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Database: PDB
Entry: 4H1L
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HEADER    IMMUNE SYSTEM                           10-SEP-12   4H1L              
TITLE     TCR INTERACTION WITH PEPTIDE MIMICS OF NICKEL OFFERS STRUCTURAL       
TITLE    2 INSIGHTS IN NICKEL CONTACT ALLERGY                                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DR ALPHA CHAIN;   
COMPND   3 CHAIN: A, D;                                                         
COMPND   4 SYNONYM: MHC CLASS II ANTIGEN DRA;                                   
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: MHC CLASS II ANTIGEN;                                      
COMPND   8 CHAIN: B, E;                                                         
COMPND   9 ENGINEERED: YES;                                                     
COMPND  10 MOL_ID: 3;                                                           
COMPND  11 MOLECULE: MIMOTOPE PEPTIDE;                                          
COMPND  12 CHAIN: C, F;                                                         
COMPND  13 ENGINEERED: YES;                                                     
COMPND  14 MOL_ID: 4;                                                           
COMPND  15 MOLECULE: ANI2.3 TCR A CHAIN;                                        
COMPND  16 CHAIN: G, I;                                                         
COMPND  17 ENGINEERED: YES;                                                     
COMPND  18 MOL_ID: 5;                                                           
COMPND  19 MOLECULE: ANI2.3 TCR B CHAIN;                                        
COMPND  20 CHAIN: H, J;                                                         
COMPND  21 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: HOMO SAPIENS;                                     
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: BACULOVIRUS;                              
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  12 ORGANISM_COMMON: HUMAN;                                              
SOURCE  13 ORGANISM_TAXID: 9606;                                                
SOURCE  14 GENE: HLA-DRB3;                                                      
SOURCE  15 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE  17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  18 EXPRESSION_SYSTEM_PLASMID: BACULOVIRUS;                              
SOURCE  19 MOL_ID: 3;                                                           
SOURCE  20 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  21 ORGANISM_TAXID: 562;                                                 
SOURCE  22 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  23 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  24 MOL_ID: 4;                                                           
SOURCE  25 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  26 ORGANISM_TAXID: 562;                                                 
SOURCE  27 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  28 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  29 MOL_ID: 5;                                                           
SOURCE  30 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  31 ORGANISM_TAXID: 562;                                                 
SOURCE  32 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  33 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    PROTEIN-PROTEIN COMPLEX, IMMUNOGLOBIN FOLD, TCR RECOGNITON OF MHC,    
KEYWDS   2 MHC II, GLYCOSIDATION, MEMBRANE, IMMUNE SYSTEM                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.W.KAPPLER,L.YIN,S.DAI,P.MARRACK                                     
REVDAT   2   04-SEP-13 4H1L    1       JRNL                                     
REVDAT   1   14-NOV-12 4H1L    0                                                
JRNL        AUTH   L.YIN,F.CRAWFORD,P.MARRACK,J.W.KAPPLER,S.DAI                 
JRNL        TITL   T-CELL RECEPTOR (TCR) INTERACTION WITH PEPTIDES THAT MIMIC   
JRNL        TITL 2 NICKEL OFFERS INSIGHT INTO NICKEL CONTACT ALLERGY.           
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 109 18517 2012              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   23091041                                                     
JRNL        DOI    10.1073/PNAS.1215928109                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.7_629)                      
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.83                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 87.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 44267                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.264                           
REMARK   3   R VALUE            (WORKING SET) : 0.263                           
REMARK   3   FREE R VALUE                     : 0.285                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.370                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2346                            
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 19.8264 -  7.7540    1.00     3493   157  0.2100 0.2463        
REMARK   3     2  7.7540 -  6.2169    0.99     3438   159  0.2103 0.2523        
REMARK   3     3  6.2169 -  5.4497    0.99     3415   153  0.2136 0.2318        
REMARK   3     4  5.4497 -  4.9600    0.98     3401   156  0.2105 0.2217        
REMARK   3     5  4.9600 -  4.6093    0.98     3334   154  0.2072 0.2376        
