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Database: PDB
Entry: 6ATZ
LinkDB: 6ATZ
Original site: 6ATZ 
HEADER    IMMUNE SYSTEM                           29-AUG-17   6ATZ              
TITLE     HLA-DRB1*1402 IN COMPLEX WITH CITRULLINATED FIBRINOGEN PEPTIDE        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DR ALPHA CHAIN;   
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 29-205;                                       
COMPND   5 SYNONYM: MHC CLASS II ANTIGEN DRA;                                   
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: MHC CLASS II ANTIGEN;                                      
COMPND   9 CHAIN: B, D;                                                         
COMPND  10 FRAGMENT: UNP RESIDUES 32-219;                                       
COMPND  11 ENGINEERED: YES;                                                     
COMPND  12 MOL_ID: 3;                                                           
COMPND  13 MOLECULE: FIBRINOGEN BETA CHAIN;                                     
COMPND  14 CHAIN: E, F;                                                         
COMPND  15 FRAGMENT: RESIDUES 69-81;                                            
COMPND  16 SYNONYM: FIBRINOGEN BETA- 74CIT69-81;                                
COMPND  17 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: HLA-DRA, HLA-DRA1;                                             
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI 'BL21-GOLD(DE3)PLYSS AG';        
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 866768;                                     
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 GENE: HLA-DRB1;                                                      
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI 'BL21-GOLD(DE3)PLYSS AG';        
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 866768;                                     
SOURCE  15 MOL_ID: 3;                                                           
SOURCE  16 SYNTHETIC: YES;                                                      
SOURCE  17 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  18 ORGANISM_COMMON: HUMAN;                                              
SOURCE  19 ORGANISM_TAXID: 9606                                                 
KEYWDS    HLA, MHC, CITRULLINE, RHEUMATOID ARTHRITIS, IMMUNE SYSTEM             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.T.TING,S.W.SCALLY,J.ROSSJOHN                                        
REVDAT   3   29-JUL-20 6ATZ    1       COMPND REMARK HETNAM LINK                
REVDAT   3 2                   1       SITE                                     
REVDAT   2   18-OCT-17 6ATZ    1       JRNL                                     
REVDAT   1   20-SEP-17 6ATZ    0                                                
JRNL        AUTH   S.W.SCALLY,S.C.LAW,Y.T.TING,J.V.HEEMST,J.SOKOLOVE,           
JRNL        AUTH 2 A.J.DEUTSCH,E.BRIDIE CLEMENS,A.K.MOUSTAKAS,G.K.PAPADOPOULOS, 
JRNL        AUTH 3 D.V.WOUDE,I.SMOLIK,C.A.HITCHON,D.B.ROBINSON,E.D.FERUCCI,     
JRNL        AUTH 4 C.N.BERNSTEIN,X.MENG,V.ANAPARTI,T.HUIZINGA,K.KEDZIERSKA,     
JRNL        AUTH 5 H.H.REID,S.RAYCHAUDHURI,R.E.TOES,J.ROSSJOHN,H.EL-GABALAWY,   
JRNL        AUTH 6 R.THOMAS                                                     
JRNL        TITL   MOLECULAR BASIS FOR INCREASED SUSCEPTIBILITY OF INDIGENOUS   
JRNL        TITL 2 NORTH AMERICANS TO SEROPOSITIVE RHEUMATOID ARTHRITIS.        
