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Database: PDB
Entry: 2IG7
LinkDB: 2IG7
Original site: 2IG7 
HEADER    TRANSFERASE                             22-SEP-06   2IG7              
TITLE     CRYSTAL STRUCTURE OF HUMAN CHOLINE KINASE B                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CHOLINE/ETHANOLAMINE KINASE;                               
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 2.7.1.32;                                                        
COMPND   5 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: CHKB, CHETK, CHKL;                                             
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3) CODON PLUS RIL;                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: P28A-LIC                                  
KEYWDS    NON-PROTEIN KINASE, CHOLINE KINASE, STRUCTURAL GENOMICS,              
KEYWDS   2 STRUCTURAL GENOMICS CONSORTIUM, SGC, TRANSFERASE                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    W.M.RABEH,W.TEMPEL,L.NEDYALKOVA,G.WASNEY,R.LANDRY,M.VEDADI,           
AUTHOR   2 C.H.ARROWSMITH,A.M.EDWARDS,M.SUNDSTROM,J.WEIGELT,                    
AUTHOR   3 A.BOCHKAREV,H.PARK,STRUCTURAL GENOMICS CONSORTIUM (SGC)              
REVDAT   3   22-SEP-09 2IG7    1       SEQADV                                   
REVDAT   2   24-FEB-09 2IG7    1       VERSN                                    
REVDAT   1   10-OCT-06 2IG7    0                                                
JRNL        AUTH   W.M.RABEH,W.TEMPEL,L.NEDYALKOVA,G.WASNEY,R.LANDRY,           
JRNL        AUTH 2 M.VEDADI,C.H.ARROWSMITH,A.M.EDWARDS,M.SUNDSTROM,             
JRNL        AUTH 3 J.WEIGELT,A.BOCHKAREV,H.PARK                                 
JRNL        TITL   CRYSTAL STRUCTURE OF HUMAN CHOLINE KINASE B                  
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019,ARP/WARP,MOLPROBITY,COOT             
REMARK   3   AUTHORS     : LAMZIN,PERRAKIS,MORRIS                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 83039                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : THIN SHELLS                     
REMARK   3   R VALUE     (WORKING + TEST SET) : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.192                           
REMARK   3   FREE R VALUE                     : 0.227                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.541                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2110                            
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) : 1.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.85                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4988                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 80.17                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2650                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 10                           
REMARK   3   BIN FREE R VALUE                    : 0.3520                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5619                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 24                                      
REMARK   3   SOLVENT ATOMS            : 252                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 23.93                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.11400                                              
REMARK   3    B22 (A**2) : -0.18300                                             
REMARK   3    B33 (A**2) : -0.93100                                             
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): 0.113         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.112         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.076         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.390         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.956                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.935                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5799 ; 0.018 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  3977 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7903 ; 1.459 ; 1.958       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  9655 ; 0.955 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   714 ; 5.568 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   293 ;36.400 ;23.754       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   965 ;13.338 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    37 ;14.777 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   830 ; 0.094 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6494 ; 0.007 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1255 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1169 ; 0.217 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  4040 ; 0.199 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2782 ; 0.185 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  2925 ; 0.086 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   272 ; 0.142 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     1 ; 0.192 ; 0.200       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    14 ; 0.127 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    57 ; 0.202 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     2 ; 0.054 ; 0.200       
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):  3793 ; 3.041 ; 2.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1375 ; 0.808 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5565 ; 3.790 ; 3.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2649 ; 3.054 ; 2.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2316 ; 4.096 ; 3.000       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK BULK SOLVENT                                    
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3  RIDING POSITIONS                                                    
REMARK   4                                                                      
REMARK   4 2IG7 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-SEP-06.                  