REMARK   3     6  4.6093 -  4.3405    0.96     3308   148  0.2274 0.2630        
REMARK   3     7  4.3405 -  4.1252    0.95     3283   147  0.2559 0.2382        
REMARK   3     8  4.1252 -  3.9471    0.92     3154   141  0.2845 0.3188        
REMARK   3     9  3.9471 -  3.7962    0.92     3126   141  0.3337 0.3463        
REMARK   3    10  3.7962 -  3.6661    0.90     3096   140  0.3573 0.3750        
REMARK   3    11  3.6661 -  3.5521    0.87     2977   146  0.3917 0.4138        
REMARK   3    12  3.5521 -  3.4511    0.75     2566   121  0.4144 0.3917        
REMARK   3    13  3.4511 -  3.3607    0.62     2113    97  0.4298 0.4281        
REMARK   3    14  3.3607 -  3.2791    0.48     1629    74  0.4407 0.4314        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.10                                          
REMARK   3   SHRINKAGE RADIUS   : 0.83                                          
REMARK   3   K_SOL              : 0.24                                          
REMARK   3   B_SOL              : 15.19                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.480            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.150           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 12.05640                                             
REMARK   3    B22 (A**2) : 12.05640                                             
REMARK   3    B33 (A**2) : -24.11290                                            
REMARK   3    B12 (A**2) : -0.00000                                             
REMARK   3    B13 (A**2) : -0.00000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
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      :  0.013           9894                                  
REMARK   3   ANGLE     :  1.502          13408                                  
REMARK   3   CHIRALITY :  0.092           1426                                  
REMARK   3   PLANARITY :  0.006           1750                                  
REMARK   3   DIHEDRAL  : 20.012           3602                                  
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 : 5                                           
REMARK   3   NCS GROUP : 1                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: chain B and (resseq 4:105 or resseq 114:    
REMARK   3                          190 )                                       
REMARK   3     SELECTION          : chain E and (resseq 4:105 or resseq 114:    
REMARK   3                          190 )                                       
REMARK   3     ATOM PAIRS NUMBER  : 1475                                        
REMARK   3     RMSD               : 0.045                                       
REMARK   3   NCS GROUP : 2                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: chain A and (resseq 3:180 )                 
REMARK   3     SELECTION          : chain D and (resseq 3:180 )                 
REMARK   3     ATOM PAIRS NUMBER  : 1465                                        
REMARK   3     RMSD               : 0.069                                       
REMARK   3   NCS GROUP : 3                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: chain G and (resseq 1:113 )                 
REMARK   3     SELECTION          : chain I and (resseq 1:113 )                 
REMARK   3     ATOM PAIRS NUMBER  : 878                                         
REMARK   3     RMSD               : 0.085                                       
REMARK   3   NCS GROUP : 4                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: chain H and (resseq 1:111 )                 
REMARK   3     SELECTION          : chain J and (resseq 1:111 )                 
REMARK   3     ATOM PAIRS NUMBER  : 890                                         
REMARK   3     RMSD               : 0.075                                       
REMARK   3   NCS GROUP : 5                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: chain C and (resseq -1:11 )                 
REMARK   3     SELECTION          : chain F and (resseq -1:11 )                 
REMARK   3     ATOM PAIRS NUMBER  : 107                                         
REMARK   3     RMSD               : 0.058                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4H1L COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-SEP-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB074903.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 8.2.2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1                                  
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 46186                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 91.9                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
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: PHASES                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 80.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 6.15                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M AMMONIUM TARTRATE DIBASIC, 12%      
REMARK 280  PEG 3350 , PH 7, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/2                                            
REMARK 290       6555   X-Y,X,Z+1/2                                             
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       83.35100            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       83.35100            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       83.35100            
