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Database: PDB
Entry: 4X90
LinkDB: 4X90
Original site: 4X90 
HEADER    TRANSFERASE                             11-DEC-14   4X90              
TITLE     CRYSTAL STRUCTURE OF LYSOSOMAL PHOSPHOLIPASE A2                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GROUP XV PHOSPHOLIPASE A2;                                 
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: UNP RESIDUES 34-412;                                       
COMPND   5 SYNONYM: 1-O-ACYLCERAMIDE SYNTHASE,ACS,LCAT-LIKE LYSOPHOSPHOLIPASE,  
COMPND   6 LLPL,LYSOPHOSPHOLIPASE 3,LYSOSOMAL PHOSPHOLIPASE A2,LPLA2;           
COMPND   7 EC: 2.3.1.-;                                                         
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: PLA2G15, LYPLA3, UNQ341/PRO540;                                
SOURCE   6 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: HEK293S GNTI-;                          
SOURCE   9 EXPRESSION_SYSTEM_ATCC_NUMBER: CRL-3022                              
KEYWDS    HYDROLASE, PHOSPHOLIPASE, ESTERASE, ACYLTRANSFERASE, TRANSFERASE      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.GLUKHOVA,J.J.G.TESMER                                               
REVDAT   5   29-JUL-20 4X90    1       COMPND REMARK HETNAM LINK                
REVDAT   5 2                   1       SITE                                     
REVDAT   4   04-DEC-19 4X90    1       REMARK                                   
REVDAT   3   13-SEP-17 4X90    1       SOURCE REMARK SSBOND                     
REVDAT   2   18-MAR-15 4X90    1       JRNL                                     
REVDAT   1   11-MAR-15 4X90    0                                                
JRNL        AUTH   A.GLUKHOVA,V.HINKOVSKA-GALCHEVA,R.KELLY,A.ABE,J.A.SHAYMAN,   
JRNL        AUTH 2 J.J.TESMER                                                   
JRNL        TITL   STRUCTURE AND FUNCTION OF LYSOSOMAL PHOSPHOLIPASE A2 AND     
JRNL        TITL 2 LECITHIN:CHOLESTEROL ACYLTRANSFERASE.                        
JRNL        REF    NAT COMMUN                    V.   6  6250 2015              
JRNL        REFN                   ESSN 2041-1723                               
JRNL        PMID   25727495                                                     
JRNL        DOI    10.1038/NCOMMS7250                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.84 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0073                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.84                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 174210                         
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) : 0.155                           
REMARK   3   R VALUE            (WORKING SET) : 0.154                           
REMARK   3   FREE R VALUE                     : 0.173                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 9229                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.84                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.89                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 11158                        
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 83.70                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2170                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 586                          
REMARK   3   BIN FREE R VALUE                    : 0.2200                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 12076                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 420                                     
REMARK   3   SOLVENT ATOMS            : 1065                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 26.42                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.71000                                              
REMARK   3    B22 (A**2) : -0.22000                                             
REMARK   3    B33 (A**2) : -1.30000                                             
REMARK   3    B12 (A**2) : -0.24000                                             
REMARK   3    B13 (A**2) : 0.13000                                              
REMARK   3    B23 (A**2) : 0.20000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.101         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.093         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.066         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.506         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.970                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.961                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 13498 ; 0.010 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A): 12557 ; 0.006 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 18501 ; 1.441 ; 1.991       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 28856 ; 1.168 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1624 ; 5.816 ; 5.006       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   609 ;33.364 ;23.563       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  2088 ;11.529 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    84 ;13.245 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2015 ; 0.085 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 15191 ; 0.008 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  3170 ; 0.005 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  6274 ; 1.271 ; 1.770       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  6273 ; 1.271 ; 1.769       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  7893 ; 2.040 ; 2.644       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NCS TYPE: LOCAL                                                    
