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LongText Report for: 4X95-pdb

Name Class
4X95-pdb
HEADER    TRANSFERASE                             11-DEC-14   4X95              
TITLE     CRYSTAL STRUCTURE OF FULLY GLYCOSYLATED LYSOSOMAL PHOSPHOLIPASE A2 IN 
TITLE    2 COMPLEX WITH METHYL ARACHIDONYL FLUOROPHOSPHONATE (MAFP)             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GROUP XV PHOSPHOLIPASE A2;                                 
COMPND   3 CHAIN: A, B;                                                         
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: HEK293T                                 
KEYWDS    HYDROLASE, PHOSPHOLIPASE, MAFP, ACYLTRANSFERASE, TRANSFERASE          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.GLUKHOVA,J.J.G.TESMER                                               
REVDAT   1   25-MAR-15 4X95    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.    3.08 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0073                                      
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) : 3.08                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 49.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 11420                          
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) : 0.220                           
REMARK   3   R VALUE            (WORKING SET) : 0.218                           
REMARK   3   FREE R VALUE                     : 0.252                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 615                             
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) : 3.08                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.16                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 80                           
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 4.71                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3620                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 3                            
REMARK   3   BIN FREE R VALUE                    : 0.2620                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6041                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 176                                     
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 150.0                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 42.72000                                             
REMARK   3    B22 (A**2) : -17.63000                                            
REMARK   3    B33 (A**2) : -25.09000                                            
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): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.736         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.407         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 54.643        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.928                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.892                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6408 ; 0.005 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  5943 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  8750 ; 1.020 ; 1.991       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 13635 ; 0.746 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   750 ; 4.998 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   289 ;29.967 ;23.495       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   998 ;14.549 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    41 ;11.182 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   967 ; 0.073 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  7078 ; 0.004 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  1491 ; 0.001 ; 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):  3006 ; 2.627 ;10.608       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  3005 ; 2.626 ;10.607       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3754 ; 4.455 ;15.904       
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  : 1                                 
REMARK   3  GROUP  CHAIN1    RANGE     CHAIN2     RANGE    COUNT RMS  WEIGHT    
REMARK   3    1     A     4    377       B     4    377   23133 0.060 0.050     
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
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   386                          
REMARK   3    ORIGIN FOR THE GROUP (A):   3.1670   8.8001  22.5619              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0181 T22:   0.1909                                     
REMARK   3      T33:   0.3918 T12:  -0.0128                                     
REMARK   3      T13:  -0.0677 T23:  -0.0040                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0226 L22:   3.0118                                     
REMARK   3      L33:   2.0959 L12:  -0.3623                                     
REMARK   3      L13:  -0.7027 L23:   0.4418                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0103 S12:  -0.1090 S13:  -0.0473                       
REMARK   3      S21:   0.1205 S22:  -0.0758 S23:   0.0598                       
REMARK   3      S31:  -0.0095 S32:  -0.0307 S33:   0.0655                       
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     3        B   386                          
REMARK   3    ORIGIN FOR THE GROUP (A):  25.4359  31.3639  -6.6904              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1300 T22:   0.4903                                     
REMARK   3      T33:   0.9609 T12:  -0.2198                                     
REMARK   3      T13:  -0.0156 T23:   0.0823                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5017 L22:   2.3590                                     
REMARK   3      L33:   2.5926 L12:  -0.4384                                     
REMARK   3      L13:   0.1183 L23:  -0.3610                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0205 S12:   0.1319 S13:   0.1752                       
REMARK   3      S21:  -0.0073 S22:  -0.0516 S23:  -0.7063                       
REMARK   3      S31:  -0.4737 S32:   0.5098 S33:   0.0720                       
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 4X95 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-DEC-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000205264.                                   
