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Database: PDB
Entry: 2I1Y
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Original site: 2I1Y 
HEADER    HYDROLASE                               15-AUG-06   2I1Y              
TITLE     CRYSTAL STRUCTURE OF THE PHOSPHATASE DOMAIN OF HUMAN PTP IA-2         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE;                
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: TYROSINE-PROTEIN PHOSPHATASE;                              
COMPND   5 SYNONYM: R-PTP-N, PTP IA-2, ISLET CELL ANTIGEN 512, ICA 512, ISLET   
COMPND   6 CELL AUTOANTIGEN 3;                                                  
COMPND   7 EC: 3.1.3.48;                                                        
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: PTPRN, ICA3, ICA512;                                           
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) CODON+ RIL;                      
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID                               
KEYWDS    RECEPTOR-TYPE PROTEIN TYROSINE PHOSPHATASE PRECURSOR, PHOSPHATASE,    
KEYWDS   2 STRUCTURAL GENOMICS, PSI, PROTEIN STRUCTURE INITIATIVE, NEW YORK SGX 
KEYWDS   3 RESEARCH CENTER FOR STRUCTURAL GENOMICS, NYSGXRC, HYDROLASE          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.FABER-BARATA,Y.PATSKOVSKY,J.ALVARADO,D.SMITH,J.KOSS,S.R.WASSERMAN,  
AUTHOR   2 S.OZYURT,S.ATWELL,A.POWELL,M.C.KEARINS,M.MALETIC,I.ROONEY,K.T.BAIN,  
AUTHOR   3 M.FREEMAN,J.C.RUSSELL,D.A.THOMPSON,S.K.BURLEY,S.C.ALMO,NEW YORK SGX  
AUTHOR   4 RESEARCH CENTER FOR STRUCTURAL GENOMICS (NYSGXRC)                    
REVDAT   3   13-JUL-11 2I1Y    1       VERSN                                    
REVDAT   2   25-MAR-08 2I1Y    1       JRNL   VERSN                             
REVDAT   1   29-AUG-06 2I1Y    0                                                
JRNL        AUTH   S.C.ALMO,J.B.BONANNO,J.M.SAUDER,S.EMTAGE,T.P.DILORENZO,      
JRNL        AUTH 2 V.MALASHKEVICH,S.R.WASSERMAN,S.SWAMINATHAN,S.ESWARAMOORTHY,  
JRNL        AUTH 3 R.AGARWAL,D.KUMARAN,M.MADEGOWDA,S.RAGUMANI,Y.PATSKOVSKY,     
JRNL        AUTH 4 J.ALVARADO,U.A.RAMAGOPAL,J.FABER-BARATA,M.R.CHANCE,A.SALI,   
JRNL        AUTH 5 A.FISER,Z.Y.ZHANG,D.S.LAWRENCE,S.K.BURLEY                    
JRNL        TITL   STRUCTURAL GENOMICS OF PROTEIN PHOSPHATASES                  
JRNL        REF    J.STRUCT.FUNCT.GENOM.         V.   8   121 2007              
JRNL        REFN                   ISSN 1345-711X                               
JRNL        PMID   18058037                                                     
JRNL        DOI    10.1007/S10969-007-9036-1                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.23 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.23                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.73                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 31493                          
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) : 0.201                           
REMARK   3   R VALUE            (WORKING SET) : 0.199                           
REMARK   3   FREE R VALUE                     : 0.267                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.200                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1035                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.23                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.29                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2177                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 95.25                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3290                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 67                           
REMARK   3   BIN FREE R VALUE                    : 0.4140                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4623                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 12                                      
REMARK   3   SOLVENT ATOMS            : 306                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 30.08                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.02000                                              
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : -0.01000                                             
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): 0.300         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.241         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.196         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.039         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.942                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.894                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4813 ; 0.008 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6535 ; 1.146 ; 1.947       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   594 ;11.151 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   225 ;38.199 ;23.289       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   824 ;19.892 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    41 ;18.201 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   714 ; 0.243 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3668 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1971 ; 0.165 ; 0.300       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  3164 ; 0.300 ; 0.500       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   436 ; 0.204 ; 0.500       
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):    60 ; 0.153 ; 0.300       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    19 ; 0.201 ; 0.500       
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):  2995 ; 4.015 ; 2.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4738 ; 5.526 ; 3.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2068 ; 6.788 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1789 ; 9.484 ; 5.000       
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 : 2                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A    691       A     771      1                      
REMARK   3           1     B    687       B     771      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   1    A    (A):    615 ;  0.11 ;  0.10           
REMARK   3   TIGHT THERMAL      1    A (A**2):    615 ;  0.85 ;  2.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 2                                  
REMARK   3     CHAIN NAMES                    : A B                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A    778       A     977      1                      
REMARK   3           1     B    778       B     976      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   2    A    (A):   1575 ;  0.12 ;  0.10           
REMARK   3   TIGHT THERMAL      2    A (A**2):   1575 ;  0.91 ;  2.00           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 2I1Y COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-AUG-06.                  