JRNL        REF    ANN. RHEUM. DIS.              V.  76  1915 2017              
JRNL        REFN                   ISSN 1468-2060                               
JRNL        PMID   28801345                                                     
JRNL        DOI    10.1136/ANNRHEUMDIS-2017-211300                              
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.11.1_2575                                   
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 45.48                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 24007                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.203                           
REMARK   3   R VALUE            (WORKING SET) : 0.201                           
REMARK   3   FREE R VALUE                     : 0.240                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.610                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1106                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 45.4846 -  5.3975    0.99     2928   170  0.2131 0.2168        
REMARK   3     2  5.3975 -  4.2852    1.00     2859   157  0.1602 0.1859        
REMARK   3     3  4.2852 -  3.7438    0.99     2868   148  0.1715 0.2135        
REMARK   3     4  3.7438 -  3.4017    0.99     2858   125  0.1938 0.2593        
REMARK   3     5  3.4017 -  3.1579    0.99     2863   115  0.2214 0.2545        
REMARK   3     6  3.1579 -  2.9718    0.99     2847   137  0.2342 0.3220        
REMARK   3     7  2.9718 -  2.8230    0.99     2833   140  0.2614 0.3715        
REMARK   3     8  2.8230 -  2.7001    0.99     2845   114  0.2547 0.3308        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.370            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.870           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 39.60                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 40.83                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.002           6322                                  
REMARK   3   ANGLE     :  0.572           8608                                  
REMARK   3   CHIRALITY :  0.044            934                                  
REMARK   3   PLANARITY :  0.003           1115                                  
REMARK   3   DIHEDRAL  : 14.582           3656                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : 1                                           
REMARK   3   NCS GROUP : 1                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: (CHAIN B AND (RESID 3 THROUGH 21 OR         
REMARK   3                          (RESID 22 THROUGH 23 AND (NAME N OR NAME    
REMARK   3                          CA OR NAME C OR NAME O OR NAME CB )) OR     
REMARK   3                          RESID 24 THROUGH 34 OR (RESID 35 AND        
REMARK   3                          (NAME N OR NAME CA OR NAME C OR NAME O OR   
REMARK   3                          NAME CB )) OR RESID 36 THROUGH 51 OR        
REMARK   3                          RESID 53 THROUGH 97 OR RESID 99 THROUGH     
REMARK   3                          137 OR (RESID 138 AND (NAME N OR NAME CA    
REMARK   3                          OR NAME C OR NAME O OR NAME CB )) OR        
REMARK   3                          RESID 139 THROUGH 161 OR RESID 163          
REMARK   3                          THROUGH 167 OR RESID 169 THROUGH 190))      
REMARK   3     SELECTION          : (CHAIN D AND (RESID 3 THROUGH 51 OR RESID   
REMARK   3                          53 THROUGH 97 OR RESID 99 THROUGH 161 OR    
REMARK   3                          RESID 163 THROUGH 188 OR (RESID 189         
REMARK   3                          THROUGH 190 AND (NAME N OR NAME CA OR       
REMARK   3                          NAME C OR NAME O OR NAME CB ))))            
REMARK   3     ATOM PAIRS NUMBER  : 2247                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6ATZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-AUG-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000229813.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 28-APR-17                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.3                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : AUSTRALIAN SYNCHROTRON             