REMARK 100 THE RCSB ID CODE IS RCSB039536.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-JUL-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 22-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97625                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : HKL                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 93258                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600                              
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     (%) : 77.3                               
REMARK 200  DATA REDUNDANCY                : 6.400                              
REMARK 200  R MERGE                    (I) : 0.06500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.66                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.54400                            
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: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57.90                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.90                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 18% PEG3350, 0.2M AMMONIUM               
REMARK 280  DIHYDROGEN PHOSPHATE, 0.1M HEPES, PH 7.0, VAPOR DIFFUSION,          
REMARK 280  SITTING DROP, TEMPERATURE 291K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
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       26.32850            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       78.97600            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       54.60400            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       78.97600            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       26.32850            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       54.60400            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE                                                          
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT             
REMARK 300 WHICH CONSISTS OF 2 CHAIN(S). THE BIOLOGICAL UNIT OF THE             
REMARK 300 PROTEIN IS NOT KNOWN                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2180 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 29470 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 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     MSE A    -5                                                      
REMARK 465     GLY A    -4                                                      
REMARK 465     SER A    -3                                                      
REMARK 465     SER A    -2                                                      
REMARK 465     HIS A    -1                                                      
REMARK 465     HIS A     0                                                      
REMARK 465     HIS A     1                                                      
REMARK 465     HIS A     2                                                      
REMARK 465     HIS A     3                                                      
REMARK 465     HIS A     4                                                      
REMARK 465     SER A     5                                                      
REMARK 465     SER A     6                                                      
REMARK 465     GLY A     7                                                      
REMARK 465     LEU A     8                                                      
REMARK 465     VAL A     9                                                      
REMARK 465     PRO A    10                                                      
REMARK 465     ARG A    11                                                      
REMARK 465     GLY A    12                                                      
REMARK 465     SER A    13                                                      
REMARK 465     VAL A    14                                                      
REMARK 465     GLY A    15                                                      
REMARK 465     GLY A    16                                                      
REMARK 465     CYS A    17                                                      
REMARK 465     LEU A    18                                                      
REMARK 465     ALA A    19                                                      
REMARK 465     LYS A    20                                                      
REMARK 465     ASP A    21                                                      
REMARK 465     GLY A    22                                                      
REMARK 465     LEU A    23                                                      
REMARK 465     GLN A    24                                                      
REMARK 465     GLN A    25                                                      
REMARK 465     SER A    26                                                      
REMARK 465     LYS A    27                                                      
REMARK 465     CYS A    28                                                      
REMARK 465     PRO A    29                                                      
REMARK 465     ASP A    30                                                      
REMARK 465     THR A    31                                                      
REMARK 465     THR A    32                                                      
REMARK 465     PRO A    33                                                      
REMARK 465     LYS A    34                                                      
REMARK 465     ARG A    35                                                      
REMARK 465     ARG A    36                                                      
REMARK 465     ARG A    37                                                      
REMARK 465     ALA A    38                                                      
REMARK 465     SER A    39                                                      
REMARK 465     SER A    40                                                      
