GenomeNet

Database: PDB
Entry: 6C7Y
LinkDB: 6C7Y
Original site: 6C7Y 
HEADER    SIGNALING PROTEIN, TRANSFERASE/INHIBITOR23-JAN-18   6C7Y              
TITLE     CRYSTAL STRUCTURE OF INHIBITORY PROTEIN SOCS1 IN COMPLEX WITH JAK1    
TITLE    2 KINASE DOMAIN                                                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TYROSINE-PROTEIN KINASE JAK1;                              
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: KINASE DOMAIN (UNP RESIDUES 869-1153);                     
COMPND   5 SYNONYM: JANUS KINASE 1, JAK-1;                                      
COMPND   6 EC: 2.7.10.2;                                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: SUPPRESSOR OF CYTOKINE SIGNALING 1;                        
COMPND  10 CHAIN: B;                                                            
COMPND  11 FRAGMENT: UNP RESIDUES 48-164;                                       
COMPND  12 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: JAK1, JAK1A, JAK1B;                                            
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: GALLUS GALLUS;                                  
SOURCE  11 ORGANISM_COMMON: CHICKEN;                                            
SOURCE  12 ORGANISM_TAXID: 9031;                                                
SOURCE  13 GENE: SOCS1;                                                         
SOURCE  14 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  15 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 7108                                        
KEYWDS    KINASE, KINASE INHIBITOR, SIGNALING PROTEIN, TRANSFERASE-INHIBITOR    
KEYWDS   2 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    N.P.D.LIAU,A.LAKTYUSHIN,I.S.LUCET,J.M.MURPHY,S.YAO,K.CALLAGHAN,       
AUTHOR   2 N.A.NICOLA,N.J.KERSHAW,J.J.BABON                                     
REVDAT   2   20-FEB-19 6C7Y    1       REMARK                                   
REVDAT   1   02-MAY-18 6C7Y    0                                                
JRNL        AUTH   N.P.D.LIAU,A.LAKTYUSHIN,I.S.LUCET,J.M.MURPHY,S.YAO,          
JRNL        AUTH 2 E.WHITLOCK,K.CALLAGHAN,N.A.NICOLA,N.J.KERSHAW,J.J.BABON      
JRNL        TITL   THE MOLECULAR BASIS OF JAK/STAT INHIBITION BY SOCS1.         
JRNL        REF    NAT COMMUN                    V.   9  1558 2018              
JRNL        REFN                   ESSN 2041-1723                               
JRNL        PMID   29674694                                                     
JRNL        DOI    10.1038/S41467-018-04013-1                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.11.1_2575                                   
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.61                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 20702                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.210                           
REMARK   3   R VALUE            (WORKING SET) : 0.207                           
REMARK   3   FREE R VALUE                     : 0.241                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.640                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1995                            
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 40.6187 -  6.0174    1.00     1468   158  0.1831 0.2191        
REMARK   3     2  6.0174 -  4.7786    1.00     1386   147  0.1880 0.2066        
REMARK   3     3  4.7786 -  4.1752    1.00     1363   144  0.1607 0.1957        
REMARK   3     4  4.1752 -  3.7938    1.00     1344   143  0.1781 0.2078        
REMARK   3     5  3.7938 -  3.5221    1.00     1327   142  0.2055 0.2538        
REMARK   3     6  3.5221 -  3.3145    1.00     1337   143  0.2108 0.2498        
REMARK   3     7  3.3145 -  3.1486    1.00     1318   141  0.2454 0.2599        
REMARK   3     8  3.1486 -  3.0116    1.00     1319   140  0.2463 0.2959        
REMARK   3     9  3.0116 -  2.8957    1.00     1303   140  0.2687 0.2927        
REMARK   3    10  2.8957 -  2.7958    1.00     1319   140  0.2704 0.3023        
REMARK   3    11  2.7958 -  2.7084    1.00     1294   138  0.2619 0.3245        
REMARK   3    12  2.7084 -  2.6310    1.00     1314   140  0.2764 0.3266        
REMARK   3    13  2.6310 -  2.5617    1.00     1316   141  0.2969 0.3316        
REMARK   3    14  2.5617 -  2.4992    1.00     1299   138  0.3061 0.3474        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.310            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.350           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 54.94                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 86.25                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.001           3165                                  
REMARK   3   ANGLE     :  0.478           4283                                  
REMARK   3   CHIRALITY :  0.038            474                                  
REMARK   3   PLANARITY :  0.003            542                                  
REMARK   3   DIHEDRAL  : 10.054           1881                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 869:921)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.0016  23.4682  -8.4362              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.6711 T22:   0.9861                                     
