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Database: PDB
Entry: 4MKP
LinkDB: 4MKP
Original site: 4MKP 
HEADER    TRANSFERASE                             05-SEP-13   4MKP              
TITLE     CRYSTAL STRUCTURE OF HUMAN CGAS APO FORM                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CYCLIC GMP-AMP SYNTHASE;                                   
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 161-522;                                      
COMPND   5 SYNONYM: CGAMP SYNTHASE, CGAS, H-CGAS, MAB-21 DOMAIN-CONTAINING      
COMPND   6 PROTEIN 1;                                                           
COMPND   7 EC: 2.7.7.-;                                                         
COMPND   8 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: MB21D1;                                                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: MODIFIED PE-SUMO                          
KEYWDS    NUCLEOTIDYLTRANSFERASE, TRANSFERASE                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.KATO,R.ISHII,R.ISHITANI,O.NUREKI                                    
REVDAT   1   30-OCT-13 4MKP    0                                                
JRNL        AUTH   K.KATO,R.ISHII,E.GOTO,R.ISHITANI,F.TOKUNAGA,O.NUREKI         
JRNL        TITL   STRUCTURAL AND FUNCTIONAL ANALYSES OF DNA-SENSING AND IMMUNE 
JRNL        TITL 2 ACTIVATION BY HUMAN CGAS                                     
JRNL        REF    PLOS ONE                      V.   8 76983 2013              
JRNL        REFN                   ESSN 1932-6203                               
JRNL        PMID   24116191                                                     
JRNL        DOI    10.1371/JOURNAL.PONE.0076983                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.95 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.7.2_869)                    
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.95                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 42.88                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 25996                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.207                           
REMARK   3   R VALUE            (WORKING SET) : 0.204                           
REMARK   3   FREE R VALUE                     : 0.252                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.040                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1311                            
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 42.8885 -  4.0615    0.99     2968   144  0.2120 0.2427        
REMARK   3     2  4.0615 -  3.2241    0.99     2808   160  0.1913 0.2435        
REMARK   3     3  3.2241 -  2.8166    0.98     2775   151  0.2055 0.2696        
REMARK   3     4  2.8166 -  2.5591    0.98     2753   132  0.2035 0.2517        
REMARK   3     5  2.5591 -  2.3757    0.97     2680   173  0.1961 0.2604        
REMARK   3     6  2.3757 -  2.2357    0.98     2705   154  0.1895 0.2484        
REMARK   3     7  2.2357 -  2.1237    0.97     2689   138  0.2052 0.2631        
REMARK   3     8  2.1237 -  2.0313    0.97     2691   136  0.2186 0.2591        
REMARK   3     9  2.0313 -  1.9531    0.95     2616   123  0.2442 0.2950        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.10                                          
REMARK   3   SHRINKAGE RADIUS   : 0.86                                          
REMARK   3   K_SOL              : 0.36                                          
REMARK   3   B_SOL              : 54.92                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.390            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.450           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 32.26                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 50.73                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.60490                                             
REMARK   3    B22 (A**2) : -5.39650                                             
REMARK   3    B33 (A**2) : 6.00150                                              
REMARK   3    B12 (A**2) : -0.00000                                             
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.011           2605                                  
REMARK   3   ANGLE     :  1.246           3519                                  
REMARK   3   CHIRALITY :  0.086            400                                  
REMARK   3   PLANARITY :  0.004            441                                  
REMARK   3   DIHEDRAL  : 17.134            953                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN A AND (RESSEQ 162:197)                           
REMARK   3    ORIGIN FOR THE GROUP (A):   6.4997  26.2593  16.2489              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4697 T22:   0.3045                                     
REMARK   3      T33:   0.3346 T12:   0.0170                                     
