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Database: PDB
Entry: 4DN5
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Original site: 4DN5 
HEADER    TRANSFERASE                             08-FEB-12   4DN5              
TITLE     CRYSTAL STRUCTURE OF NF-KB-INDUCING KINASE (NIK)                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 14;         
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 330-680;                                      
COMPND   5 SYNONYM: NF-KAPPA-BETA-INDUCING KINASE, HSNIK, SERINE/THREONINE-     
COMPND   6 PROTEIN KINASE NIK;                                                  
COMPND   7 EC: 2.7.11.25;                                                       
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: MAP3K14, NF-KB-INDUCING KINASE, NIK;                           
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: SF9;                                    
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PFASTBACHT                                
KEYWDS    NON-RD KINASE, PROTEIN SERINE/THREONINE KINASE, TRANSFERASE, ATP      
KEYWDS   2 BINDING                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    X.MIN,J.LIU,A.SUDOM,N.P.WALKER,Z.WANG                                 
REVDAT   4   17-JUL-13 4DN5    1       JRNL                                     
REVDAT   3   10-JUL-13 4DN5    1       JRNL                                     
REVDAT   2   30-JAN-13 4DN5    1       HETATM                                   
REVDAT   1   27-JUN-12 4DN5    0                                                
JRNL        AUTH   J.LIU,A.SUDOM,X.MIN,Z.CAO,X.GAO,M.AYRES,F.LEE,P.CAO,         
JRNL        AUTH 2 S.JOHNSTONE,O.PLOTNIKOVA,N.WALKER,G.CHEN,Z.WANG              
JRNL        TITL   STRUCTURE OF NUCLEAR FACTOR KAPPA B-INDUCING KINASE DOMAIN   
JRNL        TITL 2 REVEALS A CONSTITUTIVELY ACTIVE CONFORMATION                 
JRNL        REF    J.BIOL.CHEM.                  V. 287 27326 2012              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   22718757                                                     
JRNL        DOI    10.1074/JBC.M112.366658                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.6.0117                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 26957                          
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) : 0.184                           
REMARK   3   R VALUE            (WORKING SET) : 0.182                           
REMARK   3   FREE R VALUE                     : 0.222                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1417                            
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) : 2.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.56                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1922                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.57                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2420                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 125                          
REMARK   3   BIN FREE R VALUE                    : 0.3080                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5128                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 94                                      
REMARK   3   SOLVENT ATOMS            : 70                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 60.40                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 55.86                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -7.04000                                             
REMARK   3    B22 (A**2) : -7.04000                                             
REMARK   3    B33 (A**2) : 14.09000                                             
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  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.094         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.053         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.211         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.213        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.946                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.915                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5337 ; 0.005 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7225 ; 0.997 ; 1.985       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   657 ; 4.732 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   232 ;34.688 ;23.190       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   893 ;15.824 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    44 ;15.774 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   774 ; 0.066 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4024 ; 0.003 ; 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):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