REMARK 200  BEAMLINE                       : MX2                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9537                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 24028                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 47.060                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY                : 3.000                              
REMARK 200  R MERGE                    (I) : 0.12800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.1000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.83                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.48100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 4MCY                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.46                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.53                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG3350, 0.2 M POTASSIUM NITRATE,    
REMARK 280  0.1 M BIS-TRIS PROPANE, PH 7.3, VAPOR DIFFUSION, HANGING DROP,      
REMARK 280  TEMPERATURE 294K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       36.44250            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7450 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 17870 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, E                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7780 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 17720 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, F                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY D   168                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU A  40    CG   CD   OE1  OE2                                  
REMARK 470     GLU A  46    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 100    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     THR A 130    OG1  CG2                                            
REMARK 470     ARG B  23    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B  65    CG   CD   CE   NZ                                   
REMARK 470     LYS B 105    CG   CD   CE   NZ                                   
REMARK 470     LEU B 109    CG   CD1  CD2                                       
REMARK 470     GLN B 110    CG   CD   OE1  NE2                                  
REMARK 470     ARG B 189    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS C  38    CG   CD   CE   NZ                                   
REMARK 470     LYS C  39    CG   CD   CE   NZ                                   
REMARK 470     GLU C  40    CG   CD   OE1  OE2                                  
REMARK 470     GLU C  46    CG   CD   OE1  OE2                                  
REMARK 470     GLU C  71    CG   CD   OE1  OE2                                  
REMARK 470     ARG C 100    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU C 141    CG   CD   OE1  OE2                                  
REMARK 470     ASP C 171    CG   OD1  OD2                                       
REMARK 470     GLU C 172    CG   CD   OE1  OE2                                  
REMARK 470     GLU D  22    CG   CD   OE1  OE2                                  
REMARK 470     ARG D  23    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU D  35    CG   CD   OE1  OE2                                  
REMARK 470     GLU D  52    CG   CD   OE1  OE2                                  
REMARK 470     LYS D  65    CG   CD   CE   NZ                                   
REMARK 470     LYS D 105    CG   CD   CE   NZ                                   
REMARK 470     LEU D 109    CG   CD1  CD2                                       
REMARK 470     GLN D 110    CG   CD   OE1  NE2                                  
REMARK 470     GLU D 138    CG   CD   OE1  OE2                                  
REMARK 470     LYS E   8    CG   CD   CE   NZ                                   
REMARK 470     LYS F   8    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   ND2  ASN C    78     O5   NAG C   201              1.95            
REMARK 500   CG   ASN A    78     C1   NAG A   201              2.06            
