11.963 6.890   7.201   1.00 55.67  ? 42  ALA A N   1 
ATOM   338  C  CA  . ALA A  1  42  ? 12.208 6.498   5.817   1.00 54.22  ? 42  ALA A CA  1 
ATOM   339  C  C   . ALA A  1  42  ? 13.416 5.598   5.652   1.00 53.23  ? 42  ALA A C   1 
ATOM   340  O  O   . ALA A  1  42  ? 13.533 4.906   4.643   1.00 54.03  ? 42  ALA A O   1 
ATOM   341  C  CB  . ALA A  1  42  ? 12.373 7.726   4.953   1.00 54.31  ? 42  ALA A CB  1 
ATOM   342  N  N   . ARG A  1  43  ? 14.304 5.600   6.635   1.00 51.34  ? 43  ARG A N   1 
ATOM   343  C  CA  . ARG A  1  43  ? 15.503 4.784   6.567   1.00 51.06  ? 43  ARG A CA  1 
ATOM   344  C  C   . ARG A  1  43  ? 15.216 3.281   6.501   1.00 51.84  ? 43  ARG A C   1 
ATOM   345  O  O   . ARG A  1  43  ? 15.896 2.545   5.773   1.00 49.88  ? 43  ARG A O   1 
ATOM   346  C  CB  . ARG A  1  43  ? 16.385 5.084   7.762   1.00 49.82  ? 43  ARG A CB  1 
ATOM   347  C  CG  . ARG A  1  43  ? 17.761 4.513   7.675   1.00 47.78  ? 43  ARG A CG  1 
ATOM   348  C  CD  . ARG A  1  43  ? 18.671 5.188   8.684   1.00 50.17  ? 43  ARG A CD  1 
ATOM   349  N  NE  . ARG A  1  43  ? 20.053 4.800   8.430   1.00 55.15  ? 43  ARG A NE  1 
ATOM   350  C  CZ  . ARG A  1  43  ? 21.094 5.163   9.175   1.00 57.32  ? 43  ARG A CZ  1 
ATOM   351  N  NH1 . ARG A  1  43  ? 20.901 5.930   10.238  1.00 58.26  ? 43  ARG A NH1 1 
ATOM   352  N  NH2 . ARG A  1  43  ? 22.317 4.744   8.859   1.00 57.41  ? 43  ARG A NH2 1 
ATOM   353  N  N   . ASP A  1  44  ? 14.206 2.828   7.237   1.00 52.32  ? 44  ASP A N   1 
ATOM   354  C  CA  . ASP A  1  44  ? 13.860 1.415   7.245   1.00 53.06  ? 44  ASP A CA  1 
ATOM   355  C  C   . ASP A  1  44  ? 13.366 0.927   5.897   1.00 52.82  ? 44  ASP A C   1 
ATOM   356  O  O   . ASP A  1  44  ? 13.289 -0.279  5.664   1.00 55.60  ? 44  ASP A O   1 
ATOM   357  C  CB  . ASP A  1  44  ? 12.805 1.121   8.311   1.00 55.28  ? 44  ASP A CB  1 
ATOM   358  C  CG  . ASP A  1  44  ? 13.235 1.578   9.696   1.00 60.82  ? 44  ASP A CG  1 
ATOM   359  O  OD1 . ASP A  1  44  ? 14.407 1.320   10.074  1.00 61.12  ? 44  ASP A OD1 1 
ATOM   360  O  OD2 . ASP A  1  44  ? 12.406 2.189   10.414  1.00 62.40  ? 44  ASP A OD2 1 
ATOM   361  N  N   . LEU A  1  45  ? 13.041 1.849   5.001   1.00 51.28  ? 45  LEU A N   1 
ATOM   362  C  CA  . LEU A  1  45  ? 12.554 1.471   3.677   1.00 50.47  ? 45  LEU A CA  1 
ATOM   363  C  C   . LEU A  1  45  ? 13.692 1.019   2.775   1.00 50.13  ? 45  LEU A C   1 
ATOM   364  O  O   . LEU A  1  45  ? 13.446 0.473   1.697   1.00 50.41  ? 45  LEU A O   1 
ATOM   365  C  CB  . LEU A  1  45  ? 11.851 2.654   3.004   1.00 50.58  ? 45  LEU A CB  1 
ATOM   366  C  CG  . LEU A  1  45  ? 10.660 3.257   3.737   1.00 51.50  ? 45  LEU A CG  1 
ATOM   367  C  CD1 . LEU A  1  45  ? 10.274 4.582   3.098   1.00 51.56  ? 45  LEU A CD1 1 
ATOM   368  C  CD2 . LEU A  1  45  ? 9.513  2.278   3.705   1.00 47.71  ? 45  LEU A CD2 1 
ATOM   369  N  N   . PHE A  1  46  ? 14.929 1.237   3.223   1.00 48.56  ? 46  PHE A N   1 
ATOM   370  C  CA  . PHE A  1  46  ? 16.098 0.902   2.418   1.00 48.80  ? 46  PHE A CA  1 
ATOM   371  C  C   . PHE A  1  46  ? 17.005 -0.212  2.932   1.00 50.18  ? 46  PHE A C   1 
ATOM   372  O  O   . PHE A  1  46  ? 18.222 -0.192  2.691   1.00 48.92  ? 46  PHE A O   1 
ATOM   373  C  CB  . PHE A  1  46  ? 16.910 2.175   2.190   1.00 46.06  ? 46  PHE A CB  1 
ATOM   374  C  CG  . PHE A  1  46  ? 16.146 3.244   1.473   1.00 44.07  ? 46  PHE A CG  1 
ATOM   375  C  CD1 . PHE A  1  46  ? 16.175 3.330   0.077   1.00 43.56  ? 46  PHE A CD1 1 
ATOM   376  C  CD2 . PHE A  1  46  ? 15.355 4.147   2.190   1.00 42.53  ? 46  PHE A CD2 1 
ATOM   377  C  CE1 . PHE A  1  46  ? 15.420 4.305   -0.590  1.00 43.85  ? 46  PHE A CE1 1 
ATOM   378  C  CE2 . PHE A  1  46  ? 14.596 5.124   1.536   1.00 40.31  ? 46  PHE A CE2 1 
ATOM   379  C  CZ  . PHE A  1  46  ? 14.624 5.207   0.146   1.00 40.92  ? 46  PHE A CZ  1 
ATOM   380  N  N   . LYS A  1  47  ? 16.424 -1.181  3.639   1.00 52.33  ? 47  LYS A N   1 
ATOM   381  C  CA  . LYS A  1  47  ? 17.198 -2.313  4.152   1.00 53.76  ? 47  LYS A CA  1 
ATOM   382  C  C   . LYS A  1  47  ? 17.758 -3.153  2.994   1.00 52.47  ? 47  LYS A C   1 
ATOM   383  O  O   . LYS A  1  47  ? 18.783 -3.816  3.138   1.00 51.64  ? 47  LYS A O   1 
ATOM   384  C  CB  . LYS A  1  47  ? 16.328 -3.166  5.074   1.00 55.95  ? 47  LYS A CB  1 
ATOM   385  C  CG  . LYS A  1  47  ? 16.039 -2.484  6.412   1.00 63.44  ? 47  LYS A CG  1 
ATOM   386  C  CD  . LYS A  1  47  ? 15.214 -3.360  7.355   1.00 67.03  ? 47  LYS A CD  1 
ATOM   387  C  CE  . LYS A  1  47  ? 13.837 -3.670  6.780   1.00 69.66  ? 47  LYS A CE  1 
ATOM   388  N  NZ  . LYS A  1  47  ? 13.011 -4.365  7.791   1.00 72.59  ? 47  LYS A NZ  1 
ATOM   389  N  N   . SER A  1  48  ? 17.093 -3.097  1.844   1.00 50.70  ? 48  SER A N   1 
ATOM   390  C  CA  . SER A  1  48  ? 17.540 -3.823  0.660   1.00 50.35  ? 48  SER A CA  1 
ATOM   391  C  C   . SER A  1  48  ? 18.873 -3.294  0.113   1.00 50.46  ? 48  SER A C   1 
ATOM   392  O  O   . SER A  1  48  ? 19.568 -3.989  -0.621  1.00 49.92  ? 48  SER A O   1 
ATOM   393  C  CB  . SER A  1  48  ? 16.475 -3.747  -0.446  1.00 50.60  ? 48  SER A CB  1 
ATOM   394  O  OG  . SER A  1  48  ? 16.088 -2.405  -0.727  1.00 49.35  ? 48  SER A OG  1 
ATOM   395  N  N   . VAL A  1  49  ? 19.219 -2.056  0.450   1.00 49.68  ? 49  VAL A N   1 
ATOM   396  C  CA  . VAL A  1  49  ? 20.470 -1.483  -0.018  1.00 48.50  ? 49  VAL A CA  1 
ATOM   397  C  C   . VAL A  1  49  ? 21.392 -1.137  1.142   1.00 50.66  ? 49  VAL A C   1 
ATOM   398  O  O   . VAL A  1  49  ? 22.304 -0.317  1.011   1.00 50.25  ? 49  VAL A O   1 
ATOM   399  C  CB  . VAL A  1  49  ? 20.242 -0.229  -0.913  1.00 45.96  ? 49  VAL A CB  1 
ATOM   400  C  CG1 . VAL A  1  49  ? 19.853 -0.663  -2.297  1.00 40.28  ? 49  VAL A CG1 1 
ATOM   401  C  CG2 . VAL A  1  49  ? 19.172 0.666   -0.318  1.00 39.92  ? 49  VAL A CG2 1 
ATOM   402  N  N   . LYS A  1  50  ? 21.126 -1.770  2.281   1.00 53.06  ? 50  LYS A N   1 
ATOM   403  C  CA  . LYS A  1  50  ? 21.936 -1.632  3.491   1.00 55.12  ? 50  LYS A CA  1 
ATOM   404  C  C   . LYS A  1  50  ? 22.025 -0.207  4.031   1.00 55.21  ? 50  LYS A C   1 
ATOM   405  O  O   . LYS A  1  50  ? 23.113 0.266   4.355   1.00 54.09  ? 50  LYS A O   1 
ATOM   406  C  CB  . LYS A  1  50  ? 23.338 -2.178  3.213   1.00 58.61  ? 50  LYS A CB  1 
ATOM   407  C  CG  . LYS A  1  50  ? 24.033 -2.868  4.388   1.00 63.98  ? 50  LYS A CG  1 
ATOM   408  C  CD  . LYS A  1  50  ? 25.357 -3.472  3.895   1.00 68.61  ? 50  LYS A CD  1 
ATOM   409  C  CE  . LYS A  1  50  ? 26.129 -4.207  4.981   1.00 70.73  ? 50  LYS A CE  1 
ATOM   410  N  NZ  . LYS A  1  50  ? 27.473 -4.619  4.486   1.00 72.11  ? 50  LYS A NZ  1 
ATOM   411  N  N   . SER A  1  51  ? 20.872 0.462   4.131   1.00 54.90  ? 51  SER A N   1 
ATOM   412  C  CA  . SER A  1  51  ? 20.798 1.833   4.642   1.00 53.23  ? 51  SER A CA  1 
ATOM   413  C  C   . SER A  1  51  ? 21.264 1.836   6.091   1.00 52.66  ? 51  SER A C   1 
ATOM   414  O  O   . SER A  1  51  ? 21.516 2.874   6.687   1.00 51.65  ? 51  SER A O   1 
ATOM   415  C  CB  . SER A  1  51  ? 19.361 2.355   4.576   1.00 53.26  ? 51  SER A CB  1 
ATOM   416  O  OG  . SER A  1  51  ? 18.507 1.652   5.474   1.00 53.48  ? 51  SER A OG  1 
ATOM   417  N  N   . GLU A  1  52  ? 21.346 0.645   6.653   1.00 52.99  ? 52  GLU A N   1 
ATOM   418  C  CA  . GLU A  1  52  ? 21.794 0.441   8.018   1.00 55.18  ? 52  GLU A CA  1 
ATOM   419  C  C   . GLU A  1  52  ? 23.159 1.125   8.218   1.00 53.40  ? 52  GLU A C   1 
ATOM   420  O  O   . GLU A  1  52  ? 23.481 1.616   9.295   1.00 52.52  ? 52  GLU A O   1 
ATOM   421  C  CB  . GLU A  1  52  ? 21.919 -1.064  8.251   1.00 58.57  ? 52  GLU A CB  1 
ATOM   422  C  CG  . GLU A  1  52  ? 21.126 -1.865  7.211   1.00 64.45  ? 52  GLU A CG  1 
ATOM   423  C  CD  . GLU A  1  52  ? 21.568 -3.316  7.104   1.00 68.21  ? 52  GLU A CD  1 
ATOM   424  O  OE1 . GLU A  1  52  ? 21.035 -4.051  6.239   1.00 68.48  ? 52  GLU A OE1 1 
ATOM   425  O  OE2 . GLU A  1  52  ? 22.453 -3.725  7.888   1.00 70.09  ? 52  GLU A OE2 1 
ATOM   426  N  N   . ASP A  1  53  ? 23.959 1.150   7.159   1.00 51.05  ? 53  ASP A N   1 
ATOM   427  C  CA  . ASP A  1  53  ? 25.281 1.735   7.202   1.00 48.56  ? 53  ASP A CA  1 
ATOM   428  C  C   . ASP A  1  53  ? 25.497 2.510   5.918   1.00 48.60  ? 53  ASP A C   1 
ATOM   429  O  O   . ASP A  1  53  ? 25.820 1.936   4.885   1.00 47.74  ? 53  ASP A O   1 
ATOM   430  C  CB  . ASP A  1  53  ? 26.314 0.616   7.348   1.00 46.86  ? 53  ASP A CB  1 
ATOM   431  C  CG  . ASP A  1  53  ? 27.732 1.099   7.185   1.00 46.85  ? 53  ASP A CG  1 
ATOM   432  O  OD1 . ASP A  1  53  ? 28.061 2.186   7.701   1.00 43.39  ? 53  ASP A OD1 1 
ATOM   433  O  OD2 . ASP A  1  53  ? 28.529 0.383   6.550   1.00 49.96  ? 53  ASP A OD2 1 
ATOM   434  N  N   . MET A  1  54  ? 25.325 3.820   5.998   1.00 49.12  ? 54  MET A N   1 
ATOM   435  C  CA  . MET A  1  54  ? 25.460 4.682   4.839   1.00 49.20  ? 54  MET A CA  1 
ATOM   436  C  C   . MET A  1  54  ? 26.813 4.721   4.173   1.00 47.43  ? 54  MET A C   1 
ATOM   437  O  O   . MET A  1  54  ? 26.936 5.216   3.070   1.00 46.54  ? 54  MET A O   1 
ATOM   438  C  CB  . MET A  1  54  ? 25.034 6.084   5.219   1.00 50.04  ? 54  MET A CB  1 
ATOM   439  C  CG  . MET A  1  54  ? 23.550 6.194   5.458   1.00 52.50  ? 54  MET A CG  1 
ATOM   440  S  SD  . MET A  1  54  ? 23.143 7.895   5.847   1.00 57.47  ? 54  MET A SD  1 
ATOM   441  C  CE  . MET A  1  54  ? 23.106 8.593   4.194   1.00 56.29  ? 54  MET A CE  1 
ATOM   442  N  N   . ARG A  1  55  ? 27.823 4.197   4.835   1.00 49.66  ? 55  ARG A N   1 
ATOM   443  C  CA  . ARG A  1  55  ? 29.168 4.211   4.277   1.00 52.47  ? 55  ARG A CA  1 
ATOM   444  C  C   . ARG A  1  55  ? 29.450 2.905   3.557   1.00 49.07  ? 55  ARG A C   1 
ATOM   445  O  O   . ARG A  1  55  ? 30.478 2.754   2.916   1.00 50.11  ? 55  ARG A O   1 
ATOM   446  C  CB  . ARG A  1  55  ? 30.191 4.457   5.391   1.00 59.12  ? 55  ARG A CB  1 
ATOM   447  C  CG  . ARG A  1  55  ? 29.606 4.317   6.809   1.00 68.74  ? 55  ARG A CG  1 
ATOM   448  C  CD  . ARG A  1  55  ? 30.678 4.219   7.887   1.00 76.67  ? 55  ARG A CD  1 
ATOM   449  N  NE  . ARG A  1  55  ? 31.460 5.446   8.009   1.00 84.29  ? 55  ARG A NE  1 
ATOM   450  C  CZ  . ARG A  1  55  ? 32.598 5.539   8.690   1.00 87.94  ? 55  ARG A CZ  1 
ATOM   451  N  NH1 . ARG A  1  55  ? 33.246 6.697   8.751   1.00 90.40  ? 55  ARG A NH1 1 
ATOM   452  N  NH2 . ARG A  1  55  ? 33.098 4.471   9.301   1.00 89.32  ? 55  ARG A NH2 1 
ATOM   453  N  N   . SER A  1  56  ? 28.517 1.974   3.651   1.00 45.55  ? 56  SER A N   1 
ATOM   454  C  CA  . SER A  1  56  ? 28.652 0.679   3.003   1.00 42.17  ? 56  SER A CA  1 
ATOM   455  C  C   . SER A  1  56  ? 28.554 0.777   1.478   1.00 40.79  ? 56  SER A C   1 
ATOM   456  O  O   . SER A  1  56  ? 27.804 1.582   0.934   1.00 39.80  ? 56  SER A O   1 
ATOM   457  C  CB  . SER A  1  56  ? 27.557 -0.252  3.496   1.00 42.53  ? 56  SER A CB  1 
ATOM   458  O  OG  . SER A  1  56  ? 26.337 0.029   2.830   1.00 44.13  ? 56  SER A OG  1 
ATOM   459  N  N   . PRO A  1  57  ? 29.302 -0.070  0.760   1.00 40.64  ? 57  PRO A N   1 
ATOM   460  C  CA  . PRO A  1  57  ? 29.244 -0.016  -0.704  1.00 38.81  ? 57  PRO A CA  1 
ATOM   461  C  C   . PRO A  1  57  ? 27.853 -0.261  -1.272  1.00 38.21  ? 57  PRO A C   1 
ATOM   462  O  O   . PRO A  1  57  ? 27.498 0.290   -2.313  1.00 37.87  ? 57  PRO A O   1 
ATOM   463  C  CB  . PRO A  1  57  ? 30.261 -1.079  -1.134  1.00 38.92  ? 57  PRO A CB  1 
ATOM   464  C  CG  . PRO A  1  57  ? 30.214 -2.064  0.015   1.00 38.81  ? 57  PRO A CG  1 
ATOM   465  C  CD  . PRO A  1  57  ? 30.185 -1.156  1.227   1.00 38.61  ? 57  PRO A CD  1 
ATOM   466  N  N   . GLN A  1  58  ? 27.059 -1.086  -0.599  1.00 38.38  ? 58  GLN A N   1 
ATOM   467  C  CA  . GLN A  1  58  ? 25.706 -1.357  -1.066  1.00 38.01  ? 58  GLN A CA  1 
ATOM   468  C  C   . GLN A  1  58  ? 24.900 -0.062  -1.122  1.00 36.75  ? 58  GLN A C   1 
ATOM   469  O  O   . GLN A  1  58  ? 24.268 0.224   -2.136  1.00 34.93  ? 58  GLN A O   1 
ATOM   470  C  CB  . GLN A  1  58  ? 25.002 -2.354  -0.146  1.00 40.65  ? 58  GLN A CB  1 
ATOM   471  C  CG  . GLN A  1  58  ? 25.379 -3.809  -0.389  1.00 46.01  ? 58  GLN A CG  1 
ATOM   472  C  CD  . GLN A  1  58  ? 26.819 -4.134  -0.011  1.00 49.14  ? 58  GLN A CD  1 
ATOM   473  O  OE1 . GLN A  1  58  ? 27.290 -3.795  1.084   1.00 47.31  ? 58  GLN A OE1 1 
ATOM   474  N  NE2 . GLN A  1  58  ? 27.528 -4.809  -0.923  1.00 52.25  ? 58  GLN A NE2 1 
ATOM   475  N  N   . PHE A  1  59  ? 24.953 0.726   -0.047  1.00 36.21  ? 59  PHE A N   1 
ATOM   476  C  CA  . PHE A  1  59  ? 24.216 1.979   0.005   1.00 36.17  ? 59  PHE A CA  1 
ATOM   477  C  C   . PHE A  1  59  ? 24.794 3.074   -0.873  1.00 37.24  ? 59  PHE A C   1 
ATOM   478  O  O   . PHE A  1  59  ? 24.057 3.944   -1.342  1.00 37.11  ? 59  PHE A O   1 
ATOM   479  C  CB  . PHE A  1  59  ? 24.119 2.511   1.429   1.00 35.10  ? 59  PHE A CB  1 
ATOM   480  C  CG  . PHE A  1  59  ? 23.092 3.593   1.588   1.00 35.68  ? 59  PHE A CG  1 
ATOM   481  C  CD1 . PHE A  1  59  ? 23.462 4.928   1.674   1.00 36.03  ? 59  PHE A CD1 1 
ATOM   482  C  CD2 . PHE A  1  59  ? 21.734 3.273   1.608   1.00 36.31  ? 59  PHE A CD2 1 
ATOM   483  C  CE1 . PHE A  1  59  ? 22.483 5.932   1.778   1.00 37.90  ? 59  PHE A CE1 1 
ATOM   484  C  CE2 . PHE A  1  59  ? 20.759 4.264   1.708   1.00 36.12  ? 59  PHE A CE2 1 
ATOM   485  C  CZ  . PHE A  1  59  ? 21.129 5.592   1.793   1.00 35.07  ? 59  PHE A CZ  1 
ATOM   486  N  N   . LYS A  1  60  ? 26.107 3.052   -1.072  1.00 38.81  ? 60  LYS A N   1 
ATOM   487  C  CA  . LYS A  1  60  ? 26.764 4.046   -1.915  1.00 40.94  ? 60  LYS A CA  1 
ATOM   488  C  C   . LYS A  1  60  ? 26.366 3.793   -3.365  1.00 40.30  ? 60  LYS A C   1 
ATOM   489  O  O   . LYS A  1  60  ? 26.227 4.726   -4.154  1.00 39.60  ? 60  LYS A O   1 
ATOM   490  C  CB  . LYS A  1  60  ? 28.280 3.966   -1.776  1.00 42.69  ? 60  LYS A CB  1 
ATOM   491  C  CG  . LYS A  1  60  ? 28.855 4.600   -0.508  1.00 44.35  ? 60  LYS A CG  1 
ATOM   492  C  CD  . LYS A  1  60  ? 30.345 4.386   -0.534  1.00 50.78  ? 60  LYS A CD  1 
ATOM   493  C  CE  . LYS A  1  60  ? 31.056 4.893   0.681   1.00 55.03  ? 60  LYS A CE  1 
ATOM   494  N  NZ  . LYS A  1  60  ? 32.500 4.462   0.639   1.00 59.38  ? 60  LYS A NZ  1 
ATOM   495  N  N   . ALA A  1  61  ? 26.184 2.524   -3.707  1.00 39.12  ? 61  ALA A N   1 
ATOM   496  C  CA  . ALA A  1  61  ? 25.768 2.164   -5.055  1.00 38.65  ? 61  ALA A CA  1 
ATOM   497  C  C   . ALA A  1  61  ? 24.328 2.706   -5.272  1.00 38.85  ? 61  ALA A C   1 
ATOM   498  O  O   . ALA A  1  61  ? 23.937 3.124   -6.386  1.00 34.97  ? 61  ALA A O   1 
ATOM   499  C  CB  . ALA A  1  61  ? 25.804 0.639   -5.215  1.00 34.78  ? 61  ALA A CB  1 
ATOM   500  N  N   . HIS A  1  62  ? 23.544 2.680   -4.197  1.00 36.95  ? 62  HIS A N   1 
ATOM   501  C  CA  . HIS A  1  62  ? 22.182 3.167   -4.260  1.00 38.06  ? 62  HIS A CA  1 
ATOM   502  C  C   . HIS A  1  62  ? 22.197 4.687   -4.455  1.00 37.76  ? 62  HIS A C   1 
ATOM   503  O  O   . HIS A  1  62  ? 21.508 5.227   -5.331  1.00 37.03  ? 62  HIS A O   1 
ATOM   504  C  CB  . HIS A  1  62  ? 21.431 2.823   -2.983  1.00 37.93  ? 62  HIS A CB  1 
ATOM   505  C  CG  . HIS A  1  62  ? 20.065 3.414   -2.943  1.00 38.39  ? 62  HIS A CG  1 
ATOM   506  N  ND1 . HIS A  1  62  ? 19.055 3.000   -3.782  1.00 38.40  ? 62  HIS A ND1 1 
ATOM   507  C  CD2 . HIS A  1  62  ? 19.560 4.438   -2.216  1.00 39.72  ? 62  HIS A CD2 1 
ATOM   508  C  CE1 . HIS A  1  62  ? 17.983 3.743   -3.570  1.00 40.64  ? 62  HIS A CE1 1 
ATOM   509  N  NE2 . HIS A  1  62  ? 18.264 4.622   -2.622  1.00 40.07  ? 62  HIS A NE2 1 
ATOM   510  N  N   . ILE A  1  63  ? 22.984 5.368   -3.623  1.00 36.57  ? 63  ILE A N   1 
ATOM   511  C  CA  . ILE A  1  63  ? 23.124 6.814   -3.725  1.00 34.99  ? 63  ILE A CA  1 
ATOM   512  C  C   . ILE A  1  63  ? 23.522 7.177   -5.159  1.00 34.28  ? 63  ILE A C   1 
ATOM   513  O  O   . ILE A  1  63  ? 22.922 8.063   -5.772  1.00 35.27  ? 63  ILE A O   1 
ATOM   514  C  CB  . ILE A  1  63  ? 24.198 7.334   -2.752  1.00 33.98  ? 63  ILE A CB  1 
ATOM   515  C  CG1 . ILE A  1  63  ? 23.709 7.133   -1.315  1.00 34.55  ? 63  ILE A CG1 1 
ATOM   516  C  CG2 . ILE A  1  63  ? 24.500 8.804   -3.033  1.00 32.03  ? 63  ILE A CG2 1 
ATOM   517  C  CD1 . ILE A  1  63  ? 24.671 7.578   -0.261  1.00 31.86  ? 63  ILE A CD1 1 
ATOM   518  N  N   . ALA A  1  64  ? 24.505 6.458   -5.695  1.00 33.38  ? 64  ALA A N   1 
ATOM   519  C  CA  . ALA A  1  64  ? 24.993 6.711   -7.048  1.00 34.62  ? 64  ALA A CA  1 
ATOM   520  C  C   . ALA A  1  64  ? 23.897 6.504   -8.096  1.00 34.30  ? 64  ALA A C   1 
ATOM   521  O  O   . ALA A  1  64  ? 23.781 7.297   -9.045  1.00 33.40  ? 64  ALA A O   1 
ATOM   522  C  CB  . ALA A  1  64  ? 26.220 5.805   -7.365  1.00 31.28  ? 64  ALA A CB  1 
ATOM   523  N  N   . ARG A  1  65  ? 23.084 5.465   -7.915  1.00 32.73  ? 65  ARG A N   1 
ATOM   524  C  CA  . ARG A  1  65  ? 22.026 5.210   -8.879  1.00 31.84  ? 65  ARG A CA  1 
ATOM   525  C  C   . ARG A  1  65  ? 20.975 6.309   -8.850  1.00 32.61  ? 65  ARG A C   1 
ATOM   526  O  O   . ARG A  1  65  ? 20.513 6.767   -9.901  1.00 29.55  ? 65  ARG A O   1 
ATOM   527  C  CB  . ARG A  1  65  ? 21.372 3.843   -8.636  1.00 30.86  ? 65  ARG A CB  1 
ATOM   528  C  CG  . ARG A  1  65  ? 22.160 2.690   -9.258  1.00 28.65  ? 65  ARG A CG  1 
ATOM   529  C  CD  . ARG A  1  65  ? 21.408 1.368   -9.213  1.00 28.71  ? 65  ARG A CD  1 
ATOM   530  N  NE  . ARG A  1  65  ? 21.150 0.876   -7.844  1.00 31.11  ? 65  ARG A NE  1 
ATOM   531  C  CZ  . ARG A  1  65  ? 21.996 0.152   -7.102  1.00 29.65  ? 65  ARG A CZ  1 
ATOM   532  N  NH1 . ARG A  1  65  ? 23.194 -0.188  -7.566  1.00 32.85  ? 65  ARG A NH1 1 
ATOM   533  N  NH2 . ARG A  1  65  ? 21.635 -0.266  -5.898  1.00 28.32  ? 65  ARG A NH2 1 
ATOM   534  N  N   . VAL A  1  66  ? 20.623 6.741   -7.648  1.00 32.70  ? 66  VAL A N   1 
ATOM   535  C  CA  . VAL A  1  66  ? 19.620 7.776   -7.462  1.00 34.64  ? 66  VAL A CA  1 
ATOM   536  C  C   . VAL A  1  66  ? 20.018 9.142   -8.016  1.00 35.85  ? 66  VAL A C   1 
ATOM   537  O  O   . VAL A  1  66  ? 19.212 9.793   -8.663  1.00 35.57  ? 66  VAL A O   1 
ATOM   538  C  CB  . VAL A  1  66  ? 19.276 7.942   -5.971  1.00 36.09  ? 66  VAL A CB  1 
ATOM   539  C  CG1 . VAL A  1  66  ? 18.344 9.118   -5.773  1.00 35.37  ? 66  VAL A CG1 1 
ATOM   540  C  CG2 . VAL A  1  66  ? 18.658 6.670   -5.439  1.00 35.80  ? 66  VAL A CG2 1 
ATOM   541  N  N   . ILE A  1  67  ? 21.236 9.603   -7.752  1.00 37.04  ? 67  ILE A N   1 
ATOM   542  C  CA  . ILE A  1  67  ? 21.622 10.906  -8.267  1.00 36.54  ? 67  ILE A CA  1 
ATOM   543  C  C   . ILE A  1  67  ? 21.877 10.775  -9.753  1.00 36.69  ? 67  ILE A C   1 
ATOM   544  O  O   . ILE A  1  67  ? 21.720 11.733  -10.509 1.00 38.56  ? 67  ILE A O   1 
ATOM   545  C  CB  . ILE A  1  67  ? 22.869 11.479  -7.545  1.00 35.82  ? 67  ILE A CB  1 
ATOM   546  C  CG1 . ILE A  1  67  ? 24.047 10.516  -7.680  1.00 37.13  ? 67  ILE A CG1 1 
ATOM   547  C  CG2 . ILE A  1  67  ? 22.533 11.735  -6.053  1.00 35.36  ? 67  ILE A CG2 1 
ATOM   548  C  CD1 . ILE A  1  67  ? 25.293 11.031  -7.041  1.00 37.02  ? 67  ILE A CD1 1 
ATOM   549  N  N   . GLY A  1  68  ? 22.260 9.586   -10.187 1.00 36.53  ? 68  GLY A N   1 
ATOM   550  C  CA  . GLY A  1  68  ? 22.475 9.396   -11.610 1.00 36.41  ? 68  GLY A CA  1 
ATOM   551  C  C   . GLY A  1  68  ? 21.126 9.544   -12.306 1.00 38.02  ? 68  GLY A C   1 
ATOM   552  O  O   . GLY A  1  68  ? 21.029 10.080  -13.430 1.00 37.23  ? 68  GLY A O   1 
ATOM   553  N  N   . GLY A  1  69  ? 20.080 9.075   -11.617 1.00 37.31  ? 69  GLY A N   1 
ATOM   554  C  CA  . GLY A  1  69  ? 18.722 9.145   -12.129 1.00 36.82  ? 69  GLY A CA  1 
ATOM   555  C  C   . GLY A  1  69  ? 18.253 10.583  -12.160 1.00 37.36  ? 69  GLY A C   1 
ATOM   556  O  O   . GLY A  1  69  ? 17.687 11.038  -13.159 1.00 38.24  ? 69  GLY A O   1 
ATOM   557  N  N   . LEU A  1  70  ? 18.460 11.306  -11.066 1.00 35.76  ? 70  LEU A N   1 
ATOM   558  C  CA  . LEU A  1  70  ? 18.096 12.715  -11.041 1.00 35.87  ? 70  LEU A CA  1 
ATOM   559  C  C   . LEU A  1  70  ? 18.813 13.391  -12.215 1.00 37.12  ? 70  LEU A C   1 
ATOM   560  O  O   . LEU A  1  70  ? 18.203 14.143  -12.977 1.00 40.21  ? 70  LEU A O   1 
ATOM   561  C  CB  . LEU A  1  70  ? 18.563 13.352  -9.738  1.00 34.33  ? 70  LEU A CB  1 
ATOM   562  C  CG  . LEU A  1  70  ? 17.592 13.198  -8.575  1.00 34.94  ? 70  LEU A CG  1 
ATOM   563  C  CD1 . LEU A  1  70  ? 18.275 13.509  -7.232  1.00 33.70  ? 70  LEU A CD1 1 
ATOM   564  C  CD2 . LEU A  1  70  ? 16.393 14.131  -8.841  1.00 34.98  ? 70  LEU A CD2 1 
ATOM   565  N  N   . ASP A  1  71  ? 20.105 13.110  -12.371 1.00 35.92  ? 71  ASP A N   1 
ATOM   566  C  CA  . ASP A  1  71  ? 20.884 13.710  -13.455 1.00 34.68  ? 71  ASP A CA  1 
ATOM   567  C  C   . ASP A  1  71  ? 20.387 13.433  -14.875 1.00 35.31  ? 71  ASP A C   1 
ATOM   568  O  O   . ASP A  1  71  ? 20.287 14.353  -15.692 1.00 34.93  ? 71  ASP A O   1 
ATOM   569  C  CB  . ASP A  1  71  ? 22.355 13.304  -13.373 1.00 32.61  ? 71  ASP A CB  1 
ATOM   570  C  CG  . ASP A  1  71  ? 23.188 13.933  -14.492 1.00 33.25  ? 71  ASP A CG  1 
ATOM   571  O  OD1 . ASP A  1  71  ? 23.548 15.132  -14.342 1.00 31.05  ? 71  ASP A OD1 1 
ATOM   572  O  OD2 . ASP A  1  71  ? 23.454 13.243  -15.523 1.00 35.27  ? 71  ASP A OD2 1 
ATOM   573  N  N   . ARG A  1  72  ? 20.101 12.176  -15.192 1.00 37.94  ? 72  ARG A N   1 
ATOM   574  C  CA  . ARG A  1  72  ? 19.616 11.845  -16.537 1.00 38.65  ? 72  ARG A CA  1 
ATOM   575  C  C   . ARG A  1  72  ? 18.219 12.422  -16.757 1.00 39.11  ? 72  ARG A C   1 
ATOM   576  O  O   . ARG A  1  72  ? 17.871 12.820  -17.877 1.00 40.00  ? 72  ARG A O   1 
ATOM   577  C  CB  . ARG A  1  72  ? 19.586 10.343  -16.728 1.00 39.43  ? 72  ARG A CB  1 
ATOM   578  C  CG  . ARG A  1  72  ? 18.534 9.665   -15.919 1.00 42.59  ? 72  ARG A CG  1 
ATOM   579  C  CD  . ARG A  1  72  ? 18.680 8.177   -16.043 1.00 43.61  ? 72  ARG A CD  1 
ATOM   580  N  NE  . ARG A  1  72  ? 17.381 7.542   -15.918 1.00 45.01  ? 72  ARG A NE  1 
ATOM   581  C  CZ  . ARG A  1  72  ? 17.173 6.410   -15.274 1.00 43.61  ? 72  ARG A CZ  1 
ATOM   582  N  NH1 . ARG A  1  72  ? 18.188 5.796   -14.707 1.00 47.01  ? 72  ARG A NH1 1 
ATOM   583  N  NH2 . ARG A  1  72  ? 15.955 5.916   -15.185 1.00 44.86  ? 72  ARG A NH2 1 
ATOM   584  N  N   . VAL A  1  73  ? 17.422 12.489  -15.692 1.00 37.14  ? 73  VAL A N   1 
ATOM   585  C  CA  . VAL A  1  73  ? 16.086 13.057  -15.824 1.00 36.58  ? 73  VAL A CA  1 
ATOM   586  C  C   . VAL A  1  73  ? 16.197 14.561  -16.073 1.00 37.17  ? 73  VAL A C   1 
ATOM   587  O  O   . VAL A  1  73  ? 15.543 15.097  -16.970 1.00 35.91  ? 73  VAL A O   1 
ATOM   588  C  CB  . VAL A  1  73  ? 15.221 12.808  -14.559 1.00 34.57  ? 73  VAL A CB  1 
ATOM   589  C  CG1 . VAL A  1  73  ? 14.081 13.806  -14.492 1.00 34.04  ? 73  VAL A CG1 1 
ATOM   590  C  CG2 . VAL A  1  73  ? 14.669 11.398  -14.589 1.00 32.11  ? 73  VAL A CG2 1 
ATOM   591  N  N   . ILE A  1  74  ? 17.032 15.239  -15.291 1.00 38.06  ? 74  ILE A N   1 
ATOM   592  C  CA  . ILE A  1  74  ? 17.193 16.685  -15.452 1.00 39.23  ? 74  ILE A CA  1 
ATOM   593  C  C   . ILE A  1  74  ? 17.766 17.004  -16.832 1.00 39.03  ? 74  ILE A C   1 
ATOM   594  O  O   . ILE A  1  74  ? 17.423 18.024  -17.425 1.00 38.63  ? 74  ILE A O   1 
ATOM   595  C  CB  . ILE A  1  74  ? 18.089 17.290  -14.310 1.00 38.63  ? 74  ILE A CB  1 
ATOM   596  C  CG1 . ILE A  1  74  ? 17.296 17.277  -13.000 1.00 36.18  ? 74  ILE A CG1 1 
ATOM   597  C  CG2 . ILE A  1  74  ? 18.530 18.729  -14.640 1.00 34.46  ? 74  ILE A CG2 1 
ATOM   598  C  CD1 . ILE A  1  74  ? 18.116 17.636  -11.781 1.00 35.57  ? 74  ILE A CD1 1 
ATOM   599  N  N   . SER A  1  75  ? 18.592 16.117  -17.366 1.00 39.88  ? 75  SER A N   1 
ATOM   600  C  CA  . SER A  1  75  ? 19.179 16.366  -18.684 1.00 45.23  ? 75  SER A CA  1 
ATOM   601  C  C   . SER A  1  75  ? 18.156 16.262  -19.794 1.00 46.15  ? 75  SER A C   1 
ATOM   602  O  O   . SER A  1  75  ? 18.352 16.832  -20.854 1.00 47.09  ? 75  SER A O   1 
ATOM   603  C  CB  . SER A  1  75  ? 20.333 15.397  -18.988 1.00 45.11  ? 75  SER A CB  1 
ATOM   604  O  OG  . SER A  1  75  ? 19.862 14.117  -19.386 1.00 47.87  ? 75  SER A OG  1 
ATOM   605  N  N   . MET A  1  76  ? 17.083 15.512  -19.559 1.00 48.82  ? 76  MET A N   1 
ATOM   606  C  CA  . MET A  1  76  ? 16.019 15.353  -20.551 1.00 51.28  ? 76  MET A CA  1 
ATOM   607  C  C   . MET A  1  76  ? 14.902 16.400  -20.358 1.00 52.08  ? 76  MET A C   1 
ATOM   608  O  O   . MET A  1  76  ? 13.935 16.429  -21.112 1.00 50.93  ? 76  MET A O   1 
ATOM   609  C  CB  . MET A  1  76  ? 15.430 13.921  -20.483 1.00 50.81  ? 76  MET A CB  1 
ATOM   610  C  CG  . MET A  1  76  ? 16.409 12.828  -20.946 1.00 54.71  ? 76  MET A CG  1 
ATOM   611  S  SD  . MET A  1  76  ? 15.731 11.124  -21.016 1.00 57.89  ? 76  MET A SD  1 
ATOM   612  C  CE  . MET A  1  76  ? 15.964 10.561  -19.265 1.00 53.97  ? 76  MET A CE  1 
ATOM   613  N  N   . PHE A  1  77  ? 15.044 17.271  -19.359 1.00 53.34  ? 77  PHE A N   1 
ATOM   614  C  CA  . PHE A  1  77  ? 14.030 18.298  -19.105 1.00 55.71  ? 77  PHE A CA  1 
ATOM   615  C  C   . PHE A  1  77  ? 13.495 18.996  -20.367 1.00 58.02  ? 77  PHE A C   1 
ATOM   616  O  O   . PHE A  1  77  ? 12.342 19.426  -20.410 1.00 57.82  ? 77  PHE A O   1 
ATOM   617  C  CB  . PHE A  1  77  ? 14.569 19.370  -18.139 1.00 53.98  ? 77  PHE A CB  1 
ATOM   618  C  CG  . PHE A  1  77  ? 14.126 19.191  -16.713 1.00 52.08  ? 77  PHE A CG  1 
ATOM   619  C  CD1 . PHE A  1  77  ? 13.027 18.399  -16.399 1.00 51.20  ? 77  PHE A CD1 1 
ATOM   620  C  CD2 . PHE A  1  77  ? 14.783 19.846  -15.679 1.00 51.91  ? 77  PHE A CD2 1 
ATOM   621  C  CE1 . PHE A  1  77  ? 12.600 18.270  -15.078 1.00 48.51  ? 77  PHE A CE1 1 
ATOM   622  C  CE2 . PHE A  1  77  ? 14.349 19.716  -14.353 1.00 47.99  ? 77  PHE A CE2 1 
ATOM   623  C  CZ  . PHE A  1  77  ? 13.266 18.933  -14.058 1.00 45.96  ? 77  PHE A CZ  1 
ATOM   624  N  N   . ASP A  1  78  ? 14.327 19.108  -21.394 1.00 61.42  ? 78  ASP A N   1 
ATOM   625  C  CA  . ASP A  1  78  ? 13.915 19.776  -22.627 1.00 66.70  ? 78  ASP A CA  1 
ATOM   626  C  C   . ASP A  1  78  ? 13.216 18.895  -23.665 1.00 68.14  ? 78  ASP A C   1 
ATOM   627  O  O   . ASP A  1  78  ? 12.624 19.413  -24.613 1.00 69.17  ? 78  ASP A O   1 
ATOM   628  C  CB  . ASP A  1  78  ? 15.127 20.448  -23.283 1.00 69.34  ? 78  ASP A CB  1 
ATOM   629  C  CG  . ASP A  1  78  ? 16.395 19.596  -23.193 1.00 72.84  ? 78  ASP A CG  1 
ATOM   630  O  OD1 . ASP A  1  78  ? 16.292 18.363  -22.961 1.00 72.41  ? 78  ASP A OD1 1 
ATOM   631  O  OD2 . ASP A  1  78  ? 17.500 20.165  -23.363 1.00 74.51  ? 78  ASP A OD2 1 
ATOM   632  N  N   . ASN A  1  79  ? 13.293 17.577  -23.506 1.00 68.47  ? 79  ASN A N   1 
ATOM   633  C  CA  . ASN A  1  79  ? 12.648 16.668  -24.451 1.00 69.13  ? 79  ASN A CA  1 
ATOM   634  C  C   . ASN A  1  79  ? 11.604 15.824  -23.731 1.00 68.31  ? 79  ASN A C   1 
ATOM   635  O  O   . ASN A  1  79  ? 11.903 14.773  -23.171 1.00 68.01  ? 79  ASN A O   1 
ATOM   636  C  CB  . ASN A  1  79  ? 13.689 15.776  -25.131 1.00 71.47  ? 79  ASN A CB  1 
ATOM   637  C  CG  . ASN A  1  79  ? 13.110 15.010  -26.310 1.00 74.84  ? 79  ASN A CG  1 
ATOM   638  O  OD1 . ASN A  1  79  ? 12.404 14.015  -26.140 1.00 77.02  ? 79  ASN A OD1 1 
ATOM   639  N  ND2 . ASN A  1  79  ? 13.388 15.487  -27.516 1.00 76.04  ? 79  ASN A ND2 1 
ATOM   640  N  N   . GLU A  1  80  ? 10.361 16.306  -23.766 1.00 68.04  ? 80  GLU A N   1 
ATOM   641  C  CA  . GLU A  1  80  ? 9.226  15.651  -23.112 1.00 68.13  ? 80  GLU A CA  1 
ATOM   642  C  C   . GLU A  1  80  ? 9.074  14.164  -23.473 1.00 66.60  ? 80  GLU A C   1 
ATOM   643  O  O   . GLU A  1  80  ? 8.762  13.335  -22.617 1.00 65.85  ? 80  GLU A O   1 
ATOM   644  C  CB  . GLU A  1  80  ? 7.957  16.439  -23.443 1.00 70.78  ? 80  GLU A CB  1 
ATOM   645  C  CG  . GLU A  1  80  ? 6.697  15.981  -22.724 1.00 76.98  ? 80  GLU A CG  1 
ATOM   646  C  CD  . GLU A  1  80  ? 6.227  16.957  -21.654 1.00 80.70  ? 80  GLU A CD  1 
ATOM   647  O  OE1 . GLU A  1  80  ? 5.018  16.945  -21.339 1.00 81.99  ? 80  GLU A OE1 1 
ATOM   648  O  OE2 . GLU A  1  80  ? 7.055  17.725  -21.121 1.00 83.08  ? 80  GLU A OE2 1 
ATOM   649  N  N   . ASP A  1  81  ? 9.289  13.818  -24.736 1.00 64.67  ? 81  ASP A N   1 
ATOM   650  C  CA  . ASP A  1  81  ? 9.164  12.423  -25.148 1.00 62.44  ? 81  ASP A CA  1 
ATOM   651  C  C   . ASP A  1  81  ? 10.088 11.478  -24.363 1.00 59.19  ? 81  ASP A C   1 
ATOM   652  O  O   . ASP A  1  81  ? 9.645  10.450  -23.833 1.00 57.94  ? 81  ASP A O   1 
ATOM   653  C  CB  . ASP A  1  81  ? 9.460  12.283  -26.646 1.00 66.39  ? 81  ASP A CB  1 
ATOM   654  C  CG  . ASP A  1  81  ? 8.300  12.727  -27.519 1.00 69.40  ? 81  ASP A CG  1 
ATOM   655  O  OD1 . ASP A  1  81  ? 7.143  12.372  -27.194 1.00 70.31  ? 81  ASP A OD1 1 
ATOM   656  O  OD2 . ASP A  1  81  ? 8.535  13.416  -28.533 1.00 71.87  ? 81  ASP A OD2 1 
ATOM   657  N  N   . ALA A  1  82  ? 11.372 11.819  -24.312 1.00 53.48  ? 82  ALA A N   1 
ATOM   658  C  CA  . ALA A  1  82  ? 12.347 11.014  -23.595 1.00 49.22  ? 82  ALA A CA  1 
ATOM   659  C  C   . ALA A  1  82  ? 12.136 11.117  -22.093 1.00 46.47  ? 82  ALA A C   1 
ATOM   660  O  O   . ALA A  1  82  ? 12.271 10.131  -21.378 1.00 45.30  ? 82  ALA A O   1 
ATOM   661  C  CB  . ALA A  1  82  ? 13.764 11.474  -23.940 1.00 50.67  ? 82  ALA A CB  1 
ATOM   662  N  N   . LEU A  1  83  ? 11.816 12.320  -21.621 1.00 43.11  ? 83  LEU A N   1 
ATOM   663  C  CA  . LEU A  1  83  ? 11.605 12.569  -20.209 1.00 40.71  ? 83  LEU A CA  1 
ATOM   664  C  C   . LEU A  1  83  ? 10.465 11.735  -19.635 1.00 41.39  ? 83  LEU A C   1 
ATOM   665  O  O   . LEU A  1  83  ? 10.616 11.062  -18.605 1.00 41.61  ? 83  LEU A O   1 
ATOM   666  C  CB  . LEU A  1  83  ? 11.312 14.051  -19.991 1.00 40.53  ? 83  LEU A CB  1 
ATOM   667  C  CG  . LEU A  1  83  ? 10.940 14.464  -18.565 1.00 40.08  ? 83  LEU A CG  1 
ATOM   668  C  CD1 . LEU A  1  83  ? 12.115 14.241  -17.645 1.00 38.70  ? 83  LEU A CD1 1 
ATOM   669  C  CD2 . LEU A  1  83  ? 10.514 15.927  -18.550 1.00 40.31  ? 83  LEU A CD2 1 
ATOM   670  N  N   . ASN A  1  84  ? 9.318  11.772  -20.298 1.00 40.17  ? 84  ASN A N   1 
ATOM   671  C  CA  . ASN A  1  84  ? 8.183  11.005  -19.821 1.00 39.49  ? 84  ASN A CA  1 
ATOM   672  C  C   . ASN A  1  84  ? 8.393  9.493   -19.933 1.00 39.69  ? 84  ASN A C   1 
ATOM   673  O  O   . ASN A  1  84  ? 7.987  8.738   -19.046 1.00 40.15  ? 84  ASN A O   1 
ATOM   674  C  CB  . ASN A  1  84  ? 6.923  11.445  -20.546 1.00 35.49  ? 84  ASN A CB  1 
ATOM   675  C  CG  . ASN A  1  84  ? 6.540  12.849  -20.192 1.00 34.23  ? 84  ASN A CG  1 
ATOM   676  O  OD1 . ASN A  1  84  ? 6.656  13.253  -19.037 1.00 32.11  ? 84  ASN A OD1 1 
ATOM   677  N  ND2 . ASN A  1  84  ? 6.078  13.611  -21.176 1.00 32.25  ? 84  ASN A ND2 1 
ATOM   678  N  N   . ALA A  1  85  ? 9.029  9.047   -21.003 1.00 37.82  ? 85  ALA A N   1 
ATOM   679  C  CA  . ALA A  1  85  ? 9.266  7.628   -21.132 1.00 39.74  ? 85  ALA A CA  1 
ATOM   680  C  C   . ALA A  1  85  ? 10.193 7.222   -19.997 1.00 42.08  ? 85  ALA A C   1 
ATOM   681  O  O   . ALA A  1  85  ? 10.065 6.125   -19.440 1.00 43.43  ? 85  ALA A O   1 
ATOM   682  C  CB  . ALA A  1  85  ? 9.909  7.309   -22.475 1.00 35.12  ? 85  ALA A CB  1 
ATOM   683  N  N   . ASP A  1  86  ? 11.116 8.106   -19.623 1.00 41.40  ? 86  ASP A N   1 
ATOM   684  C  CA  . ASP A  1  86  ? 12.029 7.727   -18.570 1.00 41.75  ? 86  ASP A CA  1 
ATOM   685  C  C   . ASP A  1  86  ? 11.397 7.829   -17.200 1.00 40.48  ? 86  ASP A C   1 
ATOM   686  O  O   . ASP A  1  86  ? 11.730 7.044   -16.320 1.00 40.13  ? 86  ASP A O   1 
ATOM   687  C  CB  . ASP A  1  86  ? 13.320 8.534   -18.640 1.00 44.16  ? 86  ASP A CB  1 
ATOM   688  C  CG  . ASP A  1  86  ? 14.423 7.933   -17.778 1.00 45.73  ? 86  ASP A CG  1 
ATOM   689  O  OD1 . ASP A  1  86  ? 14.625 6.704   -17.872 1.00 46.05  ? 86  ASP A OD1 1 
ATOM   690  O  OD2 . ASP A  1  86  ? 15.085 8.681   -17.017 1.00 49.18  ? 86  ASP A OD2 1 
ATOM   691  N  N   . LEU A  1  87  ? 10.495 8.784   -17.008 1.00 40.50  ? 87  LEU A N   1 
ATOM   692  C  CA  . LEU A  1  87  ? 9.826  8.902   -15.713 1.00 42.46  ? 87  LEU A CA  1 
ATOM   693  C  C   . LEU A  1  87  ? 8.909  7.673   -15.548 1.00 43.35  ? 87  LEU A C   1 
ATOM   694  O  O   . LEU A  1  87  ? 8.771  7.125   -14.446 1.00 41.42  ? 87  LEU A O   1 
ATOM   695  C  CB  . LEU A  1  87  ? 9.025  10.215  -15.628 1.00 43.07  ? 87  LEU A CB  1 
ATOM   696  C  CG  . LEU A  1  87  ? 9.845  11.514  -15.613 1.00 44.54  ? 87  LEU A CG  1 
ATOM   697  C  CD1 . LEU A  1  87  ? 8.941  12.749  -15.759 1.00 42.23  ? 87  LEU A CD1 1 
ATOM   698  C  CD2 . LEU A  1  87  ? 10.624 11.558  -14.306 1.00 44.18  ? 87  LEU A CD2 1 
ATOM   699  N  N   . GLU A  1  88  ? 8.306  7.229   -16.649 1.00 44.15  ? 88  GLU A N   1 
ATOM   700  C  CA  . GLU A  1  88  ? 7.451  6.039   -16.621 1.00 47.40  ? 88  GLU A CA  1 
ATOM   701  C  C   . GLU A  1  88  ? 8.297  4.841   -16.160 1.00 46.16  ? 88  GLU A C   1 
ATOM   702  O  O   . GLU A  1  88  ? 7.873  4.019   -15.325 1.00 42.06  ? 88  GLU A O   1 
ATOM   703  C  CB  . GLU A  1  88  ? 6.882  5.741   -18.016 1.00 53.05  ? 88  GLU A CB  1 
ATOM   704  C  CG  . GLU A  1  88  ? 5.864  6.758   -18.541 1.00 61.05  ? 88  GLU A CG  1 
ATOM   705  C  CD  . GLU A  1  88  ? 5.345  6.394   -19.933 1.00 66.14  ? 88  GLU A CD  1 
ATOM   706  O  OE1 . GLU A  1  88  ? 4.847  5.256   -20.096 1.00 68.51  ? 88  GLU A OE1 1 
ATOM   707  O  OE2 . GLU A  1  88  ? 5.433  7.232   -20.864 1.00 68.17  ? 88  GLU A OE2 1 
ATOM   708  N  N   . HIS A  1  89  ? 9.500  4.756   -16.719 1.00 45.86  ? 89  HIS A N   1 
ATOM   709  C  CA  . HIS A  1  89  ? 10.442 3.698   -16.380 1.00 44.93  ? 89  HIS A CA  1 
ATOM   710  C  C   . HIS A  1  89  ? 10.704 3.725   -14.864 1.00 45.57  ? 89  HIS A C   1 
ATOM   711  O  O   . HIS A  1  89  ? 10.553 2.716   -14.160 1.00 45.16  ? 89  HIS A O   1 
ATOM   712  C  CB  . HIS A  1  89  ? 11.750 3.922   -17.146 1.00 45.62  ? 89  HIS A CB  1 
ATOM   713  C  CG  . HIS A  1  89  ? 12.715 2.786   -17.031 1.00 47.99  ? 89  HIS A CG  1 
ATOM   714  N  ND1 . HIS A  1  89  ? 12.651 1.669   -17.833 1.00 49.80  ? 89  HIS A ND1 1 
ATOM   715  C  CD2 . HIS A  1  89  ? 13.749 2.581   -16.180 1.00 47.95  ? 89  HIS A CD2 1 
ATOM   716  C  CE1 . HIS A  1  89  ? 13.603 0.825   -17.486 1.00 49.02  ? 89  HIS A CE1 1 
ATOM   717  N  NE2 . HIS A  1  89  ? 14.283 1.353   -16.484 1.00 48.22  ? 89  HIS A NE2 1 
ATOM   718  N  N   . LEU A  1  90  ? 11.087 4.894   -14.355 1.00 43.49  ? 90  LEU A N   1 
ATOM   719  C  CA  . LEU A  1  90  ? 11.370 5.020   -12.932 1.00 42.99  ? 90  LEU A CA  1 
ATOM   720  C  C   . LEU A  1  90  ? 10.127 4.680   -12.130 1.00 44.28  ? 90  LEU A C   1 
ATOM   721  O  O   . LEU A  1  90  ? 10.210 4.182   -10.985 1.00 41.37  ? 90  LEU A O   1 
ATOM   722  C  CB  . LEU A  1  90  ? 11.806 6.445   -12.598 1.00 41.38  ? 90  LEU A CB  1 
ATOM   723  C  CG  . LEU A  1  90  ? 13.094 6.922   -13.241 1.00 39.63  ? 90  LEU A CG  1 
ATOM   724  C  CD1 . LEU A  1  90  ? 13.347 8.370   -12.868 1.00 36.28  ? 90  LEU A CD1 1 
ATOM   725  C  CD2 . LEU A  1  90  ? 14.213 6.033   -12.772 1.00 40.54  ? 90  LEU A CD2 1 
ATOM   726  N  N   . LYS A  1  91  ? 8.964  4.987   -12.724 1.00 44.05  ? 91  LYS A N   1 
ATOM   727  C  CA  . LYS A  1  91  ? 7.704  4.734   -12.044 1.00 43.79  ? 91  LYS A CA  1 
ATOM   728  C  C   . LYS A  1  91  ? 7.458  3.239   -11.902 1.00 43.78  ? 91  LYS A C   1 
ATOM   729  O  O   . LYS A  1  91  ? 7.120  2.770   -10.799 1.00 43.44  ? 91  LYS A O   1 
ATOM   730  C  CB  . LYS A  1  91  ? 6.529  5.392   -12.778 1.00 44.79  ? 91  LYS A CB  1 
ATOM   731  C  CG  . LYS A  1  91  ? 5.206  5.191   -12.057 1.00 41.56  ? 91  LYS A CG  1 
ATOM   732  C  CD  . LYS A  1  91  ? 4.124  6.123   -12.606 1.00 41.72  ? 91  LYS A CD  1 
ATOM   733  C  CE  . LYS A  1  91  ? 2.754  5.843   -11.974 1.00 39.82  ? 91  LYS A CE  1 
ATOM   734  N  NZ  . LYS A  1  91  ? 2.257  4.481   -12.273 1.00 35.68  ? 91  LYS A NZ  1 
ATOM   735  N  N   . SER A  1  92  ? 7.645  2.488   -12.990 1.00 42.11  ? 92  SER A N   1 
ATOM   736  C  CA  . SER A  1  92  ? 7.433  1.047   -12.909 1.00 42.47  ? 92  SER A CA  1 
ATOM   737  C  C   . SER A  1  92  ? 8.412  0.406   -11.919 1.00 41.02  ? 92  SER A C   1 
ATOM   738  O  O   . SER A  1  92  ? 8.195  -0.709  -11.469 1.00 42.21  ? 92  SER A O   1 
ATOM   739  C  CB  . SER A  1  92  ? 7.542  0.386   -14.297 1.00 42.67  ? 92  SER A CB  1 
ATOM   740  O  OG  . SER A  1  92  ? 8.879  0.301   -14.744 1.00 46.74  ? 92  SER A OG  1 
ATOM   741  N  N   . GLN A  1  93  ? 9.469  1.125   -11.547 1.00 39.08  ? 93  GLN A N   1 
ATOM   742  C  CA  . GLN A  1  93  ? 10.420 0.592   -10.580 1.00 38.58  ? 93  GLN A CA  1 
ATOM   743  C  C   . GLN A  1  93  ? 10.073 0.962   -9.140  1.00 39.00  ? 93  GLN A C   1 
ATOM   744  O  O   . GLN A  1  93  ? 10.478 0.270   -8.213  1.00 42.03  ? 93  GLN A O   1 
ATOM   745  C  CB  . GLN A  1  93  ? 11.841 1.084   -10.872 1.00 40.61  ? 93  GLN A CB  1 
ATOM   746  C  CG  . GLN A  1  93  ? 12.421 0.596   -12.187 1.00 40.71  ? 93  GLN A CG  1 
ATOM   747  C  CD  . GLN A  1  93  ? 13.741 1.238   -12.503 1.00 40.53  ? 93  GLN A CD  1 
ATOM   748  O  OE1 . GLN A  1  93  ? 13.847 2.459   -12.575 1.00 44.86  ? 93  GLN A OE1 1 
ATOM   749  N  NE2 . GLN A  1  93  ? 14.762 0.418   -12.701 1.00 40.64  ? 93  GLN A NE2 1 
ATOM   750  N  N   . HIS A  1  94  ? 9.348  2.058   -8.936  1.00 38.38  ? 94  HIS A N   1 
ATOM   751  C  CA  . HIS A  1  94  ? 8.991  2.444   -7.586  1.00 37.96  ? 94  HIS A CA  1 
ATOM   752  C  C   . HIS A  1  94  ? 7.589  1.978   -7.175  1.00 39.60  ? 94  HIS A C   1 
ATOM   753  O  O   . HIS A  1  94  ? 7.308  1.819   -5.976  1.00 36.88  ? 94  HIS A O   1 
ATOM   754  C  CB  . HIS A  1  94  ? 9.096  3.962   -7.412  1.00 38.89  ? 94  HIS A CB  1 
ATOM   755  C  CG  . HIS A  1  94  ? 10.508 4.479   -7.373  1.00 40.51  ? 94  HIS A CG  1 
ATOM   756  N  ND1 . HIS A  1  94  ? 11.248 4.693   -8.519  1.00 39.51  ? 94  HIS A ND1 1 
ATOM   757  C  CD2 . HIS A  1  94  ? 11.302 4.859   -6.342  1.00 39.66  ? 94  HIS A CD2 1 
ATOM   758  C  CE1 . HIS A  1  94  ? 12.432 5.182   -8.189  1.00 38.45  ? 94  HIS A CE1 1 
ATOM   759  N  NE2 . HIS A  1  94  ? 12.486 5.293   -6.878  1.00 38.73  ? 94  HIS A NE2 1 
ATOM   760  N  N   . ASP A  1  95  ? 6.715  1.765   -8.162  1.00 40.27  ? 95  ASP A N   1 
ATOM   761  C  CA  . ASP A  1  95  ? 5.342  1.326   -7.913  1.00 40.53  ? 95  ASP A CA  1 
ATOM   762  C  C   . ASP A  1  95  ? 5.236  0.059   -7.060  1.00 40.94  ? 95  ASP A C   1 
ATOM   763  O  O   . ASP A  1  95  ? 4.559  0.038   -6.028  1.00 40.22  ? 95  ASP A O   1 
ATOM   764  C  CB  . ASP A  1  95  ? 4.620  1.086   -9.249  1.00 40.40  ? 95  ASP A CB  1 
ATOM   765  C  CG  . ASP A  1  95  ? 3.897  2.322   -9.780  1.00 41.10  ? 95  ASP A CG  1 
ATOM   766  O  OD1 . ASP A  1  95  ? 3.732  3.302   -9.023  1.00 39.32  ? 95  ASP A OD1 1 
ATOM   767  O  OD2 . ASP A  1  95  ? 3.479  2.294   -10.970 1.00 41.88  ? 95  ASP A OD2 1 
ATOM   768  N  N   . PRO A  1  96  ? 5.921  -1.031  -7.470  1.00 42.58  ? 96  PRO A N   1 
ATOM   769  C  CA  . PRO A  1  96  ? 5.815  -2.262  -6.665  1.00 42.98  ? 96  PRO A CA  1 
ATOM   770  C  C   . PRO A  1  96  ? 6.351  -2.219  -5.254  1.00 43.23  ? 96  PRO A C   1 
ATOM   771  O  O   . PRO A  1  96  ? 6.328  -3.228  -4.566  1.00 45.63  ? 96  PRO A O   1 
ATOM   772  C  CB  . PRO A  1  96  ? 6.530  -3.312  -7.530  1.00 41.31  ? 96  PRO A CB  1 
ATOM   773  C  CG  . PRO A  1  96  ? 7.504  -2.503  -8.325  1.00 42.66  ? 96  PRO A CG  1 
ATOM   774  C  CD  . PRO A  1  96  ? 6.748  -1.249  -8.675  1.00 41.08  ? 96  PRO A CD  1 
ATOM   775  N  N   . ARG A  1  97  ? 6.807  -1.053  -4.818  1.00 44.02  ? 97  ARG A N   1 
ATOM   776  C  CA  . ARG A  1  97  ? 7.351  -0.931  -3.468  1.00 44.26  ? 97  ARG A CA  1 
ATOM   777  C  C   . ARG A  1  97  ? 6.373  -0.300  -2.495  1.00 43.53  ? 97  ARG A C   1 
ATOM   778  O  O   . ARG A  1  97  ? 6.716  -0.090  -1.332  1.00 41.90  ? 97  ARG A O   1 
ATOM   779  C  CB  . ARG A  1  97  ? 8.643  -0.112  -3.480  1.00 48.72  ? 97  ARG A CB  1 
ATOM   780  C  CG  . ARG A  1  97  ? 9.797  -0.810  -4.181  1.00 54.27  ? 97  ARG A CG  1 
ATOM   781  C  CD  . ARG A  1  97  ? 10.802 -1.342  -3.185  1.00 59.72  ? 97  ARG A CD  1 
ATOM   782  N  NE  . ARG A  1  97  ? 11.803 -2.214  -3.808  1.00 64.17  ? 97  ARG A NE  1 
ATOM   783  C  CZ  . ARG A  1  97  ? 12.455 -1.938  -4.939  1.00 66.19  ? 97  ARG A CZ  1 
ATOM   784  N  NH1 . ARG A  1  97  ? 12.226 -0.798  -5.599  1.00 64.53  ? 97  ARG A NH1 1 
ATOM   785  N  NH2 . ARG A  1  97  ? 13.348 -2.805  -5.412  1.00 65.14  ? 97  ARG A NH2 1 
ATOM   786  N  N   . GLY A  1  98  ? 5.169  0.007   -2.989  1.00 42.20  ? 98  GLY A N   1 
ATOM   787  C  CA  . GLY A  1  98  ? 4.135  0.605   -2.165  1.00 40.97  ? 98  GLY A CA  1 
ATOM   788  C  C   . GLY A  1  98  ? 4.641  1.755   -1.319  1.00 40.62  ? 98  GLY A C   1 
ATOM   789  O  O   . GLY A  1  98  ? 4.405  1.804   -0.112  1.00 38.93  ? 98  GLY A O   1 
ATOM   790  N  N   . LEU A  1  99  ? 5.331  2.683   -1.967  1.00 41.12  ? 99  LEU A N   1 
ATOM   791  C  CA  . LEU A  1  99  ? 5.918  3.828   -1.280  1.00 42.34  ? 99  LEU A CA  1 
ATOM   792  C  C   . LEU A  1  99  ? 4.934  4.968   -1.018  1.00 41.61  ? 99  LEU A C   1 
ATOM   793  O  O   . LEU A  1  99  ? 4.240  5.423   -1.927  1.00 40.08  ? 99  LEU A O   1 
ATOM   794  C  CB  . LEU A  1  99  ? 7.100  4.355   -2.091  1.00 42.97  ? 99  LEU A CB  1 
ATOM   795  C  CG  . LEU A  1  99  ? 8.217  3.362   -2.435  1.00 45.23  ? 99  LEU A CG  1 
ATOM   796  C  CD1 . LEU A  1  99  ? 9.274  4.079   -3.295  1.00 46.52  ? 99  LEU A CD1 1 
ATOM   797  C  CD2 . LEU A  1  99  ? 8.860  2.817   -1.172  1.00 46.16  ? 99  LEU A CD2 1 
ATOM   798  N  N   . ASP A  1  100 ? 4.879  5.428   0.226   1.00 41.79  ? 100 ASP A N   1 
ATOM   799  C  CA  . ASP A  1  100 ? 4.000  6.526   0.582   1.00 42.31  ? 100 ASP A CA  1 
ATOM   800  C  C   . ASP A  1  100 ? 4.500  7.794   -0.119  1.00 41.76  ? 100 ASP A C   1 
ATOM   801  O  O   . ASP A  1  100 ? 5.632  8.205   0.088   1.00 41.67  ? 100 ASP A O   1 
ATOM   802  C  CB  . ASP A  1  100 ? 4.030  6.729   2.092   1.00 46.02  ? 100 ASP A CB  1 
ATOM   803  C  CG  . ASP A  1  100 ? 3.028  7.768   2.567   1.00 51.83  ? 100 ASP A CG  1 
ATOM   804  O  OD1 . ASP A  1  100 ? 2.920  8.864   1.963   1.00 51.41  ? 100 ASP A OD1 1 
ATOM   805  O  OD2 . ASP A  1  100 ? 2.347  7.487   3.574   1.00 57.50  ? 100 ASP A OD2 1 
ATOM   806  N  N   . ALA A  1  101 ? 3.660  8.407   -0.942  1.00 41.99  ? 101 ALA A N   1 
ATOM   807  C  CA  . ALA A  1  101 ? 4.015  9.634   -1.669  1.00 42.00  ? 101 ALA A CA  1 
ATOM   808  C  C   . ALA A  1  101 ? 4.593  10.801  -0.830  1.00 43.11  ? 101 ALA A C   1 
ATOM   809  O  O   . ALA A  1  101 ? 5.371  11.612  -1.341  1.00 40.83  ? 101 ALA A O   1 
ATOM   810  C  CB  . ALA A  1  101 ? 2.803  10.129  -2.454  1.00 39.71  ? 101 ALA A CB  1 
ATOM   811  N  N   . LEU A  1  102 ? 4.213  10.904  0.444   1.00 44.74  ? 102 LEU A N   1 
ATOM   812  C  CA  . LEU A  1  102 ? 4.724  11.979  1.289   1.00 45.46  ? 102 LEU A CA  1 
ATOM   813  C  C   . LEU A  1  102 ? 6.246  11.957  1.370   1.00 44.83  ? 102 LEU A C   1 
ATOM   814  O  O   . LEU A  1  102 ? 6.872  12.983  1.630   1.00 45.26  ? 102 LEU A O   1 
ATOM   815  C  CB  . LEU A  1  102 ? 4.127  11.888  2.693   1.00 47.89  ? 102 LEU A CB  1 
ATOM   816  C  CG  . LEU A  1  102 ? 2.638  12.255  2.777   1.00 53.23  ? 102 LEU A CG  1 
ATOM   817  C  CD1 . LEU A  1  102 ? 2.090  11.892  4.160   1.00 48.85  ? 102 LEU A CD1 1 
ATOM   818  C  CD2 . LEU A  1  102 ? 2.452  13.750  2.433   1.00 51.89  ? 102 LEU A CD2 1 
ATOM   819  N  N   . ASN A  1  103 ? 6.851  10.799  1.134   1.00 43.56  ? 103 ASN A N   1 
ATOM   820  C  CA  . ASN A  1  103 ? 8.299  10.716  1.195   1.00 42.98  ? 103 ASN A CA  1 
ATOM   821  C  C   . ASN A  1  103 ? 8.969  11.435  0.024   1.00 41.32  ? 103 ASN A C   1 
ATOM   822  O  O   . ASN A  1  103 ? 10.099 11.935  0.161   1.00 39.80  ? 103 ASN A O   1 
ATOM   823  C  CB  . ASN A  1  103 ? 8.742  9.258   1.289   1.00 45.77  ? 103 ASN A CB  1 
ATOM   824  C  CG  . ASN A  1  103 ? 8.685  8.733   2.718   1.00 50.01  ? 103 ASN A CG  1 
ATOM   825  O  OD1 . ASN A  1  103 ? 8.756  7.536   2.951   1.00 52.43  ? 103 ASN A OD1 1 
ATOM   826  N  ND2 . ASN A  1  103 ? 8.567  9.645   3.684   1.00 53.11  ? 103 ASN A ND2 1 
ATOM   827  N  N   . PHE A  1  104 ? 8.275  11.504  -1.115  1.00 37.18  ? 104 PHE A N   1 
ATOM   828  C  CA  . PHE A  1  104 ? 8.814  12.215  -2.268  1.00 35.33  ? 104 PHE A CA  1 
ATOM   829  C  C   . PHE A  1  104 ? 8.816  13.710  -1.981  1.00 33.95  ? 104 PHE A C   1 
ATOM   830  O  O   . PHE A  1  104 ? 9.583  14.446  -2.595  1.00 35.48  ? 104 PHE A O   1 
ATOM   831  C  CB  . PHE A  1  104 ? 8.016  11.910  -3.539  1.00 32.97  ? 104 PHE A CB  1 
ATOM   832  C  CG  . PHE A  1  104 ? 8.343  10.584  -4.129  1.00 30.50  ? 104 PHE A CG  1 
ATOM   833  C  CD1 . PHE A  1  104 ? 9.243  10.482  -5.194  1.00 31.26  ? 104 PHE A CD1 1 
ATOM   834  C  CD2 . PHE A  1  104 ? 7.813  9.423   -3.581  1.00 26.65  ? 104 PHE A CD2 1 
ATOM   835  C  CE1 . PHE A  1  104 ? 9.613  9.233   -5.708  1.00 28.98  ? 104 PHE A CE1 1 
ATOM   836  C  CE2 . PHE A  1  104 ? 8.173  8.188   -4.078  1.00 25.89  ? 104 PHE A CE2 1 
ATOM   837  C  CZ  . PHE A  1  104 ? 9.075  8.087   -5.147  1.00 25.62  ? 104 PHE A CZ  1 
ATOM   838  N  N   . VAL A  1  105 ? 7.976  14.150  -1.047  1.00 31.94  ? 105 VAL A N   1 
ATOM   839  C  CA  . VAL A  1  105 ? 7.960  15.549  -0.684  1.00 31.55  ? 105 VAL A CA  1 
ATOM   840  C  C   . VAL A  1  105 ? 9.181  15.792  0.199   1.00 33.80  ? 105 VAL A C   1 
ATOM   841  O  O   . VAL A  1  105 ? 9.800  16.858  0.135   1.00 34.94  ? 105 VAL A O   1 
ATOM   842  C  CB  . VAL A  1  105 ? 6.666  15.933  0.075   1.00 30.44  ? 105 VAL A CB  1 
ATOM   843  C  CG1 . VAL A  1  105 ? 6.681  17.403  0.426   1.00 24.48  ? 105 VAL A CG1 1 
ATOM   844  C  CG2 . VAL A  1  105 ? 5.457  15.609  -0.787  1.00 23.25  ? 105 VAL A CG2 1 
ATOM   845  N  N   . VAL A  1  106 ? 9.538  14.793  1.002   1.00 35.56  ? 106 VAL A N   1 
ATOM   846  C  CA  . VAL A  1  106 ? 10.701 14.920  1.892   1.00 35.76  ? 106 VAL A CA  1 
ATOM   847  C  C   . VAL A  1  106 ? 11.940 14.927  1.004   1.00 35.75  ? 106 VAL A C   1 
ATOM   848  O  O   . VAL A  1  106 ? 12.835 15.774  1.140   1.00 35.92  ? 106 VAL A O   1 
ATOM   849  C  CB  . VAL A  1  106 ? 10.766 13.757  2.945   1.00 35.88  ? 106 VAL A CB  1 
ATOM   850  C  CG1 . VAL A  1  106 ? 12.080 13.796  3.685   1.00 34.83  ? 106 VAL A CG1 1 
ATOM   851  C  CG2 . VAL A  1  106 ? 9.621  13.901  3.972   1.00 33.80  ? 106 VAL A CG2 1 
ATOM   852  N  N   . PHE A  1  107 ? 11.960 14.009  0.055   1.00 34.85  ? 107 PHE A N   1 
ATOM   853  C  CA  . PHE A  1  107 ? 13.085 13.917  -0.868  1.00 35.00  ? 107 PHE A CA  1 
ATOM   854  C  C   . PHE A  1  107 ? 13.354 15.313  -1.474  1.00 35.10  ? 107 PHE A C   1 
ATOM   855  O  O   . PHE A  1  107 ? 14.454 15.870  -1.322  1.00 34.49  ? 107 PHE A O   1 
ATOM   856  C  CB  . PHE A  1  107 ? 12.772 12.868  -1.955  1.00 30.69  ? 107 PHE A CB  1 
ATOM   857  C  CG  . PHE A  1  107 ? 13.922 12.573  -2.877  1.00 27.12  ? 107 PHE A CG  1 
ATOM   858  C  CD1 . PHE A  1  107 ? 14.334 13.508  -3.826  1.00 24.86  ? 107 PHE A CD1 1 
ATOM   859  C  CD2 . PHE A  1  107 ? 14.607 11.352  -2.782  1.00 26.84  ? 107 PHE A CD2 1 
ATOM   860  C  CE1 . PHE A  1  107 ? 15.419 13.233  -4.669  1.00 26.99  ? 107 PHE A CE1 1 
ATOM   861  C  CE2 . PHE A  1  107 ? 15.701 11.061  -3.620  1.00 26.29  ? 107 PHE A CE2 1 
ATOM   862  C  CZ  . PHE A  1  107 ? 16.108 12.000  -4.565  1.00 25.35  ? 107 PHE A CZ  1 
ATOM   863  N  N   . GLY A  1  108 ? 12.345 15.882  -2.131  1.00 33.91  ? 108 GLY A N   1 
ATOM   864  C  CA  . GLY A  1  108 ? 12.506 17.209  -2.716  1.00 34.19  ? 108 GLY A CA  1 
ATOM   865  C  C   . GLY A  1  108 ? 13.121 18.247  -1.768  1.00 33.72  ? 108 GLY A C   1 
ATOM   866  O  O   . GLY A  1  108 ? 14.074 18.961  -2.115  1.00 28.73  ? 108 GLY A O   1 
ATOM   867  N  N   . LYS A  1  109 ? 12.563 18.329  -0.562  1.00 34.36  ? 109 LYS A N   1 
ATOM   868  C  CA  . LYS A  1  109 ? 13.053 19.260  0.440   1.00 33.79  ? 109 LYS A CA  1 
ATOM   869  C  C   . LYS A  1  109 ? 14.549 19.012  0.585   1.00 33.38  ? 109 LYS A C   1 
ATOM   870  O  O   . LYS A  1  109 ? 15.360 19.933  0.437   1.00 32.87  ? 109 LYS A O   1 
ATOM   871  C  CB  . LYS A  1  109 ? 12.364 19.007  1.783   1.00 35.43  ? 109 LYS A CB  1 
ATOM   872  C  CG  . LYS A  1  109 ? 11.180 19.926  2.130   1.00 36.92  ? 109 LYS A CG  1 
ATOM   873  C  CD  . LYS A  1  109 ? 10.077 19.912  1.082   1.00 39.96  ? 109 LYS A CD  1 
ATOM   874  C  CE  . LYS A  1  109 ? 9.036  21.022  1.314   1.00 38.77  ? 109 LYS A CE  1 
ATOM   875  N  NZ  . LYS A  1  109 ? 8.419  20.986  2.665   1.00 39.04  ? 109 LYS A NZ  1 
ATOM   876  N  N   . ALA A  1  110 ? 14.915 17.756  0.839   1.00 32.59  ? 110 ALA A N   1 
ATOM   877  C  CA  . ALA A  1  110 ? 16.326 17.403  1.033   1.00 30.65  ? 110 ALA A CA  1 
ATOM   878  C  C   . ALA A  1  110 ? 17.140 17.821  -0.194  1.00 30.09  ? 110 ALA A C   1 
ATOM   879  O  O   . ALA A  1  110 ? 18.214 18.434  -0.097  1.00 30.41  ? 110 ALA A O   1 
ATOM   880  C  CB  . ALA A  1  110 ? 16.463 15.897  1.295   1.00 28.85  ? 110 ALA A CB  1 
ATOM   881  N  N   . LEU A  1  111 ? 16.602 17.505  -1.358  1.00 28.56  ? 111 LEU A N   1 
ATOM   882  C  CA  . LEU A  1  111 ? 17.254 17.881  -2.608  1.00 30.05  ? 111 LEU A CA  1 
ATOM   883  C  C   . LEU A  1  111 ? 17.550 19.404  -2.705  1.00 29.21  ? 111 LEU A C   1 
ATOM   884  O  O   . LEU A  1  111 ? 18.654 19.809  -3.075  1.00 29.36  ? 111 LEU A O   1 
ATOM   885  C  CB  . LEU A  1  111 ? 16.374 17.443  -3.787  1.00 28.37  ? 111 LEU A CB  1 
ATOM   886  C  CG  . LEU A  1  111 ? 16.881 17.791  -5.172  1.00 29.69  ? 111 LEU A CG  1 
ATOM   887  C  CD1 . LEU A  1  111 ? 18.222 17.081  -5.424  1.00 31.51  ? 111 LEU A CD1 1 
ATOM   888  C  CD2 . LEU A  1  111 ? 15.840 17.344  -6.214  1.00 29.13  ? 111 LEU A CD2 1 
ATOM   889  N  N   . PHE A  1  112 ? 16.561 20.229  -2.359  1.00 29.77  ? 112 PHE A N   1 
ATOM   890  C  CA  . PHE A  1  112 ? 16.695 21.686  -2.395  1.00 30.92  ? 112 PHE A CA  1 
ATOM   891  C  C   . PHE A  1  112 ? 17.754 22.178  -1.403  1.00 32.85  ? 112 PHE A C   1 
ATOM   892  O  O   . PHE A  1  112 ? 18.542 23.072  -1.715  1.00 33.77  ? 112 PHE A O   1 
ATOM   893  C  CB  . PHE A  1  112 ? 15.364 22.355  -2.057  1.00 29.59  ? 112 PHE A CB  1 
ATOM   894  C  CG  . PHE A  1  112 ? 14.219 21.853  -2.861  1.00 28.98  ? 112 PHE A CG  1 
ATOM   895  C  CD1 . PHE A  1  112 ? 14.411 21.434  -4.175  1.00 30.07  ? 112 PHE A CD1 1 
ATOM   896  C  CD2 . PHE A  1  112 ? 12.934 21.821  -2.326  1.00 28.32  ? 112 PHE A CD2 1 
ATOM   897  C  CE1 . PHE A  1  112 ? 13.338 20.993  -4.941  1.00 28.23  ? 112 PHE A CE1 1 
ATOM   898  C  CE2 . PHE A  1  112 ? 11.841 21.377  -3.093  1.00 26.50  ? 112 PHE A CE2 1 
ATOM   899  C  CZ  . PHE A  1  112 ? 12.041 20.967  -4.392  1.00 28.58  ? 112 PHE A CZ  1 
ATOM   900  N  N   . ALA A  1  113 ? 17.754 21.603  -0.203  1.00 31.55  ? 113 ALA A N   1 
ATOM   901  C  CA  . ALA A  1  113 ? 18.728 21.966  0.805   1.00 32.50  ? 113 ALA A CA  1 
ATOM   902  C  C   . ALA A  1  113 ? 20.130 21.652  0.269   1.00 33.02  ? 113 ALA A C   1 
ATOM   903  O  O   . ALA A  1  113 ? 21.035 22.482  0.356   1.00 34.70  ? 113 ALA A O   1 
ATOM   904  C  CB  . ALA A  1  113 ? 18.467 21.188  2.097   1.00 31.67  ? 113 ALA A CB  1 
ATOM   905  N  N   . THR A  1  114 ? 20.300 20.466  -0.314  1.00 31.72  ? 114 THR A N   1 
ATOM   906  C  CA  . THR A  1  114 ? 21.593 20.060  -0.840  1.00 31.67  ? 114 THR A CA  1 
ATOM   907  C  C   . THR A  1  114 ? 22.013 20.822  -2.113  1.00 32.80  ? 114 THR A C   1 
ATOM   908  O  O   . THR A  1  114 ? 23.204 21.134  -2.312  1.00 33.22  ? 114 THR A O   1 
ATOM   909  C  CB  . THR A  1  114 ? 21.622 18.528  -1.127  1.00 33.32  ? 114 THR A CB  1 
ATOM   910  O  OG1 . THR A  1  114 ? 21.288 17.794  0.069   1.00 34.18  ? 114 THR A OG1 1 
ATOM   911  C  CG2 . THR A  1  114 ? 23.015 18.106  -1.610  1.00 27.02  ? 114 THR A CG2 1 
ATOM   912  N  N   . VAL A  1  115 ? 21.068 21.137  -2.989  1.00 29.78  ? 115 VAL A N   1 
ATOM   913  C  CA  . VAL A  1  115 ? 21.497 21.851  -4.182  1.00 30.45  ? 115 VAL A CA  1 
ATOM   914  C  C   . VAL A  1  115 ? 21.818 23.301  -3.810  1.00 30.60  ? 115 VAL A C   1 
ATOM   915  O  O   . VAL A  1  115 ? 22.880 23.831  -4.175  1.00 30.46  ? 115 VAL A O   1 
ATOM   916  C  CB  . VAL A  1  115 ? 20.437 21.816  -5.333  1.00 31.03  ? 115 VAL A CB  1 
ATOM   917  C  CG1 . VAL A  1  115 ? 20.915 22.723  -6.478  1.00 27.84  ? 115 VAL A CG1 1 
ATOM   918  C  CG2 . VAL A  1  115 ? 20.228 20.361  -5.850  1.00 28.54  ? 115 VAL A CG2 1 
ATOM   919  N  N   . GLY A  1  116 ? 20.900 23.933  -3.086  1.00 28.76  ? 116 GLY A N   1 
ATOM   920  C  CA  . GLY A  1  116 ? 21.125 25.296  -2.658  1.00 27.77  ? 116 GLY A CA  1 
ATOM   921  C  C   . GLY A  1  116 ? 22.328 25.436  -1.726  1.00 27.60  ? 116 GLY A C   1 
ATOM   922  O  O   . GLY A  1  116 ? 23.037 26.436  -1.784  1.00 25.72  ? 116 GLY A O   1 
ATOM   923  N  N   . GLY A  1  117 ? 22.552 24.452  -0.853  1.00 28.69  ? 117 GLY A N   1 
ATOM   924  C  CA  . GLY A  1  117 ? 23.689 24.500  0.057   1.00 29.13  ? 117 GLY A CA  1 
ATOM   925  C  C   . GLY A  1  117 ? 25.004 24.463  -0.701  1.00 31.44  ? 117 GLY A C   1 
ATOM   926  O  O   . GLY A  1  117 ? 25.979 25.092  -0.295  1.00 33.23  ? 117 GLY A O   1 
ATOM   927  N  N   . GLN A  1  118 ? 25.023 23.752  -1.821  1.00 31.95  ? 118 GLN A N   1 
ATOM   928  C  CA  . GLN A  1  118 ? 26.225 23.631  -2.627  1.00 33.48  ? 118 GLN A CA  1 
ATOM   929  C  C   . GLN A  1  118 ? 26.328 24.723  -3.704  1.00 34.11  ? 118 GLN A C   1 
ATOM   930  O  O   . GLN A  1  118 ? 27.429 25.188  -4.017  1.00 34.88  ? 118 GLN A O   1 
ATOM   931  C  CB  . GLN A  1  118 ? 26.251 22.244  -3.265  1.00 36.43  ? 118 GLN A CB  1 
ATOM   932  C  CG  . GLN A  1  118 ? 27.521 21.910  -3.994  1.00 44.09  ? 118 GLN A CG  1 
ATOM   933  C  CD  . GLN A  1  118 ? 28.697 21.795  -3.071  1.00 47.43  ? 118 GLN A CD  1 
ATOM   934  O  OE1 . GLN A  1  118 ? 28.692 20.998  -2.135  1.00 51.65  ? 118 GLN A OE1 1 
ATOM   935  N  NE2 . GLN A  1  118 ? 29.724 22.599  -3.320  1.00 50.18  ? 118 GLN A NE2 1 
ATOM   936  N  N   . PHE A  1  119 ? 25.189 25.144  -4.259  1.00 32.76  ? 119 PHE A N   1 
ATOM   937  C  CA  . PHE A  1  119 ? 25.191 26.169  -5.311  1.00 30.21  ? 119 PHE A CA  1 
ATOM   938  C  C   . PHE A  1  119 ? 25.322 27.611  -4.789  1.00 28.94  ? 119 PHE A C   1 
ATOM   939  O  O   . PHE A  1  119 ? 25.824 28.516  -5.476  1.00 27.09  ? 119 PHE A O   1 
ATOM   940  C  CB  . PHE A  1  119 ? 23.931 26.061  -6.173  1.00 28.80  ? 119 PHE A CB  1 
ATOM   941  C  CG  . PHE A  1  119 ? 23.933 26.971  -7.371  1.00 27.48  ? 119 PHE A CG  1 
ATOM   942  C  CD1 . PHE A  1  119 ? 24.556 26.592  -8.544  1.00 27.19  ? 119 PHE A CD1 1 
ATOM   943  C  CD2 . PHE A  1  119 ? 23.310 28.208  -7.321  1.00 28.59  ? 119 PHE A CD2 1 
ATOM   944  C  CE1 . PHE A  1  119 ? 24.556 27.428  -9.654  1.00 28.09  ? 119 PHE A CE1 1 
ATOM   945  C  CE2 . PHE A  1  119 ? 23.305 29.046  -8.419  1.00 26.40  ? 119 PHE A CE2 1 
ATOM   946  C  CZ  . PHE A  1  119 ? 23.927 28.657  -9.592  1.00 27.55  ? 119 PHE A CZ  1 
ATOM   947  N  N   . GLY A  1  120 ? 24.851 27.828  -3.578  1.00 29.55  ? 120 GLY A N   1 
ATOM   948  C  CA  . GLY A  1  120 ? 24.954 29.151  -3.000  1.00 30.21  ? 120 GLY A CA  1 
ATOM   949  C  C   . GLY A  1  120 ? 23.694 29.994  -3.090  1.00 30.79  ? 120 GLY A C   1 
ATOM   950  O  O   . GLY A  1  120 ? 22.658 29.544  -3.560  1.00 29.81  ? 120 GLY A O   1 
ATOM   951  N  N   . VAL A  1  121 ? 23.815 31.239  -2.656  1.00 30.98  ? 121 VAL A N   1 
ATOM   952  C  CA  . VAL A  1  121 ? 22.726 32.185  -2.621  1.00 32.12  ? 121 VAL A CA  1 
ATOM   953  C  C   . VAL A  1  121 ? 21.861 32.375  -3.877  1.00 32.43  ? 121 VAL A C   1 
ATOM   954  O  O   . VAL A  1  121 ? 20.696 32.708  -3.776  1.00 33.00  ? 121 VAL A O   1 
ATOM   955  C  CB  . VAL A  1  121 ? 23.274 33.537  -2.152  1.00 32.58  ? 121 VAL A CB  1 
ATOM   956  C  CG1 . VAL A  1  121 ? 22.192 34.569  -2.187  1.00 40.69  ? 121 VAL A CG1 1 
ATOM   957  C  CG2 . VAL A  1  121 ? 23.810 33.397  -0.715  1.00 32.69  ? 121 VAL A CG2 1 
ATOM   958  N  N   . CYS A  1  122 ? 22.400 32.151  -5.060  1.00 35.03  ? 122 CYS A N   1 
ATOM   959  C  CA  . CYS A  1  122 ? 21.604 32.365  -6.272  1.00 36.70  ? 122 CYS A CA  1 
ATOM   960  C  C   . CYS A  1  122 ? 20.713 31.188  -6.662  1.00 37.39  ? 122 CYS A C   1 
ATOM   961  O  O   . CYS A  1  122 ? 20.119 31.150  -7.756  1.00 38.16  ? 122 CYS A O   1 
ATOM   962  C  CB  . CYS A  1  122 ? 22.518 32.768  -7.404  1.00 39.55  ? 122 CYS A CB  1 
ATOM   963  S  SG  . CYS A  1  122 ? 23.496 34.242  -6.944  1.00 43.40  ? 122 CYS A SG  1 
ATOM   964  N  N   . PHE A  1  123 ? 20.645 30.217  -5.760  1.00 36.82  ? 123 PHE A N   1 
ATOM   965  C  CA  . PHE A  1  123 ? 19.798 29.054  -5.925  1.00 35.11  ? 123 PHE A CA  1 
ATOM   966  C  C   . PHE A  1  123 ? 18.365 29.578  -6.158  1.00 36.56  ? 123 PHE A C   1 
ATOM   967  O  O   . PHE A  1  123 ? 17.861 30.428  -5.405  1.00 34.92  ? 123 PHE A O   1 
ATOM   968  C  CB  . PHE A  1  123 ? 19.850 28.236  -4.640  1.00 33.23  ? 123 PHE A CB  1 
ATOM   969  C  CG  . PHE A  1  123 ? 18.869 27.114  -4.593  1.00 32.52  ? 123 PHE A CG  1 
ATOM   970  C  CD1 . PHE A  1  123 ? 18.892 26.103  -5.550  1.00 33.48  ? 123 PHE A CD1 1 
ATOM   971  C  CD2 . PHE A  1  123 ? 17.961 27.016  -3.541  1.00 30.22  ? 123 PHE A CD2 1 
ATOM   972  C  CE1 . PHE A  1  123 ? 18.027 25.004  -5.453  1.00 30.22  ? 123 PHE A CE1 1 
ATOM   973  C  CE2 . PHE A  1  123 ? 17.097 25.921  -3.439  1.00 31.34  ? 123 PHE A CE2 1 
ATOM   974  C  CZ  . PHE A  1  123 ? 17.130 24.914  -4.395  1.00 31.81  ? 123 PHE A CZ  1 
ATOM   975  N  N   . ASP A  1  124 ? 17.719 29.087  -7.215  1.00 35.99  ? 124 ASP A N   1 
ATOM   976  C  CA  . ASP A  1  124 ? 16.369 29.507  -7.561  1.00 34.53  ? 124 ASP A CA  1 
ATOM   977  C  C   . ASP A  1  124 ? 15.399 28.509  -6.957  1.00 34.68  ? 124 ASP A C   1 
ATOM   978  O  O   . ASP A  1  124 ? 14.939 27.592  -7.649  1.00 35.65  ? 124 ASP A O   1 
ATOM   979  C  CB  . ASP A  1  124 ? 16.209 29.507  -9.087  1.00 34.80  ? 124 ASP A CB  1 
ATOM   980  C  CG  . ASP A  1  124 ? 14.995 30.290  -9.558  1.00 35.32  ? 124 ASP A CG  1 
ATOM   981  O  OD1 . ASP A  1  124 ? 13.938 30.258  -8.875  1.00 33.57  ? 124 ASP A OD1 1 
ATOM   982  O  OD2 . ASP A  1  124 ? 15.110 30.923  -10.635 1.00 34.92  ? 124 ASP A OD2 1 
ATOM   983  N  N   . LEU A  1  125 ? 15.080 28.667  -5.676  1.00 33.99  ? 125 LEU A N   1 
ATOM   984  C  CA  . LEU A  1  125 ? 14.165 27.727  -5.025  1.00 34.29  ? 125 LEU A CA  1 
ATOM   985  C  C   . LEU A  1  125 ? 12.780 27.576  -5.736  1.00 36.18  ? 125 LEU A C   1 
ATOM   986  O  O   . LEU A  1  125 ? 12.338 26.452  -6.005  1.00 37.06  ? 125 LEU A O   1 
ATOM   987  C  CB  . LEU A  1  125 ? 14.005 28.088  -3.532  1.00 29.35  ? 125 LEU A CB  1 
ATOM   988  C  CG  . LEU A  1  125 ? 13.034 27.268  -2.660  1.00 26.89  ? 125 LEU A CG  1 
ATOM   989  C  CD1 . LEU A  1  125 ? 13.309 25.760  -2.717  1.00 21.43  ? 125 LEU A CD1 1 
ATOM   990  C  CD2 . LEU A  1  125 ? 13.125 27.798  -1.256  1.00 19.67  ? 125 LEU A CD2 1 
ATOM   991  N  N   . PRO A  1  126 ? 12.089 28.690  -6.062  1.00 37.27  ? 126 PRO A N   1 
ATOM   992  C  CA  . PRO A  1  126 ? 10.790 28.510  -6.736  1.00 37.20  ? 126 PRO A CA  1 
ATOM   993  C  C   . PRO A  1  126 ? 10.899 27.613  -7.974  1.00 37.47  ? 126 PRO A C   1 
ATOM   994  O  O   . PRO A  1  126 ? 10.082 26.694  -8.174  1.00 38.59  ? 126 PRO A O   1 
ATOM   995  C  CB  . PRO A  1  126 ? 10.382 29.935  -7.106  1.00 34.60  ? 126 PRO A CB  1 
ATOM   996  C  CG  . PRO A  1  126 ? 10.997 30.765  -6.019  1.00 37.00  ? 126 PRO A CG  1 
ATOM   997  C  CD  . PRO A  1  126 ? 12.368 30.113  -5.810  1.00 37.49  ? 126 PRO A CD  1 
ATOM   998  N  N   . ALA A  1  127 ? 11.920 27.866  -8.791  1.00 36.37  ? 127 ALA A N   1 
ATOM   999  C  CA  . ALA A  1  127 ? 12.113 27.094  -10.009 1.00 37.68  ? 127 ALA A CA  1 
ATOM   1000 C  C   . ALA A  1  127 ? 12.303 25.612  -9.692  1.00 40.03  ? 127 ALA A C   1 
ATOM   1001 O  O   . ALA A  1  127 ? 11.818 24.733  -10.430 1.00 39.22  ? 127 ALA A O   1 
ATOM   1002 C  CB  . ALA A  1  127 ? 13.310 27.614  -10.768 1.00 37.59  ? 127 ALA A CB  1 
ATOM   1003 N  N   . TRP A  1  128 ? 12.988 25.330  -8.578  1.00 39.08  ? 128 TRP A N   1 
ATOM   1004 C  CA  . TRP A  1  128 ? 13.250 23.950  -8.213  1.00 39.35  ? 128 TRP A CA  1 
ATOM   1005 C  C   . TRP A  1  128 ? 12.028 23.237  -7.656  1.00 40.72  ? 128 TRP A C   1 
ATOM   1006 O  O   . TRP A  1  128 ? 11.831 22.042  -7.894  1.00 40.19  ? 128 TRP A O   1 
ATOM   1007 C  CB  . TRP A  1  128 ? 14.421 23.856  -7.229  1.00 38.60  ? 128 TRP A CB  1 
ATOM   1008 C  CG  . TRP A  1  128 ? 15.774 23.857  -7.893  1.00 38.84  ? 128 TRP A CG  1 
ATOM   1009 C  CD1 . TRP A  1  128 ? 16.516 24.944  -8.249  1.00 39.09  ? 128 TRP A CD1 1 
ATOM   1010 C  CD2 . TRP A  1  128 ? 16.524 22.711  -8.291  1.00 38.79  ? 128 TRP A CD2 1 
ATOM   1011 N  NE1 . TRP A  1  128 ? 17.686 24.548  -8.839  1.00 38.39  ? 128 TRP A NE1 1 
ATOM   1012 C  CE2 . TRP A  1  128 ? 17.722 23.182  -8.881  1.00 39.14  ? 128 TRP A CE2 1 
ATOM   1013 C  CE3 . TRP A  1  128 ? 16.304 21.332  -8.208  1.00 38.27  ? 128 TRP A CE3 1 
ATOM   1014 C  CZ2 . TRP A  1  128 ? 18.702 22.319  -9.390  1.00 39.66  ? 128 TRP A CZ2 1 
ATOM   1015 C  CZ3 . TRP A  1  128 ? 17.271 20.472  -8.708  1.00 39.33  ? 128 TRP A CZ3 1 
ATOM   1016 C  CH2 . TRP A  1  128 ? 18.460 20.970  -9.295  1.00 40.88  ? 128 TRP A CH2 1 
ATOM   1017 N  N   . GLU A  1  129 ? 11.193 23.956  -6.914  1.00 41.04  ? 129 GLU A N   1 
ATOM   1018 C  CA  . GLU A  1  129 ? 9.997  23.322  -6.384  1.00 42.03  ? 129 GLU A CA  1 
ATOM   1019 C  C   . GLU A  1  129 ? 9.069  22.991  -7.558  1.00 42.34  ? 129 GLU A C   1 
ATOM   1020 O  O   . GLU A  1  129 ? 8.458  21.929  -7.585  1.00 42.75  ? 129 GLU A O   1 
ATOM   1021 C  CB  . GLU A  1  129 ? 9.277  24.248  -5.412  1.00 41.21  ? 129 GLU A CB  1 
ATOM   1022 C  CG  . GLU A  1  129 ? 10.101 24.675  -4.217  1.00 41.54  ? 129 GLU A CG  1 
ATOM   1023 C  CD  . GLU A  1  129 ? 9.326  25.574  -3.290  1.00 41.30  ? 129 GLU A CD  1 
ATOM   1024 O  OE1 . GLU A  1  129 ? 8.669  26.510  -3.787  1.00 44.28  ? 129 GLU A OE1 1 
ATOM   1025 O  OE2 . GLU A  1  129 ? 9.374  25.357  -2.065  1.00 43.81  ? 129 GLU A OE2 1 
ATOM   1026 N  N   . SER A  1  130 ? 8.971  23.897  -8.529  1.00 41.78  ? 130 SER A N   1 
ATOM   1027 C  CA  . SER A  1  130 ? 8.102  23.657  -9.671  1.00 43.47  ? 130 SER A CA  1 
ATOM   1028 C  C   . SER A  1  130 ? 8.590  22.493  -10.509 1.00 43.07  ? 130 SER A C   1 
ATOM   1029 O  O   . SER A  1  130 ? 7.829  21.583  -10.798 1.00 42.74  ? 130 SER A O   1 
ATOM   1030 C  CB  . SER A  1  130 ? 7.987  24.902  -10.555 1.00 43.46  ? 130 SER A CB  1 
ATOM   1031 O  OG  . SER A  1  130 ? 7.393  25.962  -9.831  1.00 49.79  ? 130 SER A OG  1 
ATOM   1032 N  N   . CYS A  1  131 ? 9.856  22.523  -10.905 1.00 44.81  ? 131 CYS A N   1 
ATOM   1033 C  CA  . CYS A  1  131 ? 10.409 21.446  -11.715 1.00 44.93  ? 131 CYS A CA  1 
ATOM   1034 C  C   . CYS A  1  131 ? 10.561 20.102  -10.984 1.00 43.65  ? 131 CYS A C   1 
ATOM   1035 O  O   . CYS A  1  131 ? 10.499 19.043  -11.617 1.00 42.01  ? 131 CYS A O   1 
ATOM   1036 C  CB  . CYS A  1  131 ? 11.736 21.889  -12.332 1.00 46.91  ? 131 CYS A CB  1 
ATOM   1037 S  SG  . CYS A  1  131 ? 11.492 23.168  -13.608 1.00 52.10  ? 131 CYS A SG  1 
ATOM   1038 N  N   . TYR A  1  132 ? 10.739 20.123  -9.665  1.00 40.78  ? 132 TYR A N   1 
ATOM   1039 C  CA  . TYR A  1  132 ? 10.836 18.863  -8.957  1.00 39.47  ? 132 TYR A CA  1 
ATOM   1040 C  C   . TYR A  1  132 ? 9.473  18.200  -9.032  1.00 41.23  ? 132 TYR A C   1 
ATOM   1041 O  O   . TYR A  1  132 ? 9.376  16.985  -9.254  1.00 42.26  ? 132 TYR A O   1 
ATOM   1042 C  CB  . TYR A  1  132 ? 11.208 19.039  -7.490  1.00 37.04  ? 132 TYR A CB  1 
ATOM   1043 C  CG  . TYR A  1  132 ? 11.171 17.723  -6.738  1.00 36.15  ? 132 TYR A CG  1 
ATOM   1044 C  CD1 . TYR A  1  132 ? 10.213 17.487  -5.754  1.00 34.66  ? 132 TYR A CD1 1 
ATOM   1045 C  CD2 . TYR A  1  132 ? 12.059 16.691  -7.056  1.00 33.86  ? 132 TYR A CD2 1 
ATOM   1046 C  CE1 . TYR A  1  132 ? 10.129 16.264  -5.101  1.00 31.41  ? 132 TYR A CE1 1 
ATOM   1047 C  CE2 . TYR A  1  132 ? 11.986 15.463  -6.422  1.00 32.42  ? 132 TYR A CE2 1 
ATOM   1048 C  CZ  . TYR A  1  132 ? 11.015 15.250  -5.441  1.00 34.76  ? 132 TYR A CZ  1 
ATOM   1049 O  OH  . TYR A  1  132 ? 10.904 14.018  -4.814  1.00 34.17  ? 132 TYR A OH  1 
ATOM   1050 N  N   . LYS A  1  133 ? 8.415  18.989  -8.842  1.00 40.05  ? 133 LYS A N   1 
ATOM   1051 C  CA  . LYS A  1  133 ? 7.069  18.443  -8.916  1.00 40.03  ? 133 LYS A CA  1 
ATOM   1052 C  C   . LYS A  1  133 ? 6.909  17.593  -10.171 1.00 38.35  ? 133 LYS A C   1 
ATOM   1053 O  O   . LYS A  1  133 ? 6.429  16.464  -10.102 1.00 38.73  ? 133 LYS A O   1 
ATOM   1054 C  CB  . LYS A  1  133 ? 6.052  19.565  -8.927  1.00 41.54  ? 133 LYS A CB  1 
ATOM   1055 C  CG  . LYS A  1  133 ? 5.827  20.230  -7.579  1.00 44.67  ? 133 LYS A CG  1 
ATOM   1056 C  CD  . LYS A  1  133 ? 4.697  21.195  -7.733  1.00 48.00  ? 133 LYS A CD  1 
ATOM   1057 C  CE  . LYS A  1  133 ? 4.324  21.883  -6.448  1.00 49.21  ? 133 LYS A CE  1 
ATOM   1058 N  NZ  . LYS A  1  133 ? 3.174  22.825  -6.714  1.00 51.58  ? 133 LYS A NZ  1 
ATOM   1059 N  N   . VAL A  1  134 ? 7.332  18.127  -11.314 1.00 36.00  ? 134 VAL A N   1 
ATOM   1060 C  CA  . VAL A  1  134 ? 7.234  17.397  -12.572 1.00 35.48  ? 134 VAL A CA  1 
ATOM   1061 C  C   . VAL A  1  134 ? 7.895  16.025  -12.410 1.00 37.56  ? 134 VAL A C   1 
ATOM   1062 O  O   . VAL A  1  134 ? 7.350  15.017  -12.845 1.00 40.06  ? 134 VAL A O   1 
ATOM   1063 C  CB  . VAL A  1  134 ? 7.931  18.174  -13.716 1.00 32.80  ? 134 VAL A CB  1 
ATOM   1064 C  CG1 . VAL A  1  134 ? 7.934  17.392  -14.989 1.00 28.19  ? 134 VAL A CG1 1 
ATOM   1065 C  CG2 . VAL A  1  134 ? 7.245  19.473  -13.933 1.00 32.10  ? 134 VAL A CG2 1 
ATOM   1066 N  N   . ILE A  1  135 ? 9.055  15.977  -11.758 1.00 38.09  ? 135 ILE A N   1 
ATOM   1067 C  CA  . ILE A  1  135 ? 9.735  14.705  -11.576 1.00 39.56  ? 135 ILE A CA  1 
ATOM   1068 C  C   . ILE A  1  135 ? 8.957  13.739  -10.687 1.00 38.87  ? 135 ILE A C   1 
ATOM   1069 O  O   . ILE A  1  135 ? 8.642  12.630  -11.109 1.00 36.78  ? 135 ILE A O   1 
ATOM   1070 C  CB  . ILE A  1  135 ? 11.159 14.909  -11.048 1.00 39.41  ? 135 ILE A CB  1 
ATOM   1071 C  CG1 . ILE A  1  135 ? 11.992 15.578  -12.158 1.00 42.01  ? 135 ILE A CG1 1 
ATOM   1072 C  CG2 . ILE A  1  135 ? 11.784 13.564  -10.690 1.00 38.53  ? 135 ILE A CG2 1 
ATOM   1073 C  CD1 . ILE A  1  135 ? 13.386 16.086  -11.742 1.00 42.41  ? 135 ILE A CD1 1 
ATOM   1074 N  N   . ALA A  1  136 ? 8.614  14.197  -9.485  1.00 39.43  ? 136 ALA A N   1 
ATOM   1075 C  CA  . ALA A  1  136 ? 7.863  13.415  -8.509  1.00 39.05  ? 136 ALA A CA  1 
ATOM   1076 C  C   . ALA A  1  136 ? 6.582  12.854  -9.115  1.00 40.17  ? 136 ALA A C   1 
ATOM   1077 O  O   . ALA A  1  136 ? 6.246  11.682  -8.934  1.00 41.92  ? 136 ALA A O   1 
ATOM   1078 C  CB  . ALA A  1  136 ? 7.534  14.290  -7.271  1.00 36.72  ? 136 ALA A CB  1 
ATOM   1079 N  N   . MET A  1  137 ? 5.870  13.718  -9.829  1.00 41.44  ? 137 MET A N   1 
ATOM   1080 C  CA  . MET A  1  137 ? 4.620  13.371  -10.484 1.00 40.83  ? 137 MET A CA  1 
ATOM   1081 C  C   . MET A  1  137 ? 4.813  12.268  -11.515 1.00 38.60  ? 137 MET A C   1 
ATOM   1082 O  O   . MET A  1  137 ? 3.964  11.397  -11.662 1.00 40.03  ? 137 MET A O   1 
ATOM   1083 C  CB  . MET A  1  137 ? 4.043  14.621  -11.166 1.00 45.58  ? 137 MET A CB  1 
ATOM   1084 C  CG  . MET A  1  137 ? 2.817  14.376  -12.059 1.00 49.85  ? 137 MET A CG  1 
ATOM   1085 S  SD  . MET A  1  137 ? 1.370  13.607  -11.262 1.00 57.75  ? 137 MET A SD  1 
ATOM   1086 C  CE  . MET A  1  137 ? 0.567  15.040  -10.599 1.00 54.03  ? 137 MET A CE  1 
ATOM   1087 N  N   . GLY A  1  138 ? 5.931  12.297  -12.218 1.00 36.19  ? 138 GLY A N   1 
ATOM   1088 C  CA  . GLY A  1  138 ? 6.170  11.293  -13.228 1.00 36.43  ? 138 GLY A CA  1 
ATOM   1089 C  C   . GLY A  1  138 ? 6.503  9.955   -12.619 1.00 38.89  ? 138 GLY A C   1 
ATOM   1090 O  O   . GLY A  1  138 ? 6.235  8.917   -13.217 1.00 40.95  ? 138 GLY A O   1 
ATOM   1091 N  N   . ILE A  1  139 ? 7.069  9.976   -11.421 1.00 39.18  ? 139 ILE A N   1 
ATOM   1092 C  CA  . ILE A  1  139 ? 7.456  8.756   -10.750 1.00 41.02  ? 139 ILE A CA  1 
ATOM   1093 C  C   . ILE A  1  139 ? 6.360  8.183   -9.863  1.00 44.67  ? 139 ILE A C   1 
ATOM   1094 O  O   . ILE A  1  139 ? 6.253  6.969   -9.708  1.00 46.12  ? 139 ILE A O   1 
ATOM   1095 C  CB  . ILE A  1  139 ? 8.719  8.991   -9.898  1.00 39.13  ? 139 ILE A CB  1 
ATOM   1096 C  CG1 . ILE A  1  139 ? 9.875  9.421   -10.810 1.00 36.72  ? 139 ILE A CG1 1 
ATOM   1097 C  CG2 . ILE A  1  139 ? 9.068  7.728   -9.103  1.00 37.29  ? 139 ILE A CG2 1 
ATOM   1098 C  CD1 . ILE A  1  139 ? 11.126 9.897   -10.081 1.00 32.95  ? 139 ILE A CD1 1 
ATOM   1099 N  N   . THR A  1  140 ? 5.545  9.052   -9.277  1.00 47.33  ? 140 THR A N   1 
ATOM   1100 C  CA  . THR A  1  140 ? 4.487  8.603   -8.373  1.00 50.54  ? 140 THR A CA  1 
ATOM   1101 C  C   . THR A  1  140 ? 3.097  8.572   -9.006  1.00 54.54  ? 140 THR A C   1 
ATOM   1102 O  O   . THR A  1  140 ? 2.344  7.609   -8.836  1.00 53.42  ? 140 THR A O   1 
ATOM   1103 C  CB  . THR A  1  140 ? 4.402  9.506   -7.120  1.00 49.18  ? 140 THR A CB  1 
ATOM   1104 O  OG1 . THR A  1  140 ? 4.007  10.828  -7.513  1.00 47.77  ? 140 THR A OG1 1 
ATOM   1105 C  CG2 . THR A  1  140 ? 5.749  9.559   -6.401  1.00 46.47  ? 140 THR A CG2 1 
ATOM   1106 N  N   . GLY A  1  141 ? 2.766  9.644   -9.726  1.00 59.42  ? 141 GLY A N   1 
ATOM   1107 C  CA  . GLY A  1  141 ? 1.463  9.765   -10.345 1.00 61.72  ? 141 GLY A CA  1 
ATOM   1108 C  C   . GLY A  1  141 ? 0.528  10.454  -9.366  1.00 65.13  ? 141 GLY A C   1 
ATOM   1109 O  O   . GLY A  1  141 ? -0.637 10.668  -9.678  1.00 68.05  ? 141 GLY A O   1 
ATOM   1110 N  N   . ASN A  1  142 ? 1.039  10.804  -8.186  1.00 67.12  ? 142 ASN A N   1 
ATOM   1111 C  CA  . ASN A  1  142 ? 0.238  11.455  -7.157  1.00 70.29  ? 142 ASN A CA  1 
ATOM   1112 C  C   . ASN A  1  142 ? 0.022  12.920  -7.538  1.00 72.07  ? 142 ASN A C   1 
ATOM   1113 O  O   . ASN A  1  142 ? 0.965  13.630  -7.854  1.00 72.36  ? 142 ASN A O   1 
ATOM   1114 C  CB  . ASN A  1  142 ? 0.953  11.357  -5.811  1.00 71.36  ? 142 ASN A CB  1 
ATOM   1115 C  CG  . ASN A  1  142 ? 0.012  11.509  -4.635  1.00 73.39  ? 142 ASN A CG  1 
ATOM   1116 O  OD1 . ASN A  1  142 ? -0.543 12.587  -4.397  1.00 74.85  ? 142 ASN A OD1 1 
ATOM   1117 N  ND2 . ASN A  1  142 ? -0.174 10.423  -3.886  1.00 73.69  ? 142 ASN A ND2 1 
ATOM   1118 N  N   . ASP A  1  143 ? -1.232 13.364  -7.521  1.00 73.89  ? 143 ASP A N   1 
ATOM   1119 C  CA  . ASP A  1  143 ? -1.523 14.742  -7.881  1.00 75.57  ? 143 ASP A CA  1 
ATOM   1120 C  C   . ASP A  1  143 ? -1.292 15.722  -6.734  1.00 74.22  ? 143 ASP A C   1 
ATOM   1121 O  O   . ASP A  1  143 ? -1.928 16.766  -6.650  1.00 77.34  ? 143 ASP A O   1 
ATOM   1122 C  CB  . ASP A  1  143 ? -2.931 14.887  -8.444  1.00 78.89  ? 143 ASP A CB  1 
ATOM   1123 C  CG  . ASP A  1  143 ? -3.078 14.243  -9.805  1.00 81.46  ? 143 ASP A CG  1 
ATOM   1124 O  OD1 . ASP A  1  143 ? -2.046 13.961  -10.435 1.00 83.53  ? 143 ASP A OD1 1 
ATOM   1125 O  OD2 . ASP A  1  143 ? -4.231 14.026  -10.249 1.00 82.18  ? 143 ASP A OD2 1 
ATOM   1126 N  N   . MET A  1  144 ? -0.396 15.358  -5.822  1.00 71.05  ? 144 MET A N   1 
ATOM   1127 C  CA  . MET A  1  144 ? -0.082 16.271  -4.750  1.00 67.45  ? 144 MET A CA  1 
ATOM   1128 C  C   . MET A  1  144 ? 1.068  17.061  -5.368  1.00 65.60  ? 144 MET A C   1 
ATOM   1129 O  O   . MET A  1  144 ? 1.378  18.166  -4.946  1.00 67.07  ? 144 MET A O   1 
ATOM   1130 C  CB  . MET A  1  144 ? 0.323  15.547  -3.470  1.00 68.00  ? 144 MET A CB  1 
ATOM   1131 C  CG  . MET A  1  144 ? 1.305  14.394  -3.584  1.00 65.88  ? 144 MET A CG  1 
ATOM   1132 S  SD  . MET A  1  144 ? 2.061  14.073  -1.966  1.00 66.07  ? 144 MET A SD  1 
ATOM   1133 C  CE  . MET A  1  144 ? 0.740  13.364  -0.990  1.00 66.20  ? 144 MET A CE  1 
ATOM   1134 N  N   . PHE A  1  145 ? 1.674  16.478  -6.403  1.00 61.89  ? 145 PHE A N   1 
ATOM   1135 C  CA  . PHE A  1  145 ? 2.793  17.095  -7.104  1.00 60.92  ? 145 PHE A CA  1 
ATOM   1136 C  C   . PHE A  1  145 ? 2.222  17.742  -8.354  1.00 64.39  ? 145 PHE A C   1 
ATOM   1137 O  O   . PHE A  1  145 ? 2.795  17.666  -9.456  1.00 64.22  ? 145 PHE A O   1 
ATOM   1138 C  CB  . PHE A  1  145 ? 3.848  16.062  -7.487  1.00 52.78  ? 145 PHE A CB  1 
ATOM   1139 C  CG  . PHE A  1  145 ? 4.332  15.254  -6.329  1.00 44.23  ? 145 PHE A CG  1 
ATOM   1140 C  CD1 . PHE A  1  145 ? 4.063  13.895  -6.257  1.00 38.80  ? 145 PHE A CD1 1 
ATOM   1141 C  CD2 . PHE A  1  145 ? 5.019  15.865  -5.277  1.00 39.26  ? 145 PHE A CD2 1 
ATOM   1142 C  CE1 . PHE A  1  145 ? 4.464  13.154  -5.153  1.00 36.14  ? 145 PHE A CE1 1 
ATOM   1143 C  CE2 . PHE A  1  145 ? 5.424  15.140  -4.176  1.00 37.22  ? 145 PHE A CE2 1 
ATOM   1144 C  CZ  . PHE A  1  145 ? 5.145  13.773  -4.109  1.00 36.13  ? 145 PHE A CZ  1 
ATOM   1145 N  N   . SER A  1  146 ? 1.068  18.374  -8.160  1.00 67.77  ? 146 SER A N   1 
ATOM   1146 C  CA  . SER A  1  146 ? 0.366  19.036  -9.230  1.00 70.70  ? 146 SER A CA  1 
ATOM   1147 C  C   . SER A  1  146 ? 0.482  20.557  -9.090  1.00 71.42  ? 146 SER A C   1 
ATOM   1148 O  O   . SER A  1  146 ? 1.067  21.014  -8.087  1.00 72.49  ? 146 SER A O   1 
ATOM   1149 C  CB  . SER A  1  146 ? -1.098 18.599  -9.212  1.00 71.40  ? 146 SER A CB  1 
ATOM   1150 O  OG  . SER A  1  146 ? -1.807 19.158  -10.296 1.00 74.87  ? 146 SER A OG  1 
ATOM   1151 O  OXT . SER A  1  146 ? -0.006 21.272  -9.989  1.00 72.81  ? 146 SER A OXT 1 
ATOM   1152 N  N   . SER B  2  1   ? 35.854 12.445  -46.465 1.00 82.93  ? 1   SER B N   1 
ATOM   1153 C  CA  . SER B  2  1   ? 35.204 12.260  -45.175 1.00 83.77  ? 1   SER B CA  1 
ATOM   1154 C  C   . SER B  2  1   ? 33.847 12.944  -45.149 1.00 83.69  ? 1   SER B C   1 
ATOM   1155 O  O   . SER B  2  1   ? 33.611 13.916  -45.877 1.00 83.73  ? 1   SER B O   1 
ATOM   1156 C  CB  . SER B  2  1   ? 36.080 12.821  -44.057 1.00 84.75  ? 1   SER B CB  1 
ATOM   1157 O  OG  . SER B  2  1   ? 37.295 12.099  -43.958 1.00 86.00  ? 1   SER B OG  1 
ATOM   1158 N  N   . GLU B  2  2   ? 32.959 12.444  -44.297 1.00 82.89  ? 2   GLU B N   1 
ATOM   1159 C  CA  . GLU B  2  2   ? 31.617 13.004  -44.204 1.00 82.66  ? 2   GLU B CA  1 
ATOM   1160 C  C   . GLU B  2  2   ? 31.352 13.707  -42.884 1.00 79.95  ? 2   GLU B C   1 
ATOM   1161 O  O   . GLU B  2  2   ? 31.870 13.310  -41.844 1.00 79.77  ? 2   GLU B O   1 
ATOM   1162 C  CB  . GLU B  2  2   ? 30.577 11.897  -44.409 1.00 85.76  ? 2   GLU B CB  1 
ATOM   1163 C  CG  . GLU B  2  2   ? 29.549 12.179  -45.507 1.00 90.02  ? 2   GLU B CG  1 
ATOM   1164 C  CD  . GLU B  2  2   ? 30.187 12.501  -46.850 1.00 92.27  ? 2   GLU B CD  1 
ATOM   1165 O  OE1 . GLU B  2  2   ? 30.295 13.701  -47.195 1.00 93.16  ? 2   GLU B OE1 1 
ATOM   1166 O  OE2 . GLU B  2  2   ? 30.590 11.552  -47.559 1.00 93.49  ? 2   GLU B OE2 1 
ATOM   1167 N  N   . CYS B  2  3   ? 30.550 14.764  -42.934 1.00 76.79  ? 3   CYS B N   1 
ATOM   1168 C  CA  . CYS B  2  3   ? 30.200 15.504  -41.732 1.00 73.90  ? 3   CYS B CA  1 
ATOM   1169 C  C   . CYS B  2  3   ? 29.011 14.794  -41.091 1.00 71.95  ? 3   CYS B C   1 
ATOM   1170 O  O   . CYS B  2  3   ? 27.869 15.214  -41.238 1.00 71.91  ? 3   CYS B O   1 
ATOM   1171 C  CB  . CYS B  2  3   ? 29.854 16.968  -42.076 1.00 73.23  ? 3   CYS B CB  1 
ATOM   1172 S  SG  . CYS B  2  3   ? 29.283 17.996  -40.672 1.00 74.56  ? 3   CYS B SG  1 
ATOM   1173 N  N   . GLY B  2  4   ? 29.292 13.702  -40.391 1.00 70.15  ? 4   GLY B N   1 
ATOM   1174 C  CA  . GLY B  2  4   ? 28.240 12.943  -39.737 1.00 71.86  ? 4   GLY B CA  1 
ATOM   1175 C  C   . GLY B  2  4   ? 27.889 13.482  -38.365 1.00 72.08  ? 4   GLY B C   1 
ATOM   1176 O  O   . GLY B  2  4   ? 28.434 14.497  -37.949 1.00 72.67  ? 4   GLY B O   1 
ATOM   1177 N  N   . PRO B  2  5   ? 26.977 12.825  -37.637 1.00 72.52  ? 5   PRO B N   1 
ATOM   1178 C  CA  . PRO B  2  5   ? 26.556 13.253  -36.298 1.00 72.84  ? 5   PRO B CA  1 
ATOM   1179 C  C   . PRO B  2  5   ? 27.723 13.385  -35.337 1.00 72.61  ? 5   PRO B C   1 
ATOM   1180 O  O   . PRO B  2  5   ? 27.792 14.338  -34.563 1.00 72.95  ? 5   PRO B O   1 
ATOM   1181 C  CB  . PRO B  2  5   ? 25.588 12.153  -35.871 1.00 72.93  ? 5   PRO B CB  1 
ATOM   1182 C  CG  . PRO B  2  5   ? 24.956 11.762  -37.167 1.00 73.63  ? 5   PRO B CG  1 
ATOM   1183 C  CD  . PRO B  2  5   ? 26.173 11.678  -38.090 1.00 73.24  ? 5   PRO B CD  1 
ATOM   1184 N  N   . LEU B  2  6   ? 28.639 12.423  -35.393 1.00 71.15  ? 6   LEU B N   1 
ATOM   1185 C  CA  . LEU B  2  6   ? 29.798 12.449  -34.519 1.00 69.19  ? 6   LEU B CA  1 
ATOM   1186 C  C   . LEU B  2  6   ? 30.701 13.637  -34.856 1.00 67.81  ? 6   LEU B C   1 
ATOM   1187 O  O   . LEU B  2  6   ? 31.081 14.390  -33.966 1.00 66.69  ? 6   LEU B O   1 
ATOM   1188 C  CB  . LEU B  2  6   ? 30.575 11.130  -34.635 1.00 68.71  ? 6   LEU B CB  1 
ATOM   1189 C  CG  . LEU B  2  6   ? 29.858 9.846   -34.200 1.00 68.30  ? 6   LEU B CG  1 
ATOM   1190 C  CD1 . LEU B  2  6   ? 30.788 8.665   -34.352 1.00 67.41  ? 6   LEU B CD1 1 
ATOM   1191 C  CD2 . LEU B  2  6   ? 29.417 9.966   -32.757 1.00 67.34  ? 6   LEU B CD2 1 
ATOM   1192 N  N   . GLN B  2  7   ? 31.027 13.812  -36.133 1.00 66.26  ? 7   GLN B N   1 
ATOM   1193 C  CA  . GLN B  2  7   ? 31.888 14.914  -36.542 1.00 65.57  ? 7   GLN B CA  1 
ATOM   1194 C  C   . GLN B  2  7   ? 31.298 16.265  -36.162 1.00 64.76  ? 7   GLN B C   1 
ATOM   1195 O  O   . GLN B  2  7   ? 32.024 17.213  -35.866 1.00 63.79  ? 7   GLN B O   1 
ATOM   1196 C  CB  . GLN B  2  7   ? 32.129 14.882  -38.051 1.00 66.25  ? 7   GLN B CB  1 
ATOM   1197 C  CG  . GLN B  2  7   ? 32.964 13.709  -38.546 1.00 66.23  ? 7   GLN B CG  1 
ATOM   1198 C  CD  . GLN B  2  7   ? 32.300 12.363  -38.319 1.00 65.57  ? 7   GLN B CD  1 
ATOM   1199 O  OE1 . GLN B  2  7   ? 31.101 12.183  -38.570 1.00 67.65  ? 7   GLN B OE1 1 
ATOM   1200 N  NE2 . GLN B  2  7   ? 33.080 11.404  -37.857 1.00 63.08  ? 7   GLN B NE2 1 
ATOM   1201 N  N   . ARG B  2  8   ? 29.977 16.353  -36.175 1.00 64.14  ? 8   ARG B N   1 
ATOM   1202 C  CA  . ARG B  2  8   ? 29.312 17.593  -35.831 1.00 64.56  ? 8   ARG B CA  1 
ATOM   1203 C  C   . ARG B  2  8   ? 29.476 17.890  -34.339 1.00 63.77  ? 8   ARG B C   1 
ATOM   1204 O  O   . ARG B  2  8   ? 29.624 19.042  -33.937 1.00 63.57  ? 8   ARG B O   1 
ATOM   1205 C  CB  . ARG B  2  8   ? 27.840 17.498  -36.236 1.00 64.99  ? 8   ARG B CB  1 
ATOM   1206 C  CG  . ARG B  2  8   ? 27.669 17.448  -37.752 1.00 65.55  ? 8   ARG B CG  1 
ATOM   1207 C  CD  . ARG B  2  8   ? 26.285 16.970  -38.178 1.00 66.92  ? 8   ARG B CD  1 
ATOM   1208 N  NE  . ARG B  2  8   ? 26.248 16.721  -39.618 1.00 67.42  ? 8   ARG B NE  1 
ATOM   1209 C  CZ  . ARG B  2  8   ? 25.737 17.558  -40.513 1.00 67.38  ? 8   ARG B CZ  1 
ATOM   1210 N  NH1 . ARG B  2  8   ? 25.206 18.707  -40.123 1.00 67.60  ? 8   ARG B NH1 1 
ATOM   1211 N  NH2 . ARG B  2  8   ? 25.788 17.258  -41.802 1.00 66.85  ? 8   ARG B NH2 1 
ATOM   1212 N  N   . LEU B  2  9   ? 29.467 16.849  -33.519 1.00 62.00  ? 9   LEU B N   1 
ATOM   1213 C  CA  . LEU B  2  9   ? 29.642 17.039  -32.089 1.00 61.18  ? 9   LEU B CA  1 
ATOM   1214 C  C   . LEU B  2  9   ? 31.069 17.518  -31.812 1.00 59.74  ? 9   LEU B C   1 
ATOM   1215 O  O   . LEU B  2  9   ? 31.274 18.450  -31.020 1.00 60.22  ? 9   LEU B O   1 
ATOM   1216 C  CB  . LEU B  2  9   ? 29.373 15.729  -31.346 1.00 60.91  ? 9   LEU B CB  1 
ATOM   1217 C  CG  . LEU B  2  9   ? 27.910 15.295  -31.295 1.00 61.64  ? 9   LEU B CG  1 
ATOM   1218 C  CD1 . LEU B  2  9   ? 27.820 13.938  -30.659 1.00 62.90  ? 9   LEU B CD1 1 
ATOM   1219 C  CD2 . LEU B  2  9   ? 27.079 16.298  -30.517 1.00 61.29  ? 9   LEU B CD2 1 
ATOM   1220 N  N   . LYS B  2  10  ? 32.035 16.877  -32.469 1.00 56.75  ? 10  LYS B N   1 
ATOM   1221 C  CA  . LYS B  2  10  ? 33.448 17.211  -32.314 1.00 55.07  ? 10  LYS B CA  1 
ATOM   1222 C  C   . LYS B  2  10  ? 33.682 18.669  -32.709 1.00 54.54  ? 10  LYS B C   1 
ATOM   1223 O  O   . LYS B  2  10  ? 34.280 19.433  -31.953 1.00 54.19  ? 10  LYS B O   1 
ATOM   1224 C  CB  . LYS B  2  10  ? 34.314 16.298  -33.190 1.00 54.76  ? 10  LYS B CB  1 
ATOM   1225 C  CG  . LYS B  2  10  ? 35.814 16.438  -32.982 1.00 54.62  ? 10  LYS B CG  1 
ATOM   1226 C  CD  . LYS B  2  10  ? 36.308 15.414  -31.996 1.00 53.55  ? 10  LYS B CD  1 
ATOM   1227 C  CE  . LYS B  2  10  ? 37.559 14.752  -32.517 1.00 55.96  ? 10  LYS B CE  1 
ATOM   1228 N  NZ  . LYS B  2  10  ? 37.977 13.605  -31.663 1.00 58.64  ? 10  LYS B NZ  1 
ATOM   1229 N  N   . VAL B  2  11  ? 33.193 19.045  -33.888 1.00 53.92  ? 11  VAL B N   1 
ATOM   1230 C  CA  . VAL B  2  11  ? 33.341 20.404  -34.380 1.00 54.16  ? 11  VAL B CA  1 
ATOM   1231 C  C   . VAL B  2  11  ? 32.733 21.407  -33.404 1.00 54.32  ? 11  VAL B C   1 
ATOM   1232 O  O   . VAL B  2  11  ? 33.313 22.459  -33.135 1.00 53.45  ? 11  VAL B O   1 
ATOM   1233 C  CB  . VAL B  2  11  ? 32.693 20.567  -35.793 1.00 54.35  ? 11  VAL B CB  1 
ATOM   1234 C  CG1 . VAL B  2  11  ? 32.599 22.048  -36.178 1.00 52.65  ? 11  VAL B CG1 1 
ATOM   1235 C  CG2 . VAL B  2  11  ? 33.547 19.838  -36.825 1.00 52.68  ? 11  VAL B CG2 1 
ATOM   1236 N  N   . LYS B  2  12  ? 31.570 21.079  -32.863 1.00 55.10  ? 12  LYS B N   1 
ATOM   1237 C  CA  . LYS B  2  12  ? 30.925 21.976  -31.918 1.00 55.48  ? 12  LYS B CA  1 
ATOM   1238 C  C   . LYS B  2  12  ? 31.843 22.253  -30.732 1.00 54.43  ? 12  LYS B C   1 
ATOM   1239 O  O   . LYS B  2  12  ? 32.093 23.412  -30.396 1.00 54.09  ? 12  LYS B O   1 
ATOM   1240 C  CB  . LYS B  2  12  ? 29.614 21.365  -31.434 1.00 57.18  ? 12  LYS B CB  1 
ATOM   1241 C  CG  . LYS B  2  12  ? 28.479 21.439  -32.449 1.00 59.32  ? 12  LYS B CG  1 
ATOM   1242 C  CD  . LYS B  2  12  ? 27.343 20.531  -32.030 1.00 60.43  ? 12  LYS B CD  1 
ATOM   1243 C  CE  . LYS B  2  12  ? 26.099 20.772  -32.836 1.00 61.74  ? 12  LYS B CE  1 
ATOM   1244 N  NZ  . LYS B  2  12  ? 25.420 22.029  -32.424 1.00 61.24  ? 12  LYS B NZ  1 
ATOM   1245 N  N   . ARG B  2  13  ? 32.348 21.186  -30.113 1.00 52.60  ? 13  ARG B N   1 
ATOM   1246 C  CA  . ARG B  2  13  ? 33.216 21.317  -28.952 1.00 51.34  ? 13  ARG B CA  1 
ATOM   1247 C  C   . ARG B  2  13  ? 34.499 22.047  -29.319 1.00 49.72  ? 13  ARG B C   1 
ATOM   1248 O  O   . ARG B  2  13  ? 34.859 23.017  -28.670 1.00 49.96  ? 13  ARG B O   1 
ATOM   1249 C  CB  . ARG B  2  13  ? 33.534 19.930  -28.359 1.00 51.12  ? 13  ARG B CB  1 
ATOM   1250 C  CG  . ARG B  2  13  ? 34.210 19.953  -26.986 1.00 49.59  ? 13  ARG B CG  1 
ATOM   1251 C  CD  . ARG B  2  13  ? 34.279 18.559  -26.363 1.00 50.26  ? 13  ARG B CD  1 
ATOM   1252 N  NE  . ARG B  2  13  ? 34.898 17.548  -27.232 1.00 52.53  ? 13  ARG B NE  1 
ATOM   1253 C  CZ  . ARG B  2  13  ? 36.180 17.548  -27.609 1.00 54.28  ? 13  ARG B CZ  1 
ATOM   1254 N  NH1 . ARG B  2  13  ? 36.651 16.591  -28.402 1.00 53.68  ? 13  ARG B NH1 1 
ATOM   1255 N  NH2 . ARG B  2  13  ? 37.000 18.501  -27.183 1.00 55.43  ? 13  ARG B NH2 1 
ATOM   1256 N  N   . GLN B  2  14  ? 35.178 21.601  -30.368 1.00 48.26  ? 14  GLN B N   1 
ATOM   1257 C  CA  . GLN B  2  14  ? 36.416 22.245  -30.769 1.00 46.86  ? 14  GLN B CA  1 
ATOM   1258 C  C   . GLN B  2  14  ? 36.235 23.698  -31.150 1.00 45.40  ? 14  GLN B C   1 
ATOM   1259 O  O   . GLN B  2  14  ? 37.145 24.498  -30.943 1.00 45.93  ? 14  GLN B O   1 
ATOM   1260 C  CB  . GLN B  2  14  ? 37.096 21.484  -31.908 1.00 45.25  ? 14  GLN B CB  1 
ATOM   1261 C  CG  . GLN B  2  14  ? 37.500 20.071  -31.523 1.00 47.33  ? 14  GLN B CG  1 
ATOM   1262 C  CD  . GLN B  2  14  ? 38.655 19.540  -32.355 1.00 49.88  ? 14  GLN B CD  1 
ATOM   1263 O  OE1 . GLN B  2  14  ? 38.727 19.759  -33.572 1.00 50.21  ? 14  GLN B OE1 1 
ATOM   1264 N  NE2 . GLN B  2  14  ? 39.566 18.827  -31.703 1.00 48.42  ? 14  GLN B NE2 1 
ATOM   1265 N  N   . TRP B  2  15  ? 35.073 24.044  -31.694 1.00 42.96  ? 15  TRP B N   1 
ATOM   1266 C  CA  . TRP B  2  15  ? 34.805 25.429  -32.081 1.00 41.38  ? 15  TRP B CA  1 
ATOM   1267 C  C   . TRP B  2  15  ? 34.593 26.232  -30.808 1.00 41.09  ? 15  TRP B C   1 
ATOM   1268 O  O   . TRP B  2  15  ? 35.135 27.325  -30.659 1.00 38.14  ? 15  TRP B O   1 
ATOM   1269 C  CB  . TRP B  2  15  ? 33.566 25.514  -33.000 1.00 38.80  ? 15  TRP B CB  1 
ATOM   1270 C  CG  . TRP B  2  15  ? 32.982 26.891  -33.137 1.00 37.35  ? 15  TRP B CG  1 
ATOM   1271 C  CD1 . TRP B  2  15  ? 31.886 27.378  -32.479 1.00 36.93  ? 15  TRP B CD1 1 
ATOM   1272 C  CD2 . TRP B  2  15  ? 33.502 27.984  -33.911 1.00 35.83  ? 15  TRP B CD2 1 
ATOM   1273 N  NE1 . TRP B  2  15  ? 31.702 28.711  -32.789 1.00 37.42  ? 15  TRP B NE1 1 
ATOM   1274 C  CE2 . TRP B  2  15  ? 32.681 29.104  -33.665 1.00 35.53  ? 15  TRP B CE2 1 
ATOM   1275 C  CE3 . TRP B  2  15  ? 34.589 28.127  -34.790 1.00 36.53  ? 15  TRP B CE3 1 
ATOM   1276 C  CZ2 . TRP B  2  15  ? 32.914 30.346  -34.260 1.00 35.95  ? 15  TRP B CZ2 1 
ATOM   1277 C  CZ3 . TRP B  2  15  ? 34.816 29.375  -35.386 1.00 34.16  ? 15  TRP B CZ3 1 
ATOM   1278 C  CH2 . TRP B  2  15  ? 33.985 30.459  -35.116 1.00 34.66  ? 15  TRP B CH2 1 
ATOM   1279 N  N   . ALA B  2  16  ? 33.816 25.673  -29.886 1.00 43.51  ? 16  ALA B N   1 
ATOM   1280 C  CA  . ALA B  2  16  ? 33.544 26.347  -28.623 1.00 46.54  ? 16  ALA B CA  1 
ATOM   1281 C  C   . ALA B  2  16  ? 34.874 26.690  -27.940 1.00 48.09  ? 16  ALA B C   1 
ATOM   1282 O  O   . ALA B  2  16  ? 35.079 27.818  -27.484 1.00 48.42  ? 16  ALA B O   1 
ATOM   1283 C  CB  . ALA B  2  16  ? 32.687 25.462  -27.727 1.00 43.99  ? 16  ALA B CB  1 
ATOM   1284 N  N   . GLU B  2  17  ? 35.783 25.719  -27.884 1.00 49.73  ? 17  GLU B N   1 
ATOM   1285 C  CA  . GLU B  2  17  ? 37.081 25.966  -27.277 1.00 52.37  ? 17  GLU B CA  1 
ATOM   1286 C  C   . GLU B  2  17  ? 37.779 27.145  -27.963 1.00 52.20  ? 17  GLU B C   1 
ATOM   1287 O  O   . GLU B  2  17  ? 38.146 28.127  -27.310 1.00 51.49  ? 17  GLU B O   1 
ATOM   1288 C  CB  . GLU B  2  17  ? 37.955 24.700  -27.336 1.00 54.93  ? 17  GLU B CB  1 
ATOM   1289 C  CG  . GLU B  2  17  ? 37.796 23.789  -26.113 1.00 61.36  ? 17  GLU B CG  1 
ATOM   1290 C  CD  . GLU B  2  17  ? 38.020 22.303  -26.414 1.00 65.40  ? 17  GLU B CD  1 
ATOM   1291 O  OE1 . GLU B  2  17  ? 38.991 21.990  -27.140 1.00 69.25  ? 17  GLU B OE1 1 
ATOM   1292 O  OE2 . GLU B  2  17  ? 37.237 21.445  -25.917 1.00 63.52  ? 17  GLU B OE2 1 
ATOM   1293 N  N   . ALA B  2  18  ? 37.921 27.064  -29.284 1.00 51.70  ? 18  ALA B N   1 
ATOM   1294 C  CA  . ALA B  2  18  ? 38.579 28.110  -30.064 1.00 54.13  ? 18  ALA B CA  1 
ATOM   1295 C  C   . ALA B  2  18  ? 37.909 29.490  -30.016 1.00 55.54  ? 18  ALA B C   1 
ATOM   1296 O  O   . ALA B  2  18  ? 38.556 30.507  -29.719 1.00 56.10  ? 18  ALA B O   1 
ATOM   1297 C  CB  . ALA B  2  18  ? 38.715 27.657  -31.510 1.00 53.57  ? 18  ALA B CB  1 
ATOM   1298 N  N   . TYR B  2  19  ? 36.617 29.521  -30.318 1.00 56.52  ? 19  TYR B N   1 
ATOM   1299 C  CA  . TYR B  2  19  ? 35.856 30.761  -30.325 1.00 56.89  ? 19  TYR B CA  1 
ATOM   1300 C  C   . TYR B  2  19  ? 35.772 31.321  -28.908 1.00 59.54  ? 19  TYR B C   1 
ATOM   1301 O  O   . TYR B  2  19  ? 35.954 32.521  -28.695 1.00 59.98  ? 19  TYR B O   1 
ATOM   1302 C  CB  . TYR B  2  19  ? 34.469 30.496  -30.925 1.00 53.86  ? 19  TYR B CB  1 
ATOM   1303 C  CG  . TYR B  2  19  ? 33.638 31.733  -31.210 1.00 51.86  ? 19  TYR B CG  1 
ATOM   1304 C  CD1 . TYR B  2  19  ? 34.168 32.811  -31.919 1.00 51.81  ? 19  TYR B CD1 1 
ATOM   1305 C  CD2 . TYR B  2  19  ? 32.313 31.820  -30.784 1.00 50.38  ? 19  TYR B CD2 1 
ATOM   1306 C  CE1 . TYR B  2  19  ? 33.395 33.951  -32.200 1.00 50.76  ? 19  TYR B CE1 1 
ATOM   1307 C  CE2 . TYR B  2  19  ? 31.534 32.945  -31.056 1.00 49.72  ? 19  TYR B CE2 1 
ATOM   1308 C  CZ  . TYR B  2  19  ? 32.079 34.007  -31.766 1.00 50.63  ? 19  TYR B CZ  1 
ATOM   1309 O  OH  . TYR B  2  19  ? 31.304 35.114  -32.040 1.00 49.89  ? 19  TYR B OH  1 
ATOM   1310 N  N   . GLY B  2  20  ? 35.507 30.447  -27.937 1.00 62.56  ? 20  GLY B N   1 
ATOM   1311 C  CA  . GLY B  2  20  ? 35.443 30.868  -26.548 1.00 67.24  ? 20  GLY B CA  1 
ATOM   1312 C  C   . GLY B  2  20  ? 34.331 31.825  -26.173 1.00 70.84  ? 20  GLY B C   1 
ATOM   1313 O  O   . GLY B  2  20  ? 33.327 31.913  -26.873 1.00 71.31  ? 20  GLY B O   1 
ATOM   1314 N  N   . SER B  2  21  ? 34.522 32.549  -25.073 1.00 74.41  ? 21  SER B N   1 
ATOM   1315 C  CA  . SER B  2  21  ? 33.524 33.488  -24.572 1.00 78.36  ? 21  SER B CA  1 
ATOM   1316 C  C   . SER B  2  21  ? 33.614 34.909  -25.122 1.00 79.56  ? 21  SER B C   1 
ATOM   1317 O  O   . SER B  2  21  ? 32.631 35.647  -25.076 1.00 79.66  ? 21  SER B O   1 
ATOM   1318 C  CB  . SER B  2  21  ? 33.594 33.541  -23.046 1.00 81.20  ? 21  SER B CB  1 
ATOM   1319 O  OG  . SER B  2  21  ? 32.514 34.287  -22.518 1.00 85.55  ? 21  SER B OG  1 
ATOM   1320 N  N   . GLY B  2  22  ? 34.782 35.304  -25.622 1.00 81.65  ? 22  GLY B N   1 
ATOM   1321 C  CA  . GLY B  2  22  ? 34.916 36.647  -26.175 1.00 82.47  ? 22  GLY B CA  1 
ATOM   1322 C  C   . GLY B  2  22  ? 36.244 37.370  -25.995 1.00 82.41  ? 22  GLY B C   1 
ATOM   1323 O  O   . GLY B  2  22  ? 36.569 38.281  -26.764 1.00 82.82  ? 22  GLY B O   1 
ATOM   1324 N  N   . ASN B  2  23  ? 37.016 36.972  -24.987 1.00 80.96  ? 23  ASN B N   1 
ATOM   1325 C  CA  . ASN B  2  23  ? 38.298 37.610  -24.711 1.00 78.81  ? 23  ASN B CA  1 
ATOM   1326 C  C   . ASN B  2  23  ? 39.319 37.367  -25.820 1.00 75.84  ? 23  ASN B C   1 
ATOM   1327 O  O   . ASN B  2  23  ? 40.022 38.288  -26.246 1.00 75.80  ? 23  ASN B O   1 
ATOM   1328 C  CB  . ASN B  2  23  ? 38.846 37.099  -23.377 1.00 81.84  ? 23  ASN B CB  1 
ATOM   1329 C  CG  . ASN B  2  23  ? 37.826 37.208  -22.246 1.00 84.29  ? 23  ASN B CG  1 
ATOM   1330 O  OD1 . ASN B  2  23  ? 36.836 36.461  -22.204 1.00 84.07  ? 23  ASN B OD1 1 
ATOM   1331 N  ND2 . ASN B  2  23  ? 38.064 38.145  -21.326 1.00 84.23  ? 23  ASN B ND2 1 
ATOM   1332 N  N   . GLY B  2  24  ? 39.404 36.132  -26.291 1.00 71.12  ? 24  GLY B N   1 
ATOM   1333 C  CA  . GLY B  2  24  ? 40.360 35.843  -27.342 1.00 66.41  ? 24  GLY B CA  1 
ATOM   1334 C  C   . GLY B  2  24  ? 39.813 35.971  -28.750 1.00 62.27  ? 24  GLY B C   1 
ATOM   1335 O  O   . GLY B  2  24  ? 40.525 35.693  -29.709 1.00 60.19  ? 24  GLY B O   1 
ATOM   1336 N  N   . ARG B  2  25  ? 38.561 36.407  -28.869 1.00 58.80  ? 25  ARG B N   1 
ATOM   1337 C  CA  . ARG B  2  25  ? 37.900 36.548  -30.164 1.00 57.24  ? 25  ARG B CA  1 
ATOM   1338 C  C   . ARG B  2  25  ? 38.566 37.493  -31.165 1.00 56.83  ? 25  ARG B C   1 
ATOM   1339 O  O   . ARG B  2  25  ? 38.654 37.184  -32.351 1.00 54.98  ? 25  ARG B O   1 
ATOM   1340 C  CB  . ARG B  2  25  ? 36.437 36.957  -29.955 1.00 55.28  ? 25  ARG B CB  1 
ATOM   1341 C  CG  . ARG B  2  25  ? 35.561 35.824  -29.422 1.00 53.62  ? 25  ARG B CG  1 
ATOM   1342 C  CD  . ARG B  2  25  ? 34.081 36.194  -29.344 1.00 50.16  ? 25  ARG B CD  1 
ATOM   1343 N  NE  . ARG B  2  25  ? 33.290 35.070  -28.839 1.00 50.34  ? 25  ARG B NE  1 
ATOM   1344 C  CZ  . ARG B  2  25  ? 32.007 35.137  -28.501 1.00 50.37  ? 25  ARG B CZ  1 
ATOM   1345 N  NH1 . ARG B  2  25  ? 31.324 36.277  -28.608 1.00 51.83  ? 25  ARG B NH1 1 
ATOM   1346 N  NH2 . ARG B  2  25  ? 31.397 34.053  -28.057 1.00 48.90  ? 25  ARG B NH2 1 
ATOM   1347 N  N   . GLU B  2  26  ? 39.029 38.647  -30.700 1.00 57.97  ? 26  GLU B N   1 
ATOM   1348 C  CA  . GLU B  2  26  ? 39.675 39.587  -31.598 1.00 58.57  ? 26  GLU B CA  1 
ATOM   1349 C  C   . GLU B  2  26  ? 40.942 38.993  -32.194 1.00 58.76  ? 26  GLU B C   1 
ATOM   1350 O  O   . GLU B  2  26  ? 41.181 39.127  -33.391 1.00 58.48  ? 26  GLU B O   1 
ATOM   1351 C  CB  . GLU B  2  26  ? 40.031 40.885  -30.882 1.00 60.00  ? 26  GLU B CB  1 
ATOM   1352 C  CG  . GLU B  2  26  ? 40.737 41.878  -31.790 1.00 61.46  ? 26  GLU B CG  1 
ATOM   1353 C  CD  . GLU B  2  26  ? 41.290 43.057  -31.037 1.00 62.66  ? 26  GLU B CD  1 
ATOM   1354 O  OE1 . GLU B  2  26  ? 42.400 42.922  -30.485 1.00 62.11  ? 26  GLU B OE1 1 
ATOM   1355 O  OE2 . GLU B  2  26  ? 40.618 44.111  -30.986 1.00 65.76  ? 26  GLU B OE2 1 
ATOM   1356 N  N   . GLU B  2  27  ? 41.763 38.361  -31.356 1.00 58.78  ? 27  GLU B N   1 
ATOM   1357 C  CA  . GLU B  2  27  ? 42.994 37.747  -31.830 1.00 58.67  ? 27  GLU B CA  1 
ATOM   1358 C  C   . GLU B  2  27  ? 42.641 36.575  -32.749 1.00 56.49  ? 27  GLU B C   1 
ATOM   1359 O  O   . GLU B  2  27  ? 43.282 36.376  -33.770 1.00 55.93  ? 27  GLU B O   1 
ATOM   1360 C  CB  . GLU B  2  27  ? 43.848 37.271  -30.643 1.00 61.36  ? 27  GLU B CB  1 
ATOM   1361 C  CG  . GLU B  2  27  ? 45.170 36.575  -31.026 1.00 67.59  ? 27  GLU B CG  1 
ATOM   1362 C  CD  . GLU B  2  27  ? 44.989 35.129  -31.472 1.00 70.35  ? 27  GLU B CD  1 
ATOM   1363 O  OE1 . GLU B  2  27  ? 45.867 34.616  -32.195 1.00 72.02  ? 27  GLU B OE1 1 
ATOM   1364 O  OE2 . GLU B  2  27  ? 43.981 34.495  -31.092 1.00 74.40  ? 27  GLU B OE2 1 
ATOM   1365 N  N   . PHE B  2  28  ? 41.610 35.818  -32.390 1.00 55.28  ? 28  PHE B N   1 
ATOM   1366 C  CA  . PHE B  2  28  ? 41.146 34.675  -33.179 1.00 54.32  ? 28  PHE B CA  1 
ATOM   1367 C  C   . PHE B  2  28  ? 40.822 35.113  -34.603 1.00 54.42  ? 28  PHE B C   1 
ATOM   1368 O  O   . PHE B  2  28  ? 41.370 34.595  -35.576 1.00 52.71  ? 28  PHE B O   1 
ATOM   1369 C  CB  . PHE B  2  28  ? 39.882 34.087  -32.565 1.00 53.06  ? 28  PHE B CB  1 
ATOM   1370 C  CG  . PHE B  2  28  ? 39.414 32.821  -33.222 1.00 53.09  ? 28  PHE B CG  1 
ATOM   1371 C  CD1 . PHE B  2  28  ? 38.072 32.462  -33.187 1.00 54.05  ? 28  PHE B CD1 1 
ATOM   1372 C  CD2 . PHE B  2  28  ? 40.321 31.934  -33.800 1.00 53.80  ? 28  PHE B CD2 1 
ATOM   1373 C  CE1 . PHE B  2  28  ? 37.635 31.233  -33.706 1.00 51.72  ? 28  PHE B CE1 1 
ATOM   1374 C  CE2 . PHE B  2  28  ? 39.892 30.697  -34.326 1.00 52.80  ? 28  PHE B CE2 1 
ATOM   1375 C  CZ  . PHE B  2  28  ? 38.550 30.353  -34.273 1.00 51.66  ? 28  PHE B CZ  1 
ATOM   1376 N  N   . GLY B  2  29  ? 39.913 36.077  -34.701 1.00 54.68  ? 29  GLY B N   1 
ATOM   1377 C  CA  . GLY B  2  29  ? 39.496 36.587  -35.991 1.00 55.25  ? 29  GLY B CA  1 
ATOM   1378 C  C   . GLY B  2  29  ? 40.584 37.289  -36.775 1.00 54.51  ? 29  GLY B C   1 
ATOM   1379 O  O   . GLY B  2  29  ? 40.554 37.301  -37.999 1.00 53.92  ? 29  GLY B O   1 
ATOM   1380 N  N   . HIS B  2  30  ? 41.543 37.886  -36.088 1.00 55.33  ? 30  HIS B N   1 
ATOM   1381 C  CA  . HIS B  2  30  ? 42.615 38.573  -36.789 1.00 56.60  ? 30  HIS B CA  1 
ATOM   1382 C  C   . HIS B  2  30  ? 43.531 37.535  -37.422 1.00 57.38  ? 30  HIS B C   1 
ATOM   1383 O  O   . HIS B  2  30  ? 43.945 37.676  -38.575 1.00 57.63  ? 30  HIS B O   1 
ATOM   1384 C  CB  . HIS B  2  30  ? 43.410 39.470  -35.832 1.00 55.25  ? 30  HIS B CB  1 
ATOM   1385 C  CG  . HIS B  2  30  ? 44.626 40.075  -36.452 1.00 53.09  ? 30  HIS B CG  1 
ATOM   1386 N  ND1 . HIS B  2  30  ? 45.814 39.389  -36.574 1.00 53.04  ? 30  HIS B ND1 1 
ATOM   1387 C  CD2 . HIS B  2  30  ? 44.824 41.279  -37.039 1.00 53.81  ? 30  HIS B CD2 1 
ATOM   1388 C  CE1 . HIS B  2  30  ? 46.693 40.146  -37.206 1.00 54.10  ? 30  HIS B CE1 1 
ATOM   1389 N  NE2 . HIS B  2  30  ? 46.117 41.297  -37.501 1.00 53.65  ? 30  HIS B NE2 1 
ATOM   1390 N  N   . PHE B  2  31  ? 43.830 36.487  -36.664 1.00 57.82  ? 31  PHE B N   1 
ATOM   1391 C  CA  . PHE B  2  31  ? 44.690 35.417  -37.143 1.00 59.17  ? 31  PHE B CA  1 
ATOM   1392 C  C   . PHE B  2  31  ? 44.107 34.863  -38.427 1.00 61.93  ? 31  PHE B C   1 
ATOM   1393 O  O   . PHE B  2  31  ? 44.815 34.654  -39.418 1.00 63.20  ? 31  PHE B O   1 
ATOM   1394 C  CB  . PHE B  2  31  ? 44.758 34.290  -36.120 1.00 56.06  ? 31  PHE B CB  1 
ATOM   1395 C  CG  . PHE B  2  31  ? 45.726 33.206  -36.488 1.00 55.13  ? 31  PHE B CG  1 
ATOM   1396 C  CD1 . PHE B  2  31  ? 47.084 33.340  -36.202 1.00 54.79  ? 31  PHE B CD1 1 
ATOM   1397 C  CD2 . PHE B  2  31  ? 45.286 32.045  -37.110 1.00 53.83  ? 31  PHE B CD2 1 
ATOM   1398 C  CE1 . PHE B  2  31  ? 47.997 32.321  -36.528 1.00 53.94  ? 31  PHE B CE1 1 
ATOM   1399 C  CE2 . PHE B  2  31  ? 46.185 31.020  -37.440 1.00 52.83  ? 31  PHE B CE2 1 
ATOM   1400 C  CZ  . PHE B  2  31  ? 47.547 31.160  -37.146 1.00 53.18  ? 31  PHE B CZ  1 
ATOM   1401 N  N   . ILE B  2  32  ? 42.795 34.640  -38.389 1.00 63.51  ? 32  ILE B N   1 
ATOM   1402 C  CA  . ILE B  2  32  ? 42.051 34.092  -39.508 1.00 64.09  ? 32  ILE B CA  1 
ATOM   1403 C  C   . ILE B  2  32  ? 42.150 34.955  -40.752 1.00 65.24  ? 32  ILE B C   1 
ATOM   1404 O  O   . ILE B  2  32  ? 42.680 34.519  -41.765 1.00 64.41  ? 32  ILE B O   1 
ATOM   1405 C  CB  . ILE B  2  32  ? 40.561 33.871  -39.098 1.00 62.96  ? 32  ILE B CB  1 
ATOM   1406 C  CG1 . ILE B  2  32  ? 40.469 32.645  -38.183 1.00 62.87  ? 32  ILE B CG1 1 
ATOM   1407 C  CG2 . ILE B  2  32  ? 39.676 33.694  -40.315 1.00 62.34  ? 32  ILE B CG2 1 
ATOM   1408 C  CD1 . ILE B  2  32  ? 39.084 32.384  -37.611 1.00 62.52  ? 32  ILE B CD1 1 
ATOM   1409 N  N   . TRP B  2  33  ? 41.665 36.183  -40.676 1.00 68.07  ? 33  TRP B N   1 
ATOM   1410 C  CA  . TRP B  2  33  ? 41.701 37.057  -41.838 1.00 71.05  ? 33  TRP B CA  1 
ATOM   1411 C  C   . TRP B  2  33  ? 43.080 37.505  -42.309 1.00 71.58  ? 33  TRP B C   1 
ATOM   1412 O  O   . TRP B  2  33  ? 43.224 37.979  -43.431 1.00 71.92  ? 33  TRP B O   1 
ATOM   1413 C  CB  . TRP B  2  33  ? 40.802 38.272  -41.604 1.00 73.28  ? 33  TRP B CB  1 
ATOM   1414 C  CG  . TRP B  2  33  ? 39.367 37.922  -41.721 1.00 75.54  ? 33  TRP B CG  1 
ATOM   1415 C  CD1 . TRP B  2  33  ? 38.520 37.555  -40.716 1.00 76.48  ? 33  TRP B CD1 1 
ATOM   1416 C  CD2 . TRP B  2  33  ? 38.623 37.822  -42.929 1.00 77.03  ? 33  TRP B CD2 1 
ATOM   1417 N  NE1 . TRP B  2  33  ? 37.289 37.230  -41.226 1.00 76.90  ? 33  TRP B NE1 1 
ATOM   1418 C  CE2 . TRP B  2  33  ? 37.327 37.384  -42.587 1.00 77.78  ? 33  TRP B CE2 1 
ATOM   1419 C  CE3 . TRP B  2  33  ? 38.927 38.057  -44.274 1.00 78.00  ? 33  TRP B CE3 1 
ATOM   1420 C  CZ2 . TRP B  2  33  ? 36.334 37.177  -43.541 1.00 79.13  ? 33  TRP B CZ2 1 
ATOM   1421 C  CZ3 . TRP B  2  33  ? 37.941 37.850  -45.224 1.00 80.14  ? 33  TRP B CZ3 1 
ATOM   1422 C  CH2 . TRP B  2  33  ? 36.658 37.415  -44.852 1.00 81.05  ? 33  TRP B CH2 1 
ATOM   1423 N  N   . ALA B  2  34  ? 44.094 37.359  -41.463 1.00 72.42  ? 34  ALA B N   1 
ATOM   1424 C  CA  . ALA B  2  34  ? 45.446 37.746  -41.855 1.00 72.71  ? 34  ALA B CA  1 
ATOM   1425 C  C   . ALA B  2  34  ? 45.959 36.643  -42.753 1.00 72.33  ? 34  ALA B C   1 
ATOM   1426 O  O   . ALA B  2  34  ? 46.807 36.871  -43.602 1.00 72.05  ? 34  ALA B O   1 
ATOM   1427 C  CB  . ALA B  2  34  ? 46.336 37.884  -40.637 1.00 73.42  ? 34  ALA B CB  1 
ATOM   1428 N  N   . ASN B  2  35  ? 45.430 35.447  -42.542 1.00 72.59  ? 35  ASN B N   1 
ATOM   1429 C  CA  . ASN B  2  35  ? 45.782 34.277  -43.331 1.00 72.40  ? 35  ASN B CA  1 
ATOM   1430 C  C   . ASN B  2  35  ? 45.046 34.358  -44.662 1.00 72.18  ? 35  ASN B C   1 
ATOM   1431 O  O   . ASN B  2  35  ? 45.643 34.163  -45.715 1.00 72.40  ? 35  ASN B O   1 
ATOM   1432 C  CB  . ASN B  2  35  ? 45.372 32.995  -42.599 1.00 73.37  ? 35  ASN B CB  1 
ATOM   1433 C  CG  . ASN B  2  35  ? 45.502 31.751  -43.469 1.00 74.21  ? 35  ASN B CG  1 
ATOM   1434 O  OD1 . ASN B  2  35  ? 44.846 31.623  -44.505 1.00 73.32  ? 35  ASN B OD1 1 
ATOM   1435 N  ND2 . ASN B  2  35  ? 46.348 30.823  -43.043 1.00 74.40  ? 35  ASN B ND2 1 
ATOM   1436 N  N   . VAL B  2  36  ? 43.748 34.643  -44.608 1.00 71.29  ? 36  VAL B N   1 
ATOM   1437 C  CA  . VAL B  2  36  ? 42.945 34.748  -45.819 1.00 71.36  ? 36  VAL B CA  1 
ATOM   1438 C  C   . VAL B  2  36  ? 43.587 35.686  -46.833 1.00 71.81  ? 36  VAL B C   1 
ATOM   1439 O  O   . VAL B  2  36  ? 43.942 35.281  -47.945 1.00 72.01  ? 36  VAL B O   1 
ATOM   1440 C  CB  . VAL B  2  36  ? 41.514 35.272  -45.528 1.00 70.37  ? 36  VAL B CB  1 
ATOM   1441 C  CG1 . VAL B  2  36  ? 40.846 35.701  -46.832 1.00 69.79  ? 36  VAL B CG1 1 
ATOM   1442 C  CG2 . VAL B  2  36  ? 40.682 34.186  -44.865 1.00 70.12  ? 36  VAL B CG2 1 
ATOM   1443 N  N   . PHE B  2  37  ? 43.734 36.944  -46.443 1.00 71.72  ? 37  PHE B N   1 
ATOM   1444 C  CA  . PHE B  2  37  ? 44.312 37.946  -47.320 1.00 70.63  ? 37  PHE B CA  1 
ATOM   1445 C  C   . PHE B  2  37  ? 45.763 37.708  -47.731 1.00 70.98  ? 37  PHE B C   1 
ATOM   1446 O  O   . PHE B  2  37  ? 46.248 38.335  -48.671 1.00 70.28  ? 37  PHE B O   1 
ATOM   1447 C  CB  . PHE B  2  37  ? 44.161 39.332  -46.691 1.00 69.29  ? 37  PHE B CB  1 
ATOM   1448 C  CG  . PHE B  2  37  ? 42.734 39.809  -46.607 1.00 68.40  ? 37  PHE B CG  1 
ATOM   1449 C  CD1 . PHE B  2  37  ? 41.792 39.390  -47.541 1.00 67.74  ? 37  PHE B CD1 1 
ATOM   1450 C  CD2 . PHE B  2  37  ? 42.340 40.713  -45.626 1.00 68.50  ? 37  PHE B CD2 1 
ATOM   1451 C  CE1 . PHE B  2  37  ? 40.482 39.869  -47.498 1.00 67.07  ? 37  PHE B CE1 1 
ATOM   1452 C  CE2 . PHE B  2  37  ? 41.028 41.199  -45.576 1.00 68.08  ? 37  PHE B CE2 1 
ATOM   1453 C  CZ  . PHE B  2  37  ? 40.101 40.777  -46.514 1.00 67.58  ? 37  PHE B CZ  1 
ATOM   1454 N  N   . LYS B  2  38  ? 46.467 36.812  -47.048 1.00 71.95  ? 38  LYS B N   1 
ATOM   1455 C  CA  . LYS B  2  38  ? 47.849 36.548  -47.428 1.00 72.83  ? 38  LYS B CA  1 
ATOM   1456 C  C   . LYS B  2  38  ? 47.808 35.523  -48.545 1.00 74.03  ? 38  LYS B C   1 
ATOM   1457 O  O   . LYS B  2  38  ? 48.521 35.648  -49.534 1.00 74.83  ? 38  LYS B O   1 
ATOM   1458 C  CB  . LYS B  2  38  ? 48.668 36.004  -46.251 1.00 71.47  ? 38  LYS B CB  1 
ATOM   1459 C  CG  . LYS B  2  38  ? 50.168 35.963  -46.533 1.00 70.64  ? 38  LYS B CG  1 
ATOM   1460 C  CD  . LYS B  2  38  ? 50.969 35.371  -45.373 1.00 70.77  ? 38  LYS B CD  1 
ATOM   1461 C  CE  . LYS B  2  38  ? 52.488 35.548  -45.563 1.00 70.98  ? 38  LYS B CE  1 
ATOM   1462 N  NZ  . LYS B  2  38  ? 52.938 36.985  -45.647 1.00 70.30  ? 38  LYS B NZ  1 
ATOM   1463 N  N   . VAL B  2  39  ? 46.949 34.521  -48.385 1.00 75.77  ? 39  VAL B N   1 
ATOM   1464 C  CA  . VAL B  2  39  ? 46.790 33.455  -49.367 1.00 77.19  ? 39  VAL B CA  1 
ATOM   1465 C  C   . VAL B  2  39  ? 46.064 33.976  -50.602 1.00 77.37  ? 39  VAL B C   1 
ATOM   1466 O  O   . VAL B  2  39  ? 46.259 33.465  -51.707 1.00 77.94  ? 39  VAL B O   1 
ATOM   1467 C  CB  . VAL B  2  39  ? 45.978 32.274  -48.773 1.00 78.84  ? 39  VAL B CB  1 
ATOM   1468 C  CG1 . VAL B  2  39  ? 45.805 31.175  -49.809 1.00 80.26  ? 39  VAL B CG1 1 
ATOM   1469 C  CG2 . VAL B  2  39  ? 46.683 31.732  -47.541 1.00 79.89  ? 39  VAL B CG2 1 
ATOM   1470 N  N   . ALA B  2  40  ? 45.234 34.996  -50.409 1.00 77.22  ? 40  ALA B N   1 
ATOM   1471 C  CA  . ALA B  2  40  ? 44.482 35.581  -51.505 1.00 76.80  ? 40  ALA B CA  1 
ATOM   1472 C  C   . ALA B  2  40  ? 44.364 37.090  -51.346 1.00 76.40  ? 40  ALA B C   1 
ATOM   1473 O  O   . ALA B  2  40  ? 43.284 37.612  -51.067 1.00 76.56  ? 40  ALA B O   1 
ATOM   1474 C  CB  . ALA B  2  40  ? 43.101 34.957  -51.575 1.00 77.37  ? 40  ALA B CB  1 
ATOM   1475 N  N   . PRO B  2  41  ? 45.477 37.813  -51.535 1.00 75.83  ? 41  PRO B N   1 
ATOM   1476 C  CA  . PRO B  2  41  ? 45.454 39.271  -51.402 1.00 75.73  ? 41  PRO B CA  1 
ATOM   1477 C  C   . PRO B  2  41  ? 44.427 39.911  -52.323 1.00 75.88  ? 41  PRO B C   1 
ATOM   1478 O  O   . PRO B  2  41  ? 43.841 40.944  -52.014 1.00 75.39  ? 41  PRO B O   1 
ATOM   1479 C  CB  . PRO B  2  41  ? 46.891 39.667  -51.740 1.00 75.29  ? 41  PRO B CB  1 
ATOM   1480 C  CG  . PRO B  2  41  ? 47.339 38.576  -52.664 1.00 75.63  ? 41  PRO B CG  1 
ATOM   1481 C  CD  . PRO B  2  41  ? 46.793 37.348  -51.995 1.00 75.59  ? 41  PRO B CD  1 
ATOM   1482 N  N   . SER B  2  42  ? 44.199 39.276  -53.457 1.00 77.62  ? 42  SER B N   1 
ATOM   1483 C  CA  . SER B  2  42  ? 43.248 39.784  -54.430 1.00 79.64  ? 42  SER B CA  1 
ATOM   1484 C  C   . SER B  2  42  ? 41.841 39.998  -53.880 1.00 81.25  ? 42  SER B C   1 
ATOM   1485 O  O   . SER B  2  42  ? 41.142 40.929  -54.283 1.00 81.99  ? 42  SER B O   1 
ATOM   1486 C  CB  . SER B  2  42  ? 43.194 38.832  -55.624 1.00 79.24  ? 42  SER B CB  1 
ATOM   1487 O  OG  . SER B  2  42  ? 43.242 37.484  -55.193 1.00 77.51  ? 42  SER B OG  1 
ATOM   1488 N  N   . ALA B  2  43  ? 41.439 39.139  -52.941 1.00 83.28  ? 43  ALA B N   1 
ATOM   1489 C  CA  . ALA B  2  43  ? 40.095 39.183  -52.341 1.00 84.42  ? 43  ALA B CA  1 
ATOM   1490 C  C   . ALA B  2  43  ? 39.750 40.421  -51.525 1.00 85.38  ? 43  ALA B C   1 
ATOM   1491 O  O   . ALA B  2  43  ? 38.564 40.720  -51.331 1.00 86.11  ? 43  ALA B O   1 
ATOM   1492 C  CB  . ALA B  2  43  ? 39.875 37.943  -51.499 1.00 84.11  ? 43  ALA B CB  1 
ATOM   1493 N  N   . ARG B  2  44  ? 40.760 41.125  -51.027 1.00 86.02  ? 44  ARG B N   1 
ATOM   1494 C  CA  . ARG B  2  44  ? 40.519 42.305  -50.209 1.00 87.10  ? 44  ARG B CA  1 
ATOM   1495 C  C   . ARG B  2  44  ? 39.620 43.313  -50.891 1.00 87.88  ? 44  ARG B C   1 
ATOM   1496 O  O   . ARG B  2  44  ? 38.841 44.017  -50.250 1.00 87.85  ? 44  ARG B O   1 
ATOM   1497 C  CB  . ARG B  2  44  ? 41.834 43.048  -49.920 1.00 86.79  ? 44  ARG B CB  1 
ATOM   1498 C  CG  . ARG B  2  44  ? 42.989 42.169  -49.569 1.00 87.58  ? 44  ARG B CG  1 
ATOM   1499 C  CD  . ARG B  2  44  ? 44.179 43.031  -49.193 1.00 87.09  ? 44  ARG B CD  1 
ATOM   1500 N  NE  . ARG B  2  44  ? 45.045 42.344  -48.241 1.00 86.64  ? 44  ARG B NE  1 
ATOM   1501 C  CZ  . ARG B  2  44  ? 45.267 42.760  -46.995 1.00 85.46  ? 44  ARG B CZ  1 
ATOM   1502 N  NH1 . ARG B  2  44  ? 44.688 43.867  -46.543 1.00 82.76  ? 44  ARG B NH1 1 
ATOM   1503 N  NH2 . ARG B  2  44  ? 46.065 42.058  -46.204 1.00 84.96  ? 44  ARG B NH2 1 
ATOM   1504 N  N   . ASP B  2  45  ? 39.739 43.381  -52.209 1.00 88.93  ? 45  ASP B N   1 
ATOM   1505 C  CA  . ASP B  2  45  ? 38.953 44.330  -52.966 1.00 90.20  ? 45  ASP B CA  1 
ATOM   1506 C  C   . ASP B  2  45  ? 37.456 44.250  -52.734 1.00 89.47  ? 45  ASP B C   1 
ATOM   1507 O  O   . ASP B  2  45  ? 36.748 45.230  -52.924 1.00 88.98  ? 45  ASP B O   1 
ATOM   1508 C  CB  . ASP B  2  45  ? 39.256 44.195  -54.454 1.00 92.48  ? 45  ASP B CB  1 
ATOM   1509 C  CG  . ASP B  2  45  ? 38.526 45.233  -55.285 1.00 95.04  ? 45  ASP B CG  1 
ATOM   1510 O  OD1 . ASP B  2  45  ? 38.593 46.443  -54.941 1.00 95.55  ? 45  ASP B OD1 1 
ATOM   1511 O  OD2 . ASP B  2  45  ? 37.883 44.840  -56.280 1.00 95.92  ? 45  ASP B OD2 1 
ATOM   1512 N  N   . MET B  2  46  ? 36.968 43.093  -52.314 1.00 89.41  ? 46  MET B N   1 
ATOM   1513 C  CA  . MET B  2  46  ? 35.537 42.933  -52.077 1.00 89.22  ? 46  MET B CA  1 
ATOM   1514 C  C   . MET B  2  46  ? 35.110 43.527  -50.749 1.00 88.32  ? 46  MET B C   1 
ATOM   1515 O  O   . MET B  2  46  ? 33.919 43.643  -50.469 1.00 88.03  ? 46  MET B O   1 
ATOM   1516 C  CB  . MET B  2  46  ? 35.175 41.456  -52.096 1.00 90.03  ? 46  MET B CB  1 
ATOM   1517 C  CG  . MET B  2  46  ? 35.274 40.808  -53.452 1.00 91.47  ? 46  MET B CG  1 
ATOM   1518 S  SD  . MET B  2  46  ? 35.058 39.033  -53.276 1.00 94.16  ? 46  MET B SD  1 
ATOM   1519 C  CE  . MET B  2  46  ? 33.427 38.992  -52.504 1.00 94.71  ? 46  MET B CE  1 
ATOM   1520 N  N   . PHE B  2  47  ? 36.084 43.919  -49.943 1.00 87.21  ? 47  PHE B N   1 
ATOM   1521 C  CA  . PHE B  2  47  ? 35.800 44.463  -48.627 1.00 85.76  ? 47  PHE B CA  1 
ATOM   1522 C  C   . PHE B  2  47  ? 36.049 45.963  -48.497 1.00 84.97  ? 47  PHE B C   1 
ATOM   1523 O  O   . PHE B  2  47  ? 36.328 46.457  -47.400 1.00 84.43  ? 47  PHE B O   1 
ATOM   1524 C  CB  . PHE B  2  47  ? 36.642 43.712  -47.603 1.00 86.12  ? 47  PHE B CB  1 
ATOM   1525 C  CG  . PHE B  2  47  ? 36.343 42.247  -47.537 1.00 85.97  ? 47  PHE B CG  1 
ATOM   1526 C  CD1 . PHE B  2  47  ? 35.254 41.788  -46.803 1.00 86.18  ? 47  PHE B CD1 1 
ATOM   1527 C  CD2 . PHE B  2  47  ? 37.143 41.329  -48.207 1.00 85.36  ? 47  PHE B CD2 1 
ATOM   1528 C  CE1 . PHE B  2  47  ? 34.965 40.439  -46.732 1.00 87.21  ? 47  PHE B CE1 1 
ATOM   1529 C  CE2 . PHE B  2  47  ? 36.865 39.974  -48.147 1.00 87.09  ? 47  PHE B CE2 1 
ATOM   1530 C  CZ  . PHE B  2  47  ? 35.769 39.525  -47.405 1.00 88.08  ? 47  PHE B CZ  1 
ATOM   1531 N  N   . LYS B  2  48  ? 35.949 46.686  -49.605 1.00 83.50  ? 48  LYS B N   1 
ATOM   1532 C  CA  . LYS B  2  48  ? 36.169 48.131  -49.590 1.00 81.97  ? 48  LYS B CA  1 
ATOM   1533 C  C   . LYS B  2  48  ? 35.364 48.876  -48.513 1.00 79.51  ? 48  LYS B C   1 
ATOM   1534 O  O   . LYS B  2  48  ? 35.872 49.804  -47.883 1.00 78.41  ? 48  LYS B O   1 
ATOM   1535 C  CB  . LYS B  2  48  ? 35.840 48.735  -50.962 1.00 83.83  ? 48  LYS B CB  1 
ATOM   1536 C  CG  . LYS B  2  48  ? 36.905 48.532  -52.027 1.00 86.48  ? 48  LYS B CG  1 
ATOM   1537 C  CD  . LYS B  2  48  ? 38.180 49.300  -51.698 1.00 88.88  ? 48  LYS B CD  1 
ATOM   1538 C  CE  . LYS B  2  48  ? 39.248 49.138  -52.787 1.00 89.78  ? 48  LYS B CE  1 
ATOM   1539 N  NZ  . LYS B  2  48  ? 39.741 47.735  -52.930 1.00 90.42  ? 48  LYS B NZ  1 
ATOM   1540 N  N   . ARG B  2  49  ? 34.119 48.469  -48.294 1.00 76.49  ? 49  ARG B N   1 
ATOM   1541 C  CA  . ARG B  2  49  ? 33.274 49.146  -47.311 1.00 74.61  ? 49  ARG B CA  1 
ATOM   1542 C  C   . ARG B  2  49  ? 33.634 48.901  -45.844 1.00 73.41  ? 49  ARG B C   1 
ATOM   1543 O  O   . ARG B  2  49  ? 33.219 49.656  -44.960 1.00 72.41  ? 49  ARG B O   1 
ATOM   1544 C  CB  . ARG B  2  49  ? 31.813 48.765  -47.519 1.00 74.12  ? 49  ARG B CB  1 
ATOM   1545 C  CG  . ARG B  2  49  ? 30.845 49.674  -46.773 1.00 72.80  ? 49  ARG B CG  1 
ATOM   1546 C  CD  . ARG B  2  49  ? 29.446 49.124  -46.853 1.00 73.56  ? 49  ARG B CD  1 
ATOM   1547 N  NE  . ARG B  2  49  ? 29.322 47.890  -46.080 1.00 74.54  ? 49  ARG B NE  1 
ATOM   1548 C  CZ  . ARG B  2  49  ? 29.236 47.855  -44.755 1.00 74.22  ? 49  ARG B CZ  1 
ATOM   1549 N  NH1 . ARG B  2  49  ? 29.261 48.990  -44.069 1.00 75.20  ? 49  ARG B NH1 1 
ATOM   1550 N  NH2 . ARG B  2  49  ? 29.113 46.697  -44.116 1.00 71.94  ? 49  ARG B NH2 1 
ATOM   1551 N  N   . VAL B  2  50  ? 34.391 47.843  -45.578 1.00 71.69  ? 50  VAL B N   1 
ATOM   1552 C  CA  . VAL B  2  50  ? 34.766 47.525  -44.212 1.00 68.40  ? 50  VAL B CA  1 
ATOM   1553 C  C   . VAL B  2  50  ? 36.281 47.568  -44.042 1.00 68.31  ? 50  VAL B C   1 
ATOM   1554 O  O   . VAL B  2  50  ? 36.855 46.806  -43.267 1.00 69.15  ? 50  VAL B O   1 
ATOM   1555 C  CB  . VAL B  2  50  ? 34.216 46.134  -43.810 1.00 66.92  ? 50  VAL B CB  1 
ATOM   1556 C  CG1 . VAL B  2  50  ? 32.715 46.101  -44.027 1.00 64.47  ? 50  VAL B CG1 1 
ATOM   1557 C  CG2 . VAL B  2  50  ? 34.886 45.043  -44.617 1.00 65.52  ? 50  VAL B CG2 1 
ATOM   1558 N  N   . ARG B  2  51  ? 36.919 48.467  -44.787 1.00 66.71  ? 51  ARG B N   1 
ATOM   1559 C  CA  . ARG B  2  51  ? 38.364 48.668  -44.733 1.00 65.08  ? 51  ARG B CA  1 
ATOM   1560 C  C   . ARG B  2  51  ? 39.231 47.426  -44.876 1.00 64.58  ? 51  ARG B C   1 
ATOM   1561 O  O   . ARG B  2  51  ? 40.156 47.228  -44.099 1.00 65.04  ? 51  ARG B O   1 
ATOM   1562 C  CB  . ARG B  2  51  ? 38.713 49.392  -43.437 1.00 63.71  ? 51  ARG B CB  1 
ATOM   1563 C  CG  . ARG B  2  51  ? 38.131 50.787  -43.364 1.00 63.33  ? 51  ARG B CG  1 
ATOM   1564 C  CD  . ARG B  2  51  ? 38.680 51.626  -44.501 1.00 64.35  ? 51  ARG B CD  1 
ATOM   1565 N  NE  . ARG B  2  51  ? 40.143 51.652  -44.515 1.00 63.97  ? 51  ARG B NE  1 
ATOM   1566 C  CZ  . ARG B  2  51  ? 40.887 52.226  -43.575 1.00 63.62  ? 51  ARG B CZ  1 
ATOM   1567 N  NH1 . ARG B  2  51  ? 40.307 52.824  -42.536 1.00 61.35  ? 51  ARG B NH1 1 
ATOM   1568 N  NH2 . ARG B  2  51  ? 42.211 52.208  -43.676 1.00 63.43  ? 51  ARG B NH2 1 
ATOM   1569 N  N   . GLY B  2  52  ? 38.948 46.608  -45.882 1.00 65.27  ? 52  GLY B N   1 
ATOM   1570 C  CA  . GLY B  2  52  ? 39.714 45.390  -46.111 1.00 66.13  ? 52  GLY B CA  1 
ATOM   1571 C  C   . GLY B  2  52  ? 41.203 45.603  -46.327 1.00 68.36  ? 52  GLY B C   1 
ATOM   1572 O  O   . GLY B  2  52  ? 41.982 44.643  -46.341 1.00 69.71  ? 52  GLY B O   1 
ATOM   1573 N  N   . ASP B  2  53  ? 41.600 46.858  -46.508 1.00 69.12  ? 53  ASP B N   1 
ATOM   1574 C  CA  . ASP B  2  53  ? 43.001 47.207  -46.708 1.00 70.25  ? 53  ASP B CA  1 
ATOM   1575 C  C   . ASP B  2  53  ? 43.728 47.190  -45.366 1.00 71.16  ? 53  ASP B C   1 
ATOM   1576 O  O   . ASP B  2  53  ? 44.935 46.946  -45.301 1.00 72.84  ? 53  ASP B O   1 
ATOM   1577 C  CB  . ASP B  2  53  ? 43.103 48.603  -47.317 1.00 71.86  ? 53  ASP B CB  1 
ATOM   1578 C  CG  . ASP B  2  53  ? 42.199 49.604  -46.621 1.00 74.23  ? 53  ASP B CG  1 
ATOM   1579 O  OD1 . ASP B  2  53  ? 40.964 49.408  -46.648 1.00 75.92  ? 53  ASP B OD1 1 
ATOM   1580 O  OD2 . ASP B  2  53  ? 42.717 50.583  -46.044 1.00 74.28  ? 53  ASP B OD2 1 
ATOM   1581 N  N   . ASN B  2  54  ? 42.979 47.435  -44.295 1.00 70.58  ? 54  ASN B N   1 
ATOM   1582 C  CA  . ASN B  2  54  ? 43.550 47.483  -42.952 1.00 69.13  ? 54  ASN B CA  1 
ATOM   1583 C  C   . ASN B  2  54  ? 42.707 46.716  -41.932 1.00 67.50  ? 54  ASN B C   1 
ATOM   1584 O  O   . ASN B  2  54  ? 41.815 47.283  -41.296 1.00 65.45  ? 54  ASN B O   1 
ATOM   1585 C  CB  . ASN B  2  54  ? 43.667 48.940  -42.509 1.00 69.84  ? 54  ASN B CB  1 
ATOM   1586 C  CG  . ASN B  2  54  ? 44.537 49.099  -41.304 1.00 69.65  ? 54  ASN B CG  1 
ATOM   1587 O  OD1 . ASN B  2  54  ? 44.781 48.135  -40.580 1.00 69.81  ? 54  ASN B OD1 1 
ATOM   1588 N  ND2 . ASN B  2  54  ? 45.009 50.316  -41.068 1.00 70.76  ? 54  ASN B ND2 1 
ATOM   1589 N  N   . ILE B  2  55  ? 43.012 45.433  -41.764 1.00 66.38  ? 55  ILE B N   1 
ATOM   1590 C  CA  . ILE B  2  55  ? 42.272 44.579  -40.840 1.00 64.96  ? 55  ILE B CA  1 
ATOM   1591 C  C   . ILE B  2  55  ? 42.522 44.904  -39.373 1.00 64.29  ? 55  ILE B C   1 
ATOM   1592 O  O   . ILE B  2  55  ? 42.084 44.167  -38.483 1.00 65.64  ? 55  ILE B O   1 
ATOM   1593 C  CB  . ILE B  2  55  ? 42.595 43.081  -41.070 1.00 64.35  ? 55  ILE B CB  1 
ATOM   1594 C  CG1 . ILE B  2  55  ? 44.001 42.742  -40.582 1.00 63.07  ? 55  ILE B CG1 1 
ATOM   1595 C  CG2 . ILE B  2  55  ? 42.466 42.760  -42.546 1.00 66.13  ? 55  ILE B CG2 1 
ATOM   1596 C  CD1 . ILE B  2  55  ? 44.360 41.281  -40.760 1.00 62.21  ? 55  ILE B CD1 1 
ATOM   1597 N  N   . TYR B  2  56  ? 43.230 45.998  -39.120 1.00 61.58  ? 56  TYR B N   1 
ATOM   1598 C  CA  . TYR B  2  56  ? 43.518 46.411  -37.761 1.00 58.75  ? 56  TYR B CA  1 
ATOM   1599 C  C   . TYR B  2  56  ? 42.523 47.476  -37.338 1.00 57.26  ? 56  TYR B C   1 
ATOM   1600 O  O   . TYR B  2  56  ? 42.487 47.873  -36.176 1.00 57.81  ? 56  TYR B O   1 
ATOM   1601 C  CB  . TYR B  2  56  ? 44.930 46.969  -37.680 1.00 58.43  ? 56  TYR B CB  1 
ATOM   1602 C  CG  . TYR B  2  56  ? 45.999 45.941  -37.957 1.00 57.64  ? 56  TYR B CG  1 