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  TWIN DETAILS                                                        
REMARK   3   NUMBER OF TWIN DOMAINS  : 2                                        
REMARK   3      TWIN DOMAIN   : 1                                               
REMARK   3      TWIN OPERATOR : H, K, L                                         
REMARK   3      TWIN FRACTION : 0.626                                           
REMARK   3      TWIN DOMAIN   : 2                                               
REMARK   3      TWIN OPERATOR : K, H, -L                                        
REMARK   3      TWIN FRACTION : 0.374                                           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN    
REMARK   3  THE INPUT                                                           
REMARK   4                                                                      
REMARK   4 4DN5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-FEB-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB070537.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-AUG-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 90                                 
REMARK 200  PH                             : 5.4                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 5.0.2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : DOUBLE-CRYSTAL, SI(111)            
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 137194                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 47.750                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 4.800                              
REMARK 200  R MERGE                    (I) : 0.06700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.8000                            
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) : 2.64                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.49300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.400                              
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   (%): 53.83                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.66                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 12.5% POLYETHYLENE GLYCOL 3350, 200 MM   
REMARK 280  AMMONIUM SULFATE AND 0.1 M SODIUM CITRATE, PH 5.4, VAPOR            
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 293K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41                             
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,X,Z+1/4                                              
REMARK 290       4555   Y,-X,Z+3/4                                              
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       57.70000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       28.85000            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       86.55000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
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 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6350 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 29040 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.0 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     GLY A   325                                                      
REMARK 465     ALA A   326                                                      
REMARK 465     MET A   327                                                      
REMARK 465     GLY A   328                                                      
REMARK 465     SER A   329                                                      
REMARK 465     LYS A   330                                                      
REMARK 465     PHE A   331                                                      
REMARK 465     PRO A   543                                                      
REMARK 465     ASP A   544                                                      
REMARK 465     GLY A   545                                                      
