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LongText Report for: 3A6Z-pdb

Name Class
3A6Z-pdb
HEADER    HYDROLASE                               10-SEP-09   3A6Z              
TITLE     CRYSTAL STRUCTURE OF PSEUDOMONAS SP. MIS38 LIPASE (PML) IN THE OPEN   
TITLE    2 CONFORMATION FOLLOWING DIALYSIS AGAINST CA-FREE BUFFER               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: LIPASE;                                                    
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 EC: 3.1.1.3;                                                         
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PSEUDOMONAS;                                    
SOURCE   3 ORGANISM_TAXID: 91465;                                               
SOURCE   4 STRAIN: MIS38;                                                       
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: DH5;                                       
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PUC18                                     
KEYWDS    FAMILY I.3 LIPASE, BETA-ROLL, OPEN CONFORMATION, HYDROLASE            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.ANGKAWIDJAJA,H.MATSUMURA,Y.KOGA,K.TAKANO,S.KANAYA                   
REVDAT   1   26-MAY-10 3A6Z    0                                                
JRNL        AUTH   C.ANGKAWIDJAJA,H.MATSUMURA,Y.KOGA,K.TAKANO,S.KANAYA          
JRNL        TITL   X-RAY CRYSTALLOGRAPHIC AND MD SIMULATION STUDIES ON THE      
JRNL        TITL 2 MECHANISM OF INTERFACIAL ACTIVATION OF A FAMILY I.3 LIPASE   
JRNL        TITL 3 WITH TWO LIDS                                                
JRNL        REF    J.MOL.BIOL.                                2010              
JRNL        REFN                   ESSN 1089-8638                               
JRNL        PMID   20438738                                                     
JRNL        DOI    10.1016/J.JMB.2010.04.051                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.15 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD WITH PHASES                
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.15                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.11                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 83266                          
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) : 0.184                           
REMARK   3   R VALUE            (WORKING SET) : 0.182                           
REMARK   3   FREE R VALUE                     : 0.220                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4397                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.15                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.21                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 6036                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.22                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2160                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 300                          
REMARK   3   BIN FREE R VALUE                    : 0.2840                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 9078                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 17                                      
REMARK   3   SOLVENT ATOMS            : 631                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 21.34                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.01000                                              
REMARK   3    B22 (A**2) : 0.01000                                              
REMARK   3    B33 (A**2) : -0.02000                                             
REMARK   3    B12 (A**2) : 0.01000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.187         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.165         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.110         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.263         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.943                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.918                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  9266 ; 0.019 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 12593 ; 1.724 ; 1.938       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1226 ; 7.276 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   419 ;38.304 ;25.346       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1351 ;15.402 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    26 ;22.138 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1388 ; 0.122 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  7235 ; 0.007 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  4363 ; 0.220 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  6209 ; 0.306 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   745 ; 0.172 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):    60 ; 0.099 ; 0.200       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    39 ; 0.276 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     6 ; 0.510 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  6160 ; 0.977 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  9505 ; 1.573 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3583 ; 2.542 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3088 ; 3.610 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3A6Z COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 14-SEP-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB028889.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 27-FEB-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL44XU                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : DOUBLE-CRYSTAL MONOCHROMATOR       
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : BRUKER DIP-6040                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 87709                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.150                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY                : 6.900                              
REMARK 200  R MERGE                    (I) : 0.13600                            
REMARK 200  R SYM                      (I) : 0.10900                            
REMARK 200   FOR THE DATA SET  : 13.7600                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.23                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.43700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 3.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 2ZVD                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 59.21                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.02                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS-HCL, PH8.5, 0.2M AMMONIUM      
REMARK 280  ACETATE, 30% 2-PROPANOL, VAPOR DIFFUSION, HANGING DROP,             
REMARK 280  TEMPERATURE 277K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/6                                            
REMARK 290       6555   X-Y,X,Z+5/6                                             