REMARK   3   NUMBER OF DIFFERENT NCS PAIRS  : 6                                 
REMARK   3  GROUP  CHAIN1    RANGE     CHAIN2     RANGE    COUNT RMS  WEIGHT    
REMARK   3    1     A     4    379       B     4    379   23512 0.090 0.050     
REMARK   3    2     A     4    379       C     4    379   23567 0.090 0.050     
REMARK   3    3     A     4    379       D     4    379   24248 0.060 0.050     
REMARK   3    4     B     4    379       C     4    379   24220 0.060 0.050     
REMARK   3    5     B     4    379       D     4    379   23549 0.090 0.050     
REMARK   3    6     C     4    379       D     4    379   23467 0.090 0.050     
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     4        A   404                          
REMARK   3    ORIGIN FOR THE GROUP (A):   1.0334 -14.4982  21.4187              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0110 T22:   0.0144                                     
REMARK   3      T33:   0.0315 T12:  -0.0047                                     
REMARK   3      T13:   0.0036 T23:  -0.0078                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1993 L22:   0.3876                                     
REMARK   3      L33:   1.1202 L12:  -0.1050                                     
REMARK   3      L13:   0.0419 L23:  -0.3366                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0041 S12:  -0.0017 S13:  -0.0216                       
REMARK   3      S21:  -0.0116 S22:   0.0104 S23:   0.0066                       
REMARK   3      S31:   0.0946 S32:  -0.0071 S33:  -0.0146                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     4        B   403                          
REMARK   3    ORIGIN FOR THE GROUP (A):   0.3093  29.5096  25.8511              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0156 T22:   0.0162                                     
REMARK   3      T33:   0.0260 T12:   0.0084                                     
REMARK   3      T13:   0.0022 T23:  -0.0029                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1432 L22:   1.1837                                     
REMARK   3      L33:   1.1073 L12:  -0.0543                                     
REMARK   3      L13:  -0.0645 L23:   0.6691                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0203 S12:   0.0322 S13:  -0.0170                       
REMARK   3      S21:  -0.0625 S22:  -0.0244 S23:   0.0079                       
REMARK   3      S31:  -0.1103 S32:  -0.0835 S33:   0.0040                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C     4        C   403                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.3867 -29.2064 -25.7174              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0085 T22:   0.0362                                     
REMARK   3      T33:   0.0500 T12:   0.0092                                     
REMARK   3      T13:  -0.0004 T23:  -0.0010                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2288 L22:   0.9620                                     
REMARK   3      L33:   0.8193 L12:   0.1253                                     
REMARK   3      L13:   0.0800 L23:   0.4987                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0115 S12:  -0.0228 S13:   0.0079                       
REMARK   3      S21:   0.0304 S22:  -0.0180 S23:  -0.0066                       
REMARK   3      S31:   0.0515 S32:  -0.0450 S33:   0.0065                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D     4        D   404                          
REMARK   3    ORIGIN FOR THE GROUP (A):   0.8805  14.8439 -21.3974              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0087 T22:   0.0227                                     
REMARK   3      T33:   0.0456 T12:  -0.0007                                     
REMARK   3      T13:  -0.0015 T23:  -0.0040                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1624 L22:   0.7004                                     
REMARK   3      L33:   1.0835 L12:   0.0941                                     
REMARK   3      L13:  -0.0541 L23:  -0.3937                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0081 S12:  -0.0032 S13:   0.0157                       
REMARK   3      S21:   0.0214 S22:   0.0108 S23:  -0.0132                       
REMARK   3      S31:  -0.0919 S32:  -0.0094 S33:  -0.0190                       
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 U VALUES : WITH TLS ADDED                                 
REMARK   4                                                                      
REMARK   4 4X90 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-DEC-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000205001.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-JUN-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 23-ID-D                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97937                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 183439                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.830                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.8                               
REMARK 200  DATA REDUNDANCY                : 4.000                              