ATOM   1603 C  CD1 . TYR B  2  56  ? 46.614 45.247  -36.915 1.00 57.09  ? 56  TYR B CD1 1 
ATOM   1604 C  CD2 . TYR B  2  56  ? 46.399 45.656  -39.259 1.00 57.63  ? 56  TYR B CD2 1 
ATOM   1605 C  CE1 . TYR B  2  56  ? 47.611 44.296  -37.158 1.00 55.22  ? 56  TYR B CE1 1 
ATOM   1606 C  CE2 . TYR B  2  56  ? 47.399 44.703  -39.513 1.00 56.29  ? 56  TYR B CE2 1 
ATOM   1607 C  CZ  . TYR B  2  56  ? 47.993 44.036  -38.451 1.00 53.48  ? 56  TYR B CZ  1 
ATOM   1608 O  OH  . TYR B  2  56  ? 48.997 43.134  -38.666 1.00 53.38  ? 56  TYR B OH  1 
ATOM   1609 N  N   . THR B  2  57  ? 41.712 47.919  -38.291 1.00 55.84  ? 57  THR B N   1 
ATOM   1610 C  CA  . THR B  2  57  ? 40.716 48.962  -38.058 1.00 56.43  ? 57  THR B CA  1 
ATOM   1611 C  C   . THR B  2  57  ? 39.436 48.469  -37.370 1.00 56.20  ? 57  THR B C   1 
ATOM   1612 O  O   . THR B  2  57  ? 39.021 47.325  -37.527 1.00 55.32  ? 57  THR B O   1 
ATOM   1613 C  CB  . THR B  2  57  ? 40.288 49.643  -39.394 1.00 56.32  ? 57  THR B CB  1 
ATOM   1614 O  OG1 . THR B  2  57  ? 39.597 48.693  -40.210 1.00 53.60  ? 57  THR B OG1 1 
ATOM   1615 C  CG2 . THR B  2  57  ? 41.502 50.178  -40.148 1.00 55.14  ? 57  THR B CG2 1 
ATOM   1616 N  N   . PRO B  2  58  ? 38.792 49.349  -36.597 1.00 55.50  ? 58  PRO B N   1 
ATOM   1617 C  CA  . PRO B  2  58  ? 37.561 48.933  -35.922 1.00 56.08  ? 58  PRO B CA  1 
ATOM   1618 C  C   . PRO B  2  58  ? 36.525 48.435  -36.938 1.00 56.15  ? 58  PRO B C   1 
ATOM   1619 O  O   . PRO B  2  58  ? 35.821 47.455  -36.700 1.00 56.90  ? 58  PRO B O   1 
ATOM   1620 C  CB  . PRO B  2  58  ? 37.121 50.212  -35.204 1.00 56.17  ? 58  PRO B CB  1 
ATOM   1621 C  CG  . PRO B  2  58  ? 38.434 50.867  -34.872 1.00 55.57  ? 58  PRO B CG  1 
ATOM   1622 C  CD  . PRO B  2  58  ? 39.225 50.683  -36.154 1.00 54.52  ? 58  PRO B CD  1 
ATOM   1623 N  N   . ALA B  2  59  ? 36.458 49.105  -38.078 1.00 55.83  ? 59  ALA B N   1 
ATOM   1624 C  CA  . ALA B  2  59  ? 35.516 48.750  -39.133 1.00 55.60  ? 59  ALA B CA  1 
ATOM   1625 C  C   . ALA B  2  59  ? 35.665 47.298  -39.582 1.00 53.81  ? 59  ALA B C   1 
ATOM   1626 O  O   . ALA B  2  59  ? 34.680 46.560  -39.712 1.00 53.06  ? 59  ALA B O   1 
ATOM   1627 C  CB  . ALA B  2  59  ? 35.699 49.687  -40.328 1.00 56.63  ? 59  ALA B CB  1 
ATOM   1628 N  N   . PHE B  2  60  ? 36.894 46.883  -39.827 1.00 52.07  ? 60  PHE B N   1 
ATOM   1629 C  CA  . PHE B  2  60  ? 37.109 45.520  -40.259 1.00 53.13  ? 60  PHE B CA  1 
ATOM   1630 C  C   . PHE B  2  60  ? 36.918 44.566  -39.107 1.00 53.24  ? 60  PHE B C   1 
ATOM   1631 O  O   . PHE B  2  60  ? 36.395 43.466  -39.272 1.00 52.83  ? 60  PHE B O   1 
ATOM   1632 C  CB  . PHE B  2  60  ? 38.514 45.313  -40.793 1.00 53.98  ? 60  PHE B CB  1 
ATOM   1633 C  CG  . PHE B  2  60  ? 38.676 44.003  -41.468 1.00 54.21  ? 60  PHE B CG  1 
ATOM   1634 C  CD1 . PHE B  2  60  ? 38.170 43.811  -42.743 1.00 55.19  ? 60  PHE B CD1 1 
ATOM   1635 C  CD2 . PHE B  2  60  ? 39.250 42.930  -40.798 1.00 55.44  ? 60  PHE B CD2 1 
ATOM   1636 C  CE1 . PHE B  2  60  ? 38.227 42.561  -43.348 1.00 57.04  ? 60  PHE B CE1 1 
ATOM   1637 C  CE2 . PHE B  2  60  ? 39.318 41.673  -41.385 1.00 57.22  ? 60  PHE B CE2 1 
ATOM   1638 C  CZ  . PHE B  2  60  ? 38.804 41.484  -42.665 1.00 57.19  ? 60  PHE B CZ  1 
ATOM   1639 N  N   . ARG B  2  61  ? 37.398 44.978  -37.940 1.00 53.60  ? 61  ARG B N   1 
ATOM   1640 C  CA  . ARG B  2  61  ? 37.279 44.155  -36.765 1.00 51.85  ? 61  ARG B CA  1 
ATOM   1641 C  C   . ARG B  2  61  ? 35.800 43.849  -36.519 1.00 52.71  ? 61  ARG B C   1 
ATOM   1642 O  O   . ARG B  2  61  ? 35.450 42.718  -36.166 1.00 52.65  ? 61  ARG B O   1 
ATOM   1643 C  CB  . ARG B  2  61  ? 37.930 44.859  -35.575 1.00 50.06  ? 61  ARG B CB  1 
ATOM   1644 C  CG  . ARG B  2  61  ? 39.454 44.973  -35.698 1.00 50.00  ? 61  ARG B CG  1 
ATOM   1645 C  CD  . ARG B  2  61  ? 40.083 45.441  -34.377 1.00 51.34  ? 61  ARG B CD  1 
ATOM   1646 N  NE  . ARG B  2  61  ? 41.524 45.694  -34.465 1.00 51.57  ? 61  ARG B NE  1 
ATOM   1647 C  CZ  . ARG B  2  61  ? 42.480 44.761  -34.412 1.00 51.41  ? 61  ARG B CZ  1 
ATOM   1648 N  NH1 . ARG B  2  61  ? 43.757 45.109  -34.507 1.00 48.96  ? 61  ARG B NH1 1 
ATOM   1649 N  NH2 . ARG B  2  61  ? 42.176 43.482  -34.254 1.00 53.13  ? 61  ARG B NH2 1 
ATOM   1650 N  N   . ALA B  2  62  ? 34.932 44.835  -36.740 1.00 51.98  ? 62  ALA B N   1 
ATOM   1651 C  CA  . ALA B  2  62  ? 33.502 44.624  -36.549 1.00 53.27  ? 62  ALA B CA  1 
ATOM   1652 C  C   . ALA B  2  62  ? 33.003 43.598  -37.580 1.00 54.87  ? 62  ALA B C   1 
ATOM   1653 O  O   . ALA B  2  62  ? 32.181 42.731  -37.264 1.00 54.95  ? 62  ALA B O   1 
ATOM   1654 C  CB  . ALA B  2  62  ? 32.753 45.932  -36.688 1.00 51.57  ? 62  ALA B CB  1 
ATOM   1655 N  N   . HIS B  2  63  ? 33.506 43.701  -38.808 1.00 55.15  ? 63  HIS B N   1 
ATOM   1656 C  CA  . HIS B  2  63  ? 33.136 42.765  -39.868 1.00 55.69  ? 63  HIS B CA  1 
ATOM   1657 C  C   . HIS B  2  63  ? 33.587 41.370  -39.435 1.00 54.09  ? 63  HIS B C   1 
ATOM   1658 O  O   . HIS B  2  63  ? 32.788 40.429  -39.418 1.00 54.03  ? 63  HIS B O   1 
ATOM   1659 C  CB  . HIS B  2  63  ? 33.817 43.141  -41.198 1.00 58.51  ? 63  HIS B CB  1 
ATOM   1660 C  CG  . HIS B  2  63  ? 33.781 42.046  -42.220 1.00 61.07  ? 63  HIS B CG  1 
ATOM   1661 N  ND1 . HIS B  2  63  ? 32.628 41.687  -42.887 1.00 61.91  ? 63  HIS B ND1 1 
ATOM   1662 C  CD2 . HIS B  2  63  ? 34.744 41.194  -42.645 1.00 62.38  ? 63  HIS B CD2 1 
ATOM   1663 C  CE1 . HIS B  2  63  ? 32.882 40.657  -43.678 1.00 62.99  ? 63  HIS B CE1 1 
ATOM   1664 N  NE2 . HIS B  2  63  ? 34.161 40.337  -43.549 1.00 63.19  ? 63  HIS B NE2 1 
ATOM   1665 N  N   . ALA B  2  64  ? 34.865 41.239  -39.083 1.00 52.50  ? 64  ALA B N   1 
ATOM   1666 C  CA  . ALA B  2  64  ? 35.394 39.951  -38.635 1.00 52.00  ? 64  ALA B CA  1 
ATOM   1667 C  C   . ALA B  2  64  ? 34.458 39.398  -37.544 1.00 51.11  ? 64  ALA B C   1 
ATOM   1668 O  O   . ALA B  2  64  ? 34.158 38.201  -37.484 1.00 48.99  ? 64  ALA B O   1 
ATOM   1669 C  CB  . ALA B  2  64  ? 36.807 40.122  -38.089 1.00 49.64  ? 64  ALA B CB  1 
ATOM   1670 N  N   . THR B  2  65  ? 33.992 40.294  -36.685 1.00 50.75  ? 65  THR B N   1 
ATOM   1671 C  CA  . THR B  2  65  ? 33.080 39.918  -35.621 1.00 49.84  ? 65  THR B CA  1 
ATOM   1672 C  C   . THR B  2  65  ? 31.845 39.249  -36.239 1.00 49.69  ? 65  THR B C   1 
ATOM   1673 O  O   . THR B  2  65  ? 31.470 38.137  -35.852 1.00 49.21  ? 65  THR B O   1 
ATOM   1674 C  CB  . THR B  2  65  ? 32.654 41.176  -34.791 1.00 49.41  ? 65  THR B CB  1 
ATOM   1675 O  OG1 . THR B  2  65  ? 33.769 41.650  -34.032 1.00 48.33  ? 65  THR B OG1 1 
ATOM   1676 C  CG2 . THR B  2  65  ? 31.509 40.851  -33.857 1.00 47.09  ? 65  THR B CG2 1 
ATOM   1677 N  N   . ARG B  2  66  ? 31.237 39.925  -37.215 1.00 49.70  ? 66  ARG B N   1 
ATOM   1678 C  CA  . ARG B  2  66  ? 30.040 39.421  -37.887 1.00 48.28  ? 66  ARG B CA  1 
ATOM   1679 C  C   . ARG B  2  66  ? 30.266 38.086  -38.584 1.00 46.61  ? 66  ARG B C   1 
ATOM   1680 O  O   . ARG B  2  66  ? 29.394 37.222  -38.574 1.00 44.73  ? 66  ARG B O   1 
ATOM   1681 C  CB  . ARG B  2  66  ? 29.517 40.448  -38.900 1.00 47.29  ? 66  ARG B CB  1 
ATOM   1682 C  CG  . ARG B  2  66  ? 28.932 41.698  -38.269 1.00 50.42  ? 66  ARG B CG  1 
ATOM   1683 C  CD  . ARG B  2  66  ? 28.211 42.550  -39.303 1.00 52.02  ? 66  ARG B CD  1 
ATOM   1684 N  NE  . ARG B  2  66  ? 29.140 43.098  -40.283 1.00 55.83  ? 66  ARG B NE  1 
ATOM   1685 C  CZ  . ARG B  2  66  ? 29.871 44.189  -40.093 1.00 58.13  ? 66  ARG B CZ  1 
ATOM   1686 N  NH1 . ARG B  2  66  ? 30.701 44.611  -41.047 1.00 61.98  ? 66  ARG B NH1 1 
ATOM   1687 N  NH2 . ARG B  2  66  ? 29.754 44.875  -38.963 1.00 56.28  ? 66  ARG B NH2 1 
ATOM   1688 N  N   . VAL B  2  67  ? 31.441 37.906  -39.177 1.00 45.50  ? 67  VAL B N   1 
ATOM   1689 C  CA  . VAL B  2  67  ? 31.721 36.657  -39.866 1.00 47.44  ? 67  VAL B CA  1 
ATOM   1690 C  C   . VAL B  2  67  ? 31.782 35.493  -38.896 1.00 49.64  ? 67  VAL B C   1 
ATOM   1691 O  O   . VAL B  2  67  ? 31.141 34.463  -39.116 1.00 51.64  ? 67  VAL B O   1 
ATOM   1692 C  CB  . VAL B  2  67  ? 33.062 36.697  -40.631 1.00 46.20  ? 67  VAL B CB  1 
ATOM   1693 C  CG1 . VAL B  2  67  ? 33.367 35.319  -41.195 1.00 43.16  ? 67  VAL B CG1 1 
ATOM   1694 C  CG2 . VAL B  2  67  ? 33.001 37.721  -41.746 1.00 46.49  ? 67  VAL B CG2 1 
ATOM   1695 N  N   . LEU B  2  68  ? 32.565 35.646  -37.828 1.00 50.60  ? 68  LEU B N   1 
ATOM   1696 C  CA  . LEU B  2  68  ? 32.690 34.576  -36.854 1.00 49.89  ? 68  LEU B CA  1 
ATOM   1697 C  C   . LEU B  2  68  ? 31.335 34.330  -36.227 1.00 49.99  ? 68  LEU B C   1 
ATOM   1698 O  O   . LEU B  2  68  ? 30.975 33.175  -35.946 1.00 48.25  ? 68  LEU B O   1 
ATOM   1699 C  CB  . LEU B  2  68  ? 33.732 34.923  -35.787 1.00 48.42  ? 68  LEU B CB  1 
ATOM   1700 C  CG  . LEU B  2  68  ? 35.133 35.221  -36.320 1.00 47.32  ? 68  LEU B CG  1 
ATOM   1701 C  CD1 . LEU B  2  68  ? 36.122 35.057  -35.177 1.00 47.93  ? 68  LEU B CD1 1 
ATOM   1702 C  CD2 . LEU B  2  68  ? 35.505 34.283  -37.438 1.00 48.00  ? 68  LEU B CD2 1 
ATOM   1703 N  N   . GLY B  2  69  ? 30.585 35.417  -36.021 1.00 48.93  ? 69  GLY B N   1 
ATOM   1704 C  CA  . GLY B  2  69  ? 29.254 35.294  -35.457 1.00 50.97  ? 69  GLY B CA  1 
ATOM   1705 C  C   . GLY B  2  69  ? 28.403 34.400  -36.349 1.00 53.18  ? 69  GLY B C   1 
ATOM   1706 O  O   . GLY B  2  69  ? 27.511 33.678  -35.869 1.00 53.15  ? 69  GLY B O   1 
ATOM   1707 N  N   . GLY B  2  70  ? 28.695 34.449  -37.656 1.00 53.33  ? 70  GLY B N   1 
ATOM   1708 C  CA  . GLY B  2  70  ? 27.978 33.656  -38.641 1.00 52.53  ? 70  GLY B CA  1 
ATOM   1709 C  C   . GLY B  2  70  ? 28.381 32.197  -38.605 1.00 53.60  ? 70  GLY B C   1 
ATOM   1710 O  O   . GLY B  2  70  ? 27.551 31.302  -38.775 1.00 52.33  ? 70  GLY B O   1 
ATOM   1711 N  N   . LEU B  2  71  ? 29.673 31.951  -38.401 1.00 55.58  ? 71  LEU B N   1 
ATOM   1712 C  CA  . LEU B  2  71  ? 30.176 30.581  -38.320 1.00 56.06  ? 71  LEU B CA  1 
ATOM   1713 C  C   . LEU B  2  71  ? 29.599 29.929  -37.061 1.00 56.13  ? 71  LEU B C   1 
ATOM   1714 O  O   . LEU B  2  71  ? 29.182 28.771  -37.082 1.00 53.45  ? 71  LEU B O   1 
ATOM   1715 C  CB  . LEU B  2  71  ? 31.701 30.580  -38.235 1.00 56.85  ? 71  LEU B CB  1 
ATOM   1716 C  CG  . LEU B  2  71  ? 32.499 30.370  -39.516 1.00 58.77  ? 71  LEU B CG  1 
ATOM   1717 C  CD1 . LEU B  2  71  ? 33.997 30.562  -39.247 1.00 59.63  ? 71  LEU B CD1 1 
ATOM   1718 C  CD2 . LEU B  2  71  ? 32.223 28.967  -40.038 1.00 58.03  ? 71  LEU B CD2 1 
ATOM   1719 N  N   . ASP B  2  72  ? 29.573 30.702  -35.974 1.00 55.97  ? 72  ASP B N   1 
ATOM   1720 C  CA  . ASP B  2  72  ? 29.080 30.233  -34.687 1.00 56.35  ? 72  ASP B CA  1 
ATOM   1721 C  C   . ASP B  2  72  ? 27.658 29.741  -34.804 1.00 58.20  ? 72  ASP B C   1 
ATOM   1722 O  O   . ASP B  2  72  ? 27.327 28.678  -34.279 1.00 58.44  ? 72  ASP B O   1 
ATOM   1723 C  CB  . ASP B  2  72  ? 29.179 31.347  -33.630 1.00 54.65  ? 72  ASP B CB  1 
ATOM   1724 C  CG  . ASP B  2  72  ? 28.651 30.918  -32.264 1.00 50.69  ? 72  ASP B CG  1 
ATOM   1725 O  OD1 . ASP B  2  72  ? 27.488 31.217  -31.930 1.00 49.82  ? 72  ASP B OD1 1 
ATOM   1726 O  OD2 . ASP B  2  72  ? 29.397 30.265  -31.522 1.00 50.89  ? 72  ASP B OD2 1 
ATOM   1727 N  N   . MET B  2  73  ? 26.818 30.511  -35.487 1.00 60.27  ? 73  MET B N   1 
ATOM   1728 C  CA  . MET B  2  73  ? 25.425 30.122  -35.666 1.00 61.66  ? 73  MET B CA  1 
ATOM   1729 C  C   . MET B  2  73  ? 25.338 28.792  -36.407 1.00 61.50  ? 73  MET B C   1 
ATOM   1730 O  O   . MET B  2  73  ? 24.584 27.906  -36.014 1.00 62.37  ? 73  MET B O   1 
ATOM   1731 C  CB  . MET B  2  73  ? 24.680 31.190  -36.453 1.00 63.67  ? 73  MET B CB  1 
ATOM   1732 C  CG  . MET B  2  73  ? 24.688 32.536  -35.800 1.00 66.41  ? 73  MET B CG  1 
ATOM   1733 S  SD  . MET B  2  73  ? 23.783 33.688  -36.821 1.00 71.30  ? 73  MET B SD  1 
ATOM   1734 C  CE  . MET B  2  73  ? 22.114 33.330  -36.304 1.00 69.46  ? 73  MET B CE  1 
ATOM   1735 N  N   . CYS B  2  74  ? 26.120 28.651  -37.472 1.00 60.29  ? 74  CYS B N   1 
ATOM   1736 C  CA  . CYS B  2  74  ? 26.098 27.424  -38.244 1.00 61.50  ? 74  CYS B CA  1 
ATOM   1737 C  C   . CYS B  2  74  ? 26.618 26.265  -37.429 1.00 61.09  ? 74  CYS B C   1 
ATOM   1738 O  O   . CYS B  2  74  ? 26.013 25.197  -37.452 1.00 62.37  ? 74  CYS B O   1 
ATOM   1739 C  CB  . CYS B  2  74  ? 26.936 27.543  -39.519 1.00 64.37  ? 74  CYS B CB  1 
ATOM   1740 S  SG  . CYS B  2  74  ? 26.436 28.861  -40.617 1.00 70.20  ? 74  CYS B SG  1 
ATOM   1741 N  N   . VAL B  2  75  ? 27.724 26.453  -36.709 1.00 59.24  ? 75  VAL B N   1 
ATOM   1742 C  CA  . VAL B  2  75  ? 28.261 25.344  -35.921 1.00 58.16  ? 75  VAL B CA  1 
ATOM   1743 C  C   . VAL B  2  75  ? 27.231 24.936  -34.872 1.00 58.04  ? 75  VAL B C   1 
ATOM   1744 O  O   . VAL B  2  75  ? 26.965 23.748  -34.670 1.00 56.82  ? 75  VAL B O   1 
ATOM   1745 C  CB  . VAL B  2  75  ? 29.630 25.702  -35.242 1.00 57.87  ? 75  VAL B CB  1 
ATOM   1746 C  CG1 . VAL B  2  75  ? 30.080 24.574  -34.318 1.00 54.37  ? 75  VAL B CG1 1 
ATOM   1747 C  CG2 . VAL B  2  75  ? 30.699 25.914  -36.307 1.00 54.96  ? 75  VAL B CG2 1 
ATOM   1748 N  N   . ALA B  2  76  ? 26.624 25.929  -34.237 1.00 58.21  ? 76  ALA B N   1 
ATOM   1749 C  CA  . ALA B  2  76  ? 25.622 25.678  -33.209 1.00 59.92  ? 76  ALA B CA  1 
ATOM   1750 C  C   . ALA B  2  76  ? 24.400 24.975  -33.765 1.00 61.45  ? 76  ALA B C   1 
ATOM   1751 O  O   . ALA B  2  76  ? 23.666 24.329  -33.014 1.00 63.15  ? 76  ALA B O   1 
ATOM   1752 C  CB  . ALA B  2  76  ? 25.191 26.999  -32.550 1.00 59.90  ? 76  ALA B CB  1 
ATOM   1753 N  N   . LEU B  2  77  ? 24.166 25.106  -35.070 1.00 61.44  ? 77  LEU B N   1 
ATOM   1754 C  CA  . LEU B  2  77  ? 22.996 24.477  -35.682 1.00 61.08  ? 77  LEU B CA  1 
ATOM   1755 C  C   . LEU B  2  77  ? 23.302 23.191  -36.430 1.00 61.27  ? 77  LEU B C   1 
ATOM   1756 O  O   . LEU B  2  77  ? 22.393 22.518  -36.903 1.00 59.76  ? 77  LEU B O   1 
ATOM   1757 C  CB  . LEU B  2  77  ? 22.307 25.459  -36.631 1.00 60.96  ? 77  LEU B CB  1 
ATOM   1758 C  CG  . LEU B  2  77  ? 21.629 26.656  -35.964 1.00 61.24  ? 77  LEU B CG  1 
ATOM   1759 C  CD1 . LEU B  2  77  ? 21.327 27.745  -36.996 1.00 59.95  ? 77  LEU B CD1 1 
ATOM   1760 C  CD2 . LEU B  2  77  ? 20.370 26.177  -35.270 1.00 60.65  ? 77  LEU B CD2 1 
ATOM   1761 N  N   . LEU B  2  78  ? 24.583 22.839  -36.523 1.00 63.01  ? 78  LEU B N   1 
ATOM   1762 C  CA  . LEU B  2  78  ? 24.989 21.628  -37.236 1.00 64.37  ? 78  LEU B CA  1 
ATOM   1763 C  C   . LEU B  2  78  ? 24.182 20.367  -36.913 1.00 64.54  ? 78  LEU B C   1 
ATOM   1764 O  O   . LEU B  2  78  ? 24.144 19.440  -37.717 1.00 64.47  ? 78  LEU B O   1 
ATOM   1765 C  CB  . LEU B  2  78  ? 26.476 21.347  -37.006 1.00 65.26  ? 78  LEU B CB  1 
ATOM   1766 C  CG  . LEU B  2  78  ? 27.483 22.172  -37.808 1.00 66.11  ? 78  LEU B CG  1 
ATOM   1767 C  CD1 . LEU B  2  78  ? 28.897 21.803  -37.392 1.00 67.75  ? 78  LEU B CD1 1 
ATOM   1768 C  CD2 . LEU B  2  78  ? 27.297 21.894  -39.278 1.00 66.07  ? 78  LEU B CD2 1 
ATOM   1769 N  N   . ASP B  2  79  ? 23.548 20.326  -35.745 1.00 65.05  ? 79  ASP B N   1 
ATOM   1770 C  CA  . ASP B  2  79  ? 22.754 19.161  -35.357 1.00 65.86  ? 79  ASP B CA  1 
ATOM   1771 C  C   . ASP B  2  79  ? 21.259 19.449  -35.447 1.00 65.65  ? 79  ASP B C   1 
ATOM   1772 O  O   . ASP B  2  79  ? 20.455 18.811  -34.777 1.00 64.58  ? 79  ASP B O   1 
ATOM   1773 C  CB  . ASP B  2  79  ? 23.095 18.723  -33.930 1.00 65.86  ? 79  ASP B CB  1 
ATOM   1774 C  CG  . ASP B  2  79  ? 22.745 19.771  -32.901 1.00 66.61  ? 79  ASP B CG  1 
ATOM   1775 O  OD1 . ASP B  2  79  ? 22.491 19.387  -31.744 1.00 69.22  ? 79  ASP B OD1 1 
ATOM   1776 O  OD2 . ASP B  2  79  ? 22.729 20.974  -33.235 1.00 65.76  ? 79  ASP B OD2 1 
ATOM   1777 N  N   . ASP B  2  80  ? 20.894 20.413  -36.274 1.00 66.30  ? 80  ASP B N   1 
ATOM   1778 C  CA  . ASP B  2  80  ? 19.493 20.776  -36.444 1.00 68.17  ? 80  ASP B CA  1 
ATOM   1779 C  C   . ASP B  2  80  ? 19.297 21.224  -37.896 1.00 68.21  ? 80  ASP B C   1 
ATOM   1780 O  O   . ASP B  2  80  ? 18.915 22.364  -38.162 1.00 67.21  ? 80  ASP B O   1 
ATOM   1781 C  CB  . ASP B  2  80  ? 19.137 21.922  -35.497 1.00 70.52  ? 80  ASP B CB  1 
ATOM   1782 C  CG  . ASP B  2  80  ? 17.641 22.087  -35.310 1.00 72.75  ? 80  ASP B CG  1 
ATOM   1783 O  OD1 . ASP B  2  80  ? 16.878 21.850  -36.278 1.00 74.31  ? 80  ASP B OD1 1 
ATOM   1784 O  OD2 . ASP B  2  80  ? 17.238 22.472  -34.192 1.00 74.23  ? 80  ASP B OD2 1 
ATOM   1785 N  N   . GLU B  2  81  ? 19.577 20.302  -38.820 1.00 68.11  ? 81  GLU B N   1 
ATOM   1786 C  CA  . GLU B  2  81  ? 19.465 20.520  -40.264 1.00 67.95  ? 81  GLU B CA  1 
ATOM   1787 C  C   . GLU B  2  81  ? 18.384 21.521  -40.684 1.00 65.55  ? 81  GLU B C   1 
ATOM   1788 O  O   . GLU B  2  81  ? 18.653 22.479  -41.396 1.00 63.69  ? 81  GLU B O   1 
ATOM   1789 C  CB  . GLU B  2  81  ? 19.208 19.184  -40.940 1.00 70.93  ? 81  GLU B CB  1 
ATOM   1790 C  CG  . GLU B  2  81  ? 19.606 19.111  -42.392 1.00 75.31  ? 81  GLU B CG  1 
ATOM   1791 C  CD  . GLU B  2  81  ? 20.305 17.800  -42.693 1.00 79.07  ? 81  GLU B CD  1 
ATOM   1792 O  OE1 . GLU B  2  81  ? 20.475 17.472  -43.890 1.00 80.61  ? 81  GLU B OE1 1 
ATOM   1793 O  OE2 . GLU B  2  81  ? 20.690 17.104  -41.720 1.00 79.74  ? 81  GLU B OE2 1 
ATOM   1794 N  N   . SER B  2  82  ? 17.153 21.274  -40.255 1.00 63.88  ? 82  SER B N   1 
ATOM   1795 C  CA  . SER B  2  82  ? 16.044 22.158  -40.571 1.00 63.19  ? 82  SER B CA  1 
ATOM   1796 C  C   . SER B  2  82  ? 16.432 23.638  -40.416 1.00 62.05  ? 82  SER B C   1 
ATOM   1797 O  O   . SER B  2  82  ? 16.447 24.389  -41.391 1.00 62.45  ? 82  SER B O   1 
ATOM   1798 C  CB  . SER B  2  82  ? 14.852 21.832  -39.660 1.00 64.10  ? 82  SER B CB  1 
ATOM   1799 O  OG  . SER B  2  82  ? 13.765 22.701  -39.916 1.00 65.59  ? 82  SER B OG  1 
ATOM   1800 N  N   . VAL B  2  83  ? 16.770 24.048  -39.196 1.00 61.18  ? 83  VAL B N   1 
ATOM   1801 C  CA  . VAL B  2  83  ? 17.140 25.435  -38.921 1.00 58.47  ? 83  VAL B CA  1 
ATOM   1802 C  C   . VAL B  2  83  ? 18.497 25.783  -39.526 1.00 57.42  ? 83  VAL B C   1 
ATOM   1803 O  O   . VAL B  2  83  ? 18.718 26.916  -39.948 1.00 56.91  ? 83  VAL B O   1 
ATOM   1804 C  CB  . VAL B  2  83  ? 17.176 25.705  -37.402 1.00 56.76  ? 83  VAL B CB  1 
ATOM   1805 C  CG1 . VAL B  2  83  ? 17.214 27.209  -37.149 1.00 56.16  ? 83  VAL B CG1 1 
ATOM   1806 C  CG2 . VAL B  2  83  ? 15.956 25.045  -36.716 1.00 54.32  ? 83  VAL B CG2 1 
ATOM   1807 N  N   . LEU B  2  84  ? 19.399 24.806  -39.571 1.00 57.46  ? 84  LEU B N   1 
ATOM   1808 C  CA  . LEU B  2  84  ? 20.722 25.018  -40.143 1.00 58.89  ? 84  LEU B CA  1 
ATOM   1809 C  C   . LEU B  2  84  ? 20.592 25.533  -41.565 1.00 61.00  ? 84  LEU B C   1 
ATOM   1810 O  O   . LEU B  2  84  ? 21.083 26.613  -41.903 1.00 60.09  ? 84  LEU B O   1 
ATOM   1811 C  CB  . LEU B  2  84  ? 21.532 23.714  -40.163 1.00 57.52  ? 84  LEU B CB  1 
ATOM   1812 C  CG  . LEU B  2  84  ? 22.842 23.754  -40.984 1.00 56.32  ? 84  LEU B CG  1 
ATOM   1813 C  CD1 . LEU B  2  84  ? 23.794 24.786  -40.406 1.00 55.29  ? 84  LEU B CD1 1 
ATOM   1814 C  CD2 . LEU B  2  84  ? 23.506 22.388  -40.979 1.00 53.78  ? 84  LEU B CD2 1 
ATOM   1815 N  N   . ASN B  2  85  ? 19.924 24.743  -42.403 1.00 64.35  ? 85  ASN B N   1 
ATOM   1816 C  CA  . ASN B  2  85  ? 19.731 25.119  -43.800 1.00 65.92  ? 85  ASN B CA  1 
ATOM   1817 C  C   . ASN B  2  85  ? 19.031 26.467  -43.917 1.00 67.04  ? 85  ASN B C   1 
ATOM   1818 O  O   . ASN B  2  85  ? 19.342 27.248  -44.812 1.00 67.52  ? 85  ASN B O   1 
ATOM   1819 C  CB  . ASN B  2  85  ? 18.954 24.033  -44.545 1.00 63.60  ? 85  ASN B CB  1 
ATOM   1820 C  CG  . ASN B  2  85  ? 19.756 22.773  -44.697 1.00 63.32  ? 85  ASN B CG  1 
ATOM   1821 O  OD1 . ASN B  2  85  ? 20.943 22.824  -45.003 1.00 62.07  ? 85  ASN B OD1 1 
ATOM   1822 N  ND2 . ASN B  2  85  ? 19.115 21.626  -44.491 1.00 63.99  ? 85  ASN B ND2 1 
ATOM   1823 N  N   . THR B  2  86  ? 18.104 26.750  -43.007 1.00 67.97  ? 86  THR B N   1 
ATOM   1824 C  CA  . THR B  2  86  ? 17.404 28.024  -43.040 1.00 70.15  ? 86  THR B CA  1 
ATOM   1825 C  C   . THR B  2  86  ? 18.414 29.140  -42.857 1.00 73.15  ? 86  THR B C   1 
ATOM   1826 O  O   . THR B  2  86  ? 18.316 30.179  -43.502 1.00 73.67  ? 86  THR B O   1 
ATOM   1827 C  CB  . THR B  2  86  ? 16.396 28.157  -41.904 1.00 69.24  ? 86  THR B CB  1 
ATOM   1828 O  OG1 . THR B  2  86  ? 15.508 27.033  -41.914 1.00 69.44  ? 86  THR B OG1 1 
ATOM   1829 C  CG2 . THR B  2  86  ? 15.605 29.442  -42.055 1.00 67.31  ? 86  THR B CG2 1 
ATOM   1830 N  N   . GLN B  2  87  ? 19.377 28.924  -41.961 1.00 76.09  ? 87  GLN B N   1 
ATOM   1831 C  CA  . GLN B  2  87  ? 20.405 29.920  -41.674 1.00 78.12  ? 87  GLN B CA  1 
ATOM   1832 C  C   . GLN B  2  87  ? 21.388 30.052  -42.832 1.00 78.11  ? 87  GLN B C   1 
ATOM   1833 O  O   . GLN B  2  87  ? 21.788 31.164  -43.181 1.00 77.99  ? 87  GLN B O   1 
ATOM   1834 C  CB  . GLN B  2  87  ? 21.137 29.549  -40.383 1.00 80.03  ? 87  GLN B CB  1 
ATOM   1835 C  CG  . GLN B  2  87  ? 22.253 30.496  -39.990 1.00 83.94  ? 87  GLN B CG  1 
ATOM   1836 C  CD  . GLN B  2  87  ? 21.831 31.951  -40.035 1.00 86.80  ? 87  GLN B CD  1 
ATOM   1837 O  OE1 . GLN B  2  87  ? 20.674 32.284  -39.762 1.00 87.77  ? 87  GLN B OE1 1 
ATOM   1838 N  NE2 . GLN B  2  87  ? 22.772 32.833  -40.369 1.00 89.23  ? 87  GLN B NE2 1 
ATOM   1839 N  N   . LEU B  2  88  ? 21.777 28.925  -43.425 1.00 77.92  ? 88  LEU B N   1 
ATOM   1840 C  CA  . LEU B  2  88  ? 22.689 28.948  -44.563 1.00 78.17  ? 88  LEU B CA  1 
ATOM   1841 C  C   . LEU B  2  88  ? 22.063 29.760  -45.703 1.00 77.88  ? 88  LEU B C   1 
ATOM   1842 O  O   . LEU B  2  88  ? 22.760 30.490  -46.412 1.00 78.18  ? 88  LEU B O   1 
ATOM   1843 C  CB  . LEU B  2  88  ? 22.991 27.523  -45.031 1.00 78.47  ? 88  LEU B CB  1 
ATOM   1844 C  CG  . LEU B  2  88  ? 23.798 26.688  -44.027 1.00 78.30  ? 88  LEU B CG  1 
ATOM   1845 C  CD1 . LEU B  2  88  ? 23.856 25.228  -44.455 1.00 78.34  ? 88  LEU B CD1 1 
ATOM   1846 C  CD2 . LEU B  2  88  ? 25.196 27.260  -43.921 1.00 77.14  ? 88  LEU B CD2 1 
ATOM   1847 N  N   . ALA B  2  89  ? 20.746 29.643  -45.867 1.00 77.14  ? 89  ALA B N   1 
ATOM   1848 C  CA  . ALA B  2  89  ? 20.040 30.386  -46.908 1.00 76.35  ? 89  ALA B CA  1 
ATOM   1849 C  C   . ALA B  2  89  ? 20.143 31.882  -46.645 1.00 75.96  ? 89  ALA B C   1 
ATOM   1850 O  O   . ALA B  2  89  ? 20.253 32.683  -47.579 1.00 76.13  ? 89  ALA B O   1 
ATOM   1851 C  CB  . ALA B  2  89  ? 18.570 29.967  -46.958 1.00 77.05  ? 89  ALA B CB  1 
ATOM   1852 N  N   . HIS B  2  90  ? 20.107 32.262  -45.369 1.00 75.56  ? 90  HIS B N   1 
ATOM   1853 C  CA  . HIS B  2  90  ? 20.201 33.676  -45.005 1.00 75.55  ? 90  HIS B CA  1 
ATOM   1854 C  C   . HIS B  2  90  ? 21.584 34.202  -45.371 1.00 75.95  ? 90  HIS B C   1 
ATOM   1855 O  O   . HIS B  2  90  ? 21.719 35.297  -45.928 1.00 75.45  ? 90  HIS B O   1 
ATOM   1856 C  CB  . HIS B  2  90  ? 19.983 33.876  -43.510 1.00 73.61  ? 90  HIS B CB  1 
ATOM   1857 C  CG  . HIS B  2  90  ? 19.836 35.311  -43.114 1.00 71.86  ? 90  HIS B CG  1 
ATOM   1858 N  ND1 . HIS B  2  90  ? 18.661 36.011  -43.281 1.00 72.12  ? 90  HIS B ND1 1 
ATOM   1859 C  CD2 . HIS B  2  90  ? 20.714 36.180  -42.561 1.00 72.14  ? 90  HIS B CD2 1 
ATOM   1860 C  CE1 . HIS B  2  90  ? 18.820 37.246  -42.840 1.00 72.40  ? 90  HIS B CE1 1 
ATOM   1861 N  NE2 . HIS B  2  90  ? 20.058 37.375  -42.400 1.00 71.57  ? 90  HIS B NE2 1 
ATOM   1862 N  N   . LEU B  2  91  ? 22.607 33.415  -45.042 1.00 76.00  ? 91  LEU B N   1 
ATOM   1863 C  CA  . LEU B  2  91  ? 23.983 33.792  -45.341 1.00 76.33  ? 91  LEU B CA  1 
ATOM   1864 C  C   . LEU B  2  91  ? 24.144 33.874  -46.848 1.00 76.43  ? 91  LEU B C   1 
ATOM   1865 O  O   . LEU B  2  91  ? 24.803 34.775  -47.369 1.00 75.49  ? 91  LEU B O   1 
ATOM   1866 C  CB  . LEU B  2  91  ? 24.959 32.759  -44.762 1.00 76.53  ? 91  LEU B CB  1 
ATOM   1867 C  CG  . LEU B  2  91  ? 25.212 32.850  -43.249 1.00 76.80  ? 91  LEU B CG  1 
ATOM   1868 C  CD1 . LEU B  2  91  ? 26.015 31.641  -42.784 1.00 75.27  ? 91  LEU B CD1 1 
ATOM   1869 C  CD2 . LEU B  2  91  ? 25.932 34.151  -42.930 1.00 74.40  ? 91  LEU B CD2 1 
ATOM   1870 N  N   . ALA B  2  92  ? 23.520 32.923  -47.534 1.00 77.38  ? 92  ALA B N   1 
ATOM   1871 C  CA  . ALA B  2  92  ? 23.555 32.861  -48.986 1.00 77.05  ? 92  ALA B CA  1 
ATOM   1872 C  C   . ALA B  2  92  ? 23.080 34.187  -49.567 1.00 76.75  ? 92  ALA B C   1 
ATOM   1873 O  O   . ALA B  2  92  ? 23.753 34.781  -50.406 1.00 76.52  ? 92  ALA B O   1 
ATOM   1874 C  CB  . ALA B  2  92  ? 22.670 31.731  -49.481 1.00 75.53  ? 92  ALA B CB  1 
ATOM   1875 N  N   . SER B  2  93  ? 21.930 34.665  -49.098 1.00 76.69  ? 93  SER B N   1 
ATOM   1876 C  CA  . SER B  2  93  ? 21.389 35.913  -49.612 1.00 78.03  ? 93  SER B CA  1 
ATOM   1877 C  C   . SER B  2  93  ? 22.252 37.125  -49.265 1.00 78.90  ? 93  SER B C   1 
ATOM   1878 O  O   . SER B  2  93  ? 22.241 38.125  -49.982 1.00 78.68  ? 93  SER B O   1 
ATOM   1879 C  CB  . SER B  2  93  ? 19.959 36.134  -49.099 1.00 78.22  ? 93  SER B CB  1 
ATOM   1880 O  OG  . SER B  2  93  ? 19.947 36.746  -47.822 1.00 79.66  ? 93  SER B OG  1 
ATOM   1881 N  N   . GLN B  2  94  ? 23.002 37.045  -48.171 1.00 80.07  ? 94  GLN B N   1 
ATOM   1882 C  CA  . GLN B  2  94  ? 23.842 38.167  -47.778 1.00 80.62  ? 94  GLN B CA  1 
ATOM   1883 C  C   . GLN B  2  94  ? 25.091 38.243  -48.648 1.00 81.22  ? 94  GLN B C   1 
ATOM   1884 O  O   . GLN B  2  94  ? 25.761 39.269  -48.672 1.00 79.81  ? 94  GLN B O   1 
ATOM   1885 C  CB  . GLN B  2  94  ? 24.229 38.054  -46.294 1.00 80.47  ? 94  GLN B CB  1 
ATOM   1886 C  CG  . GLN B  2  94  ? 23.037 38.131  -45.323 1.00 78.44  ? 94  GLN B CG  1 
ATOM   1887 C  CD  . GLN B  2  94  ? 23.442 37.987  -43.852 1.00 77.37  ? 94  GLN B CD  1 
ATOM   1888 O  OE1 . GLN B  2  94  ? 24.059 36.992  -43.454 1.00 74.69  ? 94  GLN B OE1 1 
ATOM   1889 N  NE2 . GLN B  2  94  ? 23.089 38.983  -43.041 1.00 75.58  ? 94  GLN B NE2 1 
ATOM   1890 N  N   . HIS B  2  95  ? 25.378 37.160  -49.371 1.00 82.93  ? 95  HIS B N   1 
ATOM   1891 C  CA  . HIS B  2  95  ? 26.545 37.081  -50.252 1.00 85.47  ? 95  HIS B CA  1 
ATOM   1892 C  C   . HIS B  2  95  ? 26.198 36.982  -51.738 1.00 87.75  ? 95  HIS B C   1 
ATOM   1893 O  O   . HIS B  2  95  ? 27.085 37.041  -52.590 1.00 88.00  ? 95  HIS B O   1 
ATOM   1894 C  CB  . HIS B  2  95  ? 27.403 35.865  -49.903 1.00 84.68  ? 95  HIS B CB  1 
ATOM   1895 C  CG  . HIS B  2  95  ? 28.071 35.952  -48.567 1.00 84.89  ? 95  HIS B CG  1 
ATOM   1896 N  ND1 . HIS B  2  95  ? 27.368 35.948  -47.382 1.00 84.18  ? 95  HIS B ND1 1 
ATOM   1897 C  CD2 . HIS B  2  95  ? 29.382 36.043  -48.226 1.00 83.84  ? 95  HIS B CD2 1 
ATOM   1898 C  CE1 . HIS B  2  95  ? 28.213 36.031  -46.372 1.00 83.63  ? 95  HIS B CE1 1 
ATOM   1899 N  NE2 . HIS B  2  95  ? 29.441 36.090  -46.853 1.00 79.47  ? 95  HIS B NE2 1 
ATOM   1900 N  N   . SER B  2  96  ? 24.914 36.817  -52.044 1.00 90.58  ? 96  SER B N   1 
ATOM   1901 C  CA  . SER B  2  96  ? 24.457 36.676  -53.423 1.00 93.04  ? 96  SER B CA  1 
ATOM   1902 C  C   . SER B  2  96  ? 24.956 37.740  -54.410 1.00 94.68  ? 96  SER B C   1 
ATOM   1903 O  O   . SER B  2  96  ? 25.484 37.409  -55.476 1.00 95.13  ? 96  SER B O   1 
ATOM   1904 C  CB  . SER B  2  96  ? 22.923 36.626  -53.461 1.00 93.54  ? 96  SER B CB  1 
ATOM   1905 O  OG  . SER B  2  96  ? 22.351 37.832  -52.976 1.00 93.67  ? 96  SER B OG  1 
ATOM   1906 N  N   . SER B  2  97  ? 24.798 39.013  -54.057 1.00 95.74  ? 97  SER B N   1 
ATOM   1907 C  CA  . SER B  2  97  ? 25.218 40.092  -54.943 1.00 97.01  ? 97  SER B CA  1 
ATOM   1908 C  C   . SER B  2  97  ? 26.683 40.496  -54.780 1.00 96.41  ? 97  SER B C   1 
ATOM   1909 O  O   . SER B  2  97  ? 27.032 41.664  -54.969 1.00 97.08  ? 97  SER B O   1 
ATOM   1910 C  CB  . SER B  2  97  ? 24.322 41.317  -54.727 1.00 98.64  ? 97  SER B CB  1 
ATOM   1911 O  OG  . SER B  2  97  ? 24.445 41.808  -53.403 1.00 100.88 ? 97  SER B OG  1 
ATOM   1912 N  N   . ARG B  2  98  ? 27.547 39.536  -54.469 1.00 94.77  ? 98  ARG B N   1 
ATOM   1913 C  CA  . ARG B  2  98  ? 28.954 39.859  -54.267 1.00 93.32  ? 98  ARG B CA  1 
ATOM   1914 C  C   . ARG B  2  98  ? 29.929 39.006  -55.073 1.00 92.56  ? 98  ARG B C   1 
ATOM   1915 O  O   . ARG B  2  98  ? 31.133 39.254  -55.078 1.00 92.21  ? 98  ARG B O   1 
ATOM   1916 C  CB  . ARG B  2  98  ? 29.274 39.781  -52.772 1.00 92.59  ? 98  ARG B CB  1 
ATOM   1917 C  CG  . ARG B  2  98  ? 28.380 40.699  -51.928 1.00 89.85  ? 98  ARG B CG  1 
ATOM   1918 C  CD  . ARG B  2  98  ? 28.631 40.518  -50.451 1.00 87.31  ? 98  ARG B CD  1 
ATOM   1919 N  NE  . ARG B  2  98  ? 27.707 41.295  -49.631 1.00 85.62  ? 98  ARG B NE  1 
ATOM   1920 C  CZ  . ARG B  2  98  ? 27.708 42.619  -49.544 1.00 83.95  ? 98  ARG B CZ  1 
ATOM   1921 N  NH1 . ARG B  2  98  ? 26.824 43.225  -48.766 1.00 82.09  ? 98  ARG B NH1 1 
ATOM   1922 N  NH2 . ARG B  2  98  ? 28.589 43.336  -50.230 1.00 83.66  ? 98  ARG B NH2 1 
ATOM   1923 N  N   . GLY B  2  99  ? 29.405 37.999  -55.758 1.00 91.38  ? 99  GLY B N   1 
ATOM   1924 C  CA  . GLY B  2  99  ? 30.253 37.154  -56.574 1.00 90.47  ? 99  GLY B CA  1 
ATOM   1925 C  C   . GLY B  2  99  ? 31.451 36.526  -55.890 1.00 89.89  ? 99  GLY B C   1 
ATOM   1926 O  O   . GLY B  2  99  ? 32.596 36.797  -56.241 1.00 88.94  ? 99  GLY B O   1 
ATOM   1927 N  N   . VAL B  2  100 ? 31.187 35.673  -54.912 1.00 90.57  ? 100 VAL B N   1 
ATOM   1928 C  CA  . VAL B  2  100 ? 32.248 34.982  -54.196 1.00 90.54  ? 100 VAL B CA  1 
ATOM   1929 C  C   . VAL B  2  100 ? 32.475 33.671  -54.931 1.00 90.27  ? 100 VAL B C   1 
ATOM   1930 O  O   . VAL B  2  100 ? 31.525 32.950  -55.226 1.00 89.91  ? 100 VAL B O   1 
ATOM   1931 C  CB  . VAL B  2  100 ? 31.838 34.689  -52.733 1.00 90.27  ? 100 VAL B CB  1 
ATOM   1932 C  CG1 . VAL B  2  100 ? 32.956 33.949  -52.016 1.00 89.84  ? 100 VAL B CG1 1 
ATOM   1933 C  CG2 . VAL B  2  100 ? 31.506 35.990  -52.015 1.00 89.43  ? 100 VAL B CG2 1 
ATOM   1934 N  N   . SER B  2  101 ? 33.731 33.368  -55.234 1.00 90.56  ? 101 SER B N   1 
ATOM   1935 C  CA  . SER B  2  101 ? 34.048 32.139  -55.944 1.00 91.60  ? 101 SER B CA  1 
ATOM   1936 C  C   . SER B  2  101 ? 34.238 30.963  -54.993 1.00 93.38  ? 101 SER B C   1 
ATOM   1937 O  O   . SER B  2  101 ? 34.711 31.129  -53.872 1.00 94.32  ? 101 SER B O   1 
ATOM   1938 C  CB  . SER B  2  101 ? 35.316 32.320  -56.781 1.00 90.60  ? 101 SER B CB  1 
ATOM   1939 O  OG  . SER B  2  101 ? 36.456 32.431  -55.956 1.00 87.00  ? 101 SER B OG  1 
ATOM   1940 N  N   . ALA B  2  102 ? 33.867 29.771  -55.450 1.00 94.55  ? 102 ALA B N   1 
ATOM   1941 C  CA  . ALA B  2  102 ? 34.008 28.576  -54.632 1.00 95.61  ? 102 ALA B CA  1 
ATOM   1942 C  C   . ALA B  2  102 ? 35.450 28.396  -54.157 1.00 96.56  ? 102 ALA B C   1 
ATOM   1943 O  O   . ALA B  2  102 ? 35.714 27.635  -53.232 1.00 96.84  ? 102 ALA B O   1 
ATOM   1944 C  CB  . ALA B  2  102 ? 33.571 27.355  -55.422 1.00 95.82  ? 102 ALA B CB  1 
ATOM   1945 N  N   . GLU B  2  103 ? 36.379 29.099  -54.807 1.00 97.32  ? 103 GLU B N   1 
ATOM   1946 C  CA  . GLU B  2  103 ? 37.805 29.014  -54.448 1.00 97.65  ? 103 GLU B CA  1 
ATOM   1947 C  C   . GLU B  2  103 ? 38.131 29.954  -53.285 1.00 96.61  ? 103 GLU B C   1 
ATOM   1948 O  O   . GLU B  2  103 ? 39.078 29.715  -52.542 1.00 96.16  ? 103 GLU B O   1 
ATOM   1949 C  CB  . GLU B  2  103 ? 38.688 29.331  -55.645 1.00 99.83  ? 103 GLU B CB  1 
ATOM   1950 C  CG  . GLU B  2  103 ? 37.942 29.698  -56.932 1.00 103.68 ? 103 GLU B CG  1 
ATOM   1951 C  CD  . GLU B  2  103 ? 37.124 28.546  -57.495 1.00 105.03 ? 103 GLU B CD  1 
ATOM   1952 O  OE1 . GLU B  2  103 ? 35.901 28.721  -57.666 1.00 106.70 ? 103 GLU B OE1 1 
ATOM   1953 O  OE2 . GLU B  2  103 ? 37.701 27.469  -57.773 1.00 104.74 ? 103 GLU B OE2 1 
ATOM   1954 N  N   . GLN B  2  104 ? 37.363 31.037  -53.150 1.00 94.79  ? 104 GLN B N   1 
ATOM   1955 C  CA  . GLN B  2  104 ? 37.587 31.985  -52.063 1.00 92.16  ? 104 GLN B CA  1 
ATOM   1956 C  C   . GLN B  2  104 ? 36.952 31.347  -50.823 1.00 91.36  ? 104 GLN B C   1 
ATOM   1957 O  O   . GLN B  2  104 ? 37.468 31.477  -49.712 1.00 91.27  ? 104 GLN B O   1 
ATOM   1958 C  CB  . GLN B  2  104 ? 36.939 33.339  -52.376 1.00 91.39  ? 104 GLN B CB  1 
ATOM   1959 C  CG  . GLN B  2  104 ? 37.569 34.085  -53.547 1.00 89.51  ? 104 GLN B CG  1 
ATOM   1960 C  CD  . GLN B  2  104 ? 36.908 35.428  -53.812 1.00 89.46  ? 104 GLN B CD  1 
ATOM   1961 O  OE1 . GLN B  2  104 ? 35.687 35.515  -53.970 1.00 88.23  ? 104 GLN B OE1 1 
ATOM   1962 N  NE2 . GLN B  2  104 ? 37.717 36.485  -53.868 1.00 89.23  ? 104 GLN B NE2 1 
ATOM   1963 N  N   . TYR B  2  105 ? 35.838 30.641  -51.022 1.00 89.11  ? 105 TYR B N   1 
ATOM   1964 C  CA  . TYR B  2  105 ? 35.181 29.964  -49.910 1.00 86.80  ? 105 TYR B CA  1 
ATOM   1965 C  C   . TYR B  2  105 ? 36.132 28.921  -49.316 1.00 85.74  ? 105 TYR B C   1 
ATOM   1966 O  O   . TYR B  2  105 ? 36.209 28.772  -48.104 1.00 86.46  ? 105 TYR B O   1 
ATOM   1967 C  CB  . TYR B  2  105 ? 33.876 29.281  -50.355 1.00 85.03  ? 105 TYR B CB  1 
ATOM   1968 C  CG  . TYR B  2  105 ? 32.662 30.184  -50.340 1.00 83.47  ? 105 TYR B CG  1 
ATOM   1969 C  CD1 . TYR B  2  105 ? 32.147 30.663  -49.137 1.00 82.04  ? 105 TYR B CD1 1 
ATOM   1970 C  CD2 . TYR B  2  105 ? 32.046 30.585  -51.530 1.00 83.41  ? 105 TYR B CD2 1 
ATOM   1971 C  CE1 . TYR B  2  105 ? 31.052 31.516  -49.114 1.00 81.67  ? 105 TYR B CE1 1 
ATOM   1972 C  CE2 . TYR B  2  105 ? 30.946 31.443  -51.521 1.00 81.81  ? 105 TYR B CE2 1 
ATOM   1973 C  CZ  . TYR B  2  105 ? 30.453 31.908  -50.309 1.00 81.79  ? 105 TYR B CZ  1 
ATOM   1974 O  OH  . TYR B  2  105 ? 29.376 32.768  -50.287 1.00 79.63  ? 105 TYR B OH  1 
ATOM   1975 N  N   . ASN B  2  106 ? 36.860 28.205  -50.170 1.00 84.60  ? 106 ASN B N   1 
ATOM   1976 C  CA  . ASN B  2  106 ? 37.797 27.194  -49.686 1.00 83.49  ? 106 ASN B CA  1 
ATOM   1977 C  C   . ASN B  2  106 ? 38.963 27.828  -48.954 1.00 82.31  ? 106 ASN B C   1 
ATOM   1978 O  O   . ASN B  2  106 ? 39.539 27.222  -48.059 1.00 82.24  ? 106 ASN B O   1 
ATOM   1979 C  CB  . ASN B  2  106 ? 38.352 26.339  -50.827 1.00 83.76  ? 106 ASN B CB  1 
ATOM   1980 C  CG  . ASN B  2  106 ? 37.296 25.491  -51.488 1.00 84.39  ? 106 ASN B CG  1 
ATOM   1981 O  OD1 . ASN B  2  106 ? 36.391 24.978  -50.831 1.00 82.34  ? 106 ASN B OD1 1 
ATOM   1982 N  ND2 . ASN B  2  106 ? 37.414 25.325  -52.803 1.00 85.39  ? 106 ASN B ND2 1 
ATOM   1983 N  N   . VAL B  2  107 ? 39.325 29.044  -49.350 1.00 81.15  ? 107 VAL B N   1 
ATOM   1984 C  CA  . VAL B  2  107 ? 40.431 29.745  -48.715 1.00 80.12  ? 107 VAL B CA  1 
ATOM   1985 C  C   . VAL B  2  107 ? 40.042 30.013  -47.271 1.00 78.95  ? 107 VAL B C   1 
ATOM   1986 O  O   . VAL B  2  107 ? 40.724 29.593  -46.339 1.00 78.23  ? 107 VAL B O   1 
ATOM   1987 C  CB  . VAL B  2  107 ? 40.723 31.094  -49.416 1.00 80.92  ? 107 VAL B CB  1 
ATOM   1988 C  CG1 . VAL B  2  107 ? 41.692 31.918  -48.590 1.00 80.82  ? 107 VAL B CG1 1 
ATOM   1989 C  CG2 . VAL B  2  107 ? 41.305 30.849  -50.800 1.00 81.17  ? 107 VAL B CG2 1 
ATOM   1990 N  N   . VAL B  2  108 ? 38.931 30.719  -47.105 1.00 77.30  ? 108 VAL B N   1 
ATOM   1991 C  CA  . VAL B  2  108 ? 38.422 31.048  -45.793 1.00 76.00  ? 108 VAL B CA  1 
ATOM   1992 C  C   . VAL B  2  108 ? 38.310 29.776  -44.943 1.00 75.97  ? 108 VAL B C   1 
ATOM   1993 O  O   . VAL B  2  108 ? 38.536 29.805  -43.729 1.00 75.57  ? 108 VAL B O   1 
ATOM   1994 C  CB  . VAL B  2  108 ? 37.066 31.752  -45.931 1.00 75.10  ? 108 VAL B CB  1 
ATOM   1995 C  CG1 . VAL B  2  108 ? 36.389 31.876  -44.583 1.00 75.42  ? 108 VAL B CG1 1 
ATOM   1996 C  CG2 . VAL B  2  108 ? 37.285 33.123  -46.540 1.00 73.65  ? 108 VAL B CG2 1 
ATOM   1997 N  N   . GLU B  2  109 ? 37.989 28.662  -45.593 1.00 75.15  ? 109 GLU B N   1 
ATOM   1998 C  CA  . GLU B  2  109 ? 37.866 27.379  -44.911 1.00 74.11  ? 109 GLU B CA  1 
ATOM   1999 C  C   . GLU B  2  109 ? 39.165 26.997  -44.205 1.00 73.67  ? 109 GLU B C   1 
ATOM   2000 O  O   . GLU B  2  109 ? 39.176 26.641  -43.022 1.00 74.17  ? 109 GLU B O   1 
ATOM   2001 C  CB  . GLU B  2  109 ? 37.499 26.275  -45.911 1.00 75.46  ? 109 GLU B CB  1 
ATOM   2002 C  CG  . GLU B  2  109 ? 36.025 26.172  -46.289 1.00 76.46  ? 109 GLU B CG  1 
ATOM   2003 C  CD  . GLU B  2  109 ? 35.764 25.025  -47.271 1.00 77.76  ? 109 GLU B CD  1 
ATOM   2004 O  OE1 . GLU B  2  109 ? 36.423 23.967  -47.127 1.00 77.92  ? 109 GLU B OE1 1 
ATOM   2005 O  OE2 . GLU B  2  109 ? 34.902 25.174  -48.172 1.00 79.46  ? 109 GLU B OE2 1 
ATOM   2006 N  N   . HIS B  2  110 ? 40.265 27.067  -44.955 1.00 72.30  ? 110 HIS B N   1 
ATOM   2007 C  CA  . HIS B  2  110 ? 41.589 26.733  -44.422 1.00 70.20  ? 110 HIS B CA  1 
ATOM   2008 C  C   . HIS B  2  110 ? 42.017 27.779  -43.386 1.00 68.59  ? 110 HIS B C   1 
ATOM   2009 O  O   . HIS B  2  110 ? 42.671 27.454  -42.393 1.00 66.25  ? 110 HIS B O   1 
ATOM   2010 C  CB  . HIS B  2  110 ? 42.590 26.661  -45.557 1.00 71.24  ? 110 HIS B CB  1 
ATOM   2011 C  CG  . HIS B  2  110 ? 43.920 26.118  -45.138 1.00 72.66  ? 110 HIS B CG  1 
ATOM   2012 N  ND1 . HIS B  2  110 ? 44.105 24.798  -44.784 1.00 73.59  ? 110 HIS B ND1 1 
ATOM   2013 C  CD2 . HIS B  2  110 ? 45.132 26.715  -45.018 1.00 72.84  ? 110 HIS B CD2 1 
ATOM   2014 C  CE1 . HIS B  2  110 ? 45.374 24.604  -44.466 1.00 73.70  ? 110 HIS B CE1 1 
ATOM   2015 N  NE2 . HIS B  2  110 ? 46.020 25.751  -44.603 1.00 73.94  ? 110 HIS B NE2 1 
ATOM   2016 N  N   . ALA B  2  111 ? 41.644 29.031  -43.625 1.00 67.71  ? 111 ALA B N   1 
ATOM   2017 C  CA  . ALA B  2  111 ? 41.980 30.120  -42.713 1.00 66.59  ? 111 ALA B CA  1 
ATOM   2018 C  C   . ALA B  2  111 ? 41.322 29.842  -41.370 1.00 66.16  ? 111 ALA B C   1 
ATOM   2019 O  O   . ALA B  2  111 ? 41.953 29.963  -40.325 1.00 66.05  ? 111 ALA B O   1 
ATOM   2020 C  CB  . ALA B  2  111 ? 41.485 31.424  -43.270 1.00 65.70  ? 111 ALA B CB  1 
ATOM   2021 N  N   . VAL B  2  112 ? 40.048 29.458  -41.415 1.00 65.33  ? 112 VAL B N   1 
ATOM   2022 C  CA  . VAL B  2  112 ? 39.302 29.121  -40.215 1.00 64.22  ? 112 VAL B CA  1 
ATOM   2023 C  C   . VAL B  2  112 ? 39.918 27.900  -39.529 1.00 65.40  ? 112 VAL B C   1 
ATOM   2024 O  O   . VAL B  2  112 ? 40.057 27.885  -38.308 1.00 65.45  ? 112 VAL B O   1 
ATOM   2025 C  CB  . VAL B  2  112 ? 37.830 28.810  -40.537 1.00 64.07  ? 112 VAL B CB  1 
ATOM   2026 C  CG1 . VAL B  2  112 ? 37.172 28.128  -39.353 1.00 62.28  ? 112 VAL B CG1 1 
ATOM   2027 C  CG2 . VAL B  2  112 ? 37.093 30.095  -40.875 1.00 63.31  ? 112 VAL B CG2 1 
ATOM   2028 N  N   . MET B  2  113 ? 40.294 26.888  -40.311 1.00 65.86  ? 113 MET B N   1 
ATOM   2029 C  CA  . MET B  2  113 ? 40.885 25.678  -39.749 1.00 67.27  ? 113 MET B CA  1 
ATOM   2030 C  C   . MET B  2  113 ? 42.189 25.984  -39.037 1.00 67.28  ? 113 MET B C   1 
ATOM   2031 O  O   . MET B  2  113 ? 42.383 25.583  -37.895 1.00 66.72  ? 113 MET B O   1 
ATOM   2032 C  CB  . MET B  2  113 ? 41.127 24.622  -40.836 1.00 68.60  ? 113 MET B CB  1 
ATOM   2033 C  CG  . MET B  2  113 ? 39.844 24.067  -41.477 1.00 70.57  ? 113 MET B CG  1 
ATOM   2034 S  SD  . MET B  2  113 ? 40.079 22.533  -42.441 1.00 69.66  ? 113 MET B SD  1 
ATOM   2035 C  CE  . MET B  2  113 ? 40.216 23.206  -44.030 1.00 70.76  ? 113 MET B CE  1 
ATOM   2036 N  N   . MET B  2  114 ? 43.085 26.691  -39.721 1.00 68.64  ? 114 MET B N   1 
ATOM   2037 C  CA  . MET B  2  114 ? 44.374 27.066  -39.144 1.00 68.51  ? 114 MET B CA  1 
ATOM   2038 C  C   . MET B  2  114 ? 44.176 27.851  -37.850 1.00 67.44  ? 114 MET B C   1 
ATOM   2039 O  O   . MET B  2  114 ? 44.857 27.608  -36.852 1.00 67.05  ? 114 MET B O   1 
ATOM   2040 C  CB  . MET B  2  114 ? 45.180 27.891  -40.154 1.00 70.29  ? 114 MET B CB  1 
ATOM   2041 C  CG  . MET B  2  114 ? 45.719 27.056  -41.321 1.00 73.55  ? 114 MET B CG  1 
ATOM   2042 S  SD  . MET B  2  114 ? 46.719 25.614  -40.804 1.00 76.53  ? 114 MET B SD  1 
ATOM   2043 C  CE  . MET B  2  114 ? 45.456 24.272  -40.643 1.00 76.26  ? 114 MET B CE  1 
ATOM   2044 N  N   . GLY B  2  115 ? 43.231 28.788  -37.876 1.00 66.33  ? 115 GLY B N   1 
ATOM   2045 C  CA  . GLY B  2  115 ? 42.934 29.580  -36.696 1.00 65.53  ? 115 GLY B CA  1 
ATOM   2046 C  C   . GLY B  2  115 ? 42.479 28.735  -35.514 1.00 65.21  ? 115 GLY B C   1 
ATOM   2047 O  O   . GLY B  2  115 ? 42.910 28.954  -34.379 1.00 65.47  ? 115 GLY B O   1 
ATOM   2048 N  N   . VAL B  2  116 ? 41.594 27.776  -35.775 1.00 64.49  ? 116 VAL B N   1 
ATOM   2049 C  CA  . VAL B  2  116 ? 41.089 26.875  -34.746 1.00 63.66  ? 116 VAL B CA  1 
ATOM   2050 C  C   . VAL B  2  116 ? 42.221 25.992  -34.215 1.00 65.29  ? 116 VAL B C   1 
ATOM   2051 O  O   . VAL B  2  116 ? 42.357 25.784  -33.009 1.00 65.94  ? 116 VAL B O   1 
ATOM   2052 C  CB  . VAL B  2  116 ? 39.968 25.979  -35.309 1.00 62.08  ? 116 VAL B CB  1 
ATOM   2053 C  CG1 . VAL B  2  116 ? 39.671 24.847  -34.353 1.00 60.47  ? 116 VAL B CG1 1 
ATOM   2054 C  CG2 . VAL B  2  116 ? 38.721 26.815  -35.556 1.00 59.92  ? 116 VAL B CG2 1 
ATOM   2055 N  N   . GLU B  2  117 ? 43.032 25.465  -35.124 1.00 66.27  ? 117 GLU B N   1 
ATOM   2056 C  CA  . GLU B  2  117 ? 44.153 24.635  -34.725 1.00 67.76  ? 117 GLU B CA  1 
ATOM   2057 C  C   . GLU B  2  117 ? 45.128 25.483  -33.907 1.00 67.86  ? 117 GLU B C   1 
ATOM   2058 O  O   . GLU B  2  117 ? 45.673 25.021  -32.903 1.00 67.63  ? 117 GLU B O   1 
ATOM   2059 C  CB  . GLU B  2  117 ? 44.883 24.087  -35.946 1.00 67.88  ? 117 GLU B CB  1 
ATOM   2060 C  CG  . GLU B  2  117 ? 45.963 23.091  -35.581 1.00 70.78  ? 117 GLU B CG  1 
ATOM   2061 C  CD  . GLU B  2  117 ? 47.197 23.209  -36.458 1.00 72.86  ? 117 GLU B CD  1 
ATOM   2062 O  OE1 . GLU B  2  117 ? 47.065 23.145  -37.700 1.00 75.63  ? 117 GLU B OE1 1 
ATOM   2063 O  OE2 . GLU B  2  117 ? 48.305 23.360  -35.905 1.00 73.52  ? 117 GLU B OE2 1 
ATOM   2064 N  N   . HIS B  2  118 ? 45.346 26.724  -34.357 1.00 66.88  ? 118 HIS B N   1 
ATOM   2065 C  CA  . HIS B  2  118 ? 46.242 27.661  -33.688 1.00 65.11  ? 118 HIS B CA  1 
ATOM   2066 C  C   . HIS B  2  118 ? 45.751 27.943  -32.276 1.00 64.20  ? 118 HIS B C   1 
ATOM   2067 O  O   . HIS B  2  118 ? 46.546 28.174  -31.366 1.00 63.76  ? 118 HIS B O   1 
ATOM   2068 C  CB  . HIS B  2  118 ? 46.325 28.959  -34.495 1.00 66.97  ? 118 HIS B CB  1 
ATOM   2069 C  CG  . HIS B  2  118 ? 46.613 30.176  -33.669 1.00 70.39  ? 118 HIS B CG  1 
ATOM   2070 N  ND1 . HIS B  2  118 ? 47.812 30.376  -33.017 1.00 69.82  ? 118 HIS B ND1 1 
ATOM   2071 C  CD2 . HIS B  2  118 ? 45.844 31.254  -33.382 1.00 71.99  ? 118 HIS B CD2 1 
ATOM   2072 C  CE1 . HIS B  2  118 ? 47.769 31.524  -32.365 1.00 71.93  ? 118 HIS B CE1 1 
ATOM   2073 N  NE2 . HIS B  2  118 ? 46.587 32.076  -32.570 1.00 72.80  ? 118 HIS B NE2 1 
ATOM   2074 N  N   . GLU B  2  119 ? 44.434 27.900  -32.101 1.00 62.66  ? 119 GLU B N   1 
ATOM   2075 C  CA  . GLU B  2  119 ? 43.818 28.151  -30.807 1.00 60.75  ? 119 GLU B CA  1 
ATOM   2076 C  C   . GLU B  2  119 ? 43.804 26.917  -29.893 1.00 58.94  ? 119 GLU B C   1 
ATOM   2077 O  O   . GLU B  2  119 ? 44.145 27.015  -28.717 1.00 59.20  ? 119 GLU B O   1 
ATOM   2078 C  CB  . GLU B  2  119 ? 42.379 28.659  -30.997 1.00 61.38  ? 119 GLU B CB  1 
ATOM   2079 C  CG  . GLU B  2  119 ? 41.919 29.679  -29.943 1.00 62.86  ? 119 GLU B CG  1 
ATOM   2080 C  CD  . GLU B  2  119 ? 42.780 30.961  -30.020 1.00 63.28  ? 119 GLU B CD  1 
ATOM   2081 O  OE1 . GLU B  2  119 ? 42.847 31.644  -31.064 1.00 61.32  ? 119 GLU B OE1 1 
ATOM   2082 O  OE2 . GLU B  2  119 ? 43.425 31.335  -28.938 1.00 67.07  ? 119 GLU B OE2 1 
ATOM   2083 N  N   . ILE B  2  120 ? 43.425 25.753  -30.418 1.00 56.66  ? 120 ILE B N   1 
ATOM   2084 C  CA  . ILE B  2  120 ? 43.364 24.563  -29.571 1.00 55.04  ? 120 ILE B CA  1 
ATOM   2085 C  C   . ILE B  2  120 ? 44.539 23.604  -29.672 1.00 53.22  ? 120 ILE B C   1 
ATOM   2086 O  O   . ILE B  2  120 ? 44.629 22.658  -28.884 1.00 52.69  ? 120 ILE B O   1 
ATOM   2087 C  CB  . ILE B  2  120 ? 42.073 23.740  -29.817 1.00 55.28  ? 120 ILE B CB  1 
ATOM   2088 C  CG1 . ILE B  2  120 ? 42.073 23.180  -31.236 1.00 54.20  ? 120 ILE B CG1 1 
ATOM   2089 C  CG2 . ILE B  2  120 ? 40.843 24.606  -29.583 1.00 55.87  ? 120 ILE B CG2 1 
ATOM   2090 C  CD1 . ILE B  2  120 ? 40.877 22.336  -31.526 1.00 54.70  ? 120 ILE B CD1 1 
ATOM   2091 N  N   . GLY B  2  121 ? 45.423 23.832  -30.640 1.00 50.54  ? 121 GLY B N   1 
ATOM   2092 C  CA  . GLY B  2  121 ? 46.584 22.973  -30.783 1.00 48.54  ? 121 GLY B CA  1 
ATOM   2093 C  C   . GLY B  2  121 ? 46.425 21.803  -31.735 1.00 48.01  ? 121 GLY B C   1 
ATOM   2094 O  O   . GLY B  2  121 ? 45.372 21.162  -31.759 1.00 45.49  ? 121 GLY B O   1 
ATOM   2095 N  N   . GLN B  2  122 ? 47.488 21.535  -32.506 1.00 48.67  ? 122 GLN B N   1 
ATOM   2096 C  CA  . GLN B  2  122 ? 47.539 20.459  -33.488 1.00 50.39  ? 122 GLN B CA  1 
ATOM   2097 C  C   . GLN B  2  122 ? 47.382 19.107  -32.839 1.00 50.25  ? 122 GLN B C   1 
ATOM   2098 O  O   . GLN B  2  122 ? 47.017 18.124  -33.485 1.00 49.15  ? 122 GLN B O   1 
ATOM   2099 C  CB  . GLN B  2  122 ? 48.864 20.497  -34.247 1.00 53.31  ? 122 GLN B CB  1 
ATOM   2100 C  CG  . GLN B  2  122 ? 50.126 20.287  -33.401 1.00 55.33  ? 122 GLN B CG  1 
ATOM   2101 C  CD  . GLN B  2  122 ? 50.308 18.854  -32.917 1.00 57.89  ? 122 GLN B CD  1 
ATOM   2102 O  OE1 . GLN B  2  122 ? 50.100 17.892  -33.668 1.00 58.28  ? 122 GLN B OE1 1 
ATOM   2103 N  NE2 . GLN B  2  122 ? 50.718 18.706  -31.661 1.00 58.44  ? 122 GLN B NE2 1 
ATOM   2104 N  N   . ASN B  2  123 ? 47.674 19.065  -31.550 1.00 49.98  ? 123 ASN B N   1 
ATOM   2105 C  CA  . ASN B  2  123 ? 47.556 17.842  -30.788 1.00 51.52  ? 123 ASN B CA  1 
ATOM   2106 C  C   . ASN B  2  123 ? 46.115 17.322  -30.739 1.00 50.93  ? 123 ASN B C   1 
ATOM   2107 O  O   . ASN B  2  123 ? 45.900 16.120  -30.618 1.00 51.26  ? 123 ASN B O   1 
ATOM   2108 C  CB  . ASN B  2  123 ? 48.074 18.080  -29.371 1.00 55.93  ? 123 ASN B CB  1 
ATOM   2109 C  CG  . ASN B  2  123 ? 47.804 16.914  -28.450 1.00 58.10  ? 123 ASN B CG  1 
ATOM   2110 O  OD1 . ASN B  2  123 ? 48.238 15.787  -28.711 1.00 61.09  ? 123 ASN B OD1 1 
ATOM   2111 N  ND2 . ASN B  2  123 ? 47.078 17.170  -27.365 1.00 58.36  ? 123 ASN B ND2 1 
ATOM   2112 N  N   . VAL B  2  124 ? 45.128 18.207  -30.835 1.00 50.86  ? 124 VAL B N   1 
ATOM   2113 C  CA  . VAL B  2  124 ? 43.734 17.756  -30.788 1.00 51.98  ? 124 VAL B CA  1 
ATOM   2114 C  C   . VAL B  2  124 ? 42.902 18.122  -32.021 1.00 53.31  ? 124 VAL B C   1 
ATOM   2115 O  O   . VAL B  2  124 ? 41.753 17.669  -32.156 1.00 52.43  ? 124 VAL B O   1 
ATOM   2116 C  CB  . VAL B  2  124 ? 42.979 18.300  -29.531 1.00 50.31  ? 124 VAL B CB  1 
ATOM   2117 C  CG1 . VAL B  2  124 ? 43.586 17.734  -28.272 1.00 50.36  ? 124 VAL B CG1 1 
ATOM   2118 C  CG2 . VAL B  2  124 ? 43.026 19.807  -29.504 1.00 49.53  ? 124 VAL B CG2 1 
ATOM   2119 N  N   . PHE B  2  125 ? 43.462 18.932  -32.914 1.00 54.26  ? 125 PHE B N   1 
ATOM   2120 C  CA  . PHE B  2  125 ? 42.722 19.329  -34.106 1.00 56.25  ? 125 PHE B CA  1 
ATOM   2121 C  C   . PHE B  2  125 ? 42.286 18.145  -34.965 1.00 57.12  ? 125 PHE B C   1 
ATOM   2122 O  O   . PHE B  2  125 ? 43.105 17.292  -35.330 1.00 55.31  ? 125 PHE B O   1 
ATOM   2123 C  CB  . PHE B  2  125 ? 43.548 20.265  -34.971 1.00 57.38  ? 125 PHE B CB  1 
ATOM   2124 C  CG  . PHE B  2  125 ? 42.770 20.863  -36.102 1.00 58.40  ? 125 PHE B CG  1 
ATOM   2125 C  CD1 . PHE B  2  125 ? 41.728 21.748  -35.847 1.00 58.72  ? 125 PHE B CD1 1 
ATOM   2126 C  CD2 . PHE B  2  125 ? 43.069 20.544  -37.418 1.00 57.52  ? 125 PHE B CD2 1 
ATOM   2127 C  CE1 . PHE B  2  125 ? 41.000 22.308  -36.886 1.00 58.54  ? 125 PHE B CE1 1 
ATOM   2128 C  CE2 . PHE B  2  125 ? 42.343 21.099  -38.464 1.00 58.03  ? 125 PHE B CE2 1 
ATOM   2129 C  CZ  . PHE B  2  125 ? 41.307 21.983  -38.199 1.00 58.91  ? 125 PHE B CZ  1 
ATOM   2130 N  N   . ASP B  2  126 ? 40.994 18.104  -35.288 1.00 58.55  ? 126 ASP B N   1 
ATOM   2131 C  CA  . ASP B  2  126 ? 40.433 17.027  -36.100 1.00 60.36  ? 126 ASP B CA  1 
ATOM   2132 C  C   . ASP B  2  126 ? 40.141 17.549  -37.503 1.00 60.38  ? 126 ASP B C   1 
ATOM   2133 O  O   . ASP B  2  126 ? 39.029 17.982  -37.805 1.00 57.86  ? 126 ASP B O   1 
ATOM   2134 C  CB  . ASP B  2  126 ? 39.160 16.479  -35.437 1.00 60.71  ? 126 ASP B CB  1 
ATOM   2135 C  CG  . ASP B  2  126 ? 38.580 15.286  -36.179 1.00 61.47  ? 126 ASP B CG  1 
ATOM   2136 O  OD1 . ASP B  2  126 ? 37.710 14.590  -35.615 1.00 63.03  ? 126 ASP B OD1 1 
ATOM   2137 O  OD2 . ASP B  2  126 ? 38.986 15.044  -37.333 1.00 60.74  ? 126 ASP B OD2 1 
ATOM   2138 N  N   . LYS B  2  127 ? 41.167 17.504  -38.350 1.00 63.25  ? 127 LYS B N   1 
ATOM   2139 C  CA  . LYS B  2  127 ? 41.081 18.003  -39.720 1.00 66.04  ? 127 LYS B CA  1 
ATOM   2140 C  C   . LYS B  2  127 ? 39.958 17.413  -40.552 1.00 66.45  ? 127 LYS B C   1 
ATOM   2141 O  O   . LYS B  2  127 ? 39.252 18.152  -41.243 1.00 67.35  ? 127 LYS B O   1 
ATOM   2142 C  CB  . LYS B  2  127 ? 42.413 17.806  -40.459 1.00 66.40  ? 127 LYS B CB  1 
ATOM   2143 C  CG  . LYS B  2  127 ? 42.373 18.293  -41.913 1.00 67.94  ? 127 LYS B CG  1 
ATOM   2144 C  CD  . LYS B  2  127 ? 43.725 18.147  -42.608 1.00 69.47  ? 127 LYS B CD  1 
ATOM   2145 C  CE  . LYS B  2  127 ? 43.599 18.273  -44.128 1.00 71.33  ? 127 LYS B CE  1 
ATOM   2146 N  NZ  . LYS B  2  127 ? 42.859 17.128  -44.753 1.00 71.99  ? 127 LYS B NZ  1 
ATOM   2147 N  N   . ASP B  2  128 ? 39.801 16.093  -40.507 1.00 66.13  ? 128 ASP B N   1 
ATOM   2148 C  CA  . ASP B  2  128 ? 38.745 15.451  -41.274 1.00 66.02  ? 128 ASP B CA  1 
ATOM   2149 C  C   . ASP B  2  128 ? 37.379 16.014  -40.884 1.00 65.01  ? 128 ASP B C   1 
ATOM   2150 O  O   . ASP B  2  128 ? 36.625 16.472  -41.742 1.00 65.79  ? 128 ASP B O   1 
ATOM   2151 C  CB  . ASP B  2  128 ? 38.778 13.930  -41.077 1.00 67.48  ? 128 ASP B CB  1 
ATOM   2152 C  CG  . ASP B  2  128 ? 39.956 13.264  -41.806 1.00 69.76  ? 128 ASP B CG  1 
ATOM   2153 O  OD1 . ASP B  2  128 ? 40.409 13.813  -42.842 1.00 68.96  ? 128 ASP B OD1 1 
ATOM   2154 O  OD2 . ASP B  2  128 ? 40.414 12.183  -41.351 1.00 69.05  ? 128 ASP B OD2 1 
ATOM   2155 N  N   . ALA B  2  129 ? 37.064 16.010  -39.595 1.00 63.28  ? 129 ALA B N   1 
ATOM   2156 C  CA  . ALA B  2  129 ? 35.776 16.521  -39.157 1.00 62.42  ? 129 ALA B CA  1 
ATOM   2157 C  C   . ALA B  2  129 ? 35.563 17.974  -39.580 1.00 61.15  ? 129 ALA B C   1 
ATOM   2158 O  O   . ALA B  2  129 ? 34.491 18.319  -40.070 1.00 61.31  ? 129 ALA B O   1 
ATOM   2159 C  CB  . ALA B  2  129 ? 35.632 16.384  -37.631 1.00 62.46  ? 129 ALA B CB  1 
ATOM   2160 N  N   . TRP B  2  130 ? 36.580 18.817  -39.418 1.00 59.59  ? 130 TRP B N   1 
ATOM   2161 C  CA  . TRP B  2  130 ? 36.421 20.220  -39.775 1.00 59.38  ? 130 TRP B CA  1 
ATOM   2162 C  C   . TRP B  2  130 ? 36.181 20.459  -41.251 1.00 59.53  ? 130 TRP B C   1 
ATOM   2163 O  O   . TRP B  2  130 ? 35.277 21.208  -41.625 1.00 59.85  ? 130 TRP B O   1 
ATOM   2164 C  CB  . TRP B  2  130 ? 37.620 21.060  -39.305 1.00 57.63  ? 130 TRP B CB  1 
ATOM   2165 C  CG  . TRP B  2  130 ? 37.510 21.512  -37.868 1.00 56.14  ? 130 TRP B CG  1 
ATOM   2166 C  CD1 . TRP B  2  130 ? 38.039 20.892  -36.772 1.00 55.22  ? 130 TRP B CD1 1 
ATOM   2167 C  CD2 . TRP B  2  130 ? 36.749 22.617  -37.373 1.00 54.96  ? 130 TRP B CD2 1 
ATOM   2168 N  NE1 . TRP B  2  130 ? 37.649 21.539  -35.628 1.00 54.45  ? 130 TRP B NE1 1 
ATOM   2169 C  CE2 . TRP B  2  130 ? 36.854 22.600  -35.966 1.00 54.92  ? 130 TRP B CE2 1 
ATOM   2170 C  CE3 . TRP B  2  130 ? 35.982 23.621  -37.984 1.00 55.50  ? 130 TRP B CE3 1 
ATOM   2171 C  CZ2 . TRP B  2  130 ? 36.223 23.546  -35.157 1.00 56.89  ? 130 TRP B CZ2 1 
ATOM   2172 C  CZ3 . TRP B  2  130 ? 35.349 24.563  -37.178 1.00 56.14  ? 130 TRP B CZ3 1 
ATOM   2173 C  CH2 . TRP B  2  130 ? 35.475 24.518  -35.776 1.00 57.68  ? 130 TRP B CH2 1 
ATOM   2174 N  N   . GLN B  2  131 ? 36.989 19.827  -42.089 1.00 60.38  ? 131 GLN B N   1 
ATOM   2175 C  CA  . GLN B  2  131 ? 36.874 19.994  -43.534 1.00 60.22  ? 131 GLN B CA  1 
ATOM   2176 C  C   . GLN B  2  131 ? 35.475 19.588  -43.976 1.00 59.47  ? 131 GLN B C   1 
ATOM   2177 O  O   . GLN B  2  131 ? 34.776 20.349  -44.641 1.00 59.03  ? 131 GLN B O   1 
ATOM   2178 C  CB  . GLN B  2  131 ? 37.940 19.138  -44.233 1.00 60.85  ? 131 GLN B CB  1 
ATOM   2179 C  CG  . GLN B  2  131 ? 38.130 19.420  -45.715 1.00 60.17  ? 131 GLN B CG  1 
ATOM   2180 C  CD  . GLN B  2  131 ? 38.442 20.874  -46.001 1.00 60.38  ? 131 GLN B CD  1 
ATOM   2181 O  OE1 . GLN B  2  131 ? 37.536 21.719  -46.074 1.00 59.08  ? 131 GLN B OE1 1 
ATOM   2182 N  NE2 . GLN B  2  131 ? 39.731 21.184  -46.156 1.00 56.79  ? 131 GLN B NE2 1 
ATOM   2183 N  N   . ALA B  2  132 ? 35.069 18.390  -43.572 1.00 59.30  ? 132 ALA B N   1 
ATOM   2184 C  CA  . ALA B  2  132 ? 33.756 17.866  -43.912 1.00 61.06  ? 132 ALA B CA  1 
ATOM   2185 C  C   . ALA B  2  132 ? 32.621 18.827  -43.554 1.00 61.60  ? 132 ALA B C   1 
ATOM   2186 O  O   . ALA B  2  132 ? 31.794 19.174  -44.397 1.00 62.22  ? 132 ALA B O   1 
ATOM   2187 C  CB  . ALA B  2  132 ? 33.543 16.522  -43.214 1.00 60.15  ? 132 ALA B CB  1 
ATOM   2188 N  N   . CYS B  2  133 ? 32.595 19.269  -42.303 1.00 62.37  ? 133 CYS B N   1 
ATOM   2189 C  CA  . CYS B  2  133 ? 31.543 20.163  -41.846 1.00 64.53  ? 133 CYS B CA  1 
ATOM   2190 C  C   . CYS B  2  133 ? 31.641 21.606  -42.355 1.00 64.05  ? 133 CYS B C   1 
ATOM   2191 O  O   . CYS B  2  133 ? 30.646 22.333  -42.375 1.00 62.62  ? 133 CYS B O   1 
ATOM   2192 C  CB  . CYS B  2  133 ? 31.476 20.130  -40.318 1.00 67.23  ? 133 CYS B CB  1 
ATOM   2193 S  SG  . CYS B  2  133 ? 30.977 18.507  -39.642 1.00 72.50  ? 133 CYS B SG  1 
ATOM   2194 N  N   . LEU B  2  134 ? 32.832 22.028  -42.750 1.00 64.92  ? 134 LEU B N   1 
ATOM   2195 C  CA  . LEU B  2  134 ? 32.986 23.369  -43.294 1.00 65.88  ? 134 LEU B CA  1 
ATOM   2196 C  C   . LEU B  2  134 ? 32.507 23.298  -44.750 1.00 67.58  ? 134 LEU B C   1 
ATOM   2197 O  O   . LEU B  2  134 ? 31.936 24.263  -45.278 1.00 68.00  ? 134 LEU B O   1 
ATOM   2198 C  CB  . LEU B  2  134 ? 34.446 23.819  -43.232 1.00 64.74  ? 134 LEU B CB  1 
ATOM   2199 C  CG  . LEU B  2  134 ? 34.917 24.404  -41.900 1.00 63.83  ? 134 LEU B CG  1 
ATOM   2200 C  CD1 . LEU B  2  134 ? 36.354 24.871  -42.012 1.00 65.02  ? 134 LEU B CD1 1 
ATOM   2201 C  CD2 . LEU B  2  134 ? 34.038 25.572  -41.529 1.00 63.24  ? 134 LEU B CD2 1 
ATOM   2202 N  N   . ASP B  2  135 ? 32.749 22.155  -45.397 1.00 67.82  ? 135 ASP B N   1 
ATOM   2203 C  CA  . ASP B  2  135 ? 32.295 21.965  -46.773 1.00 67.12  ? 135 ASP B CA  1 
ATOM   2204 C  C   . ASP B  2  135 ? 30.779 22.132  -46.704 1.00 66.22  ? 135 ASP B C   1 
ATOM   2205 O  O   . ASP B  2  135 ? 30.197 22.924  -47.449 1.00 67.07  ? 135 ASP B O   1 
ATOM   2206 C  CB  . ASP B  2  135 ? 32.632 20.554  -47.299 1.00 67.78  ? 135 ASP B CB  1 
ATOM   2207 C  CG  . ASP B  2  135 ? 34.088 20.411  -47.770 1.00 68.57  ? 135 ASP B CG  1 
ATOM   2208 O  OD1 . ASP B  2  135 ? 34.698 21.417  -48.208 1.00 71.36  ? 135 ASP B OD1 1 
ATOM   2209 O  OD2 . ASP B  2  135 ? 34.610 19.272  -47.728 1.00 66.46  ? 135 ASP B OD2 1 
ATOM   2210 N  N   . VAL B  2  136 ? 30.154 21.395  -45.786 1.00 64.06  ? 136 VAL B N   1 
ATOM   2211 C  CA  . VAL B  2  136 ? 28.709 21.449  -45.595 1.00 63.45  ? 136 VAL B CA  1 
ATOM   2212 C  C   . VAL B  2  136 ? 28.212 22.868  -45.367 1.00 65.13  ? 136 VAL B C   1 
ATOM   2213 O  O   . VAL B  2  136 ? 27.102 23.208  -45.767 1.00 66.11  ? 136 VAL B O   1 
ATOM   2214 C  CB  . VAL B  2  136 ? 28.250 20.587  -44.374 1.00 61.65  ? 136 VAL B CB  1 
ATOM   2215 C  CG1 . VAL B  2  136 ? 26.803 20.900  -44.014 1.00 56.87  ? 136 VAL B CG1 1 
ATOM   2216 C  CG2 . VAL B  2  136 ? 28.380 19.113  -44.693 1.00 61.11  ? 136 VAL B CG2 1 
ATOM   2217 N  N   . ILE B  2  137 ? 29.025 23.700  -44.726 1.00 66.25  ? 137 ILE B N   1 
ATOM   2218 C  CA  . ILE B  2  137 ? 28.611 25.067  -44.437 1.00 67.98  ? 137 ILE B CA  1 
ATOM   2219 C  C   . ILE B  2  137 ? 28.751 26.032  -45.604 1.00 68.77  ? 137 ILE B C   1 
ATOM   2220 O  O   . ILE B  2  137 ? 27.817 26.772  -45.913 1.00 67.96  ? 137 ILE B O   1 
ATOM   2221 C  CB  . ILE B  2  137 ? 29.371 25.615  -43.211 1.00 68.68  ? 137 ILE B CB  1 
ATOM   2222 C  CG1 . ILE B  2  137 ? 28.941 24.818  -41.971 1.00 69.52  ? 137 ILE B CG1 1 
ATOM   2223 C  CG2 . ILE B  2  137 ? 29.083 27.112  -43.020 1.00 69.20  ? 137 ILE B CG2 1 
ATOM   2224 C  CD1 . ILE B  2  137 ? 29.703 25.161  -40.705 1.00 68.64  ? 137 ILE B CD1 1 
ATOM   2225 N  N   . THR B  2  138 ? 29.911 26.032  -46.250 1.00 69.94  ? 138 THR B N   1 
ATOM   2226 C  CA  . THR B  2  138 ? 30.128 26.916  -47.385 1.00 72.22  ? 138 THR B CA  1 
ATOM   2227 C  C   . THR B  2  138 ? 29.243 26.457  -48.525 1.00 74.26  ? 138 THR B C   1 
ATOM   2228 O  O   . THR B  2  138 ? 28.596 27.267  -49.188 1.00 74.46  ? 138 THR B O   1 
ATOM   2229 C  CB  . THR B  2  138 ? 31.586 26.884  -47.860 1.00 71.31  ? 138 THR B CB  1 
ATOM   2230 O  OG1 . THR B  2  138 ? 31.959 25.540  -48.177 1.00 69.58  ? 138 THR B OG1 1 
ATOM   2231 C  CG2 . THR B  2  138 ? 32.502 27.429  -46.782 1.00 70.69  ? 138 THR B CG2 1 
ATOM   2232 N  N   . SER B  2  139 ? 29.222 25.146  -48.735 1.00 76.92  ? 139 SER B N   1 
ATOM   2233 C  CA  . SER B  2  139 ? 28.417 24.536  -49.781 1.00 80.00  ? 139 SER B CA  1 
ATOM   2234 C  C   . SER B  2  139 ? 26.986 25.062  -49.740 1.00 82.60  ? 139 SER B C   1 
ATOM   2235 O  O   . SER B  2  139 ? 26.380 25.316  -50.778 1.00 83.15  ? 139 SER B O   1 
ATOM   2236 C  CB  . SER B  2  139 ? 28.414 23.018  -49.615 1.00 78.86  ? 139 SER B CB  1 
ATOM   2237 O  OG  . SER B  2  139 ? 27.541 22.417  -50.544 1.00 79.19  ? 139 SER B OG  1 
ATOM   2238 N  N   . GLY B  2  140 ? 26.455 25.232  -48.534 1.00 85.39  ? 140 GLY B N   1 
ATOM   2239 C  CA  . GLY B  2  140 ? 25.104 25.735  -48.382 1.00 88.92  ? 140 GLY B CA  1 
ATOM   2240 C  C   . GLY B  2  140 ? 25.000 27.240  -48.567 1.00 91.98  ? 140 GLY B C   1 
ATOM   2241 O  O   . GLY B  2  140 ? 23.942 27.743  -48.953 1.00 92.56  ? 140 GLY B O   1 
ATOM   2242 N  N   . ILE B  2  141 ? 26.083 27.966  -48.286 1.00 94.27  ? 141 ILE B N   1 
ATOM   2243 C  CA  . ILE B  2  141 ? 26.081 29.421  -48.434 1.00 96.51  ? 141 ILE B CA  1 
ATOM   2244 C  C   . ILE B  2  141 ? 26.151 29.794  -49.910 1.00 97.67  ? 141 ILE B C   1 
ATOM   2245 O  O   . ILE B  2  141 ? 25.778 30.902  -50.297 1.00 98.41  ? 141 ILE B O   1 
ATOM   2246 C  CB  . ILE B  2  141 ? 27.273 30.080  -47.691 1.00 97.06  ? 141 ILE B CB  1 
ATOM   2247 C  CG1 . ILE B  2  141 ? 27.208 29.741  -46.197 1.00 97.72  ? 141 ILE B CG1 1 
ATOM   2248 C  CG2 . ILE B  2  141 ? 27.227 31.594  -47.879 1.00 97.51  ? 141 ILE B CG2 1 
ATOM   2249 C  CD1 . ILE B  2  141 ? 28.351 30.301  -45.370 1.00 96.86  ? 141 ILE B CD1 1 
ATOM   2250 N  N   . GLN B  2  142 ? 26.631 28.861  -50.730 1.00 98.63  ? 142 GLN B N   1 
ATOM   2251 C  CA  . GLN B  2  142 ? 26.732 29.076  -52.173 1.00 99.72  ? 142 GLN B CA  1 
ATOM   2252 C  C   . GLN B  2  142 ? 25.496 28.480  -52.856 1.00 101.34 ? 142 GLN B C   1 
ATOM   2253 O  O   . GLN B  2  142 ? 25.537 28.146  -54.045 1.00 101.74 ? 142 GLN B O   1 
ATOM   2254 C  CB  . GLN B  2  142 ? 27.977 28.383  -52.753 1.00 98.19  ? 142 GLN B CB  1 
ATOM   2255 C  CG  . GLN B  2  142 ? 29.302 28.708  -52.094 1.00 95.65  ? 142 GLN B CG  1 
ATOM   2256 C  CD  . GLN B  2  142 ? 30.481 28.078  -52.826 1.00 94.32  ? 142 GLN B CD  1 
ATOM   2257 O  OE1 . GLN B  2  142 ? 30.862 28.521  -53.911 1.00 93.04  ? 142 GLN B OE1 1 
ATOM   2258 N  NE2 . GLN B  2  142 ? 31.052 27.037  -52.236 1.00 92.62  ? 142 GLN B NE2 1 
ATOM   2259 N  N   . GLY B  2  143 ? 24.401 28.355  -52.110 1.00 102.42 ? 143 GLY B N   1 
ATOM   2260 C  CA  . GLY B  2  143 ? 23.198 27.758  -52.666 1.00 103.60 ? 143 GLY B CA  1 
ATOM   2261 C  C   . GLY B  2  143 ? 23.413 26.253  -52.686 1.00 104.06 ? 143 GLY B C   1 
ATOM   2262 O  O   . GLY B  2  143 ? 22.650 25.482  -52.096 1.00 104.01 ? 143 GLY B O   1 
ATOM   2263 N  N   . ASN B  2  144 ? 24.475 25.844  -53.370 1.00 104.43 ? 144 ASN B N   1 
ATOM   2264 C  CA  . ASN B  2  144 ? 24.859 24.446  -53.474 1.00 105.24 ? 144 ASN B CA  1 
ATOM   2265 C  C   . ASN B  2  144 ? 25.988 24.296  -54.490 1.00 105.31 ? 144 ASN B C   1 
ATOM   2266 O  O   . ASN B  2  144 ? 27.014 23.684  -54.136 1.00 104.98 ? 144 ASN B O   1 
ATOM   2267 C  CB  . ASN B  2  144 ? 23.669 23.581  -53.892 1.00 106.20 ? 144 ASN B CB  1 
ATOM   2268 C  CG  . ASN B  2  144 ? 23.950 22.101  -53.726 1.00 107.11 ? 144 ASN B CG  1 
ATOM   2269 O  OD1 . ASN B  2  144 ? 24.250 21.635  -52.622 1.00 105.94 ? 144 ASN B OD1 1 
ATOM   2270 N  ND2 . ASN B  2  144 ? 23.855 21.353  -54.821 1.00 107.40 ? 144 ASN B ND2 1 
ATOM   2271 O  OXT . ASN B  2  144 ? 25.832 24.793  -55.623 1.00 106.22 ? 144 ASN B OXT 1 
ATOM   2272 N  N   . SER C  3  1   ? 28.074 60.436  -16.482 1.00 131.17 ? 1   SER C N   1 
ATOM   2273 C  CA  . SER C  3  1   ? 27.294 59.415  -15.809 1.00 130.40 ? 1   SER C CA  1 
ATOM   2274 C  C   . SER C  3  1   ? 25.859 59.920  -15.439 1.00 128.64 ? 1   SER C C   1 
ATOM   2275 O  O   . SER C  3  1   ? 25.352 60.838  -16.131 1.00 128.90 ? 1   SER C O   1 
ATOM   2276 C  CB  . SER C  3  1   ? 28.091 59.004  -14.587 1.00 131.75 ? 1   SER C CB  1 
ATOM   2277 O  OG  . SER C  3  1   ? 29.157 58.114  -14.891 1.00 132.47 ? 1   SER C OG  1 
ATOM   2278 N  N   . SER C  3  2   ? 25.233 59.326  -14.398 1.00 125.41 ? 2   SER C N   1 
ATOM   2279 C  CA  . SER C  3  2   ? 25.771 58.258  -13.578 1.00 120.97 ? 2   SER C CA  1 
ATOM   2280 C  C   . SER C  3  2   ? 25.386 56.925  -13.930 1.00 116.53 ? 2   SER C C   1 
ATOM   2281 O  O   . SER C  3  2   ? 26.400 55.842  -13.649 1.00 116.96 ? 2   SER C O   1 
ATOM   2282 C  CB  . SER C  3  2   ? 25.494 58.536  -12.068 1.00 122.65 ? 2   SER C CB  1 
ATOM   2283 O  OG  . SER C  3  2   ? 25.830 59.903  -11.755 1.00 124.08 ? 2   SER C OG  1 
ATOM   2284 N  N   . ASN C  3  3   ? 24.291 56.904  -14.829 1.00 110.13 ? 3   ASN C N   1 
ATOM   2285 C  CA  . ASN C  3  3   ? 23.704 55.659  -15.163 1.00 103.24 ? 3   ASN C CA  1 
ATOM   2286 C  C   . ASN C  3  3   ? 24.501 54.980  -16.308 1.00 97.71  ? 3   ASN C C   1 
ATOM   2287 O  O   . ASN C  3  3   ? 23.995 54.178  -17.140 1.00 97.33  ? 3   ASN C O   1 
ATOM   2288 C  CB  . ASN C  3  3   ? 22.218 55.712  -15.602 1.00 104.23 ? 3   ASN C CB  1 
ATOM   2289 C  CG  . ASN C  3  3   ? 21.356 55.581  -14.430 1.00 105.26 ? 3   ASN C CG  1 
ATOM   2290 O  OD1 . ASN C  3  3   ? 21.237 54.508  -13.892 1.00 105.81 ? 3   ASN C OD1 1 
ATOM   2291 N  ND2 . ASN C  3  3   ? 20.642 56.668  -14.076 1.00 105.98 ? 3   ASN C ND2 1 
ATOM   2292 N  N   . SER C  3  4   ? 25.771 55.382  -16.440 1.00 90.01  ? 4   SER C N   1 
ATOM   2293 C  CA  . SER C  3  4   ? 26.598 54.833  -17.496 1.00 82.75  ? 4   SER C CA  1 
ATOM   2294 C  C   . SER C  3  4   ? 26.958 53.356  -17.327 1.00 76.71  ? 4   SER C C   1 
ATOM   2295 O  O   . SER C  3  4   ? 27.039 52.831  -16.208 1.00 75.75  ? 4   SER C O   1 
ATOM   2296 C  CB  . SER C  3  4   ? 27.875 55.650  -17.616 1.00 84.01  ? 4   SER C CB  1 
ATOM   2297 O  OG  . SER C  3  4   ? 27.655 57.027  -17.882 1.00 86.60  ? 4   SER C OG  1 
ATOM   2298 N  N   . CYS C  3  5   ? 27.212 52.698  -18.454 1.00 69.21  ? 5   CYS C N   1 
ATOM   2299 C  CA  . CYS C  3  5   ? 27.628 51.302  -18.435 1.00 62.66  ? 5   CYS C CA  1 
ATOM   2300 C  C   . CYS C  3  5   ? 29.118 51.290  -18.109 1.00 59.78  ? 5   CYS C C   1 
ATOM   2301 O  O   . CYS C  3  5   ? 29.944 51.562  -18.966 1.00 58.22  ? 5   CYS C O   1 
ATOM   2302 C  CB  . CYS C  3  5   ? 27.366 50.637  -19.795 1.00 60.00  ? 5   CYS C CB  1 
ATOM   2303 S  SG  . CYS C  3  5   ? 28.120 48.983  -20.005 1.00 55.43  ? 5   CYS C SG  1 
ATOM   2304 N  N   . THR C  3  6   ? 29.451 50.958  -16.862 1.00 57.13  ? 6   THR C N   1 
ATOM   2305 C  CA  . THR C  3  6   ? 30.839 50.959  -16.419 1.00 53.78  ? 6   THR C CA  1 
ATOM   2306 C  C   . THR C  3  6   ? 31.610 49.697  -16.753 1.00 52.38  ? 6   THR C C   1 
ATOM   2307 O  O   . THR C  3  6   ? 31.039 48.687  -17.154 1.00 51.22  ? 6   THR C O   1 
ATOM   2308 C  CB  . THR C  3  6   ? 30.938 51.153  -14.898 1.00 53.81  ? 6   THR C CB  1 
ATOM   2309 O  OG1 . THR C  3  6   ? 30.553 49.938  -14.242 1.00 54.41  ? 6   THR C OG1 1 
ATOM   2310 C  CG2 . THR C  3  6   ? 30.026 52.289  -14.439 1.00 52.75  ? 6   THR C CG2 1 
ATOM   2311 N  N   . THR C  3  7   ? 32.919 49.757  -16.578 1.00 50.30  ? 7   THR C N   1 
ATOM   2312 C  CA  . THR C  3  7   ? 33.744 48.597  -16.834 1.00 49.12  ? 7   THR C CA  1 
ATOM   2313 C  C   . THR C  3  7   ? 33.258 47.409  -15.995 1.00 50.55  ? 7   THR C C   1 
ATOM   2314 O  O   . THR C  3  7   ? 33.167 46.294  -16.502 1.00 52.46  ? 7   THR C O   1 
ATOM   2315 C  CB  . THR C  3  7   ? 35.219 48.888  -16.499 1.00 46.22  ? 7   THR C CB  1 
ATOM   2316 O  OG1 . THR C  3  7   ? 35.742 49.835  -17.440 1.00 43.34  ? 7   THR C OG1 1 
ATOM   2317 C  CG2 . THR C  3  7   ? 36.035 47.624  -16.552 1.00 41.59  ? 7   THR C CG2 1 
ATOM   2318 N  N   . GLU C  3  8   ? 32.930 47.646  -14.723 1.00 50.15  ? 8   GLU C N   1 
ATOM   2319 C  CA  . GLU C  3  8   ? 32.478 46.560  -13.864 1.00 49.74  ? 8   GLU C CA  1 
ATOM   2320 C  C   . GLU C  3  8   ? 31.109 46.047  -14.263 1.00 49.12  ? 8   GLU C C   1 
ATOM   2321 O  O   . GLU C  3  8   ? 30.847 44.842  -14.205 1.00 48.26  ? 8   GLU C O   1 
ATOM   2322 C  CB  . GLU C  3  8   ? 32.496 46.961  -12.369 1.00 49.28  ? 8   GLU C CB  1 
ATOM   2323 C  CG  . GLU C  3  8   ? 32.165 48.406  -12.061 1.00 50.84  ? 8   GLU C CG  1 
ATOM   2324 C  CD  . GLU C  3  8   ? 33.335 49.346  -12.342 1.00 50.26  ? 8   GLU C CD  1 
ATOM   2325 O  OE1 . GLU C  3  8   ? 34.230 49.488  -11.482 1.00 46.25  ? 8   GLU C OE1 1 
ATOM   2326 O  OE2 . GLU C  3  8   ? 33.367 49.932  -13.437 1.00 50.66  ? 8   GLU C OE2 1 
ATOM   2327 N  N   . ASP C  3  9   ? 30.231 46.945  -14.676 1.00 49.18  ? 9   ASP C N   1 
ATOM   2328 C  CA  . ASP C  3  9   ? 28.923 46.489  -15.103 1.00 51.57  ? 9   ASP C CA  1 
ATOM   2329 C  C   . ASP C  3  9   ? 29.084 45.596  -16.318 1.00 52.58  ? 9   ASP C C   1 
ATOM   2330 O  O   . ASP C  3  9   ? 28.342 44.642  -16.484 1.00 54.69  ? 9   ASP C O   1 
ATOM   2331 C  CB  . ASP C  3  9   ? 28.019 47.657  -15.453 1.00 52.09  ? 9   ASP C CB  1 
ATOM   2332 C  CG  . ASP C  3  9   ? 27.695 48.521  -14.249 1.00 53.53  ? 9   ASP C CG  1 
ATOM   2333 O  OD1 . ASP C  3  9   ? 27.607 47.971  -13.121 1.00 53.79  ? 9   ASP C OD1 1 
ATOM   2334 O  OD2 . ASP C  3  9   ? 27.517 49.744  -14.440 1.00 52.77  ? 9   ASP C OD2 1 
ATOM   2335 N  N   . ARG C  3  10  ? 30.058 45.909  -17.162 1.00 52.94  ? 10  ARG C N   1 
ATOM   2336 C  CA  . ARG C  3  10  ? 30.324 45.118  -18.356 1.00 53.21  ? 10  ARG C CA  1 
ATOM   2337 C  C   . ARG C  3  10  ? 30.837 43.738  -17.986 1.00 54.14  ? 10  ARG C C   1 
ATOM   2338 O  O   . ARG C  3  10  ? 30.395 42.747  -18.558 1.00 53.76  ? 10  ARG C O   1 
ATOM   2339 C  CB  . ARG C  3  10  ? 31.343 45.837  -19.240 1.00 53.90  ? 10  ARG C CB  1 
ATOM   2340 C  CG  . ARG C  3  10  ? 30.781 47.109  -19.828 1.00 54.31  ? 10  ARG C CG  1 
ATOM   2341 C  CD  . ARG C  3  10  ? 31.842 48.087  -20.312 1.00 52.12  ? 10  ARG C CD  1 
ATOM   2342 N  NE  . ARG C  3  10  ? 31.227 49.405  -20.468 1.00 52.23  ? 10  ARG C NE  1 
ATOM   2343 C  CZ  . ARG C  3  10  ? 31.098 50.054  -21.624 1.00 51.32  ? 10  ARG C CZ  1 
ATOM   2344 N  NH1 . ARG C  3  10  ? 31.564 49.507  -22.742 1.00 48.16  ? 10  ARG C NH1 1 
ATOM   2345 N  NH2 . ARG C  3  10  ? 30.470 51.230  -21.656 1.00 48.38  ? 10  ARG C NH2 1 
ATOM   2346 N  N   . ARG C  3  11  ? 31.767 43.680  -17.036 1.00 55.24  ? 11  ARG C N   1 
ATOM   2347 C  CA  . ARG C  3  11  ? 32.301 42.398  -16.595 1.00 56.03  ? 11  ARG C CA  1 
ATOM   2348 C  C   . ARG C  3  11  ? 31.108 41.564  -16.109 1.00 54.22  ? 11  ARG C C   1 
ATOM   2349 O  O   . ARG C  3  11  ? 30.962 40.392  -16.443 1.00 53.10  ? 11  ARG C O   1 
ATOM   2350 C  CB  . ARG C  3  11  ? 33.287 42.586  -15.431 1.00 59.56  ? 11  ARG C CB  1 
ATOM   2351 C  CG  . ARG C  3  11  ? 34.517 43.435  -15.727 1.00 66.08  ? 11  ARG C CG  1 
ATOM   2352 C  CD  . ARG C  3  11  ? 35.487 43.412  -14.538 1.00 71.73  ? 11  ARG C CD  1 
ATOM   2353 N  NE  . ARG C  3  11  ? 36.559 44.415  -14.612 1.00 76.22  ? 11  ARG C NE  1 
ATOM   2354 C  CZ  . ARG C  3  11  ? 37.496 44.461  -15.556 1.00 78.91  ? 11  ARG C CZ  1 
ATOM   2355 N  NH1 . ARG C  3  11  ? 38.421 45.411  -15.521 1.00 79.76  ? 11  ARG C NH1 1 
ATOM   2356 N  NH2 . ARG C  3  11  ? 37.514 43.569  -16.546 1.00 80.09  ? 11  ARG C NH2 1 
ATOM   2357 N  N   . GLU C  3  12  ? 30.258 42.224  -15.320 1.00 51.88  ? 12  GLU C N   1 
ATOM   2358 C  CA  . GLU C  3  12  ? 29.066 41.619  -14.733 1.00 52.03  ? 12  GLU C CA  1 
ATOM   2359 C  C   . GLU C  3  12  ? 28.053 41.136  -15.743 1.00 52.18  ? 12  GLU C C   1 
ATOM   2360 O  O   . GLU C  3  12  ? 27.393 40.110  -15.539 1.00 52.03  ? 12  GLU C O   1 
ATOM   2361 C  CB  . GLU C  3  12  ? 28.380 42.598  -13.818 1.00 54.51  ? 12  GLU C CB  1 
ATOM   2362 C  CG  . GLU C  3  12  ? 28.525 42.329  -12.343 1.00 59.08  ? 12  GLU C CG  1 
ATOM   2363 C  CD  . GLU C  3  12  ? 27.617 43.231  -11.552 1.00 61.66  ? 12  GLU C CD  1 
ATOM   2364 O  OE1 . GLU C  3  12  ? 26.455 42.840  -11.332 1.00 60.61  ? 12  GLU C OE1 1 
ATOM   2365 O  OE2 . GLU C  3  12  ? 28.053 44.348  -11.190 1.00 63.46  ? 12  GLU C OE2 1 
ATOM   2366 N  N   . MET C  3  13  ? 27.887 41.896  -16.813 1.00 50.89  ? 13  MET C N   1 
ATOM   2367 C  CA  . MET C  3  13  ? 26.921 41.521  -17.823 1.00 50.45  ? 13  MET C CA  1 
ATOM   2368 C  C   . MET C  3  13  ? 27.462 40.350  -18.605 1.00 49.73  ? 13  MET C C   1 
ATOM   2369 O  O   . MET C  3  13  ? 26.734 39.409  -18.880 1.00 49.69  ? 13  MET C O   1 
ATOM   2370 C  CB  . MET C  3  13  ? 26.641 42.694  -18.763 1.00 52.21  ? 13  MET C CB  1 
ATOM   2371 C  CG  . MET C  3  13  ? 25.666 42.345  -19.872 1.00 50.63  ? 13  MET C CG  1 
ATOM   2372 S  SD  . MET C  3  13  ? 25.132 43.782  -20.781 1.00 53.10  ? 13  MET C SD  1 
ATOM   2373 C  CE  . MET C  3  13  ? 23.613 43.226  -21.524 1.00 50.70  ? 13  MET C CE  1 
ATOM   2374 N  N   . GLN C  3  14  ? 28.741 40.393  -18.954 1.00 48.03  ? 14  GLN C N   1 
ATOM   2375 C  CA  . GLN C  3  14  ? 29.326 39.280  -19.686 1.00 49.38  ? 14  GLN C CA  1 
ATOM   2376 C  C   . GLN C  3  14  ? 29.160 38.032  -18.827 1.00 51.21  ? 14  GLN C C   1 
ATOM   2377 O  O   . GLN C  3  14  ? 28.973 36.905  -19.367 1.00 51.19  ? 14  GLN C O   1 
ATOM   2378 C  CB  . GLN C  3  14  ? 30.791 39.555  -19.954 1.00 48.36  ? 14  GLN C CB  1 
ATOM   2379 C  CG  . GLN C  3  14  ? 30.974 40.695  -20.914 1.00 51.76  ? 14  GLN C CG  1 
ATOM   2380 C  CD  . GLN C  3  14  ? 32.423 41.065  -21.143 1.00 53.87  ? 14  GLN C CD  1 
ATOM   2381 O  OE1 . GLN C  3  14  ? 32.724 41.841  -22.042 1.00 57.27  ? 14  GLN C OE1 1 
ATOM   2382 N  NE2 . GLN C  3  14  ? 33.332 40.522  -20.329 1.00 54.99  ? 14  GLN C NE2 1 
ATOM   2383 N  N   . LEU C  3  15  ? 29.220 38.224  -17.498 1.00 51.37  ? 15  LEU C N   1 
ATOM   2384 C  CA  . LEU C  3  15  ? 29.043 37.082  -16.625 1.00 52.66  ? 15  LEU C CA  1 
ATOM   2385 C  C   . LEU C  3  15  ? 27.620 36.511  -16.626 1.00 52.14  ? 15  LEU C C   1 
ATOM   2386 O  O   . LEU C  3  15  ? 27.425 35.310  -16.895 1.00 51.48  ? 15  LEU C O   1 
ATOM   2387 C  CB  . LEU C  3  15  ? 29.457 37.352  -15.176 1.00 55.10  ? 15  LEU C CB  1 
ATOM   2388 C  CG  . LEU C  3  15  ? 29.855 35.969  -14.723 1.00 57.06  ? 15  LEU C CG  1 
ATOM   2389 C  CD1 . LEU C  3  15  ? 31.380 36.033  -14.481 1.00 56.65  ? 15  LEU C CD1 1 
ATOM   2390 C  CD2 . LEU C  3  15  ? 29.137 35.707  -13.363 1.00 56.60  ? 15  LEU C CD2 1 
ATOM   2391 N  N   . MET C  3  16  ? 26.639 37.382  -16.442 1.00 51.50  ? 16  MET C N   1 
ATOM   2392 C  CA  . MET C  3  16  ? 25.252 36.965  -16.471 1.00 52.72  ? 16  MET C CA  1 
ATOM   2393 C  C   . MET C  3  16  ? 24.919 36.309  -17.786 1.00 54.07  ? 16  MET C C   1 
ATOM   2394 O  O   . MET C  3  16  ? 24.058 35.437  -17.841 1.00 51.14  ? 16  MET C O   1 
ATOM   2395 C  CB  . MET C  3  16  ? 24.351 38.180  -16.286 1.00 52.68  ? 16  MET C CB  1 
ATOM   2396 C  CG  . MET C  3  16  ? 24.553 38.929  -14.971 1.00 53.34  ? 16  MET C CG  1 
ATOM   2397 S  SD  . MET C  3  16  ? 23.378 40.324  -14.847 1.00 53.08  ? 16  MET C SD  1 
ATOM   2398 C  CE  . MET C  3  16  ? 24.445 41.717  -15.117 1.00 55.26  ? 16  MET C CE  1 
ATOM   2399 N  N   . TRP C  3  17  ? 25.614 36.733  -18.835 1.00 56.11  ? 17  TRP C N   1 
ATOM   2400 C  CA  . TRP C  3  17  ? 25.387 36.210  -20.165 1.00 60.37  ? 17  TRP C CA  1 
ATOM   2401 C  C   . TRP C  3  17  ? 26.165 34.927  -20.404 1.00 65.36  ? 17  TRP C C   1 
ATOM   2402 O  O   . TRP C  3  17  ? 25.572 33.904  -20.732 1.00 64.82  ? 17  TRP C O   1 
ATOM   2403 C  CB  . TRP C  3  17  ? 25.773 37.274  -21.192 1.00 56.36  ? 17  TRP C CB  1 
ATOM   2404 C  CG  . TRP C  3  17  ? 25.493 36.883  -22.610 1.00 52.36  ? 17  TRP C CG  1 
ATOM   2405 C  CD1 . TRP C  3  17  ? 26.406 36.497  -23.552 1.00 51.75  ? 17  TRP C CD1 1 
ATOM   2406 C  CD2 . TRP C  3  17  ? 24.219 36.888  -23.268 1.00 49.95  ? 17  TRP C CD2 1 
ATOM   2407 N  NE1 . TRP C  3  17  ? 25.780 36.272  -24.762 1.00 51.48  ? 17  TRP C NE1 1 
ATOM   2408 C  CE2 . TRP C  3  17  ? 24.439 36.506  -24.612 1.00 50.35  ? 17  TRP C CE2 1 
ATOM   2409 C  CE3 . TRP C  3  17  ? 22.918 37.185  -22.848 1.00 47.46  ? 17  TRP C CE3 1 
ATOM   2410 C  CZ2 . TRP C  3  17  ? 23.404 36.419  -25.544 1.00 50.75  ? 17  TRP C CZ2 1 
ATOM   2411 C  CZ3 . TRP C  3  17  ? 21.889 37.094  -23.769 1.00 50.29  ? 17  TRP C CZ3 1 
ATOM   2412 C  CH2 . TRP C  3  17  ? 22.137 36.716  -25.108 1.00 49.62  ? 17  TRP C CH2 1 
ATOM   2413 N  N   . ALA C  3  18  ? 27.483 34.981  -20.224 1.00 72.29  ? 18  ALA C N   1 
ATOM   2414 C  CA  . ALA C  3  18  ? 28.349 33.821  -20.464 1.00 78.98  ? 18  ALA C CA  1 
ATOM   2415 C  C   . ALA C  3  18  ? 27.833 32.575  -19.787 1.00 83.33  ? 18  ALA C C   1 
ATOM   2416 O  O   . ALA C  3  18  ? 28.072 31.454  -20.246 1.00 84.63  ? 18  ALA C O   1 
ATOM   2417 C  CB  . ALA C  3  18  ? 29.787 34.107  -19.989 1.00 78.89  ? 18  ALA C CB  1 
ATOM   2418 N  N   . ASN C  3  19  ? 27.107 32.786  -18.702 1.00 88.56  ? 19  ASN C N   1 
ATOM   2419 C  CA  . ASN C  3  19  ? 26.534 31.707  -17.941 1.00 93.65  ? 19  ASN C CA  1 
ATOM   2420 C  C   . ASN C  3  19  ? 25.391 31.060  -18.697 1.00 95.49  ? 19  ASN C C   1 
ATOM   2421 O  O   . ASN C  3  19  ? 25.445 29.874  -19.039 1.00 97.41  ? 19  ASN C O   1 
ATOM   2422 C  CB  . ASN C  3  19  ? 26.043 32.253  -16.592 1.00 96.15  ? 19  ASN C CB  1 
ATOM   2423 C  CG  . ASN C  3  19  ? 24.820 31.514  -16.055 1.00 98.22  ? 19  ASN C CG  1 
ATOM   2424 O  OD1 . ASN C  3  19  ? 24.918 30.694  -15.148 1.00 99.64  ? 19  ASN C OD1 1 
ATOM   2425 N  ND2 . ASN C  3  19  ? 23.658 31.813  -16.623 1.00 99.15  ? 19  ASN C ND2 1 
ATOM   2426 N  N   . VAL C  3  20  ? 24.355 31.844  -18.968 1.00 96.05  ? 20  VAL C N   1 
ATOM   2427 C  CA  . VAL C  3  20  ? 23.189 31.334  -19.654 1.00 97.06  ? 20  VAL C CA  1 
ATOM   2428 C  C   . VAL C  3  20  ? 23.398 31.205  -21.164 1.00 97.54  ? 20  VAL C C   1 
ATOM   2429 O  O   . VAL C  3  20  ? 22.452 31.052  -21.929 1.00 97.89  ? 20  VAL C O   1 
ATOM   2430 C  CB  . VAL C  3  20  ? 21.978 32.230  -19.302 1.00 96.99  ? 20  VAL C CB  1 
ATOM   2431 C  CG1 . VAL C  3  20  ? 21.481 32.979  -20.508 1.00 97.61  ? 20  VAL C CG1 1 
ATOM   2432 C  CG2 . VAL C  3  20  ? 20.901 31.381  -18.687 1.00 98.23  ? 20  VAL C CG2 1 
ATOM   2433 N  N   . TRP C  3  21  ? 24.657 31.228  -21.582 1.00 98.06  ? 21  TRP C N   1 
ATOM   2434 C  CA  . TRP C  3  21  ? 24.991 31.102  -22.992 1.00 98.46  ? 21  TRP C CA  1 
ATOM   2435 C  C   . TRP C  3  21  ? 25.595 29.745  -23.342 1.00 99.48  ? 21  TRP C C   1 
ATOM   2436 O  O   . TRP C  3  21  ? 26.634 29.343  -22.803 1.00 100.24 ? 21  TRP C O   1 
ATOM   2437 C  CB  . TRP C  3  21  ? 25.959 32.214  -23.391 1.00 97.57  ? 21  TRP C CB  1 
ATOM   2438 C  CG  . TRP C  3  21  ? 26.523 32.061  -24.758 1.00 96.60  ? 21  TRP C CG  1 
ATOM   2439 C  CD1 . TRP C  3  21  ? 27.674 31.415  -25.110 1.00 96.62  ? 21  TRP C CD1 1 
ATOM   2440 C  CD2 . TRP C  3  21  ? 25.971 32.584  -25.968 1.00 96.11  ? 21  TRP C CD2 1 
ATOM   2441 N  NE1 . TRP C  3  21  ? 27.880 31.516  -26.466 1.00 96.18  ? 21  TRP C NE1 1 
ATOM   2442 C  CE2 . TRP C  3  21  ? 26.847 32.229  -27.018 1.00 95.53  ? 21  TRP C CE2 1 
ATOM   2443 C  CE3 . TRP C  3  21  ? 24.820 33.325  -26.268 1.00 96.18  ? 21  TRP C CE3 1 
ATOM   2444 C  CZ2 . TRP C  3  21  ? 26.609 32.590  -28.351 1.00 95.09  ? 21  TRP C CZ2 1 
ATOM   2445 C  CZ3 . TRP C  3  21  ? 24.581 33.684  -27.592 1.00 95.30  ? 21  TRP C CZ3 1 
ATOM   2446 C  CH2 . TRP C  3  21  ? 25.471 33.315  -28.618 1.00 94.94  ? 21  TRP C CH2 1 
ATOM   2447 N  N   . SER C  3  22  ? 24.926 29.040  -24.249 1.00 99.40  ? 22  SER C N   1 
ATOM   2448 C  CA  . SER C  3  22  ? 25.395 27.738  -24.703 1.00 99.48  ? 22  SER C CA  1 
ATOM   2449 C  C   . SER C  3  22  ? 26.276 27.935  -25.940 1.00 97.86  ? 22  SER C C   1 
ATOM   2450 O  O   . SER C  3  22  ? 25.810 28.372  -26.994 1.00 98.12  ? 22  SER C O   1 
ATOM   2451 C  CB  . SER C  3  22  ? 24.202 26.822  -25.025 1.00 100.57 ? 22  SER C CB  1 
ATOM   2452 O  OG  . SER C  3  22  ? 23.292 27.437  -25.924 1.00 101.80 ? 22  SER C OG  1 
ATOM   2453 N  N   . ALA C  3  23  ? 27.556 27.620  -25.796 1.00 95.33  ? 23  ALA C N   1 
ATOM   2454 C  CA  . ALA C  3  23  ? 28.503 27.775  -26.883 1.00 93.14  ? 23  ALA C CA  1 
ATOM   2455 C  C   . ALA C  3  23  ? 28.491 26.615  -27.867 1.00 91.65  ? 23  ALA C C   1 
ATOM   2456 O  O   . ALA C  3  23  ? 29.206 26.652  -28.866 1.00 91.09  ? 23  ALA C O   1 
ATOM   2457 C  CB  . ALA C  3  23  ? 29.895 27.952  -26.322 1.00 93.07  ? 23  ALA C CB  1 
ATOM   2458 N  N   . GLN C  3  24  ? 27.685 25.593  -27.593 1.00 90.15  ? 24  GLN C N   1 
ATOM   2459 C  CA  . GLN C  3  24  ? 27.619 24.432  -28.473 1.00 88.62  ? 24  GLN C CA  1 
ATOM   2460 C  C   . GLN C  3  24  ? 26.266 24.172  -29.141 1.00 88.44  ? 24  GLN C C   1 
ATOM   2461 O  O   . GLN C  3  24  ? 26.219 23.758  -30.307 1.00 88.80  ? 24  GLN C O   1 
ATOM   2462 C  CB  . GLN C  3  24  ? 28.059 23.174  -27.720 1.00 86.92  ? 24  GLN C CB  1 
ATOM   2463 C  CG  . GLN C  3  24  ? 29.553 23.123  -27.441 1.00 85.61  ? 24  GLN C CG  1 
ATOM   2464 C  CD  . GLN C  3  24  ? 30.020 21.767  -26.934 1.00 84.39  ? 24  GLN C CD  1 
ATOM   2465 O  OE1 . GLN C  3  24  ? 29.888 20.754  -27.615 1.00 83.27  ? 24  GLN C OE1 1 
ATOM   2466 N  NE2 . GLN C  3  24  ? 30.576 21.751  -25.735 1.00 84.27  ? 24  GLN C NE2 1 
ATOM   2467 N  N   . PHE C  3  25  ? 25.174 24.412  -28.418 1.00 87.10  ? 25  PHE C N   1 
ATOM   2468 C  CA  . PHE C  3  25  ? 23.849 24.171  -28.975 1.00 84.54  ? 25  PHE C CA  1 
ATOM   2469 C  C   . PHE C  3  25  ? 22.927 25.374  -28.889 1.00 82.60  ? 25  PHE C C   1 
ATOM   2470 O  O   . PHE C  3  25  ? 23.068 26.219  -28.013 1.00 82.09  ? 25  PHE C O   1 
ATOM   2471 C  CB  . PHE C  3  25  ? 23.232 22.953  -28.290 1.00 85.81  ? 25  PHE C CB  1 
ATOM   2472 C  CG  . PHE C  3  25  ? 24.068 21.712  -28.435 1.00 86.91  ? 25  PHE C CG  1 
ATOM   2473 C  CD1 . PHE C  3  25  ? 23.945 20.896  -29.562 1.00 87.64  ? 25  PHE C CD1 1 
ATOM   2474 C  CD2 . PHE C  3  25  ? 25.038 21.401  -27.485 1.00 87.04  ? 25  PHE C CD2 1 
ATOM   2475 C  CE1 . PHE C  3  25  ? 24.783 19.790  -29.742 1.00 87.66  ? 25  PHE C CE1 1 
ATOM   2476 C  CE2 . PHE C  3  25  ? 25.880 20.301  -27.653 1.00 87.03  ? 25  PHE C CE2 1 
ATOM   2477 C  CZ  . PHE C  3  25  ? 25.753 19.496  -28.785 1.00 87.66  ? 25  PHE C CZ  1 
ATOM   2478 N  N   . THR C  3  26  ? 21.987 25.443  -29.820 1.00 80.73  ? 26  THR C N   1 
ATOM   2479 C  CA  . THR C  3  26  ? 21.037 26.546  -29.899 1.00 78.31  ? 26  THR C CA  1 
ATOM   2480 C  C   . THR C  3  26  ? 19.900 26.458  -28.891 1.00 75.20  ? 26  THR C C   1 
ATOM   2481 O  O   . THR C  3  26  ? 19.187 27.437  -28.671 1.00 74.55  ? 26  THR C O   1 
ATOM   2482 C  CB  . THR C  3  26  ? 20.437 26.634  -31.314 1.00 79.23  ? 26  THR C CB  1 
ATOM   2483 O  OG1 . THR C  3  26  ? 19.870 25.363  -31.675 1.00 81.47  ? 26  THR C OG1 1 
ATOM   2484 C  CG2 . THR C  3  26  ? 21.516 27.009  -32.315 1.00 78.35  ? 26  THR C CG2 1 
ATOM   2485 N  N   . GLY C  3  27  ? 19.743 25.293  -28.273 1.00 72.38  ? 27  GLY C N   1 
ATOM   2486 C  CA  . GLY C  3  27  ? 18.682 25.111  -27.304 1.00 69.56  ? 27  GLY C CA  1 
ATOM   2487 C  C   . GLY C  3  27  ? 18.500 26.254  -26.324 1.00 67.03  ? 27  GLY C C   1 
ATOM   2488 O  O   . GLY C  3  27  ? 17.407 26.812  -26.218 1.00 67.05  ? 27  GLY C O   1 
ATOM   2489 N  N   . ARG C  3  28  ? 19.569 26.619  -25.626 1.00 64.41  ? 28  ARG C N   1 
ATOM   2490 C  CA  . ARG C  3  28  ? 19.493 27.685  -24.638 1.00 63.29  ? 28  ARG C CA  1 
ATOM   2491 C  C   . ARG C  3  28  ? 19.225 29.072  -25.273 1.00 59.84  ? 28  ARG C C   1 
ATOM   2492 O  O   . ARG C  3  28  ? 18.288 29.762  -24.886 1.00 57.18  ? 28  ARG C O   1 
ATOM   2493 C  CB  . ARG C  3  28  ? 20.787 27.694  -23.801 1.00 65.71  ? 28  ARG C CB  1 
ATOM   2494 C  CG  . ARG C  3  28  ? 20.599 27.991  -22.312 1.00 70.15  ? 28  ARG C CG  1 
ATOM   2495 C  CD  . ARG C  3  28  ? 21.359 26.984  -21.447 1.00 72.84  ? 28  ARG C CD  1 
ATOM   2496 N  NE  . ARG C  3  28  ? 22.767 26.881  -21.829 1.00 76.04  ? 28  ARG C NE  1 
ATOM   2497 C  CZ  . ARG C  3  28  ? 23.581 25.882  -21.473 1.00 77.36  ? 28  ARG C CZ  1 
ATOM   2498 N  NH1 . ARG C  3  28  ? 24.849 25.878  -21.872 1.00 76.42  ? 28  ARG C NH1 1 
ATOM   2499 N  NH2 . ARG C  3  28  ? 23.131 24.887  -20.722 1.00 78.87  ? 28  ARG C NH2 1 
ATOM   2500 N  N   . ARG C  3  29  ? 20.036 29.454  -26.257 1.00 57.92  ? 29  ARG C N   1 
ATOM   2501 C  CA  . ARG C  3  29  ? 19.900 30.756  -26.935 1.00 58.07  ? 29  ARG C CA  1 
ATOM   2502 C  C   . ARG C  3  29  ? 18.465 30.950  -27.417 1.00 57.16  ? 29  ARG C C   1 
ATOM   2503 O  O   . ARG C  3  29  ? 17.711 31.882  -27.051 1.00 54.96  ? 29  ARG C O   1 
ATOM   2504 C  CB  . ARG C  3  29  ? 20.783 30.798  -28.169 1.00 57.69  ? 29  ARG C CB  1 
ATOM   2505 C  CG  . ARG C  3  29  ? 22.198 30.398  -27.917 1.00 59.62  ? 29  ARG C CG  1 
ATOM   2506 C  CD  . ARG C  3  29  ? 22.974 30.453  -29.191 1.00 59.90  ? 29  ARG C CD  1 
ATOM   2507 N  NE  . ARG C  3  29  ? 24.283 29.846  -29.026 1.00 61.05  ? 29  ARG C NE  1 
ATOM   2508 C  CZ  . ARG C  3  29  ? 25.218 29.839  -29.968 1.00 62.34  ? 29  ARG C CZ  1 
ATOM   2509 N  NH1 . ARG C  3  29  ? 24.981 30.412  -31.148 1.00 62.94  ? 29  ARG C NH1 1 
ATOM   2510 N  NH2 . ARG C  3  29  ? 26.386 29.251  -29.733 1.00 60.54  ? 29  ARG C NH2 1 
ATOM   2511 N  N   . LEU C  3  30  ? 18.126 30.000  -28.286 1.00 56.91  ? 30  LEU C N   1 
ATOM   2512 C  CA  . LEU C  3  30  ? 16.808 29.896  -28.936 1.00 57.43  ? 30  LEU C CA  1 
ATOM   2513 C  C   . LEU C  3  30  ? 15.670 30.144  -27.882 1.00 56.12  ? 30  LEU C C   1 
ATOM   2514 O  O   . LEU C  3  30  ? 14.738 30.950  -28.077 1.00 55.74  ? 30  LEU C O   1 
ATOM   2515 C  CB  . LEU C  3  30  ? 16.661 28.472  -29.632 1.00 59.02  ? 30  LEU C CB  1 
ATOM   2516 C  CG  . LEU C  3  30  ? 15.696 27.889  -30.623 1.00 60.93  ? 30  LEU C CG  1 
ATOM   2517 C  CD1 . LEU C  3  30  ? 14.892 29.087  -31.219 1.00 60.36  ? 30  LEU C CD1 1 
ATOM   2518 C  CD2 . LEU C  3  30  ? 16.697 27.398  -31.712 1.00 56.88  ? 30  LEU C CD2 1 
ATOM   2519 N  N   . ALA C  3  31  ? 15.742 29.390  -26.794 1.00 54.23  ? 31  ALA C N   1 
ATOM   2520 C  CA  . ALA C  3  31  ? 14.745 29.456  -25.750 1.00 53.08  ? 31  ALA C CA  1 
ATOM   2521 C  C   . ALA C  3  31  ? 14.663 30.855  -25.165 1.00 53.02  ? 31  ALA C C   1 
ATOM   2522 O  O   . ALA C  3  31  ? 13.586 31.364  -24.885 1.00 51.49  ? 31  ALA C O   1 
ATOM   2523 C  CB  . ALA C  3  31  ? 15.086 28.464  -24.679 1.00 54.95  ? 31  ALA C CB  1 
ATOM   2524 N  N   . ILE C  3  32  ? 15.817 31.472  -24.953 1.00 53.60  ? 32  ILE C N   1 
ATOM   2525 C  CA  . ILE C  3  32  ? 15.854 32.807  -24.367 1.00 54.88  ? 32  ILE C CA  1 
ATOM   2526 C  C   . ILE C  3  32  ? 15.223 33.845  -25.295 1.00 55.66  ? 32  ILE C C   1 
ATOM   2527 O  O   . ILE C  3  32  ? 14.427 34.688  -24.872 1.00 53.62  ? 32  ILE C O   1 
ATOM   2528 C  CB  . ILE C  3  32  ? 17.303 33.210  -24.060 1.00 54.59  ? 32  ILE C CB  1 
ATOM   2529 C  CG1 . ILE C  3  32  ? 17.860 32.279  -22.988 1.00 54.20  ? 32  ILE C CG1 1 
ATOM   2530 C  CG2 . ILE C  3  32  ? 17.370 34.672  -23.652 1.00 54.92  ? 32  ILE C CG2 1 
ATOM   2531 C  CD1 . ILE C  3  32  ? 19.320 32.464  -22.745 1.00 53.78  ? 32  ILE C CD1 1 
ATOM   2532 N  N   . ALA C  3  33  ? 15.569 33.747  -26.573 1.00 56.61  ? 33  ALA C N   1 
ATOM   2533 C  CA  . ALA C  3  33  ? 15.050 34.654  -27.586 1.00 58.35  ? 33  ALA C CA  1 
ATOM   2534 C  C   . ALA C  3  33  ? 13.537 34.541  -27.727 1.00 58.73  ? 33  ALA C C   1 
ATOM   2535 O  O   . ALA C  3  33  ? 12.810 35.512  -27.490 1.00 58.98  ? 33  ALA C O   1 
ATOM   2536 C  CB  . ALA C  3  33  ? 15.724 34.375  -28.923 1.00 57.86  ? 33  ALA C CB  1 
ATOM   2537 N  N   . GLN C  3  34  ? 13.069 33.359  -28.115 1.00 59.35  ? 34  GLN C N   1 
ATOM   2538 C  CA  . GLN C  3  34  ? 11.639 33.130  -28.263 1.00 61.96  ? 34  GLN C CA  1 
ATOM   2539 C  C   . GLN C  3  34  ? 10.878 33.730  -27.074 1.00 63.42  ? 34  GLN C C   1 
ATOM   2540 O  O   . GLN C  3  34  ? 9.911  34.477  -27.254 1.00 65.53  ? 34  GLN C O   1 
ATOM   2541 C  CB  . GLN C  3  34  ? 11.348 31.631  -28.351 1.00 60.91  ? 34  GLN C CB  1 
ATOM   2542 C  CG  . GLN C  3  34  ? 12.068 30.956  -29.477 1.00 61.45  ? 34  GLN C CG  1 
ATOM   2543 C  CD  . GLN C  3  34  ? 11.749 29.476  -29.569 1.00 61.88  ? 34  GLN C CD  1 
ATOM   2544 O  OE1 . GLN C  3  34  ? 12.006 28.715  -28.637 1.00 63.79  ? 34  GLN C OE1 1 
ATOM   2545 N  NE2 . GLN C  3  34  ? 11.185 29.062  -30.698 1.00 65.42  ? 34  GLN C NE2 1 
ATOM   2546 N  N   . ALA C  3  35  ? 11.322 33.410  -25.865 1.00 63.15  ? 35  ALA C N   1 
ATOM   2547 C  CA  . ALA C  3  35  ? 10.673 33.911  -24.662 1.00 63.79  ? 35  ALA C CA  1 
ATOM   2548 C  C   . ALA C  3  35  ? 10.679 35.428  -24.612 1.00 65.10  ? 35  ALA C C   1 
ATOM   2549 O  O   . ALA C  3  35  ? 9.745  36.044  -24.089 1.00 64.08  ? 35  ALA C O   1 
ATOM   2550 C  CB  . ALA C  3  35  ? 11.358 33.352  -23.429 1.00 64.78  ? 35  ALA C CB  1 
ATOM   2551 N  N   . VAL C  3  36  ? 11.742 36.035  -25.130 1.00 66.72  ? 36  VAL C N   1 
ATOM   2552 C  CA  . VAL C  3  36  ? 11.837 37.490  -25.139 1.00 69.22  ? 36  VAL C CA  1 
ATOM   2553 C  C   . VAL C  3  36  ? 10.795 38.065  -26.096 1.00 70.80  ? 36  VAL C C   1 
ATOM   2554 O  O   . VAL C  3  36  ? 10.119 39.047  -25.773 1.00 70.30  ? 36  VAL C O   1 
ATOM   2555 C  CB  . VAL C  3  36  ? 13.242 37.973  -25.579 1.00 69.93  ? 36  VAL C CB  1 
ATOM   2556 C  CG1 . VAL C  3  36  ? 13.195 39.442  -25.982 1.00 69.93  ? 36  VAL C CG1 1 
ATOM   2557 C  CG2 . VAL C  3  36  ? 14.235 37.801  -24.444 1.00 69.14  ? 36  VAL C CG2 1 
ATOM   2558 N  N   . PHE C  3  37  ? 10.665 37.455  -27.272 1.00 71.93  ? 37  PHE C N   1 
ATOM   2559 C  CA  . PHE C  3  37  ? 9.688  37.925  -28.234 1.00 73.22  ? 37  PHE C CA  1 
ATOM   2560 C  C   . PHE C  3  37  ? 8.265  37.658  -27.757 1.00 74.68  ? 37  PHE C C   1 
ATOM   2561 O  O   . PHE C  3  37  ? 7.456  38.581  -27.792 1.00 74.43  ? 37  PHE C O   1 
ATOM   2562 C  CB  . PHE C  3  37  ? 9.964  37.330  -29.616 1.00 72.95  ? 37  PHE C CB  1 
ATOM   2563 C  CG  . PHE C  3  37  ? 11.112 38.001  -30.321 1.00 74.27  ? 37  PHE C CG  1 
ATOM   2564 C  CD1 . PHE C  3  37  ? 11.137 39.395  -30.453 1.00 73.97  ? 37  PHE C CD1 1 
ATOM   2565 C  CD2 . PHE C  3  37  ? 12.195 37.267  -30.802 1.00 75.50  ? 37  PHE C CD2 1 
ATOM   2566 C  CE1 . PHE C  3  37  ? 12.220 40.050  -31.044 1.00 71.58  ? 37  PHE C CE1 1 
ATOM   2567 C  CE2 . PHE C  3  37  ? 13.291 37.916  -31.401 1.00 74.67  ? 37  PHE C CE2 1 
ATOM   2568 C  CZ  . PHE C  3  37  ? 13.297 39.311  -31.518 1.00 73.38  ? 37  PHE C CZ  1 
ATOM   2569 N  N   . LYS C  3  38  ? 7.957  36.436  -27.293 1.00 75.40  ? 38  LYS C N   1 
ATOM   2570 C  CA  . LYS C  3  38  ? 6.615  36.156  -26.782 1.00 76.69  ? 38  LYS C CA  1 
ATOM   2571 C  C   . LYS C  3  38  ? 6.245  37.331  -25.873 1.00 77.60  ? 38  LYS C C   1 
ATOM   2572 O  O   . LYS C  3  38  ? 5.212  37.971  -26.038 1.00 78.92  ? 38  LYS C O   1 
ATOM   2573 C  CB  . LYS C  3  38  ? 6.572  34.878  -25.924 1.00 76.95  ? 38  LYS C CB  1 
ATOM   2574 C  CG  . LYS C  3  38  ? 6.619  33.552  -26.666 1.00 78.79  ? 38  LYS C CG  1 
ATOM   2575 C  CD  . LYS C  3  38  ? 6.296  32.417  -25.686 1.00 79.40  ? 38  LYS C CD  1 
ATOM   2576 C  CE  . LYS C  3  38  ? 6.175  31.052  -26.356 1.00 78.70  ? 38  LYS C CE  1 
ATOM   2577 N  NZ  . LYS C  3  38  ? 7.492  30.487  -26.742 1.00 78.14  ? 38  LYS C NZ  1 
ATOM   2578 N  N   . ASP C  3  39  ? 7.133  37.641  -24.933 1.00 78.01  ? 39  ASP C N   1 
ATOM   2579 C  CA  . ASP C  3  39  ? 6.888  38.695  -23.952 1.00 78.68  ? 39  ASP C CA  1 
ATOM   2580 C  C   . ASP C  3  39  ? 6.679  40.045  -24.624 1.00 79.82  ? 39  ASP C C   1 
ATOM   2581 O  O   . ASP C  3  39  ? 5.787  40.836  -24.230 1.00 79.86  ? 39  ASP C O   1 
ATOM   2582 C  CB  . ASP C  3  39  ? 8.072  38.803  -22.988 1.00 78.09  ? 39  ASP C CB  1 
ATOM   2583 C  CG  . ASP C  3  39  ? 7.844  39.837  -21.882 1.00 78.17  ? 39  ASP C CG  1 
ATOM   2584 O  OD1 . ASP C  3  39  ? 7.645  39.443  -20.705 1.00 76.36  ? 39  ASP C OD1 1 
ATOM   2585 O  OD2 . ASP C  3  39  ? 7.868  41.050  -22.196 1.00 79.65  ? 39  ASP C OD2 1 
ATOM   2586 N  N   . LEU C  3  40  ? 7.510  40.328  -25.636 1.00 80.26  ? 40  LEU C N   1 
ATOM   2587 C  CA  . LEU C  3  40  ? 7.344  41.624  -26.300 1.00 80.32  ? 40  LEU C CA  1 
ATOM   2588 C  C   . LEU C  3  40  ? 5.964  41.654  -27.004 1.00 80.90  ? 40  LEU C C   1 
ATOM   2589 O  O   . LEU C  3  40  ? 5.179  42.593  -26.841 1.00 80.40  ? 40  LEU C O   1 
ATOM   2590 C  CB  . LEU C  3  40  ? 8.458  41.975  -27.351 1.00 79.26  ? 40  LEU C CB  1 
ATOM   2591 C  CG  . LEU C  3  40  ? 8.225  43.225  -28.122 1.00 77.90  ? 40  LEU C CG  1 
ATOM   2592 C  CD1 . LEU C  3  40  ? 7.735  44.230  -27.063 1.00 77.41  ? 40  LEU C CD1 1 
ATOM   2593 C  CD2 . LEU C  3  40  ? 9.584  43.696  -28.615 1.00 75.67  ? 40  LEU C CD2 1 
ATOM   2594 N  N   . PHE C  3  41  ? 5.660  40.606  -27.765 1.00 81.10  ? 41  PHE C N   1 
ATOM   2595 C  CA  . PHE C  3  41  ? 4.379  40.514  -28.458 1.00 81.06  ? 41  PHE C CA  1 
ATOM   2596 C  C   . PHE C  3  41  ? 3.217  40.716  -27.475 1.00 83.60  ? 41  PHE C C   1 
ATOM   2597 O  O   . PHE C  3  41  ? 2.371  41.583  -27.676 1.00 83.27  ? 41  PHE C O   1 
ATOM   2598 C  CB  . PHE C  3  41  ? 4.251  39.155  -29.155 1.00 77.11  ? 41  PHE C CB  1 
ATOM   2599 C  CG  . PHE C  3  41  ? 5.255  38.936  -30.253 1.00 73.59  ? 41  PHE C CG  1 
ATOM   2600 C  CD1 . PHE C  3  41  ? 6.051  39.979  -30.713 1.00 71.33  ? 41  PHE C CD1 1 
ATOM   2601 C  CD2 . PHE C  3  41  ? 5.409  37.676  -30.825 1.00 73.24  ? 41  PHE C CD2 1 
ATOM   2602 C  CE1 . PHE C  3  41  ? 6.994  39.766  -31.731 1.00 71.88  ? 41  PHE C CE1 1 
ATOM   2603 C  CE2 . PHE C  3  41  ? 6.348  37.447  -31.843 1.00 72.98  ? 41  PHE C CE2 1 
ATOM   2604 C  CZ  . PHE C  3  41  ? 7.145  38.498  -32.297 1.00 71.55  ? 41  PHE C CZ  1 
ATOM   2605 N  N   . ALA C  3  42  ? 3.187  39.936  -26.398 1.00 86.58  ? 42  ALA C N   1 
ATOM   2606 C  CA  . ALA C  3  42  ? 2.112  40.052  -25.418 1.00 89.77  ? 42  ALA C CA  1 
ATOM   2607 C  C   . ALA C  3  42  ? 2.005  41.444  -24.796 1.00 92.18  ? 42  ALA C C   1 
ATOM   2608 O  O   . ALA C  3  42  ? 0.980  41.792  -24.210 1.00 93.09  ? 42  ALA C O   1 
ATOM   2609 C  CB  . ALA C  3  42  ? 2.284  39.011  -24.332 1.00 88.89  ? 42  ALA C CB  1 
ATOM   2610 N  N   . HIS C  3  43  ? 3.056  42.249  -24.933 1.00 94.84  ? 43  HIS C N   1 
ATOM   2611 C  CA  . HIS C  3  43  ? 3.050  43.607  -24.385 1.00 97.53  ? 43  HIS C CA  1 
ATOM   2612 C  C   . HIS C  3  43  ? 2.911  44.643  -25.497 1.00 99.34  ? 43  HIS C C   1 
ATOM   2613 O  O   . HIS C  3  43  ? 2.626  45.818  -25.246 1.00 98.67  ? 43  HIS C O   1 
ATOM   2614 C  CB  . HIS C  3  43  ? 4.343  43.885  -23.613 1.00 97.94  ? 43  HIS C CB  1 
ATOM   2615 C  CG  . HIS C  3  43  ? 4.464  43.130  -22.322 1.00 98.69  ? 43  HIS C CG  1 
ATOM   2616 N  ND1 . HIS C  3  43  ? 4.709  41.774  -22.270 1.00 98.16  ? 43  HIS C ND1 1 
ATOM   2617 C  CD2 . HIS C  3  43  ? 4.392  43.548  -21.036 1.00 98.42  ? 43  HIS C CD2 1 
ATOM   2618 C  CE1 . HIS C  3  43  ? 4.785  41.392  -21.007 1.00 98.04  ? 43  HIS C CE1 1 
ATOM   2619 N  NE2 . HIS C  3  43  ? 4.597  42.450  -20.238 1.00 97.73  ? 43  HIS C NE2 1 
ATOM   2620 N  N   . VAL C  3  44  ? 3.128  44.192  -26.726 1.00 101.94 ? 44  VAL C N   1 
ATOM   2621 C  CA  . VAL C  3  44  ? 3.052  45.047  -27.902 1.00 104.24 ? 44  VAL C CA  1 
ATOM   2622 C  C   . VAL C  3  44  ? 2.510  44.180  -29.031 1.00 105.78 ? 44  VAL C C   1 
ATOM   2623 O  O   . VAL C  3  44  ? 3.272  43.638  -29.832 1.00 106.33 ? 44  VAL C O   1 
ATOM   2624 C  CB  . VAL C  3  44  ? 4.453  45.561  -28.289 1.00 104.85 ? 44  VAL C CB  1 
ATOM   2625 C  CG1 . VAL C  3  44  ? 4.348  46.636  -29.333 1.00 104.91 ? 44  VAL C CG1 1 
ATOM   2626 C  CG2 . VAL C  3  44  ? 5.166  46.089  -27.061 1.00 106.19 ? 44  VAL C CG2 1 
ATOM   2627 N  N   . PRO C  3  45  ? 1.175  44.042  -29.110 1.00 106.81 ? 45  PRO C N   1 
ATOM   2628 C  CA  . PRO C  3  45  ? 0.563  43.220  -30.153 1.00 107.17 ? 45  PRO C CA  1 
ATOM   2629 C  C   . PRO C  3  45  ? 0.987  43.608  -31.564 1.00 107.67 ? 45  PRO C C   1 
ATOM   2630 O  O   . PRO C  3  45  ? 1.413  42.757  -32.353 1.00 108.01 ? 45  PRO C O   1 
ATOM   2631 C  CB  . PRO C  3  45  ? -0.931 43.423  -29.908 1.00 107.12 ? 45  PRO C CB  1 
ATOM   2632 C  CG  . PRO C  3  45  ? -0.991 44.827  -29.397 1.00 106.25 ? 45  PRO C CG  1 
ATOM   2633 C  CD  . PRO C  3  45  ? 0.155  44.853  -28.418 1.00 106.85 ? 45  PRO C CD  1 
ATOM   2634 N  N   . ASP C  3  46  ? 0.885  44.897  -31.863 1.00 107.89 ? 46  ASP C N   1 
ATOM   2635 C  CA  . ASP C  3  46  ? 1.235  45.437  -33.176 1.00 107.95 ? 46  ASP C CA  1 
ATOM   2636 C  C   . ASP C  3  46  ? 2.651  45.103  -33.643 1.00 106.68 ? 46  ASP C C   1 
ATOM   2637 O  O   . ASP C  3  46  ? 2.969  45.236  -34.826 1.00 106.42 ? 46  ASP C O   1 
ATOM   2638 C  CB  . ASP C  3  46  ? 1.048  46.957  -33.163 1.00 109.40 ? 46  ASP C CB  1 
ATOM   2639 C  CG  . ASP C  3  46  ? 1.584  47.590  -31.893 1.00 110.25 ? 46  ASP C CG  1 
ATOM   2640 O  OD1 . ASP C  3  46  ? 2.665  47.165  -31.443 1.00 110.83 ? 46  ASP C OD1 1 
ATOM   2641 O  OD2 . ASP C  3  46  ? 0.938  48.509  -31.347 1.00 110.46 ? 46  ASP C OD2 1 
ATOM   2642 N  N   . ALA C  3  47  ? 3.497  44.666  -32.717 1.00 105.23 ? 47  ALA C N   1 
ATOM   2643 C  CA  . ALA C  3  47  ? 4.883  44.346  -33.046 1.00 103.43 ? 47  ALA C CA  1 
ATOM   2644 C  C   . ALA C  3  47  ? 5.079  43.075  -33.874 1.00 102.26 ? 47  ALA C C   1 
ATOM   2645 O  O   . ALA C  3  47  ? 6.012  42.994  -34.677 1.00 102.44 ? 47  ALA C O   1 
ATOM   2646 C  CB  . ALA C  3  47  ? 5.702  44.263  -31.772 1.00 102.71 ? 47  ALA C CB  1 
ATOM   2647 N  N   . VAL C  3  48  ? 4.203  42.093  -33.692 1.00 100.28 ? 48  VAL C N   1 
ATOM   2648 C  CA  . VAL C  3  48  ? 4.324  40.827  -34.411 1.00 98.96  ? 48  VAL C CA  1 
ATOM   2649 C  C   . VAL C  3  48  ? 4.367  41.005  -35.924 1.00 99.41  ? 48  VAL C C   1 
ATOM   2650 O  O   . VAL C  3  48  ? 5.047  40.255  -36.633 1.00 98.92  ? 48  VAL C O   1 
ATOM   2651 C  CB  . VAL C  3  48  ? 3.159  39.879  -34.071 1.00 98.32  ? 48  VAL C CB  1 
ATOM   2652 C  CG1 . VAL C  3  48  ? 3.517  38.442  -34.467 1.00 96.83  ? 48  VAL C CG1 1 
ATOM   2653 C  CG2 . VAL C  3  48  ? 2.823  39.986  -32.598 1.00 97.49  ? 48  VAL C CG2 1 
ATOM   2654 N  N   . GLY C  3  49  ? 3.637  42.001  -36.416 1.00 100.02 ? 49  GLY C N   1 
ATOM   2655 C  CA  . GLY C  3  49  ? 3.593  42.257  -37.847 1.00 99.86  ? 49  GLY C CA  1 
ATOM   2656 C  C   . GLY C  3  49  ? 4.936  42.577  -38.474 1.00 99.36  ? 49  GLY C C   1 
ATOM   2657 O  O   . GLY C  3  49  ? 5.198  42.222  -39.625 1.00 99.34  ? 49  GLY C O   1 
ATOM   2658 N  N   . LEU C  3  50  ? 5.790  43.248  -37.711 1.00 99.09  ? 50  LEU C N   1 
ATOM   2659 C  CA  . LEU C  3  50  ? 7.115  43.625  -38.185 1.00 98.42  ? 50  LEU C CA  1 
ATOM   2660 C  C   . LEU C  3  50  ? 7.974  42.407  -38.513 1.00 98.41  ? 50  LEU C C   1 
ATOM   2661 O  O   . LEU C  3  50  ? 9.011  42.536  -39.164 1.00 97.92  ? 50  LEU C O   1 
ATOM   2662 C  CB  . LEU C  3  50  ? 7.814  44.464  -37.118 1.00 97.25  ? 50  LEU C CB  1 
ATOM   2663 C  CG  . LEU C  3  50  ? 7.007  45.675  -36.659 1.00 96.87  ? 50  LEU C CG  1 
ATOM   2664 C  CD1 . LEU C  3  50  ? 7.590  46.240  -35.383 1.00 97.03  ? 50  LEU C CD1 1 
ATOM   2665 C  CD2 . LEU C  3  50  ? 7.011  46.719  -37.762 1.00 97.34  ? 50  LEU C CD2 1 
ATOM   2666 N  N   . PHE C  3  51  ? 7.532  41.228  -38.083 1.00 98.69  ? 51  PHE C N   1 
ATOM   2667 C  CA  . PHE C  3  51  ? 8.299  40.001  -38.298 1.00 99.68  ? 51  PHE C CA  1 
ATOM   2668 C  C   . PHE C  3  51  ? 7.633  38.977  -39.209 1.00 101.63 ? 51  PHE C C   1 
ATOM   2669 O  O   . PHE C  3  51  ? 7.880  37.773  -39.095 1.00 100.94 ? 51  PHE C O   1 
ATOM   2670 C  CB  . PHE C  3  51  ? 8.606  39.367  -36.936 1.00 96.73  ? 51  PHE C CB  1 
ATOM   2671 C  CG  . PHE C  3  51  ? 9.286  40.314  -35.980 1.00 93.16  ? 51  PHE C CG  1 
ATOM   2672 C  CD1 . PHE C  3  51  ? 10.679 40.425  -35.961 1.00 91.20  ? 51  PHE C CD1 1 
ATOM   2673 C  CD2 . PHE C  3  51  ? 8.531  41.151  -35.155 1.00 90.41  ? 51  PHE C CD2 1 
ATOM   2674 C  CE1 . PHE C  3  51  ? 11.307 41.358  -35.140 1.00 88.99  ? 51  PHE C CE1 1 
ATOM   2675 C  CE2 . PHE C  3  51  ? 9.149  42.089  -34.332 1.00 87.96  ? 51  PHE C CE2 1 
ATOM   2676 C  CZ  . PHE C  3  51  ? 10.539 42.195  -34.324 1.00 88.27  ? 51  PHE C CZ  1 
ATOM   2677 N  N   . ASP C  3  52  ? 6.805  39.459  -40.129 1.00 104.73 ? 52  ASP C N   1 
ATOM   2678 C  CA  . ASP C  3  52  ? 6.115  38.566  -41.042 1.00 107.11 ? 52  ASP C CA  1 
ATOM   2679 C  C   . ASP C  3  52  ? 7.067  37.777  -41.933 1.00 107.02 ? 52  ASP C C   1 
ATOM   2680 O  O   . ASP C  3  52  ? 6.795  36.625  -42.271 1.00 107.03 ? 52  ASP C O   1 
ATOM   2681 C  CB  . ASP C  3  52  ? 5.118  39.347  -41.900 1.00 109.85 ? 52  ASP C CB  1 
ATOM   2682 C  CG  . ASP C  3  52  ? 3.894  39.774  -41.119 1.00 113.30 ? 52  ASP C CG  1 
ATOM   2683 O  OD1 . ASP C  3  52  ? 3.290  38.908  -40.444 1.00 115.23 ? 52  ASP C OD1 1 
ATOM   2684 O  OD2 . ASP C  3  52  ? 3.529  40.968  -41.182 1.00 115.04 ? 52  ASP C OD2 1 
ATOM   2685 N  N   . ARG C  3  53  ? 8.188  38.384  -42.307 1.00 106.89 ? 53  ARG C N   1 
ATOM   2686 C  CA  . ARG C  3  53  ? 9.147  37.698  -43.166 1.00 107.63 ? 53  ARG C CA  1 
ATOM   2687 C  C   . ARG C  3  53  ? 9.769  36.498  -42.451 1.00 110.08 ? 53  ARG C C   1 
ATOM   2688 O  O   . ARG C  3  53  ? 10.144 35.505  -43.085 1.00 109.84 ? 53  ARG C O   1 
ATOM   2689 C  CB  . ARG C  3  53  ? 10.255 38.658  -43.609 1.00 103.97 ? 53  ARG C CB  1 
ATOM   2690 C  CG  . ARG C  3  53  ? 11.149 38.083  -44.699 1.00 99.09  ? 53  ARG C CG  1 
ATOM   2691 C  CD  . ARG C  3  53  ? 12.386 38.918  -44.889 1.00 94.83  ? 53  ARG C CD  1 
ATOM   2692 N  NE  . ARG C  3  53  ? 13.414 38.597  -43.903 1.00 91.58  ? 53  ARG C NE  1 
ATOM   2693 C  CZ  . ARG C  3  53  ? 14.210 37.532  -43.961 1.00 90.51  ? 53  ARG C CZ  1 
ATOM   2694 N  NH1 . ARG C  3  53  ? 15.116 37.324  -43.015 1.00 89.82  ? 53  ARG C NH1 1 
ATOM   2695 N  NH2 . ARG C  3  53  ? 14.112 36.677  -44.968 1.00 90.46  ? 53  ARG C NH2 1 
ATOM   2696 N  N   . VAL C  3  54  ? 9.876  36.601  -41.128 1.00 112.79 ? 54  VAL C N   1 
ATOM   2697 C  CA  . VAL C  3  54  ? 10.461 35.544  -40.307 1.00 115.21 ? 54  VAL C CA  1 
ATOM   2698 C  C   . VAL C  3  54  ? 9.394  34.735  -39.567 1.00 116.38 ? 54  VAL C C   1 
ATOM   2699 O  O   . VAL C  3  54  ? 9.703  33.992  -38.632 1.00 116.46 ? 54  VAL C O   1 
ATOM   2700 C  CB  . VAL C  3  54  ? 11.465 36.139  -39.284 1.00 115.79 ? 54  VAL C CB  1 
ATOM   2701 C  CG1 . VAL C  3  54  ? 12.659 36.746  -40.017 1.00 115.59 ? 54  VAL C CG1 1 
ATOM   2702 C  CG2 . VAL C  3  54  ? 10.777 37.201  -38.431 1.00 115.89 ? 54  VAL C CG2 1 
ATOM   2703 N  N   . HIS C  3  55  ? 8.144  34.881  -39.999 1.00 117.77 ? 55  HIS C N   1 
ATOM   2704 C  CA  . HIS C  3  55  ? 7.016  34.170  -39.398 1.00 118.99 ? 55  HIS C CA  1 
ATOM   2705 C  C   . HIS C  3  55  ? 6.858  34.501  -37.912 1.00 117.78 ? 55  HIS C C   1 
ATOM   2706 O  O   . HIS C  3  55  ? 6.888  33.609  -37.059 1.00 118.22 ? 55  HIS C O   1 
ATOM   2707 C  CB  . HIS C  3  55  ? 7.196  32.659  -39.575 1.00 122.52 ? 55  HIS C CB  1 
ATOM   2708 C  CG  . HIS C  3  55  ? 7.115  32.194  -40.999 1.00 125.88 ? 55  HIS C CG  1 
ATOM   2709 N  ND1 . HIS C  3  55  ? 7.726  32.860  -42.039 1.00 127.23 ? 55  HIS C ND1 1 
ATOM   2710 C  CD2 . HIS C  3  55  ? 6.540  31.094  -41.545 1.00 127.07 ? 55  HIS C CD2 1 
ATOM   2711 C  CE1 . HIS C  3  55  ? 7.534  32.194  -43.163 1.00 127.94 ? 55  HIS C CE1 1 
ATOM   2712 N  NE2 . HIS C  3  55  ? 6.817  31.117  -42.891 1.00 128.23 ? 55  HIS C NE2 1 
ATOM   2713 N  N   . GLY C  3  56  ? 6.681  35.788  -37.614 1.00 115.62 ? 56  GLY C N   1 
ATOM   2714 C  CA  . GLY C  3  56  ? 6.522  36.231  -36.238 1.00 112.89 ? 56  GLY C CA  1 
ATOM   2715 C  C   . GLY C  3  56  ? 5.266  35.731  -35.549 1.00 111.24 ? 56  GLY C C   1 
ATOM   2716 O  O   . GLY C  3  56  ? 5.129  35.840  -34.329 1.00 111.98 ? 56  GLY C O   1 
ATOM   2717 N  N   . THR C  3  57  ? 4.337  35.192  -36.329 1.00 109.23 ? 57  THR C N   1 
ATOM   2718 C  CA  . THR C  3  57  ? 3.096  34.662  -35.778 1.00 106.93 ? 57  THR C CA  1 
ATOM   2719 C  C   . THR C  3  57  ? 3.287  33.191  -35.423 1.00 105.40 ? 57  THR C C   1 
ATOM   2720 O  O   . THR C  3  57  ? 2.431  32.585  -34.776 1.00 105.02 ? 57  THR C O   1 
ATOM   2721 C  CB  . THR C  3  57  ? 1.936  34.778  -36.791 1.00 107.00 ? 57  THR C CB  1 
ATOM   2722 O  OG1 . THR C  3  57  ? 2.262  34.049  -37.985 1.00 106.21 ? 57  THR C OG1 1 
ATOM   2723 C  CG2 . THR C  3  57  ? 1.678  36.240  -37.136 1.00 106.51 ? 57  THR C CG2 1 
ATOM   2724 N  N   . GLU C  3  58  ? 4.417  32.627  -35.851 1.00 103.30 ? 58  GLU C N   1 
ATOM   2725 C  CA  . GLU C  3  58  ? 4.741  31.222  -35.598 1.00 101.40 ? 58  GLU C CA  1 
ATOM   2726 C  C   . GLU C  3  58  ? 6.133  31.078  -34.993 1.00 99.82  ? 58  GLU C C   1 
ATOM   2727 O  O   . GLU C  3  58  ? 7.062  30.593  -35.636 1.00 98.88  ? 58  GLU C O   1 
ATOM   2728 C  CB  . GLU C  3  58  ? 4.655  30.416  -36.899 1.00 101.05 ? 58  GLU C CB  1 
ATOM   2729 C  CG  . GLU C  3  58  ? 4.860  28.916  -36.720 1.00 100.98 ? 58  GLU C CG  1 
ATOM   2730 C  CD  . GLU C  3  58  ? 4.442  28.117  -37.944 1.00 101.29 ? 58  GLU C CD  1 
ATOM   2731 O  OE1 . GLU C  3  58  ? 4.672  26.887  -37.965 1.00 100.53 ? 58  GLU C OE1 1 
ATOM   2732 O  OE2 . GLU C  3  58  ? 3.879  28.718  -38.883 1.00 101.52 ? 58  GLU C OE2 1 
ATOM   2733 N  N   . ILE C  3  59  ? 6.247  31.494  -33.736 1.00 98.33  ? 59  ILE C N   1 
ATOM   2734 C  CA  . ILE C  3  59  ? 7.496  31.461  -32.996 1.00 96.57  ? 59  ILE C CA  1 
ATOM   2735 C  C   . ILE C  3  59  ? 8.250  30.137  -33.063 1.00 96.44  ? 59  ILE C C   1 
ATOM   2736 O  O   . ILE C  3  59  ? 9.457  30.099  -32.794 1.00 96.18  ? 59  ILE C O   1 
ATOM   2737 C  CB  . ILE C  3  59  ? 7.240  31.832  -31.520 1.00 95.12  ? 59  ILE C CB  1 
ATOM   2738 C  CG1 . ILE C  3  59  ? 6.564  33.201  -31.454 1.00 94.55  ? 59  ILE C CG1 1 
ATOM   2739 C  CG2 . ILE C  3  59  ? 8.540  31.867  -30.741 1.00 94.07  ? 59  ILE C CG2 1 
ATOM   2740 C  CD1 . ILE C  3  59  ? 6.089  33.576  -30.072 1.00 95.87  ? 59  ILE C CD1 1 
ATOM   2741 N  N   . ASP C  3  60  ? 7.574  29.053  -33.438 1.00 95.56  ? 60  ASP C N   1 
ATOM   2742 C  CA  . ASP C  3  60  ? 8.269  27.773  -33.484 1.00 95.55  ? 60  ASP C CA  1 
ATOM   2743 C  C   . ASP C  3  60  ? 8.617  27.273  -34.878 1.00 95.68  ? 60  ASP C C   1 
ATOM   2744 O  O   . ASP C  3  60  ? 9.054  26.133  -35.048 1.00 94.80  ? 60  ASP C O   1 
ATOM   2745 C  CB  . ASP C  3  60  ? 7.474  26.710  -32.728 1.00 95.54  ? 60  ASP C CB  1 
ATOM   2746 C  CG  . ASP C  3  60  ? 8.378  25.746  -31.971 1.00 95.12  ? 60  ASP C CG  1 
ATOM   2747 O  OD1 . ASP C  3  60  ? 8.898  24.792  -32.591 1.00 94.10  ? 60  ASP C OD1 1 
ATOM   2748 O  OD2 . ASP C  3  60  ? 8.583  25.956  -30.754 1.00 94.23  ? 60  ASP C OD2 1 
ATOM   2749 N  N   . SER C  3  61  ? 8.438  28.141  -35.869 1.00 96.37  ? 61  SER C N   1 
ATOM   2750 C  CA  . SER C  3  61  ? 8.754  27.810  -37.256 1.00 97.16  ? 61  SER C CA  1 
ATOM   2751 C  C   . SER C  3  61  ? 10.260 27.888  -37.465 1.00 97.50  ? 61  SER C C   1 
ATOM   2752 O  O   . SER C  3  61  ? 10.943 28.616  -36.759 1.00 97.65  ? 61  SER C O   1 
ATOM   2753 C  CB  . SER C  3  61  ? 8.082  28.807  -38.190 1.00 97.44  ? 61  SER C CB  1 
ATOM   2754 O  OG  . SER C  3  61  ? 8.583  30.108  -37.940 1.00 97.50  ? 61  SER C OG  1 
ATOM   2755 N  N   . SER C  3  62  ? 10.781 27.150  -38.438 1.00 98.22  ? 62  SER C N   1 
ATOM   2756 C  CA  . SER C  3  62  ? 12.216 27.179  -38.697 1.00 99.37  ? 62  SER C CA  1 
ATOM   2757 C  C   . SER C  3  62  ? 12.688 28.586  -39.035 1.00 100.54 ? 62  SER C C   1 
ATOM   2758 O  O   . SER C  3  62  ? 13.839 28.934  -38.786 1.00 100.68 ? 62  SER C O   1 
ATOM   2759 C  CB  . SER C  3  62  ? 12.577 26.239  -39.845 1.00 98.33  ? 62  SER C CB  1 
ATOM   2760 O  OG  . SER C  3  62  ? 12.416 24.890  -39.457 1.00 96.86  ? 62  SER C OG  1 
ATOM   2761 N  N   . GLU C  3  63  ? 11.794 29.397  -39.589 1.00 102.01 ? 63  GLU C N   1 
ATOM   2762 C  CA  . GLU C  3  63  ? 12.148 30.757  -39.970 1.00 103.10 ? 63  GLU C CA  1 
ATOM   2763 C  C   . GLU C  3  63  ? 12.285 31.730  -38.811 1.00 101.09 ? 63  GLU C C   1 
ATOM   2764 O  O   . GLU C  3  63  ? 13.201 32.552  -38.817 1.00 100.95 ? 63  GLU C O   1 
ATOM   2765 C  CB  . GLU C  3  63  ? 11.147 31.319  -40.987 1.00 106.74 ? 63  GLU C CB  1 
ATOM   2766 C  CG  . GLU C  3  63  ? 9.824  30.577  -41.067 1.00 112.05 ? 63  GLU C CG  1 
ATOM   2767 C  CD  . GLU C  3  63  ? 9.927  29.267  -41.833 1.00 114.88 ? 63  GLU C CD  1 
ATOM   2768 O  OE1 . GLU C  3  63  ? 10.375 29.288  -42.998 1.00 116.35 ? 63  GLU C OE1 1 
ATOM   2769 O  OE2 . GLU C  3  63  ? 9.553  28.215  -41.274 1.00 116.75 ? 63  GLU C OE2 1 
ATOM   2770 N  N   . PHE C  3  64  ? 11.391 31.664  -37.827 1.00 98.24  ? 64  PHE C N   1 
ATOM   2771 C  CA  . PHE C  3  64  ? 11.495 32.578  -36.695 1.00 95.00  ? 64  PHE C CA  1 
ATOM   2772 C  C   . PHE C  3  64  ? 12.626 32.134  -35.778 1.00 93.52  ? 64  PHE C C   1 
ATOM   2773 O  O   . PHE C  3  64  ? 13.327 32.961  -35.186 1.00 92.53  ? 64  PHE C O   1 
ATOM   2774 C  CB  . PHE C  3  64  ? 10.196 32.631  -35.889 1.00 92.56  ? 64  PHE C CB  1 
ATOM   2775 C  CG  . PHE C  3  64  ? 10.147 33.770  -34.929 1.00 90.61  ? 64  PHE C CG  1 
ATOM   2776 C  CD1 . PHE C  3  64  ? 10.170 35.072  -35.402 1.00 90.64  ? 64  PHE C CD1 1 
ATOM   2777 C  CD2 . PHE C  3  64  ? 10.082 33.558  -33.566 1.00 91.27  ? 64  PHE C CD2 1 
ATOM   2778 C  CE1 . PHE C  3  64  ? 10.126 36.151  -34.528 1.00 91.06  ? 64  PHE C CE1 1 
ATOM   2779 C  CE2 . PHE C  3  64  ? 10.037 34.632  -32.674 1.00 91.93  ? 64  PHE C CE2 1 
ATOM   2780 C  CZ  . PHE C  3  64  ? 10.058 35.933  -33.161 1.00 91.79  ? 64  PHE C CZ  1 
ATOM   2781 N  N   . LYS C  3  65  ? 12.809 30.826  -35.673 1.00 92.05  ? 65  LYS C N   1 
ATOM   2782 C  CA  . LYS C  3  65  ? 13.861 30.271  -34.845 1.00 90.70  ? 65  LYS C CA  1 
ATOM   2783 C  C   . LYS C  3  65  ? 15.214 30.779  -35.322 1.00 89.50  ? 65  LYS C C   1 
ATOM   2784 O  O   . LYS C  3  65  ? 16.042 31.231  -34.518 1.00 89.99  ? 65  LYS C O   1 
ATOM   2785 C  CB  . LYS C  3  65  ? 13.812 28.731  -34.889 1.00 90.31  ? 65  LYS C CB  1 
ATOM   2786 C  CG  . LYS C  3  65  ? 12.473 28.170  -34.401 1.00 90.15  ? 65  LYS C CG  1 
ATOM   2787 C  CD  . LYS C  3  65  ? 12.609 26.847  -33.652 1.00 88.92  ? 65  LYS C CD  1 
ATOM   2788 C  CE  . LYS C  3  65  ? 13.106 25.718  -34.539 1.00 87.31  ? 65  LYS C CE  1 
ATOM   2789 N  NZ  . LYS C  3  65  ? 13.095 24.444  -33.773 1.00 86.20  ? 65  LYS C NZ  1 
ATOM   2790 N  N   . ALA C  3  66  ? 15.428 30.720  -36.637 1.00 86.85  ? 66  ALA C N   1 
ATOM   2791 C  CA  . ALA C  3  66  ? 16.681 31.180  -37.244 1.00 83.15  ? 66  ALA C CA  1 
ATOM   2792 C  C   . ALA C  3  66  ? 16.860 32.674  -37.034 1.00 80.41  ? 66  ALA C C   1 
ATOM   2793 O  O   . ALA C  3  66  ? 17.984 33.182  -37.026 1.00 79.69  ? 66  ALA C O   1 
ATOM   2794 C  CB  . ALA C  3  66  ? 16.690 30.850  -38.729 1.00 83.54  ? 66  ALA C CB  1 
ATOM   2795 N  N   . HIS C  3  67  ? 15.745 33.375  -36.870 1.00 77.14  ? 67  HIS C N   1 
ATOM   2796 C  CA  . HIS C  3  67  ? 15.778 34.813  -36.652 1.00 74.85  ? 67  HIS C CA  1 
ATOM   2797 C  C   . HIS C  3  67  ? 16.168 35.100  -35.207 1.00 75.68  ? 67  HIS C C   1 
ATOM   2798 O  O   . HIS C  3  67  ? 16.966 36.003  -34.925 1.00 75.83  ? 67  HIS C O   1 
ATOM   2799 C  CB  . HIS C  3  67  ? 14.406 35.428  -36.925 1.00 70.48  ? 67  HIS C CB  1 
ATOM   2800 C  CG  . HIS C  3  67  ? 14.278 36.836  -36.439 1.00 66.01  ? 67  HIS C CG  1 
ATOM   2801 N  ND1 . HIS C  3  67  ? 14.995 37.875  -36.990 1.00 64.61  ? 67  HIS C ND1 1 
ATOM   2802 C  CD2 . HIS C  3  67  ? 13.537 37.373  -35.444 1.00 65.63  ? 67  HIS C CD2 1 
ATOM   2803 C  CE1 . HIS C  3  67  ? 14.696 38.996  -36.355 1.00 63.63  ? 67  HIS C CE1 1 
ATOM   2804 N  NE2 . HIS C  3  67  ? 13.814 38.717  -35.412 1.00 64.04  ? 67  HIS C NE2 1 
ATOM   2805 N  N   . CYS C  3  68  ? 15.584 34.333  -34.288 1.00 75.57  ? 68  CYS C N   1 
ATOM   2806 C  CA  . CYS C  3  68  ? 15.887 34.499  -32.882 1.00 72.97  ? 68  CYS C CA  1 
ATOM   2807 C  C   . CYS C  3  68  ? 17.378 34.203  -32.720 1.00 71.22  ? 68  CYS C C   1 
ATOM   2808 O  O   . CYS C  3  68  ? 18.087 34.948  -32.051 1.00 70.99  ? 68  CYS C O   1 
ATOM   2809 C  CB  . CYS C  3  68  ? 15.003 33.562  -32.040 1.00 73.62  ? 68  CYS C CB  1 
ATOM   2810 S  SG  . CYS C  3  68  ? 13.287 34.159  -31.835 1.00 72.94  ? 68  CYS C SG  1 
ATOM   2811 N  N   . ILE C  3  69  ? 17.861 33.147  -33.369 1.00 69.26  ? 69  ILE C N   1 
ATOM   2812 C  CA  . ILE C  3  69  ? 19.278 32.801  -33.295 1.00 69.28  ? 69  ILE C CA  1 
ATOM   2813 C  C   . ILE C  3  69  ? 20.155 33.953  -33.778 1.00 69.57  ? 69  ILE C C   1 
ATOM   2814 O  O   . ILE C  3  69  ? 21.267 34.132  -33.282 1.00 70.55  ? 69  ILE C O   1 
ATOM   2815 C  CB  . ILE C  3  69  ? 19.588 31.550  -34.132 1.00 67.54  ? 69  ILE C CB  1 
ATOM   2816 C  CG1 . ILE C  3  69  ? 18.851 30.358  -33.530 1.00 68.58  ? 69  ILE C CG1 1 
ATOM   2817 C  CG2 . ILE C  3  69  ? 21.073 31.294  -34.176 1.00 66.41  ? 69  ILE C CG2 1 
ATOM   2818 C  CD1 . ILE C  3  69  ? 19.128 29.038  -34.214 1.00 68.29  ? 69  ILE C CD1 1 
ATOM   2819 N  N   . ARG C  3  70  ? 19.647 34.725  -34.742 1.00 68.99  ? 70  ARG C N   1 
ATOM   2820 C  CA  . ARG C  3  70  ? 20.366 35.876  -35.289 1.00 66.71  ? 70  ARG C CA  1 
ATOM   2821 C  C   . ARG C  3  70  ? 20.310 37.044  -34.318 1.00 63.73  ? 70  ARG C C   1 
ATOM   2822 O  O   . ARG C  3  70  ? 21.288 37.770  -34.160 1.00 62.66  ? 70  ARG C O   1 
ATOM   2823 C  CB  . ARG C  3  70  ? 19.780 36.311  -36.649 1.00 68.73  ? 70  ARG C CB  1 
ATOM   2824 C  CG  . ARG C  3  70  ? 20.235 35.463  -37.845 1.00 70.00  ? 70  ARG C CG  1 
ATOM   2825 C  CD  . ARG C  3  70  ? 19.921 36.123  -39.179 1.00 70.49  ? 70  ARG C CD  1 
ATOM   2826 N  NE  . ARG C  3  70  ? 18.472 36.300  -39.393 1.00 70.89  ? 70  ARG C NE  1 
ATOM   2827 C  CZ  . ARG C  3  70  ? 17.659 35.358  -39.877 1.00 69.97  ? 70  ARG C CZ  1 
ATOM   2828 N  NH1 . ARG C  3  70  ? 18.144 34.170  -40.204 1.00 69.43  ? 70  ARG C NH1 1 
ATOM   2829 N  NH2 . ARG C  3  70  ? 16.365 35.590  -40.033 1.00 69.02  ? 70  ARG C NH2 1 
ATOM   2830 N  N   . VAL C  3  71  ? 19.167 37.236  -33.676 1.00 60.92  ? 71  VAL C N   1 
ATOM   2831 C  CA  . VAL C  3  71  ? 19.070 38.325  -32.719 1.00 60.85  ? 71  VAL C CA  1 
ATOM   2832 C  C   . VAL C  3  71  ? 20.049 38.046  -31.566 1.00 60.45  ? 71  VAL C C   1 
ATOM   2833 O  O   . VAL C  3  71  ? 20.837 38.915  -31.179 1.00 59.21  ? 71  VAL C O   1 
ATOM   2834 C  CB  . VAL C  3  71  ? 17.642 38.467  -32.157 1.00 61.20  ? 71  VAL C CB  1 
ATOM   2835 C  CG1 . VAL C  3  71  ? 17.595 39.624  -31.149 1.00 59.29  ? 71  VAL C CG1 1 
ATOM   2836 C  CG2 . VAL C  3  71  ? 16.663 38.711  -33.294 1.00 60.22  ? 71  VAL C CG2 1 
ATOM   2837 N  N   . VAL C  3  72  ? 20.000 36.819  -31.043 1.00 59.10  ? 72  VAL C N   1 
ATOM   2838 C  CA  . VAL C  3  72  ? 20.866 36.385  -29.949 1.00 57.51  ? 72  VAL C CA  1 
ATOM   2839 C  C   . VAL C  3  72  ? 22.341 36.436  -30.339 1.00 56.89  ? 72  VAL C C   1 
ATOM   2840 O  O   . VAL C  3  72  ? 23.215 36.619  -29.493 1.00 56.34  ? 72  VAL C O   1 
ATOM   2841 C  CB  . VAL C  3  72  ? 20.498 34.953  -29.492 1.00 57.90  ? 72  VAL C CB  1 
ATOM   2842 C  CG1 . VAL C  3  72  ? 21.687 34.283  -28.818 1.00 58.76  ? 72  VAL C CG1 1 
ATOM   2843 C  CG2 . VAL C  3  72  ? 19.329 35.018  -28.515 1.00 55.55  ? 72  VAL C CG2 1 
ATOM   2844 N  N   . ASN C  3  73  ? 22.622 36.263  -31.620 1.00 56.69  ? 73  ASN C N   1 
ATOM   2845 C  CA  . ASN C  3  73  ? 23.995 36.341  -32.066 1.00 56.50  ? 73  ASN C CA  1 
ATOM   2846 C  C   . ASN C  3  73  ? 24.398 37.808  -32.097 1.00 55.19  ? 73  ASN C C   1 
ATOM   2847 O  O   . ASN C  3  73  ? 25.560 38.144  -31.898 1.00 56.19  ? 73  ASN C O   1 
ATOM   2848 C  CB  . ASN C  3  73  ? 24.163 35.746  -33.460 1.00 60.34  ? 73  ASN C CB  1 
ATOM   2849 C  CG  . ASN C  3  73  ? 25.601 35.822  -33.950 1.00 63.57  ? 73  ASN C CG  1 
ATOM   2850 O  OD1 . ASN C  3  73  ? 26.494 35.164  -33.406 1.00 65.21  ? 73  ASN C OD1 1 
ATOM   2851 N  ND2 . ASN C  3  73  ? 25.836 36.633  -34.972 1.00 63.98  ? 73  ASN C ND2 1 
ATOM   2852 N  N   . GLY C  3  74  ? 23.428 38.686  -32.337 1.00 53.67  ? 74  GLY C N   1 
ATOM   2853 C  CA  . GLY C  3  74  ? 23.728 40.101  -32.390 1.00 52.56  ? 74  GLY C CA  1 
ATOM   2854 C  C   . GLY C  3  74  ? 24.011 40.653  -31.014 1.00 51.31  ? 74  GLY C C   1 
ATOM   2855 O  O   . GLY C  3  74  ? 24.930 41.454  -30.836 1.00 50.38  ? 74  GLY C O   1 
ATOM   2856 N  N   . LEU C  3  75  ? 23.210 40.216  -30.043 1.00 49.71  ? 75  LEU C N   1 
ATOM   2857 C  CA  . LEU C  3  75  ? 23.359 40.649  -28.665 1.00 47.15  ? 75  LEU C CA  1 
ATOM   2858 C  C   . LEU C  3  75  ? 24.659 40.086  -28.099 1.00 46.04  ? 75  LEU C C   1 
ATOM   2859 O  O   . LEU C  3  75  ? 25.396 40.777  -27.385 1.00 43.45  ? 75  LEU C O   1 
ATOM   2860 C  CB  . LEU C  3  75  ? 22.166 40.166  -27.840 1.00 44.72  ? 75  LEU C CB  1 
ATOM   2861 C  CG  . LEU C  3  75  ? 22.148 40.799  -26.448 1.00 45.91  ? 75  LEU C CG  1 
ATOM   2862 C  CD1 . LEU C  3  75  ? 22.318 42.320  -26.576 1.00 41.10  ? 75  LEU C CD1 1 
ATOM   2863 C  CD2 . LEU C  3  75  ? 20.844 40.422  -25.696 1.00 46.44  ? 75  LEU C CD2 1 
ATOM   2864 N  N   . ASP C  3  76  ? 24.936 38.828  -28.430 1.00 45.49  ? 76  ASP C N   1 
ATOM   2865 C  CA  . ASP C  3  76  ? 26.145 38.177  -27.968 1.00 47.34  ? 76  ASP C CA  1 
ATOM   2866 C  C   . ASP C  3  76  ? 27.391 38.878  -28.493 1.00 48.52  ? 76  ASP C C   1 
ATOM   2867 O  O   . ASP C  3  76  ? 28.365 39.026  -27.756 1.00 49.27  ? 76  ASP C O   1 