REMARK 290       7555   Y,X,-Z+2/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+1/3                                          
REMARK 290      10555   -Y,-X,-Z+1/6                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+5/6                                            
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      330.11667            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      165.05833            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      247.58750            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       82.52917            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      412.64583            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      330.11667            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000      165.05833            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       82.52917            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000      247.58750            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000      412.64583            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2650 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 46810 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -110.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 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     MET A     1                                                      
REMARK 465     LEU A   464                                                      
REMARK 465     PHE A   465                                                      
REMARK 465     LYS A   466                                                      
REMARK 465     MET C     1                                                      
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    LYS A   7     -126.87     54.97                                   
REMARK 500    PHE A  45       17.50   -144.61                                   
REMARK 500    SER A 144      162.43    111.46                                   
REMARK 500    SER A 197     -166.24   -110.73                                   
REMARK 500    SER A 207     -124.61     64.76                                   
REMARK 500    ASN A 352       12.88   -147.01                                   
REMARK 500    ARG A 392     -147.87     56.53                                   
REMARK 500    ASP A 449       29.11     49.54                                   
REMARK 500    TRP A 462       53.40    -68.40                                   
REMARK 500    LEU A 512     -159.65     58.80                                   
REMARK 500    LYS C   7     -127.78     53.79                                   
REMARK 500    SER C 144      166.97    120.96                                   
REMARK 500    ASN C 149       33.25   -147.28                                   
REMARK 500    PHE C 180       18.65   -141.95                                   
REMARK 500    SER C 207     -125.29     65.44                                   
REMARK 500    TRP C 224       29.24     49.38                                   
REMARK 500    ARG C 392     -159.74     59.24                                   
REMARK 500    GLN C 419       15.63     56.16                                   
REMARK 500    LEU C 512     -158.28     60.85                                   
REMARK 500    ASP C 577      133.96    -32.37                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ASP A  262     GLY A  263                  -64.69                    
REMARK 500 GLY A  263     SER A  264                  146.49                    
REMARK 500 GLY A  459     PHE A  460                  145.42                    
REMARK 500 ASP C  262     GLY C  263                  -72.82                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    ASP A  62        23.1      L          L   OUTSIDE RANGE           
REMARK 500    SER A 264        19.7      L          L   OUTSIDE RANGE           
REMARK 500    ASN A 607        24.5      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH C 807        DISTANCE =  6.69 ANGSTROMS                       
REMARK 525    HOH C 809        DISTANCE =  5.25 ANGSTROMS                       
REMARK 525    HOH C 812        DISTANCE =  5.90 ANGSTROMS                       
REMARK 525    HOH A 839        DISTANCE =  7.03 ANGSTROMS                       
REMARK 525    HOH A 840        DISTANCE =  5.30 ANGSTROMS                       
REMARK 525    HOH A 843        DISTANCE =  5.27 ANGSTROMS                       
REMARK 525    HOH A 853        DISTANCE =  6.08 ANGSTROMS                       
REMARK 525    HOH A 872        DISTANCE =  5.24 ANGSTROMS                       
REMARK 525    HOH A 900        DISTANCE =  6.57 ANGSTROMS                       
REMARK 525    HOH A 905        DISTANCE =  5.48 ANGSTROMS                       
REMARK 525    HOH A 906        DISTANCE =  6.14 ANGSTROMS                       
REMARK 525    HOH A 908        DISTANCE =  5.48 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 628  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR A 118   O                                                      
REMARK 620 2 GLN A 120   OE1  76.8                                              
REMARK 620 3 SER A 144   O   164.6  88.4                                        
REMARK 620 4 ASP A 153   OD2  96.0  99.0  81.7                                  
REMARK 620 5 ASP A 157   OD1 122.7 160.2  72.4  83.4                            
REMARK 620 6 ASP A 157   OD2  72.8 144.6 122.6 101.8  51.8                      
REMARK 620 7 HOH A 715   O    98.1  83.8  84.6 165.9  89.4  82.8                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 618  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 253   OE2                                                    
REMARK 620 2 ASP A 275   OD1 104.9                                              
REMARK 620 3 ASP A 275   OD2  91.5  51.9                                        
REMARK 620 4 ASP A 283   O    87.2  90.0 140.1                                  
REMARK 620 5 ASN A 284   OD1  96.9 152.3 145.4  74.0                            
REMARK 620 6 HOH A 658   O   175.4  78.2  87.8  96.3  81.2                      
REMARK 620 7 HOH A 681   O    87.5 125.5  75.4 144.2  71.5  87.9                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 620  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER A 374   O                                                      
REMARK 620 2 SER A 376   O    87.2                                              
REMARK 620 3 ASP A 378   OD2  80.3  83.4                                        
REMARK 620 4 GLY A 391   O    77.7 163.8  88.5                                  
REMARK 620 5 ALA A 393   O    82.5  82.2 158.0 101.1                            
REMARK 620 6 ASP A 396   OD1 157.7  82.1  79.1 110.2 115.0                      
REMARK 620 7 ASP A 396   OD2 146.9 123.5 112.4  72.5  89.4  51.8                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 621  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLY A 383   O                                                      
REMARK 620 2 GLY A 385   O    94.5                                              