REMARK 200  R MERGE                    (I) : 0.09500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.7000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.83                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.86                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.63100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 62.51                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.28                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM HEPES PH 7.5, 3.5% PEG 8000,      
REMARK 280  28% MPD, 300 MM (NH4)2HPO4, VAPOR DIFFUSION, HANGING DROP,          
REMARK 280  TEMPERATURE 277K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,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                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
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: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A     0                                                      
REMARK 465     ALA A     1                                                      
REMARK 465     GLY A     2                                                      
REMARK 465     ARG A     3                                                      
REMARK 465     GLY B     0                                                      
REMARK 465     ALA B     1                                                      
REMARK 465     GLY B     2                                                      
REMARK 465     ARG B     3                                                      
REMARK 465     GLY C     0                                                      
REMARK 465     ALA C     1                                                      
REMARK 465     GLY C     2                                                      
REMARK 465     ARG C     3                                                      
REMARK 465     GLY D     0                                                      
REMARK 465     ALA D     1                                                      
REMARK 465     GLY D     2                                                      
REMARK 465     ARG D     3                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH B   722     O    HOH D   757              2.10            
REMARK 500   O    HOH D   519     O    HOH D   523              2.17            
REMARK 500   O    HOH A   727     O    HOH A   761              2.17            
REMARK 500   SG   CYS C   297     O    HOH C   737              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A   528     O    HOH C   534     1556     2.02            
REMARK 500   O    HOH C   533     O    HOH C   537     1655     2.08            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A 205   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    ARG A 205   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.7 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A  23       70.55   -151.46                                   
REMARK 500    VAL A  52      -57.34     73.22                                   
REMARK 500    TYR A 104      -80.84   -124.06                                   
REMARK 500    GLU A 121      -90.77   -113.64                                   
REMARK 500    GLU A 121      -90.69   -113.82                                   
REMARK 500    SER A 165     -130.00     54.89                                   
REMARK 500    ILE A 215       58.10   -169.34                                   
REMARK 500    THR A 329      -54.08   -129.62                                   
REMARK 500    ASP B  23       70.44   -150.85                                   
REMARK 500    VAL B  52      -58.11     73.33                                   
REMARK 500    TYR B 104      -79.87   -122.45                                   
REMARK 500    GLU B 121      -91.46   -113.36                                   
REMARK 500    SER B 165     -127.57     54.25                                   
REMARK 500    THR B 329      -55.06   -127.99                                   
REMARK 500    ASP C  23       69.95   -151.01                                   
REMARK 500    VAL C  52      -58.25     74.28                                   
REMARK 500    TYR C 104      -78.70   -122.44                                   
REMARK 500    GLU C 121      -90.98   -113.47                                   
REMARK 500    SER C 165     -128.02     54.50                                   
REMARK 500    THR C 329      -55.16   -128.40                                   
REMARK 500    ASP D  23       70.88   -151.01                                   
REMARK 500    VAL D  52      -57.95     72.71                                   
REMARK 500    TYR D 104      -81.55   -123.67                                   
REMARK 500    GLU D 121      -91.01   -112.41                                   
REMARK 500    GLU D 121      -91.78   -119.63                                   
REMARK 500    SER D 165     -129.83     55.20                                   
REMARK 500    ILE D 215       59.15   -168.68                                   
REMARK 500    THR D 329      -53.59   -128.45                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4X91   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4X92   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4X93   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4X94   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4X95   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4X96   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4X97   RELATED DB: PDB                                   
DBREF  4X90 A    1   379  UNP    Q8NCC3   PAG15_HUMAN     34    412             
DBREF  4X90 B    1   379  UNP    Q8NCC3   PAG15_HUMAN     34    412             