REMARK 500   O    HOH B   313     O    HOH B   317              2.08            
REMARK 500   ND2  ASN A    78     C2   NAG A   201              2.17            
REMARK 500   OD1  ASN A    78     C1   NAG A   201              2.19            
REMARK 500   O    HOH A   329     O    HOH B   311              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   OD2  ASP B    76     NH1  ARG B   166     1455     2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ARG A 100       15.32     58.95                                   
REMARK 500    HIS A 143        3.03     58.83                                   
REMARK 500    ASN B  33     -113.84     59.05                                   
REMARK 500    THR B  90      -65.35   -128.97                                   
REMARK 500    HIS B 112       96.80    -64.78                                   
REMARK 500    ASN D  33     -113.03     57.08                                   
REMARK 500    THR D  90      -64.96   -130.02                                   
REMARK 500    HIS D 112       95.97    -67.20                                   
REMARK 500    ALA F  10     -179.32    -68.01                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 6ATI   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 6ATF   RELATED DB: PDB                                   
DBREF  6ATZ A    4   180  UNP    P01903   DRA_HUMAN       29    205             
DBREF1 6ATZ B    3   190  UNP                  A0A0A1I7H6_HUMAN                 
DBREF2 6ATZ B     A0A0A1I7H6                         32         219             
DBREF  6ATZ C    4   180  UNP    P01903   DRA_HUMAN       29    205             
DBREF1 6ATZ D    3   190  UNP                  A0A0A1I7H6_HUMAN                 
DBREF2 6ATZ D     A0A0A1I7H6                         32         219             
DBREF  6ATZ E    0    11  PDB    6ATZ     6ATZ             0     11             
DBREF  6ATZ F    0    11  PDB    6ATZ     6ATZ             0     11             
SEQRES   1 A  177  GLU HIS VAL ILE ILE GLN ALA GLU PHE TYR LEU ASN PRO          
SEQRES   2 A  177  ASP GLN SER GLY GLU PHE MET PHE ASP PHE ASP GLY ASP          
SEQRES   3 A  177  GLU ILE PHE HIS VAL ASP MET ALA LYS LYS GLU THR VAL          
SEQRES   4 A  177  TRP ARG LEU GLU GLU PHE GLY ARG PHE ALA SER PHE GLU          
SEQRES   5 A  177  ALA GLN GLY ALA LEU ALA ASN ILE ALA VAL ASP LYS ALA          
SEQRES   6 A  177  ASN LEU GLU ILE MET THR LYS ARG SER ASN TYR THR PRO          
SEQRES   7 A  177  ILE THR ASN VAL PRO PRO GLU VAL THR VAL LEU THR ASN          
SEQRES   8 A  177  SER PRO VAL GLU LEU ARG GLU PRO ASN VAL LEU ILE CYS          
SEQRES   9 A  177  PHE ILE ASP LYS PHE THR PRO PRO VAL VAL ASN VAL THR          
SEQRES  10 A  177  TRP LEU ARG ASN GLY LYS PRO VAL THR THR GLY VAL SER          
SEQRES  11 A  177  GLU THR VAL PHE LEU PRO ARG GLU ASP HIS LEU PHE ARG          
SEQRES  12 A  177  LYS PHE HIS TYR LEU PRO PHE LEU PRO SER THR GLU ASP          
SEQRES  13 A  177  VAL TYR ASP CYS ARG VAL GLU HIS TRP GLY LEU ASP GLU          
SEQRES  14 A  177  PRO LEU LEU LYS HIS TRP GLU PHE                              
SEQRES   1 B  188  THR ARG PRO ARG PHE LEU GLU TYR SER THR SER GLU CYS          
SEQRES   2 B  188  HIS PHE PHE ASN GLY THR GLU ARG VAL ARG PHE LEU GLU          
SEQRES   3 B  188  ARG TYR PHE HIS ASN GLN GLU GLU ASN VAL ARG PHE ASP          
SEQRES   4 B  188  SER ASP VAL GLY GLU TYR ARG ALA VAL THR GLU LEU GLY          
SEQRES   5 B  188  ARG PRO ASP ALA GLU TYR TRP ASN SER GLN LYS ASP LEU          
SEQRES   6 B  188  LEU GLU GLN ARG ARG ALA ALA VAL ASP THR TYR CYS ARG          
SEQRES   7 B  188  HIS ASN TYR GLY VAL GLY GLU SER PHE THR VAL GLN ARG          
SEQRES   8 B  188  ARG VAL HIS PRO LYS VAL THR VAL TYR PRO SER LYS THR          
SEQRES   9 B  188  GLN PRO LEU GLN HIS HIS ASN LEU LEU VAL CYS SER VAL          
SEQRES  10 B  188  SER GLY PHE TYR PRO GLY SER ILE GLU VAL ARG TRP PHE          
SEQRES  11 B  188  ARG ASN GLY GLN GLU GLU LYS THR GLY VAL VAL SER THR          
SEQRES  12 B  188  GLY LEU ILE HIS ASN GLY ASP TRP THR PHE GLN THR LEU          
SEQRES  13 B  188  VAL MET LEU GLU THR VAL PRO ARG SER GLY GLU VAL TYR          
