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Database: PDB
Entry: 2EVZ
LinkDB: 2EVZ
Original site: 2EVZ 
HEADER    RNA BINDING PROTEIN                     01-NOV-05   2EVZ              
TITLE     STRUCTURE OF RNA BINDING DOMAINS 3 AND 4 OF POLYPYRIMIDINE TRACT      
TITLE    2 BINDING PROTEIN                                                      
CAVEAT     2EVZ    CHIRALITY ERROR AT THE CA CENTER OF ASP A 100 IN MODEL 1     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: POLYPYRIMIDINE TRACT-BINDING PROTEIN 1;                    
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RNA BINDING DOMAINS 3 AND 4;                               
COMPND   5 SYNONYM: PTB, HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN I, HNRNP I, 57 
COMPND   6 KDA RNA-BINDING PROTEIN PPTB-1;                                      
COMPND   7 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: PTBP1, PTB;                                                    
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)C+RIL;                            
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28A+                                   
KEYWDS    ALPHA-BETA SANDWICH, RNA BINDING PROTEIN                              
EXPDTA    SOLUTION NMR                                                          
NUMMDL    20                                                                    
AUTHOR    F.H.ALLAIN,S.D.AUWETER                                                
REVDAT   4   09-MAR-22 2EVZ    1       REMARK SEQADV                            
REVDAT   3   24-FEB-09 2EVZ    1       VERSN                                    
REVDAT   2   24-JAN-06 2EVZ    1       JRNL                                     
REVDAT   1   17-JAN-06 2EVZ    0                                                
JRNL        AUTH   F.VITALI,A.HENNING,F.C.OBERSTRASS,Y.HARGOUS,S.D.AUWETER,     
JRNL        AUTH 2 M.ERAT,F.H.ALLAIN                                            
JRNL        TITL   STRUCTURE OF THE TWO MOST C-TERMINAL RNA RECOGNITION MOTIFS  
JRNL        TITL 2 OF PTB USING SEGMENTAL ISOTOPE LABELING                      
JRNL        REF    EMBO J.                       V.  25   150 2006              
JRNL        REFN                   ISSN 0261-4189                               
JRNL        PMID   16362043                                                     
JRNL        DOI    10.1038/SJ.EMBOJ.7600911                                     
REMARK   2                                                                      
REMARK   2 RESOLUTION. NOT APPLICABLE.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CYANA 2.0, AMBER 7.0                                 
REMARK   3   AUTHORS     : PETER GUENTERT (CYANA), DAVID A. CASE (AMBER)        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2EVZ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-NOV-05.                  
REMARK 100 THE DEPOSITION ID IS D_1000035159.                                   
REMARK 210                                                                      
REMARK 210 EXPERIMENTAL DETAILS                                                 
REMARK 210  EXPERIMENT TYPE                : NMR                                
REMARK 210  TEMPERATURE           (KELVIN) : 303                                
REMARK 210  PH                             : 6.5                                
REMARK 210  IONIC STRENGTH                 : 20MM NACL, 10MM NA-PHOSPHATE       
REMARK 210  PRESSURE                       : 1 ATM                              
REMARK 210  SAMPLE CONTENTS                : 1MM PTB RBD34 15N; 20MM NACL;      
REMARK 210                                   10MM SODIUM PHOSPHATE; 90% H2O,    
REMARK 210                                   10% D2O; 1MM PTB RBD34 15N, 13C;   
REMARK 210                                   20MM NACL; 10MM SODIUM PHOSPHATE;  
REMARK 210                                   90% H2O, 10% D2O; 1MM PTB RBD34    
REMARK 210                                   15N; 20MM NACL; 10MM SODIUM        
REMARK 210                                   PHOSPHATE; 100% D2O; 1MM PTB       
REMARK 210                                   RBD34 15N, 13C; 20MM NACL; 10MM    
REMARK 210                                   SODIUM PHOSPHATE; 100% D2O; 1MM    
REMARK 210                                   PTB RBD3 15N, 13C, RBD4            
REMARK 210                                   UNLABELED; 20MM NACL; 10MM         
REMARK 210                                   SODIUM PHOSPHATE; 100% D2O; 1MM    
REMARK 210                                   PTB RBD3 UNLABELED, RBD4 13C,      