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                             : 3.5                                
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) : 0.97933                            
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 : AIMLESS                            
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 12079                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.080                              
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     (%) : 49.4                               
REMARK 200  DATA REDUNDANCY                : 5.100                              
REMARK 200  R MERGE                    (I) : 0.17300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 4.2000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.15                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 4.5                                
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.34200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   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: 4X90                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 66.77                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.70                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM NA CITRATE PH 3.5-4, 20% PEG      
REMARK 280  3350, AND 100 MM NACL, VAPOR DIFFUSION, HANGING DROP,               
REMARK 280  TEMPERATURE 297K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 2 21 21                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   X,-Y,-Z                                                 
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   -X,-Y+1/2,Z+1/2                                         
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        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       62.63750            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       70.10750            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       62.63750            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       70.10750            
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     GLY A     0                                                      
REMARK 465     ALA A     1                                                      
REMARK 465     GLY A     2                                                      
REMARK 465     ARG A     3                                                      
REMARK 465     PRO A   379                                                      
REMARK 465     GLY B     0                                                      
REMARK 465     ALA B     1                                                      
REMARK 465     GLY B     2                                                      
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     LEU A  14    CD2                                                 
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    VAL A  52      -62.41     74.63                                   
REMARK 500    SER A  99      -86.95    -49.62                                   
REMARK 500    TYR A 104      -82.18   -125.78                                   
REMARK 500    GLU A 121      -85.40   -118.57                                   
REMARK 500    SER A 165     -127.78     50.12                                   
REMARK 500    THR A 329      -58.94   -127.34                                   
REMARK 500    VAL B  52      -60.75     73.69                                   
REMARK 500    SER B  99      -87.06    -49.32                                   
REMARK 500    TYR B 104      -82.34   -125.74                                   
REMARK 500    GLU B 121      -85.56   -118.37                                   
REMARK 500    SER B 165     -127.99     49.91                                   
REMARK 500    THR B 329      -58.61   -127.33                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     MAY A  407                                                       
REMARK 610     MAY B  407                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MAY A 407                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MAY B 407                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A    
REMARK 800  401 through BMA A 403 bound to ASN A 66                             
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 404 bound   
REMARK 800  to ASN A 240                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 405 bound   
REMARK 800  to ASN A 256                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 406 bound   
REMARK 800  to ASN A 365                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B    
REMARK 800  401 through BMA B 403 bound to ASN B 66                             
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 404 bound   
REMARK 800  to ASN B 240                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 405 bound   
REMARK 800  to ASN B 256                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 406 bound   
REMARK 800  to ASN B 365                                                        
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4X90   RELATED DB: PDB                                   
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: 4X96   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4X97   RELATED DB: PDB                                   
DBREF  4X95 A    1   379  UNP    Q8NCC3   PAG15_HUMAN     34    412             
DBREF  4X95 B    1   379  UNP    Q8NCC3   PAG15_HUMAN     34    412             
SEQADV 4X95 GLY A    0  UNP  Q8NCC3              CLONING ARTIFACT               
SEQADV 4X95 GLY B    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                                                  
HET    NAG  A 401      14                                                       
HET    NAG  A 402      14                                                       
HET    BMA  A 403      11                                                       
HET    NAG  A 404      14                                                       
HET    NAG  A 405      14                                                       