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: PENTAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, I, J                         
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: PENTAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E, F, G, H                         
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     THR B   106                                                      
REMARK 465     GLN B   107                                                      
REMARK 465     PRO B   108                                                      
REMARK 465     LEU B   109                                                      
REMARK 465     GLN B   110                                                      
REMARK 465     HIS B   111                                                      
REMARK 465     HIS B   112                                                      
REMARK 465     ASN B   113                                                      
REMARK 465     THR E   106                                                      
REMARK 465     GLN E   107                                                      
REMARK 465     PRO E   108                                                      
REMARK 465     LEU E   109                                                      
REMARK 465     GLN E   110                                                      
REMARK 465     HIS E   111                                                      
REMARK 465     HIS E   112                                                      
REMARK 465     ASN E   113                                                      
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     TYR G   26   CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 480     LYS G   60   CG   CD   CE   NZ                                   
REMARK 480     LYS G  112   CG   CD   CE   NZ                                   
REMARK 480     LYS H   12   CG   CD   CE   NZ                                   
REMARK 480     GLN H   80   CG   CD   OE1  NE2                                  
REMARK 480     LYS H   81   CG   CD   CE   NZ                                   
REMARK 480     TYR I   26   CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 480     LYS I   60   CG   CD   CE   NZ                                   
REMARK 480     LYS I  112   CG   CD   CE   NZ                                   
REMARK 480     LYS J   12   CG   CD   CE   NZ                                   
REMARK 480     GLN J   80   CG   CD   OE1  NE2                                  
REMARK 480     LYS J   81   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   OD1  ASN B    77     OG1  THR I    29              2.05            
REMARK 500   O    LEU D    99     O    PRO D   155              2.08            
REMARK 500   O    LEU A    99     O    PRO A   155              2.09            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    ARG G  68   CZ    ARG G  68   NH1     0.086                       
REMARK 500    GLN G 105   CD    GLN G 105   OE1     0.136                       
REMARK 500    ARG I  68   CZ    ARG I  68   NH1     0.095                       
REMARK 500    ARG I  68   CZ    ARG I  68   NH2     0.128                       
REMARK 500    GLN I 105   CD    GLN I 105   OE1     0.139                       
REMARK 500    GLN I 105   CD    GLN I 105   NE2     0.157                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A  50   NE  -  CZ  -  NH1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ARG A  50   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.3 DEGREES          
REMARK 500    PRO A  87   C   -  N   -  CA  ANGL. DEV. =   9.2 DEGREES          
REMARK 500    ARG D  50   CA  -  CB  -  CG  ANGL. DEV. =  13.3 DEGREES          
REMARK 500    ARG D  50   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.9 DEGREES          
REMARK 500    ARG D  50   NE  -  CZ  -  NH2 ANGL. DEV. =   5.3 DEGREES          
REMARK 500    ARG G  68   CD  -  NE  -  CZ  ANGL. DEV. =  10.2 DEGREES          
REMARK 500    ARG G  68   NE  -  CZ  -  NH1 ANGL. DEV. =  -8.3 DEGREES          
REMARK 500    ARG G  68   NE  -  CZ  -  NH2 ANGL. DEV. =   4.9 DEGREES          
REMARK 500    ARG H  42   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.5 DEGREES          
REMARK 500    ARG H  42   NE  -  CZ  -  NH2 ANGL. DEV. =   4.8 DEGREES          
REMARK 500    PRO H  83   C   -  N   -  CA  ANGL. DEV. =   9.4 DEGREES          
REMARK 500    ARG I  68   CD  -  NE  -  CZ  ANGL. DEV. =  11.7 DEGREES          
REMARK 500    ARG I  68   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.7 DEGREES          
REMARK 500    SER I  95   N   -  CA  -  C   ANGL. DEV. = -19.5 DEGREES          
REMARK 500    GLY I  99   N   -  CA  -  C   ANGL. DEV. = -15.2 DEGREES          
REMARK 500    ARG J  42   NE  -  CZ  -  NH1 ANGL. DEV. =   4.7 DEGREES          
REMARK 500    ARG J  42   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.9 DEGREES          
REMARK 500    ILE J  49   CB  -  CA  -  C   ANGL. DEV. = -13.0 DEGREES          
REMARK 500    PRO J  83   C   -  N   -  CA  ANGL. DEV. =  10.2 DEGREES          
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    GLU A   4      -66.47   -128.85                                   
REMARK 500    SER A  77       45.13   -147.60                                   
REMARK 500    ASN A  78        9.61     50.81                                   
REMARK 500    TYR A  79       37.54     70.92                                   