REMARK 465     LEU A    41                                                      
REMARK 465     SER A    42                                                      
REMARK 465     PRO A   204                                                      
REMARK 465     THR A   205                                                      
REMARK 465     GLY A   206                                                      
REMARK 465     LEU A   207                                                      
REMARK 465     PRO A   208                                                      
REMARK 465     GLU A   209                                                      
REMARK 465     SER A   252                                                      
REMARK 465     GLU A   253                                                      
REMARK 465     PRO A   254                                                      
REMARK 465     GLU A   255                                                      
REMARK 465     ASN A   256                                                      
REMARK 465     ALA A   257                                                      
REMARK 465     ASP A   258                                                      
REMARK 465     VAL A   391                                                      
REMARK 465     HIS A   392                                                      
REMARK 465     SER A   393                                                      
REMARK 465     SER A   394                                                      
REMARK 465     SER A   395                                                      
REMARK 465     MSE B    -5                                                      
REMARK 465     GLY B    -4                                                      
REMARK 465     SER B    -3                                                      
REMARK 465     SER B    -2                                                      
REMARK 465     HIS B    -1                                                      
REMARK 465     HIS B     0                                                      
REMARK 465     HIS B     1                                                      
REMARK 465     HIS B     2                                                      
REMARK 465     HIS B     3                                                      
REMARK 465     HIS B     4                                                      
REMARK 465     SER B     5                                                      
REMARK 465     SER B     6                                                      
REMARK 465     GLY B     7                                                      
REMARK 465     LEU B     8                                                      
REMARK 465     VAL B     9                                                      
REMARK 465     PRO B    10                                                      
REMARK 465     ARG B    11                                                      
REMARK 465     GLY B    12                                                      
REMARK 465     SER B    13                                                      
REMARK 465     VAL B    14                                                      
REMARK 465     GLY B    15                                                      
REMARK 465     GLY B    16                                                      
REMARK 465     CYS B    17                                                      
REMARK 465     LEU B    18                                                      
REMARK 465     ALA B    19                                                      
REMARK 465     LYS B    20                                                      
REMARK 465     ASP B    21                                                      
REMARK 465     GLY B    22                                                      
REMARK 465     LEU B    23                                                      
REMARK 465     GLN B    24                                                      
REMARK 465     GLN B    25                                                      
REMARK 465     SER B    26                                                      
REMARK 465     LYS B    27                                                      
REMARK 465     CYS B    28                                                      
REMARK 465     PRO B    29                                                      
REMARK 465     ASP B    30                                                      
REMARK 465     THR B    31                                                      
REMARK 465     THR B    32                                                      
REMARK 465     PRO B    33                                                      
REMARK 465     LYS B    34                                                      
REMARK 465     ARG B    35                                                      
REMARK 465     ARG B    36                                                      
REMARK 465     ARG B    37                                                      
REMARK 465     ALA B    38                                                      
REMARK 465     SER B    39                                                      
REMARK 465     SER B    40                                                      
REMARK 465     LEU B    41                                                      
REMARK 465     GLY B    95                                                      
REMARK 465     GLU B    96                                                      
REMARK 465     THR B   205                                                      
REMARK 465     GLY B   206                                                      
REMARK 465     LEU B   207                                                      
REMARK 465     PRO B   208                                                      
REMARK 465     GLU B   209                                                      