REMARK 465     LEU A   546                                                      
REMARK 465     GLY A   547                                                      
REMARK 465     LYS A   548                                                      
REMARK 465     ASP A   549                                                      
REMARK 465     LEU A   550                                                      
REMARK 465     LEU A   551                                                      
REMARK 465     THR A   552                                                      
REMARK 465     GLY A   553                                                      
REMARK 465     ASP A   554                                                      
REMARK 465     TYR A   555                                                      
REMARK 465     PRO A   676                                                      
REMARK 465     PRO A   677                                                      
REMARK 465     ASN A   678                                                      
REMARK 465     GLN A   679                                                      
REMARK 465     ALA A   680                                                      
REMARK 465     GLY B   325                                                      
REMARK 465     ALA B   326                                                      
REMARK 465     MET B   327                                                      
REMARK 465     GLY B   328                                                      
REMARK 465     SER B   329                                                      
REMARK 465     LYS B   330                                                      
REMARK 465     PHE B   331                                                      
REMARK 465     SER B   332                                                      
REMARK 465     PRO B   543                                                      
REMARK 465     ASP B   544                                                      
REMARK 465     GLY B   545                                                      
REMARK 465     LEU B   546                                                      
REMARK 465     GLY B   547                                                      
REMARK 465     LYS B   548                                                      
REMARK 465     ASP B   549                                                      
REMARK 465     LEU B   550                                                      
REMARK 465     LEU B   551                                                      
REMARK 465     THR B   552                                                      
REMARK 465     GLY B   553                                                      
REMARK 465     ASP B   554                                                      
REMARK 465     TYR B   555                                                      
REMARK 465     PRO B   676                                                      
REMARK 465     PRO B   677                                                      
REMARK 465     ASN B   678                                                      
REMARK 465     GLN B   679                                                      
REMARK 465     ALA B   680                                                      
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    SER A 365      -15.20   -156.13                                   
REMARK 500    ARG A 368      150.33     70.24                                   
REMARK 500    PRO A 372     -159.79    -75.38                                   
REMARK 500    VAL A 397      -59.49   -127.97                                   
REMARK 500    LEU A 404      126.89     65.95                                   
REMARK 500    ASP A 515       44.51   -144.32                                   
REMARK 500    ASP A 534       82.45     60.95                                   
REMARK 500    TRP A 596      -40.19     69.86                                   
REMARK 500    PRO A 614       49.47    -74.54                                   
REMARK 500    ARG A 666     -134.95     62.60                                   
REMARK 500    GLU B 396      -23.56     74.85                                   
REMARK 500    GLN B 403     -150.45     51.15                                   
REMARK 500    SER B 476      103.88     65.67                                   
REMARK 500    ASP B 515       49.09   -148.12                                   