REMARK 500    LYS A 111       72.37     51.46                                   
REMARK 500    ASN A 118       79.23   -111.75                                   
REMARK 500    ASN A 124        7.46     57.48                                   
REMARK 500    HIS A 167      152.83    178.07                                   
REMARK 500    PRO A 173      123.89    -36.18                                   
REMARK 500    ASN B  19       70.87     52.31                                   
REMARK 500    GLU B  52       -6.09    -57.51                                   
REMARK 500    ASP B  76      -63.24    -97.04                                   
REMARK 500    GLN B  92       32.08    -88.17                                   
REMARK 500    TYR B 102      147.59   -170.91                                   
REMARK 500    SER B 126      119.68    -39.03                                   
REMARK 500    THR B 140      -75.44    -78.51                                   
REMARK 500    PRO B 178       27.93    -70.40                                   
REMARK 500    GLU D   4      -68.09   -127.71                                   
REMARK 500    GLU D  47       -7.23    -56.38                                   
REMARK 500    SER D  77       45.16   -146.43                                   
REMARK 500    ASN D  78        9.28     48.67                                   
REMARK 500    TYR D  79       35.87     71.69                                   
REMARK 500    PRO D  96      151.41    -40.17                                   
REMARK 500    LYS D 111       71.68     53.15                                   
REMARK 500    ASN D 118       79.77   -110.66                                   
REMARK 500    ASN D 124        8.90     57.62                                   
REMARK 500    HIS D 167      153.18    177.37                                   
REMARK 500    PRO D 173      123.20    -35.81                                   
REMARK 500    ASN E  19       70.72     53.65                                   
REMARK 500    GLU E  52       -5.20    -59.17                                   
REMARK 500    ASP E  76      -66.40    -94.51                                   
REMARK 500    THR E  90      -69.40   -120.26                                   
REMARK 500    GLN E  92       33.67    -87.38                                   
REMARK 500    TYR E 102      147.61   -171.21                                   
REMARK 500    THR E 140      -73.10    -80.16                                   
REMARK 500    PRO E 178       27.05    -70.47                                   
REMARK 500    ALA G  16     -166.83    -68.52                                   
REMARK 500    GLU G  19       86.20   -157.15                                   
REMARK 500    GLN G  41     -156.17   -117.23                                   
REMARK 500    LEU G  47      167.98    179.77                                   
REMARK 500    TYR G  49      101.23   -163.00                                   
REMARK 500    ASP G  84        2.68    -65.72                                   
REMARK 500    THR G  98     -162.65   -124.18                                   
REMARK 500    ASN H  16       76.67   -101.33                                   
REMARK 500    ASN H  24       56.09   -108.44                                   
REMARK 500    ASN H  51       -1.20     71.88                                   
REMARK 500    ARG H  66       72.60   -118.86                                   
REMARK 500    LYS H  81       28.90    -75.43                                   
REMARK 500    THR H  84       20.45    -69.46                                   
REMARK 500    ASP H  95      -82.79   -118.89                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      67 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ALA G   94     SER G   95                 -106.44                    
REMARK 500 GLY G   96     ASN G   97                 -101.90                    
REMARK 500 LYS H   81     ASN H   82                  149.24                    
REMARK 500 ASN H   82     PRO H   83                 -135.35                    
REMARK 500 ALA I   94     SER I   95                  -72.06                    
REMARK 500 GLY I   96     ASN I   97                  -61.03                    
REMARK 500 LYS J   81     ASN J   82                  149.25                    
REMARK 500 ASN J   82     PRO J   83                 -134.43                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    ARG D  50        24.6      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4H25   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4H26   RELATED DB: PDB                                   
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THESE MISMATCHES ARE CONSEQUENCE OF A GENE RARE ALLELE OF HUMAN DR   
REMARK 999 GENE (DR52C)                                                         
DBREF  4H1L A    3   180  UNP    P01903   DRA_HUMAN       28    205             
DBREF  4H1L B    6   188  UNP    D0AB36   D0AB36_HUMAN     1    183             
DBREF  4H1L D    3   180  UNP    P01903   DRA_HUMAN       28    205             
DBREF  4H1L E    6   188  UNP    D0AB36   D0AB36_HUMAN     1    183             
DBREF  4H1L C   -1    11  PDB    4H1L     4H1L            -1     11             
DBREF  4H1L F   -1    11  PDB    4H1L     4H1L            -1     11             
DBREF  4H1L G    1   113  PDB    4H1L     4H1L             1    113             