REMARK   3      T13:   0.0635 T23:   0.0194                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9036 L22:   2.7257                                     
REMARK   3      L33:   8.8226 L12:  -0.3218                                     
REMARK   3      L13:   0.3651 L23:   2.4341                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1777 S12:   0.3241 S13:   0.3742                       
REMARK   3      S21:  -0.4341 S22:  -0.1521 S23:   0.0981                       
REMARK   3      S31:  -0.7472 S32:  -0.3951 S33:  -0.1140                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN A AND (RESSEQ 198:272)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  16.5176   9.6215   0.2165              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4148 T22:   0.4670                                     
REMARK   3      T33:   0.2230 T12:   0.1028                                     
REMARK   3      T13:   0.0819 T23:  -0.0444                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.7394 L22:   3.4690                                     
REMARK   3      L33:   3.8940 L12:  -0.3226                                     
REMARK   3      L13:   0.2828 L23:  -0.6667                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0188 S12:   0.3863 S13:  -0.2090                       
REMARK   3      S21:  -0.6189 S22:  -0.0610 S23:  -0.0991                       
REMARK   3      S31:  -0.1450 S32:   0.1621 S33:   0.1576                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN A AND (RESSEQ 273:388)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  14.7526   8.9656   7.2602              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3290 T22:   0.3509                                     
REMARK   3      T33:   0.2418 T12:   0.0333                                     
REMARK   3      T13:   0.0784 T23:  -0.0122                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4736 L22:   2.1660                                     
REMARK   3      L33:   2.5340 L12:  -0.0178                                     
REMARK   3      L13:  -0.4621 L23:  -0.3649                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1667 S12:   0.5095 S13:   0.0825                       
REMARK   3      S21:  -0.5885 S22:  -0.0824 S23:  -0.3235                       
REMARK   3      S31:  -0.0965 S32:   0.3440 S33:  -0.0181                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN A AND (RESSEQ 389:521)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  19.2988  13.9010  27.6920              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1453 T22:   0.2587                                     
REMARK   3      T33:   0.2013 T12:  -0.0234                                     
REMARK   3      T13:  -0.0435 T23:   0.0072                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6631 L22:   2.6931                                     
REMARK   3      L33:   1.9817 L12:   0.5683                                     
REMARK   3      L13:  -0.3783 L23:   0.3807                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1314 S12:  -0.3628 S13:   0.0885                       
REMARK   3      S21:   0.1267 S22:  -0.0687 S23:  -0.4642                       
REMARK   3      S31:  -0.1400 S32:   0.5811 S33:  -0.0556                       
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 4MKP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 19-SEP-13.                  
REMARK 100 THE RCSB ID CODE IS RCSB082031.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-MAY-13                          
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL41XU                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 26029                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.950                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: 4K96                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 41.12                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.09                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, NH4NO3, NACL, CYMAL-7, PH      
REMARK 280  7.5, VAPOR DIFFUSION, TEMPERATURE 293K                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       4555   X+1/2,-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        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       61.77300            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       24.15550            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       61.77300            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       24.15550            
REMARK 290   SMTRY3   4  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                                     
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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A1164  LIES ON A SPECIAL POSITION.                          