ATOM   2868 C  CB  . ASP C  3  76  ? 26.155 36.702  -28.383 1.00 49.29  ? 76  ASP C CB  1 
ATOM   2869 C  CG  . ASP C  3  76  ? 27.438 35.976  -27.962 1.00 51.21  ? 76  ASP C CG  1 
ATOM   2870 O  OD1 . ASP C  3  76  ? 28.380 35.859  -28.775 1.00 51.56  ? 76  ASP C OD1 1 
ATOM   2871 O  OD2 . ASP C  3  76  ? 27.511 35.520  -26.805 1.00 53.03  ? 76  ASP C OD2 1 
ATOM   2872 N  N   . SER C  3  77  ? 27.362 39.313  -29.757 1.00 48.51  ? 77  SER C N   1 
ATOM   2873 C  CA  . SER C  3  77  ? 28.514 39.996  -30.348 1.00 49.13  ? 77  SER C CA  1 
ATOM   2874 C  C   . SER C  3  77  ? 28.711 41.353  -29.684 1.00 48.64  ? 77  SER C C   1 
ATOM   2875 O  O   . SER C  3  77  ? 29.840 41.804  -29.503 1.00 51.30  ? 77  SER C O   1 
ATOM   2876 C  CB  . SER C  3  77  ? 28.329 40.180  -31.861 1.00 48.41  ? 77  SER C CB  1 
ATOM   2877 O  OG  . SER C  3  77  ? 27.314 41.136  -32.158 1.00 53.23  ? 77  SER C OG  1 
ATOM   2878 N  N   . ALA C  3  78  ? 27.613 42.003  -29.326 1.00 45.80  ? 78  ALA C N   1 
ATOM   2879 C  CA  . ALA C  3  78  ? 27.707 43.298  -28.681 1.00 45.27  ? 78  ALA C CA  1 
ATOM   2880 C  C   . ALA C  3  78  ? 28.156 43.166  -27.213 1.00 44.43  ? 78  ALA C C   1 
ATOM   2881 O  O   . ALA C  3  78  ? 28.989 43.944  -26.741 1.00 45.76  ? 78  ALA C O   1 
ATOM   2882 C  CB  . ALA C  3  78  ? 26.357 44.025  -28.775 1.00 43.38  ? 78  ALA C CB  1 
ATOM   2883 N  N   . ILE C  3  79  ? 27.608 42.182  -26.496 1.00 42.64  ? 79  ILE C N   1 
ATOM   2884 C  CA  . ILE C  3  79  ? 27.970 41.979  -25.097 1.00 40.52  ? 79  ILE C CA  1 
ATOM   2885 C  C   . ILE C  3  79  ? 29.462 41.687  -24.966 1.00 40.89  ? 79  ILE C C   1 
ATOM   2886 O  O   . ILE C  3  79  ? 30.139 42.204  -24.059 1.00 39.69  ? 79  ILE C O   1 
ATOM   2887 C  CB  . ILE C  3  79  ? 27.121 40.869  -24.470 1.00 39.03  ? 79  ILE C CB  1 
ATOM   2888 C  CG1 . ILE C  3  79  ? 25.728 41.429  -24.157 1.00 37.47  ? 79  ILE C CG1 1 
ATOM   2889 C  CG2 . ILE C  3  79  ? 27.768 40.365  -23.193 1.00 39.36  ? 79  ILE C CG2 1 
ATOM   2890 C  CD1 . ILE C  3  79  ? 24.736 40.427  -23.732 1.00 34.06  ? 79  ILE C CD1 1 
ATOM   2891 N  N   . GLY C  3  80  ? 29.979 40.880  -25.890 1.00 39.36  ? 80  GLY C N   1 
ATOM   2892 C  CA  . GLY C  3  80  ? 31.391 40.581  -25.873 1.00 41.10  ? 80  GLY C CA  1 
ATOM   2893 C  C   . GLY C  3  80  ? 32.185 41.854  -26.157 1.00 44.78  ? 80  GLY C C   1 
ATOM   2894 O  O   . GLY C  3  80  ? 33.168 42.152  -25.467 1.00 45.99  ? 80  GLY C O   1 
ATOM   2895 N  N   . LEU C  3  81  ? 31.751 42.627  -27.156 1.00 45.12  ? 81  LEU C N   1 
ATOM   2896 C  CA  . LEU C  3  81  ? 32.454 43.850  -27.532 1.00 45.16  ? 81  LEU C CA  1 
ATOM   2897 C  C   . LEU C  3  81  ? 32.358 45.027  -26.542 1.00 46.05  ? 81  LEU C C   1 
ATOM   2898 O  O   . LEU C  3  81  ? 32.938 46.088  -26.780 1.00 45.38  ? 81  LEU C O   1 
ATOM   2899 C  CB  . LEU C  3  81  ? 32.031 44.279  -28.947 1.00 43.53  ? 81  LEU C CB  1 
ATOM   2900 C  CG  . LEU C  3  81  ? 32.552 43.345  -30.068 1.00 42.21  ? 81  LEU C CG  1 
ATOM   2901 C  CD1 . LEU C  3  81  ? 31.952 43.729  -31.393 1.00 41.21  ? 81  LEU C CD1 1 
ATOM   2902 C  CD2 . LEU C  3  81  ? 34.070 43.410  -30.154 1.00 41.36  ? 81  LEU C CD2 1 
ATOM   2903 N  N   . LEU C  3  82  ? 31.654 44.846  -25.426 1.00 47.43  ? 82  LEU C N   1 
ATOM   2904 C  CA  . LEU C  3  82  ? 31.573 45.918  -24.431 1.00 50.63  ? 82  LEU C CA  1 
ATOM   2905 C  C   . LEU C  3  82  ? 32.998 46.177  -23.928 1.00 52.04  ? 82  LEU C C   1 
ATOM   2906 O  O   . LEU C  3  82  ? 33.304 47.260  -23.443 1.00 53.23  ? 82  LEU C O   1 
ATOM   2907 C  CB  . LEU C  3  82  ? 30.664 45.515  -23.262 1.00 49.29  ? 82  LEU C CB  1 
ATOM   2908 C  CG  . LEU C  3  82  ? 29.147 45.597  -23.485 1.00 49.06  ? 82  LEU C CG  1 
ATOM   2909 C  CD1 . LEU C  3  82  ? 28.384 44.922  -22.365 1.00 47.20  ? 82  LEU C CD1 1 
ATOM   2910 C  CD2 . LEU C  3  82  ? 28.742 47.063  -23.569 1.00 48.74  ? 82  LEU C CD2 1 
ATOM   2911 N  N   . SER C  3  83  ? 33.856 45.164  -24.074 1.00 53.82  ? 83  SER C N   1 
ATOM   2912 C  CA  . SER C  3  83  ? 35.262 45.205  -23.656 1.00 55.18  ? 83  SER C CA  1 
ATOM   2913 C  C   . SER C  3  83  ? 36.189 45.964  -24.591 1.00 56.30  ? 83  SER C C   1 
ATOM   2914 O  O   . SER C  3  83  ? 37.321 46.281  -24.229 1.00 55.36  ? 83  SER C O   1 
ATOM   2915 C  CB  . SER C  3  83  ? 35.808 43.788  -23.518 1.00 55.66  ? 83  SER C CB  1 
ATOM   2916 O  OG  . SER C  3  83  ? 35.044 43.046  -22.590 1.00 59.28  ? 83  SER C OG  1 
ATOM   2917 N  N   . ASP C  3  84  ? 35.721 46.207  -25.810 1.00 57.98  ? 84  ASP C N   1 
ATOM   2918 C  CA  . ASP C  3  84  ? 36.484 46.935  -26.806 1.00 58.36  ? 84  ASP C CA  1 
ATOM   2919 C  C   . ASP C  3  84  ? 35.506 47.849  -27.539 1.00 57.90  ? 84  ASP C C   1 
ATOM   2920 O  O   . ASP C  3  84  ? 35.122 47.593  -28.683 1.00 57.41  ? 84  ASP C O   1 
ATOM   2921 C  CB  . ASP C  3  84  ? 37.155 45.958  -27.778 1.00 61.55  ? 84  ASP C CB  1 
ATOM   2922 C  CG  . ASP C  3  84  ? 37.909 46.673  -28.900 1.00 66.92  ? 84  ASP C CG  1 
ATOM   2923 O  OD1 . ASP C  3  84  ? 38.499 47.749  -28.634 1.00 68.49  ? 84  ASP C OD1 1 
ATOM   2924 O  OD2 . ASP C  3  84  ? 37.933 46.163  -30.048 1.00 68.36  ? 84  ASP C OD2 1 
ATOM   2925 N  N   . PRO C  3  85  ? 35.077 48.934  -26.862 1.00 56.72  ? 85  PRO C N   1 
ATOM   2926 C  CA  . PRO C  3  85  ? 34.141 49.904  -27.419 1.00 55.30  ? 85  PRO C CA  1 
ATOM   2927 C  C   . PRO C  3  85  ? 34.449 50.489  -28.808 1.00 54.76  ? 85  PRO C C   1 
ATOM   2928 O  O   . PRO C  3  85  ? 33.511 50.808  -29.537 1.00 54.27  ? 85  PRO C O   1 
ATOM   2929 C  CB  . PRO C  3  85  ? 34.053 50.962  -26.312 1.00 54.79  ? 85  PRO C CB  1 
ATOM   2930 C  CG  . PRO C  3  85  ? 35.287 50.765  -25.534 1.00 54.79  ? 85  PRO C CG  1 
ATOM   2931 C  CD  . PRO C  3  85  ? 35.416 49.297  -25.480 1.00 55.32  ? 85  PRO C CD  1 
ATOM   2932 N  N   . SER C  3  86  ? 35.722 50.637  -29.182 1.00 54.37  ? 86  SER C N   1 
ATOM   2933 C  CA  . SER C  3  86  ? 36.052 51.159  -30.525 1.00 54.30  ? 86  SER C CA  1 
ATOM   2934 C  C   . SER C  3  86  ? 35.324 50.323  -31.576 1.00 52.96  ? 86  SER C C   1 
ATOM   2935 O  O   . SER C  3  86  ? 34.584 50.839  -32.413 1.00 53.14  ? 86  SER C O   1 
ATOM   2936 C  CB  . SER C  3  86  ? 37.554 51.081  -30.820 1.00 54.60  ? 86  SER C CB  1 
ATOM   2937 O  OG  . SER C  3  86  ? 38.283 52.060  -30.107 1.00 61.20  ? 86  SER C OG  1 
ATOM   2938 N  N   . THR C  3  87  ? 35.550 49.019  -31.515 1.00 51.55  ? 87  THR C N   1 
ATOM   2939 C  CA  . THR C  3  87  ? 34.933 48.079  -32.430 1.00 51.13  ? 87  THR C CA  1 
ATOM   2940 C  C   . THR C  3  87  ? 33.438 47.959  -32.132 1.00 51.40  ? 87  THR C C   1 
ATOM   2941 O  O   . THR C  3  87  ? 32.631 47.795  -33.042 1.00 50.69  ? 87  THR C O   1 
ATOM   2942 C  CB  . THR C  3  87  ? 35.599 46.712  -32.302 1.00 50.02  ? 87  THR C CB  1 
ATOM   2943 O  OG1 . THR C  3  87  ? 37.021 46.875  -32.416 1.00 49.78  ? 87  THR C OG1 1 
ATOM   2944 C  CG2 . THR C  3  87  ? 35.095 45.770  -33.375 1.00 45.87  ? 87  THR C CG2 1 
ATOM   2945 N  N   . LEU C  3  88  ? 33.064 48.044  -30.860 1.00 51.19  ? 88  LEU C N   1 
ATOM   2946 C  CA  . LEU C  3  88  ? 31.653 47.963  -30.513 1.00 51.15  ? 88  LEU C CA  1 
ATOM   2947 C  C   . LEU C  3  88  ? 30.913 49.010  -31.342 1.00 51.40  ? 88  LEU C C   1 
ATOM   2948 O  O   . LEU C  3  88  ? 29.913 48.702  -31.986 1.00 49.68  ? 88  LEU C O   1 
ATOM   2949 C  CB  . LEU C  3  88  ? 31.426 48.245  -29.012 1.00 49.92  ? 88  LEU C CB  1 
ATOM   2950 C  CG  . LEU C  3  88  ? 29.959 48.427  -28.565 1.00 48.78  ? 88  LEU C CG  1 
ATOM   2951 C  CD1 . LEU C  3  88  ? 29.231 47.089  -28.612 1.00 48.15  ? 88  LEU C CD1 1 
ATOM   2952 C  CD2 . LEU C  3  88  ? 29.897 48.991  -27.163 1.00 48.43  ? 88  LEU C CD2 1 
ATOM   2953 N  N   . ASN C  3  89  ? 31.427 50.243  -31.327 1.00 53.15  ? 89  ASN C N   1 
ATOM   2954 C  CA  . ASN C  3  89  ? 30.805 51.346  -32.059 1.00 54.44  ? 89  ASN C CA  1 
ATOM   2955 C  C   . ASN C  3  89  ? 30.535 51.009  -33.508 1.00 55.19  ? 89  ASN C C   1 
ATOM   2956 O  O   . ASN C  3  89  ? 29.462 51.305  -34.019 1.00 55.48  ? 89  ASN C O   1 
ATOM   2957 C  CB  . ASN C  3  89  ? 31.660 52.607  -31.984 1.00 53.15  ? 89  ASN C CB  1 
ATOM   2958 C  CG  . ASN C  3  89  ? 31.622 53.242  -30.621 1.00 54.40  ? 89  ASN C CG  1 
ATOM   2959 O  OD1 . ASN C  3  89  ? 30.633 53.095  -29.894 1.00 54.07  ? 89  ASN C OD1 1 
ATOM   2960 N  ND2 . ASN C  3  89  ? 32.694 53.968  -30.258 1.00 54.47  ? 89  ASN C ND2 1 
ATOM   2961 N  N   . GLU C  3  90  ? 31.513 50.396  -34.167 1.00 56.29  ? 90  GLU C N   1 
ATOM   2962 C  CA  . GLU C  3  90  ? 31.362 50.009  -35.556 1.00 57.47  ? 90  GLU C CA  1 
ATOM   2963 C  C   . GLU C  3  90  ? 30.251 48.970  -35.682 1.00 58.56  ? 90  GLU C C   1 
ATOM   2964 O  O   . GLU C  3  90  ? 29.388 49.073  -36.547 1.00 59.22  ? 90  GLU C O   1 
ATOM   2965 C  CB  . GLU C  3  90  ? 32.688 49.468  -36.095 1.00 57.70  ? 90  GLU C CB  1 
ATOM   2966 C  CG  . GLU C  3  90  ? 33.752 50.543  -36.261 1.00 60.69  ? 90  GLU C CG  1 
ATOM   2967 C  CD  . GLU C  3  90  ? 33.239 51.749  -37.052 1.00 63.92  ? 90  GLU C CD  1 
ATOM   2968 O  OE1 . GLU C  3  90  ? 32.876 51.577  -38.240 1.00 63.19  ? 90  GLU C OE1 1 
ATOM   2969 O  OE2 . GLU C  3  90  ? 33.191 52.871  -36.480 1.00 63.36  ? 90  GLU C OE2 1 
ATOM   2970 N  N   . GLN C  3  91  ? 30.257 47.985  -34.790 1.00 59.39  ? 91  GLN C N   1 
ATOM   2971 C  CA  . GLN C  3  91  ? 29.253 46.929  -34.798 1.00 59.21  ? 91  GLN C CA  1 
ATOM   2972 C  C   . GLN C  3  91  ? 27.843 47.461  -34.522 1.00 57.82  ? 91  GLN C C   1 
ATOM   2973 O  O   . GLN C  3  91  ? 26.885 47.049  -35.166 1.00 55.85  ? 91  GLN C O   1 
ATOM   2974 C  CB  . GLN C  3  91  ? 29.630 45.858  -33.765 1.00 60.53  ? 91  GLN C CB  1 
ATOM   2975 C  CG  . GLN C  3  91  ? 28.733 44.620  -33.738 1.00 63.19  ? 91  GLN C CG  1 
ATOM   2976 C  CD  . GLN C  3  91  ? 28.595 43.964  -35.100 1.00 65.24  ? 91  GLN C CD  1 
ATOM   2977 O  OE1 . GLN C  3  91  ? 29.358 44.254  -36.026 1.00 65.67  ? 91  GLN C OE1 1 
ATOM   2978 N  NE2 . GLN C  3  91  ? 27.626 43.068  -35.227 1.00 65.52  ? 91  GLN C NE2 1 
ATOM   2979 N  N   . LEU C  3  92  ? 27.717 48.368  -33.560 1.00 57.55  ? 92  LEU C N   1 
ATOM   2980 C  CA  . LEU C  3  92  ? 26.419 48.928  -33.219 1.00 59.13  ? 92  LEU C CA  1 
ATOM   2981 C  C   . LEU C  3  92  ? 25.830 49.827  -34.319 1.00 60.74  ? 92  LEU C C   1 
ATOM   2982 O  O   . LEU C  3  92  ? 24.614 50.060  -34.355 1.00 59.84  ? 92  LEU C O   1 
ATOM   2983 C  CB  . LEU C  3  92  ? 26.512 49.706  -31.907 1.00 58.74  ? 92  LEU C CB  1 
ATOM   2984 C  CG  . LEU C  3  92  ? 26.736 48.911  -30.621 1.00 58.56  ? 92  LEU C CG  1 
ATOM   2985 C  CD1 . LEU C  3  92  ? 26.518 49.846  -29.432 1.00 59.20  ? 92  LEU C CD1 1 
ATOM   2986 C  CD2 . LEU C  3  92  ? 25.765 47.744  -30.539 1.00 57.34  ? 92  LEU C CD2 1 
ATOM   2987 N  N   . SER C  3  93  ? 26.692 50.344  -35.195 1.00 62.04  ? 93  SER C N   1 
ATOM   2988 C  CA  . SER C  3  93  ? 26.251 51.184  -36.306 1.00 62.42  ? 93  SER C CA  1 
ATOM   2989 C  C   . SER C  3  93  ? 25.641 50.257  -37.340 1.00 62.31  ? 93  SER C C   1 
ATOM   2990 O  O   . SER C  3  93  ? 24.516 50.455  -37.800 1.00 62.91  ? 93  SER C O   1 
ATOM   2991 C  CB  . SER C  3  93  ? 27.432 51.926  -36.928 1.00 62.11  ? 93  SER C CB  1 
ATOM   2992 O  OG  . SER C  3  93  ? 27.589 53.192  -36.321 1.00 63.96  ? 93  SER C OG  1 
ATOM   2993 N  N   . HIS C  3  94  ? 26.401 49.232  -37.689 1.00 60.92  ? 94  HIS C N   1 
ATOM   2994 C  CA  . HIS C  3  94  ? 25.936 48.266  -38.649 1.00 61.76  ? 94  HIS C CA  1 
ATOM   2995 C  C   . HIS C  3  94  ? 24.565 47.740  -38.243 1.00 63.12  ? 94  HIS C C   1 
ATOM   2996 O  O   . HIS C  3  94  ? 23.683 47.593  -39.080 1.00 64.07  ? 94  HIS C O   1 
ATOM   2997 C  CB  . HIS C  3  94  ? 26.911 47.117  -38.728 1.00 61.45  ? 94  HIS C CB  1 
ATOM   2998 C  CG  . HIS C  3  94  ? 26.590 46.135  -39.799 1.00 63.04  ? 94  HIS C CG  1 
ATOM   2999 N  ND1 . HIS C  3  94  ? 27.085 46.249  -41.080 1.00 63.35  ? 94  HIS C ND1 1 
ATOM   3000 C  CD2 . HIS C  3  94  ? 25.850 45.001  -39.777 1.00 63.42  ? 94  HIS C CD2 1 
ATOM   3001 C  CE1 . HIS C  3  94  ? 26.669 45.222  -41.802 1.00 64.40  ? 94  HIS C CE1 1 
ATOM   3002 N  NE2 . HIS C  3  94  ? 25.918 44.449  -41.034 1.00 65.30  ? 94  HIS C NE2 1 
ATOM   3003 N  N   . LEU C  3  95  ? 24.382 47.451  -36.958 1.00 64.64  ? 95  LEU C N   1 
ATOM   3004 C  CA  . LEU C  3  95  ? 23.098 46.934  -36.491 1.00 65.33  ? 95  LEU C CA  1 
ATOM   3005 C  C   . LEU C  3  95  ? 22.035 48.003  -36.665 1.00 65.99  ? 95  LEU C C   1 
ATOM   3006 O  O   . LEU C  3  95  ? 20.889 47.716  -37.010 1.00 66.84  ? 95  LEU C O   1 
ATOM   3007 C  CB  . LEU C  3  95  ? 23.177 46.505  -35.014 1.00 64.08  ? 95  LEU C CB  1 
ATOM   3008 C  CG  . LEU C  3  95  ? 23.929 45.205  -34.692 1.00 62.93  ? 95  LEU C CG  1 
ATOM   3009 C  CD1 . LEU C  3  95  ? 23.939 45.001  -33.180 1.00 63.10  ? 95  LEU C CD1 1 
ATOM   3010 C  CD2 . LEU C  3  95  ? 23.264 44.022  -35.392 1.00 60.53  ? 95  LEU C CD2 1 
ATOM   3011 N  N   . ALA C  3  96  ? 22.438 49.243  -36.430 1.00 66.73  ? 96  ALA C N   1 
ATOM   3012 C  CA  . ALA C  3  96  ? 21.547 50.386  -36.541 1.00 67.81  ? 96  ALA C CA  1 
ATOM   3013 C  C   . ALA C  3  96  ? 20.989 50.503  -37.949 1.00 68.56  ? 96  ALA C C   1 
ATOM   3014 O  O   . ALA C  3  96  ? 19.799 50.745  -38.136 1.00 67.83  ? 96  ALA C O   1 
ATOM   3015 C  CB  . ALA C  3  96  ? 22.293 51.659  -36.161 1.00 66.85  ? 96  ALA C CB  1 
ATOM   3016 N  N   . THR C  3  97  ? 21.852 50.329  -38.945 1.00 70.19  ? 97  THR C N   1 
ATOM   3017 C  CA  . THR C  3  97  ? 21.404 50.424  -40.324 1.00 71.86  ? 97  THR C CA  1 
ATOM   3018 C  C   . THR C  3  97  ? 20.577 49.192  -40.675 1.00 74.86  ? 97  THR C C   1 
ATOM   3019 O  O   . THR C  3  97  ? 19.829 49.198  -41.647 1.00 77.28  ? 97  THR C O   1 
ATOM   3020 C  CB  . THR C  3  97  ? 22.586 50.534  -41.310 1.00 70.43  ? 97  THR C CB  1 
ATOM   3021 O  OG1 . THR C  3  97  ? 23.117 49.233  -41.572 1.00 70.10  ? 97  THR C OG1 1 
ATOM   3022 C  CG2 . THR C  3  97  ? 23.677 51.428  -40.741 1.00 68.52  ? 97  THR C CG2 1 
ATOM   3023 N  N   . GLN C  3  98  ? 20.709 48.127  -39.890 1.00 77.01  ? 98  GLN C N   1 
ATOM   3024 C  CA  . GLN C  3  98  ? 19.930 46.923  -40.159 1.00 78.81  ? 98  GLN C CA  1 
ATOM   3025 C  C   . GLN C  3  98  ? 18.512 47.060  -39.601 1.00 80.66  ? 98  GLN C C   1 
ATOM   3026 O  O   . GLN C  3  98  ? 17.614 46.315  -40.000 1.00 81.30  ? 98  GLN C O   1 
ATOM   3027 C  CB  . GLN C  3  98  ? 20.619 45.680  -39.574 1.00 78.54  ? 98  GLN C CB  1 
ATOM   3028 C  CG  . GLN C  3  98  ? 21.856 45.209  -40.352 1.00 78.42  ? 98  GLN C CG  1 
ATOM   3029 C  CD  . GLN C  3  98  ? 22.445 43.922  -39.797 1.00 78.54  ? 98  GLN C CD  1 
ATOM   3030 O  OE1 . GLN C  3  98  ? 22.640 43.793  -38.593 1.00 79.91  ? 98  GLN C OE1 1 
ATOM   3031 N  NE2 . GLN C  3  98  ? 22.736 42.968  -40.674 1.00 75.49  ? 98  GLN C NE2 1 
ATOM   3032 N  N   . HIS C  3  99  ? 18.314 48.014  -38.694 1.00 82.59  ? 99  HIS C N   1 
ATOM   3033 C  CA  . HIS C  3  99  ? 17.001 48.248  -38.089 1.00 85.76  ? 99  HIS C CA  1 
ATOM   3034 C  C   . HIS C  3  99  ? 16.415 49.551  -38.589 1.00 89.71  ? 99  HIS C C   1 
ATOM   3035 O  O   . HIS C  3  99  ? 15.211 49.824  -38.458 1.00 89.77  ? 99  HIS C O   1 
ATOM   3036 C  CB  . HIS C  3  99  ? 17.120 48.288  -36.569 1.00 83.46  ? 99  HIS C CB  1 
ATOM   3037 C  CG  . HIS C  3  99  ? 17.393 46.950  -35.957 1.00 81.15  ? 99  HIS C CG  1 
ATOM   3038 N  ND1 . HIS C  3  99  ? 18.592 46.292  -36.117 1.00 79.31  ? 99  HIS C ND1 1 
ATOM   3039 C  CD2 . HIS C  3  99  ? 16.600 46.124  -35.236 1.00 79.42  ? 99  HIS C CD2 1 
ATOM   3040 C  CE1 . HIS C  3  99  ? 18.525 45.114  -35.524 1.00 78.71  ? 99  HIS C CE1 1 
ATOM   3041 N  NE2 . HIS C  3  99  ? 17.325 44.987  -34.983 1.00 77.11  ? 99  HIS C NE2 1 
ATOM   3042 N  N   . GLN C  3  100 ? 17.291 50.357  -39.161 1.00 94.45  ? 100 GLN C N   1 
ATOM   3043 C  CA  . GLN C  3  100 ? 16.942 51.642  -39.720 1.00 98.53  ? 100 GLN C CA  1 
ATOM   3044 C  C   . GLN C  3  100 ? 16.090 51.454  -40.970 1.00 100.90 ? 100 GLN C C   1 
ATOM   3045 O  O   . GLN C  3  100 ? 16.295 50.524  -41.749 1.00 100.87 ? 100 GLN C O   1 
ATOM   3046 C  CB  . GLN C  3  100 ? 18.222 52.363  -40.144 1.00 99.01  ? 100 GLN C CB  1 
ATOM   3047 C  CG  . GLN C  3  100 ? 18.579 53.614  -39.391 1.00 99.54  ? 100 GLN C CG  1 
ATOM   3048 C  CD  . GLN C  3  100 ? 19.964 54.082  -39.789 1.00 100.22 ? 100 GLN C CD  1 
ATOM   3049 O  OE1 . GLN C  3  100 ? 20.322 54.061  -40.972 1.00 101.20 ? 100 GLN C OE1 1 
ATOM   3050 N  NE2 . GLN C  3  100 ? 20.752 54.502  -38.813 1.00 99.31  ? 100 GLN C NE2 1 
ATOM   3051 N  N   . GLU C  3  101 ? 15.133 52.350  -41.146 1.00 103.58 ? 101 GLU C N   1 
ATOM   3052 C  CA  . GLU C  3  101 ? 14.281 52.296  -42.312 1.00 105.94 ? 101 GLU C CA  1 
ATOM   3053 C  C   . GLU C  3  101 ? 13.574 50.974  -42.441 1.00 104.98 ? 101 GLU C C   1 
ATOM   3054 O  O   . GLU C  3  101 ? 13.780 50.176  -43.363 1.00 104.17 ? 101 GLU C O   1 
ATOM   3055 C  CB  . GLU C  3  101 ? 15.138 52.614  -43.546 1.00 109.64 ? 101 GLU C CB  1 
ATOM   3056 C  CG  . GLU C  3  101 ? 16.030 53.817  -43.266 1.00 114.02 ? 101 GLU C CG  1 
ATOM   3057 C  CD  . GLU C  3  101 ? 15.340 54.851  -42.371 1.00 116.66 ? 101 GLU C CD  1 
ATOM   3058 O  OE1 . GLU C  3  101 ? 14.688 55.769  -42.903 1.00 117.84 ? 101 GLU C OE1 1 
ATOM   3059 O  OE2 . GLU C  3  101 ? 15.437 54.726  -41.122 1.00 117.82 ? 101 GLU C OE2 1 
ATOM   3060 N  N   . ARG C  3  102 ? 12.727 50.773  -41.453 1.00 103.49 ? 102 ARG C N   1 
ATOM   3061 C  CA  . ARG C  3  102 ? 11.890 49.607  -41.317 1.00 102.37 ? 102 ARG C CA  1 
ATOM   3062 C  C   . ARG C  3  102 ? 10.803 50.172  -40.431 1.00 101.76 ? 102 ARG C C   1 
ATOM   3063 O  O   . ARG C  3  102 ? 10.963 50.260  -39.217 1.00 102.08 ? 102 ARG C O   1 
ATOM   3064 C  CB  . ARG C  3  102 ? 12.621 48.476  -40.656 1.00 102.05 ? 102 ARG C CB  1 
ATOM   3065 C  CG  . ARG C  3  102 ? 13.048 47.424  -41.625 1.00 100.98 ? 102 ARG C CG  1 
ATOM   3066 C  CD  . ARG C  3  102 ? 13.300 46.121  -40.921 1.00 101.10 ? 102 ARG C CD  1 
ATOM   3067 N  NE  . ARG C  3  102 ? 14.721 45.804  -40.869 1.00 101.12 ? 102 ARG C NE  1 
ATOM   3068 C  CZ  . ARG C  3  102 ? 15.306 44.839  -41.571 1.00 101.08 ? 102 ARG C CZ  1 
ATOM   3069 N  NH1 . ARG C  3  102 ? 16.614 44.639  -41.447 1.00 100.37 ? 102 ARG C NH1 1 
ATOM   3070 N  NH2 . ARG C  3  102 ? 14.588 44.066  -42.387 1.00 100.35 ? 102 ARG C NH2 1 
ATOM   3071 N  N   . ALA C  3  103 ? 9.718  50.603  -41.065 1.00 100.82 ? 103 ALA C N   1 
ATOM   3072 C  CA  . ALA C  3  103 ? 8.583  51.170  -40.360 1.00 99.76  ? 103 ALA C CA  1 
ATOM   3073 C  C   . ALA C  3  103 ? 8.322  50.514  -39.009 1.00 99.19  ? 103 ALA C C   1 
ATOM   3074 O  O   . ALA C  3  103 ? 8.494  49.304  -38.855 1.00 99.47  ? 103 ALA C O   1 
ATOM   3075 C  CB  . ALA C  3  103 ? 7.343  51.041  -41.232 1.00 100.19 ? 103 ALA C CB  1 
ATOM   3076 N  N   . GLY C  3  104 ? 7.884  51.311  -38.039 1.00 97.88  ? 104 GLY C N   1 
ATOM   3077 C  CA  . GLY C  3  104 ? 7.638  50.765  -36.717 1.00 95.24  ? 104 GLY C CA  1 
ATOM   3078 C  C   . GLY C  3  104 ? 8.869  50.548  -35.881 1.00 93.36  ? 104 GLY C C   1 
ATOM   3079 O  O   . GLY C  3  104 ? 8.878  50.995  -34.740 1.00 93.09  ? 104 GLY C O   1 
ATOM   3080 N  N   . VAL C  3  105 ? 9.883  49.876  -36.449 1.00 91.72  ? 105 VAL C N   1 
ATOM   3081 C  CA  . VAL C  3  105 ? 11.107 49.647  -35.690 1.00 89.92  ? 105 VAL C CA  1 
ATOM   3082 C  C   . VAL C  3  105 ? 11.313 51.097  -35.240 1.00 88.75  ? 105 VAL C C   1 
ATOM   3083 O  O   . VAL C  3  105 ? 11.509 51.971  -36.063 1.00 89.42  ? 105 VAL C O   1 
ATOM   3084 C  CB  . VAL C  3  105 ? 12.271 49.203  -36.574 1.00 89.60  ? 105 VAL C CB  1 
ATOM   3085 C  CG1 . VAL C  3  105 ? 13.478 48.947  -35.731 1.00 88.61  ? 105 VAL C CG1 1 
ATOM   3086 C  CG2 . VAL C  3  105 ? 11.899 48.028  -37.436 1.00 89.62  ? 105 VAL C CG2 1 
ATOM   3087 N  N   . THR C  3  106 ? 11.232 51.312  -33.923 1.00 86.55  ? 106 THR C N   1 
ATOM   3088 C  CA  . THR C  3  106 ? 11.336 52.641  -33.368 1.00 84.87  ? 106 THR C CA  1 
ATOM   3089 C  C   . THR C  3  106 ? 11.920 52.442  -31.980 1.00 83.86  ? 106 THR C C   1 
ATOM   3090 O  O   . THR C  3  106 ? 11.990 51.322  -31.504 1.00 84.89  ? 106 THR C O   1 
ATOM   3091 C  CB  . THR C  3  106 ? 10.045 53.439  -33.183 1.00 85.71  ? 106 THR C CB  1 
ATOM   3092 O  OG1 . THR C  3  106 ? 9.205  52.680  -32.302 1.00 86.17  ? 106 THR C OG1 1 
ATOM   3093 C  CG2 . THR C  3  106 ? 9.364  53.684  -34.476 1.00 86.07  ? 106 THR C CG2 1 
ATOM   3094 N  N   . LYS C  3  107 ? 12.435 53.518  -31.396 1.00 81.71  ? 107 LYS C N   1 
ATOM   3095 C  CA  . LYS C  3  107 ? 13.019 53.439  -30.097 1.00 79.31  ? 107 LYS C CA  1 
ATOM   3096 C  C   . LYS C  3  107 ? 12.048 52.864  -29.073 1.00 78.85  ? 107 LYS C C   1 
ATOM   3097 O  O   . LYS C  3  107 ? 12.420 52.144  -28.137 1.00 79.11  ? 107 LYS C O   1 
ATOM   3098 C  CB  . LYS C  3  107 ? 13.527 54.818  -29.670 1.00 78.24  ? 107 LYS C CB  1 
ATOM   3099 C  CG  . LYS C  3  107 ? 14.559 55.360  -30.594 1.00 77.38  ? 107 LYS C CG  1 
ATOM   3100 C  CD  . LYS C  3  107 ? 15.170 56.620  -30.082 1.00 77.01  ? 107 LYS C CD  1 
ATOM   3101 C  CE  . LYS C  3  107 ? 16.334 57.066  -30.952 1.00 76.13  ? 107 LYS C CE  1 
ATOM   3102 N  NZ  . LYS C  3  107 ? 16.907 58.367  -30.464 1.00 75.33  ? 107 LYS C NZ  1 
ATOM   3103 N  N   . GLY C  3  108 ? 10.785 53.211  -29.235 1.00 77.80  ? 108 GLY C N   1 
ATOM   3104 C  CA  . GLY C  3  108 ? 9.766  52.722  -28.320 1.00 76.57  ? 108 GLY C CA  1 
ATOM   3105 C  C   . GLY C  3  108 ? 9.784  51.204  -28.207 1.00 75.23  ? 108 GLY C C   1 
ATOM   3106 O  O   . GLY C  3  108 ? 9.679  50.648  -27.116 1.00 74.71  ? 108 GLY C O   1 
ATOM   3107 N  N   . GLY C  3  109 ? 9.935  50.532  -29.344 1.00 74.50  ? 109 GLY C N   1 
ATOM   3108 C  CA  . GLY C  3  109 ? 9.979  49.080  -29.343 1.00 75.30  ? 109 GLY C CA  1 
ATOM   3109 C  C   . GLY C  3  109 ? 11.198 48.519  -28.631 1.00 74.95  ? 109 GLY C C   1 
ATOM   3110 O  O   . GLY C  3  109 ? 11.157 47.420  -28.067 1.00 73.92  ? 109 GLY C O   1 
ATOM   3111 N  N   . PHE C  3  110 ? 12.286 49.281  -28.660 1.00 74.60  ? 110 PHE C N   1 
ATOM   3112 C  CA  . PHE C  3  110 ? 13.522 48.862  -28.024 1.00 73.86  ? 110 PHE C CA  1 
ATOM   3113 C  C   . PHE C  3  110 ? 13.385 48.971  -26.520 1.00 73.17  ? 110 PHE C C   1 
ATOM   3114 O  O   . PHE C  3  110 ? 13.901 48.132  -25.782 1.00 73.31  ? 110 PHE C O   1 
ATOM   3115 C  CB  . PHE C  3  110 ? 14.694 49.695  -28.544 1.00 73.75  ? 110 PHE C CB  1 
ATOM   3116 C  CG  . PHE C  3  110 ? 15.351 49.107  -29.760 1.00 74.00  ? 110 PHE C CG  1 
ATOM   3117 C  CD1 . PHE C  3  110 ? 16.502 48.338  -29.632 1.00 74.31  ? 110 PHE C CD1 1 
ATOM   3118 C  CD2 . PHE C  3  110 ? 14.805 49.295  -31.031 1.00 74.86  ? 110 PHE C CD2 1 
ATOM   3119 C  CE1 . PHE C  3  110 ? 17.107 47.762  -30.744 1.00 74.37  ? 110 PHE C CE1 1 
ATOM   3120 C  CE2 . PHE C  3  110 ? 15.397 48.723  -32.157 1.00 74.23  ? 110 PHE C CE2 1 
ATOM   3121 C  CZ  . PHE C  3  110 ? 16.551 47.955  -32.014 1.00 75.33  ? 110 PHE C CZ  1 
ATOM   3122 N  N   . SER C  3  111 ? 12.677 49.996  -26.060 1.00 72.15  ? 111 SER C N   1 
ATOM   3123 C  CA  . SER C  3  111 ? 12.448 50.149  -24.628 1.00 71.20  ? 111 SER C CA  1 
ATOM   3124 C  C   . SER C  3  111 ? 11.543 49.001  -24.180 1.00 69.97  ? 111 SER C C   1 
ATOM   3125 O  O   . SER C  3  111 ? 11.644 48.520  -23.054 1.00 69.45  ? 111 SER C O   1 
ATOM   3126 C  CB  . SER C  3  111 ? 11.759 51.476  -24.324 1.00 70.75  ? 111 SER C CB  1 
ATOM   3127 O  OG  . SER C  3  111 ? 12.592 52.560  -24.673 1.00 73.35  ? 111 SER C OG  1 
ATOM   3128 N  N   . ALA C  3  112 ? 10.651 48.572  -25.071 1.00 67.91  ? 112 ALA C N   1 
ATOM   3129 C  CA  . ALA C  3  112 ? 9.741  47.475  -24.778 1.00 65.76  ? 112 ALA C CA  1 
ATOM   3130 C  C   . ALA C  3  112 ? 10.549 46.203  -24.585 1.00 64.99  ? 112 ALA C C   1 
ATOM   3131 O  O   . ALA C  3  112 ? 10.507 45.586  -23.522 1.00 64.57  ? 112 ALA C O   1 
ATOM   3132 C  CB  . ALA C  3  112 ? 8.738  47.292  -25.922 1.00 64.38  ? 112 ALA C CB  1 
ATOM   3133 N  N   . ILE C  3  113 ? 11.302 45.825  -25.608 1.00 63.92  ? 113 ILE C N   1 
ATOM   3134 C  CA  . ILE C  3  113 ? 12.095 44.613  -25.532 1.00 64.05  ? 113 ILE C CA  1 
ATOM   3135 C  C   . ILE C  3  113 ? 13.093 44.659  -24.370 1.00 66.04  ? 113 ILE C C   1 
ATOM   3136 O  O   . ILE C  3  113 ? 13.443 43.625  -23.798 1.00 65.91  ? 113 ILE C O   1 
ATOM   3137 C  CB  . ILE C  3  113 ? 12.840 44.352  -26.857 1.00 61.98  ? 113 ILE C CB  1 
ATOM   3138 C  CG1 . ILE C  3  113 ? 13.107 42.858  -26.991 1.00 59.87  ? 113 ILE C CG1 1 
ATOM   3139 C  CG2 . ILE C  3  113 ? 14.152 45.140  -26.908 1.00 59.01  ? 113 ILE C CG2 1 
ATOM   3140 C  CD1 . ILE C  3  113 ? 13.592 42.453  -28.353 1.00 58.77  ? 113 ILE C CD1 1 
ATOM   3141 N  N   . ALA C  3  114 ? 13.544 45.858  -24.012 1.00 67.17  ? 114 ALA C N   1 
ATOM   3142 C  CA  . ALA C  3  114 ? 14.475 45.996  -22.895 1.00 67.82  ? 114 ALA C CA  1 
ATOM   3143 C  C   . ALA C  3  114 ? 13.791 45.495  -21.634 1.00 68.34  ? 114 ALA C C   1 
ATOM   3144 O  O   . ALA C  3  114 ? 14.429 44.974  -20.726 1.00 70.20  ? 114 ALA C O   1 
ATOM   3145 C  CB  . ALA C  3  114 ? 14.878 47.438  -22.721 1.00 65.90  ? 114 ALA C CB  1 
ATOM   3146 N  N   . GLN C  3  115 ? 12.476 45.671  -21.590 1.00 69.04  ? 115 GLN C N   1 
ATOM   3147 C  CA  . GLN C  3  115 ? 11.664 45.238  -20.452 1.00 69.23  ? 115 GLN C CA  1 
ATOM   3148 C  C   . GLN C  3  115 ? 11.378 43.755  -20.550 1.00 67.72  ? 115 GLN C C   1 
ATOM   3149 O  O   . GLN C  3  115 ? 11.120 43.083  -19.554 1.00 67.68  ? 115 GLN C O   1 
ATOM   3150 C  CB  . GLN C  3  115 ? 10.359 46.019  -20.419 1.00 71.13  ? 115 GLN C CB  1 
ATOM   3151 C  CG  . GLN C  3  115 ? 10.535 47.407  -19.865 1.00 73.29  ? 115 GLN C CG  1 
ATOM   3152 C  CD  . GLN C  3  115 ? 11.014 47.374  -18.433 1.00 75.14  ? 115 GLN C CD  1 
ATOM   3153 O  OE1 . GLN C  3  115 ? 11.502 48.372  -17.902 1.00 76.76  ? 115 GLN C OE1 1 
ATOM   3154 N  NE2 . GLN C  3  115 ? 10.866 46.222  -17.788 1.00 76.62  ? 115 GLN C NE2 1 
ATOM   3155 N  N   . SER C  3  116 ? 11.408 43.252  -21.769 1.00 65.65  ? 116 SER C N   1 
ATOM   3156 C  CA  . SER C  3  116 ? 11.156 41.856  -21.990 1.00 65.15  ? 116 SER C CA  1 
ATOM   3157 C  C   . SER C  3  116 ? 12.380 41.094  -21.495 1.00 63.54  ? 116 SER C C   1 
ATOM   3158 O  O   . SER C  3  116 ? 12.259 40.073  -20.831 1.00 63.36  ? 116 SER C O   1 
ATOM   3159 C  CB  . SER C  3  116 ? 10.907 41.613  -23.488 1.00 67.41  ? 116 SER C CB  1 
ATOM   3160 O  OG  . SER C  3  116 ? 9.798  42.376  -23.952 1.00 70.20  ? 116 SER C OG  1 
ATOM   3161 N  N   . PHE C  3  117 ? 13.564 41.604  -21.797 1.00 62.16  ? 117 PHE C N   1 
ATOM   3162 C  CA  . PHE C  3  117 ? 14.783 40.941  -21.350 1.00 60.81  ? 117 PHE C CA  1 
ATOM   3163 C  C   . PHE C  3  117 ? 14.870 40.952  -19.838 1.00 59.74  ? 117 PHE C C   1 
ATOM   3164 O  O   . PHE C  3  117 ? 15.258 39.961  -19.235 1.00 59.42  ? 117 PHE C O   1 
ATOM   3165 C  CB  . PHE C  3  117 ? 16.012 41.614  -21.956 1.00 60.04  ? 117 PHE C CB  1 
ATOM   3166 C  CG  . PHE C  3  117 ? 16.441 41.010  -23.254 1.00 58.31  ? 117 PHE C CG  1 
ATOM   3167 C  CD1 . PHE C  3  117 ? 17.140 39.816  -23.278 1.00 58.02  ? 117 PHE C CD1 1 
ATOM   3168 C  CD2 . PHE C  3  117 ? 16.121 41.622  -24.461 1.00 58.08  ? 117 PHE C CD2 1 
ATOM   3169 C  CE1 . PHE C  3  117 ? 17.517 39.238  -24.496 1.00 59.43  ? 117 PHE C CE1 1 
ATOM   3170 C  CE2 . PHE C  3  117 ? 16.495 41.050  -25.681 1.00 58.17  ? 117 PHE C CE2 1 
ATOM   3171 C  CZ  . PHE C  3  117 ? 17.193 39.858  -25.699 1.00 57.01  ? 117 PHE C CZ  1 
ATOM   3172 N  N   . LEU C  3  118 ? 14.497 42.072  -19.229 1.00 58.28  ? 118 LEU C N   1 
ATOM   3173 C  CA  . LEU C  3  118 ? 14.528 42.188  -17.782 1.00 58.15  ? 118 LEU C CA  1 
ATOM   3174 C  C   . LEU C  3  118 ? 13.580 41.198  -17.109 1.00 58.96  ? 118 LEU C C   1 
ATOM   3175 O  O   . LEU C  3  118 ? 13.761 40.870  -15.934 1.00 59.77  ? 118 LEU C O   1 
ATOM   3176 C  CB  . LEU C  3  118 ? 14.177 43.611  -17.362 1.00 56.88  ? 118 LEU C CB  1 
ATOM   3177 C  CG  . LEU C  3  118 ? 15.312 44.614  -17.561 1.00 58.08  ? 118 LEU C CG  1 
ATOM   3178 C  CD1 . LEU C  3  118 ? 14.789 46.041  -17.492 1.00 58.53  ? 118 LEU C CD1 1 
ATOM   3179 C  CD2 . LEU C  3  118 ? 16.372 44.385  -16.502 1.00 56.71  ? 118 LEU C CD2 1 
ATOM   3180 N  N   . ARG C  3  119 ? 12.570 40.723  -17.839 1.00 58.39  ? 119 ARG C N   1 
ATOM   3181 C  CA  . ARG C  3  119 ? 11.615 39.757  -17.282 1.00 58.48  ? 119 ARG C CA  1 
ATOM   3182 C  C   . ARG C  3  119 ? 12.027 38.307  -17.559 1.00 56.44  ? 119 ARG C C   1 
ATOM   3183 O  O   . ARG C  3  119 ? 11.759 37.403  -16.766 1.00 56.11  ? 119 ARG C O   1 
ATOM   3184 C  CB  . ARG C  3  119 ? 10.205 40.003  -17.842 1.00 59.94  ? 119 ARG C CB  1 
ATOM   3185 C  CG  . ARG C  3  119 ? 9.376  41.007  -17.059 1.00 61.30  ? 119 ARG C CG  1 
ATOM   3186 C  CD  . ARG C  3  119 ? 7.935  41.040  -17.568 1.00 65.43  ? 119 ARG C CD  1 
ATOM   3187 N  NE  . ARG C  3  119 ? 7.831  41.543  -18.940 1.00 67.24  ? 119 ARG C NE  1 
ATOM   3188 C  CZ  . ARG C  3  119 ? 7.720  42.832  -19.256 1.00 67.17  ? 119 ARG C CZ  1 
ATOM   3189 N  NH1 . ARG C  3  119 ? 7.638  43.205  -20.531 1.00 66.58  ? 119 ARG C NH1 1 
ATOM   3190 N  NH2 . ARG C  3  119 ? 7.678  43.749  -18.296 1.00 62.99  ? 119 ARG C NH2 1 
ATOM   3191 N  N   . VAL C  3  120 ? 12.676 38.099  -18.694 1.00 54.80  ? 120 VAL C N   1 
ATOM   3192 C  CA  . VAL C  3  120 ? 13.147 36.784  -19.111 1.00 52.85  ? 120 VAL C CA  1 
ATOM   3193 C  C   . VAL C  3  120 ? 14.450 36.344  -18.390 1.00 53.03  ? 120 VAL C C   1 
ATOM   3194 O  O   . VAL C  3  120 ? 14.509 35.253  -17.809 1.00 53.28  ? 120 VAL C O   1 
ATOM   3195 C  CB  . VAL C  3  120 ? 13.370 36.790  -20.641 1.00 50.16  ? 120 VAL C CB  1 
ATOM   3196 C  CG1 . VAL C  3  120 ? 13.962 35.492  -21.118 1.00 49.14  ? 120 VAL C CG1 1 
ATOM   3197 C  CG2 . VAL C  3  120 ? 12.061 37.031  -21.324 1.00 52.96  ? 120 VAL C CG2 1 
ATOM   3198 N  N   . MET C  3  121 ? 15.476 37.191  -18.431 1.00 50.58  ? 121 MET C N   1 
ATOM   3199 C  CA  . MET C  3  121 ? 16.762 36.877  -17.825 1.00 50.41  ? 121 MET C CA  1 
ATOM   3200 C  C   . MET C  3  121 ? 16.717 36.286  -16.408 1.00 51.20  ? 121 MET C C   1 
ATOM   3201 O  O   . MET C  3  121 ? 17.171 35.163  -16.183 1.00 51.00  ? 121 MET C O   1 
ATOM   3202 C  CB  . MET C  3  121 ? 17.657 38.115  -17.830 1.00 48.69  ? 121 MET C CB  1 
ATOM   3203 C  CG  . MET C  3  121 ? 18.183 38.518  -19.187 1.00 47.02  ? 121 MET C CG  1 
ATOM   3204 S  SD  . MET C  3  121 ? 18.996 37.221  -20.116 1.00 46.71  ? 121 MET C SD  1 
ATOM   3205 C  CE  . MET C  3  121 ? 20.480 37.060  -19.228 1.00 44.76  ? 121 MET C CE  1 
ATOM   3206 N  N   . PRO C  3  122 ? 16.164 37.033  -15.442 1.00 50.32  ? 122 PRO C N   1 
ATOM   3207 C  CA  . PRO C  3  122 ? 16.115 36.487  -14.085 1.00 50.84  ? 122 PRO C CA  1 
ATOM   3208 C  C   . PRO C  3  122 ? 15.562 35.064  -13.967 1.00 50.57  ? 122 PRO C C   1 
ATOM   3209 O  O   . PRO C  3  122 ? 15.897 34.351  -13.028 1.00 51.00  ? 122 PRO C O   1 
ATOM   3210 C  CB  . PRO C  3  122 ? 15.272 37.518  -13.323 1.00 49.23  ? 122 PRO C CB  1 
ATOM   3211 C  CG  . PRO C  3  122 ? 14.385 38.081  -14.385 1.00 50.07  ? 122 PRO C CG  1 
ATOM   3212 C  CD  . PRO C  3  122 ? 15.322 38.237  -15.555 1.00 50.99  ? 122 PRO C CD  1 
ATOM   3213 N  N   . GLN C  3  123 ? 14.737 34.642  -14.918 1.00 50.41  ? 123 GLN C N   1 
ATOM   3214 C  CA  . GLN C  3  123 ? 14.147 33.303  -14.872 1.00 49.99  ? 123 GLN C CA  1 
ATOM   3215 C  C   . GLN C  3  123 ? 15.132 32.232  -15.310 1.00 48.77  ? 123 GLN C C   1 
ATOM   3216 O  O   . GLN C  3  123 ? 15.085 31.093  -14.843 1.00 49.21  ? 123 GLN C O   1 
ATOM   3217 C  CB  . GLN C  3  123 ? 12.932 33.228  -15.787 1.00 50.22  ? 123 GLN C CB  1 
ATOM   3218 C  CG  . GLN C  3  123 ? 11.749 34.038  -15.355 1.00 49.85  ? 123 GLN C CG  1 
ATOM   3219 C  CD  . GLN C  3  123 ? 10.649 33.935  -16.360 1.00 51.23  ? 123 GLN C CD  1 
ATOM   3220 O  OE1 . GLN C  3  123 ? 10.190 32.840  -16.679 1.00 51.88  ? 123 GLN C OE1 1 
ATOM   3221 N  NE2 . GLN C  3  123 ? 10.226 35.077  -16.891 1.00 53.00  ? 123 GLN C NE2 1 
ATOM   3222 N  N   . VAL C  3  124 ? 16.026 32.609  -16.203 1.00 47.00  ? 124 VAL C N   1 
ATOM   3223 C  CA  . VAL C  3  124 ? 16.995 31.676  -16.735 1.00 46.92  ? 124 VAL C CA  1 
ATOM   3224 C  C   . VAL C  3  124 ? 18.420 31.871  -16.188 1.00 45.83  ? 124 VAL C C   1 
ATOM   3225 O  O   . VAL C  3  124 ? 19.171 30.911  -16.064 1.00 46.58  ? 124 VAL C O   1 
ATOM   3226 C  CB  . VAL C  3  124 ? 16.953 31.760  -18.290 1.00 46.76  ? 124 VAL C CB  1 
ATOM   3227 C  CG1 . VAL C  3  124 ? 17.394 33.145  -18.744 1.00 45.71  ? 124 VAL C CG1 1 
ATOM   3228 C  CG2 . VAL C  3  124 ? 17.775 30.664  -18.907 1.00 48.08  ? 124 VAL C CG2 1 
ATOM   3229 N  N   . ALA C  3  125 ? 18.783 33.104  -15.847 1.00 44.62  ? 125 ALA C N   1 
ATOM   3230 C  CA  . ALA C  3  125 ? 20.115 33.409  -15.321 1.00 44.00  ? 125 ALA C CA  1 
ATOM   3231 C  C   . ALA C  3  125 ? 20.212 33.428  -13.791 1.00 44.21  ? 125 ALA C C   1 
ATOM   3232 O  O   . ALA C  3  125 ? 19.344 33.961  -13.095 1.00 43.76  ? 125 ALA C O   1 
ATOM   3233 C  CB  . ALA C  3  125 ? 20.592 34.734  -15.861 1.00 42.45  ? 125 ALA C CB  1 
ATOM   3234 N  N   . SER C  3  126 ? 21.293 32.848  -13.283 1.00 44.57  ? 126 SER C N   1 
ATOM   3235 C  CA  . SER C  3  126 ? 21.541 32.790  -11.851 1.00 47.26  ? 126 SER C CA  1 
ATOM   3236 C  C   . SER C  3  126 ? 22.340 34.026  -11.417 1.00 48.96  ? 126 SER C C   1 
ATOM   3237 O  O   . SER C  3  126 ? 23.269 34.444  -12.107 1.00 50.23  ? 126 SER C O   1 
ATOM   3238 C  CB  . SER C  3  126 ? 22.337 31.521  -11.495 1.00 46.75  ? 126 SER C CB  1 
ATOM   3239 O  OG  . SER C  3  126 ? 21.670 30.331  -11.876 1.00 43.56  ? 126 SER C OG  1 
ATOM   3240 N  N   . CYS C  3  127 ? 21.991 34.611  -10.279 1.00 50.31  ? 127 CYS C N   1 
ATOM   3241 C  CA  . CYS C  3  127 ? 22.720 35.786  -9.795  1.00 52.90  ? 127 CYS C CA  1 
ATOM   3242 C  C   . CYS C  3  127 ? 22.552 36.949  -10.783 1.00 53.84  ? 127 CYS C C   1 
ATOM   3243 O  O   . CYS C  3  127 ? 23.516 37.641  -11.114 1.00 54.19  ? 127 CYS C O   1 
ATOM   3244 C  CB  . CYS C  3  127 ? 24.229 35.502  -9.669  1.00 52.30  ? 127 CYS C CB  1 
ATOM   3245 S  SG  . CYS C  3  127 ? 24.891 34.321  -8.427  1.00 52.63  ? 127 CYS C SG  1 
ATOM   3246 N  N   . PHE C  3  128 ? 21.334 37.149  -11.261 1.00 54.79  ? 128 PHE C N   1 
ATOM   3247 C  CA  . PHE C  3  128 ? 21.074 38.223  -12.207 1.00 55.10  ? 128 PHE C CA  1 
ATOM   3248 C  C   . PHE C  3  128 ? 21.067 39.573  -11.493 1.00 55.46  ? 128 PHE C C   1 
ATOM   3249 O  O   . PHE C  3  128 ? 20.429 39.733  -10.441 1.00 54.02  ? 128 PHE C O   1 
ATOM   3250 C  CB  . PHE C  3  128 ? 19.735 38.004  -12.909 1.00 54.29  ? 128 PHE C CB  1 
ATOM   3251 C  CG  . PHE C  3  128 ? 19.393 39.064  -13.918 1.00 54.68  ? 128 PHE C CG  1 
ATOM   3252 C  CD1 . PHE C  3  128 ? 20.125 39.184  -15.098 1.00 54.60  ? 128 PHE C CD1 1 
ATOM   3253 C  CD2 . PHE C  3  128 ? 18.321 39.926  -13.707 1.00 55.13  ? 128 PHE C CD2 1 
ATOM   3254 C  CE1 . PHE C  3  128 ? 19.800 40.143  -16.059 1.00 54.08  ? 128 PHE C CE1 1 
ATOM   3255 C  CE2 . PHE C  3  128 ? 17.990 40.884  -14.659 1.00 54.10  ? 128 PHE C CE2 1 
ATOM   3256 C  CZ  . PHE C  3  128 ? 18.736 40.990  -15.839 1.00 55.50  ? 128 PHE C CZ  1 
ATOM   3257 N  N   . ASN C  3  129 ? 21.787 40.531  -12.077 1.00 54.94  ? 129 ASN C N   1 
ATOM   3258 C  CA  . ASN C  3  129 ? 21.883 41.893  -11.557 1.00 54.66  ? 129 ASN C CA  1 
ATOM   3259 C  C   . ASN C  3  129 ? 21.146 42.770  -12.573 1.00 52.91  ? 129 ASN C C   1 
ATOM   3260 O  O   . ASN C  3  129 ? 21.715 43.173  -13.581 1.00 52.32  ? 129 ASN C O   1 
ATOM   3261 C  CB  . ASN C  3  129 ? 23.351 42.319  -11.473 1.00 57.22  ? 129 ASN C CB  1 
ATOM   3262 C  CG  . ASN C  3  129 ? 23.537 43.640  -10.746 1.00 59.82  ? 129 ASN C CG  1 
ATOM   3263 O  OD1 . ASN C  3  129 ? 22.718 44.548  -10.869 1.00 59.92  ? 129 ASN C OD1 1 
ATOM   3264 N  ND2 . ASN C  3  129 ? 24.626 43.757  -9.993  1.00 60.64  ? 129 ASN C ND2 1 
ATOM   3265 N  N   . PRO C  3  130 ? 19.858 43.053  -12.329 1.00 52.32  ? 130 PRO C N   1 
ATOM   3266 C  CA  . PRO C  3  130 ? 19.042 43.878  -13.225 1.00 52.42  ? 130 PRO C CA  1 
ATOM   3267 C  C   . PRO C  3  130 ? 19.570 45.284  -13.497 1.00 52.26  ? 130 PRO C C   1 
ATOM   3268 O  O   . PRO C  3  130 ? 19.453 45.780  -14.622 1.00 52.00  ? 130 PRO C O   1 
ATOM   3269 C  CB  . PRO C  3  130 ? 17.670 43.876  -12.548 1.00 50.50  ? 130 PRO C CB  1 
ATOM   3270 C  CG  . PRO C  3  130 ? 17.986 43.650  -11.132 1.00 51.13  ? 130 PRO C CG  1 
ATOM   3271 C  CD  . PRO C  3  130 ? 19.043 42.583  -11.200 1.00 52.51  ? 130 PRO C CD  1 
ATOM   3272 N  N   . ASP C  3  131 ? 20.147 45.919  -12.480 1.00 52.98  ? 131 ASP C N   1 
ATOM   3273 C  CA  . ASP C  3  131 ? 20.703 47.265  -12.643 1.00 52.85  ? 131 ASP C CA  1 
ATOM   3274 C  C   . ASP C  3  131 ? 21.852 47.248  -13.644 1.00 51.28  ? 131 ASP C C   1 
ATOM   3275 O  O   . ASP C  3  131 ? 21.759 47.871  -14.705 1.00 52.58  ? 131 ASP C O   1 
ATOM   3276 C  CB  . ASP C  3  131 ? 21.217 47.837  -11.308 1.00 56.21  ? 131 ASP C CB  1 
ATOM   3277 C  CG  . ASP C  3  131 ? 20.087 48.276  -10.365 1.00 59.33  ? 131 ASP C CG  1 
ATOM   3278 O  OD1 . ASP C  3  131 ? 18.931 48.411  -10.825 1.00 58.05  ? 131 ASP C OD1 1 
ATOM   3279 O  OD2 . ASP C  3  131 ? 20.361 48.501  -9.160  1.00 60.84  ? 131 ASP C OD2 1 
ATOM   3280 N  N   . ALA C  3  132 ? 22.930 46.536  -13.313 1.00 48.71  ? 132 ALA C N   1 
ATOM   3281 C  CA  . ALA C  3  132 ? 24.085 46.475  -14.197 1.00 46.41  ? 132 ALA C CA  1 
ATOM   3282 C  C   . ALA C  3  132 ? 23.641 46.082  -15.589 1.00 45.08  ? 132 ALA C C   1 
ATOM   3283 O  O   . ALA C  3  132 ? 24.043 46.702  -16.571 1.00 43.73  ? 132 ALA C O   1 
ATOM   3284 C  CB  . ALA C  3  132 ? 25.102 45.484  -13.673 1.00 47.81  ? 132 ALA C CB  1 
ATOM   3285 N  N   . TRP C  3  133 ? 22.792 45.065  -15.667 1.00 44.92  ? 133 TRP C N   1 
ATOM   3286 C  CA  . TRP C  3  133 ? 22.315 44.590  -16.950 1.00 44.93  ? 133 TRP C CA  1 
ATOM   3287 C  C   . TRP C  3  133 ? 21.657 45.668  -17.767 1.00 46.46  ? 133 TRP C C   1 
ATOM   3288 O  O   . TRP C  3  133 ? 22.026 45.872  -18.923 1.00 45.68  ? 133 TRP C O   1 
ATOM   3289 C  CB  . TRP C  3  133 ? 21.326 43.444  -16.789 1.00 45.47  ? 133 TRP C CB  1 
ATOM   3290 C  CG  . TRP C  3  133 ? 20.594 43.121  -18.083 1.00 45.99  ? 133 TRP C CG  1 
ATOM   3291 C  CD1 . TRP C  3  133 ? 19.458 43.726  -18.561 1.00 45.74  ? 133 TRP C CD1 1 
ATOM   3292 C  CD2 . TRP C  3  133 ? 20.968 42.148  -19.067 1.00 44.71  ? 133 TRP C CD2 1 
ATOM   3293 N  NE1 . TRP C  3  133 ? 19.113 43.193  -19.775 1.00 43.86  ? 133 TRP C NE1 1 
ATOM   3294 C  CE2 . TRP C  3  133 ? 20.018 42.223  -20.110 1.00 43.90  ? 133 TRP C CE2 1 
ATOM   3295 C  CE3 . TRP C  3  133 ? 22.017 41.221  -19.172 1.00 43.91  ? 133 TRP C CE3 1 
ATOM   3296 C  CZ2 . TRP C  3  133 ? 20.085 41.405  -21.237 1.00 43.97  ? 133 TRP C CZ2 1 
ATOM   3297 C  CZ3 . TRP C  3  133 ? 22.082 40.412  -20.298 1.00 41.84  ? 133 TRP C CZ3 1 
ATOM   3298 C  CH2 . TRP C  3  133 ? 21.124 40.507  -21.310 1.00 42.56  ? 133 TRP C CH2 1 
ATOM   3299 N  N   . SER C  3  134 ? 20.684 46.365  -17.183 1.00 46.73  ? 134 SER C N   1 
ATOM   3300 C  CA  . SER C  3  134 ? 20.009 47.377  -17.975 1.00 49.04  ? 134 SER C CA  1 
ATOM   3301 C  C   . SER C  3  134 ? 20.933 48.525  -18.330 1.00 48.52  ? 134 SER C C   1 
ATOM   3302 O  O   . SER C  3  134 ? 20.849 49.048  -19.433 1.00 49.68  ? 134 SER C O   1 
ATOM   3303 C  CB  . SER C  3  134 ? 18.735 47.905  -17.288 1.00 49.41  ? 134 SER C CB  1 
ATOM   3304 O  OG  . SER C  3  134 ? 19.034 48.858  -16.297 1.00 50.66  ? 134 SER C OG  1 
ATOM   3305 N  N   . ARG C  3  135 ? 21.830 48.913  -17.433 1.00 47.76  ? 135 ARG C N   1 
ATOM   3306 C  CA  . ARG C  3  135 ? 22.710 50.021  -17.775 1.00 48.21  ? 135 ARG C CA  1 
ATOM   3307 C  C   . ARG C  3  135 ? 23.501 49.723  -19.045 1.00 50.33  ? 135 ARG C C   1 
ATOM   3308 O  O   . ARG C  3  135 ? 23.687 50.598  -19.881 1.00 52.02  ? 135 ARG C O   1 
ATOM   3309 C  CB  . ARG C  3  135 ? 23.661 50.364  -16.622 1.00 47.00  ? 135 ARG C CB  1 
ATOM   3310 C  CG  . ARG C  3  135 ? 23.017 51.201  -15.517 1.00 44.38  ? 135 ARG C CG  1 
ATOM   3311 C  CD  . ARG C  3  135 ? 24.064 51.818  -14.609 1.00 43.84  ? 135 ARG C CD  1 
ATOM   3312 N  NE  . ARG C  3  135 ? 24.752 50.813  -13.798 1.00 45.84  ? 135 ARG C NE  1 
ATOM   3313 C  CZ  . ARG C  3  135 ? 24.255 50.301  -12.677 1.00 45.73  ? 135 ARG C CZ  1 
ATOM   3314 N  NH1 . ARG C  3  135 ? 24.943 49.393  -12.004 1.00 43.51  ? 135 ARG C NH1 1 
ATOM   3315 N  NH2 . ARG C  3  135 ? 23.073 50.718  -12.224 1.00 46.92  ? 135 ARG C NH2 1 
ATOM   3316 N  N   . CYS C  3  136 ? 23.947 48.489  -19.216 1.00 51.82  ? 136 CYS C N   1 
ATOM   3317 C  CA  . CYS C  3  136 ? 24.706 48.157  -20.415 1.00 53.82  ? 136 CYS C CA  1 
ATOM   3318 C  C   . CYS C  3  136 ? 23.827 47.738  -21.600 1.00 53.96  ? 136 CYS C C   1 
ATOM   3319 O  O   . CYS C  3  136 ? 24.228 47.858  -22.757 1.00 54.48  ? 136 CYS C O   1 
ATOM   3320 C  CB  . CYS C  3  136 ? 25.737 47.078  -20.084 1.00 53.44  ? 136 CYS C CB  1 
ATOM   3321 S  SG  . CYS C  3  136 ? 26.973 47.704  -18.900 1.00 58.55  ? 136 CYS C SG  1 
ATOM   3322 N  N   . PHE C  3  137 ? 22.623 47.250  -21.316 1.00 53.58  ? 137 PHE C N   1 
ATOM   3323 C  CA  . PHE C  3  137 ? 21.726 46.869  -22.390 1.00 53.29  ? 137 PHE C CA  1 
ATOM   3324 C  C   . PHE C  3  137 ? 21.398 48.183  -23.088 1.00 52.52  ? 137 PHE C C   1 
ATOM   3325 O  O   . PHE C  3  137 ? 21.493 48.284  -24.312 1.00 51.05  ? 137 PHE C O   1 
ATOM   3326 C  CB  . PHE C  3  137 ? 20.445 46.246  -21.826 1.00 53.86  ? 137 PHE C CB  1 
ATOM   3327 C  CG  . PHE C  3  137 ? 19.549 45.648  -22.873 1.00 53.95  ? 137 PHE C CG  1 
ATOM   3328 C  CD1 . PHE C  3  137 ? 19.818 44.388  -23.412 1.00 53.68  ? 137 PHE C CD1 1 
ATOM   3329 C  CD2 . PHE C  3  137 ? 18.435 46.347  -23.322 1.00 53.75  ? 137 PHE C CD2 1 
ATOM   3330 C  CE1 . PHE C  3  137 ? 18.985 43.831  -24.389 1.00 52.78  ? 137 PHE C CE1 1 
ATOM   3331 C  CE2 . PHE C  3  137 ? 17.594 45.802  -24.300 1.00 53.45  ? 137 PHE C CE2 1 
ATOM   3332 C  CZ  . PHE C  3  137 ? 17.868 44.542  -24.836 1.00 51.57  ? 137 PHE C CZ  1 
ATOM   3333 N  N   . ASN C  3  138 ? 21.053 49.191  -22.283 1.00 51.54  ? 138 ASN C N   1 
ATOM   3334 C  CA  . ASN C  3  138 ? 20.711 50.524  -22.781 1.00 50.90  ? 138 ASN C CA  1 
ATOM   3335 C  C   . ASN C  3  138 ? 21.873 51.121  -23.584 1.00 50.28  ? 138 ASN C C   1 
ATOM   3336 O  O   . ASN C  3  138 ? 21.666 51.672  -24.659 1.00 49.79  ? 138 ASN C O   1 
ATOM   3337 C  CB  . ASN C  3  138 ? 20.302 51.450  -21.617 1.00 49.04  ? 138 ASN C CB  1 
ATOM   3338 C  CG  . ASN C  3  138 ? 18.974 51.035  -20.971 1.00 49.49  ? 138 ASN C CG  1 
ATOM   3339 O  OD1 . ASN C  3  138 ? 18.259 50.171  -21.489 1.00 48.73  ? 138 ASN C OD1 1 
ATOM   3340 N  ND2 . ASN C  3  138 ? 18.640 51.655  -19.834 1.00 49.12  ? 138 ASN C ND2 1 
ATOM   3341 N  N   . ARG C  3  139 ? 23.091 51.006  -23.059 1.00 49.79  ? 139 ARG C N   1 
ATOM   3342 C  CA  . ARG C  3  139 ? 24.277 51.484  -23.761 1.00 49.03  ? 139 ARG C CA  1 
ATOM   3343 C  C   . ARG C  3  139 ? 24.316 50.840  -25.150 1.00 48.74  ? 139 ARG C C   1 
ATOM   3344 O  O   . ARG C  3  139 ? 24.689 51.478  -26.134 1.00 48.47  ? 139 ARG C O   1 
ATOM   3345 C  CB  . ARG C  3  139 ? 25.541 51.086  -22.985 1.00 48.75  ? 139 ARG C CB  1 
ATOM   3346 C  CG  . ARG C  3  139 ? 26.823 51.070  -23.826 1.00 47.54  ? 139 ARG C CG  1 
ATOM   3347 C  CD  . ARG C  3  139 ? 27.305 52.478  -24.151 1.00 46.17  ? 139 ARG C CD  1 
ATOM   3348 N  NE  . ARG C  3  139 ? 28.441 52.463  -25.076 1.00 44.11  ? 139 ARG C NE  1 
ATOM   3349 C  CZ  . ARG C  3  139 ? 28.346 52.316  -26.394 1.00 41.61  ? 139 ARG C CZ  1 
ATOM   3350 N  NH1 . ARG C  3  139 ? 27.164 52.169  -26.973 1.00 40.56  ? 139 ARG C NH1 1 
ATOM   3351 N  NH2 . ARG C  3  139 ? 29.440 52.323  -27.140 1.00 40.15  ? 139 ARG C NH2 1 
ATOM   3352 N  N   . ILE C  3  140 ? 23.937 49.567  -25.213 1.00 48.25  ? 140 ILE C N   1 
ATOM   3353 C  CA  . ILE C  3  140 ? 23.932 48.828  -26.462 1.00 48.83  ? 140 ILE C CA  1 
ATOM   3354 C  C   . ILE C  3  140 ? 22.815 49.273  -27.395 1.00 51.93  ? 140 ILE C C   1 
ATOM   3355 O  O   . ILE C  3  140 ? 23.059 49.476  -28.588 1.00 51.35  ? 140 ILE C O   1 
ATOM   3356 C  CB  . ILE C  3  140 ? 23.828 47.306  -26.187 1.00 47.17  ? 140 ILE C CB  1 
ATOM   3357 C  CG1 . ILE C  3  140 ? 25.211 46.789  -25.770 1.00 44.67  ? 140 ILE C CG1 1 
ATOM   3358 C  CG2 . ILE C  3  140 ? 23.281 46.546  -27.426 1.00 41.09  ? 140 ILE C CG2 1 
ATOM   3359 C  CD1 . ILE C  3  140 ? 25.222 45.347  -25.335 1.00 43.25  ? 140 ILE C CD1 1 
ATOM   3360 N  N   . THR C  3  141 ? 21.597 49.424  -26.869 1.00 54.09  ? 141 THR C N   1 
ATOM   3361 C  CA  . THR C  3  141 ? 20.489 49.852  -27.717 1.00 57.71  ? 141 THR C CA  1 
ATOM   3362 C  C   . THR C  3  141 ? 20.725 51.279  -28.237 1.00 58.89  ? 141 THR C C   1 
ATOM   3363 O  O   . THR C  3  141 ? 20.485 51.550  -29.415 1.00 57.47  ? 141 THR C O   1 
ATOM   3364 C  CB  . THR C  3  141 ? 19.110 49.770  -26.984 1.00 57.67  ? 141 THR C CB  1 
ATOM   3365 O  OG1 . THR C  3  141 ? 19.108 50.615  -25.829 1.00 59.24  ? 141 THR C OG1 1 
ATOM   3366 C  CG2 . THR C  3  141 ? 18.805 48.331  -26.570 1.00 58.01  ? 141 THR C CG2 1 
ATOM   3367 N  N   . ASN C  3  142 ? 21.214 52.175  -27.377 1.00 60.35  ? 142 ASN C N   1 
ATOM   3368 C  CA  . ASN C  3  142 ? 21.477 53.554  -27.792 1.00 63.29  ? 142 ASN C CA  1 
ATOM   3369 C  C   . ASN C  3  142 ? 22.321 53.613  -29.058 1.00 63.71  ? 142 ASN C C   1 
ATOM   3370 O  O   . ASN C  3  142 ? 22.175 54.523  -29.860 1.00 64.00  ? 142 ASN C O   1 
ATOM   3371 C  CB  . ASN C  3  142 ? 22.180 54.353  -26.689 1.00 64.78  ? 142 ASN C CB  1 
ATOM   3372 C  CG  . ASN C  3  142 ? 21.295 54.573  -25.471 1.00 68.10  ? 142 ASN C CG  1 
ATOM   3373 O  OD1 . ASN C  3  142 ? 20.074 54.673  -25.583 1.00 69.33  ? 142 ASN C OD1 1 
ATOM   3374 N  ND2 . ASN C  3  142 ? 21.918 54.668  -24.300 1.00 70.63  ? 142 ASN C ND2 1 
ATOM   3375 N  N   . GLY C  3  143 ? 23.212 52.652  -29.237 1.00 65.03  ? 143 GLY C N   1 
ATOM   3376 C  CA  . GLY C  3  143 ? 24.023 52.648  -30.440 1.00 66.38  ? 143 GLY C CA  1 
ATOM   3377 C  C   . GLY C  3  143 ? 23.228 52.059  -31.590 1.00 68.32  ? 143 GLY C C   1 
ATOM   3378 O  O   . GLY C  3  143 ? 23.466 52.380  -32.748 1.00 68.03  ? 143 GLY C O   1 
ATOM   3379 N  N   . MET C  3  144 ? 22.274 51.194  -31.263 1.00 70.43  ? 144 MET C N   1 
ATOM   3380 C  CA  . MET C  3  144 ? 21.435 50.546  -32.265 1.00 72.76  ? 144 MET C CA  1 
ATOM   3381 C  C   . MET C  3  144 ? 20.312 51.428  -32.795 1.00 74.13  ? 144 MET C C   1 
ATOM   3382 O  O   . MET C  3  144 ? 19.881 51.271  -33.936 1.00 73.60  ? 144 MET C O   1 
ATOM   3383 C  CB  . MET C  3  144 ? 20.821 49.273  -31.689 1.00 71.99  ? 144 MET C CB  1 
ATOM   3384 C  CG  . MET C  3  144 ? 21.818 48.150  -31.426 1.00 71.09  ? 144 MET C CG  1 
ATOM   3385 S  SD  . MET C  3  144 ? 20.948 46.674  -30.833 1.00 67.44  ? 144 MET C SD  1 
ATOM   3386 C  CE  . MET C  3  144 ? 20.517 45.895  -32.392 1.00 66.69  ? 144 MET C CE  1 
ATOM   3387 N  N   . THR C  3  145 ? 19.841 52.357  -31.971 1.00 76.19  ? 145 THR C N   1 
ATOM   3388 C  CA  . THR C  3  145 ? 18.750 53.219  -32.379 1.00 79.12  ? 145 THR C CA  1 
ATOM   3389 C  C   . THR C  3  145 ? 19.122 54.684  -32.557 1.00 82.12  ? 145 THR C C   1 
ATOM   3390 O  O   . THR C  3  145 ? 18.262 55.555  -32.430 1.00 82.33  ? 145 THR C O   1 
ATOM   3391 C  CB  . THR C  3  145 ? 17.603 53.136  -31.376 1.00 78.16  ? 145 THR C CB  1 
ATOM   3392 O  OG1 . THR C  3  145 ? 18.008 53.730  -30.139 1.00 75.83  ? 145 THR C OG1 1 
ATOM   3393 C  CG2 . THR C  3  145 ? 17.226 51.686  -31.133 1.00 77.74  ? 145 THR C CG2 1 
ATOM   3394 N  N   . GLU C  3  146 ? 20.389 54.955  -32.871 1.00 85.24  ? 146 GLU C N   1 
ATOM   3395 C  CA  . GLU C  3  146 ? 20.855 56.329  -33.060 1.00 88.65  ? 146 GLU C CA  1 
ATOM   3396 C  C   . GLU C  3  146 ? 19.913 57.109  -33.981 1.00 89.85  ? 146 GLU C C   1 
ATOM   3397 O  O   . GLU C  3  146 ? 19.414 58.180  -33.628 1.00 90.03  ? 146 GLU C O   1 
ATOM   3398 C  CB  . GLU C  3  146 ? 22.269 56.340  -33.668 1.00 90.61  ? 146 GLU C CB  1 
ATOM   3399 C  CG  . GLU C  3  146 ? 22.984 57.672  -33.507 1.00 94.09  ? 146 GLU C CG  1 
ATOM   3400 C  CD  . GLU C  3  146 ? 23.468 57.895  -32.090 1.00 96.63  ? 146 GLU C CD  1 
ATOM   3401 O  OE1 . GLU C  3  146 ? 24.515 57.308  -31.721 1.00 97.07  ? 146 GLU C OE1 1 
ATOM   3402 O  OE2 . GLU C  3  146 ? 22.796 58.640  -31.340 1.00 97.52  ? 146 GLU C OE2 1 
ATOM   3403 N  N   . GLY C  3  147 ? 19.666 56.560  -35.163 1.00 90.49  ? 147 GLY C N   1 
ATOM   3404 C  CA  . GLY C  3  147 ? 18.781 57.234  -36.091 1.00 91.78  ? 147 GLY C CA  1 
ATOM   3405 C  C   . GLY C  3  147 ? 17.388 56.638  -36.129 1.00 92.72  ? 147 GLY C C   1 
ATOM   3406 O  O   . GLY C  3  147 ? 17.069 55.906  -37.060 1.00 92.99  ? 147 GLY C O   1 
ATOM   3407 N  N   . LEU C  3  148 ? 16.566 56.951  -35.128 1.00 93.69  ? 148 LEU C N   1 
ATOM   3408 C  CA  . LEU C  3  148 ? 15.195 56.447  -35.058 1.00 94.76  ? 148 LEU C CA  1 
ATOM   3409 C  C   . LEU C  3  148 ? 14.277 57.415  -34.290 1.00 95.99  ? 148 LEU C C   1 
ATOM   3410 O  O   . LEU C  3  148 ? 14.739 58.395  -33.697 1.00 95.45  ? 148 LEU C O   1 
ATOM   3411 C  CB  . LEU C  3  148 ? 15.163 55.062  -34.385 1.00 94.24  ? 148 LEU C CB  1 
ATOM   3412 C  CG  . LEU C  3  148 ? 15.960 53.918  -35.024 1.00 93.56  ? 148 LEU C CG  1 
ATOM   3413 C  CD1 . LEU C  3  148 ? 15.676 52.638  -34.275 1.00 93.98  ? 148 LEU C CD1 1 
ATOM   3414 C  CD2 . LEU C  3  148 ? 15.573 53.752  -36.482 1.00 93.13  ? 148 LEU C CD2 1 
ATOM   3415 N  N   . ALA C  3  149 ? 12.977 57.140  -34.310 1.00 97.59  ? 149 ALA C N   1 
ATOM   3416 C  CA  . ALA C  3  149 ? 12.010 57.987  -33.632 1.00 99.20  ? 149 ALA C CA  1 
ATOM   3417 C  C   . ALA C  3  149 ? 11.688 57.464  -32.247 1.00 100.62 ? 149 ALA C C   1 
ATOM   3418 O  O   . ALA C  3  149 ? 11.973 56.316  -31.923 1.00 101.53 ? 149 ALA C O   1 
ATOM   3419 C  CB  . ALA C  3  149 ? 10.725 58.059  -34.453 1.00 98.93  ? 149 ALA C CB  1 
ATOM   3420 N  N   . GLU C  3  150 ? 11.089 58.311  -31.419 1.00 101.93 ? 150 GLU C N   1 
ATOM   3421 C  CA  . GLU C  3  150 ? 10.715 57.903  -30.063 1.00 103.52 ? 150 GLU C CA  1 
ATOM   3422 C  C   . GLU C  3  150 ? 9.777  56.713  -30.058 1.00 104.00 ? 150 GLU C C   1 
ATOM   3423 O  O   . GLU C  3  150 ? 9.719  55.988  -31.067 1.00 103.60 ? 150 GLU C O   1 
ATOM   3424 C  CB  . GLU C  3  150 ? 10.111 59.107  -29.334 1.00 104.88 ? 150 GLU C CB  1 
ATOM   3425 C  CG  . GLU C  3  150 ? 11.109 59.919  -28.495 1.00 106.54 ? 150 GLU C CG  1 
ATOM   3426 C  CD  . GLU C  3  150 ? 12.569 59.568  -28.752 1.00 107.61 ? 150 GLU C CD  1 
ATOM   3427 O  OE1 . GLU C  3  150 ? 13.357 59.631  -27.788 1.00 108.07 ? 150 GLU C OE1 1 
ATOM   3428 O  OE2 . GLU C  3  150 ? 12.934 59.241  -29.908 1.00 108.12 ? 150 GLU C OE2 1 
ATOM   3429 O  OXT . GLU C  3  150 ? 9.116  56.524  -28.964 1.00 104.70 ? 150 GLU C OXT 1 
ATOM   3430 N  N   . PHE D  4  3   ? 40.330 -3.648  -10.581 1.00 64.11  ? 3   PHE D N   1 
ATOM   3431 C  CA  . PHE D  4  3   ? 39.866 -2.891  -11.743 1.00 63.97  ? 3   PHE D CA  1 
ATOM   3432 C  C   . PHE D  4  3   ? 40.963 -2.302  -12.611 1.00 63.42  ? 3   PHE D C   1 
ATOM   3433 O  O   . PHE D  4  3   ? 41.588 -3.016  -13.395 1.00 65.44  ? 3   PHE D O   1 
ATOM   3434 C  CB  . PHE D  4  3   ? 38.935 -1.767  -11.308 1.00 65.18  ? 3   PHE D CB  1 
ATOM   3435 C  CG  . PHE D  4  3   ? 37.514 -2.194  -11.192 1.00 65.43  ? 3   PHE D CG  1 
ATOM   3436 C  CD1 . PHE D  4  3   ? 36.957 -2.479  -9.957  1.00 65.46  ? 3   PHE D CD1 1 
ATOM   3437 C  CD2 . PHE D  4  3   ? 36.745 -2.374  -12.334 1.00 65.42  ? 3   PHE D CD2 1 
ATOM   3438 C  CE1 . PHE D  4  3   ? 35.653 -2.943  -9.864  1.00 64.65  ? 3   PHE D CE1 1 
ATOM   3439 C  CE2 . PHE D  4  3   ? 35.446 -2.837  -12.249 1.00 64.00  ? 3   PHE D CE2 1 
ATOM   3440 C  CZ  . PHE D  4  3   ? 34.898 -3.123  -11.013 1.00 65.08  ? 3   PHE D CZ  1 
ATOM   3441 N  N   . CYS D  4  4   ? 41.166 -0.991  -12.499 1.00 60.76  ? 4   CYS D N   1 
ATOM   3442 C  CA  . CYS D  4  4   ? 42.201 -0.313  -13.264 1.00 58.78  ? 4   CYS D CA  1 
ATOM   3443 C  C   . CYS D  4  4   ? 42.900 0.734   -12.407 1.00 58.75  ? 4   CYS D C   1 
ATOM   3444 O  O   . CYS D  4  4   ? 42.329 1.254   -11.451 1.00 58.09  ? 4   CYS D O   1 
ATOM   3445 C  CB  . CYS D  4  4   ? 41.630 0.334   -14.539 1.00 56.35  ? 4   CYS D CB  1 
ATOM   3446 S  SG  . CYS D  4  4   ? 40.668 1.877   -14.352 1.00 54.25  ? 4   CYS D SG  1 
ATOM   3447 N  N   . SER D  4  5   ? 44.147 1.007   -12.763 1.00 58.95  ? 5   SER D N   1 
ATOM   3448 C  CA  . SER D  4  5   ? 45.002 1.970   -12.087 1.00 57.36  ? 5   SER D CA  1 
ATOM   3449 C  C   . SER D  4  5   ? 44.315 3.305   -11.783 1.00 57.12  ? 5   SER D C   1 
ATOM   3450 O  O   . SER D  4  5   ? 43.337 3.674   -12.413 1.00 56.98  ? 5   SER D O   1 
ATOM   3451 C  CB  . SER D  4  5   ? 46.227 2.220   -12.969 1.00 56.40  ? 5   SER D CB  1 
ATOM   3452 O  OG  . SER D  4  5   ? 46.916 3.372   -12.555 1.00 57.42  ? 5   SER D OG  1 
ATOM   3453 N  N   . GLU D  4  6   ? 44.858 4.014   -10.794 1.00 56.77  ? 6   GLU D N   1 
ATOM   3454 C  CA  . GLU D  4  6   ? 44.327 5.314   -10.396 1.00 56.73  ? 6   GLU D CA  1 
ATOM   3455 C  C   . GLU D  4  6   ? 44.697 6.371   -11.449 1.00 55.16  ? 6   GLU D C   1 
ATOM   3456 O  O   . GLU D  4  6   ? 43.977 7.347   -11.648 1.00 54.76  ? 6   GLU D O   1 
ATOM   3457 C  CB  . GLU D  4  6   ? 44.874 5.717   -9.027  1.00 58.23  ? 6   GLU D CB  1 
ATOM   3458 C  CG  . GLU D  4  6   ? 44.125 6.889   -8.391  1.00 62.13  ? 6   GLU D CG  1 
ATOM   3459 C  CD  . GLU D  4  6   ? 45.038 8.041   -7.994  1.00 65.91  ? 6   GLU D CD  1 
ATOM   3460 O  OE1 . GLU D  4  6   ? 45.650 7.988   -6.899  1.00 67.42  ? 6   GLU D OE1 1 
ATOM   3461 O  OE2 . GLU D  4  6   ? 45.151 8.998   -8.797  1.00 65.32  ? 6   GLU D OE2 1 
ATOM   3462 N  N   . ALA D  4  7   ? 45.823 6.163   -12.120 1.00 53.89  ? 7   ALA D N   1 
ATOM   3463 C  CA  . ALA D  4  7   ? 46.288 7.087   -13.141 1.00 52.19  ? 7   ALA D CA  1 
ATOM   3464 C  C   . ALA D  4  7   ? 45.451 6.869   -14.391 1.00 51.43  ? 7   ALA D C   1 
ATOM   3465 O  O   . ALA D  4  7   ? 45.080 7.832   -15.073 1.00 49.37  ? 7   ALA D O   1 
ATOM   3466 C  CB  . ALA D  4  7   ? 47.758 6.831   -13.451 1.00 51.52  ? 7   ALA D CB  1 
ATOM   3467 N  N   . ASP D  4  8   ? 45.153 5.600   -14.680 1.00 50.19  ? 8   ASP D N   1 
ATOM   3468 C  CA  . ASP D  4  8   ? 44.350 5.244   -15.855 1.00 50.84  ? 8   ASP D CA  1 
ATOM   3469 C  C   . ASP D  4  8   ? 42.933 5.798   -15.709 1.00 49.83  ? 8   ASP D C   1 
ATOM   3470 O  O   . ASP D  4  8   ? 42.424 6.500   -16.599 1.00 50.62  ? 8   ASP D O   1 
ATOM   3471 C  CB  . ASP D  4  8   ? 44.288 3.719   -16.032 1.00 51.22  ? 8   ASP D CB  1 
ATOM   3472 C  CG  . ASP D  4  8   ? 45.605 3.124   -16.519 1.00 53.30  ? 8   ASP D CG  1 
ATOM   3473 O  OD1 . ASP D  4  8   ? 45.777 1.890   -16.421 1.00 51.97  ? 8   ASP D OD1 1 
ATOM   3474 O  OD2 . ASP D  4  8   ? 46.467 3.891   -17.007 1.00 53.01  ? 8   ASP D OD2 1 
ATOM   3475 N  N   . ALA D  4  9   ? 42.309 5.464   -14.578 1.00 47.95  ? 9   ALA D N   1 
ATOM   3476 C  CA  . ALA D  4  9   ? 40.962 5.917   -14.258 1.00 45.33  ? 9   ALA D CA  1 
ATOM   3477 C  C   . ALA D  4  9   ? 40.900 7.422   -14.455 1.00 44.31  ? 9   ALA D C   1 
ATOM   3478 O  O   . ALA D  4  9   ? 39.987 7.938   -15.094 1.00 43.68  ? 9   ALA D O   1 
ATOM   3479 C  CB  . ALA D  4  9   ? 40.638 5.574   -12.832 1.00 45.77  ? 9   ALA D CB  1 
ATOM   3480 N  N   . THR D  4  10  ? 41.889 8.124   -13.914 1.00 42.89  ? 10  THR D N   1 
ATOM   3481 C  CA  . THR D  4  10  ? 41.932 9.566   -14.059 1.00 42.29  ? 10  THR D CA  1 
ATOM   3482 C  C   . THR D  4  10  ? 41.778 9.996   -15.502 1.00 42.11  ? 10  THR D C   1 
ATOM   3483 O  O   . THR D  4  10  ? 40.990 10.883  -15.806 1.00 44.03  ? 10  THR D O   1 
ATOM   3484 C  CB  . THR D  4  10  ? 43.231 10.133  -13.519 1.00 41.70  ? 10  THR D CB  1 
ATOM   3485 O  OG1 . THR D  4  10  ? 43.307 9.846   -12.119 1.00 42.12  ? 10  THR D OG1 1 
ATOM   3486 C  CG2 . THR D  4  10  ? 43.285 11.648  -13.734 1.00 40.64  ? 10  THR D CG2 1 
ATOM   3487 N  N   . ILE D  4  11  ? 42.524 9.356   -16.396 1.00 41.92  ? 11  ILE D N   1 
ATOM   3488 C  CA  . ILE D  4  11  ? 42.459 9.706   -17.805 1.00 40.65  ? 11  ILE D CA  1 
ATOM   3489 C  C   . ILE D  4  11  ? 41.091 9.408   -18.369 1.00 42.49  ? 11  ILE D C   1 
ATOM   3490 O  O   . ILE D  4  11  ? 40.507 10.240  -19.075 1.00 42.52  ? 11  ILE D O   1 
ATOM   3491 C  CB  . ILE D  4  11  ? 43.507 8.947   -18.622 1.00 40.36  ? 11  ILE D CB  1 
ATOM   3492 C  CG1 . ILE D  4  11  ? 44.908 9.372   -18.173 1.00 38.55  ? 11  ILE D CG1 1 
ATOM   3493 C  CG2 . ILE D  4  11  ? 43.281 9.206   -20.129 1.00 36.60  ? 11  ILE D CG2 1 
ATOM   3494 C  CD1 . ILE D  4  11  ? 46.008 8.636   -18.883 1.00 39.76  ? 11  ILE D CD1 1 
ATOM   3495 N  N   . VAL D  4  12  ? 40.565 8.227   -18.039 1.00 42.54  ? 12  VAL D N   1 
ATOM   3496 C  CA  . VAL D  4  12  ? 39.263 7.842   -18.548 1.00 43.13  ? 12  VAL D CA  1 
ATOM   3497 C  C   . VAL D  4  12  ? 38.208 8.840   -18.108 1.00 43.95  ? 12  VAL D C   1 
ATOM   3498 O  O   . VAL D  4  12  ? 37.445 9.340   -18.924 1.00 44.55  ? 12  VAL D O   1 
ATOM   3499 C  CB  . VAL D  4  12  ? 38.882 6.434   -18.071 1.00 43.20  ? 12  VAL D CB  1 
ATOM   3500 C  CG1 . VAL D  4  12  ? 37.477 6.077   -18.566 1.00 42.21  ? 12  VAL D CG1 1 
ATOM   3501 C  CG2 . VAL D  4  12  ? 39.904 5.431   -18.586 1.00 42.69  ? 12  VAL D CG2 1 
ATOM   3502 N  N   . ILE D  4  13  ? 38.195 9.163   -16.823 1.00 45.55  ? 13  ILE D N   1 
ATOM   3503 C  CA  . ILE D  4  13  ? 37.220 10.103  -16.304 1.00 45.94  ? 13  ILE D CA  1 
ATOM   3504 C  C   . ILE D  4  13  ? 37.338 11.458  -16.982 1.00 47.38  ? 13  ILE D C   1 
ATOM   3505 O  O   . ILE D  4  13  ? 36.315 12.107  -17.263 1.00 46.82  ? 13  ILE D O   1 
ATOM   3506 C  CB  . ILE D  4  13  ? 37.375 10.265  -14.784 1.00 45.26  ? 13  ILE D CB  1 
ATOM   3507 C  CG1 . ILE D  4  13  ? 37.157 8.897   -14.114 1.00 43.41  ? 13  ILE D CG1 1 
ATOM   3508 C  CG2 . ILE D  4  13  ? 36.405 11.315  -14.273 1.00 43.70  ? 13  ILE D CG2 1 
ATOM   3509 C  CD1 . ILE D  4  13  ? 37.347 8.872   -12.626 1.00 44.37  ? 13  ILE D CD1 1 
ATOM   3510 N  N   . LYS D  4  14  ? 38.571 11.875  -17.272 1.00 47.60  ? 14  LYS D N   1 
ATOM   3511 C  CA  . LYS D  4  14  ? 38.788 13.168  -17.907 1.00 48.99  ? 14  LYS D CA  1 
ATOM   3512 C  C   . LYS D  4  14  ? 38.303 13.179  -19.341 1.00 48.12  ? 14  LYS D C   1 
ATOM   3513 O  O   . LYS D  4  14  ? 37.625 14.114  -19.757 1.00 48.59  ? 14  LYS D O   1 
ATOM   3514 C  CB  . LYS D  4  14  ? 40.268 13.569  -17.873 1.00 52.15  ? 14  LYS D CB  1 
ATOM   3515 C  CG  . LYS D  4  14  ? 40.669 14.355  -16.628 1.00 59.19  ? 14  LYS D CG  1 
ATOM   3516 C  CD  . LYS D  4  14  ? 42.130 14.838  -16.687 1.00 64.87  ? 14  LYS D CD  1 
ATOM   3517 C  CE  . LYS D  4  14  ? 42.549 15.551  -15.383 1.00 66.38  ? 14  LYS D CE  1 
ATOM   3518 N  NZ  . LYS D  4  14  ? 43.987 15.959  -15.362 1.00 67.68  ? 14  LYS D NZ  1 
ATOM   3519 N  N   . GLN D  4  15  ? 38.624 12.137  -20.095 1.00 47.14  ? 15  GLN D N   1 
ATOM   3520 C  CA  . GLN D  4  15  ? 38.216 12.099  -21.496 1.00 46.08  ? 15  GLN D CA  1 
ATOM   3521 C  C   . GLN D  4  15  ? 36.712 11.947  -21.626 1.00 44.54  ? 15  GLN D C   1 
ATOM   3522 O  O   . GLN D  4  15  ? 36.095 12.567  -22.495 1.00 41.19  ? 15  GLN D O   1 
ATOM   3523 C  CB  . GLN D  4  15  ? 38.906 10.961  -22.259 1.00 45.36  ? 15  GLN D CB  1 
ATOM   3524 C  CG  . GLN D  4  15  ? 40.431 11.001  -22.203 1.00 46.28  ? 15  GLN D CG  1 
ATOM   3525 C  CD  . GLN D  4  15  ? 41.081 10.155  -23.283 1.00 47.73  ? 15  GLN D CD  1 
ATOM   3526 O  OE1 . GLN D  4  15  ? 40.718 9.005   -23.490 1.00 48.73  ? 15  GLN D OE1 1 
ATOM   3527 N  NE2 . GLN D  4  15  ? 42.050 10.723  -23.968 1.00 47.20  ? 15  GLN D NE2 1 
ATOM   3528 N  N   . TRP D  4  16  ? 36.133 11.126  -20.752 1.00 42.88  ? 16  TRP D N   1 
ATOM   3529 C  CA  . TRP D  4  16  ? 34.703 10.888  -20.772 1.00 44.68  ? 16  TRP D CA  1 
ATOM   3530 C  C   . TRP D  4  16  ? 33.929 12.156  -20.450 1.00 47.40  ? 16  TRP D C   1 
ATOM   3531 O  O   . TRP D  4  16  ? 32.934 12.478  -21.106 1.00 47.10  ? 16  TRP D O   1 
ATOM   3532 C  CB  . TRP D  4  16  ? 34.321 9.790   -19.775 1.00 43.62  ? 16  TRP D CB  1 
ATOM   3533 C  CG  . TRP D  4  16  ? 32.853 9.699   -19.555 1.00 40.06  ? 16  TRP D CG  1 
ATOM   3534 C  CD1 . TRP D  4  16  ? 32.156 10.136  -18.469 1.00 39.39  ? 16  TRP D CD1 1 
ATOM   3535 C  CD2 . TRP D  4  16  ? 31.892 9.161   -20.458 1.00 40.04  ? 16  TRP D CD2 1 
ATOM   3536 N  NE1 . TRP D  4  16  ? 30.816 9.902   -18.643 1.00 39.39  ? 16  TRP D NE1 1 
ATOM   3537 C  CE2 . TRP D  4  16  ? 30.627 9.305   -19.857 1.00 40.30  ? 16  TRP D CE2 1 
ATOM   3538 C  CE3 . TRP D  4  16  ? 31.980 8.567   -21.726 1.00 39.81  ? 16  TRP D CE3 1 
ATOM   3539 C  CZ2 . TRP D  4  16  ? 29.452 8.874   -20.476 1.00 42.48  ? 16  TRP D CZ2 1 
ATOM   3540 C  CZ3 . TRP D  4  16  ? 30.812 8.143   -22.343 1.00 41.06  ? 16  TRP D CZ3 1 
ATOM   3541 C  CH2 . TRP D  4  16  ? 29.563 8.298   -21.719 1.00 42.22  ? 16  TRP D CH2 1 
ATOM   3542 N  N   . ASN D  4  17  ? 34.387 12.890  -19.444 1.00 50.70  ? 17  ASN D N   1 
ATOM   3543 C  CA  . ASN D  4  17  ? 33.695 14.109  -19.065 1.00 54.78  ? 17  ASN D CA  1 
ATOM   3544 C  C   . ASN D  4  17  ? 33.786 15.182  -20.141 1.00 54.19  ? 17  ASN D C   1 
ATOM   3545 O  O   . ASN D  4  17  ? 33.066 16.181  -20.102 1.00 54.36  ? 17  ASN D O   1 
ATOM   3546 C  CB  . ASN D  4  17  ? 34.218 14.602  -17.719 1.00 60.18  ? 17  ASN D CB  1 
ATOM   3547 C  CG  . ASN D  4  17  ? 33.749 13.714  -16.562 1.00 66.20  ? 17  ASN D CG  1 
ATOM   3548 O  OD1 . ASN D  4  17  ? 34.482 13.480  -15.598 1.00 69.15  ? 17  ASN D OD1 1 
ATOM   3549 N  ND2 . ASN D  4  17  ? 32.511 13.220  -16.660 1.00 66.92  ? 17  ASN D ND2 1 
ATOM   3550 N  N   . GLN D  4  18  ? 34.664 14.959  -21.112 1.00 53.92  ? 18  GLN D N   1 
ATOM   3551 C  CA  . GLN D  4  18  ? 34.833 15.874  -22.239 1.00 54.04  ? 18  GLN D CA  1 
ATOM   3552 C  C   . GLN D  4  18  ? 33.554 15.884  -23.047 1.00 53.06  ? 18  GLN D C   1 
ATOM   3553 O  O   . GLN D  4  18  ? 33.050 16.932  -23.438 1.00 53.03  ? 18  GLN D O   1 
ATOM   3554 C  CB  . GLN D  4  18  ? 35.925 15.376  -23.177 1.00 55.87  ? 18  GLN D CB  1 
ATOM   3555 C  CG  . GLN D  4  18  ? 37.243 16.075  -23.121 1.00 55.85  ? 18  GLN D CG  1 
ATOM   3556 C  CD  . GLN D  4  18  ? 38.161 15.568  -24.208 1.00 58.35  ? 18  GLN D CD  1 
ATOM   3557 O  OE1 . GLN D  4  18  ? 37.845 15.658  -25.399 1.00 58.33  ? 18  GLN D OE1 1 
ATOM   3558 N  NE2 . GLN D  4  18  ? 39.302 15.017  -23.805 1.00 59.88  ? 18  GLN D NE2 1 
ATOM   3559 N  N   . ILE D  4  19  ? 33.049 14.685  -23.315 1.00 52.65  ? 19  ILE D N   1 
ATOM   3560 C  CA  . ILE D  4  19  ? 31.844 14.514  -24.114 1.00 52.74  ? 19  ILE D CA  1 
ATOM   3561 C  C   . ILE D  4  19  ? 30.574 14.220  -23.320 1.00 53.19  ? 19  ILE D C   1 
ATOM   3562 O  O   . ILE D  4  19  ? 29.495 14.152  -23.901 1.00 52.03  ? 19  ILE D O   1 
ATOM   3563 C  CB  . ILE D  4  19  ? 32.046 13.383  -25.123 1.00 51.72  ? 19  ILE D CB  1 
ATOM   3564 C  CG1 . ILE D  4  19  ? 32.433 12.101  -24.383 1.00 51.42  ? 19  ILE D CG1 1 
ATOM   3565 C  CG2 . ILE D  4  19  ? 33.160 13.747  -26.088 1.00 51.44  ? 19  ILE D CG2 1 
ATOM   3566 C  CD1 . ILE D  4  19  ? 32.446 10.868  -25.241 1.00 52.54  ? 19  ILE D CD1 1 
ATOM   3567 N  N   . TYR D  4  20  ? 30.708 14.028  -22.006 1.00 54.44  ? 20  TYR D N   1 
ATOM   3568 C  CA  . TYR D  4  20  ? 29.548 13.732  -21.156 1.00 57.90  ? 20  TYR D CA  1 
ATOM   3569 C  C   . TYR D  4  20  ? 29.666 14.290  -19.777 1.00 59.96  ? 20  TYR D C   1 
ATOM   3570 O  O   . TYR D  4  20  ? 30.665 14.000  -19.057 1.00 60.47  ? 20  TYR D O   1 
ATOM   3571 C  CB  . TYR D  4  20  ? 29.301 12.218  -21.099 1.00 56.51  ? 20  TYR D CB  1 
ATOM   3572 C  CG  . TYR D  4  20  ? 28.045 11.805  -20.350 1.00 55.68  ? 20  TYR D CG  1 
ATOM   3573 C  CD1 . TYR D  4  20  ? 27.955 11.919  -18.963 1.00 55.87  ? 20  TYR D CD1 1 
ATOM   3574 C  CD2 . TYR D  4  20  ? 26.943 11.301  -21.033 1.00 55.90  ? 20  TYR D CD2 1 
ATOM   3575 C  CE1 . TYR D  4  20  ? 26.788 11.540  -18.274 1.00 56.24  ? 20  TYR D CE1 1 
ATOM   3576 C  CE2 . TYR D  4  20  ? 25.775 10.920  -20.356 1.00 56.04  ? 20  TYR D CE2 1 
ATOM   3577 C  CZ  . TYR D  4  20  ? 25.703 11.041  -18.980 1.00 56.01  ? 20  TYR D CZ  1 
ATOM   3578 O  OH  . TYR D  4  20  ? 24.561 10.647  -18.308 1.00 56.49  ? 20  TYR D OH  1 
ATOM   3579 N  N   . ASN D  4  21  ? 28.722 15.160  -19.415 1.00 62.40  ? 21  ASN D N   1 
ATOM   3580 C  CA  . ASN D  4  21  ? 28.700 15.711  -18.080 1.00 66.16  ? 21  ASN D CA  1 
ATOM   3581 C  C   . ASN D  4  21  ? 27.355 16.381  -17.890 1.00 67.96  ? 21  ASN D C   1 
ATOM   3582 O  O   . ASN D  4  21  ? 26.650 16.617  -18.874 1.00 69.33  ? 21  ASN D O   1 
ATOM   3583 C  CB  . ASN D  4  21  ? 29.842 16.704  -17.922 1.00 66.59  ? 21  ASN D CB  1 
ATOM   3584 C  CG  . ASN D  4  21  ? 29.754 17.831  -18.924 1.00 68.50  ? 21  ASN D CG  1 
ATOM   3585 O  OD1 . ASN D  4  21  ? 28.794 18.643  -18.876 1.00 66.89  ? 21  ASN D OD1 1 
ATOM   3586 N  ND2 . ASN D  4  21  ? 30.727 17.882  -19.869 1.00 68.50  ? 21  ASN D ND2 1 
ATOM   3587 N  N   . ALA D  4  22  ? 27.005 16.689  -16.643 1.00 68.98  ? 22  ALA D N   1 
ATOM   3588 C  CA  . ALA D  4  22  ? 25.723 17.332  -16.347 1.00 69.53  ? 22  ALA D CA  1 
ATOM   3589 C  C   . ALA D  4  22  ? 25.483 18.644  -17.145 1.00 69.78  ? 22  ALA D C   1 
ATOM   3590 O  O   . ALA D  4  22  ? 24.400 19.260  -17.047 1.00 70.27  ? 22  ALA D O   1 
ATOM   3591 C  CB  . ALA D  4  22  ? 25.634 17.622  -14.823 1.00 70.02  ? 22  ALA D CB  1 
ATOM   3592 N  N   . GLY D  4  23  ? 26.507 19.139  -17.845 1.00 69.83  ? 23  GLY D N   1 
ATOM   3593 C  CA  . GLY D  4  23  ? 26.336 20.377  -18.602 1.00 70.03  ? 23  GLY D CA  1 
ATOM   3594 C  C   . GLY D  4  23  ? 25.767 20.443  -20.022 1.00 70.69  ? 23  GLY D C   1 
ATOM   3595 O  O   . GLY D  4  23  ? 25.376 21.564  -20.452 1.00 69.89  ? 23  GLY D O   1 
ATOM   3596 N  N   . ILE D  4  24  ? 25.755 19.341  -20.776 1.00 72.19  ? 24  ILE D N   1 
ATOM   3597 C  CA  . ILE D  4  24  ? 25.140 19.476  -22.066 1.00 73.98  ? 24  ILE D CA  1 
ATOM   3598 C  C   . ILE D  4  24  ? 23.974 18.580  -22.454 1.00 75.46  ? 24  ILE D C   1 
ATOM   3599 O  O   . ILE D  4  24  ? 23.763 17.413  -21.971 1.00 75.77  ? 24  ILE D O   1 
ATOM   3600 C  CB  . ILE D  4  24  ? 26.208 19.457  -23.209 1.00 72.81  ? 24  ILE D CB  1 
ATOM   3601 C  CG1 . ILE D  4  24  ? 27.486 18.723  -22.728 1.00 72.26  ? 24  ILE D CG1 1 
ATOM   3602 C  CG2 . ILE D  4  24  ? 26.443 20.935  -23.625 1.00 71.12  ? 24  ILE D CG2 1 
ATOM   3603 C  CD1 . ILE D  4  24  ? 27.331 17.209  -22.775 1.00 69.92  ? 24  ILE D CD1 1 
ATOM   3604 N  N   . GLY D  4  25  ? 23.146 19.208  -23.290 1.00 75.93  ? 25  GLY D N   1 
ATOM   3605 C  CA  . GLY D  4  25  ? 22.030 18.521  -23.969 1.00 77.81  ? 25  GLY D CA  1 
ATOM   3606 C  C   . GLY D  4  25  ? 21.744 17.011  -24.069 1.00 78.96  ? 25  GLY D C   1 
ATOM   3607 O  O   . GLY D  4  25  ? 22.541 16.256  -24.596 1.00 79.58  ? 25  GLY D O   1 
ATOM   3608 N  N   . ALA D  4  26  ? 20.519 16.625  -23.677 1.00 80.37  ? 26  ALA D N   1 
ATOM   3609 C  CA  . ALA D  4  26  ? 20.167 15.217  -23.654 1.00 80.92  ? 26  ALA D CA  1 
ATOM   3610 C  C   . ALA D  4  26  ? 20.254 14.885  -25.145 1.00 80.43  ? 26  ALA D C   1 
ATOM   3611 O  O   . ALA D  4  26  ? 20.525 13.751  -25.512 1.00 80.69  ? 26  ALA D O   1 
ATOM   3612 C  CB  . ALA D  4  26  ? 18.767 15.026  -23.127 1.00 82.62  ? 26  ALA D CB  1 
ATOM   3613 N  N   . LYS D  4  27  ? 19.980 15.852  -26.030 1.00 79.05  ? 27  LYS D N   1 
ATOM   3614 C  CA  . LYS D  4  27  ? 20.016 15.542  -27.485 1.00 78.85  ? 27  LYS D CA  1 
ATOM   3615 C  C   . LYS D  4  27  ? 21.335 14.879  -27.852 1.00 77.22  ? 27  LYS D C   1 
ATOM   3616 O  O   . LYS D  4  27  ? 21.353 13.802  -28.442 1.00 76.86  ? 27  LYS D O   1 
ATOM   3617 C  CB  . LYS D  4  27  ? 19.825 16.782  -28.376 1.00 80.97  ? 27  LYS D CB  1 
ATOM   3618 C  CG  . LYS D  4  27  ? 19.925 16.450  -29.883 1.00 82.85  ? 27  LYS D CG  1 
ATOM   3619 C  CD  . LYS D  4  27  ? 19.885 17.686  -30.777 1.00 84.73  ? 27  LYS D CD  1 
ATOM   3620 C  CE  . LYS D  4  27  ? 18.485 18.264  -30.897 1.00 85.60  ? 27  LYS D CE  1 
ATOM   3621 N  NZ  . LYS D  4  27  ? 18.452 19.400  -31.864 1.00 85.07  ? 27  LYS D NZ  1 
ATOM   3622 N  N   . SER D  4  28  ? 22.439 15.526  -27.492 1.00 75.16  ? 28  SER D N   1 
ATOM   3623 C  CA  . SER D  4  28  ? 23.762 14.971  -27.771 1.00 73.63  ? 28  SER D CA  1 
ATOM   3624 C  C   . SER D  4  28  ? 23.909 13.598  -27.125 1.00 71.05  ? 28  SER D C   1 
ATOM   3625 O  O   . SER D  4  28  ? 24.547 12.704  -27.677 1.00 69.28  ? 28  SER D O   1 
ATOM   3626 C  CB  . SER D  4  28  ? 24.860 15.907  -27.255 1.00 73.85  ? 28  SER D CB  1 
ATOM   3627 O  OG  . SER D  4  28  ? 24.762 17.166  -27.883 1.00 74.40  ? 28  SER D OG  1 
ATOM   3628 N  N   . ARG D  4  29  ? 23.306 13.453  -25.947 1.00 69.78  ? 29  ARG D N   1 
ATOM   3629 C  CA  . ARG D  4  29  ? 23.352 12.190  -25.213 1.00 68.67  ? 29  ARG D CA  1 
ATOM   3630 C  C   . ARG D  4  29  ? 22.799 11.033  -26.018 1.00 66.50  ? 29  ARG D C   1 
ATOM   3631 O  O   . ARG D  4  29  ? 23.435 9.989   -26.114 1.00 64.61  ? 29  ARG D O   1 
ATOM   3632 C  CB  . ARG D  4  29  ? 22.592 12.313  -23.893 1.00 70.10  ? 29  ARG D CB  1 
ATOM   3633 C  CG  . ARG D  4  29  ? 23.506 12.609  -22.730 1.00 72.30  ? 29  ARG D CG  1 
ATOM   3634 C  CD  . ARG D  4  29  ? 22.759 13.022  -21.477 1.00 73.24  ? 29  ARG D CD  1 
ATOM   3635 N  NE  . ARG D  4  29  ? 23.595 13.912  -20.670 1.00 74.07  ? 29  ARG D NE  1 
ATOM   3636 C  CZ  . ARG D  4  29  ? 23.602 13.936  -19.344 1.00 74.38  ? 29  ARG D CZ  1 
ATOM   3637 N  NH1 . ARG D  4  29  ? 24.397 14.783  -18.711 1.00 76.20  ? 29  ARG D NH1 1 
ATOM   3638 N  NH2 . ARG D  4  29  ? 22.830 13.106  -18.650 1.00 72.55  ? 29  ARG D NH2 1 
ATOM   3639 N  N   . TRP D  4  30  ? 21.619 11.216  -26.602 1.00 65.42  ? 30  TRP D N   1 
ATOM   3640 C  CA  . TRP D  4  30  ? 21.021 10.137  -27.368 1.00 65.79  ? 30  TRP D CA  1 
ATOM   3641 C  C   . TRP D  4  30  ? 21.540 10.033  -28.802 1.00 63.84  ? 30  TRP D C   1 
ATOM   3642 O  O   . TRP D  4  30  ? 21.361 8.994   -29.444 1.00 63.29  ? 30  TRP D O   1 
ATOM   3643 C  CB  . TRP D  4  30  ? 19.481 10.221  -27.341 1.00 68.53  ? 30  TRP D CB  1 
ATOM   3644 C  CG  . TRP D  4  30  ? 18.866 11.347  -28.125 1.00 70.61  ? 30  TRP D CG  1 
ATOM   3645 C  CD1 . TRP D  4  30  ? 19.090 11.656  -29.441 1.00 71.67  ? 30  TRP D CD1 1 
ATOM   3646 C  CD2 . TRP D  4  30  ? 17.892 12.284  -27.652 1.00 70.37  ? 30  TRP D CD2 1 
ATOM   3647 N  NE1 . TRP D  4  30  ? 18.317 12.731  -29.813 1.00 72.37  ? 30  TRP D NE1 1 
ATOM   3648 C  CE2 . TRP D  4  30  ? 17.572 13.135  -28.734 1.00 71.77  ? 30  TRP D CE2 1 
ATOM   3649 C  CE3 . TRP D  4  30  ? 17.262 12.487  -26.422 1.00 69.84  ? 30  TRP D CE3 1 
ATOM   3650 C  CZ2 . TRP D  4  30  ? 16.646 14.178  -28.618 1.00 72.60  ? 30  TRP D CZ2 1 
ATOM   3651 C  CZ3 . TRP D  4  30  ? 16.342 13.520  -26.307 1.00 72.16  ? 30  TRP D CZ3 1 
ATOM   3652 C  CH2 . TRP D  4  30  ? 16.043 14.353  -27.399 1.00 72.42  ? 30  TRP D CH2 1 
ATOM   3653 N  N   . THR D  4  31  ? 22.177 11.084  -29.324 1.00 59.76  ? 31  THR D N   1 
ATOM   3654 C  CA  . THR D  4  31  ? 22.707 10.957  -30.678 1.00 56.80  ? 31  THR D CA  1 
ATOM   3655 C  C   . THR D  4  31  ? 23.977 10.110  -30.592 1.00 55.72  ? 31  THR D C   1 
ATOM   3656 O  O   . THR D  4  31  ? 24.384 9.479   -31.569 1.00 57.29  ? 31  THR D O   1 
ATOM   3657 C  CB  . THR D  4  31  ? 22.965 12.338  -31.404 1.00 55.50  ? 31  THR D CB  1 
ATOM   3658 O  OG1 . THR D  4  31  ? 24.244 12.316  -32.056 1.00 51.26  ? 31  THR D OG1 1 
ATOM   3659 C  CG2 . THR D  4  31  ? 22.911 13.504  -30.451 1.00 56.29  ? 31  THR D CG2 1 
ATOM   3660 N  N   . MET D  4  32  ? 24.594 10.084  -29.414 1.00 52.57  ? 32  MET D N   1 
ATOM   3661 C  CA  . MET D  4  32  ? 25.776 9.255   -29.226 1.00 52.10  ? 32  MET D CA  1 
ATOM   3662 C  C   . MET D  4  32  ? 25.206 7.854   -28.984 1.00 51.89  ? 32  MET D C   1 
ATOM   3663 O  O   . MET D  4  32  ? 25.761 6.865   -29.445 1.00 51.28  ? 32  MET D O   1 
ATOM   3664 C  CB  . MET D  4  32  ? 26.595 9.679   -27.992 1.00 51.81  ? 32  MET D CB  1 
ATOM   3665 C  CG  . MET D  4  32  ? 27.443 10.913  -28.175 1.00 52.67  ? 32  MET D CG  1 
ATOM   3666 S  SD  . MET D  4  32  ? 28.084 11.551  -26.604 1.00 53.39  ? 32  MET D SD  1 
ATOM   3667 C  CE  . MET D  4  32  ? 29.339 10.363  -26.253 1.00 55.31  ? 32  MET D CE  1 
ATOM   3668 N  N   . GLY D  4  33  ? 24.095 7.796   -28.253 1.00 51.18  ? 33  GLY D N   1 
ATOM   3669 C  CA  . GLY D  4  33  ? 23.460 6.536   -27.969 1.00 52.18  ? 33  GLY D CA  1 
ATOM   3670 C  C   . GLY D  4  33  ? 23.021 5.813   -29.231 1.00 53.96  ? 33  GLY D C   1 
ATOM   3671 O  O   . GLY D  4  33  ? 23.268 4.613   -29.401 1.00 53.24  ? 33  GLY D O   1 
ATOM   3672 N  N   . ASN D  4  34  ? 22.376 6.538   -30.136 1.00 54.86  ? 34  ASN D N   1 
ATOM   3673 C  CA  . ASN D  4  34  ? 21.926 5.898   -31.354 1.00 57.23  ? 34  ASN D CA  1 
ATOM   3674 C  C   . ASN D  4  34  ? 23.102 5.391   -32.157 1.00 57.63  ? 34  ASN D C   1 
ATOM   3675 O  O   . ASN D  4  34  ? 23.048 4.286   -32.701 1.00 59.60  ? 34  ASN D O   1 
ATOM   3676 C  CB  . ASN D  4  34  ? 21.045 6.835   -32.191 1.00 58.61  ? 34  ASN D CB  1 
ATOM   3677 C  CG  . ASN D  4  34  ? 19.641 7.003   -31.601 1.00 59.62  ? 34  ASN D CG  1 
ATOM   3678 O  OD1 . ASN D  4  34  ? 19.064 6.071   -31.027 1.00 57.79  ? 34  ASN D OD1 1 
ATOM   3679 N  ND2 . ASN D  4  34  ? 19.083 8.197   -31.758 1.00 62.42  ? 34  ASN D ND2 1 
ATOM   3680 N  N   . GLU D  4  35  ? 24.177 6.173   -32.221 1.00 56.53  ? 35  GLU D N   1 
ATOM   3681 C  CA  . GLU D  4  35  ? 25.346 5.741   -32.986 1.00 53.86  ? 35  GLU D CA  1 
ATOM   3682 C  C   . GLU D  4  35  ? 25.942 4.475   -32.388 1.00 52.88  ? 35  GLU D C   1 
ATOM   3683 O  O   . GLU D  4  35  ? 26.408 3.600   -33.108 1.00 52.30  ? 35  GLU D O   1 
ATOM   3684 C  CB  . GLU D  4  35  ? 26.418 6.812   -32.992 1.00 53.17  ? 35  GLU D CB  1 
ATOM   3685 C  CG  . GLU D  4  35  ? 27.249 6.774   -34.235 1.00 55.29  ? 35  GLU D CG  1 
ATOM   3686 C  CD  . GLU D  4  35  ? 26.542 7.440   -35.378 1.00 57.59  ? 35  GLU D CD  1 
ATOM   3687 O  OE1 . GLU D  4  35  ? 26.957 7.221   -36.533 1.00 57.92  ? 35  GLU D OE1 1 
ATOM   3688 O  OE2 . GLU D  4  35  ? 25.574 8.194   -35.116 1.00 59.42  ? 35  GLU D OE2 1 
ATOM   3689 N  N   . ILE D  4  36  ? 25.923 4.393   -31.062 1.00 52.77  ? 36  ILE D N   1 
ATOM   3690 C  CA  . ILE D  4  36  ? 26.477 3.252   -30.357 1.00 52.75  ? 36  ILE D CA  1 
ATOM   3691 C  C   . ILE D  4  36  ? 25.688 1.968   -30.631 1.00 52.75  ? 36  ILE D C   1 
ATOM   3692 O  O   . ILE D  4  36  ? 26.275 0.950   -31.000 1.00 52.09  ? 36  ILE D O   1 
ATOM   3693 C  CB  . ILE D  4  36  ? 26.548 3.556   -28.825 1.00 51.57  ? 36  ILE D CB  1 
ATOM   3694 C  CG1 . ILE D  4  36  ? 27.529 4.709   -28.608 1.00 49.53  ? 36  ILE D CG1 1 
ATOM   3695 C  CG2 . ILE D  4  36  ? 26.967 2.306   -28.028 1.00 50.21  ? 36  ILE D CG2 1 
ATOM   3696 C  CD1 . ILE D  4  36  ? 27.691 5.119   -27.169 1.00 49.96  ? 36  ILE D CD1 1 
ATOM   3697 N  N   . PHE D  4  37  ? 24.367 2.024   -30.492 1.00 52.53  ? 37  PHE D N   1 
ATOM   3698 C  CA  . PHE D  4  37  ? 23.552 0.845   -30.741 1.00 53.69  ? 37  PHE D CA  1 
ATOM   3699 C  C   . PHE D  4  37  ? 23.455 0.486   -32.226 1.00 55.72  ? 37  PHE D C   1 
ATOM   3700 O  O   . PHE D  4  37  ? 23.581 -0.692  -32.581 1.00 56.40  ? 37  PHE D O   1 
ATOM   3701 C  CB  . PHE D  4  37  ? 22.170 1.029   -30.114 1.00 52.07  ? 37  PHE D CB  1 
ATOM   3702 C  CG  . PHE D  4  37  ? 22.165 0.827   -28.632 1.00 49.41  ? 37  PHE D CG  1 
ATOM   3703 C  CD1 . PHE D  4  37  ? 22.066 -0.453  -28.099 1.00 49.48  ? 37  PHE D CD1 1 
ATOM   3704 C  CD2 . PHE D  4  37  ? 22.350 1.898   -27.764 1.00 48.00  ? 37  PHE D CD2 1 
ATOM   3705 C  CE1 . PHE D  4  37  ? 22.156 -0.665  -26.717 1.00 49.04  ? 37  PHE D CE1 1 
ATOM   3706 C  CE2 . PHE D  4  37  ? 22.445 1.699   -26.386 1.00 46.45  ? 37  PHE D CE2 1 
ATOM   3707 C  CZ  . PHE D  4  37  ? 22.348 0.417   -25.862 1.00 47.17  ? 37  PHE D CZ  1 
ATOM   3708 N  N   . SER D  4  38  ? 23.247 1.479   -33.089 1.00 55.73  ? 38  SER D N   1 
ATOM   3709 C  CA  . SER D  4  38  ? 23.194 1.211   -34.526 1.00 57.73  ? 38  SER D CA  1 
ATOM   3710 C  C   . SER D  4  38  ? 24.397 0.336   -34.879 1.00 59.53  ? 38  SER D C   1 
ATOM   3711 O  O   . SER D  4  38  ? 24.276 -0.636  -35.635 1.00 61.63  ? 38  SER D O   1 
ATOM   3712 C  CB  . SER D  4  38  ? 23.295 2.508   -35.339 1.00 55.95  ? 38  SER D CB  1 
ATOM   3713 O  OG  . SER D  4  38  ? 22.176 3.345   -35.135 1.00 57.81  ? 38  SER D OG  1 
ATOM   3714 N  N   . SER D  4  39  ? 25.554 0.701   -34.326 1.00 59.61  ? 39  SER D N   1 
ATOM   3715 C  CA  . SER D  4  39  ? 26.801 -0.012  -34.560 1.00 59.75  ? 39  SER D CA  1 
ATOM   3716 C  C   . SER D  4  39  ? 26.771 -1.407  -33.948 1.00 60.66  ? 39  SER D C   1 
ATOM   3717 O  O   . SER D  4  39  ? 27.269 -2.361  -34.542 1.00 60.55  ? 39  SER D O   1 
ATOM   3718 C  CB  . SER D  4  39  ? 27.980 0.778   -33.982 1.00 59.36  ? 39  SER D CB  1 
ATOM   3719 O  OG  . SER D  4  39  ? 28.172 2.003   -34.662 1.00 56.78  ? 39  SER D OG  1 
ATOM   3720 N  N   . LEU D  4  40  ? 26.191 -1.527  -32.756 1.00 61.33  ? 40  LEU D N   1 
ATOM   3721 C  CA  . LEU D  4  40  ? 26.098 -2.824  -32.098 1.00 63.03  ? 40  LEU D CA  1 
ATOM   3722 C  C   . LEU D  4  40  ? 25.232 -3.757  -32.938 1.00 64.07  ? 40  LEU D C   1 
ATOM   3723 O  O   . LEU D  4  40  ? 25.482 -4.960  -33.013 1.00 63.61  ? 40  LEU D O   1 
ATOM   3724 C  CB  . LEU D  4  40  ? 25.476 -2.684  -30.711 1.00 62.29  ? 40  LEU D CB  1 
ATOM   3725 C  CG  . LEU D  4  40  ? 25.280 -4.039  -30.016 1.00 61.86  ? 40  LEU D CG  1 
ATOM   3726 C  CD1 . LEU D  4  40  ? 26.626 -4.627  -29.676 1.00 61.38  ? 40  LEU D CD1 1 
ATOM   3727 C  CD2 . LEU D  4  40  ? 24.450 -3.889  -28.756 1.00 61.85  ? 40  LEU D CD2 1 
ATOM   3728 N  N   . PHE D  4  41  ? 24.207 -3.181  -33.557 1.00 65.74  ? 41  PHE D N   1 
ATOM   3729 C  CA  . PHE D  4  41  ? 23.281 -3.913  -34.417 1.00 66.10  ? 41  PHE D CA  1 
ATOM   3730 C  C   . PHE D  4  41  ? 24.007 -4.398  -35.676 1.00 67.28  ? 41  PHE D C   1 
ATOM   3731 O  O   . PHE D  4  41  ? 23.937 -5.577  -36.016 1.00 67.69  ? 41  PHE D O   1 
ATOM   3732 C  CB  . PHE D  4  41  ? 22.109 -3.005  -34.798 1.00 64.64  ? 41  PHE D CB  1 
ATOM   3733 C  CG  . PHE D  4  41  ? 21.260 -2.586  -33.629 1.00 62.23  ? 41  PHE D CG  1 
ATOM   3734 C  CD1 . PHE D  4  41  ? 20.355 -1.539  -33.758 1.00 62.76  ? 41  PHE D CD1 1 
ATOM   3735 C  CD2 . PHE D  4  41  ? 21.344 -3.251  -32.412 1.00 61.20  ? 41  PHE D CD2 1 
ATOM   3736 C  CE1 . PHE D  4  41  ? 19.545 -1.162  -32.692 1.00 63.22  ? 41  PHE D CE1 1 
ATOM   3737 C  CE2 . PHE D  4  41  ? 20.540 -2.884  -31.340 1.00 61.42  ? 41  PHE D CE2 1 
ATOM   3738 C  CZ  . PHE D  4  41  ? 19.637 -1.835  -31.481 1.00 62.70  ? 41  PHE D CZ  1 
ATOM   3739 N  N   . LYS D  4  42  ? 24.704 -3.501  -36.363 1.00 67.76  ? 42  LYS D N   1 
ATOM   3740 C  CA  . LYS D  4  42  ? 25.422 -3.897  -37.567 1.00 69.11  ? 42  LYS D CA  1 
ATOM   3741 C  C   . LYS D  4  42  ? 26.449 -4.988  -37.260 1.00 69.58  ? 42  LYS D C   1 
ATOM   3742 O  O   . LYS D  4  42  ? 26.739 -5.824  -38.113 1.00 70.15  ? 42  LYS D O   1 
ATOM   3743 C  CB  . LYS D  4  42  ? 26.102 -2.688  -38.219 1.00 69.42  ? 42  LYS D CB  1 
ATOM   3744 C  CG  . LYS D  4  42  ? 25.119 -1.619  -38.676 1.00 71.33  ? 42  LYS D CG  1 
ATOM   3745 C  CD  . LYS D  4  42  ? 25.816 -0.402  -39.267 1.00 72.12  ? 42  LYS D CD  1 
ATOM   3746 C  CE  . LYS D  4  42  ? 24.802 0.682   -39.629 1.00 74.54  ? 42  LYS D CE  1 
ATOM   3747 N  NZ  . LYS D  4  42  ? 25.436 1.947   -40.125 1.00 74.06  ? 42  LYS D NZ  1 
ATOM   3748 N  N   . LEU D  4  43  ? 26.989 -4.995  -36.044 1.00 69.37  ? 43  LEU D N   1 
ATOM   3749 C  CA  . LEU D  4  43  ? 27.967 -6.014  -35.673 1.00 70.37  ? 43  LEU D CA  1 
ATOM   3750 C  C   . LEU D  4  43  ? 27.256 -7.321  -35.326 1.00 71.42  ? 43  LEU D C   1 
ATOM   3751 O  O   . LEU D  4  43  ? 27.633 -8.389  -35.802 1.00 71.85  ? 43  LEU D O   1 
ATOM   3752 C  CB  . LEU D  4  43  ? 28.812 -5.560  -34.479 1.00 70.09  ? 43  LEU D CB  1 
ATOM   3753 C  CG  . LEU D  4  43  ? 29.981 -4.595  -34.704 1.00 69.12  ? 43  LEU D CG  1 
ATOM   3754 C  CD1 . LEU D  4  43  ? 30.720 -4.373  -33.389 1.00 69.45  ? 43  LEU D CD1 1 
ATOM   3755 C  CD2 . LEU D  4  43  ? 30.926 -5.175  -35.741 1.00 68.97  ? 43  LEU D CD2 1 
ATOM   3756 N  N   . LYS D  4  44  ? 26.240 -7.224  -34.479 1.00 72.83  ? 44  LYS D N   1 
ATOM   3757 C  CA  . LYS D  4  44  ? 25.448 -8.379  -34.055 1.00 74.04  ? 44  LYS D CA  1 
ATOM   3758 C  C   . LYS D  4  44  ? 23.986 -8.004  -34.278 1.00 75.30  ? 44  LYS D C   1 
ATOM   3759 O  O   . LYS D  4  44  ? 23.311 -7.562  -33.351 1.00 74.04  ? 44  LYS D O   1 
ATOM   3760 C  CB  . LYS D  4  44  ? 25.670 -8.666  -32.565 1.00 73.11  ? 44  LYS D CB  1 
ATOM   3761 C  CG  . LYS D  4  44  ? 27.088 -9.034  -32.183 1.00 73.52  ? 44  LYS D CG  1 
ATOM   3762 C  CD  . LYS D  4  44  ? 27.509 -10.352 -32.805 1.00 75.51  ? 44  LYS D CD  1 
ATOM   3763 C  CE  . LYS D  4  44  ? 28.846 -10.815 -32.242 1.00 76.97  ? 44  LYS D CE  1 
ATOM   3764 N  NZ  . LYS D  4  44  ? 29.276 -12.129 -32.805 1.00 79.07  ? 44  LYS D NZ  1 
ATOM   3765 N  N   . PRO D  4  45  ? 23.477 -8.168  -35.512 1.00 77.39  ? 45  PRO D N   1 
ATOM   3766 C  CA  . PRO D  4  45  ? 22.077 -7.819  -35.800 1.00 78.56  ? 45  PRO D CA  1 
ATOM   3767 C  C   . PRO D  4  45  ? 21.071 -8.644  -35.008 1.00 79.14  ? 45  PRO D C   1 
ATOM   3768 O  O   . PRO D  4  45  ? 19.949 -8.218  -34.766 1.00 77.75  ? 45  PRO D O   1 
ATOM   3769 C  CB  . PRO D  4  45  ? 21.969 -8.035  -37.310 1.00 78.59  ? 45  PRO D CB  1 
ATOM   3770 C  CG  . PRO D  4  45  ? 22.955 -9.152  -37.563 1.00 78.58  ? 45  PRO D CG  1 
ATOM   3771 C  CD  . PRO D  4  45  ? 24.134 -8.761  -36.696 1.00 77.45  ? 45  PRO D CD  1 
ATOM   3772 N  N   . GLU D  4  46  ? 21.500 -9.825  -34.597 1.00 81.70  ? 46  GLU D N   1 
ATOM   3773 C  CA  . GLU D  4  46  ? 20.671 -10.738 -33.831 1.00 84.64  ? 46  GLU D CA  1 
ATOM   3774 C  C   . GLU D  4  46  ? 20.251 -10.147 -32.481 1.00 84.72  ? 46  GLU D C   1 
ATOM   3775 O  O   . GLU D  4  46  ? 19.246 -10.561 -31.901 1.00 85.21  ? 46  GLU D O   1 
ATOM   3776 C  CB  . GLU D  4  46  ? 21.448 -12.033 -33.611 1.00 88.36  ? 46  GLU D CB  1 
ATOM   3777 C  CG  . GLU D  4  46  ? 22.796 -11.803 -32.938 1.00 94.46  ? 46  GLU D CG  1 
ATOM   3778 C  CD  . GLU D  4  46  ? 23.662 -13.051 -32.876 1.00 97.51  ? 46  GLU D CD  1 
ATOM   3779 O  OE1 . GLU D  4  46  ? 23.169 -14.106 -32.411 1.00 99.51  ? 46  GLU D OE1 1 
ATOM   3780 O  OE2 . GLU D  4  46  ? 24.842 -12.966 -33.286 1.00 96.98  ? 46  GLU D OE2 1 
ATOM   3781 N  N   . SER D  4  47  ? 21.015 -9.171  -31.987 1.00 83.41  ? 47  SER D N   1 
ATOM   3782 C  CA  . SER D  4  47  ? 20.732 -8.554  -30.693 1.00 81.03  ? 47  SER D CA  1 
ATOM   3783 C  C   . SER D  4  47  ? 19.751 -7.391  -30.726 1.00 79.14  ? 47  SER D C   1 
ATOM   3784 O  O   . SER D  4  47  ? 19.235 -6.994  -29.683 1.00 78.73  ? 47  SER D O   1 
ATOM   3785 C  CB  . SER D  4  47  ? 22.033 -8.082  -30.040 1.00 81.60  ? 47  SER D CB  1 
ATOM   3786 O  OG  . SER D  4  47  ? 22.624 -7.033  -30.784 1.00 82.92  ? 47  SER D OG  1 
ATOM   3787 N  N   . GLU D  4  48  ? 19.493 -6.839  -31.905 1.00 76.94  ? 48  GLU D N   1 
ATOM   3788 C  CA  . GLU D  4  48  ? 18.564 -5.720  -32.005 1.00 75.48  ? 48  GLU D CA  1 
ATOM   3789 C  C   . GLU D  4  48  ? 17.198 -6.038  -31.416 1.00 75.62  ? 48  GLU D C   1 
ATOM   3790 O  O   . GLU D  4  48  ? 16.586 -5.193  -30.761 1.00 74.73  ? 48  GLU D O   1 
ATOM   3791 C  CB  . GLU D  4  48  ? 18.374 -5.285  -33.459 1.00 74.56  ? 48  GLU D CB  1 
ATOM   3792 C  CG  . GLU D  4  48  ? 17.277 -4.240  -33.605 1.00 74.13  ? 48  GLU D CG  1 
ATOM   3793 C  CD  . GLU D  4  48  ? 17.165 -3.676  -35.003 1.00 73.99  ? 48  GLU D CD  1 
ATOM   3794 O  OE1 . GLU D  4  48  ? 16.291 -2.809  -35.220 1.00 73.16  ? 48  GLU D OE1 1 
ATOM   3795 O  OE2 . GLU D  4  48  ? 17.947 -4.093  -35.885 1.00 73.38  ? 48  GLU D OE2 1 
ATOM   3796 N  N   . VAL D  4  49  ? 16.717 -7.251  -31.661 1.00 76.17  ? 49  VAL D N   1 
ATOM   3797 C  CA  . VAL D  4  49  ? 15.408 -7.664  -31.164 1.00 75.87  ? 49  VAL D CA  1 
ATOM   3798 C  C   . VAL D  4  49  ? 15.266 -7.537  -29.652 1.00 74.50  ? 49  VAL D C   1 
ATOM   3799 O  O   . VAL D  4  49  ? 14.174 -7.292  -29.156 1.00 74.91  ? 49  VAL D O   1 
ATOM   3800 C  CB  . VAL D  4  49  ? 15.067 -9.133  -31.591 1.00 77.48  ? 49  VAL D CB  1 
ATOM   3801 C  CG1 . VAL D  4  49  ? 14.925 -9.213  -33.121 1.00 78.12  ? 49  VAL D CG1 1 
ATOM   3802 C  CG2 . VAL D  4  49  ? 16.148 -10.099 -31.104 1.00 76.72  ? 49  VAL D CG2 1 
ATOM   3803 N  N   . LEU D  4  50  ? 16.365 -7.683  -28.920 1.00 73.06  ? 50  LEU D N   1 
ATOM   3804 C  CA  . LEU D  4  50  ? 16.323 -7.584  -27.461 1.00 71.78  ? 50  LEU D CA  1 
ATOM   3805 C  C   . LEU D  4  50  ? 15.760 -6.252  -26.948 1.00 70.53  ? 50  LEU D C   1 
ATOM   3806 O  O   . LEU D  4  50  ? 15.314 -6.161  -25.813 1.00 70.58  ? 50  LEU D O   1 
ATOM   3807 C  CB  . LEU D  4  50  ? 17.725 -7.786  -26.880 1.00 71.24  ? 50  LEU D CB  1 
ATOM   3808 C  CG  . LEU D  4  50  ? 18.476 -9.060  -27.271 1.00 70.97  ? 50  LEU D CG  1 
ATOM   3809 C  CD1 . LEU D  4  50  ? 19.849 -9.060  -26.612 1.00 70.43  ? 50  LEU D CD1 1 
ATOM   3810 C  CD2 . LEU D  4  50  ? 17.696 -10.283 -26.847 1.00 70.37  ? 50  LEU D CD2 1 
ATOM   3811 N  N   . PHE D  4  51  ? 15.779 -5.227  -27.786 1.00 70.24  ? 51  PHE D N   1 
ATOM   3812 C  CA  . PHE D  4  51  ? 15.291 -3.912  -27.396 1.00 70.58  ? 51  PHE D CA  1 
ATOM   3813 C  C   . PHE D  4  51  ? 13.892 -3.574  -27.906 1.00 72.31  ? 51  PHE D C   1 
ATOM   3814 O  O   . PHE D  4  51  ? 13.471 -2.420  -27.838 1.00 72.95  ? 51  PHE D O   1 
ATOM   3815 C  CB  . PHE D  4  51  ? 16.282 -2.841  -27.860 1.00 68.95  ? 51  PHE D CB  1 
ATOM   3816 C  CG  . PHE D  4  51  ? 17.668 -3.039  -27.326 1.00 67.85  ? 51  PHE D CG  1 
ATOM   3817 C  CD1 . PHE D  4  51  ? 18.621 -3.756  -28.052 1.00 67.29  ? 51  PHE D CD1 1 
ATOM   3818 C  CD2 . PHE D  4  51  ? 18.002 -2.580  -26.054 1.00 67.47  ? 51  PHE D CD2 1 
ATOM   3819 C  CE1 . PHE D  4  51  ? 19.876 -4.016  -27.520 1.00 64.68  ? 51  PHE D CE1 1 
ATOM   3820 C  CE2 . PHE D  4  51  ? 19.254 -2.836  -25.514 1.00 65.14  ? 51  PHE D CE2 1 
ATOM   3821 C  CZ  . PHE D  4  51  ? 20.191 -3.557  -26.251 1.00 65.08  ? 51  PHE D CZ  1 
ATOM   3822 N  N   . ASN D  4  52  ? 13.175 -4.568  -28.418 1.00 73.92  ? 52  ASN D N   1 
ATOM   3823 C  CA  . ASN D  4  52  ? 11.826 -4.331  -28.922 1.00 74.04  ? 52  ASN D CA  1 
ATOM   3824 C  C   . ASN D  4  52  ? 10.964 -3.731  -27.825 1.00 72.75  ? 52  ASN D C   1 
ATOM   3825 O  O   . ASN D  4  52  ? 9.993  -3.039  -28.099 1.00 72.81  ? 52  ASN D O   1 
ATOM   3826 C  CB  . ASN D  4  52  ? 11.186 -5.637  -29.423 1.00 75.69  ? 52  ASN D CB  1 
ATOM   3827 C  CG  . ASN D  4  52  ? 11.795 -6.128  -30.726 1.00 77.10  ? 52  ASN D CG  1 
ATOM   3828 O  OD1 . ASN D  4  52  ? 11.960 -5.360  -31.678 1.00 77.60  ? 52  ASN D OD1 1 
ATOM   3829 N  ND2 . ASN D  4  52  ? 12.121 -7.413  -30.780 1.00 78.29  ? 52  ASN D ND2 1 
ATOM   3830 N  N   . ASN D  4  53  ? 11.338 -3.976  -26.576 1.00 72.20  ? 53  ASN D N   1 
ATOM   3831 C  CA  . ASN D  4  53  ? 10.566 -3.467  -25.453 1.00 72.17  ? 53  ASN D CA  1 
ATOM   3832 C  C   . ASN D  4  53  ? 10.710 -1.968  -25.202 1.00 71.65  ? 53  ASN D C   1 
ATOM   3833 O  O   . ASN D  4  53  ? 9.832  -1.363  -24.589 1.00 69.55  ? 53  ASN D O   1 
ATOM   3834 C  CB  . ASN D  4  53  ? 10.932 -4.219  -24.184 1.00 74.91  ? 53  ASN D CB  1 
ATOM   3835 C  CG  . ASN D  4  53  ? 9.747  -4.395  -23.260 1.00 77.03  ? 53  ASN D CG  1 
ATOM   3836 O  OD1 . ASN D  4  53  ? 8.839  -5.179  -23.538 1.00 76.44  ? 53  ASN D OD1 1 
ATOM   3837 N  ND2 . ASN D  4  53  ? 9.738  -3.651  -22.162 1.00 78.27  ? 53  ASN D ND2 1 
ATOM   3838 N  N   . VAL D  4  54  ? 11.818 -1.380  -25.654 1.00 71.45  ? 54  VAL D N   1 
ATOM   3839 C  CA  . VAL D  4  54  ? 12.056 0.053   -25.497 1.00 70.53  ? 54  VAL D CA  1 
ATOM   3840 C  C   . VAL D  4  54  ? 11.814 0.755   -26.828 1.00 70.89  ? 54  VAL D C   1 
ATOM   3841 O  O   . VAL D  4  54  ? 12.286 1.873   -27.061 1.00 71.44  ? 54  VAL D O   1 
ATOM   3842 C  CB  . VAL D  4  54  ? 13.495 0.355   -25.036 1.00 69.91  ? 54  VAL D CB  1 
ATOM   3843 C  CG1 . VAL D  4  54  ? 13.668 -0.045  -23.592 1.00 71.17  ? 54  VAL D CG1 1 
ATOM   3844 C  CG2 . VAL D  4  54  ? 14.487 -0.382  -25.912 1.00 69.97  ? 54  VAL D CG2 1 
ATOM   3845 N  N   . ASN D  4  55  ? 11.084 0.068   -27.703 1.00 70.45  ? 55  ASN D N   1 
ATOM   3846 C  CA  . ASN D  4  55  ? 10.719 0.576   -29.023 1.00 69.88  ? 55  ASN D CA  1 
ATOM   3847 C  C   . ASN D  4  55  ? 11.906 0.730   -29.971 1.00 69.83  ? 55  ASN D C   1 
ATOM   3848 O  O   . ASN D  4  55  ? 12.032 1.734   -30.662 1.00 68.83  ? 55  ASN D O   1 
ATOM   3849 C  CB  . ASN D  4  55  ? 9.971  1.911   -28.884 1.00 67.79  ? 55  ASN D CB  1 
ATOM   3850 C  CG  . ASN D  4  55  ? 9.265  2.325   -30.167 1.00 67.48  ? 55  ASN D CG  1 
ATOM   3851 O  OD1 . ASN D  4  55  ? 9.229  1.568   -31.142 1.00 65.54  ? 55  ASN D OD1 1 
ATOM   3852 N  ND2 . ASN D  4  55  ? 8.689  3.533   -30.169 1.00 67.07  ? 55  ASN D ND2 1 
ATOM   3853 N  N   . VAL D  4  56  ? 12.772 -0.279  -30.003 1.00 71.03  ? 56  VAL D N   1 
ATOM   3854 C  CA  . VAL D  4  56  ? 13.942 -0.267  -30.877 1.00 72.39  ? 56  VAL D CA  1 
ATOM   3855 C  C   . VAL D  4  56  ? 13.505 -0.113  -32.347 1.00 74.16  ? 56  VAL D C   1 
ATOM   3856 O  O   . VAL D  4  56  ? 14.308 0.244   -33.220 1.00 74.23  ? 56  VAL D O   1 
ATOM   3857 C  CB  . VAL D  4  56  ? 14.771 -1.569  -30.708 1.00 71.47  ? 56  VAL D CB  1 
ATOM   3858 C  CG1 . VAL D  4  56  ? 13.955 -2.765  -31.148 1.00 72.81  ? 56  VAL D CG1 1 
ATOM   3859 C  CG2 . VAL D  4  56  ? 16.057 -1.486  -31.504 1.00 71.34  ? 56  VAL D CG2 1 
ATOM   3860 N  N   . ALA D  4  57  ? 12.228 -0.385  -32.611 1.00 75.21  ? 57  ALA D N   1 
ATOM   3861 C  CA  . ALA D  4  57  ? 11.673 -0.255  -33.955 1.00 76.17  ? 57  ALA D CA  1 
ATOM   3862 C  C   . ALA D  4  57  ? 11.935 1.165   -34.456 1.00 77.56  ? 57  ALA D C   1 
ATOM   3863 O  O   . ALA D  4  57  ? 12.421 1.363   -35.571 1.00 77.47  ? 57  ALA D O   1 
ATOM   3864 C  CB  . ALA D  4  57  ? 10.180 -0.533  -33.927 1.00 76.02  ? 57  ALA D CB  1 
ATOM   3865 N  N   . ASN D  4  58  ? 11.595 2.152   -33.626 1.00 78.99  ? 58  ASN D N   1 
ATOM   3866 C  CA  . ASN D  4  58  ? 11.817 3.562   -33.950 1.00 79.62  ? 58  ASN D CA  1 
ATOM   3867 C  C   . ASN D  4  58  ? 12.846 4.121   -32.963 1.00 76.64  ? 58  ASN D C   1 
ATOM   3868 O  O   . ASN D  4  58  ? 12.504 4.469   -31.829 1.00 76.02  ? 58  ASN D O   1 
ATOM   3869 C  CB  . ASN D  4  58  ? 10.513 4.371   -33.840 1.00 86.79  ? 58  ASN D CB  1 
ATOM   3870 C  CG  . ASN D  4  58  ? 10.699 5.822   -34.263 1.00 95.31  ? 58  ASN D CG  1 
ATOM   3871 O  OD1 . ASN D  4  58  ? 11.828 6.236   -34.530 1.00 95.31  ? 58  ASN D OD1 1 
ATOM   3872 N  ND2 . ASN D  4  58  ? 9.621  6.604   -34.333 1.00 104.87 ? 58  ASN D ND2 1 
ATOM   3873 N  N   . MET D  4  59  ? 14.104 4.207   -33.399 1.00 72.06  ? 59  MET D N   1 
ATOM   3874 C  CA  . MET D  4  59  ? 15.178 4.709   -32.550 1.00 68.16  ? 59  MET D CA  1 
ATOM   3875 C  C   . MET D  4  59  ? 15.120 6.213   -32.275 1.00 66.64  ? 59  MET D C   1 
ATOM   3876 O  O   . MET D  4  59  ? 15.981 6.752   -31.575 1.00 67.43  ? 59  MET D O   1 
ATOM   3877 C  CB  . MET D  4  59  ? 16.539 4.336   -33.147 1.00 66.38  ? 59  MET D CB  1 
ATOM   3878 C  CG  . MET D  4  59  ? 16.900 2.864   -32.975 1.00 63.94  ? 59  MET D CG  1 
ATOM   3879 S  SD  . MET D  4  59  ? 18.410 2.369   -33.841 1.00 62.25  ? 59  MET D SD  1 
ATOM   3880 C  CE  . MET D  4  59  ? 19.661 3.022   -32.741 1.00 62.56  ? 59  MET D CE  1 
ATOM   3881 N  N   . SER D  4  60  ? 14.104 6.883   -32.809 1.00 63.19  ? 60  SER D N   1 
ATOM   3882 C  CA  . SER D  4  60  ? 13.938 8.314   -32.595 1.00 59.74  ? 60  SER D CA  1 
ATOM   3883 C  C   . SER D  4  60  ? 12.803 8.572   -31.609 1.00 56.80  ? 60  SER D C   1 
ATOM   3884 O  O   . SER D  4  60  ? 12.439 9.720   -31.352 1.00 55.47  ? 60  SER D O   1 
ATOM   3885 C  CB  . SER D  4  60  ? 13.642 9.022   -33.918 1.00 60.21  ? 60  SER D CB  1 
ATOM   3886 O  OG  . SER D  4  60  ? 14.735 8.902   -34.811 1.00 59.62  ? 60  SER D OG  1 
ATOM   3887 N  N   . SER D  4  61  ? 12.257 7.492   -31.056 1.00 54.79  ? 61  SER D N   1 
ATOM   3888 C  CA  . SER D  4  61  ? 11.156 7.572   -30.098 1.00 54.88  ? 61  SER D CA  1 
ATOM   3889 C  C   . SER D  4  61  ? 11.611 7.856   -28.670 1.00 54.34  ? 61  SER D C   1 
ATOM   3890 O  O   . SER D  4  61  ? 12.660 7.383   -28.237 1.00 54.40  ? 61  SER D O   1 
ATOM   3891 C  CB  . SER D  4  61  ? 10.376 6.266   -30.085 1.00 55.39  ? 61  SER D CB  1 
ATOM   3892 O  OG  . SER D  4  61  ? 11.177 5.215   -29.581 1.00 56.47  ? 61  SER D OG  1 
ATOM   3893 N  N   . GLY D  4  62  ? 10.796 8.598   -27.934 1.00 53.37  ? 62  GLY D N   1 
ATOM   3894 C  CA  . GLY D  4  62  ? 11.138 8.926   -26.563 1.00 52.01  ? 62  GLY D CA  1 
ATOM   3895 C  C   . GLY D  4  62  ? 11.500 7.703   -25.751 1.00 50.78  ? 62  GLY D C   1 
ATOM   3896 O  O   . GLY D  4  62  ? 12.390 7.758   -24.903 1.00 50.36  ? 62  GLY D O   1 
ATOM   3897 N  N   . ALA D  4  63  ? 10.826 6.589   -26.014 1.00 49.76  ? 63  ALA D N   1 
ATOM   3898 C  CA  . ALA D  4  63  ? 11.099 5.363   -25.268 1.00 48.91  ? 63  ALA D CA  1 
ATOM   3899 C  C   . ALA D  4  63  ? 12.508 4.839   -25.492 1.00 48.26  ? 63  ALA D C   1 
ATOM   3900 O  O   . ALA D  4  63  ? 13.156 4.371   -24.552 1.00 45.88  ? 63  ALA D O   1 
ATOM   3901 C  CB  . ALA D  4  63  ? 10.089 4.285   -25.620 1.00 47.10  ? 63  ALA D CB  1 
ATOM   3902 N  N   . PHE D  4  64  ? 12.984 4.903   -26.732 1.00 48.78  ? 64  PHE D N   1 
ATOM   3903 C  CA  . PHE D  4  64  ? 14.330 4.415   -27.020 1.00 50.16  ? 64  PHE D CA  1 
ATOM   3904 C  C   . PHE D  4  64  ? 15.396 5.454   -26.644 1.00 51.25  ? 64  PHE D C   1 
ATOM   3905 O  O   . PHE D  4  64  ? 16.485 5.092   -26.176 1.00 50.96  ? 64  PHE D O   1 
ATOM   3906 C  CB  . PHE D  4  64  ? 14.470 4.029   -28.496 1.00 50.10  ? 64  PHE D CB  1 
ATOM   3907 C  CG  . PHE D  4  64  ? 15.768 3.334   -28.816 1.00 49.29  ? 64  PHE D CG  1 
ATOM   3908 C  CD1 . PHE D  4  64  ? 15.998 2.029   -28.392 1.00 47.70  ? 64  PHE D CD1 1 
ATOM   3909 C  CD2 . PHE D  4  64  ? 16.773 3.994   -29.522 1.00 50.27  ? 64  PHE D CD2 1 
ATOM   3910 C  CE1 . PHE D  4  64  ? 17.204 1.385   -28.663 1.00 47.71  ? 64  PHE D CE1 1 
ATOM   3911 C  CE2 . PHE D  4  64  ? 17.984 3.359   -29.797 1.00 50.15  ? 64  PHE D CE2 1 
ATOM   3912 C  CZ  . PHE D  4  64  ? 18.201 2.050   -29.367 1.00 48.85  ? 64  PHE D CZ  1 
ATOM   3913 N  N   . HIS D  4  65  ? 15.093 6.737   -26.858 1.00 51.17  ? 65  HIS D N   1 
ATOM   3914 C  CA  . HIS D  4  65  ? 16.025 7.800   -26.495 1.00 50.31  ? 65  HIS D CA  1 
ATOM   3915 C  C   . HIS D  4  65  ? 16.292 7.662   -24.998 1.00 49.86  ? 65  HIS D C   1 
ATOM   3916 O  O   . HIS D  4  65  ? 17.444 7.745   -24.553 1.00 49.63  ? 65  HIS D O   1 
ATOM   3917 C  CB  . HIS D  4  65  ? 15.416 9.174   -26.797 1.00 52.62  ? 65  HIS D CB  1 
ATOM   3918 C  CG  . HIS D  4  65  ? 15.584 9.618   -28.218 1.00 54.35  ? 65  HIS D CG  1 
ATOM   3919 N  ND1 . HIS D  4  65  ? 14.974 10.748  -28.723 1.00 54.38  ? 65  HIS D ND1 1 
ATOM   3920 C  CD2 . HIS D  4  65  ? 16.335 9.113   -29.227 1.00 54.69  ? 65  HIS D CD2 1 
ATOM   3921 C  CE1 . HIS D  4  65  ? 15.342 10.920  -29.978 1.00 55.10  ? 65  HIS D CE1 1 
ATOM   3922 N  NE2 . HIS D  4  65  ? 16.172 9.945   -30.308 1.00 55.49  ? 65  HIS D NE2 1 
ATOM   3923 N  N   . ALA D  4  66  ? 15.225 7.427   -24.237 1.00 47.59  ? 66  ALA D N   1 
ATOM   3924 C  CA  . ALA D  4  66  ? 15.330 7.282   -22.787 1.00 47.00  ? 66  ALA D CA  1 
ATOM   3925 C  C   . ALA D  4  66  ? 16.152 6.065   -22.424 1.00 44.93  ? 66  ALA D C   1 
ATOM   3926 O  O   . ALA D  4  66  ? 16.818 6.038   -21.391 1.00 43.54  ? 66  ALA D O   1 
ATOM   3927 C  CB  . ALA D  4  66  ? 13.953 7.170   -22.161 1.00 46.81  ? 66  ALA D CB  1 
ATOM   3928 N  N   . HIS D  4  67  ? 16.112 5.054   -23.269 1.00 42.42  ? 67  HIS D N   1 
ATOM   3929 C  CA  . HIS D  4  67  ? 16.878 3.863   -22.974 1.00 44.28  ? 67  HIS D CA  1 
ATOM   3930 C  C   . HIS D  4  67  ? 18.377 4.158   -23.104 1.00 44.69  ? 67  HIS D C   1 
ATOM   3931 O  O   . HIS D  4  67  ? 19.159 3.864   -22.194 1.00 44.21  ? 67  HIS D O   1 
ATOM   3932 C  CB  . HIS D  4  67  ? 16.490 2.721   -23.914 1.00 44.81  ? 67  HIS D CB  1 
ATOM   3933 C  CG  . HIS D  4  67  ? 17.394 1.536   -23.806 1.00 43.22  ? 67  HIS D CG  1 
ATOM   3934 N  ND1 . HIS D  4  67  ? 17.447 0.750   -22.675 1.00 42.74  ? 67  HIS D ND1 1 
ATOM   3935 C  CD2 . HIS D  4  67  ? 18.334 1.048   -24.654 1.00 41.35  ? 67  HIS D CD2 1 
ATOM   3936 C  CE1 . HIS D  4  67  ? 18.385 -0.169  -22.825 1.00 42.21  ? 67  HIS D CE1 1 
ATOM   3937 N  NE2 . HIS D  4  67  ? 18.938 -0.011  -24.019 1.00 42.57  ? 67  HIS D NE2 1 
ATOM   3938 N  N   . THR D  4  68  ? 18.776 4.725   -24.236 1.00 42.92  ? 68  THR D N   1 
ATOM   3939 C  CA  . THR D  4  68  ? 20.174 5.070   -24.433 1.00 43.99  ? 68  THR D CA  1 
ATOM   3940 C  C   . THR D  4  68  ? 20.633 6.047   -23.340 1.00 44.90  ? 68  THR D C   1 
ATOM   3941 O  O   . THR D  4  68  ? 21.753 5.950   -22.826 1.00 45.24  ? 68  THR D O   1 
ATOM   3942 C  CB  . THR D  4  68  ? 20.403 5.742   -25.801 1.00 43.43  ? 68  THR D CB  1 
ATOM   3943 O  OG1 . THR D  4  68  ? 19.508 6.854   -25.941 1.00 44.53  ? 68  THR D OG1 1 
ATOM   3944 C  CG2 . THR D  4  68  ? 20.194 4.763   -26.915 1.00 42.01  ? 68  THR D CG2 1 
ATOM   3945 N  N   . VAL D  4  69  ? 19.780 7.018   -23.013 1.00 43.97  ? 69  VAL D N   1 
ATOM   3946 C  CA  . VAL D  4  69  ? 20.108 7.976   -21.959 1.00 42.75  ? 69  VAL D CA  1 
ATOM   3947 C  C   . VAL D  4  69  ? 20.466 7.151   -20.726 1.00 43.98  ? 69  VAL D C   1 
ATOM   3948 O  O   . VAL D  4  69  ? 21.508 7.340   -20.098 1.00 45.82  ? 69  VAL D O   1 
ATOM   3949 C  CB  . VAL D  4  69  ? 18.896 8.889   -21.646 1.00 42.19  ? 69  VAL D CB  1 
ATOM   3950 C  CG1 . VAL D  4  69  ? 19.060 9.520   -20.256 1.00 40.29  ? 69  VAL D CG1 1 
ATOM   3951 C  CG2 . VAL D  4  69  ? 18.757 9.970   -22.701 1.00 39.28  ? 69  VAL D CG2 1 
ATOM   3952 N  N   . ARG D  4  70  ? 19.590 6.211   -20.404 1.00 44.14  ? 70  ARG D N   1 
ATOM   3953 C  CA  . ARG D  4  70  ? 19.749 5.339   -19.244 1.00 45.18  ? 70  ARG D CA  1 
ATOM   3954 C  C   . ARG D  4  70  ? 21.069 4.567   -19.303 1.00 44.49  ? 70  ARG D C   1 
ATOM   3955 O  O   . ARG D  4  70  ? 21.801 4.450   -18.314 1.00 42.29  ? 70  ARG D O   1 
ATOM   3956 C  CB  . ARG D  4  70  ? 18.574 4.367   -19.236 1.00 48.15  ? 70  ARG D CB  1 
ATOM   3957 C  CG  . ARG D  4  70  ? 18.048 3.964   -17.887 1.00 51.64  ? 70  ARG D CG  1 
ATOM   3958 C  CD  . ARG D  4  70  ? 16.722 3.238   -18.088 1.00 52.93  ? 70  ARG D CD  1 
ATOM   3959 N  NE  . ARG D  4  70  ? 15.663 4.167   -18.468 1.00 53.71  ? 70  ARG D NE  1 
ATOM   3960 C  CZ  . ARG D  4  70  ? 14.787 3.942   -19.439 1.00 53.78  ? 70  ARG D CZ  1 
ATOM   3961 N  NH1 . ARG D  4  70  ? 14.847 2.812   -20.136 1.00 51.05  ? 70  ARG D NH1 1 
ATOM   3962 N  NH2 . ARG D  4  70  ? 13.844 4.842   -19.702 1.00 53.95  ? 70  ARG D NH2 1 
ATOM   3963 N  N   . VAL D  4  71  ? 21.360 4.041   -20.485 1.00 44.02  ? 71  VAL D N   1 
ATOM   3964 C  CA  . VAL D  4  71  ? 22.571 3.258   -20.700 1.00 44.90  ? 71  VAL D CA  1 
ATOM   3965 C  C   . VAL D  4  71  ? 23.847 4.083   -20.506 1.00 44.96  ? 71  VAL D C   1 
ATOM   3966 O  O   . VAL D  4  71  ? 24.803 3.637   -19.848 1.00 42.54  ? 71  VAL D O   1 
ATOM   3967 C  CB  . VAL D  4  71  ? 22.557 2.630   -22.117 1.00 44.61  ? 71  VAL D CB  1 
ATOM   3968 C  CG1 . VAL D  4  71  ? 23.888 1.975   -22.408 1.00 43.25  ? 71  VAL D CG1 1 
ATOM   3969 C  CG2 . VAL D  4  71  ? 21.439 1.589   -22.206 1.00 44.29  ? 71  VAL D CG2 1 
ATOM   3970 N  N   . LEU D  4  72  ? 23.851 5.286   -21.072 1.00 43.40  ? 72  LEU D N   1 
ATOM   3971 C  CA  . LEU D  4  72  ? 24.999 6.161   -20.936 1.00 44.37  ? 72  LEU D CA  1 
ATOM   3972 C  C   . LEU D  4  72  ? 25.159 6.647   -19.500 1.00 44.62  ? 72  LEU D C   1 
ATOM   3973 O  O   . LEU D  4  72  ? 26.287 6.784   -19.034 1.00 45.96  ? 72  LEU D O   1 
ATOM   3974 C  CB  . LEU D  4  72  ? 24.875 7.339   -21.896 1.00 44.74  ? 72  LEU D CB  1 
ATOM   3975 C  CG  . LEU D  4  72  ? 24.955 6.897   -23.353 1.00 44.92  ? 72  LEU D CG  1 
ATOM   3976 C  CD1 . LEU D  4  72  ? 24.769 8.093   -24.257 1.00 45.62  ? 72  LEU D CD1 1 
ATOM   3977 C  CD2 . LEU D  4  72  ? 26.291 6.210   -23.616 1.00 44.41  ? 72  LEU D CD2 1 
ATOM   3978 N  N   . SER D  4  73  ? 24.050 6.903   -18.804 1.00 42.77  ? 73  SER D N   1 
ATOM   3979 C  CA  . SER D  4  73  ? 24.117 7.350   -17.417 1.00 40.89  ? 73  SER D CA  1 
ATOM   3980 C  C   . SER D  4  73  ? 24.767 6.238   -16.584 1.00 39.84  ? 73  SER D C   1 
ATOM   3981 O  O   . SER D  4  73  ? 25.530 6.502   -15.653 1.00 38.55  ? 73  SER D O   1 
ATOM   3982 C  CB  . SER D  4  73  ? 22.705 7.664   -16.903 1.00 42.09  ? 73  SER D CB  1 
ATOM   3983 O  OG  . SER D  4  73  ? 22.682 7.880   -15.496 1.00 42.94  ? 73  SER D OG  1 
ATOM   3984 N  N   . GLY D  4  74  ? 24.459 4.992   -16.933 1.00 40.78  ? 74  GLY D N   1 
ATOM   3985 C  CA  . GLY D  4  74  ? 25.024 3.853   -16.220 1.00 41.80  ? 74  GLY D CA  1 
ATOM   3986 C  C   . GLY D  4  74  ? 26.525 3.800   -16.467 1.00 43.13  ? 74  GLY D C   1 
ATOM   3987 O  O   . GLY D  4  74  ? 27.344 3.650   -15.545 1.00 43.09  ? 74  GLY D O   1 
ATOM   3988 N  N   . LEU D  4  75  ? 26.882 3.931   -17.735 1.00 42.67  ? 75  LEU D N   1 
ATOM   3989 C  CA  . LEU D  4  75  ? 28.274 3.928   -18.123 1.00 43.59  ? 75  LEU D CA  1 
ATOM   3990 C  C   . LEU D  4  75  ? 29.000 5.059   -17.378 1.00 43.55  ? 75  LEU D C   1 
ATOM   3991 O  O   . LEU D  4  75  ? 30.108 4.863   -16.885 1.00 42.80  ? 75  LEU D O   1 
ATOM   3992 C  CB  . LEU D  4  75  ? 28.390 4.121   -19.631 1.00 43.99  ? 75  LEU D CB  1 
ATOM   3993 C  CG  . LEU D  4  75  ? 29.797 4.235   -20.201 1.00 46.30  ? 75  LEU D CG  1 
ATOM   3994 C  CD1 . LEU D  4  75  ? 30.661 3.122   -19.648 1.00 48.03  ? 75  LEU D CD1 1 
ATOM   3995 C  CD2 . LEU D  4  75  ? 29.731 4.156   -21.720 1.00 48.00  ? 75  LEU D CD2 1 
ATOM   3996 N  N   . ASP D  4  76  ? 28.356 6.225   -17.294 1.00 42.57  ? 76  ASP D N   1 
ATOM   3997 C  CA  . ASP D  4  76  ? 28.908 7.396   -16.630 1.00 42.97  ? 76  ASP D CA  1 
ATOM   3998 C  C   . ASP D  4  76  ? 29.089 7.108   -15.149 1.00 43.82  ? 76  ASP D C   1 
ATOM   3999 O  O   . ASP D  4  76  ? 30.135 7.392   -14.570 1.00 41.35  ? 76  ASP D O   1 
ATOM   4000 C  CB  . ASP D  4  76  ? 27.977 8.592   -16.820 1.00 42.10  ? 76  ASP D CB  1 
ATOM   4001 C  CG  . ASP D  4  76  ? 28.367 9.775   -15.961 1.00 42.33  ? 76  ASP D CG  1 
ATOM   4002 O  OD1 . ASP D  4  76  ? 27.831 9.909   -14.844 1.00 46.53  ? 76  ASP D OD1 1 
ATOM   4003 O  OD2 . ASP D  4  76  ? 29.210 10.581  -16.395 1.00 39.18  ? 76  ASP D OD2 1 
ATOM   4004 N  N   . MET D  4  77  ? 28.060 6.525   -14.552 1.00 45.17  ? 77  MET D N   1 
ATOM   4005 C  CA  . MET D  4  77  ? 28.088 6.171   -13.150 1.00 46.51  ? 77  MET D CA  1 
ATOM   4006 C  C   . MET D  4  77  ? 29.251 5.208   -12.871 1.00 45.58  ? 77  MET D C   1 
ATOM   4007 O  O   . MET D  4  77  ? 29.900 5.312   -11.837 1.00 45.25  ? 77  MET D O   1 
ATOM   4008 C  CB  . MET D  4  77  ? 26.755 5.539   -12.808 1.00 50.84  ? 77  MET D CB  1 
ATOM   4009 C  CG  . MET D  4  77  ? 26.501 5.219   -11.363 1.00 55.89  ? 77  MET D CG  1 
ATOM   4010 S  SD  . MET D  4  77  ? 24.754 4.845   -11.266 1.00 61.06  ? 77  MET D SD  1 
ATOM   4011 C  CE  . MET D  4  77  ? 24.757 3.093   -11.908 1.00 62.00  ? 77  MET D CE  1 
ATOM   4012 N  N   . GLY D  4  78  ? 29.509 4.278   -13.791 1.00 44.06  ? 78  GLY D N   1 
ATOM   4013 C  CA  . GLY D  4  78  ? 30.604 3.341   -13.606 1.00 43.41  ? 78  GLY D CA  1 
ATOM   4014 C  C   . GLY D  4  78  ? 31.980 3.996   -13.703 1.00 44.20  ? 78  GLY D C   1 
ATOM   4015 O  O   . GLY D  4  78  ? 32.887 3.740   -12.902 1.00 45.66  ? 78  GLY D O   1 
ATOM   4016 N  N   . ILE D  4  79  ? 32.143 4.851   -14.699 1.00 42.15  ? 79  ILE D N   1 
ATOM   4017 C  CA  . ILE D  4  79  ? 33.393 5.541   -14.917 1.00 39.14  ? 79  ILE D CA  1 
ATOM   4018 C  C   . ILE D  4  79  ? 33.737 6.421   -13.715 1.00 41.56  ? 79  ILE D C   1 
ATOM   4019 O  O   . ILE D  4  79  ? 34.858 6.373   -13.216 1.00 42.12  ? 79  ILE D O   1 
ATOM   4020 C  CB  . ILE D  4  79  ? 33.292 6.385   -16.207 1.00 34.84  ? 79  ILE D CB  1 
ATOM   4021 C  CG1 . ILE D  4  79  ? 33.296 5.452   -17.416 1.00 31.08  ? 79  ILE D CG1 1 
ATOM   4022 C  CG2 . ILE D  4  79  ? 34.413 7.406   -16.274 1.00 32.92  ? 79  ILE D CG2 1 
ATOM   4023 C  CD1 . ILE D  4  79  ? 33.039 6.143   -18.760 1.00 29.50  ? 79  ILE D CD1 1 
ATOM   4024 N  N   . ASN D  4  80  ? 32.776 7.226   -13.260 1.00 42.65  ? 80  ASN D N   1 
ATOM   4025 C  CA  . ASN D  4  80  ? 32.981 8.115   -12.124 1.00 43.45  ? 80  ASN D CA  1 
ATOM   4026 C  C   . ASN D  4  80  ? 33.248 7.374   -10.809 1.00 44.41  ? 80  ASN D C   1 
ATOM   4027 O  O   . ASN D  4  80  ? 33.576 7.985   -9.787  1.00 44.69  ? 80  ASN D O   1 
ATOM   4028 C  CB  . ASN D  4  80  ? 31.778 9.039   -11.971 1.00 43.95  ? 80  ASN D CB  1 
ATOM   4029 C  CG  . ASN D  4  80  ? 31.786 10.154  -12.985 1.00 46.00  ? 80  ASN D CG  1 
ATOM   4030 O  OD1 . ASN D  4  80  ? 32.298 11.239  -12.731 1.00 48.91  ? 80  ASN D OD1 1 
ATOM   4031 N  ND2 . ASN D  4  80  ? 31.235 9.886   -14.154 1.00 45.82  ? 80  ASN D ND2 1 
ATOM   4032 N  N   . TYR D  4  81  ? 33.119 6.057   -10.828 1.00 43.97  ? 81  TYR D N   1 
ATOM   4033 C  CA  . TYR D  4  81  ? 33.400 5.283   -9.634  1.00 46.40  ? 81  TYR D CA  1 
ATOM   4034 C  C   . TYR D  4  81  ? 34.604 4.350   -9.806  1.00 47.48  ? 81  TYR D C   1 
ATOM   4035 O  O   . TYR D  4  81  ? 34.836 3.474   -8.974  1.00 46.61  ? 81  TYR D O   1 
ATOM   4036 C  CB  . TYR D  4  81  ? 32.151 4.502   -9.213  1.00 45.38  ? 81  TYR D CB  1 
ATOM   4037 C  CG  . TYR D  4  81  ? 31.199 5.347   -8.411  1.00 42.38  ? 81  TYR D CG  1 
ATOM   4038 C  CD1 . TYR D  4  81  ? 31.333 5.460   -7.025  1.00 42.60  ? 81  TYR D CD1 1 
ATOM   4039 C  CD2 . TYR D  4  81  ? 30.217 6.101   -9.044  1.00 43.49  ? 81  TYR D CD2 1 
ATOM   4040 C  CE1 . TYR D  4  81  ? 30.511 6.318   -6.284  1.00 41.59  ? 81  TYR D CE1 1 
ATOM   4041 C  CE2 . TYR D  4  81  ? 29.394 6.964   -8.319  1.00 43.74  ? 81  TYR D CE2 1 
ATOM   4042 C  CZ  . TYR D  4  81  ? 29.552 7.066   -6.940  1.00 42.44  ? 81  TYR D CZ  1 
ATOM   4043 O  OH  . TYR D  4  81  ? 28.755 7.942   -6.249  1.00 45.56  ? 81  TYR D OH  1 
ATOM   4044 N  N   . LEU D  4  82  ? 35.373 4.556   -10.879 1.00 49.39  ? 82  LEU D N   1 
ATOM   4045 C  CA  . LEU D  4  82  ? 36.549 3.737   -11.170 1.00 51.21  ? 82  LEU D CA  1 
ATOM   4046 C  C   . LEU D  4  82  ? 37.545 3.707   -10.022 1.00 52.45  ? 82  LEU D C   1 
ATOM   4047 O  O   . LEU D  4  82  ? 38.208 2.694   -9.807  1.00 53.21  ? 82  LEU D O   1 
ATOM   4048 C  CB  . LEU D  4  82  ? 37.236 4.229   -12.451 1.00 50.82  ? 82  LEU D CB  1 
ATOM   4049 C  CG  . LEU D  4  82  ? 36.573 3.864   -13.803 1.00 51.72  ? 82  LEU D CG  1 
ATOM   4050 C  CD1 . LEU D  4  82  ? 37.225 4.641   -14.957 1.00 48.32  ? 82  LEU D CD1 1 
ATOM   4051 C  CD2 . LEU D  4  82  ? 36.690 2.356   -14.053 1.00 49.64  ? 82  LEU D CD2 1 
ATOM   4052 N  N   . ASN D  4  83  ? 37.638 4.804   -9.273  1.00 53.95  ? 83  ASN D N   1 
ATOM   4053 C  CA  . ASN D  4  83  ? 38.560 4.864   -8.147  1.00 54.78  ? 83  ASN D CA  1 
ATOM   4054 C  C   . ASN D  4  83  ? 37.893 4.565   -6.803  1.00 54.86  ? 83  ASN D C   1 
ATOM   4055 O  O   . ASN D  4  83  ? 38.390 4.978   -5.757  1.00 55.40  ? 83  ASN D O   1 
ATOM   4056 C  CB  . ASN D  4  83  ? 39.283 6.227   -8.096  1.00 57.75  ? 83  ASN D CB  1 
ATOM   4057 C  CG  . ASN D  4  83  ? 40.368 6.368   -9.194  1.00 60.71  ? 83  ASN D CG  1 
ATOM   4058 O  OD1 . ASN D  4  83  ? 41.162 5.449   -9.423  1.00 61.18  ? 83  ASN D OD1 1 
ATOM   4059 N  ND2 . ASN D  4  83  ? 40.397 7.519   -9.861  1.00 60.63  ? 83  ASN D ND2 1 
ATOM   4060 N  N   . ASP D  4  84  ? 36.764 3.855   -6.830  1.00 53.96  ? 84  ASP D N   1 
ATOM   4061 C  CA  . ASP D  4  84  ? 36.070 3.454   -5.600  1.00 52.62  ? 84  ASP D CA  1 
ATOM   4062 C  C   . ASP D  4  84  ? 35.714 1.990   -5.801  1.00 52.28  ? 84  ASP D C   1 
ATOM   4063 O  O   . ASP D  4  84  ? 34.542 1.636   -5.941  1.00 50.56  ? 84  ASP D O   1 
ATOM   4064 C  CB  . ASP D  4  84  ? 34.783 4.250   -5.365  1.00 53.97  ? 84  ASP D CB  1 
ATOM   4065 C  CG  . ASP D  4  84  ? 34.196 4.019   -3.959  1.00 57.45  ? 84  ASP D CG  1 
ATOM   4066 O  OD1 . ASP D  4  84  ? 34.329 2.890   -3.422  1.00 59.51  ? 84  ASP D OD1 1 
ATOM   4067 O  OD2 . ASP D  4  84  ? 33.587 4.953   -3.382  1.00 56.31  ? 84  ASP D OD2 1 
ATOM   4068 N  N   . ALA D  4  85  ? 36.743 1.149   -5.817  1.00 51.74  ? 85  ALA D N   1 
ATOM   4069 C  CA  . ALA D  4  85  ? 36.593 -0.282  -6.037  1.00 51.22  ? 85  ALA D CA  1 
ATOM   4070 C  C   . ALA D  4  85  ? 35.422 -0.924  -5.310  1.00 50.95  ? 85  ALA D C   1 
ATOM   4071 O  O   . ALA D  4  85  ? 34.680 -1.707  -5.893  1.00 50.35  ? 85  ALA D O   1 
ATOM   4072 C  CB  . ALA D  4  85  ? 37.889 -0.995  -5.661  1.00 51.26  ? 85  ALA D CB  1 
ATOM   4073 N  N   . GLY D  4  86  ? 35.259 -0.608  -4.032  1.00 51.93  ? 86  GLY D N   1 
ATOM   4074 C  CA  . GLY D  4  86  ? 34.174 -1.201  -3.274  1.00 51.97  ? 86  GLY D CA  1 
ATOM   4075 C  C   . GLY D  4  86  ? 32.808 -0.917  -3.870  1.00 52.00  ? 86  GLY D C   1 
ATOM   4076 O  O   . GLY D  4  86  ? 32.043 -1.840  -4.183  1.00 51.46  ? 86  GLY D O   1 
ATOM   4077 N  N   . THR D  4  87  ? 32.503 0.367   -4.038  1.00 51.44  ? 87  THR D N   1 
ATOM   4078 C  CA  . THR D  4  87  ? 31.209 0.765   -4.569  1.00 50.32  ? 87  THR D CA  1 
ATOM   4079 C  C   . THR D  4  87  ? 31.005 0.318   -5.999  1.00 50.26  ? 87  THR D C   1 
ATOM   4080 O  O   . THR D  4  87  ? 29.908 -0.091  -6.367  1.00 51.66  ? 87  THR D O   1 
ATOM   4081 C  CB  . THR D  4  87  ? 31.029 2.278   -4.527  1.00 49.00  ? 87  THR D CB  1 
ATOM   4082 O  OG1 . THR D  4  87  ? 31.284 2.748   -3.204  1.00 48.23  ? 87  THR D OG1 1 
ATOM   4083 C  CG2 . THR D  4  87  ? 29.615 2.654   -4.914  1.00 50.75  ? 87  THR D CG2 1 
ATOM   4084 N  N   . LEU D  4  88  ? 32.054 0.394   -6.806  1.00 49.76  ? 88  LEU D N   1 
ATOM   4085 C  CA  . LEU D  4  88  ? 31.954 0.005   -8.204  1.00 48.21  ? 88  LEU D CA  1 
ATOM   4086 C  C   . LEU D  4  88  ? 31.602 -1.466  -8.289  1.00 48.07  ? 88  LEU D C   1 
ATOM   4087 O  O   . LEU D  4  88  ? 30.770 -1.870  -9.102  1.00 46.22  ? 88  LEU D O   1 
ATOM   4088 C  CB  . LEU D  4  88  ? 33.272 0.281   -8.938  1.00 47.92  ? 88  LEU D CB  1 
ATOM   4089 C  CG  . LEU D  4  88  ? 33.260 0.107   -10.468 1.00 48.67  ? 88  LEU D CG  1 
ATOM   4090 C  CD1 . LEU D  4  88  ? 32.157 0.968   -11.106 1.00 47.87  ? 88  LEU D CD1 1 
ATOM   4091 C  CD2 . LEU D  4  88  ? 34.609 0.498   -11.024 1.00 49.24  ? 88  LEU D CD2 1 
ATOM   4092 N  N   . THR D  4  89  ? 32.228 -2.275  -7.444  1.00 48.22  ? 89  THR D N   1 
ATOM   4093 C  CA  . THR D  4  89  ? 31.941 -3.698  -7.454  1.00 48.98  ? 89  THR D CA  1 
ATOM   4094 C  C   . THR D  4  89  ? 30.442 -3.874  -7.233  1.00 48.17  ? 89  THR D C   1 
ATOM   4095 O  O   . THR D  4  89  ? 29.771 -4.610  -7.967  1.00 48.22  ? 89  THR D O   1 
ATOM   4096 C  CB  . THR D  4  89  ? 32.697 -4.413  -6.349  1.00 49.96  ? 89  THR D CB  1 
ATOM   4097 O  OG1 . THR D  4  89  ? 34.099 -4.226  -6.545  1.00 51.50  ? 89  THR D OG1 1 
ATOM   4098 C  CG2 . THR D  4  89  ? 32.370 -5.895  -6.367  1.00 49.22  ? 89  THR D CG2 1 
ATOM   4099 N  N   . SER D  4  90  ? 29.921 -3.179  -6.225  1.00 46.25  ? 90  SER D N   1 
ATOM   4100 C  CA  . SER D  4  90  ? 28.505 -3.231  -5.906  1.00 43.76  ? 90  SER D CA  1 
ATOM   4101 C  C   . SER D  4  90  ? 27.652 -2.682  -7.052  1.00 42.94  ? 90  SER D C   1 
ATOM   4102 O  O   . SER D  4  90  ? 26.593 -3.228  -7.357  1.00 42.19  ? 90  SER D O   1 
ATOM   4103 C  CB  . SER D  4  90  ? 28.233 -2.428  -4.646  1.00 44.00  ? 90  SER D CB  1 
ATOM   4104 O  OG  . SER D  4  90  ? 26.839 -2.278  -4.461  1.00 44.01  ? 90  SER D OG  1 
ATOM   4105 N  N   . LEU D  4  91  ? 28.112 -1.613  -7.689  1.00 42.67  ? 91  LEU D N   1 
ATOM   4106 C  CA  . LEU D  4  91  ? 27.376 -1.025  -8.815  1.00 41.87  ? 91  LEU D CA  1 
ATOM   4107 C  C   . LEU D  4  91  ? 27.311 -1.965  -10.011 1.00 42.86  ? 91  LEU D C   1 
ATOM   4108 O  O   . LEU D  4  91  ? 26.280 -2.076  -10.674 1.00 44.08  ? 91  LEU D O   1 
ATOM   4109 C  CB  . LEU D  4  91  ? 28.015 0.295   -9.270  1.00 40.51  ? 91  LEU D CB  1 
ATOM   4110 C  CG  . LEU D  4  91  ? 27.862 1.562   -8.411  1.00 41.42  ? 91  LEU D CG  1 
ATOM   4111 C  CD1 . LEU D  4  91  ? 28.693 2.666   -9.038  1.00 42.37  ? 91  LEU D CD1 1 
ATOM   4112 C  CD2 . LEU D  4  91  ? 26.383 1.982   -8.316  1.00 38.74  ? 91  LEU D CD2 1 
ATOM   4113 N  N   . THR D  4  92  ? 28.412 -2.643  -10.306 1.00 43.71  ? 92  THR D N   1 
ATOM   4114 C  CA  . THR D  4  92  ? 28.423 -3.538  -11.456 1.00 43.70  ? 92  THR D CA  1 
ATOM   4115 C  C   . THR D  4  92  ? 27.633 -4.806  -11.173 1.00 44.19  ? 92  THR D C   1 
ATOM   4116 O  O   . THR D  4  92  ? 27.013 -5.372  -12.083 1.00 44.64  ? 92  THR D O   1 
ATOM   4117 C  CB  . THR D  4  92  ? 29.876 -3.915  -11.887 1.00 44.56  ? 92  THR D CB  1 
ATOM   4118 O  OG1 . THR D  4  92  ? 30.563 -4.556  -10.804 1.00 42.93  ? 92  THR D OG1 1 
ATOM   4119 C  CG2 . THR D  4  92  ? 30.643 -2.665  -12.304 1.00 44.48  ? 92  THR D CG2 1 
ATOM   4120 N  N   . ALA D  4  93  ? 27.650 -5.263  -9.921  1.00 43.50  ? 93  ALA D N   1 
ATOM   4121 C  CA  . ALA D  4  93  ? 26.885 -6.466  -9.576  1.00 43.83  ? 93  ALA D CA  1 
ATOM   4122 C  C   . ALA D  4  93  ? 25.416 -6.176  -9.898  1.00 44.09  ? 93  ALA D C   1 
ATOM   4123 O  O   . ALA D  4  93  ? 24.719 -6.994  -10.506 1.00 45.00  ? 93  ALA D O   1 
ATOM   4124 C  CB  . ALA D  4  93  ? 27.071 -6.810  -8.101  1.00 41.39  ? 93  ALA D CB  1 
ATOM   4125 N  N   . HIS D  4  94  ? 24.954 -4.980  -9.511  1.00 44.43  ? 94  HIS D N   1 
ATOM   4126 C  CA  . HIS D  4  94  ? 23.557 -4.549  -9.761  1.00 43.98  ? 94  HIS D CA  1 
ATOM   4127 C  C   . HIS D  4  94  ? 23.254 -4.498  -11.267 1.00 44.77  ? 94  HIS D C   1 
ATOM   4128 O  O   . HIS D  4  94  ? 22.249 -5.053  -11.727 1.00 44.82  ? 94  HIS D O   1 
ATOM   4129 C  CB  . HIS D  4  94  ? 23.299 -3.162  -9.146  1.00 40.11  ? 94  HIS D CB  1 
ATOM   4130 C  CG  . HIS D  4  94  ? 21.870 -2.711  -9.244  1.00 38.91  ? 94  HIS D CG  1 
ATOM   4131 N  ND1 . HIS D  4  94  ? 20.925 -3.007  -8.284  1.00 39.24  ? 94  HIS D ND1 1 
ATOM   4132 C  CD2 . HIS D  4  94  ? 21.217 -1.995  -10.199 1.00 38.58  ? 94  HIS D CD2 1 