REMARK   3      T33:   1.1545 T12:   0.4580                                     
REMARK   3      T13:   0.2675 T23:   0.0587                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.3466 L22:   8.6072                                     
REMARK   3      L33:   5.6607 L12:  -1.3265                                     
REMARK   3      L13:   0.7133 L23:   5.3808                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0156 S12:   0.3028 S13:  -1.3322                       
REMARK   3      S21:  -2.1436 S22:   0.2763 S23:  -1.1251                       
REMARK   3      S31:   0.6144 S32:   1.4286 S33:  -0.2302                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 922:1030)                           
REMARK   3    ORIGIN FOR THE GROUP (A): -15.4177  28.5703  -2.0270              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1864 T22:   0.4599                                     
REMARK   3      T33:   1.0039 T12:   0.1823                                     
REMARK   3      T13:   0.0180 T23:   0.1079                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.9333 L22:   3.6539                                     
REMARK   3      L33:   3.6970 L12:   0.4625                                     
REMARK   3      L13:  -1.0078 L23:   0.1557                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1606 S12:  -0.0966 S13:  -1.7508                       
REMARK   3      S21:  -0.6226 S22:   0.1886 S23:  -0.0782                       
REMARK   3      S31:   1.5664 S32:   0.4520 S33:  -0.1450                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 1031:1153)                          
REMARK   3    ORIGIN FOR THE GROUP (A): -21.4754  45.7901  -2.7854              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4419 T22:   0.3164                                     
REMARK   3      T33:   0.3491 T12:   0.0115                                     
REMARK   3      T13:  -0.0310 T23:   0.0402                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5070 L22:   4.6465                                     
REMARK   3      L33:   5.4773 L12:   0.1134                                     
REMARK   3      L13:   0.2093 L23:  -1.3854                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0945 S12:  -0.1179 S13:  -0.4156                       
REMARK   3      S21:  -0.7725 S22:  -0.0173 S23:   0.2685                       
REMARK   3      S31:   0.6627 S32:  -0.0372 S33:  -0.0552                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: (CHAIN B AND RESID 52:168)                             
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.1893  66.7876  -9.8764              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0289 T22:   0.8288                                     
REMARK   3      T33:   0.7413 T12:  -0.3052                                     
REMARK   3      T13:   0.4366 T23:  -0.1528                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5576 L22:   2.7306                                     
REMARK   3      L33:   6.9051 L12:   1.0173                                     
REMARK   3      L13:  -2.7797 L23:  -2.7031                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.7604 S12:  -0.4761 S13:   0.3518                       
REMARK   3      S21:   0.0435 S22:  -0.0206 S23:  -0.6851                       
REMARK   3      S31:  -1.7113 S32:   1.3348 S33:  -0.3490                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6C7Y COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-JAN-18.                  
REMARK 100 THE DEPOSITION ID IS D_1000231332.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-OCT-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 77                                 
REMARK 200  PH                             : 7.0                                
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) : 0.9537                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 20768                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.613                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 8.268                              
REMARK 200  R MERGE                    (I) : 0.11300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.7700                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.56                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 8.42                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.70100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.660                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: PDB ENTRIES 6C5X & 3EYH                              
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 60.17                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.09                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM HEPES PH 7.0, 14% (W/V) PEG8000,   
REMARK 280  100MM MAGNESIUM ACETATE, 2MM TCEP, VAPOR DIFFUSION, HANGING DROP,   