REMARK 465     VAL B   391                                                      
REMARK 465     HIS B   392                                                      
REMARK 465     SER B   393                                                      
REMARK 465     SER B   394                                                      
REMARK 465     SER B   395                                                      
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     ARG A  43    CD   NE   CZ   NH1  NH2                             
REMARK 470     ARG A  47    CD   NE   CZ   NH1  NH2                             
REMARK 470     ARG A  48    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN A  51    CD   OE1  NE2                                       
REMARK 470     GLU A  55    OE1  OE2                                            
REMARK 470     TYR A  72    CD1  CD2  CE1  CE2  CZ   OH                         
REMARK 470     GLU A  96    CD   OE1  OE2                                       
REMARK 470     LYS A 154    CE   NZ                                             
REMARK 470     LYS A 197    CE   NZ                                             
REMARK 470     GLU A 214    CD   OE1  OE2                                       
REMARK 470     LYS A 219    CG   CD   CE   NZ                                   
REMARK 470     LYS A 227    CE   NZ                                             
REMARK 470     GLU A 291    CD   OE1  OE2                                       
REMARK 470     GLU A 292    CD   OE1  OE2                                       
REMARK 470     LYS A 297    CE   NZ                                             
REMARK 470     LYS A 322    CD   CE   NZ                                        
REMARK 470     GLN A 328    CD   OE1  NE2                                       
REMARK 470     GLU A 329    CD   OE1  OE2                                       
REMARK 470     ARG B  43    CD   NE   CZ   NH1  NH2                             
REMARK 470     ARG B  48    NE   CZ   NH1  NH2                                  
REMARK 470     ARG B  63    CZ   NH1  NH2                                       
REMARK 470     ARG B  70    NE   CZ   NH1  NH2                                  
REMARK 470     LYS B 197    CE   NZ                                             
REMARK 470     GLU B 214    CD   OE1  OE2                                       
REMARK 470     LYS B 219    CD   CE   NZ                                        
REMARK 470     LYS B 227    NZ                                                  
REMARK 470     GLU B 253    CD   OE1  OE2                                       
REMARK 470     GLU B 255    CD   OE1  OE2                                       
REMARK 470     LYS B 297    CD   CE   NZ                                        
REMARK 470     LYS B 322    CG   CD   CE   NZ                                   
REMARK 470     GLN B 328    CG   CD   OE1  NE2                                  
REMARK 470     GLU B 329    CD   OE1  OE2                                       
REMARK 470     ARG B 332    CD   NE   CZ   NH1  NH2                             
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OG   SER B    86    UNK   UNX B  1017              1.75            
REMARK 500   OD1  ASP B   258    UNK   UNX B  1019              2.04            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG B 159   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500    ARG B 159   NE  -  CZ  -  NH2 ANGL. DEV. =   3.9 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A  89      -46.14    -25.88                                   
REMARK 500    ASN A 241       -2.34     80.04                                   
REMARK 500    ASP A 242       44.62   -148.95                                   
REMARK 500    ASP A 264       65.35     65.16                                   
REMARK 500    SER A 269      163.27    176.72                                   
REMARK 500    ASP B 242       47.21   -149.03                                   
REMARK 500    ASP B 264       70.39     66.05                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNX B 1001                
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNX B 1002                
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNX B 1003                
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNX A 1004                
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNX B 1005                
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNX B 1006                
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNX A 1007                
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNX B 1008                
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNX A 1009                
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNX B 1010                
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNX A 1011                
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNX A 1012                
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNX A 1013                
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNX B 1014                
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNX B 1015                
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNX A 1016                
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNX B 1017                
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNX B 1018                
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNX B 1019                
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNX B 1020                
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNX B 1021                
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNX B 1022                
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNX B 1023                
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNX A 1024                
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 MSE AT POSITION -7 IS AN INITIATING MET AS WELL AS A                 