REMARK 620 3 ASP A 387   OD2  84.3  79.0                                        
REMARK 620 4 ASP A 400   OD1  87.9 161.3  82.8                                  
REMARK 620 5 ASP A 400   OD2  86.9 147.0 133.9  51.6                            
REMARK 620 6 GLY A 402   O    96.2  78.4 157.4 119.8  68.6                      
REMARK 620 7 ASN A 405   OD1 168.5  97.0  96.8  80.8  84.1  87.3                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 622  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ARG A 392   O                                                      
REMARK 620 2 GLY A 394   O   115.8                                              
REMARK 620 3 ASP A 396   OD2  87.6  86.1                                        
REMARK 620 4 GLY A 409   O    84.8 159.0  99.6                                  
REMARK 620 5 ALA A 411   O    95.3  74.4 159.6 100.8                            
REMARK 620 6 ASN A 414   OD1 168.7  75.4  95.0  84.0  86.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 623  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR A 494   O                                                      
REMARK 620 2 GLY A 496   O    86.0                                              
REMARK 620 3 ASP A 498   OD2  81.6  84.5                                        
REMARK 620 4 GLY A 511   O    80.6 165.1  87.1                                  
REMARK 620 5 ASP A 513   O    85.2  80.2 160.4 105.0                            
REMARK 620 6 ASP A 516   OD1 147.6 123.1 112.5  71.5  86.2                      
REMARK 620 7 ASP A 516   OD2 163.4  84.6  83.9 106.8 106.5  47.4                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 624  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 LEU A 512   O                                                      
REMARK 620 2 GLY A 514   O   112.0                                              
REMARK 620 3 ASP A 516   OD1  81.2  81.9                                        
REMARK 620 4 GLY A 529   O    80.2 165.9  93.4                                  
REMARK 620 5 ALA A 531   O    86.6  83.5 155.9 105.1                            
REMARK 620 6 ASP A 534   OD1 161.7  79.0  86.1  87.5 109.7                      
REMARK 620 7 ASP A 534   OD2 137.7 107.3 120.1  63.7  82.6  42.1                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 625  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLY A 521   O                                                      
REMARK 620 2 GLY A 523   O    84.7                                              
REMARK 620 3 ASP A 525   OD2  85.2  82.0                                        
REMARK 620 4 SER A 538   O    77.6 161.2  90.1                                  
REMARK 620 5 GLY A 540   O    87.1  88.8 168.5  96.5                            
REMARK 620 6 ASP A 543   OD1 164.0  79.4  90.9 118.0  94.2                      
REMARK 620 7 ASP A 543   OD2 144.9 127.6 110.0  71.2  81.1  50.7                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 626  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLY A 530   O                                                      
REMARK 620 2 GLY A 532   O    99.3                                              
REMARK 620 3 ASP A 534   OD2  86.1  85.9                                        
REMARK 620 4 PHE A 551   O    88.5  78.2 162.1                                  
REMARK 620 5 ASP A 554   OD1 167.2  89.1  84.8 102.8                            
REMARK 620 6 HOH A 761   O    81.4 177.4  91.7 104.4  89.8                      
REMARK 620 7 ASP A 554   OD2 131.2 125.6 112.5  83.8  46.0  54.7                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C 628  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR C 118   O                                                      
REMARK 620 2 GLN C 120   OE1  76.9                                              
REMARK 620 3 SER C 144   O   161.8  85.6                                        
REMARK 620 4 ASP C 153   OD2  94.6  94.7  81.8                                  
REMARK 620 5 ASP C 157   OD1  70.8 145.9 127.3  98.6                            
REMARK 620 6 ASP C 157   OD2 122.8 159.6  75.2  89.2  52.2                      
REMARK 620 7 HOH C 699   O    94.9  86.5  89.0 170.5  85.4  86.5                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C 618  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU C 253   OE2                                                    
REMARK 620 2 ASP C 275   OD1 100.9                                              
REMARK 620 3 ASP C 275   OD2  94.4  51.3                                        
REMARK 620 4 ASP C 283   O    86.8  87.0 137.9                                  
REMARK 620 5 ASN C 284   OD1  97.8 154.3 144.2  76.5                            
REMARK 620 6 HOH C 669   O    93.5 127.9  78.0 144.0  67.8                      
REMARK 620 7 HOH C 698   O   174.1  83.7  85.6  97.2  79.0  80.7                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C 620  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER C 374   O                                                      
REMARK 620 2 SER C 376   O    91.9                                              
REMARK 620 3 ASP C 378   OD2  80.7  87.0                                        
REMARK 620 4 GLY C 391   O    76.9 168.7  90.7                                  
REMARK 620 5 ALA C 393   O    86.7  82.3 163.2  97.2                            
REMARK 620 6 ASP C 396   OD1 158.6  74.5  82.1 116.1 107.3                      
REMARK 620 7 ASP C 396   OD2 148.4 116.1 113.4  74.8  83.0  52.0                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C 621  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLY C 383   O                                                      
REMARK 620 2 GLY C 385   O    91.1                                              
REMARK 620 3 ASP C 387   OD2  83.7  77.1                                        
REMARK 620 4 ASP C 400   OD1  86.8 157.8  80.6                                  
REMARK 620 5 ASP C 400   OD2  84.5 148.1 133.3  53.7                            
REMARK 620 6 GLY C 402   O    87.7  73.1 148.8 128.8  75.1                      
REMARK 620 7 ASN C 405   OD1 174.6  92.8  93.5  88.2  94.2  97.0                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C 623  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR C 494   O                                                      
REMARK 620 2 GLY C 496   O    83.8                                              
REMARK 620 3 ASP C 498   OD2  78.9  74.4                                        
REMARK 620 4 GLY C 511   O    84.5 163.0  91.4                                  
REMARK 620 5 ASP C 513   O    86.7  87.3 157.6 104.2                            
REMARK 620 6 ASP C 516   OD1 149.8 125.8 112.5  67.9  88.5                      
REMARK 620 7 ASP C 516   OD2 157.2  82.6  80.0 104.4 110.7  49.3                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C 624  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 LEU C 512   O                                                      
REMARK 620 2 GLY C 514   O   103.1                                              