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A   159                                                      
REMARK 465     SER A   160                                                      
REMARK 465     GLY A   161                                                      
REMARK 465     VAL A   218                                                      
REMARK 465     LYS A   219                                                      
REMARK 465     ILE A   220                                                      
REMARK 465     SER A   221                                                      
REMARK 465     ALA A   222                                                      
REMARK 465     ARG A   255                                                      
REMARK 465     ASN A   256                                                      
REMARK 465     PRO A   257                                                      
REMARK 465     LYS A   258                                                      
REMARK 465     GLU A   259                                                      
REMARK 465     ASN A   260                                                      
REMARK 465     ASN A   289                                                      
REMARK 465     ASP A   290                                                      
REMARK 465     ILE A   291                                                      
REMARK 465     LYS A   292                                                      
REMARK 465     ASP A   293                                                      
REMARK 465     THR A   294                                                      
REMARK 465     ASP A   295                                                      
REMARK 465     VAL A   296                                                      
REMARK 465     ILE A   297                                                      
REMARK 465     MET A   298                                                      
REMARK 465     LYS A   299                                                      
REMARK 465     ARG A   300                                                      
REMARK 465     LYS A   301                                                      
REMARK 465     ARG A   302                                                      
REMARK 465     GLY A   303                                                      
REMARK 465     GLY A   304                                                      
REMARK 465     SER A   305                                                      
REMARK 465     HIS A   363                                                      
REMARK 465     ALA A   364                                                      
REMARK 465     LYS A   365                                                      
REMARK 465     GLU A   366                                                      
REMARK 465     GLY A   367                                                      
REMARK 465     ASN A   368                                                      
REMARK 465     GLY A   369                                                      
REMARK 465     PHE A   370                                                      
REMARK 465     ASP A   426                                                      
REMARK 465     LYS A   427                                                      
REMARK 465     PHE A   522                                                      
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     SER A 163    OG                                                  
REMARK 470     ILE A 179    CG1  CG2  CD1                                       
REMARK 470     SER A 180    OG                                                  
REMARK 470     ARG A 196    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN A 210    CG   OD1  ND2                                       
REMARK 470     TYR A 215    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ARG A 236    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 240    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 254    CG   CD   CE   NZ                                   
REMARK 470     LEU A 262    CG   CD1  CD2                                       
REMARK 470     SER A 263    OG                                                  
REMARK 470     GLN A 264    CG   CD   OE1  NE2                                  
REMARK 470     PHE A 265    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLU A 269    CG   CD   OE1  OE2                                  
REMARK 470     ILE A 270    CD1                                                 
REMARK 470     LYS A 275    CG   CD   CE   NZ                                   