REMARK 999 MODIFIED RESIDUE                                                     
DBREF  2IG7 A   14   395  UNP    Q9Y259   CHKB_HUMAN      11    394             
DBREF  2IG7 B   14   395  UNP    Q9Y259   CHKB_HUMAN      11    394             
SEQADV 2IG7 MSE A   -5  UNP  Q9Y259              SEE REMARK 999                 
SEQADV 2IG7 GLY A   -4  UNP  Q9Y259              CLONING ARTIFACT               
SEQADV 2IG7 SER A   -3  UNP  Q9Y259              CLONING ARTIFACT               
SEQADV 2IG7 SER A   -2  UNP  Q9Y259              CLONING ARTIFACT               
SEQADV 2IG7 HIS A   -1  UNP  Q9Y259              EXPRESSION TAG                 
SEQADV 2IG7 HIS A    0  UNP  Q9Y259              EXPRESSION TAG                 
SEQADV 2IG7 HIS A   -1  UNP  Q9Y259              EXPRESSION TAG                 
SEQADV 2IG7 HIS A    0  UNP  Q9Y259              EXPRESSION TAG                 
SEQADV 2IG7 HIS A    1  UNP  Q9Y259              EXPRESSION TAG                 
SEQADV 2IG7 HIS A    2  UNP  Q9Y259              EXPRESSION TAG                 
SEQADV 2IG7 SER A    5  UNP  Q9Y259              CLONING ARTIFACT               
SEQADV 2IG7 SER A    6  UNP  Q9Y259              CLONING ARTIFACT               
SEQADV 2IG7 GLY A    7  UNP  Q9Y259              CLONING ARTIFACT               
SEQADV 2IG7 LEU A    8  UNP  Q9Y259              CLONING ARTIFACT               
SEQADV 2IG7 VAL A    9  UNP  Q9Y259              CLONING ARTIFACT               
SEQADV 2IG7 PRO A   10  UNP  Q9Y259              CLONING ARTIFACT               
SEQADV 2IG7 ARG A   11  UNP  Q9Y259              CLONING ARTIFACT               
SEQADV 2IG7 GLY A   12  UNP  Q9Y259              CLONING ARTIFACT               
SEQADV 2IG7 SER A   13  UNP  Q9Y259              CLONING ARTIFACT               
SEQADV 2IG7 MSE B   -5  UNP  Q9Y259              SEE REMARK 999                 
SEQADV 2IG7 GLY B   -4  UNP  Q9Y259              CLONING ARTIFACT               
SEQADV 2IG7 SER B   -3  UNP  Q9Y259              CLONING ARTIFACT               
SEQADV 2IG7 SER B   -2  UNP  Q9Y259              CLONING ARTIFACT               
SEQADV 2IG7 HIS B   -1  UNP  Q9Y259              EXPRESSION TAG                 
SEQADV 2IG7 HIS B    0  UNP  Q9Y259              EXPRESSION TAG                 
SEQADV 2IG7 HIS B   -1  UNP  Q9Y259              EXPRESSION TAG                 
SEQADV 2IG7 HIS B    0  UNP  Q9Y259              EXPRESSION TAG                 
SEQADV 2IG7 HIS B    1  UNP  Q9Y259              EXPRESSION TAG                 
SEQADV 2IG7 HIS B    2  UNP  Q9Y259              EXPRESSION TAG                 
SEQADV 2IG7 SER B    5  UNP  Q9Y259              CLONING ARTIFACT               
SEQADV 2IG7 SER B    6  UNP  Q9Y259              CLONING ARTIFACT               
SEQADV 2IG7 GLY B    7  UNP  Q9Y259              CLONING ARTIFACT               
SEQADV 2IG7 LEU B    8  UNP  Q9Y259              CLONING ARTIFACT               
SEQADV 2IG7 VAL B    9  UNP  Q9Y259              CLONING ARTIFACT               
SEQADV 2IG7 PRO B   10  UNP  Q9Y259              CLONING ARTIFACT               
SEQADV 2IG7 ARG B   11  UNP  Q9Y259              CLONING ARTIFACT               
SEQADV 2IG7 GLY B   12  UNP  Q9Y259              CLONING ARTIFACT               
SEQADV 2IG7 SER B   13  UNP  Q9Y259              CLONING ARTIFACT               
SEQRES   1 A  401  MSE GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  401  LEU VAL PRO ARG GLY SER VAL GLY GLY CYS LEU ALA LYS          
SEQRES   3 A  401  ASP GLY LEU GLN GLN SER LYS CYS PRO ASP THR THR PRO          
SEQRES   4 A  401  LYS ARG ARG ARG ALA SER SER LEU SER ARG ASP ALA GLU          
SEQRES   5 A  401  ARG ARG ALA TYR GLN TRP CYS ARG GLU TYR LEU GLY GLY          
SEQRES   6 A  401  ALA TRP ARG ARG VAL GLN PRO GLU GLU LEU ARG VAL TYR          
SEQRES   7 A  401  PRO VAL SER GLY GLY LEU SER ASN LEU LEU PHE ARG CYS          
SEQRES   8 A  401  SER LEU PRO ASP HIS LEU PRO SER VAL GLY GLU GLU PRO          
SEQRES   9 A  401  ARG GLU VAL LEU LEU ARG LEU TYR GLY ALA ILE LEU GLN          
SEQRES  10 A  401  GLY VAL ASP SER LEU VAL LEU GLU SER VAL MSE PHE ALA          
SEQRES  11 A  401  ILE LEU ALA GLU ARG SER LEU GLY PRO GLN LEU TYR GLY          
SEQRES  12 A  401  VAL PHE PRO GLU GLY ARG LEU GLU GLN TYR ILE PRO SER          
SEQRES  13 A  401  ARG PRO LEU LYS THR GLN GLU LEU ARG GLU PRO VAL LEU          
SEQRES  14 A  401  SER ALA ALA ILE ALA THR LYS MSE ALA GLN PHE HIS GLY          
SEQRES  15 A  401  MSE GLU MSE PRO PHE THR LYS GLU PRO HIS TRP LEU PHE          
SEQRES  16 A  401  GLY THR MSE GLU ARG TYR LEU LYS GLN ILE GLN ASP LEU          
SEQRES  17 A  401  PRO PRO THR GLY LEU PRO GLU MSE ASN LEU LEU GLU MSE          
SEQRES  18 A  401  TYR SER LEU LYS ASP GLU MSE GLY ASN LEU ARG LYS LEU          
SEQRES  19 A  401  LEU GLU SER THR PRO SER PRO VAL VAL PHE CYS HIS ASN          
SEQRES  20 A  401  ASP ILE GLN GLU GLY ASN ILE LEU LEU LEU SER GLU PRO          
SEQRES  21 A  401  GLU ASN ALA ASP SER LEU MSE LEU VAL ASP PHE GLU TYR          
SEQRES  22 A  401  SER SER TYR ASN TYR ARG GLY PHE ASP ILE GLY ASN HIS          
SEQRES  23 A  401  PHE CYS GLU TRP VAL TYR ASP TYR THR HIS GLU GLU TRP          
SEQRES  24 A  401  PRO PHE TYR LYS ALA ARG PRO THR ASP TYR PRO THR GLN          
SEQRES  25 A  401  GLU GLN GLN LEU HIS PHE ILE ARG HIS TYR LEU ALA GLU          
SEQRES  26 A  401  ALA LYS LYS GLY GLU THR LEU SER GLN GLU GLU GLN ARG          
SEQRES  27 A  401  LYS LEU GLU GLU ASP LEU LEU VAL GLU VAL SER ARG TYR          
SEQRES  28 A  401  ALA LEU ALA SER HIS PHE PHE TRP GLY LEU TRP SER ILE          
SEQRES  29 A  401  LEU GLN ALA SER MSE SER THR ILE GLU PHE GLY TYR LEU          
SEQRES  30 A  401  ASP TYR ALA GLN SER ARG PHE GLN PHE TYR PHE GLN GLN          
SEQRES  31 A  401  LYS GLY GLN LEU THR SER VAL HIS SER SER SER                  
SEQRES   1 B  401  MSE GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 B  401  LEU VAL PRO ARG GLY SER VAL GLY GLY CYS LEU ALA LYS          
SEQRES   3 B  401  ASP GLY LEU GLN GLN SER LYS CYS PRO ASP THR THR PRO          