SEQRES  14 B  188  THR CYS GLN VAL GLU HIS PRO SER VAL THR SER PRO LEU          
SEQRES  15 B  188  THR VAL GLU TRP ARG ALA                                      
SEQRES   1 C  177  GLU HIS VAL ILE ILE GLN ALA GLU PHE TYR LEU ASN PRO          
SEQRES   2 C  177  ASP GLN SER GLY GLU PHE MET PHE ASP PHE ASP GLY ASP          
SEQRES   3 C  177  GLU ILE PHE HIS VAL ASP MET ALA LYS LYS GLU THR VAL          
SEQRES   4 C  177  TRP ARG LEU GLU GLU PHE GLY ARG PHE ALA SER PHE GLU          
SEQRES   5 C  177  ALA GLN GLY ALA LEU ALA ASN ILE ALA VAL ASP LYS ALA          
SEQRES   6 C  177  ASN LEU GLU ILE MET THR LYS ARG SER ASN TYR THR PRO          
SEQRES   7 C  177  ILE THR ASN VAL PRO PRO GLU VAL THR VAL LEU THR ASN          
SEQRES   8 C  177  SER PRO VAL GLU LEU ARG GLU PRO ASN VAL LEU ILE CYS          
SEQRES   9 C  177  PHE ILE ASP LYS PHE THR PRO PRO VAL VAL ASN VAL THR          
SEQRES  10 C  177  TRP LEU ARG ASN GLY LYS PRO VAL THR THR GLY VAL SER          
SEQRES  11 C  177  GLU THR VAL PHE LEU PRO ARG GLU ASP HIS LEU PHE ARG          
SEQRES  12 C  177  LYS PHE HIS TYR LEU PRO PHE LEU PRO SER THR GLU ASP          
SEQRES  13 C  177  VAL TYR ASP CYS ARG VAL GLU HIS TRP GLY LEU ASP GLU          
SEQRES  14 C  177  PRO LEU LEU LYS HIS TRP GLU PHE                              
SEQRES   1 D  188  THR ARG PRO ARG PHE LEU GLU TYR SER THR SER GLU CYS          
SEQRES   2 D  188  HIS PHE PHE ASN GLY THR GLU ARG VAL ARG PHE LEU GLU          
SEQRES   3 D  188  ARG TYR PHE HIS ASN GLN GLU GLU ASN VAL ARG PHE ASP          
SEQRES   4 D  188  SER ASP VAL GLY GLU TYR ARG ALA VAL THR GLU LEU GLY          
SEQRES   5 D  188  ARG PRO ASP ALA GLU TYR TRP ASN SER GLN LYS ASP LEU          
SEQRES   6 D  188  LEU GLU GLN ARG ARG ALA ALA VAL ASP THR TYR CYS ARG          
SEQRES   7 D  188  HIS ASN TYR GLY VAL GLY GLU SER PHE THR VAL GLN ARG          
SEQRES   8 D  188  ARG VAL HIS PRO LYS VAL THR VAL TYR PRO SER LYS THR          
SEQRES   9 D  188  GLN PRO LEU GLN HIS HIS ASN LEU LEU VAL CYS SER VAL          
SEQRES  10 D  188  SER GLY PHE TYR PRO GLY SER ILE GLU VAL ARG TRP PHE          
SEQRES  11 D  188  ARG ASN GLY GLN GLU GLU LYS THR GLY VAL VAL SER THR          
SEQRES  12 D  188  GLY LEU ILE HIS ASN GLY ASP TRP THR PHE GLN THR LEU          
SEQRES  13 D  188  VAL MET LEU GLU THR VAL PRO ARG SER GLY GLU VAL TYR          
SEQRES  14 D  188  THR CYS GLN VAL GLU HIS PRO SER VAL THR SER PRO LEU          
SEQRES  15 D  188  THR VAL GLU TRP ARG ALA                                      
SEQRES   1 E   12  GLY GLY TYR ARG ALA CIR PRO ALA LYS ALA ALA THR              
SEQRES   1 F   12  GLY GLY TYR ARG ALA CIR PRO ALA LYS ALA ALA THR              
MODRES 6ATZ CIR E    5  ARG  MODIFIED RESIDUE                                   
MODRES 6ATZ CIR F    5  ARG  MODIFIED RESIDUE                                   
HET    CIR  E   5      22                                                       
HET    CIR  F   5      22                                                       
HET    NAG  A 201      27                                                       
HET    NAG  A 202      27                                                       
HET    B3P  B 201      45                                                       
HET    NAG  C 201      27                                                       
HET    NAG  C 202      27                                                       
HETNAM     CIR CITRULLINE                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     B3P 2-[3-(2-HYDROXY-1,1-DIHYDROXYMETHYL-ETHYLAMINO)-                 
HETNAM   2 B3P  PROPYLAMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL                   
FORMUL   5  CIR    2(C6 H13 N3 O3)                                              
FORMUL   7  NAG    4(C8 H15 N O6)                                               
FORMUL   9  B3P    C11 H26 N2 O6                                                
FORMUL  12  HOH   *112(H2 O)                                                    
HELIX    1 AA1 LEU A   45  ARG A   50  1                                   6    
HELIX    2 AA2 GLU A   55  SER A   77  1                                  23    