DBREF  4X90 C    1   379  UNP    Q8NCC3   PAG15_HUMAN     34    412             
DBREF  4X90 D    1   379  UNP    Q8NCC3   PAG15_HUMAN     34    412             
SEQADV 4X90 GLY A    0  UNP  Q8NCC3              CLONING ARTIFACT               
SEQADV 4X90 GLY B    0  UNP  Q8NCC3              CLONING ARTIFACT               
SEQADV 4X90 GLY C    0  UNP  Q8NCC3              CLONING ARTIFACT               
SEQADV 4X90 GLY D    0  UNP  Q8NCC3              CLONING ARTIFACT               
SEQRES   1 A  380  GLY ALA GLY ARG HIS PRO PRO VAL VAL LEU VAL PRO GLY          
SEQRES   2 A  380  ASP LEU GLY ASN GLN LEU GLU ALA LYS LEU ASP LYS PRO          
SEQRES   3 A  380  THR VAL VAL HIS TYR LEU CYS SER LYS LYS THR GLU SER          
SEQRES   4 A  380  TYR PHE THR ILE TRP LEU ASN LEU GLU LEU LEU LEU PRO          
SEQRES   5 A  380  VAL ILE ILE ASP CYS TRP ILE ASP ASN ILE ARG LEU VAL          
SEQRES   6 A  380  TYR ASN LYS THR SER ARG ALA THR GLN PHE PRO ASP GLY          
SEQRES   7 A  380  VAL ASP VAL ARG VAL PRO GLY PHE GLY LYS THR PHE SER          
SEQRES   8 A  380  LEU GLU PHE LEU ASP PRO SER LYS SER SER VAL GLY SER          
SEQRES   9 A  380  TYR PHE HIS THR MET VAL GLU SER LEU VAL GLY TRP GLY          
SEQRES  10 A  380  TYR THR ARG GLY GLU ASP VAL ARG GLY ALA PRO TYR ASP          
SEQRES  11 A  380  TRP ARG ARG ALA PRO ASN GLU ASN GLY PRO TYR PHE LEU          
SEQRES  12 A  380  ALA LEU ARG GLU MET ILE GLU GLU MET TYR GLN LEU TYR          
SEQRES  13 A  380  GLY GLY PRO VAL VAL LEU VAL ALA HIS SER MET GLY ASN          
SEQRES  14 A  380  MET TYR THR LEU TYR PHE LEU GLN ARG GLN PRO GLN ALA          
SEQRES  15 A  380  TRP LYS ASP LYS TYR ILE ARG ALA PHE VAL SER LEU GLY          
SEQRES  16 A  380  ALA PRO TRP GLY GLY VAL ALA LYS THR LEU ARG VAL LEU          
SEQRES  17 A  380  ALA SER GLY ASP ASN ASN ARG ILE PRO VAL ILE GLY PRO          
SEQRES  18 A  380  LEU LYS ILE ARG GLU GLN GLN ARG SER ALA VAL SER THR          
SEQRES  19 A  380  SER TRP LEU LEU PRO TYR ASN TYR THR TRP SER PRO GLU          
SEQRES  20 A  380  LYS VAL PHE VAL GLN THR PRO THR ILE ASN TYR THR LEU          
SEQRES  21 A  380  ARG ASP TYR ARG LYS PHE PHE GLN ASP ILE GLY PHE GLU          
SEQRES  22 A  380  ASP GLY TRP LEU MET ARG GLN ASP THR GLU GLY LEU VAL          
SEQRES  23 A  380  GLU ALA THR MET PRO PRO GLY VAL GLN LEU HIS CYS LEU          
SEQRES  24 A  380  TYR GLY THR GLY VAL PRO THR PRO ASP SER PHE TYR TYR          
SEQRES  25 A  380  GLU SER PHE PRO ASP ARG ASP PRO LYS ILE CYS PHE GLY          
SEQRES  26 A  380  ASP GLY ASP GLY THR VAL ASN LEU LYS SER ALA LEU GLN          
SEQRES  27 A  380  CYS GLN ALA TRP GLN SER ARG GLN GLU HIS GLN VAL LEU          
SEQRES  28 A  380  LEU GLN GLU LEU PRO GLY SER GLU HIS ILE GLU MET LEU          
SEQRES  29 A  380  ALA ASN ALA THR THR LEU ALA TYR LEU LYS ARG VAL LEU          
SEQRES  30 A  380  LEU GLY PRO                                                  
SEQRES   1 B  380  GLY ALA GLY ARG HIS PRO PRO VAL VAL LEU VAL PRO GLY          
SEQRES   2 B  380  ASP LEU GLY ASN GLN LEU GLU ALA LYS LEU ASP LYS PRO          
SEQRES   3 B  380  THR VAL VAL HIS TYR LEU CYS SER LYS LYS THR GLU SER          
SEQRES   4 B  380  TYR PHE THR ILE TRP LEU ASN LEU GLU LEU LEU LEU PRO          
SEQRES   5 B  380  VAL ILE ILE ASP CYS TRP ILE ASP ASN ILE ARG LEU VAL          
SEQRES   6 B  380  TYR ASN LYS THR SER ARG ALA THR GLN PHE PRO ASP GLY          
SEQRES   7 B  380  VAL ASP VAL ARG VAL PRO GLY PHE GLY LYS THR PHE SER          
SEQRES   8 B  380  LEU GLU PHE LEU ASP PRO SER LYS SER SER VAL GLY SER          
SEQRES   9 B  380  TYR PHE HIS THR MET VAL GLU SER LEU VAL GLY TRP GLY          
SEQRES  10 B  380  TYR THR ARG GLY GLU ASP VAL ARG GLY ALA PRO TYR ASP          
SEQRES  11 B  380  TRP ARG ARG ALA PRO ASN GLU ASN GLY PRO TYR PHE LEU          
SEQRES  12 B  380  ALA LEU ARG GLU MET ILE GLU GLU MET TYR GLN LEU TYR          
SEQRES  13 B  380  GLY GLY PRO VAL VAL LEU VAL ALA HIS SER MET GLY ASN          
SEQRES  14 B  380  MET TYR THR LEU TYR PHE LEU GLN ARG GLN PRO GLN ALA          
SEQRES  15 B  380  TRP LYS ASP LYS TYR ILE ARG ALA PHE VAL SER LEU GLY          
SEQRES  16 B  380  ALA PRO TRP GLY GLY VAL ALA LYS THR LEU ARG VAL LEU          
SEQRES  17 B  380  ALA SER GLY ASP ASN ASN ARG ILE PRO VAL ILE GLY PRO          
SEQRES  18 B  380  LEU LYS ILE ARG GLU GLN GLN ARG SER ALA VAL SER THR          
SEQRES  19 B  380  SER TRP LEU LEU PRO TYR ASN TYR THR TRP SER PRO GLU          
SEQRES  20 B  380  LYS VAL PHE VAL GLN THR PRO THR ILE ASN TYR THR LEU          
SEQRES  21 B  380  ARG ASP TYR ARG LYS PHE PHE GLN ASP ILE GLY PHE GLU          
SEQRES  22 B  380  ASP GLY TRP LEU MET ARG GLN ASP THR GLU GLY LEU VAL          
SEQRES  23 B  380  GLU ALA THR MET PRO PRO GLY VAL GLN LEU HIS CYS LEU          
SEQRES  24 B  380  TYR GLY THR GLY VAL PRO THR PRO ASP SER PHE TYR TYR          
SEQRES  25 B  380  GLU SER PHE PRO ASP ARG ASP PRO LYS ILE CYS PHE GLY          
SEQRES  26 B  380  ASP GLY ASP GLY THR VAL ASN LEU LYS SER ALA LEU GLN          
SEQRES  27 B  380  CYS GLN ALA TRP GLN SER ARG GLN GLU HIS GLN VAL LEU          
SEQRES  28 B  380  LEU GLN GLU LEU PRO GLY SER GLU HIS ILE GLU MET LEU          
SEQRES  29 B  380  ALA ASN ALA THR THR LEU ALA TYR LEU LYS ARG VAL LEU          
SEQRES  30 B  380  LEU GLY PRO                                                  
SEQRES   1 C  380  GLY ALA GLY ARG HIS PRO PRO VAL VAL LEU VAL PRO GLY          
SEQRES   2 C  380  ASP LEU GLY ASN GLN LEU GLU ALA LYS LEU ASP LYS PRO          
SEQRES   3 C  380  THR VAL VAL HIS TYR LEU CYS SER LYS LYS THR GLU SER          