DBREF  4H1L I    1   113  PDB    4H1L     4H1L             1    113             
DBREF  4H1L H    1   111  PDB    4H1L     4H1L             1    111             
DBREF  4H1L J    1   111  PDB    4H1L     4H1L             1    111             
SEQADV 4H1L ARG B    4  UNP  D0AB36              EXPRESSION TAG                 
SEQADV 4H1L PRO B    5  UNP  D0AB36              EXPRESSION TAG                 
SEQADV 4H1L GLN B   74  UNP  D0AB36    ARG    69 SEE REMARK 999                 
SEQADV 4H1L VAL B   86  UNP  D0AB36    GLY    81 SEE REMARK 999                 
SEQADV 4H1L ARG B  189  UNP  D0AB36              EXPRESSION TAG                 
SEQADV 4H1L ALA B  190  UNP  D0AB36              EXPRESSION TAG                 
SEQADV 4H1L ARG E    4  UNP  D0AB36              EXPRESSION TAG                 
SEQADV 4H1L PRO E    5  UNP  D0AB36              EXPRESSION TAG                 
SEQADV 4H1L GLN E   74  UNP  D0AB36    ARG    69 SEE REMARK 999                 
SEQADV 4H1L VAL E   86  UNP  D0AB36    GLY    81 SEE REMARK 999                 
SEQADV 4H1L ARG E  189  UNP  D0AB36              EXPRESSION TAG                 
SEQADV 4H1L ALA E  190  UNP  D0AB36              EXPRESSION TAG                 
SEQRES   1 A  178  GLU GLU HIS VAL ILE ILE GLN ALA GLU PHE TYR LEU ASN          
SEQRES   2 A  178  PRO ASP GLN SER GLY GLU PHE MET PHE ASP PHE ASP GLY          
SEQRES   3 A  178  ASP GLU ILE PHE HIS VAL ASP MET ALA LYS LYS GLU THR          
SEQRES   4 A  178  VAL TRP ARG LEU GLU GLU PHE GLY ARG PHE ALA SER PHE          
SEQRES   5 A  178  GLU ALA GLN GLY ALA LEU ALA ASN ILE ALA VAL ASP LYS          
SEQRES   6 A  178  ALA ASN LEU GLU ILE MET THR LYS ARG SER ASN TYR THR          
SEQRES   7 A  178  PRO ILE THR ASN VAL PRO PRO GLU VAL THR VAL LEU THR          
SEQRES   8 A  178  ASN SER PRO VAL GLU LEU ARG GLU PRO ASN VAL LEU ILE          
SEQRES   9 A  178  CYS PHE ILE ASP LYS PHE THR PRO PRO VAL VAL ASN VAL          
SEQRES  10 A  178  THR TRP LEU ARG ASN GLY LYS PRO VAL THR THR GLY VAL          
SEQRES  11 A  178  SER GLU THR VAL PHE LEU PRO ARG GLU ASP HIS LEU PHE          
SEQRES  12 A  178  ARG LYS PHE HIS TYR LEU PRO PHE LEU PRO SER THR GLU          
SEQRES  13 A  178  ASP VAL TYR ASP CYS ARG VAL GLU HIS TRP GLY LEU ASP          
SEQRES  14 A  178  GLU PRO LEU LEU LYS HIS TRP GLU PHE                          
SEQRES   1 B  187  ARG PRO ARG PHE LEU GLU LEU LEU LYS SER GLU CYS HIS          
SEQRES   2 B  187  PHE PHE ASN GLY THR GLU ARG VAL ARG PHE LEU GLU ARG          
SEQRES   3 B  187  TYR PHE HIS ASN GLN GLU GLU PHE VAL ARG PHE ASP SER          
SEQRES   4 B  187  ASP VAL GLY GLU TYR ARG ALA VAL THR GLU LEU GLY ARG          
SEQRES   5 B  187  PRO VAL ALA GLU SER TRP ASN SER GLN LYS ASP LEU LEU          
SEQRES   6 B  187  GLU GLN LYS ARG GLY GLN VAL ASP ASN TYR CYS ARG HIS          
SEQRES   7 B  187  ASN TYR GLY VAL VAL GLU SER PHE THR VAL GLN ARG ARG          
SEQRES   8 B  187  VAL HIS PRO GLN VAL THR VAL TYR PRO ALA LYS THR GLN          
SEQRES   9 B  187  PRO LEU GLN HIS HIS ASN LEU LEU VAL CYS SER VAL SER          
SEQRES  10 B  187  GLY PHE TYR PRO GLY SER ILE GLU VAL ARG TRP PHE ARG          
SEQRES  11 B  187  ASN GLY GLN GLU GLU LYS THR GLY VAL VAL SER THR GLY          
SEQRES  12 B  187  LEU ILE HIS ASN GLY ASP TRP THR PHE GLN THR LEU VAL          
SEQRES  13 B  187  MET LEU GLU THR VAL PRO ARG SER GLY GLU VAL TYR THR          
SEQRES  14 B  187  CYS GLN VAL GLU HIS PRO SER VAL THR SER PRO LEU THR          
SEQRES  15 B  187  VAL GLU TRP ARG ALA                                          
SEQRES   1 C   13  GLN HIS ILE ARG CYS ASN ILE PRO LYS ARG ILE SER ALA          
SEQRES   1 D  178  GLU GLU HIS VAL ILE ILE GLN ALA GLU PHE TYR LEU ASN          
SEQRES   2 D  178  PRO ASP GLN SER GLY GLU PHE MET PHE ASP PHE ASP GLY          
SEQRES   3 D  178  ASP GLU ILE PHE HIS VAL ASP MET ALA LYS LYS GLU THR          
SEQRES   4 D  178  VAL TRP ARG LEU GLU GLU PHE GLY ARG PHE ALA SER PHE          
SEQRES   5 D  178  GLU ALA GLN GLY ALA LEU ALA ASN ILE ALA VAL ASP LYS          
SEQRES   6 D  178  ALA ASN LEU GLU ILE MET THR LYS ARG SER ASN TYR THR          
SEQRES   7 D  178  PRO ILE THR ASN VAL PRO PRO GLU VAL THR VAL LEU THR          
SEQRES   8 D  178  ASN SER PRO VAL GLU LEU ARG GLU PRO ASN VAL LEU ILE          
SEQRES   9 D  178  CYS PHE ILE ASP LYS PHE THR PRO PRO VAL VAL ASN VAL          
SEQRES  10 D  178  THR TRP LEU ARG ASN GLY LYS PRO VAL THR THR GLY VAL          
SEQRES  11 D  178  SER GLU THR VAL PHE LEU PRO ARG GLU ASP HIS LEU PHE          
SEQRES  12 D  178  ARG LYS PHE HIS TYR LEU PRO PHE LEU PRO SER THR GLU          
SEQRES  13 D  178  ASP VAL TYR ASP CYS ARG VAL GLU HIS TRP GLY LEU ASP          
SEQRES  14 D  178  GLU PRO LEU LEU LYS HIS TRP GLU PHE                          
SEQRES   1 E  187  ARG PRO ARG PHE LEU GLU LEU LEU LYS SER GLU CYS HIS          
SEQRES   2 E  187  PHE PHE ASN GLY THR GLU ARG VAL ARG PHE LEU GLU ARG          
SEQRES   3 E  187  TYR PHE HIS ASN GLN GLU GLU PHE VAL ARG PHE ASP SER          
SEQRES   4 E  187  ASP VAL GLY GLU TYR ARG ALA VAL THR GLU LEU GLY ARG          
SEQRES   5 E  187  PRO VAL ALA GLU SER TRP ASN SER GLN LYS ASP LEU LEU          
SEQRES   6 E  187  GLU GLN LYS ARG GLY GLN VAL ASP ASN TYR CYS ARG HIS          
SEQRES   7 E  187  ASN TYR GLY VAL VAL GLU SER PHE THR VAL GLN ARG ARG          
SEQRES   8 E  187  VAL HIS PRO GLN VAL THR VAL TYR PRO ALA LYS THR GLN          
SEQRES   9 E  187  PRO LEU GLN HIS HIS ASN LEU LEU VAL CYS SER VAL SER          