REMARK 210                                   15N; 20MM NACL; 10MM SODIUM        
REMARK 210                                   PHOSPHATE; 100% D2O                
REMARK 210                                                                      
REMARK 210  NMR EXPERIMENTS CONDUCTED      : HNCA; HNCOCA; CBCACONH; HNCACB;    
REMARK 210                                   3D_15N-SEPARATED_NOESY; 3D_13C-    
REMARK 210                                   SEPARATED_NOESY; HCCH-TOCSY; 2D    
REMARK 210                                   NOESY; 2D F1-EDITED, F2-FITERED    
REMARK 210                                   NOESY; 3D_13C-SEPARATED HALF-      
REMARK 210                                   FILTERED NOESY                     
REMARK 210  SPECTROMETER FIELD STRENGTH    : 900 MHZ; 600 MHZ; 500 MHZ          
REMARK 210  SPECTROMETER MODEL             : AVANCE; DRX                        
REMARK 210  SPECTROMETER MANUFACTURER      : BRUKER                             
REMARK 210                                                                      
REMARK 210  STRUCTURE DETERMINATION.                                            
REMARK 210   SOFTWARE USED                 : NULL                               
REMARK 210   METHOD USED                   : TORSION ANGLE DYNAMICS SIMULATED   
REMARK 210                                   ANNEALING                          
REMARK 210                                                                      
REMARK 210 CONFORMERS, NUMBER CALCULATED   : 30                                 
REMARK 210 CONFORMERS, NUMBER SUBMITTED    : 20                                 
REMARK 210 CONFORMERS, SELECTION CRITERIA  : STRUCTURES WITH THE LEAST          
REMARK 210                                   RESTRAINT VIOLATIONS               
REMARK 210                                                                      
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1                   
REMARK 210                                                                      
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR      
REMARK 210  SPECTROSCOPY.                                                       
REMARK 215                                                                      
REMARK 215 NMR STUDY                                                            
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION           
REMARK 215 NMR DATA.  PROTEIN DATA BANK CONVENTIONS REQUIRE THAT                
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON              
REMARK 215 THESE RECORDS ARE MEANINGLESS.                                       
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 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. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;                   
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                            
REMARK 465   MODELS 1-20                                                        
REMARK 465     RES C SSSEQI                                                     
REMARK 465     MET A   -20                                                      
REMARK 465     GLY A   -19                                                      
REMARK 465     SER A   -18                                                      
REMARK 465     SER A   -17                                                      
REMARK 465     HIS A   -16                                                      
REMARK 465     HIS A   -15                                                      
REMARK 465     HIS A   -14                                                      
REMARK 465     HIS A   -13                                                      
REMARK 465     HIS A   -12                                                      
REMARK 465     HIS A   -11                                                      
REMARK 465     SER A   -10                                                      
REMARK 465     SER A    -9                                                      
REMARK 465     GLY A    -8                                                      
REMARK 465     LEU A    -7                                                      
REMARK 465     VAL A    -6                                                      
REMARK 465     PRO A    -5                                                      
REMARK 465     ARG A    -4                                                      
REMARK 465     GLY A    -3                                                      
REMARK 465     SER A    -2                                                      