REMARK 280  TEMPERATURE 281K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -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 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       80.71900            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       41.96300            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       41.96300            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       40.35950            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       41.96300            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       41.96300            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      121.07850            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       41.96300            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       41.96300            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       40.35950            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       41.96300            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       41.96300            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      121.07850            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       80.71900            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4530 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 17780 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -30.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
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     ASP A   895                                                      
REMARK 465     PRO A   896                                                      
REMARK 465     GLU A   897                                                      
REMARK 465     GLU A   913                                                      
REMARK 465     SER A   914                                                      
REMARK 465     GLY A   915                                                      
REMARK 465     GLY A   916                                                      
REMARK 465     ASN A   917                                                      
REMARK 465     ASP A   947                                                      
REMARK 465     GLY A   948                                                      
REMARK 465     GLY A   949                                                      
REMARK 465     ASN A   950                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU A 871    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 872    CG   CD   CE   NZ                                   
REMARK 470     ARG A 873    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     PHE A 874    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LEU A 875    CG   CD1  CD2                                       
REMARK 470     LYS A 876    CG   CD   CE   NZ                                   
REMARK 470     ARG A 877    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 888    CD   CE   NZ                                        
REMARK 470     ARG A 893    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     TYR A 894    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     THR A 901    OG1  CG2                                            
REMARK 470     GLU A 903    CG   CD   OE1  OE2                                  
REMARK 470     VAL A 905    CG1  CG2                                            
REMARK 470     LYS A 911    CG   CD   CE   NZ                                   
REMARK 470     LYS A 923    CD   CE   NZ                                        
REMARK 470     GLU A 927    CD   OE1  OE2                                       
REMARK 470     ARG A 930    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE A 943    CG1  CG2  CD1                                       
REMARK 470     LYS A 978    CD   CE   NZ                                        
REMARK 470     LYS A 982    CG   CD   CE   NZ                                   
REMARK 470     GLU B 142    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 149    CG   CD   CE   NZ                                   
REMARK 470     GLU B 152    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 159    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 160    CG   CD   CE   NZ                                   
REMARK 470     LEU B 162    CG   CD1  CD2                                       
REMARK 470     LYS B 168    CG   CD   CE   NZ                                   
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    ILE A 878      -73.52    -71.61                                   
REMARK 500    LYS A 911       77.54     55.72                                   
REMARK 500    TYR A 933       87.09   -153.19                                   
REMARK 500    LYS A 941      -73.05   -112.40                                   
REMARK 500    ASP A1003       37.47   -157.91                                   
REMARK 500    ASP A1021       84.96     58.49                                   
REMARK 500    PHE B 112      -69.54    -90.41                                   
REMARK 500    THR B 119     -162.82   -105.35                                   
REMARK 500    VAL B 163      -47.62   -141.66                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1202  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN A1008   OD1                                                    
REMARK 620 2 ASP A1021   OD2  84.0                                              
REMARK 620 3 ADP A1201   O3B 171.3  88.8                                        
REMARK 620 4 ADP A1201   O1A  77.7  82.9  96.7                                  