REMARK 100 THE RCSB ID CODE IS RCSB039034.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-APR-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 31-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97931                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 32726                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.230                              
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     (%) : 98.7                               
REMARK 200  DATA REDUNDANCY                : 6.800                              
REMARK 200  R MERGE                    (I) : 0.22500                            
REMARK 200  R SYM                      (I) : 0.19100                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 2.7000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.23                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.34                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.90                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 0.500                              
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: PDB ENTRY 2FH7                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.56                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.23                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG3350, 100 MM BIS-TRIS, 200 MM     
REMARK 280  AMMONIUM ACETATE, PH 6.0, 10% GLYCEROL, VAPOR DIFFUSION, SITTING    
REMARK 280  DROP, TEMPERATURE 294K                                              
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       36.45350            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       60.53350            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       37.11450            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       60.53350            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.45350            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       37.11450            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     SER A   679                                                      
REMARK 465     LEU A   680                                                      
REMARK 465     GLU A   681                                                      
REMARK 465     PRO A   682                                                      
REMARK 465     ALA A   683                                                      
REMARK 465     GLN A   684                                                      
REMARK 465     ALA A   685                                                      
REMARK 465     ASN A   686                                                      
REMARK 465     MET A   687                                                      
REMARK 465     ASP A   688                                                      
REMARK 465     ILE A   689                                                      
REMARK 465     SER A   690                                                      
REMARK 465     PRO A   978                                                      
REMARK 465     GLN A   979                                                      
REMARK 465     SER B   679                                                      
REMARK 465     LEU B   680                                                      
REMARK 465     GLU B   681                                                      
REMARK 465     PRO B   682                                                      
REMARK 465     ALA B   683                                                      
REMARK 465     GLN B   684                                                      
REMARK 465     ALA B   685                                                      
REMARK 465     ASN B   686                                                      
REMARK 465     LEU B   977                                                      