REMARK 465     HIS A    -1                                                      
REMARK 465     MET A     0                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
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   C    ASN A    72     H    GLY A    73              1.56            
REMARK 500   H    ASN A   190     O    LEU A   199              1.58            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500  1 PRO A   6   CA    PRO A   6   C       0.131                       
REMARK 500  1 ASN A  13   CA    ASN A  13   CB      0.176                       
REMARK 500  1 VAL A  15   N     VAL A  15   CA     -0.148                       
REMARK 500  1 VAL A  15   CB    VAL A  15   CG2     0.212                       
REMARK 500  1 VAL A  18   N     VAL A  18   CA      0.128                       
REMARK 500  1 VAL A  18   C     VAL A  18   O       0.116                       
REMARK 500  1 SER A  19   CA    SER A  19   CB      0.107                       
REMARK 500  1 SER A  19   CB    SER A  19   OG     -0.110                       
REMARK 500  1 GLU A  24   C     GLU A  24   O      -0.128                       
REMARK 500  1 ARG A  25   C     ARG A  25   O       0.170                       
REMARK 500  1 VAL A  26   CA    VAL A  26   C       0.157                       
REMARK 500  1 GLN A  29   C     SER A  30   N       0.154                       
REMARK 500  1 PHE A  32   CB    PHE A  32   CG      0.107                       
REMARK 500  1 PHE A  32   CG    PHE A  32   CD1     0.142                       
REMARK 500  1 PHE A  35   CE2   PHE A  35   CD2     0.159                       
REMARK 500  1 GLY A  36   N     GLY A  36   CA     -0.091                       
REMARK 500  1 TYR A  38   CE1   TYR A  38   CZ      0.088                       
REMARK 500  1 ASP A  40   CB    ASP A  40   CG      0.140                       
REMARK 500  1 ASP A  40   CA    ASP A  40   C       0.162                       
REMARK 500  1 GLN A  42   CG    GLN A  42   CD      0.162                       
REMARK 500  1 ARG A  43   CD    ARG A  43   NE      0.111                       
REMARK 500  1 VAL A  44   CA    VAL A  44   CB     -0.239                       
REMARK 500  1 LEU A  47   N     LEU A  47   CA      0.139                       
REMARK 500  1 PHE A  48   CG    PHE A  48   CD1     0.148                       
REMARK 500  1 GLU A  52   CD    GLU A  52   OE1     0.073                       
REMARK 500  1 GLU A  52   CD    GLU A  52   OE2    -0.078                       
REMARK 500  1 VAL A  56   CA    VAL A  56   CB     -0.140                       
REMARK 500  1 ALA A  59   CA    ALA A  59   CB      0.161                       
REMARK 500  1 ASP A  60   N     ASP A  60   CA      0.166                       
REMARK 500  1 ASP A  60   CA    ASP A  60   CB      0.167                       
REMARK 500  1 ASN A  62   CB    ASN A  62   CG      0.165                       
REMARK 500  1 ASN A  62   CA    ASN A  62   C       0.188                       
REMARK 500  1 GLN A  63   CD    GLN A  63   OE1     0.138                       
REMARK 500  1 GLN A  65   CA    GLN A  65   CB      0.147                       
REMARK 500  1 LEU A  66   N     LEU A  66   CA     -0.131                       
REMARK 500  1 HIS A  70   CB    HIS A  70   CG      0.113                       
REMARK 500  1 HIS A  74   CG    HIS A  74   CD2     0.066                       
REMARK 500  1 HIS A  74   CE1   HIS A  74   NE2    -0.101                       
REMARK 500  1 HIS A  77   CE1   HIS A  77   NE2    -0.071                       
REMARK 500  1 SER A  86   CA    SER A  86   CB      0.090                       
REMARK 500  1 VAL A  91   CB    VAL A  91   CG1     0.132                       
REMARK 500  1 GLU A  96   CA    GLU A  96   CB      0.153                       
REMARK 500  1 ASP A 100   CA    ASP A 100   CB      0.135                       
REMARK 500  1 ASP A 100   CB    ASP A 100   CG      0.180                       
REMARK 500  1 GLN A 101   C     GLY A 102   N       0.139                       
REMARK 500  1 ASP A 106   N     ASP A 106   CA     -0.123                       
REMARK 500  1 SER A 110   C     SER A 110   O       0.126                       
REMARK 500  1 LEU A 112   C     LEU A 112   O       0.130                       
REMARK 500  1 PHE A 115   CG    PHE A 115   CD1     0.104                       
REMARK 500  1 GLY A 119   N     GLY A 119   CA      0.145                       
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     253 BOND DEVIATIONS.                              