REMARK 470     LYS A 279    CG   CD   CE   NZ                                   
REMARK 470     ARG A 281    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 282    CG   CD   CE   NZ                                   
REMARK 470     GLU A 287    CG   CD   OE1  OE2                                  
REMARK 470     ILE A 288    CG1  CG2  CD1                                       
REMARK 470     THR A 309    OG1  CG2                                            
REMARK 470     LEU A 310    CG   CD1  CD2                                       
REMARK 470     GLU A 314    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 315    CG   CD   CE   NZ                                   
REMARK 470     SER A 317    OG                                                  
REMARK 470     GLN A 335    CD   OE1  NE2                                       
REMARK 470     LYS A 350    CD   CE   NZ                                        
REMARK 470     GLN A 371    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 372    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 403    CD   CE   NZ                                        
REMARK 470     GLU A 422    OE1  OE2                                            
REMARK 470     LYS A 425    CG   CD   CE   NZ                                   
REMARK 470     LYS A 428    CG   CD   CE   NZ                                   
REMARK 470     ASP A 431    CG   OD1  OD2                                       
REMARK 470     LYS A 432    CG   CD   CE   NZ                                   
REMARK 470     ARG A 457    CZ   NH1  NH2                                       
REMARK 470     ASN A 494    CG   OD1  ND2                                       
REMARK 470     LYS A 506    CG   CD   CE   NZ                                   
REMARK 470     GLU A 521    CG   CD   OE1  OE2                                  
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    VAL A 206      150.12    -48.61                                   
REMARK 500    ASN A 210       91.47     65.11                                   
REMARK 500    THR A 211     -159.79   -149.75                                   
REMARK 500    ARG A 236      103.35    -25.08                                   
REMARK 500    SER A 243     -136.36     50.06                                   
REMARK 500    ARG A 246      -32.12     71.98                                   
REMARK 500    VAL A 308      -74.58    -72.86                                   
REMARK 500    GLU A 314      107.26    -50.25                                   
REMARK 500    TRP A 343      -67.42   -104.36                                   
REMARK 500    SER A 345      153.94     99.30                                   
REMARK 500    PRO A 361       91.75    -60.71                                   
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 ILE A  312     SER A  313                  147.86                    
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                              ZN A1000  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 390   NE2                                                    
REMARK 620 2 CYS A 396   SG  116.0                                              
REMARK 620 3 CYS A 397   SG  103.9 131.0                                        
REMARK 620 4 CYS A 404   SG   93.9 100.1 104.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1000                 
DBREF  4MKP A  161   522  UNP    Q8N884   CGAS_HUMAN     161    522             
SEQADV 4MKP GLY A  159  UNP  Q8N884              EXPRESSION TAG                 
SEQADV 4MKP SER A  160  UNP  Q8N884              EXPRESSION TAG                 
SEQRES   1 A  364  GLY SER GLY ALA SER LYS LEU ARG ALA VAL LEU GLU LYS          
SEQRES   2 A  364  LEU LYS LEU SER ARG ASP ASP ILE SER THR ALA ALA GLY          
SEQRES   3 A  364  MET VAL LYS GLY VAL VAL ASP HIS LEU LEU LEU ARG LEU          
SEQRES   4 A  364  LYS CYS ASP SER ALA PHE ARG GLY VAL GLY LEU LEU ASN          
SEQRES   5 A  364  THR GLY SER TYR TYR GLU HIS VAL LYS ILE SER ALA PRO          
SEQRES   6 A  364  ASN GLU PHE ASP VAL MET PHE LYS LEU GLU VAL PRO ARG          
SEQRES   7 A  364  ILE GLN LEU GLU GLU TYR SER ASN THR ARG ALA TYR TYR          
SEQRES   8 A  364  PHE VAL LYS PHE LYS ARG ASN PRO LYS GLU ASN PRO LEU          
SEQRES   9 A  364  SER GLN PHE LEU GLU GLY GLU ILE LEU SER ALA SER LYS          
SEQRES  10 A  364  MET LEU SER LYS PHE ARG LYS ILE ILE LYS GLU GLU ILE          
SEQRES  11 A  364  ASN ASP ILE LYS ASP THR ASP VAL ILE MET LYS ARG LYS          
SEQRES  12 A  364  ARG GLY GLY SER PRO ALA VAL THR LEU LEU ILE SER GLU          
SEQRES  13 A  364  LYS ILE SER VAL ASP ILE THR LEU ALA LEU GLU SER LYS          