SEQRES  10 E  187  GLY PHE TYR PRO GLY SER ILE GLU VAL ARG TRP PHE ARG          
SEQRES  11 E  187  ASN GLY GLN GLU GLU LYS THR GLY VAL VAL SER THR GLY          
SEQRES  12 E  187  LEU ILE HIS ASN GLY ASP TRP THR PHE GLN THR LEU VAL          
SEQRES  13 E  187  MET LEU GLU THR VAL PRO ARG SER GLY GLU VAL TYR THR          
SEQRES  14 E  187  CYS GLN VAL GLU HIS PRO SER VAL THR SER PRO LEU THR          
SEQRES  15 E  187  VAL GLU TRP ARG ALA                                          
SEQRES   1 F   13  GLN HIS ILE ARG CYS ASN ILE PRO LYS ARG ILE SER ALA          
SEQRES   1 G  113  GLN SER VAL THR GLN PRO ASP ILE HIS ILE THR VAL SER          
SEQRES   2 G  113  GLU GLY ALA SER LEU GLU LEU ARG CYS ASN TYR SER TYR          
SEQRES   3 G  113  GLY ALA THR PRO TYR LEU PHE TRP TYR VAL GLN SER PRO          
SEQRES   4 G  113  GLY GLN GLY LEU GLN LEU LEU LEU LYS TYR PHE SER GLY          
SEQRES   5 G  113  ASP THR LEU VAL GLN GLY ILE LYS GLY PHE GLU ALA GLU          
SEQRES   6 G  113  PHE LYS ARG SER GLN SER SER PHE ASN LEU ARG LYS PRO          
SEQRES   7 G  113  SER VAL HIS TRP SER ASP ALA ALA GLU TYR PHE CYS ALA          
SEQRES   8 G  113  VAL GLY ALA SER GLY ASN THR GLY LYS LEU ILE PHE GLY          
SEQRES   9 G  113  GLN GLY THR THR LEU GLN VAL LYS PRO                          
SEQRES   1 H  111  GLY ILE THR GLN SER PRO LYS TYR LEU PHE ARG LYS GLU          
SEQRES   2 H  111  GLY GLN ASN VAL THR LEU SER CYS GLU GLN ASN LEU ASN          
SEQRES   3 H  111  HIS ASP ALA MET TYR TRP TYR ARG GLN ASP PRO GLY GLN          
SEQRES   4 H  111  GLY LEU ARG LEU ILE TYR TYR SER GLN ILE VAL ASN ASP          
SEQRES   5 H  111  PHE GLN LYS GLY ASP ILE ALA GLU GLY TYR SER VAL SER          
SEQRES   6 H  111  ARG GLU LYS LYS GLU SER PHE PRO LEU THR VAL THR SER          
SEQRES   7 H  111  ALA GLN LYS ASN PRO THR ALA PHE TYR LEU CYS ALA SER          
SEQRES   8 H  111  SER LEU ARG ASP GLY TYR THR GLY GLU LEU PHE PHE GLY          
SEQRES   9 H  111  GLU GLY SER ARG LEU THR VAL                                  
SEQRES   1 I  113  GLN SER VAL THR GLN PRO ASP ILE HIS ILE THR VAL SER          
SEQRES   2 I  113  GLU GLY ALA SER LEU GLU LEU ARG CYS ASN TYR SER TYR          
SEQRES   3 I  113  GLY ALA THR PRO TYR LEU PHE TRP TYR VAL GLN SER PRO          
SEQRES   4 I  113  GLY GLN GLY LEU GLN LEU LEU LEU LYS TYR PHE SER GLY          
SEQRES   5 I  113  ASP THR LEU VAL GLN GLY ILE LYS GLY PHE GLU ALA GLU          
SEQRES   6 I  113  PHE LYS ARG SER GLN SER SER PHE ASN LEU ARG LYS PRO          
SEQRES   7 I  113  SER VAL HIS TRP SER ASP ALA ALA GLU TYR PHE CYS ALA          
SEQRES   8 I  113  VAL GLY ALA SER GLY ASN THR GLY LYS LEU ILE PHE GLY          
SEQRES   9 I  113  GLN GLY THR THR LEU GLN VAL LYS PRO                          
SEQRES   1 J  111  GLY ILE THR GLN SER PRO LYS TYR LEU PHE ARG LYS GLU          
SEQRES   2 J  111  GLY GLN ASN VAL THR LEU SER CYS GLU GLN ASN LEU ASN          
SEQRES   3 J  111  HIS ASP ALA MET TYR TRP TYR ARG GLN ASP PRO GLY GLN          
SEQRES   4 J  111  GLY LEU ARG LEU ILE TYR TYR SER GLN ILE VAL ASN ASP          
SEQRES   5 J  111  PHE GLN LYS GLY ASP ILE ALA GLU GLY TYR SER VAL SER          
SEQRES   6 J  111  ARG GLU LYS LYS GLU SER PHE PRO LEU THR VAL THR SER          
SEQRES   7 J  111  ALA GLN LYS ASN PRO THR ALA PHE TYR LEU CYS ALA SER          
SEQRES   8 J  111  SER LEU ARG ASP GLY TYR THR GLY GLU LEU PHE PHE GLY          
SEQRES   9 J  111  GLU GLY SER ARG LEU THR VAL                                  
HELIX    1   1 LEU A   45  ALA A   52  5                                   8    
HELIX    2   2 GLU A   55  ARG A   76  1                                  22    
HELIX    3   3 GLY B   54  ASN B   62  1                                   9    
HELIX    4   4 GLN B   64  GLY B   73  1                                  10    
HELIX    5   5 GLY B   73  TYR B   78  1                                   6    
HELIX    6   6 TYR B   78  GLU B   87  1                                  10    
HELIX    7   7 GLU D   47  ALA D   52  1                                   6    
HELIX    8   8 GLU D   55  ARG D   76  1                                  22    
HELIX    9   9 GLY E   54  ASN E   62  1                                   9    
HELIX   10  10 GLN E   64  GLY E   73  1                                  10    
HELIX   11  11 GLY E   73  TYR E   78  1                                   6    
HELIX   12  12 TYR E   78  SER E   88  1                                  11    
HELIX   13  13 HIS G   81  ALA G   85  5                                   5    
HELIX   14  14 HIS I   81  ALA I   85  5                                   5    
SHEET    1   A 8 GLU A  40  TRP A  43  0                                        
SHEET    2   A 8 ASP A  29  ASP A  35 -1  N  ASP A  35   O  GLU A  40           
SHEET    3   A 8 SER A  19  PHE A  26 -1  N  PHE A  24   O  ILE A  31           
SHEET    4   A 8 HIS A   5  ASN A  15 -1  N  ILE A   8   O  ASP A  25           
SHEET    5   A 8 PHE B   7  PHE B  18 -1  O  LEU B  11   N  GLU A  11           
SHEET    6   A 8 ARG B  23  HIS B  32 -1  O  ARG B  25   N  HIS B  16           
SHEET    7   A 8 GLU B  36  ASP B  41 -1  O  PHE B  40   N  GLU B  28           
SHEET    8   A 8 TYR B  47  ALA B  49 -1  O  ARG B  48   N  ARG B  39           
SHEET    1   B 4 GLU A  88  THR A  93  0                                        
SHEET    2   B 4 ASN A 103  PHE A 112 -1  O  ILE A 106   N  LEU A  92           
SHEET    3   B 4 HIS A 149  PHE A 153 -1  O  LEU A 151   N  LEU A 105           
