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Database: PDB
Entry: 2QPW
LinkDB: 2QPW
Original site: 2QPW 
HEADER    TRANSCRIPTION                           25-JUL-07   2QPW              
TITLE     METHYLTRANSFERASE DOMAIN OF HUMAN PR DOMAIN-CONTAINING                
TITLE    2 PROTEIN 2                                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PR DOMAIN ZINC FINGER PROTEIN 2;                           
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: METHYLTRANSFERASE DOMAIN: RESIDUES 2-148;                  
COMPND   5 SYNONYM: PR DOMAIN-CONTAINING PROTEIN 2, RETINOBLASTOMA              
COMPND   6 PROTEIN-INTERACTING ZINC FINGER PROTEIN, ZINC FINGER                 
COMPND   7 PROTEIN RIZ, MTE-BINDING PROTEIN, MTB-ZF, GATA-3-BINDING             
COMPND   8 PROTEIN G3B;                                                         
COMPND   9 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: PRDM2, RIZ;                                                    
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: DH5A;                                      
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: P15MHL                                    
KEYWDS    METHYLTRANSFERASE, ACTIVATOR, ALTERNATIVE INITIATION,                 
KEYWDS   2 ALTERNATIVE SPLICING, DNA-BINDING, METAL-BINDING, NUCLEUS,           
KEYWDS   3 PHOSPHORYLATION, TRANSCRIPTION, TRANSCRIPTION REGULATION,            
KEYWDS   4 ZINC, ZINC-FINGER, STRUCTURAL GENOMICS, STRUCTURAL GENOMICS          
KEYWDS   5 CONSORTIUM, SGC                                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    V.V.LUNIN,H.WU,L.DOMBROVSKI,T.ANTOSHENKO,P.LOPPNAU,                   
AUTHOR   2 J.WEIGELT,M.SUNDSTROM,C.H.ARROWSMITH,A.M.EDWARDS,                    
AUTHOR   3 A.BOCHKAREV,J.MIN,A.N.PLOTNIKOV,STRUCTURAL GENOMICS                  
AUTHOR   4 CONSORTIUM (SGC)                                                     
REVDAT   3   02-MAR-10 2QPW    1       JRNL                                     
REVDAT   2   24-FEB-09 2QPW    1       VERSN                                    
REVDAT   1   14-AUG-07 2QPW    0                                                
JRNL        AUTH   H.WU,J.MIN,V.V.LUNIN,T.ANTOSHENKO,L.DOMBROVSKI,              
JRNL        AUTH 2 H.ZENG,A.ALLALI-HASSANI,V.CAMPAGNA-SLATER,M.VEDADI,          
JRNL        AUTH 3 C.H.ARROWSMITH,A.N.PLOTNIKOV,M.SCHAPIRA                      
JRNL        TITL   STRUCTURAL BIOLOGY OF HUMAN H3K9 METHYLTRANSFERASES          
JRNL        REF    PLOS ONE                      V.   5 E8570 2010              
JRNL        REFN                   ESSN 1932-6203                               
JRNL        PMID   20084102                                                     
JRNL        DOI    10.1371/JOURNAL.PONE.0008570                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.79 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
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) : 1.79                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 41.49                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 12305                          
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) : 0.171                           
REMARK   3   R VALUE            (WORKING SET) : 0.168                           
REMARK   3   FREE R VALUE                     : 0.222                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 631                             
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) : 1.79                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.84                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 841                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 94.82                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1980                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 56                           
REMARK   3   BIN FREE R VALUE                    : 0.2540                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1191                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 145                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 23.17                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.81000                                             
REMARK   3    B22 (A**2) : -0.44000                                             
REMARK   3    B33 (A**2) : 1.26000                                              
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): 0.135         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.133         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.087         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.718         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.965                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.940                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1228 ; 0.019 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  1679 ; 1.507 ; 1.957       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   150 ; 5.947 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    56 ;36.888 ;24.643       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   202 ;14.279 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     6 ; 8.909 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   178 ; 0.118 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):   952 ; 0.007 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   414 ; 0.206 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):   802 ; 0.307 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):    78 ; 0.212 ; 0.200       
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):    58 ; 0.177 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    21 ; 0.191 ; 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):   772 ; 1.198 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1208 ; 1.815 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   551 ; 2.835 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   469 ; 4.245 ; 4.500       
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                                                 
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: THE FRIEDEL PAIRS WERE USED FOR           
REMARK   3  PHASING. HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS          
REMARK   4                                                                      
REMARK   4 2QPW COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-JUL-07.                  