REMARK 620 3 ASP C 516   OD1  78.7  87.1                                        
REMARK 620 4 GLY C 529   O    85.8 171.1  94.3                                  
REMARK 620 5 ALA C 531   O    80.9  73.3 147.6 109.1                            
REMARK 620 6 ASP C 534   OD1 160.3  84.4  83.7  87.0 118.8                      
REMARK 620 7 ASP C 534   OD2 143.5 108.3 120.3  63.4  90.8  43.8                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C 625  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLY C 521   O                                                      
REMARK 620 2 GLY C 523   O    84.2                                              
REMARK 620 3 ASP C 525   OD2  89.5  84.3                                        
REMARK 620 4 SER C 538   O    73.4 156.9  89.4                                  
REMARK 620 5 GLY C 540   O    89.0  87.2 171.5  98.2                            
REMARK 620 6 ASP C 543   OD1 164.9  80.7  89.8 121.6  89.4                      
REMARK 620 7 ASP C 543   OD2 143.3 131.0 102.1  72.0  84.0  51.3                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C 626  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLY C 530   O                                                      
REMARK 620 2 GLY C 532   O    98.9                                              
REMARK 620 3 ASP C 534   OD2  86.6  86.0                                        
REMARK 620 4 PHE C 551   O    90.9  75.0 160.2                                  
REMARK 620 5 ASP C 554   OD1 170.1  86.4  85.3  98.6                            
REMARK 620 6 ASP C 554   OD2 134.1 121.3 115.3  80.1  46.2                      
REMARK 620 7 HOH C 675   O    81.3 179.6  94.4 104.6  93.5  58.4                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 618                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 620                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 621                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 622                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 623                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 624                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 625                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 626                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 628                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 618                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 620                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 621                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 623                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 624                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 625                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 626                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 628                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2Z8X   RELATED DB: PDB                                   
REMARK 900 PML CLOSED CONFORMATION                                              
REMARK 900 RELATED ID: 2ZVD   RELATED DB: PDB                                   
REMARK 900 PML OPEN CONFORMATION                                                
REMARK 900 RELATED ID: 2ZJ6   RELATED DB: PDB                                   
REMARK 900 D337A MUTANT, CLOSED CONFORMATION                                    
REMARK 900 RELATED ID: 2ZJ7   RELATED DB: PDB                                   
REMARK 900 D157A MUTANT, CLOSED CONFORMATION                                    
REMARK 900 RELATED ID: 2Z8Z   RELATED DB: PDB                                   
REMARK 900 PML CLOSED CONFORMATION, PT-DERIVATIZED                              
REMARK 900 RELATED ID: 3A70   RELATED DB: PDB                                   
DBREF  3A6Z A    1   617  UNP    Q9RBY1   Q9RBY1_9PSED     1    617             
DBREF  3A6Z C    1   617  UNP    Q9RBY1   Q9RBY1_9PSED     1    617             
SEQRES   1 A  617  MET GLY VAL TYR ASP TYR LYS ASN PHE GLY THR ALA ASP          
SEQRES   2 A  617  SER LYS ALA LEU PHE SER ASP ALA MET ALA ILE THR LEU          
SEQRES   3 A  617  TYR SER TYR HIS ASN LEU ASP ASN GLY PHE ALA ALA GLY          
SEQRES   4 A  617  TYR GLN HIS ASN GLY PHE GLY LEU GLY LEU PRO ALA THR          
SEQRES   5 A  617  LEU VAL THR ALA LEU LEU GLY GLY THR ASP SER GLN GLY          
SEQRES   6 A  617  VAL ILE PRO GLY ILE PRO TRP ASN PRO ASP SER GLU LYS          
SEQRES   7 A  617  LEU ALA LEU ASP ALA VAL LYS LYS ALA GLY TRP THR PRO          
SEQRES   8 A  617  ILE THR ALA SER GLN LEU GLY TYR ASP GLY LYS THR ASP          
SEQRES   9 A  617  ALA ARG GLY THR PHE PHE GLY GLU LYS ALA GLY TYR THR          
SEQRES  10 A  617  THR ALA GLN VAL GLU ILE LEU GLY LYS TYR ASP ALA GLN          
SEQRES  11 A  617  GLY HIS LEU THR GLU ILE GLY ILE ALA PHE ARG GLY THR          
SEQRES  12 A  617  SER GLY PRO ARG GLU ASN LEU ILE LEU ASP SER ILE GLY          
SEQRES  13 A  617  ASP VAL ILE ASN ASP LEU LEU ALA ALA PHE GLY PRO LYS          
SEQRES  14 A  617  ASP TYR ALA LYS ASN TYR VAL GLY GLU ALA PHE GLY ASN          
SEQRES  15 A  617  LEU LEU ASN ASP VAL VAL ALA PHE ALA LYS ALA ASN GLY          
SEQRES  16 A  617  LEU SER GLY LYS ASP VAL LEU VAL SER GLY HIS SER LEU          
SEQRES  17 A  617  GLY GLY LEU ALA VAL ASN SER MET ALA ASP LEU SER GLY          
SEQRES  18 A  617  GLY LYS TRP GLY GLY PHE PHE ALA ASP SER ASN TYR ILE          
SEQRES  19 A  617  ALA TYR ALA SER PRO THR GLN SER SER THR ASP LYS VAL          
SEQRES  20 A  617  LEU ASN VAL GLY TYR GLU ASN ASP PRO VAL PHE ARG ALA          
SEQRES  21 A  617  LEU ASP GLY SER THR PHE THR GLY ALA SER VAL GLY VAL          
SEQRES  22 A  617  HIS ASP ALA PRO LYS GLU SER ALA THR ASP ASN ILE VAL          
SEQRES  23 A  617  SER PHE ASN ASP HIS TYR ALA SER THR ALA TRP ASN LEU          
SEQRES  24 A  617  LEU PRO PHE SER ILE LEU ASN ILE PRO THR TRP ILE SER          
SEQRES  25 A  617  HIS LEU PRO THR ALA TYR GLY ASP GLY MET ASN ARG ILE          
SEQRES  26 A  617  ILE GLU SER LYS PHE TYR ASP LEU THR SER LYS ASP SER          
SEQRES  27 A  617  THR ILE ILE VAL ALA ASN LEU SER ASP PRO ALA ARG ALA          
SEQRES  28 A  617  ASN THR TRP VAL GLN ASP LEU ASN ARG ASN ALA GLU THR          
SEQRES  29 A  617  HIS LYS GLY SER THR PHE ILE ILE GLY SER ASP SER ASN          
SEQRES  30 A  617  ASP LEU ILE GLN GLY GLY SER GLY ASN ASP TYR LEU GLU          
SEQRES  31 A  617  GLY ARG ALA GLY ASN ASP THR PHE ARG ASP GLY GLY GLY          
SEQRES  32 A  617  TYR ASN VAL ILE LEU GLY GLY ALA GLY ASN ASN THR LEU          
SEQRES  33 A  617  ASP LEU GLN LYS SER VAL ASN THR PHE ASP PHE ALA ASN          
SEQRES  34 A  617  ASP GLY ALA GLY ASN LEU TYR VAL ARG ASP ALA ASN GLY          
SEQRES  35 A  617  GLY ILE SER ILE THR ARG ASP ILE GLY SER ILE VAL THR          
SEQRES  36 A  617  LYS GLU PRO GLY PHE LEU TRP GLY LEU PHE LYS ASP ASP          
SEQRES  37 A  617  VAL THR HIS SER VAL THR ALA SER GLY LEU LYS VAL GLY          
SEQRES  38 A  617  SER ASN VAL THR GLN TYR ASP ALA SER VAL LYS GLY THR          
SEQRES  39 A  617  ASN GLY ALA ASP THR LEU LYS ALA HIS ALA GLY GLY ASP          
