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Database: PDB
Entry: 3L5H
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HEADER    IMMUNE SYSTEM                           21-DEC-09   3L5H              
TITLE     CRYSTAL STRUCTURE OF THE FULL ECTODOMAIN OF HUMAN GP130: NEW INSIGHTS 
TITLE    2 INTO THE MOLECULAR ASSEMBLY OF RECEPTOR COMPLEXES                    
CAVEAT     3L5H    NAG C 1 HAS WRONG CHIRALITY AT ATOM C1 NAG D 1 HAS WRONG     
CAVEAT   2 3L5H    CHIRALITY AT ATOM C1 NAG E 1 HAS WRONG CHIRALITY AT ATOM C1  
CAVEAT   3 3L5H    NAG H 1 HAS WRONG CHIRALITY AT ATOM C1                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: INTERLEUKIN-6 RECEPTOR SUBUNIT BETA;                       
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: ECOTODOMAIN;                                               
COMPND   5 SYNONYM: IL-6R-BETA, INTERLEUKIN-6 SIGNAL TRANSDUCER, MEMBRANE       
COMPND   6 GLYCOPROTEIN 130, GP130, CDW130, ONCOSTATIN-M RECEPTOR SUBUNIT ALPHA;
COMPND   7 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: IL6ST;                                                         
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   9 EXPRESSION_SYSTEM_CELL_LINE: SF21;                                   
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS                           
KEYWDS    IG-LIKE, FNIII, CELL MEMBRANE, DISULFIDE BOND, GLYCOPROTEIN,          
KEYWDS   2 IMMUNOGLOBULIN DOMAIN, MEMBRANE, PHOSPHOPROTEIN, RECEPTOR, SECRETED, 
KEYWDS   3 TRANSMEMBRANE, IMMUNE SYSTEM                                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.XU,T.P.J.GARRETT,J.G.ZHANG                                          
REVDAT   4   29-JUL-20 3L5H    1       CAVEAT COMPND REMARK HET                 
REVDAT   4 2                   1       HETNAM FORMUL LINK   SITE                
REVDAT   4 3                   1       ATOM                                     
REVDAT   3   05-APR-17 3L5H    1       JRNL                                     
REVDAT   2   13-JUL-11 3L5H    1       VERSN                                    
REVDAT   1   19-MAY-10 3L5H    0                                                
JRNL        AUTH   Y.XU,N.J.KERSHAW,C.S.LUO,P.SOO,M.J.POCOCK,P.E.CZABOTAR,      
JRNL        AUTH 2 D.J.HILTON,N.A.NICOLA,T.P.GARRETT,J.G.ZHANG                  
JRNL        TITL   CRYSTAL STRUCTURE OF THE ENTIRE ECTODOMAIN OF GP130:         
JRNL        TITL 2 INSIGHTS INTO THE MOLECULAR ASSEMBLY OF THE TALL CYTOKINE    
JRNL        TITL 3 RECEPTOR COMPLEXES.                                          
JRNL        REF    J.BIOL.CHEM.                  V. 285 21214 2010              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   20489211                                                     
JRNL        DOI    10.1074/JBC.C110.129502                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0066                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 44.43                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 16833                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.267                           
REMARK   3   R VALUE            (WORKING SET) : 0.263                           
REMARK   3   FREE R VALUE                     : 0.335                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 905                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.60                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.69                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1236                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.24                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.4100                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 72                           
REMARK   3   BIN FREE R VALUE                    : 0.3760                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4439                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 262                                     
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 93.97                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.55000                                             
REMARK   3    B22 (A**2) : 1.29000                                              
REMARK   3    B33 (A**2) : 0.58000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.76000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.648         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.331         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 45.179        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.875                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.807                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4829 ; 0.018 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6656 ; 2.236 ; 1.995       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   580 ;10.347 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   188 ;42.276 ;24.681       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   646 ;25.458 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    16 ;18.823 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   816 ; 0.139 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3580 ; 0.010 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  2931 ; 0.496 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4736 ; 0.977 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1898 ; 1.443 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1920 ; 2.581 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 6                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     2        A   102                          