ATOM   4133 C  CE1 . HIS D  4  94  ? 19.759 -2.486  -8.639  1.00 38.20  ? 94  HIS D CE1 1 
ATOM   4134 N  NE2 . HIS D  4  94  ? 19.910 -1.865  -9.793  1.00 37.16  ? 94  HIS D NE2 1 
ATOM   4135 N  N   . LEU D  4  95  ? 24.108 -3.806  -12.012 1.00 45.89  ? 95  LEU D N   1 
ATOM   4136 C  CA  . LEU D  4  95  ? 23.940 -3.676  -13.459 1.00 48.25  ? 95  LEU D CA  1 
ATOM   4137 C  C   . LEU D  4  95  ? 23.968 -5.069  -14.058 1.00 49.45  ? 95  LEU D C   1 
ATOM   4138 O  O   . LEU D  4  95  ? 23.291 -5.345  -15.054 1.00 47.04  ? 95  LEU D O   1 
ATOM   4139 C  CB  . LEU D  4  95  ? 25.085 -2.858  -14.077 1.00 48.39  ? 95  LEU D CB  1 
ATOM   4140 C  CG  . LEU D  4  95  ? 24.918 -1.350  -14.177 1.00 48.87  ? 95  LEU D CG  1 
ATOM   4141 C  CD1 . LEU D  4  95  ? 26.240 -0.672  -14.512 1.00 49.55  ? 95  LEU D CD1 1 
ATOM   4142 C  CD2 . LEU D  4  95  ? 23.895 -1.080  -15.255 1.00 48.97  ? 95  LEU D CD2 1 
ATOM   4143 N  N   . ALA D  4  96  ? 24.777 -5.933  -13.442 1.00 50.10  ? 96  ALA D N   1 
ATOM   4144 C  CA  . ALA D  4  96  ? 24.925 -7.305  -13.888 1.00 51.63  ? 96  ALA D CA  1 
ATOM   4145 C  C   . ALA D  4  96  ? 23.592 -8.037  -13.715 1.00 53.11  ? 96  ALA D C   1 
ATOM   4146 O  O   . ALA D  4  96  ? 23.174 -8.818  -14.560 1.00 52.07  ? 96  ALA D O   1 
ATOM   4147 C  CB  . ALA D  4  96  ? 26.017 -7.992  -13.083 1.00 50.87  ? 96  ALA D CB  1 
ATOM   4148 N  N   . ALA D  4  97  ? 22.916 -7.777  -12.612 1.00 55.94  ? 97  ALA D N   1 
ATOM   4149 C  CA  . ALA D  4  97  ? 21.631 -8.414  -12.368 1.00 58.19  ? 97  ALA D CA  1 
ATOM   4150 C  C   . ALA D  4  97  ? 20.572 -7.907  -13.362 1.00 60.06  ? 97  ALA D C   1 
ATOM   4151 O  O   . ALA D  4  97  ? 19.671 -8.644  -13.758 1.00 58.72  ? 97  ALA D O   1 
ATOM   4152 C  CB  . ALA D  4  97  ? 21.187 -8.140  -10.935 1.00 57.34  ? 97  ALA D CB  1 
ATOM   4153 N  N   . GLN D  4  98  ? 20.677 -6.641  -13.755 1.00 63.35  ? 98  GLN D N   1 
ATOM   4154 C  CA  . GLN D  4  98  ? 19.724 -6.063  -14.693 1.00 65.85  ? 98  GLN D CA  1 
ATOM   4155 C  C   . GLN D  4  98  ? 19.893 -6.611  -16.104 1.00 67.72  ? 98  GLN D C   1 
ATOM   4156 O  O   . GLN D  4  98  ? 19.030 -6.411  -16.961 1.00 68.40  ? 98  GLN D O   1 
ATOM   4157 C  CB  . GLN D  4  98  ? 19.847 -4.536  -14.725 1.00 65.19  ? 98  GLN D CB  1 
ATOM   4158 C  CG  . GLN D  4  98  ? 19.471 -3.842  -13.414 1.00 65.72  ? 98  GLN D CG  1 
ATOM   4159 C  CD  . GLN D  4  98  ? 19.643 -2.318  -13.470 1.00 65.37  ? 98  GLN D CD  1 
ATOM   4160 O  OE1 . GLN D  4  98  ? 20.721 -1.818  -13.807 1.00 65.17  ? 98  GLN D OE1 1 
ATOM   4161 N  NE2 . GLN D  4  98  ? 18.582 -1.582  -13.134 1.00 64.80  ? 98  GLN D NE2 1 
ATOM   4162 N  N   . HIS D  4  99  ? 21.002 -7.300  -16.356 1.00 69.76  ? 99  HIS D N   1 
ATOM   4163 C  CA  . HIS D  4  99  ? 21.226 -7.858  -17.683 1.00 72.63  ? 99  HIS D CA  1 
ATOM   4164 C  C   . HIS D  4  99  ? 21.019 -9.364  -17.733 1.00 76.80  ? 99  HIS D C   1 
ATOM   4165 O  O   . HIS D  4  99  ? 20.652 -9.907  -18.767 1.00 75.65  ? 99  HIS D O   1 
ATOM   4166 C  CB  . HIS D  4  99  ? 22.623 -7.475  -18.190 1.00 67.80  ? 99  HIS D CB  1 
ATOM   4167 C  CG  . HIS D  4  99  ? 22.701 -6.075  -18.713 1.00 63.59  ? 99  HIS D CG  1 
ATOM   4168 N  ND1 . HIS D  4  99  ? 22.777 -4.973  -17.886 1.00 61.24  ? 99  HIS D ND1 1 
ATOM   4169 C  CD2 . HIS D  4  99  ? 22.648 -5.592  -19.977 1.00 60.50  ? 99  HIS D CD2 1 
ATOM   4170 C  CE1 . HIS D  4  99  ? 22.765 -3.874  -18.620 1.00 58.50  ? 99  HIS D CE1 1 
ATOM   4171 N  NE2 . HIS D  4  99  ? 22.686 -4.222  -19.891 1.00 56.47  ? 99  HIS D NE2 1 
ATOM   4172 N  N   . VAL D  4  100 ? 21.233 -10.028 -16.607 1.00 83.87  ? 100 VAL D N   1 
ATOM   4173 C  CA  . VAL D  4  100 ? 21.052 -11.472 -16.534 1.00 91.14  ? 100 VAL D CA  1 
ATOM   4174 C  C   . VAL D  4  100 ? 19.577 -11.824 -16.691 1.00 96.00  ? 100 VAL D C   1 
ATOM   4175 O  O   . VAL D  4  100 ? 19.216 -12.666 -17.511 1.00 97.09  ? 100 VAL D O   1 
ATOM   4176 C  CB  . VAL D  4  100 ? 21.546 -12.033 -15.186 1.00 91.46  ? 100 VAL D CB  1 
ATOM   4177 C  CG1 . VAL D  4  100 ? 21.385 -13.541 -15.162 1.00 92.02  ? 100 VAL D CG1 1 
ATOM   4178 C  CG2 . VAL D  4  100 ? 23.000 -11.655 -14.967 1.00 91.75  ? 100 VAL D CG2 1 
ATOM   4179 N  N   . ALA D  4  101 ? 18.726 -11.172 -15.902 1.00 101.33 ? 101 ALA D N   1 
ATOM   4180 C  CA  . ALA D  4  101 ? 17.287 -11.416 -15.958 1.00 106.13 ? 101 ALA D CA  1 
ATOM   4181 C  C   . ALA D  4  101 ? 16.755 -11.286 -17.386 1.00 108.89 ? 101 ALA D C   1 
ATOM   4182 O  O   . ALA D  4  101 ? 15.635 -11.712 -17.682 1.00 110.07 ? 101 ALA D O   1 
ATOM   4183 C  CB  . ALA D  4  101 ? 16.552 -10.429 -15.031 1.00 106.81 ? 101 ALA D CB  1 
ATOM   4184 N  N   . ARG D  4  102 ? 17.561 -10.699 -18.268 1.00 111.54 ? 102 ARG D N   1 
ATOM   4185 C  CA  . ARG D  4  102 ? 17.166 -10.517 -19.658 1.00 113.73 ? 102 ARG D CA  1 
ATOM   4186 C  C   . ARG D  4  102 ? 17.607 -11.709 -20.500 1.00 114.17 ? 102 ARG D C   1 
ATOM   4187 O  O   . ARG D  4  102 ? 18.776 -11.828 -20.863 1.00 115.22 ? 102 ARG D O   1 
ATOM   4188 C  CB  . ARG D  4  102 ? 17.787 -9.234  -20.219 1.00 114.61 ? 102 ARG D CB  1 
ATOM   4189 C  CG  . ARG D  4  102 ? 16.947 -8.579  -21.293 1.00 116.10 ? 102 ARG D CG  1 
ATOM   4190 C  CD  . ARG D  4  102 ? 15.658 -8.039  -20.698 1.00 117.09 ? 102 ARG D CD  1 
ATOM   4191 N  NE  . ARG D  4  102 ? 14.869 -7.287  -21.670 1.00 117.76 ? 102 ARG D NE  1 
ATOM   4192 C  CZ  . ARG D  4  102 ? 13.932 -6.400  -21.343 1.00 118.39 ? 102 ARG D CZ  1 
ATOM   4193 N  NH1 . ARG D  4  102 ? 13.668 -6.153  -20.066 1.00 118.40 ? 102 ARG D NH1 1 
ATOM   4194 N  NH2 . ARG D  4  102 ? 13.263 -5.759  -22.294 1.00 118.72 ? 102 ARG D NH2 1 
ATOM   4195 N  N   . THR D  4  103 ? 16.664 -12.593 -20.805 1.00 113.89 ? 103 THR D N   1 
ATOM   4196 C  CA  . THR D  4  103 ? 16.961 -13.777 -21.600 1.00 113.24 ? 103 THR D CA  1 
ATOM   4197 C  C   . THR D  4  103 ? 17.298 -13.411 -23.049 1.00 111.70 ? 103 THR D C   1 
ATOM   4198 O  O   . THR D  4  103 ? 16.616 -12.604 -23.678 1.00 111.65 ? 103 THR D O   1 
ATOM   4199 C  CB  . THR D  4  103 ? 15.770 -14.763 -21.583 1.00 113.71 ? 103 THR D CB  1 
ATOM   4200 O  OG1 . THR D  4  103 ? 15.233 -14.885 -22.902 1.00 114.54 ? 103 THR D OG1 1 
ATOM   4201 C  CG2 . THR D  4  103 ? 14.680 -14.270 -20.646 1.00 113.90 ? 103 THR D CG2 1 
ATOM   4202 N  N   . GLY D  4  104 ? 18.364 -14.011 -23.570 1.00 109.63 ? 104 GLY D N   1 
ATOM   4203 C  CA  . GLY D  4  104 ? 18.782 -13.733 -24.932 1.00 106.31 ? 104 GLY D CA  1 
ATOM   4204 C  C   . GLY D  4  104 ? 20.095 -12.974 -24.976 1.00 103.91 ? 104 GLY D C   1 
ATOM   4205 O  O   . GLY D  4  104 ? 20.609 -12.691 -26.054 1.00 103.28 ? 104 GLY D O   1 
ATOM   4206 N  N   . LEU D  4  105 ? 20.640 -12.650 -23.804 1.00 101.71 ? 105 LEU D N   1 
ATOM   4207 C  CA  . LEU D  4  105 ? 21.896 -11.915 -23.712 1.00 99.81  ? 105 LEU D CA  1 
ATOM   4208 C  C   . LEU D  4  105 ? 23.135 -12.783 -23.561 1.00 97.92  ? 105 LEU D C   1 
ATOM   4209 O  O   . LEU D  4  105 ? 23.323 -13.455 -22.545 1.00 97.83  ? 105 LEU D O   1 
ATOM   4210 C  CB  . LEU D  4  105 ? 21.861 -10.929 -22.543 1.00 100.58 ? 105 LEU D CB  1 
ATOM   4211 C  CG  . LEU D  4  105 ? 21.375 -9.528  -22.890 1.00 102.03 ? 105 LEU D CG  1 
ATOM   4212 C  CD1 . LEU D  4  105 ? 19.901 -9.573  -23.254 1.00 103.55 ? 105 LEU D CD1 1 
ATOM   4213 C  CD2 . LEU D  4  105 ? 21.604 -8.613  -21.708 1.00 102.53 ? 105 LEU D CD2 1 
ATOM   4214 N  N   . LYS D  4  106 ? 23.989 -12.750 -24.577 1.00 94.98  ? 106 LYS D N   1 
ATOM   4215 C  CA  . LYS D  4  106 ? 25.204 -13.539 -24.566 1.00 92.12  ? 106 LYS D CA  1 
ATOM   4216 C  C   . LYS D  4  106 ? 26.396 -12.647 -24.240 1.00 89.03  ? 106 LYS D C   1 
ATOM   4217 O  O   . LYS D  4  106 ? 26.417 -11.474 -24.605 1.00 88.44  ? 106 LYS D O   1 
ATOM   4218 C  CB  . LYS D  4  106 ? 25.417 -14.203 -25.935 1.00 93.06  ? 106 LYS D CB  1 
ATOM   4219 C  CG  . LYS D  4  106 ? 24.125 -14.659 -26.612 1.00 92.84  ? 106 LYS D CG  1 
ATOM   4220 C  CD  . LYS D  4  106 ? 24.431 -15.427 -27.885 1.00 92.53  ? 106 LYS D CD  1 
ATOM   4221 C  CE  . LYS D  4  106 ? 23.225 -15.502 -28.799 1.00 91.79  ? 106 LYS D CE  1 
ATOM   4222 N  NZ  . LYS D  4  106 ? 23.647 -15.769 -30.204 1.00 91.48  ? 106 LYS D NZ  1 
ATOM   4223 N  N   . ALA D  4  107 ? 27.384 -13.205 -23.548 1.00 85.68  ? 107 ALA D N   1 
ATOM   4224 C  CA  . ALA D  4  107 ? 28.574 -12.452 -23.182 1.00 83.01  ? 107 ALA D CA  1 
ATOM   4225 C  C   . ALA D  4  107 ? 29.212 -11.808 -24.402 1.00 81.13  ? 107 ALA D C   1 
ATOM   4226 O  O   . ALA D  4  107 ? 29.754 -10.708 -24.317 1.00 80.70  ? 107 ALA D O   1 
ATOM   4227 C  CB  . ALA D  4  107 ? 29.582 -13.361 -22.501 1.00 82.02  ? 107 ALA D CB  1 
ATOM   4228 N  N   . VAL D  4  108 ? 29.133 -12.496 -25.535 1.00 79.50  ? 108 VAL D N   1 
ATOM   4229 C  CA  . VAL D  4  108 ? 29.712 -12.010 -26.781 1.00 78.37  ? 108 VAL D CA  1 
ATOM   4230 C  C   . VAL D  4  108 ? 29.133 -10.669 -27.222 1.00 77.99  ? 108 VAL D C   1 
ATOM   4231 O  O   . VAL D  4  108 ? 29.778 -9.931  -27.962 1.00 77.24  ? 108 VAL D O   1 
ATOM   4232 C  CB  . VAL D  4  108 ? 29.519 -13.039 -27.922 1.00 77.48  ? 108 VAL D CB  1 
ATOM   4233 C  CG1 . VAL D  4  108 ? 30.126 -12.517 -29.227 1.00 77.44  ? 108 VAL D CG1 1 
ATOM   4234 C  CG2 . VAL D  4  108 ? 30.170 -14.341 -27.536 1.00 77.19  ? 108 VAL D CG2 1 
ATOM   4235 N  N   . TYR D  4  109 ? 27.920 -10.355 -26.780 1.00 77.81  ? 109 TYR D N   1 
ATOM   4236 C  CA  . TYR D  4  109 ? 27.317 -9.086  -27.161 1.00 78.65  ? 109 TYR D CA  1 
ATOM   4237 C  C   . TYR D  4  109 ? 28.036 -7.934  -26.478 1.00 76.69  ? 109 TYR D C   1 
ATOM   4238 O  O   . TYR D  4  109 ? 28.096 -6.823  -27.014 1.00 76.45  ? 109 TYR D O   1 
ATOM   4239 C  CB  . TYR D  4  109 ? 25.839 -9.037  -26.789 1.00 82.56  ? 109 TYR D CB  1 
ATOM   4240 C  CG  . TYR D  4  109 ? 24.980 -10.056 -27.496 1.00 87.05  ? 109 TYR D CG  1 
ATOM   4241 C  CD1 . TYR D  4  109 ? 25.122 -10.294 -28.865 1.00 89.02  ? 109 TYR D CD1 1 
ATOM   4242 C  CD2 . TYR D  4  109 ? 23.989 -10.751 -26.804 1.00 89.40  ? 109 TYR D CD2 1 
ATOM   4243 C  CE1 . TYR D  4  109 ? 24.292 -11.198 -29.530 1.00 90.80  ? 109 TYR D CE1 1 
ATOM   4244 C  CE2 . TYR D  4  109 ? 23.155 -11.654 -27.454 1.00 91.05  ? 109 TYR D CE2 1 
ATOM   4245 C  CZ  . TYR D  4  109 ? 23.310 -11.873 -28.818 1.00 91.75  ? 109 TYR D CZ  1 
ATOM   4246 O  OH  . TYR D  4  109 ? 22.478 -12.753 -29.473 1.00 93.20  ? 109 TYR D OH  1 
ATOM   4247 N  N   . PHE D  4  110 ? 28.570 -8.202  -25.288 1.00 74.09  ? 110 PHE D N   1 
ATOM   4248 C  CA  . PHE D  4  110 ? 29.299 -7.189  -24.542 1.00 71.19  ? 110 PHE D CA  1 
ATOM   4249 C  C   . PHE D  4  110 ? 30.702 -7.057  -25.087 1.00 69.63  ? 110 PHE D C   1 
ATOM   4250 O  O   . PHE D  4  110 ? 31.407 -6.100  -24.780 1.00 70.81  ? 110 PHE D O   1 
ATOM   4251 C  CB  . PHE D  4  110 ? 29.355 -7.528  -23.059 1.00 70.81  ? 110 PHE D CB  1 
ATOM   4252 C  CG  . PHE D  4  110 ? 28.115 -7.154  -22.311 1.00 70.94  ? 110 PHE D CG  1 
ATOM   4253 C  CD1 . PHE D  4  110 ? 26.936 -7.866  -22.498 1.00 71.71  ? 110 PHE D CD1 1 
ATOM   4254 C  CD2 . PHE D  4  110 ? 28.117 -6.077  -21.429 1.00 69.79  ? 110 PHE D CD2 1 
ATOM   4255 C  CE1 . PHE D  4  110 ? 25.775 -7.511  -21.811 1.00 72.34  ? 110 PHE D CE1 1 
ATOM   4256 C  CE2 . PHE D  4  110 ? 26.965 -5.716  -20.743 1.00 70.20  ? 110 PHE D CE2 1 
ATOM   4257 C  CZ  . PHE D  4  110 ? 25.792 -6.433  -20.932 1.00 70.83  ? 110 PHE D CZ  1 
ATOM   4258 N  N   . ASP D  4  111 ? 31.123 -8.034  -25.878 1.00 66.78  ? 111 ASP D N   1 
ATOM   4259 C  CA  . ASP D  4  111 ? 32.432 -7.945  -26.482 1.00 63.17  ? 111 ASP D CA  1 
ATOM   4260 C  C   . ASP D  4  111 ? 32.249 -7.010  -27.675 1.00 60.30  ? 111 ASP D C   1 
ATOM   4261 O  O   . ASP D  4  111 ? 33.091 -6.159  -27.948 1.00 60.83  ? 111 ASP D O   1 
ATOM   4262 C  CB  . ASP D  4  111 ? 32.931 -9.320  -26.943 1.00 62.97  ? 111 ASP D CB  1 
ATOM   4263 C  CG  . ASP D  4  111 ? 33.259 -10.239 -25.787 1.00 62.90  ? 111 ASP D CG  1 
ATOM   4264 O  OD1 . ASP D  4  111 ? 33.669 -9.740  -24.721 1.00 63.62  ? 111 ASP D OD1 1 
ATOM   4265 O  OD2 . ASP D  4  111 ? 33.122 -11.467 -25.951 1.00 63.59  ? 111 ASP D OD2 1 
ATOM   4266 N  N   . ALA D  4  112 ? 31.126 -7.145  -28.362 1.00 56.37  ? 112 ALA D N   1 
ATOM   4267 C  CA  . ALA D  4  112 ? 30.871 -6.314  -29.524 1.00 55.08  ? 112 ALA D CA  1 
ATOM   4268 C  C   . ALA D  4  112 ? 30.683 -4.876  -29.075 1.00 53.59  ? 112 ALA D C   1 
ATOM   4269 O  O   . ALA D  4  112 ? 31.208 -3.942  -29.710 1.00 51.76  ? 112 ALA D O   1 
ATOM   4270 C  CB  . ALA D  4  112 ? 29.646 -6.810  -30.268 1.00 54.32  ? 112 ALA D CB  1 
ATOM   4271 N  N   . MET D  4  113 ? 29.934 -4.707  -27.982 1.00 51.71  ? 113 MET D N   1 
ATOM   4272 C  CA  . MET D  4  113 ? 29.680 -3.383  -27.399 1.00 49.66  ? 113 MET D CA  1 
ATOM   4273 C  C   . MET D  4  113 ? 31.028 -2.745  -27.081 1.00 49.22  ? 113 MET D C   1 
ATOM   4274 O  O   . MET D  4  113 ? 31.209 -1.545  -27.264 1.00 48.19  ? 113 MET D O   1 
ATOM   4275 C  CB  . MET D  4  113 ? 28.858 -3.513  -26.117 1.00 47.22  ? 113 MET D CB  1 
ATOM   4276 C  CG  . MET D  4  113 ? 28.647 -2.209  -25.356 1.00 43.92  ? 113 MET D CG  1 
ATOM   4277 S  SD  . MET D  4  113 ? 27.638 -0.943  -26.208 1.00 46.34  ? 113 MET D SD  1 
ATOM   4278 C  CE  . MET D  4  113 ? 26.107 -1.153  -25.445 1.00 40.74  ? 113 MET D CE  1 
ATOM   4279 N  N   . GLY D  4  114 ? 31.964 -3.566  -26.611 1.00 48.86  ? 114 GLY D N   1 
ATOM   4280 C  CA  . GLY D  4  114 ? 33.288 -3.070  -26.293 1.00 51.34  ? 114 GLY D CA  1 
ATOM   4281 C  C   . GLY D  4  114 ? 33.966 -2.502  -27.529 1.00 54.04  ? 114 GLY D C   1 
ATOM   4282 O  O   . GLY D  4  114 ? 34.500 -1.391  -27.506 1.00 56.07  ? 114 GLY D O   1 
ATOM   4283 N  N   . LYS D  4  115 ? 33.927 -3.257  -28.625 1.00 54.37  ? 115 LYS D N   1 
ATOM   4284 C  CA  . LYS D  4  115 ? 34.568 -2.821  -29.863 1.00 54.65  ? 115 LYS D CA  1 
ATOM   4285 C  C   . LYS D  4  115 ? 33.880 -1.596  -30.440 1.00 53.43  ? 115 LYS D C   1 
ATOM   4286 O  O   . LYS D  4  115 ? 34.512 -0.798  -31.136 1.00 51.56  ? 115 LYS D O   1 
ATOM   4287 C  CB  . LYS D  4  115 ? 34.598 -3.972  -30.857 1.00 56.63  ? 115 LYS D CB  1 
ATOM   4288 C  CG  . LYS D  4  115 ? 34.751 -5.318  -30.159 1.00 58.95  ? 115 LYS D CG  1 
ATOM   4289 C  CD  . LYS D  4  115 ? 35.272 -6.403  -31.080 1.00 62.70  ? 115 LYS D CD  1 
ATOM   4290 C  CE  . LYS D  4  115 ? 34.832 -7.798  -30.615 1.00 63.99  ? 115 LYS D CE  1 
ATOM   4291 N  NZ  . LYS D  4  115 ? 35.347 -8.884  -31.507 1.00 64.08  ? 115 LYS D NZ  1 
ATOM   4292 N  N   . VAL D  4  116 ? 32.588 -1.447  -30.152 1.00 52.76  ? 116 VAL D N   1 
ATOM   4293 C  CA  . VAL D  4  116 ? 31.841 -0.298  -30.647 1.00 54.05  ? 116 VAL D CA  1 
ATOM   4294 C  C   . VAL D  4  116 ? 32.316 0.940   -29.892 1.00 53.82  ? 116 VAL D C   1 
ATOM   4295 O  O   . VAL D  4  116 ? 32.631 1.979   -30.489 1.00 53.35  ? 116 VAL D O   1 
ATOM   4296 C  CB  . VAL D  4  116 ? 30.321 -0.480  -30.413 1.00 55.35  ? 116 VAL D CB  1 
ATOM   4297 C  CG1 . VAL D  4  116 ? 29.554 0.816   -30.761 1.00 53.06  ? 116 VAL D CG1 1 
ATOM   4298 C  CG2 . VAL D  4  116 ? 29.832 -1.639  -31.257 1.00 56.39  ? 116 VAL D CG2 1 
ATOM   4299 N  N   . LEU D  4  117 ? 32.391 0.815   -28.573 1.00 52.06  ? 117 LEU D N   1 
ATOM   4300 C  CA  . LEU D  4  117 ? 32.833 1.932   -27.769 1.00 51.43  ? 117 LEU D CA  1 
ATOM   4301 C  C   . LEU D  4  117 ? 34.243 2.364   -28.176 1.00 52.09  ? 117 LEU D C   1 
ATOM   4302 O  O   . LEU D  4  117 ? 34.514 3.565   -28.298 1.00 52.90  ? 117 LEU D O   1 
ATOM   4303 C  CB  . LEU D  4  117 ? 32.770 1.584   -26.265 1.00 47.86  ? 117 LEU D CB  1 
ATOM   4304 C  CG  . LEU D  4  117 ? 31.334 1.432   -25.725 1.00 44.30  ? 117 LEU D CG  1 
ATOM   4305 C  CD1 . LEU D  4  117 ? 31.340 1.165   -24.237 1.00 41.78  ? 117 LEU D CD1 1 
ATOM   4306 C  CD2 . LEU D  4  117 ? 30.540 2.686   -26.028 1.00 41.63  ? 117 LEU D CD2 1 
ATOM   4307 N  N   . MET D  4  118 ? 35.128 1.391   -28.409 1.00 51.72  ? 118 MET D N   1 
ATOM   4308 C  CA  . MET D  4  118 ? 36.507 1.683   -28.804 1.00 51.57  ? 118 MET D CA  1 
ATOM   4309 C  C   . MET D  4  118 ? 36.578 2.281   -30.207 1.00 52.93  ? 118 MET D C   1 
ATOM   4310 O  O   . MET D  4  118 ? 37.608 2.804   -30.616 1.00 52.66  ? 118 MET D O   1 
ATOM   4311 C  CB  . MET D  4  118 ? 37.353 0.412   -28.777 1.00 51.48  ? 118 MET D CB  1 
ATOM   4312 C  CG  . MET D  4  118 ? 37.493 -0.240  -27.403 1.00 53.19  ? 118 MET D CG  1 
ATOM   4313 S  SD  . MET D  4  118 ? 38.569 0.673   -26.260 1.00 56.85  ? 118 MET D SD  1 
ATOM   4314 C  CE  . MET D  4  118 ? 37.337 1.365   -25.188 1.00 55.40  ? 118 MET D CE  1 
ATOM   4315 N  N   . THR D  4  119 ? 35.479 2.194   -30.944 1.00 54.13  ? 119 THR D N   1 
ATOM   4316 C  CA  . THR D  4  119 ? 35.419 2.711   -32.296 1.00 53.24  ? 119 THR D CA  1 
ATOM   4317 C  C   . THR D  4  119 ? 34.718 4.059   -32.323 1.00 54.41  ? 119 THR D C   1 
ATOM   4318 O  O   . THR D  4  119 ? 35.120 4.951   -33.067 1.00 54.93  ? 119 THR D O   1 
ATOM   4319 C  CB  . THR D  4  119 ? 34.639 1.748   -33.200 1.00 54.62  ? 119 THR D CB  1 
ATOM   4320 O  OG1 . THR D  4  119 ? 35.269 0.461   -33.179 1.00 54.46  ? 119 THR D OG1 1 
ATOM   4321 C  CG2 . THR D  4  119 ? 34.586 2.274   -34.622 1.00 52.37  ? 119 THR D CG2 1 
ATOM   4322 N  N   . VAL D  4  120 ? 33.665 4.206   -31.519 1.00 54.20  ? 120 VAL D N   1 
ATOM   4323 C  CA  . VAL D  4  120 ? 32.913 5.453   -31.490 1.00 52.70  ? 120 VAL D CA  1 
ATOM   4324 C  C   . VAL D  4  120 ? 33.621 6.540   -30.686 1.00 52.37  ? 120 VAL D C   1 
ATOM   4325 O  O   . VAL D  4  120 ? 33.811 7.656   -31.171 1.00 53.53  ? 120 VAL D O   1 
ATOM   4326 C  CB  . VAL D  4  120 ? 31.495 5.241   -30.905 1.00 52.82  ? 120 VAL D CB  1 
ATOM   4327 C  CG1 . VAL D  4  120 ? 30.746 6.567   -30.851 1.00 51.95  ? 120 VAL D CG1 1 
ATOM   4328 C  CG2 . VAL D  4  120 ? 30.731 4.239   -31.756 1.00 52.61  ? 120 VAL D CG2 1 
ATOM   4329 N  N   . LEU D  4  121 ? 34.037 6.210   -29.470 1.00 51.25  ? 121 LEU D N   1 
ATOM   4330 C  CA  . LEU D  4  121 ? 34.692 7.188   -28.606 1.00 49.72  ? 121 LEU D CA  1 
ATOM   4331 C  C   . LEU D  4  121 ? 35.796 8.040   -29.231 1.00 49.43  ? 121 LEU D C   1 
ATOM   4332 O  O   . LEU D  4  121 ? 35.782 9.262   -29.076 1.00 49.66  ? 121 LEU D O   1 
ATOM   4333 C  CB  . LEU D  4  121 ? 35.221 6.512   -27.345 1.00 46.90  ? 121 LEU D CB  1 
ATOM   4334 C  CG  . LEU D  4  121 ? 34.104 5.988   -26.456 1.00 46.25  ? 121 LEU D CG  1 
ATOM   4335 C  CD1 . LEU D  4  121 ? 34.700 5.386   -25.216 1.00 45.48  ? 121 LEU D CD1 1 
ATOM   4336 C  CD2 . LEU D  4  121 ? 33.141 7.110   -26.106 1.00 45.63  ? 121 LEU D CD2 1 
ATOM   4337 N  N   . PRO D  4  122 ? 36.762 7.416   -29.932 1.00 48.69  ? 122 PRO D N   1 
ATOM   4338 C  CA  . PRO D  4  122 ? 37.837 8.209   -30.550 1.00 48.56  ? 122 PRO D CA  1 
ATOM   4339 C  C   . PRO D  4  122 ? 37.362 9.304   -31.502 1.00 48.98  ? 122 PRO D C   1 
ATOM   4340 O  O   . PRO D  4  122 ? 38.083 10.269  -31.748 1.00 48.72  ? 122 PRO D O   1 
ATOM   4341 C  CB  . PRO D  4  122 ? 38.705 7.157   -31.237 1.00 45.70  ? 122 PRO D CB  1 
ATOM   4342 C  CG  . PRO D  4  122 ? 37.797 5.988   -31.389 1.00 48.78  ? 122 PRO D CG  1 
ATOM   4343 C  CD  . PRO D  4  122 ? 36.998 5.983   -30.133 1.00 48.51  ? 122 PRO D CD  1 
ATOM   4344 N  N   . SER D  4  123 ? 36.150 9.177   -32.027 1.00 50.71  ? 123 SER D N   1 
ATOM   4345 C  CA  . SER D  4  123 ? 35.630 10.184  -32.941 1.00 52.49  ? 123 SER D CA  1 
ATOM   4346 C  C   . SER D  4  123 ? 35.094 11.364  -32.161 1.00 53.74  ? 123 SER D C   1 
ATOM   4347 O  O   . SER D  4  123 ? 35.000 12.471  -32.692 1.00 55.65  ? 123 SER D O   1 
ATOM   4348 C  CB  . SER D  4  123 ? 34.505 9.615   -33.809 1.00 54.16  ? 123 SER D CB  1 
ATOM   4349 O  OG  . SER D  4  123 ? 34.962 8.543   -34.619 1.00 55.81  ? 123 SER D OG  1 
ATOM   4350 N  N   . LEU D  4  124 ? 34.737 11.131  -30.900 1.00 53.81  ? 124 LEU D N   1 
ATOM   4351 C  CA  . LEU D  4  124 ? 34.190 12.191  -30.055 1.00 52.14  ? 124 LEU D CA  1 
ATOM   4352 C  C   . LEU D  4  124 ? 35.199 12.813  -29.093 1.00 51.28  ? 124 LEU D C   1 
ATOM   4353 O  O   . LEU D  4  124 ? 35.094 13.988  -28.742 1.00 50.99  ? 124 LEU D O   1 
ATOM   4354 C  CB  . LEU D  4  124 ? 33.016 11.647  -29.241 1.00 50.82  ? 124 LEU D CB  1 
ATOM   4355 C  CG  . LEU D  4  124 ? 31.816 11.140  -30.035 1.00 51.06  ? 124 LEU D CG  1 
ATOM   4356 C  CD1 . LEU D  4  124 ? 30.980 10.257  -29.130 1.00 49.74  ? 124 LEU D CD1 1 
ATOM   4357 C  CD2 . LEU D  4  124 ? 31.011 12.320  -30.596 1.00 50.22  ? 124 LEU D CD2 1 
ATOM   4358 N  N   . ILE D  4  125 ? 36.182 12.023  -28.682 1.00 50.88  ? 125 ILE D N   1 
ATOM   4359 C  CA  . ILE D  4  125 ? 37.168 12.453  -27.695 1.00 51.18  ? 125 ILE D CA  1 
ATOM   4360 C  C   . ILE D  4  125 ? 38.543 12.897  -28.218 1.00 51.52  ? 125 ILE D C   1 
ATOM   4361 O  O   . ILE D  4  125 ? 39.126 12.245  -29.084 1.00 50.70  ? 125 ILE D O   1 
ATOM   4362 C  CB  . ILE D  4  125 ? 37.347 11.309  -26.652 1.00 49.76  ? 125 ILE D CB  1 
ATOM   4363 C  CG1 . ILE D  4  125 ? 36.042 11.118  -25.876 1.00 49.25  ? 125 ILE D CG1 1 
ATOM   4364 C  CG2 . ILE D  4  125 ? 38.506 11.592  -25.714 1.00 50.33  ? 125 ILE D CG2 1 
ATOM   4365 C  CD1 . ILE D  4  125 ? 35.997 9.841   -25.038 1.00 46.83  ? 125 ILE D CD1 1 
ATOM   4366 N  N   . ASP D  4  126 ? 39.057 13.997  -27.655 1.00 51.12  ? 126 ASP D N   1 
ATOM   4367 C  CA  . ASP D  4  126 ? 40.367 14.531  -28.029 1.00 50.79  ? 126 ASP D CA  1 
ATOM   4368 C  C   . ASP D  4  126 ? 41.462 13.604  -27.520 1.00 51.22  ? 126 ASP D C   1 
ATOM   4369 O  O   . ASP D  4  126 ? 41.522 13.308  -26.329 1.00 49.49  ? 126 ASP D O   1 
ATOM   4370 C  CB  . ASP D  4  126 ? 40.592 15.922  -27.434 1.00 50.61  ? 126 ASP D CB  1 
ATOM   4371 C  CG  . ASP D  4  126 ? 39.724 16.980  -28.073 1.00 52.52  ? 126 ASP D CG  1 
ATOM   4372 O  OD1 . ASP D  4  126 ? 39.287 16.784  -29.226 1.00 51.02  ? 126 ASP D OD1 1 
ATOM   4373 O  OD2 . ASP D  4  126 ? 39.490 18.028  -27.424 1.00 53.94  ? 126 ASP D OD2 1 
ATOM   4374 N  N   . ASN D  4  127 ? 42.336 13.162  -28.419 1.00 52.50  ? 127 ASN D N   1 
ATOM   4375 C  CA  . ASN D  4  127 ? 43.420 12.247  -28.056 1.00 53.65  ? 127 ASN D CA  1 
ATOM   4376 C  C   . ASN D  4  127 ? 42.963 11.059  -27.254 1.00 51.88  ? 127 ASN D C   1 
ATOM   4377 O  O   . ASN D  4  127 ? 43.556 10.723  -26.240 1.00 51.69  ? 127 ASN D O   1 
ATOM   4378 C  CB  . ASN D  4  127 ? 44.514 12.966  -27.271 1.00 57.85  ? 127 ASN D CB  1 
ATOM   4379 C  CG  . ASN D  4  127 ? 45.575 13.548  -28.167 1.00 61.80  ? 127 ASN D CG  1 
ATOM   4380 O  OD1 . ASN D  4  127 ? 46.301 12.827  -28.857 1.00 64.84  ? 127 ASN D OD1 1 
ATOM   4381 N  ND2 . ASN D  4  127 ? 45.668 14.866  -28.171 1.00 64.48  ? 127 ASN D ND2 1 
ATOM   4382 N  N   . PHE D  4  128 ? 41.893 10.426  -27.712 1.00 50.94  ? 128 PHE D N   1 
ATOM   4383 C  CA  . PHE D  4  128 ? 41.371 9.242   -27.051 1.00 49.05  ? 128 PHE D CA  1 
ATOM   4384 C  C   . PHE D  4  128 ? 42.519 8.281   -26.731 1.00 48.82  ? 128 PHE D C   1 
ATOM   4385 O  O   . PHE D  4  128 ? 43.401 8.053   -27.566 1.00 50.69  ? 128 PHE D O   1 
ATOM   4386 C  CB  . PHE D  4  128 ? 40.375 8.545   -27.983 1.00 46.12  ? 128 PHE D CB  1 
ATOM   4387 C  CG  . PHE D  4  128 ? 39.854 7.241   -27.450 1.00 44.50  ? 128 PHE D CG  1 
ATOM   4388 C  CD1 . PHE D  4  128 ? 38.847 7.218   -26.492 1.00 40.06  ? 128 PHE D CD1 1 
ATOM   4389 C  CD2 . PHE D  4  128 ? 40.359 6.035   -27.921 1.00 43.10  ? 128 PHE D CD2 1 
ATOM   4390 C  CE1 . PHE D  4  128 ? 38.357 6.027   -26.026 1.00 40.71  ? 128 PHE D CE1 1 
ATOM   4391 C  CE2 . PHE D  4  128 ? 39.869 4.847   -27.452 1.00 42.26  ? 128 PHE D CE2 1 
ATOM   4392 C  CZ  . PHE D  4  128 ? 38.864 4.841   -26.504 1.00 41.17  ? 128 PHE D CZ  1 
ATOM   4393 N  N   . ASN D  4  129 ? 42.503 7.704   -25.537 1.00 48.23  ? 129 ASN D N   1 
ATOM   4394 C  CA  . ASN D  4  129 ? 43.546 6.760   -25.157 1.00 47.61  ? 129 ASN D CA  1 
ATOM   4395 C  C   . ASN D  4  129 ? 43.009 5.337   -25.053 1.00 48.55  ? 129 ASN D C   1 
ATOM   4396 O  O   . ASN D  4  129 ? 42.479 4.937   -24.021 1.00 49.14  ? 129 ASN D O   1 
ATOM   4397 C  CB  . ASN D  4  129 ? 44.150 7.157   -23.828 1.00 46.07  ? 129 ASN D CB  1 
ATOM   4398 C  CG  . ASN D  4  129 ? 45.296 6.266   -23.433 1.00 45.98  ? 129 ASN D CG  1 
ATOM   4399 O  OD1 . ASN D  4  129 ? 45.275 5.047   -23.667 1.00 44.43  ? 129 ASN D OD1 1 
ATOM   4400 N  ND2 . ASN D  4  129 ? 46.304 6.863   -22.813 1.00 45.47  ? 129 ASN D ND2 1 
ATOM   4401 N  N   . PRO D  4  130 ? 43.158 4.543   -26.124 1.00 50.44  ? 130 PRO D N   1 
ATOM   4402 C  CA  . PRO D  4  130 ? 42.678 3.155   -26.143 1.00 50.82  ? 130 PRO D CA  1 
ATOM   4403 C  C   . PRO D  4  130 ? 43.167 2.243   -25.023 1.00 51.54  ? 130 PRO D C   1 
ATOM   4404 O  O   . PRO D  4  130 ? 42.429 1.389   -24.529 1.00 51.60  ? 130 PRO D O   1 
ATOM   4405 C  CB  . PRO D  4  130 ? 43.123 2.666   -27.516 1.00 50.68  ? 130 PRO D CB  1 
ATOM   4406 C  CG  . PRO D  4  130 ? 44.343 3.515   -27.790 1.00 49.62  ? 130 PRO D CG  1 
ATOM   4407 C  CD  . PRO D  4  130 ? 43.888 4.863   -27.365 1.00 48.69  ? 130 PRO D CD  1 
ATOM   4408 N  N   . ASP D  4  131 ? 44.415 2.414   -24.619 1.00 53.32  ? 131 ASP D N   1 
ATOM   4409 C  CA  . ASP D  4  131 ? 44.942 1.574   -23.558 1.00 55.14  ? 131 ASP D CA  1 
ATOM   4410 C  C   . ASP D  4  131 ? 44.318 1.887   -22.208 1.00 54.58  ? 131 ASP D C   1 
ATOM   4411 O  O   . ASP D  4  131 ? 43.834 0.989   -21.510 1.00 55.66  ? 131 ASP D O   1 
ATOM   4412 C  CB  . ASP D  4  131 ? 46.464 1.706   -23.479 1.00 56.44  ? 131 ASP D CB  1 
ATOM   4413 C  CG  . ASP D  4  131 ? 47.171 0.981   -24.628 1.00 57.73  ? 131 ASP D CG  1 
ATOM   4414 O  OD1 . ASP D  4  131 ? 48.419 0.894   -24.610 1.00 58.69  ? 131 ASP D OD1 1 
ATOM   4415 O  OD2 . ASP D  4  131 ? 46.471 0.495   -25.548 1.00 60.29  ? 131 ASP D OD2 1 
ATOM   4416 N  N   . ALA D  4  132 ? 44.321 3.156   -21.834 1.00 52.92  ? 132 ALA D N   1 
ATOM   4417 C  CA  . ALA D  4  132 ? 43.751 3.529   -20.550 1.00 52.63  ? 132 ALA D CA  1 
ATOM   4418 C  C   . ALA D  4  132 ? 42.285 3.115   -20.501 1.00 53.74  ? 132 ALA D C   1 
ATOM   4419 O  O   . ALA D  4  132 ? 41.775 2.698   -19.453 1.00 53.26  ? 132 ALA D O   1 
ATOM   4420 C  CB  . ALA D  4  132 ? 43.880 5.019   -20.333 1.00 51.73  ? 132 ALA D CB  1 
ATOM   4421 N  N   . TRP D  4  133 ? 41.600 3.232   -21.637 1.00 53.85  ? 133 TRP D N   1 
ATOM   4422 C  CA  . TRP D  4  133 ? 40.198 2.854   -21.677 1.00 54.08  ? 133 TRP D CA  1 
ATOM   4423 C  C   . TRP D  4  133 ? 40.054 1.342   -21.556 1.00 55.47  ? 133 TRP D C   1 
ATOM   4424 O  O   . TRP D  4  133 ? 39.238 0.861   -20.776 1.00 55.60  ? 133 TRP D O   1 
ATOM   4425 C  CB  . TRP D  4  133 ? 39.519 3.374   -22.952 1.00 51.37  ? 133 TRP D CB  1 
ATOM   4426 C  CG  . TRP D  4  133 ? 39.044 4.794   -22.839 1.00 48.58  ? 133 TRP D CG  1 
ATOM   4427 C  CD1 . TRP D  4  133 ? 39.765 5.916   -23.104 1.00 47.48  ? 133 TRP D CD1 1 
ATOM   4428 C  CD2 . TRP D  4  133 ? 37.741 5.241   -22.425 1.00 47.00  ? 133 TRP D CD2 1 
ATOM   4429 N  NE1 . TRP D  4  133 ? 38.996 7.039   -22.889 1.00 46.94  ? 133 TRP D NE1 1 
ATOM   4430 C  CE2 . TRP D  4  133 ? 37.749 6.656   -22.473 1.00 46.35  ? 133 TRP D CE2 1 
ATOM   4431 C  CE3 . TRP D  4  133 ? 36.570 4.583   -22.018 1.00 45.69  ? 133 TRP D CE3 1 
ATOM   4432 C  CZ2 . TRP D  4  133 ? 36.634 7.431   -22.132 1.00 44.91  ? 133 TRP D CZ2 1 
ATOM   4433 C  CZ3 . TRP D  4  133 ? 35.450 5.358   -21.674 1.00 46.12  ? 133 TRP D CZ3 1 
ATOM   4434 C  CH2 . TRP D  4  133 ? 35.498 6.771   -21.736 1.00 45.55  ? 133 TRP D CH2 1 
ATOM   4435 N  N   . ARG D  4  134 ? 40.858 0.593   -22.306 1.00 57.63  ? 134 ARG D N   1 
ATOM   4436 C  CA  . ARG D  4  134 ? 40.799 -0.866  -22.239 1.00 60.71  ? 134 ARG D CA  1 
ATOM   4437 C  C   . ARG D  4  134 ? 41.010 -1.342  -20.811 1.00 60.66  ? 134 ARG D C   1 
ATOM   4438 O  O   . ARG D  4  134 ? 40.217 -2.110  -20.279 1.00 61.17  ? 134 ARG D O   1 
ATOM   4439 C  CB  . ARG D  4  134 ? 41.854 -1.500  -23.158 1.00 62.63  ? 134 ARG D CB  1 
ATOM   4440 C  CG  . ARG D  4  134 ? 41.407 -1.588  -24.608 1.00 68.64  ? 134 ARG D CG  1 
ATOM   4441 C  CD  . ARG D  4  134 ? 42.565 -1.745  -25.586 1.00 71.44  ? 134 ARG D CD  1 
ATOM   4442 N  NE  . ARG D  4  134 ? 42.132 -1.491  -26.963 1.00 74.85  ? 134 ARG D NE  1 
ATOM   4443 C  CZ  . ARG D  4  134 ? 42.908 -0.978  -27.919 1.00 78.00  ? 134 ARG D CZ  1 
ATOM   4444 N  NH1 . ARG D  4  134 ? 44.178 -0.650  -27.661 1.00 79.94  ? 134 ARG D NH1 1 
ATOM   4445 N  NH2 . ARG D  4  134 ? 42.412 -0.777  -29.139 1.00 77.97  ? 134 ARG D NH2 1 
ATOM   4446 N  N   . ASN D  4  135 ? 42.080 -0.864  -20.195 1.00 61.50  ? 135 ASN D N   1 
ATOM   4447 C  CA  . ASN D  4  135 ? 42.419 -1.236  -18.831 1.00 62.46  ? 135 ASN D CA  1 
ATOM   4448 C  C   . ASN D  4  135 ? 41.311 -0.954  -17.841 1.00 62.51  ? 135 ASN D C   1 
ATOM   4449 O  O   . ASN D  4  135 ? 41.189 -1.660  -16.851 1.00 64.48  ? 135 ASN D O   1 
ATOM   4450 C  CB  . ASN D  4  135 ? 43.683 -0.504  -18.384 1.00 62.37  ? 135 ASN D CB  1 
ATOM   4451 C  CG  . ASN D  4  135 ? 44.892 -0.895  -19.196 1.00 64.05  ? 135 ASN D CG  1 
ATOM   4452 O  OD1 . ASN D  4  135 ? 44.872 -1.892  -19.930 1.00 64.08  ? 135 ASN D OD1 1 
ATOM   4453 N  ND2 . ASN D  4  135 ? 45.963 -0.127  -19.062 1.00 63.21  ? 135 ASN D ND2 1 
ATOM   4454 N  N   . CYS D  4  136 ? 40.508 0.075   -18.097 1.00 61.52  ? 136 CYS D N   1 
ATOM   4455 C  CA  . CYS D  4  136 ? 39.423 0.420   -17.186 1.00 60.24  ? 136 CYS D CA  1 
ATOM   4456 C  C   . CYS D  4  136 ? 38.078 -0.159  -17.580 1.00 60.88  ? 136 CYS D C   1 
ATOM   4457 O  O   . CYS D  4  136 ? 37.280 -0.515  -16.723 1.00 61.25  ? 136 CYS D O   1 
ATOM   4458 C  CB  . CYS D  4  136 ? 39.296 1.934   -17.073 1.00 57.97  ? 136 CYS D CB  1 
ATOM   4459 S  SG  . CYS D  4  136 ? 40.704 2.693   -16.222 1.00 52.85  ? 136 CYS D SG  1 
ATOM   4460 N  N   . LEU D  4  137 ? 37.822 -0.249  -18.870 1.00 62.50  ? 137 LEU D N   1 
ATOM   4461 C  CA  . LEU D  4  137 ? 36.554 -0.784  -19.344 1.00 64.51  ? 137 LEU D CA  1 
ATOM   4462 C  C   . LEU D  4  137 ? 36.414 -2.287  -19.313 1.00 65.69  ? 137 LEU D C   1 
ATOM   4463 O  O   . LEU D  4  137 ? 35.427 -2.817  -18.809 1.00 66.34  ? 137 LEU D O   1 
ATOM   4464 C  CB  . LEU D  4  137 ? 36.295 -0.359  -20.787 1.00 64.60  ? 137 LEU D CB  1 
ATOM   4465 C  CG  . LEU D  4  137 ? 35.823 1.054   -21.050 1.00 64.47  ? 137 LEU D CG  1 
ATOM   4466 C  CD1 . LEU D  4  137 ? 35.163 1.070   -22.433 1.00 64.37  ? 137 LEU D CD1 1 
ATOM   4467 C  CD2 . LEU D  4  137 ? 34.827 1.485   -19.995 1.00 64.02  ? 137 LEU D CD2 1 
ATOM   4468 N  N   . LEU D  4  138 ? 37.394 -2.967  -19.892 1.00 67.57  ? 138 LEU D N   1 
ATOM   4469 C  CA  . LEU D  4  138 ? 37.357 -4.417  -19.938 1.00 69.38  ? 138 LEU D CA  1 
ATOM   4470 C  C   . LEU D  4  138 ? 36.947 -4.991  -18.579 1.00 69.63  ? 138 LEU D C   1 
ATOM   4471 O  O   . LEU D  4  138 ? 36.009 -5.775  -18.489 1.00 69.57  ? 138 LEU D O   1 
ATOM   4472 C  CB  . LEU D  4  138 ? 38.719 -4.957  -20.386 1.00 70.39  ? 138 LEU D CB  1 
ATOM   4473 C  CG  . LEU D  4  138 ? 38.724 -6.343  -21.043 1.00 70.99  ? 138 LEU D CG  1 
ATOM   4474 C  CD1 . LEU D  4  138 ? 37.731 -6.376  -22.196 1.00 71.93  ? 138 LEU D CD1 1 
ATOM   4475 C  CD2 . LEU D  4  138 ? 40.118 -6.657  -21.536 1.00 71.32  ? 138 LEU D CD2 1 
ATOM   4476 N  N   . PRO D  4  139 ? 37.641 -4.597  -17.497 1.00 70.52  ? 139 PRO D N   1 
ATOM   4477 C  CA  . PRO D  4  139 ? 37.280 -5.119  -16.170 1.00 71.55  ? 139 PRO D CA  1 
ATOM   4478 C  C   . PRO D  4  139 ? 35.794 -4.908  -15.896 1.00 71.29  ? 139 PRO D C   1 
ATOM   4479 O  O   . PRO D  4  139 ? 35.097 -5.820  -15.397 1.00 71.09  ? 139 PRO D O   1 
ATOM   4480 C  CB  . PRO D  4  139 ? 38.180 -4.326  -15.227 1.00 71.18  ? 139 PRO D CB  1 
ATOM   4481 C  CG  . PRO D  4  139 ? 39.418 -4.110  -16.100 1.00 72.19  ? 139 PRO D CG  1 
ATOM   4482 C  CD  . PRO D  4  139 ? 38.817 -3.715  -17.420 1.00 70.49  ? 139 PRO D CD  1 
ATOM   4483 N  N   . LEU D  4  140 ? 35.324 -3.696  -16.209 1.00 70.50  ? 140 LEU D N   1 
ATOM   4484 C  CA  . LEU D  4  140 ? 33.917 -3.336  -16.046 1.00 71.20  ? 140 LEU D CA  1 
ATOM   4485 C  C   . LEU D  4  140 ? 33.042 -4.355  -16.784 1.00 72.85  ? 140 LEU D C   1 
ATOM   4486 O  O   . LEU D  4  140 ? 32.104 -4.933  -16.227 1.00 73.94  ? 140 LEU D O   1 
ATOM   4487 C  CB  . LEU D  4  140 ? 33.573 -1.891  -16.607 1.00 69.53  ? 140 LEU D CB  1 
ATOM   4488 C  CG  . LEU D  4  140 ? 33.836 -0.582  -15.992 1.00 70.09  ? 140 LEU D CG  1 
ATOM   4489 C  CD1 . LEU D  4  140 ? 32.787 0.293   -16.698 1.00 69.53  ? 140 LEU D CD1 1 
ATOM   4490 C  CD2 . LEU D  4  140 ? 33.321 -0.698  -14.490 1.00 69.82  ? 140 LEU D CD2 1 
ATOM   4491 N  N   . LYS D  4  141 ? 33.276 -4.408  -18.090 1.00 73.91  ? 141 LYS D N   1 
ATOM   4492 C  CA  . LYS D  4  141 ? 32.506 -5.237  -18.976 1.00 75.56  ? 141 LYS D CA  1 
ATOM   4493 C  C   . LYS D  4  141 ? 32.394 -6.653  -18.468 1.00 77.51  ? 141 LYS D C   1 
ATOM   4494 O  O   . LYS D  4  141 ? 31.311 -7.230  -18.503 1.00 78.79  ? 141 LYS D O   1 
ATOM   4495 C  CB  . LYS D  4  141 ? 33.124 -5.177  -20.376 1.00 75.34  ? 141 LYS D CB  1 
ATOM   4496 C  CG  . LYS D  4  141 ? 32.328 -5.948  -21.436 1.00 75.28  ? 141 LYS D CG  1 
ATOM   4497 C  CD  . LYS D  4  141 ? 32.865 -7.357  -21.613 1.00 75.44  ? 141 LYS D CD  1 
ATOM   4498 C  CE  . LYS D  4  141 ? 34.256 -7.335  -22.228 1.00 75.40  ? 141 LYS D CE  1 
ATOM   4499 N  NZ  . LYS D  4  141 ? 34.809 -8.706  -22.381 1.00 75.02  ? 141 LYS D NZ  1 
ATOM   4500 N  N   . ASN D  4  142 ? 33.504 -7.214  -17.994 1.00 78.29  ? 142 ASN D N   1 
ATOM   4501 C  CA  . ASN D  4  142 ? 33.471 -8.589  -17.504 1.00 79.61  ? 142 ASN D CA  1 
ATOM   4502 C  C   . ASN D  4  142 ? 32.546 -8.721  -16.303 1.00 79.91  ? 142 ASN D C   1 
ATOM   4503 O  O   . ASN D  4  142 ? 31.856 -9.724  -16.139 1.00 79.95  ? 142 ASN D O   1 
ATOM   4504 C  CB  . ASN D  4  142 ? 34.875 -9.075  -17.129 1.00 80.31  ? 142 ASN D CB  1 
ATOM   4505 C  CG  . ASN D  4  142 ? 35.856 -8.954  -18.272 1.00 80.93  ? 142 ASN D CG  1 
ATOM   4506 O  OD1 . ASN D  4  142 ? 35.553 -9.317  -19.410 1.00 81.72  ? 142 ASN D OD1 1 
ATOM   4507 N  ND2 . ASN D  4  142 ? 37.048 -8.443  -17.972 1.00 81.03  ? 142 ASN D ND2 1 
ATOM   4508 N  N   . ALA D  4  143 ? 32.529 -7.693  -15.468 1.00 80.58  ? 143 ALA D N   1 
ATOM   4509 C  CA  . ALA D  4  143 ? 31.683 -7.686  -14.284 1.00 81.29  ? 143 ALA D CA  1 
ATOM   4510 C  C   . ALA D  4  143 ? 30.205 -7.567  -14.649 1.00 83.15  ? 143 ALA D C   1 
ATOM   4511 O  O   . ALA D  4  143 ? 29.349 -8.141  -13.973 1.00 83.48  ? 143 ALA D O   1 
ATOM   4512 C  CB  . ALA D  4  143 ? 32.079 -6.554  -13.379 1.00 80.12  ? 143 ALA D CB  1 
ATOM   4513 N  N   . ILE D  4  144 ? 29.904 -6.825  -15.711 1.00 84.85  ? 144 ILE D N   1 
ATOM   4514 C  CA  . ILE D  4  144 ? 28.519 -6.659  -16.141 1.00 87.10  ? 144 ILE D CA  1 
ATOM   4515 C  C   . ILE D  4  144 ? 28.068 -7.802  -17.046 1.00 90.11  ? 144 ILE D C   1 
ATOM   4516 O  O   . ILE D  4  144 ? 26.874 -7.991  -17.262 1.00 90.51  ? 144 ILE D O   1 
ATOM   4517 C  CB  . ILE D  4  144 ? 28.323 -5.333  -16.898 1.00 85.12  ? 144 ILE D CB  1 
ATOM   4518 C  CG1 . ILE D  4  144 ? 28.817 -4.174  -16.039 1.00 84.25  ? 144 ILE D CG1 1 
ATOM   4519 C  CG2 . ILE D  4  144 ? 26.847 -5.127  -17.223 1.00 83.45  ? 144 ILE D CG2 1 
ATOM   4520 C  CD1 . ILE D  4  144 ? 28.761 -2.832  -16.750 1.00 83.39  ? 144 ILE D CD1 1 
ATOM   4521 N  N   . ALA D  4  145 ? 29.024 -8.567  -17.562 1.00 93.74  ? 145 ALA D N   1 
ATOM   4522 C  CA  . ALA D  4  145 ? 28.708 -9.679  -18.447 1.00 98.19  ? 145 ALA D CA  1 
ATOM   4523 C  C   . ALA D  4  145 ? 29.271 -10.995 -17.929 1.00 101.76 ? 145 ALA D C   1 
ATOM   4524 O  O   . ALA D  4  145 ? 29.512 -11.921 -18.709 1.00 102.70 ? 145 ALA D O   1 
ATOM   4525 C  CB  . ALA D  4  145 ? 29.250 -9.399  -19.843 1.00 97.72  ? 145 ALA D CB  1 
ATOM   4526 N  N   . LYS D  4  146 ? 29.479 -11.080 -16.618 1.00 105.60 ? 146 LYS D N   1 
ATOM   4527 C  CA  . LYS D  4  146 ? 30.020 -12.295 -16.011 1.00 109.56 ? 146 LYS D CA  1 
ATOM   4528 C  C   . LYS D  4  146 ? 28.881 -13.223 -15.622 1.00 111.05 ? 146 LYS D C   1 
ATOM   4529 O  O   . LYS D  4  146 ? 28.080 -12.908 -14.742 1.00 110.84 ? 146 LYS D O   1 
ATOM   4530 C  CB  . LYS D  4  146 ? 30.860 -11.947 -14.776 1.00 111.56 ? 146 LYS D CB  1 
ATOM   4531 C  CG  . LYS D  4  146 ? 32.158 -12.747 -14.663 1.00 114.18 ? 146 LYS D CG  1 
ATOM   4532 C  CD  . LYS D  4  146 ? 33.155 -12.057 -13.733 1.00 115.50 ? 146 LYS D CD  1 
ATOM   4533 C  CE  . LYS D  4  146 ? 34.532 -12.700 -13.818 1.00 115.67 ? 146 LYS D CE  1 
ATOM   4534 N  NZ  . LYS D  4  146 ? 35.530 -11.947 -13.014 1.00 116.34 ? 146 LYS D NZ  1 
ATOM   4535 N  N   . GLY D  4  147 ? 28.812 -14.364 -16.296 1.00 113.02 ? 147 GLY D N   1 
ATOM   4536 C  CA  . GLY D  4  147 ? 27.763 -15.325 -16.021 1.00 115.45 ? 147 GLY D CA  1 
ATOM   4537 C  C   . GLY D  4  147 ? 26.976 -15.691 -17.264 1.00 117.15 ? 147 GLY D C   1 
ATOM   4538 O  O   . GLY D  4  147 ? 26.739 -16.868 -17.531 1.00 117.76 ? 147 GLY D O   1 
ATOM   4539 N  N   . LEU D  4  148 ? 26.578 -14.680 -18.033 1.00 118.50 ? 148 LEU D N   1 
ATOM   4540 C  CA  . LEU D  4  148 ? 25.806 -14.887 -19.255 1.00 120.09 ? 148 LEU D CA  1 
ATOM   4541 C  C   . LEU D  4  148 ? 26.486 -15.799 -20.284 1.00 120.79 ? 148 LEU D C   1 
ATOM   4542 O  O   . LEU D  4  148 ? 27.687 -16.054 -20.194 1.00 120.77 ? 148 LEU D O   1 
ATOM   4543 C  CB  . LEU D  4  148 ? 25.491 -13.529 -19.883 1.00 121.00 ? 148 LEU D CB  1 
ATOM   4544 C  CG  . LEU D  4  148 ? 24.607 -12.629 -19.018 1.00 122.10 ? 148 LEU D CG  1 
ATOM   4545 C  CD1 . LEU D  4  148 ? 24.296 -11.336 -19.760 1.00 122.13 ? 148 LEU D CD1 1 
ATOM   4546 C  CD2 . LEU D  4  148 ? 23.321 -13.372 -18.678 1.00 123.47 ? 148 LEU D CD2 1 
ATOM   4547 N  N   . PRO D  4  149 ? 25.717 -16.305 -21.271 1.00 121.60 ? 149 PRO D N   1 
ATOM   4548 C  CA  . PRO D  4  149 ? 26.172 -17.194 -22.350 1.00 122.17 ? 149 PRO D CA  1 
ATOM   4549 C  C   . PRO D  4  149 ? 27.509 -16.836 -23.009 1.00 122.60 ? 149 PRO D C   1 
ATOM   4550 O  O   . PRO D  4  149 ? 28.232 -15.968 -22.482 1.00 122.96 ? 149 PRO D O   1 
ATOM   4551 C  CB  . PRO D  4  149 ? 25.017 -17.139 -23.342 1.00 122.09 ? 149 PRO D CB  1 
ATOM   4552 C  CG  . PRO D  4  149 ? 23.841 -17.073 -22.442 1.00 121.81 ? 149 PRO D CG  1 
ATOM   4553 C  CD  . PRO D  4  149 ? 24.268 -16.056 -21.397 1.00 121.50 ? 149 PRO D CD  1 
ATOM   4554 O  OXT . PRO D  4  149 ? 27.821 -17.444 -24.053 1.00 123.12 ? 149 PRO D OXT 1 
ATOM   4555 N  N   . ASP E  1  1   ? 5.013  22.707  12.283  1.00 82.61  ? 1   ASP E N   1 
ATOM   4556 C  CA  . ASP E  1  1   ? 4.325  23.389  13.378  1.00 81.23  ? 1   ASP E CA  1 
ATOM   4557 C  C   . ASP E  1  1   ? 5.225  24.440  14.040  1.00 77.81  ? 1   ASP E C   1 
ATOM   4558 O  O   . ASP E  1  1   ? 4.741  25.407  14.632  1.00 76.26  ? 1   ASP E O   1 
ATOM   4559 C  CB  . ASP E  1  1   ? 3.873  22.359  14.424  1.00 84.92  ? 1   ASP E CB  1 
ATOM   4560 C  CG  . ASP E  1  1   ? 3.242  23.003  15.646  1.00 87.81  ? 1   ASP E CG  1 
ATOM   4561 O  OD1 . ASP E  1  1   ? 2.309  23.816  15.469  1.00 91.16  ? 1   ASP E OD1 1 
ATOM   4562 O  OD2 . ASP E  1  1   ? 3.669  22.699  16.781  1.00 88.57  ? 1   ASP E OD2 1 
ATOM   4563 N  N   . CYS E  1  2   ? 6.534  24.232  13.914  1.00 73.81  ? 2   CYS E N   1 
ATOM   4564 C  CA  . CYS E  1  2   ? 7.567  25.094  14.495  1.00 69.10  ? 2   CYS E CA  1 
ATOM   4565 C  C   . CYS E  1  2   ? 7.606  24.980  16.019  1.00 66.78  ? 2   CYS E C   1 
ATOM   4566 O  O   . CYS E  1  2   ? 7.434  25.962  16.743  1.00 64.19  ? 2   CYS E O   1 
ATOM   4567 C  CB  . CYS E  1  2   ? 7.398  26.568  14.072  1.00 66.83  ? 2   CYS E CB  1 
ATOM   4568 S  SG  . CYS E  1  2   ? 8.737  27.649  14.699  1.00 61.67  ? 2   CYS E SG  1 
ATOM   4569 N  N   . ASN E  1  3   ? 7.842  23.755  16.488  1.00 65.89  ? 3   ASN E N   1 
ATOM   4570 C  CA  . ASN E  1  3   ? 7.940  23.464  17.913  1.00 64.63  ? 3   ASN E CA  1 
ATOM   4571 C  C   . ASN E  1  3   ? 9.215  24.112  18.459  1.00 63.94  ? 3   ASN E C   1 
ATOM   4572 O  O   . ASN E  1  3   ? 9.931  24.798  17.730  1.00 65.29  ? 3   ASN E O   1 
ATOM   4573 C  CB  . ASN E  1  3   ? 7.981  21.952  18.129  1.00 63.93  ? 3   ASN E CB  1 
ATOM   4574 C  CG  . ASN E  1  3   ? 9.024  21.272  17.267  1.00 63.00  ? 3   ASN E CG  1 
ATOM   4575 O  OD1 . ASN E  1  3   ? 10.223 21.485  17.440  1.00 61.18  ? 3   ASN E OD1 1 
ATOM   4576 N  ND2 . ASN E  1  3   ? 8.572  20.454  16.331  1.00 60.05  ? 3   ASN E ND2 1 
ATOM   4577 N  N   . ILE E  1  4   ? 9.513  23.889  19.733  1.00 61.75  ? 4   ILE E N   1 
ATOM   4578 C  CA  . ILE E  1  4   ? 10.690 24.501  20.319  1.00 59.13  ? 4   ILE E CA  1 
ATOM   4579 C  C   . ILE E  1  4   ? 12.002 24.035  19.694  1.00 57.79  ? 4   ILE E C   1 
ATOM   4580 O  O   . ILE E  1  4   ? 12.931 24.827  19.552  1.00 57.89  ? 4   ILE E O   1 
ATOM   4581 C  CB  . ILE E  1  4   ? 10.754 24.260  21.833  1.00 59.18  ? 4   ILE E CB  1 
ATOM   4582 C  CG1 . ILE E  1  4   ? 11.973 24.985  22.415  1.00 59.63  ? 4   ILE E CG1 1 
ATOM   4583 C  CG2 . ILE E  1  4   ? 10.825 22.782  22.121  1.00 58.59  ? 4   ILE E CG2 1 
ATOM   4584 C  CD1 . ILE E  1  4   ? 12.092 24.860  23.915  1.00 61.96  ? 4   ILE E CD1 1 
ATOM   4585 N  N   . LEU E  1  5   ? 12.090 22.765  19.319  1.00 55.43  ? 5   LEU E N   1 
ATOM   4586 C  CA  . LEU E  1  5   ? 13.321 22.272  18.728  1.00 53.68  ? 5   LEU E CA  1 
ATOM   4587 C  C   . LEU E  1  5   ? 13.648 22.946  17.390  1.00 54.33  ? 5   LEU E C   1 
ATOM   4588 O  O   . LEU E  1  5   ? 14.793 23.340  17.149  1.00 54.99  ? 5   LEU E O   1 
ATOM   4589 C  CB  . LEU E  1  5   ? 13.257 20.760  18.536  1.00 52.65  ? 5   LEU E CB  1 
ATOM   4590 C  CG  . LEU E  1  5   ? 13.129 19.890  19.782  1.00 52.08  ? 5   LEU E CG  1 
ATOM   4591 C  CD1 . LEU E  1  5   ? 13.306 18.424  19.364  1.00 53.88  ? 5   LEU E CD1 1 
ATOM   4592 C  CD2 . LEU E  1  5   ? 14.167 20.270  20.817  1.00 50.42  ? 5   LEU E CD2 1 
ATOM   4593 N  N   . GLN E  1  6   ? 12.649 23.076  16.524  1.00 52.97  ? 6   GLN E N   1 
ATOM   4594 C  CA  . GLN E  1  6   ? 12.856 23.696  15.228  1.00 53.82  ? 6   GLN E CA  1 
ATOM   4595 C  C   . GLN E  1  6   ? 13.229 25.169  15.398  1.00 55.04  ? 6   GLN E C   1 
ATOM   4596 O  O   . GLN E  1  6   ? 13.975 25.734  14.589  1.00 54.46  ? 6   GLN E O   1 
ATOM   4597 C  CB  . GLN E  1  6   ? 11.588 23.582  14.377  1.00 54.43  ? 6   GLN E CB  1 
ATOM   4598 C  CG  . GLN E  1  6   ? 11.185 22.163  14.002  1.00 52.87  ? 6   GLN E CG  1 
ATOM   4599 C  CD  . GLN E  1  6   ? 9.959  22.137  13.091  1.00 53.79  ? 6   GLN E CD  1 
ATOM   4600 O  OE1 . GLN E  1  6   ? 8.872  22.613  13.460  1.00 51.05  ? 6   GLN E OE1 1 
ATOM   4601 N  NE2 . GLN E  1  6   ? 10.132 21.585  11.891  1.00 52.82  ? 6   GLN E NE2 1 
ATOM   4602 N  N   . ARG E  1  7   ? 12.694 25.791  16.442  1.00 55.61  ? 7   ARG E N   1 
ATOM   4603 C  CA  . ARG E  1  7   ? 12.990 27.187  16.727  1.00 56.15  ? 7   ARG E CA  1 
ATOM   4604 C  C   . ARG E  1  7   ? 14.466 27.320  17.090  1.00 57.15  ? 7   ARG E C   1 
ATOM   4605 O  O   . ARG E  1  7   ? 15.137 28.271  16.674  1.00 58.44  ? 7   ARG E O   1 
ATOM   4606 C  CB  . ARG E  1  7   ? 12.109 27.688  17.871  1.00 55.96  ? 7   ARG E CB  1 
ATOM   4607 C  CG  . ARG E  1  7   ? 10.659 27.764  17.467  1.00 57.04  ? 7   ARG E CG  1 
ATOM   4608 C  CD  . ARG E  1  7   ? 9.737  28.261  18.566  1.00 57.42  ? 7   ARG E CD  1 
ATOM   4609 N  NE  . ARG E  1  7   ? 8.365  28.227  18.065  1.00 57.34  ? 7   ARG E NE  1 
ATOM   4610 C  CZ  . ARG E  1  7   ? 7.515  29.242  18.142  1.00 57.37  ? 7   ARG E CZ  1 
ATOM   4611 N  NH1 . ARG E  1  7   ? 7.893  30.371  18.723  1.00 58.34  ? 7   ARG E NH1 1 
ATOM   4612 N  NH2 . ARG E  1  7   ? 6.306  29.140  17.597  1.00 57.58  ? 7   ARG E NH2 1 
ATOM   4613 N  N   . LEU E  1  8   ? 14.973 26.360  17.856  1.00 56.48  ? 8   LEU E N   1 
ATOM   4614 C  CA  . LEU E  1  8   ? 16.369 26.377  18.258  1.00 55.97  ? 8   LEU E CA  1 
ATOM   4615 C  C   . LEU E  1  8   ? 17.270 26.139  17.051  1.00 55.06  ? 8   LEU E C   1 
ATOM   4616 O  O   . LEU E  1  8   ? 18.302 26.791  16.903  1.00 54.79  ? 8   LEU E O   1 
ATOM   4617 C  CB  . LEU E  1  8   ? 16.628 25.311  19.326  1.00 56.85  ? 8   LEU E CB  1 
ATOM   4618 C  CG  . LEU E  1  8   ? 15.968 25.599  20.676  1.00 59.66  ? 8   LEU E CG  1 
ATOM   4619 C  CD1 . LEU E  1  8   ? 16.294 24.461  21.619  1.00 61.83  ? 8   LEU E CD1 1 
ATOM   4620 C  CD2 . LEU E  1  8   ? 16.461 26.923  21.262  1.00 59.07  ? 8   LEU E CD2 1 
ATOM   4621 N  N   . LYS E  1  9   ? 16.867 25.206  16.198  1.00 53.73  ? 9   LYS E N   1 
ATOM   4622 C  CA  . LYS E  1  9   ? 17.606 24.852  14.991  1.00 51.64  ? 9   LYS E CA  1 
ATOM   4623 C  C   . LYS E  1  9   ? 17.708 26.115  14.124  1.00 50.44  ? 9   LYS E C   1 
ATOM   4624 O  O   . LYS E  1  9   ? 18.803 26.518  13.728  1.00 47.92  ? 9   LYS E O   1 
ATOM   4625 C  CB  . LYS E  1  9   ? 16.844 23.730  14.264  1.00 51.16  ? 9   LYS E CB  1 
ATOM   4626 C  CG  . LYS E  1  9   ? 17.443 23.186  12.973  1.00 48.52  ? 9   LYS E CG  1 
ATOM   4627 C  CD  . LYS E  1  9   ? 18.650 22.298  13.205  1.00 47.71  ? 9   LYS E CD  1 
ATOM   4628 C  CE  . LYS E  1  9   ? 18.824 21.276  12.070  1.00 45.12  ? 9   LYS E CE  1 
ATOM   4629 N  NZ  . LYS E  1  9   ? 17.771 20.232  12.145  1.00 44.68  ? 9   LYS E NZ  1 
ATOM   4630 N  N   . VAL E  1  10  ? 16.566 26.751  13.863  1.00 48.65  ? 10  VAL E N   1 
ATOM   4631 C  CA  . VAL E  1  10  ? 16.522 27.962  13.046  1.00 47.30  ? 10  VAL E CA  1 
ATOM   4632 C  C   . VAL E  1  10  ? 17.352 29.131  13.616  1.00 47.64  ? 10  VAL E C   1 
ATOM   4633 O  O   . VAL E  1  10  ? 17.978 29.881  12.853  1.00 46.74  ? 10  VAL E O   1 
ATOM   4634 C  CB  . VAL E  1  10  ? 15.040 28.410  12.810  1.00 46.85  ? 10  VAL E CB  1 
ATOM   4635 C  CG1 . VAL E  1  10  ? 14.979 29.793  12.165  1.00 43.91  ? 10  VAL E CG1 1 
ATOM   4636 C  CG2 . VAL E  1  10  ? 14.344 27.400  11.899  1.00 44.88  ? 10  VAL E CG2 1 
ATOM   4637 N  N   . LYS E  1  11  ? 17.368 29.287  14.941  1.00 46.04  ? 11  LYS E N   1 
ATOM   4638 C  CA  . LYS E  1  11  ? 18.147 30.361  15.566  1.00 46.06  ? 11  LYS E CA  1 
ATOM   4639 C  C   . LYS E  1  11  ? 19.641 30.146  15.318  1.00 46.02  ? 11  LYS E C   1 
ATOM   4640 O  O   . LYS E  1  11  ? 20.389 31.095  15.052  1.00 44.23  ? 11  LYS E O   1 
ATOM   4641 C  CB  . LYS E  1  11  ? 17.895 30.406  17.073  1.00 46.77  ? 11  LYS E CB  1 
ATOM   4642 C  CG  . LYS E  1  11  ? 16.604 31.085  17.462  1.00 48.91  ? 11  LYS E CG  1 
ATOM   4643 C  CD  . LYS E  1  11  ? 16.138 30.664  18.844  1.00 47.34  ? 11  LYS E CD  1 
ATOM   4644 C  CE  . LYS E  1  11  ? 17.096 31.131  19.920  1.00 46.71  ? 11  LYS E CE  1 
ATOM   4645 N  NZ  . LYS E  1  11  ? 17.120 32.614  20.063  1.00 45.38  ? 11  LYS E NZ  1 
ATOM   4646 N  N   . MET E  1  12  ? 20.052 28.886  15.419  1.00 46.75  ? 12  MET E N   1 
ATOM   4647 C  CA  . MET E  1  12  ? 21.429 28.468  15.231  1.00 45.74  ? 12  MET E CA  1 
ATOM   4648 C  C   . MET E  1  12  ? 21.837 28.713  13.770  1.00 43.78  ? 12  MET E C   1 
ATOM   4649 O  O   . MET E  1  12  ? 22.843 29.367  13.517  1.00 41.51  ? 12  MET E O   1 
ATOM   4650 C  CB  . MET E  1  12  ? 21.554 26.972  15.571  1.00 50.96  ? 12  MET E CB  1 
ATOM   4651 C  CG  . MET E  1  12  ? 22.914 26.504  16.096  1.00 58.01  ? 12  MET E CG  1 
ATOM   4652 S  SD  . MET E  1  12  ? 23.202 26.946  17.812  1.00 66.36  ? 12  MET E SD  1 
ATOM   4653 C  CE  . MET E  1  12  ? 23.665 28.778  17.636  1.00 66.00  ? 12  MET E CE  1 
ATOM   4654 N  N   . GLN E  1  13  ? 21.041 28.215  12.819  1.00 40.56  ? 13  GLN E N   1 
ATOM   4655 C  CA  . GLN E  1  13  ? 21.358 28.372  11.404  1.00 38.45  ? 13  GLN E CA  1 
ATOM   4656 C  C   . GLN E  1  13  ? 21.335 29.831  10.934  1.00 36.93  ? 13  GLN E C   1 
ATOM   4657 O  O   . GLN E  1  13  ? 22.140 30.242  10.086  1.00 34.02  ? 13  GLN E O   1 
ATOM   4658 C  CB  . GLN E  1  13  ? 20.425 27.515  10.550  1.00 36.62  ? 13  GLN E CB  1 
ATOM   4659 C  CG  . GLN E  1  13  ? 20.444 26.023  10.915  1.00 33.63  ? 13  GLN E CG  1 
ATOM   4660 C  CD  . GLN E  1  13  ? 19.878 25.140  9.810   1.00 34.64  ? 13  GLN E CD  1 
ATOM   4661 O  OE1 . GLN E  1  13  ? 19.005 25.549  9.045   1.00 34.22  ? 13  GLN E OE1 1 
ATOM   4662 N  NE2 . GLN E  1  13  ? 20.373 23.920  9.727   1.00 36.52  ? 13  GLN E NE2 1 
ATOM   4663 N  N   . TRP E  1  14  ? 20.427 30.616  11.488  1.00 35.55  ? 14  TRP E N   1 
ATOM   4664 C  CA  . TRP E  1  14  ? 20.371 32.017  11.118  1.00 35.64  ? 14  TRP E CA  1 
ATOM   4665 C  C   . TRP E  1  14  ? 21.650 32.733  11.559  1.00 36.28  ? 14  TRP E C   1 
ATOM   4666 O  O   . TRP E  1  14  ? 22.250 33.461  10.772  1.00 34.32  ? 14  TRP E O   1 
ATOM   4667 C  CB  . TRP E  1  14  ? 19.173 32.691  11.765  1.00 35.12  ? 14  TRP E CB  1 
ATOM   4668 C  CG  . TRP E  1  14  ? 19.313 34.180  11.837  1.00 34.05  ? 14  TRP E CG  1 
ATOM   4669 C  CD1 . TRP E  1  14  ? 19.658 34.919  12.933  1.00 33.45  ? 14  TRP E CD1 1 
ATOM   4670 C  CD2 . TRP E  1  14  ? 19.050 35.112  10.787  1.00 32.70  ? 14  TRP E CD2 1 
ATOM   4671 N  NE1 . TRP E  1  14  ? 19.608 36.264  12.632  1.00 34.13  ? 14  TRP E NE1 1 
ATOM   4672 C  CE2 . TRP E  1  14  ? 19.236 36.405  11.318  1.00 33.83  ? 14  TRP E CE2 1 
ATOM   4673 C  CE3 . TRP E  1  14  ? 18.669 34.978  9.446   1.00 32.99  ? 14  TRP E CE3 1 
ATOM   4674 C  CZ2 . TRP E  1  14  ? 19.051 37.562  10.552  1.00 34.76  ? 14  TRP E CZ2 1 
ATOM   4675 C  CZ3 . TRP E  1  14  ? 18.486 36.120  8.689   1.00 33.98  ? 14  TRP E CZ3 1 
ATOM   4676 C  CH2 . TRP E  1  14  ? 18.678 37.398  9.243   1.00 34.94  ? 14  TRP E CH2 1 
ATOM   4677 N  N   . ALA E  1  15  ? 22.045 32.519  12.821  1.00 36.87  ? 15  ALA E N   1 
ATOM   4678 C  CA  . ALA E  1  15  ? 23.236 33.144  13.383  1.00 39.83  ? 15  ALA E CA  1 
ATOM   4679 C  C   . ALA E  1  15  ? 24.463 32.890  12.527  1.00 41.93  ? 15  ALA E C   1 
ATOM   4680 O  O   . ALA E  1  15  ? 25.220 33.814  12.242  1.00 41.02  ? 15  ALA E O   1 
ATOM   4681 C  CB  . ALA E  1  15  ? 23.482 32.646  14.785  1.00 39.54  ? 15  ALA E CB  1 
ATOM   4682 N  N   . LYS E  1  16  ? 24.659 31.639  12.120  1.00 45.01  ? 16  LYS E N   1 
ATOM   4683 C  CA  . LYS E  1  16  ? 25.799 31.289  11.292  1.00 48.83  ? 16  LYS E CA  1 
ATOM   4684 C  C   . LYS E  1  16  ? 25.694 31.965  9.914   1.00 49.96  ? 16  LYS E C   1 
ATOM   4685 O  O   . LYS E  1  16  ? 26.667 32.535  9.411   1.00 48.93  ? 16  LYS E O   1 
ATOM   4686 C  CB  . LYS E  1  16  ? 25.876 29.769  11.119  1.00 51.24  ? 16  LYS E CB  1 
ATOM   4687 C  CG  . LYS E  1  16  ? 27.293 29.201  11.143  1.00 54.04  ? 16  LYS E CG  1 
ATOM   4688 C  CD  . LYS E  1  16  ? 28.108 29.638  9.950   1.00 56.73  ? 16  LYS E CD  1 
ATOM   4689 C  CE  . LYS E  1  16  ? 29.551 29.155  10.047  1.00 58.66  ? 16  LYS E CE  1 
ATOM   4690 N  NZ  . LYS E  1  16  ? 30.314 29.755  11.183  1.00 61.01  ? 16  LYS E NZ  1 
ATOM   4691 N  N   . ALA E  1  17  ? 24.507 31.930  9.321   1.00 50.88  ? 17  ALA E N   1 
ATOM   4692 C  CA  . ALA E  1  17  ? 24.331 32.515  8.003   1.00 52.71  ? 17  ALA E CA  1 
ATOM   4693 C  C   . ALA E  1  17  ? 24.321 34.034  7.956   1.00 54.54  ? 17  ALA E C   1 
ATOM   4694 O  O   . ALA E  1  17  ? 24.677 34.622  6.936   1.00 54.65  ? 17  ALA E O   1 
ATOM   4695 C  CB  . ALA E  1  17  ? 23.073 31.986  7.372   1.00 53.49  ? 17  ALA E CB  1 
ATOM   4696 N  N   . TYR E  1  18  ? 23.921 34.666  9.056   1.00 55.94  ? 18  TYR E N   1 
ATOM   4697 C  CA  . TYR E  1  18  ? 23.835 36.118  9.137   1.00 56.47  ? 18  TYR E CA  1 
ATOM   4698 C  C   . TYR E  1  18  ? 25.211 36.760  9.304   1.00 58.87  ? 18  TYR E C   1 
ATOM   4699 O  O   . TYR E  1  18  ? 25.521 37.783  8.693   1.00 59.42  ? 18  TYR E O   1 
ATOM   4700 C  CB  . TYR E  1  18  ? 22.909 36.479  10.293  1.00 55.48  ? 18  TYR E CB  1 
ATOM   4701 C  CG  . TYR E  1  18  ? 22.626 37.946  10.469  1.00 55.02  ? 18  TYR E CG  1 
ATOM   4702 C  CD1 . TYR E  1  18  ? 22.211 38.743  9.399   1.00 55.90  ? 18  TYR E CD1 1 
ATOM   4703 C  CD2 . TYR E  1  18  ? 22.727 38.531  11.720  1.00 54.78  ? 18  TYR E CD2 1 
ATOM   4704 C  CE1 . TYR E  1  18  ? 21.903 40.102  9.586   1.00 55.44  ? 18  TYR E CE1 1 
ATOM   4705 C  CE2 . TYR E  1  18  ? 22.427 39.865  11.919  1.00 54.35  ? 18  TYR E CE2 1 
ATOM   4706 C  CZ  . TYR E  1  18  ? 22.016 40.654  10.861  1.00 55.45  ? 18  TYR E CZ  1 
ATOM   4707 O  OH  . TYR E  1  18  ? 21.745 41.988  11.094  1.00 56.29  ? 18  TYR E OH  1 
ATOM   4708 N  N   . GLY E  1  19  ? 26.036 36.156  10.145  1.00 61.46  ? 19  GLY E N   1 
ATOM   4709 C  CA  . GLY E  1  19  ? 27.380 36.660  10.334  1.00 65.28  ? 19  GLY E CA  1 
ATOM   4710 C  C   . GLY E  1  19  ? 27.582 37.983  11.039  1.00 67.81  ? 19  GLY E C   1 
ATOM   4711 O  O   . GLY E  1  19  ? 26.662 38.548  11.638  1.00 67.58  ? 19  GLY E O   1 
ATOM   4712 N  N   . PHE E  1  20  ? 28.817 38.470  10.947  1.00 70.58  ? 20  PHE E N   1 
ATOM   4713 C  CA  . PHE E  1  20  ? 29.235 39.714  11.583  1.00 72.63  ? 20  PHE E CA  1 
ATOM   4714 C  C   . PHE E  1  20  ? 29.619 40.752  10.550  1.00 71.68  ? 20  PHE E C   1 
ATOM   4715 O  O   . PHE E  1  20  ? 29.791 40.439  9.377   1.00 71.81  ? 20  PHE E O   1 
ATOM   4716 C  CB  . PHE E  1  20  ? 30.444 39.463  12.486  1.00 74.31  ? 20  PHE E CB  1 
ATOM   4717 C  CG  . PHE E  1  20  ? 30.150 38.594  13.671  1.00 77.41  ? 20  PHE E CG  1 
ATOM   4718 C  CD1 . PHE E  1  20  ? 29.733 39.159  14.873  1.00 79.13  ? 20  PHE E CD1 1 
ATOM   4719 C  CD2 . PHE E  1  20  ? 30.307 37.211  13.597  1.00 78.85  ? 20  PHE E CD2 1 
ATOM   4720 C  CE1 . PHE E  1  20  ? 29.480 38.362  15.985  1.00 80.86  ? 20  PHE E CE1 1 
ATOM   4721 C  CE2 . PHE E  1  20  ? 30.054 36.402  14.705  1.00 80.56  ? 20  PHE E CE2 1 
ATOM   4722 C  CZ  . PHE E  1  20  ? 29.640 36.981  15.902  1.00 80.91  ? 20  PHE E CZ  1 
ATOM   4723 N  N   . GLY E  1  21  ? 29.749 41.988  11.010  1.00 70.84  ? 21  GLY E N   1 
ATOM   4724 C  CA  . GLY E  1  21  ? 30.149 43.077  10.146  1.00 69.81  ? 21  GLY E CA  1 
ATOM   4725 C  C   . GLY E  1  21  ? 29.430 43.262  8.822   1.00 69.64  ? 21  GLY E C   1 
ATOM   4726 O  O   . GLY E  1  21  ? 28.209 43.149  8.732   1.00 69.70  ? 21  GLY E O   1 
ATOM   4727 N  N   . THR E  1  22  ? 30.209 43.561  7.781   1.00 68.66  ? 22  THR E N   1 
ATOM   4728 C  CA  . THR E  1  22  ? 29.661 43.805  6.456   1.00 66.33  ? 22  THR E CA  1 
ATOM   4729 C  C   . THR E  1  22  ? 29.067 42.575  5.794   1.00 66.42  ? 22  THR E C   1 
ATOM   4730 O  O   . THR E  1  22  ? 28.355 42.704  4.790   1.00 66.73  ? 22  THR E O   1 
ATOM   4731 C  CB  . THR E  1  22  ? 30.722 44.416  5.504   1.00 65.25  ? 22  THR E CB  1 
ATOM   4732 O  OG1 . THR E  1  22  ? 31.714 43.437  5.171   1.00 62.32  ? 22  THR E OG1 1 
ATOM   4733 C  CG2 . THR E  1  22  ? 31.395 45.603  6.166   1.00 64.02  ? 22  THR E CG2 1 
ATOM   4734 N  N   . GLU E  1  23  ? 29.360 41.387  6.333   1.00 64.45  ? 23  GLU E N   1 
ATOM   4735 C  CA  . GLU E  1  23  ? 28.804 40.167  5.763   1.00 63.33  ? 23  GLU E CA  1 
ATOM   4736 C  C   . GLU E  1  23  ? 27.277 40.255  5.869   1.00 61.36  ? 23  GLU E C   1 
ATOM   4737 O  O   . GLU E  1  23  ? 26.563 39.608  5.106   1.00 61.91  ? 23  GLU E O   1 
ATOM   4738 C  CB  . GLU E  1  23  ? 29.271 38.927  6.524   1.00 65.73  ? 23  GLU E CB  1 
ATOM   4739 C  CG  . GLU E  1  23  ? 30.758 38.716  6.627   1.00 69.84  ? 23  GLU E CG  1 
ATOM   4740 C  CD  . GLU E  1  23  ? 31.102 37.747  7.766   1.00 73.33  ? 23  GLU E CD  1 
ATOM   4741 O  OE1 . GLU E  1  23  ? 32.298 37.429  7.952   1.00 74.07  ? 23  GLU E OE1 1 
ATOM   4742 O  OE2 . GLU E  1  23  ? 30.176 37.303  8.489   1.00 71.83  ? 23  GLU E OE2 1 
ATOM   4743 N  N   . ARG E  1  24  ? 26.781 41.046  6.819   1.00 58.33  ? 24  ARG E N   1 
ATOM   4744 C  CA  . ARG E  1  24  ? 25.337 41.211  7.001   1.00 56.60  ? 24  ARG E CA  1 
ATOM   4745 C  C   . ARG E  1  24  ? 24.737 42.029  5.877   1.00 54.82  ? 24  ARG E C   1 
ATOM   4746 O  O   . ARG E  1  24  ? 23.604 41.786  5.450   1.00 54.44  ? 24  ARG E O   1 
ATOM   4747 C  CB  . ARG E  1  24  ? 25.023 41.927  8.311   1.00 57.37  ? 24  ARG E CB  1 
ATOM   4748 C  CG  . ARG E  1  24  ? 25.441 41.191  9.558   1.00 59.80  ? 24  ARG E CG  1 
ATOM   4749 C  CD  . ARG E  1  24  ? 25.143 42.058  10.748  1.00 61.32  ? 24  ARG E CD  1 
ATOM   4750 N  NE  . ARG E  1  24  ? 25.701 41.530  11.985  1.00 64.59  ? 24  ARG E NE  1 
ATOM   4751 C  CZ  . ARG E  1  24  ? 25.751 42.231  13.114  1.00 65.95  ? 24  ARG E CZ  1 
ATOM   4752 N  NH1 . ARG E  1  24  ? 25.283 43.474  13.134  1.00 66.79  ? 24  ARG E NH1 1 
ATOM   4753 N  NH2 . ARG E  1  24  ? 26.250 41.697  14.221  1.00 66.76  ? 24  ARG E NH2 1 
ATOM   4754 N  N   . ALA E  1  25  ? 25.483 43.027  5.423   1.00 52.50  ? 25  ALA E N   1 
ATOM   4755 C  CA  . ALA E  1  25  ? 25.003 43.869  4.336   1.00 52.20  ? 25  ALA E CA  1 
ATOM   4756 C  C   . ALA E  1  25  ? 24.908 43.006  3.067   1.00 51.56  ? 25  ALA E C   1 
ATOM   4757 O  O   . ALA E  1  25  ? 23.960 43.105  2.293   1.00 50.11  ? 25  ALA E O   1 
ATOM   4758 C  CB  . ALA E  1  25  ? 25.962 45.036  4.128   1.00 50.71  ? 25  ALA E CB  1 
ATOM   4759 N  N   . LYS E  1  26  ? 25.902 42.139  2.892   1.00 51.40  ? 26  LYS E N   1 
ATOM   4760 C  CA  . LYS E  1  26  ? 25.981 41.257  1.744   1.00 51.79  ? 26  LYS E CA  1 
ATOM   4761 C  C   . LYS E  1  26  ? 24.819 40.286  1.778   1.00 51.39  ? 26  LYS E C   1 
ATOM   4762 O  O   . LYS E  1  26  ? 24.199 39.981  0.743   1.00 51.24  ? 26  LYS E O   1 
ATOM   4763 C  CB  . LYS E  1  26  ? 27.292 40.477  1.779   1.00 54.19  ? 26  LYS E CB  1 
ATOM   4764 C  CG  . LYS E  1  26  ? 27.528 39.638  0.553   1.00 59.52  ? 26  LYS E CG  1 
ATOM   4765 C  CD  . LYS E  1  26  ? 28.932 39.043  0.521   1.00 65.98  ? 26  LYS E CD  1 
ATOM   4766 C  CE  . LYS E  1  26  ? 29.205 38.396  -0.842  1.00 70.09  ? 26  LYS E CE  1 
ATOM   4767 N  NZ  . LYS E  1  26  ? 30.593 37.881  -0.990  1.00 75.18  ? 26  LYS E NZ  1 
ATOM   4768 N  N   . PHE E  1  27  ? 24.536 39.788  2.976   1.00 47.77  ? 27  PHE E N   1 
ATOM   4769 C  CA  . PHE E  1  27  ? 23.453 38.849  3.164   1.00 45.34  ? 27  PHE E CA  1 
ATOM   4770 C  C   . PHE E  1  27  ? 22.141 39.520  2.788   1.00 45.48  ? 27  PHE E C   1 
ATOM   4771 O  O   . PHE E  1  27  ? 21.318 38.948  2.071   1.00 46.49  ? 27  PHE E O   1 
ATOM   4772 C  CB  . PHE E  1  27  ? 23.416 38.371  4.621   1.00 43.93  ? 27  PHE E CB  1 
ATOM   4773 C  CG  . PHE E  1  27  ? 22.223 37.533  4.945   1.00 43.36  ? 27  PHE E CG  1 
ATOM   4774 C  CD1 . PHE E  1  27  ? 20.994 38.127  5.206   1.00 43.14  ? 27  PHE E CD1 1 
ATOM   4775 C  CD2 . PHE E  1  27  ? 22.305 36.142  4.939   1.00 43.68  ? 27  PHE E CD2 1 
ATOM   4776 C  CE1 . PHE E  1  27  ? 19.852 37.340  5.454   1.00 45.57  ? 27  PHE E CE1 1 
ATOM   4777 C  CE2 . PHE E  1  27  ? 21.181 35.348  5.186   1.00 41.86  ? 27  PHE E CE2 1 
ATOM   4778 C  CZ  . PHE E  1  27  ? 19.954 35.949  5.443   1.00 42.49  ? 27  PHE E CZ  1 
ATOM   4779 N  N   . GLY E  1  28  ? 21.963 40.744  3.259   1.00 43.66  ? 28  GLY E N   1 
ATOM   4780 C  CA  . GLY E  1  28  ? 20.744 41.465  2.974   1.00 44.56  ? 28  GLY E CA  1 
ATOM   4781 C  C   . GLY E  1  28  ? 20.567 41.793  1.510   1.00 44.24  ? 28  GLY E C   1 
ATOM   4782 O  O   . GLY E  1  28  ? 19.467 41.665  0.963   1.00 44.50  ? 28  GLY E O   1 
ATOM   4783 N  N   . ASN E  1  29  ? 21.641 42.235  0.868   1.00 43.91  ? 29  ASN E N   1 
ATOM   4784 C  CA  . ASN E  1  29  ? 21.565 42.567  -0.536  1.00 41.79  ? 29  ASN E CA  1 
ATOM   4785 C  C   . ASN E  1  29  ? 21.196 41.313  -1.323  1.00 39.24  ? 29  ASN E C   1 
ATOM   4786 O  O   . ASN E  1  29  ? 20.430 41.390  -2.281  1.00 39.73  ? 29  ASN E O   1 
ATOM   4787 C  CB  . ASN E  1  29  ? 22.891 43.152  -1.018  1.00 43.72  ? 29  ASN E CB  1 
ATOM   4788 C  CG  . ASN E  1  29  ? 22.954 43.285  -2.538  1.00 47.80  ? 29  ASN E CG  1 
ATOM   4789 O  OD1 . ASN E  1  29  ? 23.296 42.333  -3.246  1.00 51.00  ? 29  ASN E OD1 1 
ATOM   4790 N  ND2 . ASN E  1  29  ? 22.613 44.463  -3.043  1.00 48.78  ? 29  ASN E ND2 1 
ATOM   4791 N  N   . SER E  1  30  ? 21.724 40.162  -0.925  1.00 36.51  ? 30  SER E N   1 
ATOM   4792 C  CA  . SER E  1  30  ? 21.413 38.921  -1.629  1.00 37.06  ? 30  SER E CA  1 
ATOM   4793 C  C   . SER E  1  30  ? 19.932 38.588  -1.463  1.00 38.97  ? 30  SER E C   1 
ATOM   4794 O  O   . SER E  1  30  ? 19.235 38.241  -2.430  1.00 39.31  ? 30  SER E O   1 
ATOM   4795 C  CB  . SER E  1  30  ? 22.251 37.755  -1.091  1.00 37.47  ? 30  SER E CB  1 
ATOM   4796 O  OG  . SER E  1  30  ? 23.556 37.708  -1.650  1.00 38.00  ? 30  SER E OG  1 
ATOM   4797 N  N   . LEU E  1  31  ? 19.457 38.697  -0.223  1.00 37.66  ? 31  LEU E N   1 
ATOM   4798 C  CA  . LEU E  1  31  ? 18.074 38.427  0.081   1.00 37.54  ? 31  LEU E CA  1 
ATOM   4799 C  C   . LEU E  1  31  ? 17.165 39.276  -0.778  1.00 37.90  ? 31  LEU E C   1 
ATOM   4800 O  O   . LEU E  1  31  ? 16.181 38.770  -1.329  1.00 37.74  ? 31  LEU E O   1 
ATOM   4801 C  CB  . LEU E  1  31  ? 17.783 38.711  1.556   1.00 38.33  ? 31  LEU E CB  1 
ATOM   4802 C  CG  . LEU E  1  31  ? 16.282 38.744  1.855   1.00 39.28  ? 31  LEU E CG  1 
ATOM   4803 C  CD1 . LEU E  1  31  ? 15.693 37.353  1.581   1.00 37.61  ? 31  LEU E CD1 1 
ATOM   4804 C  CD2 . LEU E  1  31  ? 16.048 39.167  3.289   1.00 40.18  ? 31  LEU E CD2 1 
ATOM   4805 N  N   . TRP E  1  32  ? 17.474 40.566  -0.898  1.00 36.61  ? 32  TRP E N   1 
ATOM   4806 C  CA  . TRP E  1  32  ? 16.612 41.420  -1.702  1.00 38.42  ? 32  TRP E CA  1 
ATOM   4807 C  C   . TRP E  1  32  ? 16.807 41.306  -3.220  1.00 39.45  ? 32  TRP E C   1 
ATOM   4808 O  O   . TRP E  1  32  ? 15.896 41.619  -3.986  1.00 38.86  ? 32  TRP E O   1 
ATOM   4809 C  CB  . TRP E  1  32  ? 16.692 42.877  -1.223  1.00 36.48  ? 32  TRP E CB  1 
ATOM   4810 C  CG  . TRP E  1  32  ? 15.905 43.053  0.043   1.00 35.24  ? 32  TRP E CG  1 
ATOM   4811 C  CD1 . TRP E  1  32  ? 16.382 43.015  1.324   1.00 36.99  ? 32  TRP E CD1 1 
ATOM   4812 C  CD2 . TRP E  1  32  ? 14.488 43.232  0.150   1.00 32.44  ? 32  TRP E CD2 1 
ATOM   4813 N  NE1 . TRP E  1  32  ? 15.349 43.167  2.226   1.00 34.86  ? 32  TRP E NE1 1 
ATOM   4814 C  CE2 . TRP E  1  32  ? 14.177 43.302  1.531   1.00 34.05  ? 32  TRP E CE2 1 
ATOM   4815 C  CE3 . TRP E  1  32  ? 13.451 43.340  -0.779  1.00 33.75  ? 32  TRP E CE3 1 
ATOM   4816 C  CZ2 . TRP E  1  32  ? 12.870 43.479  1.999   1.00 34.13  ? 32  TRP E CZ2 1 
ATOM   4817 C  CZ3 . TRP E  1  32  ? 12.146 43.513  -0.315  1.00 35.46  ? 32  TRP E CZ3 1 
ATOM   4818 C  CH2 . TRP E  1  32  ? 11.871 43.581  1.064   1.00 33.37  ? 32  TRP E CH2 1 
ATOM   4819 N  N   . THR E  1  33  ? 17.970 40.843  -3.659  1.00 40.02  ? 33  THR E N   1 
ATOM   4820 C  CA  . THR E  1  33  ? 18.169 40.670  -5.092  1.00 42.60  ? 33  THR E CA  1 
ATOM   4821 C  C   . THR E  1  33  ? 17.321 39.465  -5.486  1.00 44.88  ? 33  THR E C   1 
ATOM   4822 O  O   . THR E  1  33  ? 16.715 39.432  -6.566  1.00 45.12  ? 33  THR E O   1 
ATOM   4823 C  CB  . THR E  1  33  ? 19.618 40.344  -5.450  1.00 42.51  ? 33  THR E CB  1 
ATOM   4824 O  OG1 . THR E  1  33  ? 20.475 41.399  -5.007  1.00 44.49  ? 33  THR E OG1 1 
ATOM   4825 C  CG2 . THR E  1  33  ? 19.756 40.197  -6.934  1.00 40.74  ? 33  THR E CG2 1 
ATOM   4826 N  N   . SER E  1  34  ? 17.289 38.466  -4.605  1.00 45.65  ? 34  SER E N   1 
ATOM   4827 C  CA  . SER E  1  34  ? 16.502 37.273  -4.873  1.00 46.95  ? 34  SER E CA  1 
ATOM   4828 C  C   . SER E  1  34  ? 14.996 37.579  -4.854  1.00 47.36  ? 34  SER E C   1 
ATOM   4829 O  O   . SER E  1  34  ? 14.245 37.105  -5.718  1.00 46.90  ? 34  SER E O   1 
ATOM   4830 C  CB  . SER E  1  34  ? 16.837 36.160  -3.871  1.00 47.10  ? 34  SER E CB  1 
ATOM   4831 O  OG  . SER E  1  34  ? 18.026 35.476  -4.238  1.00 45.29  ? 34  SER E OG  1 
ATOM   4832 N  N   . ILE E  1  35  ? 14.549 38.367  -3.876  1.00 46.04  ? 35  ILE E N   1 
ATOM   4833 C  CA  . ILE E  1  35  ? 13.134 38.711  -3.821  1.00 44.62  ? 35  ILE E CA  1 
ATOM   4834 C  C   . ILE E  1  35  ? 12.704 39.389  -5.137  1.00 45.50  ? 35  ILE E C   1 
ATOM   4835 O  O   . ILE E  1  35  ? 11.675 39.033  -5.704  1.00 43.14  ? 35  ILE E O   1 
ATOM   4836 C  CB  . ILE E  1  35  ? 12.793 39.659  -2.632  1.00 41.50  ? 35  ILE E CB  1 
ATOM   4837 C  CG1 . ILE E  1  35  ? 13.014 38.954  -1.289  1.00 40.58  ? 35  ILE E CG1 1 
ATOM   4838 C  CG2 . ILE E  1  35  ? 11.359 40.094  -2.721  1.00 39.09  ? 35  ILE E CG2 1 
ATOM   4839 C  CD1 . ILE E  1  35  ? 12.708 39.824  -0.041  1.00 35.73  ? 35  ILE E CD1 1 
ATOM   4840 N  N   . PHE E  1  36  ? 13.490 40.341  -5.643  1.00 46.43  ? 36  PHE E N   1 
ATOM   4841 C  CA  . PHE E  1  36  ? 13.095 41.028  -6.869  1.00 48.67  ? 36  PHE E CA  1 
ATOM   4842 C  C   . PHE E  1  36  ? 13.319 40.201  -8.135  1.00 50.02  ? 36  PHE E C   1 
ATOM   4843 O  O   . PHE E  1  36  ? 12.824 40.559  -9.209  1.00 50.49  ? 36  PHE E O   1 
ATOM   4844 C  CB  . PHE E  1  36  ? 13.781 42.406  -6.988  1.00 47.40  ? 36  PHE E CB  1 
ATOM   4845 C  CG  . PHE E  1  36  ? 13.431 43.371  -5.874  1.00 47.07  ? 36  PHE E CG  1 
ATOM   4846 C  CD1 . PHE E  1  36  ? 12.171 43.356  -5.280  1.00 47.98  ? 36  PHE E CD1 1 
ATOM   4847 C  CD2 . PHE E  1  36  ? 14.369 44.299  -5.420  1.00 48.17  ? 36  PHE E CD2 1 
ATOM   4848 C  CE1 . PHE E  1  36  ? 11.856 44.248  -4.244  1.00 48.26  ? 36  PHE E CE1 1 
ATOM   4849 C  CE2 . PHE E  1  36  ? 14.063 45.195  -4.390  1.00 47.80  ? 36  PHE E CE2 1 
ATOM   4850 C  CZ  . PHE E  1  36  ? 12.804 45.166  -3.801  1.00 48.53  ? 36  PHE E CZ  1 
ATOM   4851 N  N   . ASN E  1  37  ? 14.065 39.105  -8.035  1.00 51.74  ? 37  ASN E N   1 
ATOM   4852 C  CA  . ASN E  1  37  ? 14.252 38.257  -9.219  1.00 53.18  ? 37  ASN E CA  1 
ATOM   4853 C  C   . ASN E  1  37  ? 13.131 37.207  -9.178  1.00 54.06  ? 37  ASN E C   1 
ATOM   4854 O  O   . ASN E  1  37  ? 12.696 36.701  -10.212 1.00 53.64  ? 37  ASN E O   1 
ATOM   4855 C  CB  . ASN E  1  37  ? 15.613 37.558  -9.222  1.00 53.70  ? 37  ASN E CB  1 
ATOM   4856 C  CG  . ASN E  1  37  ? 16.770 38.491  -9.579  1.00 56.54  ? 37  ASN E CG  1 
ATOM   4857 O  OD1 . ASN E  1  37  ? 16.629 39.426  -10.368 1.00 59.87  ? 37  ASN E OD1 1 
ATOM   4858 N  ND2 . ASN E  1  37  ? 17.937 38.209  -9.017  1.00 57.30  ? 37  ASN E ND2 1 
ATOM   4859 N  N   . TYR E  1  38  ? 12.665 36.888  -7.973  1.00 53.97  ? 38  TYR E N   1 
ATOM   4860 C  CA  . TYR E  1  38  ? 11.577 35.928  -7.819  1.00 53.81  ? 38  TYR E CA  1 
ATOM   4861 C  C   . TYR E  1  38  ? 10.264 36.583  -8.257  1.00 54.18  ? 38  TYR E C   1 
ATOM   4862 O  O   . TYR E  1  38  ? 9.453  35.940  -8.922  1.00 55.50  ? 38  TYR E O   1 
ATOM   4863 C  CB  . TYR E  1  38  ? 11.449 35.451  -6.358  1.00 51.10  ? 38  TYR E CB  1 
ATOM   4864 C  CG  . TYR E  1  38  ? 12.495 34.450  -5.913  1.00 50.68  ? 38  TYR E CG  1 
ATOM   4865 C  CD1 . TYR E  1  38  ? 13.435 33.945  -6.813  1.00 49.89  ? 38  TYR E CD1 1 
ATOM   4866 C  CD2 . TYR E  1  38  ? 12.537 33.997  -4.585  1.00 49.98  ? 38  TYR E CD2 1 
ATOM   4867 C  CE1 . TYR E  1  38  ? 14.392 33.017  -6.408  1.00 48.82  ? 38  TYR E CE1 1 
ATOM   4868 C  CE2 . TYR E  1  38  ? 13.485 33.070  -4.170  1.00 47.76  ? 38  TYR E CE2 1 
ATOM   4869 C  CZ  . TYR E  1  38  ? 14.410 32.585  -5.091  1.00 47.88  ? 38  TYR E CZ  1 
ATOM   4870 O  OH  . TYR E  1  38  ? 15.350 31.657  -4.717  1.00 47.05  ? 38  TYR E OH  1 
ATOM   4871 N  N   . ALA E  1  39  ? 10.075 37.857  -7.892  1.00 53.69  ? 39  ALA E N   1 
ATOM   4872 C  CA  . ALA E  1  39  ? 8.861  38.622  -8.206  1.00 52.44  ? 39  ALA E CA  1 
ATOM   4873 C  C   . ALA E  1  39  ? 9.212  40.039  -8.627  1.00 52.04  ? 39  ALA E C   1 
ATOM   4874 O  O   . ALA E  1  39  ? 9.042  40.975  -7.859  1.00 52.64  ? 39  ALA E O   1 
ATOM   4875 C  CB  . ALA E  1  39  ? 7.955  38.675  -6.985  1.00 50.82  ? 39  ALA E CB  1 
ATOM   4876 N  N   . PRO E  1  40  ? 9.679  40.216  -9.868  1.00 52.79  ? 40  PRO E N   1 
ATOM   4877 C  CA  . PRO E  1  40  ? 10.063 41.531  -10.402 1.00 52.75  ? 40  PRO E CA  1 
ATOM   4878 C  C   . PRO E  1  40  ? 9.080  42.666  -10.151 1.00 53.36  ? 40  PRO E C   1 
ATOM   4879 O  O   . PRO E  1  40  ? 9.462  43.841  -10.153 1.00 52.40  ? 40  PRO E O   1 
ATOM   4880 C  CB  . PRO E  1  40  ? 10.239 41.260  -11.892 1.00 51.96  ? 40  PRO E CB  1 
ATOM   4881 C  CG  . PRO E  1  40  ? 10.680 39.824  -11.928 1.00 54.68  ? 40  PRO E CG  1 
ATOM   4882 C  CD  . PRO E  1  40  ? 9.762  39.178  -10.911 1.00 53.08  ? 40  PRO E CD  1 
ATOM   4883 N  N   . ASP E  1  41  ? 7.814  42.328  -9.933  1.00 55.51  ? 41  ASP E N   1 
ATOM   4884 C  CA  . ASP E  1  41  ? 6.810  43.359  -9.709  1.00 58.35  ? 41  ASP E CA  1 
ATOM   4885 C  C   . ASP E  1  41  ? 6.739  43.876  -8.293  1.00 59.13  ? 41  ASP E C   1 
ATOM   4886 O  O   . ASP E  1  41  ? 6.220  44.964  -8.055  1.00 61.45  ? 41  ASP E O   1 
ATOM   4887 C  CB  . ASP E  1  41  ? 5.422  42.874  -10.133 1.00 58.93  ? 41  ASP E CB  1 
ATOM   4888 C  CG  . ASP E  1  41  ? 5.322  42.647  -11.622 1.00 61.08  ? 41  ASP E CG  1 
ATOM   4889 O  OD1 . ASP E  1  41  ? 5.872  43.467  -12.399 1.00 62.22  ? 41  ASP E OD1 1 
ATOM   4890 O  OD2 . ASP E  1  41  ? 4.690  41.652  -12.019 1.00 60.73  ? 41  ASP E OD2 1 
ATOM   4891 N  N   . ALA E  1  42  ? 7.266  43.101  -7.353  1.00 59.95  ? 42  ALA E N   1 
ATOM   4892 C  CA  . ALA E  1  42  ? 7.258  43.494  -5.952  1.00 59.67  ? 42  ALA E CA  1 
ATOM   4893 C  C   . ALA E  1  42  ? 8.121  44.736  -5.741  1.00 59.62  ? 42  ALA E C   1 
ATOM   4894 O  O   . ALA E  1  42  ? 7.943  45.481  -4.775  1.00 59.57  ? 42  ALA E O   1 
ATOM   4895 C  CB  . ALA E  1  42  ? 7.774  42.350  -5.101  1.00 58.71  ? 42  ALA E CB  1 
ATOM   4896 N  N   . ARG E  1  43  ? 9.038  44.964  -6.672  1.00 58.95  ? 43  ARG E N   1 
ATOM   4897 C  CA  . ARG E  1  43  ? 9.940  46.102  -6.586  1.00 59.66  ? 43  ARG E CA  1 
ATOM   4898 C  C   . ARG E  1  43  ? 9.224  47.467  -6.490  1.00 60.45  ? 43  ARG E C   1 
ATOM   4899 O  O   . ARG E  1  43  ? 9.665  48.363  -5.763  1.00 59.58  ? 43  ARG E O   1 
ATOM   4900 C  CB  . ARG E  1  43  ? 10.895 46.058  -7.783  1.00 58.71  ? 43  ARG E CB  1 
ATOM   4901 C  CG  . ARG E  1  43  ? 12.177 46.860  -7.586  1.00 58.43  ? 43  ARG E CG  1 
ATOM   4902 C  CD  . ARG E  1  43  ? 13.251 46.466  -8.581  1.00 55.71  ? 43  ARG E CD  1 
ATOM   4903 N  NE  . ARG E  1  43  ? 14.394 47.365  -8.498  1.00 57.13  ? 43  ARG E NE  1 
ATOM   4904 C  CZ  . ARG E  1  43  ? 15.493 47.275  -9.245  1.00 57.34  ? 43  ARG E CZ  1 
ATOM   4905 N  NH1 . ARG E  1  43  ? 15.612 46.312  -10.150 1.00 58.14  ? 43  ARG E NH1 1 
ATOM   4906 N  NH2 . ARG E  1  43  ? 16.480 48.153  -9.078  1.00 56.63  ? 43  ARG E NH2 1 
ATOM   4907 N  N   . ASP E  1  44  ? 8.121  47.609  -7.216  1.00 61.79  ? 44  ASP E N   1 
ATOM   4908 C  CA  . ASP E  1  44  ? 7.342  48.848  -7.224  1.00 62.85  ? 44  ASP E CA  1 
ATOM   4909 C  C   . ASP E  1  44  ? 6.760  49.224  -5.866  1.00 61.54  ? 44  ASP E C   1 
ATOM   4910 O  O   . ASP E  1  44  ? 6.460  50.394  -5.611  1.00 62.14  ? 44  ASP E O   1 
ATOM   4911 C  CB  . ASP E  1  44  ? 6.184  48.747  -8.228  1.00 66.86  ? 44  ASP E CB  1 
ATOM   4912 C  CG  . ASP E  1  44  ? 6.644  48.860  -9.675  1.00 70.80  ? 44  ASP E CG  1 
ATOM   4913 O  OD1 . ASP E  1  44  ? 7.351  49.842  -9.991  1.00 71.43  ? 44  ASP E OD1 1 
ATOM   4914 O  OD2 . ASP E  1  44  ? 6.291  47.975  -10.497 1.00 72.97  ? 44  ASP E OD2 1 
ATOM   4915 N  N   . LEU E  1  45  ? 6.586  48.231  -5.002  1.00 58.55  ? 45  LEU E N   1 
ATOM   4916 C  CA  . LEU E  1  45  ? 6.009  48.468  -3.688  1.00 57.70  ? 45  LEU E CA  1 
ATOM   4917 C  C   . LEU E  1  45  ? 6.969  49.221  -2.778  1.00 56.96  ? 45  LEU E C   1 
ATOM   4918 O  O   . LEU E  1  45  ? 6.609  49.671  -1.688  1.00 56.04  ? 45  LEU E O   1 
ATOM   4919 C  CB  . LEU E  1  45  ? 5.640  47.132  -3.059  1.00 57.77  ? 45  LEU E CB  1 
ATOM   4920 C  CG  . LEU E  1  45  ? 4.770  46.249  -3.955  1.00 57.36  ? 45  LEU E CG  1 
ATOM   4921 C  CD1 . LEU E  1  45  ? 4.558  44.908  -3.294  1.00 57.37  ? 45  LEU E CD1 1 
ATOM   4922 C  CD2 . LEU E  1  45  ? 3.439  46.939  -4.203  1.00 57.85  ? 45  LEU E CD2 1 
ATOM   4923 N  N   . PHE E  1  46  ? 8.193  49.386  -3.251  1.00 57.56  ? 46  PHE E N   1 
ATOM   4924 C  CA  . PHE E  1  46  ? 9.207  50.042  -2.447  1.00 58.91  ? 46  PHE E CA  1 
ATOM   4925 C  C   . PHE E  1  46  ? 9.725  51.383  -2.934  1.00 61.70  ? 46  PHE E C   1 
ATOM   4926 O  O   . PHE E  1  46  ? 10.849 51.774  -2.583  1.00 63.04  ? 46  PHE E O   1 
ATOM   4927 C  CB  . PHE E  1  46  ? 10.376 49.087  -2.254  1.00 55.91  ? 46  PHE E CB  1 
ATOM   4928 C  CG  . PHE E  1  46  ? 9.995  47.832  -1.547  1.00 53.26  ? 46  PHE E CG  1 
ATOM   4929 C  CD1 . PHE E  1  46  ? 10.012 47.774  -0.157  1.00 52.44  ? 46  PHE E CD1 1 
ATOM   4930 C  CD2 . PHE E  1  46  ? 9.557  46.726  -2.263  1.00 50.59  ? 46  PHE E CD2 1 
ATOM   4931 C  CE1 . PHE E  1  46  ? 9.594  46.632  0.509   1.00 51.74  ? 46  PHE E CE1 1 
ATOM   4932 C  CE2 . PHE E  1  46  ? 9.135  45.581  -1.613  1.00 49.18  ? 46  PHE E CE2 1 
ATOM   4933 C  CZ  . PHE E  1  46  ? 9.151  45.529  -0.220  1.00 50.45  ? 46  PHE E CZ  1 
ATOM   4934 N  N   . LYS E  1  47  ? 8.927  52.093  -3.729  1.00 62.90  ? 47  LYS E N   1 
ATOM   4935 C  CA  . LYS E  1  47  ? 9.355  53.398  -4.220  1.00 63.43  ? 47  LYS E CA  1 
ATOM   4936 C  C   . LYS E  1  47  ? 9.676  54.304  -3.015  1.00 62.51  ? 47  LYS E C   1 
ATOM   4937 O  O   . LYS E  1  47  ? 10.572 55.151  -3.077  1.00 62.08  ? 47  LYS E O   1 
ATOM   4938 C  CB  . LYS E  1  47  ? 8.258  54.015  -5.098  1.00 65.56  ? 47  LYS E CB  1 
ATOM   4939 C  CG  . LYS E  1  47  ? 8.067  53.305  -6.431  1.00 67.64  ? 47  LYS E CG  1 
ATOM   4940 C  CD  . LYS E  1  47  ? 6.839  53.817  -7.191  1.00 70.49  ? 47  LYS E CD  1 
ATOM   4941 C  CE  . LYS E  1  47  ? 5.538  53.497  -6.455  1.00 71.39  ? 47  LYS E CE  1 
ATOM   4942 N  NZ  . LYS E  1  47  ? 4.333  53.835  -7.263  1.00 71.39  ? 47  LYS E NZ  1 
ATOM   4943 N  N   . SER E  1  48  ? 8.956  54.114  -1.915  1.00 60.73  ? 48  SER E N   1 
ATOM   4944 C  CA  . SER E  1  48  ? 9.199  54.916  -0.720  1.00 61.10  ? 48  SER E CA  1 
ATOM   4945 C  C   . SER E  1  48  ? 10.633 54.784  -0.184  1.00 62.30  ? 48  SER E C   1 
ATOM   4946 O  O   . SER E  1  48  ? 11.104 55.634  0.566   1.00 62.53  ? 48  SER E O   1 
ATOM   4947 C  CB  . SER E  1  48  ? 8.222  54.526  0.376   1.00 59.12  ? 48  SER E CB  1 
ATOM   4948 O  OG  . SER E  1  48  ? 8.242  53.122  0.567   1.00 54.59  ? 48  SER E OG  1 
ATOM   4949 N  N   . VAL E  1  49  ? 11.323 53.710  -0.550  1.00 63.04  ? 49  VAL E N   1 
ATOM   4950 C  CA  . VAL E  1  49  ? 12.687 53.512  -0.081  1.00 64.20  ? 49  VAL E CA  1 
ATOM   4951 C  C   . VAL E  1  49  ? 13.653 53.483  -1.240  1.00 65.20  ? 49  VAL E C   1 
ATOM   4952 O  O   . VAL E  1  49  ? 14.686 52.831  -1.169  1.00 65.40  ? 49  VAL E O   1 
ATOM   4953 C  CB  . VAL E  1  49  ? 12.856 52.195  0.702   1.00 64.35  ? 49  VAL E CB  1 
ATOM   4954 C  CG1 . VAL E  1  49  ? 12.294 52.337  2.103   1.00 61.94  ? 49  VAL E CG1 1 
ATOM   4955 C  CG2 . VAL E  1  49  ? 12.172 51.061  -0.049  1.00 64.14  ? 49  VAL E CG2 1 
ATOM   4956 N  N   . LYS E  1  50  ? 13.291 54.184  -2.309  1.00 67.43  ? 50  LYS E N   1 
ATOM   4957 C  CA  . LYS E  1  50  ? 14.111 54.295  -3.514  1.00 68.62  ? 50  LYS E CA  1 
ATOM   4958 C  C   . LYS E  1  50  ? 14.642 52.952  -4.049  1.00 69.12  ? 50  LYS E C   1 
ATOM   4959 O  O   . LYS E  1  50  ? 15.844 52.781  -4.261  1.00 68.80  ? 50  LYS E O   1 
ATOM   4960 C  CB  . LYS E  1  50  ? 15.271 55.265  -3.241  1.00 68.14  ? 50  LYS E CB  1 
ATOM   4961 C  CG  . LYS E  1  50  ? 16.051 55.671  -4.475  1.00 71.08  ? 50  LYS E CG  1 
ATOM   4962 C  CD  . LYS E  1  50  ? 17.129 56.694  -4.139  1.00 73.13  ? 50  LYS E CD  1 
ATOM   4963 C  CE  . LYS E  1  50  ? 18.133 56.844  -5.281  1.00 75.50  ? 50  LYS E CE  1 
ATOM   4964 N  NZ  . LYS E  1  50  ? 19.353 57.607  -4.861  1.00 75.62  ? 50  LYS E NZ  1 
ATOM   4965 N  N   . SER E  1  51  ? 13.737 52.005  -4.282  1.00 69.07  ? 51  SER E N   1 
ATOM   4966 C  CA  . SER E  1  51  ? 14.126 50.697  -4.794  1.00 69.43  ? 51  SER E CA  1 
ATOM   4967 C  C   . SER E  1  51  ? 14.580 50.725  -6.256  1.00 69.93  ? 51  SER E C   1 
ATOM   4968 O  O   . SER E  1  51  ? 14.934 49.690  -6.802  1.00 68.68  ? 51  SER E O   1 
ATOM   4969 C  CB  . SER E  1  51  ? 12.969 49.698  -4.624  1.00 68.61  ? 51  SER E CB  1 
ATOM   4970 O  OG  . SER E  1  51  ? 11.787 50.124  -5.279  1.00 68.33  ? 51  SER E OG  1 
ATOM   4971 N  N   . GLU E  1  52  ? 14.569 51.897  -6.885  1.00 71.92  ? 52  GLU E N   1 
ATOM   4972 C  CA  . GLU E  1  52  ? 14.979 52.019  -8.288  1.00 73.21  ? 52  GLU E CA  1 
ATOM   4973 C  C   . GLU E  1  52  ? 16.464 51.716  -8.374  1.00 73.02  ? 52  GLU E C   1 
ATOM   4974 O  O   . GLU E  1  52  ? 16.947 51.126  -9.345  1.00 71.83  ? 52  GLU E O   1 
ATOM   4975 C  CB  . GLU E  1  52  ? 14.747 53.439  -8.814  1.00 74.30  ? 52  GLU E CB  1 
ATOM   4976 C  CG  . GLU E  1  52  ? 13.330 53.951  -8.720  1.00 76.62  ? 52  GLU E CG  1 
ATOM   4977 C  CD  . GLU E  1  52  ? 12.828 54.030  -7.294  1.00 79.50  ? 52  GLU E CD  1 
ATOM   4978 O  OE1 . GLU E  1  52  ? 12.283 53.013  -6.803  1.00 81.11  ? 52  GLU E OE1 1 
ATOM   4979 O  OE2 . GLU E  1  52  ? 12.986 55.105  -6.665  1.00 78.25  ? 52  GLU E OE2 1 
ATOM   4980 N  N   . ASP E  1  53  ? 17.182 52.149  -7.348  1.00 72.68  ? 53  ASP E N   1 
ATOM   4981 C  CA  . ASP E  1  53  ? 18.615 51.948  -7.267  1.00 73.92  ? 53  ASP E CA  1 
ATOM   4982 C  C   . ASP E  1  53  ? 18.883 51.208  -5.973  1.00 74.23  ? 53  ASP E C   1 
ATOM   4983 O  O   . ASP E  1  53  ? 18.959 51.811  -4.905  1.00 75.18  ? 53  ASP E O   1 
ATOM   4984 C  CB  . ASP E  1  53  ? 19.329 53.297  -7.271  1.00 74.21  ? 53  ASP E CB  1 
ATOM   4985 C  CG  . ASP E  1  53  ? 20.820 53.163  -7.119  1.00 74.86  ? 53  ASP E CG  1 
ATOM   4986 O  OD1 . ASP E  1  53  ? 21.417 52.276  -7.767  1.00 76.30  ? 53  ASP E OD1 1 
ATOM   4987 O  OD2 . ASP E  1  53  ? 21.394 53.959  -6.357  1.00 75.82  ? 53  ASP E OD2 1 
ATOM   4988 N  N   . MET E  1  54  ? 19.024 49.892  -6.075  1.00 74.11  ? 54  MET E N   1 
ATOM   4989 C  CA  . MET E  1  54  ? 19.247 49.058  -4.903  1.00 74.09  ? 54  MET E CA  1 
ATOM   4990 C  C   . MET E  1  54  ? 20.483 49.379  -4.089  1.00 73.20  ? 54  MET E C   1 
ATOM   4991 O  O   . MET E  1  54  ? 20.580 48.990  -2.928  1.00 72.38  ? 54  MET E O   1 
ATOM   4992 C  CB  . MET E  1  54  ? 19.278 47.595  -5.308  1.00 74.07  ? 54  MET E CB  1 
ATOM   4993 C  CG  . MET E  1  54  ? 17.957 47.088  -5.794  1.00 74.43  ? 54  MET E CG  1 
ATOM   4994 S  SD  . MET E  1  54  ? 18.129 45.382  -6.184  1.00 75.23  ? 54  MET E SD  1 
ATOM   4995 C  CE  . MET E  1  54  ? 17.973 44.666  -4.534  1.00 75.85  ? 54  MET E CE  1 
ATOM   4996 N  N   . ARG E  1  55  ? 21.426 50.098  -4.682  1.00 73.35  ? 55  ARG E N   1 
ATOM   4997 C  CA  . ARG E  1  55  ? 22.648 50.438  -3.962  1.00 72.98  ? 55  ARG E CA  1 
ATOM   4998 C  C   . ARG E  1  55  ? 22.631 51.862  -3.402  1.00 69.54  ? 55  ARG E C   1 
ATOM   4999 O  O   . ARG E  1  55  ? 23.664 52.406  -3.015  1.00 67.95  ? 55  ARG E O   1 
ATOM   5000 C  CB  . ARG E  1  55  ? 23.863 50.221  -4.876  1.00 77.98  ? 55  ARG E CB  1 
ATOM   5001 C  CG  . ARG E  1  55  ? 23.827 48.891  -5.647  1.00 85.00  ? 55  ARG E CG  1 
ATOM   5002 C  CD  . ARG E  1  55  ? 23.349 47.718  -4.773  1.00 92.09  ? 55  ARG E CD  1 
ATOM   5003 N  NE  . ARG E  1  55  ? 24.425 47.074  -4.025  1.00 98.18  ? 55  ARG E NE  1 
ATOM   5004 C  CZ  . ARG E  1  55  ? 25.236 46.149  -4.531  1.00 101.68 ? 55  ARG E CZ  1 
ATOM   5005 N  NH1 . ARG E  1  55  ? 26.192 45.617  -3.778  1.00 102.66 ? 55  ARG E NH1 1 
ATOM   5006 N  NH2 . ARG E  1  55  ? 25.089 45.743  -5.788  1.00 103.73 ? 55  ARG E NH2 1 
ATOM   5007 N  N   . SER E  1  56  ? 21.437 52.445  -3.352  1.00 66.21  ? 56  SER E N   1 
ATOM   5008 C  CA  . SER E  1  56  ? 21.230 53.794  -2.836  1.00 63.72  ? 56  SER E CA  1 
ATOM   5009 C  C   . SER E  1  56  ? 21.142 53.762  -1.313  1.00 62.04  ? 56  SER E C   1 
ATOM   5010 O  O   . SER E  1  56  ? 20.647 52.793  -0.732  1.00 62.76  ? 56  SER E O   1 
ATOM   5011 C  CB  . SER E  1  56  ? 19.924 54.352  -3.378  1.00 63.25  ? 56  SER E CB  1 
ATOM   5012 O  OG  . SER E  1  56  ? 18.844 53.557  -2.917  1.00 63.28  ? 56  SER E OG  1 
ATOM   5013 N  N   . PRO E  1  57  ? 21.589 54.830  -0.645  1.00 59.08  ? 57  PRO E N   1 
ATOM   5014 C  CA  . PRO E  1  57  ? 21.518 54.822  0.817   1.00 57.51  ? 57  PRO E CA  1 
ATOM   5015 C  C   . PRO E  1  57  ? 20.115 54.560  1.355   1.00 55.36  ? 57  PRO E C   1 
ATOM   5016 O  O   . PRO E  1  57  ? 19.943 53.905  2.380   1.00 53.91  ? 57  PRO E O   1 
ATOM   5017 C  CB  . PRO E  1  57  ? 22.064 56.202  1.200   1.00 57.98  ? 57  PRO E CB  1 
ATOM   5018 C  CG  . PRO E  1  57  ? 21.708 57.048  0.014   1.00 57.80  ? 57  PRO E CG  1 
ATOM   5019 C  CD  . PRO E  1  57  ? 22.071 56.129  -1.139  1.00 57.36  ? 57  PRO E CD  1 
ATOM   5020 N  N   . GLN E  1  58  ? 19.105 55.060  0.660   1.00 54.97  ? 58  GLN E N   1 
ATOM   5021 C  CA  . GLN E  1  58  ? 17.741 54.839  1.120   1.00 54.49  ? 58  GLN E CA  1 
ATOM   5022 C  C   . GLN E  1  58  ? 17.399 53.353  1.110   1.00 53.40  ? 58  GLN E C   1 
ATOM   5023 O  O   . GLN E  1  58  ? 16.903 52.826  2.104   1.00 52.93  ? 58  GLN E O   1 
ATOM   5024 C  CB  . GLN E  1  58  ? 16.740 55.606  0.262   1.00 54.91  ? 58  GLN E CB  1 
ATOM   5025 C  CG  . GLN E  1  58  ? 16.874 57.124  0.360   1.00 56.85  ? 58  GLN E CG  1 
ATOM   5026 C  CD  . GLN E  1  58  ? 18.106 57.657  -0.351  1.00 57.62  ? 58  GLN E CD  1 
ATOM   5027 O  OE1 . GLN E  1  58  ? 18.380 57.293  -1.490  1.00 58.11  ? 58  GLN E OE1 1 
ATOM   5028 N  NE2 . GLN E  1  58  ? 18.840 58.534  0.313   1.00 60.29  ? 58  GLN E NE2 1 
ATOM   5029 N  N   . PHE E  1  59  ? 17.666 52.667  0.001   1.00 50.73  ? 59  PHE E N   1 
ATOM   5030 C  CA  . PHE E  1  59  ? 17.339 51.251  -0.043  1.00 49.38  ? 59  PHE E CA  1 
ATOM   5031 C  C   . PHE E  1  59  ? 18.242 50.406  0.847   1.00 48.50  ? 59  PHE E C   1 
ATOM   5032 O  O   . PHE E  1  59  ? 17.784 49.424  1.431   1.00 48.20  ? 59  PHE E O   1 
ATOM   5033 C  CB  . PHE E  1  59  ? 17.374 50.708  -1.472  1.00 46.74  ? 59  PHE E CB  1 
ATOM   5034 C  CG  . PHE E  1  59  ? 16.675 49.390  -1.612  1.00 46.02  ? 59  PHE E CG  1 
ATOM   5035 C  CD1 . PHE E  1  59  ? 17.392 48.197  -1.684  1.00 44.54  ? 59  PHE E CD1 1 
ATOM   5036 C  CD2 . PHE E  1  59  ? 15.284 49.335  -1.579  1.00 46.13  ? 59  PHE E CD2 1 
ATOM   5037 C  CE1 . PHE E  1  59  ? 16.737 46.963  -1.716  1.00 45.22  ? 59  PHE E CE1 1 
ATOM   5038 C  CE2 . PHE E  1  59  ? 14.613 48.111  -1.611  1.00 46.30  ? 59  PHE E CE2 1 
ATOM   5039 C  CZ  . PHE E  1  59  ? 15.341 46.916  -1.678  1.00 45.49  ? 59  PHE E CZ  1 
ATOM   5040 N  N   . LYS E  1  60  ? 19.515 50.771  0.954   1.00 46.14  ? 60  LYS E N   1 
ATOM   5041 C  CA  . LYS E  1  60  ? 20.410 50.007  1.802   1.00 46.06  ? 60  LYS E CA  1 
ATOM   5042 C  C   . LYS E  1  60  ? 19.960 50.136  3.242   1.00 44.57  ? 60  LYS E C   1 
ATOM   5043 O  O   . LYS E  1  60  ? 20.038 49.183  4.018   1.00 42.81  ? 60  LYS E O   1 
ATOM   5044 C  CB  . LYS E  1  60  ? 21.853 50.472  1.638   1.00 47.43  ? 60  LYS E CB  1 
ATOM   5045 C  CG  . LYS E  1  60  ? 22.451 50.010  0.309   1.00 53.31  ? 60  LYS E CG  1 
ATOM   5046 C  CD  . LYS E  1  60  ? 23.967 50.175  0.240   1.00 57.00  ? 60  LYS E CD  1 
ATOM   5047 C  CE  . LYS E  1  60  ? 24.380 51.639  0.214   1.00 61.23  ? 60  LYS E CE  1 
ATOM   5048 N  NZ  . LYS E  1  60  ? 25.867 51.815  0.287   1.00 62.34  ? 60  LYS E NZ  1 
ATOM   5049 N  N   . ALA E  1  61  ? 19.459 51.308  3.601   1.00 43.44  ? 61  ALA E N   1 
ATOM   5050 C  CA  . ALA E  1  61  ? 18.999 51.495  4.969   1.00 43.55  ? 61  ALA E CA  1 
ATOM   5051 C  C   . ALA E  1  61  ? 17.761 50.606  5.182   1.00 42.51  ? 61  ALA E C   1 
ATOM   5052 O  O   . ALA E  1  61  ? 17.502 50.128  6.296   1.00 43.26  ? 61  ALA E O   1 
ATOM   5053 C  CB  . ALA E  1  61  ? 18.667 52.973  5.230   1.00 39.90  ? 61  ALA E CB  1 
ATOM   5054 N  N   . HIS E  1  62  ? 17.000 50.386  4.117   1.00 40.56  ? 62  HIS E N   1 
ATOM   5055 C  CA  . HIS E  1  62  ? 15.801 49.558  4.217   1.00 40.88  ? 62  HIS E CA  1 
ATOM   5056 C  C   . HIS E  1  62  ? 16.226 48.095  4.406   1.00 41.45  ? 62  HIS E C   1 
ATOM   5057 O  O   . HIS E  1  62  ? 15.673 47.375  5.240   1.00 40.51  ? 62  HIS E O   1 
ATOM   5058 C  CB  . HIS E  1  62  ? 14.923 49.689  2.960   1.00 39.27  ? 62  HIS E CB  1 
ATOM   5059 C  CG  . HIS E  1  62  ? 13.825 48.678  2.892   1.00 37.35  ? 62  HIS E CG  1 
ATOM   5060 N  ND1 . HIS E  1  62  ? 12.733 48.712  3.730   1.00 38.46  ? 62  HIS E ND1 1 
ATOM   5061 C  CD2 . HIS E  1  62  ? 13.678 47.569  2.128   1.00 39.61  ? 62  HIS E CD2 1 
ATOM   5062 C  CE1 . HIS E  1  62  ? 11.959 47.666  3.485   1.00 39.06  ? 62  HIS E CE1 1 
ATOM   5063 N  NE2 . HIS E  1  62  ? 12.509 46.955  2.515   1.00 36.95  ? 62  HIS E NE2 1 
ATOM   5064 N  N   . ILE E  1  63  ? 17.217 47.666  3.626   1.00 42.09  ? 63  ILE E N   1 
ATOM   5065 C  CA  . ILE E  1  63  ? 17.716 46.307  3.720   1.00 41.03  ? 63  ILE E CA  1 
ATOM   5066 C  C   . ILE E  1  63  ? 18.142 46.071  5.160   1.00 41.82  ? 63  ILE E C   1 
ATOM   5067 O  O   . ILE E  1  63  ? 17.766 45.065  5.765   1.00 43.63  ? 63  ILE E O   1 
ATOM   5068 C  CB  . ILE E  1  63  ? 18.923 46.086  2.768   1.00 40.99  ? 63  ILE E CB  1 
ATOM   5069 C  CG1 . ILE E  1  63  ? 18.436 46.097  1.318   1.00 39.15  ? 63  ILE E CG1 1 
ATOM   5070 C  CG2 . ILE E  1  63  ? 19.624 44.762  3.072   1.00 40.98  ? 63  ILE E CG2 1 
ATOM   5071 C  CD1 . ILE E  1  63  ? 19.517 45.936  0.276   1.00 36.55  ? 63  ILE E CD1 1 
ATOM   5072 N  N   . ALA E  1  64  ? 18.899 47.011  5.716   1.00 41.35  ? 64  ALA E N   1 
ATOM   5073 C  CA  . ALA E  1  64  ? 19.371 46.886  7.089   1.00 42.42  ? 64  ALA E CA  1 
ATOM   5074 C  C   . ALA E  1  64  ? 18.224 46.749  8.096   1.00 42.68  ? 64  ALA E C   1 
ATOM   5075 O  O   . ALA E  1  64  ? 18.310 45.949  9.031   1.00 41.99  ? 64  ALA E O   1 
ATOM   5076 C  CB  . ALA E  1  64  ? 20.249 48.087  7.460   1.00 41.08  ? 64  ALA E CB  1 
ATOM   5077 N  N   . ARG E  1  65  ? 17.161 47.529  7.907   1.00 43.90  ? 65  ARG E N   1 
ATOM   5078 C  CA  . ARG E  1  65  ? 16.001 47.492  8.807   1.00 44.75  ? 65  ARG E CA  1 
ATOM   5079 C  C   . ARG E  1  65  ? 15.264 46.147  8.764   1.00 44.00  ? 65  ARG E C   1 
ATOM   5080 O  O   . ARG E  1  65  ? 14.827 45.630  9.802   1.00 41.62  ? 65  ARG E O   1 
ATOM   5081 C  CB  . ARG E  1  65  ? 15.019 48.633  8.480   1.00 45.50  ? 65  ARG E CB  1 
ATOM   5082 C  CG  . ARG E  1  65  ? 15.374 49.984  9.112   1.00 46.37  ? 65  ARG E CG  1 
ATOM   5083 C  CD  . ARG E  1  65  ? 14.221 50.988  8.942   1.00 47.19  ? 65  ARG E CD  1 
ATOM   5084 N  NE  . ARG E  1  65  ? 14.024 51.355  7.546   1.00 48.65  ? 65  ARG E NE  1 
ATOM   5085 C  CZ  . ARG E  1  65  ? 14.715 52.299  6.912   1.00 49.79  ? 65  ARG E CZ  1 
ATOM   5086 N  NH1 . ARG E  1  65  ? 15.650 52.988  7.556   1.00 50.71  ? 65  ARG E NH1 1 
ATOM   5087 N  NH2 . ARG E  1  65  ? 14.488 52.531  5.622   1.00 50.77  ? 65  ARG E NH2 1 
ATOM   5088 N  N   . VAL E  1  66  ? 15.152 45.582  7.564   1.00 42.10  ? 66  VAL E N   1 
ATOM   5089 C  CA  . VAL E  1  66  ? 14.484 44.302  7.378   1.00 41.93  ? 66  VAL E CA  1 
ATOM   5090 C  C   . VAL E  1  66  ? 15.269 43.128  7.976   1.00 42.34  ? 66  VAL E C   1 
ATOM   5091 O  O   . VAL E  1  66  ? 14.689 42.299  8.682   1.00 42.42  ? 66  VAL E O   1 
ATOM   5092 C  CB  . VAL E  1  66  ? 14.245 44.004  5.880   1.00 43.02  ? 66  VAL E CB  1 
ATOM   5093 C  CG1 . VAL E  1  66  ? 13.721 42.568  5.700   1.00 38.36  ? 66  VAL E CG1 1 
ATOM   5094 C  CG2 . VAL E  1  66  ? 13.265 45.043  5.285   1.00 42.26  ? 66  VAL E CG2 1 
ATOM   5095 N  N   . ILE E  1  67  ? 16.569 43.034  7.686   1.00 40.37  ? 67  ILE E N   1 
ATOM   5096 C  CA  . ILE E  1  67  ? 17.331 41.917  8.236   1.00 38.66  ? 67  ILE E CA  1 
ATOM   5097 C  C   . ILE E  1  67  ? 17.504 42.134  9.737   1.00 37.97  ? 67  ILE E C   1 
ATOM   5098 O  O   . ILE E  1  67  ? 17.746 41.201  10.489  1.00 38.58  ? 67  ILE E O   1 
ATOM   5099 C  CB  . ILE E  1  67  ? 18.703 41.704  7.522   1.00 38.14  ? 67  ILE E CB  1 
ATOM   5100 C  CG1 . ILE E  1  67  ? 19.571 42.943  7.633   1.00 39.80  ? 67  ILE E CG1 1 
ATOM   5101 C  CG2 . ILE E  1  67  ? 18.480 41.377  6.043   1.00 34.33  ? 67  ILE E CG2 1 
ATOM   5102 C  CD1 . ILE E  1  67  ? 20.866 42.842  6.826   1.00 42.14  ? 67  ILE E CD1 1 
ATOM   5103 N  N   . GLY E  1  68  ? 17.342 43.367  10.180  1.00 37.25  ? 68  GLY E N   1 
ATOM   5104 C  CA  . GLY E  1  68  ? 17.421 43.619  11.602  1.00 36.91  ? 68  GLY E CA  1 
ATOM   5105 C  C   . GLY E  1  68  ? 16.103 43.155  12.218  1.00 38.03  ? 68  GLY E C   1 
ATOM   5106 O  O   . GLY E  1  68  ? 16.050 42.761  13.388  1.00 37.78  ? 68  GLY E O   1 
ATOM   5107 N  N   . GLY E  1  69  ? 15.027 43.213  11.433  1.00 37.81  ? 69  GLY E N   1 
ATOM   5108 C  CA  . GLY E  1  69  ? 13.735 42.760  11.927  1.00 40.24  ? 69  GLY E CA  1 
ATOM   5109 C  C   . GLY E  1  69  ? 13.751 41.241  12.006  1.00 41.84  ? 69  GLY E C   1 
ATOM   5110 O  O   . GLY E  1  69  ? 13.255 40.620  12.956  1.00 41.25  ? 69  GLY E O   1 
ATOM   5111 N  N   . LEU E  1  70  ? 14.342 40.632  10.992  1.00 42.20  ? 70  LEU E N   1 
ATOM   5112 C  CA  . LEU E  1  70  ? 14.447 39.184  10.959  1.00 42.77  ? 70  LEU E CA  1 
ATOM   5113 C  C   . LEU E  1  70  ? 15.277 38.739  12.165  1.00 43.74  ? 70  LEU E C   1 
ATOM   5114 O  O   . LEU E  1  70  ? 14.888 37.819  12.887  1.00 45.24  ? 70  LEU E O   1 
ATOM   5115 C  CB  . LEU E  1  70  ? 15.116 38.738  9.646   1.00 42.48  ? 70  LEU E CB  1 
ATOM   5116 C  CG  . LEU E  1  70  ? 14.246 38.761  8.388   1.00 40.58  ? 70  LEU E CG  1 
ATOM   5117 C  CD1 . LEU E  1  70  ? 15.091 38.706  7.164   1.00 42.76  ? 70  LEU E CD1 1 
ATOM   5118 C  CD2 . LEU E  1  70  ? 13.311 37.597  8.404   1.00 41.70  ? 70  LEU E CD2 1 
ATOM   5119 N  N   . ASP E  1  71  ? 16.398 39.414  12.397  1.00 43.58  ? 71  ASP E N   1 
ATOM   5120 C  CA  . ASP E  1  71  ? 17.276 39.062  13.508  1.00 43.07  ? 71  ASP E CA  1 
ATOM   5121 C  C   . ASP E  1  71  ? 16.629 39.136  14.884  1.00 42.55  ? 71  ASP E C   1 
ATOM   5122 O  O   . ASP E  1  71  ? 16.668 38.172  15.646  1.00 40.62  ? 71  ASP E O   1 
ATOM   5123 C  CB  . ASP E  1  71  ? 18.524 39.947  13.516  1.00 43.12  ? 71  ASP E CB  1 
ATOM   5124 C  CG  . ASP E  1  71  ? 19.515 39.527  14.565  1.00 44.55  ? 71  ASP E CG  1 
ATOM   5125 O  OD1 . ASP E  1  71  ? 20.154 38.461  14.392  1.00 45.11  ? 71  ASP E OD1 1 
ATOM   5126 O  OD2 . ASP E  1  71  ? 19.648 40.260  15.572  1.00 46.45  ? 71  ASP E OD2 1 
ATOM   5127 N  N   . ARG E  1  72  ? 16.043 40.286  15.213  1.00 43.31  ? 72  ARG E N   1 
ATOM   5128 C  CA  . ARG E  1  72  ? 15.406 40.444  16.522  1.00 42.83  ? 72  ARG E CA  1 
ATOM   5129 C  C   . ARG E  1  72  ? 14.224 39.504  16.693  1.00 42.65  ? 72  ARG E C   1 
ATOM   5130 O  O   . ARG E  1  72  ? 13.977 39.019  17.797  1.00 41.98  ? 72  ARG E O   1 
ATOM   5131 C  CB  . ARG E  1  72  ? 14.945 41.883  16.720  1.00 41.39  ? 72  ARG E CB  1 
ATOM   5132 C  CG  . ARG E  1  72  ? 13.779 42.257  15.855  1.00 42.61  ? 72  ARG E CG  1 
ATOM   5133 C  CD  . ARG E  1  72  ? 13.511 43.749  15.915  1.00 42.38  ? 72  ARG E CD  1 
ATOM   5134 N  NE  . ARG E  1  72  ? 12.089 44.011  15.726  1.00 41.03  ? 72  ARG E NE  1 
ATOM   5135 C  CZ  . ARG E  1  72  ? 11.594 44.953  14.934  1.00 41.75  ? 72  ARG E CZ  1 
ATOM   5136 N  NH1 . ARG E  1  72  ? 12.403 45.738  14.246  1.00 43.67  ? 72  ARG E NH1 1 
ATOM   5137 N  NH2 . ARG E  1  72  ? 10.283 45.108  14.823  1.00 42.79  ? 72  ARG E NH2 1 
ATOM   5138 N  N   . VAL E  1  73  ? 13.501 39.251  15.603  1.00 43.80  ? 73  VAL E N   1 
ATOM   5139 C  CA  . VAL E  1  73  ? 12.342 38.347  15.632  1.00 45.42  ? 73  VAL E CA  1 
ATOM   5140 C  C   . VAL E  1  73  ? 12.802 36.903  15.876  1.00 46.93  ? 73  VAL E C   1 
ATOM   5141 O  O   . VAL E  1  73  ? 12.269 36.206  16.742  1.00 47.89  ? 73  VAL E O   1 
ATOM   5142 C  CB  . VAL E  1  73  ? 11.552 38.419  14.304  1.00 46.04  ? 73  VAL E CB  1 
ATOM   5143 C  CG1 . VAL E  1  73  ? 10.560 37.287  14.227  1.00 45.08  ? 73  VAL E CG1 1 
ATOM   5144 C  CG2 . VAL E  1  73  ? 10.822 39.771  14.206  1.00 46.32  ? 73  VAL E CG2 1 
ATOM   5145 N  N   . ILE E  1  74  ? 13.805 36.462  15.125  1.00 46.23  ? 74  ILE E N   1 
ATOM   5146 C  CA  . ILE E  1  74  ? 14.320 35.111  15.290  1.00 45.43  ? 74  ILE E CA  1 
ATOM   5147 C  C   . ILE E  1  74  ? 14.906 34.935  16.691  1.00 44.72  ? 74  ILE E C   1 
ATOM   5148 O  O   . ILE E  1  74  ? 14.757 33.884  17.314  1.00 43.61  ? 74  ILE E O   1 
ATOM   5149 C  CB  . ILE E  1  74  ? 15.383 34.796  14.195  1.00 45.90  ? 74  ILE E CB  1 
ATOM   5150 C  CG1 . ILE E  1  74  ? 14.678 34.519  12.868  1.00 46.73  ? 74  ILE E CG1 1 
ATOM   5151 C  CG2 . ILE E  1  74  ? 16.246 33.602  14.590  1.00 46.39  ? 74  ILE E CG2 1 
ATOM   5152 C  CD1 . ILE E  1  74  ? 15.627 34.289  11.692  1.00 48.12  ? 74  ILE E CD1 1 
ATOM   5153 N  N   . SER E  1  75  ? 15.561 35.972  17.201  1.00 45.06  ? 75  SER E N   1 
ATOM   5154 C  CA  . SER E  1  75  ? 16.145 35.875  18.532  1.00 47.04  ? 75  SER E CA  1 
ATOM   5155 C  C   . SER E  1  75  ? 15.080 35.709  19.613  1.00 48.65  ? 75  SER E C   1 
ATOM   5156 O  O   . SER E  1  75  ? 15.370 35.219  20.699  1.00 48.80  ? 75  SER E O   1 
ATOM   5157 C  CB  . SER E  1  75  ? 16.994 37.102  18.848  1.00 45.67  ? 75  SER E CB  1 
ATOM   5158 O  OG  . SER E  1  75  ? 16.180 38.212  19.142  1.00 48.09  ? 75  SER E OG  1 
ATOM   5159 N  N   . MET E  1  76  ? 13.851 36.120  19.318  1.00 51.60  ? 76  MET E N   1 
ATOM   5160 C  CA  . MET E  1  76  ? 12.772 35.991  20.287  1.00 53.88  ? 76  MET E CA  1 
ATOM   5161 C  C   . MET E  1  76  ? 11.927 34.742  20.075  1.00 55.11  ? 76  MET E C   1 
ATOM   5162 O  O   . MET E  1  76  ? 10.954 34.524  20.774  1.00 55.15  ? 76  MET E O   1 
ATOM   5163 C  CB  . MET E  1  76  ? 11.886 37.229  20.261  1.00 54.85  ? 76  MET E CB  1 
ATOM   5164 C  CG  . MET E  1  76  ? 12.583 38.467  20.785  1.00 56.44  ? 76  MET E CG  1 
ATOM   5165 S  SD  . MET E  1  76  ? 11.507 39.903  20.745  1.00 59.02  ? 76  MET E SD  1 
ATOM   5166 C  CE  . MET E  1  76  ? 11.674 40.431  19.000  1.00 55.75  ? 76  MET E CE  1 
ATOM   5167 N  N   . PHE E  1  77  ? 12.302 33.912  19.113  1.00 57.52  ? 77  PHE E N   1 
ATOM   5168 C  CA  . PHE E  1  77  ? 11.567 32.674  18.860  1.00 60.57  ? 77  PHE E CA  1 
ATOM   5169 C  C   . PHE E  1  77  ? 11.286 31.847  20.135  1.00 62.98  ? 77  PHE E C   1 
ATOM   5170 O  O   . PHE E  1  77  ? 10.297 31.108  20.214  1.00 62.75  ? 77  PHE E O   1 
ATOM   5171 C  CB  . PHE E  1  77  ? 12.340 31.793  17.864  1.00 59.50  ? 77  PHE E CB  1 
ATOM   5172 C  CG  . PHE E  1  77  ? 11.833 31.876  16.444  1.00 60.21  ? 77  PHE E CG  1 
ATOM   5173 C  CD1 . PHE E  1  77  ? 10.516 32.231  16.176  1.00 60.72  ? 77  PHE E CD1 1 
ATOM   5174 C  CD2 . PHE E  1  77  ? 12.657 31.540  15.375  1.00 60.87  ? 77  PHE E CD2 1 
ATOM   5175 C  CE1 . PHE E  1  77  ? 10.023 32.248  14.870  1.00 59.43  ? 77  PHE E CE1 1 
ATOM   5176 C  CE2 . PHE E  1  77  ? 12.165 31.553  14.066  1.00 60.73  ? 77  PHE E CE2 1 
ATOM   5177 C  CZ  . PHE E  1  77  ? 10.846 31.908  13.820  1.00 59.17  ? 77  PHE E CZ  1 
ATOM   5178 N  N   . ASP E  1  78  ? 12.155 31.976  21.128  1.00 64.84  ? 78  ASP E N   1 
ATOM   5179 C  CA  . ASP E  1  78  ? 12.011 31.218  22.361  1.00 67.05  ? 78  ASP E CA  1 
ATOM   5180 C  C   . ASP E  1  78  ? 11.135 31.871  23.448  1.00 66.97  ? 78  ASP E C   1 
ATOM   5181 O  O   . ASP E  1  78  ? 10.880 31.272  24.499  1.00 66.63  ? 78  ASP E O   1 
ATOM   5182 C  CB  . ASP E  1  78  ? 13.410 30.895  22.915  1.00 70.23  ? 78  ASP E CB  1 
ATOM   5183 C  CG  . ASP E  1  78  ? 14.352 32.092  22.862  1.00 72.98  ? 78  ASP E CG  1 
ATOM   5184 O  OD1 . ASP E  1  78  ? 13.933 33.203  23.251  1.00 72.53  ? 78  ASP E OD1 1 
ATOM   5185 O  OD2 . ASP E  1  78  ? 15.516 31.919  22.439  1.00 73.64  ? 78  ASP E OD2 1 
ATOM   5186 N  N   . ASN E  1  79  ? 10.672 33.091  23.206  1.00 65.85  ? 79  ASN E N   1 
ATOM   5187 C  CA  . ASN E  1  79  ? 9.827  33.764  24.188  1.00 65.27  ? 79  ASN E CA  1 
ATOM   5188 C  C   . ASN E  1  79  ? 8.565  34.310  23.529  1.00 64.16  ? 79  ASN E C   1 
ATOM   5189 O  O   . ASN E  1  79  ? 8.533  35.432  23.012  1.00 62.28  ? 79  ASN E O   1 
ATOM   5190 C  CB  . ASN E  1  79  ? 10.597 34.889  24.892  1.00 67.48  ? 79  ASN E CB  1 
ATOM   5191 C  CG  . ASN E  1  79  ? 9.778  35.562  25.993  1.00 70.59  ? 79  ASN E CG  1 
ATOM   5192 O  OD1 . ASN E  1  79  ? 8.834  36.319  25.724  1.00 71.35  ? 79  ASN E OD1 1 
ATOM   5193 N  ND2 . ASN E  1  79  ? 10.131 35.274  27.247  1.00 71.02  ? 79  ASN E ND2 1 
ATOM   5194 N  N   . GLU E  1  80  ? 7.525  33.478  23.565  1.00 63.70  ? 80  GLU E N   1 
ATOM   5195 C  CA  . GLU E  1  80  ? 6.219  33.765  22.988  1.00 62.88  ? 80  GLU E CA  1 
ATOM   5196 C  C   . GLU E  1  80  ? 5.673  35.168  23.202  1.00 62.15  ? 80  GLU E C   1 
ATOM   5197 O  O   . GLU E  1  80  ? 5.202  35.806  22.259  1.00 60.08  ? 80  GLU E O   1 
ATOM   5198 C  CB  . GLU E  1  80  ? 5.210  32.746  23.513  1.00 63.98  ? 80  GLU E CB  1 
ATOM   5199 C  CG  . GLU E  1  80  ? 5.136  31.486  22.697  1.00 66.61  ? 80  GLU E CG  1 
ATOM   5200 C  CD  . GLU E  1  80  ? 4.478  31.721  21.349  1.00 69.11  ? 80  GLU E CD  1 
ATOM   5201 O  OE1 . GLU E  1  80  ? 5.182  31.638  20.320  1.00 69.35  ? 80  GLU E OE1 1 
ATOM   5202 O  OE2 . GLU E  1  80  ? 3.255  31.994  21.326  1.00 70.14  ? 80  GLU E OE2 1 
ATOM   5203 N  N   . ASP E  1  81  ? 5.716  35.643  24.442  1.00 61.66  ? 81  ASP E N   1 
ATOM   5204 C  CA  . ASP E  1  81  ? 5.200  36.966  24.745  1.00 61.34  ? 81  ASP E CA  1 
ATOM   5205 C  C   . ASP E  1  81  ? 5.950  38.051  23.976  1.00 59.68  ? 81  ASP E C   1 
ATOM   5206 O  O   . ASP E  1  81  ? 5.338  38.837  23.250  1.00 58.50  ? 81  ASP E O   1 
ATOM   5207 C  CB  . ASP E  1  81  ? 5.245  37.206  26.260  1.00 64.64  ? 81  ASP E CB  1 
ATOM   5208 C  CG  . ASP E  1  81  ? 4.248  36.311  27.020  1.00 67.54  ? 81  ASP E CG  1 
ATOM   5209 O  OD1 . ASP E  1  81  ? 3.089  36.196  26.558  1.00 64.36  ? 81  ASP E OD1 1 
ATOM   5210 O  OD2 . ASP E  1  81  ? 4.612  35.735  28.072  1.00 69.64  ? 81  ASP E OD2 1 
ATOM   5211 N  N   . ALA E  1  82  ? 7.272  38.084  24.114  1.00 58.14  ? 82  ALA E N   1 
ATOM   5212 C  CA  . ALA E  1  82  ? 8.083  39.070  23.405  1.00 55.03  ? 82  ALA E CA  1 
ATOM   5213 C  C   . ALA E  1  82  ? 7.883  38.904  21.888  1.00 53.44  ? 82  ALA E C   1 
ATOM   5214 O  O   . ALA E  1  82  ? 7.650  39.885  21.176  1.00 50.86  ? 82  ALA E O   1 
ATOM   5215 C  CB  . ALA E  1  82  ? 9.567  38.893  23.780  1.00 54.56  ? 82  ALA E CB  1 
ATOM   5216 N  N   . LEU E  1  83  ? 7.965  37.660  21.403  1.00 50.93  ? 83  LEU E N   1 
ATOM   5217 C  CA  . LEU E  1  83  ? 7.806  37.382  19.973  1.00 51.00  ? 83  LEU E CA  1 
ATOM   5218 C  C   . LEU E  1  83  ? 6.518  37.954  19.370  1.00 52.97  ? 83  LEU E C   1 
ATOM   5219 O  O   . LEU E  1  83  ? 6.544  38.676  18.362  1.00 53.05  ? 83  LEU E O   1 
ATOM   5220 C  CB  . LEU E  1  83  ? 7.862  35.865  19.708  1.00 48.04  ? 83  LEU E CB  1 
ATOM   5221 C  CG  . LEU E  1  83  ? 7.521  35.378  18.286  1.00 46.64  ? 83  LEU E CG  1 
ATOM   5222 C  CD1 . LEU E  1  83  ? 8.526  35.949  17.293  1.00 44.48  ? 83  LEU E CD1 1 
ATOM   5223 C  CD2 . LEU E  1  83  ? 7.535  33.857  18.225  1.00 43.50  ? 83  LEU E CD2 1 
ATOM   5224 N  N   . ASN E  1  84  ? 5.383  37.616  19.976  1.00 53.90  ? 84  ASN E N   1 
ATOM   5225 C  CA  . ASN E  1  84  ? 4.111  38.100  19.481  1.00 52.94  ? 84  ASN E CA  1 
ATOM   5226 C  C   . ASN E  1  84  ? 3.949  39.610  19.600  1.00 52.35  ? 84  ASN E C   1 
ATOM   5227 O  O   . ASN E  1  84  ? 3.351  40.239  18.725  1.00 53.58  ? 84  ASN E O   1 
ATOM   5228 C  CB  . ASN E  1  84  ? 2.980  37.372  20.191  1.00 53.73  ? 84  ASN E CB  1 
ATOM   5229 C  CG  . ASN E  1  84  ? 2.917  35.910  19.798  1.00 55.04  ? 84  ASN E CG  1 
ATOM   5230 O  OD1 . ASN E  1  84  ? 2.934  35.578  18.611  1.00 52.07  ? 84  ASN E OD1 1 
ATOM   5231 N  ND2 . ASN E  1  84  ? 2.842  35.027  20.792  1.00 56.77  ? 84  ASN E ND2 1 
ATOM   5232 N  N   . ALA E  1  85  ? 4.479  40.209  20.657  1.00 50.18  ? 85  ALA E N   1 
ATOM   5233 C  CA  . ALA E  1  85  ? 4.340  41.649  20.772  1.00 50.43  ? 85  ALA E CA  1 
ATOM   5234 C  C   . ALA E  1  85  ? 5.050  42.331  19.590  1.00 51.61  ? 85  ALA E C   1 
ATOM   5235 O  O   . ALA E  1  85  ? 4.519  43.297  19.014  1.00 50.27  ? 85  ALA E O   1 
ATOM   5236 C  CB  . ALA E  1  85  ? 4.913  42.137  22.097  1.00 48.35  ? 85  ALA E CB  1 
ATOM   5237 N  N   . ASP E  1  86  ? 6.227  41.815  19.226  1.00 52.71  ? 86  ASP E N   1 
ATOM   5238 C  CA  . ASP E  1  86  ? 7.012  42.379  18.125  1.00 54.26  ? 86  ASP E CA  1 
ATOM   5239 C  C   . ASP E  1  86  ? 6.362  42.064  16.773  1.00 55.00  ? 86  ASP E C   1 
ATOM   5240 O  O   . ASP E  1  86  ? 6.339  42.902  15.865  1.00 55.06  ? 86  ASP E O   1 
ATOM   5241 C  CB  . ASP E  1  86  ? 8.461  41.853  18.177  1.00 54.64  ? 86  ASP E CB  1 
ATOM   5242 C  CG  . ASP E  1  86  ? 9.437  42.743  17.421  1.00 55.58  ? 86  ASP E CG  1 
ATOM   5243 O  OD1 . ASP E  1  86  ? 9.237  43.978  17.409  1.00 59.49  ? 86  ASP E OD1 1 
ATOM   5244 O  OD2 . ASP E  1  86  ? 10.412 42.218  16.857  1.00 55.36  ? 86  ASP E OD2 1 
ATOM   5245 N  N   . LEU E  1  87  ? 5.815  40.868  16.633  1.00 54.86  ? 87  LEU E N   1 
ATOM   5246 C  CA  . LEU E  1  87  ? 5.183  40.554  15.365  1.00 58.29  ? 87  LEU E CA  1 
ATOM   5247 C  C   . LEU E  1  87  ? 3.987  41.469  15.105  1.00 59.91  ? 87  LEU E C   1 
ATOM   5248 O  O   . LEU E  1  87  ? 3.708  41.814  13.954  1.00 60.53  ? 87  LEU E O   1 
ATOM   5249 C  CB  . LEU E  1  87  ? 4.765  39.088  15.315  1.00 58.22  ? 87  LEU E CB  1 
ATOM   5250 C  CG  . LEU E  1  87  ? 5.875  38.083  15.009  1.00 57.85  ? 87  LEU E CG  1 
ATOM   5251 C  CD1 . LEU E  1  87  ? 5.379  36.676  15.271  1.00 57.90  ? 87  LEU E CD1 1 
ATOM   5252 C  CD2 . LEU E  1  87  ? 6.315  38.232  13.574  1.00 55.81  ? 87  LEU E CD2 1 
ATOM   5253 N  N   . GLU E  1  88  ? 3.285  41.862  16.171  1.00 61.07  ? 88  GLU E N   1 
ATOM   5254 C  CA  . GLU E  1  88  ? 2.137  42.755  16.026  1.00 63.02  ? 88  GLU E CA  1 
ATOM   5255 C  C   . GLU E  1  88  ? 2.655  44.147  15.696  1.00 62.01  ? 88  GLU E C   1 
ATOM   5256 O  O   . GLU E  1  88  ? 2.042  44.864  14.910  1.00 62.48  ? 88  GLU E O   1 
ATOM   5257 C  CB  . GLU E  1  88  ? 1.303  42.793  17.304  1.00 66.78  ? 88  GLU E CB  1 
ATOM   5258 C  CG  . GLU E  1  88  ? 0.445  41.551  17.525  1.00 73.06  ? 88  GLU E CG  1 
ATOM   5259 C  CD  . GLU E  1  88  ? -0.648 41.369  16.464  1.00 76.11  ? 88  GLU E CD  1 
ATOM   5260 O  OE1 . GLU E  1  88  ? -0.766 40.245  15.915  1.00 76.58  ? 88  GLU E OE1 1 
ATOM   5261 O  OE2 . GLU E  1  88  ? -1.392 42.339  16.184  1.00 77.09  ? 88  GLU E OE2 1 
ATOM   5262 N  N   . HIS E  1  89  ? 3.786  44.519  16.294  1.00 60.07  ? 89  HIS E N   1 
ATOM   5263 C  CA  . HIS E  1  89  ? 4.390  45.820  16.023  1.00 58.93  ? 89  HIS E CA  1 
ATOM   5264 C  C   . HIS E  1  89  ? 4.699  45.891  14.524  1.00 57.87  ? 89  HIS E C   1 
ATOM   5265 O  O   . HIS E  1  89  ? 4.485  46.917  13.876  1.00 56.04  ? 89  HIS E O   1 
ATOM   5266 C  CB  . HIS E  1  89  ? 5.703  45.983  16.818  1.00 59.10  ? 89  HIS E CB  1 
ATOM   5267 C  CG  . HIS E  1  89  ? 6.361  47.328  16.661  1.00 60.93  ? 89  HIS E CG  1 
ATOM   5268 N  ND1 . HIS E  1  89  ? 6.154  48.369  17.542  1.00 61.08  ? 89  HIS E ND1 1 
ATOM   5269 C  CD2 . HIS E  1  89  ? 7.255  47.784  15.751  1.00 61.54  ? 89  HIS E CD2 1 
ATOM   5270 C  CE1 . HIS E  1  89  ? 6.891  49.404  17.182  1.00 61.53  ? 89  HIS E CE1 1 
ATOM   5271 N  NE2 . HIS E  1  89  ? 7.568  49.074  16.098  1.00 62.39  ? 89  HIS E NE2 1 
ATOM   5272 N  N   . LEU E  1  90  ? 5.193  44.782  13.980  1.00 58.06  ? 90  LEU E N   1 
ATOM   5273 C  CA  . LEU E  1  90  ? 5.547  44.711  12.571  1.00 59.62  ? 90  LEU E CA  1 
ATOM   5274 C  C   . LEU E  1  90  ? 4.317  44.727  11.690  1.00 60.83  ? 90  LEU E C   1 
ATOM   5275 O  O   . LEU E  1  90  ? 4.317  45.330  10.608  1.00 61.20  ? 90  LEU E O   1 
ATOM   5276 C  CB  . LEU E  1  90  ? 6.378  43.458  12.302  1.00 59.69  ? 90  LEU E CB  1 
ATOM   5277 C  CG  . LEU E  1  90  ? 7.818  43.525  12.823  1.00 59.98  ? 90  LEU E CG  1 
ATOM   5278 C  CD1 . LEU E  1  90  ? 8.432  42.135  12.806  1.00 58.83  ? 90  LEU E CD1 1 
ATOM   5279 C  CD2 . LEU E  1  90  ? 8.625  44.503  11.981  1.00 58.74  ? 90  LEU E CD2 1 
ATOM   5280 N  N   . LYS E  1  91  ? 3.271  44.053  12.147  1.00 62.25  ? 91  LYS E N   1 
ATOM   5281 C  CA  . LYS E  1  91  ? 2.020  44.023  11.408  1.00 63.82  ? 91  LYS E CA  1 
ATOM   5282 C  C   . LYS E  1  91  ? 1.462  45.451  11.301  1.00 62.93  ? 91  LYS E C   1 
ATOM   5283 O  O   . LYS E  1  91  ? 1.017  45.868  10.226  1.00 63.17  ? 91  LYS E O   1 
ATOM   5284 C  CB  . LYS E  1  91  ? 1.010  43.119  12.111  1.00 66.27  ? 91  LYS E CB  1 
ATOM   5285 C  CG  . LYS E  1  91  ? -0.386 43.222  11.524  1.00 70.27  ? 91  LYS E CG  1 
ATOM   5286 C  CD  . LYS E  1  91  ? -1.320 42.138  12.037  1.00 72.11  ? 91  LYS E CD  1 
ATOM   5287 C  CE  . LYS E  1  91  ? -2.748 42.369  11.525  1.00 75.09  ? 91  LYS E CE  1 
ATOM   5288 N  NZ  . LYS E  1  91  ? -2.833 42.571  10.039  1.00 77.54  ? 91  LYS E NZ  1 
ATOM   5289 N  N   . SER E  1  92  ? 1.502  46.191  12.409  1.00 60.10  ? 92  SER E N   1 
ATOM   5290 C  CA  . SER E  1  92  ? 1.022  47.565  12.424  1.00 60.04  ? 92  SER E CA  1 
ATOM   5291 C  C   . SER E  1  92  ? 1.739  48.425  11.376  1.00 60.27  ? 92  SER E C   1 
ATOM   5292 O  O   . SER E  1  92  ? 1.129  49.315  10.777  1.00 60.92  ? 92  SER E O   1 
ATOM   5293 C  CB  . SER E  1  92  ? 1.189  48.190  13.822  1.00 60.64  ? 92  SER E CB  1 
ATOM   5294 O  OG  . SER E  1  92  ? 2.518  48.634  14.059  1.00 63.95  ? 92  SER E OG  1 
ATOM   5295 N  N   . GLN E  1  93  ? 3.025  48.157  11.142  1.00 60.49  ? 93  GLN E N   1 
ATOM   5296 C  CA  . GLN E  1  93  ? 3.793  48.916  10.158  1.00 60.17  ? 93  GLN E CA  1 
ATOM   5297 C  C   . GLN E  1  93  ? 3.511  48.494  8.714   1.00 61.10  ? 93  GLN E C   1 
ATOM   5298 O  O   . GLN E  1  93  ? 3.669  49.298  7.790   1.00 62.23  ? 93  GLN E O   1 
ATOM   5299 C  CB  . GLN E  1  93  ? 5.290  48.789  10.445  1.00 59.15  ? 93  GLN E CB  1 
ATOM   5300 C  CG  . GLN E  1  93  ? 5.697  49.340  11.796  1.00 58.94  ? 93  GLN E CG  1 
ATOM   5301 C  CD  . GLN E  1  93  ? 7.167  49.177  12.060  1.00 59.43  ? 93  GLN E CD  1 
ATOM   5302 O  OE1 . GLN E  1  93  ? 7.695  48.077  11.937  1.00 60.03  ? 93  GLN E OE1 1 
ATOM   5303 N  NE2 . GLN E  1  93  ? 7.839  50.264  12.428  1.00 58.29  ? 93  GLN E NE2 1 
ATOM   5304 N  N   . HIS E  1  94  ? 3.091  47.245  8.515   1.00 61.38  ? 94  HIS E N   1 
ATOM   5305 C  CA  . HIS E  1  94  ? 2.810  46.748  7.170   1.00 60.97  ? 94  HIS E CA  1 
ATOM   5306 C  C   . HIS E  1  94  ? 1.353  46.854  6.696   1.00 61.63  ? 94  HIS E C   1 
ATOM   5307 O  O   . HIS E  1  94  ? 1.099  46.913  5.491   1.00 61.62  ? 94  HIS E O   1 
ATOM   5308 C  CB  . HIS E  1  94  ? 3.293  45.294  7.032   1.00 58.13  ? 94  HIS E CB  1 
ATOM   5309 C  CG  . HIS E  1  94  ? 4.785  45.152  7.006   1.00 58.16  ? 94  HIS E CG  1 
ATOM   5310 N  ND1 . HIS E  1  94  ? 5.560  45.217  8.145   1.00 55.71  ? 94  HIS E ND1 1 
ATOM   5311 C  CD2 . HIS E  1  94  ? 5.646  44.949  5.977   1.00 56.41  ? 94  HIS E CD2 1 
ATOM   5312 C  CE1 . HIS E  1  94  ? 6.831  45.057  7.824   1.00 55.54  ? 94  HIS E CE1 1 
ATOM   5313 N  NE2 . HIS E  1  94  ? 6.913  44.893  6.513   1.00 53.19  ? 94  HIS E NE2 1 
ATOM   5314 N  N   . ASP E  1  95  ? 0.396  46.896  7.622   1.00 63.61  ? 95  ASP E N   1 
ATOM   5315 C  CA  . ASP E  1  95  ? -1.016 46.974  7.229   1.00 64.92  ? 95  ASP E CA  1 
ATOM   5316 C  C   . ASP E  1  95  ? -1.397 48.189  6.384   1.00 66.06  ? 95  ASP E C   1 
ATOM   5317 O  O   . ASP E  1  95  ? -1.879 48.030  5.262   1.00 66.22  ? 95  ASP E O   1 
ATOM   5318 C  CB  . ASP E  1  95  ? -1.934 46.890  8.456   1.00 64.49  ? 95  ASP E CB  1 
ATOM   5319 C  CG  . ASP E  1  95  ? -2.039 45.471  9.021   1.00 65.30  ? 95  ASP E CG  1 
ATOM   5320 O  OD1 . ASP E  1  95  ? -1.923 44.502  8.240   1.00 64.24  ? 95  ASP E OD1 1 
ATOM   5321 O  OD2 . ASP E  1  95  ? -2.258 45.327  10.247  1.00 64.00  ? 95  ASP E OD2 1 
ATOM   5322 N  N   . PRO E  1  96  ? -1.163 49.418  6.886   1.00 67.70  ? 96  PRO E N   1 
ATOM   5323 C  CA  . PRO E  1  96  ? -1.508 50.631  6.123   1.00 67.75  ? 96  PRO E CA  1 
ATOM   5324 C  C   . PRO E  1  96  ? -0.945 50.652  4.708   1.00 67.59  ? 96  PRO E C   1 
ATOM   5325 O  O   . PRO E  1  96  ? -1.149 51.611  3.963   1.00 67.86  ? 96  PRO E O   1 
ATOM   5326 C  CB  . PRO E  1  96  ? -0.924 51.752  6.976   1.00 68.24  ? 96  PRO E CB  1 
ATOM   5327 C  CG  . PRO E  1  96  ? 0.273  51.087  7.619   1.00 69.50  ? 96  PRO E CG  1 
ATOM   5328 C  CD  . PRO E  1  96  ? -0.328 49.767  8.055   1.00 68.50  ? 96  PRO E CD  1 
ATOM   5329 N  N   . ARG E  1  97  ? -0.236 49.591  4.344   1.00 67.51  ? 97  ARG E N   1 
ATOM   5330 C  CA  . ARG E  1  97  ? 0.360  49.505  3.017   1.00 67.34  ? 97  ARG E CA  1 
ATOM   5331 C  C   . ARG E  1  97  ? -0.371 48.517  2.111   1.00 66.63  ? 97  ARG E C   1 
ATOM   5332 O  O   . ARG E  1  97  ? 0.008  48.326  0.946   1.00 66.27  ? 97  ARG E O   1 
ATOM   5333 C  CB  . ARG E  1  97  ? 1.830  49.120  3.155   1.00 67.38  ? 97  ARG E CB  1 
ATOM   5334 C  CG  . ARG E  1  97  ? 2.499  49.810  4.329   1.00 67.53  ? 97  ARG E CG  1 
ATOM   5335 C  CD  . ARG E  1  97  ? 3.988  49.858  4.148   1.00 67.60  ? 97  ARG E CD  1 
ATOM   5336 N  NE  . ARG E  1  97  ? 4.431  51.185  3.732   1.00 67.41  ? 97  ARG E NE  1 
ATOM   5337 C  CZ  . ARG E  1  97  ? 5.035  52.058  4.537   1.00 66.41  ? 97  ARG E CZ  1 
ATOM   5338 N  NH1 . ARG E  1  97  ? 5.273  51.733  5.805   1.00 64.31  ? 97  ARG E NH1 1 
ATOM   5339 N  NH2 . ARG E  1  97  ? 5.404  53.251  4.074   1.00 65.00  ? 97  ARG E NH2 1 
ATOM   5340 N  N   . GLY E  1  98  ? -1.430 47.913  2.654   1.00 65.23  ? 98  GLY E N   1 
ATOM   5341 C  CA  . GLY E  1  98  ? -2.228 46.965  1.898   1.00 63.57  ? 98  GLY E CA  1 
ATOM   5342 C  C   . GLY E  1  98  ? -1.386 46.125  0.966   1.00 62.85  ? 98  GLY E C   1 
ATOM   5343 O  O   . GLY E  1  98  ? -1.369 46.362  -0.237  1.00 63.46  ? 98  GLY E O   1 
ATOM   5344 N  N   . LEU E  1  99  ? -0.674 45.154  1.533   1.00 61.50  ? 99  LEU E N   1 
ATOM   5345 C  CA  . LEU E  1  99  ? 0.202  44.271  0.773   1.00 59.01  ? 99  LEU E CA  1 
ATOM   5346 C  C   . LEU E  1  99  ? -0.454 42.916  0.526   1.00 58.52  ? 99  LEU E C   1 
ATOM   5347 O  O   . LEU E  1  99  ? -1.108 42.345  1.411   1.00 57.57  ? 99  LEU E O   1 
ATOM   5348 C  CB  . LEU E  1  99  ? 1.509  44.058  1.540   1.00 56.87  ? 99  LEU E CB  1 
ATOM   5349 C  CG  . LEU E  1  99  ? 2.317  45.299  1.899   1.00 56.60  ? 99  LEU E CG  1 
ATOM   5350 C  CD1 . LEU E  1  99  ? 3.356  44.956  2.969   1.00 54.14  ? 99  LEU E CD1 1 
ATOM   5351 C  CD2 . LEU E  1  99  ? 2.971  45.848  0.642   1.00 55.09  ? 99  LEU E CD2 1 
ATOM   5352 N  N   . ASP E  1  100 ? -0.269 42.409  -0.688  1.00 57.68  ? 100 ASP E N   1 
ATOM   5353 C  CA  . ASP E  1  100 ? -0.812 41.118  -1.078  1.00 57.52  ? 100 ASP E CA  1 
ATOM   5354 C  C   . ASP E  1  100 ? -0.031 40.078  -0.280  1.00 56.77  ? 100 ASP E C   1 
ATOM   5355 O  O   . ASP E  1  100 ? 1.195  40.043  -0.367  1.00 57.50  ? 100 ASP E O   1 
ATOM   5356 C  CB  . ASP E  1  100 ? -0.576 40.904  -2.575  1.00 58.22  ? 100 ASP E CB  1 
ATOM   5357 C  CG  . ASP E  1  100 ? -1.350 39.726  -3.122  1.00 61.91  ? 100 ASP E CG  1 
ATOM   5358 O  OD1 . ASP E  1  100 ? -1.564 38.754  -2.357  1.00 61.28  ? 100 ASP E OD1 1 
ATOM   5359 O  OD2 . ASP E  1  100 ? -1.734 39.770  -4.319  1.00 64.16  ? 100 ASP E OD2 1 
ATOM   5360 N  N   . ALA E  1  101 ? -0.713 39.236  0.493   1.00 55.67  ? 101 ALA E N   1 
ATOM   5361 C  CA  . ALA E  1  101 ? -0.001 38.238  1.295   1.00 55.56  ? 101 ALA E CA  1 
ATOM   5362 C  C   . ALA E  1  101 ? 0.914  37.336  0.465   1.00 55.42  ? 101 ALA E C   1 
ATOM   5363 O  O   . ALA E  1  101 ? 1.959  36.904  0.949   1.00 57.35  ? 101 ALA E O   1 
ATOM   5364 C  CB  . ALA E  1  101 ? -0.974 37.399  2.099   1.00 54.15  ? 101 ALA E CB  1 
ATOM   5365 N  N   . LEU E  1  102 ? 0.547  37.059  -0.781  1.00 53.24  ? 102 LEU E N   1 
ATOM   5366 C  CA  . LEU E  1  102 ? 1.393  36.213  -1.612  1.00 53.04  ? 102 LEU E CA  1 
ATOM   5367 C  C   . LEU E  1  102 ? 2.858  36.686  -1.649  1.00 52.11  ? 102 LEU E C   1 
ATOM   5368 O  O   . LEU E  1  102 ? 3.776  35.867  -1.742  1.00 52.55  ? 102 LEU E O   1 
ATOM   5369 C  CB  . LEU E  1  102 ? 0.815  36.111  -3.035  1.00 53.29  ? 102 LEU E CB  1 
ATOM   5370 C  CG  . LEU E  1  102 ? -0.463 35.262  -3.188  1.00 55.15  ? 102 LEU E CG  1 
ATOM   5371 C  CD1 . LEU E  1  102 ? -0.921 35.293  -4.628  1.00 53.70  ? 102 LEU E CD1 1 
ATOM   5372 C  CD2 . LEU E  1  102 ? -0.216 33.811  -2.753  1.00 53.73  ? 102 LEU E CD2 1 
ATOM   5373 N  N   . ASN E  1  103 ? 3.084  37.996  -1.557  1.00 49.68  ? 103 ASN E N   1 
ATOM   5374 C  CA  . ASN E  1  103 ? 4.454  38.510  -1.575  1.00 47.60  ? 103 ASN E CA  1 
ATOM   5375 C  C   . ASN E  1  103 ? 5.254  37.928  -0.423  1.00 45.45  ? 103 ASN E C   1 
ATOM   5376 O  O   . ASN E  1  103 ? 6.448  37.655  -0.558  1.00 44.07  ? 103 ASN E O   1 
ATOM   5377 C  CB  . ASN E  1  103 ? 4.479  40.039  -1.476  1.00 47.26  ? 103 ASN E CB  1 
ATOM   5378 C  CG  . ASN E  1  103 ? 4.208  40.710  -2.797  1.00 48.22  ? 103 ASN E CG  1 
ATOM   5379 O  OD1 . ASN E  1  103 ? 3.465  41.685  -2.865  1.00 50.96  ? 103 ASN E OD1 1 
ATOM   5380 N  ND2 . ASN E  1  103 ? 4.813  40.196  -3.862  1.00 47.96  ? 103 ASN E ND2 1 
ATOM   5381 N  N   . PHE E  1  104 ? 4.598  37.745  0.716   1.00 43.24  ? 104 PHE E N   1 
ATOM   5382 C  CA  . PHE E  1  104 ? 5.286  37.194  1.862   1.00 41.80  ? 104 PHE E CA  1 
ATOM   5383 C  C   . PHE E  1  104 ? 5.716  35.760  1.626   1.00 41.30  ? 104 PHE E C   1 
ATOM   5384 O  O   . PHE E  1  104 ? 6.619  35.273  2.302   1.00 41.30  ? 104 PHE E O   1 
ATOM   5385 C  CB  . PHE E  1  104 ? 4.403  37.297  3.107   1.00 43.19  ? 104 PHE E CB  1 
ATOM   5386 C  CG  . PHE E  1  104 ? 4.398  38.674  3.724   1.00 44.09  ? 104 PHE E CG  1 
ATOM   5387 C  CD1 . PHE E  1  104 ? 5.200  38.964  4.830   1.00 41.91  ? 104 PHE E CD1 1 
ATOM   5388 C  CD2 . PHE E  1  104 ? 3.638  39.696  3.171   1.00 42.47  ? 104 PHE E CD2 1 
ATOM   5389 C  CE1 . PHE E  1  104 ? 5.238  40.251  5.367   1.00 43.91  ? 104 PHE E CE1 1 
ATOM   5390 C  CE2 . PHE E  1  104 ? 3.678  40.978  3.704   1.00 41.30  ? 104 PHE E CE2 1 
ATOM   5391 C  CZ  . PHE E  1  104 ? 4.472  41.259  4.796   1.00 42.07  ? 104 PHE E CZ  1 
ATOM   5392 N  N   . VAL E  1  105 ? 5.078  35.086  0.666   1.00 40.64  ? 105 VAL E N   1 
ATOM   5393 C  CA  . VAL E  1  105 ? 5.431  33.706  0.339   1.00 39.28  ? 105 VAL E CA  1 
ATOM   5394 C  C   . VAL E  1  105 ? 6.741  33.762  -0.435  1.00 39.59  ? 105 VAL E C   1 
ATOM   5395 O  O   . VAL E  1  105 ? 7.652  32.971  -0.181  1.00 40.97  ? 105 VAL E O   1 
ATOM   5396 C  CB  . VAL E  1  105 ? 4.345  33.004  -0.536  1.00 39.89  ? 105 VAL E CB  1 
ATOM   5397 C  CG1 . VAL E  1  105 ? 4.839  31.641  -0.998  1.00 38.74  ? 105 VAL E CG1 1 
ATOM   5398 C  CG2 . VAL E  1  105 ? 3.076  32.815  0.253   1.00 41.03  ? 105 VAL E CG2 1 