SEQRES  40 A  617  TRP LEU PHE GLY LEU ASP GLY ASN ASP HIS LEU ILE GLY          
SEQRES  41 A  617  GLY VAL GLY ASN ASP VAL PHE VAL GLY GLY ALA GLY ASN          
SEQRES  42 A  617  ASP LEU MET GLU SER GLY GLY GLY ALA ASP THR PHE LEU          
SEQRES  43 A  617  PHE ASN GLY ALA PHE GLY GLN ASP ARG VAL VAL GLY PHE          
SEQRES  44 A  617  THR SER ASN ASP LYS LEU VAL PHE LEU GLY VAL GLN GLY          
SEQRES  45 A  617  VAL LEU PRO ASN ASP ASP PHE ARG ALA HIS ALA SER MET          
SEQRES  46 A  617  VAL GLY GLN ASP THR VAL LEU LYS PHE GLY GLY ASP SER          
SEQRES  47 A  617  VAL THR LEU VAL GLY VAL ALA LEU ASN SER LEU SER ALA          
SEQRES  48 A  617  ASP GLY ILE VAL ILE ALA                                      
SEQRES   1 C  617  MET GLY VAL TYR ASP TYR LYS ASN PHE GLY THR ALA ASP          
SEQRES   2 C  617  SER LYS ALA LEU PHE SER ASP ALA MET ALA ILE THR LEU          
SEQRES   3 C  617  TYR SER TYR HIS ASN LEU ASP ASN GLY PHE ALA ALA GLY          
SEQRES   4 C  617  TYR GLN HIS ASN GLY PHE GLY LEU GLY LEU PRO ALA THR          
SEQRES   5 C  617  LEU VAL THR ALA LEU LEU GLY GLY THR ASP SER GLN GLY          
SEQRES   6 C  617  VAL ILE PRO GLY ILE PRO TRP ASN PRO ASP SER GLU LYS          
SEQRES   7 C  617  LEU ALA LEU ASP ALA VAL LYS LYS ALA GLY TRP THR PRO          
SEQRES   8 C  617  ILE THR ALA SER GLN LEU GLY TYR ASP GLY LYS THR ASP          
SEQRES   9 C  617  ALA ARG GLY THR PHE PHE GLY GLU LYS ALA GLY TYR THR          
SEQRES  10 C  617  THR ALA GLN VAL GLU ILE LEU GLY LYS TYR ASP ALA GLN          
SEQRES  11 C  617  GLY HIS LEU THR GLU ILE GLY ILE ALA PHE ARG GLY THR          
SEQRES  12 C  617  SER GLY PRO ARG GLU ASN LEU ILE LEU ASP SER ILE GLY          
SEQRES  13 C  617  ASP VAL ILE ASN ASP LEU LEU ALA ALA PHE GLY PRO LYS          
SEQRES  14 C  617  ASP TYR ALA LYS ASN TYR VAL GLY GLU ALA PHE GLY ASN          
SEQRES  15 C  617  LEU LEU ASN ASP VAL VAL ALA PHE ALA LYS ALA ASN GLY          
SEQRES  16 C  617  LEU SER GLY LYS ASP VAL LEU VAL SER GLY HIS SER LEU          
SEQRES  17 C  617  GLY GLY LEU ALA VAL ASN SER MET ALA ASP LEU SER GLY          
SEQRES  18 C  617  GLY LYS TRP GLY GLY PHE PHE ALA ASP SER ASN TYR ILE          
SEQRES  19 C  617  ALA TYR ALA SER PRO THR GLN SER SER THR ASP LYS VAL          
SEQRES  20 C  617  LEU ASN VAL GLY TYR GLU ASN ASP PRO VAL PHE ARG ALA          
SEQRES  21 C  617  LEU ASP GLY SER THR PHE THR GLY ALA SER VAL GLY VAL          
SEQRES  22 C  617  HIS ASP ALA PRO LYS GLU SER ALA THR ASP ASN ILE VAL          
SEQRES  23 C  617  SER PHE ASN ASP HIS TYR ALA SER THR ALA TRP ASN LEU          
SEQRES  24 C  617  LEU PRO PHE SER ILE LEU ASN ILE PRO THR TRP ILE SER          
SEQRES  25 C  617  HIS LEU PRO THR ALA TYR GLY ASP GLY MET ASN ARG ILE          
SEQRES  26 C  617  ILE GLU SER LYS PHE TYR ASP LEU THR SER LYS ASP SER          
SEQRES  27 C  617  THR ILE ILE VAL ALA ASN LEU SER ASP PRO ALA ARG ALA          
SEQRES  28 C  617  ASN THR TRP VAL GLN ASP LEU ASN ARG ASN ALA GLU THR          
SEQRES  29 C  617  HIS LYS GLY SER THR PHE ILE ILE GLY SER ASP SER ASN          
SEQRES  30 C  617  ASP LEU ILE GLN GLY GLY SER GLY ASN ASP TYR LEU GLU          
SEQRES  31 C  617  GLY ARG ALA GLY ASN ASP THR PHE ARG ASP GLY GLY GLY          
SEQRES  32 C  617  TYR ASN VAL ILE LEU GLY GLY ALA GLY ASN ASN THR LEU          
SEQRES  33 C  617  ASP LEU GLN LYS SER VAL ASN THR PHE ASP PHE ALA ASN          
SEQRES  34 C  617  ASP GLY ALA GLY ASN LEU TYR VAL ARG ASP ALA ASN GLY          
SEQRES  35 C  617  GLY ILE SER ILE THR ARG ASP ILE GLY SER ILE VAL THR          
SEQRES  36 C  617  LYS GLU PRO GLY PHE LEU TRP GLY LEU PHE LYS ASP ASP          
SEQRES  37 C  617  VAL THR HIS SER VAL THR ALA SER GLY LEU LYS VAL GLY          
SEQRES  38 C  617  SER ASN VAL THR GLN TYR ASP ALA SER VAL LYS GLY THR          
SEQRES  39 C  617  ASN GLY ALA ASP THR LEU LYS ALA HIS ALA GLY GLY ASP          
SEQRES  40 C  617  TRP LEU PHE GLY LEU ASP GLY ASN ASP HIS LEU ILE GLY          
SEQRES  41 C  617  GLY VAL GLY ASN ASP VAL PHE VAL GLY GLY ALA GLY ASN          
SEQRES  42 C  617  ASP LEU MET GLU SER GLY GLY GLY ALA ASP THR PHE LEU          
SEQRES  43 C  617  PHE ASN GLY ALA PHE GLY GLN ASP ARG VAL VAL GLY PHE          
SEQRES  44 C  617  THR SER ASN ASP LYS LEU VAL PHE LEU GLY VAL GLN GLY          
SEQRES  45 C  617  VAL LEU PRO ASN ASP ASP PHE ARG ALA HIS ALA SER MET          
SEQRES  46 C  617  VAL GLY GLN ASP THR VAL LEU LYS PHE GLY GLY ASP SER          
SEQRES  47 C  617  VAL THR LEU VAL GLY VAL ALA LEU ASN SER LEU SER ALA          
SEQRES  48 C  617  ASP GLY ILE VAL ILE ALA                                      
HET     CA  A 618       1                                                       
HET     CA  A 620       1                                                       
HET     CA  A 621       1                                                       
HET     CA  A 622       1                                                       
HET     CA  A 623       1                                                       
HET     CA  A 624       1                                                       
HET     CA  A 625       1                                                       
HET     CA  A 626       1                                                       
HET     CA  A 628       1                                                       
HET     CA  C 618       1                                                       
HET     CA  C 620       1                                                       
HET     CA  C 621       1                                                       
HET     CA  C 623       1                                                       
HET     CA  C 624       1                                                       
HET     CA  C 625       1                                                       
HET     CA  C 626       1                                                       
HET     CA  C 628       1                                                       
HETNAM      CA CALCIUM ION                                                      
FORMUL   3   CA    17(CA 2+)                                                    
FORMUL  20  HOH   *631(H2 O)                                                    
HELIX    1   1 GLY A   10  TYR A   29  1                                  20    
HELIX    2   2 ASP A   33  GLY A   44  1                                  12    
HELIX    3   3 GLY A   48  GLY A   59  1                                  12    
HELIX    4   4 ASP A   75  ALA A   87  1                                  13    
HELIX    5   5 THR A   93  GLY A   98  1                                   6    
HELIX    6   6 PRO A  146  GLU A  148  5                                   3    
HELIX    7   7 ASN A  149  GLY A  167  1                                  19    
HELIX    8   8 ASP A  170  ASN A  194  1                                  25    
HELIX    9   9 SER A  197  LYS A  199  5                                   3    
HELIX   10  10 SER A  207  SER A  220  1                                  14    
HELIX   11  11 LYS A  223  SER A  231  5                                   9    
HELIX   12  12 THR A  267  GLY A  272  5                                   6    