SEQRES   4 B  401  LYS ARG ARG ARG ALA SER SER LEU SER ARG ASP ALA GLU          
SEQRES   5 B  401  ARG ARG ALA TYR GLN TRP CYS ARG GLU TYR LEU GLY GLY          
SEQRES   6 B  401  ALA TRP ARG ARG VAL GLN PRO GLU GLU LEU ARG VAL TYR          
SEQRES   7 B  401  PRO VAL SER GLY GLY LEU SER ASN LEU LEU PHE ARG CYS          
SEQRES   8 B  401  SER LEU PRO ASP HIS LEU PRO SER VAL GLY GLU GLU PRO          
SEQRES   9 B  401  ARG GLU VAL LEU LEU ARG LEU TYR GLY ALA ILE LEU GLN          
SEQRES  10 B  401  GLY VAL ASP SER LEU VAL LEU GLU SER VAL MSE PHE ALA          
SEQRES  11 B  401  ILE LEU ALA GLU ARG SER LEU GLY PRO GLN LEU TYR GLY          
SEQRES  12 B  401  VAL PHE PRO GLU GLY ARG LEU GLU GLN TYR ILE PRO SER          
SEQRES  13 B  401  ARG PRO LEU LYS THR GLN GLU LEU ARG GLU PRO VAL LEU          
SEQRES  14 B  401  SER ALA ALA ILE ALA THR LYS MSE ALA GLN PHE HIS GLY          
SEQRES  15 B  401  MSE GLU MSE PRO PHE THR LYS GLU PRO HIS TRP LEU PHE          
SEQRES  16 B  401  GLY THR MSE GLU ARG TYR LEU LYS GLN ILE GLN ASP LEU          
SEQRES  17 B  401  PRO PRO THR GLY LEU PRO GLU MSE ASN LEU LEU GLU MSE          
SEQRES  18 B  401  TYR SER LEU LYS ASP GLU MSE GLY ASN LEU ARG LYS LEU          
SEQRES  19 B  401  LEU GLU SER THR PRO SER PRO VAL VAL PHE CYS HIS ASN          
SEQRES  20 B  401  ASP ILE GLN GLU GLY ASN ILE LEU LEU LEU SER GLU PRO          
SEQRES  21 B  401  GLU ASN ALA ASP SER LEU MSE LEU VAL ASP PHE GLU TYR          
SEQRES  22 B  401  SER SER TYR ASN TYR ARG GLY PHE ASP ILE GLY ASN HIS          
SEQRES  23 B  401  PHE CYS GLU TRP VAL TYR ASP TYR THR HIS GLU GLU TRP          
SEQRES  24 B  401  PRO PHE TYR LYS ALA ARG PRO THR ASP TYR PRO THR GLN          
SEQRES  25 B  401  GLU GLN GLN LEU HIS PHE ILE ARG HIS TYR LEU ALA GLU          
SEQRES  26 B  401  ALA LYS LYS GLY GLU THR LEU SER GLN GLU GLU GLN ARG          
SEQRES  27 B  401  LYS LEU GLU GLU ASP LEU LEU VAL GLU VAL SER ARG TYR          
SEQRES  28 B  401  ALA LEU ALA SER HIS PHE PHE TRP GLY LEU TRP SER ILE          
SEQRES  29 B  401  LEU GLN ALA SER MSE SER THR ILE GLU PHE GLY TYR LEU          
SEQRES  30 B  401  ASP TYR ALA GLN SER ARG PHE GLN PHE TYR PHE GLN GLN          
SEQRES  31 B  401  LYS GLY GLN LEU THR SER VAL HIS SER SER SER                  
MODRES 2IG7 MSE A  122  MET  SELENOMETHIONINE                                   
MODRES 2IG7 MSE A  171  MET  SELENOMETHIONINE                                   
MODRES 2IG7 MSE A  177  MET  SELENOMETHIONINE                                   
MODRES 2IG7 MSE A  179  MET  SELENOMETHIONINE                                   
MODRES 2IG7 MSE A  192  MET  SELENOMETHIONINE                                   
MODRES 2IG7 MSE A  210  MET  SELENOMETHIONINE                                   
MODRES 2IG7 MSE A  215  MET  SELENOMETHIONINE                                   
MODRES 2IG7 MSE A  222  MET  SELENOMETHIONINE                                   
MODRES 2IG7 MSE A  261  MET  SELENOMETHIONINE                                   
MODRES 2IG7 MSE A  363  MET  SELENOMETHIONINE                                   
MODRES 2IG7 MSE B  122  MET  SELENOMETHIONINE                                   
MODRES 2IG7 MSE B  171  MET  SELENOMETHIONINE                                   
MODRES 2IG7 MSE B  177  MET  SELENOMETHIONINE                                   
MODRES 2IG7 MSE B  179  MET  SELENOMETHIONINE                                   
MODRES 2IG7 MSE B  192  MET  SELENOMETHIONINE                                   
MODRES 2IG7 MSE B  210  MET  SELENOMETHIONINE                                   
MODRES 2IG7 MSE B  215  MET  SELENOMETHIONINE                                   
MODRES 2IG7 MSE B  222  MET  SELENOMETHIONINE                                   
MODRES 2IG7 MSE B  261  MET  SELENOMETHIONINE                                   
MODRES 2IG7 MSE B  363  MET  SELENOMETHIONINE                                   
HET    MSE  A 122       8                                                       
HET    MSE  A 171       8                                                       
HET    MSE  A 177       8                                                       
HET    MSE  A 179       8                                                       
HET    MSE  A 192       8                                                       
HET    MSE  A 210       8                                                       
HET    MSE  A 215       8                                                       
HET    MSE  A 222       8                                                       
HET    MSE  A 261       8                                                       
HET    MSE  A 363       8                                                       
HET    MSE  B 122       8                                                       
HET    MSE  B 171       8                                                       
HET    MSE  B 177       8                                                       
HET    MSE  B 179       8                                                       
HET    MSE  B 192       8                                                       
HET    MSE  B 210       8                                                       
HET    MSE  B 215       8                                                       
HET    MSE  B 222       8                                                       
HET    MSE  B 261       8                                                       
HET    MSE  B 363       8                                                       
HET    UNX  B1001       1                                                       
HET    UNX  B1002       1                                                       
HET    UNX  B1003       1                                                       
HET    UNX  A1004       1                                                       
HET    UNX  B1005       1                                                       
HET    UNX  B1006       1                                                       