SEQRES   4 C  380  TYR PHE THR ILE TRP LEU ASN LEU GLU LEU LEU LEU PRO          
SEQRES   5 C  380  VAL ILE ILE ASP CYS TRP ILE ASP ASN ILE ARG LEU VAL          
SEQRES   6 C  380  TYR ASN LYS THR SER ARG ALA THR GLN PHE PRO ASP GLY          
SEQRES   7 C  380  VAL ASP VAL ARG VAL PRO GLY PHE GLY LYS THR PHE SER          
SEQRES   8 C  380  LEU GLU PHE LEU ASP PRO SER LYS SER SER VAL GLY SER          
SEQRES   9 C  380  TYR PHE HIS THR MET VAL GLU SER LEU VAL GLY TRP GLY          
SEQRES  10 C  380  TYR THR ARG GLY GLU ASP VAL ARG GLY ALA PRO TYR ASP          
SEQRES  11 C  380  TRP ARG ARG ALA PRO ASN GLU ASN GLY PRO TYR PHE LEU          
SEQRES  12 C  380  ALA LEU ARG GLU MET ILE GLU GLU MET TYR GLN LEU TYR          
SEQRES  13 C  380  GLY GLY PRO VAL VAL LEU VAL ALA HIS SER MET GLY ASN          
SEQRES  14 C  380  MET TYR THR LEU TYR PHE LEU GLN ARG GLN PRO GLN ALA          
SEQRES  15 C  380  TRP LYS ASP LYS TYR ILE ARG ALA PHE VAL SER LEU GLY          
SEQRES  16 C  380  ALA PRO TRP GLY GLY VAL ALA LYS THR LEU ARG VAL LEU          
SEQRES  17 C  380  ALA SER GLY ASP ASN ASN ARG ILE PRO VAL ILE GLY PRO          
SEQRES  18 C  380  LEU LYS ILE ARG GLU GLN GLN ARG SER ALA VAL SER THR          
SEQRES  19 C  380  SER TRP LEU LEU PRO TYR ASN TYR THR TRP SER PRO GLU          
SEQRES  20 C  380  LYS VAL PHE VAL GLN THR PRO THR ILE ASN TYR THR LEU          
SEQRES  21 C  380  ARG ASP TYR ARG LYS PHE PHE GLN ASP ILE GLY PHE GLU          
SEQRES  22 C  380  ASP GLY TRP LEU MET ARG GLN ASP THR GLU GLY LEU VAL          
SEQRES  23 C  380  GLU ALA THR MET PRO PRO GLY VAL GLN LEU HIS CYS LEU          
SEQRES  24 C  380  TYR GLY THR GLY VAL PRO THR PRO ASP SER PHE TYR TYR          
SEQRES  25 C  380  GLU SER PHE PRO ASP ARG ASP PRO LYS ILE CYS PHE GLY          
SEQRES  26 C  380  ASP GLY ASP GLY THR VAL ASN LEU LYS SER ALA LEU GLN          
SEQRES  27 C  380  CYS GLN ALA TRP GLN SER ARG GLN GLU HIS GLN VAL LEU          
SEQRES  28 C  380  LEU GLN GLU LEU PRO GLY SER GLU HIS ILE GLU MET LEU          
SEQRES  29 C  380  ALA ASN ALA THR THR LEU ALA TYR LEU LYS ARG VAL LEU          
SEQRES  30 C  380  LEU GLY PRO                                                  
SEQRES   1 D  380  GLY ALA GLY ARG HIS PRO PRO VAL VAL LEU VAL PRO GLY          
SEQRES   2 D  380  ASP LEU GLY ASN GLN LEU GLU ALA LYS LEU ASP LYS PRO          
SEQRES   3 D  380  THR VAL VAL HIS TYR LEU CYS SER LYS LYS THR GLU SER          
SEQRES   4 D  380  TYR PHE THR ILE TRP LEU ASN LEU GLU LEU LEU LEU PRO          
SEQRES   5 D  380  VAL ILE ILE ASP CYS TRP ILE ASP ASN ILE ARG LEU VAL          
SEQRES   6 D  380  TYR ASN LYS THR SER ARG ALA THR GLN PHE PRO ASP GLY          
SEQRES   7 D  380  VAL ASP VAL ARG VAL PRO GLY PHE GLY LYS THR PHE SER          
SEQRES   8 D  380  LEU GLU PHE LEU ASP PRO SER LYS SER SER VAL GLY SER          
SEQRES   9 D  380  TYR PHE HIS THR MET VAL GLU SER LEU VAL GLY TRP GLY          
SEQRES  10 D  380  TYR THR ARG GLY GLU ASP VAL ARG GLY ALA PRO TYR ASP          
SEQRES  11 D  380  TRP ARG ARG ALA PRO ASN GLU ASN GLY PRO TYR PHE LEU          
SEQRES  12 D  380  ALA LEU ARG GLU MET ILE GLU GLU MET TYR GLN LEU TYR          
SEQRES  13 D  380  GLY GLY PRO VAL VAL LEU VAL ALA HIS SER MET GLY ASN          
SEQRES  14 D  380  MET TYR THR LEU TYR PHE LEU GLN ARG GLN PRO GLN ALA          
SEQRES  15 D  380  TRP LYS ASP LYS TYR ILE ARG ALA PHE VAL SER LEU GLY          
SEQRES  16 D  380  ALA PRO TRP GLY GLY VAL ALA LYS THR LEU ARG VAL LEU          
SEQRES  17 D  380  ALA SER GLY ASP ASN ASN ARG ILE PRO VAL ILE GLY PRO          
SEQRES  18 D  380  LEU LYS ILE ARG GLU GLN GLN ARG SER ALA VAL SER THR          
SEQRES  19 D  380  SER TRP LEU LEU PRO TYR ASN TYR THR TRP SER PRO GLU          
SEQRES  20 D  380  LYS VAL PHE VAL GLN THR PRO THR ILE ASN TYR THR LEU          
SEQRES  21 D  380  ARG ASP TYR ARG LYS PHE PHE GLN ASP ILE GLY PHE GLU          
SEQRES  22 D  380  ASP GLY TRP LEU MET ARG GLN ASP THR GLU GLY LEU VAL          
SEQRES  23 D  380  GLU ALA THR MET PRO PRO GLY VAL GLN LEU HIS CYS LEU          
SEQRES  24 D  380  TYR GLY THR GLY VAL PRO THR PRO ASP SER PHE TYR TYR          
SEQRES  25 D  380  GLU SER PHE PRO ASP ARG ASP PRO LYS ILE CYS PHE GLY          
SEQRES  26 D  380  ASP GLY ASP GLY THR VAL ASN LEU LYS SER ALA LEU GLN          
SEQRES  27 D  380  CYS GLN ALA TRP GLN SER ARG GLN GLU HIS GLN VAL LEU          
SEQRES  28 D  380  LEU GLN GLU LEU PRO GLY SER GLU HIS ILE GLU MET LEU          
SEQRES  29 D  380  ALA ASN ALA THR THR LEU ALA TYR LEU LYS ARG VAL LEU          
SEQRES  30 D  380  LEU GLY PRO                                                  
HET    NAG  A 401      14                                                       
HET    NAG  A 402      14                                                       
HET    NAG  A 403      28                                                       
HET    NAG  A 404      14                                                       
HET    EPE  A 405      15                                                       
HET     CL  A 406       1                                                       
HET    PO4  A 407       5                                                       
HET    MPD  A 408       8                                                       
HET    MPD  A 409       8                                                       
HET    MPD  A 410       8                                                       
HET    MPD  A 411       8                                                       
HET    MPD  A 412       8                                                       
HET    NAG  B 401      14                                                       