SEQRES  14 A  364  SER SER TRP PRO ALA SER THR GLN GLU GLY LEU ARG ILE          
SEQRES  15 A  364  GLN ASN TRP LEU SER ALA LYS VAL ARG LYS GLN LEU ARG          
SEQRES  16 A  364  LEU LYS PRO PHE TYR LEU VAL PRO LYS HIS ALA LYS GLU          
SEQRES  17 A  364  GLY ASN GLY PHE GLN GLU GLU THR TRP ARG LEU SER PHE          
SEQRES  18 A  364  SER HIS ILE GLU LYS GLU ILE LEU ASN ASN HIS GLY LYS          
SEQRES  19 A  364  SER LYS THR CYS CYS GLU ASN LYS GLU GLU LYS CYS CYS          
SEQRES  20 A  364  ARG LYS ASP CYS LEU LYS LEU MET LYS TYR LEU LEU GLU          
SEQRES  21 A  364  GLN LEU LYS GLU ARG PHE LYS ASP LYS LYS HIS LEU ASP          
SEQRES  22 A  364  LYS PHE SER SER TYR HIS VAL LYS THR ALA PHE PHE HIS          
SEQRES  23 A  364  VAL CYS THR GLN ASN PRO GLN ASP SER GLN TRP ASP ARG          
SEQRES  24 A  364  LYS ASP LEU GLY LEU CYS PHE ASP ASN CYS VAL THR TYR          
SEQRES  25 A  364  PHE LEU GLN CYS LEU ARG THR GLU LYS LEU GLU ASN TYR          
SEQRES  26 A  364  PHE ILE PRO GLU PHE ASN LEU PHE SER SER ASN LEU ILE          
SEQRES  27 A  364  ASP LYS ARG SER LYS GLU PHE LEU THR LYS GLN ILE GLU          
SEQRES  28 A  364  TYR GLU ARG ASN ASN GLU PHE PRO VAL PHE ASP GLU PHE          
HET     ZN  A1000       1                                                       
HETNAM      ZN ZINC ION                                                         
FORMUL   2   ZN    ZN 2+                                                        
FORMUL   3  HOH   *114(H2 O)                                                    
HELIX    1   1 ALA A  162  LEU A  174  1                                  13    
HELIX    2   2 SER A  175  LYS A  198  1                                  24    
HELIX    3   3 THR A  211  HIS A  217  1                                   7    
HELIX    4   4 LEU A  262  GLN A  264  5                                   3    
HELIX    5   5 SER A  272  ILE A  288  1                                  17    
HELIX    6   6 PRO A  331  GLN A  335  5                                   5    
HELIX    7   7 SER A  345  LEU A  354  1                                  10    
HELIX    8   8 PHE A  379  ASN A  389  1                                  11    
HELIX    9   9 ASN A  399  LYS A  403  5                                   5    
HELIX   10  10 CYS A  405  ARG A  423  1                                  19    
HELIX   11  11 SER A  434  ASN A  449  1                                  16    
HELIX   12  12 GLN A  451  LYS A  458  5                                   8    
HELIX   13  13 ASP A  459  GLU A  478  1                                  20    
HELIX   14  14 ASP A  497  ASN A  514  1                                  18    
HELIX   15  15 GLU A  515  ASP A  520  5                                   6    
SHEET    1   A 7 GLY A 207  LEU A 208  0                                        
SHEET    2   A 7 GLU A 225  GLU A 233 -1  O  LYS A 231   N  GLY A 207           
SHEET    3   A 7 ILE A 316  SER A 326  1  O  SER A 317   N  PHE A 226           
SHEET    4   A 7 PHE A 357  VAL A 360 -1  O  PHE A 357   N  SER A 326           
SHEET    5   A 7 TRP A 375  SER A 378 -1  O  ARG A 376   N  VAL A 360           
SHEET    6   A 7 TYR A 248  PHE A 253 -1  N  TYR A 249   O  TRP A 375           
SHEET    7   A 7 ILE A 237  GLU A 241 -1  N  GLN A 238   O  LYS A 252           
SHEET    1   B 4 GLY A 207  LEU A 208  0                                        
SHEET    2   B 4 GLU A 225  GLU A 233 -1  O  LYS A 231   N  GLY A 207           
SHEET    3   B 4 ILE A 316  SER A 326  1  O  SER A 317   N  PHE A 226           
SHEET    4   B 4 THR A 309  SER A 313 -1  N  THR A 309   O  ILE A 320           
SHEET    1   C 2 LEU A 266  GLU A 267  0                                        
SHEET    2   C 2 ILE A 270  LEU A 271 -1  O  ILE A 270   N  GLU A 267           
LINK         NE2 HIS A 390                ZN    ZN A1000     1555   1555  2.20  
LINK         SG  CYS A 396                ZN    ZN A1000     1555   1555  2.33  
LINK         SG  CYS A 397                ZN    ZN A1000     1555   1555  2.38  
LINK         SG  CYS A 404                ZN    ZN A1000     1555   1555  2.48  
CISPEP   1 PRO A  306    ALA A  307          0        -3.90                     
SITE     1 AC1  4 HIS A 390  CYS A 396  CYS A 397  CYS A 404                    
CRYST1  123.546   48.311   59.565  90.00  90.00  90.00 P 21 21 2     4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.008094  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.020699  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016788        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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