HET    UNX  A1007       1                                                       
HET    UNX  B1008       1                                                       
HET    UNX  A1009       1                                                       
HET    UNX  B1010       1                                                       
HET    UNX  A1011       1                                                       
HET    UNX  A1012       1                                                       
HET    UNX  A1013       1                                                       
HET    UNX  B1014       1                                                       
HET    UNX  B1015       1                                                       
HET    UNX  A1016       1                                                       
HET    UNX  B1017       1                                                       
HET    UNX  B1018       1                                                       
HET    UNX  B1019       1                                                       
HET    UNX  B1020       1                                                       
HET    UNX  B1021       1                                                       
HET    UNX  B1022       1                                                       
HET    UNX  B1023       1                                                       
HET    UNX  A1024       1                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM     UNX UNKNOWN ATOM OR ION                                              
FORMUL   1  MSE    20(C5 H11 N O2 SE)                                           
FORMUL   3  UNX    24(X)                                                        
FORMUL  27  HOH   *252(H2 O)                                                    
HELIX    1   1 ARG A   43  LEU A   57  1                                  15    
HELIX    2   2 GLY A   58  ARG A   63  5                                   6    
HELIX    3   3 GLY A  107  GLN A  111  5                                   5    
HELIX    4   4 GLY A  112  ARG A  129  1                                  18    
HELIX    5   5 LYS A  154  ARG A  159  5                                   6    
HELIX    6   6 GLU A  160  GLY A  176  1                                  17    
HELIX    7   7 HIS A  186  ASP A  201  1                                  16    
HELIX    8   8 ASN A  211  TYR A  216  1                                   6    
HELIX    9   9 SER A  217  SER A  231  1                                  15    
HELIX   10  10 GLN A  244  GLY A  246  5                                   3    
HELIX   11  11 ASP A  264  SER A  268  5                                   5    
HELIX   12  12 ARG A  273  GLU A  283  1                                  11    
HELIX   13  13 PRO A  300  TYR A  303  5                                   4    
HELIX   14  14 THR A  305  LYS A  321  1                                  17    
HELIX   15  15 SER A  327  SER A  364  1                                  38    
HELIX   16  16 GLY A  369  THR A  389  1                                  21    
HELIX   17  17 SER B   42  LEU B   57  1                                  16    
HELIX   18  18 GLY B   58  ARG B   63  5                                   6    
HELIX   19  19 GLY B  107  GLN B  111  5                                   5    
HELIX   20  20 GLY B  112  ARG B  129  1                                  18    
HELIX   21  21 LYS B  154  ARG B  159  5                                   6    
HELIX   22  22 GLU B  160  GLY B  176  1                                  17    
HELIX   23  23 HIS B  186  ASP B  201  1                                  16    
HELIX   24  24 ASN B  211  TYR B  216  1                                   6    
HELIX   25  25 SER B  217  SER B  231  1                                  15    
HELIX   26  26 GLN B  244  GLY B  246  5                                   3    
HELIX   27  27 ARG B  273  GLU B  283  1                                  11    
HELIX   28  28 PRO B  300  TYR B  303  5                                   4    
HELIX   29  29 THR B  305  LYS B  321  1                                  17    
HELIX   30  30 SER B  327  SER B  364  1                                  38    
HELIX   31  31 GLY B  369  SER B  390  1                                  22    
SHEET    1   A 5 ARG A  70  VAL A  74  0                                        
SHEET    2   A 5 LEU A  81  SER A  86 -1  O  ARG A  84   N  TYR A  72           
SHEET    3   A 5 GLU A 100  LEU A 105 -1  O  LEU A 103   N  PHE A  83           
SHEET    4   A 5 GLY A 142  GLN A 146 -1  O  ARG A 143   N  ARG A 104           
SHEET    5   A 5 LEU A 135  PHE A 139 -1  N  TYR A 136   O  LEU A 144           
SHEET    1   B 3 ARG A 151  PRO A 152  0                                        
SHEET    2   B 3 ILE A 248  LEU A 250 -1  O  LEU A 250   N  ARG A 151           
SHEET    3   B 3 MSE A 261  LEU A 262 -1  O  MSE A 261   N  LEU A 249           
SHEET    1   C 2 VAL A 236  CYS A 239  0                                        
SHEET    2   C 2 SER A 269  TYR A 272 -1  O  ASN A 271   N  VAL A 237           
SHEET    1   D 2 TYR A 286  ASP A 287  0                                        
SHEET    2   D 2 LYS A 297  ALA A 298 -1  O  LYS A 297   N  ASP A 287           
SHEET    1   E 5 ARG B  70  PRO B  73  0                                        
SHEET    2   E 5 LEU B  81  SER B  86 -1  O  SER B  86   N  ARG B  70           
SHEET    3   E 5 GLU B 100  LEU B 105 -1  O  LEU B 103   N  PHE B  83           
SHEET    4   E 5 GLY B 142  GLN B 146 -1  O  GLU B 145   N  LEU B 102           
SHEET    5   E 5 LEU B 135  PHE B 139 -1  N  TYR B 136   O  LEU B 144           
SHEET    1   F 3 SER B 150  PRO B 152  0                                        
SHEET    2   F 3 ILE B 248  LEU B 251 -1  O  LEU B 250   N  ARG B 151           
SHEET    3   F 3 LEU B 260  LEU B 262 -1  O  MSE B 261   N  LEU B 249           
SHEET    1   G 2 VAL B 236  CYS B 239  0                                        
SHEET    2   G 2 SER B 269  TYR B 272 -1  O  ASN B 271   N  VAL B 237           