ATOM   5399 N  N   . VAL E  1  106 ? 6.823  34.699  -1.381  1.00 36.51  ? 106 VAL E N   1 
ATOM   5400 C  CA  . VAL E  1  106 ? 8.028  34.894  -2.178  1.00 36.64  ? 106 VAL E CA  1 
ATOM   5401 C  C   . VAL E  1  106 ? 9.199  35.274  -1.254  1.00 38.00  ? 106 VAL E C   1 
ATOM   5402 O  O   . VAL E  1  106 ? 10.307 34.749  -1.370  1.00 37.23  ? 106 VAL E O   1 
ATOM   5403 C  CB  . VAL E  1  106 ? 7.832  36.030  -3.217  1.00 37.17  ? 106 VAL E CB  1 
ATOM   5404 C  CG1 . VAL E  1  106 ? 9.117  36.279  -3.953  1.00 35.33  ? 106 VAL E CG1 1 
ATOM   5405 C  CG2 . VAL E  1  106 ? 6.728  35.674  -4.201  1.00 35.74  ? 106 VAL E CG2 1 
ATOM   5406 N  N   . PHE E  1  107 ? 8.942  36.183  -0.319  1.00 37.38  ? 107 PHE E N   1 
ATOM   5407 C  CA  . PHE E  1  107 ? 9.972  36.623  0.617   1.00 39.49  ? 107 PHE E CA  1 
ATOM   5408 C  C   . PHE E  1  107 ? 10.596 35.421  1.342   1.00 40.64  ? 107 PHE E C   1 
ATOM   5409 O  O   . PHE E  1  107 ? 11.826 35.338  1.501   1.00 41.22  ? 107 PHE E O   1 
ATOM   5410 C  CB  . PHE E  1  107 ? 9.367  37.594  1.638   1.00 39.39  ? 107 PHE E CB  1 
ATOM   5411 C  CG  . PHE E  1  107 ? 10.353 38.155  2.625   1.00 39.42  ? 107 PHE E CG  1 
ATOM   5412 C  CD1 . PHE E  1  107 ? 10.919 37.360  3.615   1.00 38.17  ? 107 PHE E CD1 1 
ATOM   5413 C  CD2 . PHE E  1  107 ? 10.675 39.517  2.591   1.00 40.98  ? 107 PHE E CD2 1 
ATOM   5414 C  CE1 . PHE E  1  107 ? 11.788 37.920  4.562   1.00 40.60  ? 107 PHE E CE1 1 
ATOM   5415 C  CE2 . PHE E  1  107 ? 11.538 40.074  3.527   1.00 41.05  ? 107 PHE E CE2 1 
ATOM   5416 C  CZ  . PHE E  1  107 ? 12.094 39.277  4.513   1.00 39.58  ? 107 PHE E CZ  1 
ATOM   5417 N  N   . GLY E  1  108 ? 9.737  34.502  1.783   1.00 39.35  ? 108 GLY E N   1 
ATOM   5418 C  CA  . GLY E  1  108 ? 10.190 33.315  2.483   1.00 37.22  ? 108 GLY E CA  1 
ATOM   5419 C  C   . GLY E  1  108 ? 11.046 32.423  1.598   1.00 36.11  ? 108 GLY E C   1 
ATOM   5420 O  O   . GLY E  1  108 ? 12.071 31.869  2.043   1.00 32.69  ? 108 GLY E O   1 
ATOM   5421 N  N   . LYS E  1  109 ? 10.629 32.281  0.343   1.00 35.60  ? 109 LYS E N   1 
ATOM   5422 C  CA  . LYS E  1  109 ? 11.383 31.466  -0.600  1.00 37.64  ? 109 LYS E CA  1 
ATOM   5423 C  C   . LYS E  1  109 ? 12.795 32.063  -0.709  1.00 38.67  ? 109 LYS E C   1 
ATOM   5424 O  O   . LYS E  1  109 ? 13.795 31.343  -0.703  1.00 40.26  ? 109 LYS E O   1 
ATOM   5425 C  CB  . LYS E  1  109 ? 10.689 31.442  -1.971  1.00 39.53  ? 109 LYS E CB  1 
ATOM   5426 C  CG  . LYS E  1  109 ? 9.804  30.201  -2.258  1.00 39.08  ? 109 LYS E CG  1 
ATOM   5427 C  CD  . LYS E  1  109 ? 8.529  30.144  -1.440  1.00 40.25  ? 109 LYS E CD  1 
ATOM   5428 C  CE  . LYS E  1  109 ? 7.715  28.911  -1.770  1.00 38.12  ? 109 LYS E CE  1 
ATOM   5429 N  NZ  . LYS E  1  109 ? 7.353  28.915  -3.191  1.00 37.93  ? 109 LYS E NZ  1 
ATOM   5430 N  N   . ALA E  1  110 ? 12.863 33.389  -0.762  1.00 38.85  ? 110 ALA E N   1 
ATOM   5431 C  CA  . ALA E  1  110 ? 14.128 34.109  -0.869  1.00 37.22  ? 110 ALA E CA  1 
ATOM   5432 C  C   . ALA E  1  110 ? 14.925 33.941  0.418   1.00 35.71  ? 110 ALA E C   1 
ATOM   5433 O  O   . ALA E  1  110 ? 16.151 33.706  0.399   1.00 34.40  ? 110 ALA E O   1 
ATOM   5434 C  CB  . ALA E  1  110 ? 13.861 35.599  -1.134  1.00 38.42  ? 110 ALA E CB  1 
ATOM   5435 N  N   . LEU E  1  111 ? 14.222 34.051  1.536   1.00 33.84  ? 111 LEU E N   1 
ATOM   5436 C  CA  . LEU E  1  111 ? 14.885 33.900  2.819   1.00 35.30  ? 111 LEU E CA  1 
ATOM   5437 C  C   . LEU E  1  111 ? 15.598 32.530  2.859   1.00 35.80  ? 111 LEU E C   1 
ATOM   5438 O  O   . LEU E  1  111 ? 16.786 32.451  3.175   1.00 36.69  ? 111 LEU E O   1 
ATOM   5439 C  CB  . LEU E  1  111 ? 13.881 34.032  3.973   1.00 32.14  ? 111 LEU E CB  1 
ATOM   5440 C  CG  . LEU E  1  111 ? 14.501 33.780  5.353   1.00 34.59  ? 111 LEU E CG  1 
ATOM   5441 C  CD1 . LEU E  1  111 ? 15.607 34.832  5.602   1.00 32.09  ? 111 LEU E CD1 1 
ATOM   5442 C  CD2 . LEU E  1  111 ? 13.426 33.815  6.433   1.00 31.18  ? 111 LEU E CD2 1 
ATOM   5443 N  N   . PHE E  1  112 ? 14.878 31.464  2.504   1.00 34.82  ? 112 PHE E N   1 
ATOM   5444 C  CA  . PHE E  1  112 ? 15.457 30.128  2.497   1.00 34.78  ? 112 PHE E CA  1 
ATOM   5445 C  C   . PHE E  1  112 ? 16.677 29.992  1.574   1.00 34.33  ? 112 PHE E C   1 
ATOM   5446 O  O   . PHE E  1  112 ? 17.734 29.502  2.016   1.00 33.35  ? 112 PHE E O   1 
ATOM   5447 C  CB  . PHE E  1  112 ? 14.396 29.079  2.111   1.00 36.20  ? 112 PHE E CB  1 
ATOM   5448 C  CG  . PHE E  1  112 ? 13.111 29.216  2.873   1.00 35.31  ? 112 PHE E CG  1 
ATOM   5449 C  CD1 . PHE E  1  112 ? 13.101 29.748  4.164   1.00 34.78  ? 112 PHE E CD1 1 
ATOM   5450 C  CD2 . PHE E  1  112 ? 11.916 28.829  2.297   1.00 31.95  ? 112 PHE E CD2 1 
ATOM   5451 C  CE1 . PHE E  1  112 ? 11.907 29.892  4.859   1.00 35.74  ? 112 PHE E CE1 1 
ATOM   5452 C  CE2 . PHE E  1  112 ? 10.727 28.968  2.979   1.00 33.51  ? 112 PHE E CE2 1 
ATOM   5453 C  CZ  . PHE E  1  112 ? 10.713 29.500  4.264   1.00 32.78  ? 112 PHE E CZ  1 
ATOM   5454 N  N   . ALA E  1  113 ? 16.540 30.417  0.313   1.00 31.01  ? 113 ALA E N   1 
ATOM   5455 C  CA  . ALA E  1  113 ? 17.650 30.327  -0.642  1.00 31.57  ? 113 ALA E CA  1 
ATOM   5456 C  C   . ALA E  1  113 ? 18.871 31.131  -0.185  1.00 32.66  ? 113 ALA E C   1 
ATOM   5457 O  O   . ALA E  1  113 ? 20.017 30.723  -0.424  1.00 30.15  ? 113 ALA E O   1 
ATOM   5458 C  CB  . ALA E  1  113 ? 17.218 30.793  -2.022  1.00 32.13  ? 113 ALA E CB  1 
ATOM   5459 N  N   . THR E  1  114 ? 18.626 32.259  0.491   1.00 32.94  ? 114 THR E N   1 
ATOM   5460 C  CA  . THR E  1  114 ? 19.731 33.062  0.981   1.00 33.39  ? 114 THR E CA  1 
ATOM   5461 C  C   . THR E  1  114 ? 20.389 32.443  2.209   1.00 33.64  ? 114 THR E C   1 
ATOM   5462 O  O   . THR E  1  114 ? 21.611 32.305  2.249   1.00 35.83  ? 114 THR E O   1 
ATOM   5463 C  CB  . THR E  1  114 ? 19.315 34.505  1.330   1.00 33.88  ? 114 THR E CB  1 
ATOM   5464 O  OG1 . THR E  1  114 ? 18.750 35.145  0.176   1.00 33.73  ? 114 THR E OG1 1 
ATOM   5465 C  CG2 . THR E  1  114 ? 20.544 35.295  1.808   1.00 31.39  ? 114 THR E CG2 1 
ATOM   5466 N  N   . VAL E  1  115 ? 19.598 32.072  3.214   1.00 32.95  ? 115 VAL E N   1 
ATOM   5467 C  CA  . VAL E  1  115 ? 20.160 31.462  4.425   1.00 32.31  ? 115 VAL E CA  1 
ATOM   5468 C  C   . VAL E  1  115 ? 20.763 30.089  4.075   1.00 32.92  ? 115 VAL E C   1 
ATOM   5469 O  O   . VAL E  1  115 ? 21.851 29.729  4.539   1.00 32.16  ? 115 VAL E O   1 
ATOM   5470 C  CB  . VAL E  1  115 ? 19.076 31.271  5.542   1.00 33.10  ? 115 VAL E CB  1 
ATOM   5471 C  CG1 . VAL E  1  115 ? 19.709 30.565  6.746   1.00 32.10  ? 115 VAL E CG1 1 
ATOM   5472 C  CG2 . VAL E  1  115 ? 18.475 32.635  5.972   1.00 27.04  ? 115 VAL E CG2 1 
ATOM   5473 N  N   . GLY E  1  116 ? 20.051 29.324  3.255   1.00 33.07  ? 116 GLY E N   1 
ATOM   5474 C  CA  . GLY E  1  116 ? 20.555 28.026  2.851   1.00 30.30  ? 116 GLY E CA  1 
ATOM   5475 C  C   . GLY E  1  116 ? 21.836 28.172  2.045   1.00 29.60  ? 116 GLY E C   1 
ATOM   5476 O  O   . GLY E  1  116 ? 22.812 27.465  2.291   1.00 28.33  ? 116 GLY E O   1 
ATOM   5477 N  N   . GLY E  1  117 ? 21.835 29.090  1.076   1.00 30.33  ? 117 GLY E N   1 
ATOM   5478 C  CA  . GLY E  1  117 ? 23.010 29.310  0.237   1.00 30.00  ? 117 GLY E CA  1 
ATOM   5479 C  C   . GLY E  1  117 ? 24.243 29.687  1.052   1.00 32.71  ? 117 GLY E C   1 
ATOM   5480 O  O   . GLY E  1  117 ? 25.365 29.330  0.699   1.00 31.35  ? 117 GLY E O   1 
ATOM   5481 N  N   . GLN E  1  118 ? 24.035 30.381  2.159   1.00 33.30  ? 118 GLN E N   1 
ATOM   5482 C  CA  . GLN E  1  118 ? 25.137 30.809  3.014   1.00 35.29  ? 118 GLN E CA  1 
ATOM   5483 C  C   . GLN E  1  118 ? 25.497 29.724  4.033   1.00 34.50  ? 118 GLN E C   1 
ATOM   5484 O  O   . GLN E  1  118 ? 26.675 29.471  4.299   1.00 35.35  ? 118 GLN E O   1 
ATOM   5485 C  CB  . GLN E  1  118 ? 24.728 32.102  3.738   1.00 38.43  ? 118 GLN E CB  1 
ATOM   5486 C  CG  . GLN E  1  118 ? 25.856 32.950  4.295   1.00 46.71  ? 118 GLN E CG  1 
ATOM   5487 C  CD  . GLN E  1  118 ? 26.871 33.333  3.245   1.00 48.63  ? 118 GLN E CD  1 
ATOM   5488 O  OE1 . GLN E  1  118 ? 26.527 33.873  2.198   1.00 51.10  ? 118 GLN E OE1 1 
ATOM   5489 N  NE2 . GLN E  1  118 ? 28.137 33.041  3.518   1.00 50.69  ? 118 GLN E NE2 1 
ATOM   5490 N  N   . PHE E  1  119 ? 24.479 29.082  4.605   1.00 32.65  ? 119 PHE E N   1 
ATOM   5491 C  CA  . PHE E  1  119 ? 24.695 28.045  5.625   1.00 30.62  ? 119 PHE E CA  1 
ATOM   5492 C  C   . PHE E  1  119 ? 25.287 26.760  5.021   1.00 29.54  ? 119 PHE E C   1 
ATOM   5493 O  O   . PHE E  1  119 ? 26.128 26.102  5.638   1.00 28.81  ? 119 PHE E O   1 
ATOM   5494 C  CB  . PHE E  1  119 ? 23.366 27.707  6.347   1.00 30.08  ? 119 PHE E CB  1 
ATOM   5495 C  CG  . PHE E  1  119 ? 23.536 26.832  7.559   1.00 29.23  ? 119 PHE E CG  1 
ATOM   5496 C  CD1 . PHE E  1  119 ? 23.993 27.357  8.759   1.00 30.25  ? 119 PHE E CD1 1 
ATOM   5497 C  CD2 . PHE E  1  119 ? 23.281 25.464  7.483   1.00 30.53  ? 119 PHE E CD2 1 
ATOM   5498 C  CE1 . PHE E  1  119 ? 24.194 26.529  9.861   1.00 30.91  ? 119 PHE E CE1 1 
ATOM   5499 C  CE2 . PHE E  1  119 ? 23.479 24.621  8.577   1.00 27.71  ? 119 PHE E CE2 1 
ATOM   5500 C  CZ  . PHE E  1  119 ? 23.936 25.151  9.764   1.00 29.17  ? 119 PHE E CZ  1 
ATOM   5501 N  N   . GLY E  1  120 ? 24.845 26.418  3.822   1.00 27.60  ? 120 GLY E N   1 
ATOM   5502 C  CA  . GLY E  1  120 ? 25.337 25.221  3.191   1.00 26.91  ? 120 GLY E CA  1 
ATOM   5503 C  C   . GLY E  1  120 ? 24.348 24.069  3.272   1.00 28.48  ? 120 GLY E C   1 
ATOM   5504 O  O   . GLY E  1  120 ? 23.202 24.218  3.676   1.00 26.43  ? 120 GLY E O   1 
ATOM   5505 N  N   . VAL E  1  121 ? 24.842 22.896  2.903   1.00 30.40  ? 121 VAL E N   1 
ATOM   5506 C  CA  . VAL E  1  121 ? 24.086 21.668  2.855   1.00 32.18  ? 121 VAL E CA  1 
ATOM   5507 C  C   . VAL E  1  121 ? 23.270 21.214  4.077   1.00 32.20  ? 121 VAL E C   1 
ATOM   5508 O  O   . VAL E  1  121 ? 22.242 20.572  3.916   1.00 33.39  ? 121 VAL E O   1 
ATOM   5509 C  CB  . VAL E  1  121 ? 25.034 20.562  2.361   1.00 32.68  ? 121 VAL E CB  1 
ATOM   5510 C  CG1 . VAL E  1  121 ? 24.517 19.194  2.691   1.00 36.39  ? 121 VAL E CG1 1 
ATOM   5511 C  CG2 . VAL E  1  121 ? 25.205 20.725  0.860   1.00 31.90  ? 121 VAL E CG2 1 
ATOM   5512 N  N   . CYS E  1  122 ? 23.667 21.551  5.296   1.00 33.77  ? 122 CYS E N   1 
ATOM   5513 C  CA  . CYS E  1  122 ? 22.850 21.103  6.439   1.00 36.17  ? 122 CYS E CA  1 
ATOM   5514 C  C   . CYS E  1  122 ? 21.704 22.023  6.816   1.00 35.98  ? 122 CYS E C   1 
ATOM   5515 O  O   . CYS E  1  122 ? 21.185 21.965  7.932   1.00 32.67  ? 122 CYS E O   1 
ATOM   5516 C  CB  . CYS E  1  122 ? 23.699 20.834  7.650   1.00 39.62  ? 122 CYS E CB  1 
ATOM   5517 S  SG  . CYS E  1  122 ? 25.016 19.676  7.214   1.00 43.53  ? 122 CYS E SG  1 
ATOM   5518 N  N   . PHE E  1  123 ? 21.334 22.886  5.875   1.00 36.36  ? 123 PHE E N   1 
ATOM   5519 C  CA  . PHE E  1  123 ? 20.234 23.817  6.045   1.00 35.88  ? 123 PHE E CA  1 
ATOM   5520 C  C   . PHE E  1  123 ? 18.964 22.950  6.211   1.00 36.39  ? 123 PHE E C   1 
ATOM   5521 O  O   . PHE E  1  123 ? 18.743 21.994  5.473   1.00 33.15  ? 123 PHE E O   1 
ATOM   5522 C  CB  . PHE E  1  123 ? 20.157 24.696  4.790   1.00 37.67  ? 123 PHE E CB  1 
ATOM   5523 C  CG  . PHE E  1  123 ? 18.967 25.621  4.747   1.00 39.08  ? 123 PHE E CG  1 
ATOM   5524 C  CD1 . PHE E  1  123 ? 18.818 26.641  5.684   1.00 39.63  ? 123 PHE E CD1 1 
ATOM   5525 C  CD2 . PHE E  1  123 ? 17.996 25.468  3.750   1.00 39.45  ? 123 PHE E CD2 1 
ATOM   5526 C  CE1 . PHE E  1  123 ? 17.711 27.507  5.637   1.00 41.18  ? 123 PHE E CE1 1 
ATOM   5527 C  CE2 . PHE E  1  123 ? 16.879 26.325  3.684   1.00 40.55  ? 123 PHE E CE2 1 
ATOM   5528 C  CZ  . PHE E  1  123 ? 16.735 27.348  4.633   1.00 41.47  ? 123 PHE E CZ  1 
ATOM   5529 N  N   . ASP E  1  124 ? 18.153 23.276  7.208   1.00 38.02  ? 124 ASP E N   1 
ATOM   5530 C  CA  . ASP E  1  124 ? 16.931 22.545  7.505   1.00 38.03  ? 124 ASP E CA  1 
ATOM   5531 C  C   . ASP E  1  124 ? 15.705 23.252  6.892   1.00 37.40  ? 124 ASP E C   1 
ATOM   5532 O  O   . ASP E  1  124 ? 14.965 23.950  7.582   1.00 37.02  ? 124 ASP E O   1 
ATOM   5533 C  CB  . ASP E  1  124 ? 16.775 22.439  9.036   1.00 38.81  ? 124 ASP E CB  1 
ATOM   5534 C  CG  . ASP E  1  124 ? 15.721 21.412  9.457   1.00 41.85  ? 124 ASP E CG  1 
ATOM   5535 O  OD1 . ASP E  1  124 ? 14.796 21.128  8.647   1.00 42.14  ? 124 ASP E OD1 1 
ATOM   5536 O  OD2 . ASP E  1  124 ? 15.813 20.901  10.610  1.00 39.77  ? 124 ASP E OD2 1 
ATOM   5537 N  N   . LEU E  1  125 ? 15.488 23.064  5.595   1.00 36.25  ? 125 LEU E N   1 
ATOM   5538 C  CA  . LEU E  1  125 ? 14.361 23.693  4.899   1.00 35.11  ? 125 LEU E CA  1 
ATOM   5539 C  C   . LEU E  1  125 ? 12.997 23.448  5.561   1.00 35.63  ? 125 LEU E C   1 
ATOM   5540 O  O   . LEU E  1  125 ? 12.190 24.362  5.688   1.00 36.63  ? 125 LEU E O   1 
ATOM   5541 C  CB  . LEU E  1  125 ? 14.338 23.241  3.426   1.00 30.55  ? 125 LEU E CB  1 
ATOM   5542 C  CG  . LEU E  1  125 ? 13.221 23.668  2.453   1.00 29.02  ? 125 LEU E CG  1 
ATOM   5543 C  CD1 . LEU E  1  125 ? 12.966 25.161  2.465   1.00 23.94  ? 125 LEU E CD1 1 
ATOM   5544 C  CD2 . LEU E  1  125 ? 13.628 23.230  1.052   1.00 26.28  ? 125 LEU E CD2 1 
ATOM   5545 N  N   . PRO E  1  126 ? 12.718 22.211  5.985   1.00 36.40  ? 126 PRO E N   1 
ATOM   5546 C  CA  . PRO E  1  126 ? 11.411 22.017  6.618   1.00 36.01  ? 126 PRO E CA  1 
ATOM   5547 C  C   . PRO E  1  126 ? 11.238 22.879  7.878   1.00 36.40  ? 126 PRO E C   1 
ATOM   5548 O  O   . PRO E  1  126 ? 10.185 23.478  8.099   1.00 36.42  ? 126 PRO E O   1 
ATOM   5549 C  CB  . PRO E  1  126 ? 11.397 20.523  6.924   1.00 34.71  ? 126 PRO E CB  1 
ATOM   5550 C  CG  . PRO E  1  126 ? 12.205 19.949  5.791   1.00 37.99  ? 126 PRO E CG  1 
ATOM   5551 C  CD  . PRO E  1  126 ? 13.359 20.917  5.680   1.00 37.40  ? 126 PRO E CD  1 
ATOM   5552 N  N   . ALA E  1  127 ? 12.274 22.954  8.697   1.00 37.18  ? 127 ALA E N   1 
ATOM   5553 C  CA  . ALA E  1  127 ? 12.171 23.742  9.911   1.00 38.95  ? 127 ALA E CA  1 
ATOM   5554 C  C   . ALA E  1  127 ? 11.941 25.200  9.574   1.00 40.19  ? 127 ALA E C   1 
ATOM   5555 O  O   . ALA E  1  127 ? 11.148 25.892  10.216  1.00 40.36  ? 127 ALA E O   1 
ATOM   5556 C  CB  . ALA E  1  127 ? 13.429 23.606  10.741  1.00 40.04  ? 127 ALA E CB  1 
ATOM   5557 N  N   . TRP E  1  128 ? 12.658 25.668  8.568   1.00 39.56  ? 128 TRP E N   1 
ATOM   5558 C  CA  . TRP E  1  128 ? 12.536 27.041  8.159   1.00 39.53  ? 128 TRP E CA  1 
ATOM   5559 C  C   . TRP E  1  128 ? 11.172 27.343  7.545   1.00 39.98  ? 128 TRP E C   1 
ATOM   5560 O  O   . TRP E  1  128 ? 10.612 28.396  7.809   1.00 40.66  ? 128 TRP E O   1 
ATOM   5561 C  CB  . TRP E  1  128 ? 13.659 27.381  7.187   1.00 40.71  ? 128 TRP E CB  1 
ATOM   5562 C  CG  . TRP E  1  128 ? 14.924 27.740  7.879   1.00 39.74  ? 128 TRP E CG  1 
ATOM   5563 C  CD1 . TRP E  1  128 ? 15.893 26.900  8.315   1.00 40.66  ? 128 TRP E CD1 1 
ATOM   5564 C  CD2 . TRP E  1  128 ? 15.327 29.056  8.269   1.00 41.11  ? 128 TRP E CD2 1 
ATOM   5565 N  NE1 . TRP E  1  128 ? 16.885 27.609  8.960   1.00 41.42  ? 128 TRP E NE1 1 
ATOM   5566 C  CE2 . TRP E  1  128 ? 16.557 28.938  8.943   1.00 41.16  ? 128 TRP E CE2 1 
ATOM   5567 C  CE3 . TRP E  1  128 ? 14.765 30.327  8.111   1.00 39.74  ? 128 TRP E CE3 1 
ATOM   5568 C  CZ2 . TRP E  1  128 ? 17.234 30.040  9.461   1.00 39.96  ? 128 TRP E CZ2 1 
ATOM   5569 C  CZ3 . TRP E  1  128 ? 15.439 31.420  8.629   1.00 39.42  ? 128 TRP E CZ3 1 
ATOM   5570 C  CH2 . TRP E  1  128 ? 16.653 31.270  9.293   1.00 39.27  ? 128 TRP E CH2 1 
ATOM   5571 N  N   . GLU E  1  129 ? 10.627 26.435  6.737   1.00 38.78  ? 129 GLU E N   1 
ATOM   5572 C  CA  . GLU E  1  129 ? 9.324  26.684  6.146   1.00 40.48  ? 129 GLU E CA  1 
ATOM   5573 C  C   . GLU E  1  129 ? 8.275  26.804  7.253   1.00 40.93  ? 129 GLU E C   1 
ATOM   5574 O  O   . GLU E  1  129 ? 7.410  27.677  7.207   1.00 39.24  ? 129 GLU E O   1 
ATOM   5575 C  CB  . GLU E  1  129 ? 8.942  25.553  5.193   1.00 39.84  ? 129 GLU E CB  1 
ATOM   5576 C  CG  . GLU E  1  129 ? 9.765  25.499  3.942   1.00 40.92  ? 129 GLU E CG  1 
ATOM   5577 C  CD  . GLU E  1  129 ? 9.431  24.306  3.081   1.00 43.15  ? 129 GLU E CD  1 
ATOM   5578 O  OE1 . GLU E  1  129 ? 9.077  23.241  3.639   1.00 43.75  ? 129 GLU E OE1 1 
ATOM   5579 O  OE2 . GLU E  1  129 ? 9.538  24.433  1.842   1.00 46.45  ? 129 GLU E OE2 1 
ATOM   5580 N  N   . SER E  1  130 ? 8.370  25.931  8.247   1.00 42.60  ? 130 SER E N   1 
ATOM   5581 C  CA  . SER E  1  130 ? 7.430  25.931  9.361   1.00 46.46  ? 130 SER E CA  1 
ATOM   5582 C  C   . SER E  1  130 ? 7.527  27.163  10.238  1.00 47.51  ? 130 SER E C   1 
ATOM   5583 O  O   . SER E  1  130 ? 6.512  27.778  10.559  1.00 49.21  ? 130 SER E O   1 
ATOM   5584 C  CB  . SER E  1  130 ? 7.642  24.716  10.260  1.00 48.15  ? 130 SER E CB  1 
ATOM   5585 O  OG  . SER E  1  130 ? 7.432  23.523  9.542   1.00 55.27  ? 130 SER E OG  1 
ATOM   5586 N  N   . CYS E  1  131 ? 8.734  27.511  10.657  1.00 48.03  ? 131 CYS E N   1 
ATOM   5587 C  CA  . CYS E  1  131 ? 8.883  28.661  11.520  1.00 49.42  ? 131 CYS E CA  1 
ATOM   5588 C  C   . CYS E  1  131 ? 8.688  29.979  10.784  1.00 48.93  ? 131 CYS E C   1 
ATOM   5589 O  O   . CYS E  1  131 ? 8.190  30.950  11.360  1.00 49.17  ? 131 CYS E O   1 
ATOM   5590 C  CB  . CYS E  1  131 ? 10.227 28.599  12.236  1.00 52.35  ? 131 CYS E CB  1 
ATOM   5591 S  SG  . CYS E  1  131 ? 10.308 27.259  13.469  1.00 57.67  ? 131 CYS E SG  1 
ATOM   5592 N  N   . TYR E  1  132 ? 9.050  30.029  9.504   1.00 46.21  ? 132 TYR E N   1 
ATOM   5593 C  CA  . TYR E  1  132 ? 8.841  31.273  8.794   1.00 46.60  ? 132 TYR E CA  1 
ATOM   5594 C  C   . TYR E  1  132 ? 7.352  31.562  8.750   1.00 47.56  ? 132 TYR E C   1 
ATOM   5595 O  O   . TYR E  1  132 ? 6.930  32.726  8.736   1.00 48.06  ? 132 TYR E O   1 
ATOM   5596 C  CB  . TYR E  1  132 ? 9.379  31.215  7.370   1.00 45.67  ? 132 TYR E CB  1 
ATOM   5597 C  CG  . TYR E  1  132 ? 9.012  32.451  6.585   1.00 44.26  ? 132 TYR E CG  1 
ATOM   5598 C  CD1 . TYR E  1  132 ? 7.972  32.434  5.662   1.00 42.86  ? 132 TYR E CD1 1 
ATOM   5599 C  CD2 . TYR E  1  132 ? 9.688  33.644  6.789   1.00 43.96  ? 132 TYR E CD2 1 
ATOM   5600 C  CE1 . TYR E  1  132 ? 7.622  33.576  4.952   1.00 43.00  ? 132 TYR E CE1 1 
ATOM   5601 C  CE2 . TYR E  1  132 ? 9.346  34.798  6.088   1.00 43.94  ? 132 TYR E CE2 1 
ATOM   5602 C  CZ  . TYR E  1  132 ? 8.314  34.753  5.170   1.00 43.76  ? 132 TYR E CZ  1 
ATOM   5603 O  OH  . TYR E  1  132 ? 7.968  35.875  4.453   1.00 40.99  ? 132 TYR E OH  1 
ATOM   5604 N  N   . LYS E  1  133 ? 6.563  30.491  8.713   1.00 48.46  ? 133 LYS E N   1 
ATOM   5605 C  CA  . LYS E  1  133 ? 5.118  30.607  8.674   1.00 49.69  ? 133 LYS E CA  1 
ATOM   5606 C  C   . LYS E  1  133 ? 4.653  31.393  9.881   1.00 49.05  ? 133 LYS E C   1 
ATOM   5607 O  O   . LYS E  1  133 ? 3.773  32.247  9.755   1.00 49.40  ? 133 LYS E O   1 
ATOM   5608 C  CB  . LYS E  1  133 ? 4.471  29.234  8.689   1.00 53.06  ? 133 LYS E CB  1 
ATOM   5609 C  CG  . LYS E  1  133 ? 4.171  28.677  7.327   1.00 56.83  ? 133 LYS E CG  1 
ATOM   5610 C  CD  . LYS E  1  133 ? 3.401  27.382  7.483   1.00 62.07  ? 133 LYS E CD  1 
ATOM   5611 C  CE  . LYS E  1  133 ? 3.026  26.765  6.139   1.00 65.91  ? 133 LYS E CE  1 
ATOM   5612 N  NZ  . LYS E  1  133 ? 2.343  25.446  6.323   1.00 67.09  ? 133 LYS E NZ  1 
ATOM   5613 N  N   . VAL E  1  134 ? 5.246  31.109  11.042  1.00 45.46  ? 134 VAL E N   1 
ATOM   5614 C  CA  . VAL E  1  134 ? 4.870  31.826  12.242  1.00 43.60  ? 134 VAL E CA  1 
ATOM   5615 C  C   . VAL E  1  134 ? 5.100  33.307  12.014  1.00 44.03  ? 134 VAL E C   1 
ATOM   5616 O  O   . VAL E  1  134 ? 4.222  34.115  12.281  1.00 45.51  ? 134 VAL E O   1 
ATOM   5617 C  CB  . VAL E  1  134 ? 5.670  31.341  13.487  1.00 44.35  ? 134 VAL E CB  1 
ATOM   5618 C  CG1 . VAL E  1  134 ? 5.414  32.252  14.698  1.00 39.05  ? 134 VAL E CG1 1 
ATOM   5619 C  CG2 . VAL E  1  134 ? 5.266  29.911  13.823  1.00 42.50  ? 134 VAL E CG2 1 
ATOM   5620 N  N   . ILE E  1  135 ? 6.259  33.674  11.487  1.00 44.22  ? 135 ILE E N   1 
ATOM   5621 C  CA  . ILE E  1  135 ? 6.520  35.086  11.271  1.00 45.96  ? 135 ILE E CA  1 
ATOM   5622 C  C   . ILE E  1  135 ? 5.497  35.714  10.320  1.00 46.17  ? 135 ILE E C   1 
ATOM   5623 O  O   . ILE E  1  135 ? 4.862  36.718  10.645  1.00 46.68  ? 135 ILE E O   1 
ATOM   5624 C  CB  . ILE E  1  135 ? 7.953  35.313  10.737  1.00 45.17  ? 135 ILE E CB  1 
ATOM   5625 C  CG1 . ILE E  1  135 ? 8.969  34.765  11.755  1.00 46.95  ? 135 ILE E CG1 1 
ATOM   5626 C  CG2 . ILE E  1  135 ? 8.182  36.810  10.496  1.00 43.34  ? 135 ILE E CG2 1 
ATOM   5627 C  CD1 . ILE E  1  135 ? 10.435 34.819  11.296  1.00 45.86  ? 135 ILE E CD1 1 
ATOM   5628 N  N   . ALA E  1  136 ? 5.337  35.110  9.152   1.00 46.44  ? 136 ALA E N   1 
ATOM   5629 C  CA  . ALA E  1  136 ? 4.407  35.617  8.157   1.00 47.99  ? 136 ALA E CA  1 
ATOM   5630 C  C   . ALA E  1  136 ? 2.997  35.731  8.727   1.00 49.00  ? 136 ALA E C   1 
ATOM   5631 O  O   . ALA E  1  136 ? 2.303  36.721  8.497   1.00 50.08  ? 136 ALA E O   1 
ATOM   5632 C  CB  . ALA E  1  136 ? 4.418  34.709  6.927   1.00 46.83  ? 136 ALA E CB  1 
ATOM   5633 N  N   . MET E  1  137 ? 2.569  34.709  9.462   1.00 49.29  ? 137 MET E N   1 
ATOM   5634 C  CA  . MET E  1  137 ? 1.240  34.714  10.064  1.00 48.21  ? 137 MET E CA  1 
ATOM   5635 C  C   . MET E  1  137 ? 1.160  35.869  11.048  1.00 45.69  ? 137 MET E C   1 
ATOM   5636 O  O   . MET E  1  137 ? 0.165  36.573  11.106  1.00 46.82  ? 137 MET E O   1 
ATOM   5637 C  CB  . MET E  1  137 ? 0.966  33.388  10.799  1.00 50.27  ? 137 MET E CB  1 
ATOM   5638 C  CG  . MET E  1  137 ? -0.303 33.375  11.662  1.00 49.75  ? 137 MET E CG  1 
ATOM   5639 S  SD  . MET E  1  137 ? -1.797 33.831  10.755  1.00 49.38  ? 137 MET E SD  1 
ATOM   5640 C  CE  . MET E  1  137 ? -2.217 32.169  10.018  1.00 51.41  ? 137 MET E CE  1 
ATOM   5641 N  N   . GLY E  1  138 ? 2.217  36.057  11.818  1.00 43.17  ? 138 GLY E N   1 
ATOM   5642 C  CA  . GLY E  1  138 ? 2.230  37.124  12.788  1.00 43.04  ? 138 GLY E CA  1 
ATOM   5643 C  C   . GLY E  1  138 ? 2.229  38.515  12.179  1.00 44.88  ? 138 GLY E C   1 
ATOM   5644 O  O   . GLY E  1  138 ? 1.714  39.459  12.789  1.00 41.18  ? 138 GLY E O   1 
ATOM   5645 N  N   . ILE E  1  139 ? 2.786  38.653  10.974  1.00 45.72  ? 139 ILE E N   1 
ATOM   5646 C  CA  . ILE E  1  139 ? 2.853  39.958  10.324  1.00 48.16  ? 139 ILE E CA  1 
ATOM   5647 C  C   . ILE E  1  139 ? 1.659  40.288  9.429   1.00 50.18  ? 139 ILE E C   1 
ATOM   5648 O  O   . ILE E  1  139 ? 1.178  41.414  9.429   1.00 51.91  ? 139 ILE E O   1 
ATOM   5649 C  CB  . ILE E  1  139 ? 4.167  40.089  9.496   1.00 47.19  ? 139 ILE E CB  1 
ATOM   5650 C  CG1 . ILE E  1  139 ? 5.363  39.929  10.435  1.00 46.44  ? 139 ILE E CG1 1 
ATOM   5651 C  CG2 . ILE E  1  139 ? 4.223  41.436  8.754   1.00 44.20  ? 139 ILE E CG2 1 
ATOM   5652 C  CD1 . ILE E  1  139 ? 6.716  40.102  9.781   1.00 48.26  ? 139 ILE E CD1 1 
ATOM   5653 N  N   . THR E  1  140 ? 1.174  39.303  8.684   1.00 51.26  ? 140 THR E N   1 
ATOM   5654 C  CA  . THR E  1  140 ? 0.075  39.513  7.755   1.00 53.04  ? 140 THR E CA  1 
ATOM   5655 C  C   . THR E  1  140 ? -1.271 39.063  8.301   1.00 55.35  ? 140 THR E C   1 
ATOM   5656 O  O   . THR E  1  140 ? -2.292 39.678  8.016   1.00 54.64  ? 140 THR E O   1 
ATOM   5657 C  CB  . THR E  1  140 ? 0.323  38.738  6.467   1.00 52.02  ? 140 THR E CB  1 
ATOM   5658 O  OG1 . THR E  1  140 ? 0.254  37.335  6.747   1.00 54.05  ? 140 THR E OG1 1 
ATOM   5659 C  CG2 . THR E  1  140 ? 1.699  39.040  5.928   1.00 51.62  ? 140 THR E CG2 1 
ATOM   5660 N  N   . GLY E  1  141 ? -1.272 37.982  9.065   1.00 57.45  ? 141 GLY E N   1 
ATOM   5661 C  CA  . GLY E  1  141 ? -2.522 37.485  9.610   1.00 59.28  ? 141 GLY E CA  1 
ATOM   5662 C  C   . GLY E  1  141 ? -3.241 36.558  8.647   1.00 60.70  ? 141 GLY E C   1 
ATOM   5663 O  O   . GLY E  1  141 ? -4.090 35.773  9.055   1.00 60.37  ? 141 GLY E O   1 
ATOM   5664 N  N   . ASN E  1  142 ? -2.902 36.646  7.365   1.00 62.25  ? 142 ASN E N   1 
ATOM   5665 C  CA  . ASN E  1  142 ? -3.522 35.805  6.359   1.00 64.44  ? 142 ASN E CA  1 
ATOM   5666 C  C   . ASN E  1  142 ? -3.333 34.330  6.740   1.00 67.02  ? 142 ASN E C   1 
ATOM   5667 O  O   . ASN E  1  142 ? -2.205 33.856  6.839   1.00 68.44  ? 142 ASN E O   1 
ATOM   5668 C  CB  . ASN E  1  142 ? -2.897 36.100  4.997   1.00 63.64  ? 142 ASN E CB  1 
ATOM   5669 C  CG  . ASN E  1  142 ? -3.687 35.503  3.862   1.00 64.29  ? 142 ASN E CG  1 
ATOM   5670 O  OD1 . ASN E  1  142 ? -3.971 34.311  3.868   1.00 64.61  ? 142 ASN E OD1 1 
ATOM   5671 N  ND2 . ASN E  1  142 ? -4.055 36.325  2.880   1.00 64.29  ? 142 ASN E ND2 1 
ATOM   5672 N  N   . ASP E  1  143 ? -4.439 33.615  6.955   1.00 69.97  ? 143 ASP E N   1 
ATOM   5673 C  CA  . ASP E  1  143 ? -4.415 32.201  7.360   1.00 71.83  ? 143 ASP E CA  1 
ATOM   5674 C  C   . ASP E  1  143 ? -3.764 31.288  6.325   1.00 72.21  ? 143 ASP E C   1 
ATOM   5675 O  O   . ASP E  1  143 ? -3.753 30.059  6.464   1.00 72.37  ? 143 ASP E O   1 
ATOM   5676 C  CB  . ASP E  1  143 ? -5.830 31.709  7.686   1.00 74.18  ? 143 ASP E CB  1 
ATOM   5677 C  CG  . ASP E  1  143 ? -6.772 31.827  6.512   1.00 77.50  ? 143 ASP E CG  1 
ATOM   5678 O  OD1 . ASP E  1  143 ? -7.958 31.444  6.652   1.00 79.03  ? 143 ASP E OD1 1 
ATOM   5679 O  OD2 . ASP E  1  143 ? -6.328 32.303  5.447   1.00 78.47  ? 143 ASP E OD2 1 
ATOM   5680 N  N   . MET E  1  144 ? -3.233 31.913  5.284   1.00 71.05  ? 144 MET E N   1 
ATOM   5681 C  CA  . MET E  1  144 ? -2.522 31.226  4.222   1.00 68.80  ? 144 MET E CA  1 
ATOM   5682 C  C   . MET E  1  144 ? -1.230 30.743  4.883   1.00 68.55  ? 144 MET E C   1 
ATOM   5683 O  O   . MET E  1  144 ? -0.540 29.866  4.364   1.00 68.66  ? 144 MET E O   1 
ATOM   5684 C  CB  . MET E  1  144 ? -2.225 32.242  3.128   1.00 68.41  ? 144 MET E CB  1 
ATOM   5685 C  CG  . MET E  1  144 ? -1.201 31.861  2.101   1.00 68.85  ? 144 MET E CG  1 
ATOM   5686 S  SD  . MET E  1  144 ? -0.528 33.383  1.383   1.00 67.74  ? 144 MET E SD  1 
ATOM   5687 C  CE  . MET E  1  144 ? -1.948 33.989  0.457   1.00 68.93  ? 144 MET E CE  1 
ATOM   5688 N  N   . PHE E  1  145 ? -0.932 31.334  6.040   1.00 67.66  ? 145 PHE E N   1 
ATOM   5689 C  CA  . PHE E  1  145 ? 0.260  31.026  6.824   1.00 68.33  ? 145 PHE E CA  1 
ATOM   5690 C  C   . PHE E  1  145 ? -0.124 30.282  8.084   1.00 70.04  ? 145 PHE E C   1 
ATOM   5691 O  O   . PHE E  1  145 ? 0.613  30.271  9.073   1.00 69.35  ? 145 PHE E O   1 
ATOM   5692 C  CB  . PHE E  1  145 ? 1.000  32.318  7.186   1.00 66.03  ? 145 PHE E CB  1 
ATOM   5693 C  CG  . PHE E  1  145 ? 1.439  33.107  5.985   1.00 64.53  ? 145 PHE E CG  1 
ATOM   5694 C  CD1 . PHE E  1  145 ? 0.890  34.359  5.715   1.00 63.11  ? 145 PHE E CD1 1 
ATOM   5695 C  CD2 . PHE E  1  145 ? 2.374  32.580  5.096   1.00 61.99  ? 145 PHE E CD2 1 
ATOM   5696 C  CE1 . PHE E  1  145 ? 1.264  35.080  4.575   1.00 62.47  ? 145 PHE E CE1 1 
ATOM   5697 C  CE2 . PHE E  1  145 ? 2.753  33.292  3.948   1.00 61.16  ? 145 PHE E CE2 1 
ATOM   5698 C  CZ  . PHE E  1  145 ? 2.197  34.546  3.687   1.00 60.37  ? 145 PHE E CZ  1 
ATOM   5699 N  N   . SER E  1  146 ? -1.293 29.656  8.028   1.00 72.53  ? 146 SER E N   1 
ATOM   5700 C  CA  . SER E  1  146 ? -1.819 28.893  9.146   1.00 74.28  ? 146 SER E CA  1 
ATOM   5701 C  C   . SER E  1  146 ? -1.225 27.483  9.148   1.00 73.48  ? 146 SER E C   1 
ATOM   5702 O  O   . SER E  1  146 ? -0.664 27.068  8.104   1.00 72.08  ? 146 SER E O   1 
ATOM   5703 C  CB  . SER E  1  146 ? -3.343 28.824  9.031   1.00 75.55  ? 146 SER E CB  1 
ATOM   5704 O  OG  . SER E  1  146 ? -3.906 28.128  10.119  1.00 79.24  ? 146 SER E OG  1 
ATOM   5705 O  OXT . SER E  1  146 ? -1.329 26.817  10.202  1.00 72.38  ? 146 SER E OXT 1 
ATOM   5706 N  N   . SER F  2  1   ? 31.335 45.827  45.398  1.00 85.83  ? 1   SER F N   1 
ATOM   5707 C  CA  . SER F  2  1   ? 30.658 45.626  44.117  1.00 84.90  ? 1   SER F CA  1 
ATOM   5708 C  C   . SER F  2  1   ? 29.660 44.479  44.227  1.00 82.28  ? 1   SER F C   1 
ATOM   5709 O  O   . SER F  2  1   ? 29.853 43.550  45.007  1.00 82.34  ? 1   SER F O   1 
ATOM   5710 C  CB  . SER F  2  1   ? 31.679 45.320  43.013  1.00 86.66  ? 1   SER F CB  1 
ATOM   5711 O  OG  . SER F  2  1   ? 31.057 45.272  41.739  1.00 88.40  ? 1   SER F OG  1 
ATOM   5712 N  N   . GLU F  2  2   ? 28.596 44.545  43.436  1.00 79.23  ? 2   GLU F N   1 
ATOM   5713 C  CA  . GLU F  2  2   ? 27.565 43.518  43.468  1.00 76.28  ? 2   GLU F CA  1 
ATOM   5714 C  C   . GLU F  2  2   ? 27.478 42.705  42.189  1.00 71.55  ? 2   GLU F C   1 
ATOM   5715 O  O   . GLU F  2  2   ? 27.810 43.187  41.110  1.00 70.35  ? 2   GLU F O   1 
ATOM   5716 C  CB  . GLU F  2  2   ? 26.204 44.170  43.719  1.00 80.43  ? 2   GLU F CB  1 
ATOM   5717 C  CG  . GLU F  2  2   ? 26.113 44.995  44.993  1.00 85.72  ? 2   GLU F CG  1 
ATOM   5718 C  CD  . GLU F  2  2   ? 26.281 44.165  46.255  1.00 88.22  ? 2   GLU F CD  1 
ATOM   5719 O  OE1 . GLU F  2  2   ? 25.478 43.238  46.483  1.00 89.08  ? 2   GLU F OE1 1 
ATOM   5720 O  OE2 . GLU F  2  2   ? 27.220 44.439  47.030  1.00 90.00  ? 2   GLU F OE2 1 
ATOM   5721 N  N   . CYS F  2  3   ? 27.024 41.463  42.309  1.00 66.66  ? 3   CYS F N   1 
ATOM   5722 C  CA  . CYS F  2  3   ? 26.862 40.628  41.132  1.00 62.10  ? 3   CYS F CA  1 
ATOM   5723 C  C   . CYS F  2  3   ? 25.516 40.968  40.487  1.00 60.78  ? 3   CYS F C   1 
ATOM   5724 O  O   . CYS F  2  3   ? 24.576 40.161  40.498  1.00 57.99  ? 3   CYS F O   1 
ATOM   5725 C  CB  . CYS F  2  3   ? 26.918 39.137  41.491  1.00 59.40  ? 3   CYS F CB  1 
ATOM   5726 S  SG  . CYS F  2  3   ? 26.728 38.053  40.038  1.00 56.68  ? 3   CYS F SG  1 
ATOM   5727 N  N   . GLY F  2  4   ? 25.442 42.184  39.938  1.00 58.82  ? 4   GLY F N   1 
ATOM   5728 C  CA  . GLY F  2  4   ? 24.247 42.660  39.275  1.00 58.06  ? 4   GLY F CA  1 
ATOM   5729 C  C   . GLY F  2  4   ? 24.089 41.965  37.940  1.00 58.61  ? 4   GLY F C   1 
ATOM   5730 O  O   . GLY F  2  4   ? 24.879 41.081  37.612  1.00 58.58  ? 4   GLY F O   1 
ATOM   5731 N  N   . PRO F  2  5   ? 23.079 42.341  37.147  1.00 58.80  ? 5   PRO F N   1 
ATOM   5732 C  CA  . PRO F  2  5   ? 22.825 41.734  35.832  1.00 59.42  ? 5   PRO F CA  1 
ATOM   5733 C  C   . PRO F  2  5   ? 23.986 41.844  34.848  1.00 59.08  ? 5   PRO F C   1 
ATOM   5734 O  O   . PRO F  2  5   ? 24.285 40.895  34.113  1.00 58.64  ? 5   PRO F O   1 
ATOM   5735 C  CB  . PRO F  2  5   ? 21.584 42.475  35.339  1.00 59.85  ? 5   PRO F CB  1 
ATOM   5736 C  CG  . PRO F  2  5   ? 20.879 42.818  36.632  1.00 58.90  ? 5   PRO F CG  1 
ATOM   5737 C  CD  . PRO F  2  5   ? 22.020 43.301  37.491  1.00 57.58  ? 5   PRO F CD  1 
ATOM   5738 N  N   . LEU F  2  6   ? 24.641 43.005  34.843  1.00 58.41  ? 6   LEU F N   1 
ATOM   5739 C  CA  . LEU F  2  6   ? 25.748 43.248  33.930  1.00 57.61  ? 6   LEU F CA  1 
ATOM   5740 C  C   . LEU F  2  6   ? 26.935 42.342  34.247  1.00 56.81  ? 6   LEU F C   1 
ATOM   5741 O  O   . LEU F  2  6   ? 27.449 41.661  33.361  1.00 57.33  ? 6   LEU F O   1 
ATOM   5742 C  CB  . LEU F  2  6   ? 26.135 44.736  33.967  1.00 57.45  ? 6   LEU F CB  1 
ATOM   5743 C  CG  . LEU F  2  6   ? 24.982 45.714  33.637  1.00 57.60  ? 6   LEU F CG  1 
ATOM   5744 C  CD1 . LEU F  2  6   ? 25.467 47.157  33.707  1.00 55.80  ? 6   LEU F CD1 1 
ATOM   5745 C  CD2 . LEU F  2  6   ? 24.420 45.423  32.241  1.00 57.26  ? 6   LEU F CD2 1 
ATOM   5746 N  N   . GLN F  2  7   ? 27.352 42.308  35.508  1.00 55.87  ? 7   GLN F N   1 
ATOM   5747 C  CA  . GLN F  2  7   ? 28.474 41.463  35.919  1.00 53.20  ? 7   GLN F CA  1 
ATOM   5748 C  C   . GLN F  2  7   ? 28.207 40.005  35.576  1.00 52.65  ? 7   GLN F C   1 
ATOM   5749 O  O   . GLN F  2  7   ? 29.135 39.248  35.297  1.00 53.27  ? 7   GLN F O   1 
ATOM   5750 C  CB  . GLN F  2  7   ? 28.722 41.569  37.423  1.00 52.01  ? 7   GLN F CB  1 
ATOM   5751 C  CG  . GLN F  2  7   ? 29.173 42.932  37.915  1.00 53.03  ? 7   GLN F CG  1 
ATOM   5752 C  CD  . GLN F  2  7   ? 28.095 44.005  37.781  1.00 53.17  ? 7   GLN F CD  1 
ATOM   5753 O  OE1 . GLN F  2  7   ? 26.896 43.741  37.938  1.00 53.56  ? 7   GLN F OE1 1 
ATOM   5754 N  NE2 . GLN F  2  7   ? 28.526 45.227  37.516  1.00 52.96  ? 7   GLN F NE2 1 
ATOM   5755 N  N   . ARG F  2  8   ? 26.940 39.616  35.595  1.00 51.82  ? 8   ARG F N   1 
ATOM   5756 C  CA  . ARG F  2  8   ? 26.574 38.243  35.304  1.00 51.92  ? 8   ARG F CA  1 
ATOM   5757 C  C   . ARG F  2  8   ? 26.693 37.933  33.820  1.00 51.11  ? 8   ARG F C   1 
ATOM   5758 O  O   . ARG F  2  8   ? 27.004 36.805  33.433  1.00 51.92  ? 8   ARG F O   1 
ATOM   5759 C  CB  . ARG F  2  8   ? 25.149 37.956  35.805  1.00 52.72  ? 8   ARG F CB  1 
ATOM   5760 C  CG  . ARG F  2  8   ? 25.032 37.999  37.331  1.00 53.45  ? 8   ARG F CG  1 
ATOM   5761 C  CD  . ARG F  2  8   ? 23.591 37.922  37.812  1.00 55.27  ? 8   ARG F CD  1 
ATOM   5762 N  NE  . ARG F  2  8   ? 23.483 38.135  39.258  1.00 55.23  ? 8   ARG F NE  1 
ATOM   5763 C  CZ  . ARG F  2  8   ? 23.159 37.192  40.140  1.00 54.57  ? 8   ARG F CZ  1 
ATOM   5764 N  NH1 . ARG F  2  8   ? 22.894 35.950  39.743  1.00 51.23  ? 8   ARG F NH1 1 
ATOM   5765 N  NH2 . ARG F  2  8   ? 23.113 37.483  41.431  1.00 53.67  ? 8   ARG F NH2 1 
ATOM   5766 N  N   . LEU F  2  9   ? 26.441 38.925  32.976  1.00 48.04  ? 9   LEU F N   1 
ATOM   5767 C  CA  . LEU F  2  9   ? 26.568 38.683  31.556  1.00 43.46  ? 9   LEU F CA  1 
ATOM   5768 C  C   . LEU F  2  9   ? 28.061 38.619  31.277  1.00 40.68  ? 9   LEU F C   1 
ATOM   5769 O  O   . LEU F  2  9   ? 28.523 37.728  30.572  1.00 39.33  ? 9   LEU F O   1 
ATOM   5770 C  CB  . LEU F  2  9   ? 25.947 39.820  30.756  1.00 42.18  ? 9   LEU F CB  1 
ATOM   5771 C  CG  . LEU F  2  9   ? 24.427 39.872  30.660  1.00 43.24  ? 9   LEU F CG  1 
ATOM   5772 C  CD1 . LEU F  2  9   ? 24.010 41.114  29.861  1.00 43.55  ? 9   LEU F CD1 1 
ATOM   5773 C  CD2 . LEU F  2  9   ? 23.899 38.613  29.999  1.00 41.77  ? 9   LEU F CD2 1 
ATOM   5774 N  N   . LYS F  2  10  ? 28.790 39.577  31.854  1.00 37.65  ? 10  LYS F N   1 
ATOM   5775 C  CA  . LYS F  2  10  ? 30.228 39.693  31.693  1.00 36.91  ? 10  LYS F CA  1 
ATOM   5776 C  C   . LYS F  2  10  ? 30.872 38.378  32.072  1.00 38.10  ? 10  LYS F C   1 
ATOM   5777 O  O   . LYS F  2  10  ? 31.599 37.789  31.277  1.00 38.96  ? 10  LYS F O   1 
ATOM   5778 C  CB  . LYS F  2  10  ? 30.784 40.797  32.596  1.00 36.64  ? 10  LYS F CB  1 
ATOM   5779 C  CG  . LYS F  2  10  ? 32.249 41.161  32.357  1.00 36.93  ? 10  LYS F CG  1 
ATOM   5780 C  CD  . LYS F  2  10  ? 32.362 42.095  31.155  1.00 35.31  ? 10  LYS F CD  1 
ATOM   5781 C  CE  . LYS F  2  10  ? 33.769 42.641  30.973  1.00 34.57  ? 10  LYS F CE  1 
ATOM   5782 N  NZ  . LYS F  2  10  ? 34.059 43.738  31.910  1.00 29.58  ? 10  LYS F NZ  1 
ATOM   5783 N  N   . VAL F  2  11  ? 30.581 37.922  33.292  1.00 37.79  ? 11  VAL F N   1 
ATOM   5784 C  CA  . VAL F  2  11  ? 31.117 36.671  33.818  1.00 37.36  ? 11  VAL F CA  1 
ATOM   5785 C  C   . VAL F  2  11  ? 30.753 35.494  32.909  1.00 36.55  ? 11  VAL F C   1 
ATOM   5786 O  O   . VAL F  2  11  ? 31.581 34.609  32.660  1.00 36.07  ? 11  VAL F O   1 
ATOM   5787 C  CB  . VAL F  2  11  ? 30.610 36.437  35.298  1.00 38.29  ? 11  VAL F CB  1 
ATOM   5788 C  CG1 . VAL F  2  11  ? 30.883 35.020  35.779  1.00 35.56  ? 11  VAL F CG1 1 
ATOM   5789 C  CG2 . VAL F  2  11  ? 31.323 37.394  36.217  1.00 38.97  ? 11  VAL F CG2 1 
ATOM   5790 N  N   . LYS F  2  12  ? 29.522 35.486  32.412  1.00 37.81  ? 12  LYS F N   1 
ATOM   5791 C  CA  . LYS F  2  12  ? 29.069 34.424  31.505  1.00 40.70  ? 12  LYS F CA  1 
ATOM   5792 C  C   . LYS F  2  12  ? 29.920 34.391  30.244  1.00 40.84  ? 12  LYS F C   1 
ATOM   5793 O  O   . LYS F  2  12  ? 30.264 33.324  29.733  1.00 41.76  ? 12  LYS F O   1 
ATOM   5794 C  CB  . LYS F  2  12  ? 27.621 34.644  31.085  1.00 42.08  ? 12  LYS F CB  1 
ATOM   5795 C  CG  . LYS F  2  12  ? 26.590 34.102  32.029  1.00 43.63  ? 12  LYS F CG  1 
ATOM   5796 C  CD  . LYS F  2  12  ? 25.240 34.659  31.615  1.00 48.69  ? 12  LYS F CD  1 
ATOM   5797 C  CE  . LYS F  2  12  ? 24.118 34.122  32.469  1.00 47.03  ? 12  LYS F CE  1 
ATOM   5798 N  NZ  . LYS F  2  12  ? 23.996 32.644  32.331  1.00 48.40  ? 12  LYS F NZ  1 
ATOM   5799 N  N   . ARG F  2  13  ? 30.252 35.571  29.746  1.00 41.93  ? 13  ARG F N   1 
ATOM   5800 C  CA  . ARG F  2  13  ? 31.052 35.657  28.547  1.00 43.60  ? 13  ARG F CA  1 
ATOM   5801 C  C   . ARG F  2  13  ? 32.494 35.237  28.804  1.00 42.33  ? 13  ARG F C   1 
ATOM   5802 O  O   . ARG F  2  13  ? 32.993 34.348  28.128  1.00 44.88  ? 13  ARG F O   1 
ATOM   5803 C  CB  . ARG F  2  13  ? 31.002 37.073  27.954  1.00 41.47  ? 13  ARG F CB  1 
ATOM   5804 C  CG  . ARG F  2  13  ? 31.571 37.144  26.545  1.00 43.21  ? 13  ARG F CG  1 
ATOM   5805 C  CD  . ARG F  2  13  ? 31.149 38.416  25.832  1.00 42.13  ? 13  ARG F CD  1 
ATOM   5806 N  NE  . ARG F  2  13  ? 31.521 39.568  26.633  1.00 44.83  ? 13  ARG F NE  1 
ATOM   5807 C  CZ  . ARG F  2  13  ? 32.776 39.917  26.890  1.00 43.06  ? 13  ARG F CZ  1 
ATOM   5808 N  NH1 . ARG F  2  13  ? 33.024 40.983  27.644  1.00 41.98  ? 13  ARG F NH1 1 
ATOM   5809 N  NH2 . ARG F  2  13  ? 33.774 39.213  26.372  1.00 41.83  ? 13  ARG F NH2 1 
ATOM   5810 N  N   . GLN F  2  14  ? 33.153 35.854  29.779  1.00 39.01  ? 14  GLN F N   1 
ATOM   5811 C  CA  . GLN F  2  14  ? 34.537 35.525  30.055  1.00 37.99  ? 14  GLN F CA  1 
ATOM   5812 C  C   . GLN F  2  14  ? 34.693 34.082  30.454  1.00 37.41  ? 14  GLN F C   1 
ATOM   5813 O  O   . GLN F  2  14  ? 35.731 33.475  30.200  1.00 38.32  ? 14  GLN F O   1 
ATOM   5814 C  CB  . GLN F  2  14  ? 35.103 36.445  31.122  1.00 36.55  ? 14  GLN F CB  1 
ATOM   5815 C  CG  . GLN F  2  14  ? 34.978 37.898  30.731  1.00 38.16  ? 14  GLN F CG  1 
ATOM   5816 C  CD  . GLN F  2  14  ? 35.903 38.814  31.533  1.00 39.13  ? 14  GLN F CD  1 
ATOM   5817 O  OE1 . GLN F  2  14  ? 36.097 38.623  32.733  1.00 37.45  ? 14  GLN F OE1 1 
ATOM   5818 N  NE2 . GLN F  2  14  ? 36.464 39.822  30.867  1.00 39.34  ? 14  GLN F NE2 1 
ATOM   5819 N  N   . TRP F  2  15  ? 33.654 33.516  31.047  1.00 36.64  ? 15  TRP F N   1 
ATOM   5820 C  CA  . TRP F  2  15  ? 33.724 32.117  31.421  1.00 36.27  ? 15  TRP F CA  1 
ATOM   5821 C  C   . TRP F  2  15  ? 33.618 31.253  30.161  1.00 34.78  ? 15  TRP F C   1 
ATOM   5822 O  O   . TRP F  2  15  ? 34.357 30.291  30.023  1.00 35.83  ? 15  TRP F O   1 
ATOM   5823 C  CB  . TRP F  2  15  ? 32.615 31.751  32.428  1.00 34.03  ? 15  TRP F CB  1 
ATOM   5824 C  CG  . TRP F  2  15  ? 32.427 30.271  32.591  1.00 31.07  ? 15  TRP F CG  1 
ATOM   5825 C  CD1 . TRP F  2  15  ? 31.463 29.503  32.003  1.00 30.89  ? 15  TRP F CD1 1 
ATOM   5826 C  CD2 . TRP F  2  15  ? 33.262 29.369  33.333  1.00 29.90  ? 15  TRP F CD2 1 
ATOM   5827 N  NE1 . TRP F  2  15  ? 31.645 28.180  32.329  1.00 32.41  ? 15  TRP F NE1 1 
ATOM   5828 C  CE2 . TRP F  2  15  ? 32.740 28.071  33.145  1.00 29.55  ? 15  TRP F CE2 1 
ATOM   5829 C  CE3 . TRP F  2  15  ? 34.396 29.533  34.135  1.00 31.37  ? 15  TRP F CE3 1 
ATOM   5830 C  CZ2 . TRP F  2  15  ? 33.312 26.943  33.729  1.00 28.95  ? 15  TRP F CZ2 1 
ATOM   5831 C  CZ3 . TRP F  2  15  ? 34.967 28.407  34.716  1.00 30.03  ? 15  TRP F CZ3 1 
ATOM   5832 C  CH2 . TRP F  2  15  ? 34.422 27.131  34.508  1.00 29.60  ? 15  TRP F CH2 1 
ATOM   5833 N  N   . ALA F  2  16  ? 32.730 31.609  29.239  1.00 34.74  ? 16  ALA F N   1 
ATOM   5834 C  CA  . ALA F  2  16  ? 32.570 30.825  28.006  1.00 39.15  ? 16  ALA F CA  1 
ATOM   5835 C  C   . ALA F  2  16  ? 33.844 30.815  27.166  1.00 42.17  ? 16  ALA F C   1 
ATOM   5836 O  O   . ALA F  2  16  ? 34.104 29.874  26.402  1.00 39.56  ? 16  ALA F O   1 
ATOM   5837 C  CB  . ALA F  2  16  ? 31.432 31.360  27.192  1.00 38.50  ? 16  ALA F CB  1 
ATOM   5838 N  N   . GLU F  2  17  ? 34.632 31.882  27.324  1.00 43.49  ? 17  GLU F N   1 
ATOM   5839 C  CA  . GLU F  2  17  ? 35.877 32.032  26.609  1.00 46.59  ? 17  GLU F CA  1 
ATOM   5840 C  C   . GLU F  2  17  ? 36.947 31.154  27.243  1.00 48.07  ? 17  GLU F C   1 
ATOM   5841 O  O   . GLU F  2  17  ? 37.658 30.424  26.551  1.00 48.11  ? 17  GLU F O   1 
ATOM   5842 C  CB  . GLU F  2  17  ? 36.294 33.485  26.654  1.00 50.70  ? 17  GLU F CB  1 
ATOM   5843 C  CG  . GLU F  2  17  ? 37.466 33.812  25.752  1.00 55.99  ? 17  GLU F CG  1 
ATOM   5844 C  CD  . GLU F  2  17  ? 37.521 35.287  25.442  1.00 59.92  ? 17  GLU F CD  1 
ATOM   5845 O  OE1 . GLU F  2  17  ? 36.456 35.949  25.495  1.00 62.25  ? 17  GLU F OE1 1 
ATOM   5846 O  OE2 . GLU F  2  17  ? 38.624 35.784  25.130  1.00 60.67  ? 17  GLU F OE2 1 
ATOM   5847 N  N   . ALA F  2  18  ? 37.040 31.218  28.561  1.00 48.67  ? 18  ALA F N   1 
ATOM   5848 C  CA  . ALA F  2  18  ? 38.052 30.471  29.276  1.00 49.76  ? 18  ALA F CA  1 
ATOM   5849 C  C   . ALA F  2  18  ? 37.772 28.971  29.297  1.00 49.03  ? 18  ALA F C   1 
ATOM   5850 O  O   . ALA F  2  18  ? 38.649 28.163  29.018  1.00 46.59  ? 18  ALA F O   1 
ATOM   5851 C  CB  . ALA F  2  18  ? 38.163 31.014  30.699  1.00 51.65  ? 18  ALA F CB  1 
ATOM   5852 N  N   . TYR F  2  19  ? 36.536 28.614  29.615  1.00 50.06  ? 19  TYR F N   1 
ATOM   5853 C  CA  . TYR F  2  19  ? 36.140 27.223  29.685  1.00 51.86  ? 19  TYR F CA  1 
ATOM   5854 C  C   . TYR F  2  19  ? 36.190 26.631  28.271  1.00 54.67  ? 19  TYR F C   1 
ATOM   5855 O  O   . TYR F  2  19  ? 36.610 25.490  28.064  1.00 54.54  ? 19  TYR F O   1 
ATOM   5856 C  CB  . TYR F  2  19  ? 34.739 27.146  30.291  1.00 48.53  ? 19  TYR F CB  1 
ATOM   5857 C  CG  . TYR F  2  19  ? 34.268 25.768  30.690  1.00 47.08  ? 19  TYR F CG  1 
ATOM   5858 C  CD1 . TYR F  2  19  ? 35.122 24.868  31.342  1.00 46.98  ? 19  TYR F CD1 1 
ATOM   5859 C  CD2 . TYR F  2  19  ? 32.946 25.380  30.455  1.00 45.78  ? 19  TYR F CD2 1 
ATOM   5860 C  CE1 . TYR F  2  19  ? 34.664 23.604  31.749  1.00 46.83  ? 19  TYR F CE1 1 
ATOM   5861 C  CE2 . TYR F  2  19  ? 32.477 24.134  30.851  1.00 46.58  ? 19  TYR F CE2 1 
ATOM   5862 C  CZ  . TYR F  2  19  ? 33.336 23.253  31.496  1.00 47.70  ? 19  TYR F CZ  1 
ATOM   5863 O  OH  . TYR F  2  19  ? 32.863 22.019  31.889  1.00 47.89  ? 19  TYR F OH  1 
ATOM   5864 N  N   . GLY F  2  20  ? 35.780 27.428  27.295  1.00 58.25  ? 20  GLY F N   1 
ATOM   5865 C  CA  . GLY F  2  20  ? 35.829 26.964  25.924  1.00 62.84  ? 20  GLY F CA  1 
ATOM   5866 C  C   . GLY F  2  20  ? 34.821 25.885  25.592  1.00 65.87  ? 20  GLY F C   1 
ATOM   5867 O  O   . GLY F  2  20  ? 33.789 25.764  26.248  1.00 66.18  ? 20  GLY F O   1 
ATOM   5868 N  N   . SER F  2  21  ? 35.115 25.092  24.569  1.00 68.37  ? 21  SER F N   1 
ATOM   5869 C  CA  . SER F  2  21  ? 34.197 24.042  24.167  1.00 70.64  ? 21  SER F CA  1 
ATOM   5870 C  C   . SER F  2  21  ? 34.658 22.658  24.593  1.00 70.93  ? 21  SER F C   1 
ATOM   5871 O  O   . SER F  2  21  ? 33.856 21.725  24.630  1.00 70.97  ? 21  SER F O   1 
ATOM   5872 C  CB  . SER F  2  21  ? 33.992 24.075  22.658  1.00 73.18  ? 21  SER F CB  1 
ATOM   5873 O  OG  . SER F  2  21  ? 32.858 23.305  22.315  1.00 78.17  ? 21  SER F OG  1 
ATOM   5874 N  N   . GLY F  2  22  ? 35.944 22.513  24.902  1.00 71.05  ? 22  GLY F N   1 
ATOM   5875 C  CA  . GLY F  2  22  ? 36.429 21.218  25.349  1.00 72.12  ? 22  GLY F CA  1 
ATOM   5876 C  C   . GLY F  2  22  ? 37.908 20.916  25.185  1.00 72.44  ? 22  GLY F C   1 
ATOM   5877 O  O   . GLY F  2  22  ? 38.541 20.356  26.091  1.00 71.63  ? 22  GLY F O   1 
ATOM   5878 N  N   . ASN F  2  23  ? 38.460 21.290  24.036  1.00 72.49  ? 23  ASN F N   1 
ATOM   5879 C  CA  . ASN F  2  23  ? 39.862 21.026  23.720  1.00 71.95  ? 23  ASN F CA  1 
ATOM   5880 C  C   . ASN F  2  23  ? 40.883 21.569  24.718  1.00 68.91  ? 23  ASN F C   1 
ATOM   5881 O  O   . ASN F  2  23  ? 41.999 21.056  24.803  1.00 69.38  ? 23  ASN F O   1 
ATOM   5882 C  CB  . ASN F  2  23  ? 40.197 21.560  22.322  1.00 76.41  ? 23  ASN F CB  1 
ATOM   5883 C  CG  . ASN F  2  23  ? 39.169 21.152  21.282  1.00 80.96  ? 23  ASN F CG  1 
ATOM   5884 O  OD1 . ASN F  2  23  ? 38.070 21.714  21.233  1.00 84.13  ? 23  ASN F OD1 1 
ATOM   5885 N  ND2 . ASN F  2  23  ? 39.513 20.167  20.452  1.00 81.82  ? 23  ASN F ND2 1 
ATOM   5886 N  N   . GLY F  2  24  ? 40.521 22.593  25.479  1.00 64.03  ? 24  GLY F N   1 
ATOM   5887 C  CA  . GLY F  2  24  ? 41.482 23.130  26.421  1.00 58.64  ? 24  GLY F CA  1 
ATOM   5888 C  C   . GLY F  2  24  ? 41.118 23.004  27.885  1.00 54.78  ? 24  GLY F C   1 
ATOM   5889 O  O   . GLY F  2  24  ? 41.842 23.504  28.745  1.00 54.51  ? 24  GLY F O   1 
ATOM   5890 N  N   . ARG F  2  25  ? 40.015 22.322  28.175  1.00 51.20  ? 25  ARG F N   1 
ATOM   5891 C  CA  . ARG F  2  25  ? 39.551 22.161  29.550  1.00 46.17  ? 25  ARG F CA  1 
ATOM   5892 C  C   . ARG F  2  25  ? 40.518 21.428  30.485  1.00 44.89  ? 25  ARG F C   1 
ATOM   5893 O  O   . ARG F  2  25  ? 40.601 21.744  31.683  1.00 41.37  ? 25  ARG F O   1 
ATOM   5894 C  CB  . ARG F  2  25  ? 38.195 21.463  29.548  1.00 43.71  ? 25  ARG F CB  1 
ATOM   5895 C  CG  . ARG F  2  25  ? 37.054 22.344  29.097  1.00 44.39  ? 25  ARG F CG  1 
ATOM   5896 C  CD  . ARG F  2  25  ? 35.733 21.575  29.052  1.00 41.54  ? 25  ARG F CD  1 
ATOM   5897 N  NE  . ARG F  2  25  ? 34.671 22.390  28.469  1.00 39.95  ? 25  ARG F NE  1 
ATOM   5898 C  CZ  . ARG F  2  25  ? 33.465 21.931  28.159  1.00 39.27  ? 25  ARG F CZ  1 
ATOM   5899 N  NH1 . ARG F  2  25  ? 33.161 20.658  28.378  1.00 39.64  ? 25  ARG F NH1 1 
ATOM   5900 N  NH2 . ARG F  2  25  ? 32.564 22.752  27.642  1.00 37.78  ? 25  ARG F NH2 1 
ATOM   5901 N  N   . GLU F  2  26  ? 41.246 20.451  29.956  1.00 42.70  ? 26  GLU F N   1 
ATOM   5902 C  CA  . GLU F  2  26  ? 42.168 19.731  30.820  1.00 43.35  ? 26  GLU F CA  1 
ATOM   5903 C  C   . GLU F  2  26  ? 43.180 20.684  31.427  1.00 43.45  ? 26  GLU F C   1 
ATOM   5904 O  O   . GLU F  2  26  ? 43.297 20.782  32.634  1.00 42.78  ? 26  GLU F O   1 
ATOM   5905 C  CB  . GLU F  2  26  ? 42.902 18.641  30.062  1.00 43.10  ? 26  GLU F CB  1 
ATOM   5906 C  CG  . GLU F  2  26  ? 43.772 17.798  30.950  1.00 44.79  ? 26  GLU F CG  1 
ATOM   5907 C  CD  . GLU F  2  26  ? 44.685 16.848  30.168  1.00 48.26  ? 26  GLU F CD  1 
ATOM   5908 O  OE1 . GLU F  2  26  ? 45.845 17.246  29.861  1.00 50.54  ? 26  GLU F OE1 1 
ATOM   5909 O  OE2 . GLU F  2  26  ? 44.235 15.713  29.864  1.00 48.11  ? 26  GLU F OE2 1 
ATOM   5910 N  N   . GLU F  2  27  ? 43.892 21.417  30.573  1.00 44.72  ? 27  GLU F N   1 
ATOM   5911 C  CA  . GLU F  2  27  ? 44.896 22.351  31.057  1.00 44.86  ? 27  GLU F CA  1 
ATOM   5912 C  C   . GLU F  2  27  ? 44.282 23.474  31.900  1.00 43.01  ? 27  GLU F C   1 
ATOM   5913 O  O   . GLU F  2  27  ? 44.959 24.033  32.761  1.00 41.90  ? 27  GLU F O   1 
ATOM   5914 C  CB  . GLU F  2  27  ? 45.695 22.908  29.881  1.00 49.69  ? 27  GLU F CB  1 
ATOM   5915 C  CG  . GLU F  2  27  ? 47.200 22.849  30.096  1.00 59.11  ? 27  GLU F CG  1 
ATOM   5916 C  CD  . GLU F  2  27  ? 47.962 22.521  28.820  1.00 65.32  ? 27  GLU F CD  1 
ATOM   5917 O  OE1 . GLU F  2  27  ? 47.777 23.241  27.810  1.00 68.56  ? 27  GLU F OE1 1 
ATOM   5918 O  OE2 . GLU F  2  27  ? 48.755 21.544  28.826  1.00 66.83  ? 27  GLU F OE2 1 
ATOM   5919 N  N   . PHE F  2  28  ? 43.013 23.796  31.660  1.00 39.60  ? 28  PHE F N   1 
ATOM   5920 C  CA  . PHE F  2  28  ? 42.339 24.853  32.414  1.00 38.39  ? 28  PHE F CA  1 
ATOM   5921 C  C   . PHE F  2  28  ? 42.216 24.345  33.871  1.00 40.15  ? 28  PHE F C   1 
ATOM   5922 O  O   . PHE F  2  28  ? 42.807 24.895  34.799  1.00 38.46  ? 28  PHE F O   1 
ATOM   5923 C  CB  . PHE F  2  28  ? 40.963 25.105  31.786  1.00 34.42  ? 28  PHE F CB  1 
ATOM   5924 C  CG  . PHE F  2  28  ? 40.206 26.270  32.384  1.00 33.01  ? 28  PHE F CG  1 
ATOM   5925 C  CD1 . PHE F  2  28  ? 38.804 26.262  32.410  1.00 30.70  ? 28  PHE F CD1 1 
ATOM   5926 C  CD2 . PHE F  2  28  ? 40.875 27.375  32.894  1.00 31.95  ? 28  PHE F CD2 1 
ATOM   5927 C  CE1 . PHE F  2  28  ? 38.079 27.334  32.934  1.00 29.93  ? 28  PHE F CE1 1 
ATOM   5928 C  CE2 . PHE F  2  28  ? 40.156 28.468  33.432  1.00 33.68  ? 28  PHE F CE2 1 
ATOM   5929 C  CZ  . PHE F  2  28  ? 38.746 28.437  33.448  1.00 30.35  ? 28  PHE F CZ  1 
ATOM   5930 N  N   . GLY F  2  29  ? 41.468 23.260  34.046  1.00 42.38  ? 29  GLY F N   1 
ATOM   5931 C  CA  . GLY F  2  29  ? 41.316 22.671  35.358  1.00 45.03  ? 29  GLY F CA  1 
ATOM   5932 C  C   . GLY F  2  29  ? 42.642 22.460  36.083  1.00 46.52  ? 29  GLY F C   1 
ATOM   5933 O  O   . GLY F  2  29  ? 42.766 22.799  37.257  1.00 48.22  ? 29  GLY F O   1 
ATOM   5934 N  N   . HIS F  2  30  ? 43.644 21.912  35.399  1.00 47.11  ? 30  HIS F N   1 
ATOM   5935 C  CA  . HIS F  2  30  ? 44.943 21.671  36.024  1.00 46.32  ? 30  HIS F CA  1 
ATOM   5936 C  C   . HIS F  2  30  ? 45.570 22.950  36.558  1.00 47.50  ? 30  HIS F C   1 
ATOM   5937 O  O   . HIS F  2  30  ? 46.166 22.946  37.631  1.00 47.48  ? 30  HIS F O   1 
ATOM   5938 C  CB  . HIS F  2  30  ? 45.902 20.996  35.031  1.00 45.10  ? 30  HIS F CB  1 
ATOM   5939 C  CG  . HIS F  2  30  ? 47.250 20.681  35.604  1.00 46.53  ? 30  HIS F CG  1 
ATOM   5940 N  ND1 . HIS F  2  30  ? 48.258 21.618  35.705  1.00 47.39  ? 30  HIS F ND1 1 
ATOM   5941 C  CD2 . HIS F  2  30  ? 47.757 19.533  36.113  1.00 46.59  ? 30  HIS F CD2 1 
ATOM   5942 C  CE1 . HIS F  2  30  ? 49.329 21.062  36.251  1.00 47.28  ? 30  HIS F CE1 1 
ATOM   5943 N  NE2 . HIS F  2  30  ? 49.050 19.795  36.509  1.00 46.24  ? 30  HIS F NE2 1 
ATOM   5944 N  N   . PHE F  2  31  ? 45.436 24.050  35.820  1.00 48.15  ? 31  PHE F N   1 
ATOM   5945 C  CA  . PHE F  2  31  ? 46.029 25.316  36.249  1.00 47.79  ? 31  PHE F CA  1 
ATOM   5946 C  C   . PHE F  2  31  ? 45.359 25.772  37.541  1.00 49.08  ? 31  PHE F C   1 
ATOM   5947 O  O   . PHE F  2  31  ? 46.025 26.222  38.481  1.00 49.27  ? 31  PHE F O   1 
ATOM   5948 C  CB  . PHE F  2  31  ? 45.838 26.382  35.169  1.00 45.09  ? 31  PHE F CB  1 
ATOM   5949 C  CG  . PHE F  2  31  ? 46.473 27.701  35.499  1.00 45.28  ? 31  PHE F CG  1 
ATOM   5950 C  CD1 . PHE F  2  31  ? 47.796 27.954  35.167  1.00 45.60  ? 31  PHE F CD1 1 
ATOM   5951 C  CD2 . PHE F  2  31  ? 45.746 28.703  36.144  1.00 45.18  ? 31  PHE F CD2 1 
ATOM   5952 C  CE1 . PHE F  2  31  ? 48.396 29.193  35.469  1.00 46.17  ? 31  PHE F CE1 1 
ATOM   5953 C  CE2 . PHE F  2  31  ? 46.333 29.942  36.450  1.00 44.92  ? 31  PHE F CE2 1 
ATOM   5954 C  CZ  . PHE F  2  31  ? 47.658 30.184  36.112  1.00 44.80  ? 31  PHE F CZ  1 
ATOM   5955 N  N   . ILE F  2  32  ? 44.038 25.651  37.577  1.00 48.61  ? 32  ILE F N   1 
ATOM   5956 C  CA  . ILE F  2  32  ? 43.274 26.055  38.747  1.00 48.96  ? 32  ILE F CA  1 
ATOM   5957 C  C   . ILE F  2  32  ? 43.697 25.249  39.963  1.00 49.61  ? 32  ILE F C   1 
ATOM   5958 O  O   . ILE F  2  32  ? 44.131 25.802  40.961  1.00 48.90  ? 32  ILE F O   1 
ATOM   5959 C  CB  . ILE F  2  32  ? 41.748 25.891  38.480  1.00 49.14  ? 32  ILE F CB  1 
ATOM   5960 C  CG1 . ILE F  2  32  ? 41.271 27.014  37.539  1.00 47.42  ? 32  ILE F CG1 1 
ATOM   5961 C  CG2 . ILE F  2  32  ? 40.968 25.890  39.788  1.00 47.20  ? 32  ILE F CG2 1 
ATOM   5962 C  CD1 . ILE F  2  32  ? 39.960 26.727  36.810  1.00 47.10  ? 32  ILE F CD1 1 
ATOM   5963 N  N   . TRP F  2  33  ? 43.600 23.936  39.862  1.00 51.41  ? 33  TRP F N   1 
ATOM   5964 C  CA  . TRP F  2  33  ? 43.955 23.078  40.969  1.00 53.53  ? 33  TRP F CA  1 
ATOM   5965 C  C   . TRP F  2  33  ? 45.426 23.032  41.360  1.00 52.94  ? 33  TRP F C   1 
ATOM   5966 O  O   . TRP F  2  33  ? 45.755 22.636  42.471  1.00 54.14  ? 33  TRP F O   1 
ATOM   5967 C  CB  . TRP F  2  33  ? 43.439 21.676  40.691  1.00 57.60  ? 33  TRP F CB  1 
ATOM   5968 C  CG  . TRP F  2  33  ? 41.968 21.646  40.792  1.00 61.72  ? 33  TRP F CG  1 
ATOM   5969 C  CD1 . TRP F  2  33  ? 41.073 21.730  39.768  1.00 63.11  ? 33  TRP F CD1 1 
ATOM   5970 C  CD2 . TRP F  2  33  ? 41.205 21.652  41.999  1.00 63.75  ? 33  TRP F CD2 1 
ATOM   5971 N  NE1 . TRP F  2  33  ? 39.794 21.801  40.263  1.00 64.93  ? 33  TRP F NE1 1 
ATOM   5972 C  CE2 . TRP F  2  33  ? 39.844 21.757  41.631  1.00 65.09  ? 33  TRP F CE2 1 
ATOM   5973 C  CE3 . TRP F  2  33  ? 41.538 21.589  43.359  1.00 64.18  ? 33  TRP F CE3 1 
ATOM   5974 C  CZ2 . TRP F  2  33  ? 38.814 21.800  42.575  1.00 65.19  ? 33  TRP F CZ2 1 
ATOM   5975 C  CZ3 . TRP F  2  33  ? 40.520 21.633  44.297  1.00 64.87  ? 33  TRP F CZ3 1 
ATOM   5976 C  CH2 . TRP F  2  33  ? 39.171 21.735  43.901  1.00 66.35  ? 33  TRP F CH2 1 
ATOM   5977 N  N   . ALA F  2  34  ? 46.323 23.407  40.460  1.00 50.71  ? 34  ALA F N   1 
ATOM   5978 C  CA  . ALA F  2  34  ? 47.721 23.394  40.827  1.00 48.45  ? 34  ALA F CA  1 
ATOM   5979 C  C   . ALA F  2  34  ? 47.816 24.613  41.699  1.00 48.55  ? 34  ALA F C   1 
ATOM   5980 O  O   . ALA F  2  34  ? 48.615 24.665  42.625  1.00 48.35  ? 34  ALA F O   1 
ATOM   5981 C  CB  . ALA F  2  34  ? 48.615 23.547  39.608  1.00 46.61  ? 34  ALA F CB  1 
ATOM   5982 N  N   . ASN F  2  35  ? 46.970 25.593  41.407  1.00 49.62  ? 35  ASN F N   1 
ATOM   5983 C  CA  . ASN F  2  35  ? 46.965 26.834  42.159  1.00 52.43  ? 35  ASN F CA  1 
ATOM   5984 C  C   . ASN F  2  35  ? 46.422 26.595  43.568  1.00 54.14  ? 35  ASN F C   1 
ATOM   5985 O  O   . ASN F  2  35  ? 47.017 27.029  44.565  1.00 51.18  ? 35  ASN F O   1 
ATOM   5986 C  CB  . ASN F  2  35  ? 46.126 27.892  41.434  1.00 52.02  ? 35  ASN F CB  1 
ATOM   5987 C  CG  . ASN F  2  35  ? 46.112 29.226  42.167  1.00 53.73  ? 35  ASN F CG  1 
ATOM   5988 O  OD1 . ASN F  2  35  ? 45.364 29.415  43.123  1.00 52.68  ? 35  ASN F OD1 1 
ATOM   5989 N  ND2 . ASN F  2  35  ? 46.960 30.152  41.730  1.00 56.32  ? 35  ASN F ND2 1 
ATOM   5990 N  N   . VAL F  2  36  ? 45.295 25.884  43.623  1.00 56.15  ? 36  VAL F N   1 
ATOM   5991 C  CA  . VAL F  2  36  ? 44.614 25.546  44.869  1.00 58.28  ? 36  VAL F CA  1 
ATOM   5992 C  C   . VAL F  2  36  ? 45.543 24.845  45.830  1.00 58.15  ? 36  VAL F C   1 
ATOM   5993 O  O   . VAL F  2  36  ? 45.734 25.313  46.946  1.00 58.88  ? 36  VAL F O   1 
ATOM   5994 C  CB  . VAL F  2  36  ? 43.397 24.617  44.627  1.00 61.37  ? 36  VAL F CB  1 
ATOM   5995 C  CG1 . VAL F  2  36  ? 42.863 24.109  45.966  1.00 61.57  ? 36  VAL F CG1 1 
ATOM   5996 C  CG2 . VAL F  2  36  ? 42.283 25.369  43.873  1.00 61.85  ? 36  VAL F CG2 1 
ATOM   5997 N  N   . PHE F  2  37  ? 46.115 23.726  45.411  1.00 58.33  ? 37  PHE F N   1 
ATOM   5998 C  CA  . PHE F  2  37  ? 47.015 22.985  46.296  1.00 58.62  ? 37  PHE F CA  1 
ATOM   5999 C  C   . PHE F  2  37  ? 48.356 23.639  46.592  1.00 59.38  ? 37  PHE F C   1 
ATOM   6000 O  O   . PHE F  2  37  ? 49.085 23.152  47.446  1.00 59.59  ? 37  PHE F O   1 
ATOM   6001 C  CB  . PHE F  2  37  ? 47.276 21.574  45.769  1.00 57.37  ? 37  PHE F CB  1 
ATOM   6002 C  CG  . PHE F  2  37  ? 46.054 20.710  45.733  1.00 56.46  ? 37  PHE F CG  1 
ATOM   6003 C  CD1 . PHE F  2  37  ? 45.011 20.914  46.630  1.00 56.79  ? 37  PHE F CD1 1 
ATOM   6004 C  CD2 . PHE F  2  37  ? 45.940 19.698  44.798  1.00 55.94  ? 37  PHE F CD2 1 
ATOM   6005 C  CE1 . PHE F  2  37  ? 43.869 20.121  46.585  1.00 56.45  ? 37  PHE F CE1 1 
ATOM   6006 C  CE2 . PHE F  2  37  ? 44.801 18.895  44.744  1.00 56.99  ? 37  PHE F CE2 1 
ATOM   6007 C  CZ  . PHE F  2  37  ? 43.764 19.109  45.640  1.00 56.61  ? 37  PHE F CZ  1 
ATOM   6008 N  N   . LYS F  2  38  ? 48.704 24.721  45.900  1.00 59.96  ? 38  LYS F N   1 
ATOM   6009 C  CA  . LYS F  2  38  ? 49.974 25.368  46.195  1.00 61.47  ? 38  LYS F CA  1 
ATOM   6010 C  C   . LYS F  2  38  ? 49.736 26.431  47.261  1.00 63.28  ? 38  LYS F C   1 
ATOM   6011 O  O   . LYS F  2  38  ? 50.569 26.660  48.138  1.00 63.72  ? 38  LYS F O   1 
ATOM   6012 C  CB  . LYS F  2  38  ? 50.592 26.014  44.948  1.00 60.02  ? 38  LYS F CB  1 
ATOM   6013 C  CG  . LYS F  2  38  ? 51.936 26.698  45.237  1.00 58.67  ? 38  LYS F CG  1 
ATOM   6014 C  CD  . LYS F  2  38  ? 52.534 27.378  44.016  1.00 58.89  ? 38  LYS F CD  1 
ATOM   6015 C  CE  . LYS F  2  38  ? 54.002 27.684  44.219  1.00 58.12  ? 38  LYS F CE  1 
ATOM   6016 N  NZ  . LYS F  2  38  ? 54.789 26.433  44.460  1.00 60.50  ? 38  LYS F NZ  1 
ATOM   6017 N  N   . VAL F  2  39  ? 48.578 27.074  47.187  1.00 64.70  ? 39  VAL F N   1 
ATOM   6018 C  CA  . VAL F  2  39  ? 48.228 28.119  48.137  1.00 64.23  ? 39  VAL F CA  1 
ATOM   6019 C  C   . VAL F  2  39  ? 47.719 27.500  49.438  1.00 63.45  ? 39  VAL F C   1 
ATOM   6020 O  O   . VAL F  2  39  ? 47.871 28.081  50.513  1.00 62.20  ? 39  VAL F O   1 
ATOM   6021 C  CB  . VAL F  2  39  ? 47.129 29.045  47.551  1.00 64.65  ? 39  VAL F CB  1 
ATOM   6022 C  CG1 . VAL F  2  39  ? 46.720 30.085  48.573  1.00 64.76  ? 39  VAL F CG1 1 
ATOM   6023 C  CG2 . VAL F  2  39  ? 47.639 29.720  46.281  1.00 66.80  ? 39  VAL F CG2 1 
ATOM   6024 N  N   . ALA F  2  40  ? 47.134 26.309  49.332  1.00 62.26  ? 40  ALA F N   1 
ATOM   6025 C  CA  . ALA F  2  40  ? 46.568 25.617  50.487  1.00 61.64  ? 40  ALA F CA  1 
ATOM   6026 C  C   . ALA F  2  40  ? 46.764 24.101  50.414  1.00 60.64  ? 40  ALA F C   1 
ATOM   6027 O  O   . ALA F  2  40  ? 45.798 23.340  50.312  1.00 58.19  ? 40  ALA F O   1 
ATOM   6028 C  CB  . ALA F  2  40  ? 45.079 25.947  50.600  1.00 60.68  ? 40  ALA F CB  1 
ATOM   6029 N  N   . PRO F  2  41  ? 48.025 23.651  50.491  1.00 60.73  ? 41  PRO F N   1 
ATOM   6030 C  CA  . PRO F  2  41  ? 48.380 22.230  50.430  1.00 61.81  ? 41  PRO F CA  1 
ATOM   6031 C  C   . PRO F  2  41  ? 47.622 21.346  51.417  1.00 63.88  ? 41  PRO F C   1 
ATOM   6032 O  O   . PRO F  2  41  ? 47.477 20.139  51.201  1.00 64.48  ? 41  PRO F O   1 
ATOM   6033 C  CB  . PRO F  2  41  ? 49.888 22.237  50.684  1.00 59.53  ? 41  PRO F CB  1 
ATOM   6034 C  CG  . PRO F  2  41  ? 50.088 23.455  51.502  1.00 60.88  ? 41  PRO F CG  1 
ATOM   6035 C  CD  . PRO F  2  41  ? 49.202 24.468  50.836  1.00 59.95  ? 41  PRO F CD  1 
ATOM   6036 N  N   . SER F  2  42  ? 47.130 21.939  52.498  1.00 64.79  ? 42  SER F N   1 
ATOM   6037 C  CA  . SER F  2  42  ? 46.403 21.160  53.491  1.00 66.14  ? 42  SER F CA  1 
ATOM   6038 C  C   . SER F  2  42  ? 45.039 20.752  52.962  1.00 67.13  ? 42  SER F C   1 
ATOM   6039 O  O   . SER F  2  42  ? 44.393 19.879  53.529  1.00 66.88  ? 42  SER F O   1 
ATOM   6040 C  CB  . SER F  2  42  ? 46.233 21.956  54.796  1.00 66.01  ? 42  SER F CB  1 
ATOM   6041 O  OG  . SER F  2  42  ? 45.470 23.138  54.605  1.00 66.80  ? 42  SER F OG  1 
ATOM   6042 N  N   . ALA F  2  43  ? 44.598 21.373  51.873  1.00 68.17  ? 43  ALA F N   1 
ATOM   6043 C  CA  . ALA F  2  43  ? 43.290 21.048  51.323  1.00 68.78  ? 43  ALA F CA  1 
ATOM   6044 C  C   . ALA F  2  43  ? 43.273 19.748  50.522  1.00 69.48  ? 43  ALA F C   1 
ATOM   6045 O  O   . ALA F  2  43  ? 42.218 19.152  50.336  1.00 67.19  ? 43  ALA F O   1 
ATOM   6046 C  CB  . ALA F  2  43  ? 42.788 22.202  50.467  1.00 69.19  ? 43  ALA F CB  1 
ATOM   6047 N  N   . ARG F  2  44  ? 44.432 19.291  50.057  1.00 72.50  ? 44  ARG F N   1 
ATOM   6048 C  CA  . ARG F  2  44  ? 44.446 18.067  49.269  1.00 75.86  ? 44  ARG F CA  1 
ATOM   6049 C  C   . ARG F  2  44  ? 44.189 16.801  50.079  1.00 79.52  ? 44  ARG F C   1 
ATOM   6050 O  O   . ARG F  2  44  ? 44.123 15.705  49.520  1.00 78.98  ? 44  ARG F O   1 
ATOM   6051 C  CB  . ARG F  2  44  ? 45.752 17.943  48.461  1.00 74.13  ? 44  ARG F CB  1 
ATOM   6052 C  CG  . ARG F  2  44  ? 47.045 17.870  49.225  1.00 72.35  ? 44  ARG F CG  1 
ATOM   6053 C  CD  . ARG F  2  44  ? 48.171 17.499  48.254  1.00 70.53  ? 44  ARG F CD  1 
ATOM   6054 N  NE  . ARG F  2  44  ? 48.761 18.647  47.563  1.00 69.43  ? 44  ARG F NE  1 
ATOM   6055 C  CZ  . ARG F  2  44  ? 49.226 18.625  46.313  1.00 68.02  ? 44  ARG F CZ  1 
ATOM   6056 N  NH1 . ARG F  2  44  ? 49.169 17.518  45.586  1.00 64.46  ? 44  ARG F NH1 1 
ATOM   6057 N  NH2 . ARG F  2  44  ? 49.786 19.710  45.799  1.00 67.14  ? 44  ARG F NH2 1 
ATOM   6058 N  N   . ASP F  2  45  ? 44.018 16.962  51.393  1.00 83.92  ? 45  ASP F N   1 
ATOM   6059 C  CA  . ASP F  2  45  ? 43.744 15.829  52.284  1.00 87.25  ? 45  ASP F CA  1 
ATOM   6060 C  C   . ASP F  2  45  ? 42.319 15.328  52.060  1.00 88.17  ? 45  ASP F C   1 
ATOM   6061 O  O   . ASP F  2  45  ? 42.013 14.163  52.311  1.00 86.49  ? 45  ASP F O   1 
ATOM   6062 C  CB  . ASP F  2  45  ? 43.871 16.230  53.765  1.00 90.48  ? 45  ASP F CB  1 
ATOM   6063 C  CG  . ASP F  2  45  ? 45.302 16.502  54.191  1.00 93.05  ? 45  ASP F CG  1 
ATOM   6064 O  OD1 . ASP F  2  45  ? 46.220 15.824  53.683  1.00 94.28  ? 45  ASP F OD1 1 
ATOM   6065 O  OD2 . ASP F  2  45  ? 45.506 17.382  55.056  1.00 94.77  ? 45  ASP F OD2 1 
ATOM   6066 N  N   . MET F  2  46  ? 41.457 16.229  51.592  1.00 89.70  ? 46  MET F N   1 
ATOM   6067 C  CA  . MET F  2  46  ? 40.047 15.930  51.346  1.00 91.45  ? 46  MET F CA  1 
ATOM   6068 C  C   . MET F  2  46  ? 39.789 15.188  50.040  1.00 91.38  ? 46  MET F C   1 
ATOM   6069 O  O   . MET F  2  46  ? 38.751 14.551  49.878  1.00 90.90  ? 46  MET F O   1 
ATOM   6070 C  CB  . MET F  2  46  ? 39.236 17.228  51.313  1.00 93.24  ? 46  MET F CB  1 
ATOM   6071 C  CG  . MET F  2  46  ? 39.464 18.165  52.482  1.00 95.78  ? 46  MET F CG  1 
ATOM   6072 S  SD  . MET F  2  46  ? 38.450 19.647  52.315  1.00 97.63  ? 46  MET F SD  1 
ATOM   6073 C  CE  . MET F  2  46  ? 36.899 19.071  52.917  1.00 97.65  ? 46  MET F CE  1 
ATOM   6074 N  N   . PHE F  2  47  ? 40.728 15.275  49.109  1.00 91.57  ? 47  PHE F N   1 
ATOM   6075 C  CA  . PHE F  2  47  ? 40.555 14.653  47.800  1.00 91.14  ? 47  PHE F CA  1 
ATOM   6076 C  C   . PHE F  2  47  ? 41.321 13.354  47.608  1.00 92.38  ? 47  PHE F C   1 
ATOM   6077 O  O   . PHE F  2  47  ? 41.629 12.981  46.473  1.00 93.37  ? 47  PHE F O   1 
ATOM   6078 C  CB  . PHE F  2  47  ? 40.979 15.646  46.724  1.00 88.48  ? 47  PHE F CB  1 
ATOM   6079 C  CG  . PHE F  2  47  ? 40.303 16.974  46.834  1.00 85.19  ? 47  PHE F CG  1 
ATOM   6080 C  CD1 . PHE F  2  47  ? 39.078 17.190  46.226  1.00 84.02  ? 47  PHE F CD1 1 
ATOM   6081 C  CD2 . PHE F  2  47  ? 40.892 18.011  47.551  1.00 84.04  ? 47  PHE F CD2 1 
ATOM   6082 C  CE1 . PHE F  2  47  ? 38.446 18.426  46.327  1.00 82.92  ? 47  PHE F CE1 1 
ATOM   6083 C  CE2 . PHE F  2  47  ? 40.267 19.247  47.659  1.00 82.46  ? 47  PHE F CE2 1 
ATOM   6084 C  CZ  . PHE F  2  47  ? 39.041 19.457  47.046  1.00 81.90  ? 47  PHE F CZ  1 
ATOM   6085 N  N   . LYS F  2  48  ? 41.618 12.660  48.700  1.00 93.10  ? 48  LYS F N   1 
ATOM   6086 C  CA  . LYS F  2  48  ? 42.367 11.411  48.610  1.00 92.84  ? 48  LYS F CA  1 
ATOM   6087 C  C   . LYS F  2  48  ? 41.616 10.302  47.888  1.00 89.58  ? 48  LYS F C   1 
ATOM   6088 O  O   . LYS F  2  48  ? 42.224 9.379   47.348  1.00 88.48  ? 48  LYS F O   1 
ATOM   6089 C  CB  . LYS F  2  48  ? 42.791 10.960  50.005  1.00 97.87  ? 48  LYS F CB  1 
ATOM   6090 C  CG  . LYS F  2  48  ? 43.770 11.935  50.647  1.00 104.37 ? 48  LYS F CG  1 
ATOM   6091 C  CD  . LYS F  2  48  ? 44.319 11.419  51.954  1.00 109.48 ? 48  LYS F CD  1 
ATOM   6092 C  CE  . LYS F  2  48  ? 45.255 12.439  52.561  1.00 112.89 ? 48  LYS F CE  1 
ATOM   6093 N  NZ  . LYS F  2  48  ? 45.794 11.952  53.846  1.00 115.93 ? 48  LYS F NZ  1 
ATOM   6094 N  N   . ARG F  2  49  ? 40.295 10.398  47.860  1.00 86.64  ? 49  ARG F N   1 
ATOM   6095 C  CA  . ARG F  2  49  ? 39.507 9.390   47.169  1.00 83.78  ? 49  ARG F CA  1 
ATOM   6096 C  C   . ARG F  2  49  ? 39.728 9.546   45.668  1.00 81.69  ? 49  ARG F C   1 
ATOM   6097 O  O   . ARG F  2  49  ? 39.607 8.586   44.902  1.00 81.19  ? 49  ARG F O   1 
ATOM   6098 C  CB  . ARG F  2  49  ? 38.027 9.568   47.473  1.00 83.70  ? 49  ARG F CB  1 
ATOM   6099 C  CG  . ARG F  2  49  ? 37.182 8.419   46.975  1.00 82.56  ? 49  ARG F CG  1 
ATOM   6100 C  CD  . ARG F  2  49  ? 35.723 8.739   47.154  1.00 83.00  ? 49  ARG F CD  1 
ATOM   6101 N  NE  . ARG F  2  49  ? 35.246 9.649   46.122  1.00 82.49  ? 49  ARG F NE  1 
ATOM   6102 C  CZ  . ARG F  2  49  ? 35.105 9.305   44.847  1.00 82.24  ? 49  ARG F CZ  1 
ATOM   6103 N  NH1 . ARG F  2  49  ? 35.399 8.071   44.459  1.00 81.12  ? 49  ARG F NH1 1 
ATOM   6104 N  NH2 . ARG F  2  49  ? 34.666 10.189  43.961  1.00 82.23  ? 49  ARG F NH2 1 
ATOM   6105 N  N   . VAL F  2  50  ? 40.046 10.772  45.258  1.00 77.85  ? 50  VAL F N   1 
ATOM   6106 C  CA  . VAL F  2  50  ? 40.289 11.081  43.856  1.00 73.94  ? 50  VAL F CA  1 
ATOM   6107 C  C   . VAL F  2  50  ? 41.734 11.533  43.651  1.00 72.04  ? 50  VAL F C   1 
ATOM   6108 O  O   . VAL F  2  50  ? 42.005 12.544  43.003  1.00 72.58  ? 50  VAL F O   1 
ATOM   6109 C  CB  . VAL F  2  50  ? 39.328 12.179  43.371  1.00 72.66  ? 50  VAL F CB  1 
ATOM   6110 C  CG1 . VAL F  2  50  ? 37.927 11.635  43.275  1.00 72.56  ? 50  VAL F CG1 1 
ATOM   6111 C  CG2 . VAL F  2  50  ? 39.334 13.336  44.342  1.00 71.18  ? 50  VAL F CG2 1 
ATOM   6112 N  N   . ARG F  2  51  ? 42.660 10.774  44.223  1.00 68.65  ? 51  ARG F N   1 
ATOM   6113 C  CA  . ARG F  2  51  ? 44.078 11.059  44.105  1.00 65.29  ? 51  ARG F CA  1 
ATOM   6114 C  C   . ARG F  2  51  ? 44.437 12.537  44.189  1.00 63.52  ? 51  ARG F C   1 
ATOM   6115 O  O   . ARG F  2  51  ? 45.183 13.049  43.356  1.00 63.62  ? 51  ARG F O   1 
ATOM   6116 C  CB  . ARG F  2  51  ? 44.612 10.466  42.798  1.00 64.30  ? 51  ARG F CB  1 
ATOM   6117 C  CG  . ARG F  2  51  ? 44.583 8.944   42.751  1.00 61.72  ? 51  ARG F CG  1 
ATOM   6118 C  CD  . ARG F  2  51  ? 45.357 8.373   43.934  1.00 61.44  ? 51  ARG F CD  1 
ATOM   6119 N  NE  . ARG F  2  51  ? 46.743 8.837   43.984  1.00 59.06  ? 51  ARG F NE  1 
ATOM   6120 C  CZ  . ARG F  2  51  ? 47.674 8.462   43.116  1.00 59.88  ? 51  ARG F CZ  1 
ATOM   6121 N  NH1 . ARG F  2  51  ? 47.350 7.619   42.139  1.00 59.33  ? 51  ARG F NH1 1 
ATOM   6122 N  NH2 . ARG F  2  51  ? 48.921 8.919   43.224  1.00 58.48  ? 51  ARG F NH2 1 
ATOM   6123 N  N   . GLY F  2  52  ? 43.921 13.213  45.213  1.00 61.99  ? 52  GLY F N   1 
ATOM   6124 C  CA  . GLY F  2  52  ? 44.209 14.626  45.402  1.00 61.35  ? 52  GLY F CA  1 
ATOM   6125 C  C   . GLY F  2  52  ? 45.679 14.881  45.683  1.00 60.90  ? 52  GLY F C   1 
ATOM   6126 O  O   . GLY F  2  52  ? 46.113 16.021  45.860  1.00 60.94  ? 52  GLY F O   1 
ATOM   6127 N  N   . ASP F  2  53  ? 46.454 13.810  45.717  1.00 61.06  ? 53  ASP F N   1 
ATOM   6128 C  CA  . ASP F  2  53  ? 47.876 13.919  45.975  1.00 62.81  ? 53  ASP F CA  1 
ATOM   6129 C  C   . ASP F  2  53  ? 48.628 13.973  44.651  1.00 62.96  ? 53  ASP F C   1 
ATOM   6130 O  O   . ASP F  2  53  ? 49.810 14.352  44.608  1.00 64.02  ? 53  ASP F O   1 
ATOM   6131 C  CB  . ASP F  2  53  ? 48.350 12.706  46.764  1.00 63.36  ? 53  ASP F CB  1 
ATOM   6132 C  CG  . ASP F  2  53  ? 48.120 11.420  46.015  1.00 65.44  ? 53  ASP F CG  1 
ATOM   6133 O  OD1 . ASP F  2  53  ? 46.944 11.051  45.802  1.00 65.38  ? 53  ASP F OD1 1 
ATOM   6134 O  OD2 . ASP F  2  53  ? 49.119 10.787  45.616  1.00 66.99  ? 53  ASP F OD2 1 
ATOM   6135 N  N   . ASN F  2  54  ? 47.938 13.577  43.583  1.00 60.97  ? 54  ASN F N   1 
ATOM   6136 C  CA  . ASN F  2  54  ? 48.525 13.565  42.242  1.00 59.98  ? 54  ASN F CA  1 
ATOM   6137 C  C   . ASN F  2  54  ? 47.512 14.001  41.177  1.00 56.92  ? 54  ASN F C   1 
ATOM   6138 O  O   . ASN F  2  54  ? 46.849 13.163  40.556  1.00 53.57  ? 54  ASN F O   1 
ATOM   6139 C  CB  . ASN F  2  54  ? 49.049 12.163  41.909  1.00 60.70  ? 54  ASN F CB  1 
ATOM   6140 C  CG  . ASN F  2  54  ? 49.804 12.132  40.607  1.00 61.31  ? 54  ASN F CG  1 
ATOM   6141 O  OD1 . ASN F  2  54  ? 49.715 13.065  39.815  1.00 62.71  ? 54  ASN F OD1 1 
ATOM   6142 N  ND2 . ASN F  2  54  ? 50.545 11.061  40.370  1.00 60.46  ? 54  ASN F ND2 1 
ATOM   6143 N  N   . ILE F  2  55  ? 47.421 15.309  40.955  1.00 56.03  ? 55  ILE F N   1 
ATOM   6144 C  CA  . ILE F  2  55  ? 46.463 15.863  39.990  1.00 54.28  ? 55  ILE F CA  1 
ATOM   6145 C  C   . ILE F  2  55  ? 46.698 15.506  38.515  1.00 53.28  ? 55  ILE F C   1 
ATOM   6146 O  O   . ILE F  2  55  ? 45.886 15.851  37.653  1.00 52.66  ? 55  ILE F O   1 
ATOM   6147 C  CB  . ILE F  2  55  ? 46.363 17.393  40.112  1.00 52.49  ? 55  ILE F CB  1 
ATOM   6148 C  CG1 . ILE F  2  55  ? 47.699 18.041  39.766  1.00 50.52  ? 55  ILE F CG1 1 
ATOM   6149 C  CG2 . ILE F  2  55  ? 45.911 17.754  41.509  1.00 51.58  ? 55  ILE F CG2 1 
ATOM   6150 C  CD1 . ILE F  2  55  ? 47.642 19.553  39.741  1.00 50.54  ? 55  ILE F CD1 1 
ATOM   6151 N  N   . TYR F  2  56  ? 47.796 14.812  38.237  1.00 52.40  ? 56  TYR F N   1 
ATOM   6152 C  CA  . TYR F  2  56  ? 48.118 14.372  36.883  1.00 49.89  ? 56  TYR F CA  1 
ATOM   6153 C  C   . TYR F  2  56  ? 47.413 13.045  36.608  1.00 49.76  ? 56  TYR F C   1 
ATOM   6154 O  O   . TYR F  2  56  ? 47.530 12.489  35.518  1.00 50.33  ? 56  TYR F O   1 
ATOM   6155 C  CB  . TYR F  2  56  ? 49.633 14.174  36.720  1.00 46.86  ? 56  TYR F CB  1 
ATOM   6156 C  CG  . TYR F  2  56  ? 50.457 15.403  37.006  1.00 46.23  ? 56  TYR F CG  1 
ATOM   6157 C  CD1 . TYR F  2  56  ? 50.714 16.337  36.011  1.00 45.85  ? 56  TYR F CD1 1 
ATOM   6158 C  CD2 . TYR F  2  56  ? 50.961 15.652  38.288  1.00 45.41  ? 56  TYR F CD2 1 
ATOM   6159 C  CE1 . TYR F  2  56  ? 51.452 17.493  36.276  1.00 47.04  ? 56  TYR F CE1 1 
ATOM   6160 C  CE2 . TYR F  2  56  ? 51.698 16.805  38.562  1.00 46.10  ? 56  TYR F CE2 1 
ATOM   6161 C  CZ  . TYR F  2  56  ? 51.937 17.716  37.553  1.00 47.14  ? 56  TYR F CZ  1 
ATOM   6162 O  OH  . TYR F  2  56  ? 52.674 18.849  37.815  1.00 49.27  ? 56  TYR F OH  1 
ATOM   6163 N  N   . THR F  2  57  ? 46.689 12.526  37.588  1.00 49.56  ? 57  THR F N   1 
ATOM   6164 C  CA  . THR F  2  57  ? 46.011 11.249  37.390  1.00 50.48  ? 57  THR F CA  1 
ATOM   6165 C  C   . THR F  2  57  ? 44.613 11.364  36.793  1.00 48.12  ? 57  THR F C   1 
ATOM   6166 O  O   . THR F  2  57  ? 43.920 12.354  36.984  1.00 46.58  ? 57  THR F O   1 
ATOM   6167 C  CB  . THR F  2  57  ? 45.926 10.451  38.713  1.00 51.53  ? 57  THR F CB  1 
ATOM   6168 O  OG1 . THR F  2  57  ? 45.267 11.237  39.710  1.00 54.16  ? 57  THR F OG1 1 
ATOM   6169 C  CG2 . THR F  2  57  ? 47.313 10.096  39.199  1.00 50.47  ? 57  THR F CG2 1 
ATOM   6170 N  N   . PRO F  2  58  ? 44.198 10.345  36.041  1.00 47.68  ? 58  PRO F N   1 
ATOM   6171 C  CA  . PRO F  2  58  ? 42.874 10.359  35.425  1.00 48.11  ? 58  PRO F CA  1 
ATOM   6172 C  C   . PRO F  2  58  ? 41.815 10.562  36.485  1.00 48.09  ? 58  PRO F C   1 
ATOM   6173 O  O   . PRO F  2  58  ? 40.840 11.291  36.266  1.00 49.31  ? 58  PRO F O   1 
ATOM   6174 C  CB  . PRO F  2  58  ? 42.794 8.992   34.755  1.00 48.04  ? 58  PRO F CB  1 
ATOM   6175 C  CG  . PRO F  2  58  ? 44.212 8.783   34.299  1.00 48.36  ? 58  PRO F CG  1 
ATOM   6176 C  CD  . PRO F  2  58  ? 44.996 9.212   35.542  1.00 47.45  ? 58  PRO F CD  1 
ATOM   6177 N  N   . ALA F  2  59  ? 42.027 9.930   37.634  1.00 47.17  ? 59  ALA F N   1 
ATOM   6178 C  CA  . ALA F  2  59  ? 41.105 10.025  38.758  1.00 46.94  ? 59  ALA F CA  1 
ATOM   6179 C  C   . ALA F  2  59  ? 40.876 11.481  39.133  1.00 46.99  ? 59  ALA F C   1 
ATOM   6180 O  O   . ALA F  2  59  ? 39.725 11.959  39.161  1.00 44.63  ? 59  ALA F O   1 
ATOM   6181 C  CB  . ALA F  2  59  ? 41.668 9.279   39.944  1.00 48.54  ? 59  ALA F CB  1 
ATOM   6182 N  N   . PHE F  2  60  ? 41.974 12.190  39.410  1.00 46.30  ? 60  PHE F N   1 
ATOM   6183 C  CA  . PHE F  2  60  ? 41.845 13.588  39.775  1.00 48.56  ? 60  PHE F CA  1 
ATOM   6184 C  C   . PHE F  2  60  ? 41.300 14.454  38.659  1.00 49.18  ? 60  PHE F C   1 
ATOM   6185 O  O   . PHE F  2  60  ? 40.491 15.360  38.898  1.00 48.96  ? 60  PHE F O   1 
ATOM   6186 C  CB  . PHE F  2  60  ? 43.154 14.211  40.216  1.00 51.03  ? 60  PHE F CB  1 
ATOM   6187 C  CG  . PHE F  2  60  ? 42.960 15.573  40.824  1.00 57.18  ? 60  PHE F CG  1 
ATOM   6188 C  CD1 . PHE F  2  60  ? 42.520 15.700  42.141  1.00 57.59  ? 60  PHE F CD1 1 
ATOM   6189 C  CD2 . PHE F  2  60  ? 43.121 16.727  40.052  1.00 58.75  ? 60  PHE F CD2 1 
ATOM   6190 C  CE1 . PHE F  2  60  ? 42.240 16.951  42.679  1.00 60.63  ? 60  PHE F CE1 1 
ATOM   6191 C  CE2 . PHE F  2  60  ? 42.840 17.990  40.582  1.00 59.88  ? 60  PHE F CE2 1 
ATOM   6192 C  CZ  . PHE F  2  60  ? 42.399 18.102  41.893  1.00 60.41  ? 60  PHE F CZ  1 
ATOM   6193 N  N   . ARG F  2  61  ? 41.754 14.185  37.440  1.00 48.50  ? 61  ARG F N   1 
ATOM   6194 C  CA  . ARG F  2  61  ? 41.307 14.965  36.296  1.00 46.93  ? 61  ARG F CA  1 
ATOM   6195 C  C   . ARG F  2  61  ? 39.792 14.829  36.155  1.00 45.75  ? 61  ARG F C   1 
ATOM   6196 O  O   . ARG F  2  61  ? 39.101 15.808  35.840  1.00 44.27  ? 61  ARG F O   1 
ATOM   6197 C  CB  . ARG F  2  61  ? 42.042 14.510  35.022  1.00 43.63  ? 61  ARG F CB  1 
ATOM   6198 C  CG  . ARG F  2  61  ? 43.530 14.868  35.024  1.00 41.53  ? 61  ARG F CG  1 
ATOM   6199 C  CD  . ARG F  2  61  ? 44.202 14.381  33.762  1.00 41.87  ? 61  ARG F CD  1 
ATOM   6200 N  NE  . ARG F  2  61  ? 45.668 14.457  33.807  1.00 39.82  ? 61  ARG F NE  1 
ATOM   6201 C  CZ  . ARG F  2  61  ? 46.377 15.589  33.758  1.00 40.01  ? 61  ARG F CZ  1 
ATOM   6202 N  NH1 . ARG F  2  61  ? 47.708 15.551  33.791  1.00 33.10  ? 61  ARG F NH1 1 
ATOM   6203 N  NH2 . ARG F  2  61  ? 45.757 16.765  33.679  1.00 40.31  ? 61  ARG F NH2 1 
ATOM   6204 N  N   . ALA F  2  62  ? 39.282 13.626  36.424  1.00 45.04  ? 62  ALA F N   1 
ATOM   6205 C  CA  . ALA F  2  62  ? 37.848 13.397  36.324  1.00 45.33  ? 62  ALA F CA  1 
ATOM   6206 C  C   . ALA F  2  62  ? 37.155 14.247  37.377  1.00 46.01  ? 62  ALA F C   1 
ATOM   6207 O  O   . ALA F  2  62  ? 36.088 14.807  37.118  1.00 46.38  ? 62  ALA F O   1 
ATOM   6208 C  CB  . ALA F  2  62  ? 37.514 11.945  36.521  1.00 44.77  ? 62  ALA F CB  1 
ATOM   6209 N  N   . HIS F  2  63  ? 37.766 14.352  38.560  1.00 44.92  ? 63  HIS F N   1 
ATOM   6210 C  CA  . HIS F  2  63  ? 37.186 15.170  39.616  1.00 45.44  ? 63  HIS F CA  1 
ATOM   6211 C  C   . HIS F  2  63  ? 37.130 16.650  39.164  1.00 44.25  ? 63  HIS F C   1 
ATOM   6212 O  O   . HIS F  2  63  ? 36.093 17.304  39.280  1.00 43.26  ? 63  HIS F O   1 
ATOM   6213 C  CB  . HIS F  2  63  ? 37.993 15.032  40.923  1.00 44.76  ? 63  HIS F CB  1 
ATOM   6214 C  CG  . HIS F  2  63  ? 37.655 16.075  41.943  1.00 45.06  ? 63  HIS F CG  1 
ATOM   6215 N  ND1 . HIS F  2  63  ? 36.408 16.173  42.523  1.00 45.27  ? 63  HIS F ND1 1 
ATOM   6216 C  CD2 . HIS F  2  63  ? 38.368 17.133  42.400  1.00 46.52  ? 63  HIS F CD2 1 
ATOM   6217 C  CE1 . HIS F  2  63  ? 36.364 17.251  43.287  1.00 46.62  ? 63  HIS F CE1 1 
ATOM   6218 N  NE2 . HIS F  2  63  ? 37.540 17.853  43.229  1.00 47.35  ? 63  HIS F NE2 1 
ATOM   6219 N  N   . ALA F  2  64  ? 38.241 17.168  38.644  1.00 44.56  ? 64  ALA F N   1 
ATOM   6220 C  CA  . ALA F  2  64  ? 38.291 18.559  38.161  1.00 43.73  ? 64  ALA F CA  1 
ATOM   6221 C  C   . ALA F  2  64  ? 37.236 18.779  37.054  1.00 43.56  ? 64  ALA F C   1 
ATOM   6222 O  O   . ALA F  2  64  ? 36.632 19.864  36.959  1.00 40.38  ? 64  ALA F O   1 
ATOM   6223 C  CB  . ALA F  2  64  ? 39.702 18.903  37.646  1.00 40.29  ? 64  ALA F CB  1 
ATOM   6224 N  N   . THR F  2  65  ? 37.010 17.743  36.238  1.00 41.53  ? 65  THR F N   1 
ATOM   6225 C  CA  . THR F  2  65  ? 36.009 17.817  35.189  1.00 44.19  ? 65  THR F CA  1 
ATOM   6226 C  C   . THR F  2  65  ? 34.656 18.095  35.841  1.00 46.50  ? 65  THR F C   1 
ATOM   6227 O  O   . THR F  2  65  ? 33.879 18.931  35.368  1.00 47.65  ? 65  THR F O   1 
ATOM   6228 C  CB  . THR F  2  65  ? 35.891 16.487  34.409  1.00 44.09  ? 65  THR F CB  1 
ATOM   6229 O  OG1 . THR F  2  65  ? 37.067 16.280  33.624  1.00 42.92  ? 65  THR F OG1 1 
ATOM   6230 C  CG2 . THR F  2  65  ? 34.656 16.502  33.491  1.00 43.96  ? 65  THR F CG2 1 
ATOM   6231 N  N   . ARG F  2  66  ? 34.382 17.379  36.931  1.00 46.92  ? 66  ARG F N   1 
ATOM   6232 C  CA  . ARG F  2  66  ? 33.132 17.545  37.644  1.00 45.07  ? 66  ARG F CA  1 
ATOM   6233 C  C   . ARG F  2  66  ? 33.050 18.931  38.277  1.00 44.16  ? 66  ARG F C   1 
ATOM   6234 O  O   . ARG F  2  66  ? 32.028 19.604  38.163  1.00 45.29  ? 66  ARG F O   1 
ATOM   6235 C  CB  . ARG F  2  66  ? 32.977 16.466  38.728  1.00 46.79  ? 66  ARG F CB  1 
ATOM   6236 C  CG  . ARG F  2  66  ? 32.758 15.047  38.207  1.00 45.17  ? 66  ARG F CG  1 
ATOM   6237 C  CD  . ARG F  2  66  ? 32.429 14.098  39.355  1.00 44.67  ? 66  ARG F CD  1 
ATOM   6238 N  NE  . ARG F  2  66  ? 33.584 13.696  40.158  1.00 44.47  ? 66  ARG F NE  1 
ATOM   6239 C  CZ  . ARG F  2  66  ? 34.404 12.700  39.836  1.00 46.31  ? 66  ARG F CZ  1 
ATOM   6240 N  NH1 . ARG F  2  66  ? 35.431 12.394  40.618  1.00 48.03  ? 66  ARG F NH1 1 
ATOM   6241 N  NH2 . ARG F  2  66  ? 34.202 12.002  38.726  1.00 46.15  ? 66  ARG F NH2 1 
ATOM   6242 N  N   . VAL F  2  67  ? 34.117 19.370  38.935  1.00 41.85  ? 67  VAL F N   1 
ATOM   6243 C  CA  . VAL F  2  67  ? 34.085 20.682  39.560  1.00 43.85  ? 67  VAL F CA  1 
ATOM   6244 C  C   . VAL F  2  67  ? 33.757 21.772  38.527  1.00 46.00  ? 67  VAL F C   1 
ATOM   6245 O  O   . VAL F  2  67  ? 32.733 22.454  38.648  1.00 45.05  ? 67  VAL F O   1 
ATOM   6246 C  CB  . VAL F  2  67  ? 35.422 21.032  40.241  1.00 43.52  ? 67  VAL F CB  1 
ATOM   6247 C  CG1 . VAL F  2  67  ? 35.328 22.403  40.896  1.00 42.74  ? 67  VAL F CG1 1 
ATOM   6248 C  CG2 . VAL F  2  67  ? 35.766 19.976  41.258  1.00 44.73  ? 67  VAL F CG2 1 
ATOM   6249 N  N   . LEU F  2  68  ? 34.614 21.925  37.515  1.00 47.24  ? 68  LEU F N   1 
ATOM   6250 C  CA  . LEU F  2  68  ? 34.404 22.930  36.482  1.00 47.56  ? 68  LEU F CA  1 
ATOM   6251 C  C   . LEU F  2  68  ? 32.985 22.839  35.909  1.00 48.10  ? 68  LEU F C   1 
ATOM   6252 O  O   . LEU F  2  68  ? 32.354 23.872  35.655  1.00 46.68  ? 68  LEU F O   1 
ATOM   6253 C  CB  . LEU F  2  68  ? 35.455 22.774  35.376  1.00 49.75  ? 68  LEU F CB  1 
ATOM   6254 C  CG  . LEU F  2  68  ? 36.934 22.868  35.804  1.00 50.27  ? 68  LEU F CG  1 
ATOM   6255 C  CD1 . LEU F  2  68  ? 37.806 23.250  34.606  1.00 49.14  ? 68  LEU F CD1 1 
ATOM   6256 C  CD2 . LEU F  2  68  ? 37.090 23.908  36.899  1.00 51.52  ? 68  LEU F CD2 1 
ATOM   6257 N  N   . GLY F  2  69  ? 32.491 21.612  35.721  1.00 47.86  ? 69  GLY F N   1 
ATOM   6258 C  CA  . GLY F  2  69  ? 31.140 21.417  35.212  1.00 49.99  ? 69  GLY F CA  1 
ATOM   6259 C  C   . GLY F  2  69  ? 30.145 22.024  36.192  1.00 51.46  ? 69  GLY F C   1 
ATOM   6260 O  O   . GLY F  2  69  ? 29.114 22.588  35.793  1.00 50.33  ? 69  GLY F O   1 
ATOM   6261 N  N   . GLY F  2  70  ? 30.460 21.895  37.482  1.00 52.44  ? 70  GLY F N   1 
ATOM   6262 C  CA  . GLY F  2  70  ? 29.614 22.454  38.516  1.00 53.49  ? 70  GLY F CA  1 
ATOM   6263 C  C   . GLY F  2  70  ? 29.594 23.956  38.322  1.00 54.40  ? 70  GLY F C   1 
ATOM   6264 O  O   . GLY F  2  70  ? 28.525 24.558  38.233  1.00 54.61  ? 70  GLY F O   1 
ATOM   6265 N  N   . LEU F  2  71  ? 30.778 24.564  38.248  1.00 54.73  ? 71  LEU F N   1 
ATOM   6266 C  CA  . LEU F  2  71  ? 30.880 26.008  38.032  1.00 54.66  ? 71  LEU F CA  1 
ATOM   6267 C  C   . LEU F  2  71  ? 30.083 26.411  36.805  1.00 53.77  ? 71  LEU F C   1 
ATOM   6268 O  O   . LEU F  2  71  ? 29.274 27.324  36.860  1.00 52.98  ? 71  LEU F O   1 
ATOM   6269 C  CB  . LEU F  2  71  ? 32.337 26.423  37.819  1.00 54.92  ? 71  LEU F CB  1 
ATOM   6270 C  CG  . LEU F  2  71  ? 33.148 26.759  39.064  1.00 55.78  ? 71  LEU F CG  1 
ATOM   6271 C  CD1 . LEU F  2  71  ? 34.616 26.995  38.713  1.00 55.79  ? 71  LEU F CD1 1 
ATOM   6272 C  CD2 . LEU F  2  71  ? 32.545 27.994  39.699  1.00 56.44  ? 71  LEU F CD2 1 
ATOM   6273 N  N   . ASP F  2  72  ? 30.317 25.714  35.698  1.00 53.03  ? 72  ASP F N   1 
ATOM   6274 C  CA  . ASP F  2  72  ? 29.635 26.024  34.466  1.00 52.63  ? 72  ASP F CA  1 
ATOM   6275 C  C   . ASP F  2  72  ? 28.134 26.128  34.670  1.00 54.00  ? 72  ASP F C   1 
ATOM   6276 O  O   . ASP F  2  72  ? 27.513 27.099  34.221  1.00 52.60  ? 72  ASP F O   1 
ATOM   6277 C  CB  . ASP F  2  72  ? 29.949 24.972  33.418  1.00 53.46  ? 72  ASP F CB  1 
ATOM   6278 C  CG  . ASP F  2  72  ? 29.372 25.314  32.072  1.00 54.79  ? 72  ASP F CG  1 
ATOM   6279 O  OD1 . ASP F  2  72  ? 28.347 24.709  31.694  1.00 54.65  ? 72  ASP F OD1 1 
ATOM   6280 O  OD2 . ASP F  2  72  ? 29.940 26.203  31.401  1.00 57.43  ? 72  ASP F OD2 1 
ATOM   6281 N  N   . MET F  2  73  ? 27.551 25.145  35.355  1.00 55.30  ? 73  MET F N   1 
ATOM   6282 C  CA  . MET F  2  73  ? 26.105 25.167  35.581  1.00 55.90  ? 73  MET F CA  1 
ATOM   6283 C  C   . MET F  2  73  ? 25.670 26.425  36.315  1.00 53.99  ? 73  MET F C   1 
ATOM   6284 O  O   . MET F  2  73  ? 24.675 27.036  35.953  1.00 54.49  ? 73  MET F O   1 
ATOM   6285 C  CB  . MET F  2  73  ? 25.649 23.904  36.325  1.00 57.26  ? 73  MET F CB  1 
ATOM   6286 C  CG  . MET F  2  73  ? 25.833 22.641  35.493  1.00 59.45  ? 73  MET F CG  1 
ATOM   6287 S  SD  . MET F  2  73  ? 25.082 21.126  36.140  1.00 62.13  ? 73  MET F SD  1 
ATOM   6288 C  CE  . MET F  2  73  ? 26.286 20.725  37.406  1.00 60.38  ? 73  MET F CE  1 
ATOM   6289 N  N   . CYS F  2  74  ? 26.431 26.829  37.326  1.00 52.62  ? 74  CYS F N   1 
ATOM   6290 C  CA  . CYS F  2  74  ? 26.089 28.037  38.083  1.00 52.12  ? 74  CYS F CA  1 
ATOM   6291 C  C   . CYS F  2  74  ? 26.161 29.281  37.202  1.00 51.97  ? 74  CYS F C   1 
ATOM   6292 O  O   . CYS F  2  74  ? 25.248 30.128  37.192  1.00 48.81  ? 74  CYS F O   1 
ATOM   6293 C  CB  . CYS F  2  74  ? 27.031 28.207  39.275  1.00 50.62  ? 74  CYS F CB  1 
ATOM   6294 S  SG  . CYS F  2  74  ? 26.891 26.864  40.430  1.00 56.11  ? 74  CYS F SG  1 
ATOM   6295 N  N   . VAL F  2  75  ? 27.262 29.375  36.466  1.00 51.37  ? 75  VAL F N   1 
ATOM   6296 C  CA  . VAL F  2  75  ? 27.496 30.497  35.577  1.00 49.99  ? 75  VAL F CA  1 
ATOM   6297 C  C   . VAL F  2  75  ? 26.377 30.549  34.535  1.00 47.56  ? 75  VAL F C   1 
ATOM   6298 O  O   . VAL F  2  75  ? 25.788 31.601  34.278  1.00 43.00  ? 75  VAL F O   1 
ATOM   6299 C  CB  . VAL F  2  75  ? 28.868 30.337  34.893  1.00 50.49  ? 75  VAL F CB  1 
ATOM   6300 C  CG1 . VAL F  2  75  ? 28.966 31.233  33.660  1.00 50.84  ? 75  VAL F CG1 1 
ATOM   6301 C  CG2 . VAL F  2  75  ? 29.968 30.684  35.890  1.00 49.70  ? 75  VAL F CG2 1 
ATOM   6302 N  N   . ALA F  2  76  ? 26.081 29.390  33.959  1.00 46.80  ? 76  ALA F N   1 
ATOM   6303 C  CA  . ALA F  2  76  ? 25.051 29.295  32.945  1.00 47.40  ? 76  ALA F CA  1 
ATOM   6304 C  C   . ALA F  2  76  ? 23.701 29.742  33.514  1.00 48.68  ? 76  ALA F C   1 
ATOM   6305 O  O   . ALA F  2  76  ? 22.840 30.246  32.779  1.00 47.74  ? 76  ALA F O   1 
ATOM   6306 C  CB  . ALA F  2  76  ? 24.966 27.859  32.435  1.00 45.58  ? 76  ALA F CB  1 
ATOM   6307 N  N   . LEU F  2  77  ? 23.532 29.567  34.827  1.00 48.58  ? 77  LEU F N   1 
ATOM   6308 C  CA  . LEU F  2  77  ? 22.290 29.931  35.493  1.00 48.57  ? 77  LEU F CA  1 
ATOM   6309 C  C   . LEU F  2  77  ? 22.269 31.263  36.243  1.00 49.57  ? 77  LEU F C   1 
ATOM   6310 O  O   . LEU F  2  77  ? 21.264 31.592  36.865  1.00 48.50  ? 77  LEU F O   1 
ATOM   6311 C  CB  . LEU F  2  77  ? 21.875 28.815  36.441  1.00 49.24  ? 77  LEU F CB  1 
ATOM   6312 C  CG  . LEU F  2  77  ? 21.530 27.499  35.752  1.00 49.36  ? 77  LEU F CG  1 
ATOM   6313 C  CD1 . LEU F  2  77  ? 21.394 26.384  36.791  1.00 47.70  ? 77  LEU F CD1 1 
ATOM   6314 C  CD2 . LEU F  2  77  ? 20.250 27.682  34.956  1.00 48.69  ? 77  LEU F CD2 1 
ATOM   6315 N  N   . LEU F  2  78  ? 23.350 32.034  36.195  1.00 50.96  ? 78  LEU F N   1 
ATOM   6316 C  CA  . LEU F  2  78  ? 23.366 33.322  36.886  1.00 52.90  ? 78  LEU F CA  1 
ATOM   6317 C  C   . LEU F  2  78  ? 22.186 34.231  36.502  1.00 54.74  ? 78  LEU F C   1 
ATOM   6318 O  O   . LEU F  2  78  ? 21.877 35.196  37.199  1.00 53.62  ? 78  LEU F O   1 
ATOM   6319 C  CB  . LEU F  2  78  ? 24.676 34.054  36.599  1.00 52.80  ? 78  LEU F CB  1 
ATOM   6320 C  CG  . LEU F  2  78  ? 25.904 33.383  37.194  1.00 55.91  ? 78  LEU F CG  1 
ATOM   6321 C  CD1 . LEU F  2  78  ? 27.147 34.088  36.699  1.00 56.24  ? 78  LEU F CD1 1 
ATOM   6322 C  CD2 . LEU F  2  78  ? 25.815 33.415  38.734  1.00 58.72  ? 78  LEU F CD2 1 
ATOM   6323 N  N   . ASP F  2  79  ? 21.520 33.919  35.402  1.00 57.24  ? 79  ASP F N   1 
ATOM   6324 C  CA  . ASP F  2  79  ? 20.420 34.751  34.936  1.00 61.33  ? 79  ASP F CA  1 
ATOM   6325 C  C   . ASP F  2  79  ? 19.051 34.186  35.295  1.00 62.61  ? 79  ASP F C   1 
ATOM   6326 O  O   . ASP F  2  79  ? 18.025 34.799  34.992  1.00 63.55  ? 79  ASP F O   1 
ATOM   6327 C  CB  . ASP F  2  79  ? 20.536 34.951  33.413  1.00 61.03  ? 79  ASP F CB  1 
ATOM   6328 C  CG  . ASP F  2  79  ? 20.428 33.649  32.640  1.00 62.34  ? 79  ASP F CG  1 
ATOM   6329 O  OD1 . ASP F  2  79  ? 19.398 33.439  31.967  1.00 64.21  ? 79  ASP F OD1 1 
ATOM   6330 O  OD2 . ASP F  2  79  ? 21.364 32.822  32.705  1.00 62.31  ? 79  ASP F OD2 1 
ATOM   6331 N  N   . ASP F  2  80  ? 19.050 33.024  35.934  1.00 64.14  ? 80  ASP F N   1 
ATOM   6332 C  CA  . ASP F  2  80  ? 17.817 32.353  36.337  1.00 65.50  ? 80  ASP F CA  1 
ATOM   6333 C  C   . ASP F  2  80  ? 17.871 32.084  37.840  1.00 65.68  ? 80  ASP F C   1 
ATOM   6334 O  O   . ASP F  2  80  ? 18.137 30.966  38.275  1.00 63.82  ? 80  ASP F O   1 
ATOM   6335 C  CB  . ASP F  2  80  ? 17.684 31.033  35.589  1.00 66.78  ? 80  ASP F CB  1 
ATOM   6336 C  CG  . ASP F  2  80  ? 16.271 30.534  35.553  1.00 68.54  ? 80  ASP F CG  1 
ATOM   6337 O  OD1 . ASP F  2  80  ? 15.458 31.018  36.371  1.00 69.55  ? 80  ASP F OD1 1 
ATOM   6338 O  OD2 . ASP F  2  80  ? 15.985 29.657  34.707  1.00 69.65  ? 80  ASP F OD2 1 
ATOM   6339 N  N   . GLU F  2  81  ? 17.625 33.131  38.622  1.00 67.29  ? 81  GLU F N   1 
ATOM   6340 C  CA  . GLU F  2  81  ? 17.655 33.068  40.080  1.00 69.52  ? 81  GLU F CA  1 
ATOM   6341 C  C   . GLU F  2  81  ? 17.084 31.771  40.652  1.00 69.32  ? 81  GLU F C   1 
ATOM   6342 O  O   . GLU F  2  81  ? 17.746 31.047  41.413  1.00 69.04  ? 81  GLU F O   1 
ATOM   6343 C  CB  . GLU F  2  81  ? 16.876 34.252  40.656  1.00 71.19  ? 81  GLU F CB  1 
ATOM   6344 C  CG  . GLU F  2  81  ? 17.126 34.498  42.133  1.00 74.55  ? 81  GLU F CG  1 
ATOM   6345 C  CD  . GLU F  2  81  ? 18.532 34.999  42.408  1.00 76.38  ? 81  GLU F CD  1 
ATOM   6346 O  OE1 . GLU F  2  81  ? 18.881 35.156  43.600  1.00 78.13  ? 81  GLU F OE1 1 
ATOM   6347 O  OE2 . GLU F  2  81  ? 19.284 35.238  41.439  1.00 76.49  ? 81  GLU F OE2 1 
ATOM   6348 N  N   . SER F  2  82  ? 15.838 31.494  40.285  1.00 68.35  ? 82  SER F N   1 
ATOM   6349 C  CA  . SER F  2  82  ? 15.138 30.301  40.742  1.00 67.04  ? 82  SER F CA  1 
ATOM   6350 C  C   . SER F  2  82  ? 15.884 28.977  40.538  1.00 65.38  ? 82  SER F C   1 
ATOM   6351 O  O   . SER F  2  82  ? 16.091 28.221  41.497  1.00 66.36  ? 82  SER F O   1 
ATOM   6352 C  CB  . SER F  2  82  ? 13.767 30.224  40.062  1.00 67.63  ? 82  SER F CB  1 
ATOM   6353 O  OG  . SER F  2  82  ? 13.135 28.988  40.326  1.00 67.55  ? 82  SER F OG  1 
ATOM   6354 N  N   . VAL F  2  83  ? 16.286 28.684  39.302  1.00 62.58  ? 83  VAL F N   1 
ATOM   6355 C  CA  . VAL F  2  83  ? 16.985 27.430  39.035  1.00 59.90  ? 83  VAL F CA  1 
ATOM   6356 C  C   . VAL F  2  83  ? 18.434 27.493  39.478  1.00 58.76  ? 83  VAL F C   1 
ATOM   6357 O  O   . VAL F  2  83  ? 19.076 26.464  39.679  1.00 56.43  ? 83  VAL F O   1 
ATOM   6358 C  CB  . VAL F  2  83  ? 16.929 27.046  37.553  1.00 60.00  ? 83  VAL F CB  1 
ATOM   6359 C  CG1 . VAL F  2  83  ? 17.520 25.659  37.360  1.00 59.53  ? 83  VAL F CG1 1 
ATOM   6360 C  CG2 . VAL F  2  83  ? 15.495 27.069  37.060  1.00 56.82  ? 83  VAL F CG2 1 
ATOM   6361 N  N   . LEU F  2  84  ? 18.953 28.706  39.628  1.00 58.28  ? 84  LEU F N   1 
ATOM   6362 C  CA  . LEU F  2  84  ? 20.323 28.858  40.083  1.00 57.80  ? 84  LEU F CA  1 
ATOM   6363 C  C   . LEU F  2  84  ? 20.379 28.305  41.499  1.00 58.43  ? 84  LEU F C   1 
ATOM   6364 O  O   . LEU F  2  84  ? 21.094 27.337  41.772  1.00 59.06  ? 84  LEU F O   1 
ATOM   6365 C  CB  . LEU F  2  84  ? 20.740 30.337  40.081  1.00 57.07  ? 84  LEU F CB  1 
ATOM   6366 C  CG  . LEU F  2  84  ? 22.056 30.702  40.789  1.00 56.51  ? 84  LEU F CG  1 
ATOM   6367 C  CD1 . LEU F  2  84  ? 23.184 29.884  40.231  1.00 56.51  ? 84  LEU F CD1 1 
ATOM   6368 C  CD2 . LEU F  2  84  ? 22.352 32.171  40.617  1.00 56.19  ? 84  LEU F CD2 1 
ATOM   6369 N  N   . ASN F  2  85  ? 19.596 28.915  42.387  1.00 58.69  ? 85  ASN F N   1 
ATOM   6370 C  CA  . ASN F  2  85  ? 19.556 28.512  43.786  1.00 57.95  ? 85  ASN F CA  1 
ATOM   6371 C  C   . ASN F  2  85  ? 19.221 27.023  43.975  1.00 57.02  ? 85  ASN F C   1 
ATOM   6372 O  O   . ASN F  2  85  ? 19.720 26.367  44.905  1.00 54.22  ? 85  ASN F O   1 
ATOM   6373 C  CB  . ASN F  2  85  ? 18.577 29.408  44.554  1.00 58.33  ? 85  ASN F CB  1 
ATOM   6374 C  CG  . ASN F  2  85  ? 19.063 30.854  44.652  1.00 59.65  ? 85  ASN F CG  1 
ATOM   6375 O  OD1 . ASN F  2  85  ? 20.263 31.115  44.837  1.00 60.12  ? 85  ASN F OD1 1 
ATOM   6376 N  ND2 . ASN F  2  85  ? 18.135 31.800  44.543  1.00 58.62  ? 85  ASN F ND2 1 
ATOM   6377 N  N   . THR F  2  86  ? 18.384 26.488  43.090  1.00 56.68  ? 86  THR F N   1 
ATOM   6378 C  CA  . THR F  2  86  ? 18.029 25.078  43.165  1.00 56.29  ? 86  THR F CA  1 
ATOM   6379 C  C   . THR F  2  86  ? 19.319 24.304  43.009  1.00 58.68  ? 86  THR F C   1 
ATOM   6380 O  O   . THR F  2  86  ? 19.607 23.402  43.786  1.00 60.12  ? 86  THR F O   1 
ATOM   6381 C  CB  . THR F  2  86  ? 17.085 24.647  42.025  1.00 55.27  ? 86  THR F CB  1 
ATOM   6382 O  OG1 . THR F  2  86  ? 15.849 25.372  42.111  1.00 54.12  ? 86  THR F OG1 1 
ATOM   6383 C  CG2 . THR F  2  86  ? 16.811 23.142  42.098  1.00 51.42  ? 86  THR F CG2 1 
ATOM   6384 N  N   . GLN F  2  87  ? 20.103 24.676  41.998  1.00 61.44  ? 87  GLN F N   1 
ATOM   6385 C  CA  . GLN F  2  87  ? 21.378 24.012  41.715  1.00 62.06  ? 87  GLN F CA  1 
ATOM   6386 C  C   . GLN F  2  87  ? 22.433 24.289  42.793  1.00 61.27  ? 87  GLN F C   1 
ATOM   6387 O  O   . GLN F  2  87  ? 23.261 23.430  43.098  1.00 58.34  ? 87  GLN F O   1 
ATOM   6388 C  CB  . GLN F  2  87  ? 21.890 24.437  40.332  1.00 62.80  ? 87  GLN F CB  1 
ATOM   6389 C  CG  . GLN F  2  87  ? 23.233 23.828  39.924  1.00 63.84  ? 87  GLN F CG  1 
ATOM   6390 C  CD  . GLN F  2  87  ? 23.238 22.315  39.973  1.00 65.12  ? 87  GLN F CD  1 
ATOM   6391 O  OE1 . GLN F  2  87  ? 22.228 21.673  39.677  1.00 64.23  ? 87  GLN F OE1 1 
ATOM   6392 N  NE2 . GLN F  2  87  ? 24.386 21.735  40.326  1.00 63.39  ? 87  GLN F NE2 1 
ATOM   6393 N  N   . LEU F  2  88  ? 22.406 25.484  43.368  1.00 61.72  ? 88  LEU F N   1 
ATOM   6394 C  CA  . LEU F  2  88  ? 23.354 25.802  44.429  1.00 64.42  ? 88  LEU F CA  1 
ATOM   6395 C  C   . LEU F  2  88  ? 23.096 24.888  45.638  1.00 65.44  ? 88  LEU F C   1 
ATOM   6396 O  O   . LEU F  2  88  ? 24.029 24.437  46.312  1.00 64.91  ? 88  LEU F O   1 
ATOM   6397 C  CB  . LEU F  2  88  ? 23.208 27.266  44.857  1.00 64.19  ? 88  LEU F CB  1 
ATOM   6398 C  CG  . LEU F  2  88  ? 23.651 28.339  43.866  1.00 63.76  ? 88  LEU F CG  1 
ATOM   6399 C  CD1 . LEU F  2  88  ? 23.370 29.709  44.458  1.00 62.76  ? 88  LEU F CD1 1 
ATOM   6400 C  CD2 . LEU F  2  88  ? 25.132 28.163  43.562  1.00 63.09  ? 88  LEU F CD2 1 
ATOM   6401 N  N   . ALA F  2  89  ? 21.820 24.623  45.897  1.00 65.94  ? 89  ALA F N   1 
ATOM   6402 C  CA  . ALA F  2  89  ? 21.432 23.768  47.001  1.00 67.28  ? 89  ALA F CA  1 
ATOM   6403 C  C   . ALA F  2  89  ? 21.916 22.343  46.745  1.00 68.04  ? 89  ALA F C   1 
ATOM   6404 O  O   . ALA F  2  89  ? 22.339 21.637  47.669  1.00 68.41  ? 89  ALA F O   1 
ATOM   6405 C  CB  . ALA F  2  89  ? 19.924 23.794  47.174  1.00 66.75  ? 89  ALA F CB  1 
ATOM   6406 N  N   . HIS F  2  90  ? 21.855 21.911  45.494  1.00 68.62  ? 90  HIS F N   1 
ATOM   6407 C  CA  . HIS F  2  90  ? 22.315 20.567  45.159  1.00 71.29  ? 90  HIS F CA  1 
ATOM   6408 C  C   . HIS F  2  90  ? 23.827 20.480  45.433  1.00 72.20  ? 90  HIS F C   1 
ATOM   6409 O  O   . HIS F  2  90  ? 24.340 19.457  45.891  1.00 72.06  ? 90  HIS F O   1 
ATOM   6410 C  CB  . HIS F  2  90  ? 22.032 20.260  43.691  1.00 71.93  ? 90  HIS F CB  1 
ATOM   6411 C  CG  . HIS F  2  90  ? 22.355 18.854  43.295  1.00 72.37  ? 90  HIS F CG  1 
ATOM   6412 N  ND1 . HIS F  2  90  ? 21.494 17.802  43.516  1.00 72.64  ? 90  HIS F ND1 1 
ATOM   6413 C  CD2 . HIS F  2  90  ? 23.449 18.326  42.700  1.00 72.85  ? 90  HIS F CD2 1 
ATOM   6414 C  CE1 . HIS F  2  90  ? 22.042 16.684  43.070  1.00 73.49  ? 90  HIS F CE1 1 
ATOM   6415 N  NE2 . HIS F  2  90  ? 23.229 16.976  42.569  1.00 72.00  ? 90  HIS F NE2 1 
ATOM   6416 N  N   . LEU F  2  91  ? 24.535 21.566  45.143  1.00 71.97  ? 91  LEU F N   1 
ATOM   6417 C  CA  . LEU F  2  91  ? 25.968 21.617  45.386  1.00 72.93  ? 91  LEU F CA  1 
ATOM   6418 C  C   . LEU F  2  91  ? 26.205 21.731  46.879  1.00 73.04  ? 91  LEU F C   1 
ATOM   6419 O  O   . LEU F  2  91  ? 27.203 21.236  47.403  1.00 73.81  ? 91  LEU F O   1 
ATOM   6420 C  CB  . LEU F  2  91  ? 26.593 22.830  44.690  1.00 73.94  ? 91  LEU F CB  1 
ATOM   6421 C  CG  . LEU F  2  91  ? 26.865 22.692  43.189  1.00 74.17  ? 91  LEU F CG  1 
ATOM   6422 C  CD1 . LEU F  2  91  ? 26.930 24.061  42.539  1.00 73.61  ? 91  LEU F CD1 1 
ATOM   6423 C  CD2 . LEU F  2  91  ? 28.150 21.916  42.983  1.00 73.20  ? 91  LEU F CD2 1 
ATOM   6424 N  N   . ALA F  2  92  ? 25.283 22.407  47.558  1.00 72.78  ? 92  ALA F N   1 
ATOM   6425 C  CA  . ALA F  2  92  ? 25.393 22.587  48.990  1.00 72.49  ? 92  ALA F CA  1 
ATOM   6426 C  C   . ALA F  2  92  ? 25.402 21.217  49.663  1.00 72.53  ? 92  ALA F C   1 
ATOM   6427 O  O   . ALA F  2  92  ? 26.222 20.961  50.555  1.00 71.12  ? 92  ALA F O   1 
ATOM   6428 C  CB  . ALA F  2  92  ? 24.226 23.426  49.498  1.00 71.69  ? 92  ALA F CB  1 
ATOM   6429 N  N   . SER F  2  93  ? 24.513 20.337  49.209  1.00 72.15  ? 93  SER F N   1 
ATOM   6430 C  CA  . SER F  2  93  ? 24.408 19.004  49.782  1.00 72.99  ? 93  SER F CA  1 
ATOM   6431 C  C   . SER F  2  93  ? 25.517 18.054  49.351  1.00 73.88  ? 93  SER F C   1 
ATOM   6432 O  O   . SER F  2  93  ? 25.731 17.017  49.981  1.00 74.54  ? 93  SER F O   1 
ATOM   6433 C  CB  . SER F  2  93  ? 23.034 18.391  49.466  1.00 73.68  ? 93  SER F CB  1 
ATOM   6434 O  OG  . SER F  2  93  ? 22.921 17.992  48.114  1.00 72.49  ? 93  SER F OG  1 
ATOM   6435 N  N   . GLN F  2  94  ? 26.223 18.391  48.282  1.00 75.41  ? 94  GLN F N   1 
ATOM   6436 C  CA  . GLN F  2  94  ? 27.314 17.535  47.830  1.00 76.33  ? 94  GLN F CA  1 
ATOM   6437 C  C   . GLN F  2  94  ? 28.558 17.841  48.660  1.00 76.13  ? 94  GLN F C   1 
ATOM   6438 O  O   . GLN F  2  94  ? 29.510 17.067  48.670  1.00 74.82  ? 94  GLN F O   1 
ATOM   6439 C  CB  . GLN F  2  94  ? 27.606 17.761  46.346  1.00 77.86  ? 94  GLN F CB  1 
ATOM   6440 C  CG  . GLN F  2  94  ? 26.490 17.304  45.401  1.00 79.07  ? 94  GLN F CG  1 
ATOM   6441 C  CD  . GLN F  2  94  ? 26.788 17.616  43.938  1.00 78.80  ? 94  GLN F CD  1 
ATOM   6442 O  OE1 . GLN F  2  94  ? 27.141 18.750  43.591  1.00 77.38  ? 94  GLN F OE1 1 
ATOM   6443 N  NE2 . GLN F  2  94  ? 26.634 16.613  43.071  1.00 76.66  ? 94  GLN F NE2 1 
ATOM   6444 N  N   . HIS F  2  95  ? 28.532 18.970  49.366  1.00 77.82  ? 95  HIS F N   1 
ATOM   6445 C  CA  . HIS F  2  95  ? 29.653 19.398  50.210  1.00 80.22  ? 95  HIS F CA  1 
ATOM   6446 C  C   . HIS F  2  95  ? 29.324 19.432  51.712  1.00 81.64  ? 95  HIS F C   1 
ATOM   6447 O  O   . HIS F  2  95  ? 30.231 19.411  52.554  1.00 80.70  ? 95  HIS F O   1 
ATOM   6448 C  CB  . HIS F  2  95  ? 30.130 20.801  49.797  1.00 79.62  ? 95  HIS F CB  1 
ATOM   6449 C  CG  . HIS F  2  95  ? 30.772 20.857  48.446  1.00 78.50  ? 95  HIS F CG  1 
ATOM   6450 N  ND1 . HIS F  2  95  ? 30.053 20.740  47.277  1.00 78.19  ? 95  HIS F ND1 1 
ATOM   6451 C  CD2 . HIS F  2  95  ? 32.068 21.000  48.076  1.00 77.63  ? 95  HIS F CD2 1 
ATOM   6452 C  CE1 . HIS F  2  95  ? 30.876 20.803  46.247  1.00 76.85  ? 95  HIS F CE1 1 
ATOM   6453 N  NE2 . HIS F  2  95  ? 32.107 20.962  46.704  1.00 72.50  ? 95  HIS F NE2 1 
ATOM   6454 N  N   . SER F  2  96  ? 28.034 19.500  52.028  1.00 83.13  ? 96  SER F N   1 
ATOM   6455 C  CA  . SER F  2  96  ? 27.534 19.572  53.404  1.00 84.33  ? 96  SER F CA  1 
ATOM   6456 C  C   . SER F  2  96  ? 28.301 18.782  54.471  1.00 84.72  ? 96  SER F C   1 
ATOM   6457 O  O   . SER F  2  96  ? 28.745 19.341  55.479  1.00 83.79  ? 96  SER F O   1 
ATOM   6458 C  CB  . SER F  2  96  ? 26.059 19.151  53.430  1.00 84.75  ? 96  SER F CB  1 
ATOM   6459 O  OG  . SER F  2  96  ? 25.892 17.839  52.910  1.00 85.87  ? 96  SER F OG  1 
ATOM   6460 N  N   . SER F  2  97  ? 28.453 17.484  54.241  1.00 84.87  ? 97  SER F N   1 
ATOM   6461 C  CA  . SER F  2  97  ? 29.136 16.605  55.182  1.00 84.99  ? 97  SER F CA  1 
ATOM   6462 C  C   . SER F  2  97  ? 30.651 16.523  55.016  1.00 83.98  ? 97  SER F C   1 
ATOM   6463 O  O   . SER F  2  97  ? 31.283 15.627  55.572  1.00 84.29  ? 97  SER F O   1 
ATOM   6464 C  CB  . SER F  2  97  ? 28.545 15.199  55.070  1.00 86.09  ? 97  SER F CB  1 
ATOM   6465 O  OG  . SER F  2  97  ? 28.623 14.730  53.732  1.00 88.33  ? 97  SER F OG  1 
ATOM   6466 N  N   . ARG F  2  98  ? 31.242 17.446  54.270  1.00 82.44  ? 98  ARG F N   1 
ATOM   6467 C  CA  . ARG F  2  98  ? 32.684 17.395  54.063  1.00 80.80  ? 98  ARG F CA  1 
ATOM   6468 C  C   . ARG F  2  98  ? 33.480 18.424  54.864  1.00 79.73  ? 98  ARG F C   1 
ATOM   6469 O  O   . ARG F  2  98  ? 34.705 18.464  54.767  1.00 78.65  ? 98  ARG F O   1 
ATOM   6470 C  CB  . ARG F  2  98  ? 33.002 17.511  52.564  1.00 80.82  ? 98  ARG F CB  1 
ATOM   6471 C  CG  . ARG F  2  98  ? 32.370 16.393  51.718  1.00 78.78  ? 98  ARG F CG  1 
ATOM   6472 C  CD  . ARG F  2  98  ? 32.550 16.597  50.212  1.00 76.57  ? 98  ARG F CD  1 
ATOM   6473 N  NE  . ARG F  2  98  ? 31.919 15.531  49.432  1.00 73.47  ? 98  ARG F NE  1 
ATOM   6474 C  CZ  . ARG F  2  98  ? 32.319 14.258  49.427  1.00 72.07  ? 98  ARG F CZ  1 
ATOM   6475 N  NH1 . ARG F  2  98  ? 31.681 13.359  48.682  1.00 68.75  ? 98  ARG F NH1 1 
ATOM   6476 N  NH2 . ARG F  2  98  ? 33.364 13.882  50.157  1.00 69.67  ? 98  ARG F NH2 1 
ATOM   6477 N  N   . GLY F  2  99  ? 32.780 19.231  55.657  1.00 78.61  ? 99  GLY F N   1 
ATOM   6478 C  CA  . GLY F  2  99  ? 33.438 20.237  56.472  1.00 78.07  ? 99  GLY F CA  1 
ATOM   6479 C  C   . GLY F  2  99  ? 34.449 21.075  55.718  1.00 77.75  ? 99  GLY F C   1 
ATOM   6480 O  O   . GLY F  2  99  ? 35.641 21.012  56.014  1.00 78.19  ? 99  GLY F O   1 
ATOM   6481 N  N   . VAL F  2  100 ? 33.976 21.863  54.753  1.00 77.57  ? 100 VAL F N   1 
ATOM   6482 C  CA  . VAL F  2  100 ? 34.855 22.728  53.973  1.00 76.67  ? 100 VAL F CA  1 
ATOM   6483 C  C   . VAL F  2  100 ? 34.757 24.136  54.552  1.00 76.38  ? 100 VAL F C   1 
ATOM   6484 O  O   . VAL F  2  100 ? 33.656 24.673  54.677  1.00 76.42  ? 100 VAL F O   1 
ATOM   6485 C  CB  . VAL F  2  100 ? 34.423 22.751  52.498  1.00 76.94  ? 100 VAL F CB  1 
ATOM   6486 C  CG1 . VAL F  2  100 ? 35.172 23.825  51.738  1.00 76.18  ? 100 VAL F CG1 1 
ATOM   6487 C  CG2 . VAL F  2  100 ? 34.618 21.386  51.885  1.00 74.87  ? 100 VAL F CG2 1 
ATOM   6488 N  N   . SER F  2  101 ? 35.899 24.742  54.882  1.00 75.60  ? 101 SER F N   1 
ATOM   6489 C  CA  . SER F  2  101 ? 35.904 26.084  55.458  1.00 75.98  ? 101 SER F CA  1 
ATOM   6490 C  C   . SER F  2  101 ? 35.544 27.190  54.458  1.00 76.97  ? 101 SER F C   1 
ATOM   6491 O  O   . SER F  2  101 ? 35.521 26.965  53.245  1.00 76.09  ? 101 SER F O   1 
ATOM   6492 C  CB  . SER F  2  101 ? 37.275 26.382  56.084  1.00 75.45  ? 101 SER F CB  1 
ATOM   6493 O  OG  . SER F  2  101 ? 38.238 26.773  55.121  1.00 74.50  ? 101 SER F OG  1 
ATOM   6494 N  N   . ALA F  2  102 ? 35.261 28.381  54.983  1.00 78.12  ? 102 ALA F N   1 
ATOM   6495 C  CA  . ALA F  2  102 ? 34.917 29.538  54.157  1.00 79.40  ? 102 ALA F CA  1 
ATOM   6496 C  C   . ALA F  2  102 ? 36.190 30.033  53.478  1.00 80.72  ? 102 ALA F C   1 
ATOM   6497 O  O   . ALA F  2  102 ? 36.147 30.608  52.390  1.00 80.78  ? 102 ALA F O   1 
ATOM   6498 C  CB  . ALA F  2  102 ? 34.318 30.642  55.014  1.00 76.31  ? 102 ALA F CB  1 
ATOM   6499 N  N   . GLU F  2  103 ? 37.324 29.803  54.125  1.00 82.20  ? 103 GLU F N   1 
ATOM   6500 C  CA  . GLU F  2  103 ? 38.595 30.218  53.568  1.00 83.08  ? 103 GLU F CA  1 
ATOM   6501 C  C   . GLU F  2  103 ? 38.924 29.314  52.389  1.00 81.69  ? 103 GLU F C   1 
ATOM   6502 O  O   . GLU F  2  103 ? 39.396 29.780  51.355  1.00 82.17  ? 103 GLU F O   1 
ATOM   6503 C  CB  . GLU F  2  103 ? 39.691 30.138  54.633  1.00 85.63  ? 103 GLU F CB  1 
ATOM   6504 C  CG  . GLU F  2  103 ? 41.052 30.651  54.183  1.00 89.77  ? 103 GLU F CG  1 
ATOM   6505 C  CD  . GLU F  2  103 ? 40.967 31.925  53.352  1.00 91.92  ? 103 GLU F CD  1 
ATOM   6506 O  OE1 . GLU F  2  103 ? 39.957 32.657  53.450  1.00 91.87  ? 103 GLU F OE1 1 
ATOM   6507 O  OE2 . GLU F  2  103 ? 41.925 32.197  52.606  1.00 93.63  ? 103 GLU F OE2 1 
ATOM   6508 N  N   . GLN F  2  104 ? 38.656 28.021  52.537  1.00 79.15  ? 104 GLN F N   1 
ATOM   6509 C  CA  . GLN F  2  104 ? 38.933 27.081  51.468  1.00 77.49  ? 104 GLN F CA  1 
ATOM   6510 C  C   . GLN F  2  104 ? 38.108 27.426  50.227  1.00 77.13  ? 104 GLN F C   1 
ATOM   6511 O  O   . GLN F  2  104 ? 38.559 27.230  49.094  1.00 77.48  ? 104 GLN F O   1 
ATOM   6512 C  CB  . GLN F  2  104 ? 38.657 25.648  51.941  1.00 76.65  ? 104 GLN F CB  1 
ATOM   6513 C  CG  . GLN F  2  104 ? 39.618 25.191  53.038  1.00 75.97  ? 104 GLN F CG  1 
ATOM   6514 C  CD  . GLN F  2  104 ? 39.401 23.752  53.478  1.00 76.30  ? 104 GLN F CD  1 
ATOM   6515 O  OE1 . GLN F  2  104 ? 38.288 23.356  53.839  1.00 77.12  ? 104 GLN F OE1 1 
ATOM   6516 N  NE2 . GLN F  2  104 ? 40.470 22.963  53.464  1.00 75.62  ? 104 GLN F NE2 1 
ATOM   6517 N  N   . TYR F  2  105 ? 36.907 27.955  50.429  1.00 75.17  ? 105 TYR F N   1 
ATOM   6518 C  CA  . TYR F  2  105 ? 36.081 28.336  49.295  1.00 72.82  ? 105 TYR F CA  1 
ATOM   6519 C  C   . TYR F  2  105 ? 36.702 29.555  48.617  1.00 71.12  ? 105 TYR F C   1 
ATOM   6520 O  O   . TYR F  2  105 ? 36.707 29.657  47.397  1.00 71.55  ? 105 TYR F O   1 
ATOM   6521 C  CB  . TYR F  2  105 ? 34.651 28.658  49.740  1.00 73.92  ? 105 TYR F CB  1 
ATOM   6522 C  CG  . TYR F  2  105 ? 33.771 27.441  49.879  1.00 74.53  ? 105 TYR F CG  1 
ATOM   6523 C  CD1 . TYR F  2  105 ? 33.407 26.690  48.764  1.00 74.54  ? 105 TYR F CD1 1 
ATOM   6524 C  CD2 . TYR F  2  105 ? 33.322 27.020  51.132  1.00 75.66  ? 105 TYR F CD2 1 
ATOM   6525 C  CE1 . TYR F  2  105 ? 32.616 25.544  48.893  1.00 75.28  ? 105 TYR F CE1 1 
ATOM   6526 C  CE2 . TYR F  2  105 ? 32.534 25.875  51.272  1.00 75.09  ? 105 TYR F CE2 1 
ATOM   6527 C  CZ  . TYR F  2  105 ? 32.188 25.144  50.150  1.00 75.33  ? 105 TYR F CZ  1 
ATOM   6528 O  OH  . TYR F  2  105 ? 31.439 24.002  50.283  1.00 75.83  ? 105 TYR F OH  1 
ATOM   6529 N  N   . ASN F  2  106 ? 37.236 30.477  49.396  1.00 68.53  ? 106 ASN F N   1 
ATOM   6530 C  CA  . ASN F  2  106 ? 37.835 31.655  48.802  1.00 66.96  ? 106 ASN F CA  1 
ATOM   6531 C  C   . ASN F  2  106 ? 39.119 31.290  48.092  1.00 65.90  ? 106 ASN F C   1 
ATOM   6532 O  O   . ASN F  2  106 ? 39.519 31.973  47.156  1.00 67.34  ? 106 ASN F O   1 
ATOM   6533 C  CB  . ASN F  2  106 ? 38.113 32.715  49.861  1.00 66.98  ? 106 ASN F CB  1 
ATOM   6534 C  CG  . ASN F  2  106 ? 36.894 33.015  50.705  1.00 67.92  ? 106 ASN F CG  1 
ATOM   6535 O  OD1 . ASN F  2  106 ? 35.777 33.153  50.186  1.00 66.83  ? 106 ASN F OD1 1 
ATOM   6536 N  ND2 . ASN F  2  106 ? 37.095 33.119  52.010  1.00 67.94  ? 106 ASN F ND2 1 
ATOM   6537 N  N   . VAL F  2  107 ? 39.764 30.214  48.527  1.00 63.48  ? 107 VAL F N   1 
ATOM   6538 C  CA  . VAL F  2  107 ? 41.000 29.786  47.897  1.00 61.43  ? 107 VAL F CA  1 
ATOM   6539 C  C   . VAL F  2  107 ? 40.671 29.313  46.480  1.00 60.88  ? 107 VAL F C   1 
ATOM   6540 O  O   . VAL F  2  107 ? 41.323 29.722  45.508  1.00 61.06  ? 107 VAL F O   1 
ATOM   6541 C  CB  . VAL F  2  107 ? 41.678 28.657  48.707  1.00 60.44  ? 107 VAL F CB  1 
ATOM   6542 C  CG1 . VAL F  2  107 ? 42.749 27.982  47.883  1.00 61.39  ? 107 VAL F CG1 1 
ATOM   6543 C  CG2 . VAL F  2  107 ? 42.312 29.234  49.953  1.00 58.90  ? 107 VAL F CG2 1 
ATOM   6544 N  N   . VAL F  2  108 ? 39.647 28.474  46.369  1.00 58.55  ? 108 VAL F N   1 
ATOM   6545 C  CA  . VAL F  2  108 ? 39.211 27.956  45.081  1.00 56.18  ? 108 VAL F CA  1 
ATOM   6546 C  C   . VAL F  2  108 ? 38.652 29.098  44.232  1.00 56.02  ? 108 VAL F C   1 
ATOM   6547 O  O   . VAL F  2  108 ? 38.762 29.077  43.007  1.00 55.17  ? 108 VAL F O   1 
ATOM   6548 C  CB  . VAL F  2  108 ? 38.151 26.850  45.280  1.00 54.53  ? 108 VAL F CB  1 
ATOM   6549 C  CG1 . VAL F  2  108 ? 37.406 26.552  43.981  1.00 52.77  ? 108 VAL F CG1 1 
ATOM   6550 C  CG2 . VAL F  2  108 ? 38.843 25.600  45.772  1.00 52.78  ? 108 VAL F CG2 1 
ATOM   6551 N  N   . GLU F  2  109 ? 38.064 30.092  44.882  1.00 54.99  ? 109 GLU F N   1 
ATOM   6552 C  CA  . GLU F  2  109 ? 37.528 31.232  44.161  1.00 56.69  ? 109 GLU F CA  1 
ATOM   6553 C  C   . GLU F  2  109 ? 38.710 31.898  43.470  1.00 57.53  ? 109 GLU F C   1 
ATOM   6554 O  O   . GLU F  2  109 ? 38.710 32.111  42.256  1.00 58.22  ? 109 GLU F O   1 
ATOM   6555 C  CB  . GLU F  2  109 ? 36.899 32.249  45.119  1.00 57.37  ? 109 GLU F CB  1 
ATOM   6556 C  CG  . GLU F  2  109 ? 35.543 31.871  45.733  1.00 58.43  ? 109 GLU F CG  1 
ATOM   6557 C  CD  . GLU F  2  109 ? 35.047 32.948  46.702  1.00 59.11  ? 109 GLU F CD  1 
ATOM   6558 O  OE1 . GLU F  2  109 ? 35.655 34.038  46.728  1.00 59.56  ? 109 GLU F OE1 1 
ATOM   6559 O  OE2 . GLU F  2  109 ? 34.062 32.738  47.441  1.00 60.37  ? 109 GLU F OE2 1 
ATOM   6560 N  N   . HIS F  2  110 ? 39.724 32.218  44.257  1.00 56.64  ? 110 HIS F N   1 
ATOM   6561 C  CA  . HIS F  2  110 ? 40.888 32.871  43.713  1.00 56.16  ? 110 HIS F CA  1 
ATOM   6562 C  C   . HIS F  2  110 ? 41.588 32.010  42.670  1.00 55.45  ? 110 HIS F C   1 
ATOM   6563 O  O   . HIS F  2  110 ? 42.115 32.534  41.688  1.00 55.89  ? 110 HIS F O   1 
ATOM   6564 C  CB  . HIS F  2  110 ? 41.843 33.246  44.839  1.00 56.36  ? 110 HIS F CB  1 
ATOM   6565 C  CG  . HIS F  2  110 ? 43.127 33.856  44.364  1.00 57.00  ? 110 HIS F CG  1 
ATOM   6566 N  ND1 . HIS F  2  110 ? 44.261 33.106  44.133  1.00 57.32  ? 110 HIS F ND1 1 
ATOM   6567 C  CD2 . HIS F  2  110 ? 43.468 35.143  44.122  1.00 55.28  ? 110 HIS F CD2 1 
ATOM   6568 C  CE1 . HIS F  2  110 ? 45.249 33.908  43.777  1.00 57.50  ? 110 HIS F CE1 1 
ATOM   6569 N  NE2 . HIS F  2  110 ? 44.794 35.148  43.765  1.00 56.88  ? 110 HIS F NE2 1 
ATOM   6570 N  N   . ALA F  2  111 ? 41.589 30.696  42.864  1.00 53.45  ? 111 ALA F N   1 
ATOM   6571 C  CA  . ALA F  2  111 ? 42.247 29.819  41.901  1.00 51.66  ? 111 ALA F CA  1 
ATOM   6572 C  C   . ALA F  2  111 ? 41.528 29.916  40.560  1.00 50.85  ? 111 ALA F C   1 
ATOM   6573 O  O   . ALA F  2  111 ? 42.148 30.081  39.502  1.00 49.06  ? 111 ALA F O   1 
ATOM   6574 C  CB  . ALA F  2  111 ? 42.232 28.399  42.393  1.00 51.05  ? 111 ALA F CB  1 
ATOM   6575 N  N   . VAL F  2  112 ? 40.207 29.833  40.622  1.00 50.17  ? 112 VAL F N   1 
ATOM   6576 C  CA  . VAL F  2  112 ? 39.386 29.909  39.434  1.00 49.69  ? 112 VAL F CA  1 
ATOM   6577 C  C   . VAL F  2  112 ? 39.602 31.209  38.688  1.00 49.73  ? 112 VAL F C   1 
ATOM   6578 O  O   . VAL F  2  112 ? 39.608 31.233  37.454  1.00 48.92  ? 112 VAL F O   1 
ATOM   6579 C  CB  . VAL F  2  112 ? 37.899 29.808  39.792  1.00 50.16  ? 112 VAL F CB  1 
ATOM   6580 C  CG1 . VAL F  2  112 ? 37.043 30.211  38.596  1.00 47.88  ? 112 VAL F CG1 1 
ATOM   6581 C  CG2 . VAL F  2  112 ? 37.580 28.392  40.237  1.00 49.44  ? 112 VAL F CG2 1 
ATOM   6582 N  N   . MET F  2  113 ? 39.763 32.295  39.436  1.00 50.37  ? 113 MET F N   1 
ATOM   6583 C  CA  . MET F  2  113 ? 39.981 33.602  38.821  1.00 52.07  ? 113 MET F CA  1 
ATOM   6584 C  C   . MET F  2  113 ? 41.345 33.668  38.132  1.00 51.86  ? 113 MET F C   1 
ATOM   6585 O  O   . MET F  2  113 ? 41.473 34.193  37.031  1.00 51.60  ? 113 MET F O   1 
ATOM   6586 C  CB  . MET F  2  113 ? 39.830 34.716  39.860  1.00 51.56  ? 113 MET F CB  1 
ATOM   6587 C  CG  . MET F  2  113 ? 38.399 34.870  40.376  1.00 53.08  ? 113 MET F CG  1 
ATOM   6588 S  SD  . MET F  2  113 ? 38.127 36.419  41.315  1.00 57.83  ? 113 MET F SD  1 
ATOM   6589 C  CE  . MET F  2  113 ? 38.518 35.871  42.961  1.00 57.26  ? 113 MET F CE  1 
ATOM   6590 N  N   . MET F  2  114 ? 42.369 33.125  38.773  1.00 53.04  ? 114 MET F N   1 
ATOM   6591 C  CA  . MET F  2  114 ? 43.691 33.131  38.167  1.00 53.24  ? 114 MET F CA  1 
ATOM   6592 C  C   . MET F  2  114 ? 43.664 32.323  36.865  1.00 52.35  ? 114 MET F C   1 
ATOM   6593 O  O   . MET F  2  114 ? 44.293 32.696  35.885  1.00 52.81  ? 114 MET F O   1 
ATOM   6594 C  CB  . MET F  2  114 ? 44.717 32.546  39.135  1.00 55.96  ? 114 MET F CB  1 
ATOM   6595 C  CG  . MET F  2  114 ? 45.022 33.461  40.312  1.00 60.14  ? 114 MET F CG  1 
ATOM   6596 S  SD  . MET F  2  114 ? 45.664 35.124  39.831  1.00 67.26  ? 114 MET F SD  1 
ATOM   6597 C  CE  . MET F  2  114 ? 44.155 36.093  39.832  1.00 64.29  ? 114 MET F CE  1 
ATOM   6598 N  N   . GLY F  2  115 ? 42.921 31.224  36.859  1.00 50.83  ? 115 GLY F N   1 
ATOM   6599 C  CA  . GLY F  2  115 ? 42.841 30.396  35.670  1.00 48.08  ? 115 GLY F CA  1 
ATOM   6600 C  C   . GLY F  2  115 ? 42.155 31.099  34.520  1.00 45.96  ? 115 GLY F C   1 
ATOM   6601 O  O   . GLY F  2  115 ? 42.635 31.099  33.396  1.00 46.05  ? 115 GLY F O   1 
ATOM   6602 N  N   . VAL F  2  116 ? 41.016 31.703  34.814  1.00 45.48  ? 116 VAL F N   1 
ATOM   6603 C  CA  . VAL F  2  116 ? 40.237 32.430  33.827  1.00 43.24  ? 116 VAL F CA  1 
ATOM   6604 C  C   . VAL F  2  116 ? 41.074 33.558  33.227  1.00 43.90  ? 116 VAL F C   1 
ATOM   6605 O  O   . VAL F  2  116 ? 41.032 33.811  32.020  1.00 40.04  ? 116 VAL F O   1 
ATOM   6606 C  CB  . VAL F  2  116 ? 38.969 33.040  34.491  1.00 42.82  ? 116 VAL F CB  1 
ATOM   6607 C  CG1 . VAL F  2  116 ? 38.277 34.035  33.530  1.00 39.46  ? 116 VAL F CG1 1 
ATOM   6608 C  CG2 . VAL F  2  116 ? 38.008 31.912  34.894  1.00 41.70  ? 116 VAL F CG2 1 
ATOM   6609 N  N   . GLU F  2  117 ? 41.823 34.240  34.093  1.00 45.37  ? 117 GLU F N   1 
ATOM   6610 C  CA  . GLU F  2  117 ? 42.673 35.348  33.699  1.00 47.80  ? 117 GLU F CA  1 
ATOM   6611 C  C   . GLU F  2  117 ? 43.842 34.831  32.869  1.00 49.09  ? 117 GLU F C   1 
ATOM   6612 O  O   . GLU F  2  117 ? 44.256 35.452  31.897  1.00 48.32  ? 117 GLU F O   1 
ATOM   6613 C  CB  . GLU F  2  117 ? 43.185 36.069  34.950  1.00 49.26  ? 117 GLU F CB  1 
ATOM   6614 C  CG  . GLU F  2  117 ? 43.951 37.353  34.649  1.00 50.90  ? 117 GLU F CG  1 
ATOM   6615 C  CD  . GLU F  2  117 ? 45.428 37.249  34.976  1.00 50.67  ? 117 GLU F CD  1 
ATOM   6616 O  OE1 . GLU F  2  117 ? 45.837 37.576  36.110  1.00 52.26  ? 117 GLU F OE1 1 
ATOM   6617 O  OE2 . GLU F  2  117 ? 46.196 36.824  34.090  1.00 54.43  ? 117 GLU F OE2 1 
ATOM   6618 N  N   . HIS F  2  118 ? 44.365 33.679  33.262  1.00 51.30  ? 118 HIS F N   1 
ATOM   6619 C  CA  . HIS F  2  118 ? 45.476 33.048  32.565  1.00 52.47  ? 118 HIS F CA  1 
ATOM   6620 C  C   . HIS F  2  118 ? 44.994 32.632  31.186  1.00 53.04  ? 118 HIS F C   1 
ATOM   6621 O  O   . HIS F  2  118 ? 45.750 32.638  30.211  1.00 53.62  ? 118 HIS F O   1 
ATOM   6622 C  CB  . HIS F  2  118 ? 45.924 31.826  33.368  1.00 54.78  ? 118 HIS F CB  1 
ATOM   6623 C  CG  . HIS F  2  118 ? 46.650 30.790  32.568  1.00 57.10  ? 118 HIS F CG  1 
ATOM   6624 N  ND1 . HIS F  2  118 ? 47.934 30.968  32.097  1.00 56.38  ? 118 HIS F ND1 1 
ATOM   6625 C  CD2 . HIS F  2  118 ? 46.269 29.550  32.170  1.00 57.71  ? 118 HIS F CD2 1 
ATOM   6626 C  CE1 . HIS F  2  118 ? 48.313 29.884  31.446  1.00 57.44  ? 118 HIS F CE1 1 
ATOM   6627 N  NE2 . HIS F  2  118 ? 47.324 29.009  31.475  1.00 58.99  ? 118 HIS F NE2 1 
ATOM   6628 N  N   . GLU F  2  119 ? 43.717 32.291  31.108  1.00 52.78  ? 119 GLU F N   1 
ATOM   6629 C  CA  . GLU F  2  119 ? 43.130 31.854  29.855  1.00 52.70  ? 119 GLU F CA  1 
ATOM   6630 C  C   . GLU F  2  119 ? 42.746 32.999  28.906  1.00 50.67  ? 119 GLU F C   1 
ATOM   6631 O  O   . GLU F  2  119 ? 42.981 32.888  27.700  1.00 50.82  ? 119 GLU F O   1 
ATOM   6632 C  CB  . GLU F  2  119 ? 41.907 30.985  30.160  1.00 55.80  ? 119 GLU F CB  1 
ATOM   6633 C  CG  . GLU F  2  119 ? 41.727 29.746  29.318  1.00 62.44  ? 119 GLU F CG  1 
ATOM   6634 C  CD  . GLU F  2  119 ? 42.925 28.856  29.360  1.00 65.33  ? 119 GLU F CD  1 
ATOM   6635 O  OE1 . GLU F  2  119 ? 43.382 28.426  30.403  1.00 68.29  ? 119 GLU F OE1 1 
ATOM   6636 O  OE2 . GLU F  2  119 ? 43.406 28.583  28.228  1.00 70.82  ? 119 GLU F OE2 1 
ATOM   6637 N  N   . ILE F  2  120 ? 42.167 34.082  29.423  1.00 46.68  ? 120 ILE F N   1 
ATOM   6638 C  CA  . ILE F  2  120 ? 41.758 35.179  28.554  1.00 42.31  ? 120 ILE F CA  1 
ATOM   6639 C  C   . ILE F  2  120 ? 42.599 36.435  28.619  1.00 41.86  ? 120 ILE F C   1 
ATOM   6640 O  O   . ILE F  2  120 ? 42.309 37.401  27.910  1.00 42.16  ? 120 ILE F O   1 
ATOM   6641 C  CB  . ILE F  2  120 ? 40.300 35.604  28.790  1.00 41.64  ? 120 ILE F CB  1 
ATOM   6642 C  CG1 . ILE F  2  120 ? 40.148 36.233  30.173  1.00 43.46  ? 120 ILE F CG1 1 
ATOM   6643 C  CG2 . ILE F  2  120 ? 39.387 34.424  28.634  1.00 42.13  ? 120 ILE F CG2 1 
ATOM   6644 C  CD1 . ILE F  2  120 ? 38.765 36.789  30.409  1.00 43.12  ? 120 ILE F CD1 1 
ATOM   6645 N  N   . GLY F  2  121 ? 43.619 36.445  29.467  1.00 40.75  ? 121 GLY F N   1 
ATOM   6646 C  CA  . GLY F  2  121 ? 44.492 37.610  29.547  1.00 40.47  ? 121 GLY F CA  1 
ATOM   6647 C  C   . GLY F  2  121 ? 44.157 38.673  30.579  1.00 41.59  ? 121 GLY F C   1 
ATOM   6648 O  O   . GLY F  2  121 ? 43.008 39.074  30.728  1.00 42.77  ? 121 GLY F O   1 
ATOM   6649 N  N   . GLN F  2  122 ? 45.189 39.160  31.262  1.00 41.43  ? 122 GLN F N   1 
ATOM   6650 C  CA  . GLN F  2  122 ? 45.023 40.165  32.300  1.00 41.71  ? 122 GLN F CA  1 
ATOM   6651 C  C   . GLN F  2  122 ? 44.478 41.475  31.787  1.00 41.62  ? 122 GLN F C   1 
ATOM   6652 O  O   . GLN F  2  122 ? 43.920 42.271  32.535  1.00 41.19  ? 122 GLN F O   1 
ATOM   6653 C  CB  . GLN F  2  122 ? 46.358 40.422  33.012  1.00 41.64  ? 122 GLN F CB  1 
ATOM   6654 C  CG  . GLN F  2  122 ? 47.437 41.116  32.189  1.00 41.86  ? 122 GLN F CG  1 
ATOM   6655 C  CD  . GLN F  2  122 ? 47.137 42.583  31.930  1.00 46.63  ? 122 GLN F CD  1 
ATOM   6656 O  OE1 . GLN F  2  122 ? 46.607 43.286  32.797  1.00 46.55  ? 122 GLN F OE1 1 
ATOM   6657 N  NE2 . GLN F  2  122 ? 47.483 43.060  30.742  1.00 45.99  ? 122 GLN F NE2 1 
ATOM   6658 N  N   . ASN F  2  123 ? 44.631 41.724  30.505  1.00 41.65  ? 123 ASN F N   1 
ATOM   6659 C  CA  . ASN F  2  123 ? 44.158 43.010  30.061  1.00 41.87  ? 123 ASN F CA  1 
ATOM   6660 C  C   . ASN F  2  123 ? 42.646 43.073  29.884  1.00 39.61  ? 123 ASN F C   1 
ATOM   6661 O  O   . ASN F  2  123 ? 42.099 44.153  29.689  1.00 42.99  ? 123 ASN F O   1 
ATOM   6662 C  CB  . ASN F  2  123 ? 44.941 43.456  28.807  1.00 45.01  ? 123 ASN F CB  1 
ATOM   6663 C  CG  . ASN F  2  123 ? 44.067 43.675  27.609  1.00 50.09  ? 123 ASN F CG  1 