HELIX   13  13 ASN A  289  SER A  294  1                                   6    
HELIX   14  14 ALA A  296  LEU A  300  5                                   5    
HELIX   15  15 ASN A  306  HIS A  313  5                                   8    
HELIX   16  16 LEU A  314  SER A  328  1                                  15    
HELIX   17  17 PHE A  330  THR A  334  5                                   5    
HELIX   18  18 SER A  346  ALA A  351  1                                   6    
HELIX   19  19 SER A  421  PHE A  425  5                                   5    
HELIX   20  20 ASP A  578  ALA A  581  5                                   4    
HELIX   21  21 ALA A  605  LEU A  609  5                                   5    
HELIX   22  22 SER A  610  ASP A  612  5                                   3    
HELIX   23  23 PHE C    9  TYR C   29  1                                  21    
HELIX   24  24 ASP C   33  GLY C   44  1                                  12    
HELIX   25  25 GLY C   48  GLY C   59  1                                  12    
HELIX   26  26 ASP C   75  ALA C   87  1                                  13    
HELIX   27  27 THR C   93  GLY C   98  1                                   6    
HELIX   28  28 PRO C  146  GLU C  148  5                                   3    
HELIX   29  29 ASN C  149  GLY C  167  1                                  19    
HELIX   30  30 ASN C  174  ASN C  194  1                                  21    
HELIX   31  31 SER C  197  LYS C  199  5                                   3    
HELIX   32  32 SER C  207  SER C  220  1                                  14    
HELIX   33  33 LYS C  223  PHE C  227  5                                   5    
HELIX   34  34 THR C  267  GLY C  272  5                                   6    
HELIX   35  35 ASN C  289  SER C  294  1                                   6    
HELIX   36  36 ALA C  296  LEU C  300  5                                   5    
HELIX   37  37 ASN C  306  HIS C  313  5                                   8    
HELIX   38  38 LEU C  314  SER C  328  1                                  15    
HELIX   39  39 PHE C  330  THR C  334  5                                   5    
HELIX   40  40 SER C  346  ALA C  351  1                                   6    
HELIX   41  41 SER C  421  PHE C  425  5                                   5    
HELIX   42  42 ASP C  578  ALA C  581  5                                   4    
HELIX   43  43 ALA C  605  LEU C  609  5                                   5    
HELIX   44  44 SER C  610  ASP C  612  5                                   3    
SHEET    1   A 3 THR A  90  PRO A  91  0                                        
SHEET    2   A 3 GLN A 120  TYR A 127 -1  O  GLY A 125   N  THR A  90           
SHEET    3   A 3 PHE A 109  PHE A 110 -1  N  PHE A 109   O  VAL A 121           
SHEET    1   B 6 THR A  90  PRO A  91  0                                        
SHEET    2   B 6 GLN A 120  TYR A 127 -1  O  GLY A 125   N  THR A  90           
SHEET    3   B 6 LEU A 133  PHE A 140 -1  O  THR A 134   N  LYS A 126           
SHEET    4   B 6 VAL A 201  GLY A 205  1  O  SER A 204   N  ILE A 138           
SHEET    5   B 6 ASN A 232  TYR A 236  1  O  ASN A 232   N  VAL A 203           
SHEET    6   B 6 VAL A 247  VAL A 250  1  O  LEU A 248   N  ALA A 235           
SHEET    1   C 8 ILE A 285  PHE A 288  0                                        
SHEET    2   C 8 THR A 339  ALA A 343  1  O  ILE A 340   N  VAL A 286           
SHEET    3   C 8 THR A 369  ILE A 372  1  O  PHE A 370   N  ILE A 341           
SHEET    4   C 8 ASP A 387  GLU A 390  1  O  TYR A 388   N  ILE A 371           
SHEET    5   C 8 ASN A 405  LEU A 408  1  O  VAL A 406   N  LEU A 389           
SHEET    6   C 8 ILE A 444  ARG A 448  1  O  ILE A 446   N  ASN A 405           
SHEET    7   C 8 ASN A 434  ARG A 438 -1  N  LEU A 435   O  THR A 447           
SHEET    8   C 8 ASP A 426  ASN A 429 -1  N  ASP A 426   O  ARG A 438           
SHEET    1   D 8 TRP A 354  VAL A 355  0                                        
SHEET    2   D 8 LEU A 379  GLY A 382  1  O  GLN A 381   N  VAL A 355           
SHEET    3   D 8 THR A 397  ASP A 400  1  O  ARG A 399   N  ILE A 380           
SHEET    4   D 8 THR A 415  ASP A 417  1  O  ASP A 417   N  PHE A 398           
SHEET    5   D 8 SER A 452  LYS A 456  1  O  VAL A 454   N  LEU A 416           
SHEET    6   D 8 ASP A 468  THR A 474 -1  O  HIS A 471   N  ILE A 453           
SHEET    7   D 8 GLY A 477  VAL A 480 -1  O  LYS A 479   N  SER A 472           
SHEET    8   D 8 ASN A 483  THR A 485 -1  O  THR A 485   N  LEU A 478           
SHEET    1   E 6 SER A 490  LYS A 492  0                                        
SHEET    2   E 6 TRP A 508  PHE A 510  1  O  PHE A 510   N  VAL A 491           
SHEET    3   E 6 VAL A 526  VAL A 528  1  O  VAL A 526   N  LEU A 509           
SHEET    4   E 6 THR A 544  PHE A 547  1  O  THR A 544   N  PHE A 527           
SHEET    5   E 6 LYS A 564  PHE A 567  1  O  VAL A 566   N  PHE A 545           
SHEET    6   E 6 ILE A 614  ILE A 616  1  O  VAL A 615   N  PHE A 567           
SHEET    1   F 7 THR A 499  LYS A 501  0                                        
SHEET    2   F 7 HIS A 517  ILE A 519  1  O  ILE A 519   N  LEU A 500           
SHEET    3   F 7 LEU A 535  GLU A 537  1  O  LEU A 535   N  LEU A 518           
SHEET    4   F 7 GLN A 553  VAL A 557  1  O  VAL A 557   N  MET A 536           
SHEET    5   F 7 ASP A 597  LEU A 601  1  O  THR A 600   N  VAL A 556           
SHEET    6   F 7 ASP A 589  PHE A 594 -1  N  THR A 590   O  LEU A 601           
SHEET    7   F 7 ALA A 583  VAL A 586 -1  N  VAL A 586   O  ASP A 589           
SHEET    1   G 3 TRP C  89  PRO C  91  0                                        
SHEET    2   G 3 GLN C 120  TYR C 127 -1  O  GLY C 125   N  THR C  90           
SHEET    3   G 3 PHE C 109  PHE C 110 -1  N  PHE C 109   O  VAL C 121           
SHEET    1   H 6 TRP C  89  PRO C  91  0                                        
SHEET    2   H 6 GLN C 120  TYR C 127 -1  O  GLY C 125   N  THR C  90           
SHEET    3   H 6 LEU C 133  PHE C 140 -1  O  GLY C 137   N  LEU C 124           
SHEET    4   H 6 VAL C 201  HIS C 206  1  O  SER C 204   N  ILE C 138           
SHEET    5   H 6 ASN C 232  TYR C 236  1  O  ASN C 232   N  VAL C 203           
SHEET    6   H 6 VAL C 247  VAL C 250  1  O  VAL C 250   N  ALA C 235           
SHEET    1   I 8 ILE C 285  PHE C 288  0                                        
SHEET    2   I 8 THR C 339  ALA C 343  1  O  ILE C 340   N  VAL C 286           
SHEET    3   I 8 THR C 369  ILE C 372  1  O  PHE C 370   N  ILE C 341           
SHEET    4   I 8 ASP C 387  GLU C 390  1  O  TYR C 388   N  ILE C 371           
SHEET    5   I 8 ASN C 405  LEU C 408  1  O  LEU C 408   N  LEU C 389           
SHEET    6   I 8 ILE C 444  ARG C 448  1  O  ILE C 446   N  ILE C 407           
SHEET    7   I 8 LEU C 435  ARG C 438 -1  N  VAL C 437   O  SER C 445           
SHEET    8   I 8 ASP C 426  ASN C 429 -1  N  ASP C 426   O  ARG C 438           
SHEET    1   J 7 LEU C 379  GLY C 382  0                                        
SHEET    2   J 7 THR C 397  ASP C 400  1  O  ARG C 399   N  GLY C 382           