SHEET    1   H 2 TYR B 286  ASP B 287  0                                        
SHEET    2   H 2 LYS B 297  ALA B 298 -1  O  LYS B 297   N  ASP B 287           
LINK         C   VAL A 121                 N   MSE A 122     1555   1555  1.34  
LINK         C   MSE A 122                 N   PHE A 123     1555   1555  1.33  
LINK         C   LYS A 170                 N   MSE A 171     1555   1555  1.34  
LINK         C   MSE A 171                 N   ALA A 172     1555   1555  1.34  
LINK         C   GLY A 176                 N   MSE A 177     1555   1555  1.33  
LINK         C   MSE A 177                 N   GLU A 178     1555   1555  1.33  
LINK         C   GLU A 178                 N   MSE A 179     1555   1555  1.33  
LINK         C   MSE A 179                 N   PRO A 180     1555   1555  1.37  
LINK         C   THR A 191                 N   MSE A 192     1555   1555  1.33  
LINK         C   MSE A 192                 N   GLU A 193     1555   1555  1.33  
LINK         C   MSE A 210                 N   ASN A 211     1555   1555  1.33  
LINK         C   GLU A 214                 N   MSE A 215     1555   1555  1.32  
LINK         C   MSE A 215                 N   TYR A 216     1555   1555  1.34  
LINK         C   GLU A 221                 N   MSE A 222     1555   1555  1.32  
LINK         C   MSE A 222                 N   GLY A 223     1555   1555  1.33  
LINK         C   LEU A 260                 N   MSE A 261     1555   1555  1.33  
LINK         C   MSE A 261                 N   LEU A 262     1555   1555  1.34  
LINK         C   SER A 362                 N   MSE A 363     1555   1555  1.35  
LINK         C   MSE A 363                 N   SER A 364     1555   1555  1.33  
LINK         C   VAL B 121                 N   MSE B 122     1555   1555  1.33  
LINK         C   MSE B 122                 N   PHE B 123     1555   1555  1.33  
LINK         C   LYS B 170                 N   MSE B 171     1555   1555  1.33  
LINK         C   MSE B 171                 N   ALA B 172     1555   1555  1.34  
LINK         C   GLY B 176                 N   MSE B 177     1555   1555  1.33  
LINK         C   MSE B 177                 N   GLU B 178     1555   1555  1.33  
LINK         C   GLU B 178                 N   MSE B 179     1555   1555  1.32  
LINK         C   MSE B 179                 N   PRO B 180     1555   1555  1.35  
LINK         C   THR B 191                 N   MSE B 192     1555   1555  1.32  
LINK         C   MSE B 192                 N   GLU B 193     1555   1555  1.33  
LINK         C   MSE B 210                 N   ASN B 211     1555   1555  1.32  
LINK         C   GLU B 214                 N   MSE B 215     1555   1555  1.32  
LINK         C   MSE B 215                 N   TYR B 216     1555   1555  1.34  
LINK         C   GLU B 221                 N   MSE B 222     1555   1555  1.33  
LINK         C   MSE B 222                 N   GLY B 223     1555   1555  1.33  
LINK         C   LEU B 260                 N   MSE B 261     1555   1555  1.32  
LINK         C   MSE B 261                 N   LEU B 262     1555   1555  1.33  
LINK         C   SER B 362                 N   MSE B 363     1555   1555  1.34  
LINK         C   MSE B 363                 N   SER B 364     1555   1555  1.32  
CISPEP   1 TRP A  293    PRO A  294          0         4.88                     
CISPEP   2 TRP B  293    PRO B  294          0         3.85                     
SITE     1 AC1  4 GLU B 245  GLU B 283  TYR B 286  TYR B 288                    
SITE     1 AC2  2 TRP B 187  HOH B1046                                          
SITE     1 AC3  4 TRP B 293  GLY B 369  LEU B 371  ASP B 372                    
SITE     1 AC4  2 TRP A 187  HOH A1061                                          
SITE     1 AC5  3 ARG B 194  TYR B 195  GLN B 198                               
SITE     1 AC6  4 GLY B  77  LEU B  78  GLN B 244  HOH B1156                    
SITE     1 AC7  1 SER A  79                                                     
SITE     1 AC8  1 GLU B 178                                                     
SITE     1 AC9  1 GLN A 198                                                     
SITE     1 BC1  3 GLU B  46  PRO B  66  LEU B  69                               
SITE     1 BC2  5 ARG A  54  GLU A  55  LEU A  57  ARG A  62                    
SITE     2 BC2  5 LYS B 183                                                     
SITE     1 BC3  3 SER A 217  LYS A 219  ASP A 220                               
SITE     1 BC4  1 ARG A 314                                                     
SITE     1 BC5  2 TRP B  52  GLU B  55                                          
SITE     1 BC6  5 LYS A 183  ARG B  54  GLU B  55  LEU B  57                    
SITE     2 BC6  5 ARG B  62                                                     
SITE     1 BC7  4 ARG A  70  TYR A  72  ARG A  84  SER A  86                    
SITE     1 BC8  4 TYR B  72  CYS B  85  SER B  86  GLU B 100                    
SITE     1 BC9  2 VAL B 113  ASP B 114                                          
SITE     1 CC1  5 LYS B 170  ASP B 258  SER B 259  LEU B 260                    
SITE     2 CC1  5 HOH B1045                                                     
SITE     1 CC2  3 HIS B 311  ARG B 314  HIS B 315                               
SITE     1 CC3  2 LEU B 102  ILE B 148                                          
SITE     1 CC4  3 GLY B 132  GLN B 134  GLN B 146                               
SITE     1 CC5  5 ASN B  80  ARG B 104  ASP B 264  GLU B 266                    
SITE     2 CC5  5 HOH B1110                                                     
SITE     1 CC6  4 GLU A 245  GLU A 283  TYR A 286  TYR A 288                    
CRYST1   52.657  109.208  157.952  90.00  90.00  90.00 P 21 21 21    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      0.018990  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009160  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006330        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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