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  1 ARG A   2   CD  -  NE  -  CZ  ANGL. DEV. =  12.6 DEGREES          
REMARK 500  1 ILE A   3   CA  -  C   -  N   ANGL. DEV. =  14.0 DEGREES          
REMARK 500  1 LEU A   8   CA  -  C   -  O   ANGL. DEV. =  14.9 DEGREES          
REMARK 500  1 ALA A  11   N   -  CA  -  CB  ANGL. DEV. =  16.6 DEGREES          
REMARK 500  1 GLY A  12   CA  -  C   -  N   ANGL. DEV. = -13.5 DEGREES          
REMARK 500  1 ASN A  13   N   -  CA  -  CB  ANGL. DEV. = -16.3 DEGREES          
REMARK 500  1 SER A  14   CA  -  C   -  N   ANGL. DEV. =  17.8 DEGREES          
REMARK 500  1 SER A  14   O   -  C   -  N   ANGL. DEV. = -23.5 DEGREES          
REMARK 500  1 VAL A  15   C   -  N   -  CA  ANGL. DEV. =  16.0 DEGREES          
REMARK 500  1 LEU A  16   CB  -  CG  -  CD1 ANGL. DEV. = -12.6 DEGREES          
REMARK 500  1 LEU A  17   CA  -  C   -  O   ANGL. DEV. =  13.0 DEGREES          
REMARK 500  1 VAL A  18   C   -  N   -  CA  ANGL. DEV. =  16.8 DEGREES          
REMARK 500  1 VAL A  18   CA  -  CB  -  CG2 ANGL. DEV. = -11.9 DEGREES          
REMARK 500  1 SER A  19   N   -  CA  -  CB  ANGL. DEV. = -11.7 DEGREES          
REMARK 500  1 ASN A  20   CA  -  C   -  O   ANGL. DEV. =  14.2 DEGREES          
REMARK 500  1 ASN A  20   O   -  C   -  N   ANGL. DEV. = -12.2 DEGREES          
REMARK 500  1 LEU A  21   N   -  CA  -  CB  ANGL. DEV. = -12.6 DEGREES          
REMARK 500  1 LEU A  21   CA  -  CB  -  CG  ANGL. DEV. =  26.0 DEGREES          
REMARK 500  1 LEU A  21   CB  -  CG  -  CD1 ANGL. DEV. =  19.8 DEGREES          
REMARK 500  1 ASN A  22   CA  -  CB  -  CG  ANGL. DEV. =  13.9 DEGREES          
REMARK 500  1 ASN A  22   O   -  C   -  N   ANGL. DEV. = -12.6 DEGREES          
REMARK 500  1 PRO A  23   C   -  N   -  CA  ANGL. DEV. =  11.8 DEGREES          
REMARK 500  1 PRO A  23   C   -  N   -  CD  ANGL. DEV. = -14.6 DEGREES          
REMARK 500  1 GLU A  24   N   -  CA  -  CB  ANGL. DEV. = -11.2 DEGREES          
REMARK 500  1 GLU A  24   CA  -  C   -  O   ANGL. DEV. =  15.3 DEGREES          
REMARK 500  1 ARG A  25   NH1 -  CZ  -  NH2 ANGL. DEV. = -14.6 DEGREES          
REMARK 500  1 ARG A  25   NE  -  CZ  -  NH1 ANGL. DEV. =   3.9 DEGREES          
REMARK 500  1 ARG A  25   NE  -  CZ  -  NH2 ANGL. DEV. =   4.6 DEGREES          
REMARK 500  1 VAL A  26   CG1 -  CB  -  CG2 ANGL. DEV. = -16.1 DEGREES          
REMARK 500  1 VAL A  26   CA  -  CB  -  CG2 ANGL. DEV. =   9.5 DEGREES          
REMARK 500  1 THR A  27   CA  -  CB  -  CG2 ANGL. DEV. =  12.1 DEGREES          
REMARK 500  1 LEU A  31   CB  -  CA  -  C   ANGL. DEV. =  12.0 DEGREES          
REMARK 500  1 LEU A  31   O   -  C   -  N   ANGL. DEV. = -10.2 DEGREES          
REMARK 500  1 PHE A  32   CB  -  CG  -  CD2 ANGL. DEV. = -13.4 DEGREES          
REMARK 500  1 PHE A  32   CB  -  CG  -  CD1 ANGL. DEV. =  13.6 DEGREES          
REMARK 500  1 LEU A  34   CA  -  CB  -  CG  ANGL. DEV. =  15.9 DEGREES          
REMARK 500  1 LEU A  34   CB  -  CG  -  CD1 ANGL. DEV. = -11.3 DEGREES          
REMARK 500  1 LEU A  34   CB  -  CG  -  CD2 ANGL. DEV. =  17.0 DEGREES          
REMARK 500  1 PHE A  35   CD1 -  CE1 -  CZ  ANGL. DEV. = -12.5 DEGREES          
REMARK 500  1 PHE A  35   CE1 -  CZ  -  CE2 ANGL. DEV. =  18.0 DEGREES          
REMARK 500  1 PHE A  35   CZ  -  CE2 -  CD2 ANGL. DEV. = -13.5 DEGREES          
REMARK 500  1 VAL A  37   CG1 -  CB  -  CG2 ANGL. DEV. = -11.0 DEGREES          
REMARK 500  1 VAL A  37   CA  -  CB  -  CG2 ANGL. DEV. =  24.5 DEGREES          
REMARK 500  1 TYR A  38   CB  -  CG  -  CD2 ANGL. DEV. =   4.5 DEGREES          
REMARK 500  1 TYR A  38   CD1 -  CG  -  CD2 ANGL. DEV. =  -8.7 DEGREES          
REMARK 500  1 TYR A  38   CG  -  CD2 -  CE2 ANGL. DEV. =   9.5 DEGREES          
REMARK 500  1 TYR A  38   O   -  C   -  N   ANGL. DEV. =  11.8 DEGREES          
REMARK 500  1 ASP A  40   CB  -  CG  -  OD1 ANGL. DEV. =  12.1 DEGREES          
REMARK 500  1 ASP A  40   CB  -  CG  -  OD2 ANGL. DEV. = -10.2 DEGREES          
REMARK 500  1 GLN A  42   CA  -  C   -  O   ANGL. DEV. =  15.0 DEGREES          
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     688 ANGLE DEVIATIONS.                             