REMARK   3    ORIGIN FOR THE GROUP (A):   8.9717 -19.0065   1.4843              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8826 T22:   0.4496                                     
REMARK   3      T33:   0.6390 T12:   0.0429                                     
REMARK   3      T13:  -0.0088 T23:   0.0934                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5425 L22:   2.0984                                     
REMARK   3      L33:   4.9553 L12:   1.9978                                     
REMARK   3      L13:   1.2400 L23:   0.6084                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5856 S12:   0.4710 S13:   0.0245                       
REMARK   3      S21:   0.1981 S22:  -0.0614 S23:  -0.6371                       
REMARK   3      S31:   0.3517 S32:  -0.1180 S33:  -0.5242                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   103        A   196                          
REMARK   3    ORIGIN FOR THE GROUP (A):  29.6278 -17.3581  39.3990              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4162 T22:   0.0842                                     
REMARK   3      T33:   0.1439 T12:  -0.0906                                     
REMARK   3      T13:  -0.1313 T23:   0.0199                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0201 L22:   3.3947                                     
REMARK   3      L33:   9.5863 L12:  -0.7928                                     
REMARK   3      L13:   0.1034 L23:   1.3712                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3451 S12:   0.4912 S13:   0.1164                       
REMARK   3      S21:  -0.9681 S22:  -0.0475 S23:   0.4483                       
REMARK   3      S31:  -0.3102 S32:  -0.0290 S33:   0.3926                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   197        A   302                          
REMARK   3    ORIGIN FOR THE GROUP (A):  23.6972 -12.9141  73.5854              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0673 T22:   0.0664                                     
REMARK   3      T33:   0.0422 T12:   0.0314                                     
REMARK   3      T13:   0.0401 T23:   0.0487                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.7775 L22:   1.2010                                     
REMARK   3      L33:   9.4708 L12:  -1.7517                                     
REMARK   3      L13:  -4.9243 L23:   1.8015                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0252 S12:  -0.2309 S13:  -0.1577                       
REMARK   3      S21:   0.0364 S22:   0.0172 S23:   0.0435                       
REMARK   3      S31:  -0.4812 S32:   0.1311 S33:  -0.0425                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   303        A   397                          
REMARK   3    ORIGIN FOR THE GROUP (A):   0.4912  -2.4352 111.2729              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2270 T22:   0.1335                                     
REMARK   3      T33:   0.1305 T12:  -0.0111                                     
REMARK   3      T13:   0.1040 T23:   0.0714                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.8626 L22:   7.0920                                     
REMARK   3      L33:   6.7990 L12:  -3.7547                                     
REMARK   3      L13:  -1.1431 L23:   2.5322                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1311 S12:  -0.3648 S13:  -0.6154                       
REMARK   3      S21:   1.0753 S22:   0.0836 S23:   0.5907                       
REMARK   3      S31:   0.5564 S32:  -0.6604 S33:   0.0475                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   398        A   493                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.7893  14.3141  99.2546              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0655 T22:   0.0198                                     
REMARK   3      T33:   0.1859 T12:   0.0292                                     
REMARK   3      T13:  -0.0068 T23:  -0.0196                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5235 L22:   2.2112                                     
REMARK   3      L33:   8.9352 L12:   0.2425                                     
REMARK   3      L13:   1.8877 L23:  -3.1804                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3560 S12:  -0.1962 S13:   0.5776                       
REMARK   3      S21:   0.0535 S22:  -0.0961 S23:   0.2416                       
REMARK   3      S31:  -0.0380 S32:   0.1362 S33:   0.4520                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   494        A   590                          
REMARK   3    ORIGIN FOR THE GROUP (A): -36.8479  30.1004  85.6251              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0429 T22:   0.0372                                     
REMARK   3      T33:   0.1488 T12:  -0.0136                                     
REMARK   3      T13:   0.0734 T23:  -0.0243                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.9666 L22:   2.4236                                     
REMARK   3      L33:   2.5474 L12:  -3.7148                                     
REMARK   3      L13:   3.6372 L23:  -0.8560                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2633 S12:  -0.0215 S13:  -0.0493                       
REMARK   3      S21:   0.2648 S22:  -0.0247 S23:   0.3541                       
REMARK   3      S31:   0.0498 S32:  -0.1777 S33:   0.2880                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS U VALUES: RESIDUAL ONLY                                   
REMARK   4                                                                      
REMARK   4 3L5H COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 07-JAN-10.                  