REMARK 500    ASP B 534       78.55     62.32                                   
REMARK 500    ASP B 574     -154.05   -138.55                                   
REMARK 500    TRP B 596      -44.82     75.75                                   
REMARK 500    PRO B 614       27.66    -65.59                                   
REMARK 500    PRO B 624        4.54    -61.86                                   
REMARK 500    LYS B 662      -32.72   -130.01                                   
REMARK 500    GLU B 668      107.70     59.94                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH B1111        DISTANCE =  5.83 ANGSTROMS                       
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 A1001  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 AGS A1008   O1A                                                    
REMARK 620 2 AGS A1008   O2B  87.8                                              
REMARK 620 3 ASP A 534   OD2  89.7  94.0                                        
REMARK 620 4 ASN A 520   OD1  95.3 174.4  81.4                                  
REMARK 620 5 HOH A1118   O   179.2  92.7  90.8  84.2                            
REMARK 620 6 HOH A1119   O    93.3  93.9 171.6  90.5  86.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B1001  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 AGS B1003   O2A                                                    
REMARK 620 2 AGS B1003   O2B  89.4                                              
REMARK 620 3 HOH B1108   O    91.3 104.7                                        
REMARK 620 4 ASP B 534   OD1  86.9  94.9 160.4                                  
REMARK 620 5 ASN B 520   OD1  89.9 169.2  86.1  74.4                            
REMARK 620 6 HOH B1109   O   169.7  87.7  99.0  83.5  91.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1003                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1004                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1005                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1006                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1007                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AGS A 1008                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 1001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 1002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AGS B 1003                
DBREF  4DN5 A  330   680  UNP    Q99558   M3K14_HUMAN    330    680             
DBREF  4DN5 B  330   680  UNP    Q99558   M3K14_HUMAN    330    680             
SEQADV 4DN5 GLY A  325  UNP  Q99558              EXPRESSION TAG                 
SEQADV 4DN5 ALA A  326  UNP  Q99558              EXPRESSION TAG                 
SEQADV 4DN5 MET A  327  UNP  Q99558              EXPRESSION TAG                 
SEQADV 4DN5 GLY A  328  UNP  Q99558              EXPRESSION TAG                 
SEQADV 4DN5 SER A  329  UNP  Q99558              EXPRESSION TAG                 
SEQADV 4DN5 ASP A  549  UNP  Q99558    SER   549 ENGINEERED MUTATION            
SEQADV 4DN5 GLY B  325  UNP  Q99558              EXPRESSION TAG                 
SEQADV 4DN5 ALA B  326  UNP  Q99558              EXPRESSION TAG                 
SEQADV 4DN5 MET B  327  UNP  Q99558              EXPRESSION TAG                 
SEQADV 4DN5 GLY B  328  UNP  Q99558              EXPRESSION TAG                 
SEQADV 4DN5 SER B  329  UNP  Q99558              EXPRESSION TAG                 
SEQADV 4DN5 ASP B  549  UNP  Q99558    SER   549 ENGINEERED MUTATION            
SEQRES   1 A  356  GLY ALA MET GLY SER LYS PHE SER VAL GLU GLU TYR LEU          
SEQRES   2 A  356  VAL HIS ALA LEU GLN GLY SER VAL SER SER GLY GLN ALA          
SEQRES   3 A  356  HIS SER LEU THR SER LEU ALA LYS THR TRP ALA ALA ARG          
SEQRES   4 A  356  GLY SER ARG SER ARG GLU PRO SER PRO LYS THR GLU ASP          
SEQRES   5 A  356  ASN GLU GLY VAL LEU LEU THR GLU LYS LEU LYS PRO VAL          
SEQRES   6 A  356  ASP TYR GLU TYR ARG GLU GLU VAL HIS TRP ALA THR HIS          
SEQRES   7 A  356  GLN LEU ARG LEU GLY ARG GLY SER PHE GLY GLU VAL HIS          
SEQRES   8 A  356  ARG MET GLU ASP LYS GLN THR GLY PHE GLN CYS ALA VAL          
SEQRES   9 A  356  LYS LYS VAL ARG LEU GLU VAL PHE ARG ALA GLU GLU LEU          
SEQRES  10 A  356  MET ALA CYS ALA GLY LEU THR SER PRO ARG ILE VAL PRO          
SEQRES  11 A  356  LEU TYR GLY ALA VAL ARG GLU GLY PRO TRP VAL ASN ILE          