HET    NAG  A 406      14                                                       
HET    MAY  A 407       7                                                       
HET    NAG  B 401      14                                                       
HET    NAG  B 402      14                                                       
HET    BMA  B 403      11                                                       
HET    NAG  B 404      14                                                       
HET    NAG  B 405      14                                                       
HET    NAG  B 406      14                                                       
HET    MAY  B 407       7                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     BMA BETA-D-MANNOSE                                                   
HETNAM     MAY METHYL ARACHIDONYL FLUOROPHOSPHONATE                             
HETSYN     MAY MAFP                                                             
FORMUL   3  NAG    10(C8 H15 N O6)                                              
FORMUL   3  BMA    2(C6 H12 O6)                                                 
FORMUL   7  MAY    2(C21 H36 F O2 P)                                            
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 SER A  165  ARG A  177  1                                  13    
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  SER A  334  5                                   4    
HELIX   16 AB7 ALA A  335  SER A  343  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 SER B  165  ARG B  177  1                                  13    
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  ILE B  269  1                                   9    
HELIX   32 AD5 PHE B  271  GLU B  282  1                                  12    
HELIX   33 AD6 ASN B  331  SER B  334  5                                   4    
HELIX   34 AD7 ALA B  335  SER B  343  1                                   9    
HELIX   35 AD8 ILE B  360  ALA B  364  5                                   5    
HELIX   36 AD9 ASN B  365  GLY B  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  LEU A 295           
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  PHE A 249   O  TYR A 257           
SHEET    3 AA4 4 THR A 305  TYR A 310  1  O  PHE A 309   N  PHE A 249           
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  LEU B 295           
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  THR B 258  0                                        
SHEET    2 AA8 4 VAL B 248  GLN B 251 -1  N  PHE B 249   O  TYR B 257           
SHEET    3 AA8 4 THR B 305  TYR B 310  1  O  PHE B 309   N  PHE B 249           
SHEET    4 AA8 4 LYS B 320  GLY B 324 -1  O  CYS B 322   N  ASP B 307           
SSBOND   1 CYS A   32    CYS A   56                          1555   1555  2.03  
SSBOND   2 CYS B   32    CYS B   56                          1555   1555  2.03  
LINK         ND2 ASN A  66                 C1  NAG A 401     1555   1555  1.46  
LINK         OG  SER A 165                 P1  MAY A 407     1555   1555  1.63  
LINK         ND2 ASN A 240                 C1  NAG A 404     1555   1555  1.47  
LINK         ND2 ASN A 256                 C1  NAG A 405     1555   1555  1.46  
LINK         ND2 ASN A 365                 C1  NAG A 406     1555   1555  1.45  
LINK         ND2 ASN B  66                 C1  NAG B 401     1555   1555  1.48  
LINK         OG  SER B 165                 P1  MAY B 407     1555   1555  1.62  
LINK         ND2 ASN B 240                 C1  NAG B 404     1555   1555  1.46  
LINK         ND2 ASN B 256                 C1  NAG B 405     1555   1555  1.46  
LINK         ND2 ASN B 365                 C1  NAG B 406     1555   1555  1.46  
LINK         O4  NAG A 401                 C1  NAG A 402     1555   1555  1.44  
LINK         O4  NAG A 402                 C1  BMA A 403     1555   1555  1.43  
LINK         O4  NAG B 401                 C1  NAG B 402     1555   1555  1.44  
LINK         O4  NAG B 402                 C1  BMA B 403     1555   1555  1.45  
CISPEP   1 TRP A   43    LEU A   44          0        -2.93                     
CISPEP   2 PHE A  314    PRO A  315          0        -6.58                     
CISPEP   3 TRP B   43    LEU B   44          0        -2.93                     
CISPEP   4 PHE B  314    PRO B  315          0        -6.60                     
SITE     1 AC1  5 GLY A  12  ASP A  13  MET A 166  LYS A 202                    
SITE     2 AC1  5 HIS A 359                                                     
SITE     1 AC2  6 GLY B  12  ASP B  13  LEU B  14  MET B 166                    
SITE     2 AC2  6 ARG B 214  HIS B 359                                          
SITE     1 AC3  3 ASN A  66  THR A  68  GLN A  73                               
SITE     1 AC4  2 ASN A 240  ARG A 260                                          
SITE     1 AC5  2 THR A 252  ASN A 256                                          
SITE     1 AC6  2 PRO A 355  ASN A 365                                          
SITE     1 AC7  3 ASN B  66  THR B  68  GLN B  73                               
SITE     1 AC8  2 ASN B 240  GLU B 282                                          
SITE     1 AC9  3 VAL B 248  THR B 254  ASN B 256                               
SITE     1 AD1  5 LEU B 354  PRO B 355  GLU B 361  ASN B 365                    
SITE     2 AD1  5 THR B 367                                                     
CRYST1   72.385  125.275  140.215  90.00  90.00  90.00 P 2 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      0.013815  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007982  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007132        0.00000                         
TER    3012      GLY A 378                                                      
TER    6043      PRO B 379                                                      
MASTER      397    0   14   36   30    0   13    6 6217    2  190   60          
END                                                                             

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Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
For technical information about these pages see:
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