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  1 ARG A   2       75.43    -58.31                                   
REMARK 500  1 ILE A   3     -136.71   -116.76                                   
REMARK 500  1 ALA A   4       19.16     43.91                                   
REMARK 500  1 ILE A   5       38.49   -169.95                                   
REMARK 500  1 LEU A   8      -68.02     32.52                                   
REMARK 500  1 ALA A   9      -74.35    -64.50                                   
REMARK 500  1 ASN A  13       -6.73   -146.99                                   
REMARK 500  1 SER A  14      -60.03     65.67                                   
REMARK 500  1 VAL A  15       88.97    -48.81                                   
REMARK 500  1 ASN A  20       34.12     88.06                                   
REMARK 500  1 PRO A  23      -71.25    -34.76                                   
REMARK 500  1 VAL A  41      125.29    -33.80                                   
REMARK 500  1 PHE A  48      -64.41     -8.37                                   
REMARK 500  1 ASN A  49       16.63   -153.11                                   
REMARK 500  1 LYS A  50      -70.87    -90.44                                   
REMARK 500  1 ASP A  60     -166.97    175.46                                   
REMARK 500  1 ASN A  72       89.15    -47.29                                   
REMARK 500  1 LYS A  75       62.10     32.18                                   
REMARK 500  1 PRO A  80       79.18    -49.50                                   
REMARK 500  1 ILE A  81      141.88    -37.10                                   
REMARK 500  1 THR A  84     -153.85   -136.32                                   
REMARK 500  1 SER A  86      -36.89   -140.92                                   
REMARK 500  1 LYS A  87      -34.45     57.77                                   
REMARK 500  1 HIS A  88       79.58    -29.08                                   
REMARK 500  1 GLN A  89      -97.69     30.53                                   
REMARK 500  1 LEU A  93      122.31    -26.78                                   
REMARK 500  1 PRO A  94      -87.88   -102.62                                   
REMARK 500  1 GLU A  96      -73.09    -36.44                                   
REMARK 500  1 ASP A 100       -6.01     -8.67                                   
REMARK 500  1 GLN A 101      -59.16   -164.95                                   
REMARK 500  1 ASN A 109       60.23   -102.53                                   
REMARK 500  1 HIS A 113     -108.91     45.39                                   
REMARK 500  1 ARG A 114      -24.56    116.08                                   
REMARK 500  1 PHE A 115      -84.26    -76.21                                   
REMARK 500  1 LYS A 121       85.12   -158.04                                   
REMARK 500  1 ILE A 126      -53.77     -8.78                                   
REMARK 500  1 PHE A 127      108.15     43.23                                   
REMARK 500  1 PRO A 129       88.82      1.47                                   
REMARK 500  1 ASN A 137      100.64     59.85                                   
REMARK 500  1 SER A 141      -62.26   -108.65                                   
REMARK 500  1 PHE A 151        1.68    -57.83                                   
REMARK 500  1 VAL A 158       70.53      7.87                                   
REMARK 500  1 PHE A 164     -162.44    -37.04                                   
REMARK 500  1 LYS A 166      -95.72     22.90                                   
REMARK 500  1 ASP A 167      -70.29     -2.61                                   
REMARK 500  1 ARG A 168       81.08     78.86                                   
REMARK 500  1 LYS A 169      -69.72   -127.45                                   
REMARK 500  1 MET A 170      159.88    -38.03                                   
REMARK 500  1 MET A 175     -171.75    -52.99                                   
REMARK 500  1 GLU A 179      -36.37    -28.26                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     672 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 PRO A   94     ARG A   95          1      -141.27                    