REMARK 100 THE DEPOSITION ID IS D_1000056857.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 28-OCT-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0                                
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) : 0.95369                            
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 : XSCALE                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA 3.3.9, XSCALE                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 17748                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 163.400                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 4.000                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.14800                            
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) : 3.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.79                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.13400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.100                              
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: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 78.13                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 5.62                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.5-2.0M (NH4)2SO4, 0.1M IMIDAZOLE       
REMARK 280  -MALONATE BUFFER, PH 6.0, EVAPORATION, TEMPERATURE 298K             
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       25.91050            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, 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     VAL A    27                                                      
REMARK 465     ILE A    83                                                      
REMARK 465     GLU A    90                                                      
REMARK 465     GLY A   101                                                      
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     TYR A   8    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLU A  12    CG   CD   OE1  OE2                                  
REMARK 470     GLN A  17    CG   CD   OE1  NE2                                  
REMARK 470     SER A  20    OG                                                  
REMARK 470     PHE A  22    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LEU A  28    CG   CD1  CD2                                       
REMARK 470     LYS A  29    CG   CD   CE   NZ                                   
REMARK 470     GLU A  30    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  31    CG   CD   CE   NZ                                   
REMARK 470     TYR A  35    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     HIS A  37    CG   ND1  CD2  CE1  NE2                             
REMARK 470     TYR A  42    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LYS A  46    CG   CD   CE   NZ                                   
REMARK 470     ASN A  48    CG   OD1  ND2                                       
REMARK 470     PHE A  50    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS A  54    CG   CD   CE   NZ                                   
REMARK 470     GLU A  55    CG   CD   OE1  OE2                                  
REMARK 470     GLN A  56    CG   CD   OE1  NE2                                  
REMARK 470     ILE A  59    CG1  CG2  CD1                                       
REMARK 470     ILE A  60    CG1  CG2  CD1                                       
REMARK 470     ARG A  62    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE A  77    CG1  CG2  CD1                                       
REMARK 470     LEU A  79    CG   CD1  CD2                                       
REMARK 470     GLN A  91    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 106    CG   CD   CE   NZ                                   
REMARK 470     LYS A 108    CG   CD   CE   NZ                                   
REMARK 470     LYS A 118    CG   CD   CE   NZ                                   
REMARK 470     LEU A 132    CG   CD1  CD2                                       
REMARK 470     GLU A 133    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 141    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 151    CG   CD   CE   NZ                                   
REMARK 470     LYS A 184    CG   CD   CE   NZ                                   
REMARK 470     SER A 211    OG                                                  
REMARK 470     GLU A 213    CG   CD   OE1  OE2                                  
REMARK 470     LEU A 220    CG   CD1  CD2                                       
REMARK 470     LYS A 228    CG   CD   CE   NZ                                   
REMARK 470     ILE A 237    CG1  CG2  CD1                                       
REMARK 470     SER A 260    OG                                                  