REMARK 620 5 HOH A1302   O    72.0 155.2 114.6  86.1                            
REMARK 620 6 HOH A1317   O   113.2  92.2  71.8 167.7 102.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1203  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A1021   OD1                                                    
REMARK 620 2 ASP A1021   OD2  59.9                                              
REMARK 620 3 ADP A1201   O2B  75.0  82.1                                        
REMARK 620 4 ADP A1201   O3B 120.3  79.2  56.7                                  
REMARK 620 5 HOH A1325   O   102.3 161.9  96.4 115.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ADP A 1201                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1203                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 1204                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 1205                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT B 202                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 6C5X   RELATED DB: PDB                                   
REMARK 900 SOCS1 IN COMPLEX WITH ELONGIN B AND ELONGIN C                        
DBREF  6C7Y A  869  1153  UNP    P23458   JAK1_HUMAN     869   1153             
DBREF  6C7Y B   52   168  UNP    B6RCQ2   B6RCQ2_CHICK    48    164             
SEQADV 6C7Y ALA A  868  UNP  P23458              EXPRESSION TAG                 
SEQRES   1 A  286  ALA HIS PHE GLU LYS ARG PHE LEU LYS ARG ILE ARG ASP          
SEQRES   2 A  286  LEU GLY GLU GLY HIS PHE GLY LYS VAL GLU LEU CYS ARG          
SEQRES   3 A  286  TYR ASP PRO GLU GLY ASP ASN THR GLY GLU GLN VAL ALA          
SEQRES   4 A  286  VAL LYS SER LEU LYS PRO GLU SER GLY GLY ASN HIS ILE          
SEQRES   5 A  286  ALA ASP LEU LYS LYS GLU ILE GLU ILE LEU ARG ASN LEU          
SEQRES   6 A  286  TYR HIS GLU ASN ILE VAL LYS TYR LYS GLY ILE CYS THR          
SEQRES   7 A  286  GLU ASP GLY GLY ASN GLY ILE LYS LEU ILE MET GLU PHE          
SEQRES   8 A  286  LEU PRO SER GLY SER LEU LYS GLU TYR LEU PRO LYS ASN          
SEQRES   9 A  286  LYS ASN LYS ILE ASN LEU LYS GLN GLN LEU LYS TYR ALA          
SEQRES  10 A  286  VAL GLN ILE CYS LYS GLY MET ASP TYR LEU GLY SER ARG          
SEQRES  11 A  286  GLN TYR VAL HIS ARG ASP LEU ALA ALA ARG ASN VAL LEU          
SEQRES  12 A  286  VAL GLU SER GLU HIS GLN VAL LYS ILE GLY ASP PHE GLY          
SEQRES  13 A  286  LEU THR LYS ALA ILE GLU THR ASP LYS GLU TYR PTR THR          
SEQRES  14 A  286  VAL LYS ASP ASP ARG ASP SER PRO VAL PHE TRP TYR ALA          
SEQRES  15 A  286  PRO GLU CYS LEU MET GLN SER LYS PHE TYR ILE ALA SER          
SEQRES  16 A  286  ASP VAL TRP SER PHE GLY VAL THR LEU HIS GLU LEU LEU          
SEQRES  17 A  286  THR TYR CYS ASP SER ASP SER SER PRO MET ALA LEU PHE          
SEQRES  18 A  286  LEU LYS MET ILE GLY PRO THR HIS GLY GLN MET THR VAL          
SEQRES  19 A  286  THR ARG LEU VAL ASN THR LEU LYS GLU GLY LYS ARG LEU          
SEQRES  20 A  286  PRO CYS PRO PRO ASN CYS PRO ASP GLU VAL TYR GLN LEU          
SEQRES  21 A  286  MET ARG LYS CYS TRP GLU PHE GLN PRO SER ASN ARG THR          
SEQRES  22 A  286  SER PHE GLN ASN LEU ILE GLU GLY PHE GLU ALA LEU LEU          
SEQRES   1 B  117  SER THR HIS PHE ARG THR PHE ARG SER GLN ALA ASP PHE          
SEQRES   2 B  117  SER SER ILE THR ARG ALA SER SER LEU LEU ASP ALA CYS          
SEQRES   3 B  117  GLY PHE TYR TRP GLY PRO LEU THR VAL SER ALA ALA HIS          
SEQRES   4 B  117  GLU LYS LEU LYS SER GLU PRO GLU GLY THR PHE LEU ILE          
SEQRES   5 B  117  ARG ASP SER THR GLN LYS ASN CYS PHE PHE ALA ILE SER          
SEQRES   6 B  117  VAL LYS THR ALA THR GLY PRO THR SER ILE ARG ILE ASN          
SEQRES   7 B  117  PHE GLN THR GLY ARG PHE SER LEU ASP GLY SER LYS GLU          
SEQRES   8 B  117  THR PHE ASP CYS LEU PHE LYS LEU LEU GLU HIS TYR LEU          
SEQRES   9 B  117  SER SER PRO ARG LYS VAL LEU VAL THR PRO LEU ARG LYS          
MODRES 6C7Y PTR A 1035  TYR  MODIFIED RESIDUE                                   
HET    PTR  A1035      25                                                       
HET    ADP  A1201      27                                                       
HET     MG  A1202       1                                                       
HET     MG  A1203       1                                                       
HET    EDO  A1204       4                                                       
HET    EDO  A1205       4                                                       
HET    EDO  B 201       4                                                       
HET    ACT  B 202       4                                                       
HETNAM     PTR O-PHOSPHOTYROSINE                                                
HETNAM     ADP ADENOSINE-5'-DIPHOSPHATE                                         
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     ACT ACETATE ION                                                      
HETSYN     PTR PHOSPHONOTYROSINE                                                
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   1  PTR    C9 H12 N O6 P                                                
FORMUL   3  ADP    C10 H15 N5 O10 P2                                            
FORMUL   4   MG    2(MG 2+)                                                     
FORMUL   6  EDO    3(C2 H6 O2)                                                  