SHEET    3   J 7 ASN C 414  ASP C 417  1  O  ASP C 417   N  PHE C 398           
SHEET    4   J 7 ILE C 450  PRO C 458  1  O  VAL C 454   N  LEU C 416           
SHEET    5   J 7 LYS C 466  THR C 474 -1  O  HIS C 471   N  ILE C 453           
SHEET    6   J 7 GLY C 477  VAL C 480 -1  O  LYS C 479   N  SER C 472           
SHEET    7   J 7 ASN C 483  GLN C 486 -1  O  ASN C 483   N  VAL C 480           
SHEET    1   K 6 SER C 490  LYS C 492  0                                        
SHEET    2   K 6 TRP C 508  PHE C 510  1  O  PHE C 510   N  VAL C 491           
SHEET    3   K 6 VAL C 526  VAL C 528  1  O  VAL C 526   N  LEU C 509           
SHEET    4   K 6 THR C 544  PHE C 547  1  O  THR C 544   N  PHE C 527           
SHEET    5   K 6 LYS C 564  PHE C 567  1  O  VAL C 566   N  PHE C 547           
SHEET    6   K 6 ILE C 614  ILE C 616  1  O  VAL C 615   N  LEU C 565           
SHEET    1   L 7 THR C 499  LYS C 501  0                                        
SHEET    2   L 7 HIS C 517  ILE C 519  1  O  ILE C 519   N  LEU C 500           
SHEET    3   L 7 LEU C 535  GLU C 537  1  O  LEU C 535   N  LEU C 518           
SHEET    4   L 7 GLN C 553  VAL C 557  1  O  ARG C 555   N  MET C 536           
SHEET    5   L 7 ASP C 597  LEU C 601  1  O  SER C 598   N  ASP C 554           
SHEET    6   L 7 ASP C 589  PHE C 594 -1  N  LEU C 592   O  VAL C 599           
SHEET    7   L 7 ALA C 583  VAL C 586 -1  N  SER C 584   O  VAL C 591           
LINK         O   THR A 118                CA    CA A 628     1555   1555  2.29  
LINK         OE1 GLN A 120                CA    CA A 628     1555   1555  2.32  
LINK         O   SER A 144                CA    CA A 628     1555   1555  2.58  
LINK         OD2 ASP A 153                CA    CA A 628     1555   1555  2.43  
LINK         OD1 ASP A 157                CA    CA A 628     1555   1555  2.45  
LINK         OD2 ASP A 157                CA    CA A 628     1555   1555  2.59  
LINK         OE2 GLU A 253                CA    CA A 618     1555   1555  2.38  
LINK         OD1 ASP A 275                CA    CA A 618     1555   1555  2.40  
LINK         OD2 ASP A 275                CA    CA A 618     1555   1555  2.57  
LINK         O   ASP A 283                CA    CA A 618     1555   1555  2.39  
LINK         OD1 ASN A 284                CA    CA A 618     1555   1555  2.42  
LINK         O   SER A 374                CA    CA A 620     1555   1555  2.29  
LINK         O   SER A 376                CA    CA A 620     1555   1555  2.45  
LINK         OD2 ASP A 378                CA    CA A 620     1555   1555  2.37  
LINK         O   GLY A 383                CA    CA A 621     1555   1555  2.31  
LINK         O   GLY A 385                CA    CA A 621     1555   1555  2.55  
LINK         OD2 ASP A 387                CA    CA A 621     1555   1555  2.25  
LINK         O   GLY A 391                CA    CA A 620     1555   1555  2.36  
LINK         O   ARG A 392                CA    CA A 622     1555   1555  2.47  
LINK         O   ALA A 393                CA    CA A 620     1555   1555  2.31  
LINK         O   GLY A 394                CA    CA A 622     1555   1555  2.60  
LINK         OD1 ASP A 396                CA    CA A 620     1555   1555  2.40  
LINK         OD2 ASP A 396                CA    CA A 620     1555   1555  2.60  
LINK         OD2 ASP A 396                CA    CA A 622     1555   1555  2.47  
LINK         OD1 ASP A 400                CA    CA A 621     1555   1555  2.52  
LINK         OD2 ASP A 400                CA    CA A 621     1555   1555  2.51  
LINK         O   GLY A 402                CA    CA A 621     1555   1555  2.45  
LINK         OD1 ASN A 405                CA    CA A 621     1555   1555  2.33  
LINK         O   GLY A 409                CA    CA A 622     1555   1555  2.34  
LINK         O   ALA A 411                CA    CA A 622     1555   1555  2.40  
LINK         OD1 ASN A 414                CA    CA A 622     1555   1555  2.53  
LINK         O   THR A 494                CA    CA A 623     1555   1555  2.25  
LINK         O   GLY A 496                CA    CA A 623     1555   1555  2.36  
LINK         OD2 ASP A 498                CA    CA A 623     1555   1555  2.35  
LINK         O   GLY A 511                CA    CA A 623     1555   1555  2.36  
LINK         O   LEU A 512                CA    CA A 624     1555   1555  2.45  
LINK         O   ASP A 513                CA    CA A 623     1555   1555  2.39  
LINK         O   GLY A 514                CA    CA A 624     1555   1555  2.37  
LINK         OD1 ASP A 516                CA    CA A 624     1555   1555  2.27  
LINK         OD1 ASP A 516                CA    CA A 623     1555   1555  2.97  
LINK         OD2 ASP A 516                CA    CA A 623     1555   1555  2.38  
LINK         O   GLY A 521                CA    CA A 625     1555   1555  2.59  
LINK         O   GLY A 523                CA    CA A 625     1555   1555  2.60  
LINK         OD2 ASP A 525                CA    CA A 625     1555   1555  2.42  
LINK         O   GLY A 529                CA    CA A 624     1555   1555  2.50  
LINK         O   GLY A 530                CA    CA A 626     1555   1555  2.46  
LINK         O   ALA A 531                CA    CA A 624     1555   1555  2.46  
LINK         O   GLY A 532                CA    CA A 626     1555   1555  2.50  
LINK         OD1 ASP A 534                CA    CA A 624     1555   1555  2.31  
LINK         OD2 ASP A 534                CA    CA A 626     1555   1555  2.23  
LINK         O   SER A 538                CA    CA A 625     1555   1555  2.51  
LINK         O   GLY A 540                CA    CA A 625     1555   1555  2.32  
LINK         OD1 ASP A 543                CA    CA A 625     1555   1555  2.41  
LINK         OD2 ASP A 543                CA    CA A 625     1555   1555  2.64  
LINK         O   PHE A 551                CA    CA A 626     1555   1555  2.23  
LINK         OD1 ASP A 554                CA    CA A 626     1555   1555  2.48  
LINK         O   THR C 118                CA    CA C 628     1555   1555  2.31  
LINK         OE1 GLN C 120                CA    CA C 628     1555   1555  2.37  
LINK         O   SER C 144                CA    CA C 628     1555   1555  2.49  
LINK         OD2 ASP C 153                CA    CA C 628     1555   1555  2.34  
LINK         OD1 ASP C 157                CA    CA C 628     1555   1555  2.61  
LINK         OD2 ASP C 157                CA    CA C 628     1555   1555  2.40  
LINK         OE2 GLU C 253                CA    CA C 618     1555   1555  2.34  
LINK         OD1 ASP C 275                CA    CA C 618     1555   1555  2.55  
LINK         OD2 ASP C 275                CA    CA C 618     1555   1555  2.54  
LINK         O   ASP C 283                CA    CA C 618     1555   1555  2.41  
LINK         OD1 ASN C 284                CA    CA C 618     1555   1555  2.35  
LINK         O   SER C 374                CA    CA C 620     1555   1555  2.34  
LINK         O   SER C 376                CA    CA C 620     1555   1555  2.41  
LINK         OD2 ASP C 378                CA    CA C 620     1555   1555  2.40  
LINK         O   GLY C 383                CA    CA C 621     1555   1555  2.48  