REMARK 470     VAL A 264    CG1  CG2                                            
REMARK 470     LYS A 268    CG   CD   CE   NZ                                   
REMARK 470     GLU A 294    CG   CD   OE1  OE2                                  
REMARK 470     TYR A 300    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LYS A 306    CG   CD   CE   NZ                                   
REMARK 470     LYS A 313    CG   CD   CE   NZ                                   
REMARK 470     THR A 319    OG1  CG2                                            
REMARK 470     ARG A 323    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 340    CG   CD   CE   NZ                                   
REMARK 470     LEU A 342    CG   CD1  CD2                                       
REMARK 470     ARG A 350    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     TRP A 351    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP A 351    CZ3  CH2                                            
REMARK 470     LYS A 352    CG   CD   CE   NZ                                   
REMARK 470     SER A 353    OG                                                  
REMARK 470     LYS A 364    CG   CD   CE   NZ                                   
REMARK 470     LEU A 383    CG   CD1  CD2                                       
REMARK 470     LYS A 409    CG   CD   CE   NZ                                   
REMARK 470     ARG A 425    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER A 427    OG                                                  
REMARK 470     LYS A 441    CG   CD   CE   NZ                                   
REMARK 470     LYS A 489    CG   CD   CE   NZ                                   
REMARK 470     LYS A 493    CG   CD   CE   NZ                                   
REMARK 470     LYS A 506    CG   CD   CE   NZ                                   
REMARK 470     LYS A 510    CG   CD   CE   NZ                                   
REMARK 470     LYS A 590    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   N    THR A    85     O    LEU A    89              1.38            
REMARK 500   O    SER A   387     O    ASP A   388              1.54            
REMARK 500   O    ASN A   357     CD1  TYR A   358              1.60            
REMARK 500   O    LEU A   132     O    GLU A   133              1.63            
REMARK 500   O    SER A   257     O    THR A   258              1.66            
REMARK 500   CD1  LEU A   102     O    THR A   130              1.67            
REMARK 500   O    ALA A   442     O    PRO A   443              1.67            
REMARK 500   O    PRO A   496     O    PRO A   497              1.72            
REMARK 500   O    ALA A    64     OG   SER A    65              1.73            
REMARK 500   CB   VAL A    16     O    ILE A    99              1.73            
REMARK 500   O    ARG A   350     O    TRP A   351              1.73            
REMARK 500   OG   SER A    74     CD2  LEU A    75              1.76            
REMARK 500   O    THR A   359     O    VAL A   360              1.79            
REMARK 500   CD1  ILE A    43     N    VAL A    44              1.80            
REMARK 500   CG2  THR A    63     C8   NAG D     1              1.81            
REMARK 500   O    PRO A   333     N    PHE A   335              1.86            
REMARK 500   OE1  GLN A   238     NE   ARG A   276              1.88            
REMARK 500   O    THR A   574     N    GLU A   576              1.90            
REMARK 500   O    ASN A    61     N    THR A    63              1.90            
REMARK 500   OD1  ASN A   205     O5   NAG B     1              1.90            
REMARK 500   OD1  ASN A   224     OH   TYR A   235              1.91            
REMARK 500   O    THR A    47     N    HIS A    49              1.95            
REMARK 500   CD1  LEU A   515     CD1  LEU A   557              1.96            
REMARK 500   CA   VAL A    15     CD1  ILE A    99              1.96            
REMARK 500   CG2  VAL A   208     O    SER A   296              1.98            
REMARK 500   CE2  TYR A   491     CA   GLY A   527              1.98            
REMARK 500   C3   NAG H     1     O5   NAG H     2              1.98            
REMARK 500   O    THR A    51     CD   PRO A    53              1.99            
REMARK 500   CE2  TYR A   536     OG1  THR A   544              2.01            
REMARK 500   O    ASN A   382     N    VAL A   384              2.03            
REMARK 500   O    GLN A    17     N    HIS A    19              2.03            
REMARK 500   O    ASN A    41     N    ILE A    43              2.03            
REMARK 500   OE2  GLU A   345     C8   NAG G     1              2.04            
REMARK 500   O7   NAG H     1     O3   NAG H     2              2.05            
REMARK 500   N    VAL A    16     O    ILE A    99              2.08            
REMARK 500   O    TYR A   532     N    VAL A   548              2.08            