REMARK 465     PRO B   978                                                      
REMARK 465     GLN B   979                                                      
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 B 935    CB   CG   CD   OE1  OE2                             
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     GLN A  720   NE2                                                 
REMARK 480     ARG A  761   NH2                                                 
REMARK 480     ASP A  826   OD2                                                 
REMARK 480     ARG A  885   NH2                                                 
REMARK 480     ARG A  954   NH1                                                 
REMARK 480     ILE A  973   N                                                   
REMARK 480     GLN B  720   NE2                                                 
REMARK 480     ARG B  761   NH2                                                 
REMARK 480     ASP B  826   OD2                                                 
REMARK 480     ARG B  954   NH1                                                 
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 750   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 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    ASN A 724       15.25   -142.84                                   
REMARK 500    ASP A 815       70.71     12.48                                   
REMARK 500    HIS A 833     -111.19     51.46                                   
REMARK 500    CYS A 909     -114.94   -129.72                                   
REMARK 500    SER A 910      -64.89   -100.81                                   
REMARK 500    ALA A 913      -47.11   -136.45                                   
REMARK 500    VAL A 953       96.06     63.00                                   
REMARK 500    ASN B 724       13.16   -149.03                                   
REMARK 500    GLU B 772     -100.19    -88.19                                   
REMARK 500    ASP B 815     -104.65     38.68                                   
REMARK 500    HIS B 833     -114.37     53.24                                   
REMARK 500    CYS B 909     -115.91   -128.77                                   
REMARK 500    SER B 910      -67.58   -101.08                                   
REMARK 500    GLU B 935      109.28    -52.94                                   
REMARK 500    VAL B 953       93.19     65.80                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ILE A  771     GLU A  772                  141.15                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    MET B 694        24.2      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH B3362        DISTANCE =  6.18 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 3288                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 3287                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: NYSGXRC-8620A   RELATED DB: TARGETDB                     
DBREF  2I1Y A  681   979  UNP    Q16849   PTPRN_HUMAN    681    979             
DBREF  2I1Y B  681   979  UNP    Q16849   PTPRN_HUMAN    681    979             
SEQADV 2I1Y SER A  679  UNP  Q16849              CLONING ARTIFACT               
SEQADV 2I1Y LEU A  680  UNP  Q16849              CLONING ARTIFACT               
SEQADV 2I1Y SER B  679  UNP  Q16849              CLONING ARTIFACT               
SEQADV 2I1Y LEU B  680  UNP  Q16849              CLONING ARTIFACT               
SEQRES   1 A  301  SER LEU GLU PRO ALA GLN ALA ASN MET ASP ILE SER THR          
SEQRES   2 A  301  GLY HIS MET ILE LEU ALA TYR MET GLU ASP HIS LEU ARG          
SEQRES   3 A  301  ASN ARG ASP ARG LEU ALA LYS GLU TRP GLN ALA LEU CYS          
SEQRES   4 A  301  ALA TYR GLN ALA GLU PRO ASN THR CYS ALA THR ALA GLN          
SEQRES   5 A  301  GLY GLU GLY ASN ILE LYS LYS ASN ARG HIS PRO ASP PHE          