FORMUL   9  ACT    C2 H3 O2 1-                                                  
FORMUL  10  HOH   *35(H2 O)                                                     
HELIX    1 AA1 GLU A  871  LEU A  875  5                                   5    
HELIX    2 AA2 ILE A  919  LEU A  932  1                                  14    
HELIX    3 AA3 SER A  963  LEU A  968  1                                   6    
HELIX    4 AA4 ASN A  976  ARG A  997  1                                  22    
HELIX    5 AA5 ALA A 1005  ARG A 1007  5                                   3    
HELIX    6 AA6 PRO A 1044  TYR A 1048  5                                   5    
HELIX    7 AA7 ALA A 1049  SER A 1056  1                                   8    
HELIX    8 AA8 TYR A 1059  THR A 1076  1                                  18    
HELIX    9 AA9 SER A 1083  GLY A 1093  1                                  11    
HELIX   10 AB1 GLN A 1098  GLU A 1110  1                                  13    
HELIX   11 AB2 PRO A 1121  CYS A 1131  1                                  11    
HELIX   12 AB3 GLN A 1135  ARG A 1139  5                                   5    
HELIX   13 AB4 SER A 1141  ALA A 1151  1                                  11    
HELIX   14 AB5 SER B   60  CYS B   77  1                                  18    
HELIX   15 AB6 THR B   85  LYS B   94  1                                  10    
HELIX   16 AB7 CYS B  146  LEU B  155  1                                  10    
SHEET    1 AA1 5 ARG A 879  GLU A 883  0                                        
SHEET    2 AA1 5 LYS A 888  TYR A 894 -1  O  VAL A 889   N  LEU A 881           
SHEET    3 AA1 5 GLU A 903  SER A 909 -1  O  VAL A 907   N  GLU A 890           
SHEET    4 AA1 5 LYS A 953  GLU A 957 -1  O  LEU A 954   N  LYS A 908           
SHEET    5 AA1 5 TYR A 940  CYS A 944 -1  N  CYS A 944   O  LYS A 953           
SHEET    1 AA2 2 TYR A 999  VAL A1000  0                                        
SHEET    2 AA2 2 LYS A1026  ALA A1027 -1  O  LYS A1026   N  VAL A1000           
SHEET    1 AA3 2 VAL A1009  VAL A1011  0                                        
SHEET    2 AA3 2 VAL A1017  ILE A1019 -1  O  LYS A1018   N  LEU A1010           
SHEET    1 AA4 2 PTR A1035  THR A1036  0                                        
SHEET    2 AA4 2 LYS A1057  PHE A1058 -1  O  PHE A1058   N  PTR A1035           
SHEET    1 AA5 5 ARG B 134  LEU B 137  0                                        
SHEET    2 AA5 5 GLY B 122  GLN B 131 -1  N  ASN B 129   O  SER B 136           
SHEET    3 AA5 5 PHE B 113  THR B 119 -1  N  VAL B 117   O  THR B 124           
SHEET    4 AA5 5 THR B 100  ASP B 105 -1  N  ARG B 104   O  ALA B 114           
SHEET    5 AA5 5 THR B 164  PRO B 165  1  O  THR B 164   N  PHE B 101           
LINK         OD1 ASN A1008                MG    MG A1202     1555   1555  2.18  
LINK         OD1 ASP A1021                MG    MG A1203     1555   1555  2.03  
LINK         OD2 ASP A1021                MG    MG A1202     1555   1555  2.05  
LINK         OD2 ASP A1021                MG    MG A1203     1555   1555  2.33  
LINK         C   TYR A1034                 N   PTR A1035     1555   1555  1.33  
LINK         C   PTR A1035                 N   THR A1036     1555   1555  1.33  
LINK         O2B ADP A1201                MG    MG A1203     1555   1555  2.47  
LINK         O3B ADP A1201                MG    MG A1202     1555   1555  2.64  
LINK         O3B ADP A1201                MG    MG A1203     1555   1555  2.83  
LINK         O1A ADP A1201                MG    MG A1202     1555   1555  2.36  
LINK        MG    MG A1202                 O   HOH A1302     1555   1555  2.27  
LINK        MG    MG A1202                 O   HOH A1317     1555   1555  2.65  
LINK        MG    MG A1203                 O   HOH A1325     1555   1555  2.48  
SITE     1 AC1 19 GLY A 882  GLY A 884  HIS A 885  PHE A 886                    
SITE     2 AC1 19 GLY A 887  VAL A 889  ALA A 906  LYS A 908                    
SITE     3 AC1 19 MET A 956  GLU A 957  LEU A 959  SER A 963                    
SITE     4 AC1 19 GLU A 966  ARG A1007  ASN A1008  LEU A1010                    
SITE     5 AC1 19 ASP A1021   MG A1202   MG A1203                               
SITE     1 AC2  6 ASN A1008  ASP A1021  ADP A1201   MG A1203                    
SITE     2 AC2  6 HOH A1302  HOH A1317                                          
SITE     1 AC3  5 ASP A1003  ASP A1021  ADP A1201   MG A1202                    
SITE     2 AC3  5 HOH A1325                                                     
SITE     1 AC4  5 LEU A1108  LYS A1109  GLY A1111  ARG A1113                    
SITE     2 AC4  5 PHE A1134                                                     
SITE     1 AC5  6 GLN A1055  LYS A1057  HOH A1316  ARG B  59                    
SITE     2 AC5  6 SER B  60  GLN B  61                                          
SITE     1 AC6  3 GLN A1098  ARG B  59  ASP B  63                               
SITE     1 AC7  4 VAL B  86  ARG B 104  SER B 106  THR B 107                    
CRYST1   83.926   83.926  161.438  90.00  90.00  90.00 P 41 21 2     8          
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      0.011915  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011915  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006194        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system