REMARK 500   O    THR A   574     N    GLY A   577              2.09            
REMARK 500   C4   NAG C     2     C1   BMA C     3              2.09            
REMARK 500   CG2  THR A   134     CB   ASN A   180              2.10            
REMARK 500   N    ASN A   382     O    GLY A   385              2.10            
REMARK 500   CG2  THR A    80     ND2  ASN A    82              2.13            
REMARK 500   O    THR A   564     OG1  THR A   587              2.14            
REMARK 500   C4   NAG C     1     C1   NAG C     2              2.14            
REMARK 500   CD1  TYR A   536     CD2  LEU A   557              2.15            
REMARK 500   OD1  ASN A   205     O6   NAG B     1              2.15            
REMARK 500   O    THR A   556     OG   SER A   558              2.17            
REMARK 500   N    ILE A   172     O    PHE A   192              2.18            
REMARK 500   O    THR A   241     N    ASP A   243              2.19            
REMARK 500   O    THR A    85     N    GLY A    87              2.19            
REMARK 500   O    ARG A   128     N    THR A   130              2.19            
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      52 CLOSE CONTACTS                                
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   ND2  ASN A   171     O4   SO4 A   592     2646     2.11            
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    HIS A 131   CG    HIS A 131   CD2     0.076                       
REMARK 500    ASP A 549   CB    ASP A 549   CG      0.148                       
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    PRO A 104   C   -  N   -  CA  ANGL. DEV. =  10.2 DEGREES          
REMARK 500    PRO A 200   C   -  N   -  CA  ANGL. DEV. =   9.3 DEGREES          
REMARK 500    PRO A 203   C   -  N   -  CA  ANGL. DEV. =  12.1 DEGREES          
REMARK 500    PRO A 251   C   -  N   -  CA  ANGL. DEV. =   9.1 DEGREES          
REMARK 500    LEU A 365   CA  -  CB  -  CG  ANGL. DEV. = -17.3 DEGREES          
REMARK 500    ARG A 461   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500    PRO A 497   C   -  N   -  CA  ANGL. DEV. = -11.0 DEGREES          
REMARK 500    PRO A 589   C   -  N   -  CA  ANGL. DEV. =  13.4 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    LEU A   3     -147.23   -116.95                                   
REMARK 500    PRO A   5       71.59   -118.95                                   
REMARK 500    CYS A   6      -62.35     15.57                                   
REMARK 500    ILE A   9     -100.69   -103.97                                   
REMARK 500    SER A  10      100.21    164.05                                   
REMARK 500    PRO A  11     -161.74   -102.09                                   
REMARK 500    PRO A  14     -110.40   -119.77                                   
REMARK 500    VAL A  15       96.40    143.61                                   
REMARK 500    LEU A  18       19.12    -33.24                                   
REMARK 500    HIS A  19       86.69   -160.66                                   
REMARK 500    SER A  20     -178.18   -176.86                                   
REMARK 500    ALA A  24      142.25    -32.45                                   
REMARK 500    HIS A  37       27.07     87.01                                   
REMARK 500    VAL A  38     -156.98   -123.02                                   
REMARK 500    ASN A  39     -154.47   -147.40                                   
REMARK 500    ASN A  41      -89.93    -61.46                                   
REMARK 500    TYR A  42      -35.18    -12.50                                   
REMARK 500    LYS A  46     -178.34    -45.60                                   
REMARK 500    THR A  47       89.60    173.22                                   
REMARK 500    ASN A  48        5.40      8.93                                   
REMARK 500    PHE A  50     -136.57     -9.49                                   
REMARK 500    ILE A  52       85.89    -47.40                                   
REMARK 500    PRO A  53      153.49    -27.62                                   
REMARK 500    GLU A  55       -8.08    -52.04                                   
REMARK 500    ILE A  59      107.61    -48.83                                   
REMARK 500    ILE A  60      -72.09    -54.81                                   
REMARK 500    ARG A  62       15.70    -38.82                                   
REMARK 500    THR A  63       89.75   -175.72                                   
REMARK 500    ALA A  64     -121.00   -172.83                                   
REMARK 500    SER A  65       65.74    121.10                                   
REMARK 500    THR A  70     -131.07    -26.55                                   
REMARK 500    ASP A  71     -137.71   -115.80                                   
REMARK 500    ALA A  73       11.07   -153.23                                   