REMARK 500 PRO A  128     PRO A  129         19      -145.08                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500  1 ARG A   2         0.10    SIDE CHAIN                              
REMARK 500  1 ARG A  25         0.14    SIDE CHAIN                              
REMARK 500  1 PHE A  32         0.08    SIDE CHAIN                              
REMARK 500  1 TYR A  38         0.12    SIDE CHAIN                              
REMARK 500  1 PHE A  48         0.13    SIDE CHAIN                              
REMARK 500  1 ASN A  49         0.07    SIDE CHAIN                              
REMARK 500  1 ASN A  53         0.09    SIDE CHAIN                              
REMARK 500  1 HIS A  70         0.14    SIDE CHAIN                              
REMARK 500  1 ASN A  72         0.10    SIDE CHAIN                              
REMARK 500  1 HIS A  74         0.19    SIDE CHAIN                              
REMARK 500  1 HIS A  77         0.07    SIDE CHAIN                              
REMARK 500  1 ARG A  82         0.29    SIDE CHAIN                              
REMARK 500  1 HIS A  88         0.18    SIDE CHAIN                              
REMARK 500  1 ARG A  95         0.36    SIDE CHAIN                              
REMARK 500  1 HIS A 113         0.13    SIDE CHAIN                              
REMARK 500  1 PHE A 115         0.09    SIDE CHAIN                              
REMARK 500  1 PHE A 123         0.10    SIDE CHAIN                              
REMARK 500  1 ASN A 125         0.08    SIDE CHAIN                              
REMARK 500  1 PHE A 127         0.16    SIDE CHAIN                              
REMARK 500  1 HIS A 134         0.10    SIDE CHAIN                              
REMARK 500  1 GLU A 145         0.08    SIDE CHAIN                              
REMARK 500  1 ASP A 146         0.10    SIDE CHAIN                              
REMARK 500  1 PHE A 161         0.14    SIDE CHAIN                              
REMARK 500  1 PHE A 163         0.09    SIDE CHAIN                              
REMARK 500  1 GLU A 179         0.07    SIDE CHAIN                              
REMARK 500  1 GLU A 180         0.08    SIDE CHAIN                              
REMARK 500  1 HIS A 189         0.10    SIDE CHAIN                              
REMARK 500  1 HIS A 191         0.19    SIDE CHAIN                              
REMARK 500  1 HIS A 197         0.21    SIDE CHAIN                              
REMARK 500  1 ARG A 200         0.26    SIDE CHAIN                              
REMARK 500 10 ARG A  43         0.09    SIDE CHAIN                              
REMARK 500 13 ARG A  43         0.10    SIDE CHAIN                              
REMARK 500 18 ARG A 114         0.09    SIDE CHAIN                              
REMARK 500 19 ARG A   2         0.12    SIDE CHAIN                              
REMARK 500 19 ASN A  20         0.08    SIDE CHAIN                              
REMARK 500 19 ARG A  25         0.16    SIDE CHAIN                              
REMARK 500 19 TYR A  38         0.11    SIDE CHAIN                              
REMARK 500 19 PHE A  48         0.12    SIDE CHAIN                              
REMARK 500 19 ASN A  53         0.10    SIDE CHAIN                              
REMARK 500 19 HIS A  70         0.12    SIDE CHAIN                              
REMARK 500 19 HIS A  74         0.09    SIDE CHAIN                              
REMARK 500 19 HIS A  77         0.13    SIDE CHAIN                              
REMARK 500 19 ARG A  82         0.13    SIDE CHAIN                              
REMARK 500 19 ARG A  95         0.11    SIDE CHAIN                              
REMARK 500 19 TYR A 107         0.11    SIDE CHAIN                              
REMARK 500 19 ASN A 122         0.09    SIDE CHAIN                              
REMARK 500 19 PHE A 123         0.13    SIDE CHAIN                              
REMARK 500 19 GLN A 124         0.09    SIDE CHAIN                              
REMARK 500 19 PHE A 151         0.18    SIDE CHAIN                              
REMARK 500 19 PHE A 161         0.09    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      82 PLANE DEVIATIONS.                             