SHEET    4   B 4 SER A 133  GLU A 134 -1  N  SER A 133   O  TYR A 150           
SHEET    1   C 4 GLU A  88  THR A  93  0                                        
SHEET    2   C 4 ASN A 103  PHE A 112 -1  O  ILE A 106   N  LEU A  92           
SHEET    3   C 4 PHE A 145  LYS A 147 -1  O  PHE A 145   N  PHE A 112           
SHEET    4   C 4 LEU A 138  PRO A 139 -1  N  LEU A 138   O  ARG A 146           
SHEET    1   D 4 LYS A 126  VAL A 128  0                                        
SHEET    2   D 4 TRP A 121  ARG A 123 -1  N  ARG A 123   O  LYS A 126           
SHEET    3   D 4 VAL A 160  VAL A 165 -1  O  ASP A 162   N  LEU A 122           
SHEET    4   D 4 LEU A 174  GLU A 179 -1  O  TRP A 178   N  TYR A 161           
SHEET    1   E 4 GLN B  98  PRO B 103  0                                        
SHEET    2   E 4 LEU B 115  PHE B 122 -1  O  SER B 118   N  THR B 100           
SHEET    3   E 4 PHE B 155  LEU B 161 -1  O  LEU B 161   N  LEU B 115           
SHEET    4   E 4 VAL B 142  SER B 144 -1  N  VAL B 143   O  MET B 160           
SHEET    1   F 4 GLN B  98  PRO B 103  0                                        
SHEET    2   F 4 LEU B 115  PHE B 122 -1  O  SER B 118   N  THR B 100           
SHEET    3   F 4 PHE B 155  LEU B 161 -1  O  LEU B 161   N  LEU B 115           
SHEET    4   F 4 ILE B 148  HIS B 149 -1  N  ILE B 148   O  GLN B 156           
SHEET    1   G 4 GLN B 136  GLU B 137  0                                        
SHEET    2   G 4 GLU B 128  ARG B 133 -1  N  ARG B 133   O  GLN B 136           
SHEET    3   G 4 VAL B 170  HIS B 177 -1  O  GLN B 174   N  ARG B 130           
SHEET    4   G 4 VAL B 180  ARG B 189 -1  O  TRP B 188   N  TYR B 171           
SHEET    1   H 8 GLU D  40  TRP D  43  0                                        
SHEET    2   H 8 ASP D  29  ASP D  35 -1  N  ASP D  35   O  GLU D  40           
SHEET    3   H 8 SER D  19  PHE D  26 -1  N  PHE D  24   O  ILE D  31           
SHEET    4   H 8 HIS D   5  ASN D  15 -1  N  ILE D   8   O  ASP D  25           
SHEET    5   H 8 PHE E   7  PHE E  18 -1  O  PHE E  17   N  HIS D   5           
SHEET    6   H 8 ARG E  23  HIS E  32 -1  O  LEU E  27   N  GLU E  14           
SHEET    7   H 8 GLU E  36  ASP E  41 -1  O  PHE E  40   N  GLU E  28           
SHEET    8   H 8 TYR E  47  ALA E  49 -1  O  ARG E  48   N  ARG E  39           
SHEET    1   I 4 GLU D  88  THR D  93  0                                        
SHEET    2   I 4 ASN D 103  PHE D 112 -1  O  ILE D 106   N  LEU D  92           
SHEET    3   I 4 HIS D 149  PHE D 153 -1  O  LEU D 151   N  LEU D 105           
SHEET    4   I 4 SER D 133  GLU D 134 -1  N  SER D 133   O  TYR D 150           
SHEET    1   J 4 GLU D  88  THR D  93  0                                        
SHEET    2   J 4 ASN D 103  PHE D 112 -1  O  ILE D 106   N  LEU D  92           
SHEET    3   J 4 PHE D 145  LYS D 147 -1  O  PHE D 145   N  PHE D 112           
SHEET    4   J 4 LEU D 138  PRO D 139 -1  N  LEU D 138   O  ARG D 146           
SHEET    1   K 4 LYS D 126  VAL D 128  0                                        
SHEET    2   K 4 TRP D 121  ARG D 123 -1  N  ARG D 123   O  LYS D 126           
SHEET    3   K 4 VAL D 160  VAL D 165 -1  O  ASP D 162   N  LEU D 122           
SHEET    4   K 4 LEU D 174  GLU D 179 -1  O  TRP D 178   N  TYR D 161           
SHEET    1   L 4 GLN E  98  PRO E 103  0                                        
SHEET    2   L 4 LEU E 115  PHE E 122 -1  O  SER E 118   N  THR E 100           
SHEET    3   L 4 PHE E 155  LEU E 161 -1  O  LEU E 161   N  LEU E 115           
SHEET    4   L 4 VAL E 142  SER E 144 -1  N  VAL E 143   O  MET E 160           
SHEET    1   M 4 GLN E  98  PRO E 103  0                                        
SHEET    2   M 4 LEU E 115  PHE E 122 -1  O  SER E 118   N  THR E 100           
SHEET    3   M 4 PHE E 155  LEU E 161 -1  O  LEU E 161   N  LEU E 115           
SHEET    4   M 4 ILE E 148  HIS E 149 -1  N  ILE E 148   O  GLN E 156           
SHEET    1   N 4 GLN E 136  GLU E 137  0                                        
SHEET    2   N 4 GLU E 128  ARG E 133 -1  N  ARG E 133   O  GLN E 136           
SHEET    3   N 4 VAL E 170  HIS E 177 -1  O  GLN E 174   N  ARG E 130           
SHEET    4   N 4 VAL E 180  ARG E 189 -1  O  TRP E 188   N  TYR E 171           
SHEET    1   O 2 VAL G   3  THR G   4  0                                        
SHEET    2   O 2 ASN G  23  TYR G  24 -1  O  ASN G  23   N  THR G   4           
SHEET    1   P 5 HIS G   9  SER G  13  0                                        
SHEET    2   P 5 THR G 107  LYS G 112  1  O  THR G 108   N  ILE G  10           
SHEET    3   P 5 GLU G  87  GLY G  93 -1  N  TYR G  88   O  THR G 107           
SHEET    4   P 5 TYR G  31  GLN G  37 -1  N  TYR G  31   O  GLY G  93           
SHEET    5   P 5 GLN G  44  TYR G  49 -1  O  LEU G  46   N  TRP G  34           
SHEET    1   Q 4 HIS G   9  SER G  13  0                                        
SHEET    2   Q 4 THR G 107  LYS G 112  1  O  THR G 108   N  ILE G  10           
SHEET    3   Q 4 GLU G  87  GLY G  93 -1  N  TYR G  88   O  THR G 107           
SHEET    4   Q 4 LEU G 101  PHE G 103 -1  O  ILE G 102   N  VAL G  92           
SHEET    1   R 3 LEU G  55  GLN G  57  0                                        
SHEET    2   R 3 GLU G  63  LYS G  67 -1  O  ALA G  64   N  VAL G  56           
SHEET    3   R 3 SER G  72  ARG G  76 -1  O  ARG G  76   N  GLU G  63           
SHEET    1   S 4 ILE H   2  SER H   5  0                                        