REMARK 500    ASN A  76      -95.40   -108.93                                   
REMARK 500    ILE A  77      108.98     98.83                                   
REMARK 500    CYS A  81       47.66    -98.33                                   
REMARK 500    THR A  85       88.25    -59.64                                   
REMARK 500    PHE A  86      -56.16      5.72                                   
REMARK 500    GLN A  88      146.95    115.94                                   
REMARK 500    ASN A  92       73.98      6.94                                   
REMARK 500    VAL A  93      -74.56    -84.80                                   
REMARK 500    TYR A  94      -56.50   -146.53                                   
REMARK 500    ILE A  96     -153.00   -147.42                                   
REMARK 500    THR A  97       82.74   -159.61                                   
REMARK 500    ILE A  98      172.71    -58.54                                   
REMARK 500    PRO A 103     -145.40    -35.83                                   
REMARK 500    PRO A 104     -125.41    -59.32                                   
REMARK 500    GLU A 105       89.52    135.39                                   
REMARK 500    LYS A 106      110.76    -31.73                                   
REMARK 500    ASN A 109      -76.46     76.88                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     180 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 ASN A   48     HIS A   49                  145.06                    
REMARK 500 SER A  211     GLU A  212                  149.90                    
REMARK 500 LEU A  214     SER A  215                 -143.56                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 615                                                                      
REMARK 615 ZERO OCCUPANCY ATOM                                                  
REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 615   M RES C  SSEQI                                                     
REMARK 615     NAG H     1                                                      
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3L5I   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3L5J   RELATED DB: PDB                                   
DBREF  3L5H A    2   590  UNP    P40189   IL6RB_HUMAN     24    612             
SEQRES   1 A  589  LEU LEU ASP PRO CYS GLY TYR ILE SER PRO GLU SER PRO          
SEQRES   2 A  589  VAL VAL GLN LEU HIS SER ASN PHE THR ALA VAL CYS VAL          
SEQRES   3 A  589  LEU LYS GLU LYS CYS MET ASP TYR PHE HIS VAL ASN ALA          
SEQRES   4 A  589  ASN TYR ILE VAL TRP LYS THR ASN HIS PHE THR ILE PRO          
SEQRES   5 A  589  LYS GLU GLN TYR THR ILE ILE ASN ARG THR ALA SER SER          
SEQRES   6 A  589  VAL THR PHE THR ASP ILE ALA SER LEU ASN ILE GLN LEU          
SEQRES   7 A  589  THR CYS ASN ILE LEU THR PHE GLY GLN LEU GLU GLN ASN          
SEQRES   8 A  589  VAL TYR GLY ILE THR ILE ILE SER GLY LEU PRO PRO GLU          
SEQRES   9 A  589  LYS PRO LYS ASN LEU SER CYS ILE VAL ASN GLU GLY LYS          
SEQRES  10 A  589  LYS MET ARG CYS GLU TRP ASP GLY GLY ARG GLU THR HIS          
SEQRES  11 A  589  LEU GLU THR ASN PHE THR LEU LYS SER GLU TRP ALA THR          
SEQRES  12 A  589  HIS LYS PHE ALA ASP CYS LYS ALA LYS ARG ASP THR PRO          
SEQRES  13 A  589  THR SER CYS THR VAL ASP TYR SER THR VAL TYR PHE VAL          
SEQRES  14 A  589  ASN ILE GLU VAL TRP VAL GLU ALA GLU ASN ALA LEU GLY          
SEQRES  15 A  589  LYS VAL THR SER ASP HIS ILE ASN PHE ASP PRO VAL TYR          
SEQRES  16 A  589  LYS VAL LYS PRO ASN PRO PRO HIS ASN LEU SER VAL ILE          
SEQRES  17 A  589  ASN SER GLU GLU LEU SER SER ILE LEU LYS LEU THR TRP          
SEQRES  18 A  589  THR ASN PRO SER ILE LYS SER VAL ILE ILE LEU LYS TYR          
SEQRES  19 A  589  ASN ILE GLN TYR ARG THR LYS ASP ALA SER THR TRP SER          
SEQRES  20 A  589  GLN ILE PRO PRO GLU ASP THR ALA SER THR ARG SER SER          
SEQRES  21 A  589  PHE THR VAL GLN ASP LEU LYS PRO PHE THR GLU TYR VAL          
SEQRES  22 A  589  PHE ARG ILE ARG CYS MET LYS GLU ASP GLY LYS GLY TYR          
SEQRES  23 A  589  TRP SER ASP TRP SER GLU GLU ALA SER GLY ILE THR TYR          
SEQRES  24 A  589  GLU ASP ARG PRO SER LYS ALA PRO SER PHE TRP TYR LYS          
SEQRES  25 A  589  ILE ASP PRO SER HIS THR GLN GLY TYR ARG THR VAL GLN          
SEQRES  26 A  589  LEU VAL TRP LYS THR LEU PRO PRO PHE GLU ALA ASN GLY          
SEQRES  27 A  589  LYS ILE LEU ASP TYR GLU VAL THR LEU THR ARG TRP LYS          
SEQRES  28 A  589  SER HIS LEU GLN ASN TYR THR VAL ASN ALA THR LYS LEU          
SEQRES  29 A  589  THR VAL ASN LEU THR ASN ASP ARG TYR LEU ALA THR LEU          
SEQRES  30 A  589  THR VAL ARG ASN LEU VAL GLY LYS SER ASP ALA ALA VAL          
SEQRES  31 A  589  LEU THR ILE PRO ALA CYS ASP PHE GLN ALA THR HIS PRO          