SEQRES  12 A  356  PHE MET GLU LEU LEU GLU GLY GLY SER LEU GLY GLN LEU          
SEQRES  13 A  356  VAL LYS GLU GLN GLY CYS LEU PRO GLU ASP ARG ALA LEU          
SEQRES  14 A  356  TYR TYR LEU GLY GLN ALA LEU GLU GLY LEU GLU TYR LEU          
SEQRES  15 A  356  HIS SER ARG ARG ILE LEU HIS GLY ASP VAL LYS ALA ASP          
SEQRES  16 A  356  ASN VAL LEU LEU SER SER ASP GLY SER HIS ALA ALA LEU          
SEQRES  17 A  356  CYS ASP PHE GLY HIS ALA VAL CYS LEU GLN PRO ASP GLY          
SEQRES  18 A  356  LEU GLY LYS ASP LEU LEU THR GLY ASP TYR ILE PRO GLY          
SEQRES  19 A  356  THR GLU THR HIS MET ALA PRO GLU VAL VAL LEU GLY ARG          
SEQRES  20 A  356  SER CYS ASP ALA LYS VAL ASP VAL TRP SER SER CYS CYS          
SEQRES  21 A  356  MET MET LEU HIS MET LEU ASN GLY CYS HIS PRO TRP THR          
SEQRES  22 A  356  GLN PHE PHE ARG GLY PRO LEU CYS LEU LYS ILE ALA SER          
SEQRES  23 A  356  GLU PRO PRO PRO VAL ARG GLU ILE PRO PRO SER CYS ALA          
SEQRES  24 A  356  PRO LEU THR ALA GLN ALA ILE GLN GLU GLY LEU ARG LYS          
SEQRES  25 A  356  GLU PRO ILE HIS ARG VAL SER ALA ALA GLU LEU GLY GLY          
SEQRES  26 A  356  LYS VAL ASN ARG ALA LEU GLN GLN VAL GLY GLY LEU LYS          
SEQRES  27 A  356  SER PRO TRP ARG GLY GLU TYR LYS GLU PRO ARG HIS PRO          
SEQRES  28 A  356  PRO PRO ASN GLN ALA                                          
SEQRES   1 B  356  GLY ALA MET GLY SER LYS PHE SER VAL GLU GLU TYR LEU          
SEQRES   2 B  356  VAL HIS ALA LEU GLN GLY SER VAL SER SER GLY GLN ALA          
SEQRES   3 B  356  HIS SER LEU THR SER LEU ALA LYS THR TRP ALA ALA ARG          
SEQRES   4 B  356  GLY SER ARG SER ARG GLU PRO SER PRO LYS THR GLU ASP          
SEQRES   5 B  356  ASN GLU GLY VAL LEU LEU THR GLU LYS LEU LYS PRO VAL          
SEQRES   6 B  356  ASP TYR GLU TYR ARG GLU GLU VAL HIS TRP ALA THR HIS          
SEQRES   7 B  356  GLN LEU ARG LEU GLY ARG GLY SER PHE GLY GLU VAL HIS          
SEQRES   8 B  356  ARG MET GLU ASP LYS GLN THR GLY PHE GLN CYS ALA VAL          
SEQRES   9 B  356  LYS LYS VAL ARG LEU GLU VAL PHE ARG ALA GLU GLU LEU          
SEQRES  10 B  356  MET ALA CYS ALA GLY LEU THR SER PRO ARG ILE VAL PRO          
SEQRES  11 B  356  LEU TYR GLY ALA VAL ARG GLU GLY PRO TRP VAL ASN ILE          
SEQRES  12 B  356  PHE MET GLU LEU LEU GLU GLY GLY SER LEU GLY GLN LEU          
SEQRES  13 B  356  VAL LYS GLU GLN GLY CYS LEU PRO GLU ASP ARG ALA LEU          
SEQRES  14 B  356  TYR TYR LEU GLY GLN ALA LEU GLU GLY LEU GLU TYR LEU          
SEQRES  15 B  356  HIS SER ARG ARG ILE LEU HIS GLY ASP VAL LYS ALA ASP          
SEQRES  16 B  356  ASN VAL LEU LEU SER SER ASP GLY SER HIS ALA ALA LEU          
SEQRES  17 B  356  CYS ASP PHE GLY HIS ALA VAL CYS LEU GLN PRO ASP GLY          
SEQRES  18 B  356  LEU GLY LYS ASP LEU LEU THR GLY ASP TYR ILE PRO GLY          
SEQRES  19 B  356  THR GLU THR HIS MET ALA PRO GLU VAL VAL LEU GLY ARG          
SEQRES  20 B  356  SER CYS ASP ALA LYS VAL ASP VAL TRP SER SER CYS CYS          
SEQRES  21 B  356  MET MET LEU HIS MET LEU ASN GLY CYS HIS PRO TRP THR          
SEQRES  22 B  356  GLN PHE PHE ARG GLY PRO LEU CYS LEU LYS ILE ALA SER          
SEQRES  23 B  356  GLU PRO PRO PRO VAL ARG GLU ILE PRO PRO SER CYS ALA          
SEQRES  24 B  356  PRO LEU THR ALA GLN ALA ILE GLN GLU GLY LEU ARG LYS          
SEQRES  25 B  356  GLU PRO ILE HIS ARG VAL SER ALA ALA GLU LEU GLY GLY          
SEQRES  26 B  356  LYS VAL ASN ARG ALA LEU GLN GLN VAL GLY GLY LEU LYS          
SEQRES  27 B  356  SER PRO TRP ARG GLY GLU TYR LYS GLU PRO ARG HIS PRO          
SEQRES  28 B  356  PRO PRO ASN GLN ALA                                          
HET     MG  A1001       1                                                       
HET    GOL  A1002       6                                                       
HET    EDO  A1003       4                                                       
HET    EDO  A1004       4                                                       
HET    EDO  A1005       4                                                       
HET    EDO  A1006       4                                                       
HET    EDO  A1007       4                                                       
HET    AGS  A1008      31                                                       
HET     MG  B1001       1                                                       
HET    EDO  B1002       4                                                       