ATOM   6664 O  OD1 . ASN F  2  123 ? 43.618 42.713  26.984  1.00 53.35  ? 123 ASN F OD1 1 
ATOM   6665 N  ND2 . ASN F  2  123 ? 43.806 44.940  27.275  1.00 49.81  ? 123 ASN F ND2 1 
ATOM   6666 N  N   . VAL F  2  124 ? 41.949 41.947  29.978  1.00 36.27  ? 124 VAL F N   1 
ATOM   6667 C  CA  . VAL F  2  124 ? 40.494 41.982  29.855  1.00 36.42  ? 124 VAL F CA  1 
ATOM   6668 C  C   . VAL F  2  124 ? 39.777 41.417  31.090  1.00 38.51  ? 124 VAL F C   1 
ATOM   6669 O  O   . VAL F  2  124 ? 38.583 41.679  31.294  1.00 35.42  ? 124 VAL F O   1 
ATOM   6670 C  CB  . VAL F  2  124 ? 39.970 41.200  28.611  1.00 35.55  ? 124 VAL F CB  1 
ATOM   6671 C  CG1 . VAL F  2  124 ? 40.507 41.820  27.347  1.00 33.34  ? 124 VAL F CG1 1 
ATOM   6672 C  CG2 . VAL F  2  124 ? 40.343 39.721  28.718  1.00 31.65  ? 124 VAL F CG2 1 
ATOM   6673 N  N   . PHE F  2  125 ? 40.501 40.647  31.909  1.00 41.24  ? 125 PHE F N   1 
ATOM   6674 C  CA  . PHE F  2  125 ? 39.938 40.027  33.120  1.00 43.41  ? 125 PHE F CA  1 
ATOM   6675 C  C   . PHE F  2  125 ? 39.248 41.023  34.058  1.00 42.38  ? 125 PHE F C   1 
ATOM   6676 O  O   . PHE F  2  125 ? 39.862 41.941  34.604  1.00 39.10  ? 125 PHE F O   1 
ATOM   6677 C  CB  . PHE F  2  125 ? 41.021 39.276  33.908  1.00 46.73  ? 125 PHE F CB  1 
ATOM   6678 C  CG  . PHE F  2  125 ? 40.490 38.591  35.138  1.00 50.56  ? 125 PHE F CG  1 
ATOM   6679 C  CD1 . PHE F  2  125 ? 39.525 37.584  35.017  1.00 50.94  ? 125 PHE F CD1 1 
ATOM   6680 C  CD2 . PHE F  2  125 ? 40.895 38.981  36.413  1.00 49.81  ? 125 PHE F CD2 1 
ATOM   6681 C  CE1 . PHE F  2  125 ? 38.972 36.980  36.146  1.00 49.89  ? 125 PHE F CE1 1 
ATOM   6682 C  CE2 . PHE F  2  125 ? 40.343 38.381  37.542  1.00 51.45  ? 125 PHE F CE2 1 
ATOM   6683 C  CZ  . PHE F  2  125 ? 39.375 37.373  37.403  1.00 51.04  ? 125 PHE F CZ  1 
ATOM   6684 N  N   . ASP F  2  126 ? 37.959 40.814  34.243  1.00 43.37  ? 126 ASP F N   1 
ATOM   6685 C  CA  . ASP F  2  126 ? 37.149 41.703  35.071  1.00 46.55  ? 126 ASP F CA  1 
ATOM   6686 C  C   . ASP F  2  126 ? 37.056 41.141  36.505  1.00 46.97  ? 126 ASP F C   1 
ATOM   6687 O  O   . ASP F  2  126 ? 36.170 40.348  36.825  1.00 46.50  ? 126 ASP F O   1 
ATOM   6688 C  CB  . ASP F  2  126 ? 35.761 41.851  34.421  1.00 45.83  ? 126 ASP F CB  1 
ATOM   6689 C  CG  . ASP F  2  126 ? 34.922 42.915  35.081  1.00 45.99  ? 126 ASP F CG  1 
ATOM   6690 O  OD1 . ASP F  2  126 ? 33.939 43.374  34.465  1.00 46.87  ? 126 ASP F OD1 1 
ATOM   6691 O  OD2 . ASP F  2  126 ? 35.249 43.284  36.225  1.00 48.95  ? 126 ASP F OD2 1 
ATOM   6692 N  N   . LYS F  2  127 ? 37.973 41.569  37.369  1.00 48.03  ? 127 LYS F N   1 
ATOM   6693 C  CA  . LYS F  2  127 ? 38.000 41.045  38.721  1.00 50.36  ? 127 LYS F CA  1 
ATOM   6694 C  C   . LYS F  2  127 ? 36.785 41.344  39.588  1.00 51.98  ? 127 LYS F C   1 
ATOM   6695 O  O   . LYS F  2  127 ? 36.265 40.446  40.256  1.00 51.44  ? 127 LYS F O   1 
ATOM   6696 C  CB  . LYS F  2  127 ? 39.252 41.496  39.458  1.00 49.01  ? 127 LYS F CB  1 
ATOM   6697 C  CG  . LYS F  2  127 ? 39.468 40.675  40.707  1.00 50.81  ? 127 LYS F CG  1 
ATOM   6698 C  CD  . LYS F  2  127 ? 40.627 41.166  41.534  1.00 51.37  ? 127 LYS F CD  1 
ATOM   6699 C  CE  . LYS F  2  127 ? 40.592 40.522  42.907  1.00 52.19  ? 127 LYS F CE  1 
ATOM   6700 N  NZ  . LYS F  2  127 ? 41.521 41.183  43.872  1.00 50.55  ? 127 LYS F NZ  1 
ATOM   6701 N  N   . ASP F  2  128 ? 36.329 42.591  39.598  1.00 52.25  ? 128 ASP F N   1 
ATOM   6702 C  CA  . ASP F  2  128 ? 35.175 42.911  40.415  1.00 53.65  ? 128 ASP F CA  1 
ATOM   6703 C  C   . ASP F  2  128 ? 33.993 42.036  40.017  1.00 53.94  ? 128 ASP F C   1 
ATOM   6704 O  O   . ASP F  2  128 ? 33.315 41.477  40.877  1.00 53.92  ? 128 ASP F O   1 
ATOM   6705 C  CB  . ASP F  2  128 ? 34.811 44.401  40.297  1.00 55.64  ? 128 ASP F CB  1 
ATOM   6706 C  CG  . ASP F  2  128 ? 35.706 45.295  41.169  1.00 57.66  ? 128 ASP F CG  1 
ATOM   6707 O  OD1 . ASP F  2  128 ? 36.176 44.789  42.216  1.00 57.56  ? 128 ASP F OD1 1 
ATOM   6708 O  OD2 . ASP F  2  128 ? 35.922 46.487  40.829  1.00 56.77  ? 128 ASP F OD2 1 
ATOM   6709 N  N   . ALA F  2  129 ? 33.744 41.887  38.720  1.00 53.74  ? 129 ALA F N   1 
ATOM   6710 C  CA  . ALA F  2  129 ? 32.616 41.063  38.308  1.00 54.21  ? 129 ALA F CA  1 
ATOM   6711 C  C   . ALA F  2  129 ? 32.799 39.621  38.728  1.00 54.18  ? 129 ALA F C   1 
ATOM   6712 O  O   . ALA F  2  129 ? 31.837 38.975  39.133  1.00 55.79  ? 129 ALA F O   1 
ATOM   6713 C  CB  . ALA F  2  129 ? 32.408 41.135  36.813  1.00 54.93  ? 129 ALA F CB  1 
ATOM   6714 N  N   . TRP F  2  130 ? 34.023 39.114  38.635  1.00 54.13  ? 130 TRP F N   1 
ATOM   6715 C  CA  . TRP F  2  130 ? 34.290 37.729  39.000  1.00 54.81  ? 130 TRP F CA  1 
ATOM   6716 C  C   . TRP F  2  130 ? 34.245 37.428  40.499  1.00 54.66  ? 130 TRP F C   1 
ATOM   6717 O  O   . TRP F  2  130 ? 33.713 36.394  40.924  1.00 51.66  ? 130 TRP F O   1 
ATOM   6718 C  CB  . TRP F  2  130 ? 35.629 37.268  38.412  1.00 55.07  ? 130 TRP F CB  1 
ATOM   6719 C  CG  . TRP F  2  130 ? 35.497 36.729  36.998  1.00 55.15  ? 130 TRP F CG  1 
ATOM   6720 C  CD1 . TRP F  2  130 ? 35.696 37.411  35.834  1.00 54.18  ? 130 TRP F CD1 1 
ATOM   6721 C  CD2 . TRP F  2  130 ? 35.114 35.403  36.621  1.00 53.51  ? 130 TRP F CD2 1 
ATOM   6722 N  NE1 . TRP F  2  130 ? 35.464 36.590  34.760  1.00 52.78  ? 130 TRP F NE1 1 
ATOM   6723 C  CE2 . TRP F  2  130 ? 35.103 35.353  35.216  1.00 52.59  ? 130 TRP F CE2 1 
ATOM   6724 C  CE3 . TRP F  2  130 ? 34.776 34.254  37.341  1.00 53.90  ? 130 TRP F CE3 1 
ATOM   6725 C  CZ2 . TRP F  2  130 ? 34.769 34.199  34.509  1.00 54.55  ? 130 TRP F CZ2 1 
ATOM   6726 C  CZ3 . TRP F  2  130 ? 34.444 33.105  36.641  1.00 54.76  ? 130 TRP F CZ3 1 
ATOM   6727 C  CH2 . TRP F  2  130 ? 34.444 33.085  35.237  1.00 55.80  ? 130 TRP F CH2 1 
ATOM   6728 N  N   . GLN F  2  131 ? 34.806 38.335  41.295  1.00 55.80  ? 131 GLN F N   1 
ATOM   6729 C  CA  . GLN F  2  131 ? 34.806 38.177  42.739  1.00 56.08  ? 131 GLN F CA  1 
ATOM   6730 C  C   . GLN F  2  131 ? 33.352 38.217  43.209  1.00 57.50  ? 131 GLN F C   1 
ATOM   6731 O  O   . GLN F  2  131 ? 32.883 37.292  43.880  1.00 57.12  ? 131 GLN F O   1 
ATOM   6732 C  CB  . GLN F  2  131 ? 35.601 39.304  43.376  1.00 55.24  ? 131 GLN F CB  1 
ATOM   6733 C  CG  . GLN F  2  131 ? 35.863 39.128  44.854  1.00 57.54  ? 131 GLN F CG  1 
ATOM   6734 C  CD  . GLN F  2  131 ? 36.440 37.759  45.203  1.00 59.23  ? 131 GLN F CD  1 
ATOM   6735 O  OE1 . GLN F  2  131 ? 35.704 36.769  45.323  1.00 60.51  ? 131 GLN F OE1 1 
ATOM   6736 N  NE2 . GLN F  2  131 ? 37.764 37.696  45.363  1.00 57.35  ? 131 GLN F NE2 1 
ATOM   6737 N  N   . ALA F  2  132 ? 32.642 39.278  42.820  1.00 56.32  ? 132 ALA F N   1 
ATOM   6738 C  CA  . ALA F  2  132 ? 31.249 39.455  43.186  1.00 56.10  ? 132 ALA F CA  1 
ATOM   6739 C  C   . ALA F  2  132 ? 30.429 38.209  42.907  1.00 56.55  ? 132 ALA F C   1 
ATOM   6740 O  O   . ALA F  2  132 ? 29.860 37.625  43.822  1.00 59.29  ? 132 ALA F O   1 
ATOM   6741 C  CB  . ALA F  2  132 ? 30.647 40.645  42.435  1.00 54.92  ? 132 ALA F CB  1 
ATOM   6742 N  N   . CYS F  2  133 ? 30.373 37.788  41.654  1.00 55.92  ? 133 CYS F N   1 
ATOM   6743 C  CA  . CYS F  2  133 ? 29.562 36.635  41.311  1.00 55.70  ? 133 CYS F CA  1 
ATOM   6744 C  C   . CYS F  2  133 ? 30.025 35.290  41.850  1.00 56.07  ? 133 CYS F C   1 
ATOM   6745 O  O   . CYS F  2  133 ? 29.207 34.381  42.010  1.00 55.80  ? 133 CYS F O   1 
ATOM   6746 C  CB  . CYS F  2  133 ? 29.379 36.565  39.801  1.00 56.10  ? 133 CYS F CB  1 
ATOM   6747 S  SG  . CYS F  2  133 ? 28.560 38.031  39.132  1.00 56.61  ? 133 CYS F SG  1 
ATOM   6748 N  N   . LEU F  2  134 ? 31.321 35.143  42.111  1.00 56.65  ? 134 LEU F N   1 
ATOM   6749 C  CA  . LEU F  2  134 ? 31.808 33.887  42.669  1.00 57.62  ? 134 LEU F CA  1 
ATOM   6750 C  C   . LEU F  2  134 ? 31.308 33.814  44.108  1.00 58.31  ? 134 LEU F C   1 
ATOM   6751 O  O   . LEU F  2  134 ? 30.915 32.743  44.578  1.00 57.93  ? 134 LEU F O   1 
ATOM   6752 C  CB  . LEU F  2  134 ? 33.337 33.816  42.637  1.00 57.52  ? 134 LEU F CB  1 
ATOM   6753 C  CG  . LEU F  2  134 ? 33.964 33.327  41.323  1.00 57.80  ? 134 LEU F CG  1 
ATOM   6754 C  CD1 . LEU F  2  134 ? 35.482 33.358  41.450  1.00 56.83  ? 134 LEU F CD1 1 
ATOM   6755 C  CD2 . LEU F  2  134 ? 33.488 31.913  40.997  1.00 54.49  ? 134 LEU F CD2 1 
ATOM   6756 N  N   . ASP F  2  135 ? 31.308 34.958  44.794  1.00 58.92  ? 135 ASP F N   1 
ATOM   6757 C  CA  . ASP F  2  135 ? 30.829 35.001  46.172  1.00 58.88  ? 135 ASP F CA  1 
ATOM   6758 C  C   . ASP F  2  135 ? 29.400 34.487  46.163  1.00 58.26  ? 135 ASP F C   1 
ATOM   6759 O  O   . ASP F  2  135 ? 29.048 33.596  46.937  1.00 57.60  ? 135 ASP F O   1 
ATOM   6760 C  CB  . ASP F  2  135 ? 30.850 36.422  46.738  1.00 58.48  ? 135 ASP F CB  1 
ATOM   6761 C  CG  . ASP F  2  135 ? 32.238 36.888  47.096  1.00 57.44  ? 135 ASP F CG  1 
ATOM   6762 O  OD1 . ASP F  2  135 ? 33.044 36.059  47.572  1.00 57.42  ? 135 ASP F OD1 1 
ATOM   6763 O  OD2 . ASP F  2  135 ? 32.518 38.091  46.921  1.00 59.69  ? 135 ASP F OD2 1 
ATOM   6764 N  N   . VAL F  2  136 ? 28.578 35.030  45.276  1.00 57.17  ? 136 VAL F N   1 
ATOM   6765 C  CA  . VAL F  2  136 ? 27.204 34.571  45.208  1.00 57.69  ? 136 VAL F CA  1 
ATOM   6766 C  C   . VAL F  2  136 ? 27.133 33.056  45.080  1.00 59.16  ? 136 VAL F C   1 
ATOM   6767 O  O   . VAL F  2  136 ? 26.334 32.409  45.752  1.00 60.45  ? 136 VAL F O   1 
ATOM   6768 C  CB  . VAL F  2  136 ? 26.455 35.229  44.038  1.00 55.37  ? 136 VAL F CB  1 
ATOM   6769 C  CG1 . VAL F  2  136 ? 25.122 34.536  43.798  1.00 50.84  ? 136 VAL F CG1 1 
ATOM   6770 C  CG2 . VAL F  2  136 ? 26.252 36.704  44.353  1.00 54.14  ? 136 VAL F CG2 1 
ATOM   6771 N  N   . ILE F  2  137 ? 27.994 32.486  44.253  1.00 61.10  ? 137 ILE F N   1 
ATOM   6772 C  CA  . ILE F  2  137 ? 27.978 31.040  44.045  1.00 63.20  ? 137 ILE F CA  1 
ATOM   6773 C  C   . ILE F  2  137 ? 28.430 30.195  45.239  1.00 64.78  ? 137 ILE F C   1 
ATOM   6774 O  O   . ILE F  2  137 ? 27.787 29.198  45.572  1.00 64.81  ? 137 ILE F O   1 
ATOM   6775 C  CB  . ILE F  2  137 ? 28.835 30.632  42.821  1.00 62.41  ? 137 ILE F CB  1 
ATOM   6776 C  CG1 . ILE F  2  137 ? 28.258 31.260  41.553  1.00 61.30  ? 137 ILE F CG1 1 
ATOM   6777 C  CG2 . ILE F  2  137 ? 28.887 29.098  42.705  1.00 60.09  ? 137 ILE F CG2 1 
ATOM   6778 C  CD1 . ILE F  2  137 ? 29.013 30.894  40.309  1.00 61.16  ? 137 ILE F CD1 1 
ATOM   6779 N  N   . THR F  2  138 ? 29.537 30.569  45.868  1.00 65.70  ? 138 THR F N   1 
ATOM   6780 C  CA  . THR F  2  138 ? 29.998 29.790  46.999  1.00 68.62  ? 138 THR F CA  1 
ATOM   6781 C  C   . THR F  2  138 ? 29.155 30.063  48.237  1.00 70.76  ? 138 THR F C   1 
ATOM   6782 O  O   . THR F  2  138 ? 29.043 29.202  49.107  1.00 72.31  ? 138 THR F O   1 
ATOM   6783 C  CB  . THR F  2  138 ? 31.484 30.041  47.300  1.00 68.21  ? 138 THR F CB  1 
ATOM   6784 O  OG1 . THR F  2  138 ? 31.719 31.441  47.492  1.00 68.94  ? 138 THR F OG1 1 
ATOM   6785 C  CG2 . THR F  2  138 ? 32.326 29.531  46.159  1.00 67.15  ? 138 THR F CG2 1 
ATOM   6786 N  N   . SER F  2  139 ? 28.560 31.250  48.320  1.00 71.62  ? 139 SER F N   1 
ATOM   6787 C  CA  . SER F  2  139 ? 27.708 31.566  49.454  1.00 71.99  ? 139 SER F CA  1 
ATOM   6788 C  C   . SER F  2  139 ? 26.593 30.523  49.455  1.00 72.98  ? 139 SER F C   1 
ATOM   6789 O  O   . SER F  2  139 ? 26.348 29.864  50.463  1.00 74.17  ? 139 SER F O   1 
ATOM   6790 C  CB  . SER F  2  139 ? 27.109 32.965  49.304  1.00 71.46  ? 139 SER F CB  1 
ATOM   6791 O  OG  . SER F  2  139 ? 26.246 33.271  50.381  1.00 72.04  ? 139 SER F OG  1 
ATOM   6792 N  N   . GLY F  2  140 ? 25.941 30.360  48.310  1.00 73.03  ? 140 GLY F N   1 
ATOM   6793 C  CA  . GLY F  2  140 ? 24.863 29.392  48.197  1.00 74.20  ? 140 GLY F CA  1 
ATOM   6794 C  C   . GLY F  2  140 ? 25.318 27.964  48.414  1.00 75.30  ? 140 GLY F C   1 
ATOM   6795 O  O   . GLY F  2  140 ? 24.575 27.137  48.933  1.00 75.35  ? 140 GLY F O   1 
ATOM   6796 N  N   . ILE F  2  141 ? 26.543 27.664  48.006  1.00 77.66  ? 141 ILE F N   1 
ATOM   6797 C  CA  . ILE F  2  141 ? 27.084 26.319  48.170  1.00 80.22  ? 141 ILE F CA  1 
ATOM   6798 C  C   . ILE F  2  141 ? 27.236 26.005  49.669  1.00 81.47  ? 141 ILE F C   1 
ATOM   6799 O  O   . ILE F  2  141 ? 27.200 24.837  50.080  1.00 81.23  ? 141 ILE F O   1 
ATOM   6800 C  CB  . ILE F  2  141 ? 28.459 26.183  47.430  1.00 79.83  ? 141 ILE F CB  1 
ATOM   6801 C  CG1 . ILE F  2  141 ? 28.250 26.398  45.924  1.00 79.30  ? 141 ILE F CG1 1 
ATOM   6802 C  CG2 . ILE F  2  141 ? 29.079 24.817  47.703  1.00 80.08  ? 141 ILE F CG2 1 
ATOM   6803 C  CD1 . ILE F  2  141 ? 29.436 26.043  45.057  1.00 78.95  ? 141 ILE F CD1 1 
ATOM   6804 N  N   . GLN F  2  142 ? 27.383 27.057  50.472  1.00 82.32  ? 142 GLN F N   1 
ATOM   6805 C  CA  . GLN F  2  142 ? 27.536 26.942  51.925  1.00 83.71  ? 142 GLN F CA  1 
ATOM   6806 C  C   . GLN F  2  142 ? 26.196 27.130  52.638  1.00 85.81  ? 142 GLN F C   1 
ATOM   6807 O  O   . GLN F  2  142 ? 26.136 27.149  53.870  1.00 86.07  ? 142 GLN F O   1 
ATOM   6808 C  CB  . GLN F  2  142 ? 28.520 28.001  52.437  1.00 81.43  ? 142 GLN F CB  1 
ATOM   6809 C  CG  . GLN F  2  142 ? 29.984 27.685  52.183  1.00 79.10  ? 142 GLN F CG  1 
ATOM   6810 C  CD  . GLN F  2  142 ? 30.868 28.904  52.337  1.00 77.92  ? 142 GLN F CD  1 
ATOM   6811 O  OE1 . GLN F  2  142 ? 30.840 29.802  51.503  1.00 77.91  ? 142 GLN F OE1 1 
ATOM   6812 N  NE2 . GLN F  2  142 ? 31.653 28.943  53.410  1.00 76.36  ? 142 GLN F NE2 1 
ATOM   6813 N  N   . GLY F  2  143 ? 25.126 27.266  51.860  1.00 87.72  ? 143 GLY F N   1 
ATOM   6814 C  CA  . GLY F  2  143 ? 23.813 27.479  52.438  1.00 89.43  ? 143 GLY F CA  1 
ATOM   6815 C  C   . GLY F  2  143 ? 23.685 28.918  52.902  1.00 91.03  ? 143 GLY F C   1 
ATOM   6816 O  O   . GLY F  2  143 ? 22.647 29.318  53.421  1.00 91.37  ? 143 GLY F O   1 
ATOM   6817 N  N   . ASN F  2  144 ? 24.762 29.680  52.702  1.00 92.84  ? 144 ASN F N   1 
ATOM   6818 C  CA  . ASN F  2  144 ? 24.885 31.098  53.062  1.00 94.73  ? 144 ASN F CA  1 
ATOM   6819 C  C   . ASN F  2  144 ? 25.667 31.276  54.363  1.00 96.27  ? 144 ASN F C   1 
ATOM   6820 O  O   . ASN F  2  144 ? 26.814 31.765  54.281  1.00 97.29  ? 144 ASN F O   1 
ATOM   6821 C  CB  . ASN F  2  144 ? 23.512 31.773  53.186  1.00 94.37  ? 144 ASN F CB  1 
ATOM   6822 C  CG  . ASN F  2  144 ? 22.788 31.887  51.851  1.00 94.15  ? 144 ASN F CG  1 
ATOM   6823 O  OD1 . ASN F  2  144 ? 22.638 30.900  51.126  1.00 93.88  ? 144 ASN F OD1 1 
ATOM   6824 N  ND2 . ASN F  2  144 ? 22.327 33.094  51.525  1.00 93.40  ? 144 ASN F ND2 1 
ATOM   6825 O  OXT . ASN F  2  144 ? 25.137 30.916  55.440  1.00 98.11  ? 144 ASN F OXT 1 
ATOM   6826 N  N   . SER G  3  1   ? 30.219 -3.032  10.359  1.00 132.63 ? 1   SER G N   1 
ATOM   6827 C  CA  . SER G  3  1   ? 31.570 -2.679  10.783  1.00 132.02 ? 1   SER G CA  1 
ATOM   6828 C  C   . SER G  3  1   ? 31.686 -2.714  12.305  1.00 130.33 ? 1   SER G C   1 
ATOM   6829 O  O   . SER G  3  1   ? 30.690 -2.891  13.007  1.00 131.33 ? 1   SER G O   1 
ATOM   6830 C  CB  . SER G  3  1   ? 31.931 -1.276  10.276  1.00 133.27 ? 1   SER G CB  1 
ATOM   6831 O  OG  . SER G  3  1   ? 31.063 -0.291  10.812  1.00 134.07 ? 1   SER G OG  1 
ATOM   6832 N  N   . SER G  3  2   ? 32.902 -2.557  12.816  1.00 127.03 ? 2   SER G N   1 
ATOM   6833 C  CA  . SER G  3  2   ? 33.099 -2.557  14.261  1.00 122.61 ? 2   SER G CA  1 
ATOM   6834 C  C   . SER G  3  2   ? 32.295 -1.389  14.825  1.00 118.62 ? 2   SER G C   1 
ATOM   6835 O  O   . SER G  3  2   ? 32.547 -0.232  14.486  1.00 119.31 ? 2   SER G O   1 
ATOM   6836 C  CB  . SER G  3  2   ? 34.579 -2.369  14.609  1.00 123.55 ? 2   SER G CB  1 
ATOM   6837 O  OG  . SER G  3  2   ? 34.984 -1.024  14.416  1.00 124.46 ? 2   SER G OG  1 
ATOM   6838 N  N   . ASN G  3  3   ? 31.319 -1.688  15.673  1.00 112.40 ? 3   ASN G N   1 
ATOM   6839 C  CA  . ASN G  3  3   ? 30.502 -0.640  16.266  1.00 105.61 ? 3   ASN G CA  1 
ATOM   6840 C  C   . ASN G  3  3   ? 31.297 0.138   17.293  1.00 99.65  ? 3   ASN G C   1 
ATOM   6841 O  O   . ASN G  3  3   ? 30.737 0.831   18.142  1.00 98.84  ? 3   ASN G O   1 
ATOM   6842 C  CB  . ASN G  3  3   ? 29.260 -1.241  16.911  1.00 107.77 ? 3   ASN G CB  1 
ATOM   6843 C  CG  . ASN G  3  3   ? 28.274 -1.743  15.889  1.00 109.97 ? 3   ASN G CG  1 
ATOM   6844 O  OD1 . ASN G  3  3   ? 27.265 -2.365  16.229  1.00 111.66 ? 3   ASN G OD1 1 
ATOM   6845 N  ND2 . ASN G  3  3   ? 28.553 -1.472  14.614  1.00 110.67 ? 3   ASN G ND2 1 
ATOM   6846 N  N   . SER G  3  4   ? 32.613 0.021   17.209  1.00 92.34  ? 4   SER G N   1 
ATOM   6847 C  CA  . SER G  3  4   ? 33.483 0.722   18.132  1.00 84.69  ? 4   SER G CA  1 
ATOM   6848 C  C   . SER G  3  4   ? 33.424 2.214   17.861  1.00 79.12  ? 4   SER G C   1 
ATOM   6849 O  O   . SER G  3  4   ? 33.376 2.641   16.704  1.00 78.72  ? 4   SER G O   1 
ATOM   6850 C  CB  . SER G  3  4   ? 34.928 0.233   17.978  1.00 84.88  ? 4   SER G CB  1 
ATOM   6851 O  OG  . SER G  3  4   ? 35.062 -1.118  18.374  1.00 82.17  ? 4   SER G OG  1 
ATOM   6852 N  N   . CYS G  3  5   ? 33.406 2.999   18.930  1.00 71.84  ? 5   CYS G N   1 
ATOM   6853 C  CA  . CYS G  3  5   ? 33.405 4.449   18.816  1.00 65.38  ? 5   CYS G CA  1 
ATOM   6854 C  C   . CYS G  3  5   ? 34.853 4.806   18.488  1.00 62.10  ? 5   CYS G C   1 
ATOM   6855 O  O   . CYS G  3  5   ? 35.734 4.717   19.342  1.00 59.88  ? 5   CYS G O   1 
ATOM   6856 C  CB  . CYS G  3  5   ? 32.958 5.074   20.144  1.00 63.91  ? 5   CYS G CB  1 
ATOM   6857 S  SG  . CYS G  3  5   ? 33.248 6.870   20.302  1.00 60.79  ? 5   CYS G SG  1 
ATOM   6858 N  N   . THR G  3  6   ? 35.098 5.188   17.239  1.00 60.02  ? 6   THR G N   1 
ATOM   6859 C  CA  . THR G  3  6   ? 36.446 5.511   16.785  1.00 56.92  ? 6   THR G CA  1 
ATOM   6860 C  C   . THR G  3  6   ? 36.834 6.960   17.021  1.00 56.18  ? 6   THR G C   1 
ATOM   6861 O  O   . THR G  3  6   ? 36.016 7.784   17.449  1.00 53.20  ? 6   THR G O   1 
ATOM   6862 C  CB  . THR G  3  6   ? 36.606 5.240   15.279  1.00 57.31  ? 6   THR G CB  1 
ATOM   6863 O  OG1 . THR G  3  6   ? 35.845 6.207   14.532  1.00 57.54  ? 6   THR G OG1 1 
ATOM   6864 C  CG2 . THR G  3  6   ? 36.118 3.847   14.937  1.00 56.52  ? 6   THR G CG2 1 
ATOM   6865 N  N   . THR G  3  7   ? 38.102 7.254   16.736  1.00 55.72  ? 7   THR G N   1 
ATOM   6866 C  CA  . THR G  3  7   ? 38.615 8.598   16.874  1.00 56.77  ? 7   THR G CA  1 
ATOM   6867 C  C   . THR G  3  7   ? 37.842 9.554   15.965  1.00 57.18  ? 7   THR G C   1 
ATOM   6868 O  O   . THR G  3  7   ? 37.435 10.632  16.397  1.00 58.55  ? 7   THR G O   1 
ATOM   6869 C  CB  . THR G  3  7   ? 40.102 8.655   16.532  1.00 57.74  ? 7   THR G CB  1 
ATOM   6870 O  OG1 . THR G  3  7   ? 40.835 7.929   17.527  1.00 62.24  ? 7   THR G OG1 1 
ATOM   6871 C  CG2 . THR G  3  7   ? 40.592 10.100  16.500  1.00 55.79  ? 7   THR G CG2 1 
ATOM   6872 N  N   . GLU G  3  8   ? 37.621 9.178   14.711  1.00 56.58  ? 8   GLU G N   1 
ATOM   6873 C  CA  . GLU G  3  8   ? 36.878 10.081  13.845  1.00 56.77  ? 8   GLU G CA  1 
ATOM   6874 C  C   . GLU G  3  8   ? 35.420 10.224  14.277  1.00 56.16  ? 8   GLU G C   1 
ATOM   6875 O  O   . GLU G  3  8   ? 34.823 11.290  14.083  1.00 55.10  ? 8   GLU G O   1 
ATOM   6876 C  CB  . GLU G  3  8   ? 36.962 9.663   12.368  1.00 56.84  ? 8   GLU G CB  1 
ATOM   6877 C  CG  . GLU G  3  8   ? 37.065 8.195   12.104  1.00 58.10  ? 8   GLU G CG  1 
ATOM   6878 C  CD  . GLU G  3  8   ? 38.475 7.683   12.259  1.00 60.00  ? 8   GLU G CD  1 
ATOM   6879 O  OE1 . GLU G  3  8   ? 39.298 7.818   11.327  1.00 59.01  ? 8   GLU G OE1 1 
ATOM   6880 O  OE2 . GLU G  3  8   ? 38.769 7.150   13.339  1.00 63.89  ? 8   GLU G OE2 1 
ATOM   6881 N  N   . ASP G  3  9   ? 34.849 9.171   14.867  1.00 54.34  ? 9   ASP G N   1 
ATOM   6882 C  CA  . ASP G  3  9   ? 33.459 9.245   15.313  1.00 53.77  ? 9   ASP G CA  1 
ATOM   6883 C  C   . ASP G  3  9   ? 33.326 10.192  16.478  1.00 52.87  ? 9   ASP G C   1 
ATOM   6884 O  O   . ASP G  3  9   ? 32.308 10.854  16.627  1.00 54.55  ? 9   ASP G O   1 
ATOM   6885 C  CB  . ASP G  3  9   ? 32.918 7.880   15.745  1.00 54.86  ? 9   ASP G CB  1 
ATOM   6886 C  CG  . ASP G  3  9   ? 32.775 6.906   14.587  1.00 54.52  ? 9   ASP G CG  1 
ATOM   6887 O  OD1 . ASP G  3  9   ? 32.492 7.353   13.443  1.00 55.17  ? 9   ASP G OD1 1 
ATOM   6888 O  OD2 . ASP G  3  9   ? 32.931 5.693   14.852  1.00 51.55  ? 9   ASP G OD2 1 
ATOM   6889 N  N   . ARG G  3  10  ? 34.355 10.248  17.307  1.00 52.39  ? 10  ARG G N   1 
ATOM   6890 C  CA  . ARG G  3  10  ? 34.327 11.123  18.469  1.00 52.39  ? 10  ARG G CA  1 
ATOM   6891 C  C   . ARG G  3  10  ? 34.329 12.578  18.051  1.00 53.30  ? 10  ARG G C   1 
ATOM   6892 O  O   . ARG G  3  10  ? 33.517 13.368  18.525  1.00 53.20  ? 10  ARG G O   1 
ATOM   6893 C  CB  . ARG G  3  10  ? 35.514 10.814  19.374  1.00 51.34  ? 10  ARG G CB  1 
ATOM   6894 C  CG  . ARG G  3  10  ? 35.341 9.492   20.108  1.00 51.29  ? 10  ARG G CG  1 
ATOM   6895 C  CD  . ARG G  3  10  ? 36.665 8.798   20.350  1.00 52.20  ? 10  ARG G CD  1 
ATOM   6896 N  NE  . ARG G  3  10  ? 36.477 7.381   20.653  1.00 51.01  ? 10  ARG G NE  1 
ATOM   6897 C  CZ  . ARG G  3  10  ? 36.559 6.847   21.872  1.00 52.06  ? 10  ARG G CZ  1 
ATOM   6898 N  NH1 . ARG G  3  10  ? 36.834 7.623   22.913  1.00 50.83  ? 10  ARG G NH1 1 
ATOM   6899 N  NH2 . ARG G  3  10  ? 36.350 5.541   22.052  1.00 50.17  ? 10  ARG G NH2 1 
ATOM   6900 N  N   . ARG G  3  11  ? 35.233 12.926  17.145  1.00 55.86  ? 11  ARG G N   1 
ATOM   6901 C  CA  . ARG G  3  11  ? 35.330 14.297  16.654  1.00 56.76  ? 11  ARG G CA  1 
ATOM   6902 C  C   . ARG G  3  11  ? 33.973 14.700  16.096  1.00 55.10  ? 11  ARG G C   1 
ATOM   6903 O  O   . ARG G  3  11  ? 33.503 15.812  16.307  1.00 54.36  ? 11  ARG G O   1 
ATOM   6904 C  CB  . ARG G  3  11  ? 36.372 14.380  15.550  1.00 59.00  ? 11  ARG G CB  1 
ATOM   6905 C  CG  . ARG G  3  11  ? 37.767 13.967  15.969  1.00 62.29  ? 11  ARG G CG  1 
ATOM   6906 C  CD  . ARG G  3  11  ? 38.573 13.523  14.748  1.00 65.86  ? 11  ARG G CD  1 
ATOM   6907 N  NE  . ARG G  3  11  ? 39.995 13.343  15.037  1.00 67.26  ? 11  ARG G NE  1 
ATOM   6908 C  CZ  . ARG G  3  11  ? 40.880 12.861  14.170  1.00 68.66  ? 11  ARG G CZ  1 
ATOM   6909 N  NH1 . ARG G  3  11  ? 40.497 12.499  12.949  1.00 67.78  ? 11  ARG G NH1 1 
ATOM   6910 N  NH2 . ARG G  3  11  ? 42.156 12.744  14.524  1.00 70.38  ? 11  ARG G NH2 1 
ATOM   6911 N  N   . GLU G  3  12  ? 33.363 13.765  15.377  1.00 54.79  ? 12  GLU G N   1 
ATOM   6912 C  CA  . GLU G  3  12  ? 32.053 13.967  14.769  1.00 55.36  ? 12  GLU G CA  1 
ATOM   6913 C  C   . GLU G  3  12  ? 31.011 14.265  15.833  1.00 54.46  ? 12  GLU G C   1 
ATOM   6914 O  O   . GLU G  3  12  ? 30.223 15.205  15.707  1.00 53.32  ? 12  GLU G O   1 
ATOM   6915 C  CB  . GLU G  3  12  ? 31.615 12.711  14.029  1.00 57.12  ? 12  GLU G CB  1 
ATOM   6916 C  CG  . GLU G  3  12  ? 31.946 12.680  12.560  1.00 61.67  ? 12  GLU G CG  1 
ATOM   6917 C  CD  . GLU G  3  12  ? 30.774 12.150  11.745  1.00 65.43  ? 12  GLU G CD  1 
ATOM   6918 O  OE1 . GLU G  3  12  ? 29.758 12.883  11.581  1.00 65.32  ? 12  GLU G OE1 1 
ATOM   6919 O  OE2 . GLU G  3  12  ? 30.866 10.993  11.285  1.00 68.51  ? 12  GLU G OE2 1 
ATOM   6920 N  N   . MET G  3  13  ? 31.000 13.432  16.866  1.00 53.28  ? 13  MET G N   1 
ATOM   6921 C  CA  . MET G  3  13  ? 30.058 13.602  17.951  1.00 52.56  ? 13  MET G CA  1 
ATOM   6922 C  C   . MET G  3  13  ? 30.293 14.903  18.716  1.00 51.69  ? 13  MET G C   1 
ATOM   6923 O  O   . MET G  3  13  ? 29.341 15.499  19.223  1.00 51.61  ? 13  MET G O   1 
ATOM   6924 C  CB  . MET G  3  13  ? 30.118 12.415  18.919  1.00 53.06  ? 13  MET G CB  1 
ATOM   6925 C  CG  . MET G  3  13  ? 29.155 12.591  20.084  1.00 53.79  ? 13  MET G CG  1 
ATOM   6926 S  SD  . MET G  3  13  ? 29.060 11.252  21.280  1.00 55.35  ? 13  MET G SD  1 
ATOM   6927 C  CE  . MET G  3  13  ? 27.286 11.218  21.605  1.00 51.37  ? 13  MET G CE  1 
ATOM   6928 N  N   . GLN G  3  14  ? 31.550 15.339  18.801  1.00 50.15  ? 14  GLN G N   1 
ATOM   6929 C  CA  . GLN G  3  14  ? 31.871 16.576  19.502  1.00 51.40  ? 14  GLN G CA  1 
ATOM   6930 C  C   . GLN G  3  14  ? 31.371 17.763  18.700  1.00 51.74  ? 14  GLN G C   1 
ATOM   6931 O  O   . GLN G  3  14  ? 31.004 18.770  19.272  1.00 52.37  ? 14  GLN G O   1 
ATOM   6932 C  CB  . GLN G  3  14  ? 33.378 16.677  19.743  1.00 52.65  ? 14  GLN G CB  1 
ATOM   6933 C  CG  . GLN G  3  14  ? 33.830 15.809  20.913  1.00 55.61  ? 14  GLN G CG  1 
ATOM   6934 C  CD  . GLN G  3  14  ? 35.331 15.520  20.940  1.00 56.96  ? 14  GLN G CD  1 
ATOM   6935 O  OE1 . GLN G  3  14  ? 35.807 14.779  21.805  1.00 56.61  ? 14  GLN G OE1 1 
ATOM   6936 N  NE2 . GLN G  3  14  ? 36.074 16.097  19.995  1.00 55.90  ? 14  GLN G NE2 1 
ATOM   6937 N  N   . LEU G  3  15  ? 31.352 17.627  17.382  1.00 52.08  ? 15  LEU G N   1 
ATOM   6938 C  CA  . LEU G  3  15  ? 30.869 18.684  16.514  1.00 53.96  ? 15  LEU G CA  1 
ATOM   6939 C  C   . LEU G  3  15  ? 29.348 18.734  16.582  1.00 53.24  ? 15  LEU G C   1 
ATOM   6940 O  O   . LEU G  3  15  ? 28.782 19.799  16.689  1.00 53.54  ? 15  LEU G O   1 
ATOM   6941 C  CB  . LEU G  3  15  ? 31.295 18.434  15.061  1.00 56.69  ? 15  LEU G CB  1 
ATOM   6942 C  CG  . LEU G  3  15  ? 32.621 18.995  14.537  1.00 56.90  ? 15  LEU G CG  1 
ATOM   6943 C  CD1 . LEU G  3  15  ? 32.876 18.450  13.149  1.00 57.58  ? 15  LEU G CD1 1 
ATOM   6944 C  CD2 . LEU G  3  15  ? 32.569 20.519  14.510  1.00 58.24  ? 15  LEU G CD2 1 
ATOM   6945 N  N   . MET G  3  16  ? 28.687 17.585  16.506  1.00 53.19  ? 16  MET G N   1 
ATOM   6946 C  CA  . MET G  3  16  ? 27.237 17.576  16.564  1.00 55.87  ? 16  MET G CA  1 
ATOM   6947 C  C   . MET G  3  16  ? 26.782 18.196  17.865  1.00 57.78  ? 16  MET G C   1 
ATOM   6948 O  O   . MET G  3  16  ? 25.842 18.956  17.897  1.00 58.72  ? 16  MET G O   1 
ATOM   6949 C  CB  . MET G  3  16  ? 26.679 16.158  16.473  1.00 54.23  ? 16  MET G CB  1 
ATOM   6950 C  CG  . MET G  3  16  ? 26.878 15.507  15.140  1.00 53.68  ? 16  MET G CG  1 
ATOM   6951 S  SD  . MET G  3  16  ? 26.236 13.815  15.113  1.00 54.83  ? 16  MET G SD  1 
ATOM   6952 C  CE  . MET G  3  16  ? 27.690 12.879  15.472  1.00 52.88  ? 16  MET G CE  1 
ATOM   6953 N  N   . TRP G  3  17  ? 27.466 17.872  18.944  1.00 60.42  ? 17  TRP G N   1 
ATOM   6954 C  CA  . TRP G  3  17  ? 27.131 18.384  20.260  1.00 63.57  ? 17  TRP G CA  1 
ATOM   6955 C  C   . TRP G  3  17  ? 27.334 19.890  20.326  1.00 67.80  ? 17  TRP G C   1 
ATOM   6956 O  O   . TRP G  3  17  ? 26.366 20.633  20.427  1.00 68.46  ? 17  TRP G O   1 
ATOM   6957 C  CB  . TRP G  3  17  ? 27.979 17.678  21.318  1.00 60.13  ? 17  TRP G CB  1 
ATOM   6958 C  CG  . TRP G  3  17  ? 27.551 17.923  22.727  1.00 54.70  ? 17  TRP G CG  1 
ATOM   6959 C  CD1 . TRP G  3  17  ? 28.280 18.517  23.726  1.00 53.11  ? 17  TRP G CD1 1 
ATOM   6960 C  CD2 . TRP G  3  17  ? 26.278 17.606  23.290  1.00 52.53  ? 17  TRP G CD2 1 
ATOM   6961 N  NE1 . TRP G  3  17  ? 27.530 18.592  24.876  1.00 52.71  ? 17  TRP G NE1 1 
ATOM   6962 C  CE2 . TRP G  3  17  ? 26.295 18.041  24.633  1.00 52.33  ? 17  TRP G CE2 1 
ATOM   6963 C  CE3 . TRP G  3  17  ? 25.117 16.994  22.785  1.00 52.26  ? 17  TRP G CE3 1 
ATOM   6964 C  CZ2 . TRP G  3  17  ? 25.192 17.888  25.478  1.00 50.71  ? 17  TRP G CZ2 1 
ATOM   6965 C  CZ3 . TRP G  3  17  ? 24.025 16.839  23.621  1.00 50.53  ? 17  TRP G CZ3 1 
ATOM   6966 C  CH2 . TRP G  3  17  ? 24.069 17.286  24.955  1.00 50.23  ? 17  TRP G CH2 1 
ATOM   6967 N  N   . ALA G  3  18  ? 28.588 20.332  20.264  1.00 73.61  ? 18  ALA G N   1 
ATOM   6968 C  CA  . ALA G  3  18  ? 28.924 21.755  20.315  1.00 80.29  ? 18  ALA G CA  1 
ATOM   6969 C  C   . ALA G  3  18  ? 27.985 22.577  19.440  1.00 84.75  ? 18  ALA G C   1 
ATOM   6970 O  O   . ALA G  3  18  ? 27.900 23.791  19.571  1.00 85.23  ? 18  ALA G O   1 
ATOM   6971 C  CB  . ALA G  3  18  ? 30.351 21.969  19.880  1.00 79.40  ? 18  ALA G CB  1 
ATOM   6972 N  N   . ASN G  3  19  ? 27.265 21.898  18.558  1.00 90.17  ? 19  ASN G N   1 
ATOM   6973 C  CA  . ASN G  3  19  ? 26.325 22.550  17.662  1.00 95.55  ? 19  ASN G CA  1 
ATOM   6974 C  C   . ASN G  3  19  ? 25.183 23.211  18.443  1.00 97.32  ? 19  ASN G C   1 
ATOM   6975 O  O   . ASN G  3  19  ? 24.933 24.406  18.290  1.00 98.40  ? 19  ASN G O   1 
ATOM   6976 C  CB  . ASN G  3  19  ? 25.760 21.522  16.677  1.00 98.37  ? 19  ASN G CB  1 
ATOM   6977 C  CG  . ASN G  3  19  ? 25.668 22.064  15.270  1.00 101.01 ? 19  ASN G CG  1 
ATOM   6978 O  OD1 . ASN G  3  19  ? 24.585 22.472  14.795  1.00 101.96 ? 19  ASN G OD1 1 
ATOM   6979 N  ND2 . ASN G  3  19  ? 26.822 22.108  14.594  1.00 101.82 ? 19  ASN G ND2 1 
ATOM   6980 N  N   . VAL G  3  20  ? 24.483 22.428  19.260  1.00 98.29  ? 20  VAL G N   1 
ATOM   6981 C  CA  . VAL G  3  20  ? 23.377 22.954  20.046  1.00 99.91  ? 20  VAL G CA  1 
ATOM   6982 C  C   . VAL G  3  20  ? 23.744 23.015  21.540  1.00 99.66  ? 20  VAL G C   1 
ATOM   6983 O  O   . VAL G  3  20  ? 22.924 22.779  22.428  1.00 100.54 ? 20  VAL G O   1 
ATOM   6984 C  CB  . VAL G  3  20  ? 22.118 22.112  19.832  1.00 101.29 ? 20  VAL G CB  1 
ATOM   6985 C  CG1 . VAL G  3  20  ? 21.025 22.604  20.719  1.00 103.73 ? 20  VAL G CG1 1 
ATOM   6986 C  CG2 . VAL G  3  20  ? 21.585 22.323  18.422  1.00 102.93 ? 20  VAL G CG2 1 
ATOM   6987 N  N   . TRP G  3  21  ? 24.997 23.337  21.830  1.00 98.56  ? 21  TRP G N   1 
ATOM   6988 C  CA  . TRP G  3  21  ? 25.416 23.404  23.222  1.00 96.35  ? 21  TRP G CA  1 
ATOM   6989 C  C   . TRP G  3  21  ? 25.933 24.800  23.539  1.00 95.90  ? 21  TRP G C   1 
ATOM   6990 O  O   . TRP G  3  21  ? 27.131 25.042  23.478  1.00 95.31  ? 21  TRP G O   1 
ATOM   6991 C  CB  . TRP G  3  21  ? 26.519 22.385  23.473  1.00 94.61  ? 21  TRP G CB  1 
ATOM   6992 C  CG  . TRP G  3  21  ? 26.934 22.280  24.913  1.00 92.76  ? 21  TRP G CG  1 
ATOM   6993 C  CD1 . TRP G  3  21  ? 26.399 21.463  25.877  1.00 91.94  ? 21  TRP G CD1 1 
ATOM   6994 C  CD2 . TRP G  3  21  ? 27.952 23.044  25.560  1.00 92.42  ? 21  TRP G CD2 1 
ATOM   6995 N  NE1 . TRP G  3  21  ? 27.026 21.678  27.091  1.00 91.06  ? 21  TRP G NE1 1 
ATOM   6996 C  CE2 . TRP G  3  21  ? 27.984 22.644  26.923  1.00 91.62  ? 21  TRP G CE2 1 
ATOM   6997 C  CE3 . TRP G  3  21  ? 28.841 24.031  25.125  1.00 92.53  ? 21  TRP G CE3 1 
ATOM   6998 C  CZ2 . TRP G  3  21  ? 28.875 23.202  27.850  1.00 90.92  ? 21  TRP G CZ2 1 
ATOM   6999 C  CZ3 . TRP G  3  21  ? 29.729 24.589  26.052  1.00 92.43  ? 21  TRP G CZ3 1 
ATOM   7000 C  CH2 . TRP G  3  21  ? 29.736 24.171  27.397  1.00 90.92  ? 21  TRP G CH2 1 
ATOM   7001 N  N   . SER G  3  22  ? 25.018 25.709  23.880  1.00 95.96  ? 22  SER G N   1 
ATOM   7002 C  CA  . SER G  3  22  ? 25.390 27.091  24.199  1.00 96.20  ? 22  SER G CA  1 
ATOM   7003 C  C   . SER G  3  22  ? 26.242 27.132  25.464  1.00 95.98  ? 22  SER G C   1 
ATOM   7004 O  O   . SER G  3  22  ? 25.810 26.672  26.524  1.00 95.86  ? 22  SER G O   1 
ATOM   7005 C  CB  . SER G  3  22  ? 24.144 27.969  24.402  1.00 96.10  ? 22  SER G CB  1 
ATOM   7006 O  OG  . SER G  3  22  ? 23.349 27.471  25.457  1.00 95.08  ? 22  SER G OG  1 
ATOM   7007 N  N   . ALA G  3  23  ? 27.445 27.687  25.353  1.00 94.99  ? 23  ALA G N   1 
ATOM   7008 C  CA  . ALA G  3  23  ? 28.366 27.770  26.488  1.00 95.24  ? 23  ALA G CA  1 
ATOM   7009 C  C   . ALA G  3  23  ? 28.106 28.920  27.476  1.00 94.80  ? 23  ALA G C   1 
ATOM   7010 O  O   . ALA G  3  23  ? 28.780 29.014  28.507  1.00 94.36  ? 23  ALA G O   1 
ATOM   7011 C  CB  . ALA G  3  23  ? 29.799 27.854  25.970  1.00 95.47  ? 23  ALA G CB  1 
ATOM   7012 N  N   . GLN G  3  24  ? 27.124 29.771  27.174  1.00 94.26  ? 24  GLN G N   1 
ATOM   7013 C  CA  . GLN G  3  24  ? 26.814 30.923  28.022  1.00 93.17  ? 24  GLN G CA  1 
ATOM   7014 C  C   . GLN G  3  24  ? 25.478 30.908  28.756  1.00 92.85  ? 24  GLN G C   1 
ATOM   7015 O  O   . GLN G  3  24  ? 25.369 31.447  29.862  1.00 91.57  ? 24  GLN G O   1 
ATOM   7016 C  CB  . GLN G  3  24  ? 26.903 32.212  27.202  1.00 92.76  ? 24  GLN G CB  1 
ATOM   7017 C  CG  . GLN G  3  24  ? 28.314 32.753  27.053  1.00 93.63  ? 24  GLN G CG  1 
ATOM   7018 C  CD  . GLN G  3  24  ? 28.346 34.133  26.426  1.00 93.43  ? 24  GLN G CD  1 
ATOM   7019 O  OE1 . GLN G  3  24  ? 27.603 35.029  26.830  1.00 92.39  ? 24  GLN G OE1 1 
ATOM   7020 N  NE2 . GLN G  3  24  ? 29.216 34.316  25.435  1.00 93.18  ? 24  GLN G NE2 1 
ATOM   7021 N  N   . PHE G  3  25  ? 24.462 30.318  28.135  1.00 93.16  ? 25  PHE G N   1 
ATOM   7022 C  CA  . PHE G  3  25  ? 23.134 30.244  28.734  1.00 92.63  ? 25  PHE G CA  1 
ATOM   7023 C  C   . PHE G  3  25  ? 22.642 28.819  28.727  1.00 91.58  ? 25  PHE G C   1 
ATOM   7024 O  O   . PHE G  3  25  ? 23.250 27.946  28.112  1.00 91.76  ? 25  PHE G O   1 
ATOM   7025 C  CB  . PHE G  3  25  ? 22.150 31.141  27.982  1.00 94.02  ? 25  PHE G CB  1 
ATOM   7026 C  CG  . PHE G  3  25  ? 22.414 32.601  28.170  1.00 95.90  ? 25  PHE G CG  1 
ATOM   7027 C  CD1 . PHE G  3  25  ? 21.859 33.295  29.241  1.00 96.63  ? 25  PHE G CD1 1 
ATOM   7028 C  CD2 . PHE G  3  25  ? 23.272 33.274  27.306  1.00 96.97  ? 25  PHE G CD2 1 
ATOM   7029 C  CE1 . PHE G  3  25  ? 22.158 34.641  29.453  1.00 97.45  ? 25  PHE G CE1 1 
ATOM   7030 C  CE2 . PHE G  3  25  ? 23.579 34.618  27.506  1.00 97.80  ? 25  PHE G CE2 1 
ATOM   7031 C  CZ  . PHE G  3  25  ? 23.023 35.304  28.583  1.00 97.98  ? 25  PHE G CZ  1 
ATOM   7032 N  N   . THR G  3  26  ? 21.528 28.595  29.406  1.00 90.67  ? 26  THR G N   1 
ATOM   7033 C  CA  . THR G  3  26  ? 20.954 27.265  29.527  1.00 89.46  ? 26  THR G CA  1 
ATOM   7034 C  C   . THR G  3  26  ? 19.699 27.035  28.703  1.00 87.74  ? 26  THR G C   1 
ATOM   7035 O  O   . THR G  3  26  ? 19.216 25.908  28.598  1.00 88.49  ? 26  THR G O   1 
ATOM   7036 C  CB  . THR G  3  26  ? 20.629 26.973  31.000  1.00 90.11  ? 26  THR G CB  1 
ATOM   7037 O  OG1 . THR G  3  26  ? 19.862 28.058  31.544  1.00 90.20  ? 26  THR G OG1 1 
ATOM   7038 C  CG2 . THR G  3  26  ? 21.910 26.819  31.801  1.00 90.73  ? 26  THR G CG2 1 
ATOM   7039 N  N   . GLY G  3  27  ? 19.174 28.100  28.111  1.00 85.25  ? 27  GLY G N   1 
ATOM   7040 C  CA  . GLY G  3  27  ? 17.957 27.971  27.326  1.00 82.31  ? 27  GLY G CA  1 
ATOM   7041 C  C   . GLY G  3  27  ? 17.987 26.796  26.380  1.00 79.85  ? 27  GLY G C   1 
ATOM   7042 O  O   . GLY G  3  27  ? 17.080 25.963  26.380  1.00 80.37  ? 27  GLY G O   1 
ATOM   7043 N  N   . ARG G  3  28  ? 19.044 26.736  25.582  1.00 76.78  ? 28  ARG G N   1 
ATOM   7044 C  CA  . ARG G  3  28  ? 19.221 25.684  24.592  1.00 73.47  ? 28  ARG G CA  1 
ATOM   7045 C  C   . ARG G  3  28  ? 19.431 24.324  25.252  1.00 70.95  ? 28  ARG G C   1 
ATOM   7046 O  O   . ARG G  3  28  ? 18.855 23.314  24.829  1.00 70.19  ? 28  ARG G O   1 
ATOM   7047 C  CB  . ARG G  3  28  ? 20.413 26.049  23.705  1.00 74.93  ? 28  ARG G CB  1 
ATOM   7048 C  CG  . ARG G  3  28  ? 20.345 25.509  22.287  1.00 77.50  ? 28  ARG G CG  1 
ATOM   7049 C  CD  . ARG G  3  28  ? 20.903 26.532  21.304  1.00 78.34  ? 28  ARG G CD  1 
ATOM   7050 N  NE  . ARG G  3  28  ? 22.318 26.824  21.534  1.00 80.91  ? 28  ARG G NE  1 
ATOM   7051 C  CZ  . ARG G  3  28  ? 22.869 28.033  21.412  1.00 81.66  ? 28  ARG G CZ  1 
ATOM   7052 N  NH1 . ARG G  3  28  ? 24.168 28.207  21.630  1.00 80.39  ? 28  ARG G NH1 1 
ATOM   7053 N  NH2 . ARG G  3  28  ? 22.117 29.079  21.089  1.00 82.16  ? 28  ARG G NH2 1 
ATOM   7054 N  N   . ARG G  3  29  ? 20.254 24.304  26.296  1.00 68.13  ? 29  ARG G N   1 
ATOM   7055 C  CA  . ARG G  3  29  ? 20.542 23.061  27.012  1.00 65.81  ? 29  ARG G CA  1 
ATOM   7056 C  C   . ARG G  3  29  ? 19.259 22.446  27.566  1.00 64.49  ? 29  ARG G C   1 
ATOM   7057 O  O   . ARG G  3  29  ? 18.992 21.249  27.412  1.00 64.28  ? 29  ARG G O   1 
ATOM   7058 C  CB  . ARG G  3  29  ? 21.496 23.330  28.179  1.00 64.42  ? 29  ARG G CB  1 
ATOM   7059 C  CG  . ARG G  3  29  ? 22.750 24.055  27.817  1.00 64.31  ? 29  ARG G CG  1 
ATOM   7060 C  CD  . ARG G  3  29  ? 23.646 24.174  29.026  1.00 64.52  ? 29  ARG G CD  1 
ATOM   7061 N  NE  . ARG G  3  29  ? 24.820 24.990  28.755  1.00 66.16  ? 29  ARG G NE  1 
ATOM   7062 C  CZ  . ARG G  3  29  ? 25.784 25.209  29.639  1.00 67.23  ? 29  ARG G CZ  1 
ATOM   7063 N  NH1 . ARG G  3  29  ? 25.706 24.662  30.846  1.00 67.19  ? 29  ARG G NH1 1 
ATOM   7064 N  NH2 . ARG G  3  29  ? 26.827 25.963  29.317  1.00 69.49  ? 29  ARG G NH2 1 
ATOM   7065 N  N   . LEU G  3  30  ? 18.469 23.299  28.205  1.00 62.24  ? 30  LEU G N   1 
ATOM   7066 C  CA  . LEU G  3  30  ? 17.230 22.899  28.844  1.00 61.33  ? 30  LEU G CA  1 
ATOM   7067 C  C   . LEU G  3  30  ? 16.237 22.335  27.862  1.00 59.81  ? 30  LEU G C   1 
ATOM   7068 O  O   . LEU G  3  30  ? 15.701 21.258  28.061  1.00 58.90  ? 30  LEU G O   1 
ATOM   7069 C  CB  . LEU G  3  30  ? 16.638 24.110  29.567  1.00 62.56  ? 30  LEU G CB  1 
ATOM   7070 C  CG  . LEU G  3  30  ? 15.853 23.916  30.860  1.00 62.31  ? 30  LEU G CG  1 
ATOM   7071 C  CD1 . LEU G  3  30  ? 16.633 23.029  31.808  1.00 63.90  ? 30  LEU G CD1 1 
ATOM   7072 C  CD2 . LEU G  3  30  ? 15.599 25.266  31.495  1.00 61.89  ? 30  LEU G CD2 1 
ATOM   7073 N  N   . ALA G  3  31  ? 15.992 23.068  26.792  1.00 60.05  ? 31  ALA G N   1 
ATOM   7074 C  CA  . ALA G  3  31  ? 15.038 22.625  25.789  1.00 61.08  ? 31  ALA G CA  1 
ATOM   7075 C  C   . ALA G  3  31  ? 15.347 21.208  25.296  1.00 61.26  ? 31  ALA G C   1 
ATOM   7076 O  O   . ALA G  3  31  ? 14.462 20.366  25.162  1.00 60.94  ? 31  ALA G O   1 
ATOM   7077 C  CB  . ALA G  3  31  ? 15.042 23.598  24.622  1.00 59.67  ? 31  ALA G CB  1 
ATOM   7078 N  N   . ILE G  3  32  ? 16.612 20.946  25.029  1.00 61.16  ? 32  ILE G N   1 
ATOM   7079 C  CA  . ILE G  3  32  ? 16.997 19.644  24.544  1.00 60.05  ? 32  ILE G CA  1 
ATOM   7080 C  C   . ILE G  3  32  ? 16.761 18.580  25.583  1.00 60.40  ? 32  ILE G C   1 
ATOM   7081 O  O   . ILE G  3  32  ? 16.192 17.534  25.280  1.00 60.23  ? 32  ILE G O   1 
ATOM   7082 C  CB  . ILE G  3  32  ? 18.456 19.639  24.168  1.00 59.61  ? 32  ILE G CB  1 
ATOM   7083 C  CG1 . ILE G  3  32  ? 18.685 20.723  23.121  1.00 60.43  ? 32  ILE G CG1 1 
ATOM   7084 C  CG2 . ILE G  3  32  ? 18.844 18.295  23.610  1.00 57.32  ? 32  ILE G CG2 1 
ATOM   7085 C  CD1 . ILE G  3  32  ? 20.138 20.952  22.778  1.00 61.15  ? 32  ILE G CD1 1 
ATOM   7086 N  N   . ALA G  3  33  ? 17.212 18.830  26.806  1.00 60.52  ? 33  ALA G N   1 
ATOM   7087 C  CA  . ALA G  3  33  ? 17.031 17.849  27.874  1.00 62.23  ? 33  ALA G CA  1 
ATOM   7088 C  C   . ALA G  3  33  ? 15.533 17.577  28.082  1.00 63.28  ? 33  ALA G C   1 
ATOM   7089 O  O   . ALA G  3  33  ? 15.086 16.427  28.000  1.00 63.34  ? 33  ALA G O   1 
ATOM   7090 C  CB  . ALA G  3  33  ? 17.672 18.354  29.172  1.00 60.34  ? 33  ALA G CB  1 
ATOM   7091 N  N   . GLN G  3  34  ? 14.765 18.636  28.319  1.00 63.52  ? 34  GLN G N   1 
ATOM   7092 C  CA  . GLN G  3  34  ? 13.330 18.505  28.525  1.00 64.01  ? 34  GLN G CA  1 
ATOM   7093 C  C   . GLN G  3  34  ? 12.683 17.735  27.389  1.00 63.89  ? 34  GLN G C   1 
ATOM   7094 O  O   . GLN G  3  34  ? 11.743 16.988  27.605  1.00 65.56  ? 34  GLN G O   1 
ATOM   7095 C  CB  . GLN G  3  34  ? 12.679 19.875  28.631  1.00 64.38  ? 34  GLN G CB  1 
ATOM   7096 C  CG  . GLN G  3  34  ? 13.067 20.653  29.863  1.00 66.43  ? 34  GLN G CG  1 
ATOM   7097 C  CD  . GLN G  3  34  ? 12.410 22.019  29.921  1.00 70.61  ? 34  GLN G CD  1 
ATOM   7098 O  OE1 . GLN G  3  34  ? 12.590 22.846  29.027  1.00 71.77  ? 34  GLN G OE1 1 
ATOM   7099 N  NE2 . GLN G  3  34  ? 11.644 22.263  30.978  1.00 71.51  ? 34  GLN G NE2 1 
ATOM   7100 N  N   . ALA G  3  35  ? 13.185 17.924  26.175  1.00 63.11  ? 35  ALA G N   1 
ATOM   7101 C  CA  . ALA G  3  35  ? 12.641 17.223  25.019  1.00 62.98  ? 35  ALA G CA  1 
ATOM   7102 C  C   . ALA G  3  35  ? 12.991 15.744  25.058  1.00 63.32  ? 35  ALA G C   1 
ATOM   7103 O  O   . ALA G  3  35  ? 12.205 14.908  24.630  1.00 62.31  ? 35  ALA G O   1 
ATOM   7104 C  CB  . ALA G  3  35  ? 13.159 17.844  23.724  1.00 62.22  ? 35  ALA G CB  1 
ATOM   7105 N  N   . VAL G  3  36  ? 14.185 15.421  25.539  1.00 65.33  ? 36  VAL G N   1 
ATOM   7106 C  CA  . VAL G  3  36  ? 14.607 14.023  25.629  1.00 67.54  ? 36  VAL G CA  1 
ATOM   7107 C  C   . VAL G  3  36  ? 13.775 13.310  26.705  1.00 67.15  ? 36  VAL G C   1 
ATOM   7108 O  O   . VAL G  3  36  ? 13.334 12.179  26.510  1.00 65.44  ? 36  VAL G O   1 
ATOM   7109 C  CB  . VAL G  3  36  ? 16.128 13.919  25.948  1.00 67.58  ? 36  VAL G CB  1 
ATOM   7110 C  CG1 . VAL G  3  36  ? 16.456 12.576  26.601  1.00 66.03  ? 36  VAL G CG1 1 
ATOM   7111 C  CG2 . VAL G  3  36  ? 16.922 14.072  24.655  1.00 67.91  ? 36  VAL G CG2 1 
ATOM   7112 N  N   . PHE G  3  37  ? 13.550 13.984  27.829  1.00 67.15  ? 37  PHE G N   1 
ATOM   7113 C  CA  . PHE G  3  37  ? 12.759 13.387  28.888  1.00 68.01  ? 37  PHE G CA  1 
ATOM   7114 C  C   . PHE G  3  37  ? 11.273 13.296  28.536  1.00 68.30  ? 37  PHE G C   1 
ATOM   7115 O  O   . PHE G  3  37  ? 10.651 12.280  28.831  1.00 68.95  ? 37  PHE G O   1 
ATOM   7116 C  CB  . PHE G  3  37  ? 12.990 14.120  30.214  1.00 67.85  ? 37  PHE G CB  1 
ATOM   7117 C  CG  . PHE G  3  37  ? 14.237 13.676  30.923  1.00 68.00  ? 37  PHE G CG  1 
ATOM   7118 C  CD1 . PHE G  3  37  ? 14.354 12.360  31.370  1.00 68.50  ? 37  PHE G CD1 1 
ATOM   7119 C  CD2 . PHE G  3  37  ? 15.315 14.545  31.095  1.00 67.67  ? 37  PHE G CD2 1 
ATOM   7120 C  CE1 . PHE G  3  37  ? 15.519 11.909  31.972  1.00 67.51  ? 37  PHE G CE1 1 
ATOM   7121 C  CE2 . PHE G  3  37  ? 16.489 14.109  31.694  1.00 67.30  ? 37  PHE G CE2 1 
ATOM   7122 C  CZ  . PHE G  3  37  ? 16.592 12.787  32.135  1.00 68.25  ? 37  PHE G CZ  1 
ATOM   7123 N  N   . LYS G  3  38  ? 10.700 14.321  27.902  1.00 68.84  ? 38  LYS G N   1 
ATOM   7124 C  CA  . LYS G  3  38  ? 9.287  14.235  27.508  1.00 69.42  ? 38  LYS G CA  1 
ATOM   7125 C  C   . LYS G  3  38  ? 9.175  12.966  26.675  1.00 69.57  ? 38  LYS G C   1 
ATOM   7126 O  O   . LYS G  3  38  ? 8.288  12.142  26.895  1.00 70.18  ? 38  LYS G O   1 
ATOM   7127 C  CB  . LYS G  3  38  ? 8.841  15.413  26.631  1.00 69.93  ? 38  LYS G CB  1 
ATOM   7128 C  CG  . LYS G  3  38  ? 8.489  16.703  27.360  1.00 72.31  ? 38  LYS G CG  1 
ATOM   7129 C  CD  . LYS G  3  38  ? 7.815  17.663  26.382  1.00 74.84  ? 38  LYS G CD  1 
ATOM   7130 C  CE  . LYS G  3  38  ? 7.439  18.993  27.025  1.00 76.99  ? 38  LYS G CE  1 
ATOM   7131 N  NZ  . LYS G  3  38  ? 8.637  19.783  27.435  1.00 78.90  ? 38  LYS G NZ  1 
ATOM   7132 N  N   . ASP G  3  39  ? 10.100 12.818  25.728  1.00 69.20  ? 39  ASP G N   1 
ATOM   7133 C  CA  . ASP G  3  39  ? 10.151 11.659  24.843  1.00 68.96  ? 39  ASP G CA  1 
ATOM   7134 C  C   . ASP G  3  39  ? 10.378 10.352  25.612  1.00 70.04  ? 39  ASP G C   1 
ATOM   7135 O  O   . ASP G  3  39  ? 9.702  9.354   25.352  1.00 70.68  ? 39  ASP G O   1 
ATOM   7136 C  CB  . ASP G  3  39  ? 11.258 11.835  23.800  1.00 66.48  ? 39  ASP G CB  1 
ATOM   7137 C  CG  . ASP G  3  39  ? 11.325 10.682  22.811  1.00 64.67  ? 39  ASP G CG  1 
ATOM   7138 O  OD1 . ASP G  3  39  ? 10.965 10.875  21.635  1.00 66.01  ? 39  ASP G OD1 1 
ATOM   7139 O  OD2 . ASP G  3  39  ? 11.734 9.574   23.198  1.00 62.83  ? 39  ASP G OD2 1 
ATOM   7140 N  N   . LEU G  3  40  ? 11.322 10.350  26.552  1.00 69.96  ? 40  LEU G N   1 
ATOM   7141 C  CA  . LEU G  3  40  ? 11.595 9.130   27.310  1.00 70.02  ? 40  LEU G CA  1 
ATOM   7142 C  C   . LEU G  3  40  ? 10.333 8.660   28.019  1.00 70.17  ? 40  LEU G C   1 
ATOM   7143 O  O   . LEU G  3  40  ? 9.947  7.488   27.903  1.00 70.29  ? 40  LEU G O   1 
ATOM   7144 C  CB  . LEU G  3  40  ? 12.708 9.348   28.344  1.00 69.91  ? 40  LEU G CB  1 
ATOM   7145 C  CG  . LEU G  3  40  ? 13.000 8.126   29.233  1.00 71.01  ? 40  LEU G CG  1 
ATOM   7146 C  CD1 . LEU G  3  40  ? 13.492 6.986   28.366  1.00 69.13  ? 40  LEU G CD1 1 
ATOM   7147 C  CD2 . LEU G  3  40  ? 14.030 8.460   30.310  1.00 69.97  ? 40  LEU G CD2 1 
ATOM   7148 N  N   . PHE G  3  41  ? 9.690  9.579   28.739  1.00 68.29  ? 41  PHE G N   1 
ATOM   7149 C  CA  . PHE G  3  41  ? 8.475  9.256   29.473  1.00 66.49  ? 41  PHE G CA  1 
ATOM   7150 C  C   . PHE G  3  41  ? 7.326  8.704   28.589  1.00 67.58  ? 41  PHE G C   1 
ATOM   7151 O  O   . PHE G  3  41  ? 6.671  7.729   28.961  1.00 67.40  ? 41  PHE G O   1 
ATOM   7152 C  CB  . PHE G  3  41  ? 8.000  10.482  30.266  1.00 63.03  ? 41  PHE G CB  1 
ATOM   7153 C  CG  . PHE G  3  41  ? 9.012  11.005  31.263  1.00 58.38  ? 41  PHE G CG  1 
ATOM   7154 C  CD1 . PHE G  3  41  ? 10.035 10.187  31.743  1.00 56.02  ? 41  PHE G CD1 1 
ATOM   7155 C  CD2 . PHE G  3  41  ? 8.907  12.307  31.751  1.00 56.29  ? 41  PHE G CD2 1 
ATOM   7156 C  CE1 . PHE G  3  41  ? 10.941 10.658  32.701  1.00 55.37  ? 41  PHE G CE1 1 
ATOM   7157 C  CE2 . PHE G  3  41  ? 9.801  12.796  32.707  1.00 56.13  ? 41  PHE G CE2 1 
ATOM   7158 C  CZ  . PHE G  3  41  ? 10.827 11.969  33.190  1.00 56.23  ? 41  PHE G CZ  1 
ATOM   7159 N  N   . ALA G  3  42  ? 7.098  9.299   27.417  1.00 68.20  ? 42  ALA G N   1 
ATOM   7160 C  CA  . ALA G  3  42  ? 6.026  8.841   26.520  1.00 68.74  ? 42  ALA G CA  1 
ATOM   7161 C  C   . ALA G  3  42  ? 6.256  7.447   25.926  1.00 70.07  ? 42  ALA G C   1 
ATOM   7162 O  O   . ALA G  3  42  ? 5.326  6.837   25.398  1.00 71.34  ? 42  ALA G O   1 
ATOM   7163 C  CB  . ALA G  3  42  ? 5.812  9.847   25.394  1.00 66.26  ? 42  ALA G CB  1 
ATOM   7164 N  N   . HIS G  3  43  ? 7.490  6.947   26.000  1.00 71.06  ? 43  HIS G N   1 
ATOM   7165 C  CA  . HIS G  3  43  ? 7.807  5.627   25.458  1.00 72.53  ? 43  HIS G CA  1 
ATOM   7166 C  C   . HIS G  3  43  ? 7.989  4.609   26.587  1.00 74.02  ? 43  HIS G C   1 
ATOM   7167 O  O   . HIS G  3  43  ? 7.926  3.389   26.367  1.00 73.81  ? 43  HIS G O   1 
ATOM   7168 C  CB  . HIS G  3  43  ? 9.079  5.674   24.588  1.00 72.02  ? 43  HIS G CB  1 
ATOM   7169 C  CG  . HIS G  3  43  ? 8.938  6.513   23.348  1.00 71.31  ? 43  HIS G CG  1 
ATOM   7170 N  ND1 . HIS G  3  43  ? 8.761  7.880   23.392  1.00 71.35  ? 43  HIS G ND1 1 
ATOM   7171 C  CD2 . HIS G  3  43  ? 8.924  6.176   22.033  1.00 69.42  ? 43  HIS G CD2 1 
ATOM   7172 C  CE1 . HIS G  3  43  ? 8.640  8.348   22.160  1.00 70.39  ? 43  HIS G CE1 1 
ATOM   7173 N  NE2 . HIS G  3  43  ? 8.732  7.333   21.317  1.00 67.92  ? 43  HIS G NE2 1 
ATOM   7174 N  N   . VAL G  3  44  ? 8.209  5.106   27.794  1.00 76.08  ? 44  VAL G N   1 
ATOM   7175 C  CA  . VAL G  3  44  ? 8.411  4.277   28.978  1.00 78.96  ? 44  VAL G CA  1 
ATOM   7176 C  C   . VAL G  3  44  ? 7.749  5.025   30.141  1.00 80.63  ? 44  VAL G C   1 
ATOM   7177 O  O   . VAL G  3  44  ? 8.427  5.690   30.923  1.00 80.75  ? 44  VAL G O   1 
ATOM   7178 C  CB  . VAL G  3  44  ? 9.900  4.085   29.282  1.00 79.01  ? 44  VAL G CB  1 
ATOM   7179 C  CG1 . VAL G  3  44  ? 10.092 3.072   30.391  1.00 79.37  ? 44  VAL G CG1 1 
ATOM   7180 C  CG2 . VAL G  3  44  ? 10.632 3.644   28.028  1.00 79.14  ? 44  VAL G CG2 1 
ATOM   7181 N  N   . PRO G  3  45  ? 6.415  4.888   30.287  1.00 82.72  ? 45  PRO G N   1 
ATOM   7182 C  CA  . PRO G  3  45  ? 5.668  5.564   31.356  1.00 83.51  ? 45  PRO G CA  1 
ATOM   7183 C  C   . PRO G  3  45  ? 6.148  5.254   32.770  1.00 84.30  ? 45  PRO G C   1 
ATOM   7184 O  O   . PRO G  3  45  ? 5.940  6.026   33.701  1.00 84.62  ? 45  PRO G O   1 
ATOM   7185 C  CB  . PRO G  3  45  ? 4.225  5.112   31.134  1.00 83.24  ? 45  PRO G CB  1 
ATOM   7186 C  CG  . PRO G  3  45  ? 4.238  4.362   29.785  1.00 83.10  ? 45  PRO G CG  1 
ATOM   7187 C  CD  . PRO G  3  45  ? 5.618  3.776   29.737  1.00 82.25  ? 45  PRO G CD  1 
ATOM   7188 N  N   . ASP G  3  46  ? 6.773  4.090   32.922  1.00 85.49  ? 46  ASP G N   1 
ATOM   7189 C  CA  . ASP G  3  46  ? 7.254  3.663   34.221  1.00 87.04  ? 46  ASP G CA  1 
ATOM   7190 C  C   . ASP G  3  46  ? 8.391  4.552   34.741  1.00 86.30  ? 46  ASP G C   1 
ATOM   7191 O  O   . ASP G  3  46  ? 8.504  4.807   35.940  1.00 85.59  ? 46  ASP G O   1 
ATOM   7192 C  CB  . ASP G  3  46  ? 7.749  2.214   34.126  1.00 89.49  ? 46  ASP G CB  1 
ATOM   7193 C  CG  . ASP G  3  46  ? 7.793  1.518   35.476  1.00 92.53  ? 46  ASP G CG  1 
ATOM   7194 O  OD1 . ASP G  3  46  ? 8.002  2.213   36.500  1.00 94.45  ? 46  ASP G OD1 1 
ATOM   7195 O  OD2 . ASP G  3  46  ? 7.631  0.279   35.521  1.00 93.24  ? 46  ASP G OD2 1 
ATOM   7196 N  N   . ALA G  3  47  ? 9.217  5.035   33.820  1.00 85.79  ? 47  ALA G N   1 
ATOM   7197 C  CA  . ALA G  3  47  ? 10.369 5.867   34.156  1.00 85.57  ? 47  ALA G CA  1 
ATOM   7198 C  C   . ALA G  3  47  ? 10.108 7.116   34.992  1.00 84.61  ? 47  ALA G C   1 
ATOM   7199 O  O   . ALA G  3  47  ? 10.887 7.445   35.895  1.00 84.12  ? 47  ALA G O   1 
ATOM   7200 C  CB  . ALA G  3  47  ? 11.092 6.259   32.879  1.00 86.42  ? 47  ALA G CB  1 
ATOM   7201 N  N   . VAL G  3  48  ? 9.020  7.810   34.684  1.00 83.77  ? 48  VAL G N   1 
ATOM   7202 C  CA  . VAL G  3  48  ? 8.673  9.040   35.386  1.00 83.86  ? 48  VAL G CA  1 
ATOM   7203 C  C   . VAL G  3  48  ? 8.747  8.911   36.902  1.00 84.68  ? 48  VAL G C   1 
ATOM   7204 O  O   . VAL G  3  48  ? 9.105  9.861   37.601  1.00 84.09  ? 48  VAL G O   1 
ATOM   7205 C  CB  . VAL G  3  48  ? 7.262  9.512   35.007  1.00 83.08  ? 48  VAL G CB  1 
ATOM   7206 C  CG1 . VAL G  3  48  ? 7.108  10.993  35.330  1.00 82.12  ? 48  VAL G CG1 1 
ATOM   7207 C  CG2 . VAL G  3  48  ? 7.008  9.245   33.532  1.00 83.61  ? 48  VAL G CG2 1 
ATOM   7208 N  N   . GLY G  3  49  ? 8.421  7.724   37.405  1.00 85.95  ? 49  GLY G N   1 
ATOM   7209 C  CA  . GLY G  3  49  ? 8.442  7.497   38.841  1.00 87.43  ? 49  GLY G CA  1 
ATOM   7210 C  C   . GLY G  3  49  ? 9.816  7.510   39.483  1.00 87.99  ? 49  GLY G C   1 
ATOM   7211 O  O   . GLY G  3  49  ? 9.936  7.773   40.679  1.00 87.98  ? 49  GLY G O   1 
ATOM   7212 N  N   . LEU G  3  50  ? 10.849 7.224   38.694  1.00 88.14  ? 50  LEU G N   1 
ATOM   7213 C  CA  . LEU G  3  50  ? 12.215 7.198   39.196  1.00 88.53  ? 50  LEU G CA  1 
ATOM   7214 C  C   . LEU G  3  50  ? 12.671 8.601   39.571  1.00 88.50  ? 50  LEU G C   1 
ATOM   7215 O  O   . LEU G  3  50  ? 13.632 8.775   40.322  1.00 87.91  ? 50  LEU G O   1 
ATOM   7216 C  CB  . LEU G  3  50  ? 13.144 6.642   38.118  1.00 88.89  ? 50  LEU G CB  1 
ATOM   7217 C  CG  . LEU G  3  50  ? 12.644 5.371   37.430  1.00 89.47  ? 50  LEU G CG  1 
ATOM   7218 C  CD1 . LEU G  3  50  ? 13.481 5.076   36.194  1.00 90.02  ? 50  LEU G CD1 1 
ATOM   7219 C  CD2 . LEU G  3  50  ? 12.705 4.209   38.393  1.00 89.44  ? 50  LEU G CD2 1 
ATOM   7220 N  N   . PHE G  3  51  ? 11.951 9.596   39.068  1.00 88.69  ? 51  PHE G N   1 
ATOM   7221 C  CA  . PHE G  3  51  ? 12.308 10.986  39.300  1.00 89.75  ? 51  PHE G CA  1 
ATOM   7222 C  C   . PHE G  3  51  ? 11.440 11.772  40.262  1.00 90.31  ? 51  PHE G C   1 
ATOM   7223 O  O   . PHE G  3  51  ? 11.296 12.982  40.107  1.00 90.95  ? 51  PHE G O   1 
ATOM   7224 C  CB  . PHE G  3  51  ? 12.350 11.708  37.959  1.00 89.46  ? 51  PHE G CB  1 
ATOM   7225 C  CG  . PHE G  3  51  ? 13.285 11.079  36.975  1.00 88.89  ? 51  PHE G CG  1 
ATOM   7226 C  CD1 . PHE G  3  51  ? 14.663 11.246  37.101  1.00 88.19  ? 51  PHE G CD1 1 
ATOM   7227 C  CD2 . PHE G  3  51  ? 12.797 10.274  35.953  1.00 88.52  ? 51  PHE G CD2 1 
ATOM   7228 C  CE1 . PHE G  3  51  ? 15.544 10.617  36.223  1.00 86.97  ? 51  PHE G CE1 1 
ATOM   7229 C  CE2 . PHE G  3  51  ? 13.672 9.639   35.069  1.00 88.44  ? 51  PHE G CE2 1 
ATOM   7230 C  CZ  . PHE G  3  51  ? 15.051 9.812   35.207  1.00 87.30  ? 51  PHE G CZ  1 
ATOM   7231 N  N   . ASP G  3  52  ? 10.876 11.114  41.263  1.00 91.19  ? 52  ASP G N   1 
ATOM   7232 C  CA  . ASP G  3  52  ? 10.034 11.842  42.198  1.00 92.29  ? 52  ASP G CA  1 
ATOM   7233 C  C   . ASP G  3  52  ? 10.824 12.939  42.908  1.00 92.21  ? 52  ASP G C   1 
ATOM   7234 O  O   . ASP G  3  52  ? 10.334 14.061  43.078  1.00 92.24  ? 52  ASP G O   1 
ATOM   7235 C  CB  . ASP G  3  52  ? 9.415  10.891  43.229  1.00 93.80  ? 52  ASP G CB  1 
ATOM   7236 C  CG  . ASP G  3  52  ? 8.497  9.859   42.595  1.00 95.68  ? 52  ASP G CG  1 
ATOM   7237 O  OD1 . ASP G  3  52  ? 7.860  10.174  41.562  1.00 95.84  ? 52  ASP G OD1 1 
ATOM   7238 O  OD2 . ASP G  3  52  ? 8.404  8.735   43.134  1.00 95.75  ? 52  ASP G OD2 1 
ATOM   7239 N  N   . ARG G  3  53  ? 12.059 12.628  43.290  1.00 91.53  ? 53  ARG G N   1 
ATOM   7240 C  CA  . ARG G  3  53  ? 12.882 13.596  44.006  1.00 90.98  ? 53  ARG G CA  1 
ATOM   7241 C  C   . ARG G  3  53  ? 13.105 14.902  43.262  1.00 90.75  ? 53  ARG G C   1 
ATOM   7242 O  O   . ARG G  3  53  ? 13.212 15.958  43.881  1.00 91.22  ? 53  ARG G O   1 
ATOM   7243 C  CB  . ARG G  3  53  ? 14.238 12.996  44.358  1.00 90.41  ? 53  ARG G CB  1 
ATOM   7244 C  CG  . ARG G  3  53  ? 14.975 13.812  45.401  1.00 90.22  ? 53  ARG G CG  1 
ATOM   7245 C  CD  . ARG G  3  53  ? 16.370 13.277  45.655  1.00 90.20  ? 53  ARG G CD  1 
ATOM   7246 N  NE  . ARG G  3  53  ? 17.333 13.797  44.690  1.00 89.24  ? 53  ARG G NE  1 
ATOM   7247 C  CZ  . ARG G  3  53  ? 17.673 15.081  44.594  1.00 89.39  ? 53  ARG G CZ  1 
ATOM   7248 N  NH1 . ARG G  3  53  ? 18.559 15.477  43.685  1.00 89.00  ? 53  ARG G NH1 1 
ATOM   7249 N  NH2 . ARG G  3  53  ? 17.131 15.971  45.415  1.00 89.69  ? 53  ARG G NH2 1 
ATOM   7250 N  N   . VAL G  3  54  ? 13.187 14.828  41.938  1.00 89.99  ? 54  VAL G N   1 
ATOM   7251 C  CA  . VAL G  3  54  ? 13.414 16.019  41.132  1.00 88.81  ? 54  VAL G CA  1 
ATOM   7252 C  C   . VAL G  3  54  ? 12.163 16.480  40.404  1.00 88.21  ? 54  VAL G C   1 
ATOM   7253 O  O   . VAL G  3  54  ? 12.246 17.235  39.436  1.00 89.20  ? 54  VAL G O   1 
ATOM   7254 C  CB  . VAL G  3  54  ? 14.529 15.784  40.095  1.00 88.67  ? 54  VAL G CB  1 
ATOM   7255 C  CG1 . VAL G  3  54  ? 15.863 15.610  40.804  1.00 87.20  ? 54  VAL G CG1 1 
ATOM   7256 C  CG2 . VAL G  3  54  ? 14.209 14.557  39.254  1.00 87.85  ? 54  VAL G CG2 1 
ATOM   7257 N  N   . HIS G  3  55  ? 11.006 16.026  40.875  1.00 86.46  ? 55  HIS G N   1 
ATOM   7258 C  CA  . HIS G  3  55  ? 9.718  16.393  40.284  1.00 84.73  ? 55  HIS G CA  1 
ATOM   7259 C  C   . HIS G  3  55  ? 9.568  16.031  38.800  1.00 84.40  ? 55  HIS G C   1 
ATOM   7260 O  O   . HIS G  3  55  ? 9.215  16.877  37.974  1.00 83.50  ? 55  HIS G O   1 
ATOM   7261 C  CB  . HIS G  3  55  ? 9.454  17.895  40.460  1.00 82.56  ? 55  HIS G CB  1 
ATOM   7262 C  CG  . HIS G  3  55  ? 9.483  18.357  41.886  1.00 81.31  ? 55  HIS G CG  1 
ATOM   7263 N  ND1 . HIS G  3  55  ? 8.951  19.566  42.285  1.00 81.43  ? 55  HIS G ND1 1 
ATOM   7264 C  CD2 . HIS G  3  55  ? 10.010 17.793  42.999  1.00 79.92  ? 55  HIS G CD2 1 
ATOM   7265 C  CE1 . HIS G  3  55  ? 9.150  19.724  43.581  1.00 80.05  ? 55  HIS G CE1 1 
ATOM   7266 N  NE2 . HIS G  3  55  ? 9.790  18.664  44.036  1.00 79.42  ? 55  HIS G NE2 1 
ATOM   7267 N  N   . GLY G  3  56  ? 9.812  14.764  38.475  1.00 84.20  ? 56  GLY G N   1 
ATOM   7268 C  CA  . GLY G  3  56  ? 9.694  14.309  37.100  1.00 85.37  ? 56  GLY G CA  1 
ATOM   7269 C  C   . GLY G  3  56  ? 8.304  14.459  36.506  1.00 86.71  ? 56  GLY G C   1 
ATOM   7270 O  O   . GLY G  3  56  ? 8.130  14.385  35.290  1.00 87.14  ? 56  GLY G O   1 
ATOM   7271 N  N   . THR G  3  57  ? 7.308  14.663  37.363  1.00 87.88  ? 57  THR G N   1 
ATOM   7272 C  CA  . THR G  3  57  ? 5.929  14.829  36.907  1.00 88.58  ? 57  THR G CA  1 
ATOM   7273 C  C   . THR G  3  57  ? 5.700  16.249  36.389  1.00 88.94  ? 57  THR G C   1 
ATOM   7274 O  O   . THR G  3  57  ? 4.776  16.498  35.623  1.00 89.33  ? 57  THR G O   1 
ATOM   7275 C  CB  . THR G  3  57  ? 4.937  14.539  38.049  1.00 87.79  ? 57  THR G CB  1 
ATOM   7276 O  OG1 . THR G  3  57  ? 5.318  15.284  39.214  1.00 88.40  ? 57  THR G OG1 1 
ATOM   7277 C  CG2 . THR G  3  57  ? 4.919  13.057  38.375  1.00 86.55  ? 57  THR G CG2 1 
ATOM   7278 N  N   . GLU G  3  58  ? 6.550  17.177  36.822  1.00 89.37  ? 58  GLU G N   1 
ATOM   7279 C  CA  . GLU G  3  58  ? 6.451  18.575  36.403  1.00 89.31  ? 58  GLU G CA  1 
ATOM   7280 C  C   . GLU G  3  58  ? 7.748  18.900  35.671  1.00 89.05  ? 58  GLU G C   1 
ATOM   7281 O  O   . GLU G  3  58  ? 8.726  19.333  36.280  1.00 88.49  ? 58  GLU G O   1 
ATOM   7282 C  CB  . GLU G  3  58  ? 6.288  19.475  37.624  1.00 89.95  ? 58  GLU G CB  1 
ATOM   7283 C  CG  . GLU G  3  58  ? 5.136  20.475  37.543  1.00 91.31  ? 58  GLU G CG  1 
ATOM   7284 C  CD  . GLU G  3  58  ? 5.450  21.691  36.690  1.00 91.26  ? 58  GLU G CD  1 
ATOM   7285 O  OE1 . GLU G  3  58  ? 5.431  21.592  35.445  1.00 89.13  ? 58  GLU G OE1 1 
ATOM   7286 O  OE2 . GLU G  3  58  ? 5.723  22.758  37.290  1.00 90.88  ? 58  GLU G OE2 1 
ATOM   7287 N  N   . ILE G  3  59  ? 7.740  18.682  34.360  1.00 88.65  ? 59  ILE G N   1 
ATOM   7288 C  CA  . ILE G  3  59  ? 8.905  18.908  33.518  1.00 88.08  ? 59  ILE G CA  1 
ATOM   7289 C  C   . ILE G  3  59  ? 9.429  20.332  33.531  1.00 87.02  ? 59  ILE G C   1 
ATOM   7290 O  O   . ILE G  3  59  ? 10.619 20.550  33.318  1.00 86.85  ? 59  ILE G O   1 
ATOM   7291 C  CB  . ILE G  3  59  ? 8.607  18.519  32.050  1.00 88.61  ? 59  ILE G CB  1 
ATOM   7292 C  CG1 . ILE G  3  59  ? 8.166  17.056  31.980  1.00 89.95  ? 59  ILE G CG1 1 
ATOM   7293 C  CG2 . ILE G  3  59  ? 9.848  18.707  31.192  1.00 88.61  ? 59  ILE G CG2 1 
ATOM   7294 C  CD1 . ILE G  3  59  ? 7.715  16.615  30.597  1.00 90.50  ? 59  ILE G CD1 1 
ATOM   7295 N  N   . ASP G  3  60  ? 8.557  21.298  33.790  1.00 85.80  ? 60  ASP G N   1 
ATOM   7296 C  CA  . ASP G  3  60  ? 8.980  22.693  33.788  1.00 85.41  ? 60  ASP G CA  1 
ATOM   7297 C  C   . ASP G  3  60  ? 9.220  23.317  35.170  1.00 83.56  ? 60  ASP G C   1 
ATOM   7298 O  O   . ASP G  3  60  ? 9.320  24.540  35.295  1.00 82.75  ? 60  ASP G O   1 
ATOM   7299 C  CB  . ASP G  3  60  ? 7.966  23.526  32.996  1.00 87.12  ? 60  ASP G CB  1 
ATOM   7300 C  CG  . ASP G  3  60  ? 8.615  24.659  32.229  1.00 89.37  ? 60  ASP G CG  1 
ATOM   7301 O  OD1 . ASP G  3  60  ? 8.830  25.747  32.815  1.00 90.44  ? 60  ASP G OD1 1 
ATOM   7302 O  OD2 . ASP G  3  60  ? 8.925  24.454  31.036  1.00 90.50  ? 60  ASP G OD2 1 
ATOM   7303 N  N   . SER G  3  61  ? 9.326  22.481  36.198  1.00 81.88  ? 61  SER G N   1 
ATOM   7304 C  CA  . SER G  3  61  ? 9.572  22.973  37.556  1.00 81.14  ? 61  SER G CA  1 
ATOM   7305 C  C   . SER G  3  61  ? 11.066 23.222  37.792  1.00 80.36  ? 61  SER G C   1 
ATOM   7306 O  O   . SER G  3  61  ? 11.917 22.525  37.235  1.00 80.32  ? 61  SER G O   1 
ATOM   7307 C  CB  . SER G  3  61  ? 9.068  21.966  38.589  1.00 81.01  ? 61  SER G CB  1 
ATOM   7308 O  OG  . SER G  3  61  ? 9.758  20.739  38.466  1.00 80.90  ? 61  SER G OG  1 
ATOM   7309 N  N   . SER G  3  62  ? 11.384 24.209  38.628  1.00 78.71  ? 62  SER G N   1 
ATOM   7310 C  CA  . SER G  3  62  ? 12.773 24.537  38.909  1.00 77.28  ? 62  SER G CA  1 
ATOM   7311 C  C   . SER G  3  62  ? 13.578 23.312  39.269  1.00 76.88  ? 62  SER G C   1 
ATOM   7312 O  O   . SER G  3  62  ? 14.674 23.113  38.756  1.00 77.70  ? 62  SER G O   1 
ATOM   7313 C  CB  . SER G  3  62  ? 12.869 25.555  40.042  1.00 76.78  ? 62  SER G CB  1 
ATOM   7314 O  OG  . SER G  3  62  ? 12.281 26.782  39.659  1.00 76.80  ? 62  SER G OG  1 
ATOM   7315 N  N   . GLU G  3  63  ? 13.032 22.483  40.149  1.00 76.68  ? 63  GLU G N   1 
ATOM   7316 C  CA  . GLU G  3  63  ? 13.730 21.278  40.574  1.00 76.34  ? 63  GLU G CA  1 
ATOM   7317 C  C   . GLU G  3  63  ? 14.058 20.316  39.433  1.00 75.95  ? 63  GLU G C   1 
ATOM   7318 O  O   . GLU G  3  63  ? 15.123 19.694  39.435  1.00 75.75  ? 63  GLU G O   1 
ATOM   7319 C  CB  . GLU G  3  63  ? 12.928 20.551  41.653  1.00 76.13  ? 63  GLU G CB  1 
ATOM   7320 C  CG  . GLU G  3  63  ? 11.440 20.858  41.647  1.00 78.30  ? 63  GLU G CG  1 
ATOM   7321 C  CD  . GLU G  3  63  ? 11.081 22.165  42.357  1.00 79.58  ? 63  GLU G CD  1 
ATOM   7322 O  OE1 . GLU G  3  63  ? 11.530 22.376  43.506  1.00 78.52  ? 63  GLU G OE1 1 
ATOM   7323 O  OE2 . GLU G  3  63  ? 10.334 22.979  41.770  1.00 80.34  ? 63  GLU G OE2 1 
ATOM   7324 N  N   . PHE G  3  64  ? 13.155 20.188  38.460  1.00 75.07  ? 64  PHE G N   1 
ATOM   7325 C  CA  . PHE G  3  64  ? 13.421 19.292  37.340  1.00 73.87  ? 64  PHE G CA  1 
ATOM   7326 C  C   . PHE G  3  64  ? 14.342 19.996  36.339  1.00 74.28  ? 64  PHE G C   1 
ATOM   7327 O  O   . PHE G  3  64  ? 15.210 19.361  35.727  1.00 74.42  ? 64  PHE G O   1 
ATOM   7328 C  CB  . PHE G  3  64  ? 12.121 18.864  36.648  1.00 71.84  ? 64  PHE G CB  1 
ATOM   7329 C  CG  . PHE G  3  64  ? 12.298 17.698  35.710  1.00 70.73  ? 64  PHE G CG  1 
ATOM   7330 C  CD1 . PHE G  3  64  ? 12.660 16.450  36.198  1.00 69.07  ? 64  PHE G CD1 1 
ATOM   7331 C  CD2 . PHE G  3  64  ? 12.140 17.853  34.332  1.00 71.55  ? 64  PHE G CD2 1 
ATOM   7332 C  CE1 . PHE G  3  64  ? 12.870 15.374  35.336  1.00 68.84  ? 64  PHE G CE1 1 
ATOM   7333 C  CE2 . PHE G  3  64  ? 12.350 16.775  33.458  1.00 69.79  ? 64  PHE G CE2 1 
ATOM   7334 C  CZ  . PHE G  3  64  ? 12.716 15.537  33.962  1.00 69.21  ? 64  PHE G CZ  1 
ATOM   7335 N  N   . LYS G  3  65  ? 14.157 21.299  36.166  1.00 73.67  ? 65  LYS G N   1 
ATOM   7336 C  CA  . LYS G  3  65  ? 15.016 22.037  35.251  1.00 73.45  ? 65  LYS G CA  1 
ATOM   7337 C  C   . LYS G  3  65  ? 16.465 21.796  35.683  1.00 71.77  ? 65  LYS G C   1 
ATOM   7338 O  O   . LYS G  3  65  ? 17.322 21.510  34.849  1.00 72.35  ? 65  LYS G O   1 
ATOM   7339 C  CB  . LYS G  3  65  ? 14.669 23.540  35.257  1.00 73.61  ? 65  LYS G CB  1 
ATOM   7340 C  CG  . LYS G  3  65  ? 13.500 23.887  34.334  1.00 74.59  ? 65  LYS G CG  1 
ATOM   7341 C  CD  . LYS G  3  65  ? 13.107 25.356  34.376  1.00 75.85  ? 65  LYS G CD  1 
ATOM   7342 C  CE  . LYS G  3  65  ? 12.095 25.661  33.282  1.00 76.43  ? 65  LYS G CE  1 
ATOM   7343 N  NZ  . LYS G  3  65  ? 11.581 27.058  33.350  1.00 76.60  ? 65  LYS G NZ  1 
ATOM   7344 N  N   . ALA G  3  66  ? 16.728 21.885  36.984  1.00 68.22  ? 66  ALA G N   1 
ATOM   7345 C  CA  . ALA G  3  66  ? 18.076 21.672  37.498  1.00 65.55  ? 66  ALA G CA  1 
ATOM   7346 C  C   . ALA G  3  66  ? 18.549 20.265  37.154  1.00 63.92  ? 66  ALA G C   1 
ATOM   7347 O  O   . ALA G  3  66  ? 19.688 20.065  36.727  1.00 63.99  ? 66  ALA G O   1 
ATOM   7348 C  CB  . ALA G  3  66  ? 18.104 21.892  39.011  1.00 65.52  ? 66  ALA G CB  1 
ATOM   7349 N  N   . HIS G  3  67  ? 17.681 19.282  37.329  1.00 62.10  ? 67  HIS G N   1 
ATOM   7350 C  CA  . HIS G  3  67  ? 18.074 17.919  37.015  1.00 61.06  ? 67  HIS G CA  1 
ATOM   7351 C  C   . HIS G  3  67  ? 18.437 17.817  35.540  1.00 62.62  ? 67  HIS G C   1 
ATOM   7352 O  O   . HIS G  3  67  ? 19.386 17.134  35.170  1.00 64.24  ? 67  HIS G O   1 
ATOM   7353 C  CB  . HIS G  3  67  ? 16.958 16.927  37.314  1.00 55.71  ? 67  HIS G CB  1 
ATOM   7354 C  CG  . HIS G  3  67  ? 17.243 15.553  36.793  1.00 50.29  ? 67  HIS G CG  1 
ATOM   7355 N  ND1 . HIS G  3  67  ? 18.263 14.770  37.289  1.00 47.54  ? 67  HIS G ND1 1 
ATOM   7356 C  CD2 . HIS G  3  67  ? 16.694 14.859  35.770  1.00 48.74  ? 67  HIS G CD2 1 
ATOM   7357 C  CE1 . HIS G  3  67  ? 18.326 13.649  36.591  1.00 46.87  ? 67  HIS G CE1 1 
ATOM   7358 N  NE2 . HIS G  3  67  ? 17.386 13.678  35.662  1.00 46.84  ? 67  HIS G NE2 1 
ATOM   7359 N  N   . CYS G  3  68  ? 17.668 18.487  34.690  1.00 62.91  ? 68  CYS G N   1 
ATOM   7360 C  CA  . CYS G  3  68  ? 17.946 18.457  33.261  1.00 62.47  ? 68  CYS G CA  1 
ATOM   7361 C  C   . CYS G  3  68  ? 19.338 19.018  32.962  1.00 61.17  ? 68  CYS G C   1 
ATOM   7362 O  O   . CYS G  3  68  ? 20.105 18.422  32.207  1.00 58.03  ? 68  CYS G O   1 
ATOM   7363 C  CB  . CYS G  3  68  ? 16.877 19.253  32.515  1.00 63.20  ? 68  CYS G CB  1 
ATOM   7364 S  SG  . CYS G  3  68  ? 15.391 18.288  32.145  1.00 67.91  ? 68  CYS G SG  1 
ATOM   7365 N  N   . ILE G  3  69  ? 19.651 20.158  33.574  1.00 61.26  ? 69  ILE G N   1 
ATOM   7366 C  CA  . ILE G  3  69  ? 20.938 20.813  33.392  1.00 60.77  ? 69  ILE G CA  1 
ATOM   7367 C  C   . ILE G  3  69  ? 22.059 19.908  33.877  1.00 61.78  ? 69  ILE G C   1 
ATOM   7368 O  O   . ILE G  3  69  ? 23.137 19.852  33.263  1.00 62.52  ? 69  ILE G O   1 
ATOM   7369 C  CB  . ILE G  3  69  ? 20.986 22.148  34.157  1.00 59.28  ? 69  ILE G CB  1 
ATOM   7370 C  CG1 . ILE G  3  69  ? 20.128 23.173  33.421  1.00 58.74  ? 69  ILE G CG1 1 
ATOM   7371 C  CG2 . ILE G  3  69  ? 22.429 22.642  34.309  1.00 59.02  ? 69  ILE G CG2 1 
ATOM   7372 C  CD1 . ILE G  3  69  ? 20.069 24.520  34.101  1.00 60.11  ? 69  ILE G CD1 1 
ATOM   7373 N  N   . ARG G  3  70  ? 21.792 19.194  34.971  1.00 61.50  ? 70  ARG G N   1 
ATOM   7374 C  CA  . ARG G  3  70  ? 22.775 18.272  35.543  1.00 61.51  ? 70  ARG G CA  1 
ATOM   7375 C  C   . ARG G  3  70  ? 23.047 17.096  34.602  1.00 60.42  ? 70  ARG G C   1 
ATOM   7376 O  O   . ARG G  3  70  ? 24.182 16.609  34.492  1.00 60.75  ? 70  ARG G O   1 
ATOM   7377 C  CB  . ARG G  3  70  ? 22.314 17.757  36.921  1.00 62.31  ? 70  ARG G CB  1 
ATOM   7378 C  CG  . ARG G  3  70  ? 22.578 18.730  38.086  1.00 62.53  ? 70  ARG G CG  1 
ATOM   7379 C  CD  . ARG G  3  70  ? 22.485 18.066  39.477  1.00 60.56  ? 70  ARG G CD  1 
ATOM   7380 N  NE  . ARG G  3  70  ? 21.148 17.580  39.818  1.00 59.13  ? 70  ARG G NE  1 
ATOM   7381 C  CZ  . ARG G  3  70  ? 20.115 18.351  40.163  1.00 59.19  ? 70  ARG G CZ  1 
ATOM   7382 N  NH1 . ARG G  3  70  ? 20.233 19.672  40.228  1.00 56.76  ? 70  ARG G NH1 1 
ATOM   7383 N  NH2 . ARG G  3  70  ? 18.943 17.788  40.433  1.00 60.73  ? 70  ARG G NH2 1 
ATOM   7384 N  N   . VAL G  3  71  ? 22.004 16.640  33.922  1.00 59.11  ? 71  VAL G N   1 
ATOM   7385 C  CA  . VAL G  3  71  ? 22.146 15.534  32.990  1.00 58.58  ? 71  VAL G CA  1 
ATOM   7386 C  C   . VAL G  3  71  ? 23.000 15.947  31.785  1.00 58.39  ? 71  VAL G C   1 
ATOM   7387 O  O   . VAL G  3  71  ? 24.037 15.317  31.515  1.00 57.40  ? 71  VAL G O   1 
ATOM   7388 C  CB  . VAL G  3  71  ? 20.758 15.016  32.505  1.00 60.22  ? 71  VAL G CB  1 
ATOM   7389 C  CG1 . VAL G  3  71  ? 20.939 13.896  31.476  1.00 57.56  ? 71  VAL G CG1 1 
ATOM   7390 C  CG2 . VAL G  3  71  ? 19.958 14.491  33.685  1.00 62.06  ? 71  VAL G CG2 1 
ATOM   7391 N  N   . VAL G  3  72  ? 22.586 17.004  31.070  1.00 56.45  ? 72  VAL G N   1 
ATOM   7392 C  CA  . VAL G  3  72  ? 23.363 17.423  29.906  1.00 54.76  ? 72  VAL G CA  1 
ATOM   7393 C  C   . VAL G  3  72  ? 24.795 17.767  30.294  1.00 53.16  ? 72  VAL G C   1 
ATOM   7394 O  O   . VAL G  3  72  ? 25.726 17.468  29.535  1.00 53.28  ? 72  VAL G O   1 
ATOM   7395 C  CB  . VAL G  3  72  ? 22.712 18.612  29.105  1.00 54.44  ? 72  VAL G CB  1 
ATOM   7396 C  CG1 . VAL G  3  72  ? 21.440 18.142  28.453  1.00 52.85  ? 72  VAL G CG1 1 
ATOM   7397 C  CG2 . VAL G  3  72  ? 22.436 19.792  29.997  1.00 54.99  ? 72  VAL G CG2 1 
ATOM   7398 N  N   . ASN G  3  73  ? 24.979 18.370  31.472  1.00 48.94  ? 73  ASN G N   1 
ATOM   7399 C  CA  . ASN G  3  73  ? 26.325 18.703  31.927  1.00 47.35  ? 73  ASN G CA  1 
ATOM   7400 C  C   . ASN G  3  73  ? 27.108 17.410  32.039  1.00 47.23  ? 73  ASN G C   1 
ATOM   7401 O  O   . ASN G  3  73  ? 28.324 17.376  31.834  1.00 46.75  ? 73  ASN G O   1 
ATOM   7402 C  CB  . ASN G  3  73  ? 26.297 19.384  33.300  1.00 48.84  ? 73  ASN G CB  1 
ATOM   7403 C  CG  . ASN G  3  73  ? 27.706 19.591  33.892  1.00 51.54  ? 73  ASN G CG  1 
ATOM   7404 O  OD1 . ASN G  3  73  ? 28.439 20.498  33.488  1.00 53.38  ? 73  ASN G OD1 1 
ATOM   7405 N  ND2 . ASN G  3  73  ? 28.088 18.740  34.844  1.00 51.77  ? 73  ASN G ND2 1 
ATOM   7406 N  N   . GLY G  3  74  ? 26.392 16.336  32.368  1.00 46.41  ? 74  GLY G N   1 
ATOM   7407 C  CA  . GLY G  3  74  ? 27.029 15.045  32.534  1.00 45.58  ? 74  GLY G CA  1 
ATOM   7408 C  C   . GLY G  3  74  ? 27.415 14.410  31.225  1.00 44.37  ? 74  GLY G C   1 
ATOM   7409 O  O   . GLY G  3  74  ? 28.466 13.787  31.109  1.00 42.75  ? 74  GLY G O   1 
ATOM   7410 N  N   . LEU G  3  75  ? 26.540 14.549  30.240  1.00 44.77  ? 75  LEU G N   1 
ATOM   7411 C  CA  . LEU G  3  75  ? 26.783 13.990  28.920  1.00 45.51  ? 75  LEU G CA  1 
ATOM   7412 C  C   . LEU G  3  75  ? 27.866 14.840  28.263  1.00 46.25  ? 75  LEU G C   1 
ATOM   7413 O  O   . LEU G  3  75  ? 28.734 14.314  27.569  1.00 44.56  ? 75  LEU G O   1 
ATOM   7414 C  CB  . LEU G  3  75  ? 25.495 14.022  28.086  1.00 43.43  ? 75  LEU G CB  1 
ATOM   7415 C  CG  . LEU G  3  75  ? 25.630 13.634  26.609  1.00 45.21  ? 75  LEU G CG  1 
ATOM   7416 C  CD1 . LEU G  3  75  ? 26.201 12.245  26.480  1.00 43.92  ? 75  LEU G CD1 1 
ATOM   7417 C  CD2 . LEU G  3  75  ? 24.269 13.720  25.917  1.00 46.16  ? 75  LEU G CD2 1 
ATOM   7418 N  N   . ASP G  3  76  ? 27.800 16.154  28.495  1.00 47.00  ? 76  ASP G N   1 
ATOM   7419 C  CA  . ASP G  3  76  ? 28.787 17.075  27.943  1.00 47.86  ? 76  ASP G CA  1 
ATOM   7420 C  C   . ASP G  3  76  ? 30.171 16.698  28.430  1.00 48.81  ? 76  ASP G C   1 
ATOM   7421 O  O   . ASP G  3  76  ? 31.103 16.658  27.646  1.00 49.81  ? 76  ASP G O   1 
ATOM   7422 C  CB  . ASP G  3  76  ? 28.489 18.521  28.351  1.00 47.09  ? 76  ASP G CB  1 
ATOM   7423 C  CG  . ASP G  3  76  ? 29.560 19.492  27.879  1.00 47.31  ? 76  ASP G CG  1 
ATOM   7424 O  OD1 . ASP G  3  76  ? 30.354 19.968  28.713  1.00 45.97  ? 76  ASP G OD1 1 
ATOM   7425 O  OD2 . ASP G  3  76  ? 29.619 19.775  26.665  1.00 51.59  ? 76  ASP G OD2 1 
ATOM   7426 N  N   . SER G  3  77  ? 30.309 16.421  29.720  1.00 50.60  ? 77  SER G N   1 
ATOM   7427 C  CA  . SER G  3  77  ? 31.602 16.045  30.267  1.00 52.09  ? 77  SER G CA  1 
ATOM   7428 C  C   . SER G  3  77  ? 32.057 14.741  29.634  1.00 52.24  ? 77  SER G C   1 
ATOM   7429 O  O   . SER G  3  77  ? 33.249 14.531  29.426  1.00 54.31  ? 77  SER G O   1 
ATOM   7430 C  CB  . SER G  3  77  ? 31.535 15.892  31.792  1.00 53.71  ? 77  SER G CB  1 
ATOM   7431 O  OG  . SER G  3  77  ? 30.867 14.698  32.189  1.00 55.86  ? 77  SER G OG  1 
ATOM   7432 N  N   . ALA G  3  78  ? 31.112 13.866  29.312  1.00 50.48  ? 78  ALA G N   1 
ATOM   7433 C  CA  . ALA G  3  78  ? 31.469 12.587  28.712  1.00 49.63  ? 78  ALA G CA  1 
ATOM   7434 C  C   . ALA G  3  78  ? 31.863 12.751  27.252  1.00 48.47  ? 78  ALA G C   1 
ATOM   7435 O  O   . ALA G  3  78  ? 32.853 12.172  26.793  1.00 49.92  ? 78  ALA G O   1 
ATOM   7436 C  CB  . ALA G  3  78  ? 30.303 11.596  28.836  1.00 49.14  ? 78  ALA G CB  1 
ATOM   7437 N  N   . ILE G  3  79  ? 31.092 13.530  26.512  1.00 45.97  ? 79  ILE G N   1 
ATOM   7438 C  CA  . ILE G  3  79  ? 31.422 13.719  25.118  1.00 45.99  ? 79  ILE G CA  1 
ATOM   7439 C  C   . ILE G  3  79  ? 32.762 14.425  25.047  1.00 45.69  ? 79  ILE G C   1 
ATOM   7440 O  O   . ILE G  3  79  ? 33.583 14.112  24.191  1.00 47.36  ? 79  ILE G O   1 
ATOM   7441 C  CB  . ILE G  3  79  ? 30.336 14.513  24.400  1.00 45.43  ? 79  ILE G CB  1 
ATOM   7442 C  CG1 . ILE G  3  79  ? 29.065 13.663  24.341  1.00 43.74  ? 79  ILE G CG1 1 
ATOM   7443 C  CG2 . ILE G  3  79  ? 30.792 14.886  23.004  1.00 45.56  ? 79  ILE G CG2 1 
ATOM   7444 C  CD1 . ILE G  3  79  ? 27.897 14.370  23.742  1.00 45.41  ? 79  ILE G CD1 1 
ATOM   7445 N  N   . GLY G  3  80  ? 32.992 15.342  25.973  1.00 44.67  ? 80  GLY G N   1 
ATOM   7446 C  CA  . GLY G  3  80  ? 34.248 16.055  26.000  1.00 43.90  ? 80  GLY G CA  1 
ATOM   7447 C  C   . GLY G  3  80  ? 35.380 15.080  26.216  1.00 44.71  ? 80  GLY G C   1 
ATOM   7448 O  O   . GLY G  3  80  ? 36.328 15.053  25.424  1.00 46.49  ? 80  GLY G O   1 
ATOM   7449 N  N   . LEU G  3  81  ? 35.267 14.251  27.257  1.00 43.88  ? 81  LEU G N   1 
ATOM   7450 C  CA  . LEU G  3  81  ? 36.313 13.278  27.589  1.00 42.66  ? 81  LEU G CA  1 
ATOM   7451 C  C   . LEU G  3  81  ? 36.504 12.110  26.608  1.00 43.90  ? 81  LEU G C   1 
ATOM   7452 O  O   . LEU G  3  81  ? 37.317 11.229  26.857  1.00 45.93  ? 81  LEU G O   1 
ATOM   7453 C  CB  . LEU G  3  81  ? 36.116 12.746  29.014  1.00 38.66  ? 81  LEU G CB  1 
ATOM   7454 C  CG  . LEU G  3  81  ? 36.361 13.785  30.107  1.00 37.24  ? 81  LEU G CG  1 
ATOM   7455 C  CD1 . LEU G  3  81  ? 36.020 13.184  31.459  1.00 37.10  ? 81  LEU G CD1 1 
ATOM   7456 C  CD2 . LEU G  3  81  ? 37.798 14.245  30.070  1.00 31.71  ? 81  LEU G CD2 1 
ATOM   7457 N  N   . LEU G  3  82  ? 35.776 12.083  25.495  1.00 43.51  ? 82  LEU G N   1 
ATOM   7458 C  CA  . LEU G  3  82  ? 35.996 11.007  24.536  1.00 42.08  ? 82  LEU G CA  1 
ATOM   7459 C  C   . LEU G  3  82  ? 37.418 11.167  23.998  1.00 42.30  ? 82  LEU G C   1 
ATOM   7460 O  O   . LEU G  3  82  ? 38.011 10.211  23.532  1.00 40.10  ? 82  LEU G O   1 
ATOM   7461 C  CB  . LEU G  3  82  ? 35.004 11.090  23.387  1.00 42.37  ? 82  LEU G CB  1 
ATOM   7462 C  CG  . LEU G  3  82  ? 33.545 10.700  23.646  1.00 43.04  ? 82  LEU G CG  1 
ATOM   7463 C  CD1 . LEU G  3  82  ? 32.703 11.086  22.465  1.00 43.50  ? 82  LEU G CD1 1 
ATOM   7464 C  CD2 . LEU G  3  82  ? 33.448 9.208   23.862  1.00 42.92  ? 82  LEU G CD2 1 
ATOM   7465 N  N   . SER G  3  83  ? 37.953 12.383  24.081  1.00 43.97  ? 83  SER G N   1 
ATOM   7466 C  CA  . SER G  3  83  ? 39.303 12.694  23.611  1.00 46.43  ? 83  SER G CA  1 
ATOM   7467 C  C   . SER G  3  83  ? 40.381 12.084  24.506  1.00 47.71  ? 83  SER G C   1 
ATOM   7468 O  O   . SER G  3  83  ? 41.481 11.788  24.050  1.00 47.35  ? 83  SER G O   1 
ATOM   7469 C  CB  . SER G  3  83  ? 39.531 14.212  23.558  1.00 46.29  ? 83  SER G CB  1 
ATOM   7470 O  OG  . SER G  3  83  ? 38.675 14.850  22.639  1.00 50.02  ? 83  SER G OG  1 
ATOM   7471 N  N   . ASP G  3  84  ? 40.076 11.931  25.786  1.00 50.55  ? 84  ASP G N   1 
ATOM   7472 C  CA  . ASP G  3  84  ? 41.023 11.349  26.728  1.00 53.29  ? 84  ASP G CA  1 
ATOM   7473 C  C   . ASP G  3  84  ? 40.334 10.209  27.477  1.00 52.59  ? 84  ASP G C   1 
ATOM   7474 O  O   . ASP G  3  84  ? 39.855 10.377  28.598  1.00 52.85  ? 84  ASP G O   1 
ATOM   7475 C  CB  . ASP G  3  84  ? 41.515 12.416  27.710  1.00 57.71  ? 84  ASP G CB  1 
ATOM   7476 C  CG  . ASP G  3  84  ? 42.499 11.866  28.712  1.00 62.31  ? 84  ASP G CG  1 
ATOM   7477 O  OD1 . ASP G  3  84  ? 43.508 11.262  28.299  1.00 64.17  ? 84  ASP G OD1 1 
ATOM   7478 O  OD2 . ASP G  3  84  ? 42.264 12.035  29.925  1.00 65.36  ? 84  ASP G OD2 1 
ATOM   7479 N  N   . PRO G  3  85  ? 40.257 9.033   26.848  1.00 52.32  ? 85  PRO G N   1 
ATOM   7480 C  CA  . PRO G  3  85  ? 39.621 7.847   27.436  1.00 52.95  ? 85  PRO G CA  1 
ATOM   7481 C  C   . PRO G  3  85  ? 40.031 7.482   28.875  1.00 52.53  ? 85  PRO G C   1 
ATOM   7482 O  O   . PRO G  3  85  ? 39.185 7.104   29.672  1.00 51.80  ? 85  PRO G O   1 
ATOM   7483 C  CB  . PRO G  3  85  ? 39.959 6.750   26.428  1.00 52.47  ? 85  PRO G CB  1 
ATOM   7484 C  CG  . PRO G  3  85  ? 39.957 7.501   25.120  1.00 52.20  ? 85  PRO G CG  1 
ATOM   7485 C  CD  . PRO G  3  85  ? 40.718 8.756   25.474  1.00 52.05  ? 85  PRO G CD  1 
ATOM   7486 N  N   . SER G  3  86  ? 41.313 7.589   29.211  1.00 52.95  ? 86  SER G N   1 
ATOM   7487 C  CA  . SER G  3  86  ? 41.756 7.253   30.567  1.00 51.87  ? 86  SER G CA  1 
ATOM   7488 C  C   . SER G  3  86  ? 40.874 7.978   31.569  1.00 51.17  ? 86  SER G C   1 
ATOM   7489 O  O   . SER G  3  86  ? 40.280 7.346   32.447  1.00 52.28  ? 86  SER G O   1 
ATOM   7490 C  CB  . SER G  3  86  ? 43.217 7.654   30.791  1.00 51.44  ? 86  SER G CB  1 
ATOM   7491 O  OG  . SER G  3  86  ? 43.358 9.060   30.917  1.00 55.68  ? 86  SER G OG  1 
ATOM   7492 N  N   . THR G  3  87  ? 40.788 9.302   31.423  1.00 49.80  ? 87  THR G N   1 
ATOM   7493 C  CA  . THR G  3  87  ? 39.973 10.141  32.303  1.00 49.68  ? 87  THR G CA  1 
ATOM   7494 C  C   . THR G  3  87  ? 38.488 9.862   32.142  1.00 48.60  ? 87  THR G C   1 
ATOM   7495 O  O   . THR G  3  87  ? 37.737 9.995   33.095  1.00 47.95  ? 87  THR G O   1 
ATOM   7496 C  CB  . THR G  3  87  ? 40.195 11.640  32.036  1.00 50.05  ? 87  THR G CB  1 
ATOM   7497 O  OG1 . THR G  3  87  ? 41.571 11.967  32.268  1.00 49.51  ? 87  THR G OG1 1 
ATOM   7498 C  CG2 . THR G  3  87  ? 39.333 12.478  32.960  1.00 49.40  ? 87  THR G CG2 1 
ATOM   7499 N  N   . LEU G  3  88  ? 38.073 9.490   30.933  1.00 49.51  ? 88  LEU G N   1 
ATOM   7500 C  CA  . LEU G  3  88  ? 36.670 9.192   30.649  1.00 49.47  ? 88  LEU G CA  1 
ATOM   7501 C  C   . LEU G  3  88  ? 36.205 8.059   31.540  1.00 50.56  ? 88  LEU G C   1 
ATOM   7502 O  O   . LEU G  3  88  ? 35.175 8.141   32.219  1.00 51.06  ? 88  LEU G O   1 
ATOM   7503 C  CB  . LEU G  3  88  ? 36.489 8.767   29.191  1.00 47.20  ? 88  LEU G CB  1 
ATOM   7504 C  CG  . LEU G  3  88  ? 35.088 8.253   28.794  1.00 45.06  ? 88  LEU G CG  1 
ATOM   7505 C  CD1 . LEU G  3  88  ? 34.088 9.390   29.000  1.00 41.72  ? 88  LEU G CD1 1 
ATOM   7506 C  CD2 . LEU G  3  88  ? 35.067 7.763   27.318  1.00 40.74  ? 88  LEU G CD2 1 
ATOM   7507 N  N   . ASN G  3  89  ? 36.984 6.988   31.531  1.00 52.27  ? 89  ASN G N   1 
ATOM   7508 C  CA  . ASN G  3  89  ? 36.657 5.821   32.320  1.00 52.94  ? 89  ASN G CA  1 
ATOM   7509 C  C   . ASN G  3  89  ? 36.388 6.184   33.773  1.00 52.38  ? 89  ASN G C   1 
ATOM   7510 O  O   . ASN G  3  89  ? 35.443 5.682   34.362  1.00 53.16  ? 89  ASN G O   1 
ATOM   7511 C  CB  . ASN G  3  89  ? 37.767 4.779   32.189  1.00 53.67  ? 89  ASN G CB  1 
ATOM   7512 C  CG  . ASN G  3  89  ? 37.789 4.129   30.812  1.00 55.21  ? 89  ASN G CG  1 
ATOM   7513 O  OD1 . ASN G  3  89  ? 36.740 3.916   30.195  1.00 56.47  ? 89  ASN G OD1 1 
ATOM   7514 N  ND2 . ASN G  3  89  ? 38.987 3.790   30.332  1.00 55.12  ? 89  ASN G ND2 1 
ATOM   7515 N  N   . GLU G  3  90  ? 37.193 7.073   34.346  1.00 52.88  ? 90  GLU G N   1 
ATOM   7516 C  CA  . GLU G  3  90  ? 36.974 7.485   35.736  1.00 54.71  ? 90  GLU G CA  1 
ATOM   7517 C  C   . GLU G  3  90  ? 35.635 8.223   35.901  1.00 55.26  ? 90  GLU G C   1 
ATOM   7518 O  O   . GLU G  3  90  ? 34.858 7.933   36.823  1.00 57.26  ? 90  GLU G O   1 
ATOM   7519 C  CB  . GLU G  3  90  ? 38.127 8.373   36.224  1.00 52.17  ? 90  GLU G CB  1 
ATOM   7520 C  CG  . GLU G  3  90  ? 39.445 7.630   36.361  1.00 53.91  ? 90  GLU G CG  1 
ATOM   7521 C  CD  . GLU G  3  90  ? 39.315 6.362   37.201  1.00 56.89  ? 90  GLU G CD  1 
ATOM   7522 O  OE1 . GLU G  3  90  ? 39.065 6.481   38.417  1.00 59.48  ? 90  GLU G OE1 1 
ATOM   7523 O  OE2 . GLU G  3  90  ? 39.453 5.251   36.643  1.00 57.65  ? 90  GLU G OE2 1 
ATOM   7524 N  N   . GLN G  3  91  ? 35.371 9.163   34.998  1.00 54.23  ? 91  GLN G N   1 
ATOM   7525 C  CA  . GLN G  3  91  ? 34.143 9.944   35.015  1.00 52.74  ? 91  GLN G CA  1 
ATOM   7526 C  C   . GLN G  3  91  ? 32.899 9.087   34.834  1.00 53.18  ? 91  GLN G C   1 
ATOM   7527 O  O   . GLN G  3  91  ? 31.874 9.353   35.457  1.00 53.05  ? 91  GLN G O   1 
ATOM   7528 C  CB  . GLN G  3  91  ? 34.194 11.008  33.915  1.00 51.92  ? 91  GLN G CB  1 
ATOM   7529 C  CG  . GLN G  3  91  ? 32.928 11.815  33.749  1.00 48.99  ? 91  GLN G CG  1 
ATOM   7530 C  CD  . GLN G  3  91  ? 32.644 12.694  34.945  1.00 51.48  ? 91  GLN G CD  1 
ATOM   7531 O  OE1 . GLN G  3  91  ? 33.496 12.875  35.821  1.00 51.56  ? 91  GLN G OE1 1 
ATOM   7532 N  NE2 . GLN G  3  91  ? 31.447 13.266  34.981  1.00 48.50  ? 91  GLN G NE2 1 
ATOM   7533 N  N   . LEU G  3  92  ? 32.978 8.068   33.980  1.00 53.46  ? 92  LEU G N   1 
ATOM   7534 C  CA  . LEU G  3  92  ? 31.828 7.195   33.743  1.00 56.22  ? 92  LEU G CA  1 
ATOM   7535 C  C   . LEU G  3  92  ? 31.589 6.298   34.957  1.00 57.16  ? 92  LEU G C   1 
ATOM   7536 O  O   . LEU G  3  92  ? 30.450 5.951   35.277  1.00 57.54  ? 92  LEU G O   1 
ATOM   7537 C  CB  . LEU G  3  92  ? 32.058 6.329   32.503  1.00 54.88  ? 92  LEU G CB  1 
ATOM   7538 C  CG  . LEU G  3  92  ? 32.201 7.083   31.179  1.00 55.63  ? 92  LEU G CG  1 
ATOM   7539 C  CD1 . LEU G  3  92  ? 32.338 6.094   30.033  1.00 53.16  ? 92  LEU G CD1 1 
ATOM   7540 C  CD2 . LEU G  3  92  ? 30.992 7.985   30.966  1.00 55.17  ? 92  LEU G CD2 1 
ATOM   7541 N  N   . SER G  3  93  ? 32.674 5.928   35.631  1.00 56.84  ? 93  SER G N   1 
ATOM   7542 C  CA  . SER G  3  93  ? 32.571 5.103   36.819  1.00 56.24  ? 93  SER G CA  1 
ATOM   7543 C  C   . SER G  3  93  ? 31.783 5.891   37.837  1.00 55.39  ? 93  SER G C   1 
ATOM   7544 O  O   . SER G  3  93  ? 30.811 5.410   38.414  1.00 56.32  ? 93  SER G O   1 
ATOM   7545 C  CB  . SER G  3  93  ? 33.958 4.801   37.375  1.00 55.60  ? 93  SER G CB  1 
ATOM   7546 O  OG  . SER G  3  93  ? 34.584 3.790   36.614  1.00 55.86  ? 93  SER G OG  1 
ATOM   7547 N  N   . HIS G  3  94  ? 32.209 7.124   38.047  1.00 54.74  ? 94  HIS G N   1 
ATOM   7548 C  CA  . HIS G  3  94  ? 31.532 7.975   38.995  1.00 54.70  ? 94  HIS G CA  1 
ATOM   7549 C  C   . HIS G  3  94  ? 30.052 8.122   38.644  1.00 57.12  ? 94  HIS G C   1 
ATOM   7550 O  O   . HIS G  3  94  ? 29.200 8.152   39.527  1.00 59.37  ? 94  HIS G O   1 
ATOM   7551 C  CB  . HIS G  3  94  ? 32.188 9.337   39.015  1.00 52.38  ? 94  HIS G CB  1 
ATOM   7552 C  CG  . HIS G  3  94  ? 31.605 10.258  40.032  1.00 48.66  ? 94  HIS G CG  1 
ATOM   7553 N  ND1 . HIS G  3  94  ? 32.165 10.433  41.276  1.00 48.33  ? 94  HIS G ND1 1 
ATOM   7554 C  CD2 . HIS G  3  94  ? 30.498 11.035  40.000  1.00 47.85  ? 94  HIS G CD2 1 
ATOM   7555 C  CE1 . HIS G  3  94  ? 31.423 11.280  41.968  1.00 49.57  ? 94  HIS G CE1 1 
ATOM   7556 N  NE2 . HIS G  3  94  ? 30.407 11.660  41.215  1.00 47.69  ? 94  HIS G NE2 1 
ATOM   7557 N  N   . LEU G  3  95  ? 29.743 8.225   37.356  1.00 59.61  ? 95  LEU G N   1 
ATOM   7558 C  CA  . LEU G  3  95  ? 28.357 8.371   36.914  1.00 61.57  ? 95  LEU G CA  1 
ATOM   7559 C  C   . LEU G  3  95  ? 27.587 7.083   37.125  1.00 63.00  ? 95  LEU G C   1 
ATOM   7560 O  O   . LEU G  3  95  ? 26.375 7.107   37.378  1.00 62.62  ? 95  LEU G O   1 
ATOM   7561 C  CB  . LEU G  3  95  ? 28.293 8.751   35.436  1.00 61.06  ? 95  LEU G CB  1 
ATOM   7562 C  CG  . LEU G  3  95  ? 28.487 10.237  35.119  1.00 60.40  ? 95  LEU G CG  1 
ATOM   7563 C  CD1 . LEU G  3  95  ? 28.670 10.392  33.620  1.00 58.48  ? 95  LEU G CD1 1 
ATOM   7564 C  CD2 . LEU G  3  95  ? 27.285 11.043  35.610  1.00 59.42  ? 95  LEU G CD2 1 
ATOM   7565 N  N   . ALA G  3  96  ? 28.298 5.963   37.019  1.00 63.88  ? 96  ALA G N   1 
ATOM   7566 C  CA  . ALA G  3  96  ? 27.697 4.649   37.204  1.00 64.56  ? 96  ALA G CA  1 
ATOM   7567 C  C   . ALA G  3  96  ? 27.264 4.502   38.662  1.00 65.39  ? 96  ALA G C   1 
ATOM   7568 O  O   . ALA G  3  96  ? 26.122 4.143   38.938  1.00 65.33  ? 96  ALA G O   1 
ATOM   7569 C  CB  . ALA G  3  96  ? 28.695 3.561   36.826  1.00 63.14  ? 96  ALA G CB  1 
ATOM   7570 N  N   . THR G  3  97  ? 28.160 4.812   39.595  1.00 65.70  ? 97  THR G N   1 
ATOM   7571 C  CA  . THR G  3  97  ? 27.808 4.693   40.998  1.00 67.49  ? 97  THR G CA  1 
ATOM   7572 C  C   . THR G  3  97  ? 26.680 5.666   41.369  1.00 70.05  ? 97  THR G C   1 
ATOM   7573 O  O   . THR G  3  97  ? 25.891 5.399   42.286  1.00 70.75  ? 97  THR G O   1 
ATOM   7574 C  CB  . THR G  3  97  ? 29.036 4.928   41.914  1.00 66.21  ? 97  THR G CB  1 
ATOM   7575 O  OG1 . THR G  3  97  ? 29.241 6.332   42.108  1.00 64.79  ? 97  THR G OG1 1 
ATOM   7576 C  CG2 . THR G  3  97  ? 30.289 4.303   41.288  1.00 64.03  ? 97  THR G CG2 1 
ATOM   7577 N  N   . GLN G  3  98  ? 26.593 6.787   40.659  1.00 71.53  ? 98  GLN G N   1 
ATOM   7578 C  CA  . GLN G  3  98  ? 25.546 7.757   40.936  1.00 73.34  ? 98  GLN G CA  1 
ATOM   7579 C  C   . GLN G  3  98  ? 24.186 7.209   40.499  1.00 75.02  ? 98  GLN G C   1 
ATOM   7580 O  O   . GLN G  3  98  ? 23.150 7.571   41.064  1.00 73.39  ? 98  GLN G O   1 
ATOM   7581 C  CB  . GLN G  3  98  ? 25.839 9.075   40.222  1.00 73.44  ? 98  GLN G CB  1 
ATOM   7582 C  CG  . GLN G  3  98  ? 26.974 9.876   40.822  1.00 75.16  ? 98  GLN G CG  1 
ATOM   7583 C  CD  . GLN G  3  98  ? 27.075 11.276  40.229  1.00 76.98  ? 98  GLN G CD  1 
ATOM   7584 O  OE1 . GLN G  3  98  ? 27.187 11.433  39.013  1.00 80.12  ? 98  GLN G OE1 1 
ATOM   7585 N  NE2 . GLN G  3  98  ? 27.038 12.296  41.082  1.00 76.05  ? 98  GLN G NE2 1 
ATOM   7586 N  N   . HIS G  3  99  ? 24.192 6.331   39.500  1.00 77.34  ? 99  HIS G N   1 
ATOM   7587 C  CA  . HIS G  3  99  ? 22.957 5.742   39.002  1.00 81.22  ? 99  HIS G CA  1 
ATOM   7588 C  C   . HIS G  3  99  ? 22.668 4.409   39.677  1.00 84.54  ? 99  HIS G C   1 
ATOM   7589 O  O   . HIS G  3  99  ? 21.570 3.858   39.554  1.00 85.62  ? 99  HIS G O   1 
ATOM   7590 C  CB  . HIS G  3  99  ? 23.036 5.554   37.488  1.00 79.81  ? 99  HIS G CB  1 
ATOM   7591 C  CG  . HIS G  3  99  ? 22.834 6.822   36.717  1.00 79.79  ? 99  HIS G CG  1 
ATOM   7592 N  ND1 . HIS G  3  99  ? 23.712 7.882   36.786  1.00 78.76  ? 99  HIS G ND1 1 
ATOM   7593 C  CD2 . HIS G  3  99  ? 21.836 7.210   35.887  1.00 78.76  ? 99  HIS G CD2 1 
ATOM   7594 C  CE1 . HIS G  3  99  ? 23.263 8.868   36.033  1.00 77.32  ? 99  HIS G CE1 1 
ATOM   7595 N  NE2 . HIS G  3  99  ? 22.126 8.489   35.475  1.00 75.29  ? 99  HIS G NE2 1 
ATOM   7596 N  N   . GLN G  3  100 ? 23.664 3.904   40.397  1.00 87.15  ? 100 GLN G N   1 
ATOM   7597 C  CA  . GLN G  3  100 ? 23.539 2.648   41.109  1.00 89.00  ? 100 GLN G CA  1 
ATOM   7598 C  C   . GLN G  3  100 ? 22.700 2.805   42.371  1.00 91.54  ? 100 GLN G C   1 
ATOM   7599 O  O   . GLN G  3  100 ? 22.633 3.881   42.964  1.00 90.72  ? 100 GLN G O   1 
ATOM   7600 C  CB  . GLN G  3  100 ? 24.925 2.116   41.451  1.00 87.82  ? 100 GLN G CB  1 
ATOM   7601 C  CG  . GLN G  3  100 ? 25.407 1.064   40.477  1.00 88.69  ? 100 GLN G CG  1 
ATOM   7602 C  CD  . GLN G  3  100 ? 26.922 0.952   40.429  1.00 89.82  ? 100 GLN G CD  1 
ATOM   7603 O  OE1 . GLN G  3  100 ? 27.604 1.076   41.453  1.00 89.35  ? 100 GLN G OE1 1 
ATOM   7604 N  NE2 . GLN G  3  100 ? 27.457 0.698   39.232  1.00 89.36  ? 100 GLN G NE2 1 
ATOM   7605 N  N   . GLU G  3  101 ? 22.048 1.717   42.762  1.00 95.43  ? 101 GLU G N   1 
ATOM   7606 C  CA  . GLU G  3  101 ? 21.204 1.690   43.951  1.00 98.98  ? 101 GLU G CA  1 
ATOM   7607 C  C   . GLU G  3  101 ? 20.009 2.635   43.864  1.00 100.06 ? 101 GLU G C   1 
ATOM   7608 O  O   . GLU G  3  101 ? 19.734 3.413   44.782  1.00 100.26 ? 101 GLU G O   1 
ATOM   7609 C  CB  . GLU G  3  101 ? 22.031 1.996   45.201  1.00 100.60 ? 101 GLU G CB  1 
ATOM   7610 C  CG  . GLU G  3  101 ? 23.103 0.955   45.479  1.00 103.90 ? 101 GLU G CG  1 
ATOM   7611 C  CD  . GLU G  3  101 ? 23.639 1.039   46.892  1.00 105.47 ? 101 GLU G CD  1 
ATOM   7612 O  OE1 . GLU G  3  101 ? 24.164 2.107   47.267  1.00 106.65 ? 101 GLU G OE1 1 
ATOM   7613 O  OE2 . GLU G  3  101 ? 23.532 0.034   47.628  1.00 107.14 ? 101 GLU G OE2 1 
ATOM   7614 N  N   . ARG G  3  102 ? 19.309 2.554   42.739  1.00 99.92  ? 102 ARG G N   1 
ATOM   7615 C  CA  . ARG G  3  102 ? 18.117 3.345   42.503  1.00 99.74  ? 102 ARG G CA  1 
ATOM   7616 C  C   . ARG G  3  102 ? 17.163 2.394   41.820  1.00 100.14 ? 102 ARG G C   1 
ATOM   7617 O  O   . ARG G  3  102 ? 17.276 2.149   40.619  1.00 99.94  ? 102 ARG G O   1 
ATOM   7618 C  CB  . ARG G  3  102 ? 18.415 4.526   41.586  1.00 98.96  ? 102 ARG G CB  1 
ATOM   7619 C  CG  . ARG G  3  102 ? 19.270 5.599   42.225  1.00 97.46  ? 102 ARG G CG  1 
ATOM   7620 C  CD  . ARG G  3  102 ? 19.484 6.755   41.263  1.00 95.60  ? 102 ARG G CD  1 
ATOM   7621 N  NE  . ARG G  3  102 ? 20.401 7.756   41.801  1.00 92.51  ? 102 ARG G NE  1 
ATOM   7622 C  CZ  . ARG G  3  102 ? 20.107 8.591   42.792  1.00 91.30  ? 102 ARG G CZ  1 
ATOM   7623 N  NH1 . ARG G  3  102 ? 21.010 9.464   43.216  1.00 90.02  ? 102 ARG G NH1 1 
ATOM   7624 N  NH2 . ARG G  3  102 ? 18.906 8.565   43.354  1.00 90.09  ? 102 ARG G NH2 1 
ATOM   7625 N  N   . ALA G  3  103 ? 16.241 1.832   42.590  1.00 100.80 ? 103 ALA G N   1 
ATOM   7626 C  CA  . ALA G  3  103 ? 15.285 0.888   42.034  1.00 101.49 ? 103 ALA G CA  1 
ATOM   7627 C  C   . ALA G  3  103 ? 14.622 1.507   40.810  1.00 101.28 ? 103 ALA G C   1 
ATOM   7628 O  O   . ALA G  3  103 ? 14.104 2.626   40.872  1.00 102.09 ? 103 ALA G O   1 
ATOM   7629 C  CB  . ALA G  3  103 ? 14.233 0.524   43.080  1.00 102.02 ? 103 ALA G CB  1 
ATOM   7630 N  N   . GLY G  3  104 ? 14.658 0.784   39.698  1.00 100.03 ? 104 GLY G N   1 
ATOM   7631 C  CA  . GLY G  3  104 ? 14.048 1.283   38.481  1.00 98.50  ? 104 GLY G CA  1 
ATOM   7632 C  C   . GLY G  3  104 ? 15.052 1.724   37.435  1.00 97.48  ? 104 GLY G C   1 
ATOM   7633 O  O   . GLY G  3  104 ? 14.758 1.702   36.242  1.00 98.24  ? 104 GLY G O   1 
ATOM   7634 N  N   . VAL G  3  105 ? 16.237 2.138   37.876  1.00 96.07  ? 105 VAL G N   1 
ATOM   7635 C  CA  . VAL G  3  105 ? 17.273 2.568   36.949  1.00 94.37  ? 105 VAL G CA  1 
ATOM   7636 C  C   . VAL G  3  105 ? 17.995 1.332   36.422  1.00 93.22  ? 105 VAL G C   1 
ATOM   7637 O  O   . VAL G  3  105 ? 18.809 0.720   37.117  1.00 93.41  ? 105 VAL G O   1 
ATOM   7638 C  CB  . VAL G  3  105 ? 18.286 3.513   37.629  1.00 94.74  ? 105 VAL G CB  1 
ATOM   7639 C  CG1 . VAL G  3  105 ? 19.467 3.771   36.699  1.00 94.81  ? 105 VAL G CG1 1 
ATOM   7640 C  CG2 . VAL G  3  105 ? 17.606 4.828   37.984  1.00 93.85  ? 105 VAL G CG2 1 
ATOM   7641 N  N   . THR G  3  106 ? 17.690 0.976   35.179  1.00 91.32  ? 106 THR G N   1 
ATOM   7642 C  CA  . THR G  3  106 ? 18.272 -0.200  34.553  1.00 89.29  ? 106 THR G CA  1 
ATOM   7643 C  C   . THR G  3  106 ? 18.917 0.080   33.203  1.00 87.47  ? 106 THR G C   1 
ATOM   7644 O  O   . THR G  3  106 ? 18.890 1.200   32.697  1.00 87.05  ? 106 THR G O   1 
ATOM   7645 C  CB  . THR G  3  106 ? 17.196 -1.259  34.322  1.00 89.97  ? 106 THR G CB  1 
ATOM   7646 O  OG1 . THR G  3  106 ? 16.183 -0.724  33.456  1.00 89.44  ? 106 THR G OG1 1 
ATOM   7647 C  CG2 . THR G  3  106 ? 16.570 -1.664  35.638  1.00 90.87  ? 106 THR G CG2 1 
ATOM   7648 N  N   . LYS G  3  107 ? 19.486 -0.963  32.616  1.00 85.18  ? 107 LYS G N   1 
ATOM   7649 C  CA  . LYS G  3  107 ? 20.113 -0.841  31.318  1.00 83.31  ? 107 LYS G CA  1 
ATOM   7650 C  C   . LYS G  3  107 ? 19.017 -0.611  30.302  1.00 82.93  ? 107 LYS G C   1 
ATOM   7651 O  O   . LYS G  3  107 ? 19.218 0.067   29.295  1.00 83.85  ? 107 LYS G O   1 
ATOM   7652 C  CB  . LYS G  3  107 ? 20.875 -2.115  30.972  1.00 81.99  ? 107 LYS G CB  1 
ATOM   7653 C  CG  . LYS G  3  107 ? 22.096 -2.330  31.832  1.00 80.53  ? 107 LYS G CG  1 
ATOM   7654 C  CD  . LYS G  3  107 ? 22.986 -3.410  31.247  1.00 79.64  ? 107 LYS G CD  1 
ATOM   7655 C  CE  . LYS G  3  107 ? 24.284 -3.523  32.027  1.00 79.35  ? 107 LYS G CE  1 
ATOM   7656 N  NZ  . LYS G  3  107 ? 25.182 -4.553  31.446  1.00 78.74  ? 107 LYS G NZ  1 
ATOM   7657 N  N   . GLY G  3  108 ? 17.853 -1.188  30.570  1.00 82.30  ? 108 GLY G N   1 
ATOM   7658 C  CA  . GLY G  3  108 ? 16.731 -1.017  29.671  1.00 80.81  ? 108 GLY G CA  1 
ATOM   7659 C  C   . GLY G  3  108 ? 16.341 0.447   29.605  1.00 79.42  ? 108 GLY G C   1 
ATOM   7660 O  O   . GLY G  3  108 ? 15.808 0.908   28.599  1.00 78.66  ? 108 GLY G O   1 
ATOM   7661 N  N   . GLY G  3  109 ? 16.617 1.178   30.681  1.00 78.85  ? 109 GLY G N   1 
ATOM   7662 C  CA  . GLY G  3  109 ? 16.288 2.594   30.725  1.00 78.31  ? 109 GLY G CA  1 
ATOM   7663 C  C   . GLY G  3  109 ? 17.191 3.394   29.804  1.00 77.85  ? 109 GLY G C   1 
ATOM   7664 O  O   . GLY G  3  109 ? 16.733 4.273   29.067  1.00 76.41  ? 109 GLY G O   1 
ATOM   7665 N  N   . PHE G  3  110 ? 18.483 3.076   29.854  1.00 77.11  ? 110 PHE G N   1 
ATOM   7666 C  CA  . PHE G  3  110 ? 19.498 3.727   29.031  1.00 74.93  ? 110 PHE G CA  1 
ATOM   7667 C  C   . PHE G  3  110 ? 19.319 3.376   27.558  1.00 75.10  ? 110 PHE G C   1 
ATOM   7668 O  O   . PHE G  3  110 ? 19.579 4.194   26.683  1.00 76.20  ? 110 PHE G O   1 
ATOM   7669 C  CB  . PHE G  3  110 ? 20.888 3.305   29.497  1.00 72.36  ? 110 PHE G CB  1 
ATOM   7670 C  CG  . PHE G  3  110 ? 21.373 4.057   30.693  1.00 69.97  ? 110 PHE G CG  1 
ATOM   7671 C  CD1 . PHE G  3  110 ? 22.127 5.209   30.537  1.00 71.60  ? 110 PHE G CD1 1 
ATOM   7672 C  CD2 . PHE G  3  110 ? 21.081 3.623   31.974  1.00 68.53  ? 110 PHE G CD2 1 
ATOM   7673 C  CE1 . PHE G  3  110 ? 22.586 5.918   31.651  1.00 71.01  ? 110 PHE G CE1 1 
ATOM   7674 C  CE2 . PHE G  3  110 ? 21.532 4.324   33.090  1.00 68.39  ? 110 PHE G CE2 1 
ATOM   7675 C  CZ  . PHE G  3  110 ? 22.283 5.470   32.928  1.00 69.48  ? 110 PHE G CZ  1 
ATOM   7676 N  N   . SER G  3  111 ? 18.881 2.155   27.282  1.00 74.34  ? 111 SER G N   1 
ATOM   7677 C  CA  . SER G  3  111 ? 18.661 1.744   25.905  1.00 73.14  ? 111 SER G CA  1 
ATOM   7678 C  C   . SER G  3  111 ? 17.491 2.543   25.338  1.00 71.17  ? 111 SER G C   1 
ATOM   7679 O  O   . SER G  3  111 ? 17.438 2.813   24.141  1.00 70.61  ? 111 SER G O   1 
ATOM   7680 C  CB  . SER G  3  111 ? 18.352 0.251   25.852  1.00 74.68  ? 111 SER G CB  1 
ATOM   7681 O  OG  . SER G  3  111 ? 19.355 -0.489  26.531  1.00 75.63  ? 111 SER G OG  1 
ATOM   7682 N  N   . ALA G  3  112 ? 16.558 2.925   26.206  1.00 68.44  ? 112 ALA G N   1 
ATOM   7683 C  CA  . ALA G  3  112 ? 15.395 3.687   25.780  1.00 67.61  ? 112 ALA G CA  1 
ATOM   7684 C  C   . ALA G  3  112 ? 15.725 5.160   25.584  1.00 67.65  ? 112 ALA G C   1 
ATOM   7685 O  O   . ALA G  3  112 ? 15.321 5.771   24.596  1.00 67.38  ? 112 ALA G O   1 
ATOM   7686 C  CB  . ALA G  3  112 ? 14.266 3.546   26.792  1.00 66.42  ? 112 ALA G CB  1 
ATOM   7687 N  N   . ILE G  3  113 ? 16.466 5.740   26.522  1.00 67.21  ? 113 ILE G N   1 
ATOM   7688 C  CA  . ILE G  3  113 ? 16.806 7.151   26.409  1.00 66.34  ? 113 ILE G CA  1 
ATOM   7689 C  C   . ILE G  3  113 ? 17.717 7.366   25.208  1.00 67.14  ? 113 ILE G C   1 
ATOM   7690 O  O   . ILE G  3  113 ? 17.691 8.429   24.581  1.00 66.50  ? 113 ILE G O   1 
ATOM   7691 C  CB  . ILE G  3  113 ? 17.487 7.669   27.684  1.00 65.20  ? 113 ILE G CB  1 
ATOM   7692 C  CG1 . ILE G  3  113 ? 17.376 9.188   27.735  1.00 63.20  ? 113 ILE G CG1 1 
ATOM   7693 C  CG2 . ILE G  3  113 ? 18.945 7.215   27.718  1.00 64.47  ? 113 ILE G CG2 1 
ATOM   7694 C  CD1 . ILE G  3  113 ? 17.672 9.788   29.086  1.00 60.85  ? 113 ILE G CD1 1 
ATOM   7695 N  N   . ALA G  3  114 ? 18.514 6.350   24.889  1.00 67.74  ? 114 ALA G N   1 
ATOM   7696 C  CA  . ALA G  3  114 ? 19.419 6.417   23.747  1.00 68.79  ? 114 ALA G CA  1 
ATOM   7697 C  C   . ALA G  3  114 ? 18.574 6.609   22.499  1.00 69.86  ? 114 ALA G C   1 
ATOM   7698 O  O   . ALA G  3  114 ? 18.994 7.269   21.548  1.00 70.37  ? 114 ALA G O   1 
ATOM   7699 C  CB  . ALA G  3  114 ? 20.232 5.129   23.629  1.00 68.06  ? 114 ALA G CB  1 
ATOM   7700 N  N   . GLN G  3  115 ? 17.376 6.033   22.515  1.00 70.73  ? 115 GLN G N   1 
ATOM   7701 C  CA  . GLN G  3  115 ? 16.463 6.141   21.388  1.00 71.27  ? 115 GLN G CA  1 
ATOM   7702 C  C   . GLN G  3  115 ? 15.821 7.513   21.386  1.00 69.10  ? 115 GLN G C   1 
ATOM   7703 O  O   . GLN G  3  115 ? 15.509 8.046   20.328  1.00 69.25  ? 115 GLN G O   1 
ATOM   7704 C  CB  . GLN G  3  115 ? 15.393 5.053   21.465  1.00 74.58  ? 115 GLN G CB  1 
ATOM   7705 C  CG  . GLN G  3  115 ? 15.970 3.649   21.427  1.00 81.49  ? 115 GLN G CG  1 
ATOM   7706 C  CD  . GLN G  3  115 ? 14.922 2.573   21.661  1.00 85.93  ? 115 GLN G CD  1 
ATOM   7707 O  OE1 . GLN G  3  115 ? 14.169 2.617   22.645  1.00 87.10  ? 115 GLN G OE1 1 
ATOM   7708 N  NE2 . GLN G  3  115 ? 14.873 1.591   20.761  1.00 86.80  ? 115 GLN G NE2 1 
ATOM   7709 N  N   . SER G  3  116 ? 15.628 8.085   22.568  1.00 66.67  ? 116 SER G N   1 
ATOM   7710 C  CA  . SER G  3  116 ? 15.045 9.419   22.673  1.00 66.01  ? 116 SER G CA  1 
ATOM   7711 C  C   . SER G  3  116 ? 15.997 10.409  21.996  1.00 64.12  ? 116 SER G C   1 
ATOM   7712 O  O   . SER G  3  116 ? 15.584 11.236  21.184  1.00 63.29  ? 116 SER G O   1 
ATOM   7713 C  CB  . SER G  3  116 ? 14.851 9.795   24.141  1.00 67.04  ? 116 SER G CB  1 
ATOM   7714 O  OG  . SER G  3  116 ? 14.032 8.840   24.787  1.00 68.18  ? 116 SER G OG  1 
ATOM   7715 N  N   . PHE G  3  117 ? 17.281 10.306  22.343  1.00 61.92  ? 117 PHE G N   1 
ATOM   7716 C  CA  . PHE G  3  117 ? 18.314 11.161  21.769  1.00 59.19  ? 117 PHE G CA  1 
ATOM   7717 C  C   . PHE G  3  117 ? 18.349 11.011  20.245  1.00 58.26  ? 117 PHE G C   1 
ATOM   7718 O  O   . PHE G  3  117 ? 18.509 11.992  19.530  1.00 57.75  ? 117 PHE G O   1 
ATOM   7719 C  CB  . PHE G  3  117 ? 19.682 10.800  22.355  1.00 56.28  ? 117 PHE G CB  1 
ATOM   7720 C  CG  . PHE G  3  117 ? 20.046 11.587  23.579  1.00 53.74  ? 117 PHE G CG  1 
ATOM   7721 C  CD1 . PHE G  3  117 ? 20.481 12.898  23.474  1.00 54.75  ? 117 PHE G CD1 1 
ATOM   7722 C  CD2 . PHE G  3  117 ? 19.961 11.022  24.840  1.00 52.49  ? 117 PHE G CD2 1 
ATOM   7723 C  CE1 . PHE G  3  117 ? 20.825 13.630  24.617  1.00 51.71  ? 117 PHE G CE1 1 
ATOM   7724 C  CE2 . PHE G  3  117 ? 20.303 11.752  25.977  1.00 51.01  ? 117 PHE G CE2 1 
ATOM   7725 C  CZ  . PHE G  3  117 ? 20.733 13.051  25.861  1.00 50.53  ? 117 PHE G CZ  1 
ATOM   7726 N  N   . LEU G  3  118 ? 18.209 9.788   19.742  1.00 56.77  ? 118 LEU G N   1 
ATOM   7727 C  CA  . LEU G  3  118 ? 18.220 9.585   18.300  1.00 55.83  ? 118 LEU G CA  1 
ATOM   7728 C  C   . LEU G  3  118 ? 17.007 10.241  17.639  1.00 55.04  ? 118 LEU G C   1 
ATOM   7729 O  O   . LEU G  3  118 ? 17.000 10.472  16.431  1.00 54.94  ? 118 LEU G O   1 
ATOM   7730 C  CB  . LEU G  3  118 ? 18.264 8.095   17.978  1.00 55.28  ? 118 LEU G CB  1 
ATOM   7731 C  CG  . LEU G  3  118 ? 19.621 7.463   18.258  1.00 56.04  ? 118 LEU G CG  1 
ATOM   7732 C  CD1 . LEU G  3  118 ? 19.580 5.942   18.082  1.00 55.22  ? 118 LEU G CD1 1 
ATOM   7733 C  CD2 . LEU G  3  118 ? 20.619 8.082   17.313  1.00 56.42  ? 118 LEU G CD2 1 
ATOM   7734 N  N   . ARG G  3  119 ? 15.985 10.545  18.434  1.00 53.66  ? 119 ARG G N   1 
ATOM   7735 C  CA  . ARG G  3  119 ? 14.794 11.189  17.903  1.00 55.32  ? 119 ARG G CA  1 
ATOM   7736 C  C   . ARG G  3  119 ? 14.851 12.715  18.057  1.00 55.24  ? 119 ARG G C   1 
ATOM   7737 O  O   . ARG G  3  119 ? 14.403 13.449  17.175  1.00 54.17  ? 119 ARG G O   1 
ATOM   7738 C  CB  . ARG G  3  119 ? 13.534 10.650  18.595  1.00 57.18  ? 119 ARG G CB  1 
ATOM   7739 C  CG  . ARG G  3  119 ? 12.964 9.358   17.982  1.00 57.73  ? 119 ARG G CG  1 
ATOM   7740 C  CD  . ARG G  3  119 ? 11.610 9.015   18.589  1.00 57.62  ? 119 ARG G CD  1 
ATOM   7741 N  NE  . ARG G  3  119 ? 11.712 8.677   20.011  1.00 56.99  ? 119 ARG G NE  1 
ATOM   7742 C  CZ  . ARG G  3  119 ? 11.943 7.445   20.475  1.00 55.90  ? 119 ARG G CZ  1 
ATOM   7743 N  NH1 . ARG G  3  119 ? 12.026 7.222   21.786  1.00 52.74  ? 119 ARG G NH1 1 
ATOM   7744 N  NH2 . ARG G  3  119 ? 12.077 6.430   19.627  1.00 50.27  ? 119 ARG G NH2 1 
ATOM   7745 N  N   . VAL G  3  120 ? 15.424 13.185  19.162  1.00 54.03  ? 120 VAL G N   1 
ATOM   7746 C  CA  . VAL G  3  120 ? 15.510 14.612  19.439  1.00 53.94  ? 120 VAL G CA  1 
ATOM   7747 C  C   . VAL G  3  120 ? 16.642 15.368  18.720  1.00 53.74  ? 120 VAL G C   1 
ATOM   7748 O  O   . VAL G  3  120 ? 16.420 16.450  18.162  1.00 53.98  ? 120 VAL G O   1 
ATOM   7749 C  CB  . VAL G  3  120 ? 15.615 14.847  20.973  1.00 55.44  ? 120 VAL G CB  1 
ATOM   7750 C  CG1 . VAL G  3  120 ? 15.859 16.326  21.276  1.00 54.57  ? 120 VAL G CG1 1 
ATOM   7751 C  CG2 . VAL G  3  120 ? 14.333 14.389  21.653  1.00 56.22  ? 120 VAL G CG2 1 
ATOM   7752 N  N   . MET G  3  121 ? 17.849 14.799  18.725  1.00 52.97  ? 121 MET G N   1 
ATOM   7753 C  CA  . MET G  3  121 ? 19.008 15.425  18.088  1.00 50.90  ? 121 MET G CA  1 
ATOM   7754 C  C   . MET G  3  121 ? 18.834 15.859  16.633  1.00 51.32  ? 121 MET G C   1 
ATOM   7755 O  O   . MET G  3  121 ? 19.093 17.016  16.304  1.00 52.10  ? 121 MET G O   1 
ATOM   7756 C  CB  . MET G  3  121 ? 20.240 14.518  18.183  1.00 48.99  ? 121 MET G CB  1 
ATOM   7757 C  CG  . MET G  3  121 ? 20.817 14.382  19.584  1.00 49.23  ? 121 MET G CG  1 
ATOM   7758 S  SD  . MET G  3  121 ? 21.229 15.959  20.360  1.00 52.25  ? 121 MET G SD  1 
ATOM   7759 C  CE  . MET G  3  121 ? 22.802 16.321  19.609  1.00 50.82  ? 121 MET G CE  1 
ATOM   7760 N  N   . PRO G  3  122 ? 18.397 14.953  15.735  1.00 50.62  ? 122 PRO G N   1 
ATOM   7761 C  CA  . PRO G  3  122 ? 18.257 15.440  14.359  1.00 50.79  ? 122 PRO G CA  1 
ATOM   7762 C  C   . PRO G  3  122 ? 17.377 16.673  14.238  1.00 51.55  ? 122 PRO G C   1 
ATOM   7763 O  O   . PRO G  3  122 ? 17.568 17.499  13.355  1.00 50.81  ? 122 PRO G O   1 
ATOM   7764 C  CB  . PRO G  3  122 ? 17.697 14.227  13.608  1.00 49.87  ? 122 PRO G CB  1 
ATOM   7765 C  CG  . PRO G  3  122 ? 17.025 13.429  14.672  1.00 49.46  ? 122 PRO G CG  1 
ATOM   7766 C  CD  . PRO G  3  122 ? 17.932 13.561  15.860  1.00 49.73  ? 122 PRO G CD  1 
ATOM   7767 N  N   . GLN G  3  123 ? 16.426 16.818  15.147  1.00 53.55  ? 123 GLN G N   1 
ATOM   7768 C  CA  . GLN G  3  123 ? 15.538 17.974  15.099  1.00 54.31  ? 123 GLN G CA  1 
ATOM   7769 C  C   . GLN G  3  123 ? 16.235 19.268  15.505  1.00 54.59  ? 123 GLN G C   1 
ATOM   7770 O  O   . GLN G  3  123 ? 15.788 20.355  15.154  1.00 56.20  ? 123 GLN G O   1 
ATOM   7771 C  CB  . GLN G  3  123 ? 14.350 17.777  16.033  1.00 54.83  ? 123 GLN G CB  1 
ATOM   7772 C  CG  . GLN G  3  123 ? 13.364 16.697  15.664  1.00 53.38  ? 123 GLN G CG  1 
ATOM   7773 C  CD  . GLN G  3  123 ? 12.360 16.479  16.796  1.00 55.56  ? 123 GLN G CD  1 
ATOM   7774 O  OE1 . GLN G  3  123 ? 11.482 17.319  17.050  1.00 54.36  ? 123 GLN G OE1 1 
ATOM   7775 N  NE2 . GLN G  3  123 ? 12.508 15.361  17.505  1.00 55.16  ? 123 GLN G NE2 1 
ATOM   7776 N  N   . VAL G  3  124 ? 17.327 19.160  16.244  1.00 54.34  ? 124 VAL G N   1 
ATOM   7777 C  CA  . VAL G  3  124 ? 17.994 20.361  16.714  1.00 53.87  ? 124 VAL G CA  1 
ATOM   7778 C  C   . VAL G  3  124 ? 19.432 20.548  16.215  1.00 52.76  ? 124 VAL G C   1 
ATOM   7779 O  O   . VAL G  3  124 ? 19.886 21.680  16.018  1.00 50.89  ? 124 VAL G O   1 
ATOM   7780 C  CB  . VAL G  3  124 ? 17.962 20.387  18.268  1.00 54.35  ? 124 VAL G CB  1 
ATOM   7781 C  CG1 . VAL G  3  124 ? 18.978 19.393  18.828  1.00 51.51  ? 124 VAL G CG1 1 
ATOM   7782 C  CG2 . VAL G  3  124 ? 18.206 21.811  18.787  1.00 55.45  ? 124 VAL G CG2 1 
ATOM   7783 N  N   . ALA G  3  125 ? 20.127 19.438  16.003  1.00 52.91  ? 125 ALA G N   1 
ATOM   7784 C  CA  . ALA G  3  125 ? 21.512 19.453  15.551  1.00 52.82  ? 125 ALA G CA  1 
ATOM   7785 C  C   . ALA G  3  125 ? 21.663 19.449  14.034  1.00 53.73  ? 125 ALA G C   1 
ATOM   7786 O  O   . ALA G  3  125 ? 20.963 18.741  13.311  1.00 54.34  ? 125 ALA G O   1 
ATOM   7787 C  CB  . ALA G  3  125 ? 22.266 18.271  16.147  1.00 51.38  ? 125 ALA G CB  1 
ATOM   7788 N  N   . SER G  3  126 ? 22.595 20.257  13.550  1.00 55.21  ? 126 SER G N   1 
ATOM   7789 C  CA  . SER G  3  126 ? 22.819 20.336  12.121  1.00 55.42  ? 126 SER G CA  1 
ATOM   7790 C  C   . SER G  3  126 ? 23.793 19.241  11.728  1.00 56.76  ? 126 SER G C   1 
ATOM   7791 O  O   . SER G  3  126 ? 24.660 18.860  12.521  1.00 56.90  ? 126 SER G O   1 
ATOM   7792 C  CB  . SER G  3  126 ? 23.362 21.718  11.742  1.00 53.51  ? 126 SER G CB  1 
ATOM   7793 O  OG  . SER G  3  126 ? 22.364 22.713  11.915  1.00 49.04  ? 126 SER G OG  1 
ATOM   7794 N  N   . CYS G  3  127 ? 23.622 18.710  10.520  1.00 57.09  ? 127 CYS G N   1 
ATOM   7795 C  CA  . CYS G  3  127 ? 24.506 17.678  10.005  1.00 58.26  ? 127 CYS G CA  1 
ATOM   7796 C  C   . CYS G  3  127 ? 24.583 16.438  10.909  1.00 59.37  ? 127 CYS G C   1 
ATOM   7797 O  O   . CYS G  3  127 ? 25.632 15.818  10.996  1.00 59.37  ? 127 CYS G O   1 
ATOM   7798 C  CB  . CYS G  3  127 ? 25.916 18.218  9.850   1.00 56.44  ? 127 CYS G CB  1 
ATOM   7799 S  SG  . CYS G  3  127 ? 26.219 19.731  8.856   1.00 56.90  ? 127 CYS G SG  1 
ATOM   7800 N  N   . PHE G  3  128 ? 23.482 16.079  11.555  1.00 60.22  ? 128 PHE G N   1 
ATOM   7801 C  CA  . PHE G  3  128 ? 23.474 14.939  12.464  1.00 60.49  ? 128 PHE G CA  1 
ATOM   7802 C  C   . PHE G  3  128 ? 23.800 13.595  11.814  1.00 60.68  ? 128 PHE G C   1 
ATOM   7803 O  O   . PHE G  3  128 ? 23.233 13.256  10.778  1.00 63.06  ? 128 PHE G O   1 
ATOM   7804 C  CB  . PHE G  3  128 ? 22.122 14.839  13.149  1.00 59.53  ? 128 PHE G CB  1 
ATOM   7805 C  CG  . PHE G  3  128 ? 22.083 13.843  14.257  1.00 59.18  ? 128 PHE G CG  1 
ATOM   7806 C  CD1 . PHE G  3  128 ? 22.812 14.063  15.423  1.00 57.21  ? 128 PHE G CD1 1 
ATOM   7807 C  CD2 . PHE G  3  128 ? 21.331 12.680  14.138  1.00 58.84  ? 128 PHE G CD2 1 
ATOM   7808 C  CE1 . PHE G  3  128 ? 22.793 13.138  16.452  1.00 56.21  ? 128 PHE G CE1 1 
ATOM   7809 C  CE2 . PHE G  3  128 ? 21.308 11.745  15.168  1.00 58.15  ? 128 PHE G CE2 1 
ATOM   7810 C  CZ  . PHE G  3  128 ? 22.041 11.975  16.327  1.00 56.47  ? 128 PHE G CZ  1 
ATOM   7811 N  N   . ASN G  3  129 ? 24.706 12.835  12.429  1.00 59.65  ? 129 ASN G N   1 
ATOM   7812 C  CA  . ASN G  3  129 ? 25.098 11.513  11.933  1.00 58.45  ? 129 ASN G CA  1 
ATOM   7813 C  C   . ASN G  3  129 ? 24.702 10.514  13.015  1.00 57.98  ? 129 ASN G C   1 
ATOM   7814 O  O   . ASN G  3  129 ? 25.462 10.272  13.959  1.00 57.81  ? 129 ASN G O   1 
ATOM   7815 C  CB  . ASN G  3  129 ? 26.614 11.459  11.708  1.00 59.61  ? 129 ASN G CB  1 
ATOM   7816 C  CG  . ASN G  3  129 ? 27.080 10.131  11.112  1.00 60.38  ? 129 ASN G CG  1 
ATOM   7817 O  OD1 . ASN G  3  129 ? 26.534 9.074   11.415  1.00 63.06  ? 129 ASN G OD1 1 
ATOM   7818 N  ND2 . ASN G  3  129 ? 28.114 10.190  10.281  1.00 58.33  ? 129 ASN G ND2 1 
ATOM   7819 N  N   . PRO G  3  130 ? 23.503 9.922   12.897  1.00 56.99  ? 130 PRO G N   1 
ATOM   7820 C  CA  . PRO G  3  130 ? 23.001 8.949   13.872  1.00 55.86  ? 130 PRO G CA  1 
ATOM   7821 C  C   . PRO G  3  130 ? 23.917 7.762   14.140  1.00 54.97  ? 130 PRO G C   1 
ATOM   7822 O  O   . PRO G  3  130 ? 24.075 7.353   15.288  1.00 54.27  ? 130 PRO G O   1 
ATOM   7823 C  CB  . PRO G  3  130 ? 21.640 8.547   13.293  1.00 54.05  ? 130 PRO G CB  1 
ATOM   7824 C  CG  . PRO G  3  130 ? 21.827 8.725   11.842  1.00 55.84  ? 130 PRO G CG  1 
ATOM   7825 C  CD  . PRO G  3  130 ? 22.573 10.035  11.762  1.00 56.18  ? 130 PRO G CD  1 
ATOM   7826 N  N   . ASP G  3  131 ? 24.517 7.202   13.099  1.00 55.11  ? 131 ASP G N   1 
ATOM   7827 C  CA  . ASP G  3  131 ? 25.401 6.070   13.324  1.00 56.87  ? 131 ASP G CA  1 
ATOM   7828 C  C   . ASP G  3  131 ? 26.547 6.481   14.244  1.00 56.06  ? 131 ASP G C   1 
ATOM   7829 O  O   . ASP G  3  131 ? 26.630 6.020   15.381  1.00 57.02  ? 131 ASP G O   1 
ATOM   7830 C  CB  . ASP G  3  131 ? 25.931 5.531   11.998  1.00 58.79  ? 131 ASP G CB  1 
ATOM   7831 C  CG  . ASP G  3  131 ? 24.833 4.865   11.154  1.00 62.13  ? 131 ASP G CG  1 
ATOM   7832 O  OD1 . ASP G  3  131 ? 23.723 4.580   11.685  1.00 58.99  ? 131 ASP G OD1 1 
ATOM   7833 O  OD2 . ASP G  3  131 ? 25.097 4.617   9.952   1.00 64.96  ? 131 ASP G OD2 1 
ATOM   7834 N  N   . ALA G  3  132 ? 27.411 7.365   13.764  1.00 53.85  ? 132 ALA G N   1 
ATOM   7835 C  CA  . ALA G  3  132 ? 28.533 7.827   14.566  1.00 52.13  ? 132 ALA G CA  1 
ATOM   7836 C  C   . ALA G  3  132 ? 28.111 8.224   15.979  1.00 50.22  ? 132 ALA G C   1 
ATOM   7837 O  O   . ALA G  3  132 ? 28.799 7.916   16.948  1.00 48.48  ? 132 ALA G O   1 
ATOM   7838 C  CB  . ALA G  3  132 ? 29.228 9.004   13.873  1.00 51.87  ? 132 ALA G CB  1 
ATOM   7839 N  N   . TRP G  3  133 ? 26.978 8.907   16.091  1.00 49.14  ? 133 TRP G N   1 
ATOM   7840 C  CA  . TRP G  3  133 ? 26.486 9.350   17.382  1.00 49.96  ? 133 TRP G CA  1 
ATOM   7841 C  C   . TRP G  3  133 ? 26.155 8.168   18.278  1.00 52.97  ? 133 TRP G C   1 
ATOM   7842 O  O   . TRP G  3  133 ? 26.566 8.135   19.444  1.00 53.86  ? 133 TRP G O   1 
ATOM   7843 C  CB  . TRP G  3  133 ? 25.246 10.231  17.200  1.00 47.41  ? 133 TRP G CB  1 
ATOM   7844 C  CG  . TRP G  3  133 ? 24.465 10.430  18.449  1.00 46.67  ? 133 TRP G CG  1 
ATOM   7845 C  CD1 . TRP G  3  133 ? 23.578 9.559   18.998  1.00 46.84  ? 133 TRP G CD1 1 
ATOM   7846 C  CD2 . TRP G  3  133 ? 24.540 11.547  19.344  1.00 46.65  ? 133 TRP G CD2 1 
ATOM   7847 N  NE1 . TRP G  3  133 ? 23.090 10.059  20.185  1.00 47.17  ? 133 TRP G NE1 1 
ATOM   7848 C  CE2 . TRP G  3  133 ? 23.666 11.280  20.419  1.00 46.93  ? 133 TRP G CE2 1 
ATOM   7849 C  CE3 . TRP G  3  133 ? 25.261 12.744  19.344  1.00 46.04  ? 133 TRP G CE3 1 
ATOM   7850 C  CZ2 . TRP G  3  133 ? 23.493 12.172  21.484  1.00 47.64  ? 133 TRP G CZ2 1 
ATOM   7851 C  CZ3 . TRP G  3  133 ? 25.094 13.629  20.405  1.00 45.25  ? 133 TRP G CZ3 1 
ATOM   7852 C  CH2 . TRP G  3  133 ? 24.216 13.337  21.461  1.00 45.47  ? 133 TRP G CH2 1 
ATOM   7853 N  N   . SER G  3  134 ? 25.425 7.197   17.731  1.00 54.05  ? 134 SER G N   1 
ATOM   7854 C  CA  . SER G  3  134 ? 25.028 6.023   18.491  1.00 55.34  ? 134 SER G CA  1 
ATOM   7855 C  C   . SER G  3  134 ? 26.237 5.215   18.972  1.00 55.65  ? 134 SER G C   1 
ATOM   7856 O  O   . SER G  3  134 ? 26.317 4.853   20.146  1.00 53.59  ? 134 SER G O   1 
ATOM   7857 C  CB  . SER G  3  134 ? 24.106 5.140   17.646  1.00 57.15  ? 134 SER G CB  1 
ATOM   7858 O  OG  . SER G  3  134 ? 23.239 4.366   18.472  1.00 58.60  ? 134 SER G OG  1 
ATOM   7859 N  N   . ARG G  3  135 ? 27.178 4.937   18.069  1.00 56.46  ? 135 ARG G N   1 
ATOM   7860 C  CA  . ARG G  3  135 ? 28.371 4.182   18.427  1.00 55.56  ? 135 ARG G CA  1 
ATOM   7861 C  C   . ARG G  3  135 ? 29.048 4.791   19.637  1.00 56.43  ? 135 ARG G C   1 
ATOM   7862 O  O   . ARG G  3  135 ? 29.447 4.086   20.563  1.00 57.63  ? 135 ARG G O   1 
ATOM   7863 C  CB  . ARG G  3  135 ? 29.367 4.131   17.263  1.00 55.66  ? 135 ARG G CB  1 
ATOM   7864 C  CG  . ARG G  3  135 ? 28.979 3.167   16.158  1.00 56.75  ? 135 ARG G CG  1 
ATOM   7865 C  CD  . ARG G  3  135 ? 30.148 2.861   15.233  1.00 60.05  ? 135 ARG G CD  1 
ATOM   7866 N  NE  . ARG G  3  135 ? 30.565 4.002   14.419  1.00 61.86  ? 135 ARG G NE  1 
ATOM   7867 C  CZ  . ARG G  3  135 ? 29.861 4.490   13.402  1.00 63.65  ? 135 ARG G CZ  1 
ATOM   7868 N  NH1 . ARG G  3  135 ? 30.311 5.533   12.712  1.00 64.31  ? 135 ARG G NH1 1 
ATOM   7869 N  NH2 . ARG G  3  135 ? 28.698 3.940   13.072  1.00 62.51  ? 135 ARG G NH2 1 
ATOM   7870 N  N   . CYS G  3  136 ? 29.165 6.110   19.651  1.00 57.25  ? 136 CYS G N   1 
ATOM   7871 C  CA  . CYS G  3  136 ? 29.817 6.754   20.776  1.00 57.64  ? 136 CYS G CA  1 
ATOM   7872 C  C   . CYS G  3  136 ? 28.876 7.021   21.926  1.00 58.56  ? 136 CYS G C   1 
ATOM   7873 O  O   . CYS G  3  136 ? 29.317 7.179   23.070  1.00 59.07  ? 136 CYS G O   1 
ATOM   7874 C  CB  . CYS G  3  136 ? 30.480 8.052   20.342  1.00 56.81  ? 136 CYS G CB  1 
ATOM   7875 S  SG  . CYS G  3  136 ? 31.827 7.747   19.167  1.00 57.83  ? 136 CYS G SG  1 
ATOM   7876 N  N   . PHE G  3  137 ? 27.581 7.099   21.643  1.00 58.76  ? 137 PHE G N   1 
ATOM   7877 C  CA  . PHE G  3  137 ? 26.645 7.325   22.732  1.00 59.65  ? 137 PHE G CA  1 
ATOM   7878 C  C   . PHE G  3  137 ? 26.620 6.046   23.574  1.00 59.98  ? 137 PHE G C   1 
ATOM   7879 O  O   . PHE G  3  137 ? 26.627 6.107   24.800  1.00 58.01  ? 137 PHE G O   1 
ATOM   7880 C  CB  . PHE G  3  137 ? 25.232 7.624   22.228  1.00 59.58  ? 137 PHE G CB  1 
ATOM   7881 C  CG  . PHE G  3  137 ? 24.262 7.908   23.334  1.00 59.45  ? 137 PHE G CG  1 
ATOM   7882 C  CD1 . PHE G  3  137 ? 24.115 9.197   23.828  1.00 60.29  ? 137 PHE G CD1 1 
ATOM   7883 C  CD2 . PHE G  3  137 ? 23.552 6.873   23.937  1.00 58.98  ? 137 PHE G CD2 1 
ATOM   7884 C  CE1 . PHE G  3  137 ? 23.278 9.456   24.915  1.00 60.50  ? 137 PHE G CE1 1 
ATOM   7885 C  CE2 . PHE G  3  137 ? 22.711 7.117   25.024  1.00 59.41  ? 137 PHE G CE2 1 
ATOM   7886 C  CZ  . PHE G  3  137 ? 22.574 8.408   25.515  1.00 60.35  ? 137 PHE G CZ  1 
ATOM   7887 N  N   . ASN G  3  138 ? 26.598 4.894   22.903  1.00 60.29  ? 138 ASN G N   1 
ATOM   7888 C  CA  . ASN G  3  138 ? 26.576 3.611   23.595  1.00 61.49  ? 138 ASN G CA  1 
ATOM   7889 C  C   . ASN G  3  138 ? 27.872 3.400   24.365  1.00 60.94  ? 138 ASN G C   1 
ATOM   7890 O  O   . ASN G  3  138 ? 27.860 2.912   25.496  1.00 61.77  ? 138 ASN G O   1 
ATOM   7891 C  CB  . ASN G  3  138 ? 26.359 2.460   22.604  1.00 62.52  ? 138 ASN G CB  1 
ATOM   7892 C  CG  . ASN G  3  138 ? 24.986 2.503   21.953  1.00 64.19  ? 138 ASN G CG  1 
ATOM   7893 O  OD1 . ASN G  3  138 ? 23.997 2.852   22.596  1.00 65.43  ? 138 ASN G OD1 1 
ATOM   7894 N  ND2 . ASN G  3  138 ? 24.917 2.136   20.680  1.00 64.77  ? 138 ASN G ND2 1 
ATOM   7895 N  N   . ARG G  3  139 ? 28.994 3.760   23.752  1.00 59.83  ? 139 ARG G N   1 
ATOM   7896 C  CA  . ARG G  3  139 ? 30.285 3.633   24.423  1.00 57.41  ? 139 ARG G CA  1 
ATOM   7897 C  C   . ARG G  3  139 ? 30.213 4.377   25.762  1.00 55.92  ? 139 ARG G C   1 
ATOM   7898 O  O   . ARG G  3  139 ? 30.854 3.987   26.741  1.00 55.88  ? 139 ARG G O   1 
ATOM   7899 C  CB  . ARG G  3  139 ? 31.398 4.241   23.562  1.00 57.84  ? 139 ARG G CB  1 
ATOM   7900 C  CG  . ARG G  3  139 ? 32.660 4.651   24.351  1.00 58.41  ? 139 ARG G CG  1 
ATOM   7901 C  CD  . ARG G  3  139 ? 33.586 3.467   24.626  1.00 59.75  ? 139 ARG G CD  1 
ATOM   7902 N  NE  . ARG G  3  139 ? 34.780 3.819   25.397  1.00 58.95  ? 139 ARG G NE  1 
ATOM   7903 C  CZ  . ARG G  3  139 ? 34.813 3.969   26.716  1.00 58.15  ? 139 ARG G CZ  1 
ATOM   7904 N  NH1 . ARG G  3  139 ? 33.710 3.798   27.431  1.00 57.08  ? 139 ARG G NH1 1 
ATOM   7905 N  NH2 . ARG G  3  139 ? 35.956 4.276   27.324  1.00 57.83  ? 139 ARG G NH2 1 
ATOM   7906 N  N   . ILE G  3  140 ? 29.436 5.451   25.815  1.00 52.95  ? 140 ILE G N   1 
ATOM   7907 C  CA  . ILE G  3  140 ? 29.341 6.206   27.059  1.00 51.98  ? 140 ILE G CA  1 
ATOM   7908 C  C   . ILE G  3  140 ? 28.413 5.534   28.070  1.00 52.56  ? 140 ILE G C   1 
ATOM   7909 O  O   . ILE G  3  140 ? 28.708 5.502   29.266  1.00 52.77  ? 140 ILE G O   1 
ATOM   7910 C  CB  . ILE G  3  140 ? 28.872 7.673   26.800  1.00 49.51  ? 140 ILE G CB  1 
ATOM   7911 C  CG1 . ILE G  3  140 ? 29.998 8.450   26.108  1.00 50.07  ? 140 ILE G CG1 1 
ATOM   7912 C  CG2 . ILE G  3  140 ? 28.458 8.353   28.106  1.00 41.24  ? 140 ILE G CG2 1 
ATOM   7913 C  CD1 . ILE G  3  140 ? 29.611 9.862   25.682  1.00 49.88  ? 140 ILE G CD1 1 
ATOM   7914 N  N   . THR G  3  141 ? 27.295 5.000   27.594  1.00 52.65  ? 141 THR G N   1 
ATOM   7915 C  CA  . THR G  3  141 ? 26.350 4.338   28.474  1.00 53.96  ? 141 THR G CA  1 
ATOM   7916 C  C   . THR G  3  141 ? 26.933 3.025   29.023  1.00 54.64  ? 141 THR G C   1 
ATOM   7917 O  O   . THR G  3  141 ? 26.778 2.714   30.202  1.00 53.93  ? 141 THR G O   1 
ATOM   7918 C  CB  . THR G  3  141 ? 25.000 4.093   27.748  1.00 53.58  ? 141 THR G CB  1 
ATOM   7919 O  OG1 . THR G  3  141 ? 25.227 3.434   26.493  1.00 53.33  ? 141 THR G OG1 1 
ATOM   7920 C  CG2 . THR G  3  141 ? 24.303 5.413   27.490  1.00 52.24  ? 141 THR G CG2 1 
ATOM   7921 N  N   . ASN G  3  142 ? 27.635 2.271   28.188  1.00 55.97  ? 142 ASN G N   1 
ATOM   7922 C  CA  . ASN G  3  142 ? 28.230 1.035   28.654  1.00 58.13  ? 142 ASN G CA  1 
ATOM   7923 C  C   . ASN G  3  142 ? 29.046 1.264   29.910  1.00 61.09  ? 142 ASN G C   1 
ATOM   7924 O  O   . ASN G  3  142 ? 29.117 0.401   30.772  1.00 62.70  ? 142 ASN G O   1 
ATOM   7925 C  CB  . ASN G  3  142 ? 29.117 0.440   27.577  1.00 56.60  ? 142 ASN G CB  1 
ATOM   7926 C  CG  . ASN G  3  142 ? 28.332 0.000   26.379  1.00 56.13  ? 142 ASN G CG  1 
ATOM   7927 O  OD1 . ASN G  3  142 ? 27.092 0.013   26.385  1.00 55.27  ? 142 ASN G OD1 1 
ATOM   7928 N  ND2 . ASN G  3  142 ? 29.038 -0.401  25.337  1.00 56.27  ? 142 ASN G ND2 1 