REMARK 100 THE RCSB ID CODE IS RCSB043906.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-JUN-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 2                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : CHESS                              
REMARK 200  BEAMLINE                       : A1                                 
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97770                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 23999                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.790                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 7.200                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.06300                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 34.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.79                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.86                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.40                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.30100                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 6.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: OBTAINED VIA SE-SAD FROM SECOND CRYSTAL              
REMARK 200  (DIFFERENT CRYSTAL FORM) AT LOW RESOLUTION                          
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 36.62                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.94                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 22% PEG 5000 MME, 0.2 M AMMONIUM         
REMARK 280  SULFATE, 0.1 M MES PH 7.0, VAPOR DIFFUSION, HANGING DROP,           
REMARK 280  TEMPERATURE 298K                                                    
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       18.23100            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       35.44350            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       25.59800            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       35.44350            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       18.23100            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       25.59800            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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    -1                                                      
REMARK 465     SER A     0                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;            
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU A 108    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 109    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 143    CG   OD1                                            
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   O    HOH A   177     O    HOH A   268              2.11            
REMARK 500   OE2  GLU A    93     O    HOH A   239              2.17            
REMARK 500   OE1  GLN A    67     O    HOH A   266              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  2QPW A    1   147  UNP    Q13029   PRDM2_HUMAN      2    148             
SEQADV 2QPW GLY A   -1  UNP  Q13029              EXPRESSION TAG                 
SEQADV 2QPW SER A    0  UNP  Q13029              EXPRESSION TAG                 
SEQRES   1 A  149  GLY SER ASN GLN ASN THR THR GLU PRO VAL ALA ALA THR          
SEQRES   2 A  149  GLU THR LEU ALA GLU VAL PRO GLU HIS VAL LEU ARG GLY          
SEQRES   3 A  149  LEU PRO GLU GLU VAL ARG LEU PHE PRO SER ALA VAL ASP          
SEQRES   4 A  149  LYS THR ARG ILE GLY VAL TRP ALA THR LYS PRO ILE LEU          
SEQRES   5 A  149  LYS GLY LYS LYS PHE GLY PRO PHE VAL GLY ASP LYS LYS          
SEQRES   6 A  149  LYS ARG SER GLN VAL LYS ASN ASN VAL TYR MET TRP GLU          
SEQRES   7 A  149  VAL TYR TYR PRO ASN LEU GLY TRP MET CYS ILE ASP ALA          
SEQRES   8 A  149  THR ASP PRO GLU LYS GLY ASN TRP LEU ARG TYR VAL ASN          
SEQRES   9 A  149  TRP ALA CYS SER GLY GLU GLU GLN ASN LEU PHE PRO LEU          
SEQRES  10 A  149  GLU ILE ASN ARG ALA ILE TYR TYR LYS THR LEU LYS PRO          
SEQRES  11 A  149  ILE ALA PRO GLY GLU GLU LEU LEU VAL TRP TYR ASN GLY          
SEQRES  12 A  149  GLU ASP ASN PRO GLU ILE                                      
FORMUL   2  HOH   *145(H2 O)                                                    
HELIX    1   1 THR A   13  VAL A   17  5                                   5    
HELIX    2   2 PRO A   18  GLY A   24  1                                   7    
HELIX    3   3 LYS A   64  VAL A   68  5                                   5    
HELIX    4   4 ASP A   91  GLY A   95  5                                   5    
HELIX    5   5 ASN A   96  VAL A  101  5                                   6    
SHEET    1   A 2 VAL A  29  PRO A  33  0                                        
SHEET    2   A 2 ILE A  41  ALA A  45 -1  O  TRP A  44   N  ARG A  30           
SHEET    1   B 3 LYS A  54  PHE A  55  0                                        
SHEET    2   B 3 ALA A 120  THR A 125 -1  O  TYR A 123   N  PHE A  55           
SHEET    3   B 3 LEU A 112  ILE A 117 -1  N  PHE A 113   O  LYS A 124           
SHEET    1   C 3 ASP A  61  LYS A  63  0                                        
SHEET    2   C 3 GLY A  83  ASP A  88 -1  O  CYS A  86   N  LYS A  63           
SHEET    3   C 3 MET A  74  TYR A  79 -1  N  TRP A  75   O  ILE A  87           
SHEET    1   D 2 ASN A 102  TRP A 103  0                                        
SHEET    2   D 2 LEU A 136  VAL A 137  1  O  VAL A 137   N  ASN A 102           
CISPEP   1 GLY A   56    PRO A   57          0         7.56                     
CRYST1   36.462   51.196   70.887  90.00  90.00  90.00 P 21 21 21    4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.027426  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.019533  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014107        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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