HET    NAG  B 402      14                                                       
HET    NAG  B 403      28                                                       
HET    NAG  B 404      14                                                       
HET    EPE  B 405      15                                                       
HET     CL  B 406       1                                                       
HET    PO4  B 407       5                                                       
HET    MPD  B 408       8                                                       
HET    MPD  B 409       8                                                       
HET    NAG  C 401      14                                                       
HET    NAG  C 402      14                                                       
HET    NAG  C 403      28                                                       
HET    NAG  C 404      14                                                       
HET    EPE  C 405      15                                                       
HET     CL  C 406       1                                                       
HET    PO4  C 407       5                                                       
HET    MPD  C 408       8                                                       
HET    MPD  C 409       8                                                       
HET    MPD  D 401       8                                                       
HET    NAG  D 402      14                                                       
HET    NAG  D 403      14                                                       
HET    NAG  D 404      28                                                       
HET    NAG  D 405      14                                                       
HET    EPE  D 406      15                                                       
HET     CL  D 407       1                                                       
HET    PO4  D 408       5                                                       
HET    MPD  D 409       8                                                       
HET    MPD  D 410       8                                                       
HET    MPD  D 411       8                                                       
HET    MPD  D 412       8                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID              
HETNAM      CL CHLORIDE ION                                                     
HETNAM     PO4 PHOSPHATE ION                                                    
HETNAM     MPD (4S)-2-METHYL-2,4-PENTANEDIOL                                    
HETSYN     EPE HEPES                                                            
FORMUL   5  NAG    16(C8 H15 N O6)                                              
FORMUL   9  EPE    4(C8 H18 N2 O4 S)                                            
FORMUL  10   CL    4(CL 1-)                                                     
FORMUL  11  PO4    4(O4 P 3-)                                                   
FORMUL  12  MPD    14(C6 H14 O2)                                                
FORMUL  47  HOH   *1065(H2 O)                                                   
HELIX    1 AA1 ASN A   45  LEU A   50  5                                   6    
HELIX    2 AA2 VAL A   52  ARG A   62  1                                  11    
HELIX    3 AA3 THR A   88  PHE A   93  1                                   6    
HELIX    4 AA4 SER A   99  SER A  103  5                                   5    
HELIX    5 AA5 PHE A  105  TRP A  115  1                                  11    
HELIX    6 AA6 ALA A  133  GLU A  136  5                                   4    
HELIX    7 AA7 ASN A  137  GLY A  156  1                                  20    
HELIX    8 AA8 MET A  166  ARG A  177  1                                  12    
HELIX    9 AA9 PRO A  179  TYR A  186  1                                   8    
HELIX   10 AB1 ALA A  201  GLY A  210  1                                  10    
HELIX   11 AB2 GLY A  219  ALA A  230  1                                  12    
HELIX   12 AB3 ALA A  230  LEU A  236  1                                   7    
HELIX   13 AB4 ASP A  261  ILE A  269  1                                   9    
HELIX   14 AB5 PHE A  271  GLU A  282  1                                  12    
HELIX   15 AB6 ASN A  331  LYS A  333  5                                   3    
HELIX   16 AB7 SER A  334  GLN A  342  1                                   9    
HELIX   17 AB8 ILE A  360  ALA A  364  5                                   5    
HELIX   18 AB9 ASN A  365  GLY A  378  1                                  14    
HELIX   19 AC1 ASN B   45  LEU B   50  5                                   6    
HELIX   20 AC2 VAL B   52  ARG B   62  1                                  11    
HELIX   21 AC3 THR B   88  PHE B   93  1                                   6    
HELIX   22 AC4 SER B   99  SER B  103  5                                   5    
HELIX   23 AC5 PHE B  105  TRP B  115  1                                  11    
HELIX   24 AC6 ALA B  133  GLU B  136  5                                   4    
HELIX   25 AC7 ASN B  137  GLY B  156  1                                  20    
HELIX   26 AC8 MET B  166  ARG B  177  1                                  12    
HELIX   27 AC9 PRO B  179  TYR B  186  1                                   8    
HELIX   28 AD1 ALA B  201  GLY B  210  1                                  10    
HELIX   29 AD2 GLY B  219  ALA B  230  1                                  12    
HELIX   30 AD3 ALA B  230  LEU B  236  1                                   7    