ATOM   7929 N  N   . GLY G  3  143 ? 29.663 2.433   30.011  1.00 63.98  ? 143 GLY G N   1 
ATOM   7930 C  CA  . GLY G  3  143 ? 30.453 2.750   31.184  1.00 68.01  ? 143 GLY G CA  1 
ATOM   7931 C  C   . GLY G  3  143 ? 29.581 3.203   32.337  1.00 70.58  ? 143 GLY G C   1 
ATOM   7932 O  O   . GLY G  3  143 ? 29.941 3.014   33.495  1.00 72.10  ? 143 GLY G O   1 
ATOM   7933 N  N   . MET G  3  144 ? 28.436 3.803   32.025  1.00 72.83  ? 144 MET G N   1 
ATOM   7934 C  CA  . MET G  3  144 ? 27.512 4.282   33.053  1.00 76.15  ? 144 MET G CA  1 
ATOM   7935 C  C   . MET G  3  144 ? 26.681 3.141   33.656  1.00 79.30  ? 144 MET G C   1 
ATOM   7936 O  O   . MET G  3  144 ? 26.384 3.145   34.847  1.00 80.09  ? 144 MET G O   1 
ATOM   7937 C  CB  . MET G  3  144 ? 26.567 5.346   32.470  1.00 73.92  ? 144 MET G CB  1 
ATOM   7938 C  CG  . MET G  3  144 ? 27.225 6.676   32.103  1.00 71.23  ? 144 MET G CG  1 
ATOM   7939 S  SD  . MET G  3  144 ? 25.985 7.885   31.547  1.00 67.20  ? 144 MET G SD  1 
ATOM   7940 C  CE  . MET G  3  144 ? 25.354 8.431   33.012  1.00 69.40  ? 144 MET G CE  1 
ATOM   7941 N  N   . THR G  3  145 ? 26.324 2.166   32.831  1.00 82.42  ? 145 THR G N   1 
ATOM   7942 C  CA  . THR G  3  145 ? 25.514 1.047   33.273  1.00 85.55  ? 145 THR G CA  1 
ATOM   7943 C  C   . THR G  3  145 ? 26.349 -0.145  33.703  1.00 88.73  ? 145 THR G C   1 
ATOM   7944 O  O   . THR G  3  145 ? 25.870 -1.281  33.679  1.00 89.31  ? 145 THR G O   1 
ATOM   7945 C  CB  . THR G  3  145 ? 24.584 0.576   32.149  1.00 85.77  ? 145 THR G CB  1 
ATOM   7946 O  OG1 . THR G  3  145 ? 25.356 -0.094  31.141  1.00 83.36  ? 145 THR G OG1 1 
ATOM   7947 C  CG2 . THR G  3  145 ? 23.860 1.768   31.529  1.00 84.94  ? 145 THR G CG2 1 
ATOM   7948 N  N   . GLU G  3  146 ? 27.593 0.100   34.101  1.00 91.66  ? 146 GLU G N   1 
ATOM   7949 C  CA  . GLU G  3  146 ? 28.468 -0.990  34.519  1.00 94.29  ? 146 GLU G CA  1 
ATOM   7950 C  C   . GLU G  3  146 ? 27.814 -1.926  35.530  1.00 94.03  ? 146 GLU G C   1 
ATOM   7951 O  O   . GLU G  3  146 ? 27.653 -3.118  35.263  1.00 94.15  ? 146 GLU G O   1 
ATOM   7952 C  CB  . GLU G  3  146 ? 29.774 -0.433  35.086  1.00 96.69  ? 146 GLU G CB  1 
ATOM   7953 C  CG  . GLU G  3  146 ? 30.981 -0.723  34.203  1.00 102.32 ? 146 GLU G CG  1 
ATOM   7954 C  CD  . GLU G  3  146 ? 31.208 -2.216  34.001  1.00 105.30 ? 146 GLU G CD  1 
ATOM   7955 O  OE1 . GLU G  3  146 ? 31.378 -2.931  35.010  1.00 106.99 ? 146 GLU G OE1 1 
ATOM   7956 O  OE2 . GLU G  3  146 ? 31.217 -2.674  32.836  1.00 107.62 ? 146 GLU G OE2 1 
ATOM   7957 N  N   . GLY G  3  147 ? 27.422 -1.385  36.681  1.00 92.93  ? 147 GLY G N   1 
ATOM   7958 C  CA  . GLY G  3  147 ? 26.790 -2.208  37.691  1.00 91.41  ? 147 GLY G CA  1 
ATOM   7959 C  C   . GLY G  3  147 ? 25.290 -2.010  37.819  1.00 91.25  ? 147 GLY G C   1 
ATOM   7960 O  O   . GLY G  3  147 ? 24.780 -1.777  38.915  1.00 91.77  ? 147 GLY G O   1 
ATOM   7961 N  N   . LEU G  3  148 ? 24.571 -2.102  36.705  1.00 90.58  ? 148 LEU G N   1 
ATOM   7962 C  CA  . LEU G  3  148 ? 23.121 -1.940  36.731  1.00 89.92  ? 148 LEU G CA  1 
ATOM   7963 C  C   . LEU G  3  148 ? 22.410 -3.178  36.200  1.00 89.56  ? 148 LEU G C   1 
ATOM   7964 O  O   . LEU G  3  148 ? 22.937 -3.888  35.346  1.00 90.22  ? 148 LEU G O   1 
ATOM   7965 C  CB  . LEU G  3  148 ? 22.698 -0.731  35.896  1.00 90.20  ? 148 LEU G CB  1 
ATOM   7966 C  CG  . LEU G  3  148 ? 23.043 0.674   36.384  1.00 89.67  ? 148 LEU G CG  1 
ATOM   7967 C  CD1 . LEU G  3  148 ? 22.411 1.679   35.437  1.00 88.70  ? 148 LEU G CD1 1 
ATOM   7968 C  CD2 . LEU G  3  148 ? 22.525 0.879   37.799  1.00 89.39  ? 148 LEU G CD2 1 
ATOM   7969 N  N   . ALA G  3  149 ? 21.208 -3.431  36.703  1.00 88.79  ? 149 ALA G N   1 
ATOM   7970 C  CA  . ALA G  3  149 ? 20.430 -4.582  36.259  1.00 88.93  ? 149 ALA G CA  1 
ATOM   7971 C  C   . ALA G  3  149 ? 19.913 -4.304  34.855  1.00 89.16  ? 149 ALA G C   1 
ATOM   7972 O  O   . ALA G  3  149 ? 19.615 -3.159  34.531  1.00 89.21  ? 149 ALA G O   1 
ATOM   7973 C  CB  . ALA G  3  149 ? 19.266 -4.821  37.209  1.00 89.16  ? 149 ALA G CB  1 
ATOM   7974 N  N   . GLU G  3  150 ? 19.801 -5.345  34.028  1.00 89.57  ? 150 GLU G N   1 
ATOM   7975 C  CA  . GLU G  3  150 ? 19.324 -5.185  32.654  1.00 90.28  ? 150 GLU G CA  1 
ATOM   7976 C  C   . GLU G  3  150 ? 18.079 -4.311  32.590  1.00 90.37  ? 150 GLU G C   1 
ATOM   7977 O  O   . GLU G  3  150 ? 17.490 -4.057  33.664  1.00 90.50  ? 150 GLU G O   1 
ATOM   7978 C  CB  . GLU G  3  150 ? 19.002 -6.547  32.033  1.00 91.15  ? 150 GLU G CB  1 
ATOM   7979 C  CG  . GLU G  3  150 ? 20.193 -7.475  31.854  1.00 93.42  ? 150 GLU G CG  1 
ATOM   7980 C  CD  . GLU G  3  150 ? 21.285 -6.892  30.966  1.00 94.58  ? 150 GLU G CD  1 
ATOM   7981 O  OE1 . GLU G  3  150 ? 20.961 -6.337  29.891  1.00 94.75  ? 150 GLU G OE1 1 
ATOM   7982 O  OE2 . GLU G  3  150 ? 22.474 -7.004  31.341  1.00 94.79  ? 150 GLU G OE2 1 
ATOM   7983 O  OXT . GLU G  3  150 ? 17.702 -3.899  31.470  1.00 90.00  ? 150 GLU G OXT 1 
ATOM   7984 N  N   . GLU H  4  2   ? 30.633 62.288  7.490   1.00 73.73  ? 2   GLU H N   1 
ATOM   7985 C  CA  . GLU H  4  2   ? 30.317 62.720  8.847   1.00 74.67  ? 2   GLU H CA  1 
ATOM   7986 C  C   . GLU H  4  2   ? 30.590 61.595  9.890   1.00 73.43  ? 2   GLU H C   1 
ATOM   7987 O  O   . GLU H  4  2   ? 31.345 60.643  9.614   1.00 74.46  ? 2   GLU H O   1 
ATOM   7988 C  CB  . GLU H  4  2   ? 28.827 63.112  8.891   1.00 75.82  ? 2   GLU H CB  1 
ATOM   7989 C  CG  . GLU H  4  2   ? 27.983 62.623  7.724   1.00 76.94  ? 2   GLU H CG  1 
ATOM   7990 C  CD  . GLU H  4  2   ? 26.501 63.082  7.846   1.00 78.47  ? 2   GLU H CD  1 
ATOM   7991 O  OE1 . GLU H  4  2   ? 25.685 62.670  6.926   1.00 79.46  ? 2   GLU H OE1 1 
ATOM   7992 O  OE2 . GLU H  4  2   ? 26.205 63.834  8.862   1.00 77.89  ? 2   GLU H OE2 1 
ATOM   7993 N  N   . PHE H  4  3   ? 29.966 61.724  11.067  1.00 70.33  ? 3   PHE H N   1 
ATOM   7994 C  CA  . PHE H  4  3   ? 30.141 60.746  12.148  1.00 68.14  ? 3   PHE H CA  1 
ATOM   7995 C  C   . PHE H  4  3   ? 31.530 60.626  12.798  1.00 65.86  ? 3   PHE H C   1 
ATOM   7996 O  O   . PHE H  4  3   ? 31.977 61.557  13.456  1.00 66.86  ? 3   PHE H O   1 
ATOM   7997 C  CB  . PHE H  4  3   ? 29.641 59.393  11.627  1.00 68.62  ? 3   PHE H CB  1 
ATOM   7998 C  CG  . PHE H  4  3   ? 28.176 59.405  11.303  1.00 69.51  ? 3   PHE H CG  1 
ATOM   7999 C  CD1 . PHE H  4  3   ? 27.225 59.557  12.329  1.00 70.88  ? 3   PHE H CD1 1 
ATOM   8000 C  CD2 . PHE H  4  3   ? 27.741 59.390  9.985   1.00 69.81  ? 3   PHE H CD2 1 
ATOM   8001 C  CE1 . PHE H  4  3   ? 25.849 59.703  12.026  1.00 70.42  ? 3   PHE H CE1 1 
ATOM   8002 C  CE2 . PHE H  4  3   ? 26.377 59.535  9.663   1.00 69.85  ? 3   PHE H CE2 1 
ATOM   8003 C  CZ  . PHE H  4  3   ? 25.428 59.693  10.683  1.00 70.73  ? 3   PHE H CZ  1 
ATOM   8004 N  N   . CYS H  4  4   ? 32.204 59.487  12.648  1.00 63.16  ? 4   CYS H N   1 
ATOM   8005 C  CA  . CYS H  4  4   ? 33.542 59.308  13.260  1.00 58.95  ? 4   CYS H CA  1 
ATOM   8006 C  C   . CYS H  4  4   ? 34.517 58.688  12.266  1.00 57.32  ? 4   CYS H C   1 
ATOM   8007 O  O   . CYS H  4  4   ? 34.125 58.295  11.175  1.00 56.87  ? 4   CYS H O   1 
ATOM   8008 C  CB  . CYS H  4  4   ? 33.433 58.425  14.531  1.00 58.43  ? 4   CYS H CB  1 
ATOM   8009 S  SG  . CYS H  4  4   ? 32.684 56.759  14.367  1.00 55.93  ? 4   CYS H SG  1 
ATOM   8010 N  N   . SER H  4  5   ? 35.789 58.608  12.636  1.00 55.01  ? 5   SER H N   1 
ATOM   8011 C  CA  . SER H  4  5   ? 36.802 58.041  11.739  1.00 53.13  ? 5   SER H CA  1 
ATOM   8012 C  C   . SER H  4  5   ? 36.707 56.528  11.621  1.00 52.80  ? 5   SER H C   1 
ATOM   8013 O  O   . SER H  4  5   ? 36.158 55.859  12.496  1.00 51.64  ? 5   SER H O   1 
ATOM   8014 C  CB  . SER H  4  5   ? 38.192 58.400  12.233  1.00 51.88  ? 5   SER H CB  1 
ATOM   8015 O  OG  . SER H  4  5   ? 38.478 57.704  13.428  1.00 53.78  ? 5   SER H OG  1 
ATOM   8016 N  N   . GLU H  4  6   ? 37.280 55.997  10.545  1.00 52.23  ? 6   GLU H N   1 
ATOM   8017 C  CA  . GLU H  4  6   ? 37.273 54.565  10.287  1.00 53.75  ? 6   GLU H CA  1 
ATOM   8018 C  C   . GLU H  4  6   ? 37.911 53.757  11.415  1.00 53.45  ? 6   GLU H C   1 
ATOM   8019 O  O   . GLU H  4  6   ? 37.420 52.668  11.762  1.00 52.47  ? 6   GLU H O   1 
ATOM   8020 C  CB  . GLU H  4  6   ? 37.994 54.271  8.961   1.00 56.22  ? 6   GLU H CB  1 
ATOM   8021 C  CG  . GLU H  4  6   ? 38.209 52.776  8.650   1.00 60.43  ? 6   GLU H CG  1 
ATOM   8022 C  CD  . GLU H  4  6   ? 38.790 52.532  7.262   1.00 63.31  ? 6   GLU H CD  1 
ATOM   8023 O  OE1 . GLU H  4  6   ? 38.069 52.727  6.261   1.00 66.69  ? 6   GLU H OE1 1 
ATOM   8024 O  OE2 . GLU H  4  6   ? 39.974 52.152  7.159   1.00 63.96  ? 6   GLU H OE2 1 
ATOM   8025 N  N   . ALA H  4  7   ? 39.005 54.277  11.975  1.00 51.51  ? 7   ALA H N   1 
ATOM   8026 C  CA  . ALA H  4  7   ? 39.693 53.575  13.055  1.00 50.08  ? 7   ALA H CA  1 
ATOM   8027 C  C   . ALA H  4  7   ? 38.834 53.547  14.320  1.00 49.42  ? 7   ALA H C   1 
ATOM   8028 O  O   . ALA H  4  7   ? 38.769 52.512  15.000  1.00 50.05  ? 7   ALA H O   1 
ATOM   8029 C  CB  . ALA H  4  7   ? 41.046 54.215  13.340  1.00 47.96  ? 7   ALA H CB  1 
ATOM   8030 N  N   . ASP H  4  8   ? 38.176 54.666  14.633  1.00 47.18  ? 8   ASP H N   1 
ATOM   8031 C  CA  . ASP H  4  8   ? 37.315 54.723  15.823  1.00 47.71  ? 8   ASP H CA  1 
ATOM   8032 C  C   . ASP H  4  8   ? 36.094 53.816  15.651  1.00 47.24  ? 8   ASP H C   1 
ATOM   8033 O  O   . ASP H  4  8   ? 35.718 53.065  16.560  1.00 47.87  ? 8   ASP H O   1 
ATOM   8034 C  CB  . ASP H  4  8   ? 36.849 56.156  16.103  1.00 45.82  ? 8   ASP H CB  1 
ATOM   8035 C  CG  . ASP H  4  8   ? 37.947 57.016  16.655  1.00 46.14  ? 8   ASP H CG  1 
ATOM   8036 O  OD1 . ASP H  4  8   ? 37.751 58.238  16.784  1.00 46.41  ? 8   ASP H OD1 1 
ATOM   8037 O  OD2 . ASP H  4  8   ? 39.018 56.467  16.966  1.00 48.68  ? 8   ASP H OD2 1 
ATOM   8038 N  N   . ALA H  4  9   ? 35.476 53.882  14.479  1.00 44.77  ? 9   ALA H N   1 
ATOM   8039 C  CA  . ALA H  4  9   ? 34.323 53.046  14.220  1.00 44.56  ? 9   ALA H CA  1 
ATOM   8040 C  C   . ALA H  4  9   ? 34.671 51.552  14.368  1.00 43.79  ? 9   ALA H C   1 
ATOM   8041 O  O   . ALA H  4  9   ? 33.882 50.780  14.913  1.00 41.52  ? 9   ALA H O   1 
ATOM   8042 C  CB  . ALA H  4  9   ? 33.798 53.321  12.822  1.00 43.05  ? 9   ALA H CB  1 
ATOM   8043 N  N   . THR H  4  10  ? 35.855 51.160  13.893  1.00 42.85  ? 10  THR H N   1 
ATOM   8044 C  CA  . THR H  4  10  ? 36.254 49.756  13.938  1.00 42.28  ? 10  THR H CA  1 
ATOM   8045 C  C   . THR H  4  10  ? 36.347 49.250  15.353  1.00 41.26  ? 10  THR H C   1 
ATOM   8046 O  O   . THR H  4  10  ? 36.024 48.089  15.621  1.00 40.44  ? 10  THR H O   1 
ATOM   8047 C  CB  . THR H  4  10  ? 37.607 49.503  13.204  1.00 43.44  ? 10  THR H CB  1 
ATOM   8048 O  OG1 . THR H  4  10  ? 37.477 49.874  11.820  1.00 46.30  ? 10  THR H OG1 1 
ATOM   8049 C  CG2 . THR H  4  10  ? 37.987 48.023  13.272  1.00 37.44  ? 10  THR H CG2 1 
ATOM   8050 N  N   . ILE H  4  11  ? 36.796 50.122  16.251  1.00 40.14  ? 11  ILE H N   1 
ATOM   8051 C  CA  . ILE H  4  11  ? 36.898 49.764  17.653  1.00 41.07  ? 11  ILE H CA  1 
ATOM   8052 C  C   . ILE H  4  11  ? 35.504 49.605  18.236  1.00 40.37  ? 11  ILE H C   1 
ATOM   8053 O  O   . ILE H  4  11  ? 35.210 48.593  18.877  1.00 41.69  ? 11  ILE H O   1 
ATOM   8054 C  CB  . ILE H  4  11  ? 37.650 50.838  18.462  1.00 41.37  ? 11  ILE H CB  1 
ATOM   8055 C  CG1 . ILE H  4  11  ? 39.141 50.742  18.140  1.00 39.90  ? 11  ILE H CG1 1 
ATOM   8056 C  CG2 . ILE H  4  11  ? 37.407 50.649  19.964  1.00 37.82  ? 11  ILE H CG2 1 
ATOM   8057 C  CD1 . ILE H  4  11  ? 39.916 51.999  18.460  1.00 40.69  ? 11  ILE H CD1 1 
ATOM   8058 N  N   . VAL H  4  12  ? 34.648 50.596  17.998  1.00 37.71  ? 12  VAL H N   1 
ATOM   8059 C  CA  . VAL H  4  12  ? 33.293 50.549  18.515  1.00 36.82  ? 12  VAL H CA  1 
ATOM   8060 C  C   . VAL H  4  12  ? 32.540 49.347  17.974  1.00 37.90  ? 12  VAL H C   1 
ATOM   8061 O  O   . VAL H  4  12  ? 31.861 48.659  18.729  1.00 39.37  ? 12  VAL H O   1 
ATOM   8062 C  CB  . VAL H  4  12  ? 32.489 51.853  18.193  1.00 34.90  ? 12  VAL H CB  1 
ATOM   8063 C  CG1 . VAL H  4  12  ? 31.012 51.661  18.559  1.00 31.97  ? 12  VAL H CG1 1 
ATOM   8064 C  CG2 . VAL H  4  12  ? 33.075 53.040  18.965  1.00 27.85  ? 12  VAL H CG2 1 
ATOM   8065 N  N   . ILE H  4  13  ? 32.663 49.078  16.678  1.00 38.92  ? 13  ILE H N   1 
ATOM   8066 C  CA  . ILE H  4  13  ? 31.954 47.949  16.086  1.00 40.42  ? 13  ILE H CA  1 
ATOM   8067 C  C   . ILE H  4  13  ? 32.404 46.632  16.665  1.00 43.18  ? 13  ILE H C   1 
ATOM   8068 O  O   . ILE H  4  13  ? 31.594 45.722  16.870  1.00 45.83  ? 13  ILE H O   1 
ATOM   8069 C  CB  . ILE H  4  13  ? 32.137 47.874  14.558  1.00 39.35  ? 13  ILE H CB  1 
ATOM   8070 C  CG1 . ILE H  4  13  ? 31.442 49.063  13.894  1.00 38.03  ? 13  ILE H CG1 1 
ATOM   8071 C  CG2 . ILE H  4  13  ? 31.570 46.547  14.031  1.00 35.30  ? 13  ILE H CG2 1 
ATOM   8072 C  CD1 . ILE H  4  13  ? 31.755 49.207  12.413  1.00 40.37  ? 13  ILE H CD1 1 
ATOM   8073 N  N   . LYS H  4  14  ? 33.698 46.520  16.913  1.00 46.72  ? 14  LYS H N   1 
ATOM   8074 C  CA  . LYS H  4  14  ? 34.242 45.292  17.479  1.00 50.16  ? 14  LYS H CA  1 
ATOM   8075 C  C   . LYS H  4  14  ? 33.799 45.114  18.937  1.00 49.45  ? 14  LYS H C   1 
ATOM   8076 O  O   . LYS H  4  14  ? 33.439 44.008  19.364  1.00 49.04  ? 14  LYS H O   1 
ATOM   8077 C  CB  . LYS H  4  14  ? 35.778 45.290  17.384  1.00 52.69  ? 14  LYS H CB  1 
ATOM   8078 C  CG  . LYS H  4  14  ? 36.405 44.078  18.063  1.00 59.21  ? 14  LYS H CG  1 
ATOM   8079 C  CD  . LYS H  4  14  ? 37.914 43.994  17.889  1.00 63.83  ? 14  LYS H CD  1 
ATOM   8080 C  CE  . LYS H  4  14  ? 38.489 42.922  18.822  1.00 68.45  ? 14  LYS H CE  1 
ATOM   8081 N  NZ  . LYS H  4  14  ? 39.954 42.693  18.636  1.00 69.05  ? 14  LYS H NZ  1 
ATOM   8082 N  N   . GLN H  4  15  ? 33.830 46.200  19.705  1.00 47.16  ? 15  GLN H N   1 
ATOM   8083 C  CA  . GLN H  4  15  ? 33.437 46.096  21.098  1.00 46.90  ? 15  GLN H CA  1 
ATOM   8084 C  C   . GLN H  4  15  ? 31.953 45.811  21.243  1.00 47.34  ? 15  GLN H C   1 
ATOM   8085 O  O   . GLN H  4  15  ? 31.544 45.109  22.172  1.00 48.60  ? 15  GLN H O   1 
ATOM   8086 C  CB  . GLN H  4  15  ? 33.802 47.364  21.856  1.00 44.21  ? 15  GLN H CB  1 
ATOM   8087 C  CG  . GLN H  4  15  ? 35.265 47.647  21.827  1.00 41.32  ? 15  GLN H CG  1 
ATOM   8088 C  CD  . GLN H  4  15  ? 35.690 48.596  22.912  1.00 42.01  ? 15  GLN H CD  1 
ATOM   8089 O  OE1 . GLN H  4  15  ? 34.936 49.504  23.309  1.00 42.70  ? 15  GLN H OE1 1 
ATOM   8090 N  NE2 . GLN H  4  15  ? 36.909 48.414  23.398  1.00 37.67  ? 15  GLN H NE2 1 
ATOM   8091 N  N   . TRP H  4  16  ? 31.150 46.341  20.324  1.00 45.30  ? 16  TRP H N   1 
ATOM   8092 C  CA  . TRP H  4  16  ? 29.718 46.121  20.378  1.00 45.73  ? 16  TRP H CA  1 
ATOM   8093 C  C   . TRP H  4  16  ? 29.387 44.698  20.006  1.00 46.96  ? 16  TRP H C   1 
ATOM   8094 O  O   . TRP H  4  16  ? 28.542 44.073  20.647  1.00 47.53  ? 16  TRP H O   1 
ATOM   8095 C  CB  . TRP H  4  16  ? 28.973 47.068  19.424  1.00 44.69  ? 16  TRP H CB  1 
ATOM   8096 C  CG  . TRP H  4  16  ? 27.516 46.729  19.227  1.00 43.25  ? 16  TRP H CG  1 
ATOM   8097 C  CD1 . TRP H  4  16  ? 26.945 46.119  18.139  1.00 45.71  ? 16  TRP H CD1 1 
ATOM   8098 C  CD2 . TRP H  4  16  ? 26.441 47.003  20.132  1.00 44.13  ? 16  TRP H CD2 1 
ATOM   8099 N  NE1 . TRP H  4  16  ? 25.579 46.006  18.307  1.00 44.57  ? 16  TRP H NE1 1 
ATOM   8100 C  CE2 . TRP H  4  16  ? 25.245 46.542  19.523  1.00 45.01  ? 16  TRP H CE2 1 
ATOM   8101 C  CE3 . TRP H  4  16  ? 26.368 47.597  21.396  1.00 45.07  ? 16  TRP H CE3 1 
ATOM   8102 C  CZ2 . TRP H  4  16  ? 23.997 46.662  20.139  1.00 43.48  ? 16  TRP H CZ2 1 
ATOM   8103 C  CZ3 . TRP H  4  16  ? 25.128 47.714  22.012  1.00 45.91  ? 16  TRP H CZ3 1 
ATOM   8104 C  CH2 . TRP H  4  16  ? 23.959 47.249  21.382  1.00 44.30  ? 16  TRP H CH2 1 
ATOM   8105 N  N   . ASN H  4  17  ? 30.052 44.189  18.968  1.00 47.46  ? 17  ASN H N   1 
ATOM   8106 C  CA  . ASN H  4  17  ? 29.784 42.828  18.521  1.00 48.40  ? 17  ASN H CA  1 
ATOM   8107 C  C   . ASN H  4  17  ? 30.104 41.814  19.597  1.00 47.73  ? 17  ASN H C   1 
ATOM   8108 O  O   . ASN H  4  17  ? 29.566 40.706  19.583  1.00 47.10  ? 17  ASN H O   1 
ATOM   8109 C  CB  . ASN H  4  17  ? 30.508 42.533  17.206  1.00 50.63  ? 17  ASN H CB  1 
ATOM   8110 C  CG  . ASN H  4  17  ? 29.884 43.296  16.020  1.00 54.17  ? 17  ASN H CG  1 
ATOM   8111 O  OD1 . ASN H  4  17  ? 28.688 43.620  16.023  1.00 54.55  ? 17  ASN H OD1 1 
ATOM   8112 N  ND2 . ASN H  4  17  ? 30.699 43.573  14.997  1.00 54.24  ? 17  ASN H ND2 1 
ATOM   8113 N  N   . GLN H  4  18  ? 30.947 42.214  20.546  1.00 48.10  ? 18  GLN H N   1 
ATOM   8114 C  CA  . GLN H  4  18  ? 31.297 41.354  21.659  1.00 51.89  ? 18  GLN H CA  1 
ATOM   8115 C  C   . GLN H  4  18  ? 30.019 40.957  22.413  1.00 53.86  ? 18  GLN H C   1 
ATOM   8116 O  O   . GLN H  4  18  ? 29.776 39.777  22.701  1.00 54.77  ? 18  GLN H O   1 
ATOM   8117 C  CB  . GLN H  4  18  ? 32.191 42.094  22.646  1.00 54.77  ? 18  GLN H CB  1 
ATOM   8118 C  CG  . GLN H  4  18  ? 33.667 42.059  22.381  1.00 59.72  ? 18  GLN H CG  1 
ATOM   8119 C  CD  . GLN H  4  18  ? 34.445 42.794  23.471  1.00 64.28  ? 18  GLN H CD  1 
ATOM   8120 O  OE1 . GLN H  4  18  ? 34.247 42.545  24.663  1.00 63.21  ? 18  GLN H OE1 1 
ATOM   8121 N  NE2 . GLN H  4  18  ? 35.333 43.703  23.066  1.00 65.70  ? 18  GLN H NE2 1 
ATOM   8122 N  N   . ILE H  4  19  ? 29.204 41.965  22.712  1.00 53.13  ? 19  ILE H N   1 
ATOM   8123 C  CA  . ILE H  4  19  ? 27.982 41.765  23.454  1.00 54.80  ? 19  ILE H CA  1 
ATOM   8124 C  C   . ILE H  4  19  ? 26.669 41.722  22.677  1.00 55.97  ? 19  ILE H C   1 
ATOM   8125 O  O   . ILE H  4  19  ? 25.610 41.519  23.268  1.00 55.65  ? 19  ILE H O   1 
ATOM   8126 C  CB  . ILE H  4  19  ? 27.870 42.829  24.530  1.00 55.58  ? 19  ILE H CB  1 
ATOM   8127 C  CG1 . ILE H  4  19  ? 27.830 44.218  23.885  1.00 55.42  ? 19  ILE H CG1 1 
ATOM   8128 C  CG2 . ILE H  4  19  ? 29.082 42.748  25.435  1.00 56.99  ? 19  ILE H CG2 1 
ATOM   8129 C  CD1 . ILE H  4  19  ? 27.780 45.350  24.884  1.00 52.32  ? 19  ILE H CD1 1 
ATOM   8130 N  N   . TYR H  4  20  ? 26.721 41.911  21.365  1.00 58.27  ? 20  TYR H N   1 
ATOM   8131 C  CA  . TYR H  4  20  ? 25.502 41.879  20.563  1.00 60.41  ? 20  TYR H CA  1 
ATOM   8132 C  C   . TYR H  4  20  ? 25.766 41.334  19.171  1.00 63.55  ? 20  TYR H C   1 
ATOM   8133 O  O   . TYR H  4  20  ? 26.607 41.856  18.424  1.00 65.00  ? 20  TYR H O   1 
ATOM   8134 C  CB  . TYR H  4  20  ? 24.907 43.286  20.468  1.00 59.40  ? 20  TYR H CB  1 
ATOM   8135 C  CG  . TYR H  4  20  ? 23.534 43.360  19.848  1.00 59.52  ? 20  TYR H CG  1 
ATOM   8136 C  CD1 . TYR H  4  20  ? 23.340 43.075  18.499  1.00 60.52  ? 20  TYR H CD1 1 
ATOM   8137 C  CD2 . TYR H  4  20  ? 22.428 43.728  20.611  1.00 58.97  ? 20  TYR H CD2 1 
ATOM   8138 C  CE1 . TYR H  4  20  ? 22.079 43.148  17.919  1.00 61.16  ? 20  TYR H CE1 1 
ATOM   8139 C  CE2 . TYR H  4  20  ? 21.164 43.806  20.051  1.00 59.84  ? 20  TYR H CE2 1 
ATOM   8140 C  CZ  . TYR H  4  20  ? 20.990 43.516  18.703  1.00 61.98  ? 20  TYR H CZ  1 
ATOM   8141 O  OH  . TYR H  4  20  ? 19.721 43.581  18.154  1.00 62.46  ? 20  TYR H OH  1 
ATOM   8142 N  N   . ASN H  4  21  ? 25.042 40.277  18.824  1.00 66.21  ? 21  ASN H N   1 
ATOM   8143 C  CA  . ASN H  4  21  ? 25.182 39.654  17.513  1.00 69.64  ? 21  ASN H CA  1 
ATOM   8144 C  C   . ASN H  4  21  ? 24.123 38.579  17.379  1.00 71.27  ? 21  ASN H C   1 
ATOM   8145 O  O   . ASN H  4  21  ? 23.494 38.213  18.365  1.00 70.97  ? 21  ASN H O   1 
ATOM   8146 C  CB  . ASN H  4  21  ? 26.578 39.045  17.369  1.00 69.89  ? 21  ASN H CB  1 
ATOM   8147 C  CG  . ASN H  4  21  ? 26.904 38.067  18.479  1.00 70.57  ? 21  ASN H CG  1 
ATOM   8148 O  OD1 . ASN H  4  21  ? 26.323 36.989  18.554  1.00 71.07  ? 21  ASN H OD1 1 
ATOM   8149 N  ND2 . ASN H  4  21  ? 27.834 38.442  19.354  1.00 68.26  ? 21  ASN H ND2 1 
ATOM   8150 N  N   . ALA H  4  22  ? 23.934 38.075  16.161  1.00 73.68  ? 22  ALA H N   1 
ATOM   8151 C  CA  . ALA H  4  22  ? 22.937 37.043  15.889  1.00 74.92  ? 22  ALA H CA  1 
ATOM   8152 C  C   . ALA H  4  22  ? 22.968 35.873  16.882  1.00 76.16  ? 22  ALA H C   1 
ATOM   8153 O  O   . ALA H  4  22  ? 21.939 35.232  17.125  1.00 77.15  ? 22  ALA H O   1 
ATOM   8154 C  CB  . ALA H  4  22  ? 23.110 36.523  14.464  1.00 75.86  ? 22  ALA H CB  1 
ATOM   8155 N  N   . GLY H  4  23  ? 24.136 35.604  17.458  1.00 76.34  ? 23  GLY H N   1 
ATOM   8156 C  CA  . GLY H  4  23  ? 24.259 34.512  18.411  1.00 76.75  ? 23  GLY H CA  1 
ATOM   8157 C  C   . GLY H  4  23  ? 23.863 34.853  19.841  1.00 77.52  ? 23  GLY H C   1 
ATOM   8158 O  O   . GLY H  4  23  ? 23.872 33.980  20.711  1.00 77.68  ? 23  GLY H O   1 
ATOM   8159 N  N   . ILE H  4  24  ? 23.519 36.114  20.086  1.00 78.02  ? 24  ILE H N   1 
ATOM   8160 C  CA  . ILE H  4  24  ? 23.118 36.573  21.414  1.00 78.63  ? 24  ILE H CA  1 
ATOM   8161 C  C   . ILE H  4  24  ? 21.598 36.416  21.578  1.00 78.90  ? 24  ILE H C   1 
ATOM   8162 O  O   . ILE H  4  24  ? 20.813 36.989  20.814  1.00 78.31  ? 24  ILE H O   1 
ATOM   8163 C  CB  . ILE H  4  24  ? 23.516 38.056  21.627  1.00 79.33  ? 24  ILE H CB  1 
ATOM   8164 C  CG1 . ILE H  4  24  ? 25.010 38.248  21.317  1.00 79.08  ? 24  ILE H CG1 1 
ATOM   8165 C  CG2 . ILE H  4  24  ? 23.192 38.486  23.054  1.00 79.16  ? 24  ILE H CG2 1 
ATOM   8166 C  CD1 . ILE H  4  24  ? 25.953 37.455  22.223  1.00 76.69  ? 24  ILE H CD1 1 
ATOM   8167 N  N   . GLY H  4  25  ? 21.197 35.631  22.574  1.00 79.02  ? 25  GLY H N   1 
ATOM   8168 C  CA  . GLY H  4  25  ? 19.784 35.384  22.809  1.00 78.30  ? 25  GLY H CA  1 
ATOM   8169 C  C   . GLY H  4  25  ? 18.995 36.597  23.259  1.00 77.95  ? 25  GLY H C   1 
ATOM   8170 O  O   . GLY H  4  25  ? 19.543 37.507  23.887  1.00 78.31  ? 25  GLY H O   1 
ATOM   8171 N  N   . ALA H  4  26  ? 17.702 36.604  22.948  1.00 76.65  ? 26  ALA H N   1 
ATOM   8172 C  CA  . ALA H  4  26  ? 16.830 37.716  23.312  1.00 75.28  ? 26  ALA H CA  1 
ATOM   8173 C  C   . ALA H  4  26  ? 16.885 38.059  24.801  1.00 74.19  ? 26  ALA H C   1 
ATOM   8174 O  O   . ALA H  4  26  ? 16.797 39.231  25.168  1.00 73.35  ? 26  ALA H O   1 
ATOM   8175 C  CB  . ALA H  4  26  ? 15.396 37.415  22.900  1.00 75.33  ? 26  ALA H CB  1 
ATOM   8176 N  N   . LYS H  4  27  ? 17.036 37.048  25.659  1.00 73.18  ? 27  LYS H N   1 
ATOM   8177 C  CA  . LYS H  4  27  ? 17.079 37.289  27.101  1.00 71.17  ? 27  LYS H CA  1 
ATOM   8178 C  C   . LYS H  4  27  ? 18.211 38.211  27.525  1.00 69.80  ? 27  LYS H C   1 
ATOM   8179 O  O   . LYS H  4  27  ? 18.009 39.088  28.366  1.00 70.07  ? 27  LYS H O   1 
ATOM   8180 C  CB  . LYS H  4  27  ? 17.178 35.983  27.882  1.00 71.21  ? 27  LYS H CB  1 
ATOM   8181 C  CG  . LYS H  4  27  ? 17.002 36.186  29.386  1.00 72.87  ? 27  LYS H CG  1 
ATOM   8182 C  CD  . LYS H  4  27  ? 16.889 34.871  30.131  1.00 74.07  ? 27  LYS H CD  1 
ATOM   8183 C  CE  . LYS H  4  27  ? 16.636 35.109  31.612  1.00 74.61  ? 27  LYS H CE  1 
ATOM   8184 N  NZ  . LYS H  4  27  ? 16.449 33.830  32.368  1.00 75.42  ? 27  LYS H NZ  1 
ATOM   8185 N  N   . SER H  4  28  ? 19.400 38.015  26.956  1.00 67.66  ? 28  SER H N   1 
ATOM   8186 C  CA  . SER H  4  28  ? 20.544 38.868  27.273  1.00 65.70  ? 28  SER H CA  1 
ATOM   8187 C  C   . SER H  4  28  ? 20.268 40.273  26.740  1.00 63.47  ? 28  SER H C   1 
ATOM   8188 O  O   . SER H  4  28  ? 20.711 41.275  27.305  1.00 61.94  ? 28  SER H O   1 
ATOM   8189 C  CB  . SER H  4  28  ? 21.802 38.337  26.596  1.00 65.89  ? 28  SER H CB  1 
ATOM   8190 O  OG  . SER H  4  28  ? 21.781 36.927  26.561  1.00 69.56  ? 28  SER H OG  1 
ATOM   8191 N  N   . ARG H  4  29  ? 19.534 40.333  25.635  1.00 61.67  ? 29  ARG H N   1 
ATOM   8192 C  CA  . ARG H  4  29  ? 19.209 41.606  25.020  1.00 61.19  ? 29  ARG H CA  1 
ATOM   8193 C  C   . ARG H  4  29  ? 18.310 42.460  25.898  1.00 59.77  ? 29  ARG H C   1 
ATOM   8194 O  O   . ARG H  4  29  ? 18.683 43.575  26.243  1.00 59.71  ? 29  ARG H O   1 
ATOM   8195 C  CB  . ARG H  4  29  ? 18.578 41.386  23.634  1.00 62.94  ? 29  ARG H CB  1 
ATOM   8196 C  CG  . ARG H  4  29  ? 19.509 40.673  22.669  1.00 63.02  ? 29  ARG H CG  1 
ATOM   8197 C  CD  . ARG H  4  29  ? 18.995 40.695  21.256  1.00 64.71  ? 29  ARG H CD  1 
ATOM   8198 N  NE  . ARG H  4  29  ? 19.804 39.829  20.404  1.00 65.92  ? 29  ARG H NE  1 
ATOM   8199 C  CZ  . ARG H  4  29  ? 19.724 39.797  19.082  1.00 65.62  ? 29  ARG H CZ  1 
ATOM   8200 N  NH1 . ARG H  4  29  ? 20.499 38.975  18.394  1.00 67.33  ? 29  ARG H NH1 1 
ATOM   8201 N  NH2 . ARG H  4  29  ? 18.877 40.593  18.442  1.00 65.14  ? 29  ARG H NH2 1 
ATOM   8202 N  N   . TRP H  4  30  ? 17.141 41.952  26.285  1.00 59.01  ? 30  TRP H N   1 
ATOM   8203 C  CA  . TRP H  4  30  ? 16.273 42.767  27.126  1.00 58.35  ? 30  TRP H CA  1 
ATOM   8204 C  C   . TRP H  4  30  ? 16.838 42.952  28.537  1.00 56.33  ? 30  TRP H C   1 
ATOM   8205 O  O   . TRP H  4  30  ? 16.410 43.847  29.256  1.00 55.87  ? 30  TRP H O   1 
ATOM   8206 C  CB  . TRP H  4  30  ? 14.825 42.225  27.156  1.00 60.59  ? 30  TRP H CB  1 
ATOM   8207 C  CG  . TRP H  4  30  ? 14.568 40.961  27.925  1.00 61.32  ? 30  TRP H CG  1 
ATOM   8208 C  CD1 . TRP H  4  30  ? 14.824 40.735  29.249  1.00 61.39  ? 30  TRP H CD1 1 
ATOM   8209 C  CD2 . TRP H  4  30  ? 13.959 39.759  27.421  1.00 62.20  ? 30  TRP H CD2 1 
ATOM   8210 N  NE1 . TRP H  4  30  ? 14.414 39.466  29.600  1.00 63.55  ? 30  TRP H NE1 1 
ATOM   8211 C  CE2 . TRP H  4  30  ? 13.881 38.846  28.499  1.00 62.87  ? 30  TRP H CE2 1 
ATOM   8212 C  CE3 . TRP H  4  30  ? 13.471 39.364  26.165  1.00 62.34  ? 30  TRP H CE3 1 
ATOM   8213 C  CZ2 . TRP H  4  30  ? 13.335 37.562  28.358  1.00 61.29  ? 30  TRP H CZ2 1 
ATOM   8214 C  CZ3 . TRP H  4  30  ? 12.929 38.086  26.026  1.00 62.77  ? 30  TRP H CZ3 1 
ATOM   8215 C  CH2 . TRP H  4  30  ? 12.867 37.203  27.119  1.00 61.90  ? 30  TRP H CH2 1 
ATOM   8216 N  N   . THR H  4  31  ? 17.803 42.114  28.920  1.00 53.57  ? 31  THR H N   1 
ATOM   8217 C  CA  . THR H  4  31  ? 18.454 42.235  30.217  1.00 51.73  ? 31  THR H CA  1 
ATOM   8218 C  C   . THR H  4  31  ? 19.281 43.504  30.152  1.00 49.80  ? 31  THR H C   1 
ATOM   8219 O  O   . THR H  4  31  ? 19.373 44.226  31.131  1.00 49.08  ? 31  THR H O   1 
ATOM   8220 C  CB  . THR H  4  31  ? 19.401 41.041  30.522  1.00 54.15  ? 31  THR H CB  1 
ATOM   8221 O  OG1 . THR H  4  31  ? 18.628 39.839  30.626  1.00 55.24  ? 31  THR H OG1 1 
ATOM   8222 C  CG2 . THR H  4  31  ? 20.167 41.261  31.843  1.00 50.55  ? 31  THR H CG2 1 
ATOM   8223 N  N   . MET H  4  32  ? 19.882 43.758  28.993  1.00 49.23  ? 32  MET H N   1 
ATOM   8224 C  CA  . MET H  4  32  ? 20.677 44.964  28.769  1.00 50.24  ? 32  MET H CA  1 
ATOM   8225 C  C   . MET H  4  32  ? 19.677 46.105  28.598  1.00 47.82  ? 32  MET H C   1 
ATOM   8226 O  O   . MET H  4  32  ? 19.836 47.195  29.147  1.00 45.61  ? 32  MET H O   1 
ATOM   8227 C  CB  . MET H  4  32  ? 21.538 44.828  27.494  1.00 52.99  ? 32  MET H CB  1 
ATOM   8228 C  CG  . MET H  4  32  ? 22.654 43.772  27.580  1.00 56.03  ? 32  MET H CG  1 
ATOM   8229 S  SD  . MET H  4  32  ? 23.564 43.482  26.031  1.00 57.11  ? 32  MET H SD  1 
ATOM   8230 C  CE  . MET H  4  32  ? 24.572 44.882  25.960  1.00 55.41  ? 32  MET H CE  1 
ATOM   8231 N  N   . GLY H  4  33  ? 18.623 45.824  27.841  1.00 47.22  ? 33  GLY H N   1 
ATOM   8232 C  CA  . GLY H  4  33  ? 17.591 46.822  27.605  1.00 50.11  ? 33  GLY H CA  1 
ATOM   8233 C  C   . GLY H  4  33  ? 16.963 47.368  28.885  1.00 50.41  ? 33  GLY H C   1 
ATOM   8234 O  O   . GLY H  4  33  ? 16.680 48.565  29.000  1.00 48.17  ? 33  GLY H O   1 
ATOM   8235 N  N   . ASN H  4  34  ? 16.756 46.484  29.852  1.00 51.63  ? 34  ASN H N   1 
ATOM   8236 C  CA  . ASN H  4  34  ? 16.163 46.882  31.111  1.00 53.28  ? 34  ASN H CA  1 
ATOM   8237 C  C   . ASN H  4  34  ? 17.114 47.725  31.945  1.00 52.54  ? 34  ASN H C   1 
ATOM   8238 O  O   . ASN H  4  34  ? 16.715 48.779  32.455  1.00 52.37  ? 34  ASN H O   1 
ATOM   8239 C  CB  . ASN H  4  34  ? 15.697 45.649  31.886  1.00 55.01  ? 34  ASN H CB  1 
ATOM   8240 C  CG  . ASN H  4  34  ? 14.297 45.215  31.488  1.00 57.08  ? 34  ASN H CG  1 
ATOM   8241 O  OD1 . ASN H  4  34  ? 13.834 45.467  30.364  1.00 58.51  ? 34  ASN H OD1 1 
ATOM   8242 N  ND2 . ASN H  4  34  ? 13.613 44.551  32.407  1.00 60.05  ? 34  ASN H ND2 1 
ATOM   8243 N  N   . GLU H  4  35  ? 18.368 47.286  32.070  1.00 50.79  ? 35  GLU H N   1 
ATOM   8244 C  CA  . GLU H  4  35  ? 19.345 48.043  32.844  1.00 49.02  ? 35  GLU H CA  1 
ATOM   8245 C  C   . GLU H  4  35  ? 19.529 49.430  32.252  1.00 46.54  ? 35  GLU H C   1 
ATOM   8246 O  O   . GLU H  4  35  ? 19.688 50.401  32.990  1.00 45.28  ? 35  GLU H O   1 
ATOM   8247 C  CB  . GLU H  4  35  ? 20.685 47.329  32.867  1.00 51.03  ? 35  GLU H CB  1 
ATOM   8248 C  CG  . GLU H  4  35  ? 20.672 46.068  33.664  1.00 56.70  ? 35  GLU H CG  1 
ATOM   8249 C  CD  . GLU H  4  35  ? 20.321 46.318  35.107  1.00 61.00  ? 35  GLU H CD  1 
ATOM   8250 O  OE1 . GLU H  4  35  ? 21.020 47.127  35.764  1.00 61.80  ? 35  GLU H OE1 1 
ATOM   8251 O  OE2 . GLU H  4  35  ? 19.343 45.701  35.583  1.00 62.45  ? 35  GLU H OE2 1 
ATOM   8252 N  N   . ILE H  4  36  ? 19.505 49.518  30.924  1.00 43.99  ? 36  ILE H N   1 
ATOM   8253 C  CA  . ILE H  4  36  ? 19.653 50.795  30.240  1.00 44.61  ? 36  ILE H CA  1 
ATOM   8254 C  C   . ILE H  4  36  ? 18.486 51.761  30.503  1.00 45.32  ? 36  ILE H C   1 
ATOM   8255 O  O   . ILE H  4  36  ? 18.707 52.869  30.993  1.00 45.21  ? 36  ILE H O   1 
ATOM   8256 C  CB  . ILE H  4  36  ? 19.848 50.573  28.724  1.00 43.01  ? 36  ILE H CB  1 
ATOM   8257 C  CG1 . ILE H  4  36  ? 21.292 50.128  28.485  1.00 41.49  ? 36  ILE H CG1 1 
ATOM   8258 C  CG2 . ILE H  4  36  ? 19.539 51.853  27.922  1.00 39.08  ? 36  ILE H CG2 1 
ATOM   8259 C  CD1 . ILE H  4  36  ? 21.613 49.738  27.051  1.00 42.43  ? 36  ILE H CD1 1 
ATOM   8260 N  N   . PHE H  4  37  ? 17.259 51.353  30.192  1.00 46.20  ? 37  PHE H N   1 
ATOM   8261 C  CA  . PHE H  4  37  ? 16.096 52.214  30.419  1.00 47.55  ? 37  PHE H CA  1 
ATOM   8262 C  C   . PHE H  4  37  ? 15.881 52.523  31.908  1.00 47.62  ? 37  PHE H C   1 
ATOM   8263 O  O   . PHE H  4  37  ? 15.492 53.635  32.264  1.00 48.34  ? 37  PHE H O   1 
ATOM   8264 C  CB  . PHE H  4  37  ? 14.846 51.586  29.787  1.00 45.98  ? 37  PHE H CB  1 
ATOM   8265 C  CG  . PHE H  4  37  ? 14.770 51.782  28.302  1.00 46.69  ? 37  PHE H CG  1 
ATOM   8266 C  CD1 . PHE H  4  37  ? 14.347 53.002  27.774  1.00 45.21  ? 37  PHE H CD1 1 
ATOM   8267 C  CD2 . PHE H  4  37  ? 15.194 50.777  27.427  1.00 46.64  ? 37  PHE H CD2 1 
ATOM   8268 C  CE1 . PHE H  4  37  ? 14.347 53.229  26.402  1.00 44.82  ? 37  PHE H CE1 1 
ATOM   8269 C  CE2 . PHE H  4  37  ? 15.199 50.991  26.056  1.00 46.29  ? 37  PHE H CE2 1 
ATOM   8270 C  CZ  . PHE H  4  37  ? 14.774 52.226  25.541  1.00 45.31  ? 37  PHE H CZ  1 
ATOM   8271 N  N   . SER H  4  38  ? 16.152 51.556  32.776  1.00 47.51  ? 38  SER H N   1 
ATOM   8272 C  CA  . SER H  4  38  ? 16.018 51.791  34.204  1.00 48.80  ? 38  SER H CA  1 
ATOM   8273 C  C   . SER H  4  38  ? 16.929 52.968  34.535  1.00 50.09  ? 38  SER H C   1 
ATOM   8274 O  O   . SER H  4  38  ? 16.525 53.914  35.215  1.00 51.04  ? 38  SER H O   1 
ATOM   8275 C  CB  . SER H  4  38  ? 16.450 50.558  35.015  1.00 47.26  ? 38  SER H CB  1 
ATOM   8276 O  OG  . SER H  4  38  ? 15.447 49.552  35.007  1.00 46.08  ? 38  SER H OG  1 
ATOM   8277 N  N   . SER H  4  39  ? 18.157 52.904  34.033  1.00 50.69  ? 39  SER H N   1 
ATOM   8278 C  CA  . SER H  4  39  ? 19.139 53.950  34.263  1.00 52.43  ? 39  SER H CA  1 
ATOM   8279 C  C   . SER H  4  39  ? 18.692 55.280  33.675  1.00 52.70  ? 39  SER H C   1 
ATOM   8280 O  O   . SER H  4  39  ? 18.929 56.343  34.265  1.00 54.20  ? 39  SER H O   1 
ATOM   8281 C  CB  . SER H  4  39  ? 20.487 53.550  33.662  1.00 52.32  ? 39  SER H CB  1 
ATOM   8282 O  OG  . SER H  4  39  ? 21.086 52.520  34.428  1.00 52.97  ? 39  SER H OG  1 
ATOM   8283 N  N   . LEU H  4  40  ? 18.053 55.217  32.510  1.00 51.01  ? 40  LEU H N   1 
ATOM   8284 C  CA  . LEU H  4  40  ? 17.564 56.413  31.840  1.00 51.68  ? 40  LEU H CA  1 
ATOM   8285 C  C   . LEU H  4  40  ? 16.516 57.087  32.694  1.00 52.48  ? 40  LEU H C   1 
ATOM   8286 O  O   . LEU H  4  40  ? 16.588 58.290  32.947  1.00 52.97  ? 40  LEU H O   1 
ATOM   8287 C  CB  . LEU H  4  40  ? 16.935 56.063  30.495  1.00 51.83  ? 40  LEU H CB  1 
ATOM   8288 C  CG  . LEU H  4  40  ? 16.395 57.296  29.754  1.00 49.22  ? 40  LEU H CG  1 
ATOM   8289 C  CD1 . LEU H  4  40  ? 17.556 58.132  29.216  1.00 50.00  ? 40  LEU H CD1 1 
ATOM   8290 C  CD2 . LEU H  4  40  ? 15.500 56.854  28.623  1.00 47.88  ? 40  LEU H CD2 1 
ATOM   8291 N  N   . PHE H  4  41  ? 15.531 56.291  33.116  1.00 51.93  ? 41  PHE H N   1 
ATOM   8292 C  CA  . PHE H  4  41  ? 14.426 56.752  33.954  1.00 50.83  ? 41  PHE H CA  1 
ATOM   8293 C  C   . PHE H  4  41  ? 14.947 57.374  35.232  1.00 51.50  ? 41  PHE H C   1 
ATOM   8294 O  O   . PHE H  4  41  ? 14.451 58.424  35.652  1.00 51.08  ? 41  PHE H O   1 
ATOM   8295 C  CB  . PHE H  4  41  ? 13.511 55.570  34.253  1.00 48.01  ? 41  PHE H CB  1 
ATOM   8296 C  CG  . PHE H  4  41  ? 12.825 55.025  33.032  1.00 45.50  ? 41  PHE H CG  1 
ATOM   8297 C  CD1 . PHE H  4  41  ? 12.373 53.707  33.000  1.00 44.14  ? 41  PHE H CD1 1 
ATOM   8298 C  CD2 . PHE H  4  41  ? 12.654 55.831  31.903  1.00 45.05  ? 41  PHE H CD2 1 
ATOM   8299 C  CE1 . PHE H  4  41  ? 11.769 53.195  31.860  1.00 44.79  ? 41  PHE H CE1 1 
ATOM   8300 C  CE2 . PHE H  4  41  ? 12.053 55.337  30.765  1.00 44.79  ? 41  PHE H CE2 1 
ATOM   8301 C  CZ  . PHE H  4  41  ? 11.608 54.007  30.738  1.00 44.39  ? 41  PHE H CZ  1 
ATOM   8302 N  N   . LYS H  4  42  ? 15.944 56.734  35.842  1.00 51.72  ? 42  LYS H N   1 
ATOM   8303 C  CA  . LYS H  4  42  ? 16.542 57.255  37.065  1.00 54.63  ? 42  LYS H CA  1 
ATOM   8304 C  C   . LYS H  4  42  ? 17.048 58.673  36.849  1.00 55.28  ? 42  LYS H C   1 
ATOM   8305 O  O   . LYS H  4  42  ? 16.762 59.571  37.641  1.00 55.63  ? 42  LYS H O   1 
ATOM   8306 C  CB  . LYS H  4  42  ? 17.723 56.381  37.508  1.00 56.96  ? 42  LYS H CB  1 
ATOM   8307 C  CG  . LYS H  4  42  ? 17.345 55.262  38.451  1.00 58.69  ? 42  LYS H CG  1 
ATOM   8308 C  CD  . LYS H  4  42  ? 17.968 55.507  39.815  1.00 61.33  ? 42  LYS H CD  1 
ATOM   8309 C  CE  . LYS H  4  42  ? 19.172 54.604  40.049  1.00 62.39  ? 42  LYS H CE  1 
ATOM   8310 N  NZ  . LYS H  4  42  ? 20.250 55.304  40.806  1.00 61.67  ? 42  LYS H NZ  1 
ATOM   8311 N  N   . LEU H  4  43  ? 17.796 58.871  35.767  1.00 55.61  ? 43  LEU H N   1 
ATOM   8312 C  CA  . LEU H  4  43  ? 18.338 60.187  35.454  1.00 56.71  ? 43  LEU H CA  1 
ATOM   8313 C  C   . LEU H  4  43  ? 17.285 61.186  35.001  1.00 56.23  ? 43  LEU H C   1 
ATOM   8314 O  O   . LEU H  4  43  ? 17.409 62.380  35.240  1.00 56.45  ? 43  LEU H O   1 
ATOM   8315 C  CB  . LEU H  4  43  ? 19.421 60.070  34.373  1.00 57.85  ? 43  LEU H CB  1 
ATOM   8316 C  CG  . LEU H  4  43  ? 20.737 59.390  34.749  1.00 58.98  ? 43  LEU H CG  1 
ATOM   8317 C  CD1 . LEU H  4  43  ? 21.669 59.375  33.545  1.00 57.11  ? 43  LEU H CD1 1 
ATOM   8318 C  CD2 . LEU H  4  43  ? 21.387 60.126  35.906  1.00 59.62  ? 43  LEU H CD2 1 
ATOM   8319 N  N   . LYS H  4  44  ? 16.252 60.696  34.334  1.00 56.83  ? 44  LYS H N   1 
ATOM   8320 C  CA  . LYS H  4  44  ? 15.197 61.573  33.845  1.00 58.47  ? 44  LYS H CA  1 
ATOM   8321 C  C   . LYS H  4  44  ? 13.862 60.889  34.114  1.00 58.55  ? 44  LYS H C   1 
ATOM   8322 O  O   . LYS H  4  44  ? 13.223 60.373  33.201  1.00 57.84  ? 44  LYS H O   1 
ATOM   8323 C  CB  . LYS H  4  44  ? 15.396 61.830  32.341  1.00 57.93  ? 44  LYS H CB  1 
ATOM   8324 C  CG  . LYS H  4  44  ? 16.650 62.646  31.995  1.00 56.63  ? 44  LYS H CG  1 
ATOM   8325 C  CD  . LYS H  4  44  ? 16.549 64.105  32.471  1.00 57.05  ? 44  LYS H CD  1 
ATOM   8326 C  CE  . LYS H  4  44  ? 17.714 64.950  31.953  1.00 56.96  ? 44  LYS H CE  1 
ATOM   8327 N  NZ  . LYS H  4  44  ? 17.575 66.405  32.198  1.00 55.40  ? 44  LYS H NZ  1 
ATOM   8328 N  N   . PRO H  4  45  ? 13.425 60.885  35.383  1.00 59.46  ? 45  PRO H N   1 
ATOM   8329 C  CA  . PRO H  4  45  ? 12.157 60.254  35.786  1.00 58.64  ? 45  PRO H CA  1 
ATOM   8330 C  C   . PRO H  4  45  ? 10.985 60.670  34.917  1.00 58.88  ? 45  PRO H C   1 
ATOM   8331 O  O   . PRO H  4  45  ? 10.076 59.879  34.661  1.00 56.29  ? 45  PRO H O   1 
ATOM   8332 C  CB  . PRO H  4  45  ? 11.978 60.715  37.231  1.00 57.12  ? 45  PRO H CB  1 
ATOM   8333 C  CG  . PRO H  4  45  ? 13.394 60.903  37.699  1.00 57.99  ? 45  PRO H CG  1 
ATOM   8334 C  CD  . PRO H  4  45  ? 14.029 61.602  36.520  1.00 57.99  ? 45  PRO H CD  1 
ATOM   8335 N  N   . GLU H  4  46  ? 11.021 61.917  34.462  1.00 60.11  ? 46  GLU H N   1 
ATOM   8336 C  CA  . GLU H  4  46  ? 9.942  62.466  33.656  1.00 61.87  ? 46  GLU H CA  1 
ATOM   8337 C  C   . GLU H  4  46  ? 9.748  61.745  32.330  1.00 60.68  ? 46  GLU H C   1 
ATOM   8338 O  O   . GLU H  4  46  ? 8.642  61.720  31.798  1.00 61.75  ? 46  GLU H O   1 
ATOM   8339 C  CB  . GLU H  4  46  ? 10.190 63.955  33.405  1.00 65.81  ? 46  GLU H CB  1 
ATOM   8340 C  CG  . GLU H  4  46  ? 11.400 64.224  32.506  1.00 72.29  ? 46  GLU H CG  1 
ATOM   8341 C  CD  . GLU H  4  46  ? 12.545 64.960  33.209  1.00 75.26  ? 46  GLU H CD  1 
ATOM   8342 O  OE1 . GLU H  4  46  ? 13.101 64.431  34.204  1.00 74.53  ? 46  GLU H OE1 1 
ATOM   8343 O  OE2 . GLU H  4  46  ? 12.892 66.073  32.746  1.00 77.41  ? 46  GLU H OE2 1 
ATOM   8344 N  N   . SER H  4  47  ? 10.813 61.148  31.800  1.00 59.48  ? 47  SER H N   1 
ATOM   8345 C  CA  . SER H  4  47  ? 10.733 60.440  30.519  1.00 58.03  ? 47  SER H CA  1 
ATOM   8346 C  C   . SER H  4  47  ? 9.957  59.112  30.556  1.00 56.46  ? 47  SER H C   1 
ATOM   8347 O  O   . SER H  4  47  ? 9.318  58.721  29.586  1.00 56.34  ? 47  SER H O   1 
ATOM   8348 C  CB  . SER H  4  47  ? 12.142 60.172  29.972  1.00 57.20  ? 47  SER H CB  1 
ATOM   8349 O  OG  . SER H  4  47  ? 12.777 59.144  30.713  1.00 58.38  ? 47  SER H OG  1 
ATOM   8350 N  N   . GLU H  4  48  ? 10.009 58.423  31.680  1.00 56.61  ? 48  GLU H N   1 
ATOM   8351 C  CA  . GLU H  4  48  ? 9.331  57.144  31.819  1.00 57.99  ? 48  GLU H CA  1 
ATOM   8352 C  C   . GLU H  4  48  ? 7.925  57.085  31.227  1.00 58.73  ? 48  GLU H C   1 
ATOM   8353 O  O   . GLU H  4  48  ? 7.620  56.169  30.476  1.00 60.13  ? 48  GLU H O   1 
ATOM   8354 C  CB  . GLU H  4  48  ? 9.301  56.727  33.303  1.00 57.55  ? 48  GLU H CB  1 
ATOM   8355 C  CG  . GLU H  4  48  ? 8.768  55.311  33.565  1.00 56.91  ? 48  GLU H CG  1 
ATOM   8356 C  CD  . GLU H  4  48  ? 9.091  54.805  34.976  1.00 58.16  ? 48  GLU H CD  1 
ATOM   8357 O  OE1 . GLU H  4  48  ? 8.583  53.728  35.369  1.00 57.20  ? 48  GLU H OE1 1 
ATOM   8358 O  OE2 . GLU H  4  48  ? 9.863  55.482  35.698  1.00 58.26  ? 48  GLU H OE2 1 
ATOM   8359 N  N   . VAL H  4  49  ? 7.066  58.047  31.547  1.00 59.83  ? 49  VAL H N   1 
ATOM   8360 C  CA  . VAL H  4  49  ? 5.697  58.010  31.018  1.00 60.10  ? 49  VAL H CA  1 
ATOM   8361 C  C   . VAL H  4  49  ? 5.612  57.891  29.505  1.00 58.71  ? 49  VAL H C   1 
ATOM   8362 O  O   . VAL H  4  49  ? 4.614  57.411  28.983  1.00 58.20  ? 49  VAL H O   1 
ATOM   8363 C  CB  . VAL H  4  49  ? 4.847  59.247  31.454  1.00 60.08  ? 49  VAL H CB  1 
ATOM   8364 C  CG1 . VAL H  4  49  ? 4.432  59.093  32.888  1.00 60.12  ? 49  VAL H CG1 1 
ATOM   8365 C  CG2 . VAL H  4  49  ? 5.641  60.549  31.268  1.00 61.81  ? 49  VAL H CG2 1 
ATOM   8366 N  N   . LEU H  4  50  ? 6.649  58.320  28.798  1.00 58.93  ? 50  LEU H N   1 
ATOM   8367 C  CA  . LEU H  4  50  ? 6.628  58.246  27.343  1.00 59.56  ? 50  LEU H CA  1 
ATOM   8368 C  C   . LEU H  4  50  ? 6.514  56.818  26.838  1.00 59.42  ? 50  LEU H C   1 
ATOM   8369 O  O   . LEU H  4  50  ? 6.206  56.609  25.670  1.00 58.95  ? 50  LEU H O   1 
ATOM   8370 C  CB  . LEU H  4  50  ? 7.890  58.878  26.764  1.00 60.55  ? 50  LEU H CB  1 
ATOM   8371 C  CG  . LEU H  4  50  ? 8.048  60.383  26.962  1.00 62.05  ? 50  LEU H CG  1 
ATOM   8372 C  CD1 . LEU H  4  50  ? 9.460  60.780  26.616  1.00 63.18  ? 50  LEU H CD1 1 
ATOM   8373 C  CD2 . LEU H  4  50  ? 7.043  61.137  26.101  1.00 62.70  ? 50  LEU H CD2 1 
ATOM   8374 N  N   . PHE H  4  51  ? 6.750  55.844  27.724  1.00 60.61  ? 51  PHE H N   1 
ATOM   8375 C  CA  . PHE H  4  51  ? 6.710  54.424  27.359  1.00 61.91  ? 51  PHE H CA  1 
ATOM   8376 C  C   . PHE H  4  51  ? 5.514  53.627  27.874  1.00 63.31  ? 51  PHE H C   1 
ATOM   8377 O  O   . PHE H  4  51  ? 5.596  52.407  28.020  1.00 62.02  ? 51  PHE H O   1 
ATOM   8378 C  CB  . PHE H  4  51  ? 8.000  53.718  27.820  1.00 59.92  ? 51  PHE H CB  1 
ATOM   8379 C  CG  . PHE H  4  51  ? 9.254  54.375  27.327  1.00 59.98  ? 51  PHE H CG  1 
ATOM   8380 C  CD1 . PHE H  4  51  ? 9.826  55.430  28.034  1.00 59.81  ? 51  PHE H CD1 1 
ATOM   8381 C  CD2 . PHE H  4  51  ? 9.833  53.985  26.121  1.00 59.98  ? 51  PHE H CD2 1 
ATOM   8382 C  CE1 . PHE H  4  51  ? 10.949 56.088  27.554  1.00 59.62  ? 51  PHE H CE1 1 
ATOM   8383 C  CE2 . PHE H  4  51  ? 10.954 54.635  25.629  1.00 59.85  ? 51  PHE H CE2 1 
ATOM   8384 C  CZ  . PHE H  4  51  ? 11.514 55.693  26.350  1.00 59.79  ? 51  PHE H CZ  1 
ATOM   8385 N  N   . ASN H  4  52  ? 4.397  54.295  28.135  1.00 65.74  ? 52  ASN H N   1 
ATOM   8386 C  CA  . ASN H  4  52  ? 3.234  53.578  28.635  1.00 68.27  ? 52  ASN H CA  1 
ATOM   8387 C  C   . ASN H  4  52  ? 2.631  52.715  27.543  1.00 68.31  ? 52  ASN H C   1 
ATOM   8388 O  O   . ASN H  4  52  ? 1.894  51.773  27.821  1.00 69.19  ? 52  ASN H O   1 
ATOM   8389 C  CB  . ASN H  4  52  ? 2.186  54.554  29.177  1.00 70.53  ? 52  ASN H CB  1 
ATOM   8390 C  CG  . ASN H  4  52  ? 2.636  55.228  30.456  1.00 73.92  ? 52  ASN H CG  1 
ATOM   8391 O  OD1 . ASN H  4  52  ? 3.023  54.565  31.420  1.00 74.10  ? 52  ASN H OD1 1 
ATOM   8392 N  ND2 . ASN H  4  52  ? 2.589  56.553  30.472  1.00 76.45  ? 52  ASN H ND2 1 
ATOM   8393 N  N   . ASN H  4  53  ? 2.946  53.031  26.295  1.00 67.74  ? 53  ASN H N   1 
ATOM   8394 C  CA  . ASN H  4  53  ? 2.413  52.251  25.188  1.00 67.75  ? 53  ASN H CA  1 
ATOM   8395 C  C   . ASN H  4  53  ? 3.052  50.876  25.102  1.00 66.69  ? 53  ASN H C   1 
ATOM   8396 O  O   . ASN H  4  53  ? 2.453  49.948  24.566  1.00 65.77  ? 53  ASN H O   1 
ATOM   8397 C  CB  . ASN H  4  53  ? 2.605  53.005  23.869  1.00 70.70  ? 53  ASN H CB  1 
ATOM   8398 C  CG  . ASN H  4  53  ? 1.337  53.702  23.413  1.00 72.79  ? 53  ASN H CG  1 
ATOM   8399 O  OD1 . ASN H  4  53  ? 0.618  54.300  24.220  1.00 74.36  ? 53  ASN H OD1 1 
ATOM   8400 N  ND2 . ASN H  4  53  ? 1.055  53.635  22.115  1.00 74.38  ? 53  ASN H ND2 1 
ATOM   8401 N  N   . VAL H  4  54  ? 4.263  50.747  25.634  1.00 65.90  ? 54  VAL H N   1 
ATOM   8402 C  CA  . VAL H  4  54  ? 4.974  49.476  25.604  1.00 63.97  ? 54  VAL H CA  1 
ATOM   8403 C  C   . VAL H  4  54  ? 4.931  48.799  26.964  1.00 63.24  ? 54  VAL H C   1 
ATOM   8404 O  O   . VAL H  4  54  ? 5.730  47.904  27.245  1.00 62.92  ? 54  VAL H O   1 
ATOM   8405 C  CB  . VAL H  4  54  ? 6.445  49.663  25.145  1.00 63.91  ? 54  VAL H CB  1 
ATOM   8406 C  CG1 . VAL H  4  54  ? 6.463  50.071  23.699  1.00 62.93  ? 54  VAL H CG1 1 
ATOM   8407 C  CG2 . VAL H  4  54  ? 7.153  50.715  25.985  1.00 63.32  ? 54  VAL H CG2 1 
ATOM   8408 N  N   . ASN H  4  55  ? 3.986  49.237  27.794  1.00 62.07  ? 55  ASN H N   1 
ATOM   8409 C  CA  . ASN H  4  55  ? 3.780  48.691  29.137  1.00 62.49  ? 55  ASN H CA  1 
ATOM   8410 C  C   . ASN H  4  55  ? 5.030  48.851  30.015  1.00 61.65  ? 55  ASN H C   1 
ATOM   8411 O  O   . ASN H  4  55  ? 5.521  47.886  30.600  1.00 59.77  ? 55  ASN H O   1 
ATOM   8412 C  CB  . ASN H  4  55  ? 3.370  47.209  29.021  1.00 63.62  ? 55  ASN H CB  1 
ATOM   8413 C  CG  . ASN H  4  55  ? 2.835  46.629  30.331  1.00 63.21  ? 55  ASN H CG  1 
ATOM   8414 O  OD1 . ASN H  4  55  ? 3.045  47.180  31.405  1.00 65.82  ? 55  ASN H OD1 1 
ATOM   8415 N  ND2 . ASN H  4  55  ? 2.158  45.498  30.234  1.00 61.85  ? 55  ASN H ND2 1 
ATOM   8416 N  N   . VAL H  4  56  ? 5.541  50.075  30.096  1.00 62.30  ? 56  VAL H N   1 
ATOM   8417 C  CA  . VAL H  4  56  ? 6.722  50.355  30.905  1.00 62.65  ? 56  VAL H CA  1 
ATOM   8418 C  C   . VAL H  4  56  ? 6.373  50.105  32.363  1.00 63.79  ? 56  VAL H C   1 
ATOM   8419 O  O   . VAL H  4  56  ? 7.260  50.007  33.208  1.00 63.11  ? 56  VAL H O   1 
ATOM   8420 C  CB  . VAL H  4  56  ? 7.181  51.821  30.742  1.00 61.41  ? 56  VAL H CB  1 
ATOM   8421 C  CG1 . VAL H  4  56  ? 6.067  52.760  31.129  1.00 60.89  ? 56  VAL H CG1 1 
ATOM   8422 C  CG2 . VAL H  4  56  ? 8.404  52.084  31.580  1.00 60.44  ? 56  VAL H CG2 1 
ATOM   8423 N  N   . ALA H  4  57  ? 5.074  50.009  32.644  1.00 65.33  ? 57  ALA H N   1 
ATOM   8424 C  CA  . ALA H  4  57  ? 4.574  49.766  33.994  1.00 67.07  ? 57  ALA H CA  1 
ATOM   8425 C  C   . ALA H  4  57  ? 5.167  48.455  34.511  1.00 68.28  ? 57  ALA H C   1 
ATOM   8426 O  O   . ALA H  4  57  ? 5.557  48.341  35.681  1.00 67.75  ? 57  ALA H O   1 
ATOM   8427 C  CB  . ALA H  4  57  ? 3.052  49.687  33.976  1.00 66.57  ? 57  ALA H CB  1 
ATOM   8428 N  N   . ASN H  4  58  ? 5.216  47.462  33.631  1.00 69.32  ? 58  ASN H N   1 
ATOM   8429 C  CA  . ASN H  4  58  ? 5.801  46.169  33.963  1.00 71.39  ? 58  ASN H CA  1 
ATOM   8430 C  C   . ASN H  4  58  ? 6.914  45.931  32.952  1.00 69.41  ? 58  ASN H C   1 
ATOM   8431 O  O   . ASN H  4  58  ? 6.662  45.421  31.852  1.00 68.85  ? 58  ASN H O   1 
ATOM   8432 C  CB  . ASN H  4  58  ? 4.776  45.042  33.853  1.00 77.50  ? 58  ASN H CB  1 
ATOM   8433 C  CG  . ASN H  4  58  ? 5.341  43.711  34.308  1.00 85.31  ? 58  ASN H CG  1 
ATOM   8434 O  OD1 . ASN H  4  58  ? 6.488  43.655  34.751  1.00 84.79  ? 58  ASN H OD1 1 
ATOM   8435 N  ND2 . ASN H  4  58  ? 4.548  42.646  34.209  1.00 95.17  ? 58  ASN H ND2 1 
ATOM   8436 N  N   . MET H  4  59  ? 8.139  46.300  33.332  1.00 65.57  ? 59  MET H N   1 
ATOM   8437 C  CA  . MET H  4  59  ? 9.292  46.167  32.454  1.00 63.20  ? 59  MET H CA  1 
ATOM   8438 C  C   . MET H  4  59  ? 9.688  44.755  32.101  1.00 60.88  ? 59  MET H C   1 
ATOM   8439 O  O   . MET H  4  59  ? 10.529 44.549  31.238  1.00 59.22  ? 59  MET H O   1 
ATOM   8440 C  CB  . MET H  4  59  ? 10.487 46.927  33.032  1.00 62.78  ? 59  MET H CB  1 
ATOM   8441 C  CG  . MET H  4  59  ? 10.363 48.417  32.776  1.00 64.71  ? 59  MET H CG  1 
ATOM   8442 S  SD  . MET H  4  59  ? 11.699 49.422  33.403  1.00 67.50  ? 59  MET H SD  1 
ATOM   8443 C  CE  . MET H  4  59  ? 13.020 48.198  33.526  1.00 67.17  ? 59  MET H CE  1 
ATOM   8444 N  N   . SER H  4  60  ? 9.092  43.772  32.756  1.00 59.64  ? 60  SER H N   1 
ATOM   8445 C  CA  . SER H  4  60  ? 9.414  42.399  32.424  1.00 59.61  ? 60  SER H CA  1 
ATOM   8446 C  C   . SER H  4  60  ? 8.262  41.808  31.610  1.00 59.52  ? 60  SER H C   1 
ATOM   8447 O  O   . SER H  4  60  ? 8.060  40.594  31.563  1.00 59.50  ? 60  SER H O   1 
ATOM   8448 C  CB  . SER H  4  60  ? 9.687  41.582  33.698  1.00 59.63  ? 60  SER H CB  1 
ATOM   8449 O  OG  . SER H  4  60  ? 8.706  41.791  34.688  1.00 62.71  ? 60  SER H OG  1 
ATOM   8450 N  N   . SER H  4  61  ? 7.515  42.694  30.954  1.00 58.45  ? 61  SER H N   1 
ATOM   8451 C  CA  . SER H  4  61  ? 6.394  42.290  30.122  1.00 58.34  ? 61  SER H CA  1 
ATOM   8452 C  C   . SER H  4  61  ? 6.803  42.067  28.665  1.00 57.18  ? 61  SER H C   1 
ATOM   8453 O  O   . SER H  4  61  ? 7.735  42.688  28.177  1.00 57.94  ? 61  SER H O   1 
ATOM   8454 C  CB  . SER H  4  61  ? 5.291  43.355  30.176  1.00 59.52  ? 61  SER H CB  1 
ATOM   8455 O  OG  . SER H  4  61  ? 5.627  44.516  29.436  1.00 59.45  ? 61  SER H OG  1 
ATOM   8456 N  N   . GLY H  4  62  ? 6.095  41.181  27.973  1.00 56.70  ? 62  GLY H N   1 
ATOM   8457 C  CA  . GLY H  4  62  ? 6.405  40.912  26.584  1.00 56.77  ? 62  GLY H CA  1 
ATOM   8458 C  C   . GLY H  4  62  ? 6.464  42.188  25.765  1.00 56.92  ? 62  GLY H C   1 
ATOM   8459 O  O   . GLY H  4  62  ? 7.333  42.346  24.905  1.00 58.78  ? 62  GLY H O   1 
ATOM   8460 N  N   . ALA H  4  63  ? 5.549  43.109  26.032  1.00 55.09  ? 63  ALA H N   1 
ATOM   8461 C  CA  . ALA H  4  63  ? 5.516  44.365  25.304  1.00 54.25  ? 63  ALA H CA  1 
ATOM   8462 C  C   . ALA H  4  63  ? 6.765  45.222  25.533  1.00 53.75  ? 63  ALA H C   1 
ATOM   8463 O  O   . ALA H  4  63  ? 7.281  45.839  24.590  1.00 52.74  ? 63  ALA H O   1 
ATOM   8464 C  CB  . ALA H  4  63  ? 4.268  45.155  25.685  1.00 53.65  ? 63  ALA H CB  1 
ATOM   8465 N  N   . PHE H  4  64  ? 7.262  45.267  26.766  1.00 51.53  ? 64  PHE H N   1 
ATOM   8466 C  CA  . PHE H  4  64  ? 8.435  46.097  27.027  1.00 51.03  ? 64  PHE H CA  1 
ATOM   8467 C  C   . PHE H  4  64  ? 9.707  45.406  26.585  1.00 50.79  ? 64  PHE H C   1 
ATOM   8468 O  O   . PHE H  4  64  ? 10.709 46.052  26.260  1.00 52.30  ? 64  PHE H O   1 
ATOM   8469 C  CB  . PHE H  4  64  ? 8.550  46.471  28.514  1.00 45.99  ? 64  PHE H CB  1 
ATOM   8470 C  CG  . PHE H  4  64  ? 9.453  47.651  28.754  1.00 41.72  ? 64  PHE H CG  1 
ATOM   8471 C  CD1 . PHE H  4  64  ? 9.110  48.913  28.243  1.00 39.39  ? 64  PHE H CD1 1 
ATOM   8472 C  CD2 . PHE H  4  64  ? 10.665 47.504  29.413  1.00 38.59  ? 64  PHE H CD2 1 
ATOM   8473 C  CE1 . PHE H  4  64  ? 9.965  50.014  28.382  1.00 35.04  ? 64  PHE H CE1 1 
ATOM   8474 C  CE2 . PHE H  4  64  ? 11.524 48.593  29.557  1.00 37.56  ? 64  PHE H CE2 1 
ATOM   8475 C  CZ  . PHE H  4  64  ? 11.169 49.856  29.038  1.00 35.05  ? 64  PHE H CZ  1 
ATOM   8476 N  N   . HIS H  4  65  ? 9.666  44.085  26.605  1.00 50.18  ? 65  HIS H N   1 
ATOM   8477 C  CA  . HIS H  4  65  ? 10.812 43.312  26.217  1.00 51.45  ? 65  HIS H CA  1 
ATOM   8478 C  C   . HIS H  4  65  ? 11.059 43.552  24.741  1.00 50.52  ? 65  HIS H C   1 
ATOM   8479 O  O   . HIS H  4  65  ? 12.178 43.897  24.336  1.00 48.27  ? 65  HIS H O   1 
ATOM   8480 C  CB  . HIS H  4  65  ? 10.559 41.836  26.532  1.00 53.93  ? 65  HIS H CB  1 
ATOM   8481 C  CG  . HIS H  4  65  ? 10.914 41.462  27.938  1.00 58.04  ? 65  HIS H CG  1 
ATOM   8482 N  ND1 . HIS H  4  65  ? 10.651 40.214  28.471  1.00 58.58  ? 65  HIS H ND1 1 
ATOM   8483 C  CD2 . HIS H  4  65  ? 11.561 42.154  28.905  1.00 59.44  ? 65  HIS H CD2 1 
ATOM   8484 C  CE1 . HIS H  4  65  ? 11.126 40.156  29.706  1.00 59.90  ? 65  HIS H CE1 1 
ATOM   8485 N  NE2 . HIS H  4  65  ? 11.684 41.321  29.992  1.00 61.68  ? 65  HIS H NE2 1 
ATOM   8486 N  N   . ALA H  4  66  ? 9.995  43.400  23.951  1.00 49.72  ? 66  ALA H N   1 
ATOM   8487 C  CA  . ALA H  4  66  ? 10.047 43.605  22.510  1.00 48.77  ? 66  ALA H CA  1 
ATOM   8488 C  C   . ALA H  4  66  ? 10.453 45.034  22.180  1.00 48.07  ? 66  ALA H C   1 
ATOM   8489 O  O   . ALA H  4  66  ? 11.077 45.267  21.151  1.00 49.55  ? 66  ALA H O   1 
ATOM   8490 C  CB  . ALA H  4  66  ? 8.709  43.291  21.896  1.00 47.96  ? 66  ALA H CB  1 
ATOM   8491 N  N   . HIS H  4  67  ? 10.114 45.987  23.038  1.00 45.78  ? 67  HIS H N   1 
ATOM   8492 C  CA  . HIS H  4  67  ? 10.500 47.367  22.780  1.00 45.86  ? 67  HIS H CA  1 
ATOM   8493 C  C   . HIS H  4  67  ? 12.006 47.550  22.935  1.00 45.42  ? 67  HIS H C   1 
ATOM   8494 O  O   . HIS H  4  67  ? 12.652 48.134  22.070  1.00 44.76  ? 67  HIS H O   1 
ATOM   8495 C  CB  . HIS H  4  67  ? 9.816  48.337  23.746  1.00 44.66  ? 67  HIS H CB  1 
ATOM   8496 C  CG  . HIS H  4  67  ? 10.352 49.730  23.649  1.00 43.93  ? 67  HIS H CG  1 
ATOM   8497 N  ND1 . HIS H  4  67  ? 10.198 50.503  22.519  1.00 43.54  ? 67  HIS H ND1 1 
ATOM   8498 C  CD2 . HIS H  4  67  ? 11.114 50.457  24.505  1.00 42.90  ? 67  HIS H CD2 1 
ATOM   8499 C  CE1 . HIS H  4  67  ? 10.843 51.647  22.677  1.00 42.69  ? 67  HIS H CE1 1 
ATOM   8500 N  NE2 . HIS H  4  67  ? 11.408 51.645  23.875  1.00 42.77  ? 67  HIS H NE2 1 
ATOM   8501 N  N   . THR H  4  68  ? 12.559 47.082  24.051  1.00 45.50  ? 68  THR H N   1 
ATOM   8502 C  CA  . THR H  4  68  ? 13.985 47.224  24.275  1.00 47.35  ? 68  THR H CA  1 
ATOM   8503 C  C   . THR H  4  68  ? 14.749 46.458  23.204  1.00 48.38  ? 68  THR H C   1 
ATOM   8504 O  O   . THR H  4  68  ? 15.811 46.901  22.767  1.00 50.39  ? 68  THR H O   1 
ATOM   8505 C  CB  . THR H  4  68  ? 14.390 46.732  25.683  1.00 47.12  ? 68  THR H CB  1 
ATOM   8506 O  OG1 . THR H  4  68  ? 13.949 45.386  25.879  1.00 47.98  ? 68  THR H OG1 1 
ATOM   8507 C  CG2 . THR H  4  68  ? 13.752 47.610  26.745  1.00 49.46  ? 68  THR H CG2 1 
ATOM   8508 N  N   . VAL H  4  69  ? 14.194 45.339  22.748  1.00 48.30  ? 69  VAL H N   1 
ATOM   8509 C  CA  . VAL H  4  69  ? 14.855 44.540  21.723  1.00 48.67  ? 69  VAL H CA  1 
ATOM   8510 C  C   . VAL H  4  69  ? 14.924 45.268  20.378  1.00 49.76  ? 69  VAL H C   1 
ATOM   8511 O  O   . VAL H  4  69  ? 15.922 45.131  19.643  1.00 51.72  ? 69  VAL H O   1 
ATOM   8512 C  CB  . VAL H  4  69  ? 14.164 43.154  21.549  1.00 47.87  ? 69  VAL H CB  1 
ATOM   8513 C  CG1 . VAL H  4  69  ? 14.595 42.509  20.252  1.00 47.48  ? 69  VAL H CG1 1 
ATOM   8514 C  CG2 . VAL H  4  69  ? 14.554 42.237  22.711  1.00 45.95  ? 69  VAL H CG2 1 
ATOM   8515 N  N   . ARG H  4  70  ? 13.893 46.044  20.052  1.00 47.05  ? 70  ARG H N   1 
ATOM   8516 C  CA  . ARG H  4  70  ? 13.939 46.760  18.800  1.00 47.40  ? 70  ARG H CA  1 
ATOM   8517 C  C   . ARG H  4  70  ? 14.775 48.021  18.955  1.00 45.81  ? 70  ARG H C   1 
ATOM   8518 O  O   . ARG H  4  70  ? 15.319 48.520  17.972  1.00 46.81  ? 70  ARG H O   1 
ATOM   8519 C  CB  . ARG H  4  70  ? 12.530 47.068  18.265  1.00 48.69  ? 70  ARG H CB  1 
ATOM   8520 C  CG  . ARG H  4  70  ? 11.682 47.984  19.067  1.00 52.72  ? 70  ARG H CG  1 
ATOM   8521 C  CD  . ARG H  4  70  ? 10.341 48.176  18.355  1.00 56.84  ? 70  ARG H CD  1 
ATOM   8522 N  NE  . ARG H  4  70  ? 9.445  47.041  18.517  1.00 58.45  ? 70  ARG H NE  1 
ATOM   8523 C  CZ  . ARG H  4  70  ? 8.526  46.951  19.473  1.00 58.53  ? 70  ARG H CZ  1 
ATOM   8524 N  NH1 . ARG H  4  70  ? 8.382  47.934  20.350  1.00 60.22  ? 70  ARG H NH1 1 
ATOM   8525 N  NH2 . ARG H  4  70  ? 7.772  45.862  19.569  1.00 57.13  ? 70  ARG H NH2 1 
ATOM   8526 N  N   . VAL H  4  71  ? 14.910 48.510  20.187  1.00 42.56  ? 71  VAL H N   1 
ATOM   8527 C  CA  . VAL H  4  71  ? 15.726 49.691  20.420  1.00 41.33  ? 71  VAL H CA  1 
ATOM   8528 C  C   . VAL H  4  71  ? 17.177 49.276  20.212  1.00 41.78  ? 71  VAL H C   1 
ATOM   8529 O  O   . VAL H  4  71  ? 17.934 49.912  19.470  1.00 39.08  ? 71  VAL H O   1 
ATOM   8530 C  CB  . VAL H  4  71  ? 15.589 50.239  21.865  1.00 42.78  ? 71  VAL H CB  1 
ATOM   8531 C  CG1 . VAL H  4  71  ? 16.596 51.379  22.079  1.00 39.51  ? 71  VAL H CG1 1 
ATOM   8532 C  CG2 . VAL H  4  71  ? 14.177 50.724  22.123  1.00 41.24  ? 71  VAL H CG2 1 
ATOM   8533 N  N   . LEU H  4  72  ? 17.554 48.185  20.869  1.00 41.76  ? 72  LEU H N   1 
ATOM   8534 C  CA  . LEU H  4  72  ? 18.915 47.691  20.773  1.00 41.84  ? 72  LEU H CA  1 
ATOM   8535 C  C   . LEU H  4  72  ? 19.245 47.285  19.354  1.00 41.77  ? 72  LEU H C   1 
ATOM   8536 O  O   . LEU H  4  72  ? 20.378 47.429  18.907  1.00 41.32  ? 72  LEU H O   1 
ATOM   8537 C  CB  . LEU H  4  72  ? 19.110 46.517  21.714  1.00 39.23  ? 72  LEU H CB  1 
ATOM   8538 C  CG  . LEU H  4  72  ? 19.090 46.891  23.196  1.00 39.56  ? 72  LEU H CG  1 
ATOM   8539 C  CD1 . LEU H  4  72  ? 19.144 45.601  23.959  1.00 41.34  ? 72  LEU H CD1 1 
ATOM   8540 C  CD2 . LEU H  4  72  ? 20.262 47.817  23.595  1.00 37.04  ? 72  LEU H CD2 1 
ATOM   8541 N  N   . SER H  4  73  ? 18.247 46.779  18.647  1.00 41.13  ? 73  SER H N   1 
ATOM   8542 C  CA  . SER H  4  73  ? 18.458 46.382  17.273  1.00 41.50  ? 73  SER H CA  1 
ATOM   8543 C  C   . SER H  4  73  ? 18.751 47.652  16.464  1.00 41.41  ? 73  SER H C   1 
ATOM   8544 O  O   . SER H  4  73  ? 19.588 47.649  15.544  1.00 41.41  ? 73  SER H O   1 
ATOM   8545 C  CB  . SER H  4  73  ? 17.217 45.664  16.746  1.00 42.86  ? 73  SER H CB  1 
ATOM   8546 O  OG  . SER H  4  73  ? 17.375 45.334  15.379  1.00 45.00  ? 73  SER H OG  1 
ATOM   8547 N  N   . GLY H  4  74  ? 18.078 48.745  16.827  1.00 38.46  ? 74  GLY H N   1 
ATOM   8548 C  CA  . GLY H  4  74  ? 18.308 50.002  16.135  1.00 36.94  ? 74  GLY H CA  1 
ATOM   8549 C  C   . GLY H  4  74  ? 19.709 50.558  16.375  1.00 36.65  ? 74  GLY H C   1 
ATOM   8550 O  O   . GLY H  4  74  ? 20.331 51.132  15.489  1.00 35.61  ? 74  GLY H O   1 
ATOM   8551 N  N   . LEU H  4  75  ? 20.205 50.386  17.589  1.00 37.12  ? 75  LEU H N   1 
ATOM   8552 C  CA  . LEU H  4  75  ? 21.521 50.883  17.956  1.00 39.20  ? 75  LEU H CA  1 
ATOM   8553 C  C   . LEU H  4  75  ? 22.561 50.043  17.235  1.00 41.20  ? 75  LEU H C   1 
ATOM   8554 O  O   . LEU H  4  75  ? 23.586 50.548  16.772  1.00 39.51  ? 75  LEU H O   1 
ATOM   8555 C  CB  . LEU H  4  75  ? 21.707 50.781  19.478  1.00 37.30  ? 75  LEU H CB  1 
ATOM   8556 C  CG  . LEU H  4  75  ? 23.048 51.208  20.086  1.00 37.34  ? 75  LEU H CG  1 
ATOM   8557 C  CD1 . LEU H  4  75  ? 23.430 52.583  19.561  1.00 36.48  ? 75  LEU H CD1 1 
ATOM   8558 C  CD2 . LEU H  4  75  ? 22.949 51.253  21.610  1.00 37.33  ? 75  LEU H CD2 1 
ATOM   8559 N  N   . ASP H  4  76  ? 22.253 48.757  17.125  1.00 43.69  ? 76  ASP H N   1 
ATOM   8560 C  CA  . ASP H  4  76  ? 23.126 47.803  16.470  1.00 46.76  ? 76  ASP H CA  1 
ATOM   8561 C  C   . ASP H  4  76  ? 23.268 48.109  14.991  1.00 46.04  ? 76  ASP H C   1 
ATOM   8562 O  O   . ASP H  4  76  ? 24.361 48.012  14.417  1.00 45.28  ? 76  ASP H O   1 
ATOM   8563 C  CB  . ASP H  4  76  ? 22.577 46.384  16.632  1.00 48.10  ? 76  ASP H CB  1 
ATOM   8564 C  CG  . ASP H  4  76  ? 23.293 45.399  15.749  1.00 47.10  ? 76  ASP H CG  1 
ATOM   8565 O  OD1 . ASP H  4  76  ? 22.772 45.079  14.659  1.00 46.05  ? 76  ASP H OD1 1 
ATOM   8566 O  OD2 . ASP H  4  76  ? 24.389 44.978  16.167  1.00 51.59  ? 76  ASP H OD2 1 
ATOM   8567 N  N   . MET H  4  77  ? 22.150 48.462  14.384  1.00 45.48  ? 77  MET H N   1 
ATOM   8568 C  CA  . MET H  4  77  ? 22.116 48.801  12.970  1.00 46.67  ? 77  MET H CA  1 
ATOM   8569 C  C   . MET H  4  77  ? 22.986 50.050  12.774  1.00 46.43  ? 77  MET H C   1 
ATOM   8570 O  O   . MET H  4  77  ? 23.846 50.116  11.883  1.00 46.75  ? 77  MET H O   1 
ATOM   8571 C  CB  . MET H  4  77  ? 20.678 49.090  12.597  1.00 48.91  ? 77  MET H CB  1 
ATOM   8572 C  CG  . MET H  4  77  ? 20.288 48.747  11.214  1.00 52.49  ? 77  MET H CG  1 
ATOM   8573 S  SD  . MET H  4  77  ? 18.489 48.681  11.232  1.00 58.71  ? 77  MET H SD  1 
ATOM   8574 C  CE  . MET H  4  77  ? 18.085 50.398  11.732  1.00 58.21  ? 77  MET H CE  1 
ATOM   8575 N  N   . GLY H  4  78  ? 22.767 51.042  13.634  1.00 44.55  ? 78  GLY H N   1 
ATOM   8576 C  CA  . GLY H  4  78  ? 23.543 52.267  13.542  1.00 43.17  ? 78  GLY H CA  1 
ATOM   8577 C  C   . GLY H  4  78  ? 25.040 52.052  13.699  1.00 42.90  ? 78  GLY H C   1 
ATOM   8578 O  O   . GLY H  4  78  ? 25.853 52.591  12.950  1.00 43.02  ? 78  GLY H O   1 
ATOM   8579 N  N   . ILE H  4  79  ? 25.420 51.257  14.686  1.00 41.41  ? 79  ILE H N   1 
ATOM   8580 C  CA  . ILE H  4  79  ? 26.824 51.011  14.926  1.00 39.93  ? 79  ILE H CA  1 
ATOM   8581 C  C   . ILE H  4  79  ? 27.456 50.293  13.747  1.00 40.25  ? 79  ILE H C   1 
ATOM   8582 O  O   . ILE H  4  79  ? 28.502 50.705  13.250  1.00 41.09  ? 79  ILE H O   1 
ATOM   8583 C  CB  . ILE H  4  79  ? 27.019 50.187  16.233  1.00 40.52  ? 79  ILE H CB  1 
ATOM   8584 C  CG1 . ILE H  4  79  ? 26.648 51.055  17.433  1.00 40.07  ? 79  ILE H CG1 1 
ATOM   8585 C  CG2 . ILE H  4  79  ? 28.462 49.730  16.386  1.00 40.31  ? 79  ILE H CG2 1 
ATOM   8586 C  CD1 . ILE H  4  79  ? 26.695 50.336  18.751  1.00 40.16  ? 79  ILE H CD1 1 
ATOM   8587 N  N   . ASN H  4  80  ? 26.822 49.228  13.280  1.00 40.05  ? 80  ASN H N   1 
ATOM   8588 C  CA  . ASN H  4  80  ? 27.403 48.468  12.176  1.00 41.26  ? 80  ASN H CA  1 
ATOM   8589 C  C   . ASN H  4  80  ? 27.538 49.233  10.862  1.00 40.27  ? 80  ASN H C   1 
ATOM   8590 O  O   . ASN H  4  80  ? 28.260 48.803  9.972   1.00 37.82  ? 80  ASN H O   1 
ATOM   8591 C  CB  . ASN H  4  80  ? 26.628 47.159  11.977  1.00 40.99  ? 80  ASN H CB  1 
ATOM   8592 C  CG  . ASN H  4  80  ? 27.089 46.088  12.934  1.00 44.21  ? 80  ASN H CG  1 
ATOM   8593 O  OD1 . ASN H  4  80  ? 28.204 45.588  12.827  1.00 47.07  ? 80  ASN H OD1 1 
ATOM   8594 N  ND2 . ASN H  4  80  ? 26.251 45.756  13.895  1.00 47.63  ? 80  ASN H ND2 1 
ATOM   8595 N  N   . TYR H  4  81  ? 26.855 50.371  10.758  1.00 40.58  ? 81  TYR H N   1 
ATOM   8596 C  CA  . TYR H  4  81  ? 26.912 51.189  9.556   1.00 39.93  ? 81  TYR H CA  1 
ATOM   8597 C  C   . TYR H  4  81  ? 27.711 52.476  9.751   1.00 39.10  ? 81  TYR H C   1 
ATOM   8598 O  O   . TYR H  4  81  ? 27.634 53.385  8.939   1.00 37.23  ? 81  TYR H O   1 
ATOM   8599 C  CB  . TYR H  4  81  ? 25.489 51.504  9.089   1.00 39.15  ? 81  TYR H CB  1 
ATOM   8600 C  CG  . TYR H  4  81  ? 24.874 50.366  8.291   1.00 41.28  ? 81  TYR H CG  1 
ATOM   8601 C  CD1 . TYR H  4  81  ? 25.062 50.290  6.902   1.00 40.99  ? 81  TYR H CD1 1 
ATOM   8602 C  CD2 . TYR H  4  81  ? 24.195 49.307  8.930   1.00 38.50  ? 81  TYR H CD2 1 
ATOM   8603 C  CE1 . TYR H  4  81  ? 24.607 49.196  6.173   1.00 38.61  ? 81  TYR H CE1 1 
ATOM   8604 C  CE2 . TYR H  4  81  ? 23.727 48.207  8.206   1.00 38.18  ? 81  TYR H CE2 1 
ATOM   8605 C  CZ  . TYR H  4  81  ? 23.943 48.166  6.821   1.00 40.30  ? 81  TYR H CZ  1 
ATOM   8606 O  OH  . TYR H  4  81  ? 23.490 47.103  6.067   1.00 39.90  ? 81  TYR H OH  1 
ATOM   8607 N  N   . LEU H  4  82  ? 28.488 52.545  10.829  1.00 41.60  ? 82  LEU H N   1 
ATOM   8608 C  CA  . LEU H  4  82  ? 29.302 53.732  11.094  1.00 45.50  ? 82  LEU H CA  1 
ATOM   8609 C  C   . LEU H  4  82  ? 30.270 54.063  9.959   1.00 47.07  ? 82  LEU H C   1 
ATOM   8610 O  O   . LEU H  4  82  ? 30.583 55.229  9.756   1.00 46.46  ? 82  LEU H O   1 
ATOM   8611 C  CB  . LEU H  4  82  ? 30.086 53.570  12.408  1.00 44.55  ? 82  LEU H CB  1 
ATOM   8612 C  CG  . LEU H  4  82  ? 29.228 53.733  13.672  1.00 44.81  ? 82  LEU H CG  1 
ATOM   8613 C  CD1 . LEU H  4  82  ? 29.992 53.322  14.941  1.00 42.95  ? 82  LEU H CD1 1 
ATOM   8614 C  CD2 . LEU H  4  82  ? 28.783 55.181  13.753  1.00 46.19  ? 82  LEU H CD2 1 
ATOM   8615 N  N   . ASN H  4  83  ? 30.715 53.046  9.218   1.00 49.24  ? 83  ASN H N   1 
ATOM   8616 C  CA  . ASN H  4  83  ? 31.656 53.247  8.124   1.00 52.81  ? 83  ASN H CA  1 
ATOM   8617 C  C   . ASN H  4  83  ? 31.029 53.364  6.747   1.00 53.99  ? 83  ASN H C   1 
ATOM   8618 O  O   . ASN H  4  83  ? 31.713 53.227  5.730   1.00 56.75  ? 83  ASN H O   1 
ATOM   8619 C  CB  . ASN H  4  83  ? 32.721 52.144  8.123   1.00 52.87  ? 83  ASN H CB  1 
ATOM   8620 C  CG  . ASN H  4  83  ? 33.815 52.406  9.151   1.00 54.95  ? 83  ASN H CG  1 
ATOM   8621 O  OD1 . ASN H  4  83  ? 34.304 53.542  9.275   1.00 56.11  ? 83  ASN H OD1 1 
ATOM   8622 N  ND2 . ASN H  4  83  ? 34.208 51.369  9.888   1.00 53.93  ? 83  ASN H ND2 1 
ATOM   8623 N  N   . ASP H  4  84  ? 29.727 53.622  6.730   1.00 54.54  ? 84  ASP H N   1 
ATOM   8624 C  CA  . ASP H  4  84  ? 28.957 53.794  5.502   1.00 54.75  ? 84  ASP H CA  1 
ATOM   8625 C  C   . ASP H  4  84  ? 28.066 55.006  5.783   1.00 54.43  ? 84  ASP H C   1 
ATOM   8626 O  O   . ASP H  4  84  ? 26.847 54.878  5.866   1.00 54.82  ? 84  ASP H O   1 
ATOM   8627 C  CB  . ASP H  4  84  ? 28.088 52.558  5.218   1.00 55.32  ? 84  ASP H CB  1 
ATOM   8628 C  CG  . ASP H  4  84  ? 27.315 52.664  3.890   1.00 58.48  ? 84  ASP H CG  1 
ATOM   8629 O  OD1 . ASP H  4  84  ? 26.899 53.785  3.519   1.00 59.47  ? 84  ASP H OD1 1 
ATOM   8630 O  OD2 . ASP H  4  84  ? 27.107 51.620  3.216   1.00 58.72  ? 84  ASP H OD2 1 
ATOM   8631 N  N   . ALA H  4  85  ? 28.690 56.171  5.942   1.00 53.89  ? 85  ALA H N   1 
ATOM   8632 C  CA  . ALA H  4  85  ? 27.981 57.413  6.250   1.00 52.91  ? 85  ALA H CA  1 
ATOM   8633 C  C   . ALA H  4  85  ? 26.722 57.632  5.420   1.00 51.57  ? 85  ALA H C   1 
ATOM   8634 O  O   . ALA H  4  85  ? 25.711 58.107  5.940   1.00 49.97  ? 85  ALA H O   1 
ATOM   8635 C  CB  . ALA H  4  85  ? 28.923 58.603  6.091   1.00 53.02  ? 85  ALA H CB  1 
ATOM   8636 N  N   . GLY H  4  86  ? 26.777 57.290  4.134   1.00 50.37  ? 86  GLY H N   1 
ATOM   8637 C  CA  . GLY H  4  86  ? 25.602 57.464  3.292   1.00 49.37  ? 86  GLY H CA  1 
ATOM   8638 C  C   . GLY H  4  86  ? 24.396 56.743  3.892   1.00 50.23  ? 86  GLY H C   1 
ATOM   8639 O  O   . GLY H  4  86  ? 23.383 57.365  4.244   1.00 50.47  ? 86  GLY H O   1 
ATOM   8640 N  N   . THR H  4  87  ? 24.523 55.425  4.022   1.00 48.41  ? 87  THR H N   1 
ATOM   8641 C  CA  . THR H  4  87  ? 23.475 54.593  4.573   1.00 47.11  ? 87  THR H CA  1 
ATOM   8642 C  C   . THR H  4  87  ? 23.163 54.959  6.011   1.00 46.77  ? 87  THR H C   1 
ATOM   8643 O  O   . THR H  4  87  ? 22.011 54.896  6.431   1.00 47.07  ? 87  THR H O   1 
ATOM   8644 C  CB  . THR H  4  87  ? 23.865 53.105  4.550   1.00 46.70  ? 87  THR H CB  1 
ATOM   8645 O  OG1 . THR H  4  87  ? 24.179 52.708  3.210   1.00 45.04  ? 87  THR H OG1 1 
ATOM   8646 C  CG2 . THR H  4  87  ? 22.715 52.258  5.076   1.00 47.02  ? 87  THR H CG2 1 
ATOM   8647 N  N   . LEU H  4  88  ? 24.177 55.336  6.778   1.00 44.86  ? 88  LEU H N   1 
ATOM   8648 C  CA  . LEU H  4  88  ? 23.953 55.675  8.179   1.00 43.52  ? 88  LEU H CA  1 
ATOM   8649 C  C   . LEU H  4  88  ? 23.104 56.923  8.326   1.00 43.42  ? 88  LEU H C   1 
ATOM   8650 O  O   . LEU H  4  88  ? 22.238 57.002  9.205   1.00 41.90  ? 88  LEU H O   1 
ATOM   8651 C  CB  . LEU H  4  88  ? 25.297 55.869  8.884   1.00 41.82  ? 88  LEU H CB  1 
ATOM   8652 C  CG  . LEU H  4  88  ? 25.196 56.073  10.402  1.00 42.53  ? 88  LEU H CG  1 
ATOM   8653 C  CD1 . LEU H  4  88  ? 24.264 55.018  11.027  1.00 42.08  ? 88  LEU H CD1 1 
ATOM   8654 C  CD2 . LEU H  4  88  ? 26.583 55.995  11.032  1.00 40.75  ? 88  LEU H CD2 1 
ATOM   8655 N  N   . THR H  4  89  ? 23.358 57.888  7.446   1.00 43.89  ? 89  THR H N   1 
ATOM   8656 C  CA  . THR H  4  89  ? 22.632 59.153  7.437   1.00 42.73  ? 89  THR H CA  1 
ATOM   8657 C  C   . THR H  4  89  ? 21.150 58.846  7.166   1.00 42.43  ? 89  THR H C   1 
ATOM   8658 O  O   . THR H  4  89  ? 20.247 59.413  7.777   1.00 41.62  ? 89  THR H O   1 
ATOM   8659 C  CB  . THR H  4  89  ? 23.183 60.095  6.324   1.00 42.73  ? 89  THR H CB  1 
ATOM   8660 O  OG1 . THR H  4  89  ? 24.520 60.491  6.643   1.00 41.04  ? 89  THR H OG1 1 
ATOM   8661 C  CG2 . THR H  4  89  ? 22.305 61.343  6.174   1.00 39.48  ? 89  THR H CG2 1 
ATOM   8662 N  N   . SER H  4  90  ? 20.916 57.931  6.240   1.00 41.86  ? 90  SER H N   1 
ATOM   8663 C  CA  . SER H  4  90  ? 19.558 57.560  5.881   1.00 40.97  ? 90  SER H CA  1 
ATOM   8664 C  C   . SER H  4  90  ? 18.903 56.744  6.988   1.00 40.97  ? 90  SER H C   1 
ATOM   8665 O  O   . SER H  4  90  ? 17.691 56.802  7.194   1.00 42.00  ? 90  SER H O   1 
ATOM   8666 C  CB  . SER H  4  90  ? 19.568 56.781  4.574   1.00 37.11  ? 90  SER H CB  1 
ATOM   8667 O  OG  . SER H  4  90  ? 18.262 56.386  4.244   1.00 38.54  ? 90  SER H OG  1 
ATOM   8668 N  N   . LEU H  4  91  ? 19.709 55.972  7.698   1.00 42.03  ? 91  LEU H N   1 
ATOM   8669 C  CA  . LEU H  4  91  ? 19.198 55.161  8.793   1.00 41.95  ? 91  LEU H CA  1 
ATOM   8670 C  C   . LEU H  4  91  ? 18.861 56.045  10.000  1.00 42.54  ? 91  LEU H C   1 
ATOM   8671 O  O   . LEU H  4  91  ? 17.838 55.837  10.680  1.00 42.55  ? 91  LEU H O   1 
ATOM   8672 C  CB  . LEU H  4  91  ? 20.236 54.108  9.210   1.00 42.52  ? 91  LEU H CB  1 
ATOM   8673 C  CG  . LEU H  4  91  ? 20.296 52.796  8.430   1.00 42.13  ? 91  LEU H CG  1 
ATOM   8674 C  CD1 . LEU H  4  91  ? 21.504 52.008  8.887   1.00 40.13  ? 91  LEU H CD1 1 
ATOM   8675 C  CD2 . LEU H  4  91  ? 19.010 52.009  8.640   1.00 40.45  ? 91  LEU H CD2 1 
ATOM   8676 N  N   . THR H  4  92  ? 19.717 57.028  10.272  1.00 41.33  ? 92  THR H N   1 
ATOM   8677 C  CA  . THR H  4  92  ? 19.469 57.905  11.411  1.00 42.23  ? 92  THR H CA  1 
ATOM   8678 C  C   . THR H  4  92  ? 18.263 58.795  11.148  1.00 42.24  ? 92  THR H C   1 
ATOM   8679 O  O   . THR H  4  92  ? 17.466 59.071  12.059  1.00 39.24  ? 92  THR H O   1 
ATOM   8680 C  CB  . THR H  4  92  ? 20.681 58.786  11.736  1.00 43.38  ? 92  THR H CB  1 
ATOM   8681 O  OG1 . THR H  4  92  ? 21.194 59.376  10.533  1.00 45.74  ? 92  THR H OG1 1 
ATOM   8682 C  CG2 . THR H  4  92  ? 21.750 57.953  12.411  1.00 43.76  ? 92  THR H CG2 1 
ATOM   8683 N  N   . ALA H  4  93  ? 18.127 59.216  9.888   1.00 42.75  ? 93  ALA H N   1 
ATOM   8684 C  CA  . ALA H  4  93  ? 17.028 60.078  9.465   1.00 42.39  ? 93  ALA H CA  1 
ATOM   8685 C  C   . ALA H  4  93  ? 15.713 59.376  9.753   1.00 42.88  ? 93  ALA H C   1 
ATOM   8686 O  O   . ALA H  4  93  ? 14.792 59.959  10.313  1.00 42.07  ? 93  ALA H O   1 
ATOM   8687 C  CB  . ALA H  4  93  ? 17.132 60.386  7.972   1.00 41.06  ? 93  ALA H CB  1 
ATOM   8688 N  N   . HIS H  4  94  ? 15.641 58.103  9.371   1.00 44.00  ? 94  HIS H N   1 
ATOM   8689 C  CA  . HIS H  4  94  ? 14.444 57.291  9.571   1.00 43.49  ? 94  HIS H CA  1 
ATOM   8690 C  C   . HIS H  4  94  ? 14.148 57.136  11.060  1.00 44.01  ? 94  HIS H C   1 
ATOM   8691 O  O   . HIS H  4  94  ? 13.015 57.346  11.510  1.00 43.32  ? 94  HIS H O   1 
ATOM   8692 C  CB  . HIS H  4  94  ? 14.648 55.925  8.928   1.00 43.80  ? 94  HIS H CB  1 
ATOM   8693 C  CG  . HIS H  4  94  ? 13.423 55.070  8.922   1.00 42.19  ? 94  HIS H CG  1 
ATOM   8694 N  ND1 . HIS H  4  94  ? 12.925 54.482  10.063  1.00 41.69  ? 94  HIS H ND1 1 
ATOM   8695 C  CD2 . HIS H  4  94  ? 12.579 54.726  7.917   1.00 43.33  ? 94  HIS H CD2 1 
ATOM   8696 C  CE1 . HIS H  4  94  ? 11.828 53.810  9.767   1.00 41.72  ? 94  HIS H CE1 1 
ATOM   8697 N  NE2 . HIS H  4  94  ? 11.593 53.941  8.471   1.00 44.80  ? 94  HIS H NE2 1 
ATOM   8698 N  N   . LEU H  4  95  ? 15.165 56.752  11.820  1.00 44.01  ? 95  LEU H N   1 
ATOM   8699 C  CA  . LEU H  4  95  ? 15.009 56.605  13.269  1.00 46.20  ? 95  LEU H CA  1 
ATOM   8700 C  C   . LEU H  4  95  ? 14.493 57.912  13.890  1.00 46.70  ? 95  LEU H C   1 
ATOM   8701 O  O   . LEU H  4  95  ? 13.600 57.909  14.748  1.00 44.07  ? 95  LEU H O   1 
ATOM   8702 C  CB  . LEU H  4  95  ? 16.350 56.266  13.924  1.00 45.94  ? 95  LEU H CB  1 
ATOM   8703 C  CG  . LEU H  4  95  ? 16.863 54.848  13.799  1.00 45.46  ? 95  LEU H CG  1 
ATOM   8704 C  CD1 . LEU H  4  95  ? 18.327 54.766  14.188  1.00 46.97  ? 95  LEU H CD1 1 
ATOM   8705 C  CD2 . LEU H  4  95  ? 16.006 54.001  14.711  1.00 46.69  ? 95  LEU H CD2 1 
ATOM   8706 N  N   . ALA H  4  96  ? 15.065 59.029  13.454  1.00 46.84  ? 96  ALA H N   1 
ATOM   8707 C  CA  . ALA H  4  96  ? 14.671 60.328  13.981  1.00 49.59  ? 96  ALA H CA  1 
ATOM   8708 C  C   . ALA H  4  96  ? 13.178 60.527  13.784  1.00 51.99  ? 96  ALA H C   1 
ATOM   8709 O  O   . ALA H  4  96  ? 12.447 60.878  14.715  1.00 51.48  ? 96  ALA H O   1 
ATOM   8710 C  CB  . ALA H  4  96  ? 15.463 61.432  13.286  1.00 46.90  ? 96  ALA H CB  1 
ATOM   8711 N  N   . ALA H  4  97  ? 12.734 60.294  12.555  1.00 54.84  ? 97  ALA H N   1 
ATOM   8712 C  CA  . ALA H  4  97  ? 11.334 60.435  12.221  1.00 56.00  ? 97  ALA H CA  1 
ATOM   8713 C  C   . ALA H  4  97  ? 10.478 59.638  13.202  1.00 57.42  ? 97  ALA H C   1 
ATOM   8714 O  O   . ALA H  4  97  ? 9.449  60.122  13.656  1.00 56.60  ? 97  ALA H O   1 
ATOM   8715 C  CB  . ALA H  4  97  ? 11.090 59.954  10.797  1.00 55.49  ? 97  ALA H CB  1 
ATOM   8716 N  N   . GLN H  4  98  ? 10.910 58.423  13.540  1.00 59.83  ? 98  GLN H N   1 
ATOM   8717 C  CA  . GLN H  4  98  ? 10.144 57.580  14.454  1.00 62.36  ? 98  GLN H CA  1 
ATOM   8718 C  C   . GLN H  4  98  ? 10.020 58.172  15.860  1.00 63.42  ? 98  GLN H C   1 
ATOM   8719 O  O   . GLN H  4  98  ? 9.090  57.849  16.596  1.00 63.00  ? 98  GLN H O   1 
ATOM   8720 C  CB  . GLN H  4  98  ? 10.753 56.173  14.519  1.00 62.68  ? 98  GLN H CB  1 
ATOM   8721 C  CG  . GLN H  4  98  ? 10.761 55.454  13.163  1.00 65.85  ? 98  GLN H CG  1 
ATOM   8722 C  CD  . GLN H  4  98  ? 11.281 54.021  13.234  1.00 66.55  ? 98  GLN H CD  1 
ATOM   8723 O  OE1 . GLN H  4  98  ? 12.373 53.770  13.745  1.00 68.58  ? 98  GLN H OE1 1 
ATOM   8724 N  NE2 . GLN H  4  98  ? 10.500 53.080  12.706  1.00 65.25  ? 98  GLN H NE2 1 
ATOM   8725 N  N   . HIS H  4  99  ? 10.949 59.052  16.223  1.00 65.08  ? 99  HIS H N   1 
ATOM   8726 C  CA  . HIS H  4  99  ? 10.918 59.664  17.541  1.00 67.76  ? 99  HIS H CA  1 
ATOM   8727 C  C   . HIS H  4  99  ? 10.175 60.998  17.542  1.00 71.15  ? 99  HIS H C   1 
ATOM   8728 O  O   . HIS H  4  99  ? 9.334  61.238  18.408  1.00 72.31  ? 99  HIS H O   1 
ATOM   8729 C  CB  . HIS H  4  99  ? 12.342 59.845  18.085  1.00 64.58  ? 99  HIS H CB  1 
ATOM   8730 C  CG  . HIS H  4  99  ? 12.976 58.566  18.543  1.00 61.98  ? 99  HIS H CG  1 
ATOM   8731 N  ND1 . HIS H  4  99  ? 13.534 57.656  17.673  1.00 59.53  ? 99  HIS H ND1 1 
ATOM   8732 C  CD2 . HIS H  4  99  ? 13.112 58.033  19.779  1.00 60.59  ? 99  HIS H CD2 1 
ATOM   8733 C  CE1 . HIS H  4  99  ? 13.984 56.618  18.353  1.00 58.26  ? 99  HIS H CE1 1 
ATOM   8734 N  NE2 . HIS H  4  99  ? 13.741 56.820  19.634  1.00 57.52  ? 99  HIS H NE2 1 
ATOM   8735 N  N   . VAL H  4  100 ? 10.480 61.856  16.573  1.00 74.65  ? 100 VAL H N   1 
ATOM   8736 C  CA  . VAL H  4  100 ? 9.834  63.164  16.468  1.00 78.73  ? 100 VAL H CA  1 
ATOM   8737 C  C   . VAL H  4  100 ? 8.322  62.957  16.332  1.00 80.74  ? 100 VAL H C   1 
ATOM   8738 O  O   . VAL H  4  100 ? 7.524  63.807  16.724  1.00 79.91  ? 100 VAL H O   1 
ATOM   8739 C  CB  . VAL H  4  100 ? 10.378 63.954  15.236  1.00 79.67  ? 100 VAL H CB  1 
ATOM   8740 C  CG1 . VAL H  4  100 ? 9.802  65.353  15.209  1.00 80.96  ? 100 VAL H CG1 1 
ATOM   8741 C  CG2 . VAL H  4  100 ? 11.906 64.033  15.290  1.00 79.91  ? 100 VAL H CG2 1 
ATOM   8742 N  N   . ALA H  4  101 ? 7.943  61.810  15.775  1.00 84.28  ? 101 ALA H N   1 
ATOM   8743 C  CA  . ALA H  4  101 ? 6.539  61.456  15.594  1.00 86.63  ? 101 ALA H CA  1 
ATOM   8744 C  C   . ALA H  4  101 ? 5.893  61.362  16.971  1.00 88.43  ? 101 ALA H C   1 
ATOM   8745 O  O   . ALA H  4  101 ? 4.723  61.698  17.146  1.00 88.47  ? 101 ALA H O   1 
ATOM   8746 C  CB  . ALA H  4  101 ? 6.422  60.117  14.862  1.00 86.22  ? 101 ALA H CB  1 
ATOM   8747 N  N   . ARG H  4  102 ? 6.671  60.893  17.944  1.00 90.72  ? 102 ARG H N   1 
ATOM   8748 C  CA  . ARG H  4  102 ? 6.207  60.765  19.323  1.00 92.96  ? 102 ARG H CA  1 
ATOM   8749 C  C   . ARG H  4  102 ? 6.477  62.084  20.048  1.00 92.43  ? 102 ARG H C   1 
ATOM   8750 O  O   . ARG H  4  102 ? 7.566  62.646  19.937  1.00 93.21  ? 102 ARG H O   1 
ATOM   8751 C  CB  . ARG H  4  102 ? 6.944  59.610  20.022  1.00 95.32  ? 102 ARG H CB  1 
ATOM   8752 C  CG  . ARG H  4  102 ? 6.674  58.221  19.429  1.00 98.85  ? 102 ARG H CG  1 
ATOM   8753 C  CD  . ARG H  4  102 ? 5.179  57.903  19.415  1.00 102.55 ? 102 ARG H CD  1 
ATOM   8754 N  NE  . ARG H  4  102 ? 4.592  57.944  20.756  1.00 106.15 ? 102 ARG H NE  1 
ATOM   8755 C  CZ  . ARG H  4  102 ? 4.565  56.915  21.597  1.00 107.68 ? 102 ARG H CZ  1 
ATOM   8756 N  NH1 . ARG H  4  102 ? 5.082  55.753  21.236  1.00 108.60 ? 102 ARG H NH1 1 
ATOM   8757 N  NH2 . ARG H  4  102 ? 4.028  57.043  22.804  1.00 109.06 ? 102 ARG H NH2 1 
ATOM   8758 N  N   . THR H  4  103 ? 5.495  62.586  20.783  1.00 91.27  ? 103 THR H N   1 
ATOM   8759 C  CA  . THR H  4  103 ? 5.678  63.847  21.495  1.00 91.03  ? 103 THR H CA  1 
ATOM   8760 C  C   . THR H  4  103 ? 6.048  63.682  22.958  1.00 90.19  ? 103 THR H C   1 
ATOM   8761 O  O   . THR H  4  103 ? 5.677  62.706  23.606  1.00 90.12  ? 103 THR H O   1 
ATOM   8762 C  CB  . THR H  4  103 ? 4.417  64.729  21.415  1.00 91.82  ? 103 THR H CB  1 
ATOM   8763 O  OG1 . THR H  4  103 ? 3.255  63.936  21.690  1.00 92.35  ? 103 THR H OG1 1 
ATOM   8764 C  CG2 . THR H  4  103 ? 4.300  65.365  20.040  1.00 92.57  ? 103 THR H CG2 1 
ATOM   8765 N  N   . GLY H  4  104 ? 6.776  64.663  23.477  1.00 89.21  ? 104 GLY H N   1 
ATOM   8766 C  CA  . GLY H  4  104 ? 7.193  64.620  24.863  1.00 87.55  ? 104 GLY H CA  1 
ATOM   8767 C  C   . GLY H  4  104 ? 8.687  64.398  24.979  1.00 86.12  ? 104 GLY H C   1 
ATOM   8768 O  O   . GLY H  4  104 ? 9.280  64.637  26.032  1.00 85.96  ? 104 GLY H O   1 
ATOM   8769 N  N   . LEU H  4  105 ? 9.300  63.948  23.890  1.00 84.37  ? 105 LEU H N   1 
ATOM   8770 C  CA  . LEU H  4  105 ? 10.733 63.688  23.884  1.00 81.99  ? 105 LEU H CA  1 
ATOM   8771 C  C   . LEU H  4  105 ? 11.518 64.982  23.856  1.00 79.61  ? 105 LEU H C   1 
ATOM   8772 O  O   . LEU H  4  105 ? 11.176 65.911  23.129  1.00 79.12  ? 105 LEU H O   1 
ATOM   8773 C  CB  . LEU H  4  105 ? 11.119 62.852  22.667  1.00 82.31  ? 105 LEU H CB  1 
ATOM   8774 C  CG  . LEU H  4  105 ? 10.308 61.595  22.372  1.00 81.49  ? 105 LEU H CG  1 
ATOM   8775 C  CD1 . LEU H  4  105 ? 10.901 60.914  21.168  1.00 81.97  ? 105 LEU H CD1 1 
ATOM   8776 C  CD2 . LEU H  4  105 ? 10.323 60.660  23.547  1.00 81.47  ? 105 LEU H CD2 1 
ATOM   8777 N  N   . LYS H  4  106 ? 12.578 65.032  24.646  1.00 77.10  ? 106 LYS H N   1 
ATOM   8778 C  CA  . LYS H  4  106 ? 13.413 66.217  24.697  1.00 75.76  ? 106 LYS H CA  1 
ATOM   8779 C  C   . LYS H  4  106 ? 14.854 65.850  24.341  1.00 74.02  ? 106 LYS H C   1 
ATOM   8780 O  O   . LYS H  4  106 ? 15.290 64.723  24.575  1.00 73.66  ? 106 LYS H O   1 
ATOM   8781 C  CB  . LYS H  4  106 ? 13.351 66.826  26.100  1.00 74.92  ? 106 LYS H CB  1 
ATOM   8782 C  CG  . LYS H  4  106 ? 11.938 67.047  26.620  1.00 73.73  ? 106 LYS H CG  1 
ATOM   8783 C  CD  . LYS H  4  106 ? 11.966 67.700  27.999  1.00 73.80  ? 106 LYS H CD  1 
ATOM   8784 C  CE  . LYS H  4  106 ? 10.574 67.997  28.527  1.00 72.87  ? 106 LYS H CE  1 
ATOM   8785 N  NZ  . LYS H  4  106 ? 10.626 68.830  29.764  1.00 72.23  ? 106 LYS H NZ  1 
ATOM   8786 N  N   . ALA H  4  107 ? 15.589 66.797  23.769  1.00 71.99  ? 107 ALA H N   1 
ATOM   8787 C  CA  . ALA H  4  107 ? 16.975 66.534  23.403  1.00 70.90  ? 107 ALA H CA  1 
ATOM   8788 C  C   . ALA H  4  107 ? 17.766 66.052  24.622  1.00 69.93  ? 107 ALA H C   1 
ATOM   8789 O  O   . ALA H  4  107 ? 18.581 65.138  24.514  1.00 70.08  ? 107 ALA H O   1 
ATOM   8790 C  CB  . ALA H  4  107 ? 17.618 67.794  22.819  1.00 69.29  ? 107 ALA H CB  1 
ATOM   8791 N  N   . VAL H  4  108 ? 17.510 66.663  25.777  1.00 68.65  ? 108 VAL H N   1 
ATOM   8792 C  CA  . VAL H  4  108 ? 18.216 66.307  27.002  1.00 66.39  ? 108 VAL H CA  1 
ATOM   8793 C  C   . VAL H  4  108 ? 18.001 64.833  27.335  1.00 65.28  ? 108 VAL H C   1 
ATOM   8794 O  O   . VAL H  4  108 ? 18.802 64.230  28.048  1.00 65.13  ? 108 VAL H O   1 
ATOM   8795 C  CB  . VAL H  4  108 ? 17.756 67.195  28.193  1.00 65.55  ? 108 VAL H CB  1 
ATOM   8796 C  CG1 . VAL H  4  108 ? 18.552 66.854  29.444  1.00 67.27  ? 108 VAL H CG1 1 
ATOM   8797 C  CG2 . VAL H  4  108 ? 17.952 68.656  27.853  1.00 64.79  ? 108 VAL H CG2 1 
ATOM   8798 N  N   . TYR H  4  109 ? 16.928 64.242  26.817  1.00 64.13  ? 109 TYR H N   1 
ATOM   8799 C  CA  . TYR H  4  109 ? 16.676 62.830  27.099  1.00 63.78  ? 109 TYR H CA  1 
ATOM   8800 C  C   . TYR H  4  109 ? 17.679 61.945  26.353  1.00 62.49  ? 109 TYR H C   1 
ATOM   8801 O  O   . TYR H  4  109 ? 18.048 60.866  26.827  1.00 62.06  ? 109 TYR H O   1 
ATOM   8802 C  CB  . TYR H  4  109 ? 15.244 62.417  26.715  1.00 63.85  ? 109 TYR H CB  1 
ATOM   8803 C  CG  . TYR H  4  109 ? 14.131 63.026  27.552  1.00 65.13  ? 109 TYR H CG  1 
ATOM   8804 C  CD1 . TYR H  4  109 ? 14.389 63.628  28.790  1.00 64.91  ? 109 TYR H CD1 1 
ATOM   8805 C  CD2 . TYR H  4  109 ? 12.807 62.983  27.107  1.00 65.73  ? 109 TYR H CD2 1 
ATOM   8806 C  CE1 . TYR H  4  109 ? 13.352 64.175  29.559  1.00 64.53  ? 109 TYR H CE1 1 
ATOM   8807 C  CE2 . TYR H  4  109 ? 11.765 63.522  27.867  1.00 66.65  ? 109 TYR H CE2 1 
ATOM   8808 C  CZ  . TYR H  4  109 ? 12.042 64.121  29.090  1.00 65.50  ? 109 TYR H CZ  1 
ATOM   8809 O  OH  . TYR H  4  109 ? 11.007 64.675  29.820  1.00 62.64  ? 109 TYR H OH  1 
ATOM   8810 N  N   . PHE H  4  110 ? 18.114 62.405  25.181  1.00 60.96  ? 110 PHE H N   1 
ATOM   8811 C  CA  . PHE H  4  110 ? 19.095 61.650  24.410  1.00 59.17  ? 110 PHE H CA  1 
ATOM   8812 C  C   . PHE H  4  110 ? 20.491 61.836  24.966  1.00 57.83  ? 110 PHE H C   1 
ATOM   8813 O  O   . PHE H  4  110 ? 21.315 60.928  24.898  1.00 56.74  ? 110 PHE H O   1 
ATOM   8814 C  CB  . PHE H  4  110 ? 19.035 62.034  22.936  1.00 58.60  ? 110 PHE H CB  1 
ATOM   8815 C  CG  . PHE H  4  110 ? 17.939 61.338  22.201  1.00 59.35  ? 110 PHE H CG  1 
ATOM   8816 C  CD1 . PHE H  4  110 ? 16.610 61.646  22.468  1.00 58.67  ? 110 PHE H CD1 1 
ATOM   8817 C  CD2 . PHE H  4  110 ? 18.221 60.324  21.292  1.00 58.14  ? 110 PHE H CD2 1 
ATOM   8818 C  CE1 . PHE H  4  110 ? 15.576 60.948  21.842  1.00 57.62  ? 110 PHE H CE1 1 
ATOM   8819 C  CE2 . PHE H  4  110 ? 17.192 59.625  20.666  1.00 57.27  ? 110 PHE H CE2 1 
ATOM   8820 C  CZ  . PHE H  4  110 ? 15.869 59.938  20.942  1.00 56.54  ? 110 PHE H CZ  1 
ATOM   8821 N  N   . ASP H  4  111 ? 20.752 63.004  25.538  1.00 56.43  ? 111 ASP H N   1 
ATOM   8822 C  CA  . ASP H  4  111 ? 22.062 63.226  26.117  1.00 56.51  ? 111 ASP H CA  1 
ATOM   8823 C  C   . ASP H  4  111 ? 22.113 62.288  27.340  1.00 54.72  ? 111 ASP H C   1 
ATOM   8824 O  O   . ASP H  4  111 ? 23.161 61.708  27.656  1.00 54.02  ? 111 ASP H O   1 
ATOM   8825 C  CB  . ASP H  4  111 ? 22.232 64.700  26.553  1.00 58.78  ? 111 ASP H CB  1 
ATOM   8826 C  CG  . ASP H  4  111 ? 21.876 65.697  25.443  1.00 62.56  ? 111 ASP H CG  1 
ATOM   8827 O  OD1 . ASP H  4  111 ? 21.792 65.272  24.268  1.00 63.09  ? 111 ASP H OD1 1 
ATOM   8828 O  OD2 . ASP H  4  111 ? 21.682 66.904  25.736  1.00 62.25  ? 111 ASP H OD2 1 
ATOM   8829 N  N   . ALA H  4  112 ? 20.966 62.124  27.998  1.00 51.47  ? 112 ALA H N   1 
ATOM   8830 C  CA  . ALA H  4  112 ? 20.895 61.267  29.169  1.00 50.00  ? 112 ALA H CA  1 
ATOM   8831 C  C   . ALA H  4  112 ? 21.224 59.845  28.755  1.00 49.00  ? 112 ALA H C   1 
ATOM   8832 O  O   . ALA H  4  112 ? 22.063 59.192  29.366  1.00 47.75  ? 112 ALA H O   1 
ATOM   8833 C  CB  . ALA H  4  112 ? 19.494 61.330  29.790  1.00 50.44  ? 112 ALA H CB  1 
ATOM   8834 N  N   . MET H  4  113 ? 20.568 59.383  27.698  1.00 49.49  ? 113 MET H N   1 
ATOM   8835 C  CA  . MET H  4  113 ? 20.794 58.044  27.176  1.00 49.38  ? 113 MET H CA  1 
ATOM   8836 C  C   . MET H  4  113 ? 22.289 57.855  26.909  1.00 49.23  ? 113 MET H C   1 
ATOM   8837 O  O   . MET H  4  113 ? 22.849 56.794  27.173  1.00 49.15  ? 113 MET H O   1 
ATOM   8838 C  CB  . MET H  4  113 ? 20.002 57.851  25.881  1.00 51.13  ? 113 MET H CB  1 
ATOM   8839 C  CG  . MET H  4  113 ? 20.208 56.508  25.210  1.00 51.78  ? 113 MET H CG  1 
ATOM   8840 S  SD  . MET H  4  113 ? 19.596 55.138  26.209  1.00 55.87  ? 113 MET H SD  1 
ATOM   8841 C  CE  . MET H  4  113 ? 17.966 54.896  25.499  1.00 54.36  ? 113 MET H CE  1 
ATOM   8842 N  N   . GLY H  4  114 ? 22.933 58.899  26.398  1.00 48.96  ? 114 GLY H N   1 
ATOM   8843 C  CA  . GLY H  4  114 ? 24.353 58.816  26.125  1.00 48.13  ? 114 GLY H CA  1 
ATOM   8844 C  C   . GLY H  4  114 ? 25.133 58.494  27.386  1.00 48.59  ? 114 GLY H C   1 
ATOM   8845 O  O   . GLY H  4  114 ? 26.004 57.616  27.375  1.00 49.28  ? 114 GLY H O   1 
ATOM   8846 N  N   . LYS H  4  115 ? 24.823 59.193  28.477  1.00 48.22  ? 115 LYS H N   1 
ATOM   8847 C  CA  . LYS H  4  115 ? 25.513 58.961  29.749  1.00 48.54  ? 115 LYS H CA  1 
ATOM   8848 C  C   . LYS H  4  115 ? 25.270 57.539  30.231  1.00 46.83  ? 115 LYS H C   1 
ATOM   8849 O  O   . LYS H  4  115 ? 26.185 56.860  30.684  1.00 45.60  ? 115 LYS H O   1 
ATOM   8850 C  CB  . LYS H  4  115 ? 25.063 59.991  30.804  1.00 51.39  ? 115 LYS H CB  1 
ATOM   8851 C  CG  . LYS H  4  115 ? 25.408 61.425  30.389  1.00 56.23  ? 115 LYS H CG  1 
ATOM   8852 C  CD  . LYS H  4  115 ? 25.043 62.487  31.418  1.00 60.23  ? 115 LYS H CD  1 
ATOM   8853 C  CE  . LYS H  4  115 ? 25.119 63.897  30.803  1.00 62.91  ? 115 LYS H CE  1 
ATOM   8854 N  NZ  . LYS H  4  115 ? 24.957 64.973  31.831  1.00 63.76  ? 115 LYS H NZ  1 
ATOM   8855 N  N   . VAL H  4  116 ? 24.029 57.086  30.111  1.00 46.89  ? 116 VAL H N   1 
ATOM   8856 C  CA  . VAL H  4  116 ? 23.653 55.733  30.515  1.00 46.96  ? 116 VAL H CA  1 
ATOM   8857 C  C   . VAL H  4  116 ? 24.505 54.711  29.766  1.00 47.79  ? 116 VAL H C   1 
ATOM   8858 O  O   . VAL H  4  116 ? 25.055 53.785  30.364  1.00 50.07  ? 116 VAL H O   1 
ATOM   8859 C  CB  . VAL H  4  116 ? 22.160 55.458  30.216  1.00 46.55  ? 116 VAL H CB  1 
ATOM   8860 C  CG1 . VAL H  4  116 ? 21.852 53.981  30.403  1.00 46.53  ? 116 VAL H CG1 1 
ATOM   8861 C  CG2 . VAL H  4  116 ? 21.282 56.287  31.136  1.00 43.76  ? 116 VAL H CG2 1 
ATOM   8862 N  N   . LEU H  4  117 ? 24.611 54.878  28.452  1.00 46.25  ? 117 LEU H N   1 
ATOM   8863 C  CA  . LEU H  4  117 ? 25.410 53.964  27.644  1.00 44.58  ? 117 LEU H CA  1 
ATOM   8864 C  C   . LEU H  4  117 ? 26.884 54.006  28.061  1.00 45.08  ? 117 LEU H C   1 
ATOM   8865 O  O   . LEU H  4  117 ? 27.527 52.959  28.184  1.00 44.68  ? 117 LEU H O   1 
ATOM   8866 C  CB  . LEU H  4  117 ? 25.254 54.309  26.157  1.00 42.16  ? 117 LEU H CB  1 
ATOM   8867 C  CG  . LEU H  4  117 ? 23.840 54.076  25.589  1.00 39.35  ? 117 LEU H CG  1 
ATOM   8868 C  CD1 . LEU H  4  117 ? 23.687 54.628  24.201  1.00 35.68  ? 117 LEU H CD1 1 
ATOM   8869 C  CD2 . LEU H  4  117 ? 23.563 52.594  25.579  1.00 40.91  ? 117 LEU H CD2 1 
ATOM   8870 N  N   . MET H  4  118 ? 27.408 55.211  28.283  1.00 44.96  ? 118 MET H N   1 
ATOM   8871 C  CA  . MET H  4  118 ? 28.793 55.370  28.697  1.00 45.82  ? 118 MET H CA  1 
ATOM   8872 C  C   . MET H  4  118 ? 29.004 54.799  30.099  1.00 45.88  ? 118 MET H C   1 
ATOM   8873 O  O   . MET H  4  118 ? 30.137 54.511  30.501  1.00 46.29  ? 118 MET H O   1 
ATOM   8874 C  CB  . MET H  4  118 ? 29.188 56.842  28.702  1.00 48.06  ? 118 MET H CB  1 
ATOM   8875 C  CG  . MET H  4  118 ? 29.278 57.473  27.349  1.00 50.19  ? 118 MET H CG  1 
ATOM   8876 S  SD  . MET H  4  118 ? 30.641 56.784  26.398  1.00 54.41  ? 118 MET H SD  1 
ATOM   8877 C  CE  . MET H  4  118 ? 29.760 55.811  25.242  1.00 54.39  ? 118 MET H CE  1 
ATOM   8878 N  N   . THR H  4  119 ? 27.919 54.639  30.849  1.00 45.36  ? 119 THR H N   1 
ATOM   8879 C  CA  . THR H  4  119 ? 28.028 54.092  32.199  1.00 45.49  ? 119 THR H CA  1 
ATOM   8880 C  C   . THR H  4  119 ? 27.798 52.593  32.183  1.00 44.90  ? 119 THR H C   1 
ATOM   8881 O  O   . THR H  4  119 ? 28.476 51.848  32.886  1.00 47.10  ? 119 THR H O   1 
ATOM   8882 C  CB  . THR H  4  119 ? 26.992 54.708  33.181  1.00 45.03  ? 119 THR H CB  1 
ATOM   8883 O  OG1 . THR H  4  119 ? 27.183 56.126  33.280  1.00 43.41  ? 119 THR H OG1 1 
ATOM   8884 C  CG2 . THR H  4  119 ? 27.126 54.070  34.574  1.00 39.46  ? 119 THR H CG2 1 
ATOM   8885 N  N   . VAL H  4  120 ? 26.833 52.162  31.380  1.00 43.99  ? 120 VAL H N   1 
ATOM   8886 C  CA  . VAL H  4  120 ? 26.476 50.752  31.296  1.00 44.93  ? 120 VAL H CA  1 
ATOM   8887 C  C   . VAL H  4  120 ? 27.459 49.860  30.515  1.00 45.51  ? 120 VAL H C   1 
ATOM   8888 O  O   . VAL H  4  120 ? 27.923 48.847  31.028  1.00 47.50  ? 120 VAL H O   1 
ATOM   8889 C  CB  . VAL H  4  120 ? 25.045 50.617  30.707  1.00 44.45  ? 120 VAL H CB  1 
ATOM   8890 C  CG1 . VAL H  4  120 ? 24.740 49.174  30.377  1.00 42.10  ? 120 VAL H CG1 1 
ATOM   8891 C  CG2 . VAL H  4  120 ? 24.030 51.167  31.712  1.00 42.93  ? 120 VAL H CG2 1 
ATOM   8892 N  N   . LEU H  4  121 ? 27.795 50.247  29.295  1.00 45.59  ? 121 LEU H N   1 
ATOM   8893 C  CA  . LEU H  4  121 ? 28.699 49.467  28.472  1.00 46.53  ? 121 LEU H CA  1 
ATOM   8894 C  C   . LEU H  4  121 ? 30.024 48.981  29.079  1.00 47.38  ? 121 LEU H C   1 
ATOM   8895 O  O   . LEU H  4  121 ? 30.389 47.817  28.904  1.00 47.48  ? 121 LEU H O   1 
ATOM   8896 C  CB  . LEU H  4  121 ? 28.988 50.227  27.186  1.00 46.90  ? 121 LEU H CB  1 
ATOM   8897 C  CG  . LEU H  4  121 ? 27.740 50.453  26.340  1.00 47.60  ? 121 LEU H CG  1 
ATOM   8898 C  CD1 . LEU H  4  121 ? 28.116 51.197  25.070  1.00 46.62  ? 121 LEU H CD1 1 
ATOM   8899 C  CD2 . LEU H  4  121 ? 27.092 49.104  26.017  1.00 49.62  ? 121 LEU H CD2 1 
ATOM   8900 N  N   . PRO H  4  122 ? 30.770 49.854  29.767  1.00 47.53  ? 122 PRO H N   1 
ATOM   8901 C  CA  . PRO H  4  122 ? 32.023 49.332  30.316  1.00 49.72  ? 122 PRO H CA  1 
ATOM   8902 C  C   . PRO H  4  122 ? 31.873 48.084  31.194  1.00 51.14  ? 122 PRO H C   1 
ATOM   8903 O  O   . PRO H  4  122 ? 32.807 47.287  31.319  1.00 52.02  ? 122 PRO H O   1 
ATOM   8904 C  CB  . PRO H  4  122 ? 32.624 50.537  31.055  1.00 48.51  ? 122 PRO H CB  1 
ATOM   8905 C  CG  . PRO H  4  122 ? 31.508 51.576  31.097  1.00 47.21  ? 122 PRO H CG  1 
ATOM   8906 C  CD  . PRO H  4  122 ? 30.714 51.322  29.869  1.00 46.99  ? 122 PRO H CD  1 
ATOM   8907 N  N   . SER H  4  123 ? 30.698 47.897  31.782  1.00 52.16  ? 123 SER H N   1 
ATOM   8908 C  CA  . SER H  4  123 ? 30.468 46.732  32.629  1.00 53.39  ? 123 SER H CA  1 
ATOM   8909 C  C   . SER H  4  123 ? 30.132 45.505  31.797  1.00 54.15  ? 123 SER H C   1 
ATOM   8910 O  O   . SER H  4  123 ? 30.055 44.399  32.329  1.00 56.30  ? 123 SER H O   1 
ATOM   8911 C  CB  . SER H  4  123 ? 29.314 46.989  33.610  1.00 54.33  ? 123 SER H CB  1 
ATOM   8912 O  OG  . SER H  4  123 ? 29.632 48.012  34.536  1.00 54.48  ? 123 SER H OG  1 
ATOM   8913 N  N   . LEU H  4  124 ? 29.915 45.696  30.497  1.00 53.59  ? 124 LEU H N   1 
ATOM   8914 C  CA  . LEU H  4  124 ? 29.584 44.580  29.613  1.00 51.64  ? 124 LEU H CA  1 
ATOM   8915 C  C   . LEU H  4  124 ? 30.723 44.264  28.636  1.00 49.90  ? 124 LEU H C   1 
ATOM   8916 O  O   . LEU H  4  124 ? 31.011 43.105  28.341  1.00 49.50  ? 124 LEU H O   1 
ATOM   8917 C  CB  . LEU H  4  124 ? 28.305 44.896  28.829  1.00 51.18  ? 124 LEU H CB  1 
ATOM   8918 C  CG  . LEU H  4  124 ? 26.980 45.073  29.593  1.00 51.78  ? 124 LEU H CG  1 
ATOM   8919 C  CD1 . LEU H  4  124 ? 25.951 45.743  28.704  1.00 51.09  ? 124 LEU H CD1 1 
ATOM   8920 C  CD2 . LEU H  4  124 ? 26.464 43.735  30.061  1.00 51.16  ? 124 LEU H CD2 1 
ATOM   8921 N  N   . ILE H  4  125 ? 31.375 45.317  28.160  1.00 48.60  ? 125 ILE H N   1 
ATOM   8922 C  CA  . ILE H  4  125 ? 32.446 45.216  27.176  1.00 46.81  ? 125 ILE H CA  1 
ATOM   8923 C  C   . ILE H  4  125 ? 33.868 45.065  27.723  1.00 47.06  ? 125 ILE H C   1 
ATOM   8924 O  O   . ILE H  4  125 ? 34.254 45.713  28.697  1.00 46.83  ? 125 ILE H O   1 
ATOM   8925 C  CB  . ILE H  4  125 ? 32.374 46.445  26.234  1.00 45.17  ? 125 ILE H CB  1 
ATOM   8926 C  CG1 . ILE H  4  125 ? 31.069 46.371  25.408  1.00 43.27  ? 125 ILE H CG1 1 
ATOM   8927 C  CG2 . ILE H  4  125 ? 33.616 46.522  25.366  1.00 43.41  ? 125 ILE H CG2 1 
ATOM   8928 C  CD1 . ILE H  4  125 ? 30.715 47.641  24.648  1.00 39.24  ? 125 ILE H CD1 1 
ATOM   8929 N  N   . ASP H  4  126 ? 34.639 44.183  27.085  1.00 48.09  ? 126 ASP H N   1 
ATOM   8930 C  CA  . ASP H  4  126 ? 36.017 43.959  27.481  1.00 47.89  ? 126 ASP H CA  1 
ATOM   8931 C  C   . ASP H  4  126 ? 36.836 45.170  27.134  1.00 47.93  ? 126 ASP H C   1 
ATOM   8932 O  O   . ASP H  4  126 ? 36.913 45.578  25.985  1.00 47.76  ? 126 ASP H O   1 
ATOM   8933 C  CB  . ASP H  4  126 ? 36.621 42.750  26.773  1.00 46.63  ? 126 ASP H CB  1 
ATOM   8934 C  CG  . ASP H  4  126 ? 36.046 41.434  27.265  1.00 49.19  ? 126 ASP H CG  1 
ATOM   8935 O  OD1 . ASP H  4  126 ? 35.623 41.341  28.447  1.00 50.01  ? 126 ASP H OD1 1 
ATOM   8936 O  OD2 . ASP H  4  126 ? 36.035 40.476  26.464  1.00 46.81  ? 126 ASP H OD2 1 
ATOM   8937 N  N   . ASN H  4  127 ? 37.434 45.753  28.156  1.00 48.57  ? 127 ASN H N   1 
ATOM   8938 C  CA  . ASN H  4  127 ? 38.288 46.901  27.985  1.00 48.73  ? 127 ASN H CA  1 
ATOM   8939 C  C   . ASN H  4  127 ? 37.694 47.961  27.086  1.00 48.55  ? 127 ASN H C   1 
ATOM   8940 O  O   . ASN H  4  127 ? 38.237 48.306  26.043  1.00 48.49  ? 127 ASN H O   1 
ATOM   8941 C  CB  . ASN H  4  127 ? 39.634 46.435  27.462  1.00 52.10  ? 127 ASN H CB  1 
ATOM   8942 C  CG  . ASN H  4  127 ? 40.710 47.429  27.712  1.00 56.11  ? 127 ASN H CG  1 
ATOM   8943 O  OD1 . ASN H  4  127 ? 40.856 47.945  28.828  1.00 59.46  ? 127 ASN H OD1 1 
ATOM   8944 N  ND2 . ASN H  4  127 ? 41.491 47.708  26.685  1.00 58.90  ? 127 ASN H ND2 1 
ATOM   8945 N  N   . PHE H  4  128 ? 36.558 48.473  27.540  1.00 49.61  ? 128 PHE H N   1 
ATOM   8946 C  CA  . PHE H  4  128 ? 35.790 49.528  26.887  1.00 49.55  ? 128 PHE H CA  1 
ATOM   8947 C  C   . PHE H  4  128 ? 36.648 50.751  26.598  1.00 50.78  ? 128 PHE H C   1 
ATOM   8948 O  O   . PHE H  4  128 ? 37.485 51.145  27.405  1.00 51.48  ? 128 PHE H O   1 
ATOM   8949 C  CB  . PHE H  4  128 ? 34.632 49.930  27.817  1.00 48.17  ? 128 PHE H CB  1 
ATOM   8950 C  CG  . PHE H  4  128 ? 33.693 50.950  27.234  1.00 44.10  ? 128 PHE H CG  1 
ATOM   8951 C  CD1 . PHE H  4  128 ? 32.744 50.571  26.282  1.00 43.24  ? 128 PHE H CD1 1 
ATOM   8952 C  CD2 . PHE H  4  128 ? 33.738 52.283  27.659  1.00 41.70  ? 128 PHE H CD2 1 
ATOM   8953 C  CE1 . PHE H  4  128 ? 31.854 51.494  25.766  1.00 42.51  ? 128 PHE H CE1 1 
ATOM   8954 C  CE2 . PHE H  4  128 ? 32.850 53.224  27.150  1.00 40.00  ? 128 PHE H CE2 1 
ATOM   8955 C  CZ  . PHE H  4  128 ? 31.905 52.828  26.202  1.00 43.70  ? 128 PHE H CZ  1 
ATOM   8956 N  N   . ASN H  4  129 ? 36.418 51.365  25.445  1.00 52.90  ? 129 ASN H N   1 
ATOM   8957 C  CA  . ASN H  4  129 ? 37.166 52.545  25.038  1.00 54.31  ? 129 ASN H CA  1 
ATOM   8958 C  C   . ASN H  4  129 ? 36.204 53.716  25.054  1.00 55.56  ? 129 ASN H C   1 
ATOM   8959 O  O   . ASN H  4  129 ? 35.438 53.914  24.110  1.00 57.03  ? 129 ASN H O   1 
ATOM   8960 C  CB  . ASN H  4  129 ? 37.716 52.366  23.615  1.00 54.62  ? 129 ASN H CB  1 
ATOM   8961 C  CG  . ASN H  4  129 ? 38.697 53.470  23.210  1.00 54.70  ? 129 ASN H CG  1 
ATOM   8962 O  OD1 . ASN H  4  129 ? 38.522 54.636  23.554  1.00 54.43  ? 129 ASN H OD1 1 
ATOM   8963 N  ND2 . ASN H  4  129 ? 39.728 53.099  22.461  1.00 55.26  ? 129 ASN H ND2 1 
ATOM   8964 N  N   . PRO H  4  130 ? 36.231 54.512  26.129  1.00 56.23  ? 130 PRO H N   1 
ATOM   8965 C  CA  . PRO H  4  130 ? 35.342 55.678  26.251  1.00 55.03  ? 130 PRO H CA  1 
ATOM   8966 C  C   . PRO H  4  130 ? 35.517 56.760  25.180  1.00 55.19  ? 130 PRO H C   1 
ATOM   8967 O  O   . PRO H  4  130 ? 34.549 57.430  24.804  1.00 55.16  ? 130 PRO H O   1 
ATOM   8968 C  CB  . PRO H  4  130 ? 35.646 56.203  27.657  1.00 53.80  ? 130 PRO H CB  1 
ATOM   8969 C  CG  . PRO H  4  130 ? 37.052 55.797  27.887  1.00 54.61  ? 130 PRO H CG  1 
ATOM   8970 C  CD  . PRO H  4  130 ? 37.088 54.377  27.323  1.00 56.25  ? 130 PRO H CD  1 
ATOM   8971 N  N   . ASP H  4  131 ? 36.740 56.946  24.694  1.00 55.14  ? 131 ASP H N   1 
ATOM   8972 C  CA  . ASP H  4  131 ? 36.987 57.974  23.682  1.00 55.15  ? 131 ASP H CA  1 
ATOM   8973 C  C   . ASP H  4  131 ? 36.452 57.604  22.313  1.00 53.88  ? 131 ASP H C   1 
ATOM   8974 O  O   . ASP H  4  131 ? 35.809 58.427  21.649  1.00 51.85  ? 131 ASP H O   1 
ATOM   8975 C  CB  . ASP H  4  131 ? 38.481 58.288  23.584  1.00 56.20  ? 131 ASP H CB  1 
ATOM   8976 C  CG  . ASP H  4  131 ? 38.974 59.135  24.742  1.00 57.10  ? 131 ASP H CG  1 
ATOM   8977 O  OD1 . ASP H  4  131 ? 40.157 59.522  24.742  1.00 57.14  ? 131 ASP H OD1 1 
ATOM   8978 O  OD2 . ASP H  4  131 ? 38.181 59.420  25.662  1.00 59.78  ? 131 ASP H OD2 1 
ATOM   8979 N  N   . ALA H  4  132 ? 36.723 56.373  21.895  1.00 53.97  ? 132 ALA H N   1 
ATOM   8980 C  CA  . ALA H  4  132 ? 36.263 55.890  20.600  1.00 54.66  ? 132 ALA H CA  1 
ATOM   8981 C  C   . ALA H  4  132 ? 34.745 55.863  20.596  1.00 55.26  ? 132 ALA H C   1 
ATOM   8982 O  O   . ALA H  4  132 ? 34.140 56.254  19.601  1.00 55.26  ? 132 ALA H O   1 
ATOM   8983 C  CB  . ALA H  4  132 ? 36.832 54.493  20.306  1.00 53.08  ? 132 ALA H CB  1 
ATOM   8984 N  N   . TRP H  4  133 ? 34.128 55.423  21.700  1.00 55.29  ? 133 TRP H N   1 
ATOM   8985 C  CA  . TRP H  4  133 ? 32.664 55.391  21.764  1.00 55.57  ? 133 TRP H CA  1 
ATOM   8986 C  C   . TRP H  4  133 ? 32.081 56.807  21.752  1.00 57.17  ? 133 TRP H C   1 
ATOM   8987 O  O   . TRP H  4  133 ? 31.111 57.072  21.037  1.00 56.36  ? 133 TRP H O   1 
ATOM   8988 C  CB  . TRP H  4  133 ? 32.174 54.613  23.002  1.00 51.81  ? 133 TRP H CB  1 
ATOM   8989 C  CG  . TRP H  4  133 ? 32.139 53.115  22.770  1.00 51.76  ? 133 TRP H CG  1 
ATOM   8990 C  CD1 . TRP H  4  133 ? 33.188 52.235  22.862  1.00 53.23  ? 133 TRP H CD1 1 
ATOM   8991 C  CD2 . TRP H  4  133 ? 31.015 52.342  22.328  1.00 50.11  ? 133 TRP H CD2 1 
ATOM   8992 N  NE1 . TRP H  4  133 ? 32.783 50.969  22.498  1.00 52.70  ? 133 TRP H NE1 1 
ATOM   8993 C  CE2 . TRP H  4  133 ? 31.454 51.011  22.169  1.00 50.51  ? 133 TRP H CE2 1 
ATOM   8994 C  CE3 . TRP H  4  133 ? 29.679 52.653  22.044  1.00 50.38  ? 133 TRP H CE3 1 
ATOM   8995 C  CZ2 . TRP H  4  133 ? 30.604 49.989  21.738  1.00 51.56  ? 133 TRP H CZ2 1 
ATOM   8996 C  CZ3 . TRP H  4  133 ? 28.833 51.635  21.618  1.00 49.66  ? 133 TRP H CZ3 1 
ATOM   8997 C  CH2 . TRP H  4  133 ? 29.299 50.319  21.469  1.00 50.90  ? 133 TRP H CH2 1 
ATOM   8998 N  N   . ARG H  4  134 ? 32.677 57.720  22.518  1.00 58.58  ? 134 ARG H N   1 
ATOM   8999 C  CA  . ARG H  4  134 ? 32.178 59.086  22.539  1.00 61.63  ? 134 ARG H CA  1 
ATOM   9000 C  C   . ARG H  4  134 ? 32.264 59.666  21.149  1.00 62.55  ? 134 ARG H C   1 
ATOM   9001 O  O   . ARG H  4  134 ? 31.327 60.301  20.685  1.00 63.37  ? 134 ARG H O   1 
ATOM   9002 C  CB  . ARG H  4  134 ? 32.990 59.978  23.470  1.00 64.94  ? 134 ARG H CB  1 
ATOM   9003 C  CG  . ARG H  4  134 ? 32.686 59.824  24.940  1.00 70.44  ? 134 ARG H CG  1 
ATOM   9004 C  CD  . ARG H  4  134 ? 33.224 61.015  25.732  1.00 72.58  ? 134 ARG H CD  1 
ATOM   9005 N  NE  . ARG H  4  134 ? 33.080 60.805  27.169  1.00 76.82  ? 134 ARG H NE  1 
ATOM   9006 C  CZ  . ARG H  4  134 ? 33.952 60.125  27.909  1.00 80.31  ? 134 ARG H CZ  1 
ATOM   9007 N  NH1 . ARG H  4  134 ? 35.039 59.601  27.342  1.00 82.22  ? 134 ARG H NH1 1 
ATOM   9008 N  NH2 . ARG H  4  134 ? 33.729 59.958  29.209  1.00 80.69  ? 134 ARG H NH2 1 
ATOM   9009 N  N   . ASN H  4  135 ? 33.396 59.457  20.489  1.00 62.42  ? 135 ASN H N   1 
ATOM   9010 C  CA  . ASN H  4  135 ? 33.579 59.980  19.145  1.00 63.15  ? 135 ASN H CA  1 
ATOM   9011 C  C   . ASN H  4  135 ? 32.513 59.508  18.172  1.00 62.17  ? 135 ASN H C   1 
ATOM   9012 O  O   . ASN H  4  135 ? 32.068 60.288  17.331  1.00 61.48  ? 135 ASN H O   1 
ATOM   9013 C  CB  . ASN H  4  135 ? 34.949 59.594  18.605  1.00 65.52  ? 135 ASN H CB  1 
ATOM   9014 C  CG  . ASN H  4  135 ? 36.062 60.389  19.244  1.00 67.74  ? 135 ASN H CG  1 
ATOM   9015 O  OD1 . ASN H  4  135 ? 35.809 61.404  19.891  1.00 66.91  ? 135 ASN H OD1 1 
ATOM   9016 N  ND2 . ASN H  4  135 ? 37.306 59.945  19.056  1.00 69.14  ? 135 ASN H ND2 1 
ATOM   9017 N  N   . CYS H  4  136 ? 32.120 58.239  18.288  1.00 61.09  ? 136 CYS H N   1 
ATOM   9018 C  CA  . CYS H  4  136 ? 31.113 57.663  17.405  1.00 61.65  ? 136 CYS H CA  1 
ATOM   9019 C  C   . CYS H  4  136 ? 29.662 57.770  17.890  1.00 62.99  ? 136 CYS H C   1 
ATOM   9020 O  O   . CYS H  4  136 ? 28.760 57.977  17.077  1.00 62.56  ? 136 CYS H O   1 
ATOM   9021 C  CB  . CYS H  4  136 ? 31.429 56.197  17.109  1.00 59.91  ? 136 CYS H CB  1 
ATOM   9022 S  SG  . CYS H  4  136 ? 32.965 55.887  16.170  1.00 59.53  ? 136 CYS H SG  1 
ATOM   9023 N  N   . LEU H  4  137 ? 29.423 57.624  19.193  1.00 63.55  ? 137 LEU H N   1 
ATOM   9024 C  CA  . LEU H  4  137 ? 28.052 57.712  19.695  1.00 64.23  ? 137 LEU H CA  1 
ATOM   9025 C  C   . LEU H  4  137 ? 27.428 59.098  19.609  1.00 64.80  ? 137 LEU H C   1 
ATOM   9026 O  O   . LEU H  4  137 ? 26.293 59.236  19.178  1.00 64.88  ? 137 LEU H O   1 
ATOM   9027 C  CB  . LEU H  4  137 ? 27.969 57.236  21.145  1.00 64.19  ? 137 LEU H CB  1 
ATOM   9028 C  CG  . LEU H  4  137 ? 27.687 55.753  21.372  1.00 64.48  ? 137 LEU H CG  1 
ATOM   9029 C  CD1 . LEU H  4  137 ? 27.139 55.562  22.786  1.00 63.92  ? 137 LEU H CD1 1 
ATOM   9030 C  CD2 . LEU H  4  137 ? 26.667 55.254  20.371  1.00 64.00  ? 137 LEU H CD2 1 
ATOM   9031 N  N   . LEU H  4  138 ? 28.165 60.121  20.020  1.00 66.16  ? 138 LEU H N   1 
ATOM   9032 C  CA  . LEU H  4  138 ? 27.639 61.486  19.989  1.00 67.44  ? 138 LEU H CA  1 
ATOM   9033 C  C   . LEU H  4  138 ? 27.030 61.886  18.635  1.00 66.87  ? 138 LEU H C   1 
ATOM   9034 O  O   . LEU H  4  138 ? 25.890 62.345  18.569  1.00 65.44  ? 138 LEU H O   1 
ATOM   9035 C  CB  . LEU H  4  138 ? 28.734 62.475  20.418  1.00 69.45  ? 138 LEU H CB  1 
ATOM   9036 C  CG  . LEU H  4  138 ? 28.644 63.064  21.847  1.00 71.64  ? 138 LEU H CG  1 
ATOM   9037 C  CD1 . LEU H  4  138 ? 28.755 61.977  22.910  1.00 69.76  ? 138 LEU H CD1 1 
ATOM   9038 C  CD2 . LEU H  4  138 ? 29.758 64.088  22.012  1.00 71.93  ? 138 LEU H CD2 1 
ATOM   9039 N  N   . PRO H  4  139 ? 27.767 61.710  17.530  1.00 66.72  ? 139 PRO H N   1 
ATOM   9040 C  CA  . PRO H  4  139 ? 27.180 62.095  16.243  1.00 66.23  ? 139 PRO H CA  1 
ATOM   9041 C  C   . PRO H  4  139 ? 25.933 61.282  15.928  1.00 66.58  ? 139 PRO H C   1 
ATOM   9042 O  O   . PRO H  4  139 ? 24.987 61.785  15.328  1.00 66.45  ? 139 PRO H O   1 
ATOM   9043 C  CB  . PRO H  4  139 ? 28.299 61.821  15.252  1.00 66.18  ? 139 PRO H CB  1 
ATOM   9044 C  CG  . PRO H  4  139 ? 29.529 62.082  16.081  1.00 67.49  ? 139 PRO H CG  1 
ATOM   9045 C  CD  . PRO H  4  139 ? 29.203 61.414  17.389  1.00 66.34  ? 139 PRO H CD  1 
ATOM   9046 N  N   . LEU H  4  140 ? 25.953 60.020  16.341  1.00 67.37  ? 140 LEU H N   1 
ATOM   9047 C  CA  . LEU H  4  140 ? 24.843 59.107  16.121  1.00 67.88  ? 140 LEU H CA  1 
ATOM   9048 C  C   . LEU H  4  140 ? 23.627 59.568  16.910  1.00 67.78  ? 140 LEU H C   1 
ATOM   9049 O  O   . LEU H  4  140 ? 22.514 59.650  16.398  1.00 67.81  ? 140 LEU H O   1 
ATOM   9050 C  CB  . LEU H  4  140 ? 25.231 57.700  16.566  1.00 68.08  ? 140 LEU H CB  1 
ATOM   9051 C  CG  . LEU H  4  140 ? 25.081 56.583  15.540  1.00 71.02  ? 140 LEU H CG  1 
ATOM   9052 C  CD1 . LEU H  4  140 ? 25.595 55.279  16.144  1.00 71.87  ? 140 LEU H CD1 1 
ATOM   9053 C  CD2 . LEU H  4  140 ? 23.623 56.459  15.106  1.00 70.87  ? 140 LEU H CD2 1 
ATOM   9054 N  N   . LYS H  4  141 ? 23.859 59.877  18.172  1.00 67.62  ? 141 LYS H N   1 
ATOM   9055 C  CA  . LYS H  4  141 ? 22.797 60.323  19.038  1.00 68.01  ? 141 LYS H CA  1 
ATOM   9056 C  C   . LYS H  4  141 ? 22.232 61.631  18.502  1.00 67.24  ? 141 LYS H C   1 
ATOM   9057 O  O   . LYS H  4  141 ? 21.020 61.825  18.498  1.00 67.58  ? 141 LYS H O   1 
ATOM   9058 C  CB  . LYS H  4  141 ? 23.345 60.478  20.463  1.00 70.28  ? 141 LYS H CB  1 
ATOM   9059 C  CG  . LYS H  4  141 ? 22.333 60.916  21.508  1.00 70.93  ? 141 LYS H CG  1 
ATOM   9060 C  CD  . LYS H  4  141 ? 22.441 62.400  21.755  1.00 71.75  ? 141 LYS H CD  1 
ATOM   9061 C  CE  . LYS H  4  141 ? 23.824 62.745  22.285  1.00 73.37  ? 141 LYS H CE  1 
ATOM   9062 N  NZ  . LYS H  4  141 ? 24.015 64.212  22.437  1.00 73.82  ? 141 LYS H NZ  1 
ATOM   9063 N  N   . ASN H  4  142 ? 23.097 62.523  18.029  1.00 65.66  ? 142 ASN H N   1 
ATOM   9064 C  CA  . ASN H  4  142 ? 22.606 63.795  17.505  1.00 65.11  ? 142 ASN H CA  1 
ATOM   9065 C  C   . ASN H  4  142 ? 21.766 63.626  16.254  1.00 65.08  ? 142 ASN H C   1 
ATOM   9066 O  O   . ASN H  4  142 ? 20.787 64.342  16.059  1.00 67.27  ? 142 ASN H O   1 
ATOM   9067 C  CB  . ASN H  4  142 ? 23.742 64.772  17.191  1.00 62.78  ? 142 ASN H CB  1 
ATOM   9068 C  CG  . ASN H  4  142 ? 24.467 65.244  18.426  1.00 62.12  ? 142 ASN H CG  1 
ATOM   9069 O  OD1 . ASN H  4  142 ? 23.923 65.233  19.545  1.00 58.39  ? 142 ASN H OD1 1 
ATOM   9070 N  ND2 . ASN H  4  142 ? 25.711 65.677  18.236  1.00 62.23  ? 142 ASN H ND2 1 
ATOM   9071 N  N   . ALA H  4  143 ? 22.143 62.688  15.396  1.00 64.54  ? 143 ALA H N   1 
ATOM   9072 C  CA  . ALA H  4  143 ? 21.384 62.474  14.177  1.00 64.68  ? 143 ALA H CA  1 
ATOM   9073 C  C   . ALA H  4  143 ? 19.978 61.950  14.474  1.00 65.18  ? 143 ALA H C   1 
ATOM   9074 O  O   . ALA H  4  143 ? 19.007 62.339  13.817  1.00 65.11  ? 143 ALA H O   1 
ATOM   9075 C  CB  . ALA H  4  143 ? 22.122 61.506  13.264  1.00 62.56  ? 143 ALA H CB  1 
ATOM   9076 N  N   . ILE H  4  144 ? 19.869 61.069  15.465  1.00 65.58  ? 144 ILE H N   1 
ATOM   9077 C  CA  . ILE H  4  144 ? 18.580 60.493  15.824  1.00 67.45  ? 144 ILE H CA  1 
ATOM   9078 C  C   . ILE H  4  144 ? 17.700 61.498  16.563  1.00 69.17  ? 144 ILE H C   1 
ATOM   9079 O  O   . ILE H  4  144 ? 16.487 61.506  16.406  1.00 69.71  ? 144 ILE H O   1 
ATOM   9080 C  CB  . ILE H  4  144 ? 18.749 59.237  16.718  1.00 66.53  ? 144 ILE H CB  1 
ATOM   9081 C  CG1 . ILE H  4  144 ? 19.557 58.173  15.971  1.00 65.48  ? 144 ILE H CG1 1 
ATOM   9082 C  CG2 . ILE H  4  144 ? 17.380 58.683  17.123  1.00 64.37  ? 144 ILE H CG2 1 
ATOM   9083 C  CD1 . ILE H  4  144 ? 19.838 56.944  16.794  1.00 64.87  ? 144 ILE H CD1 1 
ATOM   9084 N  N   . ALA H  4  145 ? 18.322 62.351  17.364  1.00 70.91  ? 145 ALA H N   1 
ATOM   9085 C  CA  . ALA H  4  145 ? 17.588 63.339  18.136  1.00 72.41  ? 145 ALA H CA  1 
ATOM   9086 C  C   . ALA H  4  145 ? 17.482 64.651  17.364  1.00 73.47  ? 145 ALA H C   1 
ATOM   9087 O  O   . ALA H  4  145 ? 17.240 65.710  17.943  1.00 74.25  ? 145 ALA H O   1 
ATOM   9088 C  CB  . ALA H  4  145 ? 18.276 63.558  19.485  1.00 70.88  ? 145 ALA H CB  1 
ATOM   9089 N  N   . LYS H  4  146 ? 17.679 64.573  16.052  1.00 74.37  ? 146 LYS H N   1 
ATOM   9090 C  CA  . LYS H  4  146 ? 17.629 65.744  15.180  1.00 75.22  ? 146 LYS H CA  1 
ATOM   9091 C  C   . LYS H  4  146 ? 16.223 66.342  15.153  1.00 75.51  ? 146 LYS H C   1 
ATOM   9092 O  O   . LYS H  4  146 ? 15.298 65.723  14.636  1.00 76.42  ? 146 LYS H O   1 
ATOM   9093 C  CB  . LYS H  4  146 ? 18.027 65.325  13.765  1.00 75.96  ? 146 LYS H CB  1 
ATOM   9094 C  CG  . LYS H  4  146 ? 18.874 66.330  13.000  1.00 77.03  ? 146 LYS H CG  1 
ATOM   9095 C  CD  . LYS H  4  146 ? 18.402 66.403  11.559  1.00 78.12  ? 146 LYS H CD  1 
ATOM   9096 C  CE  . LYS H  4  146 ? 19.551 66.459  10.563  1.00 79.58  ? 146 LYS H CE  1 
ATOM   9097 N  NZ  . LYS H  4  146 ? 19.053 66.362  9.154   1.00 80.47  ? 146 LYS H NZ  1 
ATOM   9098 N  N   . GLY H  4  147 ? 16.059 67.537  15.706  1.00 75.45  ? 147 GLY H N   1 
ATOM   9099 C  CA  . GLY H  4  147 ? 14.749 68.167  15.693  1.00 76.37  ? 147 GLY H CA  1 
ATOM   9100 C  C   . GLY H  4  147 ? 13.945 68.075  16.982  1.00 76.56  ? 147 GLY H C   1 
ATOM   9101 O  O   . GLY H  4  147 ? 12.782 68.487  17.031  1.00 77.26  ? 147 GLY H O   1 
ATOM   9102 N  N   . LEU H  4  148 ? 14.553 67.525  18.027  1.00 75.88  ? 148 LEU H N   1 
ATOM   9103 C  CA  . LEU H  4  148 ? 13.880 67.403  19.310  1.00 74.59  ? 148 LEU H CA  1 
ATOM   9104 C  C   . LEU H  4  148 ? 14.203 68.635  20.148  1.00 75.23  ? 148 LEU H C   1 
ATOM   9105 O  O   . LEU H  4  148 ? 15.319 69.160  20.095  1.00 74.43  ? 148 LEU H O   1 
ATOM   9106 C  CB  . LEU H  4  148 ? 14.328 66.131  20.042  1.00 72.54  ? 148 LEU H CB  1 
ATOM   9107 C  CG  . LEU H  4  148 ? 14.034 64.804  19.335  1.00 70.40  ? 148 LEU H CG  1 
ATOM   9108 C  CD1 . LEU H  4  148 ? 14.644 63.681  20.108  1.00 68.52  ? 148 LEU H CD1 1 
ATOM   9109 C  CD2 . LEU H  4  148 ? 12.530 64.592  19.200  1.00 70.23  ? 148 LEU H CD2 1 
ATOM   9110 N  N   . PRO H  4  149 ? 13.221 69.124  20.919  1.00 76.03  ? 149 PRO H N   1 
ATOM   9111 C  CA  . PRO H  4  149 ? 13.359 70.299  21.781  1.00 76.82  ? 149 PRO H CA  1 
ATOM   9112 C  C   . PRO H  4  149 ? 14.089 70.008  23.092  1.00 78.14  ? 149 PRO H C   1 
ATOM   9113 O  O   . PRO H  4  149 ? 15.094 70.696  23.372  1.00 78.51  ? 149 PRO H O   1 
ATOM   9114 C  CB  . PRO H  4  149 ? 11.914 70.723  22.002  1.00 77.06  ? 149 PRO H CB  1 
ATOM   9115 C  CG  . PRO H  4  149 ? 11.192 69.399  22.031  1.00 75.80  ? 149 PRO H CG  1 
ATOM   9116 C  CD  . PRO H  4  149 ? 11.815 68.672  20.868  1.00 75.79  ? 149 PRO H CD  1 
ATOM   9117 O  OXT . PRO H  4  149 ? 13.642 69.097  23.829  1.00 79.84  ? 149 PRO H OXT 1 
HETATM 9118 C  CHA . HEM I  5  .   ? 15.573 2.721   -6.335  1.00 38.86  ? 201 HEM A CHA 1 
HETATM 9119 C  CHB . HEM I  5  .   ? 15.589 6.962   -8.399  1.00 37.95  ? 201 HEM A CHB 1 
HETATM 9120 C  CHC . HEM I  5  .   ? 12.887 8.754   -4.924  1.00 36.89  ? 201 HEM A CHC 1 
HETATM 9121 C  CHD . HEM I  5  .   ? 12.830 4.469   -2.861  1.00 37.21  ? 201 HEM A CHD 1 
HETATM 9122 C  C1A . HEM I  5  .   ? 15.847 3.714   -7.257  1.00 39.02  ? 201 HEM A C1A 1 
HETATM 9123 C  C2A . HEM I  5  .   ? 16.655 3.525   -8.400  1.00 42.49  ? 201 HEM A C2A 1 
HETATM 9124 C  C3A . HEM I  5  .   ? 16.662 4.722   -8.997  1.00 41.04  ? 201 HEM A C3A 1 
HETATM 9125 C  C4A . HEM I  5  .   ? 15.847 5.650   -8.190  1.00 40.42  ? 201 HEM A C4A 1 
HETATM 9126 C  CMA . HEM I  5  .   ? 17.376 5.128   -10.274 1.00 40.94  ? 201 HEM A CMA 1 
HETATM 9127 C  CAA . HEM I  5  .   ? 17.372 2.262   -8.852  1.00 45.01  ? 201 HEM A CAA 1 
HETATM 9128 C  CBA . HEM I  5  .   ? 16.572 1.443   -9.819  1.00 47.23  ? 201 HEM A CBA 1 
HETATM 9129 C  CGA . HEM I  5  .   ? 17.282 0.172   -10.296 1.00 50.61  ? 201 HEM A CGA 1 
HETATM 9130 O  O1A . HEM I  5  .   ? 16.871 -0.961  -9.930  1.00 50.57  ? 201 HEM A O1A 1 
HETATM 9131 O  O2A . HEM I  5  .   ? 18.232 0.304   -11.019 1.00 53.22  ? 201 HEM A O2A 1 
HETATM 9132 C  C1B . HEM I  5  .   ? 14.843 7.904   -7.649  1.00 36.04  ? 201 HEM A C1B 1 
HETATM 9133 C  C2B . HEM I  5  .   ? 14.673 9.312   -7.996  1.00 36.42  ? 201 HEM A C2B 1 
HETATM 9134 C  C3B . HEM I  5  .   ? 13.863 9.822   -6.954  1.00 37.06  ? 201 HEM A C3B 1 
HETATM 9135 C  C4B . HEM I  5  .   ? 13.639 8.712   -6.104  1.00 37.10  ? 201 HEM A C4B 1 
HETATM 9136 C  CMB . HEM I  5  .   ? 15.243 10.002  -9.167  1.00 35.01  ? 201 HEM A CMB 1 
HETATM 9137 C  CAB . HEM I  5  .   ? 13.431 11.192  -6.858  1.00 41.89  ? 201 HEM A CAB 1 
HETATM 9138 C  CBB . HEM I  5  .   ? 12.400 11.698  -7.495  1.00 43.36  ? 201 HEM A CBB 1 
HETATM 9139 C  C1C . HEM I  5  .   ? 12.636 7.725   -4.049  1.00 37.66  ? 201 HEM A C1C 1 
HETATM 9140 C  C2C . HEM I  5  .   ? 11.829 7.925   -2.811  1.00 39.31  ? 201 HEM A C2C 1 
HETATM 9141 C  C3C . HEM I  5  .   ? 11.785 6.686   -2.179  1.00 40.33  ? 201 HEM A C3C 1 
HETATM 9142 C  C4C . HEM I  5  .   ? 12.603 5.788   -3.116  1.00 36.83  ? 201 HEM A C4C 1 
HETATM 9143 C  CMC . HEM I  5  .   ? 11.198 9.264   -2.356  1.00 39.46  ? 201 HEM A CMC 1 
HETATM 9144 C  CAC . HEM I  5  .   ? 11.174 6.384   -1.013  1.00 43.05  ? 201 HEM A CAC 1 
HETATM 9145 C  CBC . HEM I  5  .   ? 11.332 6.649   0.238   1.00 44.74  ? 201 HEM A CBC 1 
HETATM 9146 C  C1D . HEM I  5  .   ? 13.578 3.581   -3.626  1.00 37.40  ? 201 HEM A C1D 1 
HETATM 9147 C  C2D . HEM I  5  .   ? 13.804 2.101   -3.243  1.00 37.74  ? 201 HEM A C2D 1 
HETATM 9148 C  C3D . HEM I  5  .   ? 14.591 1.630   -4.256  1.00 37.36  ? 201 HEM A C3D 1 
HETATM 9149 C  C4D . HEM I  5  .   ? 14.819 2.789   -5.198  1.00 37.53  ? 201 HEM A C4D 1 
HETATM 9150 C  CMD . HEM I  5  .   ? 13.246 1.406   -1.999  1.00 34.94  ? 201 HEM A CMD 1 
HETATM 9151 C  CAD . HEM I  5  .   ? 15.143 0.234   -4.435  1.00 36.58  ? 201 HEM A CAD 1 
HETATM 9152 C  CBD . HEM I  5  .   ? 16.487 0.057   -3.815  1.00 37.18  ? 201 HEM A CBD 1 
HETATM 9153 C  CGD . HEM I  5  .   ? 16.995 -1.283  -4.053  1.00 38.37  ? 201 HEM A CGD 1 
HETATM 9154 O  O1D . HEM I  5  .   ? 16.918 -2.154  -3.132  1.00 38.65  ? 201 HEM A O1D 1 
HETATM 9155 O  O2D . HEM I  5  .   ? 17.499 -1.536  -5.180  1.00 39.61  ? 201 HEM A O2D 1 
HETATM 9156 N  NA  . HEM I  5  .   ? 15.356 5.009   -7.127  1.00 37.17  ? 201 HEM A NA  1 
HETATM 9157 N  NB  . HEM I  5  .   ? 14.245 7.537   -6.553  1.00 35.56  ? 201 HEM A NB  1 
HETATM 9158 N  NC  . HEM I  5  .   ? 13.068 6.435   -4.175  1.00 36.49  ? 201 HEM A NC  1 
HETATM 9159 N  ND  . HEM I  5  .   ? 14.200 3.910   -4.769  1.00 38.54  ? 201 HEM A ND  1 
HETATM 9160 FE FE  . HEM I  5  .   ? 14.204 5.721   -5.669  1.00 31.89  ? 201 HEM A FE  1 
HETATM 9161 O  O1  . OXY J  6  .   ? 15.674 6.049   -4.554  1.00 41.34  ? 202 OXY A O1  1 
HETATM 9162 O  O2  . OXY J  6  .   ? 15.730 5.868   -3.290  1.00 40.84  ? 202 OXY A O2  1 
HETATM 9163 CA CA  . CA  K  7  .   ? 0.000  0.000   -5.688  0.33 56.03  ? 203 CA  A CA  1 
HETATM 9164 C  CHA . HEM L  5  .   ? 29.690 39.682  -45.229 1.00 64.07  ? 201 HEM B CHA 1 
HETATM 9165 C  CHB . HEM L  5  .   ? 29.529 35.475  -43.087 1.00 59.84  ? 201 HEM B CHB 1 
HETATM 9166 C  CHC . HEM L  5  .   ? 32.653 33.658  -46.286 1.00 61.95  ? 201 HEM B CHC 1 
HETATM 9167 C  CHD . HEM L  5  .   ? 32.800 37.964  -48.440 1.00 63.07  ? 201 HEM B CHD 1 
HETATM 9168 C  C1A . HEM L  5  .   ? 29.367 38.698  -44.346 1.00 63.80  ? 201 HEM B C1A 1 
HETATM 9169 C  C2A . HEM L  5  .   ? 28.485 38.880  -43.271 1.00 64.72  ? 201 HEM B C2A 1 
HETATM 9170 C  C3A . HEM L  5  .   ? 28.430 37.694  -42.653 1.00 63.45  ? 201 HEM B C3A 1 
HETATM 9171 C  C4A . HEM L  5  .   ? 29.294 36.754  -43.365 1.00 62.83  ? 201 HEM B C4A 1 
HETATM 9172 C  CMA . HEM L  5  .   ? 27.604 37.343  -41.407 1.00 62.32  ? 201 HEM B CMA 1 
HETATM 9173 C  CAA . HEM L  5  .   ? 27.750 40.140  -42.874 1.00 66.98  ? 201 HEM B CAA 1 
HETATM 9174 C  CBA . HEM L  5  .   ? 26.441 40.319  -43.590 1.00 69.31  ? 201 HEM B CBA 1 
HETATM 9175 C  CGA . HEM L  5  .   ? 25.694 41.590  -43.190 1.00 71.99  ? 201 HEM B CGA 1 
HETATM 9176 O  O1A . HEM L  5  .   ? 25.427 41.813  -41.977 1.00 73.90  ? 201 HEM B O1A 1 
HETATM 9177 O  O2A . HEM L  5  .   ? 25.386 42.351  -44.056 1.00 72.57  ? 201 HEM B O2A 1 
HETATM 9178 C  C1B . HEM L  5  .   ? 30.360 34.570  -43.765 1.00 60.34  ? 201 HEM B C1B 1 
HETATM 9179 C  C2B . HEM L  5  .   ? 30.535 33.182  -43.373 1.00 60.60  ? 201 HEM B C2B 1 
HETATM 9180 C  C3B . HEM L  5  .   ? 31.464 32.647  -44.329 1.00 60.31  ? 201 HEM B C3B 1 
HETATM 9181 C  C4B . HEM L  5  .   ? 31.774 33.735  -45.204 1.00 61.66  ? 201 HEM B C4B 1 
HETATM 9182 C  CMB . HEM L  5  .   ? 29.885 32.484  -42.241 1.00 59.45  ? 201 HEM B CMB 1 
HETATM 9183 C  CAB . HEM L  5  .   ? 31.905 31.271  -44.300 1.00 59.20  ? 201 HEM B CAB 1 
HETATM 9184 C  CBB . HEM L  5  .   ? 33.117 30.886  -43.992 1.00 61.22  ? 201 HEM B CBB 1 
HETATM 9185 C  C1C . HEM L  5  .   ? 32.963 34.699  -47.149 1.00 62.16  ? 201 HEM B C1C 1 
HETATM 9186 C  C2C . HEM L  5  .   ? 33.898 34.540  -48.264 1.00 62.43  ? 201 HEM B C2C 1 
HETATM 9187 C  C3C . HEM L  5  .   ? 33.977 35.784  -48.919 1.00 63.06  ? 201 HEM B C3C 1 
HETATM 9188 C  C4C . HEM L  5  .   ? 33.033 36.665  -48.132 1.00 63.88  ? 201 HEM B C4C 1 
HETATM 9189 C  CMC . HEM L  5  .   ? 34.645 33.257  -48.630 1.00 63.38  ? 201 HEM B CMC 1 
HETATM 9190 C  CAC . HEM L  5  .   ? 34.726 36.109  -49.991 1.00 63.64  ? 201 HEM B CAC 1 
HETATM 9191 C  CBC . HEM L  5  .   ? 35.966 36.325  -50.262 1.00 63.41  ? 201 HEM B CBC 1 
HETATM 9192 C  C1D . HEM L  5  .   ? 31.954 38.821  -47.753 1.00 63.68  ? 201 HEM B C1D 1 
HETATM 9193 C  C2D . HEM L  5  .   ? 31.717 40.262  -48.128 1.00 63.00  ? 201 HEM B C2D 1 
HETATM 9194 C  C3D . HEM L  5  .   ? 30.830 40.724  -47.201 1.00 62.64  ? 201 HEM B C3D 1 