HET    AGS  B1003      31                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     GOL GLYCEROL                                                         
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER                       
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
HETSYN     EDO ETHYLENE GLYCOL                                                  
HETSYN     AGS ATP-GAMMA-S; ADENOSINE 5'-(3-THIOTRIPHOSPHATE);                  
HETSYN   2 AGS  ADENOSINE 5'-(GAMMA-THIOTRIPHOSPHATE); ADENOSINE-5'-            
HETSYN   3 AGS  DIPHOSPHATE MONOTHIOPHOSPHATE                                   
FORMUL   3   MG    2(MG 2+)                                                     
FORMUL   4  GOL    C3 H8 O3                                                     
FORMUL   5  EDO    6(C2 H6 O2)                                                  
FORMUL  10  AGS    2(C10 H16 N5 O12 P3 S)                                       
FORMUL  14  HOH   *70(H2 O)                                                     
HELIX    1   1 VAL A  333  GLN A  342  1                                  10    
HELIX    2   2 GLN A  349  GLY A  364  1                                  16    
HELIX    3   3 ALA A  438  ALA A  443  1                                   6    
HELIX    4   4 SER A  476  GLY A  485  1                                  10    
HELIX    5   5 PRO A  488  ARG A  509  1                                  22    
HELIX    6   6 LYS A  517  ASP A  519  5                                   3    
HELIX    7   7 THR A  559  MET A  563  5                                   5    
HELIX    8   8 ALA A  564  LEU A  569  1                                   6    
HELIX    9   9 ALA A  575  GLY A  592  1                                  18    
HELIX   10  10 LEU A  604  GLU A  611  1                                   8    
HELIX   11  11 PRO A  613  ILE A  618  5                                   6    
HELIX   12  12 ALA A  623  LEU A  634  1                                  12    
HELIX   13  13 SER A  643  GLY A  659  1                                  17    
HELIX   14  14 GLU B  334  GLN B  342  1                                   9    
HELIX   15  15 GLN B  349  GLY B  364  1                                  16    
HELIX   16  16 ALA B  438  ALA B  443  1                                   6    
HELIX   17  17 SER B  476  GLN B  484  1                                   9    
HELIX   18  18 PRO B  488  SER B  508  1                                  21    
HELIX   19  19 LYS B  517  ASP B  519  5                                   3    
HELIX   20  20 THR B  559  MET B  563  5                                   5    
HELIX   21  21 ALA B  564  GLY B  570  1                                   7    
HELIX   22  22 ALA B  575  GLY B  592  1                                  18    
HELIX   23  23 LEU B  604  GLU B  611  1                                   8    
HELIX   24  24 PRO B  613  ILE B  618  5                                   6    
HELIX   25  25 LEU B  625  LEU B  634  1                                  10    
HELIX   26  26 SER B  643  VAL B  658  1                                  16    
SHEET    1   A 7 VAL A 345  SER A 347  0                                        
SHEET    2   A 7 ASN A 377  LEU A 381  1  O  LEU A 381   N  SER A 346           
SHEET    3   A 7 LEU A 455  GLU A 461 -1  O  ARG A 460   N  GLU A 378           
SHEET    4   A 7 TRP A 464  MET A 469 -1  O  TRP A 464   N  GLU A 461           
SHEET    5   A 7 GLN A 425  ARG A 432 -1  N  VAL A 431   O  VAL A 465           
SHEET    6   A 7 GLU A 413  ASP A 419 -1  N  GLU A 413   O  LYS A 430           
SHEET    7   A 7 TRP A 399  THR A 401 -1  N  ALA A 400   O  GLU A 418           
SHEET    1   B 7 VAL A 345  SER A 347  0                                        
SHEET    2   B 7 ASN A 377  LEU A 381  1  O  LEU A 381   N  SER A 346           
SHEET    3   B 7 LEU A 455  GLU A 461 -1  O  ARG A 460   N  GLU A 378           
SHEET    4   B 7 TRP A 464  MET A 469 -1  O  TRP A 464   N  GLU A 461           
SHEET    5   B 7 GLN A 425  ARG A 432 -1  N  VAL A 431   O  VAL A 465           
SHEET    6   B 7 GLU A 413  ASP A 419 -1  N  GLU A 413   O  LYS A 430           
SHEET    7   B 7 GLY A 407  ARG A 408 -1  N  GLY A 407   O  VAL A 414           
SHEET    1   C 2 ILE A 511  LEU A 512  0                                        
SHEET    2   C 2 VAL A 539  CYS A 540 -1  O  VAL A 539   N  LEU A 512           
SHEET    1   D 2 VAL A 521  LEU A 523  0                                        