SHEET    2   S 4 THR H  18  GLN H  23 -1  O  GLU H  22   N  THR H   3           
SHEET    3   S 4 LEU H  74  VAL H  76 -1  O  LEU H  74   N  LEU H  19           
SHEET    4   S 4 TYR H  62  VAL H  64 -1  N  SER H  63   O  THR H  75           
SHEET    1   T 6 TYR H   8  PHE H  10  0                                        
SHEET    2   T 6 SER H 107  THR H 110  1  O  ARG H 108   N  LEU H   9           
SHEET    3   T 6 PHE H  86  SER H  92 -1  N  TYR H  87   O  SER H 107           
SHEET    4   T 6 ALA H  29  GLN H  35 -1  N  TYR H  31   O  ALA H  90           
SHEET    5   T 6 LEU H  41  SER H  47 -1  O  ILE H  44   N  TRP H  32           
SHEET    6   T 6 GLN H  54  LYS H  55 -1  O  GLN H  54   N  TYR H  46           
SHEET    1   U 4 TYR H   8  PHE H  10  0                                        
SHEET    2   U 4 SER H 107  THR H 110  1  O  ARG H 108   N  LEU H   9           
SHEET    3   U 4 PHE H  86  SER H  92 -1  N  TYR H  87   O  SER H 107           
SHEET    4   U 4 PHE H 102  PHE H 103 -1  O  PHE H 102   N  SER H  91           
SHEET    1   V 2 VAL I   3  THR I   4  0                                        
SHEET    2   V 2 ASN I  23  TYR I  24 -1  O  ASN I  23   N  THR I   4           
SHEET    1   W 5 HIS I   9  SER I  13  0                                        
SHEET    2   W 5 THR I 107  LYS I 112  1  O  THR I 108   N  ILE I  10           
SHEET    3   W 5 GLU I  87  GLY I  93 -1  N  TYR I  88   O  THR I 107           
SHEET    4   W 5 TYR I  31  GLN I  37 -1  N  TYR I  31   O  GLY I  93           
SHEET    5   W 5 GLN I  44  TYR I  49 -1  O  LEU I  46   N  TRP I  34           
SHEET    1   X 4 HIS I   9  SER I  13  0                                        
SHEET    2   X 4 THR I 107  LYS I 112  1  O  THR I 108   N  ILE I  10           
SHEET    3   X 4 GLU I  87  GLY I  93 -1  N  TYR I  88   O  THR I 107           
SHEET    4   X 4 LEU I 101  PHE I 103 -1  O  ILE I 102   N  VAL I  92           
SHEET    1   Y 3 LEU I  55  GLN I  57  0                                        
SHEET    2   Y 3 GLU I  63  LYS I  67 -1  O  ALA I  64   N  VAL I  56           
SHEET    3   Y 3 SER I  72  ARG I  76 -1  O  ARG I  76   N  GLU I  63           
SHEET    1   Z 4 ILE J   2  SER J   5  0                                        
SHEET    2   Z 4 THR J  18  GLN J  23 -1  O  GLU J  22   N  THR J   3           
SHEET    3   Z 4 LEU J  74  VAL J  76 -1  O  LEU J  74   N  LEU J  19           
SHEET    4   Z 4 TYR J  62  VAL J  64 -1  N  SER J  63   O  THR J  75           
SHEET    1  AA 6 TYR J   8  PHE J  10  0                                        
SHEET    2  AA 6 SER J 107  THR J 110  1  O  ARG J 108   N  LEU J   9           
SHEET    3  AA 6 PHE J  86  SER J  92 -1  N  TYR J  87   O  SER J 107           
SHEET    4  AA 6 ALA J  29  GLN J  35 -1  N  TYR J  31   O  ALA J  90           
SHEET    5  AA 6 LEU J  41  SER J  47 -1  O  ILE J  44   N  TRP J  32           
SHEET    6  AA 6 GLN J  54  LYS J  55 -1  O  GLN J  54   N  TYR J  46           
SHEET    1  AB 4 TYR J   8  PHE J  10  0                                        
SHEET    2  AB 4 SER J 107  THR J 110  1  O  ARG J 108   N  LEU J   9           
SHEET    3  AB 4 PHE J  86  SER J  92 -1  N  TYR J  87   O  SER J 107           
SHEET    4  AB 4 PHE J 102  PHE J 103 -1  O  PHE J 102   N  SER J  91           
SSBOND   1 CYS A  107    CYS A  163                          1555   1555  2.04  
SSBOND   2 CYS B   15    CYS B   79                          1555   1555  1.98  
SSBOND   3 CYS B  117    CYS B  173                          1555   1555  2.05  
SSBOND   4 CYS D  107    CYS D  163                          1555   1555  2.04  
SSBOND   5 CYS E   15    CYS E   79                          1555   1555  1.99  
SSBOND   6 CYS E  117    CYS E  173                          1555   1555  2.04  
SSBOND   7 CYS G   22    CYS G   90                          1555   1555  2.02  
SSBOND   8 CYS H   21    CYS H   89                          1555   1555  2.04  
SSBOND   9 CYS I   22    CYS I   90                          1555   1555  2.03  
SSBOND  10 CYS J   21    CYS J   89                          1555   1555  2.02  
CISPEP   1 ASN A   15    PRO A   16          0        -3.23                     
CISPEP   2 THR A  113    PRO A  114          0       -15.08                     
CISPEP   3 TYR B  123    PRO B  124          0        -1.98                     
CISPEP   4 ASN D   15    PRO D   16          0        -0.96                     
CISPEP   5 THR D  113    PRO D  114          0       -14.97                     
CISPEP   6 TYR E  123    PRO E  124          0        -1.89                     
CISPEP   7 THR G   98    GLY G   99          0        24.27                     
CISPEP   8 SER H    5    PRO H    6          0        -7.48                     
CISPEP   9 TYR H   97    THR H   98          0         1.85                     
CISPEP  10 THR I   98    GLY I   99          0        26.51                     
CISPEP  11 SER J    5    PRO J    6          0        -8.32                     
CISPEP  12 TYR J   97    THR J   98          0        -1.40                     
CRYST1  186.722  186.722  166.702  90.00  90.00 120.00 P 63         12          
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      0.005356  0.003092  0.000000        0.00000                         
SCALE2      0.000000  0.006184  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005999        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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