SEQRES  32 A  589  VAL MET ASP LEU LYS ALA PHE PRO LYS ASP ASN MET LEU          
SEQRES  33 A  589  TRP VAL GLU TRP THR THR PRO ARG GLU SER VAL LYS LYS          
SEQRES  34 A  589  TYR ILE LEU GLU TRP CYS VAL LEU SER ASP LYS ALA PRO          
SEQRES  35 A  589  CYS ILE THR ASP TRP GLN GLN GLU ASP GLY THR VAL HIS          
SEQRES  36 A  589  ARG THR TYR LEU ARG GLY ASN LEU ALA GLU SER LYS CYS          
SEQRES  37 A  589  TYR LEU ILE THR VAL THR PRO VAL TYR ALA ASP GLY PRO          
SEQRES  38 A  589  GLY SER PRO GLU SER ILE LYS ALA TYR LEU LYS GLN ALA          
SEQRES  39 A  589  PRO PRO SER LYS GLY PRO THR VAL ARG THR LYS LYS VAL          
SEQRES  40 A  589  GLY LYS ASN GLU ALA VAL LEU GLU TRP ASP GLN LEU PRO          
SEQRES  41 A  589  VAL ASP VAL GLN ASN GLY PHE ILE ARG ASN TYR THR ILE          
SEQRES  42 A  589  PHE TYR ARG THR ILE ILE GLY ASN GLU THR ALA VAL ASN          
SEQRES  43 A  589  VAL ASP SER SER HIS THR GLU TYR THR LEU SER SER LEU          
SEQRES  44 A  589  THR SER ASP THR LEU TYR MET VAL ARG MET ALA ALA TYR          
SEQRES  45 A  589  THR ASP GLU GLY GLY LYS ASP GLY PRO GLU PHE THR PHE          
SEQRES  46 A  589  THR THR PRO LYS                                              
MODRES 3L5H ASN A  361  ASN  GLYCOSYLATION SITE                                 
MODRES 3L5H ASN A  531  ASN  GLYCOSYLATION SITE                                 
MODRES 3L5H ASN A  205  ASN  GLYCOSYLATION SITE                                 
MODRES 3L5H ASN A   61  ASN  GLYCOSYLATION SITE                                 
MODRES 3L5H ASN A  357  ASN  GLYCOSYLATION SITE                                 
MODRES 3L5H ASN A   21  ASN  GLYCOSYLATION SITE                                 
HET    NAG  B   1      14                                                       
HET    NAG  B   2      14                                                       
HET    NAG  C   1      14                                                       
HET    NAG  C   2      14                                                       
HET    BMA  C   3      11                                                       
HET    BMA  C   4      11                                                       
HET    NAG  D   1      14                                                       
HET    NAG  D   2      14                                                       
HET    NAG  E   1      14                                                       
HET    NAG  E   2      14                                                       
HET    BMA  E   3      11                                                       
HET    NAG  F   1      14                                                       
HET    NAG  F   2      14                                                       
HET    BMA  F   3      11                                                       
HET    BMA  F   4      11                                                       
HET    NAG  G   1      14                                                       
HET    FUC  G   2      10                                                       
HET    NAG  H   1      14                                                       
HET    NAG  H   2      14                                                       
HET    SO4  A   1       5                                                       
HET    SO4  A 591       5                                                       
HET    SO4  A 592       5                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     BMA BETA-D-MANNOPYRANOSE                                             
HETNAM     FUC ALPHA-L-FUCOPYRANOSE                                             
HETNAM     SO4 SULFATE ION                                                      
FORMUL   2  NAG    13(C8 H15 N O6)                                              
FORMUL   3  BMA    5(C6 H12 O6)                                                 
FORMUL   7  FUC    C6 H12 O5                                                    
FORMUL   9  SO4    3(O4 S 2-)                                                   
HELIX    1   1 PRO A   53  TYR A   57  5                                   5    
HELIX    2   2 ASP A  193  TYR A  196  5                                   4    
HELIX    3   3 PRO A  225  VAL A  230  5                                   6    
HELIX    4   4 PRO A  521  ASN A  526  1                                   6    
SHEET    1   A 3 MET A 120  ASP A 125  0                                        
SHEET    2   A 3 LYS A 108  ASN A 115 -1  N  ILE A 113   O  ARG A 121           
SHEET    3   A 3 VAL A 198  LYS A 199  1  O  LYS A 199   N  VAL A 114           
SHEET    1   B 3 CYS A 150  LYS A 151  0                                        
SHEET    2   B 3 THR A 134  LEU A 138 -1  N  LEU A 138   O  CYS A 150           
SHEET    3   B 3 VAL A 176  ASN A 180 -1  O  GLU A 179   N  ASN A 135           