HELIX    3 AA3 THR B   51  LEU B   53  5                                   3    
HELIX    4 AA4 GLY B   54  SER B   63  1                                  10    
HELIX    5 AA5 GLN B   64  ALA B   73  1                                  10    
HELIX    6 AA6 ALA B   73  TYR B   78  1                                   6    
HELIX    7 AA7 TYR B   78  GLY B   86  1                                   9    
HELIX    8 AA8 GLU B   87  THR B   90  5                                   4    
HELIX    9 AA9 LEU C   45  PHE C   51  5                                   7    
HELIX   10 AB1 GLU C   55  SER C   77  1                                  23    
HELIX   11 AB2 THR D   51  LEU D   53  5                                   3    
HELIX   12 AB3 GLY D   54  SER D   63  1                                  10    
HELIX   13 AB4 GLN D   64  ALA D   73  1                                  10    
HELIX   14 AB5 ALA D   73  TYR D   78  1                                   6    
HELIX   15 AB6 TYR D   78  GLY D   86  1                                   9    
HELIX   16 AB7 GLU D   87  THR D   90  5                                   4    
SHEET    1 AA1 8 GLU A  40  TRP A  43  0                                        
SHEET    2 AA1 8 ASP A  29  ASP A  35 -1  N  HIS A  33   O  VAL A  42           
SHEET    3 AA1 8 SER A  19  PHE A  26 -1  N  PHE A  26   O  ASP A  29           
SHEET    4 AA1 8 HIS A   5  ASN A  15 -1  N  ILE A   8   O  ASP A  25           
SHEET    5 AA1 8 PHE B   7  PHE B  18 -1  O  PHE B  17   N  HIS A   5           
SHEET    6 AA1 8 ARG B  23  HIS B  32 -1  O  ARG B  25   N  HIS B  16           
SHEET    7 AA1 8 GLU B  35  ASP B  41 -1  O  ASN B  37   N  TYR B  30           
SHEET    8 AA1 8 TYR B  47  ALA B  49 -1  O  ARG B  48   N  ARG B  39           
SHEET    1 AA2 4 GLU A  88  THR A  93  0                                        
SHEET    2 AA2 4 ASN A 103  PHE A 112 -1  O  ILE A 106   N  LEU A  92           
SHEET    3 AA2 4 PHE A 145  PHE A 153 -1  O  LEU A 151   N  LEU A 105           
SHEET    4 AA2 4 SER A 133  GLU A 134 -1  N  SER A 133   O  TYR A 150           
SHEET    1 AA3 4 GLU A  88  THR A  93  0                                        
SHEET    2 AA3 4 ASN A 103  PHE A 112 -1  O  ILE A 106   N  LEU A  92           
SHEET    3 AA3 4 PHE A 145  PHE A 153 -1  O  LEU A 151   N  LEU A 105           
SHEET    4 AA3 4 LEU A 138  PRO A 139 -1  N  LEU A 138   O  ARG A 146           
SHEET    1 AA4 4 LYS A 126  VAL A 128  0                                        
SHEET    2 AA4 4 ASN A 118  ARG A 123 -1  N  ARG A 123   O  LYS A 126           
SHEET    3 AA4 4 TYR A 161  GLU A 166 -1  O  ARG A 164   N  THR A 120           
SHEET    4 AA4 4 LEU A 174  TRP A 178 -1  O  TRP A 178   N  TYR A 161           
SHEET    1 AA5 4 LYS B  98  SER B 104  0                                        
SHEET    2 AA5 4 LEU B 114  PHE B 122 -1  O  LEU B 114   N  SER B 104           
SHEET    3 AA5 4 PHE B 155  GLU B 162 -1  O  THR B 157   N  VAL B 119           
SHEET    4 AA5 4 VAL B 142  SER B 144 -1  N  VAL B 143   O  MET B 160           
SHEET    1 AA6 4 LYS B  98  SER B 104  0                                        
SHEET    2 AA6 4 LEU B 114  PHE B 122 -1  O  LEU B 114   N  SER B 104           
SHEET    3 AA6 4 PHE B 155  GLU B 162 -1  O  THR B 157   N  VAL B 119           
SHEET    4 AA6 4 ILE B 148  HIS B 149 -1  N  ILE B 148   O  GLN B 156           
SHEET    1 AA7 4 GLN B 136  GLU B 138  0                                        
SHEET    2 AA7 4 GLU B 128  ARG B 133 -1  N  ARG B 133   O  GLN B 136           
SHEET    3 AA7 4 VAL B 170  GLU B 176 -1  O  GLN B 174   N  ARG B 130           
SHEET    4 AA7 4 LEU B 184  ARG B 189 -1  O  LEU B 184   N  VAL B 175           
SHEET    1 AA8 8 GLU C  40  TRP C  43  0                                        
SHEET    2 AA8 8 ASP C  29  ASP C  35 -1  N  HIS C  33   O  VAL C  42           
SHEET    3 AA8 8 SER C  19  PHE C  26 -1  N  PHE C  26   O  ASP C  29           
SHEET    4 AA8 8 HIS C   5  ASN C  15 -1  N  ALA C  10   O  MET C  23           
SHEET    5 AA8 8 PHE D   7  PHE D  18 -1  O  CYS D  15   N  ILE C   7           