HELIX   31 AD4 ASP B  261  GLY B  270  1                                  10    
HELIX   32 AD5 PHE B  271  GLU B  282  1                                  12    
HELIX   33 AD6 ASN B  331  LYS B  333  5                                   3    
HELIX   34 AD7 SER B  334  GLN B  342  1                                   9    
HELIX   35 AD8 ILE B  360  ALA B  364  5                                   5    
HELIX   36 AD9 ASN B  365  GLY B  378  1                                  14    
HELIX   37 AE1 ASN C   45  LEU C   50  5                                   6    
HELIX   38 AE2 VAL C   52  ARG C   62  1                                  11    
HELIX   39 AE3 THR C   88  PHE C   93  1                                   6    
HELIX   40 AE4 SER C   99  SER C  103  5                                   5    
HELIX   41 AE5 PHE C  105  TRP C  115  1                                  11    
HELIX   42 AE6 ALA C  133  GLU C  136  5                                   4    
HELIX   43 AE7 ASN C  137  GLY C  156  1                                  20    
HELIX   44 AE8 MET C  166  ARG C  177  1                                  12    
HELIX   45 AE9 PRO C  179  TYR C  186  1                                   8    
HELIX   46 AF1 ALA C  201  GLY C  210  1                                  10    
HELIX   47 AF2 GLY C  219  ALA C  230  1                                  12    
HELIX   48 AF3 ALA C  230  LEU C  236  1                                   7    
HELIX   49 AF4 ASP C  261  GLY C  270  1                                  10    
HELIX   50 AF5 GLU C  272  GLU C  282  1                                  11    
HELIX   51 AF6 ASN C  331  LYS C  333  5                                   3    
HELIX   52 AF7 SER C  334  GLN C  342  1                                   9    
HELIX   53 AF8 ILE C  360  ALA C  364  5                                   5    
HELIX   54 AF9 ASN C  365  GLY C  378  1                                  14    
HELIX   55 AG1 ASN D   45  LEU D   50  5                                   6    
HELIX   56 AG2 VAL D   52  ARG D   62  1                                  11    
HELIX   57 AG3 THR D   88  PHE D   93  1                                   6    
HELIX   58 AG4 SER D   99  SER D  103  5                                   5    
HELIX   59 AG5 PHE D  105  TRP D  115  1                                  11    
HELIX   60 AG6 ALA D  133  GLU D  136  5                                   4    
HELIX   61 AG7 ASN D  137  GLY D  156  1                                  20    
HELIX   62 AG8 MET D  166  ARG D  177  1                                  12    
HELIX   63 AG9 PRO D  179  TYR D  186  1                                   8    
HELIX   64 AH1 ALA D  201  GLY D  210  1                                  10    
HELIX   65 AH2 GLY D  219  ALA D  230  1                                  12    
HELIX   66 AH3 ALA D  230  LEU D  236  1                                   7    
HELIX   67 AH4 ASP D  261  ILE D  269  1                                   9    
HELIX   68 AH5 PHE D  271  GLU D  282  1                                  12    
HELIX   69 AH6 ASN D  331  LYS D  333  5                                   3    
HELIX   70 AH7 SER D  334  GLN D  342  1                                   9    
HELIX   71 AH8 ILE D  360  ALA D  364  5                                   5    
HELIX   72 AH9 ASN D  365  GLY D  378  1                                  14    
SHEET    1 AA1 6 VAL A 123  GLY A 125  0                                        
SHEET    2 AA1 6 VAL A   7  VAL A  10  1  N  LEU A   9   O  ARG A 124           
SHEET    3 AA1 6 VAL A 159  HIS A 164  1  O  VAL A 162   N  VAL A   8           
SHEET    4 AA1 6 ILE A 187  LEU A 193  1  O  VAL A 191   N  LEU A 161           
SHEET    5 AA1 6 LEU A 295  THR A 301  1  O  HIS A 296   N  SER A 192           
SHEET    6 AA1 6 VAL A 349  PRO A 355  1  O  LEU A 350   N  CYS A 297           
SHEET    1 AA2 3 PHE A  40  TRP A  43  0                                        
SHEET    2 AA2 3 LEU A  18  LEU A  22 -1  N  ALA A  20   O  PHE A  40           
SHEET    3 AA2 3 VAL A  78  ARG A  81 -1  O  ARG A  81   N  GLU A  19           
SHEET    1 AA3 2 VAL A  64  ASN A  66  0                                        
SHEET    2 AA3 2 ALA A  71  GLN A  73 -1  O  GLN A  73   N  VAL A  64           
SHEET    1 AA4 4 ASN A 256  THR A 258  0                                        
SHEET    2 AA4 4 VAL A 248  GLN A 251 -1  N  VAL A 250   O  TYR A 257           
SHEET    3 AA4 4 THR A 305  TYR A 310  1  O  PHE A 309   N  GLN A 251           
SHEET    4 AA4 4 LYS A 320  GLY A 324 -1  O  CYS A 322   N  ASP A 307           
SHEET    1 AA5 6 VAL B 123  GLY B 125  0                                        
SHEET    2 AA5 6 VAL B   7  VAL B  10  1  N  LEU B   9   O  ARG B 124           
SHEET    3 AA5 6 VAL B 159  HIS B 164  1  O  VAL B 162   N  VAL B   8           
SHEET    4 AA5 6 ILE B 187  LEU B 193  1  O  VAL B 191   N  LEU B 161           
SHEET    5 AA5 6 LEU B 295  THR B 301  1  O  HIS B 296   N  SER B 192           
SHEET    6 AA5 6 VAL B 349  PRO B 355  1  O  LEU B 350   N  CYS B 297           
SHEET    1 AA6 3 PHE B  40  TRP B  43  0                                        
SHEET    2 AA6 3 LEU B  18  LEU B  22 -1  N  ALA B  20   O  PHE B  40           
SHEET    3 AA6 3 VAL B  78  ARG B  81 -1  O  ARG B  81   N  GLU B  19           
SHEET    1 AA7 2 VAL B  64  ASN B  66  0                                        
SHEET    2 AA7 2 ALA B  71  GLN B  73 -1  O  GLN B  73   N  VAL B  64           
SHEET    1 AA8 4 ASN B 256  TYR B 257  0                                        
SHEET    2 AA8 4 VAL B 250  GLN B 251 -1  N  VAL B 250   O  TYR B 257           