SHEET    1   C 2 ILE A 172  VAL A 174  0                                        
SHEET    2   C 2 ILE A 190  PHE A 192 -1  O  PHE A 192   N  ILE A 172           
SHEET    1   D 3 SER A 207  ILE A 209  0                                        
SHEET    2   D 3 LEU A 218  THR A 221 -1  O  LYS A 219   N  ILE A 209           
SHEET    3   D 3 SER A 261  VAL A 264 -1  O  PHE A 262   N  LEU A 220           
SHEET    1   E 2 LEU A 233  THR A 241  0                                        
SHEET    2   E 2 TYR A 273  LYS A 281 -1  O  MET A 280   N  LYS A 234           
SHEET    1   F 3 PHE A 310  LYS A 313  0                                        
SHEET    2   F 3 VAL A 325  TRP A 329 -1  O  GLN A 326   N  LYS A 313           
SHEET    3   F 3 THR A 366  VAL A 367 -1  O  VAL A 367   N  VAL A 325           
SHEET    1   G 2 ASP A 343  LEU A 348  0                                        
SHEET    2   G 2 ALA A 376  ARG A 381 -1  O  THR A 379   N  GLU A 345           
SHEET    1   H 3 LYS A 409  PRO A 412  0                                        
SHEET    2   H 3 LEU A 417  GLU A 420 -1  O  TRP A 418   N  PHE A 411           
SHEET    3   H 3 ARG A 457  TYR A 459 -1  O  THR A 458   N  VAL A 419           
SHEET    1   I 4 THR A 446  TRP A 448  0                                        
SHEET    2   I 4 GLU A 434  LEU A 438 -1  N  TRP A 435   O  ASP A 447           
SHEET    3   I 4 CYS A 469  VAL A 474 -1  O  CYS A 469   N  LEU A 438           
SHEET    4   I 4 GLU A 486  TYR A 491 -1  O  GLU A 486   N  VAL A 474           
SHEET    1   J 2 VAL A 477  TYR A 478  0                                        
SHEET    2   J 2 GLY A 481  PRO A 482 -1  O  GLY A 481   N  TYR A 478           
SHEET    1   K 2 THR A 505  LYS A 506  0                                        
SHEET    2   K 2 VAL A 514  LEU A 515 -1  O  VAL A 514   N  LYS A 506           
SHEET    1   L 4 VAL A 546  VAL A 548  0                                        
SHEET    2   L 4 ILE A 529  ILE A 534 -1  N  TYR A 532   O  VAL A 548           
SHEET    3   L 4 MET A 570  THR A 574 -1  O  ALA A 571   N  THR A 533           
SHEET    4   L 4 GLY A 577  ASP A 580 -1  O  GLY A 577   N  THR A 574           
SHEET    1   M 2 TYR A 566  MET A 567  0                                        
SHEET    2   M 2 THR A 585  PHE A 586 -1  O  PHE A 586   N  TYR A 566           
SSBOND   1 CYS A    6    CYS A   32                          1555   1555  2.04  
SSBOND   2 CYS A   26    CYS A   81                          1555   1555  2.06  
SSBOND   3 CYS A  112    CYS A  122                          1555   1555  2.08  
SSBOND   4 CYS A  150    CYS A  160                          1555   1555  2.07  
SSBOND   5 CYS A  436    CYS A  444                          1555   1555  2.07  
LINK         ND2 ASN A  21                 C1  NAG H   1     1555   1555  1.54  
LINK         ND2 ASN A  61                 C1  NAG D   1     1555   1555  1.46  
LINK         ND2 ASN A 135                 C1  NAG C   1     1555   1555  1.45  
LINK         ND2 ASN A 205                 C1  NAG B   1     1555   1555  1.46  
LINK         ND2 ASN A 357                 C1  NAG G   1     1555   1555  1.48  
LINK         ND2 ASN A 361                 C1  NAG E   1     1555   1555  1.43  
LINK         ND2 ASN A 531                 C1  NAG F   1     1555   1555  1.45  
LINK         O4  NAG B   1                 C1  NAG B   2     1555   1555  1.50  
LINK         O4  NAG C   1                 C1  NAG C   2     1555   1555  1.44  
LINK         O4  NAG C   2                 C1  BMA C   3     1555   1555  1.44  
LINK         O4  BMA C   3                 C1  BMA C   4     1555   1555  1.45  
LINK         O4  NAG D   1                 C1  NAG D   2     1555   1555  1.45  
LINK         O4  NAG E   1                 C1  NAG E   2     1555   1555  1.44  
LINK         O4  NAG E   2                 C1  BMA E   3     1555   1555  1.46  
LINK         O4  NAG F   1                 C1  NAG F   2     1555   1555  1.44  
LINK         O4  NAG F   2                 C1  BMA F   3     1555   1555  1.45  
LINK         O4  BMA F   3                 C1  BMA F   4     1555   1555  1.45  
LINK         O6  NAG G   1                 C1  FUC G   2     1555   1555  1.46  
LINK         O4  NAG H   1                 C1  NAG H   2     1555   1555  1.45  
CISPEP   1 SER A   10    PRO A   11          0       -15.46                     
CISPEP   2 GLY A  385    LYS A  386          0         9.86                     
CISPEP   3 LYS A  413    ASP A  414          0         1.63                     
CRYST1   89.001   51.821  167.157  90.00 102.17  90.00 P 1 21 1      2          
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      0.011236  0.000000  0.002423        0.00000                         
SCALE2      0.000000  0.019297  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006120        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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