SEQRES   6 A  301  LEU PRO TYR ASP HIS ALA ARG ILE LYS LEU LYS VAL GLU          
SEQRES   7 A  301  SER SER PRO SER ARG SER ASP TYR ILE ASN ALA SER PRO          
SEQRES   8 A  301  ILE ILE GLU HIS ASP PRO ARG MET PRO ALA TYR ILE ALA          
SEQRES   9 A  301  THR GLN GLY PRO LEU SER HIS THR ILE ALA ASP PHE TRP          
SEQRES  10 A  301  GLN MET VAL TRP GLU SER GLY CYS THR VAL ILE VAL MET          
SEQRES  11 A  301  LEU THR PRO LEU VAL GLU ASP GLY VAL LYS GLN CYS ASP          
SEQRES  12 A  301  ARG TYR TRP PRO ASP GLU GLY ALA SER LEU TYR HIS VAL          
SEQRES  13 A  301  TYR GLU VAL ASN LEU VAL SER GLU HIS ILE TRP CYS GLU          
SEQRES  14 A  301  ASP PHE LEU VAL ARG SER PHE TYR LEU LYS ASN VAL GLN          
SEQRES  15 A  301  THR GLN GLU THR ARG THR LEU THR GLN PHE HIS PHE LEU          
SEQRES  16 A  301  SER TRP PRO ALA GLU GLY THR PRO ALA SER THR ARG PRO          
SEQRES  17 A  301  LEU LEU ASP PHE ARG ARG LYS VAL ASN LYS CYS TYR ARG          
SEQRES  18 A  301  GLY ARG SER CYS PRO ILE ILE VAL HIS CYS SER ASP GLY          
SEQRES  19 A  301  ALA GLY ARG THR GLY THR TYR ILE LEU ILE ASP MET VAL          
SEQRES  20 A  301  LEU ASN ARG MET ALA LYS GLY VAL LYS GLU ILE ASP ILE          
SEQRES  21 A  301  ALA ALA THR LEU GLU HIS VAL ARG ASP GLN ARG PRO GLY          
SEQRES  22 A  301  LEU VAL ARG SER LYS ASP GLN PHE GLU PHE ALA LEU THR          
SEQRES  23 A  301  ALA VAL ALA GLU GLU VAL ASN ALA ILE LEU LYS ALA LEU          
SEQRES  24 A  301  PRO GLN                                                      
SEQRES   1 B  301  SER LEU GLU PRO ALA GLN ALA ASN MET ASP ILE SER THR          
SEQRES   2 B  301  GLY HIS MET ILE LEU ALA TYR MET GLU ASP HIS LEU ARG          
SEQRES   3 B  301  ASN ARG ASP ARG LEU ALA LYS GLU TRP GLN ALA LEU CYS          
SEQRES   4 B  301  ALA TYR GLN ALA GLU PRO ASN THR CYS ALA THR ALA GLN          
SEQRES   5 B  301  GLY GLU GLY ASN ILE LYS LYS ASN ARG HIS PRO ASP PHE          
SEQRES   6 B  301  LEU PRO TYR ASP HIS ALA ARG ILE LYS LEU LYS VAL GLU          
SEQRES   7 B  301  SER SER PRO SER ARG SER ASP TYR ILE ASN ALA SER PRO          
SEQRES   8 B  301  ILE ILE GLU HIS ASP PRO ARG MET PRO ALA TYR ILE ALA          
SEQRES   9 B  301  THR GLN GLY PRO LEU SER HIS THR ILE ALA ASP PHE TRP          
SEQRES  10 B  301  GLN MET VAL TRP GLU SER GLY CYS THR VAL ILE VAL MET          
SEQRES  11 B  301  LEU THR PRO LEU VAL GLU ASP GLY VAL LYS GLN CYS ASP          
SEQRES  12 B  301  ARG TYR TRP PRO ASP GLU GLY ALA SER LEU TYR HIS VAL          
SEQRES  13 B  301  TYR GLU VAL ASN LEU VAL SER GLU HIS ILE TRP CYS GLU          
SEQRES  14 B  301  ASP PHE LEU VAL ARG SER PHE TYR LEU LYS ASN VAL GLN          
SEQRES  15 B  301  THR GLN GLU THR ARG THR LEU THR GLN PHE HIS PHE LEU          
SEQRES  16 B  301  SER TRP PRO ALA GLU GLY THR PRO ALA SER THR ARG PRO          
SEQRES  17 B  301  LEU LEU ASP PHE ARG ARG LYS VAL ASN LYS CYS TYR ARG          
SEQRES  18 B  301  GLY ARG SER CYS PRO ILE ILE VAL HIS CYS SER ASP GLY          
SEQRES  19 B  301  ALA GLY ARG THR GLY THR TYR ILE LEU ILE ASP MET VAL          
SEQRES  20 B  301  LEU ASN ARG MET ALA LYS GLY VAL LYS GLU ILE ASP ILE          
SEQRES  21 B  301  ALA ALA THR LEU GLU HIS VAL ARG ASP GLN ARG PRO GLY          
SEQRES  22 B  301  LEU VAL ARG SER LYS ASP GLN PHE GLU PHE ALA LEU THR          
SEQRES  23 B  301  ALA VAL ALA GLU GLU VAL ASN ALA ILE LEU LYS ALA LEU          
SEQRES  24 B  301  PRO GLN                                                      
HET    GOL  A3288       6                                                       
HET    GOL  B3287       6                                                       
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3  GOL    2(C3 H8 O3)                                                  
FORMUL   5  HOH   *306(H2 O)                                                    
HELIX    1   1 THR A  691  ASN A  705  1                                  15    