SHEET    6 AA8 8 ARG D  23  HIS D  32 -1  O  ARG D  25   N  HIS D  16           
SHEET    7 AA8 8 GLU D  35  ASP D  41 -1  O  ASN D  37   N  TYR D  30           
SHEET    8 AA8 8 TYR D  47  ALA D  49 -1  O  ARG D  48   N  ARG D  39           
SHEET    1 AA9 4 GLU C  88  THR C  93  0                                        
SHEET    2 AA9 4 ASN C 103  PHE C 112 -1  O  ILE C 106   N  LEU C  92           
SHEET    3 AA9 4 PHE C 145  PHE C 153 -1  O  HIS C 149   N  CYS C 107           
SHEET    4 AA9 4 SER C 133  GLU C 134 -1  N  SER C 133   O  TYR C 150           
SHEET    1 AB1 4 GLU C  88  THR C  93  0                                        
SHEET    2 AB1 4 ASN C 103  PHE C 112 -1  O  ILE C 106   N  LEU C  92           
SHEET    3 AB1 4 PHE C 145  PHE C 153 -1  O  HIS C 149   N  CYS C 107           
SHEET    4 AB1 4 LEU C 138  PRO C 139 -1  N  LEU C 138   O  ARG C 146           
SHEET    1 AB2 4 LYS C 126  VAL C 128  0                                        
SHEET    2 AB2 4 ASN C 118  ARG C 123 -1  N  TRP C 121   O  VAL C 128           
SHEET    3 AB2 4 TYR C 161  GLU C 166 -1  O  ARG C 164   N  THR C 120           
SHEET    4 AB2 4 LEU C 174  TRP C 178 -1  O  LEU C 174   N  VAL C 165           
SHEET    1 AB3 4 LYS D  98  SER D 104  0                                        
SHEET    2 AB3 4 LEU D 114  PHE D 122 -1  O  SER D 118   N  THR D 100           
SHEET    3 AB3 4 PHE D 155  GLU D 162 -1  O  THR D 157   N  VAL D 119           
SHEET    4 AB3 4 VAL D 142  SER D 144 -1  N  VAL D 143   O  MET D 160           
SHEET    1 AB4 4 LYS D  98  SER D 104  0                                        
SHEET    2 AB4 4 LEU D 114  PHE D 122 -1  O  SER D 118   N  THR D 100           
SHEET    3 AB4 4 PHE D 155  GLU D 162 -1  O  THR D 157   N  VAL D 119           
SHEET    4 AB4 4 ILE D 148  HIS D 149 -1  N  ILE D 148   O  GLN D 156           
SHEET    1 AB5 4 GLN D 136  GLU D 138  0                                        
SHEET    2 AB5 4 GLU D 128  ARG D 133 -1  N  ARG D 133   O  GLN D 136           
SHEET    3 AB5 4 VAL D 170  GLU D 176 -1  O  GLN D 174   N  ARG D 130           
SHEET    4 AB5 4 LEU D 184  ARG D 189 -1  O  LEU D 184   N  VAL D 175           
SSBOND   1 CYS A  107    CYS A  163                          1555   1555  2.03  
SSBOND   2 CYS B   15    CYS B   79                          1555   1555  2.04  
SSBOND   3 CYS B  117    CYS B  173                          1555   1555  2.03  
SSBOND   4 CYS C  107    CYS C  163                          1555   1555  2.03  
SSBOND   5 CYS D   15    CYS D   79                          1555   1555  2.04  
SSBOND   6 CYS D  117    CYS D  173                          1555   1555  2.03  
LINK         ND2 ASN A  78                 C1  NAG A 201     1555   1555  1.44  
LINK         ND2 ASN A 118                 C1  NAG A 202     1555   1555  1.44  
LINK         ND2 ASN C  78                 C1  NAG C 201     1555   1555  1.43  
LINK         ND2 ASN C 118                 C1  NAG C 202     1555   1555  1.43  
LINK         C   ALA E   4                 N2  CIR E   5     1555   1555  1.34  
LINK         C1  CIR E   5                 N   PRO E   6     1555   1555  1.30  
LINK         C   ALA F   4                 N2  CIR F   5     1555   1555  1.33  
LINK         C1  CIR F   5                 N   PRO F   6     1555   1555  1.31  
CISPEP   1 ASN A   15    PRO A   16          0        -2.25                     
CISPEP   2 THR A  113    PRO A  114          0         0.21                     
CISPEP   3 TYR B  123    PRO B  124          0         2.93                     
CISPEP   4 ASN C   15    PRO C   16          0         1.31                     
CISPEP   5 THR C  113    PRO C  114          0         0.59                     
CISPEP   6 TYR D  123    PRO D  124          0         3.08                     
CRYST1   66.881   72.885   95.316  90.00 107.40  90.00 P 1 21 1      4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.014952  0.000000  0.004685        0.00000                         
SCALE2      0.000000  0.013720  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010994        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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