LINK         O   GLY C 385                CA    CA C 621     1555   1555  2.48  
LINK         OD2 ASP C 387                CA    CA C 621     1555   1555  2.48  
LINK         O   GLY C 391                CA    CA C 620     1555   1555  2.32  
LINK         O   ALA C 393                CA    CA C 620     1555   1555  2.41  
LINK         OD1 ASP C 396                CA    CA C 620     1555   1555  2.44  
LINK         OD2 ASP C 396                CA    CA C 620     1555   1555  2.56  
LINK         OD1 ASP C 400                CA    CA C 621     1555   1555  2.52  
LINK         OD2 ASP C 400                CA    CA C 621     1555   1555  2.37  
LINK         O   GLY C 402                CA    CA C 621     1555   1555  2.32  
LINK         OD1 ASN C 405                CA    CA C 621     1555   1555  2.35  
LINK         O   THR C 494                CA    CA C 623     1555   1555  2.27  
LINK         O   GLY C 496                CA    CA C 623     1555   1555  2.59  
LINK         OD2 ASP C 498                CA    CA C 623     1555   1555  2.43  
LINK         O   GLY C 511                CA    CA C 623     1555   1555  2.34  
LINK         O   LEU C 512                CA    CA C 624     1555   1555  2.25  
LINK         O   ASP C 513                CA    CA C 623     1555   1555  2.33  
LINK         O   GLY C 514                CA    CA C 624     1555   1555  2.50  
LINK         OD1 ASP C 516                CA    CA C 624     1555   1555  2.50  
LINK         OD1 ASP C 516                CA    CA C 623     1555   1555  2.79  
LINK         OD2 ASP C 516                CA    CA C 623     1555   1555  2.43  
LINK         O   GLY C 521                CA    CA C 625     1555   1555  2.64  
LINK         O   GLY C 523                CA    CA C 625     1555   1555  2.54  
LINK         OD2 ASP C 525                CA    CA C 625     1555   1555  2.39  
LINK         O   GLY C 529                CA    CA C 624     1555   1555  2.40  
LINK         O   GLY C 530                CA    CA C 626     1555   1555  2.46  
LINK         O   ALA C 531                CA    CA C 624     1555   1555  2.45  
LINK         O   GLY C 532                CA    CA C 626     1555   1555  2.53  
LINK         OD1 ASP C 534                CA    CA C 624     1555   1555  2.30  
LINK         OD2 ASP C 534                CA    CA C 626     1555   1555  2.26  
LINK         O   SER C 538                CA    CA C 625     1555   1555  2.54  
LINK         O   GLY C 540                CA    CA C 625     1555   1555  2.41  
LINK         OD1 ASP C 543                CA    CA C 625     1555   1555  2.46  
LINK         OD2 ASP C 543                CA    CA C 625     1555   1555  2.63  
LINK         O   PHE C 551                CA    CA C 626     1555   1555  2.35  
LINK         OD1 ASP C 554                CA    CA C 626     1555   1555  2.38  
LINK         OD2 ASP C 554                CA    CA C 626     1555   1555  2.97  
LINK        CA    CA A 618                 O   HOH A 658     1555   1555  2.47  
LINK        CA    CA A 618                 O   HOH A 681     1555   1555  2.37  
LINK        CA    CA A 626                 O   HOH A 761     1555   1555  2.50  
LINK        CA    CA A 628                 O   HOH A 715     1555   1555  2.22  
LINK        CA    CA C 618                 O   HOH C 669     1555   1555  2.46  
LINK        CA    CA C 618                 O   HOH C 698     1555   1555  2.58  
LINK        CA    CA C 626                 O   HOH C 675     1555   1555  2.21  
LINK        CA    CA C 628                 O   HOH C 699     1555   1555  2.32  
LINK         OD2 ASP A 554                CA    CA A 626     1555   1555  3.06  
LINK         OD2 ASP C 534                CA    CA C 624     1555   1555  3.12  
LINK         OD2 ASP A 534                CA    CA A 624     1555   1555  3.20  
SITE     1 AC1  6 GLU A 253  ASP A 275  ASP A 283  ASN A 284                    
SITE     2 AC1  6 HOH A 658  HOH A 681                                          
SITE     1 AC2  6 SER A 374  SER A 376  ASP A 378  GLY A 391                    
SITE     2 AC2  6 ALA A 393  ASP A 396                                          
SITE     1 AC3  6 GLY A 383  GLY A 385  ASP A 387  ASP A 400                    
SITE     2 AC3  6 GLY A 402  ASN A 405                                          
SITE     1 AC4  6 ARG A 392  GLY A 394  ASP A 396  GLY A 409                    
SITE     2 AC4  6 ALA A 411  ASN A 414                                          
SITE     1 AC5  6 THR A 494  GLY A 496  ASP A 498  GLY A 511                    
SITE     2 AC5  6 ASP A 513  ASP A 516                                          
SITE     1 AC6  6 LEU A 512  GLY A 514  ASP A 516  GLY A 529                    
SITE     2 AC6  6 ALA A 531  ASP A 534                                          
SITE     1 AC7  6 GLY A 521  GLY A 523  ASP A 525  SER A 538                    
SITE     2 AC7  6 GLY A 540  ASP A 543                                          
SITE     1 AC8  6 GLY A 530  GLY A 532  ASP A 534  PHE A 551                    
SITE     2 AC8  6 ASP A 554  HOH A 761                                          
SITE     1 AC9  6 THR A 118  GLN A 120  SER A 144  ASP A 153                    
SITE     2 AC9  6 ASP A 157  HOH A 715                                          
SITE     1 BC1  6 GLU C 253  ASP C 275  ASP C 283  ASN C 284                    
SITE     2 BC1  6 HOH C 669  HOH C 698                                          
SITE     1 BC2  6 SER C 374  SER C 376  ASP C 378  GLY C 391                    
SITE     2 BC2  6 ALA C 393  ASP C 396                                          
SITE     1 BC3  6 GLY C 383  GLY C 385  ASP C 387  ASP C 400                    
SITE     2 BC3  6 GLY C 402  ASN C 405                                          
SITE     1 BC4  6 THR C 494  GLY C 496  ASP C 498  GLY C 511                    
SITE     2 BC4  6 ASP C 513  ASP C 516                                          
SITE     1 BC5  6 LEU C 512  GLY C 514  ASP C 516  GLY C 529                    
SITE     2 BC5  6 ALA C 531  ASP C 534                                          
SITE     1 BC6  6 GLY C 521  GLY C 523  ASP C 525  SER C 538                    
SITE     2 BC6  6 GLY C 540  ASP C 543                                          
SITE     1 BC7  6 GLY C 530  GLY C 532  ASP C 534  PHE C 551                    
SITE     2 BC7  6 ASP C 554  HOH C 675                                          
SITE     1 BC8  6 THR C 118  GLN C 120  SER C 144  ASP C 153                    
SITE     2 BC8  6 ASP C 157  HOH C 699                                          
CRYST1  104.382  104.382  495.175  90.00  90.00 120.00 P 65 2 2     24          
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      0.009580  0.005531  0.000000        0.00000                         
SCALE2      0.000000  0.011062  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.002019        0.00000                         
TER    4526      ALA A 617                                                      
TER    9080      ALA C 617                                                      
MASTER      662    0   17   44   75    0   34    6 9726    2  147   96          
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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