HELIX    2   2 ASN A  705  ALA A  718  1                                  14    
HELIX    3   3 CYS A  726  GLY A  731  1                                   6    
HELIX    4   4 ASN A  734  ASN A  738  5                                   5    
HELIX    5   5 LYS A  754  SER A  758  5                                   5    
HELIX    6   6 LEU A  787  HIS A  789  5                                   3    
HELIX    7   7 THR A  790  GLY A  802  1                                  13    
HELIX    8   8 THR A  884  CYS A  897  1                                  14    
HELIX    9   9 ALA A  913  LYS A  931  1                                  19    
HELIX   10  10 ASP A  937  ASP A  947  1                                  11    
HELIX   11  11 SER A  955  ALA A  976  1                                  22    
HELIX   12  12 SER B  690  ASN B  705  1                                  16    
HELIX   13  13 ASN B  705  ALA B  718  1                                  14    
HELIX   14  14 ASN B  734  ASN B  738  5                                   5    
HELIX   15  15 LYS B  754  SER B  758  5                                   5    
HELIX   16  16 LEU B  787  HIS B  789  5                                   3    
HELIX   17  17 THR B  790  GLY B  802  1                                  13    
HELIX   18  18 THR B  884  LYS B  896  1                                  13    
HELIX   19  19 ALA B  913  LYS B  931  1                                  19    
HELIX   20  20 ASP B  937  ASP B  947  1                                  11    
HELIX   21  21 SER B  955  ALA B  976  1                                  22    
SHEET    1   A 8 ALA A 767  ILE A 770  0                                        
SHEET    2   A 8 TYR A 780  THR A 783 -1  O  TYR A 780   N  ILE A 770           
SHEET    3   A 8 ILE A 905  HIS A 908  1  O  VAL A 907   N  ILE A 781           
SHEET    4   A 8 VAL A 805  MET A 808  1  N  VAL A 807   O  ILE A 906           
SHEET    5   A 8 THR A 864  PHE A 872  1  O  PHE A 870   N  ILE A 806           
SHEET    6   A 8 PHE A 849  ASN A 858 -1  N  PHE A 854   O  LEU A 867           
SHEET    7   A 8 TYR A 835  ILE A 844 -1  N  GLU A 836   O  LYS A 857           
SHEET    8   A 8 ALA A 829  TYR A 832 -1  N  SER A 830   O  VAL A 837           
SHEET    1   B 2 VAL A 813  GLU A 814  0                                        
SHEET    2   B 2 VAL A 817  LYS A 818 -1  O  VAL A 817   N  GLU A 814           
SHEET    1   C 8 ALA B 767  ILE B 770  0                                        
SHEET    2   C 8 TYR B 780  THR B 783 -1  O  TYR B 780   N  ILE B 770           
SHEET    3   C 8 ILE B 905  HIS B 908  1  O  VAL B 907   N  ILE B 781           
SHEET    4   C 8 VAL B 805  MET B 808  1  N  VAL B 807   O  ILE B 906           
SHEET    5   C 8 THR B 864  PHE B 872  1  O  PHE B 870   N  ILE B 806           
SHEET    6   C 8 PHE B 849  ASN B 858 -1  N  PHE B 854   O  LEU B 867           
SHEET    7   C 8 TYR B 835  ILE B 844 -1  N  GLU B 836   O  LYS B 857           
SHEET    8   C 8 ALA B 829  TYR B 832 -1  N  SER B 830   O  VAL B 837           
SHEET    1   D 2 VAL B 813  GLU B 814  0                                        
SHEET    2   D 2 VAL B 817  LYS B 818 -1  O  VAL B 817   N  GLU B 814           
CISPEP   1 GLU A  722    PRO A  723          0         4.53                     
CISPEP   2 GLU B  722    PRO B  723          0        -1.65                     
SITE     1 AC1  4 LEU A 926  MET A 929  ALA A 930  ILE A 973                    
SITE     1 AC2  4 LEU B 926  MET B 929  VAL B 970  ILE B 973                    
CRYST1   72.907   74.229  121.067  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      0.013716  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013472  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008260        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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