SHEET    2   D 2 ALA A 530  LEU A 532 -1  O  ALA A 531   N  LEU A 522           
SHEET    1   E 7 VAL B 345  SER B 347  0                                        
SHEET    2   E 7 ASN B 377  LEU B 381  1  O  LEU B 381   N  SER B 346           
SHEET    3   E 7 LEU B 455  GLU B 461 -1  O  ARG B 460   N  GLU B 378           
SHEET    4   E 7 TRP B 464  MET B 469 -1  O  PHE B 468   N  GLY B 457           
SHEET    5   E 7 GLN B 425  ARG B 432 -1  N  VAL B 431   O  VAL B 465           
SHEET    6   E 7 GLU B 413  ASP B 419 -1  N  MET B 417   O  CYS B 426           
SHEET    7   E 7 TRP B 399  ARG B 408 -1  N  HIS B 402   O  ARG B 416           
SHEET    1   F 2 ILE B 511  LEU B 512  0                                        
SHEET    2   F 2 VAL B 539  CYS B 540 -1  O  VAL B 539   N  LEU B 512           
SHEET    1   G 2 VAL B 521  LEU B 523  0                                        
SHEET    2   G 2 ALA B 530  LEU B 532 -1  O  ALA B 531   N  LEU B 522           
LINK        MG    MG A1001                 O1A AGS A1008     1555   1555  1.83  
LINK        MG    MG B1001                 O2A AGS B1003     1555   1555  1.86  
LINK        MG    MG B1001                 O2B AGS B1003     1555   1555  1.88  
LINK        MG    MG A1001                 O2B AGS A1008     1555   1555  2.03  
LINK        MG    MG B1001                 O   HOH B1108     1555   1555  2.08  
LINK         OD2 ASP A 534                MG    MG A1001     1555   1555  2.09  
LINK         OD1 ASN A 520                MG    MG A1001     1555   1555  2.15  
LINK         OD1 ASP B 534                MG    MG B1001     1555   1555  2.17  
LINK        MG    MG A1001                 O   HOH A1118     1555   1555  2.18  
LINK        MG    MG A1001                 O   HOH A1119     1555   1555  2.20  
LINK         OD1 ASN B 520                MG    MG B1001     1555   1555  2.30  
LINK        MG    MG B1001                 O   HOH B1109     1555   1555  2.53  
CISPEP   1 GLY A  602    PRO A  603          0         0.53                     
CISPEP   2 GLY B  602    PRO B  603          0         1.76                     
SITE     1 AC1  5 ASN A 520  ASP A 534  AGS A1008  HOH A1118                    
SITE     2 AC1  5 HOH A1119                                                     
SITE     1 AC2  3 SER A 621  CYS A 622  PRO B 675                               
SITE     1 AC3  2 GLN A 479  ARG A 666                                          
SITE     1 AC4  2 ARG A 491  ASP A 526                                          
SITE     1 AC5  1 GLU A 392                                                     
SITE     1 AC6  6 PHE A 411  ARG A 437  GLY A 536  HIS A 537                    
SITE     2 AC6  6 AGS A1008  ARG B 368                                          
SITE     1 AC7  4 ARG A 571  GLU A 637  THR B 422  GLY B 423                    
SITE     1 AC8 24 GLY A 407  GLY A 409  SER A 410  PHE A 411                    
SITE     2 AC8 24 GLY A 412  VAL A 414  ALA A 427  LYS A 429                    
SITE     3 AC8 24 MET A 469  GLU A 470  LEU A 472  SER A 476                    
SITE     4 AC8 24 GLN A 479  ASP A 515  ASP A 519  ASN A 520                    
SITE     5 AC8 24 LEU A 522  ASP A 534  HIS A 537   MG A1001                    
SITE     6 AC8 24 EDO A1006  HOH A1118  HOH A1119  HOH A1129                    
SITE     1 AC9  5 ASN B 520  ASP B 534  AGS B1003  HOH B1108                    
SITE     2 AC9  5 HOH B1109                                                     
SITE     1 BC1  6 GLU B 440  MET B 469  CYS B 533  ASP B 534                    
SITE     2 BC1  6 PHE B 535  AGS B1003                                          
SITE     1 BC2 22 GLY B 407  GLY B 409  SER B 410  PHE B 411                    
SITE     2 BC2 22 GLY B 412  VAL B 414  LYS B 429  MET B 469                    
SITE     3 BC2 22 GLU B 470  LEU B 472  SER B 476  ASP B 515                    
SITE     4 BC2 22 ASP B 519  ASN B 520  LEU B 522  ASP B 534                    
SITE     5 BC2 22 HIS B 537   MG B1001  EDO B1002  HOH B1108                    
SITE     6 BC2 22 HOH B1109  HOH B1122                                          
CRYST1   85.060   85.060  115.400  90.00  90.00  90.00 P 41          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      0.011756  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011756  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008666        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system