HETATM 9195 C  C4D . HEM L  5  .   ? 30.538 39.605  -46.294 1.00 64.19  ? 201 HEM B C4D 1 
HETATM 9196 C  CMD . HEM L  5  .   ? 32.368 40.960  -49.303 1.00 65.26  ? 201 HEM B CMD 1 
HETATM 9197 C  CAD . HEM L  5  .   ? 30.242 42.108  -47.107 1.00 61.18  ? 201 HEM B CAD 1 
HETATM 9198 C  CBD . HEM L  5  .   ? 31.004 43.045  -46.240 1.00 61.63  ? 201 HEM B CBD 1 
HETATM 9199 C  CGD . HEM L  5  .   ? 30.345 44.346  -46.190 1.00 62.69  ? 201 HEM B CGD 1 
HETATM 9200 O  O1D . HEM L  5  .   ? 29.323 44.496  -45.471 1.00 63.59  ? 201 HEM B O1D 1 
HETATM 9201 O  O2D . HEM L  5  .   ? 30.791 45.279  -46.865 1.00 64.03  ? 201 HEM B O2D 1 
HETATM 9202 N  NA  . HEM L  5  .   ? 29.880 37.404  -44.419 1.00 63.04  ? 201 HEM B NA  1 
HETATM 9203 N  NB  . HEM L  5  .   ? 31.078 34.928  -44.844 1.00 61.96  ? 201 HEM B NB  1 
HETATM 9204 N  NC  . HEM L  5  .   ? 32.467 35.993  -47.109 1.00 63.53  ? 201 HEM B NC  1 
HETATM 9205 N  ND  . HEM L  5  .   ? 31.224 38.490  -46.670 1.00 64.02  ? 201 HEM B ND  1 
HETATM 9206 FE FE  . HEM L  5  .   ? 31.169 36.706  -45.773 1.00 65.15  ? 201 HEM B FE  1 
HETATM 9207 O  O1  . OXY M  6  .   ? 32.660 37.240  -44.916 1.00 70.90  ? 202 OXY B O1  1 
HETATM 9208 O  O2  . OXY M  6  .   ? 33.700 37.890  -45.118 1.00 70.43  ? 202 OXY B O2  1 
HETATM 9209 CA CA  . CA  N  7  .   ? 35.413 23.267  -49.506 1.00 77.67  ? 203 CA  B CA  1 
HETATM 9210 CA CA  . CA  O  7  .   ? 42.323 30.826  -26.590 1.00 91.21  ? 204 CA  B CA  1 
HETATM 9211 C  CHA . HEM P  5  .   ? 16.565 41.967  -37.532 1.00 71.39  ? 200 HEM C CHA 1 
HETATM 9212 C  CHB . HEM P  5  .   ? 19.247 42.060  -33.643 1.00 68.50  ? 200 HEM C CHB 1 
HETATM 9213 C  CHC . HEM P  5  .   ? 15.841 44.554  -31.275 1.00 68.73  ? 200 HEM C CHC 1 
HETATM 9214 C  CHD . HEM P  5  .   ? 13.171 44.488  -35.282 1.00 71.01  ? 200 HEM C CHD 1 
HETATM 9215 C  C1A . HEM P  5  .   ? 17.610 41.771  -36.691 1.00 70.34  ? 200 HEM C C1A 1 
HETATM 9216 C  C2A . HEM P  5  .   ? 18.767 41.065  -37.055 1.00 70.78  ? 200 HEM C C2A 1 
HETATM 9217 C  C3A . HEM P  5  .   ? 19.545 41.090  -35.951 1.00 70.04  ? 200 HEM C C3A 1 
HETATM 9218 C  C4A . HEM P  5  .   ? 18.847 41.821  -34.889 1.00 69.08  ? 200 HEM C C4A 1 
HETATM 9219 C  CMA . HEM P  5  .   ? 20.942 40.461  -35.781 1.00 69.37  ? 200 HEM C CMA 1 
HETATM 9220 C  CAA . HEM P  5  .   ? 19.085 40.397  -38.407 1.00 70.95  ? 200 HEM C CAA 1 
HETATM 9221 C  CBA . HEM P  5  .   ? 19.885 41.263  -39.352 1.00 72.77  ? 200 HEM C CBA 1 
HETATM 9222 C  CGA . HEM P  5  .   ? 20.222 40.620  -40.715 1.00 74.68  ? 200 HEM C CGA 1 
HETATM 9223 O  O1A . HEM P  5  .   ? 20.897 39.549  -40.769 1.00 74.11  ? 200 HEM C O1A 1 
HETATM 9224 O  O2A . HEM P  5  .   ? 19.819 41.165  -41.711 1.00 75.40  ? 200 HEM C O2A 1 
HETATM 9225 C  C1B . HEM P  5  .   ? 18.570 42.754  -32.606 1.00 69.21  ? 200 HEM C C1B 1 
HETATM 9226 C  C2B . HEM P  5  .   ? 19.099 42.944  -31.259 1.00 68.47  ? 200 HEM C C2B 1 
HETATM 9227 C  C3B . HEM P  5  .   ? 18.070 43.684  -30.565 1.00 68.44  ? 200 HEM C C3B 1 
HETATM 9228 C  C4B . HEM P  5  .   ? 17.034 43.876  -31.528 1.00 69.15  ? 200 HEM C C4B 1 
HETATM 9229 C  CMB . HEM P  5  .   ? 20.404 42.465  -30.739 1.00 66.74  ? 200 HEM C CMB 1 
HETATM 9230 C  CAB . HEM P  5  .   ? 18.168 44.086  -29.167 1.00 67.72  ? 200 HEM C CAB 1 
HETATM 9231 C  CBB . HEM P  5  .   ? 18.802 45.155  -28.727 1.00 67.16  ? 200 HEM C CBB 1 
HETATM 9232 C  C1C . HEM P  5  .   ? 14.816 44.751  -32.187 1.00 68.56  ? 200 HEM C C1C 1 
HETATM 9233 C  C2C . HEM P  5  .   ? 13.582 45.494  -31.843 1.00 69.25  ? 200 HEM C C2C 1 
HETATM 9234 C  C3C . HEM P  5  .   ? 12.771 45.500  -32.996 1.00 70.23  ? 200 HEM C C3C 1 
HETATM 9235 C  C4C . HEM P  5  .   ? 13.601 44.728  -34.013 1.00 70.13  ? 200 HEM C C4C 1 
HETATM 9236 C  CMC . HEM P  5  .   ? 13.264 46.130  -30.481 1.00 67.25  ? 200 HEM C CMC 1 
HETATM 9237 C  CAC . HEM P  5  .   ? 11.541 46.067  -33.157 1.00 70.81  ? 200 HEM C CAC 1 
HETATM 9238 C  CBC . HEM P  5  .   ? 10.382 46.114  -32.592 1.00 71.87  ? 200 HEM C CBC 1 
HETATM 9239 C  C1D . HEM P  5  .   ? 13.867 43.782  -36.260 1.00 71.21  ? 200 HEM C C1D 1 
HETATM 9240 C  C2D . HEM P  5  .   ? 13.334 43.518  -37.657 1.00 71.38  ? 200 HEM C C2D 1 
HETATM 9241 C  C3D . HEM P  5  .   ? 14.322 42.790  -38.264 1.00 72.63  ? 200 HEM C C3D 1 
HETATM 9242 C  C4D . HEM P  5  .   ? 15.411 42.636  -37.279 1.00 72.28  ? 200 HEM C C4D 1 
HETATM 9243 C  CMD . HEM P  5  .   ? 11.992 43.984  -38.179 1.00 70.84  ? 200 HEM C CMD 1 
HETATM 9244 C  CAD . HEM P  5  .   ? 14.337 42.226  -39.666 1.00 72.90  ? 200 HEM C CAD 1 
HETATM 9245 C  CBD . HEM P  5  .   ? 13.931 40.766  -39.603 1.00 74.43  ? 200 HEM C CBD 1 
HETATM 9246 C  CGD . HEM P  5  .   ? 13.923 40.059  -40.884 1.00 75.96  ? 200 HEM C CGD 1 
HETATM 9247 O  O1D . HEM P  5  .   ? 12.882 40.059  -41.589 1.00 79.00  ? 200 HEM C O1D 1 
HETATM 9248 O  O2D . HEM P  5  .   ? 14.936 39.446  -41.242 1.00 75.78  ? 200 HEM C O2D 1 
HETATM 9249 N  NA  . HEM P  5  .   ? 17.638 42.247  -35.368 1.00 69.32  ? 200 HEM C NA  1 
HETATM 9250 N  NB  . HEM P  5  .   ? 17.354 43.292  -32.790 1.00 70.32  ? 200 HEM C NB  1 
HETATM 9251 N  NC  . HEM P  5  .   ? 14.784 44.325  -33.504 1.00 68.53  ? 200 HEM C NC  1 
HETATM 9252 N  ND  . HEM P  5  .   ? 15.088 43.236  -36.100 1.00 71.32  ? 200 HEM C ND  1 
HETATM 9253 FE FE  . HEM P  5  .   ? 16.215 43.291  -34.442 1.00 69.10  ? 200 HEM C FE  1 
HETATM 9254 O  O1  . OXY Q  6  .   ? 15.262 41.848  -33.982 1.00 78.73  ? 201 OXY C O1  1 
HETATM 9255 O  O2  . OXY Q  6  .   ? 14.347 41.016  -34.099 1.00 84.68  ? 201 OXY C O2  1 
HETATM 9256 C  CHA . HEM R  5  .   ? 19.167 -2.215  -19.976 1.00 56.98  ? 201 HEM D CHA 1 
HETATM 9257 C  CHB . HEM R  5  .   ? 23.441 -0.316  -19.165 1.00 55.37  ? 201 HEM D CHB 1 
HETATM 9258 C  CHC . HEM R  5  .   ? 25.422 -3.090  -22.601 1.00 60.94  ? 201 HEM D CHC 1 
HETATM 9259 C  CHD . HEM R  5  .   ? 21.069 -5.060  -23.352 1.00 60.93  ? 201 HEM D CHD 1 
HETATM 9260 C  C1A . HEM R  5  .   ? 20.156 -1.447  -19.442 1.00 55.11  ? 201 HEM D C1A 1 
HETATM 9261 C  C2A . HEM R  5  .   ? 19.939 -0.503  -18.437 1.00 54.29  ? 201 HEM D C2A 1 
HETATM 9262 C  C3A . HEM R  5  .   ? 21.135 0.036   -18.186 1.00 55.17  ? 201 HEM D C3A 1 
HETATM 9263 C  C4A . HEM R  5  .   ? 22.129 -0.581  -19.065 1.00 55.76  ? 201 HEM D C4A 1 
HETATM 9264 C  CMA . HEM R  5  .   ? 21.454 1.132   -17.159 1.00 53.03  ? 201 HEM D CMA 1 
HETATM 9265 C  CAA . HEM R  5  .   ? 18.637 -0.145  -17.775 1.00 52.80  ? 201 HEM D CAA 1 
HETATM 9266 C  CBA . HEM R  5  .   ? 18.353 -0.940  -16.553 1.00 51.76  ? 201 HEM D CBA 1 
HETATM 9267 C  CGA . HEM R  5  .   ? 17.033 -0.580  -15.893 1.00 52.59  ? 201 HEM D CGA 1 
HETATM 9268 O  O1A . HEM R  5  .   ? 16.100 -1.423  -15.874 1.00 52.60  ? 201 HEM D O1A 1 
HETATM 9269 O  O2A . HEM R  5  .   ? 16.927 0.519   -15.418 1.00 52.34  ? 201 HEM D O2A 1 
HETATM 9270 C  C1B . HEM R  5  .   ? 24.403 -0.887  -20.029 1.00 55.88  ? 201 HEM D C1B 1 
HETATM 9271 C  C2B . HEM R  5  .   ? 25.815 -0.498  -20.074 1.00 57.15  ? 201 HEM D C2B 1 
HETATM 9272 C  C3B . HEM R  5  .   ? 26.391 -1.325  -21.111 1.00 58.68  ? 201 HEM D C3B 1 
HETATM 9273 C  C4B . HEM R  5  .   ? 25.309 -2.132  -21.583 1.00 58.99  ? 201 HEM D C4B 1 
HETATM 9274 C  CMB . HEM R  5  .   ? 26.488 0.523   -19.236 1.00 55.05  ? 201 HEM D CMB 1 
HETATM 9275 C  CAB . HEM R  5  .   ? 27.798 -1.265  -21.511 1.00 59.40  ? 201 HEM D CAB 1 
HETATM 9276 C  CBB . HEM R  5  .   ? 28.764 -1.999  -20.992 1.00 61.59  ? 201 HEM D CBB 1 
HETATM 9277 C  C1C . HEM R  5  .   ? 24.384 -3.885  -23.094 1.00 60.61  ? 201 HEM D C1C 1 
HETATM 9278 C  C2C . HEM R  5  .   ? 24.592 -4.875  -24.165 1.00 59.96  ? 201 HEM D C2C 1 
HETATM 9279 C  C3C . HEM R  5  .   ? 23.338 -5.483  -24.416 1.00 60.39  ? 201 HEM D C3C 1 
HETATM 9280 C  C4C . HEM R  5  .   ? 22.401 -4.786  -23.437 1.00 60.04  ? 201 HEM D C4C 1 
HETATM 9281 C  CMC . HEM R  5  .   ? 25.932 -5.164  -24.854 1.00 58.10  ? 201 HEM D CMC 1 
HETATM 9282 C  CAC . HEM R  5  .   ? 23.055 -6.457  -25.321 1.00 60.19  ? 201 HEM D CAC 1 
HETATM 9283 C  CBC . HEM R  5  .   ? 22.568 -6.584  -26.499 1.00 61.22  ? 201 HEM D CBC 1 
HETATM 9284 C  C1D . HEM R  5  .   ? 20.155 -4.452  -22.489 1.00 60.48  ? 201 HEM D C1D 1 
HETATM 9285 C  C2D . HEM R  5  .   ? 18.670 -4.778  -22.452 1.00 60.57  ? 201 HEM D C2D 1 
HETATM 9286 C  C3D . HEM R  5  .   ? 18.152 -3.950  -21.487 1.00 60.63  ? 201 HEM D C3D 1 
HETATM 9287 C  C4D . HEM R  5  .   ? 19.283 -3.156  -20.955 1.00 59.80  ? 201 HEM D C4D 1 
HETATM 9288 C  CMD . HEM R  5  .   ? 17.987 -5.808  -23.331 1.00 60.85  ? 201 HEM D CMD 1 
HETATM 9289 C  CAD . HEM R  5  .   ? 16.701 -3.847  -21.037 1.00 60.04  ? 201 HEM D CAD 1 
HETATM 9290 C  CBD . HEM R  5  .   ? 15.920 -2.908  -21.936 1.00 60.38  ? 201 HEM D CBD 1 
HETATM 9291 C  CGD . HEM R  5  .   ? 14.498 -2.715  -21.578 1.00 59.59  ? 201 HEM D CGD 1 
HETATM 9292 O  O1D . HEM R  5  .   ? 14.196 -2.030  -20.564 1.00 59.07  ? 201 HEM D O1D 1 
HETATM 9293 O  O2D . HEM R  5  .   ? 13.617 -3.201  -22.302 1.00 57.94  ? 201 HEM D O2D 1 
HETATM 9294 N  NA  . HEM R  5  .   ? 21.502 -1.512  -19.847 1.00 57.12  ? 201 HEM D NA  1 
HETATM 9295 N  NB  . HEM R  5  .   ? 24.077 -1.838  -20.915 1.00 58.77  ? 201 HEM D NB  1 
HETATM 9296 N  NC  . HEM R  5  .   ? 23.048 -3.867  -22.687 1.00 59.85  ? 201 HEM D NC  1 
HETATM 9297 N  ND  . HEM R  5  .   ? 20.455 -3.485  -21.590 1.00 60.40  ? 201 HEM D ND  1 
HETATM 9298 FE FE  . HEM R  5  .   ? 22.282 -2.697  -21.250 1.00 54.66  ? 201 HEM D FE  1 
HETATM 9299 O  O1  . OXY S  6  .   ? 21.966 -1.391  -22.425 1.00 58.05  ? 202 OXY D O1  1 
HETATM 9300 O  O2  . OXY S  6  .   ? 21.411 -1.514  -23.520 1.00 64.51  ? 202 OXY D O2  1 
HETATM 9301 C  C1  . NAG T  8  .   ? 9.638  7.801   -35.109 1.00 120.31 ? 203 NAG D C1  1 
HETATM 9302 C  C2  . NAG T  8  .   ? 8.576  7.757   -36.206 1.00 121.21 ? 203 NAG D C2  1 
HETATM 9303 C  C3  . NAG T  8  .   ? 8.713  8.998   -37.042 1.00 123.93 ? 203 NAG D C3  1 
HETATM 9304 C  C4  . NAG T  8  .   ? 8.627  10.219  -36.122 1.00 124.65 ? 203 NAG D C4  1 
HETATM 9305 C  C5  . NAG T  8  .   ? 9.656  10.134  -35.007 1.00 120.62 ? 203 NAG D C5  1 
HETATM 9306 C  C6  . NAG T  8  .   ? 9.599  11.297  -34.043 1.00 114.70 ? 203 NAG D C6  1 
HETATM 9307 C  C7  . NAG T  8  .   ? 7.663  6.016   -37.563 1.00 118.84 ? 203 NAG D C7  1 
HETATM 9308 C  C8  . NAG T  8  .   ? 7.651  5.700   -39.062 1.00 117.42 ? 203 NAG D C8  1 
HETATM 9309 N  N2  . NAG T  8  .   ? 8.741  6.595   -37.053 1.00 119.48 ? 203 NAG D N2  1 
HETATM 9310 O  O3  . NAG T  8  .   ? 7.678  9.031   -38.017 1.00 124.25 ? 203 NAG D O3  1 
HETATM 9311 O  O4  . NAG T  8  .   ? 8.911  11.383  -36.877 1.00 133.10 ? 203 NAG D O4  1 
HETATM 9312 O  O5  . NAG T  8  .   ? 9.426  8.936   -34.272 1.00 119.21 ? 203 NAG D O5  1 
HETATM 9313 O  O6  . NAG T  8  .   ? 8.253  11.429  -33.551 1.00 108.76 ? 203 NAG D O6  1 
HETATM 9314 O  O7  . NAG T  8  .   ? 6.682  5.727   -36.867 1.00 119.08 ? 203 NAG D O7  1 
HETATM 9315 C  C1  . NAG U  8  .   ? 8.286  12.550  -36.472 1.00 141.22 ? 204 NAG D C1  1 
HETATM 9316 C  C2  . NAG U  8  .   ? 9.002  13.723  -37.206 1.00 144.05 ? 204 NAG D C2  1 
HETATM 9317 C  C3  . NAG U  8  .   ? 8.198  15.030  -37.200 1.00 146.93 ? 204 NAG D C3  1 
HETATM 9318 C  C4  . NAG U  8  .   ? 6.793  14.702  -37.730 1.00 148.85 ? 204 NAG D C4  1 
HETATM 9319 C  C5  . NAG U  8  .   ? 6.109  13.624  -36.872 1.00 145.86 ? 204 NAG D C5  1 
HETATM 9320 C  C6  . NAG U  8  .   ? 4.763  13.238  -37.448 1.00 145.49 ? 204 NAG D C6  1 
HETATM 9321 C  C7  . NAG U  8  .   ? 11.269 14.506  -37.458 1.00 146.04 ? 204 NAG D C7  1 
HETATM 9322 C  C8  . NAG U  8  .   ? 12.473 15.202  -36.797 1.00 145.31 ? 204 NAG D C8  1 
HETATM 9323 N  N2  . NAG U  8  .   ? 10.343 13.945  -36.671 1.00 144.94 ? 204 NAG D N2  1 
HETATM 9324 O  O3  . NAG U  8  .   ? 8.842  15.980  -38.062 1.00 144.77 ? 204 NAG D O3  1 
HETATM 9325 O  O4  . NAG U  8  .   ? 5.978  15.878  -37.738 1.00 155.88 ? 204 NAG D O4  1 
HETATM 9326 O  O5  . NAG U  8  .   ? 6.884  12.402  -36.844 1.00 143.74 ? 204 NAG D O5  1 
HETATM 9327 O  O6  . NAG U  8  .   ? 3.722  13.901  -36.760 1.00 145.07 ? 204 NAG D O6  1 
HETATM 9328 O  O7  . NAG U  8  .   ? 11.170 14.492  -38.694 1.00 146.31 ? 204 NAG D O7  1 
HETATM 9329 C  C1  . MAN V  9  .   ? 5.809  16.485  -38.968 1.00 162.23 ? 205 MAN D C1  1 
HETATM 9330 C  C2  . MAN V  9  .   ? 6.809  17.653  -39.087 1.00 164.66 ? 205 MAN D C2  1 
HETATM 9331 C  C3  . MAN V  9  .   ? 6.139  19.047  -39.086 1.00 167.87 ? 205 MAN D C3  1 
HETATM 9332 C  C4  . MAN V  9  .   ? 4.911  19.189  -38.130 1.00 167.85 ? 205 MAN D C4  1 
HETATM 9333 C  C5  . MAN V  9  .   ? 4.160  17.852  -37.931 1.00 167.53 ? 205 MAN D C5  1 
HETATM 9334 C  C6  . MAN V  9  .   ? 2.638  17.957  -37.809 1.00 168.60 ? 205 MAN D C6  1 
HETATM 9335 O  O2  . MAN V  9  .   ? 7.582  17.497  -40.272 1.00 161.69 ? 205 MAN D O2  1 
HETATM 9336 O  O3  . MAN V  9  .   ? 5.768  19.414  -40.432 1.00 172.03 ? 205 MAN D O3  1 
HETATM 9337 O  O4  . MAN V  9  .   ? 5.341  19.690  -36.864 1.00 166.67 ? 205 MAN D O4  1 
HETATM 9338 O  O5  . MAN V  9  .   ? 4.457  16.948  -39.021 1.00 164.56 ? 205 MAN D O5  1 
HETATM 9339 O  O6  . MAN V  9  .   ? 2.008  17.658  -39.075 1.00 168.27 ? 205 MAN D O6  1 
HETATM 9340 C  C1  . MAN W  9  .   ? 6.004  20.761  -40.765 1.00 175.52 ? 206 MAN D C1  1 
HETATM 9341 C  C2  . MAN W  9  .   ? 5.300  21.118  -42.106 1.00 176.24 ? 206 MAN D C2  1 
HETATM 9342 C  C3  . MAN W  9  .   ? 6.038  20.501  -43.311 1.00 176.74 ? 206 MAN D C3  1 
HETATM 9343 C  C4  . MAN W  9  .   ? 7.535  20.868  -43.265 1.00 177.76 ? 206 MAN D C4  1 
HETATM 9344 C  C5  . MAN W  9  .   ? 8.147  20.470  -41.895 1.00 177.59 ? 206 MAN D C5  1 
HETATM 9345 C  C6  . MAN W  9  .   ? 9.612  20.876  -41.729 1.00 178.17 ? 206 MAN D C6  1 
HETATM 9346 O  O2  . MAN W  9  .   ? 5.204  22.534  -42.270 1.00 176.90 ? 206 MAN D O2  1 
HETATM 9347 O  O3  . MAN W  9  .   ? 5.458  20.971  -44.526 1.00 175.56 ? 206 MAN D O3  1 
HETATM 9348 O  O4  . MAN W  9  .   ? 8.228  20.205  -44.320 1.00 178.17 ? 206 MAN D O4  1 
HETATM 9349 O  O5  . MAN W  9  .   ? 7.402  21.086  -40.806 1.00 176.45 ? 206 MAN D O5  1 
HETATM 9350 O  O6  . MAN W  9  .   ? 10.258 20.107  -40.718 1.00 178.04 ? 206 MAN D O6  1 
HETATM 9351 C  C1  . MAN X  9  .   ? 0.628  17.921  -39.091 1.00 168.84 ? 207 MAN D C1  1 
HETATM 9352 C  C2  . MAN X  9  .   ? 0.076  17.661  -40.507 1.00 168.23 ? 207 MAN D C2  1 
HETATM 9353 C  C3  . MAN X  9  .   ? 0.403  18.802  -41.488 1.00 169.01 ? 207 MAN D C3  1 
HETATM 9354 C  C4  . MAN X  9  .   ? 0.124  20.196  -40.895 1.00 169.18 ? 207 MAN D C4  1 
HETATM 9355 C  C5  . MAN X  9  .   ? 0.717  20.346  -39.481 1.00 169.64 ? 207 MAN D C5  1 
HETATM 9356 C  C6  . MAN X  9  .   ? 0.228  21.644  -38.833 1.00 170.17 ? 207 MAN D C6  1 
HETATM 9357 O  O2  . MAN X  9  .   ? -1.324 17.416  -40.487 1.00 167.99 ? 207 MAN D O2  1 
HETATM 9358 O  O3  . MAN X  9  .   ? -0.381 18.629  -42.660 1.00 169.06 ? 207 MAN D O3  1 
HETATM 9359 O  O4  . MAN X  9  .   ? 0.669  21.201  -41.749 1.00 168.61 ? 207 MAN D O4  1 
HETATM 9360 O  O5  . MAN X  9  .   ? 0.288  19.244  -38.628 1.00 169.02 ? 207 MAN D O5  1 
HETATM 9361 O  O6  . MAN X  9  .   ? 1.062  22.058  -37.758 1.00 169.60 ? 207 MAN D O6  1 
HETATM 9362 C  C1  . FUC Y  10 .   ? 8.211  11.244  -32.161 1.00 105.24 ? 208 FUC D C1  1 
HETATM 9363 C  C2  . FUC Y  10 .   ? 6.901  11.796  -31.572 1.00 103.51 ? 208 FUC D C2  1 
HETATM 9364 C  C3  . FUC Y  10 .   ? 5.708  10.895  -31.910 1.00 102.30 ? 208 FUC D C3  1 
HETATM 9365 C  C4  . FUC Y  10 .   ? 6.016  9.391   -31.682 1.00 101.82 ? 208 FUC D C4  1 
HETATM 9366 C  C5  . FUC Y  10 .   ? 7.390  8.990   -32.250 1.00 102.31 ? 208 FUC D C5  1 
HETATM 9367 C  C6  . FUC Y  10 .   ? 7.791  7.601   -31.826 1.00 100.85 ? 208 FUC D C6  1 
HETATM 9368 O  O2  . FUC Y  10 .   ? 6.658  13.120  -32.049 1.00 100.61 ? 208 FUC D O2  1 
HETATM 9369 O  O3  . FUC Y  10 .   ? 4.609  11.285  -31.097 1.00 101.50 ? 208 FUC D O3  1 
HETATM 9370 O  O4  . FUC Y  10 .   ? 5.943  9.053   -30.301 1.00 100.60 ? 208 FUC D O4  1 
HETATM 9371 O  O5  . FUC Y  10 .   ? 8.408  9.883   -31.772 1.00 103.26 ? 208 FUC D O5  1 
HETATM 9372 C  CHA . HEM Z  5  .   ? 9.113  48.010  5.998   1.00 48.79  ? 200 HEM E CHA 1 
HETATM 9373 C  CHB . HEM Z  5  .   ? 10.317 43.986  8.168   1.00 48.10  ? 200 HEM E CHB 1 
HETATM 9374 C  CHC . HEM Z  5  .   ? 8.335  41.412  4.609   1.00 46.94  ? 200 HEM E CHC 1 
HETATM 9375 C  CHD . HEM Z  5  .   ? 7.088  45.520  2.463   1.00 48.14  ? 200 HEM E CHD 1 
HETATM 9376 C  C1A . HEM Z  5  .   ? 9.631  47.145  6.906   1.00 47.74  ? 200 HEM E C1A 1 
HETATM 9377 C  C2A . HEM Z  5  .   ? 10.311 47.555  8.048   1.00 49.49  ? 200 HEM E C2A 1 
HETATM 9378 C  C3A . HEM Z  5  .   ? 10.660 46.423  8.683   1.00 49.26  ? 200 HEM E C3A 1 
HETATM 9379 C  C4A . HEM Z  5  .   ? 10.180 45.287  7.908   1.00 47.81  ? 200 HEM E C4A 1 
HETATM 9380 C  CMA . HEM Z  5  .   ? 11.434 46.291  10.006  1.00 46.64  ? 200 HEM E CMA 1 
HETATM 9381 C  CAA . HEM Z  5  .   ? 10.604 48.974  8.478   1.00 50.92  ? 200 HEM E CAA 1 
HETATM 9382 C  CBA . HEM Z  5  .   ? 9.591  49.517  9.441   1.00 51.38  ? 200 HEM E CBA 1 
HETATM 9383 C  CGA . HEM Z  5  .   ? 9.878  50.953  9.867   1.00 52.79  ? 200 HEM E CGA 1 
HETATM 9384 O  O1A . HEM Z  5  .   ? 9.295  51.910  9.285   1.00 53.58  ? 200 HEM E O1A 1 
HETATM 9385 O  O2A . HEM Z  5  .   ? 10.679 51.125  10.731  1.00 50.79  ? 200 HEM E O2A 1 
HETATM 9386 C  C1B . HEM Z  5  .   ? 9.870  42.881  7.402   1.00 48.48  ? 200 HEM E C1B 1 
HETATM 9387 C  C2B . HEM Z  5  .   ? 10.084 41.492  7.775   1.00 49.80  ? 200 HEM E C2B 1 
HETATM 9388 C  C3B . HEM Z  5  .   ? 9.493  40.738  6.694   1.00 48.83  ? 200 HEM E C3B 1 
HETATM 9389 C  C4B . HEM Z  5  .   ? 8.977  41.712  5.792   1.00 46.83  ? 200 HEM E C4B 1 
HETATM 9390 C  CMB . HEM Z  5  .   ? 10.771 40.976  9.000   1.00 49.61  ? 200 HEM E CMB 1 
HETATM 9391 C  CAB . HEM Z  5  .   ? 9.492  39.276  6.649   1.00 48.60  ? 200 HEM E CAB 1 
HETATM 9392 C  CBB . HEM Z  5  .   ? 8.497  38.494  6.986   1.00 50.62  ? 200 HEM E CBB 1 
HETATM 9393 C  C1C . HEM Z  5  .   ? 7.821  42.333  3.714   1.00 46.76  ? 200 HEM E C1C 1 
HETATM 9394 C  C2C . HEM Z  5  .   ? 7.149  41.928  2.478   1.00 48.11  ? 200 HEM E C2C 1 
HETATM 9395 C  C3C . HEM Z  5  .   ? 6.764  43.103  1.817   1.00 49.41  ? 200 HEM E C3C 1 
HETATM 9396 C  C4C . HEM Z  5  .   ? 7.251  44.204  2.735   1.00 47.90  ? 200 HEM E C4C 1 
HETATM 9397 C  CMC . HEM Z  5  .   ? 6.921  40.489  2.013   1.00 46.99  ? 200 HEM E CMC 1 
HETATM 9398 C  CAC . HEM Z  5  .   ? 6.115  43.213  0.632   1.00 50.97  ? 200 HEM E CAC 1 
HETATM 9399 C  CBC . HEM Z  5  .   ? 6.375  43.155  -0.628  1.00 51.95  ? 200 HEM E CBC 1 
HETATM 9400 C  C1D . HEM Z  5  .   ? 7.524  46.573  3.249   1.00 48.31  ? 200 HEM E C1D 1 
HETATM 9401 C  C2D . HEM Z  5  .   ? 7.335  48.036  2.896   1.00 48.98  ? 200 HEM E C2D 1 
HETATM 9402 C  C3D . HEM Z  5  .   ? 7.925  48.710  3.931   1.00 49.61  ? 200 HEM E C3D 1 
HETATM 9403 C  C4D . HEM Z  5  .   ? 8.447  47.706  4.857   1.00 48.33  ? 200 HEM E C4D 1 
HETATM 9404 C  CMD . HEM Z  5  .   ? 6.631  48.551  1.646   1.00 48.84  ? 200 HEM E CMD 1 
HETATM 9405 C  CAD . HEM Z  5  .   ? 8.034  50.195  4.123   1.00 51.58  ? 200 HEM E CAD 1 
HETATM 9406 C  CBD . HEM Z  5  .   ? 9.281  50.784  3.559   1.00 53.54  ? 200 HEM E CBD 1 
HETATM 9407 C  CGD . HEM Z  5  .   ? 9.340  52.228  3.813   1.00 54.28  ? 200 HEM E CGD 1 
HETATM 9408 O  O1D . HEM Z  5  .   ? 8.780  53.049  3.023   1.00 54.69  ? 200 HEM E O1D 1 
HETATM 9409 O  O2D . HEM Z  5  .   ? 9.942  52.619  4.812   1.00 56.68  ? 200 HEM E O2D 1 
HETATM 9410 N  NA  . HEM Z  5  .   ? 9.542  45.754  6.792   1.00 46.74  ? 200 HEM E NA  1 
HETATM 9411 N  NB  . HEM Z  5  .   ? 9.218  43.038  6.239   1.00 47.38  ? 200 HEM E NB  1 
HETATM 9412 N  NC  . HEM Z  5  .   ? 7.863  43.711  3.820   1.00 46.79  ? 200 HEM E NC  1 
HETATM 9413 N  ND  . HEM Z  5  .   ? 8.185  46.452  4.414   1.00 47.98  ? 200 HEM E ND  1 
HETATM 9414 FE FE  . HEM Z  5  .   ? 8.678  44.741  5.320   1.00 53.39  ? 200 HEM E FE  1 
HETATM 9415 O  O1  . OXY AA 6  .   ? 10.110 44.626  4.268   1.00 54.32  ? 201 OXY E O1  1 
HETATM 9416 O  O2  . OXY AA 6  .   ? 10.310 45.100  3.134   1.00 61.03  ? 201 OXY E O2  1 
HETATM 9417 C  CHA . HEM BA 5  .   ? 33.211 17.346  45.057  1.00 56.96  ? 201 HEM F CHA 1 
HETATM 9418 C  CHB . HEM BA 5  .   ? 31.806 21.307  42.876  1.00 55.33  ? 201 HEM F CHB 1 
HETATM 9419 C  CHC . HEM BA 5  .   ? 34.440 23.989  45.913  1.00 58.45  ? 201 HEM F CHC 1 
HETATM 9420 C  CHD . HEM BA 5  .   ? 35.858 19.952  48.079  1.00 58.13  ? 201 HEM F CHD 1 
HETATM 9421 C  C1A . HEM BA 5  .   ? 32.597 18.183  44.177  1.00 56.11  ? 201 HEM F C1A 1 
HETATM 9422 C  C2A . HEM BA 5  .   ? 31.758 17.733  43.148  1.00 55.97  ? 201 HEM F C2A 1 
HETATM 9423 C  C3A . HEM BA 5  .   ? 31.350 18.850  42.524  1.00 53.66  ? 201 HEM F C3A 1 
HETATM 9424 C  C4A . HEM BA 5  .   ? 31.948 20.012  43.171  1.00 55.55  ? 201 HEM F C4A 1 
HETATM 9425 C  CMA . HEM BA 5  .   ? 30.409 18.938  41.331  1.00 51.44  ? 201 HEM F CMA 1 
HETATM 9426 C  CAA . HEM BA 5  .   ? 31.384 16.280  42.808  1.00 56.21  ? 201 HEM F CAA 1 
HETATM 9427 C  CBA . HEM BA 5  .   ? 30.226 15.755  43.636  1.00 57.04  ? 201 HEM F CBA 1 
HETATM 9428 C  CGA . HEM BA 5  .   ? 29.813 14.292  43.389  1.00 58.46  ? 201 HEM F CGA 1 
HETATM 9429 O  O1A . HEM BA 5  .   ? 29.627 13.873  42.205  1.00 59.52  ? 201 HEM F O1A 1 
HETATM 9430 O  O2A . HEM BA 5  .   ? 29.685 13.568  44.357  1.00 55.87  ? 201 HEM F O2A 1 
HETATM 9431 C  C1B . HEM BA 5  .   ? 32.386 22.425  43.514  1.00 56.33  ? 201 HEM F C1B 1 
HETATM 9432 C  C2B . HEM BA 5  .   ? 32.153 23.803  43.111  1.00 59.17  ? 201 HEM F C2B 1 
HETATM 9433 C  C3B . HEM BA 5  .   ? 32.939 24.580  44.025  1.00 58.88  ? 201 HEM F C3B 1 
HETATM 9434 C  C4B . HEM BA 5  .   ? 33.568 23.640  44.880  1.00 58.24  ? 201 HEM F C4B 1 
HETATM 9435 C  CMB . HEM BA 5  .   ? 31.289 24.288  42.000  1.00 60.30  ? 201 HEM F CMB 1 
HETATM 9436 C  CAB . HEM BA 5  .   ? 32.996 26.014  43.986  1.00 57.94  ? 201 HEM F CAB 1 
HETATM 9437 C  CBB . HEM BA 5  .   ? 33.924 26.678  43.339  1.00 60.46  ? 201 HEM F CBB 1 
HETATM 9438 C  C1C . HEM BA 5  .   ? 35.063 23.100  46.760  1.00 56.74  ? 201 HEM F C1C 1 
HETATM 9439 C  C2C . HEM BA 5  .   ? 35.974 23.537  47.815  1.00 56.39  ? 201 HEM F C2C 1 
HETATM 9440 C  C3C . HEM BA 5  .   ? 36.429 22.383  48.475  1.00 58.02  ? 201 HEM F C3C 1 
HETATM 9441 C  C4C . HEM BA 5  .   ? 35.717 21.255  47.745  1.00 57.82  ? 201 HEM F C4C 1 
HETATM 9442 C  CMC . HEM BA 5  .   ? 36.349 24.979  48.130  1.00 54.87  ? 201 HEM F CMC 1 
HETATM 9443 C  CAC . HEM BA 5  .   ? 37.302 22.309  49.523  1.00 58.31  ? 201 HEM F CAC 1 
HETATM 9444 C  CBC . HEM BA 5  .   ? 38.573 22.417  49.747  1.00 56.44  ? 201 HEM F CBC 1 
HETATM 9445 C  C1D . HEM BA 5  .   ? 35.246 18.876  47.454  1.00 58.38  ? 201 HEM F C1D 1 
HETATM 9446 C  C2D . HEM BA 5  .   ? 35.429 17.437  47.873  1.00 57.84  ? 201 HEM F C2D 1 
HETATM 9447 C  C3D . HEM BA 5  .   ? 34.667 16.720  46.997  1.00 58.01  ? 201 HEM F C3D 1 
HETATM 9448 C  C4D . HEM BA 5  .   ? 34.044 17.687  46.076  1.00 57.98  ? 201 HEM F C4D 1 
HETATM 9449 C  CMD . HEM BA 5  .   ? 36.291 16.982  49.034  1.00 56.76  ? 201 HEM F CMD 1 
HETATM 9450 C  CAD . HEM BA 5  .   ? 34.481 15.225  46.970  1.00 58.78  ? 201 HEM F CAD 1 
HETATM 9451 C  CBD . HEM BA 5  .   ? 35.496 14.510  46.152  1.00 62.09  ? 201 HEM F CBD 1 
HETATM 9452 C  CGD . HEM BA 5  .   ? 35.248 13.065  46.148  1.00 64.87  ? 201 HEM F CGD 1 
HETATM 9453 O  O1D . HEM BA 5  .   ? 34.332 12.583  45.407  1.00 67.06  ? 201 HEM F O1D 1 
HETATM 9454 O  O2D . HEM BA 5  .   ? 35.936 12.333  46.877  1.00 66.55  ? 201 HEM F O2D 1 
HETATM 9455 N  NA  . HEM BA 5  .   ? 32.731 19.576  44.211  1.00 56.68  ? 201 HEM F NA  1 
HETATM 9456 N  NB  . HEM BA 5  .   ? 33.210 22.301  44.560  1.00 55.79  ? 201 HEM F NB  1 
HETATM 9457 N  NC  . HEM BA 5  .   ? 34.944 21.719  46.750  1.00 56.33  ? 201 HEM F NC  1 
HETATM 9458 N  ND  . HEM BA 5  .   ? 34.408 18.961  46.400  1.00 58.39  ? 201 HEM F ND  1 
HETATM 9459 FE FE  . HEM BA 5  .   ? 33.827 20.647  45.491  1.00 60.44  ? 201 HEM F FE  1 
HETATM 9460 O  O1  . OXY CA 6  .   ? 35.299 20.354  44.518  1.00 66.84  ? 202 OXY F O1  1 
HETATM 9461 O  O2  . OXY CA 6  .   ? 36.524 20.309  44.733  1.00 67.50  ? 202 OXY F O2  1 
HETATM 9462 CA CA  . CA  DA 7  .   ? 34.510 34.687  48.867  1.00 60.58  ? 203 CA  F CA  1 
HETATM 9463 CA CA  . CA  EA 7  .   ? 42.246 29.182  26.293  1.00 83.03  ? 204 CA  F CA  1 
HETATM 9464 CA CA  . CA  FA 7  .   ? 36.776 22.239  57.765  1.00 81.88  ? 205 CA  F CA  1 
HETATM 9465 C  CHA . HEM GA 5  .   ? 20.799 11.425  38.082  1.00 69.85  ? 200 HEM G CHA 1 
HETATM 9466 C  CHB . HEM GA 5  .   ? 23.285 11.854  34.071  1.00 66.29  ? 200 HEM G CHB 1 
HETATM 9467 C  CHC . HEM GA 5  .   ? 20.537 8.519   31.950  1.00 68.85  ? 200 HEM G CHC 1 
HETATM 9468 C  CHD . HEM GA 5  .   ? 18.080 8.060   36.032  1.00 68.30  ? 200 HEM G CHD 1 
HETATM 9469 C  C1A . HEM GA 5  .   ? 21.740 11.847  37.185  1.00 69.86  ? 200 HEM G C1A 1 
HETATM 9470 C  C2A . HEM GA 5  .   ? 22.699 12.824  37.473  1.00 70.63  ? 200 HEM G C2A 1 
HETATM 9471 C  C3A . HEM GA 5  .   ? 23.420 12.954  36.342  1.00 70.89  ? 200 HEM G C3A 1 
HETATM 9472 C  C4A . HEM GA 5  .   ? 22.884 12.037  35.328  1.00 68.88  ? 200 HEM G C4A 1 
HETATM 9473 C  CMA . HEM GA 5  .   ? 24.611 13.908  36.110  1.00 69.65  ? 200 HEM G CMA 1 
HETATM 9474 C  CAA . HEM GA 5  .   ? 22.896 13.588  38.763  1.00 71.46  ? 200 HEM G CAA 1 
HETATM 9475 C  CBA . HEM GA 5  .   ? 23.857 12.917  39.713  1.00 73.06  ? 200 HEM G CBA 1 
HETATM 9476 C  CGA . HEM GA 5  .   ? 24.059 13.673  41.035  1.00 75.54  ? 200 HEM G CGA 1 
HETATM 9477 O  O1A . HEM GA 5  .   ? 24.219 14.921  41.019  1.00 76.64  ? 200 HEM G O1A 1 
HETATM 9478 O  O2A . HEM GA 5  .   ? 24.041 13.044  42.060  1.00 76.40  ? 200 HEM G O2A 1 
HETATM 9479 C  C1B . HEM GA 5  .   ? 22.762 10.987  33.096  1.00 66.82  ? 200 HEM G C1B 1 
HETATM 9480 C  C2B . HEM GA 5  .   ? 23.265 10.881  31.730  1.00 67.99  ? 200 HEM G C2B 1 
HETATM 9481 C  C3B . HEM GA 5  .   ? 22.428 9.886   31.112  1.00 68.41  ? 200 HEM G C3B 1 
HETATM 9482 C  C4B . HEM GA 5  .   ? 21.523 9.480   32.129  1.00 69.05  ? 200 HEM G C4B 1 
HETATM 9483 C  CMB . HEM GA 5  .   ? 24.382 11.645  31.127  1.00 66.95  ? 200 HEM G CMB 1 
HETATM 9484 C  CAB . HEM GA 5  .   ? 22.558 9.465   29.728  1.00 67.99  ? 200 HEM G CAB 1 
HETATM 9485 C  CBB . HEM GA 5  .   ? 23.348 8.514   29.301  1.00 70.93  ? 200 HEM G CBB 1 
HETATM 9486 C  C1C . HEM GA 5  .   ? 19.640 8.100   32.904  1.00 67.87  ? 200 HEM G C1C 1 
HETATM 9487 C  C2C . HEM GA 5  .   ? 18.638 7.069   32.616  1.00 67.92  ? 200 HEM G C2C 1 
HETATM 9488 C  C3C . HEM GA 5  .   ? 17.884 6.891   33.799  1.00 67.89  ? 200 HEM G C3C 1 
HETATM 9489 C  C4C . HEM GA 5  .   ? 18.518 7.884   34.764  1.00 68.25  ? 200 HEM G C4C 1 
HETATM 9490 C  CMC . HEM GA 5  .   ? 18.479 6.350   31.266  1.00 65.53  ? 200 HEM G CMC 1 
HETATM 9491 C  CAC . HEM GA 5  .   ? 16.851 6.043   34.017  1.00 67.68  ? 200 HEM G CAC 1 
HETATM 9492 C  CBC . HEM GA 5  .   ? 15.729 5.705   33.487  1.00 69.73  ? 200 HEM G CBC 1 
HETATM 9493 C  C1D . HEM GA 5  .   ? 18.599 8.946   36.960  1.00 67.88  ? 200 HEM G C1D 1 
HETATM 9494 C  C2D . HEM GA 5  .   ? 18.056 9.113   38.356  1.00 68.00  ? 200 HEM G C2D 1 
HETATM 9495 C  C3D . HEM GA 5  .   ? 18.843 10.079  38.916  1.00 68.88  ? 200 HEM G C3D 1 
HETATM 9496 C  C4D . HEM GA 5  .   ? 19.829 10.476  37.895  1.00 68.82  ? 200 HEM G C4D 1 
HETATM 9497 C  CMD . HEM GA 5  .   ? 16.882 8.335   38.926  1.00 67.76  ? 200 HEM G CMD 1 
HETATM 9498 C  CAD . HEM GA 5  .   ? 18.748 10.654  40.313  1.00 69.62  ? 200 HEM G CAD 1 
HETATM 9499 C  CBD . HEM GA 5  .   ? 17.939 11.912  40.321  1.00 71.06  ? 200 HEM G CBD 1 
HETATM 9500 C  CGD . HEM GA 5  .   ? 17.857 12.527  41.649  1.00 74.13  ? 200 HEM G CGD 1 
HETATM 9501 O  O1D . HEM GA 5  .   ? 17.001 12.112  42.498  1.00 76.06  ? 200 HEM G O1D 1 
HETATM 9502 O  O2D . HEM GA 5  .   ? 18.642 13.455  41.924  1.00 75.09  ? 200 HEM G O2D 1 
HETATM 9503 N  NA  . HEM GA 5  .   ? 21.838 11.342  35.875  1.00 69.34  ? 200 HEM G NA  1 
HETATM 9504 N  NB  . HEM GA 5  .   ? 21.732 10.170  33.354  1.00 67.98  ? 200 HEM G NB  1 
HETATM 9505 N  NC  . HEM GA 5  .   ? 19.533 8.555   34.198  1.00 67.55  ? 200 HEM G NC  1 
HETATM 9506 N  ND  . HEM GA 5  .   ? 19.636 9.776   36.743  1.00 68.86  ? 200 HEM G ND  1 
HETATM 9507 FE FE  . HEM GA 5  .   ? 20.689 9.941   35.036  1.00 66.76  ? 200 HEM G FE  1 
HETATM 9508 O  O1  . OXY HA 6  .   ? 19.433 11.202  34.701  1.00 70.21  ? 201 OXY G O1  1 
HETATM 9509 O  O2  . OXY HA 6  .   ? 18.236 11.177  34.377  1.00 70.63  ? 201 OXY G O2  1 
HETATM 9510 C  CHA . HEM IA 5  .   ? 10.954 53.815  19.787  1.00 57.21  ? 201 HEM H CHA 1 
HETATM 9511 C  CHB . HEM IA 5  .   ? 15.624 53.341  19.000  1.00 53.82  ? 201 HEM H CHB 1 
HETATM 9512 C  CHC . HEM IA 5  .   ? 16.622 56.617  22.406  1.00 54.34  ? 201 HEM H CHC 1 
HETATM 9513 C  CHD . HEM IA 5  .   ? 11.907 57.120  23.151  1.00 53.08  ? 201 HEM H CHD 1 
HETATM 9514 C  C1A . HEM IA 5  .   ? 12.156 53.376  19.258  1.00 55.43  ? 201 HEM H C1A 1 
HETATM 9515 C  C2A . HEM IA 5  .   ? 12.266 52.394  18.254  1.00 55.33  ? 201 HEM H C2A 1 
HETATM 9516 C  C3A . HEM IA 5  .   ? 13.580 52.261  18.029  1.00 54.11  ? 201 HEM H C3A 1 
HETATM 9517 C  C4A . HEM IA 5  .   ? 14.308 53.169  18.903  1.00 53.16  ? 201 HEM H C4A 1 
HETATM 9518 C  CMA . HEM IA 5  .   ? 14.260 51.308  17.025  1.00 53.07  ? 201 HEM H CMA 1 
HETATM 9519 C  CAA . HEM IA 5  .   ? 11.156 51.635  17.570  1.00 57.71  ? 201 HEM H CAA 1 
HETATM 9520 C  CBA . HEM IA 5  .   ? 10.685 52.329  16.324  1.00 60.21  ? 201 HEM H CBA 1 
HETATM 9521 C  CGA . HEM IA 5  .   ? 9.552  51.621  15.593  1.00 62.91  ? 201 HEM H CGA 1 
HETATM 9522 O  O1A . HEM IA 5  .   ? 8.395  52.124  15.604  1.00 62.23  ? 201 HEM H O1A 1 
HETATM 9523 O  O2A . HEM IA 5  .   ? 9.807  50.588  15.033  1.00 62.66  ? 201 HEM H O2A 1 
HETATM 9524 C  C1B . HEM IA 5  .   ? 16.346 54.198  19.856  1.00 52.86  ? 201 HEM H C1B 1 
HETATM 9525 C  C2B . HEM IA 5  .   ? 17.790 54.285  19.884  1.00 54.33  ? 201 HEM H C2B 1 
HETATM 9526 C  C3B . HEM IA 5  .   ? 18.079 55.255  20.910  1.00 55.66  ? 201 HEM H C3B 1 
HETATM 9527 C  C4B . HEM IA 5  .   ? 16.806 55.670  21.396  1.00 54.51  ? 201 HEM H C4B 1 
HETATM 9528 C  CMB . HEM IA 5  .   ? 18.747 53.531  19.041  1.00 54.02  ? 201 HEM H CMB 1 
HETATM 9529 C  CAB . HEM IA 5  .   ? 19.429 55.647  21.284  1.00 54.73  ? 201 HEM H CAB 1 
HETATM 9530 C  CBB . HEM IA 5  .   ? 20.026 56.741  20.863  1.00 58.42  ? 201 HEM H CBB 1 
HETATM 9531 C  C1C . HEM IA 5  .   ? 15.401 57.036  22.906  1.00 52.63  ? 201 HEM H C1C 1 
HETATM 9532 C  C2C . HEM IA 5  .   ? 15.287 58.037  23.969  1.00 52.95  ? 201 HEM H C2C 1 
HETATM 9533 C  C3C . HEM IA 5  .   ? 13.909 58.218  24.223  1.00 53.72  ? 201 HEM H C3C 1 
HETATM 9534 C  C4C . HEM IA 5  .   ? 13.245 57.266  23.243  1.00 52.47  ? 201 HEM H C4C 1 
HETATM 9535 C  CMC . HEM IA 5  .   ? 16.458 58.739  24.663  1.00 52.38  ? 201 HEM H CMC 1 
HETATM 9536 C  CAC . HEM IA 5  .   ? 13.325 59.047  25.128  1.00 51.84  ? 201 HEM H CAC 1 
HETATM 9537 C  CBC . HEM IA 5  .   ? 13.248 59.200  26.398  1.00 51.73  ? 201 HEM H CBC 1 
HETATM 9538 C  C1D . HEM IA 5  .   ? 11.228 56.270  22.303  1.00 54.76  ? 201 HEM H C1D 1 
HETATM 9539 C  C2D . HEM IA 5  .   ? 9.722  56.148  22.273  1.00 57.09  ? 201 HEM H C2D 1 
HETATM 9540 C  C3D . HEM IA 5  .   ? 9.464  55.202  21.313  1.00 57.80  ? 201 HEM H C3D 1 
HETATM 9541 C  C4D . HEM IA 5  .   ? 10.779 54.767  20.775  1.00 57.81  ? 201 HEM H C4D 1 
HETATM 9542 C  CMD . HEM IA 5  .   ? 8.770  56.947  23.166  1.00 57.34  ? 201 HEM H CMD 1 
HETATM 9543 C  CAD . HEM IA 5  .   ? 8.103  54.697  20.886  1.00 58.39  ? 201 HEM H CAD 1 
HETATM 9544 C  CBD . HEM IA 5  .   ? 7.708  53.449  21.636  1.00 61.37  ? 201 HEM H CBD 1 
HETATM 9545 C  CGD . HEM IA 5  .   ? 6.376  52.906  21.261  1.00 63.87  ? 201 HEM H CGD 1 
HETATM 9546 O  O1D . HEM IA 5  .   ? 6.152  52.454  20.088  1.00 64.47  ? 201 HEM H O1D 1 
HETATM 9547 O  O2D . HEM IA 5  .   ? 5.481  52.901  22.119  1.00 65.88  ? 201 HEM H O2D 1 
HETATM 9548 N  NA  . HEM IA 5  .   ? 13.408 53.862  19.671  1.00 54.26  ? 201 HEM H NA  1 
HETATM 9549 N  NB  . HEM IA 5  .   ? 15.733 55.008  20.732  1.00 53.71  ? 201 HEM H NB  1 
HETATM 9550 N  NC  . HEM IA 5  .   ? 14.141 56.611  22.498  1.00 53.36  ? 201 HEM H NC  1 
HETATM 9551 N  ND  . HEM IA 5  .   ? 11.798 55.447  21.407  1.00 55.28  ? 201 HEM H ND  1 
HETATM 9552 FE FE  . HEM IA 5  .   ? 13.759 55.249  21.072  1.00 57.10  ? 201 HEM H FE  1 
HETATM 9553 O  O1  . OXY JA 6  .   ? 13.768 53.964  22.318  1.00 65.16  ? 202 OXY H O1  1 
HETATM 9554 O  O2  . OXY JA 6  .   ? 13.328 53.987  23.481  1.00 71.47  ? 202 OXY H O2  1 
HETATM 9555 C  C1  . NAG KA 8  .   ? 4.937  41.359  34.702  1.00 117.05 ? 203 NAG H C1  1 
HETATM 9556 C  C2  . NAG KA 8  .   ? 4.181  40.981  36.012  1.00 116.75 ? 203 NAG H C2  1 
HETATM 9557 C  C3  . NAG KA 8  .   ? 4.737  39.660  36.497  1.00 117.85 ? 203 NAG H C3  1 
HETATM 9558 C  C4  . NAG KA 8  .   ? 4.464  38.647  35.400  1.00 119.26 ? 203 NAG H C4  1 
HETATM 9559 C  C5  . NAG KA 8  .   ? 5.195  39.079  34.109  1.00 117.23 ? 203 NAG H C5  1 
HETATM 9560 C  C6  . NAG KA 8  .   ? 4.996  38.140  32.966  1.00 114.03 ? 203 NAG H C6  1 
HETATM 9561 C  C7  . NAG KA 8  .   ? 3.234  42.578  37.537  1.00 116.31 ? 203 NAG H C7  1 
HETATM 9562 C  C8  . NAG KA 8  .   ? 2.975  42.531  39.056  1.00 114.28 ? 203 NAG H C8  1 
HETATM 9563 N  N2  . NAG KA 8  .   ? 4.319  41.985  37.054  1.00 116.31 ? 203 NAG H N2  1 
HETATM 9564 O  O3  . NAG KA 8  .   ? 4.099  39.283  37.703  1.00 114.16 ? 203 NAG H O3  1 
HETATM 9565 O  O4  . NAG KA 8  .   ? 4.904  37.349  35.820  1.00 125.65 ? 203 NAG H O4  1 
HETATM 9566 O  O5  . NAG KA 8  .   ? 4.697  40.366  33.692  1.00 116.06 ? 203 NAG H O5  1 
HETATM 9567 O  O6  . NAG KA 8  .   ? 3.620  38.190  32.590  1.00 112.95 ? 203 NAG H O6  1 
HETATM 9568 O  O7  . NAG KA 8  .   ? 2.422  43.162  36.791  1.00 117.91 ? 203 NAG H O7  1 
HETATM 9569 C  C1  . NAG LA 8  .   ? 4.070  36.299  35.470  1.00 131.75 ? 204 NAG H C1  1 
HETATM 9570 C  C2  . NAG LA 8  .   ? 4.840  34.985  35.645  1.00 134.01 ? 204 NAG H C2  1 
HETATM 9571 C  C3  . NAG LA 8  .   ? 3.915  33.729  35.637  1.00 136.88 ? 204 NAG H C3  1 
HETATM 9572 C  C4  . NAG LA 8  .   ? 2.628  33.935  36.446  1.00 138.85 ? 204 NAG H C4  1 
HETATM 9573 C  C5  . NAG LA 8  .   ? 1.980  35.262  36.002  1.00 136.07 ? 204 NAG H C5  1 
HETATM 9574 C  C6  . NAG LA 8  .   ? 0.658  35.604  36.661  1.00 135.72 ? 204 NAG H C6  1 
HETATM 9575 C  C7  . NAG LA 8  .   ? 7.108  34.842  34.828  1.00 133.80 ? 204 NAG H C7  1 
HETATM 9576 C  C8  . NAG LA 8  .   ? 8.008  34.205  33.766  1.00 133.60 ? 204 NAG H C8  1 
HETATM 9577 N  N2  . NAG LA 8  .   ? 5.805  34.902  34.556  1.00 133.28 ? 204 NAG H N2  1 
HETATM 9578 O  O3  . NAG LA 8  .   ? 4.607  32.599  36.165  1.00 135.64 ? 204 NAG H O3  1 
HETATM 9579 O  O4  . NAG LA 8  .   ? 1.748  32.813  36.206  1.00 146.94 ? 204 NAG H O4  1 
HETATM 9580 O  O5  . NAG LA 8  .   ? 2.887  36.349  36.293  1.00 133.72 ? 204 NAG H O5  1 
HETATM 9581 O  O6  . NAG LA 8  .   ? -0.403 35.594  35.715  1.00 134.39 ? 204 NAG H O6  1 
HETATM 9582 O  O7  . NAG LA 8  .   ? 7.592  35.254  35.896  1.00 132.91 ? 204 NAG H O7  1 
HETATM 9583 C  C1  . MAN MA 9  .   ? 0.956  32.394  37.272  1.00 155.28 ? 205 MAN H C1  1 
HETATM 9584 C  C2  . MAN MA 9  .   ? 1.677  31.331  38.156  1.00 158.18 ? 205 MAN H C2  1 
HETATM 9585 C  C3  . MAN MA 9  .   ? 1.293  29.826  37.959  1.00 161.43 ? 205 MAN H C3  1 
HETATM 9586 C  C4  . MAN MA 9  .   ? 0.037  29.567  37.092  1.00 161.77 ? 205 MAN H C4  1 
HETATM 9587 C  C5  . MAN MA 9  .   ? -0.232 30.684  36.083  1.00 161.65 ? 205 MAN H C5  1 
HETATM 9588 C  C6  . MAN MA 9  .   ? -1.562 30.476  35.377  1.00 163.83 ? 205 MAN H C6  1 
HETATM 9589 O  O2  . MAN MA 9  .   ? 1.523  31.669  39.527  1.00 157.63 ? 205 MAN H O2  1 
HETATM 9590 O  O3  . MAN MA 9  .   ? 1.101  29.205  39.263  1.00 165.23 ? 205 MAN H O3  1 
HETATM 9591 O  O4  . MAN MA 9  .   ? 0.200  28.347  36.380  1.00 162.22 ? 205 MAN H O4  1 
HETATM 9592 O  O5  . MAN MA 9  .   ? -0.312 31.948  36.769  1.00 157.73 ? 205 MAN H O5  1 
HETATM 9593 O  O6  . MAN MA 9  .   ? -2.624 30.586  36.346  1.00 166.98 ? 205 MAN H O6  1 
HETATM 9594 C  C1  . MAN NA 9  .   ? 1.607  27.897  39.448  1.00 168.56 ? 206 MAN H C1  1 
HETATM 9595 C  C2  . MAN NA 9  .   ? 0.503  26.923  39.971  1.00 169.22 ? 206 MAN H C2  1 
HETATM 9596 C  C3  . MAN NA 9  .   ? 0.280  27.053  41.499  1.00 169.52 ? 206 MAN H C3  1 
HETATM 9597 C  C4  . MAN NA 9  .   ? 1.624  26.927  42.241  1.00 169.77 ? 206 MAN H C4  1 
HETATM 9598 C  C5  . MAN NA 9  .   ? 2.601  27.994  41.707  1.00 169.60 ? 206 MAN H C5  1 
HETATM 9599 C  C6  . MAN NA 9  .   ? 3.971  27.890  42.362  1.00 170.06 ? 206 MAN H C6  1 
HETATM 9600 O  O2  . MAN NA 9  .   ? 0.855  25.579  39.660  1.00 169.85 ? 206 MAN H O2  1 
HETATM 9601 O  O3  . MAN NA 9  .   ? -0.633 26.055  41.959  1.00 169.06 ? 206 MAN H O3  1 
HETATM 9602 O  O4  . MAN NA 9  .   ? 1.436  27.089  43.647  1.00 169.38 ? 206 MAN H O4  1 
HETATM 9603 O  O5  . MAN NA 9  .   ? 2.797  27.844  40.267  1.00 169.28 ? 206 MAN H O5  1 
HETATM 9604 O  O6  . MAN NA 9  .   ? 4.688  29.110  42.245  1.00 170.22 ? 206 MAN H O6  1 
HETATM 9605 C  C1  . MAN OA 9  .   ? -3.902 30.295  35.840  1.00 169.89 ? 207 MAN H C1  1 
HETATM 9606 C  C2  . MAN OA 9  .   ? -4.972 31.010  36.707  1.00 170.42 ? 207 MAN H C2  1 
HETATM 9607 C  C3  . MAN OA 9  .   ? -5.182 30.280  38.061  1.00 171.10 ? 207 MAN H C3  1 
HETATM 9608 C  C4  . MAN OA 9  .   ? -5.437 28.778  37.861  1.00 170.97 ? 207 MAN H C4  1 
HETATM 9609 C  C5  . MAN OA 9  .   ? -4.297 28.167  37.020  1.00 171.53 ? 207 MAN H C5  1 
HETATM 9610 C  C6  . MAN OA 9  .   ? -4.536 26.695  36.697  1.00 171.94 ? 207 MAN H C6  1 
HETATM 9611 O  O2  . MAN OA 9  .   ? -6.204 31.111  36.000  1.00 171.06 ? 207 MAN H O2  1 
HETATM 9612 O  O3  . MAN OA 9  .   ? -6.266 30.854  38.781  1.00 170.63 ? 207 MAN H O3  1 
HETATM 9613 O  O4  . MAN OA 9  .   ? -5.520 28.133  39.130  1.00 170.47 ? 207 MAN H O4  1 
HETATM 9614 O  O5  . MAN OA 9  .   ? -4.165 28.876  35.748  1.00 170.78 ? 207 MAN H O5  1 
HETATM 9615 O  O6  . MAN OA 9  .   ? -3.466 25.881  37.158  1.00 171.13 ? 207 MAN H O6  1 
HETATM 9616 C  C1  . FUC PA 10 .   ? 3.453  37.980  31.226  1.00 113.43 ? 208 FUC H C1  1 
HETATM 9617 C  C2  . FUC PA 10 .   ? 2.117  37.282  30.989  1.00 112.95 ? 208 FUC H C2  1 
HETATM 9618 C  C3  . FUC PA 10 .   ? 0.934  38.222  31.210  1.00 113.24 ? 208 FUC H C3  1 
HETATM 9619 C  C4  . FUC PA 10 .   ? 1.122  39.575  30.509  1.00 113.95 ? 208 FUC H C4  1 
HETATM 9620 C  C5  . FUC PA 10 .   ? 2.497  40.152  30.828  1.00 113.77 ? 208 FUC H C5  1 
HETATM 9621 C  C6  . FUC PA 10 .   ? 2.773  41.426  30.054  1.00 113.33 ? 208 FUC H C6  1 
HETATM 9622 O  O2  . FUC PA 10 .   ? 1.998  36.184  31.881  1.00 111.08 ? 208 FUC H O2  1 
HETATM 9623 O  O3  . FUC PA 10 .   ? -0.234 37.599  30.708  1.00 111.96 ? 208 FUC H O3  1 
HETATM 9624 O  O4  . FUC PA 10 .   ? 0.968  39.436  29.102  1.00 116.40 ? 208 FUC H O4  1 
HETATM 9625 O  O5  . FUC PA 10 .   ? 3.519  39.192  30.481  1.00 114.79 ? 208 FUC H O5  1 
HETATM 9626 O  O   . HOH QA 11 .   ? 21.599 18.426  2.535   1.00 34.68  ? 301 HOH A O   1 
HETATM 9627 O  O   . HOH QA 11 .   ? 5.627  3.101   -4.604  1.00 31.31  ? 302 HOH A O   1 
HETATM 9628 O  O   . HOH QA 11 .   ? 24.792 31.036  -5.496  1.00 24.04  ? 303 HOH A O   1 
HETATM 9629 O  O   . HOH QA 11 .   ? 20.875 24.576  1.814   1.00 30.67  ? 304 HOH A O   1 
HETATM 9630 O  O   . HOH QA 11 .   ? 26.422 -5.636  -3.517  1.00 41.40  ? 305 HOH A O   1 
HETATM 9631 O  O   . HOH QA 11 .   ? 28.168 17.772  0.727   1.00 25.49  ? 306 HOH A O   1 
HETATM 9632 O  O   . HOH QA 11 .   ? 28.097 18.506  -1.952  1.00 34.37  ? 307 HOH A O   1 
HETATM 9633 O  O   . HOH QA 11 .   ? 6.274  4.671   -22.163 1.00 44.81  ? 308 HOH A O   1 
HETATM 9634 O  O   . HOH QA 11 .   ? 5.959  4.799   -8.194  1.00 31.38  ? 309 HOH A O   1 
HETATM 9635 O  O   . HOH QA 11 .   ? 8.551  20.713  -5.026  1.00 36.98  ? 310 HOH A O   1 
HETATM 9636 O  O   . HOH QA 11 .   ? 29.170 28.316  -3.006  1.00 56.47  ? 311 HOH A O   1 
HETATM 9637 O  O   . HOH RA 11 .   ? 41.702 39.399  -28.410 1.00 33.59  ? 301 HOH B O   1 
HETATM 9638 O  O   . HOH RA 11 .   ? 46.418 43.591  -43.123 1.00 48.37  ? 302 HOH B O   1 
HETATM 9639 O  O   . HOH SA 11 .   ? 37.925 50.183  -27.570 1.00 59.40  ? 301 HOH C O   1 
HETATM 9640 O  O   . HOH SA 11 .   ? 23.245 32.763  -31.743 1.00 38.22  ? 302 HOH C O   1 
HETATM 9641 O  O   . HOH SA 11 .   ? 13.343 30.604  -12.766 1.00 49.99  ? 303 HOH C O   1 
HETATM 9642 O  O   . HOH SA 11 .   ? 16.723 50.072  -24.452 1.00 44.23  ? 304 HOH C O   1 
HETATM 9643 O  O   . HOH SA 11 .   ? 16.507 37.774  -39.026 1.00 57.20  ? 305 HOH C O   1 
HETATM 9644 O  O   . HOH SA 11 .   ? 29.482 36.260  -21.911 1.00 51.21  ? 306 HOH C O   1 
HETATM 9645 O  O   . HOH SA 11 .   ? 29.030 34.115  -23.088 1.00 53.18  ? 307 HOH C O   1 
HETATM 9646 O  O   . HOH TA 11 .   ? 47.032 12.769  -31.447 1.00 47.89  ? 301 HOH D O   1 
HETATM 9647 O  O   . HOH TA 11 .   ? 20.930 -4.403  -5.909  1.00 43.98  ? 302 HOH D O   1 
HETATM 9648 O  O   . HOH TA 11 .   ? 36.165 -7.122  -13.265 1.00 50.99  ? 303 HOH D O   1 
HETATM 9649 O  O   . HOH TA 11 .   ? 46.125 9.619   -22.303 1.00 57.02  ? 304 HOH D O   1 
HETATM 9650 O  O   . HOH TA 11 .   ? 13.682 -13.812 -17.495 1.00 43.51  ? 305 HOH D O   1 
HETATM 9651 O  O   . HOH TA 11 .   ? 36.134 15.450  -14.255 1.00 38.53  ? 306 HOH D O   1 
HETATM 9652 O  O   . HOH TA 11 .   ? 35.948 -11.233 -22.650 1.00 63.78  ? 307 HOH D O   1 
HETATM 9653 O  O   . HOH TA 11 .   ? 25.417 9.629   -13.850 1.00 41.42  ? 308 HOH D O   1 
HETATM 9654 O  O   . HOH TA 11 .   ? 16.118 0.026   -20.331 1.00 54.57  ? 309 HOH D O   1 
HETATM 9655 O  O   . HOH UA 11 .   ? 22.789 45.646  1.635   1.00 41.89  ? 301 HOH E O   1 
HETATM 9656 O  O   . HOH UA 11 .   ? 11.855 50.727  5.855   1.00 48.10  ? 302 HOH E O   1 
HETATM 9657 O  O   . HOH UA 11 .   ? 6.704  39.592  -11.023 1.00 37.97  ? 303 HOH E O   1 
HETATM 9658 O  O   . HOH UA 11 .   ? 27.564 22.914  2.445   1.00 36.76  ? 304 HOH E O   1 
HETATM 9659 O  O   . HOH UA 11 .   ? 1.807  53.955  -6.156  1.00 59.52  ? 305 HOH E O   1 
HETATM 9660 O  O   . HOH UA 11 .   ? -1.149 50.786  12.045  1.00 31.24  ? 306 HOH E O   1 
HETATM 9661 O  O   . HOH UA 11 .   ? 0.649  43.092  7.420   1.00 51.60  ? 307 HOH E O   1 
HETATM 9662 O  O   . HOH UA 11 .   ? 28.177 26.786  7.767   1.00 39.34  ? 308 HOH E O   1 
HETATM 9663 O  O   . HOH UA 11 .   ? 0.336  46.368  -2.726  1.00 47.02  ? 309 HOH E O   1 
HETATM 9664 O  O   . HOH UA 11 .   ? 28.924 26.566  2.442   1.00 57.39  ? 310 HOH E O   1 
HETATM 9665 O  O   . HOH UA 11 .   ? 28.463 28.171  -0.554  1.00 53.96  ? 311 HOH E O   1 
HETATM 9666 O  O   . HOH VA 11 .   ? 39.254 20.118  34.041  1.00 33.07  ? 301 HOH F O   1 
HETATM 9667 O  O   . HOH VA 11 .   ? 29.272 14.713  47.506  1.00 39.21  ? 302 HOH F O   1 
HETATM 9668 O  O   . HOH VA 11 .   ? 49.646 17.925  51.487  1.00 43.21  ? 303 HOH F O   1 
HETATM 9669 O  O   . HOH VA 11 .   ? 46.351 40.537  28.269  1.00 55.59  ? 304 HOH F O   1 
HETATM 9670 O  O   . HOH VA 11 .   ? 15.873 34.749  37.157  1.00 44.10  ? 305 HOH F O   1 
HETATM 9671 O  O   . HOH VA 11 .   ? 41.468 15.278  30.255  1.00 49.70  ? 306 HOH F O   1 
HETATM 9672 O  O   . HOH VA 11 .   ? 29.618 44.542  48.091  1.00 49.20  ? 307 HOH F O   1 
HETATM 9673 O  O   . HOH VA 11 .   ? 13.599 32.719  41.864  1.00 68.29  ? 308 HOH F O   1 
HETATM 9674 O  O   . HOH VA 11 .   ? 48.436 29.957  39.591  1.00 40.34  ? 309 HOH F O   1 
HETATM 9675 O  O   . HOH WA 11 .   ? 7.444  6.335   42.618  1.00 42.36  ? 301 HOH G O   1 
HETATM 9676 O  O   . HOH WA 11 .   ? 34.339 1.688   21.702  1.00 41.50  ? 302 HOH G O   1 
HETATM 9677 O  O   . HOH WA 11 .   ? 15.544 5.484   40.783  1.00 56.98  ? 303 HOH G O   1 
HETATM 9678 O  O   . HOH XA 11 .   ? 42.117 48.062  31.192  1.00 50.55  ? 301 HOH H O   1 
HETATM 9679 O  O   . HOH XA 11 .   ? 8.665  46.529  35.869  1.00 37.79  ? 302 HOH H O   1 
HETATM 9680 O  O   . HOH XA 11 .   ? 20.092 62.030  9.798   1.00 46.92  ? 303 HOH H O   1 
HETATM 9681 O  O   . HOH XA 11 .   ? 15.312 46.416  14.068  1.00 45.34  ? 304 HOH H O   1 
HETATM 9682 O  O   . HOH XA 11 .   ? 22.312 47.271  3.670   1.00 32.27  ? 305 HOH H O   1 
HETATM 9683 O  O   . HOH XA 11 .   ? 40.927 50.841  14.748  1.00 39.51  ? 306 HOH H O   1 
HETATM 9684 O  O   . HOH XA 11 .   ? 40.367 50.603  22.109  1.00 38.85  ? 307 HOH H O   1 
# 
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 A . n 
A 1 2   CYS 2   2   2   CYS CYS A . n 
A 1 3   ASN 3   3   3   ASN ASN A . n 
A 1 4   ILE 4   4   4   ILE ILE A . n 
A 1 5   LEU 5   5   5   LEU LEU A . n 
A 1 6   GLN 6   6   6   GLN GLN A . n 
A 1 7   ARG 7   7   7   ARG ARG A . n 
A 1 8   LEU 8   8   8   LEU LEU A . n 
A 1 9   LYS 9   9   9   LYS LYS A . n 
A 1 10  VAL 10  10  10  VAL VAL A . n 
A 1 11  LYS 11  11  11  LYS LYS A . n 
A 1 12  MET 12  12  12  MET MET A . n 
A 1 13  GLN 13  13  13  GLN GLN A . n 
A 1 14  TRP 14  14  14  TRP TRP A . n 
A 1 15  ALA 15  15  15  ALA ALA A . n 
A 1 16  LYS 16  16  16  LYS LYS A . n 
A 1 17  ALA 17  17  17  ALA ALA A . n 
A 1 18  TYR 18  18  18  TYR TYR A . n 
A 1 19  GLY 19  19  19  GLY GLY A . n 
A 1 20  PHE 20  20  20  PHE PHE A . n 
A 1 21  GLY 21  21  21  GLY GLY A . n 
A 1 22  THR 22  22  22  THR THR A . n 
A 1 23  GLU 23  23  23  GLU GLU A . n 
A 1 24  ARG 24  24  24  ARG ARG A . n 
A 1 25  ALA 25  25  25  ALA ALA A . n 
A 1 26  LYS 26  26  26  LYS LYS A . n 
A 1 27  PHE 27  27  27  PHE PHE A . n 
A 1 28  GLY 28  28  28  GLY GLY A . n 
A 1 29  ASN 29  29  29  ASN ASN A . n 
A 1 30  SER 30  30  30  SER SER A . n 
A 1 31  LEU 31  31  31  LEU LEU A . n 
A 1 32  TRP 32  32  32  TRP TRP A . n 
A 1 33  THR 33  33  33  THR THR A . n 
A 1 34  SER 34  34  34  SER SER A . n 
A 1 35  ILE 35  35  35  ILE ILE A . n 
A 1 36  PHE 36  36  36  PHE PHE A . n 
A 1 37  ASN 37  37  37  ASN ASN A . n 
A 1 38  TYR 38  38  38  TYR TYR A . n 
A 1 39  ALA 39  39  39  ALA ALA A . n 
A 1 40  PRO 40  40  40  PRO PRO A . n 
A 1 41  ASP 41  41  41  ASP ASP A . n 
A 1 42  ALA 42  42  42  ALA ALA A . n 
A 1 43  ARG 43  43  43  ARG ARG A . n 
A 1 44  ASP 44  44  44  ASP ASP A . n 
A 1 45  LEU 45  45  45  LEU LEU A . n 
A 1 46  PHE 46  46  46  PHE PHE A . n 
A 1 47  LYS 47  47  47  LYS LYS A . n 
A 1 48  SER 48  48  48  SER SER A . n 
A 1 49  VAL 49  49  49  VAL VAL A . n 
A 1 50  LYS 50  50  50  LYS LYS A . n 
A 1 51  SER 51  51  51  SER SER A . n 
A 1 52  GLU 52  52  52  GLU GLU A . n 
A 1 53  ASP 53  53  53  ASP ASP A . n 
A 1 54  MET 54  54  54  MET MET A . n 
A 1 55  ARG 55  55  55  ARG ARG A . n 
A 1 56  SER 56  56  56  SER SER A . n 
A 1 57  PRO 57  57  57  PRO PRO A . n 
A 1 58  GLN 58  58  58  GLN GLN A . n 
A 1 59  PHE 59  59  59  PHE PHE A . n 
A 1 60  LYS 60  60  60  LYS LYS A . n 
A 1 61  ALA 61  61  61  ALA ALA A . n 
A 1 62  HIS 62  62  62  HIS HIS A . n 
A 1 63  ILE 63  63  63  ILE ILE A . n 
A 1 64  ALA 64  64  64  ALA ALA A . n 
A 1 65  ARG 65  65  65  ARG ARG A . n 
A 1 66  VAL 66  66  66  VAL VAL A . n 
A 1 67  ILE 67  67  67  ILE ILE A . n 
A 1 68  GLY 68  68  68  GLY GLY A . n 
A 1 69  GLY 69  69  69  GLY GLY A . n 
A 1 70  LEU 70  70  70  LEU LEU A . n 
A 1 71  ASP 71  71  71  ASP ASP A . n 
A 1 72  ARG 72  72  72  ARG ARG A . n 
A 1 73  VAL 73  73  73  VAL VAL A . n 
A 1 74  ILE 74  74  74  ILE ILE A . n 
A 1 75  SER 75  75  75  SER SER A . n 
A 1 76  MET 76  76  76  MET MET A . n 
A 1 77  PHE 77  77  77  PHE PHE A . n 
A 1 78  ASP 78  78  78  ASP ASP A . n 
A 1 79  ASN 79  79  79  ASN ASN A . n 
A 1 80  GLU 80  80  80  GLU GLU A . n 
A 1 81  ASP 81  81  81  ASP ASP A . n 
A 1 82  ALA 82  82  82  ALA ALA A . n 
A 1 83  LEU 83  83  83  LEU LEU A . n 
A 1 84  ASN 84  84  84  ASN ASN A . n 
A 1 85  ALA 85  85  85  ALA ALA A . n 
A 1 86  ASP 86  86  86  ASP ASP A . n 
A 1 87  LEU 87  87  87  LEU LEU A . n 
A 1 88  GLU 88  88  88  GLU GLU A . n 
A 1 89  HIS 89  89  89  HIS HIS A . n 
A 1 90  LEU 90  90  90  LEU LEU A . n 
A 1 91  LYS 91  91  91  LYS LYS A . n 
A 1 92  SER 92  92  92  SER SER A . n 
A 1 93  GLN 93  93  93  GLN GLN A . n 
A 1 94  HIS 94  94  94  HIS HIS A . n 
A 1 95  ASP 95  95  95  ASP ASP A . n 
A 1 96  PRO 96  96  96  PRO PRO A . n 
A 1 97  ARG 97  97  97  ARG ARG A . n 
A 1 98  GLY 98  98  98  GLY GLY A . n 
A 1 99  LEU 99  99  99  LEU LEU A . n 
A 1 100 ASP 100 100 100 ASP ASP A . n 
A 1 101 ALA 101 101 101 ALA ALA A . n 
A 1 102 LEU 102 102 102 LEU LEU A . n 
A 1 103 ASN 103 103 103 ASN ASN A . n 
A 1 104 PHE 104 104 104 PHE PHE A . n 
A 1 105 VAL 105 105 105 VAL VAL A . n 
A 1 106 VAL 106 106 106 VAL VAL A . n 
A 1 107 PHE 107 107 107 PHE PHE A . n 
A 1 108 GLY 108 108 108 GLY GLY A . n 
A 1 109 LYS 109 109 109 LYS LYS A . n 
A 1 110 ALA 110 110 110 ALA ALA A . n 
A 1 111 LEU 111 111 111 LEU LEU A . n 
A 1 112 PHE 112 112 112 PHE PHE A . n 
A 1 113 ALA 113 113 113 ALA ALA A . n 
A 1 114 THR 114 114 114 THR THR A . n 
A 1 115 VAL 115 115 115 VAL VAL A . n 
A 1 116 GLY 116 116 116 GLY GLY A . n 
A 1 117 GLY 117 117 117 GLY GLY A . n 
A 1 118 GLN 118 118 118 GLN GLN A . n 
A 1 119 PHE 119 119 119 PHE PHE A . n 
A 1 120 GLY 120 120 120 GLY GLY A . n 
A 1 121 VAL 121 121 121 VAL VAL A . n 
A 1 122 CYS 122 122 122 CYS CYS A . n 
A 1 123 PHE 123 123 123 PHE PHE A . n 
A 1 124 ASP 124 124 124 ASP ASP A . n 
A 1 125 LEU 125 125 125 LEU LEU A . n 
A 1 126 PRO 126 126 126 PRO PRO A . n 
A 1 127 ALA 127 127 127 ALA ALA A . n 
A 1 128 TRP 128 128 128 TRP TRP A . n 
A 1 129 GLU 129 129 129 GLU GLU A . n 
A 1 130 SER 130 130 130 SER SER A . n 
A 1 131 CYS 131 131 131 CYS CYS A . n 
A 1 132 TYR 132 132 132 TYR TYR A . n 
A 1 133 LYS 133 133 133 LYS LYS A . n 
A 1 134 VAL 134 134 134 VAL VAL A . n 
A 1 135 ILE 135 135 135 ILE ILE A . n 
A 1 136 ALA 136 136 136 ALA ALA A . n 
A 1 137 MET 137 137 137 MET MET A . n 
A 1 138 GLY 138 138 138 GLY GLY A . n 
A 1 139 ILE 139 139 139 ILE ILE A . n 
A 1 140 THR 140 140 140 THR THR A . n 
A 1 141 GLY 141 141 141 GLY GLY A . n 
A 1 142 ASN 142 142 142 ASN ASN A . n 
A 1 143 ASP 143 143 143 ASP ASP A . n 
A 1 144 MET 144 144 144 MET MET A . n 
A 1 145 PHE 145 145 145 PHE PHE A . n 
A 1 146 SER 146 146 146 SER SER A . n 
B 2 1   SER 1   1   1   SER SER B . n 
B 2 2   GLU 2   2   2   GLU GLU B . n 
B 2 3   CYS 3   3   3   CYS CYS B . n 
B 2 4   GLY 4   4   4   GLY GLY B . n 
B 2 5   PRO 5   5   5   PRO PRO B . n 
B 2 6   LEU 6   6   6   LEU LEU B . n 
B 2 7   GLN 7   7   7   GLN GLN B . n 
B 2 8   ARG 8   8   8   ARG ARG B . n 
B 2 9   LEU 9   9   9   LEU LEU B . n 
B 2 10  LYS 10  10  10  LYS LYS B . n 
B 2 11  VAL 11  11  11  VAL VAL B . n 
B 2 12  LYS 12  12  12  LYS LYS B . n 
B 2 13  ARG 13  13  13  ARG ARG B . n 
B 2 14  GLN 14  14  14  GLN GLN B . n 
B 2 15  TRP 15  15  15  TRP TRP B . n 
B 2 16  ALA 16  16  16  ALA ALA B . n 
B 2 17  GLU 17  17  17  GLU GLU B . n 
B 2 18  ALA 18  18  18  ALA ALA B . n 
B 2 19  TYR 19  19  19  TYR TYR B . n 
B 2 20  GLY 20  20  20  GLY GLY B . n 
B 2 21  SER 21  21  21  SER SER B . n 
B 2 22  GLY 22  22  22  GLY GLY B . n 
B 2 23  ASN 23  23  23  ASN ASN B . n 
B 2 24  GLY 24  24  24  GLY GLY B . n 
B 2 25  ARG 25  25  25  ARG ARG B . n 
B 2 26  GLU 26  26  26  GLU GLU B . n 
B 2 27  GLU 27  27  27  GLU GLU B . n 
B 2 28  PHE 28  28  28  PHE PHE B . n 
B 2 29  GLY 29  29  29  GLY GLY B . n 
B 2 30  HIS 30  30  30  HIS HIS B . n 
B 2 31  PHE 31  31  31  PHE PHE B . n 
B 2 32  ILE 32  32  32  ILE ILE B . n 
B 2 33  TRP 33  33  33  TRP TRP B . n 
B 2 34  ALA 34  34  34  ALA ALA B . n 
B 2 35  ASN 35  35  35  ASN ASN B . n 
B 2 36  VAL 36  36  36  VAL VAL B . n 
B 2 37  PHE 37  37  37  PHE PHE B . n 
B 2 38  LYS 38  38  38  LYS LYS B . n 
B 2 39  VAL 39  39  39  VAL VAL B . n 
B 2 40  ALA 40  40  40  ALA ALA B . n 
B 2 41  PRO 41  41  41  PRO PRO B . n 
B 2 42  SER 42  42  42  SER SER B . n 
B 2 43  ALA 43  43  43  ALA ALA B . n 
B 2 44  ARG 44  44  44  ARG ARG B . n 
B 2 45  ASP 45  45  45  ASP ASP B . n 
B 2 46  MET 46  46  46  MET MET B . n 
B 2 47  PHE 47  47  47  PHE PHE B . n 
B 2 48  LYS 48  48  48  LYS LYS B . n 
B 2 49  ARG 49  49  49  ARG ARG B . n 
B 2 50  VAL 50  50  50  VAL VAL B . n 
B 2 51  ARG 51  51  51  ARG ARG B . n 
B 2 52  GLY 52  52  52  GLY GLY B . n 
B 2 53  ASP 53  53  53  ASP ASP B . n 
B 2 54  ASN 54  54  54  ASN ASN B . n 
B 2 55  ILE 55  55  55  ILE ILE B . n 
B 2 56  TYR 56  56  56  TYR TYR B . n 
B 2 57  THR 57  57  57  THR THR B . n 
B 2 58  PRO 58  58  58  PRO PRO B . n 
B 2 59  ALA 59  59  59  ALA ALA B . n 
B 2 60  PHE 60  60  60  PHE PHE B . n 
B 2 61  ARG 61  61  61  ARG ARG B . n 
B 2 62  ALA 62  62  62  ALA ALA B . n 
B 2 63  HIS 63  63  63  HIS HIS B . n 
B 2 64  ALA 64  64  64  ALA ALA B . n 
B 2 65  THR 65  65  65  THR THR B . n 
B 2 66  ARG 66  66  66  ARG ARG B . n 
B 2 67  VAL 67  67  67  VAL VAL B . n 
B 2 68  LEU 68  68  68  LEU LEU B . n 
B 2 69  GLY 69  69  69  GLY GLY B . n 
B 2 70  GLY 70  70  70  GLY GLY B . n 
B 2 71  LEU 71  71  71  LEU LEU B . n 
B 2 72  ASP 72  72  72  ASP ASP B . n 
B 2 73  MET 73  73  73  MET MET B . n 
B 2 74  CYS 74  74  74  CYS CYS B . n 
B 2 75  VAL 75  75  75  VAL VAL B . n 
B 2 76  ALA 76  76  76  ALA ALA B . n 
B 2 77  LEU 77  77  77  LEU LEU B . n 
B 2 78  LEU 78  78  78  LEU LEU B . n 
B 2 79  ASP 79  79  79  ASP ASP B . n 
B 2 80  ASP 80  80  80  ASP ASP B . n 
B 2 81  GLU 81  81  81  GLU GLU B . n 
B 2 82  SER 82  82  82  SER SER B . n 
B 2 83  VAL 83  83  83  VAL VAL B . n 
B 2 84  LEU 84  84  84  LEU LEU B . n 
B 2 85  ASN 85  85  85  ASN ASN B . n 
B 2 86  THR 86  86  86  THR THR B . n 
B 2 87  GLN 87  87  87  GLN GLN B . n 
B 2 88  LEU 88  88  88  LEU LEU B . n 
B 2 89  ALA 89  89  89  ALA ALA B . n 
B 2 90  HIS 90  90  90  HIS HIS B . n 
B 2 91  LEU 91  91  91  LEU LEU B . n 
B 2 92  ALA 92  92  92  ALA ALA B . n 
B 2 93  SER 93  93  93  SER SER B . n 
B 2 94  GLN 94  94  94  GLN GLN B . n 
B 2 95  HIS 95  95  95  HIS HIS B . n 
B 2 96  SER 96  96  96  SER SER B . n 
B 2 97  SER 97  97  97  SER SER B . n 
B 2 98  ARG 98  98  98  ARG ARG B . n 
B 2 99  GLY 99  99  99  GLY GLY B . n 
B 2 100 VAL 100 100 100 VAL VAL B . n 
B 2 101 SER 101 101 101 SER SER B . n 
B 2 102 ALA 102 102 102 ALA ALA B . n 
B 2 103 GLU 103 103 103 GLU GLU B . n 
B 2 104 GLN 104 104 104 GLN GLN B . n 
B 2 105 TYR 105 105 105 TYR TYR B . n 
B 2 106 ASN 106 106 106 ASN ASN B . n 
B 2 107 VAL 107 107 107 VAL VAL B . n 
B 2 108 VAL 108 108 108 VAL VAL B . n 
B 2 109 GLU 109 109 109 GLU GLU B . n 
B 2 110 HIS 110 110 110 HIS HIS B . n 
B 2 111 ALA 111 111 111 ALA ALA B . n 
B 2 112 VAL 112 112 112 VAL VAL B . n 
B 2 113 MET 113 113 113 MET MET B . n 
B 2 114 MET 114 114 114 MET MET B . n 
B 2 115 GLY 115 115 115 GLY GLY B . n 
B 2 116 VAL 116 116 116 VAL VAL B . n 
B 2 117 GLU 117 117 117 GLU GLU B . n 
B 2 118 HIS 118 118 118 HIS HIS B . n 
B 2 119 GLU 119 119 119 GLU GLU B . n 
B 2 120 ILE 120 120 120 ILE ILE B . n 
B 2 121 GLY 121 121 121 GLY GLY B . n 
B 2 122 GLN 122 122 122 GLN GLN B . n 
B 2 123 ASN 123 123 123 ASN ASN B . n 
B 2 124 VAL 124 124 124 VAL VAL B . n 
B 2 125 PHE 125 125 125 PHE PHE B . n 
B 2 126 ASP 126 126 126 ASP ASP B . n 
B 2 127 LYS 127 127 127 LYS LYS B . n 
B 2 128 ASP 128 128 128 ASP ASP B . n 
B 2 129 ALA 129 129 129 ALA ALA B . n 
B 2 130 TRP 130 130 130 TRP TRP B . n 
B 2 131 GLN 131 131 131 GLN GLN B . n 
B 2 132 ALA 132 132 132 ALA ALA B . n 
B 2 133 CYS 133 133 133 CYS CYS B . n 
B 2 134 LEU 134 134 134 LEU LEU B . n 
B 2 135 ASP 135 135 135 ASP ASP B . n 
B 2 136 VAL 136 136 136 VAL VAL B . n 
B 2 137 ILE 137 137 137 ILE ILE B . n 
B 2 138 THR 138 138 138 THR THR B . n 
B 2 139 SER 139 139 139 SER SER B . n 
B 2 140 GLY 140 140 140 GLY GLY B . n 
B 2 141 ILE 141 141 141 ILE ILE B . n 
B 2 142 GLN 142 142 142 GLN GLN B . n 
B 2 143 GLY 143 143 143 GLY GLY B . n 
B 2 144 ASN 144 144 144 ASN ASN B . n 
C 3 1   SER 1   1   1   SER SER C . n 
C 3 2   SER 2   2   2   SER SER C . n 
C 3 3   ASN 3   3   3   ASN ASN C . n 
C 3 4   SER 4   4   4   SER SER C . n 
C 3 5   CYS 5   5   5   CYS CYS C . n 
C 3 6   THR 6   6   6   THR THR C . n 
C 3 7   THR 7   7   7   THR THR C . n 
C 3 8   GLU 8   8   8   GLU GLU C . n 
C 3 9   ASP 9   9   9   ASP ASP C . n 
C 3 10  ARG 10  10  10  ARG ARG C . n 
C 3 11  ARG 11  11  11  ARG ARG C . n 
C 3 12  GLU 12  12  12  GLU GLU C . n 
C 3 13  MET 13  13  13  MET MET C . n 
C 3 14  GLN 14  14  14  GLN GLN C . n 
C 3 15  LEU 15  15  15  LEU LEU C . n 
C 3 16  MET 16  16  16  MET MET C . n 
C 3 17  TRP 17  17  17  TRP TRP C . n 
C 3 18  ALA 18  18  18  ALA ALA C . n 
C 3 19  ASN 19  19  19  ASN ASN C . n 
C 3 20  VAL 20  20  20  VAL VAL C . n 
C 3 21  TRP 21  21  21  TRP TRP C . n 
C 3 22  SER 22  22  22  SER SER C . n 
C 3 23  ALA 23  23  23  ALA ALA C . n 
C 3 24  GLN 24  24  24  GLN GLN C . n 
C 3 25  PHE 25  25  25  PHE PHE C . n 
C 3 26  THR 26  26  26  THR THR C . n 
C 3 27  GLY 27  27  27  GLY GLY C . n 
C 3 28  ARG 28  28  28  ARG ARG C . n 
C 3 29  ARG 29  29  29  ARG ARG C . n 
C 3 30  LEU 30  30  30  LEU LEU C . n 
C 3 31  ALA 31  31  31  ALA ALA C . n 
C 3 32  ILE 32  32  32  ILE ILE C . n 
C 3 33  ALA 33  33  33  ALA ALA C . n 
C 3 34  GLN 34  34  34  GLN GLN C . n 
C 3 35  ALA 35  35  35  ALA ALA C . n 
C 3 36  VAL 36  36  36  VAL VAL C . n 
C 3 37  PHE 37  37  37  PHE PHE C . n 
C 3 38  LYS 38  38  38  LYS LYS C . n 
C 3 39  ASP 39  39  39  ASP ASP C . n 
C 3 40  LEU 40  40  40  LEU LEU C . n 
C 3 41  PHE 41  41  41  PHE PHE C . n 
C 3 42  ALA 42  42  42  ALA ALA C . n 
C 3 43  HIS 43  43  43  HIS HIS C . n 
C 3 44  VAL 44  44  44  VAL VAL C . n 
C 3 45  PRO 45  45  45  PRO PRO C . n 
C 3 46  ASP 46  46  46  ASP ASP C . n 
C 3 47  ALA 47  47  47  ALA ALA C . n 
C 3 48  VAL 48  48  48  VAL VAL C . n 
C 3 49  GLY 49  49  49  GLY GLY C . n 
C 3 50  LEU 50  50  50  LEU LEU C . n 
C 3 51  PHE 51  51  51  PHE PHE C . n 
C 3 52  ASP 52  52  52  ASP ASP C . n 
C 3 53  ARG 53  53  53  ARG ARG C . n 
C 3 54  VAL 54  54  54  VAL VAL C . n 
C 3 55  HIS 55  55  55  HIS HIS C . n 
C 3 56  GLY 56  56  56  GLY GLY C . n 
C 3 57  THR 57  57  57  THR THR C . n 
C 3 58  GLU 58  58  58  GLU GLU C . n 
C 3 59  ILE 59  59  59  ILE ILE C . n 
C 3 60  ASP 60  60  60  ASP ASP C . n 
C 3 61  SER 61  61  61  SER SER C . n 
C 3 62  SER 62  62  62  SER SER C . n 
C 3 63  GLU 63  63  63  GLU GLU C . n 
C 3 64  PHE 64  64  64  PHE PHE C . n 
C 3 65  LYS 65  65  65  LYS LYS C . n 
C 3 66  ALA 66  66  66  ALA ALA C . n 
C 3 67  HIS 67  67  67  HIS HIS C . n 
C 3 68  CYS 68  68  68  CYS CYS C . n 
C 3 69  ILE 69  69  69  ILE ILE C . n 
C 3 70  ARG 70  70  70  ARG ARG C . n 
C 3 71  VAL 71  71  71  VAL VAL C . n 
C 3 72  VAL 72  72  72  VAL VAL C . n 
C 3 73  ASN 73  73  73  ASN ASN C . n 
C 3 74  GLY 74  74  74  GLY GLY C . n 
C 3 75  LEU 75  75  75  LEU LEU C . n 
C 3 76  ASP 76  76  76  ASP ASP C . n 
C 3 77  SER 77  77  77  SER SER C . n 
C 3 78  ALA 78  78  78  ALA ALA C . n 
C 3 79  ILE 79  79  79  ILE ILE C . n 
C 3 80  GLY 80  80  80  GLY GLY C . n 
C 3 81  LEU 81  81  81  LEU LEU C . n 
C 3 82  LEU 82  82  82  LEU LEU C . n 
C 3 83  SER 83  83  83  SER SER C . n 
C 3 84  ASP 84  84  84  ASP ASP C . n 
C 3 85  PRO 85  85  85  PRO PRO C . n 
C 3 86  SER 86  86  86  SER SER C . n 
C 3 87  THR 87  87  87  THR THR C . n 
C 3 88  LEU 88  88  88  LEU LEU C . n 
C 3 89  ASN 89  89  89  ASN ASN C . n 
C 3 90  GLU 90  90  90  GLU GLU C . n 
C 3 91  GLN 91  91  91  GLN GLN C . n 
C 3 92  LEU 92  92  92  LEU LEU C . n 
C 3 93  SER 93  93  93  SER SER C . n 
C 3 94  HIS 94  94  94  HIS HIS C . n 
C 3 95  LEU 95  95  95  LEU LEU C . n 
C 3 96  ALA 96  96  96  ALA ALA C . n 
C 3 97  THR 97  97  97  THR THR C . n 
C 3 98  GLN 98  98  98  GLN GLN C . n 
C 3 99  HIS 99  99  99  HIS HIS C . n 
C 3 100 GLN 100 100 100 GLN GLN C . n 
C 3 101 GLU 101 101 101 GLU GLU C . n 
C 3 102 ARG 102 102 102 ARG ARG C . n 
C 3 103 ALA 103 103 103 ALA ALA C . n 
C 3 104 GLY 104 104 104 GLY GLY C . n 
C 3 105 VAL 105 105 105 VAL VAL C . n 
C 3 106 THR 106 106 106 THR THR C . n 
C 3 107 LYS 107 107 107 LYS LYS C . n 
C 3 108 GLY 108 108 108 GLY GLY C . n 
C 3 109 GLY 109 109 109 GLY GLY C . n 
C 3 110 PHE 110 110 110 PHE PHE C . n 
C 3 111 SER 111 111 111 SER SER C . n 
C 3 112 ALA 112 112 112 ALA ALA C . n 
C 3 113 ILE 113 113 113 ILE ILE C . n 
C 3 114 ALA 114 114 114 ALA ALA C . n 
C 3 115 GLN 115 115 115 GLN GLN C . n 
C 3 116 SER 116 116 116 SER SER C . n 
C 3 117 PHE 117 117 117 PHE PHE C . n 
C 3 118 LEU 118 118 118 LEU LEU C . n 
C 3 119 ARG 119 119 119 ARG ARG C . n 
C 3 120 VAL 120 120 120 VAL VAL C . n 
C 3 121 MET 121 121 121 MET MET C . n 
C 3 122 PRO 122 122 122 PRO PRO C . n 
C 3 123 GLN 123 123 123 GLN GLN C . n 
C 3 124 VAL 124 124 124 VAL VAL C . n 
C 3 125 ALA 125 125 125 ALA ALA C . n 
C 3 126 SER 126 126 126 SER SER C . n 
C 3 127 CYS 127 127 127 CYS CYS C . n 
C 3 128 PHE 128 128 128 PHE PHE C . n 
C 3 129 ASN 129 129 129 ASN ASN C . n 
C 3 130 PRO 130 130 130 PRO PRO C . n 
C 3 131 ASP 131 131 131 ASP ASP C . n 
C 3 132 ALA 132 132 132 ALA ALA C . n 
C 3 133 TRP 133 133 133 TRP TRP C . n 
C 3 134 SER 134 134 134 SER SER C . n 
C 3 135 ARG 135 135 135 ARG ARG C . n 
C 3 136 CYS 136 136 136 CYS CYS C . n 
C 3 137 PHE 137 137 137 PHE PHE C . n 
C 3 138 ASN 138 138 138 ASN ASN C . n 
C 3 139 ARG 139 139 139 ARG ARG C . n 
C 3 140 ILE 140 140 140 ILE ILE C . n 
C 3 141 THR 141 141 141 THR THR C . n 
C 3 142 ASN 142 142 142 ASN ASN C . n 
C 3 143 GLY 143 143 143 GLY GLY C . n 
C 3 144 MET 144 144 144 MET MET C . n 
C 3 145 THR 145 145 145 THR THR C . n 
C 3 146 GLU 146 146 146 GLU GLU C . n 
C 3 147 GLY 147 147 147 GLY GLY C . n 
C 3 148 LEU 148 148 148 LEU LEU C . n 
C 3 149 ALA 149 149 149 ALA ALA C . n 
C 3 150 GLU 150 150 150 GLU GLU C . n 
D 4 1   SER 1   1   ?   ?   ?   D . n 
D 4 2   GLU 2   2   ?   ?   ?   D . n 
D 4 3   PHE 3   3   3   PHE PHE D . n 
D 4 4   CYS 4   4   4   CYS CYS D . n 
D 4 5   SER 5   5   5   SER SER D . n 
D 4 6   GLU 6   6   6   GLU GLU D . n 
D 4 7   ALA 7   7   7   ALA ALA D . n 
D 4 8   ASP 8   8   8   ASP ASP D . n 
D 4 9   ALA 9   9   9   ALA ALA D . n 
D 4 10  THR 10  10  10  THR THR D . n 
D 4 11  ILE 11  11  11  ILE ILE D . n 
D 4 12  VAL 12  12  12  VAL VAL D . n 
D 4 13  ILE 13  13  13  ILE ILE D . n 
D 4 14  LYS 14  14  14  LYS LYS D . n 
D 4 15  GLN 15  15  15  GLN GLN D . n 
D 4 16  TRP 16  16  16  TRP TRP D . n 
D 4 17  ASN 17  17  17  ASN ASN D . n 
D 4 18  GLN 18  18  18  GLN GLN D . n 
D 4 19  ILE 19  19  19  ILE ILE D . n 
D 4 20  TYR 20  20  20  TYR TYR D . n 
D 4 21  ASN 21  21  21  ASN ASN D . n 
D 4 22  ALA 22  22  22  ALA ALA D . n 
D 4 23  GLY 23  23  23  GLY GLY D . n 
D 4 24  ILE 24  24  24  ILE ILE D . n 
D 4 25  GLY 25  25  25  GLY GLY D . n 
D 4 26  ALA 26  26  26  ALA ALA D . n 
D 4 27  LYS 27  27  27  LYS LYS D . n 
D 4 28  SER 28  28  28  SER SER D . n 
D 4 29  ARG 29  29  29  ARG ARG D . n 
D 4 30  TRP 30  30  30  TRP TRP D . n 
D 4 31  THR 31  31  31  THR THR D . n 
D 4 32  MET 32  32  32  MET MET D . n 
D 4 33  GLY 33  33  33  GLY GLY D . n 
D 4 34  ASN 34  34  34  ASN ASN D . n 
D 4 35  GLU 35  35  35  GLU GLU D . n 
D 4 36  ILE 36  36  36  ILE ILE D . n 
D 4 37  PHE 37  37  37  PHE PHE D . n 
D 4 38  SER 38  38  38  SER SER D . n 
D 4 39  SER 39  39  39  SER SER D . n 
D 4 40  LEU 40  40  40  LEU LEU D . n 
D 4 41  PHE 41  41  41  PHE PHE D . n 
D 4 42  LYS 42  42  42  LYS LYS D . n 
D 4 43  LEU 43  43  43  LEU LEU D . n 
D 4 44  LYS 44  44  44  LYS LYS D . n 
D 4 45  PRO 45  45  45  PRO PRO D . n 
D 4 46  GLU 46  46  46  GLU GLU D . n 
D 4 47  SER 47  47  47  SER SER D . n 
D 4 48  GLU 48  48  48  GLU GLU D . n 
D 4 49  VAL 49  49  49  VAL VAL D . n 
D 4 50  LEU 50  50  50  LEU LEU D . n 
D 4 51  PHE 51  51  51  PHE PHE D . n 
D 4 52  ASN 52  52  52  ASN ASN D . n 
D 4 53  ASN 53  53  53  ASN ASN D . n 
D 4 54  VAL 54  54  54  VAL VAL D . n 
D 4 55  ASN 55  55  55  ASN ASN D . n 
D 4 56  VAL 56  56  56  VAL VAL D . n 
D 4 57  ALA 57  57  57  ALA ALA D . n 
D 4 58  ASN 58  58  58  ASN ASN D . n 
D 4 59  MET 59  59  59  MET MET D . n 
D 4 60  SER 60  60  60  SER SER D . n 
D 4 61  SER 61  61  61  SER SER D . n 
D 4 62  GLY 62  62  62  GLY GLY D . n 
D 4 63  ALA 63  63  63  ALA ALA D . n 
D 4 64  PHE 64  64  64  PHE PHE D . n 
D 4 65  HIS 65  65  65  HIS HIS D . n 
D 4 66  ALA 66  66  66  ALA ALA D . n 
D 4 67  HIS 67  67  67  HIS HIS D . n 
D 4 68  THR 68  68  68  THR THR D . n 
D 4 69  VAL 69  69  69  VAL VAL D . n 
D 4 70  ARG 70  70  70  ARG ARG D . n 
D 4 71  VAL 71  71  71  VAL VAL D . n 
D 4 72  LEU 72  72  72  LEU LEU D . n 
D 4 73  SER 73  73  73  SER SER D . n 
D 4 74  GLY 74  74  74  GLY GLY D . n 
D 4 75  LEU 75  75  75  LEU LEU D . n 
D 4 76  ASP 76  76  76  ASP ASP D . n 
D 4 77  MET 77  77  77  MET MET D . n 
D 4 78  GLY 78  78  78  GLY GLY D . n 
D 4 79  ILE 79  79  79  ILE ILE D . n 
D 4 80  ASN 80  80  80  ASN ASN D . n 
D 4 81  TYR 81  81  81  TYR TYR D . n 
D 4 82  LEU 82  82  82  LEU LEU D . n 
D 4 83  ASN 83  83  83  ASN ASN D . n 
D 4 84  ASP 84  84  84  ASP ASP D . n 
D 4 85  ALA 85  85  85  ALA ALA D . n 
D 4 86  GLY 86  86  86  GLY GLY D . n 
D 4 87  THR 87  87  87  THR THR D . n 
D 4 88  LEU 88  88  88  LEU LEU D . n 
D 4 89  THR 89  89  89  THR THR D . n 
D 4 90  SER 90  90  90  SER SER D . n 
D 4 91  LEU 91  91  91  LEU LEU D . n 
D 4 92  THR 92  92  92  THR THR D . n 
D 4 93  ALA 93  93  93  ALA ALA D . n 
D 4 94  HIS 94  94  94  HIS HIS D . n 
D 4 95  LEU 95  95  95  LEU LEU D . n 
D 4 96  ALA 96  96  96  ALA ALA D . n 
D 4 97  ALA 97  97  97  ALA ALA D . n 
D 4 98  GLN 98  98  98  GLN GLN D . n 
D 4 99  HIS 99  99  99  HIS HIS D . n 
D 4 100 VAL 100 100 100 VAL VAL D . n 
D 4 101 ALA 101 101 101 ALA ALA D . n 
D 4 102 ARG 102 102 102 ARG ARG D . n 
D 4 103 THR 103 103 103 THR THR D . n 
D 4 104 GLY 104 104 104 GLY GLY D . n 
D 4 105 LEU 105 105 105 LEU LEU D . n 
D 4 106 LYS 106 106 106 LYS LYS D . n 
D 4 107 ALA 107 107 107 ALA ALA D . n 
D 4 108 VAL 108 108 108 VAL VAL D . n 
D 4 109 TYR 109 109 109 TYR TYR D . n 
D 4 110 PHE 110 110 110 PHE PHE D . n 
D 4 111 ASP 111 111 111 ASP ASP D . n 
D 4 112 ALA 112 112 112 ALA ALA D . n 
D 4 113 MET 113 113 113 MET MET D . n 
D 4 114 GLY 114 114 114 GLY GLY D . n 
D 4 115 LYS 115 115 115 LYS LYS D . n 
D 4 116 VAL 116 116 116 VAL VAL D . n 
D 4 117 LEU 117 117 117 LEU LEU D . n 
D 4 118 MET 118 118 118 MET MET D . n 
D 4 119 THR 119 119 119 THR THR D . n 
D 4 120 VAL 120 120 120 VAL VAL D . n 
D 4 121 LEU 121 121 121 LEU LEU D . n 
D 4 122 PRO 122 122 122 PRO PRO D . n 
D 4 123 SER 123 123 123 SER SER D . n 
D 4 124 LEU 124 124 124 LEU LEU D . n 
D 4 125 ILE 125 125 125 ILE ILE D . n 
D 4 126 ASP 126 126 126 ASP ASP D . n 
D 4 127 ASN 127 127 127 ASN ASN D . n 
D 4 128 PHE 128 128 128 PHE PHE D . n 
D 4 129 ASN 129 129 129 ASN ASN D . n 
D 4 130 PRO 130 130 130 PRO PRO D . n 
D 4 131 ASP 131 131 131 ASP ASP D . n 
D 4 132 ALA 132 132 132 ALA ALA D . n 
D 4 133 TRP 133 133 133 TRP TRP D . n 
D 4 134 ARG 134 134 134 ARG ARG D . n 
D 4 135 ASN 135 135 135 ASN ASN D . n 
D 4 136 CYS 136 136 136 CYS CYS D . n 
D 4 137 LEU 137 137 137 LEU LEU D . n 
D 4 138 LEU 138 138 138 LEU LEU D . n 
D 4 139 PRO 139 139 139 PRO PRO D . n 
D 4 140 LEU 140 140 140 LEU LEU D . n 
D 4 141 LYS 141 141 141 LYS LYS D . n 
D 4 142 ASN 142 142 142 ASN ASN D . n 
D 4 143 ALA 143 143 143 ALA ALA D . n 
D 4 144 ILE 144 144 144 ILE ILE D . n 
D 4 145 ALA 145 145 145 ALA ALA D . n 
D 4 146 LYS 146 146 146 LYS LYS D . n 
D 4 147 GLY 147 147 147 GLY GLY D . n 
D 4 148 LEU 148 148 148 LEU LEU D . n 
D 4 149 PRO 149 149 149 PRO PRO D . n 
E 1 1   ASP 1   1   1   ASP ASP E . n 
E 1 2   CYS 2   2   2   CYS CYS E . n 
E 1 3   ASN 3   3   3   ASN ASN E . n 
E 1 4   ILE 4   4   4   ILE ILE E . n 
E 1 5   LEU 5   5   5   LEU LEU E . n 
E 1 6   GLN 6   6   6   GLN GLN E . n 
E 1 7   ARG 7   7   7   ARG ARG E . n 
E 1 8   LEU 8   8   8   LEU LEU E . n 
E 1 9   LYS 9   9   9   LYS LYS E . n 
E 1 10  VAL 10  10  10  VAL VAL E . n 
E 1 11  LYS 11  11  11  LYS LYS E . n 
E 1 12  MET 12  12  12  MET MET E . n 
E 1 13  GLN 13  13  13  GLN GLN E . n 
E 1 14  TRP 14  14  14  TRP TRP E . n 
E 1 15  ALA 15  15  15  ALA ALA E . n 
E 1 16  LYS 16  16  16  LYS LYS E . n 
E 1 17  ALA 17  17  17  ALA ALA E . n 
E 1 18  TYR 18  18  18  TYR TYR E . n 
E 1 19  GLY 19  19  19  GLY GLY E . n 
E 1 20  PHE 20  20  20  PHE PHE E . n 
E 1 21  GLY 21  21  21  GLY GLY E . n 
E 1 22  THR 22  22  22  THR THR E . n 
E 1 23  GLU 23  23  23  GLU GLU E . n 
E 1 24  ARG 24  24  24  ARG ARG E . n 
E 1 25  ALA 25  25  25  ALA ALA E . n 
E 1 26  LYS 26  26  26  LYS LYS E . n 
E 1 27  PHE 27  27  27  PHE PHE E . n 
E 1 28  GLY 28  28  28  GLY GLY E . n 
E 1 29  ASN 29  29  29  ASN ASN E . n 
E 1 30  SER 30  30  30  SER SER E . n 
E 1 31  LEU 31  31  31  LEU LEU E . n 
E 1 32  TRP 32  32  32  TRP TRP E . n 
E 1 33  THR 33  33  33  THR THR E . n 
E 1 34  SER 34  34  34  SER SER E . n 
E 1 35  ILE 35  35  35  ILE ILE E . n 
E 1 36  PHE 36  36  36  PHE PHE E . n 
E 1 37  ASN 37  37  37  ASN ASN E . n 
E 1 38  TYR 38  38  38  TYR TYR E . n 
E 1 39  ALA 39  39  39  ALA ALA E . n 
E 1 40  PRO 40  40  40  PRO PRO E . n 
E 1 41  ASP 41  41  41  ASP ASP E . n 
E 1 42  ALA 42  42  42  ALA ALA E . n 
E 1 43  ARG 43  43  43  ARG ARG E . n 
E 1 44  ASP 44  44  44  ASP ASP E . n 
E 1 45  LEU 45  45  45  LEU LEU E . n 
E 1 46  PHE 46  46  46  PHE PHE E . n 
E 1 47  LYS 47  47  47  LYS LYS E . n 
E 1 48  SER 48  48  48  SER SER E . n 
E 1 49  VAL 49  49  49  VAL VAL E . n 
E 1 50  LYS 50  50  50  LYS LYS E . n 
E 1 51  SER 51  51  51  SER SER E . n 
E 1 52  GLU 52  52  52  GLU GLU E . n 
E 1 53  ASP 53  53  53  ASP ASP E . n 
E 1 54  MET 54  54  54  MET MET E . n 
E 1 55  ARG 55  55  55  ARG ARG E . n 
E 1 56  SER 56  56  56  SER SER E . n 
E 1 57  PRO 57  57  57  PRO PRO E . n 
E 1 58  GLN 58  58  58  GLN GLN E . n 
E 1 59  PHE 59  59  59  PHE PHE E . n 
E 1 60  LYS 60  60  60  LYS LYS E . n 
E 1 61  ALA 61  61  61  ALA ALA E . n 
E 1 62  HIS 62  62  62  HIS HIS E . n 
E 1 63  ILE 63  63  63  ILE ILE E . n 
E 1 64  ALA 64  64  64  ALA ALA E . n 
E 1 65  ARG 65  65  65  ARG ARG E . n 
E 1 66  VAL 66  66  66  VAL VAL E . n 
E 1 67  ILE 67  67  67  ILE ILE E . n 
E 1 68  GLY 68  68  68  GLY GLY E . n 
E 1 69  GLY 69  69  69  GLY GLY E . n 
E 1 70  LEU 70  70  70  LEU LEU E . n 
E 1 71  ASP 71  71  71  ASP ASP E . n 
E 1 72  ARG 72  72  72  ARG ARG E . n 
E 1 73  VAL 73  73  73  VAL VAL E . n 
E 1 74  ILE 74  74  74  ILE ILE E . n 
E 1 75  SER 75  75  75  SER SER E . n 
E 1 76  MET 76  76  76  MET MET E . n 
E 1 77  PHE 77  77  77  PHE PHE E . n 
E 1 78  ASP 78  78  78  ASP ASP E . n 
E 1 79  ASN 79  79  79  ASN ASN E . n 
E 1 80  GLU 80  80  80  GLU GLU E . n 
E 1 81  ASP 81  81  81  ASP ASP E . n 
E 1 82  ALA 82  82  82  ALA ALA E . n 
E 1 83  LEU 83  83  83  LEU LEU E . n 
E 1 84  ASN 84  84  84  ASN ASN E . n 
E 1 85  ALA 85  85  85  ALA ALA E . n 
E 1 86  ASP 86  86  86  ASP ASP E . n 
E 1 87  LEU 87  87  87  LEU LEU E . n 
E 1 88  GLU 88  88  88  GLU GLU E . n 
E 1 89  HIS 89  89  89  HIS HIS E . n 
E 1 90  LEU 90  90  90  LEU LEU E . n 
E 1 91  LYS 91  91  91  LYS LYS E . n 
E 1 92  SER 92  92  92  SER SER E . n 
E 1 93  GLN 93  93  93  GLN GLN E . n 
E 1 94  HIS 94  94  94  HIS HIS E . n 
E 1 95  ASP 95  95  95  ASP ASP E . n 
E 1 96  PRO 96  96  96  PRO PRO E . n 
E 1 97  ARG 97  97  97  ARG ARG E . n 
E 1 98  GLY 98  98  98  GLY GLY E . n 
E 1 99  LEU 99  99  99  LEU LEU E . n 
E 1 100 ASP 100 100 100 ASP ASP E . n 
E 1 101 ALA 101 101 101 ALA ALA E . n 
E 1 102 LEU 102 102 102 LEU LEU E . n 
E 1 103 ASN 103 103 103 ASN ASN E . n 
E 1 104 PHE 104 104 104 PHE PHE E . n 
E 1 105 VAL 105 105 105 VAL VAL E . n 
E 1 106 VAL 106 106 106 VAL VAL E . n 
E 1 107 PHE 107 107 107 PHE PHE E . n 
E 1 108 GLY 108 108 108 GLY GLY E . n 
E 1 109 LYS 109 109 109 LYS LYS E . n 
E 1 110 ALA 110 110 110 ALA ALA E . n 
E 1 111 LEU 111 111 111 LEU LEU E . n 
E 1 112 PHE 112 112 112 PHE PHE E . n 
E 1 113 ALA 113 113 113 ALA ALA E . n 
E 1 114 THR 114 114 114 THR THR E . n 
E 1 115 VAL 115 115 115 VAL VAL E . n 
E 1 116 GLY 116 116 116 GLY GLY E . n 
E 1 117 GLY 117 117 117 GLY GLY E . n 
E 1 118 GLN 118 118 118 GLN GLN E . n 
E 1 119 PHE 119 119 119 PHE PHE E . n 
E 1 120 GLY 120 120 120 GLY GLY E . n 
E 1 121 VAL 121 121 121 VAL VAL E . n 
E 1 122 CYS 122 122 122 CYS CYS E . n 
E 1 123 PHE 123 123 123 PHE PHE E . n 
E 1 124 ASP 124 124 124 ASP ASP E . n 
E 1 125 LEU 125 125 125 LEU LEU E . n 
E 1 126 PRO 126 126 126 PRO PRO E . n 
E 1 127 ALA 127 127 127 ALA ALA E . n 
E 1 128 TRP 128 128 128 TRP TRP E . n 
E 1 129 GLU 129 129 129 GLU GLU E . n 
E 1 130 SER 130 130 130 SER SER E . n 
E 1 131 CYS 131 131 131 CYS CYS E . n 
E 1 132 TYR 132 132 132 TYR TYR E . n 
E 1 133 LYS 133 133 133 LYS LYS E . n 
E 1 134 VAL 134 134 134 VAL VAL E . n 
E 1 135 ILE 135 135 135 ILE ILE E . n 
E 1 136 ALA 136 136 136 ALA ALA E . n 
E 1 137 MET 137 137 137 MET MET E . n 
E 1 138 GLY 138 138 138 GLY GLY E . n 
E 1 139 ILE 139 139 139 ILE ILE E . n 
E 1 140 THR 140 140 140 THR THR E . n 
E 1 141 GLY 141 141 141 GLY GLY E . n 
E 1 142 ASN 142 142 142 ASN ASN E . n 
E 1 143 ASP 143 143 143 ASP ASP E . n 
E 1 144 MET 144 144 144 MET MET E . n 
E 1 145 PHE 145 145 145 PHE PHE E . n 
E 1 146 SER 146 146 146 SER SER E . n 
F 2 1   SER 1   1   1   SER SER F . n 
F 2 2   GLU 2   2   2   GLU GLU F . n 
F 2 3   CYS 3   3   3   CYS CYS F . n 
F 2 4   GLY 4   4   4   GLY GLY F . n 
F 2 5   PRO 5   5   5   PRO PRO F . n 
F 2 6   LEU 6   6   6   LEU LEU F . n 
F 2 7   GLN 7   7   7   GLN GLN F . n 
F 2 8   ARG 8   8   8   ARG ARG F . n 
F 2 9   LEU 9   9   9   LEU LEU F . n 
F 2 10  LYS 10  10  10  LYS LYS F . n 
F 2 11  VAL 11  11  11  VAL VAL F . n 
F 2 12  LYS 12  12  12  LYS LYS F . n 
F 2 13  ARG 13  13  13  ARG ARG F . n 
F 2 14  GLN 14  14  14  GLN GLN F . n 
F 2 15  TRP 15  15  15  TRP TRP F . n 
F 2 16  ALA 16  16  16  ALA ALA F . n 
F 2 17  GLU 17  17  17  GLU GLU F . n 
F 2 18  ALA 18  18  18  ALA ALA F . n 
F 2 19  TYR 19  19  19  TYR TYR F . n 
F 2 20  GLY 20  20  20  GLY GLY F . n 
F 2 21  SER 21  21  21  SER SER F . n 
F 2 22  GLY 22  22  22  GLY GLY F . n 
F 2 23  ASN 23  23  23  ASN ASN F . n 
F 2 24  GLY 24  24  24  GLY GLY F . n 
F 2 25  ARG 25  25  25  ARG ARG F . n 
F 2 26  GLU 26  26  26  GLU GLU F . n 
F 2 27  GLU 27  27  27  GLU GLU F . n 
F 2 28  PHE 28  28  28  PHE PHE F . n 
F 2 29  GLY 29  29  29  GLY GLY F . n 
F 2 30  HIS 30  30  30  HIS HIS F . n 
F 2 31  PHE 31  31  31  PHE PHE F . n 
F 2 32  ILE 32  32  32  ILE ILE F . n 
F 2 33  TRP 33  33  33  TRP TRP F . n 
F 2 34  ALA 34  34  34  ALA ALA F . n 
F 2 35  ASN 35  35  35  ASN ASN F . n 
F 2 36  VAL 36  36  36  VAL VAL F . n 
F 2 37  PHE 37  37  37  PHE PHE F . n 
F 2 38  LYS 38  38  38  LYS LYS F . n 
F 2 39  VAL 39  39  39  VAL VAL F . n 
F 2 40  ALA 40  40  40  ALA ALA F . n 
F 2 41  PRO 41  41  41  PRO PRO F . n 
F 2 42  SER 42  42  42  SER SER F . n 
F 2 43  ALA 43  43  43  ALA ALA F . n 
F 2 44  ARG 44  44  44  ARG ARG F . n 
F 2 45  ASP 45  45  45  ASP ASP F . n 
F 2 46  MET 46  46  46  MET MET F . n 
F 2 47  PHE 47  47  47  PHE PHE F . n 
F 2 48  LYS 48  48  48  LYS LYS F . n 
F 2 49  ARG 49  49  49  ARG ARG F . n 
F 2 50  VAL 50  50  50  VAL VAL F . n 
F 2 51  ARG 51  51  51  ARG ARG F . n 
F 2 52  GLY 52  52  52  GLY GLY F . n 
F 2 53  ASP 53  53  53  ASP ASP F . n 
F 2 54  ASN 54  54  54  ASN ASN F . n 
F 2 55  ILE 55  55  55  ILE ILE F . n 
F 2 56  TYR 56  56  56  TYR TYR F . n 
F 2 57  THR 57  57  57  THR THR F . n 
F 2 58  PRO 58  58  58  PRO PRO F . n 
F 2 59  ALA 59  59  59  ALA ALA F . n 
F 2 60  PHE 60  60  60  PHE PHE F . n 
F 2 61  ARG 61  61  61  ARG ARG F . n 
F 2 62  ALA 62  62  62  ALA ALA F . n 
F 2 63  HIS 63  63  63  HIS HIS F . n 
F 2 64  ALA 64  64  64  ALA ALA F . n 
F 2 65  THR 65  65  65  THR THR F . n 
F 2 66  ARG 66  66  66  ARG ARG F . n 
F 2 67  VAL 67  67  67  VAL VAL F . n 
F 2 68  LEU 68  68  68  LEU LEU F . n 
F 2 69  GLY 69  69  69  GLY GLY F . n 
F 2 70  GLY 70  70  70  GLY GLY F . n 
F 2 71  LEU 71  71  71  LEU LEU F . n 
F 2 72  ASP 72  72  72  ASP ASP F . n 
F 2 73  MET 73  73  73  MET MET F . n 
F 2 74  CYS 74  74  74  CYS CYS F . n 
F 2 75  VAL 75  75  75  VAL VAL F . n 
F 2 76  ALA 76  76  76  ALA ALA F . n 
F 2 77  LEU 77  77  77  LEU LEU F . n 
F 2 78  LEU 78  78  78  LEU LEU F . n 
F 2 79  ASP 79  79  79  ASP ASP F . n 
F 2 80  ASP 80  80  80  ASP ASP F . n 
F 2 81  GLU 81  81  81  GLU GLU F . n 
F 2 82  SER 82  82  82  SER SER F . n 
F 2 83  VAL 83  83  83  VAL VAL F . n 
F 2 84  LEU 84  84  84  LEU LEU F . n 
F 2 85  ASN 85  85  85  ASN ASN F . n 
F 2 86  THR 86  86  86  THR THR F . n 
F 2 87  GLN 87  87  87  GLN GLN F . n 
F 2 88  LEU 88  88  88  LEU LEU F . n 
F 2 89  ALA 89  89  89  ALA ALA F . n 
F 2 90  HIS 90  90  90  HIS HIS F . n 
F 2 91  LEU 91  91  91  LEU LEU F . n 
F 2 92  ALA 92  92  92  ALA ALA F . n 
F 2 93  SER 93  93  93  SER SER F . n 
F 2 94  GLN 94  94  94  GLN GLN F . n 
F 2 95  HIS 95  95  95  HIS HIS F . n 
F 2 96  SER 96  96  96  SER SER F . n 
F 2 97  SER 97  97  97  SER SER F . n 
F 2 98  ARG 98  98  98  ARG ARG F . n 
F 2 99  GLY 99  99  99  GLY GLY F . n 
F 2 100 VAL 100 100 100 VAL VAL F . n 
F 2 101 SER 101 101 101 SER SER F . n 
F 2 102 ALA 102 102 102 ALA ALA F . n 
F 2 103 GLU 103 103 103 GLU GLU F . n 
F 2 104 GLN 104 104 104 GLN GLN F . n 
F 2 105 TYR 105 105 105 TYR TYR F . n 
F 2 106 ASN 106 106 106 ASN ASN F . n 
F 2 107 VAL 107 107 107 VAL VAL F . n 
F 2 108 VAL 108 108 108 VAL VAL F . n 
F 2 109 GLU 109 109 109 GLU GLU F . n 
F 2 110 HIS 110 110 110 HIS HIS F . n 
F 2 111 ALA 111 111 111 ALA ALA F . n 
F 2 112 VAL 112 112 112 VAL VAL F . n 
F 2 113 MET 113 113 113 MET MET F . n 
F 2 114 MET 114 114 114 MET MET F . n 
F 2 115 GLY 115 115 115 GLY GLY F . n 
F 2 116 VAL 116 116 116 VAL VAL F . n 
F 2 117 GLU 117 117 117 GLU GLU F . n 
F 2 118 HIS 118 118 118 HIS HIS F . n 
F 2 119 GLU 119 119 119 GLU GLU F . n 
F 2 120 ILE 120 120 120 ILE ILE F . n 
F 2 121 GLY 121 121 121 GLY GLY F . n 
F 2 122 GLN 122 122 122 GLN GLN F . n 
F 2 123 ASN 123 123 123 ASN ASN F . n 
F 2 124 VAL 124 124 124 VAL VAL F . n 
F 2 125 PHE 125 125 125 PHE PHE F . n 
F 2 126 ASP 126 126 126 ASP ASP F . n 
F 2 127 LYS 127 127 127 LYS LYS F . n 
F 2 128 ASP 128 128 128 ASP ASP F . n 
F 2 129 ALA 129 129 129 ALA ALA F . n 
F 2 130 TRP 130 130 130 TRP TRP F . n 
F 2 131 GLN 131 131 131 GLN GLN F . n 
F 2 132 ALA 132 132 132 ALA ALA F . n 
F 2 133 CYS 133 133 133 CYS CYS F . n 
F 2 134 LEU 134 134 134 LEU LEU F . n 
F 2 135 ASP 135 135 135 ASP ASP F . n 
F 2 136 VAL 136 136 136 VAL VAL F . n 
F 2 137 ILE 137 137 137 ILE ILE F . n 
F 2 138 THR 138 138 138 THR THR F . n 
F 2 139 SER 139 139 139 SER SER F . n 
F 2 140 GLY 140 140 140 GLY GLY F . n 
F 2 141 ILE 141 141 141 ILE ILE F . n 
F 2 142 GLN 142 142 142 GLN GLN F . n 
F 2 143 GLY 143 143 143 GLY GLY F . n 
F 2 144 ASN 144 144 144 ASN ASN F . n 
G 3 1   SER 1   1   1   SER SER G . n 
G 3 2   SER 2   2   2   SER SER G . n 
G 3 3   ASN 3   3   3   ASN ASN G . n 
G 3 4   SER 4   4   4   SER SER G . n 
G 3 5   CYS 5   5   5   CYS CYS G . n 
G 3 6   THR 6   6   6   THR THR G . n 
G 3 7   THR 7   7   7   THR THR G . n 
G 3 8   GLU 8   8   8   GLU GLU G . n 
G 3 9   ASP 9   9   9   ASP ASP G . n 
G 3 10  ARG 10  10  10  ARG ARG G . n 
G 3 11  ARG 11  11  11  ARG ARG G . n 
G 3 12  GLU 12  12  12  GLU GLU G . n 
G 3 13  MET 13  13  13  MET MET G . n 
G 3 14  GLN 14  14  14  GLN GLN G . n 
G 3 15  LEU 15  15  15  LEU LEU G . n 
G 3 16  MET 16  16  16  MET MET G . n 
G 3 17  TRP 17  17  17  TRP TRP G . n 
G 3 18  ALA 18  18  18  ALA ALA G . n 
G 3 19  ASN 19  19  19  ASN ASN G . n 
G 3 20  VAL 20  20  20  VAL VAL G . n 
G 3 21  TRP 21  21  21  TRP TRP G . n 
G 3 22  SER 22  22  22  SER SER G . n 
G 3 23  ALA 23  23  23  ALA ALA G . n 
G 3 24  GLN 24  24  24  GLN GLN G . n 
G 3 25  PHE 25  25  25  PHE PHE G . n 
G 3 26  THR 26  26  26  THR THR G . n 
G 3 27  GLY 27  27  27  GLY GLY G . n 
G 3 28  ARG 28  28  28  ARG ARG G . n 
G 3 29  ARG 29  29  29  ARG ARG G . n 
G 3 30  LEU 30  30  30  LEU LEU G . n 
G 3 31  ALA 31  31  31  ALA ALA G . n 
G 3 32  ILE 32  32  32  ILE ILE G . n 
G 3 33  ALA 33  33  33  ALA ALA G . n 
G 3 34  GLN 34  34  34  GLN GLN G . n 
G 3 35  ALA 35  35  35  ALA ALA G . n 
G 3 36  VAL 36  36  36  VAL VAL G . n 
G 3 37  PHE 37  37  37  PHE PHE G . n 
G 3 38  LYS 38  38  38  LYS LYS G . n 
G 3 39  ASP 39  39  39  ASP ASP G . n 
G 3 40  LEU 40  40  40  LEU LEU G . n 
G 3 41  PHE 41  41  41  PHE PHE G . n 
G 3 42  ALA 42  42  42  ALA ALA G . n 
G 3 43  HIS 43  43  43  HIS HIS G . n 
G 3 44  VAL 44  44  44  VAL VAL G . n 
G 3 45  PRO 45  45  45  PRO PRO G . n 
G 3 46  ASP 46  46  46  ASP ASP G . n 
G 3 47  ALA 47  47  47  ALA ALA G . n 
G 3 48  VAL 48  48  48  VAL VAL G . n 
G 3 49  GLY 49  49  49  GLY GLY G . n 
G 3 50  LEU 50  50  50  LEU LEU G . n 
G 3 51  PHE 51  51  51  PHE PHE G . n 
G 3 52  ASP 52  52  52  ASP ASP G . n 
G 3 53  ARG 53  53  53  ARG ARG G . n 
G 3 54  VAL 54  54  54  VAL VAL G . n 
G 3 55  HIS 55  55  55  HIS HIS G . n 
G 3 56  GLY 56  56  56  GLY GLY G . n 
G 3 57  THR 57  57  57  THR THR G . n 
G 3 58  GLU 58  58  58  GLU GLU G . n 
G 3 59  ILE 59  59  59  ILE ILE G . n 
G 3 60  ASP 60  60  60  ASP ASP G . n 
G 3 61  SER 61  61  61  SER SER G . n 
G 3 62  SER 62  62  62  SER SER G . n 
G 3 63  GLU 63  63  63  GLU GLU G . n 
G 3 64  PHE 64  64  64  PHE PHE G . n 
G 3 65  LYS 65  65  65  LYS LYS G . n 
G 3 66  ALA 66  66  66  ALA ALA G . n 
G 3 67  HIS 67  67  67  HIS HIS G . n 
G 3 68  CYS 68  68  68  CYS CYS G . n 
G 3 69  ILE 69  69  69  ILE ILE G . n 
G 3 70  ARG 70  70  70  ARG ARG G . n 
G 3 71  VAL 71  71  71  VAL VAL G . n 
G 3 72  VAL 72  72  72  VAL VAL G . n 
G 3 73  ASN 73  73  73  ASN ASN G . n 
G 3 74  GLY 74  74  74  GLY GLY G . n 
G 3 75  LEU 75  75  75  LEU LEU G . n 
G 3 76  ASP 76  76  76  ASP ASP G . n 
G 3 77  SER 77  77  77  SER SER G . n 
G 3 78  ALA 78  78  78  ALA ALA G . n 
G 3 79  ILE 79  79  79  ILE ILE G . n 
G 3 80  GLY 80  80  80  GLY GLY G . n 
G 3 81  LEU 81  81  81  LEU LEU G . n 
G 3 82  LEU 82  82  82  LEU LEU G . n 
G 3 83  SER 83  83  83  SER SER G . n 
G 3 84  ASP 84  84  84  ASP ASP G . n 
G 3 85  PRO 85  85  85  PRO PRO G . n 
G 3 86  SER 86  86  86  SER SER G . n 
G 3 87  THR 87  87  87  THR THR G . n 
G 3 88  LEU 88  88  88  LEU LEU G . n 
G 3 89  ASN 89  89  89  ASN ASN G . n 
G 3 90  GLU 90  90  90  GLU GLU G . n 
G 3 91  GLN 91  91  91  GLN GLN G . n 
G 3 92  LEU 92  92  92  LEU LEU G . n 
G 3 93  SER 93  93  93  SER SER G . n 
G 3 94  HIS 94  94  94  HIS HIS G . n 
G 3 95  LEU 95  95  95  LEU LEU G . n 
G 3 96  ALA 96  96  96  ALA ALA G . n 
G 3 97  THR 97  97  97  THR THR G . n 
G 3 98  GLN 98  98  98  GLN GLN G . n 
G 3 99  HIS 99  99  99  HIS HIS G . n 
G 3 100 GLN 100 100 100 GLN GLN G . n 
G 3 101 GLU 101 101 101 GLU GLU G . n 
G 3 102 ARG 102 102 102 ARG ARG G . n 
G 3 103 ALA 103 103 103 ALA ALA G . n 
G 3 104 GLY 104 104 104 GLY GLY G . n 
G 3 105 VAL 105 105 105 VAL VAL G . n 
G 3 106 THR 106 106 106 THR THR G . n 
G 3 107 LYS 107 107 107 LYS LYS G . n 
G 3 108 GLY 108 108 108 GLY GLY G . n 
G 3 109 GLY 109 109 109 GLY GLY G . n 
G 3 110 PHE 110 110 110 PHE PHE G . n 
G 3 111 SER 111 111 111 SER SER G . n 
G 3 112 ALA 112 112 112 ALA ALA G . n 
G 3 113 ILE 113 113 113 ILE ILE G . n 
G 3 114 ALA 114 114 114 ALA ALA G . n 
G 3 115 GLN 115 115 115 GLN GLN G . n 
G 3 116 SER 116 116 116 SER SER G . n 
G 3 117 PHE 117 117 117 PHE PHE G . n 
G 3 118 LEU 118 118 118 LEU LEU G . n 
G 3 119 ARG 119 119 119 ARG ARG G . n 
G 3 120 VAL 120 120 120 VAL VAL G . n 
G 3 121 MET 121 121 121 MET MET G . n 
G 3 122 PRO 122 122 122 PRO PRO G . n 
G 3 123 GLN 123 123 123 GLN GLN G . n 
G 3 124 VAL 124 124 124 VAL VAL G . n 
G 3 125 ALA 125 125 125 ALA ALA G . n 
G 3 126 SER 126 126 126 SER SER G . n 
G 3 127 CYS 127 127 127 CYS CYS G . n 
G 3 128 PHE 128 128 128 PHE PHE G . n 
G 3 129 ASN 129 129 129 ASN ASN G . n 
G 3 130 PRO 130 130 130 PRO PRO G . n 
G 3 131 ASP 131 131 131 ASP ASP G . n 
G 3 132 ALA 132 132 132 ALA ALA G . n 
G 3 133 TRP 133 133 133 TRP TRP G . n 
G 3 134 SER 134 134 134 SER SER G . n 
G 3 135 ARG 135 135 135 ARG ARG G . n 
G 3 136 CYS 136 136 136 CYS CYS G . n 
G 3 137 PHE 137 137 137 PHE PHE G . n 
G 3 138 ASN 138 138 138 ASN ASN G . n 
G 3 139 ARG 139 139 139 ARG ARG G . n 
G 3 140 ILE 140 140 140 ILE ILE G . n 
G 3 141 THR 141 141 141 THR THR G . n 
G 3 142 ASN 142 142 142 ASN ASN G . n 
G 3 143 GLY 143 143 143 GLY GLY G . n 
G 3 144 MET 144 144 144 MET MET G . n 
G 3 145 THR 145 145 145 THR THR G . n 
G 3 146 GLU 146 146 146 GLU GLU G . n 
G 3 147 GLY 147 147 147 GLY GLY G . n 
G 3 148 LEU 148 148 148 LEU LEU G . n 
G 3 149 ALA 149 149 149 ALA ALA G . n 
G 3 150 GLU 150 150 150 GLU GLU G . n 
H 4 1   SER 1   1   ?   ?   ?   H . n 
H 4 2   GLU 2   2   2   GLU GLU H . n 
H 4 3   PHE 3   3   3   PHE PHE H . n 
H 4 4   CYS 4   4   4   CYS CYS H . n 
H 4 5   SER 5   5   5   SER SER H . n 
H 4 6   GLU 6   6   6   GLU GLU H . n 
H 4 7   ALA 7   7   7   ALA ALA H . n 
H 4 8   ASP 8   8   8   ASP ASP H . n 
H 4 9   ALA 9   9   9   ALA ALA H . n 
H 4 10  THR 10  10  10  THR THR H . n 
H 4 11  ILE 11  11  11  ILE ILE H . n 
H 4 12  VAL 12  12  12  VAL VAL H . n 
H 4 13  ILE 13  13  13  ILE ILE H . n 
H 4 14  LYS 14  14  14  LYS LYS H . n 
H 4 15  GLN 15  15  15  GLN GLN H . n 
H 4 16  TRP 16  16  16  TRP TRP H . n 
H 4 17  ASN 17  17  17  ASN ASN H . n 
H 4 18  GLN 18  18  18  GLN GLN H . n 
H 4 19  ILE 19  19  19  ILE ILE H . n 
H 4 20  TYR 20  20  20  TYR TYR H . n 
H 4 21  ASN 21  21  21  ASN ASN H . n 
H 4 22  ALA 22  22  22  ALA ALA H . n 
H 4 23  GLY 23  23  23  GLY GLY H . n 
H 4 24  ILE 24  24  24  ILE ILE H . n 
H 4 25  GLY 25  25  25  GLY GLY H . n 
H 4 26  ALA 26  26  26  ALA ALA H . n 
H 4 27  LYS 27  27  27  LYS LYS H . n 
H 4 28  SER 28  28  28  SER SER H . n 
H 4 29  ARG 29  29  29  ARG ARG H . n 
H 4 30  TRP 30  30  30  TRP TRP H . n 
H 4 31  THR 31  31  31  THR THR H . n 
H 4 32  MET 32  32  32  MET MET H . n 
H 4 33  GLY 33  33  33  GLY GLY H . n 
H 4 34  ASN 34  34  34  ASN ASN H . n 
H 4 35  GLU 35  35  35  GLU GLU H . n 
H 4 36  ILE 36  36  36  ILE ILE H . n 
H 4 37  PHE 37  37  37  PHE PHE H . n 
H 4 38  SER 38  38  38  SER SER H . n 
H 4 39  SER 39  39  39  SER SER H . n 
H 4 40  LEU 40  40  40  LEU LEU H . n 
H 4 41  PHE 41  41  41  PHE PHE H . n 
H 4 42  LYS 42  42  42  LYS LYS H . n 
H 4 43  LEU 43  43  43  LEU LEU H . n 
H 4 44  LYS 44  44  44  LYS LYS H . n 
H 4 45  PRO 45  45  45  PRO PRO H . n 
H 4 46  GLU 46  46  46  GLU GLU H . n 
H 4 47  SER 47  47  47  SER SER H . n 
H 4 48  GLU 48  48  48  GLU GLU H . n 
H 4 49  VAL 49  49  49  VAL VAL H . n 
H 4 50  LEU 50  50  50  LEU LEU H . n 
H 4 51  PHE 51  51  51  PHE PHE H . n 
H 4 52  ASN 52  52  52  ASN ASN H . n 
H 4 53  ASN 53  53  53  ASN ASN H . n 
H 4 54  VAL 54  54  54  VAL VAL H . n 
H 4 55  ASN 55  55  55  ASN ASN H . n 
H 4 56  VAL 56  56  56  VAL VAL H . n 
H 4 57  ALA 57  57  57  ALA ALA H . n 
H 4 58  ASN 58  58  58  ASN ASN H . n 
H 4 59  MET 59  59  59  MET MET H . n 
H 4 60  SER 60  60  60  SER SER H . n 
H 4 61  SER 61  61  61  SER SER H . n 
H 4 62  GLY 62  62  62  GLY GLY H . n 
H 4 63  ALA 63  63  63  ALA ALA H . n 
H 4 64  PHE 64  64  64  PHE PHE H . n 
H 4 65  HIS 65  65  65  HIS HIS H . n 
H 4 66  ALA 66  66  66  ALA ALA H . n 
H 4 67  HIS 67  67  67  HIS HIS H . n 
H 4 68  THR 68  68  68  THR THR H . n 
H 4 69  VAL 69  69  69  VAL VAL H . n 
H 4 70  ARG 70  70  70  ARG ARG H . n 
H 4 71  VAL 71  71  71  VAL VAL H . n 
H 4 72  LEU 72  72  72  LEU LEU H . n 
H 4 73  SER 73  73  73  SER SER H . n 
H 4 74  GLY 74  74  74  GLY GLY H . n 
H 4 75  LEU 75  75  75  LEU LEU H . n 
H 4 76  ASP 76  76  76  ASP ASP H . n 
H 4 77  MET 77  77  77  MET MET H . n 
H 4 78  GLY 78  78  78  GLY GLY H . n 
H 4 79  ILE 79  79  79  ILE ILE H . n 
H 4 80  ASN 80  80  80  ASN ASN H . n 
H 4 81  TYR 81  81  81  TYR TYR H . n 
H 4 82  LEU 82  82  82  LEU LEU H . n 
H 4 83  ASN 83  83  83  ASN ASN H . n 
H 4 84  ASP 84  84  84  ASP ASP H . n 
H 4 85  ALA 85  85  85  ALA ALA H . n 
H 4 86  GLY 86  86  86  GLY GLY H . n 
H 4 87  THR 87  87  87  THR THR H . n 
H 4 88  LEU 88  88  88  LEU LEU H . n 
H 4 89  THR 89  89  89  THR THR H . n 
H 4 90  SER 90  90  90  SER SER H . n 
H 4 91  LEU 91  91  91  LEU LEU H . n 
H 4 92  THR 92  92  92  THR THR H . n 
H 4 93  ALA 93  93  93  ALA ALA H . n 
H 4 94  HIS 94  94  94  HIS HIS H . n 
H 4 95  LEU 95  95  95  LEU LEU H . n 
H 4 96  ALA 96  96  96  ALA ALA H . n 
H 4 97  ALA 97  97  97  ALA ALA H . n 
H 4 98  GLN 98  98  98  GLN GLN H . n 
H 4 99  HIS 99  99  99  HIS HIS H . n 
H 4 100 VAL 100 100 100 VAL VAL H . n 
H 4 101 ALA 101 101 101 ALA ALA H . n 
H 4 102 ARG 102 102 102 ARG ARG H . n 
H 4 103 THR 103 103 103 THR THR H . n 
H 4 104 GLY 104 104 104 GLY GLY H . n 
H 4 105 LEU 105 105 105 LEU LEU H . n 
H 4 106 LYS 106 106 106 LYS LYS H . n 
H 4 107 ALA 107 107 107 ALA ALA H . n 
H 4 108 VAL 108 108 108 VAL VAL H . n 
H 4 109 TYR 109 109 109 TYR TYR H . n 
H 4 110 PHE 110 110 110 PHE PHE H . n 
H 4 111 ASP 111 111 111 ASP ASP H . n 
H 4 112 ALA 112 112 112 ALA ALA H . n 
H 4 113 MET 113 113 113 MET MET H . n 
H 4 114 GLY 114 114 114 GLY GLY H . n 
H 4 115 LYS 115 115 115 LYS LYS H . n 
H 4 116 VAL 116 116 116 VAL VAL H . n 
H 4 117 LEU 117 117 117 LEU LEU H . n 
H 4 118 MET 118 118 118 MET MET H . n 
H 4 119 THR 119 119 119 THR THR H . n 
H 4 120 VAL 120 120 120 VAL VAL H . n 
H 4 121 LEU 121 121 121 LEU LEU H . n 
H 4 122 PRO 122 122 122 PRO PRO H . n 
H 4 123 SER 123 123 123 SER SER H . n 
H 4 124 LEU 124 124 124 LEU LEU H . n 
H 4 125 ILE 125 125 125 ILE ILE H . n 
H 4 126 ASP 126 126 126 ASP ASP H . n 
H 4 127 ASN 127 127 127 ASN ASN H . n 
H 4 128 PHE 128 128 128 PHE PHE H . n 
H 4 129 ASN 129 129 129 ASN ASN H . n 
H 4 130 PRO 130 130 130 PRO PRO H . n 
H 4 131 ASP 131 131 131 ASP ASP H . n 
H 4 132 ALA 132 132 132 ALA ALA H . n 
H 4 133 TRP 133 133 133 TRP TRP H . n 
H 4 134 ARG 134 134 134 ARG ARG H . n 
H 4 135 ASN 135 135 135 ASN ASN H . n 
H 4 136 CYS 136 136 136 CYS CYS H . n 
H 4 137 LEU 137 137 137 LEU LEU H . n 
H 4 138 LEU 138 138 138 LEU LEU H . n 
H 4 139 PRO 139 139 139 PRO PRO H . n 
H 4 140 LEU 140 140 140 LEU LEU H . n 
H 4 141 LYS 141 141 141 LYS LYS H . n 
H 4 142 ASN 142 142 142 ASN ASN H . n 
H 4 143 ALA 143 143 143 ALA ALA H . n 
H 4 144 ILE 144 144 144 ILE ILE H . n 
H 4 145 ALA 145 145 145 ALA ALA H . n 
H 4 146 LYS 146 146 146 LYS LYS H . n 
H 4 147 GLY 147 147 147 GLY GLY H . n 
H 4 148 LEU 148 148 148 LEU LEU H . n 
H 4 149 PRO 149 149 149 PRO PRO H . n 
# 
loop_
_pdbx_struct_mod_residue.id 
_pdbx_struct_mod_residue.label_asym_id 
_pdbx_struct_mod_residue.label_comp_id 
_pdbx_struct_mod_residue.label_seq_id 
_pdbx_struct_mod_residue.auth_asym_id 
_pdbx_struct_mod_residue.auth_comp_id 
_pdbx_struct_mod_residue.auth_seq_id 
_pdbx_struct_mod_residue.PDB_ins_code 
_pdbx_struct_mod_residue.parent_comp_id 
_pdbx_struct_mod_residue.details 
1 D ASN 58 D ASN 58 ? ASN 'GLYCOSYLATION SITE' 
2 H ASN 58 H ASN 58 ? ASN 'GLYCOSYLATION SITE' 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   24-meric 
_pdbx_struct_assembly.oligomeric_count     24 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2,3 
_pdbx_struct_assembly_gen.asym_id_list      
A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S,T,U,V,W,X,Y,Z,AA,BA,CA,DA,EA,FA,GA,HA,IA,JA,KA,LA,MA,NA,OA,PA,QA,RA,SA,TA,UA,VA,WA,XA 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 54890  ? 
1 MORE         -196   ? 
1 'SSA (A^2)'  136820 ? 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z         1.0000000000  0.0000000000  0.0000000000 0.0000000000   0.0000000000  
1.0000000000  0.0000000000 0.0000000000  0.0000000000 0.0000000000 1.0000000000 0.0000000000 
2 'crystal symmetry operation' 2_655 -y+1,x-y,z    -0.5000000000 -0.8660254038 0.0000000000 108.9440000000 0.8660254038  
-0.5000000000 0.0000000000 0.0000000000  0.0000000000 0.0000000000 1.0000000000 0.0000000000 
3 'crystal symmetry operation' 3_665 -x+y+1,-x+1,z -0.5000000000 0.8660254038  0.0000000000 54.4720000000  -0.8660254038 
-0.5000000000 0.0000000000 94.3482715899 0.0000000000 0.0000000000 1.0000000000 0.0000000000 
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    A 
_pdbx_struct_special_symmetry.auth_comp_id    CA 
_pdbx_struct_special_symmetry.auth_seq_id     203 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   K 
_pdbx_struct_special_symmetry.label_comp_id   CA 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1   O1  ? AA OXY .   ? E OXY 201 ? 1_555 FE ? Z  HEM . ? E HEM 200 ? 1_555 NA  ? Z  HEM .   ? E HEM 200 ? 1_555 97.0  ? 
2   O1  ? AA OXY .   ? E OXY 201 ? 1_555 FE ? Z  HEM . ? E HEM 200 ? 1_555 NB  ? Z  HEM .   ? E HEM 200 ? 1_555 90.0  ? 
3   NA  ? Z  HEM .   ? E HEM 200 ? 1_555 FE ? Z  HEM . ? E HEM 200 ? 1_555 NB  ? Z  HEM .   ? E HEM 200 ? 1_555 88.6  ? 
4   O1  ? AA OXY .   ? E OXY 201 ? 1_555 FE ? Z  HEM . ? E HEM 200 ? 1_555 NC  ? Z  HEM .   ? E HEM 200 ? 1_555 81.4  ? 
5   NA  ? Z  HEM .   ? E HEM 200 ? 1_555 FE ? Z  HEM . ? E HEM 200 ? 1_555 NC  ? Z  HEM .   ? E HEM 200 ? 1_555 178.3 ? 
6   NB  ? Z  HEM .   ? E HEM 200 ? 1_555 FE ? Z  HEM . ? E HEM 200 ? 1_555 NC  ? Z  HEM .   ? E HEM 200 ? 1_555 90.9  ? 
7   O1  ? AA OXY .   ? E OXY 201 ? 1_555 FE ? Z  HEM . ? E HEM 200 ? 1_555 ND  ? Z  HEM .   ? E HEM 200 ? 1_555 89.2  ? 
8   NA  ? Z  HEM .   ? E HEM 200 ? 1_555 FE ? Z  HEM . ? E HEM 200 ? 1_555 ND  ? Z  HEM .   ? E HEM 200 ? 1_555 90.4  ? 
9   NB  ? Z  HEM .   ? E HEM 200 ? 1_555 FE ? Z  HEM . ? E HEM 200 ? 1_555 ND  ? Z  HEM .   ? E HEM 200 ? 1_555 178.6 ? 
10  NC  ? Z  HEM .   ? E HEM 200 ? 1_555 FE ? Z  HEM . ? E HEM 200 ? 1_555 ND  ? Z  HEM .   ? E HEM 200 ? 1_555 90.0  ? 
11  O1  ? AA OXY .   ? E OXY 201 ? 1_555 FE ? Z  HEM . ? E HEM 200 ? 1_555 NE2 ? E  HIS 94  ? E HIS 94  ? 1_555 177.7 ? 
12  NA  ? Z  HEM .   ? E HEM 200 ? 1_555 FE ? Z  HEM . ? E HEM 200 ? 1_555 NE2 ? E  HIS 94  ? E HIS 94  ? 1_555 84.8  ? 
13  NB  ? Z  HEM .   ? E HEM 200 ? 1_555 FE ? Z  HEM . ? E HEM 200 ? 1_555 NE2 ? E  HIS 94  ? E HIS 94  ? 1_555 91.5  ? 
14  NC  ? Z  HEM .   ? E HEM 200 ? 1_555 FE ? Z  HEM . ? E HEM 200 ? 1_555 NE2 ? E  HIS 94  ? E HIS 94  ? 1_555 96.8  ? 
15  ND  ? Z  HEM .   ? E HEM 200 ? 1_555 FE ? Z  HEM . ? E HEM 200 ? 1_555 NE2 ? E  HIS 94  ? E HIS 94  ? 1_555 89.3  ? 
16  O1  ? S  OXY .   ? D OXY 202 ? 1_555 FE ? R  HEM . ? D HEM 201 ? 1_555 NA  ? R  HEM .   ? D HEM 201 ? 1_555 87.7  ? 
17  O1  ? S  OXY .   ? D OXY 202 ? 1_555 FE ? R  HEM . ? D HEM 201 ? 1_555 NB  ? R  HEM .   ? D HEM 201 ? 1_555 87.4  ? 
18  NA  ? R  HEM .   ? D HEM 201 ? 1_555 FE ? R  HEM . ? D HEM 201 ? 1_555 NB  ? R  HEM .   ? D HEM 201 ? 1_555 88.8  ? 
19  O1  ? S  OXY .   ? D OXY 202 ? 1_555 FE ? R  HEM . ? D HEM 201 ? 1_555 NC  ? R  HEM .   ? D HEM 201 ? 1_555 91.3  ? 
20  NA  ? R  HEM .   ? D HEM 201 ? 1_555 FE ? R  HEM . ? D HEM 201 ? 1_555 NC  ? R  HEM .   ? D HEM 201 ? 1_555 178.9 ? 
21  NB  ? R  HEM .   ? D HEM 201 ? 1_555 FE ? R  HEM . ? D HEM 201 ? 1_555 NC  ? R  HEM .   ? D HEM 201 ? 1_555 91.6  ? 
22  O1  ? S  OXY .   ? D OXY 202 ? 1_555 FE ? R  HEM . ? D HEM 201 ? 1_555 ND  ? R  HEM .   ? D HEM 201 ? 1_555 90.8  ? 
23  NA  ? R  HEM .   ? D HEM 201 ? 1_555 FE ? R  HEM . ? D HEM 201 ? 1_555 ND  ? R  HEM .   ? D HEM 201 ? 1_555 89.8  ? 
24  NB  ? R  HEM .   ? D HEM 201 ? 1_555 FE ? R  HEM . ? D HEM 201 ? 1_555 ND  ? R  HEM .   ? D HEM 201 ? 1_555 177.8 ? 
25  NC  ? R  HEM .   ? D HEM 201 ? 1_555 FE ? R  HEM . ? D HEM 201 ? 1_555 ND  ? R  HEM .   ? D HEM 201 ? 1_555 89.8  ? 
26  O1  ? S  OXY .   ? D OXY 202 ? 1_555 FE ? R  HEM . ? D HEM 201 ? 1_555 NE2 ? D  HIS 99  ? D HIS 99  ? 1_555 179.0 ? 
27  NA  ? R  HEM .   ? D HEM 201 ? 1_555 FE ? R  HEM . ? D HEM 201 ? 1_555 NE2 ? D  HIS 99  ? D HIS 99  ? 1_555 93.0  ? 
28  NB  ? R  HEM .   ? D HEM 201 ? 1_555 FE ? R  HEM . ? D HEM 201 ? 1_555 NE2 ? D  HIS 99  ? D HIS 99  ? 1_555 91.8  ? 
29  NC  ? R  HEM .   ? D HEM 201 ? 1_555 FE ? R  HEM . ? D HEM 201 ? 1_555 NE2 ? D  HIS 99  ? D HIS 99  ? 1_555 88.1  ? 
30  ND  ? R  HEM .   ? D HEM 201 ? 1_555 FE ? R  HEM . ? D HEM 201 ? 1_555 NE2 ? D  HIS 99  ? D HIS 99  ? 1_555 90.0  ? 
31  O1  ? CA OXY .   ? F OXY 202 ? 1_555 FE ? BA HEM . ? F HEM 201 ? 1_555 NA  ? BA HEM .   ? F HEM 201 ? 1_555 90.9  ? 
32  O1  ? CA OXY .   ? F OXY 202 ? 1_555 FE ? BA HEM . ? F HEM 201 ? 1_555 NB  ? BA HEM .   ? F HEM 201 ? 1_555 97.8  ? 
33  NA  ? BA HEM .   ? F HEM 201 ? 1_555 FE ? BA HEM . ? F HEM 201 ? 1_555 NB  ? BA HEM .   ? F HEM 201 ? 1_555 88.6  ? 
34  O1  ? CA OXY .   ? F OXY 202 ? 1_555 FE ? BA HEM . ? F HEM 201 ? 1_555 NC  ? BA HEM .   ? F HEM 201 ? 1_555 88.3  ? 
35  NA  ? BA HEM .   ? F HEM 201 ? 1_555 FE ? BA HEM . ? F HEM 201 ? 1_555 NC  ? BA HEM .   ? F HEM 201 ? 1_555 179.1 ? 
36  NB  ? BA HEM .   ? F HEM 201 ? 1_555 FE ? BA HEM . ? F HEM 201 ? 1_555 NC  ? BA HEM .   ? F HEM 201 ? 1_555 91.3  ? 
37  O1  ? CA OXY .   ? F OXY 202 ? 1_555 FE ? BA HEM . ? F HEM 201 ? 1_555 ND  ? BA HEM .   ? F HEM 201 ? 1_555 82.5  ? 
38  NA  ? BA HEM .   ? F HEM 201 ? 1_555 FE ? BA HEM . ? F HEM 201 ? 1_555 ND  ? BA HEM .   ? F HEM 201 ? 1_555 89.9  ? 
39  NB  ? BA HEM .   ? F HEM 201 ? 1_555 FE ? BA HEM . ? F HEM 201 ? 1_555 ND  ? BA HEM .   ? F HEM 201 ? 1_555 178.5 ? 
40  NC  ? BA HEM .   ? F HEM 201 ? 1_555 FE ? BA HEM . ? F HEM 201 ? 1_555 ND  ? BA HEM .   ? F HEM 201 ? 1_555 90.2  ? 
41  O1  ? CA OXY .   ? F OXY 202 ? 1_555 FE ? BA HEM . ? F HEM 201 ? 1_555 NE2 ? F  HIS 95  ? F HIS 95  ? 1_555 178.1 ? 
42  NA  ? BA HEM .   ? F HEM 201 ? 1_555 FE ? BA HEM . ? F HEM 201 ? 1_555 NE2 ? F  HIS 95  ? F HIS 95  ? 1_555 90.1  ? 
43  NB  ? BA HEM .   ? F HEM 201 ? 1_555 FE ? BA HEM . ? F HEM 201 ? 1_555 NE2 ? F  HIS 95  ? F HIS 95  ? 1_555 83.9  ? 
44  NC  ? BA HEM .   ? F HEM 201 ? 1_555 FE ? BA HEM . ? F HEM 201 ? 1_555 NE2 ? F  HIS 95  ? F HIS 95  ? 1_555 90.8  ? 
45  ND  ? BA HEM .   ? F HEM 201 ? 1_555 FE ? BA HEM . ? F HEM 201 ? 1_555 NE2 ? F  HIS 95  ? F HIS 95  ? 1_555 95.8  ? 
46  O1  ? Q  OXY .   ? C OXY 201 ? 1_555 FE ? P  HEM . ? C HEM 200 ? 1_555 NA  ? P  HEM .   ? C HEM 200 ? 1_555 94.4  ? 
47  O1  ? Q  OXY .   ? C OXY 201 ? 1_555 FE ? P  HEM . ? C HEM 200 ? 1_555 NB  ? P  HEM .   ? C HEM 200 ? 1_555 95.2  ? 
48  NA  ? P  HEM .   ? C HEM 200 ? 1_555 FE ? P  HEM . ? C HEM 200 ? 1_555 NB  ? P  HEM .   ? C HEM 200 ? 1_555 88.7  ? 
49  O1  ? Q  OXY .   ? C OXY 201 ? 1_555 FE ? P  HEM . ? C HEM 200 ? 1_555 NC  ? P  HEM .   ? C HEM 200 ? 1_555 85.1  ? 
50  NA  ? P  HEM .   ? C HEM 200 ? 1_555 FE ? P  HEM . ? C HEM 200 ? 1_555 NC  ? P  HEM .   ? C HEM 200 ? 1_555 179.5 ? 
51  NB  ? P  HEM .   ? C HEM 200 ? 1_555 FE ? P  HEM . ? C HEM 200 ? 1_555 NC  ? P  HEM .   ? C HEM 200 ? 1_555 91.1  ? 
52  O1  ? Q  OXY .   ? C OXY 201 ? 1_555 FE ? P  HEM . ? C HEM 200 ? 1_555 ND  ? P  HEM .   ? C HEM 200 ? 1_555 83.7  ? 
53  NA  ? P  HEM .   ? C HEM 200 ? 1_555 FE ? P  HEM . ? C HEM 200 ? 1_555 ND  ? P  HEM .   ? C HEM 200 ? 1_555 90.2  ? 
54  NB  ? P  HEM .   ? C HEM 200 ? 1_555 FE ? P  HEM . ? C HEM 200 ? 1_555 ND  ? P  HEM .   ? C HEM 200 ? 1_555 178.4 ? 
55  NC  ? P  HEM .   ? C HEM 200 ? 1_555 FE ? P  HEM . ? C HEM 200 ? 1_555 ND  ? P  HEM .   ? C HEM 200 ? 1_555 90.0  ? 
56  O1  ? Q  OXY .   ? C OXY 201 ? 1_555 FE ? P  HEM . ? C HEM 200 ? 1_555 NE2 ? C  HIS 99  ? C HIS 99  ? 1_555 179.8 ? 
57  NA  ? P  HEM .   ? C HEM 200 ? 1_555 FE ? P  HEM . ? C HEM 200 ? 1_555 NE2 ? C  HIS 99  ? C HIS 99  ? 1_555 85.7  ? 
58  NB  ? P  HEM .   ? C HEM 200 ? 1_555 FE ? P  HEM . ? C HEM 200 ? 1_555 NE2 ? C  HIS 99  ? C HIS 99  ? 1_555 84.9  ? 
59  NC  ? P  HEM .   ? C HEM 200 ? 1_555 FE ? P  HEM . ? C HEM 200 ? 1_555 NE2 ? C  HIS 99  ? C HIS 99  ? 1_555 94.7  ? 
60  ND  ? P  HEM .   ? C HEM 200 ? 1_555 FE ? P  HEM . ? C HEM 200 ? 1_555 NE2 ? C  HIS 99  ? C HIS 99  ? 1_555 96.1  ? 
61  O1  ? JA OXY .   ? H OXY 202 ? 1_555 FE ? IA HEM . ? H HEM 201 ? 1_555 NA  ? IA HEM .   ? H HEM 201 ? 1_555 89.5  ? 
62  O1  ? JA OXY .   ? H OXY 202 ? 1_555 FE ? IA HEM . ? H HEM 201 ? 1_555 NB  ? IA HEM .   ? H HEM 201 ? 1_555 91.5  ? 
63  NA  ? IA HEM .   ? H HEM 201 ? 1_555 FE ? IA HEM . ? H HEM 201 ? 1_555 NB  ? IA HEM .   ? H HEM 201 ? 1_555 88.3  ? 
64  O1  ? JA OXY .   ? H OXY 202 ? 1_555 FE ? IA HEM . ? H HEM 201 ? 1_555 NC  ? IA HEM .   ? H HEM 201 ? 1_555 89.5  ? 
65  NA  ? IA HEM .   ? H HEM 201 ? 1_555 FE ? IA HEM . ? H HEM 201 ? 1_555 NC  ? IA HEM .   ? H HEM 201 ? 1_555 178.7 ? 
66  NB  ? IA HEM .   ? H HEM 201 ? 1_555 FE ? IA HEM . ? H HEM 201 ? 1_555 NC  ? IA HEM .   ? H HEM 201 ? 1_555 90.8  ? 
67  O1  ? JA OXY .   ? H OXY 202 ? 1_555 FE ? IA HEM . ? H HEM 201 ? 1_555 ND  ? IA HEM .   ? H HEM 201 ? 1_555 87.7  ? 
68  NA  ? IA HEM .   ? H HEM 201 ? 1_555 FE ? IA HEM . ? H HEM 201 ? 1_555 ND  ? IA HEM .   ? H HEM 201 ? 1_555 90.8  ? 
69  NB  ? IA HEM .   ? H HEM 201 ? 1_555 FE ? IA HEM . ? H HEM 201 ? 1_555 ND  ? IA HEM .   ? H HEM 201 ? 1_555 178.8 ? 
70  NC  ? IA HEM .   ? H HEM 201 ? 1_555 FE ? IA HEM . ? H HEM 201 ? 1_555 ND  ? IA HEM .   ? H HEM 201 ? 1_555 90.0  ? 
71  O1  ? JA OXY .   ? H OXY 202 ? 1_555 FE ? IA HEM . ? H HEM 201 ? 1_555 NE2 ? H  HIS 99  ? H HIS 99  ? 1_555 178.3 ? 
72  NA  ? IA HEM .   ? H HEM 201 ? 1_555 FE ? IA HEM . ? H HEM 201 ? 1_555 NE2 ? H  HIS 99  ? H HIS 99  ? 1_555 92.1  ? 
73  NB  ? IA HEM .   ? H HEM 201 ? 1_555 FE ? IA HEM . ? H HEM 201 ? 1_555 NE2 ? H  HIS 99  ? H HIS 99  ? 1_555 89.0  ? 
74  NC  ? IA HEM .   ? H HEM 201 ? 1_555 FE ? IA HEM . ? H HEM 201 ? 1_555 NE2 ? H  HIS 99  ? H HIS 99  ? 1_555 88.9  ? 
75  ND  ? IA HEM .   ? H HEM 201 ? 1_555 FE ? IA HEM . ? H HEM 201 ? 1_555 NE2 ? H  HIS 99  ? H HIS 99  ? 1_555 91.8  ? 
76  O1  ? M  OXY .   ? B OXY 202 ? 1_555 FE ? L  HEM . ? B HEM 201 ? 1_555 NA  ? L  HEM .   ? B HEM 201 ? 1_555 96.2  ? 
77  O1  ? M  OXY .   ? B OXY 202 ? 1_555 FE ? L  HEM . ? B HEM 201 ? 1_555 NB  ? L  HEM .   ? B HEM 201 ? 1_555 94.6  ? 
78  NA  ? L  HEM .   ? B HEM 201 ? 1_555 FE ? L  HEM . ? B HEM 201 ? 1_555 NB  ? L  HEM .   ? B HEM 201 ? 1_555 88.1  ? 
79  O1  ? M  OXY .   ? B OXY 202 ? 1_555 FE ? L  HEM . ? B HEM 201 ? 1_555 NC  ? L  HEM .   ? B HEM 201 ? 1_555 83.5  ? 
80  NA  ? L  HEM .   ? B HEM 201 ? 1_555 FE ? L  HEM . ? B HEM 201 ? 1_555 NC  ? L  HEM .   ? B HEM 201 ? 1_555 179.3 ? 
81  NB  ? L  HEM .   ? B HEM 201 ? 1_555 FE ? L  HEM . ? B HEM 201 ? 1_555 NC  ? L  HEM .   ? B HEM 201 ? 1_555 91.3  ? 
82  O1  ? M  OXY .   ? B OXY 202 ? 1_555 FE ? L  HEM . ? B HEM 201 ? 1_555 ND  ? L  HEM .   ? B HEM 201 ? 1_555 85.8  ? 
83  NA  ? L  HEM .   ? B HEM 201 ? 1_555 FE ? L  HEM . ? B HEM 201 ? 1_555 ND  ? L  HEM .   ? B HEM 201 ? 1_555 90.6  ? 
84  NB  ? L  HEM .   ? B HEM 201 ? 1_555 FE ? L  HEM . ? B HEM 201 ? 1_555 ND  ? L  HEM .   ? B HEM 201 ? 1_555 178.6 ? 
85  NC  ? L  HEM .   ? B HEM 201 ? 1_555 FE ? L  HEM . ? B HEM 201 ? 1_555 ND  ? L  HEM .   ? B HEM 201 ? 1_555 90.0  ? 
86  O1  ? M  OXY .   ? B OXY 202 ? 1_555 FE ? L  HEM . ? B HEM 201 ? 1_555 NE2 ? B  HIS 95  ? B HIS 95  ? 1_555 177.9 ? 
87  NA  ? L  HEM .   ? B HEM 201 ? 1_555 FE ? L  HEM . ? B HEM 201 ? 1_555 NE2 ? B  HIS 95  ? B HIS 95  ? 1_555 85.5  ? 
88  NB  ? L  HEM .   ? B HEM 201 ? 1_555 FE ? L  HEM . ? B HEM 201 ? 1_555 NE2 ? B  HIS 95  ? B HIS 95  ? 1_555 86.7  ? 
89  NC  ? L  HEM .   ? B HEM 201 ? 1_555 FE ? L  HEM . ? B HEM 201 ? 1_555 NE2 ? B  HIS 95  ? B HIS 95  ? 1_555 94.9  ? 
90  ND  ? L  HEM .   ? B HEM 201 ? 1_555 FE ? L  HEM . ? B HEM 201 ? 1_555 NE2 ? B  HIS 95  ? B HIS 95  ? 1_555 93.0  ? 
91  O1  ? HA OXY .   ? G OXY 201 ? 1_555 FE ? GA HEM . ? G HEM 200 ? 1_555 NA  ? GA HEM .   ? G HEM 200 ? 1_555 89.3  ? 
92  O1  ? HA OXY .   ? G OXY 201 ? 1_555 FE ? GA HEM . ? G HEM 200 ? 1_555 NB  ? GA HEM .   ? G HEM 200 ? 1_555 97.3  ? 
93  NA  ? GA HEM .   ? G HEM 200 ? 1_555 FE ? GA HEM . ? G HEM 200 ? 1_555 NB  ? GA HEM .   ? G HEM 200 ? 1_555 88.4  ? 
94  O1  ? HA OXY .   ? G OXY 201 ? 1_555 FE ? GA HEM . ? G HEM 200 ? 1_555 NC  ? GA HEM .   ? G HEM 200 ? 1_555 90.2  ? 
95  NA  ? GA HEM .   ? G HEM 200 ? 1_555 FE ? GA HEM . ? G HEM 200 ? 1_555 NC  ? GA HEM .   ? G HEM 200 ? 1_555 179.6 ? 
96  NB  ? GA HEM .   ? G HEM 200 ? 1_555 FE ? GA HEM . ? G HEM 200 ? 1_555 NC  ? GA HEM .   ? G HEM 200 ? 1_555 91.6  ? 
97  O1  ? HA OXY .   ? G OXY 201 ? 1_555 FE ? GA HEM . ? G HEM 200 ? 1_555 ND  ? GA HEM .   ? G HEM 200 ? 1_555 81.4  ? 
98  NA  ? GA HEM .   ? G HEM 200 ? 1_555 FE ? GA HEM . ? G HEM 200 ? 1_555 ND  ? GA HEM .   ? G HEM 200 ? 1_555 90.1  ? 
99  NB  ? GA HEM .   ? G HEM 200 ? 1_555 FE ? GA HEM . ? G HEM 200 ? 1_555 ND  ? GA HEM .   ? G HEM 200 ? 1_555 178.1 ? 
100 NC  ? GA HEM .   ? G HEM 200 ? 1_555 FE ? GA HEM . ? G HEM 200 ? 1_555 ND  ? GA HEM .   ? G HEM 200 ? 1_555 89.8  ? 
101 O1  ? HA OXY .   ? G OXY 201 ? 1_555 FE ? GA HEM . ? G HEM 200 ? 1_555 NE2 ? G  HIS 99  ? G HIS 99  ? 1_555 178.5 ? 
102 NA  ? GA HEM .   ? G HEM 200 ? 1_555 FE ? GA HEM . ? G HEM 200 ? 1_555 NE2 ? G  HIS 99  ? G HIS 99  ? 1_555 90.2  ? 
103 NB  ? GA HEM .   ? G HEM 200 ? 1_555 FE ? GA HEM . ? G HEM 200 ? 1_555 NE2 ? G  HIS 99  ? G HIS 99  ? 1_555 84.1  ? 
104 NC  ? GA HEM .   ? G HEM 200 ? 1_555 FE ? GA HEM . ? G HEM 200 ? 1_555 NE2 ? G  HIS 99  ? G HIS 99  ? 1_555 90.2  ? 
105 ND  ? GA HEM .   ? G HEM 200 ? 1_555 FE ? GA HEM . ? G HEM 200 ? 1_555 NE2 ? G  HIS 99  ? G HIS 99  ? 1_555 97.2  ? 
106 O1  ? J  OXY .   ? A OXY 202 ? 1_555 FE ? I  HEM . ? A HEM 201 ? 1_555 NA  ? I  HEM .   ? A HEM 201 ? 1_555 92.5  ? 
107 O1  ? J  OXY .   ? A OXY 202 ? 1_555 FE ? I  HEM . ? A HEM 201 ? 1_555 NB  ? I  HEM .   ? A HEM 201 ? 1_555 95.0  ? 
108 NA  ? I  HEM .   ? A HEM 201 ? 1_555 FE ? I  HEM . ? A HEM 201 ? 1_555 NB  ? I  HEM .   ? A HEM 201 ? 1_555 89.4  ? 
109 O1  ? J  OXY .   ? A OXY 202 ? 1_555 FE ? I  HEM . ? A HEM 201 ? 1_555 NC  ? I  HEM .   ? A HEM 201 ? 1_555 86.5  ? 
110 NA  ? I  HEM .   ? A HEM 201 ? 1_555 FE ? I  HEM . ? A HEM 201 ? 1_555 NC  ? I  HEM .   ? A HEM 201 ? 1_555 179.0 ? 
111 NB  ? I  HEM .   ? A HEM 201 ? 1_555 FE ? I  HEM . ? A HEM 201 ? 1_555 NC  ? I  HEM .   ? A HEM 201 ? 1_555 91.0  ? 
112 O1  ? J  OXY .   ? A OXY 202 ? 1_555 FE ? I  HEM . ? A HEM 201 ? 1_555 ND  ? I  HEM .   ? A HEM 201 ? 1_555 83.9  ? 
113 NA  ? I  HEM .   ? A HEM 201 ? 1_555 FE ? I  HEM . ? A HEM 201 ? 1_555 ND  ? I  HEM .   ? A HEM 201 ? 1_555 90.4  ? 
114 NB  ? I  HEM .   ? A HEM 201 ? 1_555 FE ? I  HEM . ? A HEM 201 ? 1_555 ND  ? I  HEM .   ? A HEM 201 ? 1_555 178.9 ? 
115 NC  ? I  HEM .   ? A HEM 201 ? 1_555 FE ? I  HEM . ? A HEM 201 ? 1_555 ND  ? I  HEM .   ? A HEM 201 ? 1_555 89.2  ? 
116 O1  ? J  OXY .   ? A OXY 202 ? 1_555 FE ? I  HEM . ? A HEM 201 ? 1_555 NE2 ? A  HIS 94  ? A HIS 94  ? 1_555 177.5 ? 
117 NA  ? I  HEM .   ? A HEM 201 ? 1_555 FE ? I  HEM . ? A HEM 201 ? 1_555 NE2 ? A  HIS 94  ? A HIS 94  ? 1_555 88.8  ? 
118 NB  ? I  HEM .   ? A HEM 201 ? 1_555 FE ? I  HEM . ? A HEM 201 ? 1_555 NE2 ? A  HIS 94  ? A HIS 94  ? 1_555 87.1  ? 
119 NC  ? I  HEM .   ? A HEM 201 ? 1_555 FE ? I  HEM . ? A HEM 201 ? 1_555 NE2 ? A  HIS 94  ? A HIS 94  ? 1_555 92.1  ? 
120 ND  ? I  HEM .   ? A HEM 201 ? 1_555 FE ? I  HEM . ? A HEM 201 ? 1_555 NE2 ? A  HIS 94  ? A HIS 94  ? 1_555 94.0  ? 
121 OD1 ? B  ASP 135 ? B ASP 135 ? 1_555 CA ? N  CA  . ? B CA  203 ? 1_555 OD1 ? B  ASN 106 ? B ASN 106 ? 1_555 172.8 ? 
122 OD1 ? B  ASP 135 ? B ASP 135 ? 1_555 CA ? N  CA  . ? B CA  203 ? 1_555 OE2 ? B  GLU 109 ? B GLU 109 ? 1_555 104.7 ? 
123 OD1 ? B  ASN 106 ? B ASN 106 ? 1_555 CA ? N  CA  . ? B CA  203 ? 1_555 OE2 ? B  GLU 109 ? B GLU 109 ? 1_555 79.9  ? 
124 OD1 ? B  ASP 135 ? B ASP 135 ? 1_555 CA ? N  CA  . ? B CA  203 ? 1_555 OE1 ? B  GLU 109 ? B GLU 109 ? 1_555 80.3  ? 
125 OD1 ? B  ASN 106 ? B ASN 106 ? 1_555 CA ? N  CA  . ? B CA  203 ? 1_555 OE1 ? B  GLU 109 ? B GLU 109 ? 1_555 98.7  ? 
126 OE2 ? B  GLU 109 ? B GLU 109 ? 1_555 CA ? N  CA  . ? B CA  203 ? 1_555 OE1 ? B  GLU 109 ? B GLU 109 ? 1_555 51.3  ? 
127 OD1 ? F  ASN 106 ? F ASN 106 ? 1_555 CA ? DA CA  . ? F CA  203 ? 1_555 OD1 ? F  ASP 135 ? F ASP 135 ? 1_555 173.8 ? 
128 OD1 ? F  ASN 106 ? F ASN 106 ? 1_555 CA ? DA CA  . ? F CA  203 ? 1_555 OE2 ? F  GLU 109 ? F GLU 109 ? 1_555 84.7  ? 
129 OD1 ? F  ASP 135 ? F ASP 135 ? 1_555 CA ? DA CA  . ? F CA  203 ? 1_555 OE2 ? F  GLU 109 ? F GLU 109 ? 1_555 91.7  ? 
130 OD1 ? F  ASN 106 ? F ASN 106 ? 1_555 CA ? DA CA  . ? F CA  203 ? 1_555 OE1 ? F  GLU 109 ? F GLU 109 ? 1_555 93.6  ? 
131 OD1 ? F  ASP 135 ? F ASP 135 ? 1_555 CA ? DA CA  . ? F CA  203 ? 1_555 OE1 ? F  GLU 109 ? F GLU 109 ? 1_555 88.1  ? 
132 OE2 ? F  GLU 109 ? F GLU 109 ? 1_555 CA ? DA CA  . ? F CA  203 ? 1_555 OE1 ? F  GLU 109 ? F GLU 109 ? 1_555 51.9  ? 
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2014-06-04 
2 'Structure model' 1 1 2014-08-06 
# 
_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_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
BSS      'data collection' .   ? 1 
CNS      refinement        1.2 ? 2 
HKL-2000 'data reduction'  .   ? 3 
HKL-2000 'data scaling'    .   ? 4 
CNS      phasing           1.2 ? 5 
# 
_pdbx_validate_rmsd_bond.id                        1 
_pdbx_validate_rmsd_bond.PDB_model_num             1 
_pdbx_validate_rmsd_bond.auth_atom_id_1            C 
_pdbx_validate_rmsd_bond.auth_asym_id_1            C 
_pdbx_validate_rmsd_bond.auth_comp_id_1            SER 
_pdbx_validate_rmsd_bond.auth_seq_id_1             2 
_pdbx_validate_rmsd_bond.PDB_ins_code_1            ? 
_pdbx_validate_rmsd_bond.label_alt_id_1            ? 
_pdbx_validate_rmsd_bond.auth_atom_id_2            O 
_pdbx_validate_rmsd_bond.auth_asym_id_2            C 
_pdbx_validate_rmsd_bond.auth_comp_id_2            SER 
_pdbx_validate_rmsd_bond.auth_seq_id_2             2 
_pdbx_validate_rmsd_bond.PDB_ins_code_2            ? 
_pdbx_validate_rmsd_bond.label_alt_id_2            ? 
_pdbx_validate_rmsd_bond.bond_value                1.510 
_pdbx_validate_rmsd_bond.bond_target_value         1.229 
_pdbx_validate_rmsd_bond.bond_deviation            0.281 
_pdbx_validate_rmsd_bond.bond_standard_deviation   0.019 
_pdbx_validate_rmsd_bond.linker_flag               N 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 CA C LEU 15  ? ? CB C LEU 15  ? ? CG  C LEU 15  ? ? 101.18 115.30 -14.12 2.30 N 
2 1 CA C LEU 30  ? ? CB C LEU 30  ? ? CG  C LEU 30  ? ? 134.07 115.30 18.77  2.30 N 
3 1 CB C LEU 30  ? ? CG C LEU 30  ? ? CD2 C LEU 30  ? ? 99.83  111.00 -11.17 1.70 N 
4 1 CA C CYS 127 ? ? CB C CYS 127 ? ? SG  C CYS 127 ? ? 121.78 114.20 7.58   1.10 N 
5 1 N  D GLY 25  ? ? CA D GLY 25  ? ? C   D GLY 25  ? ? 128.80 113.10 15.70  2.50 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 PRO A 96  ? ? -63.95 3.82    
2  1 PHE A 145 ? ? -99.06 41.71   
3  1 SER B 97  ? ? -86.99 33.70   
4  1 ILE C 59  ? ? -48.43 -18.48  
5  1 ALA C 103 ? ? -35.25 144.54  
6  1 SER D 5   ? ? -45.91 157.50  
7  1 ALA D 22  ? ? -54.44 -9.22   
8  1 ASN E 3   ? ? -68.78 -176.27 
9  1 PRO E 96  ? ? -52.25 0.45    
10 1 ASP E 143 ? ? -62.27 5.05    
11 1 ARG F 51  ? ? 39.92  49.75   
12 1 ALA G 18  ? ? -43.50 -15.54  
13 1 LEU G 81  ? ? -68.93 3.57    
14 1 PHE H 3   ? ? 65.96  -114.60 
# 
_pdbx_validate_main_chain_plane.id                       1 
_pdbx_validate_main_chain_plane.PDB_model_num            1 
_pdbx_validate_main_chain_plane.auth_comp_id             SER 
_pdbx_validate_main_chain_plane.auth_asym_id             C 
_pdbx_validate_main_chain_plane.auth_seq_id              2 
_pdbx_validate_main_chain_plane.PDB_ins_code             ? 
_pdbx_validate_main_chain_plane.label_alt_id             ? 
_pdbx_validate_main_chain_plane.improper_torsion_angle   -10.20 
# 
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 D SER 1 ? D SER 1 
2 1 Y 1 D GLU 2 ? D GLU 2 
3 1 Y 1 H SER 1 ? H SER 1 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
5  'PROTOPORPHYRIN IX CONTAINING FE' HEM 
6  'OXYGEN MOLECULE'                 OXY 
7  'CALCIUM ION'                     CA  
8  N-ACETYL-D-GLUCOSAMINE            NAG 
9  ALPHA-D-MANNOSE                   MAN 
10 ALPHA-L-FUCOSE                    FUC 
11 water                             HOH 
# 
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 
I  5  HEM 1  201 200 HEM HEM A . 
J  6  OXY 1  202 201 OXY OXY A . 
K  7  CA  1  203 401 CA  CA  A . 
L  5  HEM 1  201 200 HEM HEM B . 
M  6  OXY 1  202 201 OXY OXY B . 
N  7  CA  1  203 401 CA  CA  B . 
O  7  CA  1  204 402 CA  CA  B . 
P  5  HEM 1  200 200 HEM HEM C . 
Q  6  OXY 1  201 201 OXY OXY C . 
R  5  HEM 1  201 200 HEM HEM D . 
S  6  OXY 1  202 201 OXY OXY D . 
T  8  NAG 1  203 301 NAG NAG D . 
U  8  NAG 2  204 302 NAG NAG D . 
V  9  MAN 3  205 303 MAN MAN D . 
W  9  MAN 4  206 304 MAN MAN D . 
X  9  MAN 5  207 305 MAN MAN D . 
Y  10 FUC 6  208 306 FUC FUC D . 
Z  5  HEM 1  200 200 HEM HEM E . 
AA 6  OXY 1  201 201 OXY OXY E . 
BA 5  HEM 1  201 200 HEM HEM F . 
CA 6  OXY 1  202 201 OXY OXY F . 
DA 7  CA  1  203 401 CA  CA  F . 
EA 7  CA  1  204 402 CA  CA  F . 
FA 7  CA  1  205 403 CA  CA  F . 
GA 5  HEM 1  200 200 HEM HEM G . 
HA 6  OXY 1  201 201 OXY OXY G . 
IA 5  HEM 1  201 200 HEM HEM H . 
JA 6  OXY 1  202 201 OXY OXY H . 
KA 8  NAG 1  203 301 NAG NAG H . 
LA 8  NAG 2  204 302 NAG NAG H . 
MA 9  MAN 3  205 303 MAN MAN H . 
NA 9  MAN 4  206 304 MAN MAN H . 
OA 9  MAN 5  207 305 MAN MAN H . 
PA 10 FUC 6  208 306 FUC FUC H . 
QA 11 HOH 1  301 2   HOH HOH A . 
QA 11 HOH 2  302 4   HOH HOH A . 
QA 11 HOH 3  303 12  HOH HOH A . 
QA 11 HOH 4  304 14  HOH HOH A . 
QA 11 HOH 5  305 22  HOH HOH A . 
QA 11 HOH 6  306 27  HOH HOH A . 
QA 11 HOH 7  307 38  HOH HOH A . 
QA 11 HOH 8  308 46  HOH HOH A . 
QA 11 HOH 9  309 68  HOH HOH A . 
QA 11 HOH 10 310 107 HOH HOH A . 
QA 11 HOH 11 311 205 HOH HOH A . 
RA 11 HOH 1  301 17  HOH HOH B . 
RA 11 HOH 2  302 208 HOH HOH B . 
SA 11 HOH 1  301 18  HOH HOH C . 
SA 11 HOH 2  302 40  HOH HOH C . 
SA 11 HOH 3  303 50  HOH HOH C . 
SA 11 HOH 4  304 73  HOH HOH C . 
SA 11 HOH 5  305 201 HOH HOH C . 
SA 11 HOH 6  306 206 HOH HOH C . 
SA 11 HOH 7  307 207 HOH HOH C . 
TA 11 HOH 1  301 23  HOH HOH D . 
TA 11 HOH 2  302 29  HOH HOH D . 
TA 11 HOH 3  303 49  HOH HOH D . 
TA 11 HOH 4  304 52  HOH HOH D . 
TA 11 HOH 5  305 66  HOH HOH D . 
TA 11 HOH 6  306 119 HOH HOH D . 
TA 11 HOH 7  307 139 HOH HOH D . 
TA 11 HOH 8  308 149 HOH HOH D . 
TA 11 HOH 9  309 202 HOH HOH D . 
UA 11 HOH 1  301 10  HOH HOH E . 
UA 11 HOH 2  302 43  HOH HOH E . 
UA 11 HOH 3  303 53  HOH HOH E . 
UA 11 HOH 4  304 95  HOH HOH E . 
UA 11 HOH 5  305 116 HOH HOH E . 
UA 11 HOH 6  306 125 HOH HOH E . 
UA 11 HOH 7  307 144 HOH HOH E . 
UA 11 HOH 8  308 151 HOH HOH E . 
UA 11 HOH 9  309 170 HOH HOH E . 
UA 11 HOH 10 310 203 HOH HOH E . 
UA 11 HOH 11 311 204 HOH HOH E . 
VA 11 HOH 1  301 44  HOH HOH F . 
VA 11 HOH 2  302 85  HOH HOH F . 
VA 11 HOH 3  303 89  HOH HOH F . 
VA 11 HOH 4  304 113 HOH HOH F . 
VA 11 HOH 5  305 114 HOH HOH F . 
VA 11 HOH 6  306 132 HOH HOH F . 
VA 11 HOH 7  307 152 HOH HOH F . 
VA 11 HOH 8  308 157 HOH HOH F . 
VA 11 HOH 9  309 173 HOH HOH F . 
WA 11 HOH 1  301 102 HOH HOH G . 
WA 11 HOH 2  302 103 HOH HOH G . 
WA 11 HOH 3  303 183 HOH HOH G . 
XA 11 HOH 1  301 9   HOH HOH H . 
XA 11 HOH 2  302 30  HOH HOH H . 
XA 11 HOH 3  303 31  HOH HOH H . 
XA 11 HOH 4  304 32  HOH HOH H . 
XA 11 HOH 5  305 41  HOH HOH H . 
XA 11 HOH 6  306 62  HOH HOH H . 
XA 11 HOH 7  307 123 HOH HOH H . 
# 