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500  1 ALA A   9        -11.92                                           
REMARK 500  1 ASN A  13         18.13                                           
REMARK 500  1 SER A  14         12.87                                           
REMARK 500  1 ARG A  25        -10.01                                           
REMARK 500  1 PHE A  32         10.77                                           
REMARK 500  1 GLY A  36        -16.71                                           
REMARK 500  1 LEU A  47        -12.54                                           
REMARK 500  1 PHE A  48        -13.29                                           
REMARK 500  1 LYS A  51         10.11                                           
REMARK 500  1 ALA A  54         15.48                                           
REMARK 500  1 LEU A  55         11.34                                           
REMARK 500  1 ASP A  60         12.61                                           
REMARK 500  1 MET A  68        -21.24                                           
REMARK 500  1 HIS A  70         15.56                                           
REMARK 500  1 SER A  86        -13.26                                           
REMARK 500  1 GLN A  92         14.01                                           
REMARK 500  1 GLY A  97        -13.80                                           
REMARK 500  1 ASP A 100         14.01                                           
REMARK 500  1 GLY A 102         15.70                                           
REMARK 500  1 THR A 104        -24.67                                           
REMARK 500  1 GLN A 124         13.96                                           
REMARK 500  1 ALA A 131         12.71                                           
REMARK 500  1 LEU A 135         13.35                                           
REMARK 500  1 ASN A 137        -13.73                                           
REMARK 500  1 SER A 152        -16.17                                           
REMARK 500  1 VAL A 158         11.91                                           
REMARK 500  1 LYS A 159        -15.84                                           
REMARK 500  1 MET A 170        -10.55                                           
REMARK 500  1 GLU A 180         10.89                                           
REMARK 500  1 ALA A 181        -12.21                                           
REMARK 500  1 VAL A 182        -10.04                                           
REMARK 500  1 LEU A 185         18.12                                           
REMARK 500  1 ILE A 186         13.21                                           
REMARK 500  1 HIS A 198        -12.27                                           
REMARK 500 19 ALA A   9         14.40                                           
REMARK 500 19 VAL A  18         11.96                                           
REMARK 500 19 SER A  19        -11.99                                           
REMARK 500 19 ASN A  20        -10.81                                           
REMARK 500 19 ILE A  33         10.27                                           
REMARK 500 19 GLY A  39         10.19                                           
REMARK 500 19 LYS A  45        -18.36                                           
REMARK 500 19 MET A  58        -13.43                                           
REMARK 500 19 ASP A  60         10.58                                           
REMARK 500 19 ASN A  62        -15.34                                           
REMARK 500 19 HIS A  74        -16.69                                           
REMARK 500 19 GLY A  78        -12.85                                           
REMARK 500 19 LYS A  79         16.74                                           
REMARK 500 19 SER A  86        -13.44                                           
REMARK 500 19 ASP A 100         13.61                                           
REMARK 500 19 LEU A 112        -12.24                                           
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      96 MAIN CHAIN PLANARITY DEVIATIONS.              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  2EVZ A    1   208  UNP    P26599   PTBP1_HUMAN    324    531             
SEQADV 2EVZ MET A  -20  UNP  P26599              CLONING ARTIFACT               
SEQADV 2EVZ GLY A  -19  UNP  P26599              CLONING ARTIFACT               
SEQADV 2EVZ SER A  -18  UNP  P26599              CLONING ARTIFACT               