SHEET    3 AA8 4 THR B 305  TYR B 310  1  O  PHE B 309   N  GLN B 251           
SHEET    4 AA8 4 LYS B 320  GLY B 324 -1  O  GLY B 324   N  THR B 305           
SHEET    1 AA9 6 VAL C 123  GLY C 125  0                                        
SHEET    2 AA9 6 VAL C   7  VAL C  10  1  N  LEU C   9   O  ARG C 124           
SHEET    3 AA9 6 VAL C 159  HIS C 164  1  O  VAL C 162   N  VAL C   8           
SHEET    4 AA9 6 ILE C 187  LEU C 193  1  O  VAL C 191   N  LEU C 161           
SHEET    5 AA9 6 LEU C 295  THR C 301  1  O  HIS C 296   N  SER C 192           
SHEET    6 AA9 6 VAL C 349  PRO C 355  1  O  LEU C 350   N  CYS C 297           
SHEET    1 AB1 3 PHE C  40  TRP C  43  0                                        
SHEET    2 AB1 3 LEU C  18  LEU C  22 -1  N  ALA C  20   O  PHE C  40           
SHEET    3 AB1 3 VAL C  78  ARG C  81 -1  O  ARG C  81   N  GLU C  19           
SHEET    1 AB2 2 VAL C  64  ASN C  66  0                                        
SHEET    2 AB2 2 ALA C  71  GLN C  73 -1  O  GLN C  73   N  VAL C  64           
SHEET    1 AB3 4 ASN C 256  TYR C 257  0                                        
SHEET    2 AB3 4 VAL C 250  GLN C 251 -1  N  VAL C 250   O  TYR C 257           
SHEET    3 AB3 4 THR C 305  TYR C 310  1  O  PHE C 309   N  GLN C 251           
SHEET    4 AB3 4 LYS C 320  GLY C 324 -1  O  CYS C 322   N  ASP C 307           
SHEET    1 AB4 6 VAL D 123  GLY D 125  0                                        
SHEET    2 AB4 6 VAL D   7  VAL D  10  1  N  LEU D   9   O  ARG D 124           
SHEET    3 AB4 6 VAL D 159  HIS D 164  1  O  VAL D 162   N  VAL D   8           
SHEET    4 AB4 6 ILE D 187  LEU D 193  1  O  VAL D 191   N  LEU D 161           
SHEET    5 AB4 6 LEU D 295  THR D 301  1  O  HIS D 296   N  SER D 192           
SHEET    6 AB4 6 VAL D 349  PRO D 355  1  O  LEU D 350   N  CYS D 297           
SHEET    1 AB5 3 PHE D  40  TRP D  43  0                                        
SHEET    2 AB5 3 LEU D  18  LEU D  22 -1  N  ALA D  20   O  PHE D  40           
SHEET    3 AB5 3 VAL D  78  ARG D  81 -1  O  ARG D  81   N  GLU D  19           
SHEET    1 AB6 2 VAL D  64  ASN D  66  0                                        
SHEET    2 AB6 2 ALA D  71  GLN D  73 -1  O  GLN D  73   N  VAL D  64           
SHEET    1 AB7 4 ASN D 256  THR D 258  0                                        
SHEET    2 AB7 4 VAL D 248  GLN D 251 -1  N  VAL D 250   O  TYR D 257           
SHEET    3 AB7 4 THR D 305  TYR D 310  1  O  PHE D 309   N  GLN D 251           
SHEET    4 AB7 4 LYS D 320  GLY D 324 -1  O  CYS D 322   N  ASP D 307           
SSBOND   1 CYS A   32    CYS A   56                          1555   1555  2.04  
SSBOND   2 CYS B   32    CYS B   56                          1555   1555  2.05  
SSBOND   3 CYS C   32    CYS C   56                          1555   1555  2.06  
SSBOND   4 CYS D   32    CYS D   56                          1555   1555  2.05  
LINK         ND2 ASN A  66                 C1  NAG A 401     1555   1555  1.45  
LINK         ND2 ASN A 240                 C1  NAG A 402     1555   1555  1.43  
LINK         ND2AASN A 256                 C1 ANAG A 403     1555   1555  1.45  
LINK         ND2BASN A 256                 C1 BNAG A 403     1555   1555  1.45  
LINK         ND2 ASN A 365                 C1  NAG A 404     1555   1555  1.43  
LINK         ND2 ASN B  66                 C1  NAG B 401     1555   1555  1.45  
LINK         ND2 ASN B 240                 C1  NAG B 402     1555   1555  1.44  
LINK         ND2AASN B 256                 C1 ANAG B 403     1555   1555  1.44  
LINK         ND2BASN B 256                 C1 BNAG B 403     1555   1555  1.45  
LINK         ND2 ASN B 365                 C1  NAG B 404     1555   1555  1.43  
LINK         ND2 ASN C  66                 C1  NAG C 401     1555   1555  1.46  
LINK         ND2 ASN C 240                 C1  NAG C 402     1555   1555  1.44  
LINK         ND2AASN C 256                 C1 ANAG C 403     1555   1555  1.45  
LINK         ND2BASN C 256                 C1 BNAG C 403     1555   1555  1.44  
LINK         ND2 ASN C 365                 C1  NAG C 404     1555   1555  1.42  
LINK         ND2 ASN D  66                 C1  NAG D 402     1555   1555  1.44  
LINK         ND2 ASN D 240                 C1  NAG D 403     1555   1555  1.43  
LINK         ND2AASN D 256                 C1 ANAG D 404     1555   1555  1.45  
LINK         ND2BASN D 256                 C1 BNAG D 404     1555   1555  1.45  
LINK         ND2 ASN D 365                 C1  NAG D 405     1555   1555  1.43  
CISPEP   1 TRP A   43    LEU A   44          0        -0.96                     
CISPEP   2 PHE A  314    PRO A  315          0         0.82                     
CISPEP   3 TRP B   43    LEU B   44          0        -1.78                     
CISPEP   4 PHE B  314    PRO B  315          0         3.23                     
CISPEP   5 TRP C   43    LEU C   44          0        -1.40                     
CISPEP   6 PHE C  314    PRO C  315          0         1.93                     
CISPEP   7 TRP D   43    LEU D   44          0        -0.63                     
CISPEP   8 PHE D  314    PRO D  315          0         2.66                     
CRYST1   62.806   91.151  100.266  78.13  88.46  88.50 P 1           4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.015922 -0.000416 -0.000349        0.00000                         
SCALE2      0.000000  0.010975 -0.002300        0.00000                         
SCALE3      0.000000  0.000000  0.010194        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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