SEQADV 2EVZ SER A  -17  UNP  P26599              CLONING ARTIFACT               
SEQADV 2EVZ HIS A  -16  UNP  P26599              EXPRESSION TAG                 
SEQADV 2EVZ HIS A  -15  UNP  P26599              EXPRESSION TAG                 
SEQADV 2EVZ HIS A  -14  UNP  P26599              EXPRESSION TAG                 
SEQADV 2EVZ HIS A  -13  UNP  P26599              EXPRESSION TAG                 
SEQADV 2EVZ HIS A  -12  UNP  P26599              EXPRESSION TAG                 
SEQADV 2EVZ HIS A  -11  UNP  P26599              EXPRESSION TAG                 
SEQADV 2EVZ SER A  -10  UNP  P26599              CLONING ARTIFACT               
SEQADV 2EVZ SER A   -9  UNP  P26599              CLONING ARTIFACT               
SEQADV 2EVZ GLY A   -8  UNP  P26599              CLONING ARTIFACT               
SEQADV 2EVZ LEU A   -7  UNP  P26599              CLONING ARTIFACT               
SEQADV 2EVZ VAL A   -6  UNP  P26599              CLONING ARTIFACT               
SEQADV 2EVZ PRO A   -5  UNP  P26599              CLONING ARTIFACT               
SEQADV 2EVZ ARG A   -4  UNP  P26599              CLONING ARTIFACT               
SEQADV 2EVZ GLY A   -3  UNP  P26599              CLONING ARTIFACT               
SEQADV 2EVZ SER A   -2  UNP  P26599              CLONING ARTIFACT               
SEQADV 2EVZ HIS A   -1  UNP  P26599              CLONING ARTIFACT               
SEQADV 2EVZ MET A    0  UNP  P26599              CLONING ARTIFACT               
SEQRES   1 A  229  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  229  LEU VAL PRO ARG GLY SER HIS MET GLY ARG ILE ALA ILE          
SEQRES   3 A  229  PRO GLY LEU ALA GLY ALA GLY ASN SER VAL LEU LEU VAL          
SEQRES   4 A  229  SER ASN LEU ASN PRO GLU ARG VAL THR PRO GLN SER LEU          
SEQRES   5 A  229  PHE ILE LEU PHE GLY VAL TYR GLY ASP VAL GLN ARG VAL          
SEQRES   6 A  229  LYS ILE LEU PHE ASN LYS LYS GLU ASN ALA LEU VAL GLN          
SEQRES   7 A  229  MET ALA ASP GLY ASN GLN ALA GLN LEU ALA MET SER HIS          
SEQRES   8 A  229  LEU ASN GLY HIS LYS LEU HIS GLY LYS PRO ILE ARG ILE          
SEQRES   9 A  229  THR LEU SER LYS HIS GLN ASN VAL GLN LEU PRO ARG GLU          
SEQRES  10 A  229  GLY GLN GLU ASP GLN GLY LEU THR LYS ASP TYR GLY ASN          
SEQRES  11 A  229  SER PRO LEU HIS ARG PHE LYS LYS PRO GLY SER LYS ASN          
SEQRES  12 A  229  PHE GLN ASN ILE PHE PRO PRO SER ALA THR LEU HIS LEU          
SEQRES  13 A  229  SER ASN ILE PRO PRO SER VAL SER GLU GLU ASP LEU LYS          
SEQRES  14 A  229  VAL LEU PHE SER SER ASN GLY GLY VAL VAL LYS GLY PHE          
SEQRES  15 A  229  LYS PHE PHE GLN LYS ASP ARG LYS MET ALA LEU ILE GLN          
SEQRES  16 A  229  MET GLY SER VAL GLU GLU ALA VAL GLN ALA LEU ILE ASP          
SEQRES  17 A  229  LEU HIS ASN HIS ASP LEU GLY GLU ASN HIS HIS LEU ARG          
SEQRES  18 A  229  VAL SER PHE SER LYS SER THR ILE                              
HELIX    1   1 THR A   27  GLY A   39  1                                  13    
HELIX    2   2 ASP A   60  ASN A   72  1                                  13    
HELIX    3   3 ARG A   95  ASP A  100  1                                   6    
HELIX    4   4 SER A  143  ASN A  154  1                                  12    
HELIX    5   5 SER A  177  HIS A  189  1                                  13    
SHEET    1   A 5 ARG A  82  LEU A  85  0                                        
SHEET    2   A 5 VAL A  15  SER A  19 -1  N  SER A  19   O  ARG A  82           
SHEET    3   A 5 ASN A  53  GLN A  57 -1  O  VAL A  56   N  LEU A  16           
SHEET    4   A 5 ARG A  43  ILE A  46 -1  N  ARG A  43   O  GLN A  57           
SHEET    5   A 5 THR A 104  LYS A 105 -1  O  LYS A 105   N  VAL A  44           
SHEET    1   B 4 GLY A 160  PHE A 163  0                                        
SHEET    2   B 4 ALA A 171  GLN A 174 -1  O  LEU A 172   N  LYS A 162           
SHEET    3   B 4 LEU A 133  SER A 136 -1  N  LEU A 133   O  ILE A 173           
SHEET    4   B 4 ARG A 200  PHE A 203 -1  O  ARG A 200   N  SER A 136           
CRYST1    1.000    1.000    1.000  90.00  90.00  90.00 P 1           1          
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      1.000000  0.000000  0.000000        0.00000                         
SCALE2      0.000000  1.000000  0.000000        0.00000                         
SCALE3      0.000000  0.000000  1.000000        0.00000                         
MODEL        1                                                                  
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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